HEADER    SIGNALING PROTEIN, HYDROLASE            12-AUG-10   3OE8              
TITLE     CRYSTAL STRUCTURE OF THE CXCR4 CHEMOKINE RECEPTOR IN COMPLEX WITH A   
TITLE    2 SMALL MOLECULE ANTAGONIST IT1T IN P1 SPACEGROUP                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: C-X-C CHEMOKINE RECEPTOR TYPE 4, LYSOZYME CHIMERA;         
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: CXCR4 RESIDUES 2-229, LYSOZYME RESIDUES 1002-1161, CXCR4   
COMPND   5 RESIDUES 230-319;                                                    
COMPND   6 SYNONYM: CXC-R4, CXCR-4, STROMAL CELL-DERIVED FACTOR 1 RECEPTOR, SDF-
COMPND   7 1 RECEPTOR, FUSIN, LEUKOCYTE-DERIVED SEVEN TRANSMEMBRANE DOMAIN      
COMPND   8 RECEPTOR, LESTR, LCR1, FB22, NPYRL, HM89, LYSIS PROTEIN, MURAMIDASE, 
COMPND   9 ENDOLYSIN;                                                           
COMPND  10 EC: 3.2.1.17;                                                        
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4;          
SOURCE   3 ORGANISM_TAXID: 9606, 10665;                                         
SOURCE   4 GENE: CXCR4, CXCR4_HUMAN,E;                                          
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACMID;                               
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PFASTBAC                                  
KEYWDS    STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE, ACCELERATED 
KEYWDS   2 TECHNOLOGIES CENTER FOR GENE TO 3D STRUCTURE, ATCG3D, 7TM, G         
KEYWDS   3 PROTEIN-COUPLED RECEPTOR, GPCR, SIGNAL TRANSDUCTION, HYDROLASE,      
KEYWDS   4 CANCER, HIV-1 CO-RECEPTOR, CHEMOTAXIS, CHEMOKINE, CXCL12, SDF1,      
KEYWDS   5 ISOTHIOUREA, CHIMERA, T4L FUSION, MEMBRANE PROTEIN, TRANSMEMBRANE,   
KEYWDS   6 SINGNALING PROTEIN, PSI-BIOLOGY, GPCR NETWORK, SIGNALING PROTEIN     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.WU,C.D.MOL,G.W.HAN,V.KATRITCH,E.Y.T.CHIEN,W.LIU,V.CHEREZOV,         
AUTHOR   2 R.C.STEVENS,ACCELERATED TECHNOLOGIES CENTER FOR GENE TO 3D STRUCTURE 
AUTHOR   3 (ATCG3D),GPCR NETWORK (GPCR)                                         
REVDAT   7   06-OCT-21 3OE8    1       REMARK SEQADV LINK                       
REVDAT   6   13-JUN-18 3OE8    1       REMARK DBREF  SEQADV                     
REVDAT   5   26-JUL-17 3OE8    1       SOURCE REMARK                            
REVDAT   4   02-MAY-12 3OE8    1       REMARK VERSN                             
REVDAT   3   16-FEB-11 3OE8    1       HEADER                                   
REVDAT   2   05-JAN-11 3OE8    1       JRNL                                     
REVDAT   1   27-OCT-10 3OE8    0                                                
JRNL        AUTH   B.WU,E.Y.CHIEN,C.D.MOL,G.FENALTI,W.LIU,V.KATRITCH,R.ABAGYAN, 
JRNL        AUTH 2 A.BROOUN,P.WELLS,F.C.BI,D.J.HAMEL,P.KUHN,T.M.HANDEL,         
JRNL        AUTH 3 V.CHEREZOV,R.C.STEVENS                                       
JRNL        TITL   STRUCTURES OF THE CXCR4 CHEMOKINE GPCR WITH SMALL-MOLECULE   
JRNL        TITL 2 AND CYCLIC PEPTIDE ANTAGONISTS.                              
JRNL        REF    SCIENCE                       V. 330  1066 2010              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   20929726                                                     
JRNL        DOI    10.1126/SCIENCE.1194396                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.8.0                                         
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.97                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 28647                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.253                          
REMARK   3   R VALUE            (WORKING SET)  : 0.250                          
REMARK   3   FREE R VALUE                      : 0.295                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.030                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1441                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 14                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.10                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.22                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 1954                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2584                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 1871                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2558                   
REMARK   3   BIN FREE R VALUE                        : 0.3204                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.25                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 83                       
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10292                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 81                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 102.4                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 103.6                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.68450                                              
REMARK   3    B22 (A**2) : 10.37890                                             
REMARK   3    B33 (A**2) : -13.06340                                            
REMARK   3    B12 (A**2) : -4.10050                                             
REMARK   3    B13 (A**2) : -0.95230                                             
REMARK   3    B23 (A**2) : 0.66120                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.838               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.895                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.854                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 10635  ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 14450  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 3546   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 191    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1532   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 10545  ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1410   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 12091  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.40                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.25                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 21.60                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|27 - A|229 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):  -27.1542    1.6998   35.2206           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2163 T22:   -0.0339                                    
REMARK   3     T33:   -0.1883 T12:   -0.0250                                    
REMARK   3     T13:   -0.0162 T23:    0.0751                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.7244 L22:    2.3650                                    
REMARK   3     L33:    2.8683 L12:    0.1898                                    
REMARK   3     L13:   -0.9018 L23:   -0.8128                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0202 S12:    0.3570 S13:    0.3592                     
REMARK   3     S21:    0.2502 S22:    0.0887 S23:   -0.0802                     
REMARK   3     S31:   -0.1683 S32:   -0.1644 S33:   -0.1089                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { A|900 - A|901 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -25.6706  -23.0882   68.2627           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1129 T22:    0.0244                                    
REMARK   3     T33:    0.0349 T12:    0.0310                                    
REMARK   3     T13:   -0.0106 T23:   -0.0094                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0242 L22:    0.0792                                    
REMARK   3     L33:    0.0217 L12:   -0.0276                                    
REMARK   3     L13:   -0.0036 L23:   -0.0469                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0013 S12:    0.0011 S13:    0.0033                     
REMARK   3     S21:   -0.0007 S22:    0.0015 S23:   -0.0034                     
REMARK   3     S31:   -0.0019 S32:    0.0004 S33:   -0.0003                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { A|1002 - A|1161 }                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -16.3508  -18.8147   78.4237           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0305 T22:    0.0520                                    
REMARK   3     T33:   -0.3362 T12:   -0.0240                                    
REMARK   3     T13:   -0.1183 T23:    0.0277                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.5567 L22:    3.1571                                    
REMARK   3     L33:    3.9214 L12:   -1.3737                                    
REMARK   3     L13:   -1.0970 L23:    1.0632                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0857 S12:    0.0031 S13:   -0.0011                     
REMARK   3     S21:    0.0103 S22:   -0.0253 S23:    0.0682                     
REMARK   3     S31:    0.0700 S32:   -0.1052 S33:   -0.0604                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { A|232 - A|305 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -33.0890   -8.7081   31.7780           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1402 T22:    0.2082                                    
REMARK   3     T33:   -0.2361 T12:   -0.0808                                    
REMARK   3     T13:   -0.0474 T23:    0.0924                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.8254 L22:    2.5690                                    
REMARK   3     L33:    2.5444 L12:    0.5971                                    
REMARK   3     L13:    0.4843 L23:   -0.2585                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0388 S12:    0.1669 S13:   -0.0763                     
REMARK   3     S21:    0.0711 S22:    0.0127 S23:    0.2861                     
REMARK   3     S31:   -0.0167 S32:   -0.1231 S33:   -0.0515                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: { B|27 - B|226 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):  -66.4418   11.3855   33.3222           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1584 T22:   -0.1138                                    
REMARK   3     T33:   -0.1501 T12:   -0.0178                                    
REMARK   3     T13:    0.0916 T23:   -0.0136                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.2433 L22:    1.4565                                    
REMARK   3     L33:    5.6998 L12:    0.2012                                    
REMARK   3     L13:    2.2949 L23:    0.4152                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0651 S12:    0.0740 S13:   -0.0540                     
REMARK   3     S21:    0.0867 S22:    0.0274 S23:    0.1679                     
REMARK   3     S31:   -0.0486 S32:    0.0919 S33:    0.0377                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: { B|1002 - B|1161 }                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -45.5156    5.9077   79.2088           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0330 T22:    0.1309                                    
REMARK   3     T33:   -0.2827 T12:    0.0274                                    
REMARK   3     T13:    0.0013 T23:    0.1353                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.3042 L22:    2.4432                                    
REMARK   3     L33:    2.7826 L12:    1.1038                                    
REMARK   3     L13:    1.3717 L23:    0.8815                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0005 S12:   -0.3085 S13:    0.2501                     
REMARK   3     S21:    0.2325 S22:    0.1367 S23:   -0.1800                     
REMARK   3     S31:   -0.2166 S32:   -0.3057 S33:   -0.1372                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: { B|1200 - B|1201 }                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -53.8271    8.7772   62.3260           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0217 T22:    0.0210                                    
REMARK   3     T33:    0.0192 T12:    0.0018                                    
REMARK   3     T13:   -0.0146 T23:    0.0033                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0333 L22:    0.0096                                    
REMARK   3     L33:    0.0043 L12:   -0.0172                                    
REMARK   3     L13:    0.0156 L23:    0.0007                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0002 S12:    0.0004 S13:   -0.0021                     
REMARK   3     S21:    0.0026 S22:    0.0010 S23:    0.0007                     
REMARK   3     S31:    0.0010 S32:   -0.0015 S33:   -0.0008                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: { B|230 - B|304 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -56.5048    3.4250   32.0329           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1229 T22:    0.0231                                    
REMARK   3     T33:   -0.1076 T12:    0.0958                                    
REMARK   3     T13:    0.0012 T23:   -0.0714                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.6490 L22:    1.3804                                    
REMARK   3     L33:    3.3552 L12:   -0.7468                                    
REMARK   3     L13:    2.7982 L23:    0.2774                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0082 S12:    0.1536 S13:   -0.2049                     
REMARK   3     S21:    0.0997 S22:   -0.0363 S23:    0.0215                     
REMARK   3     S31:    0.1160 S32:    0.0666 S33:    0.0281                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: { C|27 - C|227 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):  -44.0917   38.4251   35.8887           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0751 T22:   -0.0266                                    
REMARK   3     T33:   -0.3247 T12:   -0.0846                                    
REMARK   3     T13:   -0.0136 T23:   -0.0334                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.3582 L22:    2.3521                                    
REMARK   3     L33:    2.5424 L12:   -0.0202                                    
REMARK   3     L13:   -0.1243 L23:    0.4788                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1420 S12:    0.1478 S13:   -0.1373                     
REMARK   3     S21:    0.2674 S22:    0.0842 S23:   -0.2651                     
REMARK   3     S31:    0.3499 S32:    0.1778 S33:    0.0579                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: { C|1002 - C|1161 }                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -67.2350   38.2804   82.7051           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0274 T22:    0.1349                                    
REMARK   3     T33:   -0.3446 T12:    0.0845                                    
REMARK   3     T13:   -0.0790 T23:   -0.0113                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.5721 L22:    2.8985                                    
REMARK   3     L33:    2.6219 L12:    1.1157                                    
REMARK   3     L13:    1.0930 L23:    0.0006                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0168 S12:   -0.1513 S13:   -0.2523                     
REMARK   3     S21:    0.0510 S22:   -0.0636 S23:    0.1092                     
REMARK   3     S31:    0.1179 S32:    0.1816 S33:    0.0469                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: { C|1200 - C|1201 }                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -55.4766   45.8414   69.5709           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0006 T22:    0.0094                                    
REMARK   3     T33:    0.0172 T12:    0.0113                                    
REMARK   3     T13:   -0.0016 T23:   -0.0083                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0100 L22:    0.0172                                    
REMARK   3     L33:   -0.0018 L12:    0.0134                                    
REMARK   3     L13:   -0.0247 L23:    0.0189                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0001 S12:    0.0017 S13:   -0.0005                     
REMARK   3     S21:   -0.0020 S22:    0.0022 S23:   -0.0040                     
REMARK   3     S31:    0.0005 S32:    0.0010 S33:   -0.0023                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: { C|230 - C|305 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):  -55.0013   45.5716   33.9298           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1383 T22:    0.0022                                    
REMARK   3     T33:   -0.3215 T12:   -0.1271                                    
REMARK   3     T13:    0.0051 T23:   -0.0488                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.8993 L22:    2.2347                                    
REMARK   3     L33:    1.7421 L12:    1.1578                                    
REMARK   3     L13:   -1.7420 L23:   -2.7984                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1496 S12:    0.2402 S13:    0.1150                     
REMARK   3     S21:    0.2885 S22:    0.1892 S23:   -0.0232                     
REMARK   3     S31:    0.0477 S32:   -0.0628 S33:   -0.0396                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3OE8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-OCT-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000061004.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 11                                 
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0330                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28801                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 87.3                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.15000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 59.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.77                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: LIPIDIC CUBIC PHASE MADE OF MONOOLEIN    
REMARK 280  AND CHOLESTEROL, 26% PEG400, 0.3M SODIUM MALONATE, 5MM STRONTIUM    
REMARK 280  CHLORIDE, 0.1M MES PH 6.0, LIPIDIC CUBIC PHASE, TEMPERATURE 293K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1320 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 46550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 67690 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP A    -9                                                      
REMARK 465     TYR A    -8                                                      
REMARK 465     LYS A    -7                                                      
REMARK 465     ASP A    -6                                                      
REMARK 465     ASP A    -5                                                      
REMARK 465     ASP A    -4                                                      
REMARK 465     ASP A    -3                                                      
REMARK 465     ALA A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     PRO A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     ILE A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     ILE A     6                                                      
REMARK 465     TYR A     7                                                      
REMARK 465     THR A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     ASP A    10                                                      
REMARK 465     ASN A    11                                                      
REMARK 465     TYR A    12                                                      
REMARK 465     THR A    13                                                      
REMARK 465     GLU A    14                                                      
REMARK 465     GLU A    15                                                      
REMARK 465     MET A    16                                                      
REMARK 465     GLY A    17                                                      
REMARK 465     SER A    18                                                      
REMARK 465     GLY A    19                                                      
REMARK 465     ASP A    20                                                      
REMARK 465     TYR A    21                                                      
REMARK 465     ASP A    22                                                      
REMARK 465     SER A    23                                                      
REMARK 465     MET A    24                                                      
REMARK 465     LYS A    25                                                      
REMARK 465     GLU A    26                                                      
REMARK 465     PHE A    29                                                      
REMARK 465     ARG A    30                                                      
REMARK 465     GLU A    31                                                      
REMARK 465     GLU A    32                                                      
REMARK 465     ASN A    33                                                      
REMARK 465     ALA A    34                                                      
REMARK 465     GLY A  1200                                                      
REMARK 465     SER A  1201                                                      
REMARK 465     LYS A   230                                                      
REMARK 465     GLY A   231                                                      
REMARK 465     GLY A   306                                                      
REMARK 465     ALA A   307                                                      
REMARK 465     LYS A   308                                                      
REMARK 465     PHE A   309                                                      
REMARK 465     LYS A   310                                                      
REMARK 465     THR A   311                                                      
REMARK 465     SER A   312                                                      
REMARK 465     ALA A   313                                                      
REMARK 465     GLN A   314                                                      
REMARK 465     HIS A   315                                                      
REMARK 465     ALA A   316                                                      
REMARK 465     LEU A   317                                                      
REMARK 465     THR A   318                                                      
REMARK 465     SER A   319                                                      
REMARK 465     GLY A   320                                                      
REMARK 465     ARG A   321                                                      
REMARK 465     PRO A   322                                                      
REMARK 465     LEU A   323                                                      
REMARK 465     GLU A   324                                                      
REMARK 465     VAL A   325                                                      
REMARK 465     LEU A   326                                                      
REMARK 465     PHE A   327                                                      
REMARK 465     GLN A   328                                                      
REMARK 465     ASP B    -9                                                      
REMARK 465     TYR B    -8                                                      
REMARK 465     LYS B    -7                                                      
REMARK 465     ASP B    -6                                                      
REMARK 465     ASP B    -5                                                      
REMARK 465     ASP B    -4                                                      
REMARK 465     ASP B    -3                                                      
REMARK 465     ALA B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     PRO B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     ILE B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     ILE B     6                                                      
REMARK 465     TYR B     7                                                      
REMARK 465     THR B     8                                                      
REMARK 465     SER B     9                                                      
REMARK 465     ASP B    10                                                      
REMARK 465     ASN B    11                                                      
REMARK 465     TYR B    12                                                      
REMARK 465     THR B    13                                                      
REMARK 465     GLU B    14                                                      
REMARK 465     GLU B    15                                                      
REMARK 465     MET B    16                                                      
REMARK 465     GLY B    17                                                      
REMARK 465     SER B    18                                                      
REMARK 465     GLY B    19                                                      
REMARK 465     ASP B    20                                                      
REMARK 465     TYR B    21                                                      
REMARK 465     ASP B    22                                                      
REMARK 465     SER B    23                                                      
REMARK 465     MET B    24                                                      
REMARK 465     LYS B    25                                                      
REMARK 465     GLU B    26                                                      
REMARK 465     ARG B    30                                                      
REMARK 465     GLU B    31                                                      
REMARK 465     GLU B    32                                                      
REMARK 465     THR B   142                                                      
REMARK 465     ASN B   143                                                      
REMARK 465     SER B   144                                                      
REMARK 465     SER B   227                                                      
REMARK 465     HIS B   228                                                      
REMARK 465     SER B   229                                                      
REMARK 465     GLY B   900                                                      
REMARK 465     SER B   901                                                      
REMARK 465     LEU B   267                                                      
REMARK 465     GLU B   268                                                      
REMARK 465     ILE B   269                                                      
REMARK 465     ILE B   270                                                      
REMARK 465     LYS B   271                                                      
REMARK 465     LEU B   305                                                      
REMARK 465     GLY B   306                                                      
REMARK 465     ALA B   307                                                      
REMARK 465     LYS B   308                                                      
REMARK 465     PHE B   309                                                      
REMARK 465     LYS B   310                                                      
REMARK 465     THR B   311                                                      
REMARK 465     SER B   312                                                      
REMARK 465     ALA B   313                                                      
REMARK 465     GLN B   314                                                      
REMARK 465     HIS B   315                                                      
REMARK 465     ALA B   316                                                      
REMARK 465     LEU B   317                                                      
REMARK 465     THR B   318                                                      
REMARK 465     SER B   319                                                      
REMARK 465     GLY B   320                                                      
REMARK 465     ARG B   321                                                      
REMARK 465     PRO B   322                                                      
REMARK 465     LEU B   323                                                      
REMARK 465     GLU B   324                                                      
REMARK 465     VAL B   325                                                      
REMARK 465     LEU B   326                                                      
REMARK 465     PHE B   327                                                      
REMARK 465     GLN B   328                                                      
REMARK 465     ASP C    -9                                                      
REMARK 465     TYR C    -8                                                      
REMARK 465     LYS C    -7                                                      
REMARK 465     ASP C    -6                                                      
REMARK 465     ASP C    -5                                                      
REMARK 465     ASP C    -4                                                      
REMARK 465     ASP C    -3                                                      
REMARK 465     ALA C    -2                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     ALA C     0                                                      
REMARK 465     PRO C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     GLY C     3                                                      
REMARK 465     ILE C     4                                                      
REMARK 465     SER C     5                                                      
REMARK 465     ILE C     6                                                      
REMARK 465     TYR C     7                                                      
REMARK 465     THR C     8                                                      
REMARK 465     SER C     9                                                      
REMARK 465     ASP C    10                                                      
REMARK 465     ASN C    11                                                      
REMARK 465     TYR C    12                                                      
REMARK 465     THR C    13                                                      
REMARK 465     GLU C    14                                                      
REMARK 465     GLU C    15                                                      
REMARK 465     MET C    16                                                      
REMARK 465     GLY C    17                                                      
REMARK 465     SER C    18                                                      
REMARK 465     GLY C    19                                                      
REMARK 465     ASP C    20                                                      
REMARK 465     TYR C    21                                                      
REMARK 465     ASP C    22                                                      
REMARK 465     SER C    23                                                      
REMARK 465     MET C    24                                                      
REMARK 465     LYS C    25                                                      
REMARK 465     GLU C    26                                                      
REMARK 465     ARG C    30                                                      
REMARK 465     GLU C    31                                                      
REMARK 465     GLU C    32                                                      
REMARK 465     ASN C    33                                                      
REMARK 465     ALA C    34                                                      
REMARK 465     ASN C    35                                                      
REMARK 465     THR C   142                                                      
REMARK 465     ASN C   143                                                      
REMARK 465     SER C   144                                                      
REMARK 465     ASP C   181                                                      
REMARK 465     ASP C   182                                                      
REMARK 465     HIS C   228                                                      
REMARK 465     SER C   229                                                      
REMARK 465     GLY C   900                                                      
REMARK 465     SER C   901                                                      
REMARK 465     GLY C   306                                                      
REMARK 465     ALA C   307                                                      
REMARK 465     LYS C   308                                                      
REMARK 465     PHE C   309                                                      
REMARK 465     LYS C   310                                                      
REMARK 465     THR C   311                                                      
REMARK 465     SER C   312                                                      
REMARK 465     ALA C   313                                                      
REMARK 465     GLN C   314                                                      
REMARK 465     HIS C   315                                                      
REMARK 465     ALA C   316                                                      
REMARK 465     LEU C   317                                                      
REMARK 465     THR C   318                                                      
REMARK 465     SER C   319                                                      
REMARK 465     GLY C   320                                                      
REMARK 465     ARG C   321                                                      
REMARK 465     PRO C   322                                                      
REMARK 465     LEU C   323                                                      
REMARK 465     GLU C   324                                                      
REMARK 465     VAL C   325                                                      
REMARK 465     LEU C   326                                                      
REMARK 465     PHE C   327                                                      
REMARK 465     GLN C   328                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LEU A  69    CG   CD1  CD2                                       
REMARK 470     VAL A  99    CG1  CG2                                            
REMARK 470     ASP A 182    CG   OD1  OD2                                       
REMARK 470     ARG A 183    CD   NE   CZ   NH1  NH2                             
REMARK 470     ILE A1003    CG1  CG2  CD1                                       
REMARK 470     ILE A1009    CG1  CG2  CD1                                       
REMARK 470     LYS A 234    CG   CD   CE   NZ                                   
REMARK 470     LEU A 267    CG   CD1  CD2                                       
REMARK 470     LYS A 271    CG   CD   CE   NZ                                   
REMARK 470     ASN B  33    CG   OD1  ND2                                       
REMARK 470     ASP B1020    CG   OD1  OD2                                       
REMARK 470     TYR B1025    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS B1065    CD   CE   NZ                                        
REMARK 470     LYS B 234    CG   CD   CE   NZ                                   
REMARK 470     ILE B 257    CG1  CG2  CD1                                       
REMARK 470     SER B 260    OG                                                  
REMARK 470     SER B 263    OG                                                  
REMARK 470     GLU B 277    CG   CD   OE1  OE2                                  
REMARK 470     LYS C  68    CG   CD   CE   NZ                                   
REMARK 470     ARG C  70    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C 145    CG   CD   OE1  NE2                                  
REMARK 470     SER C1201    OG                                                  
REMARK 470     LYS C 230    CG   CD   CE   NZ                                   
REMARK 470     LYS C 234    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLY C1200   CA    GLY C1200   C      -0.102                       
REMARK 500    SER C1201   CA    SER C1201   C      -0.208                       
REMARK 500    SER C1201   C     SER C1201   O       0.190                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    VAL A  99   CB  -  CA  -  C   ANGL. DEV. = -15.7 DEGREES          
REMARK 500    ALA A 100   CB  -  CA  -  C   ANGL. DEV. = -14.7 DEGREES          
REMARK 500    ALA A 100   N   -  CA  -  C   ANGL. DEV. = -16.8 DEGREES          
REMARK 500    ASN A 101   N   -  CA  -  CB  ANGL. DEV. = -13.3 DEGREES          
REMARK 500    ALA A 137   CB  -  CA  -  C   ANGL. DEV. =  13.6 DEGREES          
REMARK 500    VAL A 139   CB  -  CA  -  C   ANGL. DEV. =  13.8 DEGREES          
REMARK 500    HIS A 140   N   -  CA  -  CB  ANGL. DEV. = -15.1 DEGREES          
REMARK 500    ALA A 141   CB  -  CA  -  C   ANGL. DEV. = -10.1 DEGREES          
REMARK 500    ILE A 173   CB  -  CA  -  C   ANGL. DEV. = -18.9 DEGREES          
REMARK 500    ILE A 173   N   -  CA  -  C   ANGL. DEV. =  16.8 DEGREES          
REMARK 500    ASP A 182   CB  -  CA  -  C   ANGL. DEV. = -13.5 DEGREES          
REMARK 500    ARG A 183   N   -  CA  -  CB  ANGL. DEV. =  13.0 DEGREES          
REMARK 500    SER A 229   CA  -  C   -  N   ANGL. DEV. =  19.4 DEGREES          
REMARK 500    SER A 229   O   -  C   -  N   ANGL. DEV. = -20.6 DEGREES          
REMARK 500    GLY A 900   C   -  N   -  CA  ANGL. DEV. =  13.8 DEGREES          
REMARK 500    GLY A 900   N   -  CA  -  C   ANGL. DEV. =  28.6 DEGREES          
REMARK 500    GLU A1005   CB  -  CA  -  C   ANGL. DEV. = -19.6 DEGREES          
REMARK 500    MET A1006   N   -  CA  -  C   ANGL. DEV. = -20.8 DEGREES          
REMARK 500    THR A1115   N   -  CA  -  C   ANGL. DEV. =  17.3 DEGREES          
REMARK 500    HIS A 232   N   -  CA  -  CB  ANGL. DEV. = -22.8 DEGREES          
REMARK 500    HIS A 232   N   -  CA  -  C   ANGL. DEV. =  30.0 DEGREES          
REMARK 500    LEU A 266   CB  -  CA  -  C   ANGL. DEV. = -13.8 DEGREES          
REMARK 500    LEU B 208   N   -  CA  -  C   ANGL. DEV. =  19.0 DEGREES          
REMARK 500    SER B1201   CB  -  CA  -  C   ANGL. DEV. = -17.1 DEGREES          
REMARK 500    SER B1201   N   -  CA  -  C   ANGL. DEV. =  37.7 DEGREES          
REMARK 500    GLY B 231   N   -  CA  -  C   ANGL. DEV. = -19.8 DEGREES          
REMARK 500    ILE B 257   CB  -  CA  -  C   ANGL. DEV. = -16.4 DEGREES          
REMARK 500    ILE B 259   CB  -  CA  -  C   ANGL. DEV. = -12.4 DEGREES          
REMARK 500    SER B 260   CB  -  CA  -  C   ANGL. DEV. = -14.8 DEGREES          
REMARK 500    ILE B 261   CB  -  CA  -  C   ANGL. DEV. = -15.1 DEGREES          
REMARK 500    ALA C 100   CB  -  CA  -  C   ANGL. DEV. = -14.7 DEGREES          
REMARK 500    ALA C 100   N   -  CA  -  C   ANGL. DEV. = -16.4 DEGREES          
REMARK 500    ASN C 101   N   -  CA  -  CB  ANGL. DEV. = -20.8 DEGREES          
REMARK 500    GLY C1023   N   -  CA  -  C   ANGL. DEV. =  27.4 DEGREES          
REMARK 500    SER C1201   C   -  N   -  CA  ANGL. DEV. =  25.3 DEGREES          
REMARK 500    SER C1201   CB  -  CA  -  C   ANGL. DEV. = -25.6 DEGREES          
REMARK 500    SER C1201   N   -  CA  -  C   ANGL. DEV. =  35.5 DEGREES          
REMARK 500    SER C1201   CA  -  C   -  O   ANGL. DEV. = -14.9 DEGREES          
REMARK 500    SER C1201   O   -  C   -  N   ANGL. DEV. = -19.3 DEGREES          
REMARK 500    LYS C 230   C   -  N   -  CA  ANGL. DEV. =  25.3 DEGREES          
REMARK 500    GLU C 268   N   -  CA  -  C   ANGL. DEV. =  22.4 DEGREES          
REMARK 500    ILE C 269   N   -  CA  -  C   ANGL. DEV. =  23.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 181       86.20    -66.45                                   
REMARK 500    ASP A 182        9.03     96.26                                   
REMARK 500    HIS A 228       40.95    -92.41                                   
REMARK 500    SER A 229     -151.66   -129.65                                   
REMARK 500    SER A 901       -2.82   -147.32                                   
REMARK 500    ASN A1002        4.35     55.56                                   
REMARK 500    CYS A 274      -37.60    -31.41                                   
REMARK 500    SER C1201       42.18    -86.99                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY C 1200     SER C 1201                  125.17                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    GLY C1200         11.51                                           
REMARK 500    SER C1201        -42.74                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ITD A 1500                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ITD B 1500                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ITD C 1500                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: ATCG3D_11   RELATED DB: TARGETDB                         
REMARK 900 RELATED ID: 3ODU   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN AT 2.5 A IN P21 SPACEGROUP                              
REMARK 900 RELATED ID: 3OE0   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN IN COMPLEX WITH A CYCLIC PEPTIDE CVX15                  
REMARK 900 RELATED ID: 3OE6   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN IN I222 SPACEGROUP                                      
REMARK 900 RELATED ID: 3OE9   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN IN P1 SPACEGROUP WITH 2 MOLECULES PER ASYMMETRIC UNIT   
REMARK 900 RELATED ID: GPCR-34   RELATED DB: TARGETTRACK                        
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE PROTEIN IS A FUSION PROTEIN WITH RESIDUES ASN1002-TYR1161 OF T4  
REMARK 999 LYSOZYME INSERTED BETWEEN SER229 AND LYS230 OF CXCR4, AS INDICATED   
REMARK 999 AS CXCR4-2 IN THE PUBLICATION.                                       
DBREF  3OE8 A    2   229  UNP    P61073   CXCR4_HUMAN      2    229             
DBREF  3OE8 A 1002  1161  UNP    P00720   LYS_BPT4      1002   1161             
DBREF  3OE8 A  230   319  UNP    P61073   CXCR4_HUMAN    230    319             
DBREF  3OE8 B    2   229  UNP    P61073   CXCR4_HUMAN      2    229             
DBREF  3OE8 B 1002  1161  UNP    P00720   LYS_BPT4      1002   1161             
DBREF  3OE8 B  230   319  UNP    P61073   CXCR4_HUMAN    230    319             
DBREF  3OE8 C    2   229  UNP    P61073   CXCR4_HUMAN      2    229             
DBREF  3OE8 C 1002  1161  UNP    P00720   LYS_BPT4      1002   1161             
DBREF  3OE8 C  230   319  UNP    P61073   CXCR4_HUMAN    230    319             
SEQADV 3OE8 ASP A   -9  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 TYR A   -8  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 LYS A   -7  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 ASP A   -6  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 ASP A   -5  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 ASP A   -4  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 ASP A   -3  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 ALA A   -2  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 GLY A   -1  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 ALA A    0  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 PRO A    1  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 TRP A  125  UNP  P61073    LEU   125 ENGINEERED MUTATION            
SEQADV 3OE8 GLY A  900  UNP  P61073              LINKER                         
SEQADV 3OE8 SER A  901  UNP  P61073              LINKER                         
SEQADV 3OE8 GLY A 1200  UNP  P61073              LINKER                         
SEQADV 3OE8 SER A 1201  UNP  P61073              LINKER                         
SEQADV 3OE8 THR A 1054  UNP  P00720    CYS  1054 ENGINEERED MUTATION            
SEQADV 3OE8 ALA A 1097  UNP  P00720    CYS  1097 ENGINEERED MUTATION            
SEQADV 3OE8 GLY A  320  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 ARG A  321  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 PRO A  322  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 LEU A  323  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 GLU A  324  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 VAL A  325  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 LEU A  326  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 PHE A  327  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 GLN A  328  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 ASP B   -9  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 TYR B   -8  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 LYS B   -7  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 ASP B   -6  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 ASP B   -5  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 ASP B   -4  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 ASP B   -3  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 ALA B   -2  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 GLY B   -1  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 ALA B    0  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 PRO B    1  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 TRP B  125  UNP  P61073    LEU   125 ENGINEERED MUTATION            
SEQADV 3OE8 GLY B  900  UNP  P61073              LINKER                         
SEQADV 3OE8 SER B  901  UNP  P61073              LINKER                         
SEQADV 3OE8 GLY B 1200  UNP  P61073              LINKER                         
SEQADV 3OE8 SER B 1201  UNP  P61073              LINKER                         
SEQADV 3OE8 THR B 1054  UNP  P00720    CYS  1054 ENGINEERED MUTATION            
SEQADV 3OE8 ALA B 1097  UNP  P00720    CYS  1097 ENGINEERED MUTATION            
SEQADV 3OE8 GLY B  320  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 ARG B  321  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 PRO B  322  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 LEU B  323  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 GLU B  324  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 VAL B  325  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 LEU B  326  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 PHE B  327  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 GLN B  328  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 ASP C   -9  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 TYR C   -8  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 LYS C   -7  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 ASP C   -6  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 ASP C   -5  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 ASP C   -4  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 ASP C   -3  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 ALA C   -2  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 GLY C   -1  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 ALA C    0  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 PRO C    1  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 TRP C  125  UNP  P61073    LEU   125 ENGINEERED MUTATION            
SEQADV 3OE8 GLY C  900  UNP  P61073              LINKER                         
SEQADV 3OE8 SER C  901  UNP  P61073              LINKER                         
SEQADV 3OE8 GLY C 1200  UNP  P61073              LINKER                         
SEQADV 3OE8 SER C 1201  UNP  P61073              LINKER                         
SEQADV 3OE8 THR C 1054  UNP  P00720    CYS  1054 ENGINEERED MUTATION            
SEQADV 3OE8 ALA C 1097  UNP  P00720    CYS  1097 ENGINEERED MUTATION            
SEQADV 3OE8 GLY C  320  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 ARG C  321  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 PRO C  322  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 LEU C  323  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 GLU C  324  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 VAL C  325  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 LEU C  326  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 PHE C  327  UNP  P61073              EXPRESSION TAG                 
SEQADV 3OE8 GLN C  328  UNP  P61073              EXPRESSION TAG                 
SEQRES   1 A  502  ASP TYR LYS ASP ASP ASP ASP ALA GLY ALA PRO GLU GLY          
SEQRES   2 A  502  ILE SER ILE TYR THR SER ASP ASN TYR THR GLU GLU MET          
SEQRES   3 A  502  GLY SER GLY ASP TYR ASP SER MET LYS GLU PRO CYS PHE          
SEQRES   4 A  502  ARG GLU GLU ASN ALA ASN PHE ASN LYS ILE PHE LEU PRO          
SEQRES   5 A  502  THR ILE TYR SER ILE ILE PHE LEU THR GLY ILE VAL GLY          
SEQRES   6 A  502  ASN GLY LEU VAL ILE LEU VAL MET GLY TYR GLN LYS LYS          
SEQRES   7 A  502  LEU ARG SER MET THR ASP LYS TYR ARG LEU HIS LEU SER          
SEQRES   8 A  502  VAL ALA ASP LEU LEU PHE VAL ILE THR LEU PRO PHE TRP          
SEQRES   9 A  502  ALA VAL ASP ALA VAL ALA ASN TRP TYR PHE GLY ASN PHE          
SEQRES  10 A  502  LEU CYS LYS ALA VAL HIS VAL ILE TYR THR VAL ASN LEU          
SEQRES  11 A  502  TYR SER SER VAL TRP ILE LEU ALA PHE ILE SER LEU ASP          
SEQRES  12 A  502  ARG TYR LEU ALA ILE VAL HIS ALA THR ASN SER GLN ARG          
SEQRES  13 A  502  PRO ARG LYS LEU LEU ALA GLU LYS VAL VAL TYR VAL GLY          
SEQRES  14 A  502  VAL TRP ILE PRO ALA LEU LEU LEU THR ILE PRO ASP PHE          
SEQRES  15 A  502  ILE PHE ALA ASN VAL SER GLU ALA ASP ASP ARG TYR ILE          
SEQRES  16 A  502  CYS ASP ARG PHE TYR PRO ASN ASP LEU TRP VAL VAL VAL          
SEQRES  17 A  502  PHE GLN PHE GLN HIS ILE MET VAL GLY LEU ILE LEU PRO          
SEQRES  18 A  502  GLY ILE VAL ILE LEU SER CYS TYR CYS ILE ILE ILE SER          
SEQRES  19 A  502  LYS LEU SER HIS SER GLY SER ASN ILE PHE GLU MET LEU          
SEQRES  20 A  502  ARG ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP          
SEQRES  21 A  502  THR GLU GLY TYR TYR THR ILE GLY ILE GLY HIS LEU LEU          
SEQRES  22 A  502  THR LYS SER PRO SER LEU ASN ALA ALA LYS SER GLU LEU          
SEQRES  23 A  502  ASP LYS ALA ILE GLY ARG ASN THR ASN GLY VAL ILE THR          
SEQRES  24 A  502  LYS ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP          
SEQRES  25 A  502  ALA ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS          
SEQRES  26 A  502  PRO VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA          
SEQRES  27 A  502  LEU ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL          
SEQRES  28 A  502  ALA GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS          
SEQRES  29 A  502  ARG TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG          
SEQRES  30 A  502  TRP TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE          
SEQRES  31 A  502  THR THR PHE ARG THR GLY THR TRP ASP ALA TYR GLY SER          
SEQRES  32 A  502  LYS GLY HIS GLN LYS ARG LYS ALA LEU LYS THR THR VAL          
SEQRES  33 A  502  ILE LEU ILE LEU ALA PHE PHE ALA CYS TRP LEU PRO TYR          
SEQRES  34 A  502  TYR ILE GLY ILE SER ILE ASP SER PHE ILE LEU LEU GLU          
SEQRES  35 A  502  ILE ILE LYS GLN GLY CYS GLU PHE GLU ASN THR VAL HIS          
SEQRES  36 A  502  LYS TRP ILE SER ILE THR GLU ALA LEU ALA PHE PHE HIS          
SEQRES  37 A  502  CYS CYS LEU ASN PRO ILE LEU TYR ALA PHE LEU GLY ALA          
SEQRES  38 A  502  LYS PHE LYS THR SER ALA GLN HIS ALA LEU THR SER GLY          
SEQRES  39 A  502  ARG PRO LEU GLU VAL LEU PHE GLN                              
SEQRES   1 B  502  ASP TYR LYS ASP ASP ASP ASP ALA GLY ALA PRO GLU GLY          
SEQRES   2 B  502  ILE SER ILE TYR THR SER ASP ASN TYR THR GLU GLU MET          
SEQRES   3 B  502  GLY SER GLY ASP TYR ASP SER MET LYS GLU PRO CYS PHE          
SEQRES   4 B  502  ARG GLU GLU ASN ALA ASN PHE ASN LYS ILE PHE LEU PRO          
SEQRES   5 B  502  THR ILE TYR SER ILE ILE PHE LEU THR GLY ILE VAL GLY          
SEQRES   6 B  502  ASN GLY LEU VAL ILE LEU VAL MET GLY TYR GLN LYS LYS          
SEQRES   7 B  502  LEU ARG SER MET THR ASP LYS TYR ARG LEU HIS LEU SER          
SEQRES   8 B  502  VAL ALA ASP LEU LEU PHE VAL ILE THR LEU PRO PHE TRP          
SEQRES   9 B  502  ALA VAL ASP ALA VAL ALA ASN TRP TYR PHE GLY ASN PHE          
SEQRES  10 B  502  LEU CYS LYS ALA VAL HIS VAL ILE TYR THR VAL ASN LEU          
SEQRES  11 B  502  TYR SER SER VAL TRP ILE LEU ALA PHE ILE SER LEU ASP          
SEQRES  12 B  502  ARG TYR LEU ALA ILE VAL HIS ALA THR ASN SER GLN ARG          
SEQRES  13 B  502  PRO ARG LYS LEU LEU ALA GLU LYS VAL VAL TYR VAL GLY          
SEQRES  14 B  502  VAL TRP ILE PRO ALA LEU LEU LEU THR ILE PRO ASP PHE          
SEQRES  15 B  502  ILE PHE ALA ASN VAL SER GLU ALA ASP ASP ARG TYR ILE          
SEQRES  16 B  502  CYS ASP ARG PHE TYR PRO ASN ASP LEU TRP VAL VAL VAL          
SEQRES  17 B  502  PHE GLN PHE GLN HIS ILE MET VAL GLY LEU ILE LEU PRO          
SEQRES  18 B  502  GLY ILE VAL ILE LEU SER CYS TYR CYS ILE ILE ILE SER          
SEQRES  19 B  502  LYS LEU SER HIS SER GLY SER ASN ILE PHE GLU MET LEU          
SEQRES  20 B  502  ARG ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP          
SEQRES  21 B  502  THR GLU GLY TYR TYR THR ILE GLY ILE GLY HIS LEU LEU          
SEQRES  22 B  502  THR LYS SER PRO SER LEU ASN ALA ALA LYS SER GLU LEU          
SEQRES  23 B  502  ASP LYS ALA ILE GLY ARG ASN THR ASN GLY VAL ILE THR          
SEQRES  24 B  502  LYS ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP          
SEQRES  25 B  502  ALA ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS          
SEQRES  26 B  502  PRO VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA          
SEQRES  27 B  502  LEU ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL          
SEQRES  28 B  502  ALA GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS          
SEQRES  29 B  502  ARG TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG          
SEQRES  30 B  502  TRP TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE          
SEQRES  31 B  502  THR THR PHE ARG THR GLY THR TRP ASP ALA TYR GLY SER          
SEQRES  32 B  502  LYS GLY HIS GLN LYS ARG LYS ALA LEU LYS THR THR VAL          
SEQRES  33 B  502  ILE LEU ILE LEU ALA PHE PHE ALA CYS TRP LEU PRO TYR          
SEQRES  34 B  502  TYR ILE GLY ILE SER ILE ASP SER PHE ILE LEU LEU GLU          
SEQRES  35 B  502  ILE ILE LYS GLN GLY CYS GLU PHE GLU ASN THR VAL HIS          
SEQRES  36 B  502  LYS TRP ILE SER ILE THR GLU ALA LEU ALA PHE PHE HIS          
SEQRES  37 B  502  CYS CYS LEU ASN PRO ILE LEU TYR ALA PHE LEU GLY ALA          
SEQRES  38 B  502  LYS PHE LYS THR SER ALA GLN HIS ALA LEU THR SER GLY          
SEQRES  39 B  502  ARG PRO LEU GLU VAL LEU PHE GLN                              
SEQRES   1 C  502  ASP TYR LYS ASP ASP ASP ASP ALA GLY ALA PRO GLU GLY          
SEQRES   2 C  502  ILE SER ILE TYR THR SER ASP ASN TYR THR GLU GLU MET          
SEQRES   3 C  502  GLY SER GLY ASP TYR ASP SER MET LYS GLU PRO CYS PHE          
SEQRES   4 C  502  ARG GLU GLU ASN ALA ASN PHE ASN LYS ILE PHE LEU PRO          
SEQRES   5 C  502  THR ILE TYR SER ILE ILE PHE LEU THR GLY ILE VAL GLY          
SEQRES   6 C  502  ASN GLY LEU VAL ILE LEU VAL MET GLY TYR GLN LYS LYS          
SEQRES   7 C  502  LEU ARG SER MET THR ASP LYS TYR ARG LEU HIS LEU SER          
SEQRES   8 C  502  VAL ALA ASP LEU LEU PHE VAL ILE THR LEU PRO PHE TRP          
SEQRES   9 C  502  ALA VAL ASP ALA VAL ALA ASN TRP TYR PHE GLY ASN PHE          
SEQRES  10 C  502  LEU CYS LYS ALA VAL HIS VAL ILE TYR THR VAL ASN LEU          
SEQRES  11 C  502  TYR SER SER VAL TRP ILE LEU ALA PHE ILE SER LEU ASP          
SEQRES  12 C  502  ARG TYR LEU ALA ILE VAL HIS ALA THR ASN SER GLN ARG          
SEQRES  13 C  502  PRO ARG LYS LEU LEU ALA GLU LYS VAL VAL TYR VAL GLY          
SEQRES  14 C  502  VAL TRP ILE PRO ALA LEU LEU LEU THR ILE PRO ASP PHE          
SEQRES  15 C  502  ILE PHE ALA ASN VAL SER GLU ALA ASP ASP ARG TYR ILE          
SEQRES  16 C  502  CYS ASP ARG PHE TYR PRO ASN ASP LEU TRP VAL VAL VAL          
SEQRES  17 C  502  PHE GLN PHE GLN HIS ILE MET VAL GLY LEU ILE LEU PRO          
SEQRES  18 C  502  GLY ILE VAL ILE LEU SER CYS TYR CYS ILE ILE ILE SER          
SEQRES  19 C  502  LYS LEU SER HIS SER GLY SER ASN ILE PHE GLU MET LEU          
SEQRES  20 C  502  ARG ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP          
SEQRES  21 C  502  THR GLU GLY TYR TYR THR ILE GLY ILE GLY HIS LEU LEU          
SEQRES  22 C  502  THR LYS SER PRO SER LEU ASN ALA ALA LYS SER GLU LEU          
SEQRES  23 C  502  ASP LYS ALA ILE GLY ARG ASN THR ASN GLY VAL ILE THR          
SEQRES  24 C  502  LYS ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP          
SEQRES  25 C  502  ALA ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS          
SEQRES  26 C  502  PRO VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA          
SEQRES  27 C  502  LEU ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL          
SEQRES  28 C  502  ALA GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS          
SEQRES  29 C  502  ARG TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG          
SEQRES  30 C  502  TRP TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE          
SEQRES  31 C  502  THR THR PHE ARG THR GLY THR TRP ASP ALA TYR GLY SER          
SEQRES  32 C  502  LYS GLY HIS GLN LYS ARG LYS ALA LEU LYS THR THR VAL          
SEQRES  33 C  502  ILE LEU ILE LEU ALA PHE PHE ALA CYS TRP LEU PRO TYR          
SEQRES  34 C  502  TYR ILE GLY ILE SER ILE ASP SER PHE ILE LEU LEU GLU          
SEQRES  35 C  502  ILE ILE LYS GLN GLY CYS GLU PHE GLU ASN THR VAL HIS          
SEQRES  36 C  502  LYS TRP ILE SER ILE THR GLU ALA LEU ALA PHE PHE HIS          
SEQRES  37 C  502  CYS CYS LEU ASN PRO ILE LEU TYR ALA PHE LEU GLY ALA          
SEQRES  38 C  502  LYS PHE LYS THR SER ALA GLN HIS ALA LEU THR SER GLY          
SEQRES  39 C  502  ARG PRO LEU GLU VAL LEU PHE GLN                              
HET    ITD  A1500      27                                                       
HET    ITD  B1500      27                                                       
HET    ITD  C1500      27                                                       
HETNAM     ITD (6,6-DIMETHYL-5,6-DIHYDROIMIDAZO[2,1-B][1,3]THIAZOL-3-           
HETNAM   2 ITD  YL)METHYL N,N'-DICYCLOHEXYLIMIDOTHIOCARBAMATE                   
FORMUL   4  ITD    3(C21 H34 N4 S2)                                             
HELIX    1   1 PHE A   36  GLN A   66  1                                  31    
HELIX    2   2 SER A   71  ILE A   89  1                                  19    
HELIX    3   3 THR A   90  ALA A  100  1                                  11    
HELIX    4   4 GLY A  105  HIS A  140  1                                  36    
HELIX    5   5 SER A  144  LYS A  154  1                                  11    
HELIX    6   6 LYS A  154  VAL A  160  1                                   7    
HELIX    7   7 VAL A  160  LEU A  167  1                                   8    
HELIX    8   8 THR A  168  PHE A  174  1                                   7    
HELIX    9   9 ASN A  192  LEU A  208  1                                  17    
HELIX   10  10 LEU A  208  LEU A  226  1                                  19    
HELIX   11  11 ILE A 1003  GLU A 1011  1                                   9    
HELIX   12  12 SER A 1038  GLY A 1051  1                                  14    
HELIX   13  13 THR A 1059  LEU A 1079  1                                  21    
HELIX   14  14 LEU A 1084  SER A 1090  1                                   7    
HELIX   15  15 ASP A 1092  MET A 1106  1                                  15    
HELIX   16  16 GLY A 1107  ALA A 1112  1                                   6    
HELIX   17  17 THR A 1115  GLN A 1123  1                                   9    
HELIX   18  18 ARG A 1125  LYS A 1135  1                                  11    
HELIX   19  19 SER A 1136  THR A 1142  1                                   7    
HELIX   20  20 THR A 1142  GLY A 1156  1                                  15    
HELIX   21  21 GLN A  233  GLU A  268  1                                  36    
HELIX   22  22 GLY A  273  PHE A  292  1                                  20    
HELIX   23  23 PHE A  293  LEU A  305  1                                  13    
HELIX   24  24 PHE B   36  MET B   63  1                                  28    
HELIX   25  25 SER B   71  ILE B   89  1                                  19    
HELIX   26  26 THR B   90  ALA B  100  1                                  11    
HELIX   27  27 PHE B  104  VAL B  139  1                                  36    
HELIX   28  28 PRO B  147  LYS B  154  1                                   8    
HELIX   29  29 LYS B  154  VAL B  160  1                                   7    
HELIX   30  30 VAL B  160  LEU B  167  1                                   8    
HELIX   31  31 THR B  168  PHE B  174  1                                   7    
HELIX   32  32 ASN B  192  LEU B  208  1                                  17    
HELIX   33  33 LEU B  208  LEU B  226  1                                  19    
HELIX   34  34 ASN B 1002  GLU B 1011  1                                  10    
HELIX   35  35 LEU B 1039  GLY B 1051  1                                  13    
HELIX   36  36 THR B 1059  ASN B 1081  1                                  23    
HELIX   37  37 LEU B 1084  LEU B 1091  1                                   8    
HELIX   38  38 ASP B 1092  GLY B 1107  1                                  16    
HELIX   39  39 GLY B 1107  GLY B 1113  1                                   7    
HELIX   40  40 PHE B 1114  GLN B 1123  1                                  10    
HELIX   41  41 ARG B 1125  SER B 1136  1                                  12    
HELIX   42  42 SER B 1136  THR B 1142  1                                   7    
HELIX   43  43 THR B 1142  GLY B 1156  1                                  15    
HELIX   44  44 HIS B  232  SER B  263  1                                  32    
HELIX   45  45 GLY B  273  PHE B  292  1                                  20    
HELIX   46  46 PHE B  293  CYS B  295  5                                   3    
HELIX   47  47 CYS B  296  ALA B  303  1                                   8    
HELIX   48  48 PHE C   36  GLY C   64  1                                  29    
HELIX   49  49 SER C   71  ILE C   89  1                                  19    
HELIX   50  50 THR C   90  ALA C  100  1                                  11    
HELIX   51  51 PHE C  104  VAL C  139  1                                  36    
HELIX   52  52 ARG C  146  LYS C  154  1                                   9    
HELIX   53  53 LYS C  154  VAL C  160  1                                   7    
HELIX   54  54 VAL C  160  LEU C  167  1                                   8    
HELIX   55  55 THR C  168  PHE C  174  1                                   7    
HELIX   56  56 ASN C  192  LEU C  208  1                                  17    
HELIX   57  57 LEU C  208  LYS C  225  1                                  18    
HELIX   58  58 ASN C 1002  GLU C 1011  1                                  10    
HELIX   59  59 ALA C 1041  GLY C 1051  1                                  11    
HELIX   60  60 THR C 1059  ASN C 1081  1                                  23    
HELIX   61  61 LYS C 1083  LEU C 1091  1                                   9    
HELIX   62  62 ASP C 1092  MET C 1106  1                                  15    
HELIX   63  63 GLY C 1107  ALA C 1112  1                                   6    
HELIX   64  64 PHE C 1114  GLN C 1123  1                                  10    
HELIX   65  65 ARG C 1125  LYS C 1135  1                                  11    
HELIX   66  66 SER C 1136  THR C 1142  1                                   7    
HELIX   67  67 THR C 1142  GLY C 1156  1                                  15    
HELIX   68  68 THR C 1157  TYR C 1161  5                                   5    
HELIX   69  69 HIS C  232  LEU C  267  1                                  36    
HELIX   70  70 GLY C  273  PHE C  292  1                                  20    
HELIX   71  71 PHE C  293  LEU C  305  1                                  13    
SHEET    1   A 2 ALA A 175  ALA A 180  0                                        
SHEET    2   A 2 ARG A 183  ARG A 188 -1  O  ILE A 185   N  SER A 178           
SHEET    1   B 3 ARG A1014  LYS A1019  0                                        
SHEET    2   B 3 TYR A1025  GLY A1028 -1  O  THR A1026   N  TYR A1018           
SHEET    3   B 3 HIS A1031  THR A1034 -1  O  LEU A1033   N  TYR A1025           
SHEET    1   C 2 ALA B 175  GLU B 179  0                                        
SHEET    2   C 2 TYR B 184  ARG B 188 -1  O  ILE B 185   N  SER B 178           
SHEET    1   D 3 ARG B1014  LYS B1019  0                                        
SHEET    2   D 3 TYR B1025  GLY B1028 -1  O  THR B1026   N  TYR B1018           
SHEET    3   D 3 HIS B1031  LEU B1032 -1  O  HIS B1031   N  ILE B1027           
SHEET    1   E 2 ALA C 175  SER C 178  0                                        
SHEET    2   E 2 ILE C 185  ARG C 188 -1  O  ILE C 185   N  SER C 178           
SHEET    1   F 3 TYR C1018  LYS C1019  0                                        
SHEET    2   F 3 TYR C1025  ILE C1027 -1  O  THR C1026   N  TYR C1018           
SHEET    3   F 3 HIS C1031  LEU C1032 -1  O  HIS C1031   N  ILE C1027           
SSBOND   1 CYS A   28    CYS A  274                          1555   1555  1.98  
SSBOND   2 CYS A  109    CYS A  186                          1555   1555  2.03  
SSBOND   3 CYS B   28    CYS B  274                          1555   1555  2.04  
SSBOND   4 CYS B  109    CYS B  186                          1555   1555  2.04  
SSBOND   5 CYS C   28    CYS C  274                          1555   1555  2.04  
SSBOND   6 CYS C  109    CYS C  186                          1555   1555  2.03  
LINK         C   SER A 229                 N   GLY A 900     1555   1555  1.28  
LINK         C   SER A 901                 N   ASN A1002     1555   1555  1.33  
LINK         N   LYS B 230                 C   SER B1201     1555   1555  1.33  
LINK         C   TYR B1161                 N   GLY B1200     1555   1555  1.38  
LINK         N   LYS C 230                 C   SER C1201     1555   1555  1.40  
LINK         C   TYR C1161                 N   GLY C1200     1555   1555  1.31  
SITE     1 AC1  8 TRP A  94  ASP A  97  TRP A 102  VAL A 112                    
SITE     2 AC1  8 TYR A 116  CYS A 186  ASP A 187  GLU A 288                    
SITE     1 AC2  9 TRP B  94  ASP B  97  TYR B 116  ARG B 183                    
SITE     2 AC2  9 ILE B 185  CYS B 186  ASP B 187  ARG B 188                    
SITE     3 AC2  9 GLU B 288                                                     
SITE     1 AC3  7 TRP C  94  ASP C  97  TYR C 116  ARG C 183                    
SITE     2 AC3  7 CYS C 186  ASP C 187  GLU C 288                               
CRYST1   69.369   76.602   91.719  96.00  97.78  97.38 P 1           3          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014416  0.001867  0.002218        0.00000                         
SCALE2      0.000000  0.013164  0.001646        0.00000                         
SCALE3      0.000000  0.000000  0.011090        0.00000                         
ATOM      1  N   PRO A  27     -25.974  -7.973   4.062  1.00127.64           N  
ANISOU    1  N   PRO A  27    15707  23199   9592  -2134    729   -426       N  
ATOM      2  CA  PRO A  27     -27.054  -7.090   3.590  1.00128.42           C  
ANISOU    2  CA  PRO A  27    15629  23694   9471  -2211    476   -124       C  
ATOM      3  C   PRO A  27     -28.318  -7.215   4.442  1.00130.42           C  
ANISOU    3  C   PRO A  27    15768  23898   9889  -2321    212   -116       C  
ATOM      4  O   PRO A  27     -28.633  -6.283   5.186  1.00127.66           O  
ANISOU    4  O   PRO A  27    15213  23463   9831  -2189    107    197       O  
ATOM      5  CB  PRO A  27     -27.256  -7.519   2.130  1.00134.75           C  
ANISOU    5  CB  PRO A  27    16579  24928   9694  -2395    481   -277       C  
ATOM      6  CG  PRO A  27     -25.953  -8.158   1.737  1.00140.45           C  
ANISOU    6  CG  PRO A  27    17516  25482  10367  -2321    809   -532       C  
ATOM      7  CD  PRO A  27     -25.467  -8.842   2.983  1.00132.87           C  
ANISOU    7  CD  PRO A  27    16611  24000   9873  -2232    916   -739       C  
ATOM      8  N   CYS A  28     -29.016  -8.372   4.346  1.00128.28           N  
ANISOU    8  N   CYS A  28    15635  23665   9440  -2566    122   -467       N  
ATOM      9  CA  CYS A  28     -30.227  -8.756   5.084  1.00127.20           C  
ANISOU    9  CA  CYS A  28    15416  23488   9425  -2721   -106   -531       C  
ATOM     10  C   CYS A  28     -31.235  -7.631   5.327  1.00130.26           C  
ANISOU   10  C   CYS A  28    15508  24102   9882  -2674   -348   -123       C  
ATOM     11  O   CYS A  28     -31.830  -7.123   4.379  1.00132.70           O  
ANISOU   11  O   CYS A  28    15715  24860   9846  -2750   -495     62       O  
ATOM     12  CB  CYS A  28     -29.864  -9.478   6.379  1.00124.49           C  
ANISOU   12  CB  CYS A  28    15161  22626   9513  -2661      0   -739       C  
ATOM     13  SG  CYS A  28     -31.119 -10.653   6.964  1.00128.87           S  
ANISOU   13  SG  CYS A  28    15770  23101  10093  -2952   -179  -1038       S  
ATOM     14  N   ASN A  35     -43.730  -2.132  12.753  1.00129.42           N  
ANISOU   14  N   ASN A  35    12536  24743  11896  -2148  -1960   2500       N  
ATOM     15  CA  ASN A  35     -44.940  -1.339  12.543  1.00131.86           C  
ANISOU   15  CA  ASN A  35    12474  25425  12201  -2044  -2111   2893       C  
ATOM     16  C   ASN A  35     -45.777  -1.202  13.818  1.00134.02           C  
ANISOU   16  C   ASN A  35    12575  25514  12834  -1937  -2061   2980       C  
ATOM     17  O   ASN A  35     -46.244  -0.101  14.112  1.00134.25           O  
ANISOU   17  O   ASN A  35    12395  25564  13051  -1654  -2031   3346       O  
ATOM     18  CB  ASN A  35     -45.778  -1.900  11.384  1.00137.46           C  
ANISOU   18  CB  ASN A  35    13007  26717  12505  -2341  -2375   2883       C  
ATOM     19  CG  ASN A  35     -46.954  -1.033  10.981  1.00166.96           C  
ANISOU   19  CG  ASN A  35    16336  30906  16194  -2220  -2552   3333       C  
ATOM     20  OD1 ASN A  35     -48.109  -1.476  10.973  1.00167.37           O  
ANISOU   20  OD1 ASN A  35    16124  31279  16189  -2407  -2732   3355       O  
ATOM     21  ND2 ASN A  35     -46.688   0.216  10.611  1.00157.87           N  
ANISOU   21  ND2 ASN A  35    15115  29801  15069  -1908  -2506   3716       N  
ATOM     22  N   PHE A  36     -45.984  -2.314  14.560  1.00128.47           N  
ANISOU   22  N   PHE A  36    11960  24630  12224  -2158  -2039   2653       N  
ATOM     23  CA  PHE A  36     -46.738  -2.304  15.819  1.00126.58           C  
ANISOU   23  CA  PHE A  36    11582  24203  12311  -2079  -1968   2703       C  
ATOM     24  C   PHE A  36     -45.855  -1.795  16.962  1.00123.99           C  
ANISOU   24  C   PHE A  36    11475  23321  12314  -1804  -1720   2678       C  
ATOM     25  O   PHE A  36     -46.374  -1.208  17.912  1.00122.35           O  
ANISOU   25  O   PHE A  36    11139  22965  12384  -1600  -1629   2854       O  
ATOM     26  CB  PHE A  36     -47.341  -3.687  16.141  1.00129.33           C  
ANISOU   26  CB  PHE A  36    11931  24587  12620  -2437  -2040   2388       C  
ATOM     27  CG  PHE A  36     -48.210  -3.724  17.380  1.00130.34           C  
ANISOU   27  CG  PHE A  36    11892  24574  13057  -2379  -1967   2456       C  
ATOM     28  CD1 PHE A  36     -49.536  -3.308  17.335  1.00136.20           C  
ANISOU   28  CD1 PHE A  36    12230  25687  13832  -2352  -2088   2753       C  
ATOM     29  CD2 PHE A  36     -47.700  -4.173  18.595  1.00129.33           C  
ANISOU   29  CD2 PHE A  36    12002  23957  13180  -2342  -1773   2237       C  
ATOM     30  CE1 PHE A  36     -50.334  -3.337  18.482  1.00136.60           C  
ANISOU   30  CE1 PHE A  36    12121  25613  14167  -2289  -1995   2821       C  
ATOM     31  CE2 PHE A  36     -48.500  -4.198  19.741  1.00131.57           C  
ANISOU   31  CE2 PHE A  36    12142  24121  13727  -2285  -1690   2306       C  
ATOM     32  CZ  PHE A  36     -49.810  -3.783  19.675  1.00132.41           C  
ANISOU   32  CZ  PHE A  36    11851  24592  13867  -2259  -1792   2592       C  
ATOM     33  N   ASN A  37     -44.526  -1.988  16.847  1.00117.22           N  
ANISOU   33  N   ASN A  37    10940  22178  11420  -1797  -1611   2466       N  
ATOM     34  CA  ASN A  37     -43.535  -1.519  17.819  1.00113.15           C  
ANISOU   34  CA  ASN A  37    10646  21162  11182  -1565  -1399   2426       C  
ATOM     35  C   ASN A  37     -43.517   0.015  17.908  1.00116.38           C  
ANISOU   35  C   ASN A  37    10940  21526  11754  -1221  -1328   2805       C  
ATOM     36  O   ASN A  37     -43.135   0.560  18.944  1.00113.05           O  
ANISOU   36  O   ASN A  37    10617  20722  11613  -1016  -1167   2831       O  
ATOM     37  CB  ASN A  37     -42.139  -2.057  17.475  1.00111.60           C  
ANISOU   37  CB  ASN A  37    10772  20752  10879  -1646  -1322   2148       C  
ATOM     38  CG  ASN A  37     -41.918  -3.520  17.792  1.00132.51           C  
ANISOU   38  CG  ASN A  37    13614  23248  13486  -1911  -1308   1750       C  
ATOM     39  OD1 ASN A  37     -42.845  -4.280  18.099  1.00130.29           O  
ANISOU   39  OD1 ASN A  37    13234  23067  13203  -2102  -1382   1651       O  
ATOM     40  ND2 ASN A  37     -40.670  -3.951  17.711  1.00121.75           N  
ANISOU   40  ND2 ASN A  37    12528  21633  12097  -1927  -1203   1521       N  
ATOM     41  N   LYS A  38     -43.970   0.703  16.832  1.00115.95           N  
ANISOU   41  N   LYS A  38    10677  21863  11517  -1163  -1449   3103       N  
ATOM     42  CA  LYS A  38     -44.082   2.164  16.748  1.00116.42           C  
ANISOU   42  CA  LYS A  38    10602  21921  11710   -840  -1391   3505       C  
ATOM     43  C   LYS A  38     -45.058   2.718  17.798  1.00120.89           C  
ANISOU   43  C   LYS A  38    10974  22384  12574   -644  -1323   3696       C  
ATOM     44  O   LYS A  38     -44.923   3.874  18.192  1.00120.57           O  
ANISOU   44  O   LYS A  38    10926  22132  12752   -347  -1191   3937       O  
ATOM     45  CB  LYS A  38     -44.514   2.589  15.343  1.00122.06           C  
ANISOU   45  CB  LYS A  38    11112  23135  12131   -852  -1562   3786       C  
ATOM     46  CG  LYS A  38     -43.389   2.661  14.323  1.00133.03           C  
ANISOU   46  CG  LYS A  38    12699  24563  13283   -897  -1554   3740       C  
ATOM     47  CD  LYS A  38     -43.904   3.142  12.973  1.00143.85           C  
ANISOU   47  CD  LYS A  38    13855  26452  14347   -893  -1724   4056       C  
ATOM     48  CE  LYS A  38     -42.799   3.448  11.999  1.00151.80           C  
ANISOU   48  CE  LYS A  38    15047  27487  15144   -879  -1679   4084       C  
ATOM     49  NZ  LYS A  38     -43.330   4.012  10.729  1.00163.55           N  
ANISOU   49  NZ  LYS A  38    16325  29485  16330   -847  -1840   4438       N  
ATOM     50  N   ILE A  39     -46.040   1.893  18.233  1.00117.92           N  
ANISOU   50  N   ILE A  39    10445  22153  12204   -814  -1399   3586       N  
ATOM     51  CA  ILE A  39     -47.017   2.201  19.285  1.00117.87           C  
ANISOU   51  CA  ILE A  39    10253  22067  12467   -665  -1320   3720       C  
ATOM     52  C   ILE A  39     -46.588   1.450  20.557  1.00118.30           C  
ANISOU   52  C   ILE A  39    10553  21697  12701   -745  -1176   3382       C  
ATOM     53  O   ILE A  39     -46.568   2.047  21.629  1.00116.80           O  
ANISOU   53  O   ILE A  39    10417  21183  12780   -521  -1003   3438       O  
ATOM     54  CB  ILE A  39     -48.478   1.843  18.872  1.00124.81           C  
ANISOU   54  CB  ILE A  39    10746  23443  13232   -800  -1504   3876       C  
ATOM     55  CG1 ILE A  39     -48.946   2.675  17.657  1.00129.10           C  
ANISOU   55  CG1 ILE A  39    11023  24429  13600   -686  -1655   4262       C  
ATOM     56  CG2 ILE A  39     -49.455   1.994  20.059  1.00125.70           C  
ANISOU   56  CG2 ILE A  39    10676  23452  13632   -669  -1391   3971       C  
ATOM     57  CD1 ILE A  39     -50.180   2.098  16.890  1.00138.59           C  
ANISOU   57  CD1 ILE A  39    11863  26224  14572   -921  -1913   4362       C  
ATOM     58  N   PHE A  40     -46.229   0.151  20.421  1.00113.48           N  
ANISOU   58  N   PHE A  40    10101  21083  11932  -1058  -1244   3033       N  
ATOM     59  CA  PHE A  40     -45.812  -0.744  21.508  1.00110.36           C  
ANISOU   59  CA  PHE A  40     9942  20322  11667  -1169  -1131   2709       C  
ATOM     60  C   PHE A  40     -44.592  -0.288  22.318  1.00109.48           C  
ANISOU   60  C   PHE A  40    10133  19723  11742   -976   -946   2613       C  
ATOM     61  O   PHE A  40     -44.619  -0.412  23.543  1.00107.70           O  
ANISOU   61  O   PHE A  40    10001  19200  11720   -912   -818   2521       O  
ATOM     62  CB  PHE A  40     -45.630  -2.184  21.001  1.00112.72           C  
ANISOU   62  CB  PHE A  40    10358  20726  11743  -1535  -1241   2380       C  
ATOM     63  CG  PHE A  40     -45.467  -3.228  22.081  1.00112.66           C  
ANISOU   63  CG  PHE A  40    10542  20400  11865  -1673  -1142   2084       C  
ATOM     64  CD1 PHE A  40     -44.252  -3.875  22.267  1.00113.65           C  
ANISOU   64  CD1 PHE A  40    11001  20204  11978  -1740  -1064   1797       C  
ATOM     65  CD2 PHE A  40     -46.533  -3.575  22.905  1.00115.78           C  
ANISOU   65  CD2 PHE A  40    10773  20823  12396  -1730  -1121   2111       C  
ATOM     66  CE1 PHE A  40     -44.107  -4.858  23.253  1.00113.11           C  
ANISOU   66  CE1 PHE A  40    11107  19844  12024  -1856   -975   1550       C  
ATOM     67  CE2 PHE A  40     -46.382  -4.543  23.904  1.00117.10           C  
ANISOU   67  CE2 PHE A  40    11125  20693  12674  -1856  -1022   1860       C  
ATOM     68  CZ  PHE A  40     -45.171  -5.179  24.069  1.00112.96           C  
ANISOU   68  CZ  PHE A  40    10940  19849  12130  -1915   -954   1586       C  
ATOM     69  N   LEU A  41     -43.524   0.203  21.655  1.00103.98           N  
ANISOU   69  N   LEU A  41     9586  18955  10968   -901   -934   2629       N  
ATOM     70  CA  LEU A  41     -42.320   0.678  22.355  1.00100.42           C  
ANISOU   70  CA  LEU A  41     9398  18067  10690   -739   -776   2548       C  
ATOM     71  C   LEU A  41     -42.547   1.995  23.124  1.00102.27           C  
ANISOU   71  C   LEU A  41     9578  18102  11179   -431   -646   2795       C  
ATOM     72  O   LEU A  41     -42.253   2.002  24.323  1.00100.58           O  
ANISOU   72  O   LEU A  41     9517  17541  11155   -356   -519   2674       O  
ATOM     73  CB  LEU A  41     -41.059   0.737  21.465  1.00 99.90           C  
ANISOU   73  CB  LEU A  41     9504  17972  10481   -771   -785   2476       C  
ATOM     74  CG  LEU A  41     -40.531  -0.593  20.905  1.00104.47           C  
ANISOU   74  CG  LEU A  41    10229  18621  10844  -1045   -851   2164       C  
ATOM     75  CD1 LEU A  41     -39.597  -0.349  19.740  1.00105.39           C  
ANISOU   75  CD1 LEU A  41    10425  18845  10773  -1054   -869   2185       C  
ATOM     76  CD2 LEU A  41     -39.823  -1.423  21.978  1.00103.67           C  
ANISOU   76  CD2 LEU A  41    10370  18137  10882  -1102   -750   1866       C  
ATOM     77  N   PRO A  42     -43.122   3.087  22.537  1.00 98.49           N  
ANISOU   77  N   PRO A  42     8888  17822  10711   -246   -665   3139       N  
ATOM     78  CA  PRO A  42     -43.377   4.289  23.351  1.00 97.36           C  
ANISOU   78  CA  PRO A  42     8718  17442  10832     52   -512   3350       C  
ATOM     79  C   PRO A  42     -44.422   4.056  24.448  1.00 98.71           C  
ANISOU   79  C   PRO A  42     8779  17570  11156     93   -443   3337       C  
ATOM     80  O   PRO A  42     -44.421   4.793  25.432  1.00 96.94           O  
ANISOU   80  O   PRO A  42     8632  17045  11155    304   -278   3387       O  
ATOM     81  CB  PRO A  42     -43.835   5.327  22.324  1.00102.01           C  
ANISOU   81  CB  PRO A  42     9087  18301  11371    218   -562   3729       C  
ATOM     82  CG  PRO A  42     -44.401   4.537  21.228  1.00108.61           C  
ANISOU   82  CG  PRO A  42     9732  19611  11923     -4   -767   3740       C  
ATOM     83  CD  PRO A  42     -43.559   3.300  21.141  1.00102.43           C  
ANISOU   83  CD  PRO A  42     9176  18758  10984   -286   -817   3359       C  
ATOM     84  N   THR A  43     -45.281   3.015  24.297  1.00 95.34           N  
ANISOU   84  N   THR A  43     8186  17433  10606   -122   -559   3256       N  
ATOM     85  CA  THR A  43     -46.273   2.624  25.305  1.00 95.18           C  
ANISOU   85  CA  THR A  43     8051  17400  10714   -128   -492   3229       C  
ATOM     86  C   THR A  43     -45.530   2.158  26.558  1.00 94.55           C  
ANISOU   86  C   THR A  43     8280  16892  10754   -154   -356   2941       C  
ATOM     87  O   THR A  43     -45.780   2.691  27.639  1.00 93.80           O  
ANISOU   87  O   THR A  43     8223  16563  10853     33   -193   2985       O  
ATOM     88  CB  THR A  43     -47.255   1.559  24.759  1.00106.05           C  
ANISOU   88  CB  THR A  43     9186  19187  11920   -402   -662   3194       C  
ATOM     89  OG1 THR A  43     -47.991   2.117  23.672  1.00110.72           O  
ANISOU   89  OG1 THR A  43     9469  20195  12403   -348   -795   3498       O  
ATOM     90  CG2 THR A  43     -48.241   1.060  25.813  1.00103.60           C  
ANISOU   90  CG2 THR A  43     8757  18861  11746   -439   -582   3157       C  
ATOM     91  N   ILE A  44     -44.589   1.202  26.389  1.00 88.04           N  
ANISOU   91  N   ILE A  44     7679  15967   9805   -372   -416   2657       N  
ATOM     92  CA  ILE A  44     -43.746   0.640  27.447  1.00 84.77           C  
ANISOU   92  CA  ILE A  44     7561  15176   9471   -417   -317   2384       C  
ATOM     93  C   ILE A  44     -42.915   1.760  28.091  1.00 86.75           C  
ANISOU   93  C   ILE A  44     7996  15077   9888   -169   -180   2432       C  
ATOM     94  O   ILE A  44     -42.884   1.867  29.322  1.00 84.74           O  
ANISOU   94  O   ILE A  44     7871  14552   9777    -78    -51   2356       O  
ATOM     95  CB  ILE A  44     -42.872  -0.526  26.888  1.00 86.65           C  
ANISOU   95  CB  ILE A  44     7972  15414   9537   -673   -415   2115       C  
ATOM     96  CG1 ILE A  44     -43.743  -1.747  26.519  1.00 88.36           C  
ANISOU   96  CG1 ILE A  44     8053  15903   9616   -949   -525   2013       C  
ATOM     97  CG2 ILE A  44     -41.743  -0.926  27.859  1.00 84.90           C  
ANISOU   97  CG2 ILE A  44     8064  14793   9403   -670   -319   1876       C  
ATOM     98  CD1 ILE A  44     -43.019  -2.837  25.807  1.00 94.14           C  
ANISOU   98  CD1 ILE A  44     8940  16662  10167  -1194   -613   1763       C  
ATOM     99  N   TYR A  45     -42.288   2.615  27.247  1.00 83.46           N  
ANISOU   99  N   TYR A  45     7587  14678   9445    -70   -206   2566       N  
ATOM    100  CA  TYR A  45     -41.469   3.744  27.692  1.00 82.14           C  
ANISOU  100  CA  TYR A  45     7584  14190   9434    137    -87   2622       C  
ATOM    101  C   TYR A  45     -42.236   4.750  28.544  1.00 86.22           C  
ANISOU  101  C   TYR A  45     8038  14572  10150    383     61   2797       C  
ATOM    102  O   TYR A  45     -41.642   5.326  29.453  1.00 85.29           O  
ANISOU  102  O   TYR A  45     8124  14107  10175    500    185   2724       O  
ATOM    103  CB  TYR A  45     -40.798   4.456  26.512  1.00 84.09           C  
ANISOU  103  CB  TYR A  45     7817  14522   9613    182   -138   2772       C  
ATOM    104  CG  TYR A  45     -39.782   3.632  25.750  1.00 85.41           C  
ANISOU  104  CG  TYR A  45     8100  14749   9602    -22   -236   2584       C  
ATOM    105  CD1 TYR A  45     -39.002   2.676  26.397  1.00 85.43           C  
ANISOU  105  CD1 TYR A  45     8310  14548   9601   -159   -226   2285       C  
ATOM    106  CD2 TYR A  45     -39.544   3.862  24.397  1.00 87.66           C  
ANISOU  106  CD2 TYR A  45     8298  15282   9728    -55   -321   2717       C  
ATOM    107  CE1 TYR A  45     -38.045   1.935  25.705  1.00 85.99           C  
ANISOU  107  CE1 TYR A  45     8489  14657   9528   -318   -289   2117       C  
ATOM    108  CE2 TYR A  45     -38.586   3.130  23.696  1.00 87.81           C  
ANISOU  108  CE2 TYR A  45     8435  15349   9581   -226   -382   2539       C  
ATOM    109  CZ  TYR A  45     -37.836   2.170  24.355  1.00 93.79           C  
ANISOU  109  CZ  TYR A  45     9391  15891  10355   -351   -359   2236       C  
ATOM    110  OH  TYR A  45     -36.895   1.442  23.669  1.00 94.50           O  
ANISOU  110  OH  TYR A  45     9593  16017  10296   -496   -396   2064       O  
ATOM    111  N   SER A  46     -43.539   4.960  28.264  1.00 83.64           N  
ANISOU  111  N   SER A  46     7429  14521   9831    460     52   3021       N  
ATOM    112  CA  SER A  46     -44.376   5.887  29.027  1.00 84.18           C  
ANISOU  112  CA  SER A  46     7409  14483  10092    716    214   3204       C  
ATOM    113  C   SER A  46     -44.702   5.320  30.403  1.00 85.71           C  
ANISOU  113  C   SER A  46     7705  14497  10362    691    328   3015       C  
ATOM    114  O   SER A  46     -44.713   6.072  31.377  1.00 84.95           O  
ANISOU  114  O   SER A  46     7732  14119  10426    886    504   3023       O  
ATOM    115  CB  SER A  46     -45.653   6.221  28.266  1.00 90.87           C  
ANISOU  115  CB  SER A  46     7891  15712  10922    810    163   3519       C  
ATOM    116  OG  SER A  46     -45.349   6.797  27.005  1.00100.52           O  
ANISOU  116  OG  SER A  46     9029  17107  12059    848     62   3720       O  
ATOM    117  N   ILE A  47     -44.932   3.988  30.484  1.00 81.02           N  
ANISOU  117  N   ILE A  47     7083  14053   9646    444    234   2837       N  
ATOM    118  CA  ILE A  47     -45.218   3.260  31.727  1.00 79.85           C  
ANISOU  118  CA  ILE A  47     7036  13763   9541    381    330   2658       C  
ATOM    119  C   ILE A  47     -44.005   3.377  32.663  1.00 82.68           C  
ANISOU  119  C   ILE A  47     7755  13711   9950    410    412   2439       C  
ATOM    120  O   ILE A  47     -44.175   3.663  33.848  1.00 82.31           O  
ANISOU  120  O   ILE A  47     7826  13444  10004    530    568   2392       O  
ATOM    121  CB  ILE A  47     -45.611   1.773  31.447  1.00 82.63           C  
ANISOU  121  CB  ILE A  47     7296  14350   9748     81    200   2519       C  
ATOM    122  CG1 ILE A  47     -46.894   1.674  30.587  1.00 85.85           C  
ANISOU  122  CG1 ILE A  47     7322  15193  10104     30    104   2736       C  
ATOM    123  CG2 ILE A  47     -45.764   0.972  32.754  1.00 81.62           C  
ANISOU  123  CG2 ILE A  47     7310  14039   9663      5    307   2334       C  
ATOM    124  CD1 ILE A  47     -47.101   0.356  29.800  1.00 92.55           C  
ANISOU  124  CD1 ILE A  47     8075  16322  10767   -307    -81   2609       C  
ATOM    125  N   ILE A  48     -42.789   3.184  32.112  1.00 78.20           N  
ANISOU  125  N   ILE A  48     7350  13060   9303    304    308   2313       N  
ATOM    126  CA  ILE A  48     -41.535   3.268  32.859  1.00 75.95           C  
ANISOU  126  CA  ILE A  48     7374  12428   9055    309    350   2117       C  
ATOM    127  C   ILE A  48     -41.238   4.710  33.259  1.00 80.31           C  
ANISOU  127  C   ILE A  48     8024  12734   9757    542    476   2220       C  
ATOM    128  O   ILE A  48     -40.887   4.943  34.413  1.00 79.50           O  
ANISOU  128  O   ILE A  48     8129  12352   9725    605    580   2095       O  
ATOM    129  CB  ILE A  48     -40.363   2.540  32.142  1.00 77.52           C  
ANISOU  129  CB  ILE A  48     7685  12635   9135    123    212   1960       C  
ATOM    130  CG1 ILE A  48     -40.725   1.056  31.923  1.00 78.18           C  
ANISOU  130  CG1 ILE A  48     7713  12906   9086   -109    121   1826       C  
ATOM    131  CG2 ILE A  48     -39.056   2.644  32.952  1.00 76.08           C  
ANISOU  131  CG2 ILE A  48     7788  12115   9003    133    245   1778       C  
ATOM    132  CD1 ILE A  48     -40.007   0.366  30.822  1.00 88.03           C  
ANISOU  132  CD1 ILE A  48     8976  14279  10193   -281    -11   1733       C  
ATOM    133  N   PHE A  49     -41.443   5.674  32.339  1.00 78.39           N  
ANISOU  133  N   PHE A  49     7634  12593   9557    670    473   2453       N  
ATOM    134  CA  PHE A  49     -41.226   7.098  32.604  1.00 79.32           C  
ANISOU  134  CA  PHE A  49     7839  12463   9836    894    606   2575       C  
ATOM    135  C   PHE A  49     -42.077   7.595  33.778  1.00 84.74           C  
ANISOU  135  C   PHE A  49     8551  12996  10651   1077    796   2600       C  
ATOM    136  O   PHE A  49     -41.521   8.127  34.732  1.00 83.60           O  
ANISOU  136  O   PHE A  49     8651  12522  10589   1148    907   2473       O  
ATOM    137  CB  PHE A  49     -41.445   7.960  31.341  1.00 82.95           C  
ANISOU  137  CB  PHE A  49     8110  13092  10316   1005    573   2863       C  
ATOM    138  CG  PHE A  49     -41.389   9.447  31.600  1.00 86.21           C  
ANISOU  138  CG  PHE A  49     8600  13235  10919   1252    735   3019       C  
ATOM    139  CD1 PHE A  49     -42.556  10.198  31.692  1.00 92.02           C  
ANISOU  139  CD1 PHE A  49     9164  14023  11775   1488    865   3260       C  
ATOM    140  CD2 PHE A  49     -40.172  10.091  31.798  1.00 87.79           C  
ANISOU  140  CD2 PHE A  49     9047  13116  11195   1248    770   2921       C  
ATOM    141  CE1 PHE A  49     -42.505  11.570  31.964  1.00 94.65           C  
ANISOU  141  CE1 PHE A  49     9597  14065  12302   1727   1040   3395       C  
ATOM    142  CE2 PHE A  49     -40.121  11.463  32.064  1.00 92.31           C  
ANISOU  142  CE2 PHE A  49     9715  13403  11955   1456    931   3048       C  
ATOM    143  CZ  PHE A  49     -41.287  12.193  32.145  1.00 92.94           C  
ANISOU  143  CZ  PHE A  49     9648  13511  12154   1700   1073   3280       C  
ATOM    144  N   LEU A  50     -43.407   7.393  33.717  1.00 83.73           N  
ANISOU  144  N   LEU A  50     8170  13115  10528   1142    834   2754       N  
ATOM    145  CA  LEU A  50     -44.345   7.815  34.761  1.00 85.33           C  
ANISOU  145  CA  LEU A  50     8355  13217  10848   1331   1037   2802       C  
ATOM    146  C   LEU A  50     -44.067   7.158  36.120  1.00 88.24           C  
ANISOU  146  C   LEU A  50     8965  13380  11181   1244   1110   2531       C  
ATOM    147  O   LEU A  50     -43.884   7.871  37.106  1.00 88.53           O  
ANISOU  147  O   LEU A  50     9212  13119  11306   1387   1276   2456       O  
ATOM    148  CB  LEU A  50     -45.800   7.587  34.315  1.00 87.59           C  
ANISOU  148  CB  LEU A  50     8273  13868  11140   1387   1040   3034       C  
ATOM    149  CG  LEU A  50     -46.584   8.832  33.891  1.00 95.28           C  
ANISOU  149  CG  LEU A  50     9045  14892  12265   1681   1157   3358       C  
ATOM    150  CD1 LEU A  50     -46.184   9.304  32.492  1.00 95.69           C  
ANISOU  150  CD1 LEU A  50     8988  15091  12280   1683   1010   3549       C  
ATOM    151  CD2 LEU A  50     -48.079   8.558  33.921  1.00101.07           C  
ANISOU  151  CD2 LEU A  50     9433  15940  13030   1755   1208   3550       C  
ATOM    152  N   THR A  51     -43.983   5.817  36.157  1.00 83.27           N  
ANISOU  152  N   THR A  51     8326  12897  10415   1007    987   2380       N  
ATOM    153  CA  THR A  51     -43.706   5.043  37.371  1.00 81.80           C  
ANISOU  153  CA  THR A  51     8357  12549  10173    907   1034   2146       C  
ATOM    154  C   THR A  51     -42.324   5.389  37.959  1.00 83.30           C  
ANISOU  154  C   THR A  51     8886  12405  10361    893   1026   1948       C  
ATOM    155  O   THR A  51     -42.195   5.519  39.178  1.00 82.82           O  
ANISOU  155  O   THR A  51     9036  12124  10306    947   1145   1818       O  
ATOM    156  CB  THR A  51     -43.875   3.543  37.077  1.00 91.29           C  
ANISOU  156  CB  THR A  51     9465  13976  11244    651    895   2057       C  
ATOM    157  OG1 THR A  51     -45.105   3.338  36.374  1.00 93.08           O  
ANISOU  157  OG1 THR A  51     9354  14538  11475    640    873   2251       O  
ATOM    158  CG2 THR A  51     -43.831   2.675  38.334  1.00 89.98           C  
ANISOU  158  CG2 THR A  51     9484  13679  11027    561    963   1870       C  
ATOM    159  N   GLY A  52     -41.332   5.557  37.084  1.00 77.98           N  
ANISOU  159  N   GLY A  52     8247  11713   9669    820    889   1937       N  
ATOM    160  CA  GLY A  52     -39.959   5.884  37.450  1.00 76.02           C  
ANISOU  160  CA  GLY A  52     8268  11191   9427    783    852   1773       C  
ATOM    161  C   GLY A  52     -39.749   7.288  37.973  1.00 80.75           C  
ANISOU  161  C   GLY A  52     9017  11507  10156    967    994   1800       C  
ATOM    162  O   GLY A  52     -39.159   7.453  39.037  1.00 79.46           O  
ANISOU  162  O   GLY A  52     9105  11097   9989    961   1043   1622       O  
ATOM    163  N   ILE A  53     -40.214   8.313  37.232  1.00 79.77           N  
ANISOU  163  N   ILE A  53     8751  11412  10145   1128   1060   2022       N  
ATOM    164  CA  ILE A  53     -40.061   9.728  37.604  1.00 81.37           C  
ANISOU  164  CA  ILE A  53     9097  11320  10499   1313   1216   2068       C  
ATOM    165  C   ILE A  53     -40.632  10.047  39.000  1.00 86.08           C  
ANISOU  165  C   ILE A  53     9855  11719  11133   1444   1417   1967       C  
ATOM    166  O   ILE A  53     -39.944  10.669  39.810  1.00 85.63           O  
ANISOU  166  O   ILE A  53    10072  11354  11111   1460   1486   1808       O  
ATOM    167  CB  ILE A  53     -40.534  10.696  36.463  1.00 86.43           C  
ANISOU  167  CB  ILE A  53     9535  12047  11259   1477   1254   2367       C  
ATOM    168  CG1 ILE A  53     -39.719  12.025  36.375  1.00 87.65           C  
ANISOU  168  CG1 ILE A  53     9871  11875  11558   1565   1329   2396       C  
ATOM    169  CG2 ILE A  53     -42.066  10.861  36.354  1.00 89.52           C  
ANISOU  169  CG2 ILE A  53     9669  12637  11706   1670   1376   2595       C  
ATOM    170  CD1 ILE A  53     -39.979  13.159  37.447  1.00 95.86           C  
ANISOU  170  CD1 ILE A  53    11124  12551  12749   1763   1570   2351       C  
ATOM    171  N   VAL A  54     -41.853   9.564  39.289  1.00 83.50           N  
ANISOU  171  N   VAL A  54     9360  11582  10783   1516   1506   2046       N  
ATOM    172  CA  VAL A  54     -42.533   9.766  40.570  1.00 84.69           C  
ANISOU  172  CA  VAL A  54     9632  11595  10951   1649   1720   1970       C  
ATOM    173  C   VAL A  54     -41.872   8.903  41.659  1.00 86.97           C  
ANISOU  173  C   VAL A  54    10171  11786  11089   1475   1668   1692       C  
ATOM    174  O   VAL A  54     -41.518   9.415  42.724  1.00 86.66           O  
ANISOU  174  O   VAL A  54    10408  11478  11041   1526   1782   1530       O  
ATOM    175  CB  VAL A  54     -44.052   9.472  40.451  1.00 90.22           C  
ANISOU  175  CB  VAL A  54    10029  12568  11681   1770   1829   2170       C  
ATOM    176  CG1 VAL A  54     -44.771   9.747  41.767  1.00 91.67           C  
ANISOU  176  CG1 VAL A  54    10335  12608  11889   1931   2087   2104       C  
ATOM    177  CG2 VAL A  54     -44.687  10.268  39.312  1.00 91.93           C  
ANISOU  177  CG2 VAL A  54     9970  12925  12035   1944   1850   2475       C  
ATOM    178  N   GLY A  55     -41.726   7.610  41.361  1.00 82.24           N  
ANISOU  178  N   GLY A  55     9474  11406  10367   1273   1496   1647       N  
ATOM    179  CA  GLY A  55     -41.149   6.604  42.244  1.00 80.60           C  
ANISOU  179  CA  GLY A  55     9457  11152  10013   1105   1425   1430       C  
ATOM    180  C   GLY A  55     -39.745   6.916  42.708  1.00 83.80           C  
ANISOU  180  C   GLY A  55    10153  11304  10384   1026   1340   1235       C  
ATOM    181  O   GLY A  55     -39.486   6.938  43.913  1.00 84.06           O  
ANISOU  181  O   GLY A  55    10428  11167  10342   1027   1407   1072       O  
ATOM    182  N   ASN A  56     -38.824   7.143  41.758  1.00 79.42           N  
ANISOU  182  N   ASN A  56     9568  10739   9871    948   1188   1255       N  
ATOM    183  CA  ASN A  56     -37.431   7.467  42.066  1.00 78.30           C  
ANISOU  183  CA  ASN A  56     9654  10380   9715    855   1089   1092       C  
ATOM    184  C   ASN A  56     -37.282   8.896  42.596  1.00 83.84           C  
ANISOU  184  C   ASN A  56    10542  10792  10520    986   1231   1057       C  
ATOM    185  O   ASN A  56     -36.360   9.164  43.364  1.00 83.59           O  
ANISOU  185  O   ASN A  56    10755  10556  10450    912   1193    874       O  
ATOM    186  CB  ASN A  56     -36.499   7.164  40.889  1.00 76.95           C  
ANISOU  186  CB  ASN A  56     9377  10307   9554    722    898   1128       C  
ATOM    187  CG  ASN A  56     -36.422   5.688  40.554  1.00 90.03           C  
ANISOU  187  CG  ASN A  56    10929  12186  11094    570    762   1094       C  
ATOM    188  OD1 ASN A  56     -35.774   4.889  41.250  1.00 81.69           O  
ANISOU  188  OD1 ASN A  56    10011  11084   9941    461    684    939       O  
ATOM    189  ND2 ASN A  56     -37.092   5.290  39.481  1.00 76.83           N  
ANISOU  189  ND2 ASN A  56     9014  10756   9423    559    731   1242       N  
ATOM    190  N   GLY A  57     -38.224   9.770  42.236  1.00 82.03           N  
ANISOU  190  N   GLY A  57    10201  10548  10419   1179   1397   1230       N  
ATOM    191  CA  GLY A  57     -38.279  11.141  42.728  1.00 84.18           C  
ANISOU  191  CA  GLY A  57    10651  10522  10810   1334   1579   1211       C  
ATOM    192  C   GLY A  57     -38.627  11.179  44.205  1.00 89.50           C  
ANISOU  192  C   GLY A  57    11561  11048  11398   1391   1735   1033       C  
ATOM    193  O   GLY A  57     -38.022  11.940  44.962  1.00 89.77           O  
ANISOU  193  O   GLY A  57    11873  10799  11437   1385   1791    863       O  
ATOM    194  N   LEU A  58     -39.586  10.329  44.629  1.00 86.83           N  
ANISOU  194  N   LEU A  58    11118  10906  10968   1428   1803   1064       N  
ATOM    195  CA  LEU A  58     -40.006  10.207  46.025  1.00 88.25           C  
ANISOU  195  CA  LEU A  58    11502  10995  11034   1479   1963    913       C  
ATOM    196  C   LEU A  58     -38.879   9.630  46.883  1.00 91.34           C  
ANISOU  196  C   LEU A  58    12153  11304  11248   1279   1807    668       C  
ATOM    197  O   LEU A  58     -38.611  10.165  47.956  1.00 92.83           O  
ANISOU  197  O   LEU A  58    12629  11277  11364   1300   1901    488       O  
ATOM    198  CB  LEU A  58     -41.271   9.340  46.163  1.00 88.70           C  
ANISOU  198  CB  LEU A  58    11346  11312  11043   1540   2062   1035       C  
ATOM    199  CG  LEU A  58     -42.606   9.958  45.744  1.00 96.07           C  
ANISOU  199  CG  LEU A  58    12044  12327  12132   1781   2277   1266       C  
ATOM    200  CD1 LEU A  58     -43.727   8.934  45.825  1.00 96.39           C  
ANISOU  200  CD1 LEU A  58    11841  12664  12117   1778   2327   1380       C  
ATOM    201  CD2 LEU A  58     -42.954  11.187  46.586  1.00102.30           C  
ANISOU  201  CD2 LEU A  58    13047  12828  12993   2005   2557   1206       C  
ATOM    202  N   VAL A  59     -38.205   8.563  46.396  1.00 85.33           N  
ANISOU  202  N   VAL A  59    11293  10714  10413   1090   1570    662       N  
ATOM    203  CA  VAL A  59     -37.095   7.899  47.092  1.00 84.24           C  
ANISOU  203  CA  VAL A  59    11353  10536  10117    908   1397    471       C  
ATOM    204  C   VAL A  59     -35.916   8.876  47.299  1.00 89.44           C  
ANISOU  204  C   VAL A  59    12229  10944  10810    846   1323    326       C  
ATOM    205  O   VAL A  59     -35.295   8.874  48.362  1.00 89.46           O  
ANISOU  205  O   VAL A  59    12483  10831  10676    768   1283    135       O  
ATOM    206  CB  VAL A  59     -36.700   6.551  46.413  1.00 85.83           C  
ANISOU  206  CB  VAL A  59    11380  10966  10266    751   1188    522       C  
ATOM    207  CG1 VAL A  59     -35.434   5.948  47.026  1.00 84.81           C  
ANISOU  207  CG1 VAL A  59    11431  10787  10006    587   1000    355       C  
ATOM    208  CG2 VAL A  59     -37.847   5.544  46.485  1.00 85.43           C  
ANISOU  208  CG2 VAL A  59    11172  11129  10161    774   1269    620       C  
ATOM    209  N   ILE A  60     -35.657   9.809  46.314  1.00 87.20           N  
ANISOU  209  N   ILE A  60    11856  10569  10709    882   1320    422       N  
ATOM    210  CA  ILE A  60     -34.642  10.868  46.436  1.00 88.65           C  
ANISOU  210  CA  ILE A  60    12229  10490  10962    819   1280    303       C  
ATOM    211  C   ILE A  60     -35.045  11.960  47.448  1.00 97.59           C  
ANISOU  211  C   ILE A  60    13630  11349  12102    937   1500    176       C  
ATOM    212  O   ILE A  60     -34.232  12.364  48.272  1.00 98.08           O  
ANISOU  212  O   ILE A  60    13954  11225  12088    827   1450    -35       O  
ATOM    213  CB  ILE A  60     -34.318  11.507  45.072  1.00 91.27           C  
ANISOU  213  CB  ILE A  60    12385  10804  11489    826   1236    469       C  
ATOM    214  CG1 ILE A  60     -33.685  10.469  44.140  1.00 88.75           C  
ANISOU  214  CG1 ILE A  60    11855  10729  11137    683   1014    544       C  
ATOM    215  CG2 ILE A  60     -33.356  12.696  45.236  1.00 93.54           C  
ANISOU  215  CG2 ILE A  60    12876  10790  11876    756   1229    355       C  
ATOM    216  CD1 ILE A  60     -33.526  10.906  42.708  1.00 94.46           C  
ANISOU  216  CD1 ILE A  60    12372  11507  12012    699    981    737       C  
ATOM    217  N   LEU A  61     -36.288  12.423  47.365  1.00 97.92           N  
ANISOU  217  N   LEU A  61    13598  11374  12233   1158   1741    304       N  
ATOM    218  CA  LEU A  61     -36.767  13.490  48.237  1.00101.87           C  
ANISOU  218  CA  LEU A  61    14345  11600  12760   1306   1994    196       C  
ATOM    219  C   LEU A  61     -36.950  13.021  49.678  1.00109.32           C  
ANISOU  219  C   LEU A  61    15525  12541  13470   1284   2060    -10       C  
ATOM    220  O   LEU A  61     -36.502  13.680  50.616  1.00111.28           O  
ANISOU  220  O   LEU A  61    16092  12550  13639   1243   2116   -235       O  
ATOM    221  CB  LEU A  61     -38.080  14.067  47.703  1.00103.47           C  
ANISOU  221  CB  LEU A  61    14368  11810  13138   1579   2246    423       C  
ATOM    222  CG  LEU A  61     -38.221  15.590  47.753  1.00111.10           C  
ANISOU  222  CG  LEU A  61    15504  12423  14287   1741   2469    413       C  
ATOM    223  CD1 LEU A  61     -39.654  15.987  48.073  1.00113.64           C  
ANISOU  223  CD1 LEU A  61    15776  12724  14679   2039   2792    527       C  
ATOM    224  CD2 LEU A  61     -37.256  16.186  48.766  1.00114.76           C  
ANISOU  224  CD2 LEU A  61    16363  12580  14661   1596   2454    100       C  
ATOM    225  N   VAL A  62     -37.613  11.882  49.845  1.00106.36           N  
ANISOU  225  N   VAL A  62    15001  12434  12977   1300   2056     69       N  
ATOM    226  CA  VAL A  62     -37.896  11.346  51.173  1.00107.99           C  
ANISOU  226  CA  VAL A  62    15408  12671  12952   1292   2137    -83       C  
ATOM    227  C   VAL A  62     -36.623  11.035  51.956  1.00114.10           C  
ANISOU  227  C   VAL A  62    16434  13390  13528   1069   1918   -313       C  
ATOM    228  O   VAL A  62     -36.423  11.542  53.060  1.00115.91           O  
ANISOU  228  O   VAL A  62    16977  13449  13615   1058   2000   -524       O  
ATOM    229  CB  VAL A  62     -38.759  10.072  51.093  1.00110.42           C  
ANISOU  229  CB  VAL A  62    15481  13286  13187   1315   2148     69       C  
ATOM    230  CG1 VAL A  62     -38.807   9.379  52.446  1.00110.90           C  
ANISOU  230  CG1 VAL A  62    15761  13390  12985   1262   2185    -80       C  
ATOM    231  CG2 VAL A  62     -40.161  10.412  50.611  1.00111.51           C  
ANISOU  231  CG2 VAL A  62    15387  13494  13486   1546   2396    280       C  
ATOM    232  N   MET A  63     -35.768  10.196  51.380  1.00110.44           N  
ANISOU  232  N   MET A  63    15830  13083  13050    896   1641   -270       N  
ATOM    233  CA  MET A  63     -34.552   9.774  52.042  1.00111.29           C  
ANISOU  233  CA  MET A  63    16116  13188  12982    693   1410   -445       C  
ATOM    234  C   MET A  63     -33.573  10.897  51.951  1.00119.18           C  
ANISOU  234  C   MET A  63    17267  13948  14068    599   1333   -578       C  
ATOM    235  O   MET A  63     -33.113  11.428  52.964  1.00121.41           O  
ANISOU  235  O   MET A  63    17845  14071  14215    528   1334   -796       O  
ATOM    236  CB  MET A  63     -33.944   8.560  51.359  1.00111.13           C  
ANISOU  236  CB  MET A  63    15877  13393  12955    562   1161   -339       C  
ATOM    237  CG  MET A  63     -34.705   7.296  51.579  1.00114.39           C  
ANISOU  237  CG  MET A  63    16179  14026  13257    596   1198   -239       C  
ATOM    238  SD  MET A  63     -33.522   5.975  51.795  1.00117.51           S  
ANISOU  238  SD  MET A  63    16578  14568  13503    403    900   -276       S  
ATOM    239  CE  MET A  63     -33.736   5.066  50.267  1.00111.68           C  
ANISOU  239  CE  MET A  63    15477  14024  12934    388    820    -65       C  
ATOM    240  N   GLY A  64     -33.269  11.271  50.713  1.00116.46           N  
ANISOU  240  N   GLY A  64    16720  13583  13947    589   1269   -445       N  
ATOM    241  CA  GLY A  64     -32.245  12.261  50.445  1.00118.15           C  
ANISOU  241  CA  GLY A  64    17031  13584  14277    470   1176   -537       C  
ATOM    242  C   GLY A  64     -32.235  13.314  51.516  1.00127.66           C  
ANISOU  242  C   GLY A  64    18582  14508  15416    474   1316   -764       C  
ATOM    243  O   GLY A  64     -31.183  13.647  52.053  1.00128.39           O  
ANISOU  243  O   GLY A  64    18864  14487  15430    284   1164   -956       O  
ATOM    244  N   TYR A  65     -33.404  13.806  51.864  1.00127.76           N  
ANISOU  244  N   TYR A  65    18678  14417  15448    684   1607   -750       N  
ATOM    245  CA  TYR A  65     -33.457  14.902  52.797  1.00131.81           C  
ANISOU  245  CA  TYR A  65    19537  14627  15917    709   1782   -974       C  
ATOM    246  C   TYR A  65     -33.959  14.697  54.213  1.00139.31           C  
ANISOU  246  C   TYR A  65    20759  15575  16596    756   1919  -1161       C  
ATOM    247  O   TYR A  65     -33.243  14.947  55.183  1.00140.68           O  
ANISOU  247  O   TYR A  65    21229  15643  16581    596   1833  -1416       O  
ATOM    248  CB  TYR A  65     -34.225  15.998  52.129  1.00134.80           C  
ANISOU  248  CB  TYR A  65    19871  14786  16559    920   2045   -848       C  
ATOM    249  CG  TYR A  65     -33.485  16.463  50.922  1.00136.03           C  
ANISOU  249  CG  TYR A  65    19860  14874  16953    830   1908   -720       C  
ATOM    250  CD1 TYR A  65     -33.212  15.616  49.888  1.00134.97           C  
ANISOU  250  CD1 TYR A  65    19399  15010  16872    774   1710   -515       C  
ATOM    251  CD2 TYR A  65     -33.009  17.736  50.844  1.00139.41           C  
ANISOU  251  CD2 TYR A  65    20474  14957  17537    786   1979   -816       C  
ATOM    252  CE1 TYR A  65     -32.521  16.045  48.826  1.00135.20           C  
ANISOU  252  CE1 TYR A  65    19291  14986  17095    692   1600   -402       C  
ATOM    253  CE2 TYR A  65     -32.327  18.153  49.790  1.00139.75           C  
ANISOU  253  CE2 TYR A  65    20372  14939  17788    697   1867   -691       C  
ATOM    254  CZ  TYR A  65     -32.086  17.329  48.791  1.00144.52           C  
ANISOU  254  CZ  TYR A  65    20653  15828  18432    655   1682   -483       C  
ATOM    255  OH  TYR A  65     -31.393  17.827  47.748  1.00145.99           O  
ANISOU  255  OH  TYR A  65    20711  15940  18817    570   1594   -358       O  
ATOM    256  N   GLN A  66     -35.179  14.251  54.359  1.00137.28           N  
ANISOU  256  N   GLN A  66    20404  15449  16307    963   2131  -1036       N  
ATOM    257  CA  GLN A  66     -35.674  14.086  55.682  1.00139.99           C  
ANISOU  257  CA  GLN A  66    21005  15794  16392   1015   2288  -1200       C  
ATOM    258  C   GLN A  66     -34.997  13.054  56.518  1.00144.36           C  
ANISOU  258  C   GLN A  66    21661  16547  16643    825   2056  -1312       C  
ATOM    259  O   GLN A  66     -34.756  13.297  57.672  1.00146.58           O  
ANISOU  259  O   GLN A  66    22267  16742  16685    760   2085  -1546       O  
ATOM    260  CB  GLN A  66     -37.127  13.715  55.625  1.00141.67           C  
ANISOU  260  CB  GLN A  66    21044  16142  16642   1268   2560  -1012       C  
ATOM    261  CG  GLN A  66     -37.974  14.744  54.978  1.00164.89           C  
ANISOU  261  CG  GLN A  66    23895  18899  19859   1507   2834   -886       C  
ATOM    262  CD  GLN A  66     -39.419  14.317  54.872  1.00188.55           C  
ANISOU  262  CD  GLN A  66    26660  22076  22904   1751   3083   -671       C  
ATOM    263  OE1 GLN A  66     -40.176  14.338  55.844  1.00187.24           O  
ANISOU  263  OE1 GLN A  66    26652  21896  22596   1882   3335   -751       O  
ATOM    264  NE2 GLN A  66     -39.805  13.930  53.687  1.00179.03           N  
ANISOU  264  NE2 GLN A  66    25074  21055  21893   1806   3015   -396       N  
ATOM    265  N   LYS A  67     -34.705  11.890  55.952  1.00138.35           N  
ANISOU  265  N   LYS A  67    20633  16053  15882    743   1833  -1144       N  
ATOM    266  CA  LYS A  67     -34.291  10.740  56.753  1.00137.73           C  
ANISOU  266  CA  LYS A  67    20619  16188  15523    617   1656  -1190       C  
ATOM    267  C   LYS A  67     -32.957  10.827  57.541  1.00142.86           C  
ANISOU  267  C   LYS A  67    21517  16799  15963    385   1396  -1416       C  
ATOM    268  O   LYS A  67     -31.902  11.044  56.981  1.00141.58           O  
ANISOU  268  O   LYS A  67    21285  16598  15911    228   1163  -1436       O  
ATOM    269  CB  LYS A  67     -34.330   9.465  55.903  1.00137.06           C  
ANISOU  269  CB  LYS A  67    20192  16369  15514    596   1503   -952       C  
ATOM    270  CG  LYS A  67     -35.575   8.652  56.003  1.00152.08           C  
ANISOU  270  CG  LYS A  67    21957  18445  17380    743   1694   -792       C  
ATOM    271  CD  LYS A  67     -35.306   7.189  55.672  1.00162.01           C  
ANISOU  271  CD  LYS A  67    23012  19951  18592    645   1491   -648       C  
ATOM    272  CE  LYS A  67     -36.491   6.494  54.886  1.00175.84           C  
ANISOU  272  CE  LYS A  67    24452  21871  20489    760   1630   -411       C  
ATOM    273  NZ  LYS A  67     -36.376   5.044  54.414  1.00183.92           N  
ANISOU  273  NZ  LYS A  67    25265  23112  21505    664   1467   -265       N  
ATOM    274  N   LYS A  68     -33.042  10.589  58.851  1.00141.27           N  
ANISOU  274  N   LYS A  68    21589  16640  15446    362   1435  -1567       N  
ATOM    275  CA  LYS A  68     -31.887  10.643  59.738  1.00142.40           C  
ANISOU  275  CA  LYS A  68    21979  16785  15341    146   1190  -1780       C  
ATOM    276  C   LYS A  68     -31.408   9.283  60.271  1.00144.22           C  
ANISOU  276  C   LYS A  68    22169  17299  15328     53    960  -1705       C  
ATOM    277  O   LYS A  68     -30.228   9.087  60.528  1.00143.95           O  
ANISOU  277  O   LYS A  68    22177  17333  15183   -138    659  -1780       O  
ATOM    278  CB  LYS A  68     -32.101  11.648  60.867  1.00148.93           C  
ANISOU  278  CB  LYS A  68    23212  17409  15965    150   1375  -2061       C  
ATOM    279  CG  LYS A  68     -30.969  12.643  61.055  1.00166.58           C  
ANISOU  279  CG  LYS A  68    25653  19448  18192    -69   1196  -2307       C  
ATOM    280  CD  LYS A  68     -31.001  13.735  60.029  1.00175.42           C  
ANISOU  280  CD  LYS A  68    26682  20296  19674    -31   1303  -2291       C  
ATOM    281  CE  LYS A  68     -29.850  14.685  60.216  1.00186.15           C  
ANISOU  281  CE  LYS A  68    28238  21453  21036   -280   1122  -2532       C  
ATOM    282  NZ  LYS A  68     -30.071  15.970  59.491  1.00195.03           N  
ANISOU  282  NZ  LYS A  68    29389  22234  22480   -218   1320  -2560       N  
ATOM    283  N   LEU A  69     -32.308   8.316  60.380  1.00138.77           N  
ANISOU  283  N   LEU A  69    21372  16776  14578    187   1095  -1533       N  
ATOM    284  CA  LEU A  69     -31.882   6.966  60.730  1.00136.74           C  
ANISOU  284  CA  LEU A  69    21048  16765  14143    115    891  -1418       C  
ATOM    285  C   LEU A  69     -31.841   6.103  59.473  1.00134.80           C  
ANISOU  285  C   LEU A  69    20427  16634  14158    132    788  -1174       C  
ATOM    286  O   LEU A  69     -32.851   5.499  59.110  1.00133.24           O  
ANISOU  286  O   LEU A  69    20066  16516  14045    258    964  -1005       O  
ATOM    287  CB  LEU A  69     -32.829   6.353  61.763  1.00138.27           C  
ANISOU  287  CB  LEU A  69    21394  17070  14073    224   1101  -1387       C  
ATOM    288  N   ARG A  70     -30.687   5.980  58.826  1.00127.56           N  
ANISOU  288  N   ARG A  70    19368  15741  13358     -3    505  -1154       N  
ATOM    289  CA  ARG A  70     -30.612   5.161  57.610  1.00122.90           C  
ANISOU  289  CA  ARG A  70    18441  15255  12999     12    419   -943       C  
ATOM    290  C   ARG A  70     -29.677   3.949  57.712  1.00121.59           C  
ANISOU  290  C   ARG A  70    18192  15265  12742    -84    150   -853       C  
ATOM    291  O   ARG A  70     -28.580   4.050  58.259  1.00122.46           O  
ANISOU  291  O   ARG A  70    18411  15398  12719   -211    -78   -951       O  
ATOM    292  CB  ARG A  70     -30.211   6.026  56.412  1.00122.79           C  
ANISOU  292  CB  ARG A  70    18261  15115  13278    -19    376   -941       C  
ATOM    293  CG  ARG A  70     -31.384   6.508  55.574  1.00133.42           C  
ANISOU  293  CG  ARG A  70    19465  16386  14843    138    637   -841       C  
ATOM    294  CD  ARG A  70     -30.970   6.745  54.130  1.00141.33           C  
ANISOU  294  CD  ARG A  70    20202  17369  16128    111    546   -733       C  
ATOM    295  NE  ARG A  70     -29.749   7.540  54.035  1.00149.45           N  
ANISOU  295  NE  ARG A  70    21299  18277  17209    -35    366   -857       N  
ATOM    296  CZ  ARG A  70     -29.650   8.679  53.358  1.00163.62           C  
ANISOU  296  CZ  ARG A  70    23068  19894  19206    -34    427   -878       C  
ATOM    297  NH1 ARG A  70     -30.702   9.162  52.711  1.00151.81           N  
ANISOU  297  NH1 ARG A  70    21476  18330  17873    127    657   -773       N  
ATOM    298  NH2 ARG A  70     -28.499   9.336  53.326  1.00149.21           N  
ANISOU  298  NH2 ARG A  70    21302  17964  17425   -195    256   -990       N  
ATOM    299  N   SER A  71     -30.112   2.808  57.172  1.00112.62           N  
ANISOU  299  N   SER A  71    16857  14249  11685    -25    178   -663       N  
ATOM    300  CA  SER A  71     -29.243   1.626  57.084  1.00109.80           C  
ANISOU  300  CA  SER A  71    16394  14027  11297    -90    -51   -555       C  
ATOM    301  C   SER A  71     -28.361   1.692  55.829  1.00107.89           C  
ANISOU  301  C   SER A  71    15910  13778  11307   -152   -219   -509       C  
ATOM    302  O   SER A  71     -28.733   2.357  54.865  1.00106.39           O  
ANISOU  302  O   SER A  71    15589  13507  11327   -123   -118   -501       O  
ATOM    303  CB  SER A  71     -30.072   0.346  57.090  1.00112.58           C  
ANISOU  303  CB  SER A  71    16669  14483  11624    -14     67   -384       C  
ATOM    304  OG  SER A  71     -30.975   0.294  55.997  1.00119.76           O  
ANISOU  304  OG  SER A  71    17363  15377  12761     50    230   -289       O  
ATOM    305  N   MET A  72     -27.188   1.030  55.847  1.00101.42           N  
ANISOU  305  N   MET A  72    15026  13046  10462   -228   -466   -468       N  
ATOM    306  CA  MET A  72     -26.244   1.027  54.717  1.00 98.35           C  
ANISOU  306  CA  MET A  72    14405  12666  10296   -286   -622   -421       C  
ATOM    307  C   MET A  72     -26.908   0.682  53.383  1.00 97.19           C  
ANISOU  307  C   MET A  72    14030  12519  10378   -218   -489   -302       C  
ATOM    308  O   MET A  72     -26.601   1.315  52.369  1.00 95.66           O  
ANISOU  308  O   MET A  72    13690  12278  10378   -246   -506   -305       O  
ATOM    309  CB  MET A  72     -25.032   0.118  54.992  1.00100.74           C  
ANISOU  309  CB  MET A  72    14653  13089  10534   -336   -872   -356       C  
ATOM    310  CG  MET A  72     -24.161   0.596  56.139  1.00106.42           C  
ANISOU  310  CG  MET A  72    15551  13840  11044   -436  -1063   -473       C  
ATOM    311  SD  MET A  72     -23.332   2.164  55.796  1.00111.21           S  
ANISOU  311  SD  MET A  72    16145  14336  11772   -585  -1171   -644       S  
ATOM    312  CE  MET A  72     -23.110   2.757  57.434  1.00111.26           C  
ANISOU  312  CE  MET A  72    16479  14352  11444   -683  -1267   -829       C  
ATOM    313  N   THR A  73     -27.863  -0.275  53.406  1.00 90.99           N  
ANISOU  313  N   THR A  73    13223  11789   9559   -142   -351   -199       N  
ATOM    314  CA  THR A  73     -28.647  -0.701  52.243  1.00 87.94           C  
ANISOU  314  CA  THR A  73    12635  11427   9351    -96   -223    -94       C  
ATOM    315  C   THR A  73     -29.425   0.496  51.694  1.00 88.64           C  
ANISOU  315  C   THR A  73    12684  11440   9558    -55    -65   -130       C  
ATOM    316  O   THR A  73     -29.392   0.721  50.485  1.00 86.88           O  
ANISOU  316  O   THR A  73    12270  11222   9517    -58    -65    -79       O  
ATOM    317  CB  THR A  73     -29.568  -1.883  52.599  1.00 97.95           C  
ANISOU  317  CB  THR A  73    13921  12758  10536    -50   -100      5       C  
ATOM    318  OG1 THR A  73     -28.868  -2.816  53.428  1.00 99.02           O  
ANISOU  318  OG1 THR A  73    14162  12937  10525    -68   -229     38       O  
ATOM    319  CG2 THR A  73     -30.113  -2.594  51.364  1.00 95.80           C  
ANISOU  319  CG2 THR A  73    13429  12536  10437    -47    -32    108       C  
ATOM    320  N   ASP A  74     -30.064   1.295  52.590  1.00 84.46           N  
ANISOU  320  N   ASP A  74    12340  10834   8916     -9     71   -216       N  
ATOM    321  CA  ASP A  74     -30.816   2.499  52.222  1.00 83.66           C  
ANISOU  321  CA  ASP A  74    12229  10632   8925     59    243   -246       C  
ATOM    322  C   ASP A  74     -29.937   3.532  51.521  1.00 85.54           C  
ANISOU  322  C   ASP A  74    12416  10769   9315      0    139   -301       C  
ATOM    323  O   ASP A  74     -30.430   4.221  50.628  1.00 84.91           O  
ANISOU  323  O   ASP A  74    12215  10642   9407     56    246   -247       O  
ATOM    324  CB  ASP A  74     -31.515   3.119  53.429  1.00 87.53           C  
ANISOU  324  CB  ASP A  74    12963  11042   9252    124    414   -348       C  
ATOM    325  CG  ASP A  74     -32.820   2.466  53.806  1.00 99.35           C  
ANISOU  325  CG  ASP A  74    14450  12620  10677    220    622   -258       C  
ATOM    326  OD1 ASP A  74     -33.747   2.354  53.002  1.00 98.87           O  
ANISOU  326  OD1 ASP A  74    14194  12610  10762    288    755   -140       O  
ATOM    327  OD2 ASP A  74     -33.053   2.045  54.973  1.00108.21           O  
ANISOU  327  OD2 ASP A  74    15760  13772  11581    231    676   -294       O  
ATOM    328  N   LYS A  75     -28.639   3.621  51.896  1.00 80.95           N  
ANISOU  328  N   LYS A  75    11911  10170   8677   -115    -73   -390       N  
ATOM    329  CA  LYS A  75     -27.689   4.545  51.271  1.00 80.14           C  
ANISOU  329  CA  LYS A  75    11751   9978   8722   -201   -185   -438       C  
ATOM    330  C   LYS A  75     -27.380   4.131  49.832  1.00 79.88           C  
ANISOU  330  C   LYS A  75    11440  10026   8884   -207   -240   -301       C  
ATOM    331  O   LYS A  75     -27.370   4.989  48.940  1.00 79.08           O  
ANISOU  331  O   LYS A  75    11242   9850   8954   -205   -191   -271       O  
ATOM    332  CB  LYS A  75     -26.396   4.684  52.098  1.00 84.44           C  
ANISOU  332  CB  LYS A  75    12424  10512   9146   -340   -408   -562       C  
ATOM    333  CG  LYS A  75     -26.493   5.654  53.290  1.00106.38           C  
ANISOU  333  CG  LYS A  75    15496  13157  11767   -378   -363   -750       C  
ATOM    334  CD  LYS A  75     -26.680   7.144  52.895  1.00119.95           C  
ANISOU  334  CD  LYS A  75    17273  14659  13644   -385   -237   -834       C  
ATOM    335  CE  LYS A  75     -25.407   7.855  52.494  1.00129.13           C  
ANISOU  335  CE  LYS A  75    18384  15747  14931   -552   -420   -895       C  
ATOM    336  NZ  LYS A  75     -25.696   9.196  51.916  1.00138.01           N  
ANISOU  336  NZ  LYS A  75    19539  16647  16251   -539   -266   -928       N  
ATOM    337  N   TYR A  76     -27.166   2.812  49.599  1.00 73.23           N  
ANISOU  337  N   TYR A  76    10483   9330   8012   -209   -324   -213       N  
ATOM    338  CA  TYR A  76     -26.908   2.281  48.256  1.00 70.17           C  
ANISOU  338  CA  TYR A  76     9853   9030   7778   -213   -360    -99       C  
ATOM    339  C   TYR A  76     -28.162   2.372  47.403  1.00 72.55           C  
ANISOU  339  C   TYR A  76    10039   9358   8169   -128   -177     -6       C  
ATOM    340  O   TYR A  76     -28.060   2.571  46.196  1.00 71.66           O  
ANISOU  340  O   TYR A  76     9750   9280   8196   -132   -175     68       O  
ATOM    341  CB  TYR A  76     -26.441   0.826  48.304  1.00 69.71           C  
ANISOU  341  CB  TYR A  76     9735   9089   7661   -225   -466    -45       C  
ATOM    342  CG  TYR A  76     -25.058   0.610  48.874  1.00 71.17           C  
ANISOU  342  CG  TYR A  76     9956   9293   7794   -298   -675    -88       C  
ATOM    343  CD1 TYR A  76     -23.923   1.008  48.174  1.00 72.71           C  
ANISOU  343  CD1 TYR A  76    10013   9492   8120   -367   -800    -85       C  
ATOM    344  CD2 TYR A  76     -24.877  -0.077  50.069  1.00 72.74           C  
ANISOU  344  CD2 TYR A  76    10299   9526   7811   -294   -749   -106       C  
ATOM    345  CE1 TYR A  76     -22.645   0.796  48.688  1.00 74.36           C  
ANISOU  345  CE1 TYR A  76    10217   9745   8292   -434  -1000   -107       C  
ATOM    346  CE2 TYR A  76     -23.604  -0.299  50.591  1.00 74.45           C  
ANISOU  346  CE2 TYR A  76    10523   9789   7975   -354   -959   -122       C  
ATOM    347  CZ  TYR A  76     -22.489   0.129  49.892  1.00 80.34           C  
ANISOU  347  CZ  TYR A  76    11113  10547   8865   -424  -1088   -122       C  
ATOM    348  OH  TYR A  76     -21.232  -0.101  50.397  1.00 81.61           O  
ANISOU  348  OH  TYR A  76    11245  10778   8985   -482  -1301   -122       O  
ATOM    349  N   ARG A  77     -29.348   2.244  48.036  1.00 68.79           N  
ANISOU  349  N   ARG A  77     9651   8883   7605    -51    -23     -1       N  
ATOM    350  CA  ARG A  77     -30.643   2.337  47.364  1.00 67.51           C  
ANISOU  350  CA  ARG A  77     9364   8770   7517     33    151     98       C  
ATOM    351  C   ARG A  77     -30.951   3.762  46.907  1.00 72.59           C  
ANISOU  351  C   ARG A  77     9988   9307   8286     93    251    110       C  
ATOM    352  O   ARG A  77     -31.755   3.931  45.992  1.00 72.64           O  
ANISOU  352  O   ARG A  77     9827   9379   8394    157    349    226       O  
ATOM    353  CB  ARG A  77     -31.768   1.721  48.206  1.00 65.87           C  
ANISOU  353  CB  ARG A  77     9232   8608   7188     92    290    114       C  
ATOM    354  CG  ARG A  77     -31.773   0.189  48.160  1.00 69.07           C  
ANISOU  354  CG  ARG A  77     9578   9132   7533     41    233    167       C  
ATOM    355  CD  ARG A  77     -32.814  -0.440  49.074  1.00 74.03           C  
ANISOU  355  CD  ARG A  77    10292   9797   8040     79    373    191       C  
ATOM    356  NE  ARG A  77     -34.083  -0.692  48.386  1.00 75.76           N  
ANISOU  356  NE  ARG A  77    10331  10117   8339    109    516    298       N  
ATOM    357  CZ  ARG A  77     -35.143  -1.277  48.938  1.00 88.89           C  
ANISOU  357  CZ  ARG A  77    12001  11837   9936    130    659    350       C  
ATOM    358  NH1 ARG A  77     -35.105  -1.683  50.201  1.00 79.54           N  
ANISOU  358  NH1 ARG A  77    11015  10614   8592    135    693    310       N  
ATOM    359  NH2 ARG A  77     -36.249  -1.460  48.232  1.00 75.27           N  
ANISOU  359  NH2 ARG A  77    10077  10225   8298    139    767    451       N  
ATOM    360  N   LEU A  78     -30.275   4.778  47.501  1.00 69.87           N  
ANISOU  360  N   LEU A  78     9810   8800   7939     64    220     -5       N  
ATOM    361  CA  LEU A  78     -30.405   6.183  47.106  1.00 70.68           C  
ANISOU  361  CA  LEU A  78     9926   8750   8179    111    315     -1       C  
ATOM    362  C   LEU A  78     -29.575   6.416  45.830  1.00 75.46           C  
ANISOU  362  C   LEU A  78    10352   9381   8939     44    205     79       C  
ATOM    363  O   LEU A  78     -30.080   7.016  44.877  1.00 75.45           O  
ANISOU  363  O   LEU A  78    10221   9375   9072    114    300    200       O  
ATOM    364  CB  LEU A  78     -29.965   7.136  48.238  1.00 72.48           C  
ANISOU  364  CB  LEU A  78    10423   8775   8340     76    325   -176       C  
ATOM    365  CG  LEU A  78     -29.875   8.635  47.892  1.00 77.95           C  
ANISOU  365  CG  LEU A  78    11171   9254   9192     96    414   -196       C  
ATOM    366  CD1 LEU A  78     -31.254   9.275  47.782  1.00 78.88           C  
ANISOU  366  CD1 LEU A  78    11286   9302   9383    284    673   -115       C  
ATOM    367  CD2 LEU A  78     -29.046   9.377  48.904  1.00 81.73           C  
ANISOU  367  CD2 LEU A  78    11907   9548   9599    -17    347   -401       C  
ATOM    368  N   HIS A  79     -28.309   5.921  45.811  1.00 71.92           N  
ANISOU  368  N   HIS A  79     9886   8974   8468    -84     10     29       N  
ATOM    369  CA  HIS A  79     -27.393   5.998  44.659  1.00 70.64           C  
ANISOU  369  CA  HIS A  79     9548   8857   8435   -156    -94    101       C  
ATOM    370  C   HIS A  79     -28.062   5.387  43.436  1.00 73.62           C  
ANISOU  370  C   HIS A  79     9711   9401   8861    -94    -37    253       C  
ATOM    371  O   HIS A  79     -28.060   5.989  42.361  1.00 73.65           O  
ANISOU  371  O   HIS A  79     9585   9411   8985    -79     -1    357       O  
ATOM    372  CB  HIS A  79     -26.095   5.230  44.952  1.00 70.60           C  
ANISOU  372  CB  HIS A  79     9533   8917   8374   -271   -294     38       C  
ATOM    373  CG  HIS A  79     -25.095   6.028  45.710  1.00 75.35           C  
ANISOU  373  CG  HIS A  79    10270   9386   8974   -381   -401    -86       C  
ATOM    374  ND1 HIS A  79     -24.217   6.867  45.063  1.00 77.71           N  
ANISOU  374  ND1 HIS A  79    10491   9613   9421   -471   -455    -71       N  
ATOM    375  CD2 HIS A  79     -24.873   6.103  47.041  1.00 78.58           C  
ANISOU  375  CD2 HIS A  79    10884   9732   9242   -428   -464   -225       C  
ATOM    376  CE1 HIS A  79     -23.477   7.411  46.010  1.00 78.78           C  
ANISOU  376  CE1 HIS A  79    10777   9642   9514   -584   -557   -209       C  
ATOM    377  NE2 HIS A  79     -23.833   6.982  47.216  1.00 79.77           N  
ANISOU  377  NE2 HIS A  79    11079   9776   9453   -562   -573   -310       N  
ATOM    378  N   LEU A  80     -28.684   4.207  43.642  1.00 69.01           N  
ANISOU  378  N   LEU A  80     9101   8948   8172    -66    -25    266       N  
ATOM    379  CA  LEU A  80     -29.404   3.433  42.648  1.00 67.75           C  
ANISOU  379  CA  LEU A  80     8760   8960   8022    -38     17    378       C  
ATOM    380  C   LEU A  80     -30.596   4.222  42.113  1.00 73.46           C  
ANISOU  380  C   LEU A  80     9401   9697   8815     65    169    490       C  
ATOM    381  O   LEU A  80     -30.889   4.127  40.926  1.00 72.81           O  
ANISOU  381  O   LEU A  80     9137   9744   8782     72    176    606       O  
ATOM    382  CB  LEU A  80     -29.846   2.101  43.281  1.00 66.98           C  
ANISOU  382  CB  LEU A  80     8702   8947   7799    -47     13    345       C  
ATOM    383  CG  LEU A  80     -30.500   1.044  42.394  1.00 69.94           C  
ANISOU  383  CG  LEU A  80     8917   9494   8164    -62     35    423       C  
ATOM    384  CD1 LEU A  80     -29.685   0.765  41.154  1.00 69.19           C  
ANISOU  384  CD1 LEU A  80     8682   9481   8127   -121    -54    455       C  
ATOM    385  CD2 LEU A  80     -30.699  -0.233  43.162  1.00 70.82           C  
ANISOU  385  CD2 LEU A  80     9107   9633   8169    -91     25    379       C  
ATOM    386  N   SER A  81     -31.247   5.028  42.976  1.00 71.63           N  
ANISOU  386  N   SER A  81     9301   9334   8581    150    291    460       N  
ATOM    387  CA  SER A  81     -32.386   5.864  42.598  1.00 72.55           C  
ANISOU  387  CA  SER A  81     9343   9442   8780    281    455    579       C  
ATOM    388  C   SER A  81     -31.936   7.064  41.758  1.00 76.81           C  
ANISOU  388  C   SER A  81     9835   9882   9468    303    464    659       C  
ATOM    389  O   SER A  81     -32.696   7.521  40.902  1.00 76.48           O  
ANISOU  389  O   SER A  81     9643   9910   9507    398    551    821       O  
ATOM    390  CB  SER A  81     -33.138   6.331  43.839  1.00 77.84           C  
ANISOU  390  CB  SER A  81    10188   9983   9405    379    605    510       C  
ATOM    391  OG  SER A  81     -34.390   6.897  43.496  1.00 87.93           O  
ANISOU  391  OG  SER A  81    11357  11291  10760    529    779    647       O  
ATOM    392  N   VAL A  82     -30.700   7.562  41.987  1.00 73.72           N  
ANISOU  392  N   VAL A  82     9559   9339   9112    208    372    560       N  
ATOM    393  CA  VAL A  82     -30.123   8.686  41.229  1.00 74.07           C  
ANISOU  393  CA  VAL A  82     9571   9265   9306    198    379    632       C  
ATOM    394  C   VAL A  82     -29.817   8.247  39.783  1.00 75.75           C  
ANISOU  394  C   VAL A  82     9554   9675   9552    159    304    776       C  
ATOM    395  O   VAL A  82     -30.122   8.992  38.847  1.00 75.28           O  
ANISOU  395  O   VAL A  82     9387   9622   9593    225    374    936       O  
ATOM    396  CB  VAL A  82     -28.904   9.339  41.946  1.00 78.54           C  
ANISOU  396  CB  VAL A  82    10320   9618   9905     79    300    477       C  
ATOM    397  CG1 VAL A  82     -28.301  10.470  41.119  1.00 79.10           C  
ANISOU  397  CG1 VAL A  82    10350   9559  10148     48    318    565       C  
ATOM    398  CG2 VAL A  82     -29.299   9.857  43.325  1.00 79.96           C  
ANISOU  398  CG2 VAL A  82    10748   9606  10028    120    392    326       C  
ATOM    399  N   ALA A  83     -29.260   7.024  39.614  1.00 70.83           N  
ANISOU  399  N   ALA A  83     8865   9212   8835     62    174    723       N  
ATOM    400  CA  ALA A  83     -28.940   6.429  38.314  1.00 69.93           C  
ANISOU  400  CA  ALA A  83     8560   9293   8716     16    110    820       C  
ATOM    401  C   ALA A  83     -30.215   6.233  37.483  1.00 75.76           C  
ANISOU  401  C   ALA A  83     9143  10216   9428    104    189    970       C  
ATOM    402  O   ALA A  83     -30.270   6.682  36.336  1.00 75.56           O  
ANISOU  402  O   ALA A  83     8982  10278   9450    126    206   1118       O  
ATOM    403  CB  ALA A  83     -28.229   5.099  38.510  1.00 69.20           C  
ANISOU  403  CB  ALA A  83     8464   9300   8528    -78    -12    712       C  
ATOM    404  N   ASP A  84     -31.252   5.618  38.098  1.00 73.93           N  
ANISOU  404  N   ASP A  84     8926  10047   9119    150    238    942       N  
ATOM    405  CA  ASP A  84     -32.562   5.332  37.512  1.00 74.73           C  
ANISOU  405  CA  ASP A  84     8867  10340   9187    216    303   1071       C  
ATOM    406  C   ASP A  84     -33.358   6.590  37.137  1.00 81.26           C  
ANISOU  406  C   ASP A  84     9624  11131  10118    362    424   1244       C  
ATOM    407  O   ASP A  84     -34.005   6.584  36.091  1.00 81.55           O  
ANISOU  407  O   ASP A  84     9471  11366  10149    396    429   1407       O  
ATOM    408  CB  ASP A  84     -33.380   4.409  38.435  1.00 76.74           C  
ANISOU  408  CB  ASP A  84     9166  10640   9350    216    337    992       C  
ATOM    409  CG  ASP A  84     -32.789   3.023  38.690  1.00 89.01           C  
ANISOU  409  CG  ASP A  84    10769  12248  10804     89    232    860       C  
ATOM    410  OD1 ASP A  84     -31.720   2.709  38.109  1.00 88.95           O  
ANISOU  410  OD1 ASP A  84    10747  12257  10795      7    131    823       O  
ATOM    411  OD2 ASP A  84     -33.380   2.262  39.496  1.00 95.98           O  
ANISOU  411  OD2 ASP A  84    11706  13146  11616     79    265    803       O  
ATOM    412  N   LEU A  85     -33.309   7.661  37.967  1.00 79.33           N  
ANISOU  412  N   LEU A  85     9538  10638   9967    447    522   1212       N  
ATOM    413  CA  LEU A  85     -34.010   8.919  37.671  1.00 81.07           C  
ANISOU  413  CA  LEU A  85     9717  10773  10314    609    663   1380       C  
ATOM    414  C   LEU A  85     -33.378   9.616  36.472  1.00 85.45           C  
ANISOU  414  C   LEU A  85    10181  11333  10953    596    627   1525       C  
ATOM    415  O   LEU A  85     -34.094  10.162  35.630  1.00 86.22           O  
ANISOU  415  O   LEU A  85    10127  11528  11106    712    691   1742       O  
ATOM    416  CB  LEU A  85     -34.049   9.870  38.885  1.00 82.60           C  
ANISOU  416  CB  LEU A  85    10138  10661  10583    695    794   1278       C  
ATOM    417  CG  LEU A  85     -34.879  11.161  38.708  1.00 89.69           C  
ANISOU  417  CG  LEU A  85    11016  11430  11630    897    980   1448       C  
ATOM    418  CD1 LEU A  85     -36.366  10.916  38.943  1.00 90.69           C  
ANISOU  418  CD1 LEU A  85    11022  11701  11736   1054   1106   1549       C  
ATOM    419  CD2 LEU A  85     -34.381  12.263  39.616  1.00 93.71           C  
ANISOU  419  CD2 LEU A  85    11793  11577  12237    924   1081   1318       C  
ATOM    420  N   LEU A  86     -32.035   9.580  36.391  1.00 81.56           N  
ANISOU  420  N   LEU A  86     9768  10752  10468    457    525   1422       N  
ATOM    421  CA  LEU A  86     -31.276  10.180  35.297  1.00 81.80           C  
ANISOU  421  CA  LEU A  86     9723  10784  10574    419    495   1550       C  
ATOM    422  C   LEU A  86     -31.566   9.477  33.986  1.00 84.82           C  
ANISOU  422  C   LEU A  86     9885  11487  10857    399    430   1691       C  
ATOM    423  O   LEU A  86     -31.655  10.139  32.960  1.00 85.17           O  
ANISOU  423  O   LEU A  86     9817  11594  10948    453    462   1893       O  
ATOM    424  CB  LEU A  86     -29.776  10.179  35.609  1.00 81.38           C  
ANISOU  424  CB  LEU A  86     9784  10588  10548    262    400   1396       C  
ATOM    425  CG  LEU A  86     -29.156  11.537  35.976  1.00 88.16           C  
ANISOU  425  CG  LEU A  86    10789  11135  11571    255    466   1387       C  
ATOM    426  CD1 LEU A  86     -29.771  12.130  37.264  1.00 89.55           C  
ANISOU  426  CD1 LEU A  86    11166  11073  11786    341    576   1275       C  
ATOM    427  CD2 LEU A  86     -27.654  11.415  36.130  1.00 90.41           C  
ANISOU  427  CD2 LEU A  86    11127  11348  11877     73    346   1257       C  
ATOM    428  N   PHE A  87     -31.776   8.152  34.023  1.00 80.25           N  
ANISOU  428  N   PHE A  87     9250  11107  10133    323    346   1590       N  
ATOM    429  CA  PHE A  87     -32.114   7.402  32.821  1.00 79.76           C  
ANISOU  429  CA  PHE A  87     9000  11353   9953    282    282   1687       C  
ATOM    430  C   PHE A  87     -33.540   7.731  32.352  1.00 84.22           C  
ANISOU  430  C   PHE A  87     9406  12084  10509    410    346   1888       C  
ATOM    431  O   PHE A  87     -33.718   8.084  31.186  1.00 84.45           O  
ANISOU  431  O   PHE A  87     9290  12282  10516    439    335   2079       O  
ATOM    432  CB  PHE A  87     -31.913   5.887  33.019  1.00 80.22           C  
ANISOU  432  CB  PHE A  87     9067  11538   9875    154    188   1508       C  
ATOM    433  CG  PHE A  87     -32.372   5.050  31.843  1.00 82.17           C  
ANISOU  433  CG  PHE A  87     9145  12093   9983     92    129   1571       C  
ATOM    434  CD1 PHE A  87     -33.562   4.332  31.901  1.00 85.89           C  
ANISOU  434  CD1 PHE A  87     9527  12738  10369     86    126   1577       C  
ATOM    435  CD2 PHE A  87     -31.638   5.017  30.664  1.00 84.65           C  
ANISOU  435  CD2 PHE A  87     9389  12531  10245     31     83   1626       C  
ATOM    436  CE1 PHE A  87     -34.001   3.584  30.803  1.00 87.22           C  
ANISOU  436  CE1 PHE A  87     9547  13197  10398      1     60   1620       C  
ATOM    437  CE2 PHE A  87     -32.084   4.277  29.566  1.00 87.94           C  
ANISOU  437  CE2 PHE A  87     9669  13238  10506    -36     31   1669       C  
ATOM    438  CZ  PHE A  87     -33.257   3.561  29.644  1.00 86.27           C  
ANISOU  438  CZ  PHE A  87     9379  13194  10207    -59     11   1657       C  
ATOM    439  N   VAL A  88     -34.544   7.629  33.263  1.00 80.78           N  
ANISOU  439  N   VAL A  88     8990  11616  10088    490    416   1859       N  
ATOM    440  CA  VAL A  88     -35.962   7.890  32.965  1.00 81.66           C  
ANISOU  440  CA  VAL A  88     8925  11896  10205    621    483   2051       C  
ATOM    441  C   VAL A  88     -36.233   9.264  32.348  1.00 86.77           C  
ANISOU  441  C   VAL A  88     9501  12491  10978    789    572   2304       C  
ATOM    442  O   VAL A  88     -37.050   9.358  31.437  1.00 87.62           O  
ANISOU  442  O   VAL A  88     9395  12847  11047    855    558   2520       O  
ATOM    443  CB  VAL A  88     -36.987   7.496  34.074  1.00 85.46           C  
ANISOU  443  CB  VAL A  88     9423  12362  10686    679    562   1981       C  
ATOM    444  CG1 VAL A  88     -36.862   6.025  34.459  1.00 83.50           C  
ANISOU  444  CG1 VAL A  88     9209  12215  10303    507    470   1784       C  
ATOM    445  CG2 VAL A  88     -36.889   8.394  35.302  1.00 85.81           C  
ANISOU  445  CG2 VAL A  88     9673  12075  10855    798    703   1908       C  
ATOM    446  N   ILE A  89     -35.493  10.309  32.792  1.00 83.44           N  
ANISOU  446  N   ILE A  89     9255  11748  10700    844    654   2282       N  
ATOM    447  CA  ILE A  89     -35.615  11.678  32.277  1.00 85.28           C  
ANISOU  447  CA  ILE A  89     9463  11857  11081   1001    760   2517       C  
ATOM    448  C   ILE A  89     -35.227  11.791  30.773  1.00 87.84           C  
ANISOU  448  C   ILE A  89     9635  12393  11349    958    677   2716       C  
ATOM    449  O   ILE A  89     -35.468  12.824  30.146  1.00 89.27           O  
ANISOU  449  O   ILE A  89     9752  12538  11629   1096    755   2967       O  
ATOM    450  CB  ILE A  89     -34.932  12.710  33.231  1.00 89.51           C  
ANISOU  450  CB  ILE A  89    10255  11968  11786   1038    875   2406       C  
ATOM    451  CG1 ILE A  89     -35.587  14.107  33.146  1.00 93.42           C  
ANISOU  451  CG1 ILE A  89    10752  12275  12466   1267   1056   2632       C  
ATOM    452  CG2 ILE A  89     -33.402  12.763  33.075  1.00 88.93           C  
ANISOU  452  CG2 ILE A  89    10304  11760  11726    858    787   2282       C  
ATOM    453  CD1 ILE A  89     -35.403  15.009  34.414  1.00105.13           C  
ANISOU  453  CD1 ILE A  89    12509  13332  14103   1336   1214   2479       C  
ATOM    454  N   THR A  90     -34.664  10.701  30.202  1.00 81.41           N  
ANISOU  454  N   THR A  90     8766  11799  10365    775    531   2608       N  
ATOM    455  CA  THR A  90     -34.280  10.606  28.790  1.00 80.71           C  
ANISOU  455  CA  THR A  90     8545  11949  10171    712    452   2757       C  
ATOM    456  C   THR A  90     -35.241   9.705  27.998  1.00 84.09           C  
ANISOU  456  C   THR A  90     8760  12785  10407    680    355   2835       C  
ATOM    457  O   THR A  90     -35.161   9.669  26.768  1.00 84.69           O  
ANISOU  457  O   THR A  90     8711  13106  10363    646    291   2986       O  
ATOM    458  CB  THR A  90     -32.791  10.236  28.598  1.00 80.37           C  
ANISOU  458  CB  THR A  90     8609  11832  10095    539    387   2594       C  
ATOM    459  OG1 THR A  90     -32.579   8.843  28.846  1.00 75.41           O  
ANISOU  459  OG1 THR A  90     7996  11334   9324    392    286   2360       O  
ATOM    460  CG2 THR A  90     -31.844  11.108  29.424  1.00 76.69           C  
ANISOU  460  CG2 THR A  90     8338  10982   9818    536    461   2507       C  
ATOM    461  N   LEU A  91     -36.172   9.009  28.695  1.00 79.09           N  
ANISOU  461  N   LEU A  91     8084  12229   9737    683    346   2739       N  
ATOM    462  CA  LEU A  91     -37.167   8.146  28.052  1.00 79.17           C  
ANISOU  462  CA  LEU A  91     7886  12617   9578    626    251   2798       C  
ATOM    463  C   LEU A  91     -38.120   8.865  27.087  1.00 85.68           C  
ANISOU  463  C   LEU A  91     8479  13688  10386    767    251   3135       C  
ATOM    464  O   LEU A  91     -38.467   8.242  26.086  1.00 85.29           O  
ANISOU  464  O   LEU A  91     8267  13991  10148    667    129   3198       O  
ATOM    465  CB  LEU A  91     -37.915   7.240  29.035  1.00 78.41           C  
ANISOU  465  CB  LEU A  91     7791  12539   9463    579    252   2629       C  
ATOM    466  CG  LEU A  91     -37.130   6.052  29.621  1.00 80.75           C  
ANISOU  466  CG  LEU A  91     8251  12744   9684    390    193   2318       C  
ATOM    467  CD1 LEU A  91     -37.882   5.431  30.761  1.00 80.55           C  
ANISOU  467  CD1 LEU A  91     8254  12671   9680    384    236   2194       C  
ATOM    468  CD2 LEU A  91     -36.833   4.979  28.565  1.00 82.40           C  
ANISOU  468  CD2 LEU A  91     8391  13223   9695    200     59   2244       C  
ATOM    469  N   PRO A  92     -38.513  10.161  27.278  1.00 85.05           N  
ANISOU  469  N   PRO A  92     8382  13444  10490    995    382   3362       N  
ATOM    470  CA  PRO A  92     -39.349  10.824  26.256  1.00 87.87           C  
ANISOU  470  CA  PRO A  92     8504  14058  10824   1142    371   3718       C  
ATOM    471  C   PRO A  92     -38.624  10.938  24.907  1.00 93.11           C  
ANISOU  471  C   PRO A  92     9132  14900  11346   1061    281   3845       C  
ATOM    472  O   PRO A  92     -39.267  10.836  23.864  1.00 94.23           O  
ANISOU  472  O   PRO A  92     9059  15412  11333   1068    184   4058       O  
ATOM    473  CB  PRO A  92     -39.621  12.211  26.859  1.00 91.19           C  
ANISOU  473  CB  PRO A  92     8987  14158  11503   1405    562   3895       C  
ATOM    474  CG  PRO A  92     -39.378  12.051  28.319  1.00 93.85           C  
ANISOU  474  CG  PRO A  92     9541  14160  11957   1388    660   3610       C  
ATOM    475  CD  PRO A  92     -38.239  11.089  28.396  1.00 86.71           C  
ANISOU  475  CD  PRO A  92     8788  13230  10928   1134    547   3312       C  
ATOM    476  N   PHE A  93     -37.274  11.104  24.936  1.00 89.34           N  
ANISOU  476  N   PHE A  93     8859  14180  10907    972    309   3709       N  
ATOM    477  CA  PHE A  93     -36.407  11.187  23.747  1.00 89.82           C  
ANISOU  477  CA  PHE A  93     8915  14373  10840    883    253   3799       C  
ATOM    478  C   PHE A  93     -36.394   9.855  23.010  1.00 92.22           C  
ANISOU  478  C   PHE A  93     9138  15042  10861    675     95   3654       C  
ATOM    479  O   PHE A  93     -36.474   9.848  21.783  1.00 93.18           O  
ANISOU  479  O   PHE A  93     9136  15471  10798    646     22   3828       O  
ATOM    480  CB  PHE A  93     -34.975  11.603  24.118  1.00 90.68           C  
ANISOU  480  CB  PHE A  93     9248  14126  11082    823    330   3661       C  
ATOM    481  CG  PHE A  93     -34.867  12.947  24.790  1.00 93.74           C  
ANISOU  481  CG  PHE A  93     9750  14123  11745    992    489   3778       C  
ATOM    482  CD1 PHE A  93     -34.752  14.111  24.039  1.00 99.19           C  
ANISOU  482  CD1 PHE A  93    10407  14758  12522   1118    570   4090       C  
ATOM    483  CD2 PHE A  93     -34.865  13.050  26.177  1.00 95.37           C  
ANISOU  483  CD2 PHE A  93    10113  14005  12116   1020    566   3571       C  
ATOM    484  CE1 PHE A  93     -34.648  15.358  24.663  1.00101.49           C  
ANISOU  484  CE1 PHE A  93    10829  14650  13083   1265    733   4185       C  
ATOM    485  CE2 PHE A  93     -34.759  14.297  26.801  1.00 99.60           C  
ANISOU  485  CE2 PHE A  93    10784  14162  12898   1163    722   3650       C  
ATOM    486  CZ  PHE A  93     -34.647  15.443  26.039  1.00 99.91           C  
ANISOU  486  CZ  PHE A  93    10795  14124  13042   1281    809   3950       C  
ATOM    487  N   TRP A  94     -36.312   8.734  23.770  1.00 86.15           N  
ANISOU  487  N   TRP A  94     8449  14231  10053    532     50   3337       N  
ATOM    488  CA  TRP A  94     -36.373   7.353  23.282  1.00 85.16           C  
ANISOU  488  CA  TRP A  94     8280  14390   9687    326    -80   3147       C  
ATOM    489  C   TRP A  94     -37.768   7.114  22.674  1.00 91.49           C  
ANISOU  489  C   TRP A  94     8837  15580  10344    335   -177   3319       C  
ATOM    490  O   TRP A  94     -37.879   6.502  21.606  1.00 92.29           O  
ANISOU  490  O   TRP A  94     8846  16021  10201    200   -294   3327       O  
ATOM    491  CB  TRP A  94     -36.209   6.378  24.461  1.00 81.60           C  
ANISOU  491  CB  TRP A  94     7964  13750   9288    221    -77   2823       C  
ATOM    492  CG  TRP A  94     -34.808   6.080  24.894  1.00 80.44           C  
ANISOU  492  CG  TRP A  94     8027  13341   9195    136    -44   2594       C  
ATOM    493  CD1 TRP A  94     -33.975   6.898  25.596  1.00 82.79           C  
ANISOU  493  CD1 TRP A  94     8469  13299   9690    215     48   2580       C  
ATOM    494  CD2 TRP A  94     -34.144   4.812  24.804  1.00 78.81           C  
ANISOU  494  CD2 TRP A  94     7907  13179   8860    -44   -104   2331       C  
ATOM    495  NE1 TRP A  94     -32.798   6.243  25.881  1.00 80.66           N  
ANISOU  495  NE1 TRP A  94     8340  12894   9412     94     33   2346       N  
ATOM    496  CE2 TRP A  94     -32.878   4.958  25.408  1.00 81.45           C  
ANISOU  496  CE2 TRP A  94     8410  13216   9321    -50    -49   2197       C  
ATOM    497  CE3 TRP A  94     -34.480   3.573  24.231  1.00 80.01           C  
ANISOU  497  CE3 TRP A  94     8010  13588   8802   -206   -194   2198       C  
ATOM    498  CZ2 TRP A  94     -31.948   3.913  25.455  1.00 79.37           C  
ANISOU  498  CZ2 TRP A  94     8249  12915   8991   -182    -76   1959       C  
ATOM    499  CZ3 TRP A  94     -33.557   2.542  24.274  1.00 79.97           C  
ANISOU  499  CZ3 TRP A  94     8137  13513   8734   -340   -205   1944       C  
ATOM    500  CH2 TRP A  94     -32.308   2.716  24.878  1.00 79.23           C  
ANISOU  500  CH2 TRP A  94     8194  13131   8779   -313   -144   1839       C  
ATOM    501  N   ALA A  95     -38.826   7.607  23.377  1.00 88.69           N  
ANISOU  501  N   ALA A  95     8377  15179  10140    491   -123   3452       N  
ATOM    502  CA  ALA A  95     -40.234   7.481  23.006  1.00 90.48           C  
ANISOU  502  CA  ALA A  95     8338  15756  10284    526   -202   3638       C  
ATOM    503  C   ALA A  95     -40.574   8.150  21.686  1.00 97.08           C  
ANISOU  503  C   ALA A  95     8985  16909  10993    607   -272   3978       C  
ATOM    504  O   ALA A  95     -41.252   7.531  20.871  1.00 98.86           O  
ANISOU  504  O   ALA A  95     9023  17545  10993    487   -423   4030       O  
ATOM    505  CB  ALA A  95     -41.129   8.015  24.114  1.00 91.58           C  
ANISOU  505  CB  ALA A  95     8422  15724  10652    717    -85   3721       C  
ATOM    506  N   VAL A  96     -40.123   9.403  21.472  1.00 93.71           N  
ANISOU  506  N   VAL A  96     8606  16298  10701    800   -165   4213       N  
ATOM    507  CA  VAL A  96     -40.390  10.150  20.233  1.00 96.00           C  
ANISOU  507  CA  VAL A  96     8730  16863  10881    906   -213   4581       C  
ATOM    508  C   VAL A  96     -39.669   9.486  19.051  1.00 98.91           C  
ANISOU  508  C   VAL A  96     9131  17503  10946    692   -337   4499       C  
ATOM    509  O   VAL A  96     -40.294   9.241  18.015  1.00100.38           O  
ANISOU  509  O   VAL A  96     9126  18128  10887    637   -480   4660       O  
ATOM    510  CB  VAL A  96     -40.069  11.671  20.366  1.00101.04           C  
ANISOU  510  CB  VAL A  96     9438  17184  11770   1167    -41   4856       C  
ATOM    511  CG1 VAL A  96     -40.174  12.396  19.023  1.00103.79           C  
ANISOU  511  CG1 VAL A  96     9644  17805  11987   1264    -86   5244       C  
ATOM    512  CG2 VAL A  96     -40.973  12.340  21.400  1.00101.66           C  
ANISOU  512  CG2 VAL A  96     9461  17048  12118   1401     89   4965       C  
ATOM    513  N   ASP A  97     -38.373   9.157  19.244  1.00 92.87           N  
ANISOU  513  N   ASP A  97     8605  16489  10193    569   -281   4238       N  
ATOM    514  CA  ASP A  97     -37.476   8.515  18.277  1.00 92.31           C  
ANISOU  514  CA  ASP A  97     8612  16592   9870    378   -346   4111       C  
ATOM    515  C   ASP A  97     -38.038   7.214  17.693  1.00 96.93           C  
ANISOU  515  C   ASP A  97     9103  17575  10151    158   -515   3940       C  
ATOM    516  O   ASP A  97     -37.784   6.913  16.527  1.00 97.77           O  
ANISOU  516  O   ASP A  97     9186  17983   9980     46   -595   3970       O  
ATOM    517  CB  ASP A  97     -36.094   8.302  18.913  1.00 91.29           C  
ANISOU  517  CB  ASP A  97     8733  16082   9870    303   -241   3831       C  
ATOM    518  CG  ASP A  97     -35.192   7.310  18.213  1.00101.05           C  
ANISOU  518  CG  ASP A  97    10066  17456  10873     94   -288   3599       C  
ATOM    519  OD1 ASP A  97     -35.160   6.136  18.644  1.00 99.60           O  
ANISOU  519  OD1 ASP A  97     9949  17268  10627    -61   -337   3286       O  
ATOM    520  OD2 ASP A  97     -34.503   7.710  17.247  1.00109.30           O  
ANISOU  520  OD2 ASP A  97    11126  18599  11803     92   -260   3734       O  
ATOM    521  N   ALA A  98     -38.803   6.473  18.488  1.00 92.97           N  
ANISOU  521  N   ALA A  98     8554  17072   9698     89   -562   3764       N  
ATOM    522  CA  ALA A  98     -39.463   5.269  18.000  1.00 93.61           C  
ANISOU  522  CA  ALA A  98     8536  17513   9519   -136   -722   3606       C  
ATOM    523  C   ALA A  98     -40.431   5.640  16.882  1.00101.24           C  
ANISOU  523  C   ALA A  98     9242  18952  10274   -109   -860   3925       C  
ATOM    524  O   ALA A  98     -40.339   5.124  15.769  1.00102.99           O  
ANISOU  524  O   ALA A  98     9440  19511  10181   -274   -979   3894       O  
ATOM    525  CB  ALA A  98     -40.196   4.569  19.131  1.00 93.08           C  
ANISOU  525  CB  ALA A  98     8445  17338   9585   -193   -726   3417       C  
ATOM    526  N   VAL A  99     -41.360   6.540  17.187  1.00 99.39           N  
ANISOU  526  N   VAL A  99     8813  18745  10206    108   -842   4234       N  
ATOM    527  CA  VAL A  99     -42.347   6.984  16.210  1.00103.06           C  
ANISOU  527  CA  VAL A  99     8995  19662  10500    173   -977   4589       C  
ATOM    528  C   VAL A  99     -42.128   8.080  15.172  1.00109.19           C  
ANISOU  528  C   VAL A  99     9706  20590  11189    343   -972   4975       C  
ATOM    529  O   VAL A  99     -42.556   7.957  14.024  1.00111.23           O  
ANISOU  529  O   VAL A  99     9805  21311  11145    266  -1134   5143       O  
ATOM    530  CB  VAL A  99     -43.553   7.657  16.891  1.00108.45           C  
ANISOU  530  CB  VAL A  99     9444  20343  11418    398   -944   4851       C  
ATOM    531  N   ALA A 100     -41.458   9.152  15.583  1.00105.49           N  
ANISOU  531  N   ALA A 100     9370  19732  10981    563   -786   5116       N  
ATOM    532  CA  ALA A 100     -41.181  10.271  14.691  1.00108.17           C  
ANISOU  532  CA  ALA A 100     9673  20142  11284    739   -746   5500       C  
ATOM    533  C   ALA A 100     -39.677  10.241  14.938  1.00111.47           C  
ANISOU  533  C   ALA A 100    10397  20174  11783    663   -604   5254       C  
ATOM    534  O   ALA A 100     -39.204   9.584  15.865  1.00109.78           O  
ANISOU  534  O   ALA A 100    10347  19675  11691    553   -550   4893       O  
ATOM    535  CB  ALA A 100     -41.399  11.648  15.299  1.00109.61           C  
ANISOU  535  CB  ALA A 100     9832  19995  11821   1066   -573   5812       C  
ATOM    536  N   ASN A 101     -38.930  10.958  14.104  1.00108.89           N  
ANISOU  536  N   ASN A 101    10134  19851  11389    725   -543   5467       N  
ATOM    537  CA  ASN A 101     -37.479  11.014  14.231  1.00106.69           C  
ANISOU  537  CA  ASN A 101    10108  19240  11188    655   -405   5280       C  
ATOM    538  C   ASN A 101     -36.692  12.007  15.079  1.00109.16           C  
ANISOU  538  C   ASN A 101    10587  19016  11874    804   -200   5314       C  
ATOM    539  O   ASN A 101     -37.267  12.760  15.864  1.00109.42           O  
ANISOU  539  O   ASN A 101    10583  18810  12181    996   -121   5453       O  
ATOM    540  CB  ASN A 101     -37.163  11.222  12.748  1.00109.31           C  
ANISOU  540  CB  ASN A 101    10396  19930  11207    620   -455   5514       C  
ATOM    541  CG  ASN A 101     -36.940  12.680  12.399  1.00123.30           C  
ANISOU  541  CG  ASN A 101    12157  21556  13138    852   -324   5945       C  
ATOM    542  OD1 ASN A 101     -37.527  13.574  13.011  1.00114.31           O  
ANISOU  542  OD1 ASN A 101    10952  20201  12281   1074   -251   6168       O  
ATOM    543  ND2 ASN A 101     -36.089  12.929  11.411  1.00114.48           N  
ANISOU  543  ND2 ASN A 101    11111  20543  11844    806   -278   6067       N  
ATOM    544  N   TRP A 102     -35.373  12.003  14.914  1.00103.90           N  
ANISOU  544  N   TRP A 102    10101  18162  11214    707   -109   5182       N  
ATOM    545  CA  TRP A 102     -34.504  12.902  15.664  1.00102.60           C  
ANISOU  545  CA  TRP A 102    10098  17499  11386    797     71   5190       C  
ATOM    546  C   TRP A 102     -34.798  14.361  15.331  1.00110.11           C  
ANISOU  546  C   TRP A 102    10990  18349  12496   1032    175   5639       C  
ATOM    547  O   TRP A 102     -34.758  14.762  14.168  1.00113.02           O  
ANISOU  547  O   TRP A 102    11281  18977  12683   1066    161   5938       O  
ATOM    548  CB  TRP A 102     -33.034  12.584  15.384  1.00 99.95           C  
ANISOU  548  CB  TRP A 102     9921  17056  11000    633    136   4996       C  
ATOM    549  CG  TRP A 102     -32.178  12.574  16.612  1.00 98.07           C  
ANISOU  549  CG  TRP A 102     9857  16357  11047    588    232   4715       C  
ATOM    550  CD1 TRP A 102     -30.983  13.210  16.784  1.00100.57           C  
ANISOU  550  CD1 TRP A 102    10302  16358  11552    568    364   4716       C  
ATOM    551  CD2 TRP A 102     -32.450  11.894  17.844  1.00 95.43           C  
ANISOU  551  CD2 TRP A 102     9583  15845  10832    546    196   4400       C  
ATOM    552  NE1 TRP A 102     -30.494  12.968  18.045  1.00 97.41           N  
ANISOU  552  NE1 TRP A 102    10031  15610  11370    513    395   4416       N  
ATOM    553  CE2 TRP A 102     -31.377  12.163  18.716  1.00 97.60           C  
ANISOU  553  CE2 TRP A 102    10024  15709  11349    507    297   4223       C  
ATOM    554  CE3 TRP A 102     -33.498  11.085  18.294  1.00 96.13           C  
ANISOU  554  CE3 TRP A 102     9593  16089  10842    528     87   4260       C  
ATOM    555  CZ2 TRP A 102     -31.320  11.652  20.011  1.00 94.56           C  
ANISOU  555  CZ2 TRP A 102     9741  15080  11109    463    288   3918       C  
ATOM    556  CZ3 TRP A 102     -33.440  10.578  19.580  1.00 95.13           C  
ANISOU  556  CZ3 TRP A 102     9571  15701  10872    486     98   3962       C  
ATOM    557  CH2 TRP A 102     -32.359  10.864  20.423  1.00 94.01           C  
ANISOU  557  CH2 TRP A 102     9605  15163  10950    460    194   3798       C  
ATOM    558  N   TYR A 103     -35.092  15.150  16.359  1.00106.48           N  
ANISOU  558  N   TYR A 103    10580  17505  12373   1196    288   5687       N  
ATOM    559  CA  TYR A 103     -35.393  16.577  16.176  1.00109.48           C  
ANISOU  559  CA  TYR A 103    10929  17710  12957   1442    417   6103       C  
ATOM    560  C   TYR A 103     -34.430  17.243  17.170  1.00112.03           C  
ANISOU  560  C   TYR A 103    11485  17459  13622   1439    594   5948       C  
ATOM    561  O   TYR A 103     -34.099  18.421  17.029  1.00113.29           O  
ANISOU  561  O   TYR A 103    11712  17349  13982   1562    742   6209       O  
ATOM    562  CB  TYR A 103     -36.821  17.119  16.415  1.00113.02           C  
ANISOU  562  CB  TYR A 103    11205  18225  13514   1695    416   6377       C  
ATOM    563  CG  TYR A 103     -37.909  16.427  15.618  1.00116.43           C  
ANISOU  563  CG  TYR A 103    11377  19232  13632   1686    216   6508       C  
ATOM    564  CD1 TYR A 103     -38.665  15.400  16.175  1.00116.60           C  
ANISOU  564  CD1 TYR A 103    11302  19430  13570   1595     92   6249       C  
ATOM    565  CD2 TYR A 103     -38.197  16.816  14.312  1.00120.89           C  
ANISOU  565  CD2 TYR A 103    11786  20169  13978   1760    148   6902       C  
ATOM    566  CE1 TYR A 103     -39.671  14.764  15.448  1.00118.86           C  
ANISOU  566  CE1 TYR A 103    11339  20249  13572   1555   -103   6361       C  
ATOM    567  CE2 TYR A 103     -39.201  16.187  13.575  1.00123.80           C  
ANISOU  567  CE2 TYR A 103    11907  21092  14039   1730    -58   7018       C  
ATOM    568  CZ  TYR A 103     -39.934  15.159  14.146  1.00129.41           C  
ANISOU  568  CZ  TYR A 103    12520  21968  14681   1617   -187   6738       C  
ATOM    569  OH  TYR A 103     -40.928  14.540  13.421  1.00132.45           O  
ANISOU  569  OH  TYR A 103    12652  22906  14768   1558   -400   6845       O  
ATOM    570  N   PHE A 104     -34.001  16.479  18.175  1.00106.15           N  
ANISOU  570  N   PHE A 104    10863  16532  12938   1290    573   5529       N  
ATOM    571  CA  PHE A 104     -33.174  16.876  19.321  1.00104.39           C  
ANISOU  571  CA  PHE A 104    10854  15804  13005   1250    695   5300       C  
ATOM    572  C   PHE A 104     -31.732  17.333  19.063  1.00108.83           C  
ANISOU  572  C   PHE A 104    11555  16139  13657   1124    786   5284       C  
ATOM    573  O   PHE A 104     -31.168  18.058  19.890  1.00108.71           O  
ANISOU  573  O   PHE A 104    11700  15683  13920   1128    906   5207       O  
ATOM    574  CB  PHE A 104     -33.270  15.818  20.438  1.00102.85           C  
ANISOU  574  CB  PHE A 104    10720  15554  12802   1135    619   4883       C  
ATOM    575  CG  PHE A 104     -34.630  15.161  20.501  1.00104.11           C  
ANISOU  575  CG  PHE A 104    10711  16021  12825   1205    513   4893       C  
ATOM    576  CD1 PHE A 104     -34.816  13.867  20.033  1.00105.75           C  
ANISOU  576  CD1 PHE A 104    10821  16615  12743   1043    352   4728       C  
ATOM    577  CD2 PHE A 104     -35.745  15.872  20.931  1.00107.82           C  
ANISOU  577  CD2 PHE A 104    11105  16409  13453   1436    584   5095       C  
ATOM    578  CE1 PHE A 104     -36.080  13.275  20.052  1.00107.11           C  
ANISOU  578  CE1 PHE A 104    10820  17082  12793   1079    248   4748       C  
ATOM    579  CE2 PHE A 104     -37.011  15.282  20.940  1.00111.08           C  
ANISOU  579  CE2 PHE A 104    11323  17136  13745   1494    486   5132       C  
ATOM    580  CZ  PHE A 104     -37.168  13.986  20.508  1.00107.91           C  
ANISOU  580  CZ  PHE A 104    10823  17117  13061   1302    311   4956       C  
ATOM    581  N   GLY A 105     -31.158  16.926  17.934  1.00105.52           N  
ANISOU  581  N   GLY A 105    11072  16020  12999   1009    735   5353       N  
ATOM    582  CA  GLY A 105     -29.800  17.306  17.562  1.00105.33           C  
ANISOU  582  CA  GLY A 105    11142  15840  13040    886    828   5367       C  
ATOM    583  C   GLY A 105     -28.729  16.286  17.887  1.00106.10           C  
ANISOU  583  C   GLY A 105    11309  15935  13070    661    776   4984       C  
ATOM    584  O   GLY A 105     -29.029  15.185  18.361  1.00102.95           O  
ANISOU  584  O   GLY A 105    10899  15665  12551    593    663   4696       O  
ATOM    585  N   ASN A 106     -27.460  16.671  17.635  1.00103.31           N  
ANISOU  585  N   ASN A 106    11020  15424  12808    549    871   4998       N  
ATOM    586  CA  ASN A 106     -26.265  15.847  17.828  1.00100.93           C  
ANISOU  586  CA  ASN A 106    10763  15114  12472    351    849   4693       C  
ATOM    587  C   ASN A 106     -25.740  15.773  19.264  1.00101.77           C  
ANISOU  587  C   ASN A 106    10995  14847  12828    273    844   4381       C  
ATOM    588  O   ASN A 106     -25.272  14.706  19.672  1.00 98.78           O  
ANISOU  588  O   ASN A 106    10629  14535  12369    156    764   4074       O  
ATOM    589  CB  ASN A 106     -25.163  16.259  16.860  1.00103.59           C  
ANISOU  589  CB  ASN A 106    11077  15498  12784    266    955   4868       C  
ATOM    590  CG  ASN A 106     -24.192  15.151  16.553  1.00130.51           C  
ANISOU  590  CG  ASN A 106    14463  19100  16023    102    925   4622       C  
ATOM    591  OD1 ASN A 106     -24.565  14.068  16.085  1.00124.70           O  
ANISOU  591  OD1 ASN A 106    13676  18704  15002     81    832   4496       O  
ATOM    592  ND2 ASN A 106     -22.915  15.407  16.788  1.00124.72           N  
ANISOU  592  ND2 ASN A 106    13764  18156  15469    -19   1009   4551       N  
ATOM    593  N   PHE A 107     -25.791  16.894  20.021  1.00 98.90           N  
ANISOU  593  N   PHE A 107    10731  14088  12757    335    932   4456       N  
ATOM    594  CA  PHE A 107     -25.333  16.935  21.414  1.00 97.04           C  
ANISOU  594  CA  PHE A 107    10632  13496  12742    255    923   4166       C  
ATOM    595  C   PHE A 107     -26.188  16.039  22.298  1.00 98.79           C  
ANISOU  595  C   PHE A 107    10873  13782  12880    300    813   3916       C  
ATOM    596  O   PHE A 107     -25.657  15.355  23.176  1.00 96.32           O  
ANISOU  596  O   PHE A 107    10626  13380  12590    187    745   3609       O  
ATOM    597  CB  PHE A 107     -25.314  18.373  21.967  1.00100.77           C  
ANISOU  597  CB  PHE A 107    11230  13532  13526    313   1054   4301       C  
ATOM    598  CG  PHE A 107     -24.927  18.465  23.428  1.00101.22           C  
ANISOU  598  CG  PHE A 107    11445  13231  13781    226   1038   3994       C  
ATOM    599  CD1 PHE A 107     -25.888  18.690  24.407  1.00104.02           C  
ANISOU  599  CD1 PHE A 107    11901  13400  14220    354   1049   3906       C  
ATOM    600  CD2 PHE A 107     -23.605  18.286  23.829  1.00102.85           C  
ANISOU  600  CD2 PHE A 107    11691  13314  14074     15   1008   3791       C  
ATOM    601  CE1 PHE A 107     -25.533  18.751  25.758  1.00104.21           C  
ANISOU  601  CE1 PHE A 107    12087  13118  14389    266   1031   3612       C  
ATOM    602  CE2 PHE A 107     -23.252  18.350  25.180  1.00104.89           C  
ANISOU  602  CE2 PHE A 107    12093  13277  14483    -77    970   3507       C  
ATOM    603  CZ  PHE A 107     -24.218  18.585  26.134  1.00102.83           C  
ANISOU  603  CZ  PHE A 107    11956  12834  14282     46    981   3415       C  
ATOM    604  N   LEU A 108     -27.509  16.053  22.064  1.00 95.88           N  
ANISOU  604  N   LEU A 108    10436  13577  12416    466    797   4067       N  
ATOM    605  CA  LEU A 108     -28.471  15.248  22.810  1.00 93.77           C  
ANISOU  605  CA  LEU A 108    10162  13398  12067    517    708   3877       C  
ATOM    606  C   LEU A 108     -28.421  13.776  22.408  1.00 94.31           C  
ANISOU  606  C   LEU A 108    10146  13824  11863    404    577   3690       C  
ATOM    607  O   LEU A 108     -28.766  12.925  23.221  1.00 91.87           O  
ANISOU  607  O   LEU A 108     9869  13522  11514    372    503   3444       O  
ATOM    608  CB  LEU A 108     -29.883  15.842  22.676  1.00 95.70           C  
ANISOU  608  CB  LEU A 108    10333  13698  12330    734    747   4130       C  
ATOM    609  CG  LEU A 108     -30.438  16.616  23.889  1.00101.14           C  
ANISOU  609  CG  LEU A 108    11146  14016  13266    864    843   4090       C  
ATOM    610  CD1 LEU A 108     -29.463  17.676  24.414  1.00102.18           C  
ANISOU  610  CD1 LEU A 108    11457  13702  13664    814    963   4066       C  
ATOM    611  CD2 LEU A 108     -31.738  17.291  23.539  1.00106.70           C  
ANISOU  611  CD2 LEU A 108    11744  14797  14002   1105    907   4404       C  
ATOM    612  N   CYS A 109     -27.939  13.476  21.180  1.00 90.67           N  
ANISOU  612  N   CYS A 109     9596  13638  11218    336    563   3798       N  
ATOM    613  CA  CYS A 109     -27.763  12.116  20.660  1.00 88.77           C  
ANISOU  613  CA  CYS A 109     9298  13719  10713    220    465   3616       C  
ATOM    614  C   CYS A 109     -26.722  11.370  21.500  1.00 89.95           C  
ANISOU  614  C   CYS A 109     9544  13698  10935     84    442   3286       C  
ATOM    615  O   CYS A 109     -26.956  10.229  21.907  1.00 88.25           O  
ANISOU  615  O   CYS A 109     9340  13580  10609     30    357   3047       O  
ATOM    616  CB  CYS A 109     -27.371  12.154  19.185  1.00 90.46           C  
ANISOU  616  CB  CYS A 109     9423  14221  10727    187    491   3815       C  
ATOM    617  SG  CYS A 109     -27.032  10.530  18.461  1.00 93.41           S  
ANISOU  617  SG  CYS A 109     9761  14959  10771     39    407   3572       S  
ATOM    618  N   LYS A 110     -25.581  12.043  21.762  1.00 85.54           N  
ANISOU  618  N   LYS A 110     9046  12883  10571     27    516   3290       N  
ATOM    619  CA  LYS A 110     -24.468  11.562  22.576  1.00 82.98           C  
ANISOU  619  CA  LYS A 110     8793  12383  10354    -95    494   3026       C  
ATOM    620  C   LYS A 110     -24.896  11.518  24.049  1.00 85.44           C  
ANISOU  620  C   LYS A 110     9216  12445  10802    -71    445   2833       C  
ATOM    621  O   LYS A 110     -24.586  10.548  24.747  1.00 83.22           O  
ANISOU  621  O   LYS A 110     8975  12157  10487   -138    371   2578       O  
ATOM    622  CB  LYS A 110     -23.251  12.494  22.415  1.00 85.75           C  
ANISOU  622  CB  LYS A 110     9152  12537  10892   -168    586   3132       C  
ATOM    623  CG  LYS A 110     -22.648  12.472  21.023  1.00 90.33           C  
ANISOU  623  CG  LYS A 110     9627  13359  11336   -206    654   3306       C  
ATOM    624  CD  LYS A 110     -21.639  13.590  20.794  1.00 92.43           C  
ANISOU  624  CD  LYS A 110     9888  13425  11806   -269    767   3479       C  
ATOM    625  CE  LYS A 110     -21.052  13.569  19.401  1.00 93.14           C  
ANISOU  625  CE  LYS A 110     9873  13771  11746   -301    855   3668       C  
ATOM    626  NZ  LYS A 110     -20.284  12.325  19.118  1.00 94.08           N  
ANISOU  626  NZ  LYS A 110     9936  14104  11708   -384    830   3458       N  
ATOM    627  N   ALA A 111     -25.628  12.570  24.506  1.00 82.65           N  
ANISOU  627  N   ALA A 111     8919  11888  10597     38    500   2965       N  
ATOM    628  CA  ALA A 111     -26.108  12.720  25.882  1.00 81.21           C  
ANISOU  628  CA  ALA A 111     8860  11456  10542     79    487   2807       C  
ATOM    629  C   ALA A 111     -26.991  11.561  26.327  1.00 81.92           C  
ANISOU  629  C   ALA A 111     8934  11718  10473    106    400   2640       C  
ATOM    630  O   ALA A 111     -26.789  11.062  27.431  1.00 79.89           O  
ANISOU  630  O   ALA A 111     8776  11327  10253     57    353   2405       O  
ATOM    631  CB  ALA A 111     -26.828  14.047  26.059  1.00 83.90           C  
ANISOU  631  CB  ALA A 111     9251  11578  11048    219    595   3010       C  
ATOM    632  N   VAL A 112     -27.931  11.105  25.468  1.00 78.00           N  
ANISOU  632  N   VAL A 112     8314  11530   9794    168    374   2763       N  
ATOM    633  CA  VAL A 112     -28.801   9.968  25.793  1.00 76.17           C  
ANISOU  633  CA  VAL A 112     8052  11478   9411    166    293   2614       C  
ATOM    634  C   VAL A 112     -28.038   8.638  25.787  1.00 78.98           C  
ANISOU  634  C   VAL A 112     8424  11944   9640     23    214   2372       C  
ATOM    635  O   VAL A 112     -28.389   7.736  26.543  1.00 77.09           O  
ANISOU  635  O   VAL A 112     8229  11704   9355     -6    160   2179       O  
ATOM    636  CB  VAL A 112     -30.137   9.900  25.005  1.00 80.60           C  
ANISOU  636  CB  VAL A 112     8466  12332   9827    258    273   2808       C  
ATOM    637  CG1 VAL A 112     -30.958  11.172  25.187  1.00 81.81           C  
ANISOU  637  CG1 VAL A 112     8602  12348  10135    436    364   3047       C  
ATOM    638  CG2 VAL A 112     -29.912   9.596  23.526  1.00 81.50           C  
ANISOU  638  CG2 VAL A 112     8462  12765   9738    202    239   2935       C  
ATOM    639  N   HIS A 113     -26.987   8.527  24.947  1.00 76.23           N  
ANISOU  639  N   HIS A 113     8041  11678   9243    -56    225   2393       N  
ATOM    640  CA  HIS A 113     -26.166   7.321  24.857  1.00 75.01           C  
ANISOU  640  CA  HIS A 113     7898  11614   8987   -167    180   2182       C  
ATOM    641  C   HIS A 113     -25.264   7.189  26.073  1.00 78.67           C  
ANISOU  641  C   HIS A 113     8468  11813   9612   -216    160   1989       C  
ATOM    642  O   HIS A 113     -25.124   6.085  26.592  1.00 77.14           O  
ANISOU  642  O   HIS A 113     8316  11635   9360   -261    104   1785       O  
ATOM    643  CB  HIS A 113     -25.354   7.294  23.557  1.00 76.66           C  
ANISOU  643  CB  HIS A 113     8029  12005   9092   -218    223   2279       C  
ATOM    644  CG  HIS A 113     -26.084   6.652  22.421  1.00 80.77           C  
ANISOU  644  CG  HIS A 113     8469  12867   9351   -226    198   2332       C  
ATOM    645  ND1 HIS A 113     -26.863   7.395  21.550  1.00 84.31           N  
ANISOU  645  ND1 HIS A 113     8831  13487   9717   -158    214   2593       N  
ATOM    646  CD2 HIS A 113     -26.145   5.349  22.059  1.00 81.95           C  
ANISOU  646  CD2 HIS A 113     8620  13209   9309   -300    156   2152       C  
ATOM    647  CE1 HIS A 113     -27.358   6.526  20.684  1.00 84.22           C  
ANISOU  647  CE1 HIS A 113     8764  13789   9445   -208    164   2557       C  
ATOM    648  NE2 HIS A 113     -26.953   5.283  20.947  1.00 83.23           N  
ANISOU  648  NE2 HIS A 113     8699  13675   9250   -301    134   2283       N  
ATOM    649  N   VAL A 114     -24.689   8.318  26.551  1.00 76.42           N  
ANISOU  649  N   VAL A 114     8230  11281   9526   -212    202   2056       N  
ATOM    650  CA  VAL A 114     -23.823   8.335  27.734  1.00 75.70           C  
ANISOU  650  CA  VAL A 114     8234  10947   9581   -275    164   1884       C  
ATOM    651  C   VAL A 114     -24.581   8.089  29.040  1.00 77.64           C  
ANISOU  651  C   VAL A 114     8596  11058   9845   -235    119   1738       C  
ATOM    652  O   VAL A 114     -24.071   7.361  29.887  1.00 75.76           O  
ANISOU  652  O   VAL A 114     8419  10758   9607   -288     51   1549       O  
ATOM    653  CB  VAL A 114     -22.809   9.509  27.817  1.00 81.46           C  
ANISOU  653  CB  VAL A 114     8978  11465  10508   -332    210   1967       C  
ATOM    654  CG1 VAL A 114     -21.858   9.504  26.630  1.00 82.19           C  
ANISOU  654  CG1 VAL A 114     8947  11706  10574   -392    257   2079       C  
ATOM    655  CG2 VAL A 114     -23.503  10.859  27.937  1.00 82.96           C  
ANISOU  655  CG2 VAL A 114     9226  11472  10824   -256    288   2132       C  
ATOM    656  N   ILE A 115     -25.804   8.660  29.188  1.00 74.76           N  
ANISOU  656  N   ILE A 115     8252  10664   9487   -130    165   1839       N  
ATOM    657  CA  ILE A 115     -26.660   8.469  30.373  1.00 74.11           C  
ANISOU  657  CA  ILE A 115     8273  10475   9412    -75    153   1722       C  
ATOM    658  C   ILE A 115     -27.136   7.009  30.458  1.00 76.71           C  
ANISOU  658  C   ILE A 115     8574  10998   9574   -100     87   1590       C  
ATOM    659  O   ILE A 115     -27.048   6.411  31.530  1.00 74.69           O  
ANISOU  659  O   ILE A 115     8417  10646   9314   -126     44   1415       O  
ATOM    660  CB  ILE A 115     -27.822   9.507  30.476  1.00 78.49           C  
ANISOU  660  CB  ILE A 115     8839  10945  10038     63    246   1883       C  
ATOM    661  CG1 ILE A 115     -27.269  10.944  30.708  1.00 80.53           C  
ANISOU  661  CG1 ILE A 115     9186  10915  10496     75    324   1964       C  
ATOM    662  CG2 ILE A 115     -28.808   9.121  31.594  1.00 78.12           C  
ANISOU  662  CG2 ILE A 115     8871  10846   9965    126    251   1765       C  
ATOM    663  CD1 ILE A 115     -28.288  12.128  30.544  1.00 88.16           C  
ANISOU  663  CD1 ILE A 115    10155  11778  11565    238    450   2177       C  
ATOM    664  N   TYR A 116     -27.599   6.435  29.323  1.00 74.36           N  
ANISOU  664  N   TYR A 116     8152  10970   9132   -104     78   1671       N  
ATOM    665  CA  TYR A 116     -28.044   5.038  29.229  1.00 73.89           C  
ANISOU  665  CA  TYR A 116     8067  11093   8913   -153     24   1545       C  
ATOM    666  C   TYR A 116     -26.920   4.087  29.646  1.00 77.62           C  
ANISOU  666  C   TYR A 116     8608  11503   9380   -239    -24   1350       C  
ATOM    667  O   TYR A 116     -27.181   3.148  30.399  1.00 76.45           O  
ANISOU  667  O   TYR A 116     8527  11332   9190   -260    -60   1203       O  
ATOM    668  CB  TYR A 116     -28.555   4.707  27.808  1.00 76.12           C  
ANISOU  668  CB  TYR A 116     8212  11677   9031   -171     18   1659       C  
ATOM    669  CG  TYR A 116     -28.629   3.229  27.467  1.00 77.80           C  
ANISOU  669  CG  TYR A 116     8417  12065   9077   -267    -32   1500       C  
ATOM    670  CD1 TYR A 116     -29.736   2.464  27.824  1.00 79.51           C  
ANISOU  670  CD1 TYR A 116     8627  12368   9215   -287    -63   1432       C  
ATOM    671  CD2 TYR A 116     -27.618   2.609  26.740  1.00 78.90           C  
ANISOU  671  CD2 TYR A 116     8554  12282   9144   -339    -32   1424       C  
ATOM    672  CE1 TYR A 116     -29.822   1.111  27.491  1.00 79.54           C  
ANISOU  672  CE1 TYR A 116     8640  12505   9077   -393    -99   1279       C  
ATOM    673  CE2 TYR A 116     -27.692   1.256  26.402  1.00 79.67           C  
ANISOU  673  CE2 TYR A 116     8667  12509   9094   -422    -57   1265       C  
ATOM    674  CZ  TYR A 116     -28.798   0.511  26.777  1.00 85.05           C  
ANISOU  674  CZ  TYR A 116     9358  13252   9704   -457    -94   1189       C  
ATOM    675  OH  TYR A 116     -28.874  -0.822  26.448  1.00 84.09           O  
ANISOU  675  OH  TYR A 116     9271  13229   9451   -558   -110   1024       O  
ATOM    676  N   THR A 117     -25.680   4.345  29.160  1.00 74.49           N  
ANISOU  676  N   THR A 117     8186  11083   9036   -279    -17   1368       N  
ATOM    677  CA  THR A 117     -24.475   3.560  29.447  1.00 73.53           C  
ANISOU  677  CA  THR A 117     8092  10914   8933   -340    -54   1221       C  
ATOM    678  C   THR A 117     -24.066   3.682  30.914  1.00 76.30           C  
ANISOU  678  C   THR A 117     8555  11036   9398   -344   -105   1108       C  
ATOM    679  O   THR A 117     -23.649   2.686  31.507  1.00 74.68           O  
ANISOU  679  O   THR A 117     8397  10809   9168   -365   -155    968       O  
ATOM    680  CB  THR A 117     -23.359   3.931  28.466  1.00 84.24           C  
ANISOU  680  CB  THR A 117     9358  12331  10320   -374    -14   1305       C  
ATOM    681  OG1 THR A 117     -23.866   3.814  27.134  1.00 85.37           O  
ANISOU  681  OG1 THR A 117     9415  12705  10315   -369     32   1411       O  
ATOM    682  CG2 THR A 117     -22.117   3.061  28.619  1.00 83.24           C  
ANISOU  682  CG2 THR A 117     9222  12191  10215   -416    -36   1176       C  
ATOM    683  N   VAL A 118     -24.192   4.894  31.495  1.00 73.59           N  
ANISOU  683  N   VAL A 118     8266  10523   9174   -321    -90   1170       N  
ATOM    684  CA  VAL A 118     -23.892   5.149  32.909  1.00 73.06           C  
ANISOU  684  CA  VAL A 118     8327  10244   9190   -336   -140   1056       C  
ATOM    685  C   VAL A 118     -24.853   4.325  33.785  1.00 76.82           C  
ANISOU  685  C   VAL A 118     8894  10725   9571   -295   -158    951       C  
ATOM    686  O   VAL A 118     -24.381   3.528  34.585  1.00 75.72           O  
ANISOU  686  O   VAL A 118     8819  10546   9405   -324   -224    823       O  
ATOM    687  CB  VAL A 118     -23.841   6.667  33.259  1.00 77.77           C  
ANISOU  687  CB  VAL A 118     8983  10638   9928   -332    -99   1129       C  
ATOM    688  CG1 VAL A 118     -24.084   6.924  34.744  1.00 77.66           C  
ANISOU  688  CG1 VAL A 118     9137  10428   9941   -326   -127   1000       C  
ATOM    689  CG2 VAL A 118     -22.512   7.278  32.828  1.00 78.48           C  
ANISOU  689  CG2 VAL A 118     9009  10674  10136   -421   -112   1175       C  
ATOM    690  N   ASN A 119     -26.184   4.444  33.560  1.00 74.54           N  
ANISOU  690  N   ASN A 119     8589  10507   9227   -228    -96   1025       N  
ATOM    691  CA  ASN A 119     -27.217   3.680  34.281  1.00 74.05           C  
ANISOU  691  CA  ASN A 119     8585  10472   9078   -197    -92    952       C  
ATOM    692  C   ASN A 119     -27.033   2.159  34.104  1.00 77.64           C  
ANISOU  692  C   ASN A 119     9022  11050   9427   -254   -140    850       C  
ATOM    693  O   ASN A 119     -27.332   1.395  35.019  1.00 77.06           O  
ANISOU  693  O   ASN A 119     9038  10932   9310   -257   -158    751       O  
ATOM    694  CB  ASN A 119     -28.632   4.113  33.841  1.00 74.36           C  
ANISOU  694  CB  ASN A 119     8552  10609   9092   -120    -16   1083       C  
ATOM    695  CG  ASN A 119     -29.770   3.310  34.445  1.00 95.20           C  
ANISOU  695  CG  ASN A 119    11211  13311  11648   -102      2   1031       C  
ATOM    696  OD1 ASN A 119     -30.508   2.612  33.743  1.00 89.38           O  
ANISOU  696  OD1 ASN A 119    10369  12772  10820   -127     -1   1067       O  
ATOM    697  ND2 ASN A 119     -29.931   3.375  35.763  1.00 88.22           N  
ANISOU  697  ND2 ASN A 119    10466  12267  10786    -73     20    941       N  
ATOM    698  N   LEU A 120     -26.519   1.740  32.935  1.00 74.30           N  
ANISOU  698  N   LEU A 120     8498  10769   8963   -295   -146    876       N  
ATOM    699  CA  LEU A 120     -26.265   0.349  32.568  1.00 73.54           C  
ANISOU  699  CA  LEU A 120     8392  10775   8777   -345   -167    777       C  
ATOM    700  C   LEU A 120     -25.249  -0.284  33.520  1.00 76.93           C  
ANISOU  700  C   LEU A 120     8910  11068   9251   -354   -221    658       C  
ATOM    701  O   LEU A 120     -25.607  -1.183  34.280  1.00 75.56           O  
ANISOU  701  O   LEU A 120     8822  10854   9034   -355   -235    572       O  
ATOM    702  CB  LEU A 120     -25.755   0.319  31.112  1.00 74.10           C  
ANISOU  702  CB  LEU A 120     8350  11005   8802   -375   -142    834       C  
ATOM    703  CG  LEU A 120     -25.957  -0.919  30.251  1.00 78.74           C  
ANISOU  703  CG  LEU A 120     8910  11755   9251   -428   -127    759       C  
ATOM    704  CD1 LEU A 120     -27.416  -1.383  30.246  1.00 78.94           C  
ANISOU  704  CD1 LEU A 120     8933  11884   9176   -457   -127    752       C  
ATOM    705  CD2 LEU A 120     -25.508  -0.636  28.820  1.00 81.64           C  
ANISOU  705  CD2 LEU A 120     9175  12288   9557   -447    -88    837       C  
ATOM    706  N   TYR A 121     -24.016   0.242  33.533  1.00 74.62           N  
ANISOU  706  N   TYR A 121     8591  10708   9052   -360   -251    671       N  
ATOM    707  CA  TYR A 121     -22.914  -0.253  34.360  1.00 74.55           C  
ANISOU  707  CA  TYR A 121     8628  10602   9096   -365   -321    589       C  
ATOM    708  C   TYR A 121     -22.985   0.098  35.859  1.00 76.10           C  
ANISOU  708  C   TYR A 121     8951  10644   9319   -357   -385    539       C  
ATOM    709  O   TYR A 121     -22.515  -0.689  36.676  1.00 75.31           O  
ANISOU  709  O   TYR A 121     8912  10497   9203   -349   -446    468       O  
ATOM    710  CB  TYR A 121     -21.554   0.149  33.752  1.00 77.32           C  
ANISOU  710  CB  TYR A 121     8868  10972   9537   -388   -332    631       C  
ATOM    711  CG  TYR A 121     -21.293  -0.414  32.368  1.00 81.05           C  
ANISOU  711  CG  TYR A 121     9236  11601   9959   -389   -259    656       C  
ATOM    712  CD1 TYR A 121     -21.121  -1.781  32.169  1.00 83.31           C  
ANISOU  712  CD1 TYR A 121     9537  11935  10182   -369   -237    567       C  
ATOM    713  CD2 TYR A 121     -21.181   0.423  31.263  1.00 83.17           C  
ANISOU  713  CD2 TYR A 121     9404  11959  10239   -408   -200    768       C  
ATOM    714  CE1 TYR A 121     -20.872  -2.305  30.900  1.00 85.39           C  
ANISOU  714  CE1 TYR A 121     9728  12333  10381   -373   -154    563       C  
ATOM    715  CE2 TYR A 121     -20.909  -0.087  29.992  1.00 84.98           C  
ANISOU  715  CE2 TYR A 121     9550  12346  10391   -411   -125    783       C  
ATOM    716  CZ  TYR A 121     -20.758  -1.453  29.814  1.00 93.33           C  
ANISOU  716  CZ  TYR A 121    10635  13451  11374   -395   -100    668       C  
ATOM    717  OH  TYR A 121     -20.496  -1.961  28.563  1.00 95.65           O  
ANISOU  717  OH  TYR A 121    10871  13894  11577   -401    -11    660       O  
ATOM    718  N   SER A 122     -23.555   1.264  36.219  1.00 71.82           N  
ANISOU  718  N   SER A 122     8456  10022   8810   -351   -365    579       N  
ATOM    719  CA  SER A 122     -23.644   1.702  37.615  1.00 71.20           C  
ANISOU  719  CA  SER A 122     8520   9796   8737   -349   -409    516       C  
ATOM    720  C   SER A 122     -24.671   0.933  38.441  1.00 74.58           C  
ANISOU  720  C   SER A 122     9058  10218   9059   -309   -385    462       C  
ATOM    721  O   SER A 122     -24.348   0.535  39.561  1.00 74.51           O  
ANISOU  721  O   SER A 122     9160  10141   9011   -313   -450    387       O  
ATOM    722  CB  SER A 122     -23.874   3.208  37.720  1.00 74.08           C  
ANISOU  722  CB  SER A 122     8920  10045   9181   -351   -369    562       C  
ATOM    723  OG  SER A 122     -25.153   3.577  37.231  1.00 79.67           O  
ANISOU  723  OG  SER A 122     9608  10793   9869   -287   -262    644       O  
ATOM    724  N   SER A 123     -25.899   0.727  37.902  1.00 70.35           N  
ANISOU  724  N   SER A 123     8484   9770   8474   -278   -296    510       N  
ATOM    725  CA  SER A 123     -26.984   0.016  38.595  1.00 69.57           C  
ANISOU  725  CA  SER A 123     8464   9681   8287   -253   -253    477       C  
ATOM    726  C   SER A 123     -26.568  -1.376  39.057  1.00 71.52           C  
ANISOU  726  C   SER A 123     8767   9932   8476   -276   -303    404       C  
ATOM    727  O   SER A 123     -26.750  -1.704  40.231  1.00 70.97           O  
ANISOU  727  O   SER A 123     8825   9788   8354   -261   -316    358       O  
ATOM    728  CB  SER A 123     -28.234  -0.068  37.725  1.00 73.58           C  
ANISOU  728  CB  SER A 123     8868  10324   8763   -241   -169    554       C  
ATOM    729  OG  SER A 123     -27.975  -0.786  36.528  1.00 83.22           O  
ANISOU  729  OG  SER A 123     9979  11683   9960   -289   -183    565       O  
ATOM    730  N   VAL A 124     -25.971  -2.172  38.146  1.00 67.06           N  
ANISOU  730  N   VAL A 124     8116   9446   7919   -304   -321    398       N  
ATOM    731  CA  VAL A 124     -25.511  -3.525  38.449  1.00 66.38           C  
ANISOU  731  CA  VAL A 124     8079   9341   7801   -308   -348    340       C  
ATOM    732  C   VAL A 124     -24.406  -3.559  39.519  1.00 70.19           C  
ANISOU  732  C   VAL A 124     8638   9723   8307   -282   -447    312       C  
ATOM    733  O   VAL A 124     -24.479  -4.392  40.428  1.00 70.43           O  
ANISOU  733  O   VAL A 124     8775   9701   8285   -262   -465    287       O  
ATOM    734  CB  VAL A 124     -25.225  -4.384  37.184  1.00 69.82           C  
ANISOU  734  CB  VAL A 124     8423   9871   8236   -334   -314    325       C  
ATOM    735  CG1 VAL A 124     -23.922  -3.987  36.484  1.00 69.75           C  
ANISOU  735  CG1 VAL A 124     8314   9887   8301   -324   -348    345       C  
ATOM    736  CG2 VAL A 124     -25.257  -5.873  37.504  1.00 69.63           C  
ANISOU  736  CG2 VAL A 124     8480   9802   8175   -337   -295    265       C  
ATOM    737  N   TRP A 125     -23.429  -2.628  39.449  1.00 65.94           N  
ANISOU  737  N   TRP A 125     8044   9167   7843   -292   -514    328       N  
ATOM    738  CA  TRP A 125     -22.350  -2.582  40.432  1.00 66.12           C  
ANISOU  738  CA  TRP A 125     8112   9127   7883   -289   -633    305       C  
ATOM    739  C   TRP A 125     -22.745  -2.028  41.793  1.00 69.10           C  
ANISOU  739  C   TRP A 125     8646   9419   8190   -294   -675    268       C  
ATOM    740  O   TRP A 125     -22.125  -2.404  42.787  1.00 68.75           O  
ANISOU  740  O   TRP A 125     8674   9346   8100   -287   -775    247       O  
ATOM    741  CB  TRP A 125     -21.051  -2.024  39.855  1.00 65.64           C  
ANISOU  741  CB  TRP A 125     7914   9093   7931   -318   -697    332       C  
ATOM    742  CG  TRP A 125     -20.415  -2.985  38.892  1.00 66.80           C  
ANISOU  742  CG  TRP A 125     7943   9318   8120   -285   -663    353       C  
ATOM    743  CD1 TRP A 125     -20.614  -3.043  37.544  1.00 69.63           C  
ANISOU  743  CD1 TRP A 125     8202   9759   8496   -290   -564    376       C  
ATOM    744  CD2 TRP A 125     -19.566  -4.096  39.220  1.00 67.36           C  
ANISOU  744  CD2 TRP A 125     7999   9389   8206   -228   -711    351       C  
ATOM    745  NE1 TRP A 125     -19.910  -4.096  37.004  1.00 69.51           N  
ANISOU  745  NE1 TRP A 125     8123   9785   8504   -247   -537    367       N  
ATOM    746  CE2 TRP A 125     -19.245  -4.750  38.009  1.00 71.52           C  
ANISOU  746  CE2 TRP A 125     8421   9981   8774   -198   -620    359       C  
ATOM    747  CE3 TRP A 125     -19.003  -4.574  40.415  1.00 69.43           C  
ANISOU  747  CE3 TRP A 125     8325   9609   8449   -192   -821    354       C  
ATOM    748  CZ2 TRP A 125     -18.392  -5.860  37.960  1.00 71.55           C  
ANISOU  748  CZ2 TRP A 125     8384   9983   8819   -120   -617    364       C  
ATOM    749  CZ3 TRP A 125     -18.166  -5.678  40.365  1.00 71.48           C  
ANISOU  749  CZ3 TRP A 125     8528   9880   8750   -111   -834    383       C  
ATOM    750  CH2 TRP A 125     -17.870  -6.310  39.150  1.00 72.20           C  
ANISOU  750  CH2 TRP A 125     8517  10012   8903    -69   -723    386       C  
ATOM    751  N   ILE A 126     -23.831  -1.212  41.856  1.00 65.15           N  
ANISOU  751  N   ILE A 126     8201   8887   7666   -295   -588    266       N  
ATOM    752  CA  ILE A 126     -24.407  -0.704  43.114  1.00 65.33           C  
ANISOU  752  CA  ILE A 126     8392   8824   7604   -286   -581    219       C  
ATOM    753  C   ILE A 126     -25.004  -1.918  43.847  1.00 68.50           C  
ANISOU  753  C   ILE A 126     8892   9241   7893   -249   -555    213       C  
ATOM    754  O   ILE A 126     -24.784  -2.080  45.046  1.00 68.09           O  
ANISOU  754  O   ILE A 126     8978   9147   7747   -244   -616    178       O  
ATOM    755  CB  ILE A 126     -25.435   0.448  42.878  1.00 68.51           C  
ANISOU  755  CB  ILE A 126     8811   9183   8035   -267   -463    234       C  
ATOM    756  CG1 ILE A 126     -24.709   1.796  42.689  1.00 69.82           C  
ANISOU  756  CG1 ILE A 126     8961   9266   8301   -312   -503    224       C  
ATOM    757  CG2 ILE A 126     -26.445   0.551  44.029  1.00 69.51           C  
ANISOU  757  CG2 ILE A 126     9104   9251   8054   -224   -387    194       C  
ATOM    758  CD1 ILE A 126     -25.443   2.831  41.833  1.00 77.45           C  
ANISOU  758  CD1 ILE A 126     9863  10209   9355   -280   -382    295       C  
ATOM    759  N   LEU A 127     -25.684  -2.805  43.092  1.00 65.10           N  
ANISOU  759  N   LEU A 127     8390   8875   7468   -238   -470    251       N  
ATOM    760  CA  LEU A 127     -26.244  -4.062  43.597  1.00 65.20           C  
ANISOU  760  CA  LEU A 127     8480   8890   7401   -223   -427    257       C  
ATOM    761  C   LEU A 127     -25.124  -4.995  44.092  1.00 69.85           C  
ANISOU  761  C   LEU A 127     9108   9453   7977   -204   -533    259       C  
ATOM    762  O   LEU A 127     -25.313  -5.679  45.101  1.00 70.15           O  
ANISOU  762  O   LEU A 127     9275   9454   7926   -181   -537    270       O  
ATOM    763  CB  LEU A 127     -27.089  -4.761  42.520  1.00 64.50           C  
ANISOU  763  CB  LEU A 127     8293   8876   7339   -249   -327    282       C  
ATOM    764  CG  LEU A 127     -28.343  -4.020  42.062  1.00 68.76           C  
ANISOU  764  CG  LEU A 127     8769   9474   7882   -257   -226    312       C  
ATOM    765  CD1 LEU A 127     -28.735  -4.455  40.706  1.00 68.32           C  
ANISOU  765  CD1 LEU A 127     8572   9529   7859   -303   -185    333       C  
ATOM    766  CD2 LEU A 127     -29.493  -4.234  43.014  1.00 71.72           C  
ANISOU  766  CD2 LEU A 127     9241   9832   8179   -243   -136    322       C  
ATOM    767  N   ALA A 128     -23.950  -4.990  43.397  1.00 65.96           N  
ANISOU  767  N   ALA A 128     8499   8986   7577   -205   -611    265       N  
ATOM    768  CA  ALA A 128     -22.761  -5.758  43.774  1.00 66.03           C  
ANISOU  768  CA  ALA A 128     8502   8984   7602   -165   -715    288       C  
ATOM    769  C   ALA A 128     -22.194  -5.204  45.091  1.00 71.59           C  
ANISOU  769  C   ALA A 128     9302   9667   8230   -167   -849    280       C  
ATOM    770  O   ALA A 128     -21.675  -5.969  45.907  1.00 71.99           O  
ANISOU  770  O   ALA A 128     9415   9711   8226   -122   -927    318       O  
ATOM    771  CB  ALA A 128     -21.716  -5.676  42.677  1.00 66.42           C  
ANISOU  771  CB  ALA A 128     8379   9083   7775   -164   -745    300       C  
ATOM    772  N   PHE A 129     -22.326  -3.874  45.301  1.00 68.27           N  
ANISOU  772  N   PHE A 129     8906   9233   7801   -221   -871    232       N  
ATOM    773  CA  PHE A 129     -21.903  -3.188  46.519  1.00 69.13           C  
ANISOU  773  CA  PHE A 129     9132   9318   7818   -255   -990    189       C  
ATOM    774  C   PHE A 129     -22.883  -3.475  47.655  1.00 73.92           C  
ANISOU  774  C   PHE A 129     9938   9891   8257   -227   -931    173       C  
ATOM    775  O   PHE A 129     -22.455  -3.542  48.808  1.00 75.32           O  
ANISOU  775  O   PHE A 129    10234  10075   8308   -230  -1040    161       O  
ATOM    776  CB  PHE A 129     -21.722  -1.682  46.271  1.00 71.30           C  
ANISOU  776  CB  PHE A 129     9380   9555   8155   -331  -1007    129       C  
ATOM    777  CG  PHE A 129     -20.287  -1.255  46.045  1.00 74.04           C  
ANISOU  777  CG  PHE A 129     9596   9937   8600   -394  -1160    133       C  
ATOM    778  CD1 PHE A 129     -19.603  -1.629  44.893  1.00 76.36           C  
ANISOU  778  CD1 PHE A 129     9690  10291   9035   -379  -1154    197       C  
ATOM    779  CD2 PHE A 129     -19.619  -0.477  46.985  1.00 78.03           C  
ANISOU  779  CD2 PHE A 129    10176  10423   9050   -479  -1304     68       C  
ATOM    780  CE1 PHE A 129     -18.277  -1.245  44.694  1.00 78.22           C  
ANISOU  780  CE1 PHE A 129     9780  10571   9371   -437  -1282    215       C  
ATOM    781  CE2 PHE A 129     -18.295  -0.083  46.778  1.00 81.68           C  
ANISOU  781  CE2 PHE A 129    10491  10931   9613   -560  -1452     78       C  
ATOM    782  CZ  PHE A 129     -17.636  -0.467  45.633  1.00 79.13           C  
ANISOU  782  CZ  PHE A 129     9948  10671   9445   -534  -1435    161       C  
ATOM    783  N   ILE A 130     -24.193  -3.682  47.327  1.00 69.35           N  
ANISOU  783  N   ILE A 130     9386   9294   7668   -202   -759    182       N  
ATOM    784  CA  ILE A 130     -25.241  -4.061  48.293  1.00 69.23           C  
ANISOU  784  CA  ILE A 130     9536   9258   7511   -173   -663    186       C  
ATOM    785  C   ILE A 130     -24.949  -5.508  48.722  1.00 74.74           C  
ANISOU  785  C   ILE A 130    10274   9967   8156   -133   -698    260       C  
ATOM    786  O   ILE A 130     -25.034  -5.830  49.906  1.00 76.28           O  
ANISOU  786  O   ILE A 130    10626  10157   8201   -112   -723    279       O  
ATOM    787  CB  ILE A 130     -26.695  -3.902  47.742  1.00 70.95           C  
ANISOU  787  CB  ILE A 130     9724   9475   7759   -165   -473    195       C  
ATOM    788  CG1 ILE A 130     -27.003  -2.444  47.352  1.00 70.90           C  
ANISOU  788  CG1 ILE A 130     9683   9441   7814   -175   -425    147       C  
ATOM    789  CG2 ILE A 130     -27.706  -4.372  48.777  1.00 72.23           C  
ANISOU  789  CG2 ILE A 130    10038   9626   7780   -137   -365    213       C  
ATOM    790  CD1 ILE A 130     -28.373  -2.174  46.666  1.00 74.66           C  
ANISOU  790  CD1 ILE A 130    10080   9944   8343   -150   -252    185       C  
ATOM    791  N   SER A 131     -24.565  -6.354  47.747  1.00 70.77           N  
ANISOU  791  N   SER A 131     9639   9475   7774   -119   -694    305       N  
ATOM    792  CA  SER A 131     -24.191  -7.754  47.932  1.00 71.36           C  
ANISOU  792  CA  SER A 131     9737   9527   7848    -68   -708    381       C  
ATOM    793  C   SER A 131     -22.934  -7.884  48.811  1.00 75.54           C  
ANISOU  793  C   SER A 131    10300  10080   8322    -24   -888    426       C  
ATOM    794  O   SER A 131     -22.830  -8.835  49.590  1.00 75.99           O  
ANISOU  794  O   SER A 131    10455  10116   8300     33   -907    509       O  
ATOM    795  CB  SER A 131     -23.961  -8.412  46.574  1.00 75.54           C  
ANISOU  795  CB  SER A 131    10120  10053   8530    -65   -655    387       C  
ATOM    796  OG  SER A 131     -23.673  -9.793  46.715  1.00 89.22           O  
ANISOU  796  OG  SER A 131    11893  11727  10279     -8   -637    454       O  
ATOM    797  N   LEU A 132     -21.990  -6.924  48.684  1.00 71.84           N  
ANISOU  797  N   LEU A 132     9740   9660   7895    -57  -1024    384       N  
ATOM    798  CA  LEU A 132     -20.753  -6.862  49.469  1.00 73.04           C  
ANISOU  798  CA  LEU A 132     9884   9869   7997    -43  -1224    421       C  
ATOM    799  C   LEU A 132     -21.039  -6.474  50.919  1.00 77.42           C  
ANISOU  799  C   LEU A 132    10641  10443   8334    -68  -1291    397       C  
ATOM    800  O   LEU A 132     -20.388  -6.999  51.825  1.00 78.42           O  
ANISOU  800  O   LEU A 132    10821  10622   8354    -27  -1425    474       O  
ATOM    801  CB  LEU A 132     -19.763  -5.851  48.855  1.00 73.21           C  
ANISOU  801  CB  LEU A 132     9740   9940   8136   -108  -1336    372       C  
ATOM    802  CG  LEU A 132     -18.380  -6.366  48.400  1.00 78.87           C  
ANISOU  802  CG  LEU A 132    10263  10721   8983    -58  -1452    454       C  
ATOM    803  CD1 LEU A 132     -17.608  -7.052  49.538  1.00 80.89           C  
ANISOU  803  CD1 LEU A 132    10560  11039   9137      7  -1616    553       C  
ATOM    804  CD2 LEU A 132     -18.475  -7.242  47.144  1.00 80.36           C  
ANISOU  804  CD2 LEU A 132    10336  10872   9323     13  -1305    492       C  
ATOM    805  N   ASP A 133     -22.015  -5.555  51.128  1.00 72.56           N  
ANISOU  805  N   ASP A 133    10136   9789   7646   -125  -1191    298       N  
ATOM    806  CA  ASP A 133     -22.448  -5.047  52.432  1.00 73.11           C  
ANISOU  806  CA  ASP A 133    10420   9863   7496   -152  -1207    242       C  
ATOM    807  C   ASP A 133     -23.028  -6.171  53.284  1.00 75.87           C  
ANISOU  807  C   ASP A 133    10916  10215   7695    -80  -1141    341       C  
ATOM    808  O   ASP A 133     -22.651  -6.299  54.448  1.00 76.44           O  
ANISOU  808  O   ASP A 133    11123  10344   7575    -73  -1256    368       O  
ATOM    809  CB  ASP A 133     -23.472  -3.910  52.250  1.00 74.28           C  
ANISOU  809  CB  ASP A 133    10632   9944   7646   -196  -1057    127       C  
ATOM    810  CG  ASP A 133     -23.716  -3.067  53.488  1.00 85.79           C  
ANISOU  810  CG  ASP A 133    12310  11392   8894   -236  -1075     24       C  
ATOM    811  OD1 ASP A 133     -24.829  -3.150  54.055  1.00 86.63           O  
ANISOU  811  OD1 ASP A 133    12564  11471   8879   -197   -912     16       O  
ATOM    812  OD2 ASP A 133     -22.811  -2.291  53.866  1.00 91.86           O  
ANISOU  812  OD2 ASP A 133    13101  12179   9621   -315  -1242    -57       O  
ATOM    813  N   ARG A 134     -23.903  -7.013  52.684  1.00 70.73           N  
ANISOU  813  N   ARG A 134    10234   9510   7131    -38   -963    401       N  
ATOM    814  CA  ARG A 134     -24.552  -8.162  53.342  1.00 70.86           C  
ANISOU  814  CA  ARG A 134    10376   9502   7044     15   -864    509       C  
ATOM    815  C   ARG A 134     -23.566  -9.208  53.834  1.00 75.59           C  
ANISOU  815  C   ARG A 134    10986  10125   7609     88  -1000    644       C  
ATOM    816  O   ARG A 134     -23.859  -9.918  54.791  1.00 75.76           O  
ANISOU  816  O   ARG A 134    11161  10146   7480    131   -972    743       O  
ATOM    817  CB  ARG A 134     -25.641  -8.798  52.452  1.00 68.05           C  
ANISOU  817  CB  ARG A 134     9957   9080   6818      9   -656    530       C  
ATOM    818  CG  ARG A 134     -26.873  -7.925  52.232  1.00 72.50           C  
ANISOU  818  CG  ARG A 134    10528   9641   7377    -37   -497    445       C  
ATOM    819  CD  ARG A 134     -27.692  -7.726  53.497  1.00 81.83           C  
ANISOU  819  CD  ARG A 134    11907  10833   8352    -26   -404    448       C  
ATOM    820  NE  ARG A 134     -27.274  -6.538  54.243  1.00 90.10           N  
ANISOU  820  NE  ARG A 134    13059  11909   9264    -37   -499    346       N  
ATOM    821  CZ  ARG A 134     -27.880  -6.086  55.335  1.00107.62           C  
ANISOU  821  CZ  ARG A 134    15467  14141  11283    -29   -420    307       C  
ATOM    822  NH1 ARG A 134     -27.437  -4.993  55.942  1.00 91.77           N  
ANISOU  822  NH1 ARG A 134    13568  12144   9156    -56   -510    188       N  
ATOM    823  NH2 ARG A 134     -28.941  -6.717  55.825  1.00101.52           N  
ANISOU  823  NH2 ARG A 134    14782  13366  10426     -2   -240    381       N  
ATOM    824  N   TYR A 135     -22.401  -9.293  53.183  1.00 72.82           N  
ANISOU  824  N   TYR A 135    10466   9798   7402    110  -1136    664       N  
ATOM    825  CA  TYR A 135     -21.322 -10.183  53.571  1.00 74.57           C  
ANISOU  825  CA  TYR A 135    10656  10054   7622    202  -1279    806       C  
ATOM    826  C   TYR A 135     -20.690  -9.587  54.842  1.00 80.74           C  
ANISOU  826  C   TYR A 135    11535  10960   8183    180  -1484    810       C  
ATOM    827  O   TYR A 135     -20.672 -10.237  55.887  1.00 81.69           O  
ANISOU  827  O   TYR A 135    11794  11115   8129    239  -1528    930       O  
ATOM    828  CB  TYR A 135     -20.298 -10.320  52.416  1.00 75.12           C  
ANISOU  828  CB  TYR A 135    10492  10127   7925    234  -1341    814       C  
ATOM    829  CG  TYR A 135     -19.033 -11.054  52.805  1.00 79.05           C  
ANISOU  829  CG  TYR A 135    10912  10682   8441    344  -1505    966       C  
ATOM    830  CD1 TYR A 135     -18.961 -12.441  52.740  1.00 82.09           C  
ANISOU  830  CD1 TYR A 135    11316  10978   8898    473  -1425   1113       C  
ATOM    831  CD2 TYR A 135     -17.910 -10.362  53.252  1.00 81.04           C  
ANISOU  831  CD2 TYR A 135    11071  11076   8646    319  -1741    970       C  
ATOM    832  CE1 TYR A 135     -17.812 -13.125  53.133  1.00 85.91           C  
ANISOU  832  CE1 TYR A 135    11723  11513   9408    604  -1567   1280       C  
ATOM    833  CE2 TYR A 135     -16.753 -11.034  53.640  1.00 84.10           C  
ANISOU  833  CE2 TYR A 135    11359  11544   9051    430  -1903   1133       C  
ATOM    834  CZ  TYR A 135     -16.708 -12.418  53.580  1.00 93.97           C  
ANISOU  834  CZ  TYR A 135    12623  12704  10376    588  -1812   1298       C  
ATOM    835  OH  TYR A 135     -15.572 -13.095  53.960  1.00 98.36           O  
ANISOU  835  OH  TYR A 135    13070  13337  10964    727  -1962   1485       O  
ATOM    836  N   LEU A 136     -20.214  -8.351  54.745  1.00 77.49           N  
ANISOU  836  N   LEU A 136    11061  10611   7769     83  -1604    680       N  
ATOM    837  CA  LEU A 136     -19.610  -7.668  55.884  1.00 79.37           C  
ANISOU  837  CA  LEU A 136    11395  10970   7793     23  -1811    644       C  
ATOM    838  C   LEU A 136     -20.532  -7.634  57.103  1.00 85.35           C  
ANISOU  838  C   LEU A 136    12426  11735   8270     14  -1737    627       C  
ATOM    839  O   LEU A 136     -20.121  -7.992  58.207  1.00 87.28           O  
ANISOU  839  O   LEU A 136    12783  12083   8298     42  -1876    716       O  
ATOM    840  CB  LEU A 136     -19.201  -6.245  55.498  1.00 78.69           C  
ANISOU  840  CB  LEU A 136    11230  10902   7769   -112  -1897    471       C  
ATOM    841  CG  LEU A 136     -18.052  -6.118  54.495  1.00 81.51           C  
ANISOU  841  CG  LEU A 136    11311  11294   8364   -125  -2012    495       C  
ATOM    842  CD1 LEU A 136     -17.976  -4.704  53.940  1.00 80.24           C  
ANISOU  842  CD1 LEU A 136    11093  11098   8294   -265  -2018    326       C  
ATOM    843  CD2 LEU A 136     -16.732  -6.518  55.138  1.00 85.56           C  
ANISOU  843  CD2 LEU A 136    11729  11961   8818   -100  -2273    614       C  
ATOM    844  N   ALA A 137     -21.773  -7.200  56.903  1.00 81.19           N  
ANISOU  844  N   ALA A 137    11997  11112   7739    -17  -1517    524       N  
ATOM    845  CA  ALA A 137     -22.702  -7.069  57.987  1.00 82.18           C  
ANISOU  845  CA  ALA A 137    12370  11243   7611    -22  -1410    496       C  
ATOM    846  C   ALA A 137     -22.985  -8.372  58.664  1.00 87.06           C  
ANISOU  846  C   ALA A 137    13093  11875   8110     74  -1357    685       C  
ATOM    847  O   ALA A 137     -23.193  -8.409  59.850  1.00 89.51           O  
ANISOU  847  O   ALA A 137    13606  12254   8150     79  -1374    712       O  
ATOM    848  CB  ALA A 137     -23.763  -6.067  57.630  1.00 81.64           C  
ANISOU  848  CB  ALA A 137    12350  11089   7582    -75  -1216    335       C  
ATOM    849  N   ILE A 138     -22.993  -9.454  57.915  1.00 81.37           N  
ANISOU  849  N   ILE A 138    12249  11081   7587    148  -1283    816       N  
ATOM    850  CA  ILE A 138     -23.080 -10.747  58.545  1.00 82.41           C  
ANISOU  850  CA  ILE A 138    12477  11202   7633    242  -1248   1018       C  
ATOM    851  C   ILE A 138     -21.912 -11.629  58.815  1.00 89.77           C  
ANISOU  851  C   ILE A 138    13348  12188   8574    342  -1433   1202       C  
ATOM    852  O   ILE A 138     -21.773 -12.189  59.878  1.00 91.86           O  
ANISOU  852  O   ILE A 138    13753  12517   8631    402  -1494   1350       O  
ATOM    853  CB  ILE A 138     -23.909 -11.453  57.521  1.00 83.01           C  
ANISOU  853  CB  ILE A 138    12472  11131   7938    256  -1022   1041       C  
ATOM    854  CG1 ILE A 138     -25.197 -10.697  57.256  1.00 81.98           C  
ANISOU  854  CG1 ILE A 138    12379  10961   7807    175   -821    898       C  
ATOM    855  CG2 ILE A 138     -24.262 -12.814  58.018  1.00 84.13           C  
ANISOU  855  CG2 ILE A 138    12723  11205   8037    333   -918   1238       C  
ATOM    856  CD1 ILE A 138     -26.324 -11.595  56.832  1.00 86.07           C  
ANISOU  856  CD1 ILE A 138    12901  11372   8429    173   -583    966       C  
ATOM    857  N   VAL A 139     -21.056 -11.765  57.835  1.00 86.46           N  
ANISOU  857  N   VAL A 139    12710  11748   8395    371  -1516   1209       N  
ATOM    858  CA  VAL A 139     -19.924 -12.617  58.022  1.00 88.44           C  
ANISOU  858  CA  VAL A 139    12871  12046   8685    491  -1676   1399       C  
ATOM    859  C   VAL A 139     -19.094 -12.017  59.118  1.00 95.62           C  
ANISOU  859  C   VAL A 139    13824  13157   9351    464  -1944   1417       C  
ATOM    860  O   VAL A 139     -18.425 -12.712  59.853  1.00 97.38           O  
ANISOU  860  O   VAL A 139    14064  13468   9467    565  -2085   1613       O  
ATOM    861  CB  VAL A 139     -19.403 -13.070  56.700  1.00 91.03           C  
ANISOU  861  CB  VAL A 139    12976  12281   9330    548  -1634   1410       C  
ATOM    862  CG1 VAL A 139     -18.303 -14.044  56.901  1.00 92.84           C  
ANISOU  862  CG1 VAL A 139    13115  12539   9621    705  -1760   1626       C  
ATOM    863  CG2 VAL A 139     -20.509 -13.681  55.911  1.00 89.10           C  
ANISOU  863  CG2 VAL A 139    12772  11852   9231    540  -1360   1377       C  
ATOM    864  N   HIS A 140     -19.124 -10.708  59.218  1.00 92.82           N  
ANISOU  864  N   HIS A 140    13487  12875   8907    323  -2019   1213       N  
ATOM    865  CA  HIS A 140     -18.316 -10.042  60.203  1.00 95.67           C  
ANISOU  865  CA  HIS A 140    13890  13429   9032    257  -2287   1189       C  
ATOM    866  C   HIS A 140     -19.100  -9.105  61.041  1.00101.10           C  
ANISOU  866  C   HIS A 140    14821  14146   9447    138  -2242   1017       C  
ATOM    867  O   HIS A 140     -18.809  -7.936  61.118  1.00100.97           O  
ANISOU  867  O   HIS A 140    14806  14183   9374      3  -2353    829       O  
ATOM    868  CB  HIS A 140     -17.483  -9.266  59.206  1.00 95.47           C  
ANISOU  868  CB  HIS A 140    13614  13418   9241    180  -2397   1071       C  
ATOM    869  CG  HIS A 140     -16.534 -10.121  58.442  1.00 98.93           C  
ANISOU  869  CG  HIS A 140    13800  13857   9932    305  -2458   1238       C  
ATOM    870  ND1 HIS A 140     -15.706 -11.029  59.053  1.00103.22           N  
ANISOU  870  ND1 HIS A 140    14293  14509  10416    436  -2617   1470       N  
ATOM    871  CD2 HIS A 140     -16.297 -10.228  57.118  1.00 98.77           C  
ANISOU  871  CD2 HIS A 140    13568  13740  10220    333  -2364   1214       C  
ATOM    872  CE1 HIS A 140     -14.992 -11.656  58.139  1.00102.21           C  
ANISOU  872  CE1 HIS A 140    13930  14339  10566    549  -2608   1577       C  
ATOM    873  NE2 HIS A 140     -15.331 -11.187  56.956  1.00 99.81           N  
ANISOU  873  NE2 HIS A 140    13531  13913  10479    484  -2453   1416       N  
ATOM    874  N   ALA A 141     -20.124  -9.643  61.665  1.00 99.07           N  
ANISOU  874  N   ALA A 141    14776  13839   9027    190  -2056   1083       N  
ATOM    875  CA  ALA A 141     -21.058  -8.845  62.418  1.00 99.97           C  
ANISOU  875  CA  ALA A 141    15134  13958   8892    104  -1942    924       C  
ATOM    876  C   ALA A 141     -20.699  -7.767  63.426  1.00107.11           C  
ANISOU  876  C   ALA A 141    16201  15007   9490    -18  -2120    763       C  
ATOM    877  O   ALA A 141     -21.238  -6.680  63.401  1.00106.47           O  
ANISOU  877  O   ALA A 141    16217  14868   9370   -118  -2025    538       O  
ATOM    878  CB  ALA A 141     -21.892  -9.739  63.279  1.00102.01           C  
ANISOU  878  CB  ALA A 141    15603  14211   8947    189  -1783   1081       C  
ATOM    879  N   THR A 142     -19.789  -8.087  64.325  1.00106.94           N  
ANISOU  879  N   THR A 142    16213  15174   9246     -8  -2379    883       N  
ATOM    880  CA  THR A 142     -19.414  -7.213  65.426  1.00109.96           C  
ANISOU  880  CA  THR A 142    16777  15724   9278   -136  -2574    743       C  
ATOM    881  C   THR A 142     -18.436  -6.191  64.875  1.00114.56           C  
ANISOU  881  C   THR A 142    17177  16341  10008   -283  -2792    569       C  
ATOM    882  O   THR A 142     -18.614  -4.988  65.029  1.00114.70           O  
ANISOU  882  O   THR A 142    17313  16328   9941   -434  -2788    310       O  
ATOM    883  CB  THR A 142     -18.641  -7.997  66.426  1.00119.13           C  
ANISOU  883  CB  THR A 142    17976  17104  10182    -74  -2815    968       C  
ATOM    884  OG1 THR A 142     -17.409  -8.371  65.820  1.00119.89           O  
ANISOU  884  OG1 THR A 142    17768  17273  10511    -35  -3047   1104       O  
ATOM    885  CG2 THR A 142     -19.397  -9.250  66.787  1.00115.88           C  
ANISOU  885  CG2 THR A 142    17683  16641   9705     94  -2613   1215       C  
ATOM    886  N   ASN A 143     -17.381  -6.688  64.257  1.00111.28           N  
ANISOU  886  N   ASN A 143    16476  15986   9819   -236  -2973    718       N  
ATOM    887  CA  ASN A 143     -16.255  -5.870  63.860  1.00111.94           C  
ANISOU  887  CA  ASN A 143    16354  16152  10024   -376  -3222    609       C  
ATOM    888  C   ASN A 143     -16.387  -5.160  62.537  1.00113.18           C  
ANISOU  888  C   ASN A 143    16343  16125  10534   -436  -3084    455       C  
ATOM    889  O   ASN A 143     -15.390  -4.781  61.949  1.00112.84           O  
ANISOU  889  O   ASN A 143    16060  16134  10680   -512  -3257    438       O  
ATOM    890  CB  ASN A 143     -15.032  -6.752  63.820  1.00114.52           C  
ANISOU  890  CB  ASN A 143    16427  16648  10436   -279  -3469    865       C  
ATOM    891  CG  ASN A 143     -15.306  -8.053  63.122  1.00138.17           C  
ANISOU  891  CG  ASN A 143    19306  19521  13673    -56  -3281   1100       C  
ATOM    892  OD1 ASN A 143     -14.487  -8.552  62.352  1.00133.62           O  
ANISOU  892  OD1 ASN A 143    18450  18954  13366     30  -3352   1236       O  
ATOM    893  ND2 ASN A 143     -16.477  -8.612  63.380  1.00128.31           N  
ANISOU  893  ND2 ASN A 143    18272  18146  12332     34  -3024   1144       N  
ATOM    894  N   SER A 144     -17.601  -4.985  62.049  1.00107.45           N  
ANISOU  894  N   SER A 144    15727  15201   9900   -402  -2774    361       N  
ATOM    895  CA  SER A 144     -17.761  -4.450  60.702  1.00104.49           C  
ANISOU  895  CA  SER A 144    15174  14662   9866   -431  -2635    263       C  
ATOM    896  C   SER A 144     -18.570  -3.166  60.553  1.00107.83           C  
ANISOU  896  C   SER A 144    15746  14940  10286   -545  -2470     10       C  
ATOM    897  O   SER A 144     -19.099  -2.875  59.481  1.00104.45           O  
ANISOU  897  O   SER A 144    15217  14358  10109   -525  -2280    -36       O  
ATOM    898  CB  SER A 144     -18.473  -5.604  59.993  1.00105.60           C  
ANISOU  898  CB  SER A 144    15246  14692  10186   -255  -2403    431       C  
ATOM    899  OG  SER A 144     -19.813  -5.263  59.682  1.00111.80           O  
ANISOU  899  OG  SER A 144    16159  15319  11003   -249  -2114    322       O  
ATOM    900  N   GLN A 145     -18.665  -2.405  61.639  1.00107.60           N  
ANISOU  900  N   GLN A 145    15963  14958   9961   -658  -2541   -150       N  
ATOM    901  CA  GLN A 145     -19.399  -1.146  61.631  1.00107.34           C  
ANISOU  901  CA  GLN A 145    16106  14771   9909   -755  -2376   -397       C  
ATOM    902  C   GLN A 145     -18.755  -0.133  60.693  1.00109.95           C  
ANISOU  902  C   GLN A 145    16257  15012  10506   -887  -2447   -521       C  
ATOM    903  O   GLN A 145     -19.404   0.807  60.236  1.00108.74           O  
ANISOU  903  O   GLN A 145    16171  14679  10466   -925  -2261   -675       O  
ATOM    904  CB  GLN A 145     -19.489  -0.572  63.046  1.00112.16           C  
ANISOU  904  CB  GLN A 145    17035  15456  10124   -858  -2453   -558       C  
ATOM    905  CG  GLN A 145     -18.305  -0.918  63.933  1.00131.70           C  
ANISOU  905  CG  GLN A 145    19498  18178  12364   -939  -2807   -489       C  
ATOM    906  CD  GLN A 145     -17.294   0.209  64.021  1.00153.52           C  
ANISOU  906  CD  GLN A 145    22227  20980  15122  -1175  -3057   -686       C  
ATOM    907  OE1 GLN A 145     -17.106   0.965  63.068  1.00146.74           O  
ANISOU  907  OE1 GLN A 145    21223  19977  14554  -1254  -3015   -785       O  
ATOM    908  NE2 GLN A 145     -16.637   0.326  65.169  1.00149.61           N  
ANISOU  908  NE2 GLN A 145    21867  20687  14289  -1300  -3323   -737       N  
ATOM    909  N   ARG A 146     -17.472  -0.331  60.409  1.00106.59           N  
ANISOU  909  N   ARG A 146    15594  14715  10189   -950  -2709   -437       N  
ATOM    910  CA  ARG A 146     -16.735   0.569  59.530  1.00105.72           C  
ANISOU  910  CA  ARG A 146    15289  14542  10336  -1089  -2790   -527       C  
ATOM    911  C   ARG A 146     -16.505   0.098  58.097  1.00105.27           C  
ANISOU  911  C   ARG A 146    14920  14440  10640   -992  -2710   -377       C  
ATOM    912  O   ARG A 146     -16.658   0.867  57.149  1.00103.83           O  
ANISOU  912  O   ARG A 146    14652  14113  10684  -1042  -2591   -456       O  
ATOM    913  CB  ARG A 146     -15.321   0.803  60.066  1.00110.26           C  
ANISOU  913  CB  ARG A 146    15760  15310  10825  -1258  -3149   -540       C  
ATOM    914  CG  ARG A 146     -14.959   2.268  60.245  1.00127.81           C  
ANISOU  914  CG  ARG A 146    18077  17452  13032  -1510  -3238   -795       C  
ATOM    915  CD  ARG A 146     -13.496   2.433  60.623  1.00147.51           C  
ANISOU  915  CD  ARG A 146    20402  20161  15486  -1698  -3609   -786       C  
ATOM    916  NE  ARG A 146     -13.210   3.772  61.129  1.00163.43           N  
ANISOU  916  NE  ARG A 146    22587  22113  17396  -1973  -3718  -1059       N  
ATOM    917  CZ  ARG A 146     -12.782   4.029  62.361  1.00183.61           C  
ANISOU  917  CZ  ARG A 146    25321  24825  19615  -2139  -3958  -1180       C  
ATOM    918  NH1 ARG A 146     -12.588   3.036  63.219  1.00172.11           N  
ANISOU  918  NH1 ARG A 146    23888  23616  17892  -2041  -4119  -1026       N  
ATOM    919  NH2 ARG A 146     -12.546   5.279  62.736  1.00174.90           N  
ANISOU  919  NH2 ARG A 146    24384  23630  18438  -2408  -4037  -1455       N  
ATOM    920  N   PRO A 147     -16.135  -1.170  57.949  1.00 99.79           N  
ANISOU  920  N   PRO A 147    14066  13862   9987   -848  -2767   -159       N  
ATOM    921  CA  PRO A 147     -15.875  -1.748  56.626  1.00 96.25           C  
ANISOU  921  CA  PRO A 147    13336  13380   9853   -745  -2685    -21       C  
ATOM    922  C   PRO A 147     -16.991  -1.330  55.674  1.00 94.07           C  
ANISOU  922  C   PRO A 147    13094  12907   9739   -709  -2392    -95       C  
ATOM    923  O   PRO A 147     -16.744  -1.136  54.484  1.00 91.31           O  
ANISOU  923  O   PRO A 147    12540  12506   9649   -710  -2331    -73       O  
ATOM    924  CB  PRO A 147     -15.984  -3.242  56.941  1.00 98.16           C  
ANISOU  924  CB  PRO A 147    13572  13700  10023   -557  -2671    188       C  
ATOM    925  CG  PRO A 147     -16.801  -3.302  58.183  1.00104.41           C  
ANISOU  925  CG  PRO A 147    14674  14502  10496   -549  -2630    141       C  
ATOM    926  CD  PRO A 147     -16.421  -2.088  58.979  1.00102.58           C  
ANISOU  926  CD  PRO A 147    14577  14318  10080   -746  -2797    -53       C  
ATOM    927  N   ARG A 148     -18.205  -1.194  56.199  1.00 88.70           N  
ANISOU  927  N   ARG A 148    12663  12138   8902   -672  -2212   -171       N  
ATOM    928  CA  ARG A 148     -19.351  -0.803  55.387  1.00 85.69           C  
ANISOU  928  CA  ARG A 148    12307  11594   8656   -626  -1939   -224       C  
ATOM    929  C   ARG A 148     -19.403   0.709  55.194  1.00 89.40           C  
ANISOU  929  C   ARG A 148    12836  11942   9188   -760  -1907   -406       C  
ATOM    930  O   ARG A 148     -19.469   1.199  54.067  1.00 87.64           O  
ANISOU  930  O   ARG A 148    12468  11631   9201   -770  -1811   -408       O  
ATOM    931  CB  ARG A 148     -20.652  -1.297  56.023  1.00 84.63           C  
ANISOU  931  CB  ARG A 148    12387  11422   8347   -522  -1742   -210       C  
ATOM    932  CG  ARG A 148     -20.757  -2.810  56.125  1.00 89.03           C  
ANISOU  932  CG  ARG A 148    12902  12053   8873   -390  -1726    -21       C  
ATOM    933  CD  ARG A 148     -21.704  -3.223  57.239  1.00 94.85           C  
ANISOU  933  CD  ARG A 148    13890  12799   9350   -334  -1613     -8       C  
ATOM    934  NE  ARG A 148     -23.074  -3.385  56.761  1.00 98.85           N  
ANISOU  934  NE  ARG A 148    14426  13202   9932   -262  -1330      1       N  
ATOM    935  CZ  ARG A 148     -24.139  -3.456  57.553  1.00115.87           C  
ANISOU  935  CZ  ARG A 148    16783  15337  11903   -223  -1162    -14       C  
ATOM    936  NH1 ARG A 148     -23.995  -3.381  58.869  1.00105.28           N  
ANISOU  936  NH1 ARG A 148    15661  14069  10270   -244  -1242    -48       N  
ATOM    937  NH2 ARG A 148     -25.348  -3.603  57.030  1.00104.78           N  
ANISOU  937  NH2 ARG A 148    15356  13859  10597   -166   -915      8       N  
ATOM    938  N   LYS A 149     -19.373   1.443  56.302  1.00 87.59           N  
ANISOU  938  N   LYS A 149    12836  11704   8739   -865  -1982   -560       N  
ATOM    939  CA  LYS A 149     -19.422   2.899  56.258  1.00 87.91           C  
ANISOU  939  CA  LYS A 149    12981  11596   8826  -1001  -1943   -752       C  
ATOM    940  C   LYS A 149     -18.534   3.451  55.147  1.00 89.94           C  
ANISOU  940  C   LYS A 149    12987  11819   9368  -1098  -2024   -734       C  
ATOM    941  O   LYS A 149     -19.018   4.092  54.214  1.00 88.82           O  
ANISOU  941  O   LYS A 149    12791  11530   9427  -1080  -1849   -748       O  
ATOM    942  CB  LYS A 149     -19.004   3.490  57.606  1.00 93.69           C  
ANISOU  942  CB  LYS A 149    13955  12366   9279  -1150  -2109   -924       C  
ATOM    943  CG  LYS A 149     -19.274   4.979  57.742  1.00107.42           C  
ANISOU  943  CG  LYS A 149    15883  13903  11028  -1280  -2018  -1156       C  
ATOM    944  CD  LYS A 149     -18.085   5.702  58.355  1.00119.31           C  
ANISOU  944  CD  LYS A 149    17433  15457  12442  -1526  -2295  -1306       C  
ATOM    945  CE  LYS A 149     -18.504   7.023  58.979  1.00130.34           C  
ANISOU  945  CE  LYS A 149    19144  16651  13727  -1653  -2196  -1577       C  
ATOM    946  NZ  LYS A 149     -17.330   7.875  59.317  1.00141.28           N  
ANISOU  946  NZ  LYS A 149    20543  18043  15093  -1934  -2454  -1739       N  
ATOM    947  N   LEU A 150     -17.234   3.199  55.254  1.00 86.04           N  
ANISOU  947  N   LEU A 150    12330  11474   8889  -1196  -2287   -685       N  
ATOM    948  CA  LEU A 150     -16.276   3.677  54.263  1.00 85.01           C  
ANISOU  948  CA  LEU A 150    11942  11338   9022  -1299  -2372   -653       C  
ATOM    949  C   LEU A 150     -16.600   3.202  52.850  1.00 84.74           C  
ANISOU  949  C   LEU A 150    11690  11268   9238  -1158  -2194   -504       C  
ATOM    950  O   LEU A 150     -16.497   3.997  51.921  1.00 83.31           O  
ANISOU  950  O   LEU A 150    11405  10982   9266  -1219  -2115   -522       O  
ATOM    951  CB  LEU A 150     -14.845   3.282  54.665  1.00 87.03           C  
ANISOU  951  CB  LEU A 150    12021  11803   9244  -1400  -2684   -589       C  
ATOM    952  CG  LEU A 150     -13.757   4.357  54.530  1.00 93.52           C  
ANISOU  952  CG  LEU A 150    12730  12618  10184  -1645  -2860   -685       C  
ATOM    953  CD1 LEU A 150     -13.955   5.502  55.532  1.00 96.26           C  
ANISOU  953  CD1 LEU A 150    13377  12854  10342  -1839  -2908   -933       C  
ATOM    954  CD2 LEU A 150     -12.402   3.752  54.747  1.00 96.86           C  
ANISOU  954  CD2 LEU A 150    12903  13288  10613  -1700  -3149   -564       C  
ATOM    955  N   LEU A 151     -17.006   1.929  52.687  1.00 79.75           N  
ANISOU  955  N   LEU A 151    11004  10718   8579   -980  -2125   -362       N  
ATOM    956  CA  LEU A 151     -17.367   1.342  51.387  1.00 76.82           C  
ANISOU  956  CA  LEU A 151    10451  10329   8409   -851  -1958   -236       C  
ATOM    957  C   LEU A 151     -18.589   2.028  50.755  1.00 78.83           C  
ANISOU  957  C   LEU A 151    10792  10423   8738   -814  -1708   -289       C  
ATOM    958  O   LEU A 151     -18.639   2.173  49.530  1.00 77.22           O  
ANISOU  958  O   LEU A 151    10422  10189   8731   -790  -1607   -227       O  
ATOM    959  CB  LEU A 151     -17.611  -0.172  51.520  1.00 76.13           C  
ANISOU  959  CB  LEU A 151    10341  10335   8252   -688  -1933    -99       C  
ATOM    960  CG  LEU A 151     -17.547  -0.993  50.233  1.00 79.72           C  
ANISOU  960  CG  LEU A 151    10577  10809   8904   -581  -1831     30       C  
ATOM    961  CD1 LEU A 151     -16.124  -1.429  49.924  1.00 81.21           C  
ANISOU  961  CD1 LEU A 151    10529  11121   9207   -587  -2002    126       C  
ATOM    962  CD2 LEU A 151     -18.436  -2.212  50.325  1.00 82.01           C  
ANISOU  962  CD2 LEU A 151    10946  11095   9120   -436  -1698    108       C  
ATOM    963  N   ALA A 152     -19.559   2.455  51.599  1.00 75.39           N  
ANISOU  963  N   ALA A 152    10609   9897   8137   -803  -1607   -394       N  
ATOM    964  CA  ALA A 152     -20.791   3.124  51.183  1.00 73.85           C  
ANISOU  964  CA  ALA A 152    10505   9558   7996   -746  -1367   -435       C  
ATOM    965  C   ALA A 152     -20.599   4.610  50.938  1.00 78.41           C  
ANISOU  965  C   ALA A 152    11124   9981   8686   -862  -1342   -545       C  
ATOM    966  O   ALA A 152     -21.184   5.142  49.994  1.00 77.03           O  
ANISOU  966  O   ALA A 152    10883   9711   8673   -814  -1176   -506       O  
ATOM    967  CB  ALA A 152     -21.884   2.906  52.219  1.00 75.01           C  
ANISOU  967  CB  ALA A 152    10894   9679   7926   -668  -1248   -488       C  
ATOM    968  N   GLU A 153     -19.805   5.280  51.791  1.00 77.13           N  
ANISOU  968  N   GLU A 153    11077   9793   8435  -1019  -1507   -678       N  
ATOM    969  CA  GLU A 153     -19.568   6.722  51.710  1.00 78.58           C  
ANISOU  969  CA  GLU A 153    11341   9797   8718  -1159  -1489   -808       C  
ATOM    970  C   GLU A 153     -18.414   7.145  50.801  1.00 83.91           C  
ANISOU  970  C   GLU A 153    11780  10482   9620  -1291  -1607   -755       C  
ATOM    971  O   GLU A 153     -18.446   8.265  50.292  1.00 84.64           O  
ANISOU  971  O   GLU A 153    11890  10401   9870  -1365  -1517   -799       O  
ATOM    972  CB  GLU A 153     -19.375   7.321  53.108  1.00 82.75           C  
ANISOU  972  CB  GLU A 153    12145  10271   9024  -1292  -1591  -1012       C  
ATOM    973  CG  GLU A 153     -20.637   7.337  53.955  1.00 94.20           C  
ANISOU  973  CG  GLU A 153    13873  11647  10272  -1172  -1404  -1098       C  
ATOM    974  CD  GLU A 153     -20.419   7.356  55.457  1.00122.42           C  
ANISOU  974  CD  GLU A 153    17707  15271  13537  -1266  -1534  -1261       C  
ATOM    975  OE1 GLU A 153     -19.384   7.896  55.912  1.00122.33           O  
ANISOU  975  OE1 GLU A 153    17732  15270  13478  -1472  -1749  -1382       O  
ATOM    976  OE2 GLU A 153     -21.304   6.851  56.186  1.00117.82           O  
ANISOU  976  OE2 GLU A 153    17294  14724  12748  -1142  -1418  -1267       O  
ATOM    977  N   LYS A 154     -17.389   6.284  50.617  1.00 80.25           N  
ANISOU  977  N   LYS A 154    11098  10215   9180  -1316  -1796   -651       N  
ATOM    978  CA  LYS A 154     -16.206   6.625  49.815  1.00 80.15           C  
ANISOU  978  CA  LYS A 154    10836  10240   9376  -1444  -1910   -590       C  
ATOM    979  C   LYS A 154     -15.988   5.745  48.569  1.00 81.20           C  
ANISOU  979  C   LYS A 154    10686  10496   9670  -1318  -1855   -396       C  
ATOM    980  O   LYS A 154     -15.963   6.269  47.457  1.00 79.92           O  
ANISOU  980  O   LYS A 154    10395  10267   9703  -1328  -1742   -332       O  
ATOM    981  CB  LYS A 154     -14.929   6.654  50.687  1.00 84.95           C  
ANISOU  981  CB  LYS A 154    11406  10972   9900  -1629  -2201   -654       C  
ATOM    982  CG  LYS A 154     -15.068   7.339  52.047  1.00100.62           C  
ANISOU  982  CG  LYS A 154    13690  12879  11664  -1766  -2290   -865       C  
ATOM    983  CD  LYS A 154     -14.580   8.781  52.036  1.00115.65           C  
ANISOU  983  CD  LYS A 154    15657  14604  13679  -2008  -2324  -1014       C  
ATOM    984  CE  LYS A 154     -14.547   9.360  53.431  1.00132.69           C  
ANISOU  984  CE  LYS A 154    18111  16712  15592  -2170  -2446  -1245       C  
ATOM    985  NZ  LYS A 154     -13.935  10.715  53.457  1.00145.59           N  
ANISOU  985  NZ  LYS A 154    19807  18170  17341  -2444  -2505  -1406       N  
ATOM    986  N   VAL A 155     -15.812   4.422  48.766  1.00 77.27           N  
ANISOU  986  N   VAL A 155    10105  10169   9084  -1201  -1927   -303       N  
ATOM    987  CA  VAL A 155     -15.531   3.410  47.729  1.00 75.81           C  
ANISOU  987  CA  VAL A 155     9679  10104   9022  -1076  -1882   -141       C  
ATOM    988  C   VAL A 155     -16.599   3.340  46.600  1.00 78.59           C  
ANISOU  988  C   VAL A 155    10014  10384   9461   -952  -1635    -81       C  
ATOM    989  O   VAL A 155     -16.246   2.996  45.470  1.00 77.52           O  
ANISOU  989  O   VAL A 155     9674  10312   9468   -909  -1581     23       O  
ATOM    990  CB  VAL A 155     -15.188   2.011  48.349  1.00 79.76           C  
ANISOU  990  CB  VAL A 155    10144  10763   9399   -968  -2000    -64       C  
ATOM    991  CG1 VAL A 155     -14.646   1.032  47.306  1.00 78.42           C  
ANISOU  991  CG1 VAL A 155     9721  10699   9375   -856  -1964     85       C  
ATOM    992  CG2 VAL A 155     -14.197   2.142  49.504  1.00 82.19           C  
ANISOU  992  CG2 VAL A 155    10467  11168   9593  -1091  -2261   -109       C  
ATOM    993  N   VAL A 156     -17.873   3.699  46.887  1.00 74.95           N  
ANISOU  993  N   VAL A 156     9759   9806   8914   -899  -1487   -144       N  
ATOM    994  CA  VAL A 156     -18.937   3.678  45.873  1.00 73.29           C  
ANISOU  994  CA  VAL A 156     9519   9554   8774   -790  -1273    -78       C  
ATOM    995  C   VAL A 156     -18.740   4.719  44.736  1.00 77.70           C  
ANISOU  995  C   VAL A 156     9957  10040   9525   -849  -1193    -34       C  
ATOM    996  O   VAL A 156     -19.204   4.502  43.617  1.00 75.82           O  
ANISOU  996  O   VAL A 156     9605   9840   9363   -768  -1064     64       O  
ATOM    997  CB  VAL A 156     -20.367   3.665  46.487  1.00 76.80           C  
ANISOU  997  CB  VAL A 156    10174   9924   9082   -699  -1132   -129       C  
ATOM    998  CG1 VAL A 156     -20.891   5.077  46.747  1.00 77.71           C  
ANISOU  998  CG1 VAL A 156    10444   9860   9221   -747  -1039   -219       C  
ATOM    999  CG2 VAL A 156     -21.338   2.871  45.614  1.00 74.56           C  
ANISOU  999  CG2 VAL A 156     9809   9702   8819   -568   -977    -29       C  
ATOM   1000  N   TYR A 157     -18.035   5.824  45.021  1.00 76.57           N  
ANISOU 1000  N   TYR A 157     9842   9798   9452   -999  -1271   -102       N  
ATOM   1001  CA  TYR A 157     -17.785   6.867  44.029  1.00 77.02           C  
ANISOU 1001  CA  TYR A 157     9801   9764   9699  -1069  -1193    -48       C  
ATOM   1002  C   TYR A 157     -16.608   6.507  43.135  1.00 81.85           C  
ANISOU 1002  C   TYR A 157    10145  10513  10442  -1118  -1266     60       C  
ATOM   1003  O   TYR A 157     -16.711   6.613  41.913  1.00 81.07           O  
ANISOU 1003  O   TYR A 157     9909  10439  10454  -1074  -1146    174       O  
ATOM   1004  CB  TYR A 157     -17.585   8.229  44.712  1.00 80.13           C  
ANISOU 1004  CB  TYR A 157    10360   9958  10127  -1224  -1222   -174       C  
ATOM   1005  CG  TYR A 157     -18.815   8.707  45.454  1.00 82.13           C  
ANISOU 1005  CG  TYR A 157    10881  10053  10270  -1151  -1095   -275       C  
ATOM   1006  CD1 TYR A 157     -18.969   8.465  46.816  1.00 85.13           C  
ANISOU 1006  CD1 TYR A 157    11463  10429  10452  -1170  -1179   -419       C  
ATOM   1007  CD2 TYR A 157     -19.840   9.375  44.789  1.00 82.47           C  
ANISOU 1007  CD2 TYR A 157    10968   9967  10400  -1049   -881   -213       C  
ATOM   1008  CE1 TYR A 157     -20.106   8.892  47.502  1.00 86.99           C  
ANISOU 1008  CE1 TYR A 157    11946  10525  10582  -1091  -1035   -513       C  
ATOM   1009  CE2 TYR A 157     -20.979   9.810  45.464  1.00 83.97           C  
ANISOU 1009  CE2 TYR A 157    11385  10017  10504   -960   -743   -295       C  
ATOM   1010  CZ  TYR A 157     -21.103   9.576  46.824  1.00 94.22           C  
ANISOU 1010  CZ  TYR A 157    12889  11303  11609   -983   -812   -452       C  
ATOM   1011  OH  TYR A 157     -22.223  10.008  47.492  1.00 97.46           O  
ANISOU 1011  OH  TYR A 157    13523  11578  11931   -885   -651   -534       O  
ATOM   1012  N   VAL A 158     -15.501   6.032  43.735  1.00 79.68           N  
ANISOU 1012  N   VAL A 158     9786  10347  10144  -1197  -1459     34       N  
ATOM   1013  CA  VAL A 158     -14.254   5.628  43.085  1.00 79.97           C  
ANISOU 1013  CA  VAL A 158     9552  10530  10303  -1237  -1543    133       C  
ATOM   1014  C   VAL A 158     -14.428   4.325  42.277  1.00 81.64           C  
ANISOU 1014  C   VAL A 158     9632  10887  10501  -1058  -1457    241       C  
ATOM   1015  O   VAL A 158     -13.939   4.241  41.151  1.00 80.76           O  
ANISOU 1015  O   VAL A 158     9324  10847  10513  -1044  -1386    342       O  
ATOM   1016  CB  VAL A 158     -13.115   5.517  44.145  1.00 86.27           C  
ANISOU 1016  CB  VAL A 158    10306  11411  11063  -1365  -1789     76       C  
ATOM   1017  CG1 VAL A 158     -12.941   4.087  44.655  1.00 85.76           C  
ANISOU 1017  CG1 VAL A 158    10202  11508  10875  -1228  -1882    116       C  
ATOM   1018  CG2 VAL A 158     -11.793   6.058  43.602  1.00 87.86           C  
ANISOU 1018  CG2 VAL A 158    10260  11669  11455  -1521  -1872    139       C  
ATOM   1019  N   GLY A 159     -15.128   3.347  42.879  1.00 77.44           N  
ANISOU 1019  N   GLY A 159     9224  10386   9814   -935  -1455    211       N  
ATOM   1020  CA  GLY A 159     -15.319   2.014  42.310  1.00 76.01           C  
ANISOU 1020  CA  GLY A 159     8961  10313   9606   -780  -1383    285       C  
ATOM   1021  C   GLY A 159     -16.529   1.761  41.432  1.00 78.39           C  
ANISOU 1021  C   GLY A 159     9310  10594   9882   -679  -1188    312       C  
ATOM   1022  O   GLY A 159     -16.542   0.763  40.701  1.00 76.90           O  
ANISOU 1022  O   GLY A 159     9030  10493   9697   -584  -1118    366       O  
ATOM   1023  N   VAL A 160     -17.570   2.621  41.514  1.00 74.59           N  
ANISOU 1023  N   VAL A 160     8972   9999   9369   -696  -1098    274       N  
ATOM   1024  CA  VAL A 160     -18.792   2.457  40.706  1.00 72.54           C  
ANISOU 1024  CA  VAL A 160     8737   9745   9081   -606   -929    314       C  
ATOM   1025  C   VAL A 160     -19.015   3.642  39.770  1.00 76.18           C  
ANISOU 1025  C   VAL A 160     9145  10152   9649   -645   -828    375       C  
ATOM   1026  O   VAL A 160     -19.138   3.434  38.563  1.00 75.09           O  
ANISOU 1026  O   VAL A 160     8883  10103   9547   -606   -736    462       O  
ATOM   1027  CB  VAL A 160     -20.072   2.115  41.534  1.00 75.48           C  
ANISOU 1027  CB  VAL A 160     9300  10068   9312   -538   -878    257       C  
ATOM   1028  CG1 VAL A 160     -21.248   1.740  40.635  1.00 73.75           C  
ANISOU 1028  CG1 VAL A 160     9053   9900   9067   -457   -726    313       C  
ATOM   1029  CG2 VAL A 160     -19.807   1.005  42.538  1.00 75.47           C  
ANISOU 1029  CG2 VAL A 160     9367  10106   9202   -504   -977    217       C  
ATOM   1030  N   TRP A 161     -19.079   4.870  40.320  1.00 73.71           N  
ANISOU 1030  N   TRP A 161     8938   9689   9378   -721   -838    331       N  
ATOM   1031  CA  TRP A 161     -19.346   6.084  39.550  1.00 74.32           C  
ANISOU 1031  CA  TRP A 161     8995   9673   9570   -748   -729    403       C  
ATOM   1032  C   TRP A 161     -18.253   6.500  38.577  1.00 79.90           C  
ANISOU 1032  C   TRP A 161     9514  10422  10421   -832   -738    495       C  
ATOM   1033  O   TRP A 161     -18.577   6.838  37.437  1.00 80.08           O  
ANISOU 1033  O   TRP A 161     9452  10478  10496   -795   -619    614       O  
ATOM   1034  CB  TRP A 161     -19.786   7.236  40.454  1.00 74.42           C  
ANISOU 1034  CB  TRP A 161     9206   9478   9594   -793   -710    318       C  
ATOM   1035  CG  TRP A 161     -21.109   6.981  41.107  1.00 74.64           C  
ANISOU 1035  CG  TRP A 161     9396   9471   9494   -679   -630    268       C  
ATOM   1036  CD1 TRP A 161     -21.324   6.589  42.394  1.00 77.83           C  
ANISOU 1036  CD1 TRP A 161     9963   9846   9763   -674   -693    144       C  
ATOM   1037  CD2 TRP A 161     -22.397   7.015  40.477  1.00 73.59           C  
ANISOU 1037  CD2 TRP A 161     9255   9360   9347   -550   -472    358       C  
ATOM   1038  NE1 TRP A 161     -22.666   6.400  42.613  1.00 76.43           N  
ANISOU 1038  NE1 TRP A 161     9881   9658   9499   -553   -566    149       N  
ATOM   1039  CE2 TRP A 161     -23.350   6.653  41.453  1.00 77.09           C  
ANISOU 1039  CE2 TRP A 161     9852   9778   9663   -476   -436    280       C  
ATOM   1040  CE3 TRP A 161     -22.840   7.327  39.179  1.00 74.53           C  
ANISOU 1040  CE3 TRP A 161     9242   9535   9541   -493   -362    509       C  
ATOM   1041  CZ2 TRP A 161     -24.720   6.595  41.178  1.00 75.80           C  
ANISOU 1041  CZ2 TRP A 161     9692   9643   9465   -351   -293    347       C  
ATOM   1042  CZ3 TRP A 161     -24.199   7.270  38.906  1.00 75.32           C  
ANISOU 1042  CZ3 TRP A 161     9350   9674   9592   -368   -239    578       C  
ATOM   1043  CH2 TRP A 161     -25.123   6.915  39.900  1.00 75.89           C  
ANISOU 1043  CH2 TRP A 161     9556   9720   9559   -300   -204    497       C  
ATOM   1044  N   ILE A 162     -16.970   6.468  39.009  1.00 76.81           N  
ANISOU 1044  N   ILE A 162     9047  10049  10087   -945   -878    455       N  
ATOM   1045  CA  ILE A 162     -15.816   6.792  38.160  1.00 77.18           C  
ANISOU 1045  CA  ILE A 162     8889  10155  10280  -1035   -887    548       C  
ATOM   1046  C   ILE A 162     -15.631   5.783  36.995  1.00 80.14           C  
ANISOU 1046  C   ILE A 162     9084  10725  10640   -934   -812    648       C  
ATOM   1047  O   ILE A 162     -15.585   6.241  35.852  1.00 79.60           O  
ANISOU 1047  O   ILE A 162     8914  10689  10642   -938   -698    763       O  
ATOM   1048  CB  ILE A 162     -14.530   7.131  38.983  1.00 81.97           C  
ANISOU 1048  CB  ILE A 162     9444  10738  10964  -1201  -1063    482       C  
ATOM   1049  CG1 ILE A 162     -14.349   8.650  39.128  1.00 84.65           C  
ANISOU 1049  CG1 ILE A 162     9856  10877  11429  -1365  -1052    463       C  
ATOM   1050  CG2 ILE A 162     -13.251   6.491  38.426  1.00 82.57           C  
ANISOU 1050  CG2 ILE A 162     9259  10993  11122  -1223  -1120    563       C  
ATOM   1051  CD1 ILE A 162     -15.279   9.332  40.142  1.00 94.59           C  
ANISOU 1051  CD1 ILE A 162    11396  11932  12612  -1375  -1041    331       C  
ATOM   1052  N   PRO A 163     -15.603   4.437  37.213  1.00 76.09           N  
ANISOU 1052  N   PRO A 163     8550  10332  10027   -838   -853    610       N  
ATOM   1053  CA  PRO A 163     -15.462   3.522  36.069  1.00 75.31           C  
ANISOU 1053  CA  PRO A 163     8312  10391   9912   -747   -758    681       C  
ATOM   1054  C   PRO A 163     -16.662   3.556  35.122  1.00 78.03           C  
ANISOU 1054  C   PRO A 163     8704  10765  10179   -674   -608    731       C  
ATOM   1055  O   PRO A 163     -16.483   3.335  33.921  1.00 78.23           O  
ANISOU 1055  O   PRO A 163     8609  10908  10207   -646   -510    810       O  
ATOM   1056  CB  PRO A 163     -15.273   2.149  36.728  1.00 76.72           C  
ANISOU 1056  CB  PRO A 163     8507  10633  10009   -663   -833    615       C  
ATOM   1057  CG  PRO A 163     -14.888   2.447  38.149  1.00 81.89           C  
ANISOU 1057  CG  PRO A 163     9246  11207  10663   -734  -1000    541       C  
ATOM   1058  CD  PRO A 163     -15.663   3.674  38.474  1.00 77.46           C  
ANISOU 1058  CD  PRO A 163     8834  10498  10098   -807   -976    507       C  
ATOM   1059  N   ALA A 164     -17.869   3.889  35.649  1.00 73.33           N  
ANISOU 1059  N   ALA A 164     8274  10075   9512   -645   -589    693       N  
ATOM   1060  CA  ALA A 164     -19.105   4.011  34.862  1.00 72.20           C  
ANISOU 1060  CA  ALA A 164     8162   9972   9299   -578   -467    755       C  
ATOM   1061  C   ALA A 164     -18.948   5.091  33.794  1.00 76.91           C  
ANISOU 1061  C   ALA A 164     8667  10573   9984   -613   -380    893       C  
ATOM   1062  O   ALA A 164     -19.357   4.879  32.653  1.00 76.26           O  
ANISOU 1062  O   ALA A 164     8509  10624   9841   -567   -289    980       O  
ATOM   1063  CB  ALA A 164     -20.285   4.334  35.765  1.00 72.44           C  
ANISOU 1063  CB  ALA A 164     8364   9889   9271   -542   -462    702       C  
ATOM   1064  N   LEU A 165     -18.298   6.215  34.157  1.00 74.56           N  
ANISOU 1064  N   LEU A 165     8376  10132   9823   -707   -410    913       N  
ATOM   1065  CA  LEU A 165     -18.015   7.334  33.265  1.00 75.34           C  
ANISOU 1065  CA  LEU A 165     8397  10193  10034   -758   -325   1056       C  
ATOM   1066  C   LEU A 165     -16.895   7.003  32.268  1.00 79.89           C  
ANISOU 1066  C   LEU A 165     8778  10923  10655   -797   -297   1137       C  
ATOM   1067  O   LEU A 165     -16.937   7.469  31.129  1.00 79.56           O  
ANISOU 1067  O   LEU A 165     8655  10948  10628   -790   -188   1283       O  
ATOM   1068  CB  LEU A 165     -17.657   8.573  34.085  1.00 76.71           C  
ANISOU 1068  CB  LEU A 165     8663  10135  10349   -869   -365   1026       C  
ATOM   1069  CG  LEU A 165     -18.773   9.583  34.259  1.00 81.80           C  
ANISOU 1069  CG  LEU A 165     9457  10606  11015   -819   -276   1064       C  
ATOM   1070  CD1 LEU A 165     -19.555   9.321  35.522  1.00 81.35           C  
ANISOU 1070  CD1 LEU A 165     9583  10458  10868   -769   -325    911       C  
ATOM   1071  CD2 LEU A 165     -18.217  10.980  34.309  1.00 87.00           C  
ANISOU 1071  CD2 LEU A 165    10149  11052  11854   -939   -245   1114       C  
ATOM   1072  N   LEU A 166     -15.899   6.198  32.695  1.00 77.30           N  
ANISOU 1072  N   LEU A 166     8370  10657  10341   -827   -388   1054       N  
ATOM   1073  CA  LEU A 166     -14.776   5.787  31.842  1.00 78.27           C  
ANISOU 1073  CA  LEU A 166     8296  10930  10514   -844   -349   1122       C  
ATOM   1074  C   LEU A 166     -15.255   4.913  30.685  1.00 82.14           C  
ANISOU 1074  C   LEU A 166     8744  11603  10862   -734   -232   1161       C  
ATOM   1075  O   LEU A 166     -14.706   4.995  29.582  1.00 82.67           O  
ANISOU 1075  O   LEU A 166     8677  11789  10945   -741   -129   1265       O  
ATOM   1076  CB  LEU A 166     -13.686   5.055  32.647  1.00 78.79           C  
ANISOU 1076  CB  LEU A 166     8281  11026  10630   -870   -475   1034       C  
ATOM   1077  CG  LEU A 166     -12.965   5.860  33.727  1.00 85.19           C  
ANISOU 1077  CG  LEU A 166     9096  11703  11570  -1013   -616    990       C  
ATOM   1078  CD1 LEU A 166     -12.244   4.951  34.695  1.00 85.83           C  
ANISOU 1078  CD1 LEU A 166     9133  11838  11640  -1001   -768    899       C  
ATOM   1079  CD2 LEU A 166     -12.003   6.874  33.129  1.00 89.72           C  
ANISOU 1079  CD2 LEU A 166     9512  12262  12316  -1151   -576   1107       C  
ATOM   1080  N   LEU A 167     -16.288   4.090  30.935  1.00 77.69           N  
ANISOU 1080  N   LEU A 167     8299  11065  10154   -646   -242   1073       N  
ATOM   1081  CA  LEU A 167     -16.879   3.220  29.917  1.00 77.35           C  
ANISOU 1081  CA  LEU A 167     8246  11189   9956   -568   -147   1078       C  
ATOM   1082  C   LEU A 167     -17.846   3.991  29.011  1.00 82.44           C  
ANISOU 1082  C   LEU A 167     8907  11885  10532   -559    -60   1203       C  
ATOM   1083  O   LEU A 167     -18.259   3.475  27.973  1.00 82.21           O  
ANISOU 1083  O   LEU A 167     8848  12024  10364   -521     18   1231       O  
ATOM   1084  CB  LEU A 167     -17.581   2.007  30.560  1.00 76.08           C  
ANISOU 1084  CB  LEU A 167     8197  11028   9680   -502   -194    937       C  
ATOM   1085  CG  LEU A 167     -16.705   1.029  31.357  1.00 80.76           C  
ANISOU 1085  CG  LEU A 167     8777  11592  10316   -477   -268    836       C  
ATOM   1086  CD1 LEU A 167     -17.552  -0.024  32.019  1.00 79.85           C  
ANISOU 1086  CD1 LEU A 167     8799  11446  10093   -421   -302    724       C  
ATOM   1087  CD2 LEU A 167     -15.642   0.361  30.482  1.00 84.02           C  
ANISOU 1087  CD2 LEU A 167     9046  12128  10751   -444   -189    854       C  
ATOM   1088  N   THR A 168     -18.184   5.233  29.398  1.00 80.12           N  
ANISOU 1088  N   THR A 168     8663  11445  10333   -593    -72   1280       N  
ATOM   1089  CA  THR A 168     -19.098   6.107  28.672  1.00 80.63           C  
ANISOU 1089  CA  THR A 168     8741  11529  10364   -564      6   1431       C  
ATOM   1090  C   THR A 168     -18.417   6.945  27.562  1.00 85.52           C  
ANISOU 1090  C   THR A 168     9244  12204  11048   -606    103   1615       C  
ATOM   1091  O   THR A 168     -19.114   7.565  26.762  1.00 85.88           O  
ANISOU 1091  O   THR A 168     9282  12307  11043   -568    176   1773       O  
ATOM   1092  CB  THR A 168     -20.036   6.823  29.666  1.00 93.29           C  
ANISOU 1092  CB  THR A 168    10482  12945  12018   -539    -29   1412       C  
ATOM   1093  OG1 THR A 168     -21.385   6.681  29.233  1.00 95.90           O  
ANISOU 1093  OG1 THR A 168    10839  13379  12220   -453     11   1469       O  
ATOM   1094  CG2 THR A 168     -19.701   8.292  29.885  1.00 94.06           C  
ANISOU 1094  CG2 THR A 168    10606  12838  12293   -595      0   1511       C  
ATOM   1095  N   ILE A 169     -17.064   6.938  27.500  1.00 82.45           N  
ANISOU 1095  N   ILE A 169     8750  11811  10767   -681    106   1611       N  
ATOM   1096  CA  ILE A 169     -16.268   7.642  26.479  1.00 83.59           C  
ANISOU 1096  CA  ILE A 169     8766  12014  10980   -735    211   1786       C  
ATOM   1097  C   ILE A 169     -16.558   7.101  25.052  1.00 88.84           C  
ANISOU 1097  C   ILE A 169     9367  12941  11449   -671    322   1874       C  
ATOM   1098  O   ILE A 169     -16.899   7.926  24.206  1.00 89.33           O  
ANISOU 1098  O   ILE A 169     9409  13046  11485   -665    407   2065       O  
ATOM   1099  CB  ILE A 169     -14.747   7.754  26.844  1.00 87.24           C  
ANISOU 1099  CB  ILE A 169     9107  12421  11621   -842    184   1761       C  
ATOM   1100  CG1 ILE A 169     -14.545   8.575  28.136  1.00 87.82           C  
ANISOU 1100  CG1 ILE A 169     9259  12238  11872   -940     72   1697       C  
ATOM   1101  CG2 ILE A 169     -13.926   8.371  25.706  1.00 89.32           C  
ANISOU 1101  CG2 ILE A 169     9220  12772  11947   -899    318   1952       C  
ATOM   1102  CD1 ILE A 169     -13.444   8.084  29.060  1.00 93.24           C  
ANISOU 1102  CD1 ILE A 169     9873  12899  12656  -1013    -50   1565       C  
ATOM   1103  N   PRO A 170     -16.536   5.763  24.754  1.00 85.81           N  
ANISOU 1103  N   PRO A 170     8969  12725  10908   -619    327   1744       N  
ATOM   1104  CA  PRO A 170     -16.870   5.308  23.384  1.00 86.80           C  
ANISOU 1104  CA  PRO A 170     9062  13099  10819   -577    432   1807       C  
ATOM   1105  C   PRO A 170     -18.300   5.640  22.922  1.00 92.95           C  
ANISOU 1105  C   PRO A 170     9912  13960  11445   -534    425   1900       C  
ATOM   1106  O   PRO A 170     -18.678   5.324  21.796  1.00 93.26           O  
ANISOU 1106  O   PRO A 170     9930  14226  11280   -513    489   1958       O  
ATOM   1107  CB  PRO A 170     -16.616   3.793  23.437  1.00 87.45           C  
ANISOU 1107  CB  PRO A 170     9157  13275  10795   -539    428   1604       C  
ATOM   1108  CG  PRO A 170     -15.724   3.597  24.601  1.00 91.14           C  
ANISOU 1108  CG  PRO A 170     9600  13574  11456   -558    349   1502       C  
ATOM   1109  CD  PRO A 170     -16.168   4.610  25.600  1.00 86.15           C  
ANISOU 1109  CD  PRO A 170     9037  12738  10959   -599    248   1539       C  
ATOM   1110  N   ASP A 171     -19.088   6.288  23.789  1.00 90.26           N  
ANISOU 1110  N   ASP A 171     9651  13447  11196   -519    349   1917       N  
ATOM   1111  CA  ASP A 171     -20.437   6.744  23.482  1.00 90.78           C  
ANISOU 1111  CA  ASP A 171     9758  13571  11162   -461    342   2034       C  
ATOM   1112  C   ASP A 171     -20.413   8.258  23.294  1.00 95.46           C  
ANISOU 1112  C   ASP A 171    10334  14036  11901   -458    401   2269       C  
ATOM   1113  O   ASP A 171     -21.316   8.802  22.661  1.00 95.78           O  
ANISOU 1113  O   ASP A 171    10365  14168  11860   -395    431   2448       O  
ATOM   1114  CB  ASP A 171     -21.425   6.325  24.581  1.00 91.97           C  
ANISOU 1114  CB  ASP A 171    10011  13622  11313   -424    245   1890       C  
ATOM   1115  CG  ASP A 171     -21.731   4.839  24.610  1.00107.71           C  
ANISOU 1115  CG  ASP A 171    12031  15752  13141   -426    201   1694       C  
ATOM   1116  OD1 ASP A 171     -22.929   4.483  24.662  1.00108.72           O  
ANISOU 1116  OD1 ASP A 171    12194  15961  13154   -397    161   1671       O  
ATOM   1117  OD2 ASP A 171     -20.769   4.028  24.607  1.00115.10           O  
ANISOU 1117  OD2 ASP A 171    12951  16704  14077   -457    212   1567       O  
ATOM   1118  N   PHE A 172     -19.368   8.910  23.778  1.00 92.40           N  
ANISOU 1118  N   PHE A 172     9933  13450  11725   -528    419   2278       N  
ATOM   1119  CA  PHE A 172     -19.235  10.334  23.566  1.00 93.72           C  
ANISOU 1119  CA  PHE A 172    10095  13465  12050   -546    492   2496       C  
ATOM   1120  C   PHE A 172     -18.883  10.555  22.126  1.00 97.36           C  
ANISOU 1120  C   PHE A 172    10450  14134  12408   -548    607   2707       C  
ATOM   1121  O   PHE A 172     -19.142  11.603  21.560  1.00 98.48           O  
ANISOU 1121  O   PHE A 172    10585  14240  12595   -524    686   2949       O  
ATOM   1122  CB  PHE A 172     -18.136  10.889  24.434  1.00 96.29           C  
ANISOU 1122  CB  PHE A 172    10428  13538  12621   -659    472   2429       C  
ATOM   1123  CG  PHE A 172     -18.596  11.293  25.775  1.00 97.76           C  
ANISOU 1123  CG  PHE A 172    10751  13460  12933   -659    392   2307       C  
ATOM   1124  CD1 PHE A 172     -17.927  10.879  26.897  1.00100.95           C  
ANISOU 1124  CD1 PHE A 172    11187  13747  13422   -738    289   2095       C  
ATOM   1125  CD2 PHE A 172     -19.696  12.085  25.918  1.00100.48           C  
ANISOU 1125  CD2 PHE A 172    11190  13684  13302   -572    425   2411       C  
ATOM   1126  CE1 PHE A 172     -18.347  11.253  28.136  1.00101.61           C  
ANISOU 1126  CE1 PHE A 172    11414  13601  13591   -744    221   1973       C  
ATOM   1127  CE2 PHE A 172     -20.120  12.457  27.150  1.00103.21           C  
ANISOU 1127  CE2 PHE A 172    11676  13786  13754   -565    375   2287       C  
ATOM   1128  CZ  PHE A 172     -19.445  12.041  28.263  1.00100.76           C  
ANISOU 1128  CZ  PHE A 172    11416  13365  13505   -657    273   2060       C  
ATOM   1129  N   ILE A 173     -18.291   9.534  21.538  1.00 92.31           N  
ANISOU 1129  N   ILE A 173     9737  13712  11623   -570    627   2615       N  
ATOM   1130  CA  ILE A 173     -17.873   9.566  20.160  1.00 93.16           C  
ANISOU 1130  CA  ILE A 173     9751  14052  11592   -575    748   2781       C  
ATOM   1131  C   ILE A 173     -18.598   9.012  18.961  1.00 96.47           C  
ANISOU 1131  C   ILE A 173    10159  14795  11701   -515    782   2847       C  
ATOM   1132  O   ILE A 173     -18.821   9.690  17.980  1.00 98.38           O  
ANISOU 1132  O   ILE A 173    10365  15163  11853   -492    861   3092       O  
ATOM   1133  CB  ILE A 173     -16.716   8.646  19.972  1.00 96.09           C  
ANISOU 1133  CB  ILE A 173    10044  14528  11940   -623    791   2638       C  
ATOM   1134  CG1 ILE A 173     -15.441   9.243  20.527  1.00 97.36           C  
ANISOU 1134  CG1 ILE A 173    10127  14491  12375   -720    815   2656       C  
ATOM   1135  CG2 ILE A 173     -16.576   8.324  18.532  1.00 97.89           C  
ANISOU 1135  CG2 ILE A 173    10210  15051  11931   -603    914   2745       C  
ATOM   1136  CD1 ILE A 173     -14.494   8.192  21.004  1.00104.72           C  
ANISOU 1136  CD1 ILE A 173    10996  15447  13346   -742    786   2443       C  
ATOM   1137  N   PHE A 174     -18.961   7.745  19.070  1.00 89.84           N  
ANISOU 1137  N   PHE A 174     9355  14086  10692   -499    717   2622       N  
ATOM   1138  CA  PHE A 174     -19.499   6.955  17.975  1.00 89.44           C  
ANISOU 1138  CA  PHE A 174     9304  14355  10325   -478    738   2606       C  
ATOM   1139  C   PHE A 174     -20.983   7.221  17.883  1.00 92.46           C  
ANISOU 1139  C   PHE A 174     9722  14824  10587   -424    650   2703       C  
ATOM   1140  O   PHE A 174     -21.660   6.645  17.046  1.00 93.28           O  
ANISOU 1140  O   PHE A 174     9825  15203  10416   -422    631   2698       O  
ATOM   1141  CB  PHE A 174     -19.295   5.471  18.188  1.00 89.72           C  
ANISOU 1141  CB  PHE A 174     9380  14457  10251   -496    711   2310       C  
ATOM   1142  CG  PHE A 174     -17.880   5.052  18.108  1.00 91.33           C  
ANISOU 1142  CG  PHE A 174     9527  14635  10538   -522    812   2225       C  
ATOM   1143  CD1 PHE A 174     -17.361   4.184  19.018  1.00 92.78           C  
ANISOU 1143  CD1 PHE A 174     9733  14683  10836   -522    770   1997       C  
ATOM   1144  CD2 PHE A 174     -17.066   5.533  17.116  1.00 94.65           C  
ANISOU 1144  CD2 PHE A 174     9860  15177  10923   -538    957   2393       C  
ATOM   1145  CE1 PHE A 174     -16.065   3.812  18.934  1.00 93.96           C  
ANISOU 1145  CE1 PHE A 174     9804  14823  11073   -527    865   1943       C  
ATOM   1146  CE2 PHE A 174     -15.779   5.153  17.031  1.00 97.47           C  
ANISOU 1146  CE2 PHE A 174    10141  15527  11367   -553   1063   2329       C  
ATOM   1147  CZ  PHE A 174     -15.278   4.298  17.938  1.00 94.30           C  
ANISOU 1147  CZ  PHE A 174     9747  14995  11090   -542   1015   2105       C  
ATOM   1148  N   ALA A 175     -21.506   8.073  18.738  1.00 86.96           N  
ANISOU 1148  N   ALA A 175     9051  13901  10087   -383    598   2785       N  
ATOM   1149  CA  ALA A 175     -22.914   8.355  18.682  1.00 86.28           C  
ANISOU 1149  CA  ALA A 175     8973  13898   9912   -311    528   2896       C  
ATOM   1150  C   ALA A 175     -23.110   9.596  17.866  1.00 91.93           C  
ANISOU 1150  C   ALA A 175     9635  14662  10632   -253    601   3241       C  
ATOM   1151  O   ALA A 175     -22.606  10.650  18.208  1.00 92.23           O  
ANISOU 1151  O   ALA A 175     9683  14453  10908   -244    668   3377       O  
ATOM   1152  CB  ALA A 175     -23.438   8.562  20.037  1.00 85.30           C  
ANISOU 1152  CB  ALA A 175     8915  13508   9986   -275    455   2799       C  
ATOM   1153  N   ASN A 176     -23.846   9.475  16.776  1.00 89.52           N  
ANISOU 1153  N   ASN A 176     9277  14678  10060   -222    586   3389       N  
ATOM   1154  CA  ASN A 176     -24.086  10.629  15.900  1.00 91.64           C  
ANISOU 1154  CA  ASN A 176     9488  15029  10303   -150    654   3759       C  
ATOM   1155  C   ASN A 176     -25.409  10.507  15.148  1.00 97.16           C  
ANISOU 1155  C   ASN A 176    10124  16058  10735    -84    566   3910       C  
ATOM   1156  O   ASN A 176     -25.892   9.397  14.927  1.00 95.97           O  
ANISOU 1156  O   ASN A 176     9967  16148  10348   -140    473   3718       O  
ATOM   1157  CB  ASN A 176     -22.945  10.786  14.876  1.00 92.87           C  
ANISOU 1157  CB  ASN A 176     9611  15304  10372   -210    786   3871       C  
ATOM   1158  CG  ASN A 176     -21.601  11.132  15.461  1.00110.02           C  
ANISOU 1158  CG  ASN A 176    11801  17180  12823   -279    882   3802       C  
ATOM   1159  OD1 ASN A 176     -21.388  12.220  16.006  1.00103.40           O  
ANISOU 1159  OD1 ASN A 176    10979  16047  12262   -262    927   3942       O  
ATOM   1160  ND2 ASN A 176     -20.661  10.208  15.359  1.00100.23           N  
ANISOU 1160  ND2 ASN A 176    10553  16010  11519   -362    918   3583       N  
ATOM   1161  N   VAL A 177     -25.973  11.650  14.722  1.00 96.43           N  
ANISOU 1161  N   VAL A 177     9979  15980  10681     30    597   4265       N  
ATOM   1162  CA  VAL A 177     -27.209  11.698  13.938  1.00 98.31           C  
ANISOU 1162  CA  VAL A 177    10123  16557  10674    108    508   4478       C  
ATOM   1163  C   VAL A 177     -26.817  11.534  12.466  1.00106.58           C  
ANISOU 1163  C   VAL A 177    11131  17970  11396     55    547   4623       C  
ATOM   1164  O   VAL A 177     -25.865  12.174  12.011  1.00106.95           O  
ANISOU 1164  O   VAL A 177    11195  17934  11507     47    685   4782       O  
ATOM   1165  CB  VAL A 177     -28.011  13.006  14.177  1.00103.23           C  
ANISOU 1165  CB  VAL A 177    10702  17023  11498    285    532   4818       C  
ATOM   1166  CG1 VAL A 177     -29.403  12.926  13.555  1.00104.62           C  
ANISOU 1166  CG1 VAL A 177    10749  17563  11439    375    409   5015       C  
ATOM   1167  CG2 VAL A 177     -28.115  13.324  15.663  1.00101.04           C  
ANISOU 1167  CG2 VAL A 177    10502  16319  11569    332    548   4665       C  
ATOM   1168  N   SER A 178     -27.536  10.665  11.735  1.00106.31           N  
ANISOU 1168  N   SER A 178    11048  18339  11004      4    428   4558       N  
ATOM   1169  CA  SER A 178     -27.286  10.401  10.316  1.00109.67           C  
ANISOU 1169  CA  SER A 178    11452  19160  11057    -56    450   4663       C  
ATOM   1170  C   SER A 178     -28.586  10.271   9.522  1.00117.53           C  
ANISOU 1170  C   SER A 178    12343  20585  11728    -31    293   4834       C  
ATOM   1171  O   SER A 178     -29.562   9.737  10.040  1.00115.86           O  
ANISOU 1171  O   SER A 178    12087  20430  11505    -42    148   4696       O  
ATOM   1172  CB  SER A 178     -26.438   9.144  10.142  1.00112.50           C  
ANISOU 1172  CB  SER A 178    11899  19594  11252   -211    486   4288       C  
ATOM   1173  OG  SER A 178     -27.236   7.975  10.045  1.00121.76           O  
ANISOU 1173  OG  SER A 178    13077  21017  12171   -302    339   4037       O  
ATOM   1174  N   GLU A 179     -28.633  10.801   8.325  1.00119.09           N  
ANISOU 1174  N   GLU A 179    12489  21082  11679      6    317   5152       N  
ATOM   1175  CA  GLU A 179     -29.879  10.741   7.583  1.00122.31           C  
ANISOU 1175  CA  GLU A 179    12775  21920  11776     32    146   5345       C  
ATOM   1176  C   GLU A 179     -30.066   9.347   7.059  1.00127.91           C  
ANISOU 1176  C   GLU A 179    13520  22979  12102   -158     32   5010       C  
ATOM   1177  O   GLU A 179     -29.110   8.608   6.882  1.00126.37           O  
ANISOU 1177  O   GLU A 179    13448  22754  11815   -280    128   4729       O  
ATOM   1178  CB  GLU A 179     -29.945  11.755   6.435  1.00127.54           C  
ANISOU 1178  CB  GLU A 179    13368  22829  12262    138    190   5824       C  
ATOM   1179  CG  GLU A 179     -30.796  13.009   6.767  1.00141.64           C  
ANISOU 1179  CG  GLU A 179    15035  24482  14300    360    171   6242       C  
ATOM   1180  CD  GLU A 179     -30.647  14.179   5.777  1.00170.74           C  
ANISOU 1180  CD  GLU A 179    18678  28289  17907    492    266   6754       C  
ATOM   1181  OE1 GLU A 179     -29.540  14.386   5.242  1.00167.63           O  
ANISOU 1181  OE1 GLU A 179    18375  27849  17466    437    429   6798       O  
ATOM   1182  OE2 GLU A 179     -31.639  14.909   5.548  1.00166.58           O  
ANISOU 1182  OE2 GLU A 179    18016  27898  17377    661    187   7131       O  
ATOM   1183  N   ALA A 180     -31.322   9.003   6.825  1.00127.13           N  
ANISOU 1183  N   ALA A 180    13306  23204  11791   -182   -169   5046       N  
ATOM   1184  CA  ALA A 180     -31.672   7.726   6.248  1.00128.15           C  
ANISOU 1184  CA  ALA A 180    13464  23698  11529   -383   -300   4749       C  
ATOM   1185  C   ALA A 180     -32.925   7.873   5.408  1.00136.51           C  
ANISOU 1185  C   ALA A 180    14353  25252  12260   -384   -507   5011       C  
ATOM   1186  O   ALA A 180     -33.380   8.971   5.122  1.00138.01           O  
ANISOU 1186  O   ALA A 180    14412  25528  12497   -210   -524   5451       O  
ATOM   1187  CB  ALA A 180     -31.889   6.708   7.328  1.00125.72           C  
ANISOU 1187  CB  ALA A 180    13209  23168  11391   -487   -357   4332       C  
ATOM   1188  N   ASP A 181     -33.485   6.745   5.020  1.00134.64           N  
ANISOU 1188  N   ASP A 181    14120  25343  11695   -584   -666   4739       N  
ATOM   1189  CA  ASP A 181     -34.690   6.735   4.229  1.00138.00           C  
ANISOU 1189  CA  ASP A 181    14372  26283  11779   -629   -895   4943       C  
ATOM   1190  C   ASP A 181     -35.885   7.273   4.996  1.00141.15           C  
ANISOU 1190  C   ASP A 181    14553  26635  12444   -489  -1025   5167       C  
ATOM   1191  O   ASP A 181     -36.640   6.511   5.586  1.00140.36           O  
ANISOU 1191  O   ASP A 181    14391  26554  12385   -602  -1156   4930       O  
ATOM   1192  CB  ASP A 181     -34.965   5.305   3.823  1.00140.71           C  
ANISOU 1192  CB  ASP A 181    14791  26913  11760   -913  -1027   4523       C  
ATOM   1193  CG  ASP A 181     -33.861   4.388   4.236  1.00148.96           C  
ANISOU 1193  CG  ASP A 181    16076  27630  12892  -1030   -856   4065       C  
ATOM   1194  OD1 ASP A 181     -32.695   4.706   3.926  1.00149.14           O  
ANISOU 1194  OD1 ASP A 181    16227  27506  12933   -967   -652   4094       O  
ATOM   1195  OD2 ASP A 181     -34.154   3.369   4.890  1.00153.05           O  
ANISOU 1195  OD2 ASP A 181    16644  28029  13477  -1176   -917   3695       O  
ATOM   1196  N   ASP A 182     -36.073   8.581   4.981  1.00137.26           N  
ANISOU 1196  N   ASP A 182    13940  26075  12136   -241   -976   5632       N  
ATOM   1197  CA  ASP A 182     -37.284   9.132   5.553  1.00136.67           C  
ANISOU 1197  CA  ASP A 182    13638  26015  12274    -84  -1091   5888       C  
ATOM   1198  C   ASP A 182     -37.194   9.627   6.980  1.00134.60           C  
ANISOU 1198  C   ASP A 182    13401  25192  12548     81   -952   5852       C  
ATOM   1199  O   ASP A 182     -38.216   9.922   7.580  1.00134.50           O  
ANISOU 1199  O   ASP A 182    13212  25167  12723    200  -1030   5994       O  
ATOM   1200  CB  ASP A 182     -38.321   8.062   5.798  1.00138.52           C  
ANISOU 1200  CB  ASP A 182    13758  26501  12373   -271  -1307   5625       C  
ATOM   1201  N   ARG A 183     -35.991   9.694   7.540  1.00125.83           N  
ANISOU 1201  N   ARG A 183    12501  23632  11676     84   -748   5655       N  
ATOM   1202  CA  ARG A 183     -35.868  10.084   8.939  1.00121.53           C  
ANISOU 1202  CA  ARG A 183    12005  22562  11611    209   -628   5572       C  
ATOM   1203  C   ARG A 183     -34.400  10.210   9.314  1.00121.53           C  
ANISOU 1203  C   ARG A 183    12226  22141  11808    188   -419   5393       C  
ATOM   1204  O   ARG A 183     -33.527   9.723   8.604  1.00120.71           O  
ANISOU 1204  O   ARG A 183    12237  22154  11475     52   -373   5251       O  
ATOM   1205  CB  ARG A 183     -36.653   9.432  10.067  1.00118.34           C  
ANISOU 1205  CB  ARG A 183    11547  22028  11387    168   -709   5315       C  
ATOM   1206  CG  ARG A 183     -36.347   7.973  10.307  1.00122.06           C  
ANISOU 1206  CG  ARG A 183    12144  22513  11721    -91   -760   4818       C  
ATOM   1207  N   TYR A 184     -34.134  10.850  10.445  1.00115.38           N  
ANISOU 1207  N   TYR A 184    11505  20882  11452    318   -293   5393       N  
ATOM   1208  CA  TYR A 184     -32.743  11.005  10.851  1.00112.54           C  
ANISOU 1208  CA  TYR A 184    11332  20133  11296    286   -113   5232       C  
ATOM   1209  C   TYR A 184     -32.582   9.786  11.753  1.00111.07           C  
ANISOU 1209  C   TYR A 184    11238  19802  11162    131   -153   4756       C  
ATOM   1210  O   TYR A 184     -33.557   9.278  12.307  1.00109.79           O  
ANISOU 1210  O   TYR A 184    11002  19702  11013    115   -270   4641       O  
ATOM   1211  CB  TYR A 184     -32.394  12.279  11.622  1.00113.50           C  
ANISOU 1211  CB  TYR A 184    11499  19791  11836    467     45   5434       C  
ATOM   1212  CG  TYR A 184     -32.095  13.468  10.737  1.00118.82           C  
ANISOU 1212  CG  TYR A 184    12145  20502  12500    593    148   5871       C  
ATOM   1213  CD1 TYR A 184     -30.807  13.710  10.278  1.00121.29           C  
ANISOU 1213  CD1 TYR A 184    12569  20705  12810    524    292   5882       C  
ATOM   1214  CD2 TYR A 184     -33.101  14.348  10.360  1.00122.55           C  
ANISOU 1214  CD2 TYR A 184    12471  21120  12975    787    109   6292       C  
ATOM   1215  CE1 TYR A 184     -30.529  14.795   9.468  1.00125.27           C  
ANISOU 1215  CE1 TYR A 184    13052  21233  13310    630    400   6297       C  
ATOM   1216  CE2 TYR A 184     -32.832  15.436   9.551  1.00126.46           C  
ANISOU 1216  CE2 TYR A 184    12949  21634  13466    912    212   6717       C  
ATOM   1217  CZ  TYR A 184     -31.545  15.654   9.108  1.00134.67           C  
ANISOU 1217  CZ  TYR A 184    14115  22554  14499    825    359   6716       C  
ATOM   1218  OH  TYR A 184     -31.273  16.736   8.302  1.00139.91           O  
ANISOU 1218  OH  TYR A 184    14767  23230  15164    939    475   7153       O  
ATOM   1219  N   ILE A 185     -31.345   9.320  11.896  1.00104.30           N  
ANISOU 1219  N   ILE A 185    10535  18754  10341     23    -49   4496       N  
ATOM   1220  CA  ILE A 185     -31.055   8.159  12.728  1.00100.57           C  
ANISOU 1220  CA  ILE A 185    10163  18123   9924   -110    -70   4062       C  
ATOM   1221  C   ILE A 185     -29.887   8.430  13.670  1.00101.81           C  
ANISOU 1221  C   ILE A 185    10450  17823  10412    -90     72   3923       C  
ATOM   1222  O   ILE A 185     -28.758   8.645  13.228  1.00102.28           O  
ANISOU 1222  O   ILE A 185    10570  17820  10471   -117    190   3943       O  
ATOM   1223  CB  ILE A 185     -30.737   6.918  11.874  1.00104.01           C  
ANISOU 1223  CB  ILE A 185    10657  18862  10002   -299   -113   3806       C  
ATOM   1224  CG1 ILE A 185     -32.027   6.287  11.347  1.00106.20           C  
ANISOU 1224  CG1 ILE A 185    10823  19546   9981   -383   -300   3798       C  
ATOM   1225  CG2 ILE A 185     -29.936   5.907  12.681  1.00101.75           C  
ANISOU 1225  CG2 ILE A 185    10513  18310   9836   -404    -59   3397       C  
ATOM   1226  CD1 ILE A 185     -31.823   5.392  10.145  1.00117.35           C  
ANISOU 1226  CD1 ILE A 185    12284  21335  10969   -556   -341   3652       C  
ATOM   1227  N   CYS A 186     -30.165   8.418  14.969  1.00 95.25           N  
ANISOU 1227  N   CYS A 186     9651  16688   9851    -49     60   3786       N  
ATOM   1228  CA  CYS A 186     -29.136   8.658  15.977  1.00 92.42           C  
ANISOU 1228  CA  CYS A 186     9410  15907   9797    -43    166   3640       C  
ATOM   1229  C   CYS A 186     -28.749   7.337  16.614  1.00 93.06           C  
ANISOU 1229  C   CYS A 186     9583  15917   9859   -171    130   3243       C  
ATOM   1230  O   CYS A 186     -29.598   6.685  17.228  1.00 91.91           O  
ANISOU 1230  O   CYS A 186     9429  15789   9703   -194     39   3092       O  
ATOM   1231  CB  CYS A 186     -29.600   9.678  17.019  1.00 92.02           C  
ANISOU 1231  CB  CYS A 186     9361  15537  10064    100    198   3773       C  
ATOM   1232  SG  CYS A 186     -28.788   9.525  18.640  1.00 92.90           S  
ANISOU 1232  SG  CYS A 186     9623  15176  10496     66    247   3469       S  
ATOM   1233  N   ASP A 187     -27.472   6.940  16.442  1.00 87.99           N  
ANISOU 1233  N   ASP A 187     9018  15199   9215   -249    212   3091       N  
ATOM   1234  CA  ASP A 187     -26.858   5.743  17.018  1.00 85.55           C  
ANISOU 1234  CA  ASP A 187     8802  14785   8919   -347    209   2739       C  
ATOM   1235  C   ASP A 187     -25.341   5.717  16.875  1.00 88.10           C  
ANISOU 1235  C   ASP A 187     9171  14982   9320   -381    329   2670       C  
ATOM   1236  O   ASP A 187     -24.770   6.570  16.195  1.00 88.99           O  
ANISOU 1236  O   ASP A 187     9243  15125   9444   -352    419   2890       O  
ATOM   1237  CB  ASP A 187     -27.547   4.420  16.601  1.00 87.80           C  
ANISOU 1237  CB  ASP A 187     9097  15337   8926   -454    118   2529       C  
ATOM   1238  CG  ASP A 187     -26.985   3.687  15.408  1.00102.68           C  
ANISOU 1238  CG  ASP A 187    11010  17479  10523   -549    164   2435       C  
ATOM   1239  OD1 ASP A 187     -27.389   4.009  14.270  1.00106.70           O  
ANISOU 1239  OD1 ASP A 187    11455  18298  10788   -556    146   2623       O  
ATOM   1240  OD2 ASP A 187     -26.221   2.721  15.617  1.00108.04           O  
ANISOU 1240  OD2 ASP A 187    11781  18065  11203   -613    215   2167       O  
ATOM   1241  N   ARG A 188     -24.689   4.764  17.559  1.00 82.58           N  
ANISOU 1241  N   ARG A 188     8547  14134   8694   -436    336   2383       N  
ATOM   1242  CA  ARG A 188     -23.238   4.600  17.564  1.00 81.54           C  
ANISOU 1242  CA  ARG A 188     8436  13883   8662   -461    443   2296       C  
ATOM   1243  C   ARG A 188     -22.781   3.911  16.291  1.00 86.01           C  
ANISOU 1243  C   ARG A 188     9001  14726   8954   -514    523   2245       C  
ATOM   1244  O   ARG A 188     -23.146   2.757  16.047  1.00 85.25           O  
ANISOU 1244  O   ARG A 188     8961  14768   8660   -571    490   2033       O  
ATOM   1245  CB  ARG A 188     -22.780   3.833  18.817  1.00 79.24           C  
ANISOU 1245  CB  ARG A 188     8215  13341   8552   -477    411   2032       C  
ATOM   1246  CG  ARG A 188     -23.161   4.523  20.126  1.00 89.71           C  
ANISOU 1246  CG  ARG A 188     9565  14392  10131   -431    342   2063       C  
ATOM   1247  CD  ARG A 188     -22.928   3.644  21.341  1.00101.84           C  
ANISOU 1247  CD  ARG A 188    11179  15733  11782   -449    289   1808       C  
ATOM   1248  NE  ARG A 188     -23.813   2.476  21.360  1.00112.53           N  
ANISOU 1248  NE  ARG A 188    12583  17209  12965   -482    226   1636       N  
ATOM   1249  CZ  ARG A 188     -23.714   1.468  22.222  1.00127.28           C  
ANISOU 1249  CZ  ARG A 188    14530  18952  14880   -502    190   1414       C  
ATOM   1250  NH1 ARG A 188     -24.562   0.451  22.160  1.00115.42           N  
ANISOU 1250  NH1 ARG A 188    13074  17556  13226   -550    145   1273       N  
ATOM   1251  NH2 ARG A 188     -22.764   1.467  23.148  1.00114.86           N  
ANISOU 1251  NH2 ARG A 188    12986  17153  13504   -482    196   1339       N  
ATOM   1252  N   PHE A 189     -22.017   4.639  15.459  1.00 83.99           N  
ANISOU 1252  N   PHE A 189     8689  14547   8678   -500    641   2443       N  
ATOM   1253  CA  PHE A 189     -21.482   4.127  14.203  1.00 85.50           C  
ANISOU 1253  CA  PHE A 189     8882  15004   8602   -539    751   2421       C  
ATOM   1254  C   PHE A 189     -20.021   3.766  14.390  1.00 89.44           C  
ANISOU 1254  C   PHE A 189     9375  15362   9246   -543    885   2297       C  
ATOM   1255  O   PHE A 189     -19.163   4.646  14.474  1.00 88.88           O  
ANISOU 1255  O   PHE A 189     9231  15166   9374   -525    970   2465       O  
ATOM   1256  CB  PHE A 189     -21.686   5.127  13.051  1.00 89.60           C  
ANISOU 1256  CB  PHE A 189     9335  15750   8957   -517    802   2749       C  
ATOM   1257  CG  PHE A 189     -23.129   5.479  12.782  1.00 91.48           C  
ANISOU 1257  CG  PHE A 189     9550  16169   9040   -496    665   2904       C  
ATOM   1258  CD1 PHE A 189     -23.988   4.560  12.189  1.00 95.45           C  
ANISOU 1258  CD1 PHE A 189    10084  16963   9218   -561    574   2769       C  
ATOM   1259  CD2 PHE A 189     -23.628   6.733  13.108  1.00 93.51           C  
ANISOU 1259  CD2 PHE A 189     9747  16305   9479   -413    630   3190       C  
ATOM   1260  CE1 PHE A 189     -25.327   4.883  11.947  1.00 97.36           C  
ANISOU 1260  CE1 PHE A 189    10269  17401   9322   -546    433   2928       C  
ATOM   1261  CE2 PHE A 189     -24.967   7.056  12.863  1.00 97.46           C  
ANISOU 1261  CE2 PHE A 189    10198  16984   9849   -370    509   3356       C  
ATOM   1262  CZ  PHE A 189     -25.809   6.126  12.292  1.00 96.39           C  
ANISOU 1262  CZ  PHE A 189    10066  17166   9394   -438    402   3231       C  
ATOM   1263  N   TYR A 190     -19.760   2.457  14.509  1.00 86.77           N  
ANISOU 1263  N   TYR A 190     9108  15032   8829   -568    904   2003       N  
ATOM   1264  CA  TYR A 190     -18.434   1.881  14.727  1.00 87.11           C  
ANISOU 1264  CA  TYR A 190     9138  14955   9003   -550   1030   1858       C  
ATOM   1265  C   TYR A 190     -17.680   1.591  13.410  1.00 94.29           C  
ANISOU 1265  C   TYR A 190    10036  16103   9688   -554   1220   1871       C  
ATOM   1266  O   TYR A 190     -18.325   1.330  12.393  1.00 95.37           O  
ANISOU 1266  O   TYR A 190    10231  16510   9497   -590   1229   1870       O  
ATOM   1267  CB  TYR A 190     -18.550   0.604  15.572  1.00 86.86           C  
ANISOU 1267  CB  TYR A 190     9200  14783   9020   -551    970   1551       C  
ATOM   1268  CG  TYR A 190     -19.104   0.820  16.963  1.00 87.07           C  
ANISOU 1268  CG  TYR A 190     9243  14563   9278   -542    810   1525       C  
ATOM   1269  CD1 TYR A 190     -20.314   0.251  17.348  1.00 88.35           C  
ANISOU 1269  CD1 TYR A 190     9490  14735   9344   -573    683   1403       C  
ATOM   1270  CD2 TYR A 190     -18.409   1.576  17.905  1.00 87.13           C  
ANISOU 1270  CD2 TYR A 190     9181  14334   9591   -513    791   1614       C  
ATOM   1271  CE1 TYR A 190     -20.829   0.441  18.629  1.00 87.48           C  
ANISOU 1271  CE1 TYR A 190     9399  14408   9431   -558    558   1382       C  
ATOM   1272  CE2 TYR A 190     -18.922   1.786  19.184  1.00 86.33           C  
ANISOU 1272  CE2 TYR A 190     9114  14015   9672   -506    653   1579       C  
ATOM   1273  CZ  TYR A 190     -20.129   1.207  19.545  1.00 93.91           C  
ANISOU 1273  CZ  TYR A 190    10164  14991  10528   -519    547   1465       C  
ATOM   1274  OH  TYR A 190     -20.634   1.389  20.809  1.00 94.80           O  
ANISOU 1274  OH  TYR A 190    10316  14899  10807   -505    433   1430       O  
ATOM   1275  N   PRO A 191     -16.321   1.611  13.419  1.00 92.01           N  
ANISOU 1275  N   PRO A 191     9666  15733   9560   -519   1373   1879       N  
ATOM   1276  CA  PRO A 191     -15.556   1.358  12.179  1.00 94.74           C  
ANISOU 1276  CA  PRO A 191     9995  16305   9699   -509   1586   1899       C  
ATOM   1277  C   PRO A 191     -15.926   0.099  11.386  1.00100.47           C  
ANISOU 1277  C   PRO A 191    10864  17232  10080   -525   1647   1649       C  
ATOM   1278  O   PRO A 191     -15.987   0.164  10.156  1.00102.39           O  
ANISOU 1278  O   PRO A 191    11137  17751  10017   -548   1754   1716       O  
ATOM   1279  CB  PRO A 191     -14.107   1.324  12.663  1.00 96.45           C  
ANISOU 1279  CB  PRO A 191    10090  16353  10205   -460   1713   1886       C  
ATOM   1280  CG  PRO A 191     -14.107   2.167  13.874  1.00 98.70           C  
ANISOU 1280  CG  PRO A 191    10300  16376  10826   -475   1564   1995       C  
ATOM   1281  CD  PRO A 191     -15.414   1.924  14.542  1.00 92.21           C  
ANISOU 1281  CD  PRO A 191     9597  15479   9959   -493   1360   1889       C  
ATOM   1282  N   ASN A 192     -16.171  -1.034  12.083  1.00 95.78           N  
ANISOU 1282  N   ASN A 192    10370  16494   9527   -520   1583   1362       N  
ATOM   1283  CA  ASN A 192     -16.570  -2.311  11.476  1.00 96.80           C  
ANISOU 1283  CA  ASN A 192    10664  16752   9362   -555   1633   1083       C  
ATOM   1284  C   ASN A 192     -17.311  -3.224  12.466  1.00 98.33           C  
ANISOU 1284  C   ASN A 192    10967  16755   9640   -582   1481    845       C  
ATOM   1285  O   ASN A 192     -17.609  -2.793  13.584  1.00 95.51           O  
ANISOU 1285  O   ASN A 192    10555  16197   9536   -570   1328    916       O  
ATOM   1286  CB  ASN A 192     -15.389  -3.018  10.788  1.00100.59           C  
ANISOU 1286  CB  ASN A 192    11162  17285   9771   -489   1896    956       C  
ATOM   1287  CG  ASN A 192     -14.292  -3.424  11.720  1.00126.38           C  
ANISOU 1287  CG  ASN A 192    14351  20283  13384   -382   1972    878       C  
ATOM   1288  OD1 ASN A 192     -14.335  -4.494  12.329  1.00122.35           O  
ANISOU 1288  OD1 ASN A 192    13938  19603  12945   -351   1957    637       O  
ATOM   1289  ND2 ASN A 192     -13.276  -2.585  11.838  1.00119.55           N  
ANISOU 1289  ND2 ASN A 192    13302  19379  12740   -329   2056   1093       N  
ATOM   1290  N   ASP A 193     -17.637  -4.468  12.037  1.00 96.04           N  
ANISOU 1290  N   ASP A 193    10842  16523   9126   -629   1530    563       N  
ATOM   1291  CA  ASP A 193     -18.370  -5.476  12.815  1.00 94.51           C  
ANISOU 1291  CA  ASP A 193    10775  16162   8973   -676   1415    322       C  
ATOM   1292  C   ASP A 193     -17.729  -5.806  14.172  1.00 95.16           C  
ANISOU 1292  C   ASP A 193    10824  15906   9428   -575   1402    267       C  
ATOM   1293  O   ASP A 193     -18.448  -5.908  15.171  1.00 91.87           O  
ANISOU 1293  O   ASP A 193    10430  15334   9144   -605   1236    237       O  
ATOM   1294  CB  ASP A 193     -18.583  -6.761  11.991  1.00 98.88           C  
ANISOU 1294  CB  ASP A 193    11524  16816   9229   -748   1522     20       C  
ATOM   1295  CG  ASP A 193     -19.372  -6.564  10.709  1.00113.45           C  
ANISOU 1295  CG  ASP A 193    13424  19021  10661   -879   1493     40       C  
ATOM   1296  OD1 ASP A 193     -18.746  -6.539   9.623  1.00117.78           O  
ANISOU 1296  OD1 ASP A 193    13996  19762  10993   -860   1674     43       O  
ATOM   1297  OD2 ASP A 193     -20.620  -6.472  10.785  1.00117.32           O  
ANISOU 1297  OD2 ASP A 193    13929  19615  11031  -1001   1292     52       O  
ATOM   1298  N   LEU A 194     -16.379  -5.954  14.202  1.00 92.22           N  
ANISOU 1298  N   LEU A 194    10383  15438   9217   -454   1579    268       N  
ATOM   1299  CA  LEU A 194     -15.586  -6.277  15.397  1.00 90.28           C  
ANISOU 1299  CA  LEU A 194    10079  14910   9311   -344   1577    238       C  
ATOM   1300  C   LEU A 194     -15.864  -5.377  16.597  1.00 90.38           C  
ANISOU 1300  C   LEU A 194     9988  14775   9576   -352   1373    408       C  
ATOM   1301  O   LEU A 194     -15.942  -5.879  17.716  1.00 88.66           O  
ANISOU 1301  O   LEU A 194     9808  14341   9540   -320   1281    320       O  
ATOM   1302  CB  LEU A 194     -14.084  -6.288  15.079  1.00 91.92           C  
ANISOU 1302  CB  LEU A 194    10167  15116   9644   -217   1792    288       C  
ATOM   1303  CG  LEU A 194     -13.484  -7.647  14.750  1.00 98.57           C  
ANISOU 1303  CG  LEU A 194    11122  15892  10439   -124   2000     45       C  
ATOM   1304  CD1 LEU A 194     -13.580  -7.949  13.254  1.00101.51           C  
ANISOU 1304  CD1 LEU A 194    11606  16511  10454   -167   2186    -56       C  
ATOM   1305  CD2 LEU A 194     -12.039  -7.721  15.207  1.00101.19           C  
ANISOU 1305  CD2 LEU A 194    11285  16101  11061     40   2130    115       C  
ATOM   1306  N   TRP A 195     -16.025  -4.058  16.361  1.00 85.34           N  
ANISOU 1306  N   TRP A 195     9235  14247   8942   -392   1311    651       N  
ATOM   1307  CA  TRP A 195     -16.315  -3.055  17.391  1.00 82.56           C  
ANISOU 1307  CA  TRP A 195     8801  13757   8810   -406   1138    816       C  
ATOM   1308  C   TRP A 195     -17.691  -3.274  18.016  1.00 83.66           C  
ANISOU 1308  C   TRP A 195     9049  13841   8897   -469    960    740       C  
ATOM   1309  O   TRP A 195     -17.863  -3.031  19.208  1.00 81.27           O  
ANISOU 1309  O   TRP A 195     8735  13344   8799   -455    836    760       O  
ATOM   1310  CB  TRP A 195     -16.223  -1.644  16.813  1.00 82.13           C  
ANISOU 1310  CB  TRP A 195     8627  13829   8750   -435   1149   1089       C  
ATOM   1311  CG  TRP A 195     -14.847  -1.227  16.402  1.00 84.78           C  
ANISOU 1311  CG  TRP A 195     8821  14191   9199   -389   1311   1207       C  
ATOM   1312  CD1 TRP A 195     -14.157  -1.644  15.302  1.00 89.93           C  
ANISOU 1312  CD1 TRP A 195     9459  15016   9693   -358   1516   1179       C  
ATOM   1313  CD2 TRP A 195     -14.017  -0.257  17.054  1.00 84.28           C  
ANISOU 1313  CD2 TRP A 195     8606  13990   9428   -383   1289   1380       C  
ATOM   1314  NE1 TRP A 195     -12.930  -1.027  15.250  1.00 90.59           N  
ANISOU 1314  NE1 TRP A 195     9371  15081   9968   -323   1629   1334       N  
ATOM   1315  CE2 TRP A 195     -12.820  -0.162  16.308  1.00 90.45           C  
ANISOU 1315  CE2 TRP A 195     9263  14875  10230   -350   1484   1460       C  
ATOM   1316  CE3 TRP A 195     -14.163   0.536  18.206  1.00 83.87           C  
ANISOU 1316  CE3 TRP A 195     8515  13735   9616   -411   1128   1465       C  
ATOM   1317  CZ2 TRP A 195     -11.774   0.695  16.674  1.00 90.13           C  
ANISOU 1317  CZ2 TRP A 195     9041  14748  10456   -362   1510   1629       C  
ATOM   1318  CZ3 TRP A 195     -13.128   1.385  18.567  1.00 85.83           C  
ANISOU 1318  CZ3 TRP A 195     8609  13889  10113   -428   1148   1613       C  
ATOM   1319  CH2 TRP A 195     -11.949   1.457  17.808  1.00 88.55           C  
ANISOU 1319  CH2 TRP A 195     8812  14345  10487   -411   1331   1698       C  
ATOM   1320  N   VAL A 196     -18.662  -3.741  17.213  1.00 80.54           N  
ANISOU 1320  N   VAL A 196     8754  13628   8220   -546    951    652       N  
ATOM   1321  CA  VAL A 196     -20.022  -4.043  17.675  1.00 78.69           C  
ANISOU 1321  CA  VAL A 196     8603  13381   7915   -622    794    577       C  
ATOM   1322  C   VAL A 196     -19.975  -5.326  18.527  1.00 80.43           C  
ANISOU 1322  C   VAL A 196     8941  13389   8231   -608    791    336       C  
ATOM   1323  O   VAL A 196     -20.607  -5.378  19.576  1.00 77.78           O  
ANISOU 1323  O   VAL A 196     8631  12904   8017   -620    666    321       O  
ATOM   1324  CB  VAL A 196     -21.040  -4.142  16.501  1.00 83.79           C  
ANISOU 1324  CB  VAL A 196     9295  14320   8221   -729    771    567       C  
ATOM   1325  CG1 VAL A 196     -22.477  -4.099  17.010  1.00 82.25           C  
ANISOU 1325  CG1 VAL A 196     9116  14141   7993   -806    592    573       C  
ATOM   1326  CG2 VAL A 196     -20.808  -3.035  15.473  1.00 85.10           C  
ANISOU 1326  CG2 VAL A 196     9356  14711   8266   -718    823    809       C  
ATOM   1327  N   VAL A 197     -19.180  -6.324  18.092  1.00 78.07           N  
ANISOU 1327  N   VAL A 197     8712  13064   7886   -570    947    164       N  
ATOM   1328  CA  VAL A 197     -18.973  -7.600  18.781  1.00 77.55           C  
ANISOU 1328  CA  VAL A 197     8766  12780   7919   -533    985    -52       C  
ATOM   1329  C   VAL A 197     -18.265  -7.373  20.119  1.00 79.52           C  
ANISOU 1329  C   VAL A 197     8937  12790   8485   -424    929     29       C  
ATOM   1330  O   VAL A 197     -18.761  -7.848  21.141  1.00 78.16           O  
ANISOU 1330  O   VAL A 197     8838  12447   8413   -430    831    -40       O  
ATOM   1331  CB  VAL A 197     -18.203  -8.614  17.891  1.00 83.96           C  
ANISOU 1331  CB  VAL A 197     9668  13619   8613   -490   1199   -235       C  
ATOM   1332  CG1 VAL A 197     -17.828  -9.878  18.665  1.00 83.79           C  
ANISOU 1332  CG1 VAL A 197     9761  13331   8746   -414   1260   -422       C  
ATOM   1333  CG2 VAL A 197     -18.999  -8.967  16.640  1.00 85.63           C  
ANISOU 1333  CG2 VAL A 197     9994  14066   8475   -627   1236   -359       C  
ATOM   1334  N   VAL A 198     -17.119  -6.651  20.113  1.00 76.19           N  
ANISOU 1334  N   VAL A 198     8366  12370   8213   -336    987    177       N  
ATOM   1335  CA  VAL A 198     -16.343  -6.376  21.331  1.00 74.98           C  
ANISOU 1335  CA  VAL A 198     8119  12023   8346   -251    920    257       C  
ATOM   1336  C   VAL A 198     -17.112  -5.620  22.413  1.00 77.55           C  
ANISOU 1336  C   VAL A 198     8440  12254   8774   -300    724    351       C  
ATOM   1337  O   VAL A 198     -17.057  -6.037  23.566  1.00 76.07           O  
ANISOU 1337  O   VAL A 198     8290  11883   8729   -261    644    302       O  
ATOM   1338  CB  VAL A 198     -14.890  -5.855  21.135  1.00 79.75           C  
ANISOU 1338  CB  VAL A 198     8546  12652   9105   -166   1022    385       C  
ATOM   1339  CG1 VAL A 198     -14.045  -6.823  20.312  1.00 81.53           C  
ANISOU 1339  CG1 VAL A 198     8784  12924   9270    -76   1240    268       C  
ATOM   1340  CG2 VAL A 198     -14.859  -4.450  20.544  1.00 79.88           C  
ANISOU 1340  CG2 VAL A 198     8439  12817   9096   -229   1011    593       C  
ATOM   1341  N   PHE A 199     -17.853  -4.546  22.045  1.00 74.48           N  
ANISOU 1341  N   PHE A 199     8012  11986   8302   -376    657    487       N  
ATOM   1342  CA  PHE A 199     -18.641  -3.772  23.006  1.00 73.30           C  
ANISOU 1342  CA  PHE A 199     7865  11744   8243   -409    499    575       C  
ATOM   1343  C   PHE A 199     -19.879  -4.527  23.496  1.00 77.61           C  
ANISOU 1343  C   PHE A 199     8543  12244   8700   -456    419    448       C  
ATOM   1344  O   PHE A 199     -20.379  -4.221  24.584  1.00 76.16           O  
ANISOU 1344  O   PHE A 199     8383  11931   8622   -456    309    475       O  
ATOM   1345  CB  PHE A 199     -18.968  -2.355  22.505  1.00 75.64           C  
ANISOU 1345  CB  PHE A 199     8072  12152   8516   -447    474    782       C  
ATOM   1346  CG  PHE A 199     -17.794  -1.399  22.461  1.00 78.46           C  
ANISOU 1346  CG  PHE A 199     8296  12477   9037   -420    519    935       C  
ATOM   1347  CD1 PHE A 199     -16.959  -1.241  23.562  1.00 81.61           C  
ANISOU 1347  CD1 PHE A 199     8649  12691   9668   -390    464    934       C  
ATOM   1348  CD2 PHE A 199     -17.552  -0.621  21.335  1.00 82.38           C  
ANISOU 1348  CD2 PHE A 199     8708  13138   9454   -440    610   1091       C  
ATOM   1349  CE1 PHE A 199     -15.870  -0.357  23.517  1.00 83.48           C  
ANISOU 1349  CE1 PHE A 199     8748  12906  10065   -396    497   1071       C  
ATOM   1350  CE2 PHE A 199     -16.471   0.270  21.296  1.00 86.06           C  
ANISOU 1350  CE2 PHE A 199     9045  13567  10088   -437    661   1240       C  
ATOM   1351  CZ  PHE A 199     -15.640   0.398  22.387  1.00 83.66           C  
ANISOU 1351  CZ  PHE A 199     8687  13076  10025   -424    601   1223       C  
ATOM   1352  N   GLN A 200     -20.356  -5.530  22.710  1.00 75.46           N  
ANISOU 1352  N   GLN A 200     8362  12076   8235   -506    484    300       N  
ATOM   1353  CA  GLN A 200     -21.464  -6.403  23.106  1.00 74.91           C  
ANISOU 1353  CA  GLN A 200     8415  11961   8087   -576    424    162       C  
ATOM   1354  C   GLN A 200     -20.889  -7.451  24.050  1.00 80.02           C  
ANISOU 1354  C   GLN A 200     9149  12376   8878   -509    450     31       C  
ATOM   1355  O   GLN A 200     -21.528  -7.764  25.056  1.00 78.47           O  
ANISOU 1355  O   GLN A 200     9021  12049   8745   -526    367     -2       O  
ATOM   1356  CB  GLN A 200     -22.158  -7.058  21.904  1.00 77.44           C  
ANISOU 1356  CB  GLN A 200     8803  12476   8144   -684    475     44       C  
ATOM   1357  CG  GLN A 200     -23.247  -6.171  21.293  1.00 86.90           C  
ANISOU 1357  CG  GLN A 200     9927  13904   9187   -767    387    180       C  
ATOM   1358  CD  GLN A 200     -23.965  -6.760  20.093  1.00105.02           C  
ANISOU 1358  CD  GLN A 200    12275  16435  11193   -896    405     72       C  
ATOM   1359  OE1 GLN A 200     -25.164  -6.530  19.890  1.00 98.04           O  
ANISOU 1359  OE1 GLN A 200    11358  15708  10184   -992    300    121       O  
ATOM   1360  NE2 GLN A 200     -23.254  -7.487  19.234  1.00100.02           N  
ANISOU 1360  NE2 GLN A 200    11717  15851  10436   -904    539    -72       N  
ATOM   1361  N   PHE A 201     -19.647  -7.932  23.767  1.00 78.73           N  
ANISOU 1361  N   PHE A 201     8971  12165   8777   -418    571    -17       N  
ATOM   1362  CA  PHE A 201     -18.917  -8.875  24.626  1.00 79.05           C  
ANISOU 1362  CA  PHE A 201     9069  11991   8977   -318    605   -100       C  
ATOM   1363  C   PHE A 201     -18.383  -8.189  25.896  1.00 82.97           C  
ANISOU 1363  C   PHE A 201     9477  12362   9687   -247    489     33       C  
ATOM   1364  O   PHE A 201     -18.137  -8.865  26.897  1.00 83.08           O  
ANISOU 1364  O   PHE A 201     9548  12203   9816   -181    457     -6       O  
ATOM   1365  CB  PHE A 201     -17.801  -9.623  23.866  1.00 82.66           C  
ANISOU 1365  CB  PHE A 201     9524  12449   9434   -225    787   -186       C  
ATOM   1366  CG  PHE A 201     -18.251 -10.806  23.031  1.00 85.96           C  
ANISOU 1366  CG  PHE A 201    10108  12878   9675   -280    913   -397       C  
ATOM   1367  CD1 PHE A 201     -19.487 -11.414  23.255  1.00 88.77           C  
ANISOU 1367  CD1 PHE A 201    10610  13187   9931   -403    848   -514       C  
ATOM   1368  CD2 PHE A 201     -17.426 -11.335  22.044  1.00 90.25           C  
ANISOU 1368  CD2 PHE A 201    10668  13470  10155   -215   1107   -487       C  
ATOM   1369  CE1 PHE A 201     -19.895 -12.512  22.490  1.00 91.29           C  
ANISOU 1369  CE1 PHE A 201    11094  13504  10089   -484    960   -728       C  
ATOM   1370  CE2 PHE A 201     -17.838 -12.434  21.279  1.00 94.71           C  
ANISOU 1370  CE2 PHE A 201    11415  14026  10545   -278   1232   -710       C  
ATOM   1371  CZ  PHE A 201     -19.072 -13.007  21.503  1.00 92.49           C  
ANISOU 1371  CZ  PHE A 201    11283  13694  10166   -424   1149   -834       C  
ATOM   1372  N   GLN A 202     -18.231  -6.853  25.858  1.00 78.86           N  
ANISOU 1372  N   GLN A 202     8829  11925   9209   -267    425    192       N  
ATOM   1373  CA  GLN A 202     -17.813  -6.041  26.995  1.00 77.90           C  
ANISOU 1373  CA  GLN A 202     8636  11698   9263   -237    305    304       C  
ATOM   1374  C   GLN A 202     -19.033  -5.878  27.909  1.00 81.13           C  
ANISOU 1374  C   GLN A 202     9146  12032   9649   -292    185    296       C  
ATOM   1375  O   GLN A 202     -18.905  -5.950  29.133  1.00 79.35           O  
ANISOU 1375  O   GLN A 202     8957  11665   9530   -259     96    298       O  
ATOM   1376  CB  GLN A 202     -17.332  -4.661  26.512  1.00 79.59           C  
ANISOU 1376  CB  GLN A 202     8704  12012   9524   -264    302    463       C  
ATOM   1377  CG  GLN A 202     -16.449  -3.912  27.503  1.00 97.26           C  
ANISOU 1377  CG  GLN A 202    10847  14145  11964   -242    208    558       C  
ATOM   1378  CD  GLN A 202     -16.498  -2.426  27.261  1.00116.81           C  
ANISOU 1378  CD  GLN A 202    13239  16665  14480   -310    177    706       C  
ATOM   1379  OE1 GLN A 202     -17.424  -1.729  27.698  1.00111.92           O  
ANISOU 1379  OE1 GLN A 202    12681  16000  13842   -355     98    743       O  
ATOM   1380  NE2 GLN A 202     -15.503  -1.906  26.558  1.00108.39           N  
ANISOU 1380  NE2 GLN A 202    12029  15678  13477   -312    254    802       N  
ATOM   1381  N   HIS A 203     -20.215  -5.675  27.295  1.00 79.20           N  
ANISOU 1381  N   HIS A 203     8938  11900   9253   -374    186    292       N  
ATOM   1382  CA  HIS A 203     -21.498  -5.488  27.969  1.00 78.77           C  
ANISOU 1382  CA  HIS A 203     8953  11814   9163   -426     99    298       C  
ATOM   1383  C   HIS A 203     -21.922  -6.730  28.754  1.00 82.47           C  
ANISOU 1383  C   HIS A 203     9554  12152   9629   -428     90    168       C  
ATOM   1384  O   HIS A 203     -22.376  -6.585  29.887  1.00 81.36           O  
ANISOU 1384  O   HIS A 203     9463  11902   9547   -421     13    188       O  
ATOM   1385  CB  HIS A 203     -22.569  -5.041  26.962  1.00 80.33           C  
ANISOU 1385  CB  HIS A 203     9119  12204   9200   -506    108    344       C  
ATOM   1386  CG  HIS A 203     -23.869  -4.600  27.562  1.00 83.51           C  
ANISOU 1386  CG  HIS A 203     9541  12605   9585   -543     29    394       C  
ATOM   1387  ND1 HIS A 203     -24.995  -4.420  26.773  1.00 86.10           N  
ANISOU 1387  ND1 HIS A 203     9832  13118   9765   -613     21    433       N  
ATOM   1388  CD2 HIS A 203     -24.191  -4.316  28.848  1.00 84.72           C  
ANISOU 1388  CD2 HIS A 203     9739  12609   9843   -513    -36    415       C  
ATOM   1389  CE1 HIS A 203     -25.956  -4.049  27.601  1.00 85.10           C  
ANISOU 1389  CE1 HIS A 203     9713  12942   9678   -613    -38    483       C  
ATOM   1390  NE2 HIS A 203     -25.524  -3.993  28.862  1.00 84.57           N  
ANISOU 1390  NE2 HIS A 203     9709  12669   9755   -554    -65    465       N  
ATOM   1391  N   ILE A 204     -21.742  -7.941  28.180  1.00 79.80           N  
ANISOU 1391  N   ILE A 204     9285  11810   9226   -435    181     36       N  
ATOM   1392  CA  ILE A 204     -22.054  -9.209  28.860  1.00 79.61           C  
ANISOU 1392  CA  ILE A 204     9401  11631   9217   -437    197    -83       C  
ATOM   1393  C   ILE A 204     -21.079  -9.393  30.043  1.00 83.03           C  
ANISOU 1393  C   ILE A 204     9843  11887   9818   -316    160    -43       C  
ATOM   1394  O   ILE A 204     -21.510  -9.734  31.139  1.00 81.58           O  
ANISOU 1394  O   ILE A 204     9744  11578   9673   -310    103    -44       O  
ATOM   1395  CB  ILE A 204     -22.014 -10.426  27.878  1.00 84.31           C  
ANISOU 1395  CB  ILE A 204    10085  12240   9711   -475    325   -245       C  
ATOM   1396  CG1 ILE A 204     -22.895 -10.227  26.611  1.00 85.84           C  
ANISOU 1396  CG1 ILE A 204    10260  12652   9701   -611    344   -288       C  
ATOM   1397  CG2 ILE A 204     -22.283 -11.771  28.580  1.00 84.94           C  
ANISOU 1397  CG2 ILE A 204    10325  12118   9831   -477    360   -362       C  
ATOM   1398  CD1 ILE A 204     -24.421 -10.451  26.731  1.00 94.30           C  
ANISOU 1398  CD1 ILE A 204    11383  13779  10669   -758    278   -328       C  
ATOM   1399  N   MET A 205     -19.777  -9.138  29.817  1.00 80.74           N  
ANISOU 1399  N   MET A 205     9451  11606   9620   -223    189      6       N  
ATOM   1400  CA  MET A 205     -18.736  -9.296  30.832  1.00 80.98           C  
ANISOU 1400  CA  MET A 205     9452  11511   9805   -109    139     59       C  
ATOM   1401  C   MET A 205     -18.870  -8.321  32.007  1.00 83.13           C  
ANISOU 1401  C   MET A 205     9700  11747  10138   -123    -13    158       C  
ATOM   1402  O   MET A 205     -19.118  -8.767  33.125  1.00 82.36           O  
ANISOU 1402  O   MET A 205     9699  11532  10063    -98    -76    153       O  
ATOM   1403  CB  MET A 205     -17.335  -9.246  30.198  1.00 84.80           C  
ANISOU 1403  CB  MET A 205     9798  12046  10375    -17    215     95       C  
ATOM   1404  CG  MET A 205     -16.295 -10.049  30.958  1.00 89.96           C  
ANISOU 1404  CG  MET A 205    10438  12575  11169    124    216    112       C  
ATOM   1405  SD  MET A 205     -16.565 -11.839  30.880  1.00 95.84           S  
ANISOU 1405  SD  MET A 205    11369  13156  11889    192    355    -28       S  
ATOM   1406  CE  MET A 205     -15.347 -12.404  32.085  1.00 93.69           C  
ANISOU 1406  CE  MET A 205    11041  12750  11806    380    300     76       C  
ATOM   1407  N   VAL A 206     -18.744  -7.004  31.746  1.00 78.72           N  
ANISOU 1407  N   VAL A 206     9032  11281   9595   -167    -59    245       N  
ATOM   1408  CA  VAL A 206     -18.815  -5.935  32.756  1.00 77.38           C  
ANISOU 1408  CA  VAL A 206     8851  11066   9483   -192   -187    322       C  
ATOM   1409  C   VAL A 206     -20.226  -5.757  33.371  1.00 79.28           C  
ANISOU 1409  C   VAL A 206     9214  11269   9641   -247   -226    303       C  
ATOM   1410  O   VAL A 206     -20.334  -5.492  34.571  1.00 78.51           O  
ANISOU 1410  O   VAL A 206     9180  11080   9571   -238   -315    317       O  
ATOM   1411  CB  VAL A 206     -18.202  -4.597  32.237  1.00 81.39           C  
ANISOU 1411  CB  VAL A 206     9216  11652  10055   -228   -201    419       C  
ATOM   1412  CG1 VAL A 206     -18.141  -3.537  33.336  1.00 80.81           C  
ANISOU 1412  CG1 VAL A 206     9153  11498  10054   -263   -327    471       C  
ATOM   1413  CG2 VAL A 206     -16.810  -4.819  31.649  1.00 82.35           C  
ANISOU 1413  CG2 VAL A 206     9196  11826  10266   -175   -147    448       C  
ATOM   1414  N   GLY A 207     -21.271  -5.919  32.562  1.00 74.89           N  
ANISOU 1414  N   GLY A 207     8682  10796   8976   -303   -159    272       N  
ATOM   1415  CA  GLY A 207     -22.650  -5.753  33.010  1.00 74.11           C  
ANISOU 1415  CA  GLY A 207     8659  10692   8805   -353   -179    270       C  
ATOM   1416  C   GLY A 207     -23.347  -6.961  33.612  1.00 78.26           C  
ANISOU 1416  C   GLY A 207     9313  11139   9285   -366   -161    189       C  
ATOM   1417  O   GLY A 207     -24.228  -6.789  34.460  1.00 77.62           O  
ANISOU 1417  O   GLY A 207     9296  11014   9181   -385   -191    204       O  
ATOM   1418  N   LEU A 208     -22.996  -8.192  33.170  1.00 74.95           N  
ANISOU 1418  N   LEU A 208     8936  10691   8851   -359    -94    103       N  
ATOM   1419  CA  LEU A 208     -23.656  -9.418  33.648  1.00 74.52           C  
ANISOU 1419  CA  LEU A 208     9014  10537   8763   -387    -58     25       C  
ATOM   1420  C   LEU A 208     -22.770 -10.456  34.380  1.00 77.81           C  
ANISOU 1420  C   LEU A 208     9516  10787   9261   -292    -45      2       C  
ATOM   1421  O   LEU A 208     -23.117 -10.848  35.495  1.00 77.08           O  
ANISOU 1421  O   LEU A 208     9524  10585   9180   -276    -77     22       O  
ATOM   1422  CB  LEU A 208     -24.489 -10.058  32.510  1.00 75.14           C  
ANISOU 1422  CB  LEU A 208     9108  10709   8732   -499     22    -68       C  
ATOM   1423  CG  LEU A 208     -24.967 -11.507  32.676  1.00 80.69           C  
ANISOU 1423  CG  LEU A 208     9952  11293   9413   -554     91   -178       C  
ATOM   1424  CD1 LEU A 208     -26.216 -11.589  33.533  1.00 80.53           C  
ANISOU 1424  CD1 LEU A 208     9986  11243   9366   -630     62   -154       C  
ATOM   1425  CD2 LEU A 208     -25.239 -12.132  31.338  1.00 84.28           C  
ANISOU 1425  CD2 LEU A 208    10417  11837   9767   -656    173   -301       C  
ATOM   1426  N   ILE A 209     -21.675 -10.931  33.736  1.00 74.54           N  
ANISOU 1426  N   ILE A 209     9061  10361   8900   -219     14    -27       N  
ATOM   1427  CA  ILE A 209     -20.772 -11.974  34.256  1.00 74.81           C  
ANISOU 1427  CA  ILE A 209     9154  10244   9026   -101     46    -33       C  
ATOM   1428  C   ILE A 209     -19.957 -11.535  35.481  1.00 78.14           C  
ANISOU 1428  C   ILE A 209     9536  10619   9536     -1    -77     82       C  
ATOM   1429  O   ILE A 209     -20.054 -12.181  36.525  1.00 77.75           O  
ANISOU 1429  O   ILE A 209     9592  10447   9502     45   -107    111       O  
ATOM   1430  CB  ILE A 209     -19.930 -12.660  33.121  1.00 78.90           C  
ANISOU 1430  CB  ILE A 209     9640  10764   9573    -41    178   -106       C  
ATOM   1431  CG1 ILE A 209     -20.851 -13.331  32.072  1.00 79.62           C  
ANISOU 1431  CG1 ILE A 209     9826  10879   9547   -163    294   -251       C  
ATOM   1432  CG2 ILE A 209     -18.914 -13.667  33.684  1.00 80.77           C  
ANISOU 1432  CG2 ILE A 209     9914  10840   9933    120    221    -81       C  
ATOM   1433  CD1 ILE A 209     -20.151 -13.905  30.845  1.00 88.50           C  
ANISOU 1433  CD1 ILE A 209    10943  12024  10658   -124    442   -351       C  
ATOM   1434  N   LEU A 210     -19.161 -10.453  35.351  1.00 74.82           N  
ANISOU 1434  N   LEU A 210     8966  10299   9164     18   -149    149       N  
ATOM   1435  CA  LEU A 210     -18.321  -9.915  36.432  1.00 75.07           C  
ANISOU 1435  CA  LEU A 210     8939  10315   9267     79   -287    245       C  
ATOM   1436  C   LEU A 210     -19.097  -9.520  37.712  1.00 78.50           C  
ANISOU 1436  C   LEU A 210     9486  10702   9637     34   -393    271       C  
ATOM   1437  O   LEU A 210     -18.676  -9.968  38.782  1.00 79.24           O  
ANISOU 1437  O   LEU A 210     9634  10726   9749    105   -468    321       O  
ATOM   1438  CB  LEU A 210     -17.366  -8.800  35.954  1.00 75.36           C  
ANISOU 1438  CB  LEU A 210     8790  10466   9375     71   -335    301       C  
ATOM   1439  CG  LEU A 210     -16.340  -9.191  34.878  1.00 81.60           C  
ANISOU 1439  CG  LEU A 210     9450  11312  10244    143   -229    301       C  
ATOM   1440  CD1 LEU A 210     -15.832  -7.971  34.136  1.00 81.81           C  
ANISOU 1440  CD1 LEU A 210     9311  11468  10306     84   -237    350       C  
ATOM   1441  CD2 LEU A 210     -15.187  -9.988  35.461  1.00 86.37           C  
ANISOU 1441  CD2 LEU A 210     9998  11859  10960    288   -252    359       C  
ATOM   1442  N   PRO A 211     -20.225  -8.750  37.672  1.00 73.15           N  
ANISOU 1442  N   PRO A 211     8851  10064   8880    -67   -392    248       N  
ATOM   1443  CA  PRO A 211     -20.958  -8.493  38.926  1.00 71.99           C  
ANISOU 1443  CA  PRO A 211     8824   9862   8667    -90   -460    266       C  
ATOM   1444  C   PRO A 211     -21.751  -9.730  39.377  1.00 75.31           C  
ANISOU 1444  C   PRO A 211     9392  10188   9034    -83   -391    241       C  
ATOM   1445  O   PRO A 211     -21.934  -9.932  40.580  1.00 75.65           O  
ANISOU 1445  O   PRO A 211     9543  10165   9035    -57   -443    278       O  
ATOM   1446  CB  PRO A 211     -21.861  -7.296  38.601  1.00 72.77           C  
ANISOU 1446  CB  PRO A 211     8898  10030   8721   -175   -449    259       C  
ATOM   1447  CG  PRO A 211     -21.763  -7.091  37.132  1.00 77.52           C  
ANISOU 1447  CG  PRO A 211     9380  10729   9346   -206   -377    245       C  
ATOM   1448  CD  PRO A 211     -20.921  -8.151  36.514  1.00 74.00           C  
ANISOU 1448  CD  PRO A 211     8900  10272   8944   -150   -321    217       C  
ATOM   1449  N   GLY A 212     -22.156 -10.569  38.415  1.00 70.70           N  
ANISOU 1449  N   GLY A 212     8819   9597   8448   -113   -274    179       N  
ATOM   1450  CA  GLY A 212     -22.863 -11.824  38.663  1.00 70.57           C  
ANISOU 1450  CA  GLY A 212     8940   9470   8403   -132   -189    145       C  
ATOM   1451  C   GLY A 212     -22.064 -12.775  39.533  1.00 73.99           C  
ANISOU 1451  C   GLY A 212     9454   9768   8890    -14   -207    201       C  
ATOM   1452  O   GLY A 212     -22.625 -13.385  40.449  1.00 73.26           O  
ANISOU 1452  O   GLY A 212     9496   9580   8761    -15   -195    234       O  
ATOM   1453  N   ILE A 213     -20.726 -12.862  39.276  1.00 70.52           N  
ANISOU 1453  N   ILE A 213     8919   9332   8542     97   -235    233       N  
ATOM   1454  CA  ILE A 213     -19.760 -13.663  40.046  1.00 71.06           C  
ANISOU 1454  CA  ILE A 213     9017   9301   8680    244   -269    320       C  
ATOM   1455  C   ILE A 213     -19.642 -13.056  41.454  1.00 71.57           C  
ANISOU 1455  C   ILE A 213     9110   9395   8687    263   -428    417       C  
ATOM   1456  O   ILE A 213     -19.840 -13.768  42.436  1.00 71.09           O  
ANISOU 1456  O   ILE A 213     9180   9240   8592    312   -438    483       O  
ATOM   1457  CB  ILE A 213     -18.376 -13.770  39.326  1.00 75.49           C  
ANISOU 1457  CB  ILE A 213     9425   9897   9362    359   -254    339       C  
ATOM   1458  CG1 ILE A 213     -18.476 -14.645  38.062  1.00 77.04           C  
ANISOU 1458  CG1 ILE A 213     9647  10029   9594    361    -68    231       C  
ATOM   1459  CG2 ILE A 213     -17.284 -14.314  40.269  1.00 77.91           C  
ANISOU 1459  CG2 ILE A 213     9708  10150   9746    526   -334    472       C  
ATOM   1460  CD1 ILE A 213     -17.331 -14.432  37.035  1.00 89.46           C  
ANISOU 1460  CD1 ILE A 213    11048  11687  11255    439    -18    221       C  
ATOM   1461  N   VAL A 214     -19.351 -11.737  41.531  1.00 66.26           N  
ANISOU 1461  N   VAL A 214     8331   8848   7997    214   -542    420       N  
ATOM   1462  CA  VAL A 214     -19.220 -10.942  42.758  1.00 66.16           C  
ANISOU 1462  CA  VAL A 214     8348   8878   7911    201   -697    474       C  
ATOM   1463  C   VAL A 214     -20.436 -11.156  43.683  1.00 71.06           C  
ANISOU 1463  C   VAL A 214     9157   9437   8405    156   -668    473       C  
ATOM   1464  O   VAL A 214     -20.249 -11.395  44.880  1.00 71.82           O  
ANISOU 1464  O   VAL A 214     9346   9510   8431    205   -752    546       O  
ATOM   1465  CB  VAL A 214     -18.970  -9.442  42.418  1.00 68.88           C  
ANISOU 1465  CB  VAL A 214     8571   9333   8267    117   -775    440       C  
ATOM   1466  CG1 VAL A 214     -19.205  -8.526  43.616  1.00 68.66           C  
ANISOU 1466  CG1 VAL A 214     8628   9324   8136     63   -899    445       C  
ATOM   1467  CG2 VAL A 214     -17.570  -9.233  41.859  1.00 69.43           C  
ANISOU 1467  CG2 VAL A 214     8448   9473   8460    166   -832    478       C  
ATOM   1468  N   ILE A 215     -21.668 -11.110  43.114  1.00 66.76           N  
ANISOU 1468  N   ILE A 215     8657   8882   7826     64   -546    401       N  
ATOM   1469  CA  ILE A 215     -22.923 -11.310  43.851  1.00 66.26           C  
ANISOU 1469  CA  ILE A 215     8743   8775   7659     11   -487    402       C  
ATOM   1470  C   ILE A 215     -23.057 -12.756  44.346  1.00 71.82           C  
ANISOU 1470  C   ILE A 215     9576   9351   8362     63   -419    458       C  
ATOM   1471  O   ILE A 215     -23.159 -12.961  45.555  1.00 71.47           O  
ANISOU 1471  O   ILE A 215     9651   9272   8233     99   -461    534       O  
ATOM   1472  CB  ILE A 215     -24.179 -10.783  43.080  1.00 67.90           C  
ANISOU 1472  CB  ILE A 215     8919   9038   7843   -102   -388    330       C  
ATOM   1473  CG1 ILE A 215     -24.114  -9.247  42.910  1.00 67.55           C  
ANISOU 1473  CG1 ILE A 215     8784   9091   7792   -132   -454    309       C  
ATOM   1474  CG2 ILE A 215     -25.484 -11.191  43.788  1.00 68.02           C  
ANISOU 1474  CG2 ILE A 215     9063   9011   7772   -153   -302    344       C  
ATOM   1475  CD1 ILE A 215     -24.870  -8.656  41.714  1.00 72.15           C  
ANISOU 1475  CD1 ILE A 215     9262   9757   8396   -207   -378    265       C  
ATOM   1476  N   LEU A 216     -23.043 -13.748  43.418  1.00 70.68           N  
ANISOU 1476  N   LEU A 216     9421   9128   8305     64   -307    420       N  
ATOM   1477  CA  LEU A 216     -23.173 -15.176  43.743  1.00 72.70           C  
ANISOU 1477  CA  LEU A 216     9812   9221   8591    106   -214    465       C  
ATOM   1478  C   LEU A 216     -22.196 -15.617  44.813  1.00 79.15           C  
ANISOU 1478  C   LEU A 216    10679   9982   9411    257   -305    603       C  
ATOM   1479  O   LEU A 216     -22.614 -16.268  45.772  1.00 80.68           O  
ANISOU 1479  O   LEU A 216    11021  10087   9547    277   -279    690       O  
ATOM   1480  CB  LEU A 216     -23.066 -16.088  42.504  1.00 73.50           C  
ANISOU 1480  CB  LEU A 216     9898   9234   8796     93    -83    379       C  
ATOM   1481  CG  LEU A 216     -24.304 -16.183  41.599  1.00 78.16           C  
ANISOU 1481  CG  LEU A 216    10497   9843   9357    -81     29    256       C  
ATOM   1482  CD1 LEU A 216     -23.985 -16.949  40.320  1.00 79.29           C  
ANISOU 1482  CD1 LEU A 216    10626   9920   9579    -95    138    146       C  
ATOM   1483  CD2 LEU A 216     -25.495 -16.823  42.324  1.00 80.63           C  
ANISOU 1483  CD2 LEU A 216    10954  10063   9619   -174    106    285       C  
ATOM   1484  N   SER A 217     -20.915 -15.209  44.682  1.00 75.42           N  
ANISOU 1484  N   SER A 217    10073   9583   8999    358   -419    638       N  
ATOM   1485  CA  SER A 217     -19.859 -15.525  45.642  1.00 76.39           C  
ANISOU 1485  CA  SER A 217    10196   9703   9127    506   -540    784       C  
ATOM   1486  C   SER A 217     -20.252 -15.121  47.074  1.00 80.02           C  
ANISOU 1486  C   SER A 217    10773  10212   9419    484   -648    861       C  
ATOM   1487  O   SER A 217     -20.200 -15.968  47.967  1.00 80.94           O  
ANISOU 1487  O   SER A 217    11012  10248   9494    570   -649    989       O  
ATOM   1488  CB  SER A 217     -18.533 -14.896  45.220  1.00 79.33           C  
ANISOU 1488  CB  SER A 217    10362  10195   9585    574   -658    797       C  
ATOM   1489  OG  SER A 217     -18.141 -15.385  43.946  1.00 86.01           O  
ANISOU 1489  OG  SER A 217    11117  10991  10573    615   -532    736       O  
ATOM   1490  N   CYS A 218     -20.726 -13.865  47.265  1.00 75.06           N  
ANISOU 1490  N   CYS A 218    10128   9702   8689    372   -715    783       N  
ATOM   1491  CA  CYS A 218     -21.176 -13.339  48.556  1.00 75.28           C  
ANISOU 1491  CA  CYS A 218    10282   9782   8537    338   -795    818       C  
ATOM   1492  C   CYS A 218     -22.294 -14.203  49.130  1.00 80.51           C  
ANISOU 1492  C   CYS A 218    11131  10338   9123    321   -656    867       C  
ATOM   1493  O   CYS A 218     -22.097 -14.833  50.167  1.00 81.51           O  
ANISOU 1493  O   CYS A 218    11375  10431   9165    398   -694    997       O  
ATOM   1494  CB  CYS A 218     -21.609 -11.879  48.439  1.00 74.30           C  
ANISOU 1494  CB  CYS A 218    10118   9761   8352    224   -834    700       C  
ATOM   1495  SG  CYS A 218     -20.266 -10.727  48.058  1.00 78.11           S  
ANISOU 1495  SG  CYS A 218    10406  10366   8906    216  -1015    662       S  
ATOM   1496  N   TYR A 219     -23.442 -14.278  48.428  1.00 76.79           N  
ANISOU 1496  N   TYR A 219    10673   9819   8683    216   -496    777       N  
ATOM   1497  CA  TYR A 219     -24.600 -15.055  48.870  1.00 77.31           C  
ANISOU 1497  CA  TYR A 219    10889   9790   8696    165   -348    815       C  
ATOM   1498  C   TYR A 219     -24.349 -16.515  49.109  1.00 83.32           C  
ANISOU 1498  C   TYR A 219    11752  10390   9517    244   -278    931       C  
ATOM   1499  O   TYR A 219     -24.892 -17.051  50.068  1.00 84.19           O  
ANISOU 1499  O   TYR A 219    12014  10440   9534    247   -223   1033       O  
ATOM   1500  CB  TYR A 219     -25.825 -14.811  48.003  1.00 77.27           C  
ANISOU 1500  CB  TYR A 219    10837   9797   8724     25   -212    701       C  
ATOM   1501  CG  TYR A 219     -26.363 -13.414  48.201  1.00 78.24           C  
ANISOU 1501  CG  TYR A 219    10917  10055   8755    -32   -249    637       C  
ATOM   1502  CD1 TYR A 219     -26.023 -12.386  47.328  1.00 78.73           C  
ANISOU 1502  CD1 TYR A 219    10830  10209   8875    -54   -311    546       C  
ATOM   1503  CD2 TYR A 219     -27.144 -13.097  49.310  1.00 79.70           C  
ANISOU 1503  CD2 TYR A 219    11222  10266   8792    -48   -213    676       C  
ATOM   1504  CE1 TYR A 219     -26.493 -11.090  47.520  1.00 78.19           C  
ANISOU 1504  CE1 TYR A 219    10737  10232   8740    -91   -330    495       C  
ATOM   1505  CE2 TYR A 219     -27.614 -11.801  49.516  1.00 79.98           C  
ANISOU 1505  CE2 TYR A 219    11235  10402   8752    -79   -225    611       C  
ATOM   1506  CZ  TYR A 219     -27.290 -10.803  48.613  1.00 85.20           C  
ANISOU 1506  CZ  TYR A 219    11752  11130   9492    -99   -284    521       C  
ATOM   1507  OH  TYR A 219     -27.738  -9.526  48.807  1.00 86.07           O  
ANISOU 1507  OH  TYR A 219    11852  11305   9546   -118   -281    464       O  
ATOM   1508  N   CYS A 220     -23.474 -17.140  48.304  1.00 80.72           N  
ANISOU 1508  N   CYS A 220    11346   9983   9341    322   -273    928       N  
ATOM   1509  CA  CYS A 220     -23.095 -18.537  48.488  1.00 82.99           C  
ANISOU 1509  CA  CYS A 220    11733  10085   9715    429   -196   1045       C  
ATOM   1510  C   CYS A 220     -22.342 -18.720  49.817  1.00 85.61           C  
ANISOU 1510  C   CYS A 220    12134  10442   9952    577   -326   1240       C  
ATOM   1511  O   CYS A 220     -22.503 -19.754  50.457  1.00 87.06           O  
ANISOU 1511  O   CYS A 220    12465  10483  10130    640   -250   1381       O  
ATOM   1512  CB  CYS A 220     -22.278 -19.043  47.306  1.00 84.82           C  
ANISOU 1512  CB  CYS A 220    11862  10237  10129    498   -148    984       C  
ATOM   1513  SG  CYS A 220     -22.026 -20.833  47.298  1.00 92.02           S  
ANISOU 1513  SG  CYS A 220    12921  10856  11185    616     15   1090       S  
ATOM   1514  N   ILE A 221     -21.556 -17.703  50.240  1.00 79.26           N  
ANISOU 1514  N   ILE A 221    11227   9824   9064    619   -525   1251       N  
ATOM   1515  CA  ILE A 221     -20.817 -17.699  51.504  1.00 79.79           C  
ANISOU 1515  CA  ILE A 221    11340   9973   9003    735   -692   1422       C  
ATOM   1516  C   ILE A 221     -21.789 -17.358  52.645  1.00 82.42           C  
ANISOU 1516  C   ILE A 221    11847  10359   9109    652   -684   1449       C  
ATOM   1517  O   ILE A 221     -21.783 -18.050  53.663  1.00 83.58           O  
ANISOU 1517  O   ILE A 221    12137  10469   9153    731   -690   1622       O  
ATOM   1518  CB  ILE A 221     -19.559 -16.774  51.436  1.00 82.74           C  
ANISOU 1518  CB  ILE A 221    11523  10530   9386    782   -912   1407       C  
ATOM   1519  CG1 ILE A 221     -18.472 -17.392  50.521  1.00 83.85           C  
ANISOU 1519  CG1 ILE A 221    11499  10610   9748    916   -900   1446       C  
ATOM   1520  CG2 ILE A 221     -18.982 -16.490  52.829  1.00 84.88           C  
ANISOU 1520  CG2 ILE A 221    11844  10944   9463    841  -1120   1547       C  
ATOM   1521  CD1 ILE A 221     -17.497 -16.403  49.877  1.00 87.90           C  
ANISOU 1521  CD1 ILE A 221    11777  11283  10338    903  -1037   1366       C  
ATOM   1522  N   ILE A 222     -22.634 -16.315  52.461  1.00 76.64           N  
ANISOU 1522  N   ILE A 222    11107   9711   8303    506   -654   1289       N  
ATOM   1523  CA  ILE A 222     -23.649 -15.881  53.437  1.00 76.32           C  
ANISOU 1523  CA  ILE A 222    11221   9723   8056    428   -610   1288       C  
ATOM   1524  C   ILE A 222     -24.600 -17.045  53.766  1.00 82.85           C  
ANISOU 1524  C   ILE A 222    12204  10398   8879    416   -414   1393       C  
ATOM   1525  O   ILE A 222     -24.814 -17.326  54.945  1.00 84.15           O  
ANISOU 1525  O   ILE A 222    12527  10577   8870    452   -414   1526       O  
ATOM   1526  CB  ILE A 222     -24.406 -14.586  53.000  1.00 76.77           C  
ANISOU 1526  CB  ILE A 222    11217   9869   8083    297   -578   1100       C  
ATOM   1527  CG1 ILE A 222     -23.461 -13.369  52.917  1.00 76.54           C  
ANISOU 1527  CG1 ILE A 222    11072   9977   8033    296   -774   1013       C  
ATOM   1528  CG2 ILE A 222     -25.593 -14.283  53.926  1.00 76.98           C  
ANISOU 1528  CG2 ILE A 222    11402   9925   7922    234   -472   1102       C  
ATOM   1529  CD1 ILE A 222     -23.890 -12.294  51.864  1.00 80.48           C  
ANISOU 1529  CD1 ILE A 222    11441  10510   8628    195   -728    840       C  
ATOM   1530  N   ILE A 223     -25.118 -17.753  52.740  1.00 80.02           N  
ANISOU 1530  N   ILE A 223    11806   9893   8703    358   -251   1339       N  
ATOM   1531  CA  ILE A 223     -26.005 -18.893  52.988  1.00 81.58           C  
ANISOU 1531  CA  ILE A 223    12147   9926   8924    316    -60   1431       C  
ATOM   1532  C   ILE A 223     -25.274 -20.236  53.245  1.00 89.24           C  
ANISOU 1532  C   ILE A 223    13206  10717   9982    455    -39   1613       C  
ATOM   1533  O   ILE A 223     -25.891 -21.301  53.179  1.00 90.87           O  
ANISOU 1533  O   ILE A 223    13522  10733  10272    413    136   1674       O  
ATOM   1534  CB  ILE A 223     -27.294 -18.968  52.116  1.00 83.14           C  
ANISOU 1534  CB  ILE A 223    12308  10070   9213    138    123   1298       C  
ATOM   1535  CG1 ILE A 223     -26.990 -19.199  50.628  1.00 82.34           C  
ANISOU 1535  CG1 ILE A 223    12071   9901   9315    100    148   1161       C  
ATOM   1536  CG2 ILE A 223     -28.185 -17.740  52.367  1.00 82.50           C  
ANISOU 1536  CG2 ILE A 223    12187  10162   8997     42    128   1204       C  
ATOM   1537  CD1 ILE A 223     -28.203 -19.187  49.679  1.00 90.31           C  
ANISOU 1537  CD1 ILE A 223    13017  10903  10394    -91    290   1020       C  
ATOM   1538  N   SER A 224     -23.965 -20.161  53.580  1.00 86.20           N  
ANISOU 1538  N   SER A 224    12771  10397   9584    620   -219   1710       N  
ATOM   1539  CA  SER A 224     -23.117 -21.292  53.961  1.00 88.24           C  
ANISOU 1539  CA  SER A 224    13092  10521   9913    800   -231   1920       C  
ATOM   1540  C   SER A 224     -22.726 -21.074  55.416  1.00 94.70           C  
ANISOU 1540  C   SER A 224    14002  11485  10494    895   -387   2108       C  
ATOM   1541  O   SER A 224     -22.864 -21.995  56.219  1.00 96.61           O  
ANISOU 1541  O   SER A 224    14404  11620  10683    972   -320   2317       O  
ATOM   1542  CB  SER A 224     -21.872 -21.378  53.079  1.00 91.09           C  
ANISOU 1542  CB  SER A 224    13279  10869  10461    925   -316   1891       C  
ATOM   1543  OG  SER A 224     -20.993 -22.416  53.493  1.00101.08           O  
ANISOU 1543  OG  SER A 224    14586  12018  11803   1132   -330   2115       O  
ATOM   1544  N   LYS A 225     -22.277 -19.841  55.762  1.00 90.87           N  
ANISOU 1544  N   LYS A 225    13428  11241   9856    875   -591   2031       N  
ATOM   1545  CA  LYS A 225     -21.919 -19.422  57.119  1.00 92.32           C  
ANISOU 1545  CA  LYS A 225    13699  11609   9771    927   -767   2158       C  
ATOM   1546  C   LYS A 225     -23.126 -19.651  58.022  1.00 97.88           C  
ANISOU 1546  C   LYS A 225    14624  12282  10284    852   -616   2222       C  
ATOM   1547  O   LYS A 225     -22.998 -20.329  59.034  1.00100.58           O  
ANISOU 1547  O   LYS A 225    15110  12617  10489    948   -630   2448       O  
ATOM   1548  CB  LYS A 225     -21.461 -17.940  57.134  1.00 93.46           C  
ANISOU 1548  CB  LYS A 225    13723  11985   9805    854   -971   1989       C  
ATOM   1549  CG  LYS A 225     -21.575 -17.196  58.482  1.00107.12           C  
ANISOU 1549  CG  LYS A 225    15590  13908  11204    816  -1104   2013       C  
ATOM   1550  CD  LYS A 225     -20.528 -17.612  59.532  1.00119.89           C  
ANISOU 1550  CD  LYS A 225    17241  15649  12664    959  -1317   2245       C  
ATOM   1551  CE  LYS A 225     -19.337 -16.683  59.571  1.00126.81           C  
ANISOU 1551  CE  LYS A 225    17948  16736  13499    955  -1604   2181       C  
ATOM   1552  NZ  LYS A 225     -18.429 -16.996  60.705  1.00135.46           N  
ANISOU 1552  NZ  LYS A 225    19076  17999  14393   1070  -1834   2407       N  
ATOM   1553  N   LEU A 226     -24.304 -19.166  57.593  1.00 93.11           N  
ANISOU 1553  N   LEU A 226    14032  11654   9690    689   -456   2045       N  
ATOM   1554  CA  LEU A 226     -25.601 -19.297  58.265  1.00 93.78           C  
ANISOU 1554  CA  LEU A 226    14287  11714   9631    596   -271   2077       C  
ATOM   1555  C   LEU A 226     -25.983 -20.755  58.523  1.00101.04           C  
ANISOU 1555  C   LEU A 226    15344  12423  10624    635    -94   2285       C  
ATOM   1556  O   LEU A 226     -26.605 -21.056  59.541  1.00101.94           O  
ANISOU 1556  O   LEU A 226    15632  12547  10556    626     -2   2426       O  
ATOM   1557  CB  LEU A 226     -26.681 -18.632  57.389  1.00 91.27           C  
ANISOU 1557  CB  LEU A 226    13880  11391   9406    430   -128   1852       C  
ATOM   1558  CG  LEU A 226     -27.123 -17.204  57.731  1.00 94.77           C  
ANISOU 1558  CG  LEU A 226    14316  12022   9672    355   -172   1695       C  
ATOM   1559  CD1 LEU A 226     -25.964 -16.318  58.086  1.00 94.95           C  
ANISOU 1559  CD1 LEU A 226    14297  12203   9579    421   -429   1652       C  
ATOM   1560  CD2 LEU A 226     -27.883 -16.588  56.581  1.00 94.90           C  
ANISOU 1560  CD2 LEU A 226    14183  12027   9848    233    -69   1496       C  
ATOM   1561  N   SER A 227     -25.614 -21.650  57.588  1.00 99.69           N  
ANISOU 1561  N   SER A 227    15105  12052  10720    676    -32   2300       N  
ATOM   1562  CA  SER A 227     -25.908 -23.081  57.632  1.00102.43           C  
ANISOU 1562  CA  SER A 227    15580  12141  11196    706    153   2473       C  
ATOM   1563  C   SER A 227     -25.052 -23.831  58.643  1.00113.02           C  
ANISOU 1563  C   SER A 227    17039  13454  12448    908     66   2769       C  
ATOM   1564  O   SER A 227     -25.611 -24.519  59.500  1.00114.84           O  
ANISOU 1564  O   SER A 227    17453  13602  12577    911    191   2964       O  
ATOM   1565  CB  SER A 227     -25.754 -23.698  56.248  1.00104.52           C  
ANISOU 1565  CB  SER A 227    15747  12198  11769    680    250   2354       C  
ATOM   1566  OG  SER A 227     -26.577 -23.043  55.296  1.00110.47           O  
ANISOU 1566  OG  SER A 227    16388  12996  12589    490    321   2100       O  
ATOM   1567  N   HIS A 228     -23.731 -23.693  58.547  1.00113.02           N  
ANISOU 1567  N   HIS A 228    16923  13535  12485   1074   -141   2819       N  
ATOM   1568  CA  HIS A 228     -22.801 -24.456  59.379  1.00117.52           C  
ANISOU 1568  CA  HIS A 228    17562  14087  13004   1293   -241   3122       C  
ATOM   1569  C   HIS A 228     -22.386 -23.757  60.676  1.00124.66           C  
ANISOU 1569  C   HIS A 228    18512  15285  13567   1349   -468   3243       C  
ATOM   1570  O   HIS A 228     -21.222 -23.809  61.073  1.00126.08           O  
ANISOU 1570  O   HIS A 228    18619  15584  13701   1520   -682   3401       O  
ATOM   1571  CB  HIS A 228     -21.556 -24.835  58.572  1.00119.14           C  
ANISOU 1571  CB  HIS A 228    17597  14215  13455   1464   -329   3145       C  
ATOM   1572  CG  HIS A 228     -20.551 -23.731  58.459  1.00122.02           C  
ANISOU 1572  CG  HIS A 228    17752  14857  13754   1502   -603   3045       C  
ATOM   1573  ND1 HIS A 228     -20.903 -22.399  58.476  1.00121.89           N  
ANISOU 1573  ND1 HIS A 228    17676  15062  13575   1336   -706   2822       N  
ATOM   1574  CD2 HIS A 228     -19.203 -23.762  58.326  1.00125.20           C  
ANISOU 1574  CD2 HIS A 228    17983  15345  14243   1683   -788   3144       C  
ATOM   1575  CE1 HIS A 228     -19.817 -21.656  58.360  1.00121.21           C  
ANISOU 1575  CE1 HIS A 228    17403  15174  13477   1393   -945   2780       C  
ATOM   1576  NE2 HIS A 228     -18.772 -22.459  58.267  1.00123.53           N  
ANISOU 1576  NE2 HIS A 228    17612  15404  13919   1599  -1004   2975       N  
ATOM   1577  N   SER A 229     -23.344 -23.114  61.333  1.00122.33           N  
ANISOU 1577  N   SER A 229    18336  15114  13029   1203   -419   3168       N  
ATOM   1578  CA  SER A 229     -23.131 -22.527  62.626  1.00124.78           C  
ANISOU 1578  CA  SER A 229    18747  15684  12981   1232   -592   3267       C  
ATOM   1579  C   SER A 229     -24.214 -22.961  63.593  1.00133.13           C  
ANISOU 1579  C   SER A 229    20046  16703  13832   1179   -398   3410       C  
ATOM   1580  O   SER A 229     -24.959 -23.891  63.318  1.00132.74           O  
ANISOU 1580  O   SER A 229    20079  16410  13947   1144   -150   3489       O  
ATOM   1581  CB  SER A 229     -23.138 -21.015  62.489  1.00125.52           C  
ANISOU 1581  CB  SER A 229    18741  16006  12944   1103   -735   2982       C  
ATOM   1582  OG  SER A 229     -24.430 -20.554  62.172  1.00129.72           O  
ANISOU 1582  OG  SER A 229    19318  16488  13482    929   -525   2786       O  
ATOM   1583  N   GLY A 900     -24.767 -22.457  64.634  1.00110.20           N  
ANISOU 1583  N   GLY A 900    14513  13626  13730    309   -102    -92       N  
ATOM   1584  CA  GLY A 900     -25.843 -22.833  65.533  1.00110.97           C  
ANISOU 1584  CA  GLY A 900    14611  13725  13828    309   -104    -93       C  
ATOM   1585  C   GLY A 900     -26.095 -23.336  66.940  1.00116.84           C  
ANISOU 1585  C   GLY A 900    15353  14468  14571    309   -105    -93       C  
ATOM   1586  O   GLY A 900     -26.645 -24.421  67.132  1.00117.06           O  
ANISOU 1586  O   GLY A 900    15382  14497  14599    310   -105    -94       O  
ATOM   1587  N   SER A 901     -25.677 -22.555  67.929  1.00113.63           N  
ANISOU 1587  N   SER A 901    14946  14061  14166    310   -105    -94       N  
ATOM   1588  CA  SER A 901     -25.848 -22.937  69.325  1.00113.38           C  
ANISOU 1588  CA  SER A 901    14915  14029  14134    311   -106    -95       C  
ATOM   1589  C   SER A 901     -26.066 -21.703  70.189  1.00116.68           C  
ANISOU 1589  C   SER A 901    15335  14447  14553    311   -107    -95       C  
ATOM   1590  O   SER A 901     -26.285 -21.805  71.396  1.00116.56           O  
ANISOU 1590  O   SER A 901    15320  14430  14536    313   -107    -96       O  
ATOM   1591  CB  SER A 901     -24.631 -23.719  69.821  1.00116.61           C  
ANISOU 1591  CB  SER A 901    15324  14439  14544    310   -106    -95       C  
ATOM   1592  OG  SER A 901     -24.849 -25.116  69.728  1.00124.47           O  
ANISOU 1592  OG  SER A 901    16319  15436  15539    311   -106    -96       O  
ATOM   1593  N   ASN A1002     -26.005 -20.536  69.558  1.00112.18           N  
ANISOU 1593  N   ASN A1002    14020  17044  11559    138  -2138   -547       N  
ATOM   1594  CA  ASN A1002     -26.197 -19.276  70.260  1.00110.57           C  
ANISOU 1594  CA  ASN A1002    13816  16829  11366    261  -2048   -370       C  
ATOM   1595  C   ASN A1002     -25.239 -19.119  71.434  1.00110.44           C  
ANISOU 1595  C   ASN A1002    13951  16559  11450    147  -1855   -218       C  
ATOM   1596  O   ASN A1002     -25.321 -18.145  72.183  1.00109.87           O  
ANISOU 1596  O   ASN A1002    13893  16444  11410    213  -1763    -98       O  
ATOM   1597  CB  ASN A1002     -27.628 -19.173  70.792  1.00112.63           C  
ANISOU 1597  CB  ASN A1002    13801  17249  11746    228  -2088   -470       C  
ATOM   1598  CG  ASN A1002     -28.531 -18.363  69.883  1.00134.63           C  
ANISOU 1598  CG  ASN A1002    16457  20310  14386    505  -2253   -505       C  
ATOM   1599  OD1 ASN A1002     -28.847 -18.782  68.769  1.00131.69           O  
ANISOU 1599  OD1 ASN A1002    16016  20129  13892    581  -2435   -654       O  
ATOM   1600  ND2 ASN A1002     -28.951 -17.195  70.354  1.00126.66           N  
ANISOU 1600  ND2 ASN A1002    15422  19327  13376    681  -2196   -376       N  
ATOM   1601  N   ILE A1003     -24.330 -20.077  71.595  1.00104.20           N  
ANISOU 1601  N   ILE A1003    13275  15613  10705     -6  -1804   -237       N  
ATOM   1602  CA  ILE A1003     -23.380 -20.014  72.679  1.00101.16           C  
ANISOU 1602  CA  ILE A1003    13018  15027  10392    -92  -1655   -113       C  
ATOM   1603  C   ILE A1003     -22.053 -20.185  72.024  1.00102.02           C  
ANISOU 1603  C   ILE A1003    13303  15051  10411    -44  -1640    -69       C  
ATOM   1604  O   ILE A1003     -21.035 -19.832  72.576  1.00 99.77           O  
ANISOU 1604  O   ILE A1003    13128  14641  10139    -48  -1540     38       O  
ATOM   1605  CB  ILE A1003     -23.551 -21.122  73.705  1.00104.07           C  
ANISOU 1605  CB  ILE A1003    13347  15283  10911   -311  -1586   -164       C  
ATOM   1606  N   PHE A1004     -22.069 -20.723  70.820  1.00 98.39           N  
ANISOU 1606  N   PHE A1004    12852  14678   9852      6  -1743   -172       N  
ATOM   1607  CA  PHE A1004     -20.816 -21.029  70.140  1.00 96.69           C  
ANISOU 1607  CA  PHE A1004    12794  14397   9548     52  -1714   -149       C  
ATOM   1608  C   PHE A1004     -20.075 -19.755  69.750  1.00 96.96           C  
ANISOU 1608  C   PHE A1004    12938  14433   9469    215  -1634     18       C  
ATOM   1609  O   PHE A1004     -18.990 -19.475  70.260  1.00 95.70           O  
ANISOU 1609  O   PHE A1004    12861  14143   9356    183  -1515    115       O  
ATOM   1610  CB  PHE A1004     -21.075 -21.888  68.901  1.00100.35           C  
ANISOU 1610  CB  PHE A1004    13249  14971   9908     84  -1843   -323       C  
ATOM   1611  CG  PHE A1004     -19.904 -22.737  68.496  1.00101.68           C  
ANISOU 1611  CG  PHE A1004    13553  15034  10047     66  -1801   -362       C  
ATOM   1612  CD1 PHE A1004     -19.342 -23.635  69.387  1.00103.86           C  
ANISOU 1612  CD1 PHE A1004    13867  15118  10476    -79  -1726   -371       C  
ATOM   1613  CD2 PHE A1004     -19.366 -22.637  67.224  1.00104.56           C  
ANISOU 1613  CD2 PHE A1004    14014  15499  10216    223  -1826   -381       C  
ATOM   1614  CE1 PHE A1004     -18.264 -24.418  69.017  1.00104.76           C  
ANISOU 1614  CE1 PHE A1004    14098  15139  10566    -60  -1689   -410       C  
ATOM   1615  CE2 PHE A1004     -18.288 -23.417  66.848  1.00107.21           C  
ANISOU 1615  CE2 PHE A1004    14461  15749  10525    224  -1774   -428       C  
ATOM   1616  CZ  PHE A1004     -17.737 -24.308  67.746  1.00104.43           C  
ANISOU 1616  CZ  PHE A1004    14131  15203  10346     87  -1710   -448       C  
ATOM   1617  N   GLU A1005     -20.667 -18.987  68.841  1.00 91.68           N  
ANISOU 1617  N   GLU A1005    12266  13912   8656    393  -1696     48       N  
ATOM   1618  CA  GLU A1005     -20.065 -17.742  68.381  1.00 90.59           C  
ANISOU 1618  CA  GLU A1005    12260  13748   8412    555  -1591    228       C  
ATOM   1619  C   GLU A1005     -20.190 -16.496  69.270  1.00 91.79           C  
ANISOU 1619  C   GLU A1005    12419  13796   8661    574  -1486    365       C  
ATOM   1620  O   GLU A1005     -19.916 -15.382  68.823  1.00 92.76           O  
ANISOU 1620  O   GLU A1005    12656  13880   8708    718  -1395    513       O  
ATOM   1621  CB  GLU A1005     -20.939 -17.090  67.307  1.00 94.03           C  
ANISOU 1621  CB  GLU A1005    12701  14372   8655    791  -1689    257       C  
ATOM   1622  CG  GLU A1005     -21.981 -18.019  66.707  1.00105.88           C  
ANISOU 1622  CG  GLU A1005    14060  16085  10085    805  -1900     47       C  
ATOM   1623  CD  GLU A1005     -21.405 -18.928  65.639  1.00122.56           C  
ANISOU 1623  CD  GLU A1005    16253  18267  12048    825  -1955    -65       C  
ATOM   1624  OE1 GLU A1005     -20.707 -18.420  64.736  1.00116.91           O  
ANISOU 1624  OE1 GLU A1005    15702  17577  11139    994  -1884     55       O  
ATOM   1625  OE2 GLU A1005     -21.649 -20.151  65.703  1.00108.87           O  
ANISOU 1625  OE2 GLU A1005    14427  16546  10392    671  -2050   -274       O  
ATOM   1626  N   MET A1006     -20.606 -16.686  70.522  1.00 84.82           N  
ANISOU 1626  N   MET A1006    11432  12857   7940    434  -1482    316       N  
ATOM   1627  CA  MET A1006     -20.777 -15.597  71.432  1.00 83.13           C  
ANISOU 1627  CA  MET A1006    11221  12551   7814    450  -1391    403       C  
ATOM   1628  C   MET A1006     -19.364 -15.730  71.866  1.00 84.36           C  
ANISOU 1628  C   MET A1006    11465  12555   8032    329  -1281    434       C  
ATOM   1629  O   MET A1006     -18.701 -14.756  72.120  1.00 83.87           O  
ANISOU 1629  O   MET A1006    11484  12375   8010    341  -1162    522       O  
ATOM   1630  CB  MET A1006     -21.670 -16.035  72.563  1.00 84.89           C  
ANISOU 1630  CB  MET A1006    11295  12802   8157    335  -1426    314       C  
ATOM   1631  CG  MET A1006     -20.992 -15.994  73.887  1.00 86.88           C  
ANISOU 1631  CG  MET A1006    11577  12909   8524    196  -1322    331       C  
ATOM   1632  SD  MET A1006     -22.068 -15.410  75.177  1.00 90.98           S  
ANISOU 1632  SD  MET A1006    11993  13444   9131    189  -1281    315       S  
ATOM   1633  CE  MET A1006     -22.095 -13.692  74.808  1.00 88.80           C  
ANISOU 1633  CE  MET A1006    11811  13105   8824    389  -1215    420       C  
ATOM   1634  N   LEU A1007     -18.873 -16.955  71.903  1.00 79.59           N  
ANISOU 1634  N   LEU A1007    10842  11954   7444    217  -1320    350       N  
ATOM   1635  CA  LEU A1007     -17.484 -17.151  72.294  1.00 78.08           C  
ANISOU 1635  CA  LEU A1007    10708  11653   7307    131  -1233    368       C  
ATOM   1636  C   LEU A1007     -16.539 -17.165  71.115  1.00 80.90           C  
ANISOU 1636  C   LEU A1007    11150  12021   7567    201  -1182    404       C  
ATOM   1637  O   LEU A1007     -15.364 -16.848  71.290  1.00 80.37           O  
ANISOU 1637  O   LEU A1007    11114  11874   7548    160  -1074    443       O  
ATOM   1638  CB  LEU A1007     -17.313 -18.360  73.219  1.00 77.40           C  
ANISOU 1638  CB  LEU A1007    10575  11531   7301      0  -1271    286       C  
ATOM   1639  CG  LEU A1007     -17.650 -18.042  74.669  1.00 81.44           C  
ANISOU 1639  CG  LEU A1007    11043  11997   7902    -73  -1242    294       C  
ATOM   1640  CD1 LEU A1007     -18.616 -19.033  75.257  1.00 81.70           C  
ANISOU 1640  CD1 LEU A1007    11011  12055   7976   -154  -1292    235       C  
ATOM   1641  CD2 LEU A1007     -16.404 -17.826  75.497  1.00 83.16           C  
ANISOU 1641  CD2 LEU A1007    11292  12138   8168   -120  -1179    308       C  
ATOM   1642  N   ARG A1008     -17.058 -17.468  69.902  1.00 76.97           N  
ANISOU 1642  N   ARG A1008    10679  11641   6924    314  -1256    381       N  
ATOM   1643  CA  ARG A1008     -16.278 -17.441  68.663  1.00 77.03           C  
ANISOU 1643  CA  ARG A1008    10786  11689   6791    415  -1195    424       C  
ATOM   1644  C   ARG A1008     -15.853 -15.993  68.391  1.00 81.12           C  
ANISOU 1644  C   ARG A1008    11398  12135   7288    495  -1034    596       C  
ATOM   1645  O   ARG A1008     -14.730 -15.764  67.950  1.00 80.89           O  
ANISOU 1645  O   ARG A1008    11434  12057   7244    490   -889    659       O  
ATOM   1646  CB  ARG A1008     -17.090 -18.003  67.486  1.00 77.97           C  
ANISOU 1646  CB  ARG A1008    10917  11981   6728    541  -1332    343       C  
ATOM   1647  CG  ARG A1008     -16.227 -18.364  66.283  1.00 89.50           C  
ANISOU 1647  CG  ARG A1008    12481  13502   8024    634  -1278    340       C  
ATOM   1648  CD  ARG A1008     -17.038 -18.688  65.042  1.00100.52           C  
ANISOU 1648  CD  ARG A1008    13907  15098   9189    798  -1420    258       C  
ATOM   1649  NE  ARG A1008     -16.202 -18.668  63.838  1.00110.04           N  
ANISOU 1649  NE  ARG A1008    15251  16373  10187    937  -1323    306       N  
ATOM   1650  CZ  ARG A1008     -16.561 -19.167  62.659  1.00124.78           C  
ANISOU 1650  CZ  ARG A1008    17170  18428  11813   1087  -1434    201       C  
ATOM   1651  NH1 ARG A1008     -17.746 -19.746  62.509  1.00114.88           N  
ANISOU 1651  NH1 ARG A1008    15819  17312  10519   1100  -1662     18       N  
ATOM   1652  NH2 ARG A1008     -15.735 -19.100  61.624  1.00109.83           N  
ANISOU 1652  NH2 ARG A1008    15415  16598   9716   1221  -1312    261       N  
ATOM   1653  N   ILE A1009     -16.744 -15.025  68.698  1.00 78.16           N  
ANISOU 1653  N   ILE A1009    11028  11738   6931    562  -1041    668       N  
ATOM   1654  CA  ILE A1009     -16.517 -13.583  68.558  1.00 78.83           C  
ANISOU 1654  CA  ILE A1009    11226  11699   7026    640   -878    835       C  
ATOM   1655  C   ILE A1009     -15.552 -13.078  69.652  1.00 82.25           C  
ANISOU 1655  C   ILE A1009    11635  11947   7671    457   -740    831       C  
ATOM   1656  O   ILE A1009     -14.584 -12.386  69.336  1.00 82.91           O  
ANISOU 1656  O   ILE A1009    11796  11914   7791    428   -557    920       O  
ATOM   1657  CB  ILE A1009     -17.878 -12.819  68.579  1.00 82.66           C  
ANISOU 1657  CB  ILE A1009    11715  12224   7466    803   -952    888       C  
ATOM   1658  N   ASP A1010     -15.837 -13.420  70.930  1.00 77.25           N  
ANISOU 1658  N   ASP A1010    10887  11297   7166    335   -823    720       N  
ATOM   1659  CA  ASP A1010     -15.098 -12.988  72.120  1.00 76.27           C  
ANISOU 1659  CA  ASP A1010    10721  11043   7216    180   -745    673       C  
ATOM   1660  C   ASP A1010     -13.709 -13.611  72.307  1.00 79.87           C  
ANISOU 1660  C   ASP A1010    11119  11494   7733     52   -704    607       C  
ATOM   1661  O   ASP A1010     -12.733 -12.876  72.463  1.00 79.52           O  
ANISOU 1661  O   ASP A1010    11075  11345   7792    -31   -566    617       O  
ATOM   1662  CB  ASP A1010     -15.967 -13.159  73.381  1.00 77.05           C  
ANISOU 1662  CB  ASP A1010    10736  11162   7379    135   -848    586       C  
ATOM   1663  CG  ASP A1010     -17.201 -12.269  73.430  1.00 87.85           C  
ANISOU 1663  CG  ASP A1010    12132  12515   8732    260   -853    638       C  
ATOM   1664  OD1 ASP A1010     -17.152 -11.144  72.871  1.00 90.78           O  
ANISOU 1664  OD1 ASP A1010    12615  12779   9099    357   -740    747       O  
ATOM   1665  OD2 ASP A1010     -18.198 -12.675  74.060  1.00 90.73           O  
ANISOU 1665  OD2 ASP A1010    12409  12966   9099    265   -951    575       O  
ATOM   1666  N   GLU A1011     -13.625 -14.954  72.317  1.00 76.65           N  
ANISOU 1666  N   GLU A1011    10652  11192   7277     37   -820    527       N  
ATOM   1667  CA  GLU A1011     -12.368 -15.687  72.477  1.00 76.68           C  
ANISOU 1667  CA  GLU A1011    10594  11214   7325    -35   -803    461       C  
ATOM   1668  C   GLU A1011     -11.672 -15.865  71.123  1.00 82.02           C  
ANISOU 1668  C   GLU A1011    11319  11933   7913     32   -711    508       C  
ATOM   1669  O   GLU A1011     -10.566 -15.359  70.928  1.00 82.90           O  
ANISOU 1669  O   GLU A1011    11405  12005   8088    -19   -565    529       O  
ATOM   1670  CB  GLU A1011     -12.602 -17.053  73.156  1.00 77.24           C  
ANISOU 1670  CB  GLU A1011    10614  11342   7390    -56   -947    370       C  
ATOM   1671  CG  GLU A1011     -12.718 -16.996  74.669  1.00 90.47           C  
ANISOU 1671  CG  GLU A1011    12236  12990   9149   -131   -996    322       C  
ATOM   1672  CD  GLU A1011     -11.549 -17.564  75.456  1.00117.75           C  
ANISOU 1672  CD  GLU A1011    15622  16463  12653   -170  -1018    253       C  
ATOM   1673  OE1 GLU A1011     -10.389 -17.433  74.998  1.00118.03           O  
ANISOU 1673  OE1 GLU A1011    15610  16515  12722   -176   -950    235       O  
ATOM   1674  OE2 GLU A1011     -11.795 -18.114  76.555  1.00110.02           O  
ANISOU 1674  OE2 GLU A1011    14632  15496  11674   -182  -1096    221       O  
ATOM   1675  N   GLY A1012     -12.335 -16.562  70.205  1.00 78.63           N  
ANISOU 1675  N   GLY A1012    10947  11592   7334    139   -790    509       N  
ATOM   1676  CA  GLY A1012     -11.804 -16.847  68.882  1.00 79.67           C  
ANISOU 1676  CA  GLY A1012    11144  11795   7333    232   -717    537       C  
ATOM   1677  C   GLY A1012     -11.640 -18.332  68.636  1.00 83.37           C  
ANISOU 1677  C   GLY A1012    11589  12339   7748    256   -824    412       C  
ATOM   1678  O   GLY A1012     -11.208 -19.072  69.528  1.00 82.21           O  
ANISOU 1678  O   GLY A1012    11366  12159   7710    181   -878    329       O  
ATOM   1679  N   LEU A1013     -11.985 -18.770  67.414  1.00 80.46           N  
ANISOU 1679  N   LEU A1013    11302  12070   7198    378   -856    393       N  
ATOM   1680  CA  LEU A1013     -11.892 -20.162  66.985  1.00 80.11           C  
ANISOU 1680  CA  LEU A1013    11265  12082   7092    413   -949    249       C  
ATOM   1681  C   LEU A1013     -10.595 -20.391  66.214  1.00 84.48           C  
ANISOU 1681  C   LEU A1013    11840  12675   7583    478   -805    248       C  
ATOM   1682  O   LEU A1013     -10.309 -19.657  65.266  1.00 85.66           O  
ANISOU 1682  O   LEU A1013    12061  12884   7602    563   -668    349       O  
ATOM   1683  CB  LEU A1013     -13.110 -20.510  66.113  1.00 81.13           C  
ANISOU 1683  CB  LEU A1013    11453  12320   7052    507  -1091    179       C  
ATOM   1684  CG  LEU A1013     -13.248 -21.957  65.659  1.00 86.45           C  
ANISOU 1684  CG  LEU A1013    12143  13028   7676    523  -1206    -13       C  
ATOM   1685  CD1 LEU A1013     -14.101 -22.757  66.630  1.00 85.85           C  
ANISOU 1685  CD1 LEU A1013    11997  12867   7755    390  -1344   -120       C  
ATOM   1686  CD2 LEU A1013     -13.859 -22.022  64.278  1.00 90.79           C  
ANISOU 1686  CD2 LEU A1013    12771  13746   7979    672  -1280    -80       C  
ATOM   1687  N   ARG A1014      -9.808 -21.396  66.636  1.00 80.12           N  
ANISOU 1687  N   ARG A1014    11230  12090   7122    452   -819    145       N  
ATOM   1688  CA  ARG A1014      -8.552 -21.787  65.987  1.00 80.78           C  
ANISOU 1688  CA  ARG A1014    11301  12226   7165    528   -688    111       C  
ATOM   1689  C   ARG A1014      -8.622 -23.282  65.685  1.00 85.14           C  
ANISOU 1689  C   ARG A1014    11901  12776   7670    601   -799    -57       C  
ATOM   1690  O   ARG A1014      -8.541 -24.108  66.599  1.00 84.07           O  
ANISOU 1690  O   ARG A1014    11727  12544   7670    557   -887   -127       O  
ATOM   1691  CB  ARG A1014      -7.320 -21.404  66.828  1.00 79.30           C  
ANISOU 1691  CB  ARG A1014    10968  12005   7158    449   -575    145       C  
ATOM   1692  CG  ARG A1014      -7.034 -19.902  66.818  1.00 90.45           C  
ANISOU 1692  CG  ARG A1014    12346  13403   8618    370   -408    286       C  
ATOM   1693  CD  ARG A1014      -5.747 -19.525  67.537  1.00106.65           C  
ANISOU 1693  CD  ARG A1014    14217  15446  10858    273   -295    270       C  
ATOM   1694  NE  ARG A1014      -4.547 -19.929  66.794  1.00121.46           N  
ANISOU 1694  NE  ARG A1014    16020  17420  12709    344   -144    229       N  
ATOM   1695  CZ  ARG A1014      -3.937 -19.183  65.876  1.00138.83           C  
ANISOU 1695  CZ  ARG A1014    18223  19661  14866    341    100    317       C  
ATOM   1696  NH1 ARG A1014      -2.857 -19.637  65.254  1.00127.33           N  
ANISOU 1696  NH1 ARG A1014    16679  18311  13388    411    245    265       N  
ATOM   1697  NH2 ARG A1014      -4.407 -17.979  65.567  1.00126.97           N  
ANISOU 1697  NH2 ARG A1014    16818  18086  13339    281    220    466       N  
ATOM   1698  N   LEU A1015      -8.847 -23.614  64.395  1.00 82.84           N  
ANISOU 1698  N   LEU A1015    11717  12584   7174    723   -795   -125       N  
ATOM   1699  CA  LEU A1015      -9.031 -24.974  63.867  1.00 83.52           C  
ANISOU 1699  CA  LEU A1015    11878  12665   7190    798   -896   -322       C  
ATOM   1700  C   LEU A1015      -7.755 -25.832  63.766  1.00 88.62           C  
ANISOU 1700  C   LEU A1015    12503  13290   7877    887   -801   -407       C  
ATOM   1701  O   LEU A1015      -7.835 -27.023  63.446  1.00 89.19           O  
ANISOU 1701  O   LEU A1015    12651  13311   7924    953   -875   -582       O  
ATOM   1702  CB  LEU A1015      -9.798 -24.929  62.537  1.00 85.17           C  
ANISOU 1702  CB  LEU A1015    12203  13019   7138    908   -950   -391       C  
ATOM   1703  CG  LEU A1015     -11.178 -24.289  62.610  1.00 89.04           C  
ANISOU 1703  CG  LEU A1015    12696  13552   7584    859  -1087   -348       C  
ATOM   1704  CD1 LEU A1015     -11.371 -23.279  61.505  1.00 90.64           C  
ANISOU 1704  CD1 LEU A1015    12983  13928   7528   1004  -1018   -231       C  
ATOM   1705  CD2 LEU A1015     -12.257 -25.326  62.601  1.00 91.31           C  
ANISOU 1705  CD2 LEU A1015    12991  13814   7888    808  -1298   -565       C  
ATOM   1706  N   LYS A1016      -6.592 -25.228  64.059  1.00 85.14           N  
ANISOU 1706  N   LYS A1016    11950  12884   7517    888   -638   -299       N  
ATOM   1707  CA  LYS A1016      -5.292 -25.893  64.090  1.00 85.96           C  
ANISOU 1707  CA  LYS A1016    11976  13000   7684    985   -540   -367       C  
ATOM   1708  C   LYS A1016      -4.707 -25.714  65.501  1.00 88.13           C  
ANISOU 1708  C   LYS A1016    12091  13206   8187    898   -561   -307       C  
ATOM   1709  O   LYS A1016      -5.077 -24.754  66.183  1.00 86.48           O  
ANISOU 1709  O   LYS A1016    11826  12977   8055    762   -577   -195       O  
ATOM   1710  CB  LYS A1016      -4.354 -25.308  63.023  1.00 90.54           C  
ANISOU 1710  CB  LYS A1016    12526  13741   8135   1076   -307   -319       C  
ATOM   1711  CG  LYS A1016      -3.217 -26.247  62.629  1.00109.48           C  
ANISOU 1711  CG  LYS A1016    14878  16192  10529   1235   -212   -446       C  
ATOM   1712  CD  LYS A1016      -2.000 -25.492  62.100  1.00122.09           C  
ANISOU 1712  CD  LYS A1016    16338  17941  12110   1265     62   -365       C  
ATOM   1713  CE  LYS A1016      -0.825 -26.402  61.826  1.00134.22           C  
ANISOU 1713  CE  LYS A1016    17781  19549  13667   1436    160   -498       C  
ATOM   1714  NZ  LYS A1016      -0.992 -27.167  60.561  1.00144.03           N  
ANISOU 1714  NZ  LYS A1016    19207  20854  14663   1620    196   -628       N  
ATOM   1715  N   ILE A1017      -3.828 -26.645  65.951  1.00 85.17           N  
ANISOU 1715  N   ILE A1017    11651  12802   7908   1000   -573   -391       N  
ATOM   1716  CA  ILE A1017      -3.194 -26.604  67.278  1.00 84.33           C  
ANISOU 1716  CA  ILE A1017    11390  12671   7980    972   -620   -355       C  
ATOM   1717  C   ILE A1017      -2.370 -25.329  67.442  1.00 87.96           C  
ANISOU 1717  C   ILE A1017    11646  13262   8513    880   -481   -275       C  
ATOM   1718  O   ILE A1017      -1.677 -24.929  66.506  1.00 88.89           O  
ANISOU 1718  O   ILE A1017    11702  13496   8576    913   -296   -273       O  
ATOM   1719  CB  ILE A1017      -2.358 -27.892  67.576  1.00 89.11           C  
ANISOU 1719  CB  ILE A1017    11977  13238   8642   1163   -657   -457       C  
ATOM   1720  CG1 ILE A1017      -3.275 -29.117  67.816  1.00 89.40           C  
ANISOU 1720  CG1 ILE A1017    12229  13064   8676   1201   -800   -518       C  
ATOM   1721  CG2 ILE A1017      -1.390 -27.693  68.769  1.00 90.65           C  
ANISOU 1721  CG2 ILE A1017    11961  13501   8982   1189   -688   -426       C  
ATOM   1722  CD1 ILE A1017      -2.551 -30.494  67.974  1.00 98.09           C  
ANISOU 1722  CD1 ILE A1017    13379  14066   9822   1423   -820   -613       C  
ATOM   1723  N   TYR A1018      -2.459 -24.698  68.630  1.00 83.43           N  
ANISOU 1723  N   TYR A1018    10973  12663   8064    755   -556   -220       N  
ATOM   1724  CA  TYR A1018      -1.725 -23.480  68.987  1.00 83.61           C  
ANISOU 1724  CA  TYR A1018    10792  12777   8199    629   -446   -181       C  
ATOM   1725  C   TYR A1018      -1.294 -23.493  70.466  1.00 86.22           C  
ANISOU 1725  C   TYR A1018    10967  13127   8667    606   -583   -220       C  
ATOM   1726  O   TYR A1018      -1.703 -24.378  71.217  1.00 84.82           O  
ANISOU 1726  O   TYR A1018    10879  12875   8473    691   -750   -232       O  
ATOM   1727  CB  TYR A1018      -2.554 -22.216  68.646  1.00 84.27           C  
ANISOU 1727  CB  TYR A1018    10960  12807   8250    467   -366    -66       C  
ATOM   1728  CG  TYR A1018      -3.739 -21.964  69.555  1.00 84.52           C  
ANISOU 1728  CG  TYR A1018    11089  12726   8299    375   -528    -20       C  
ATOM   1729  CD1 TYR A1018      -3.674 -21.016  70.572  1.00 85.89           C  
ANISOU 1729  CD1 TYR A1018    11155  12881   8598    237   -545     -1       C  
ATOM   1730  CD2 TYR A1018      -4.936 -22.653  69.382  1.00 84.57           C  
ANISOU 1730  CD2 TYR A1018    11281  12651   8202    419   -654    -16       C  
ATOM   1731  CE1 TYR A1018      -4.763 -20.776  71.410  1.00 84.80           C  
ANISOU 1731  CE1 TYR A1018    11104  12652   8462    169   -674     36       C  
ATOM   1732  CE2 TYR A1018      -6.032 -22.422  70.214  1.00 84.06           C  
ANISOU 1732  CE2 TYR A1018    11279  12500   8161    332   -778     24       C  
ATOM   1733  CZ  TYR A1018      -5.943 -21.477  71.222  1.00 89.49           C  
ANISOU 1733  CZ  TYR A1018    11869  13177   8954    218   -781     58       C  
ATOM   1734  OH  TYR A1018      -7.018 -21.249  72.043  1.00 87.84           O  
ANISOU 1734  OH  TYR A1018    11722  12896   8757    149   -884     92       O  
ATOM   1735  N   LYS A1019      -0.464 -22.513  70.871  1.00 83.20           N  
ANISOU 1735  N   LYS A1019    10356  12843   8412    490   -503   -245       N  
ATOM   1736  CA  LYS A1019       0.010 -22.342  72.246  1.00 82.62           C  
ANISOU 1736  CA  LYS A1019    10107  12835   8450    463   -640   -313       C  
ATOM   1737  C   LYS A1019      -0.709 -21.137  72.845  1.00 85.60           C  
ANISOU 1737  C   LYS A1019    10515  13132   8878    254   -651   -267       C  
ATOM   1738  O   LYS A1019      -0.746 -20.068  72.226  1.00 84.71           O  
ANISOU 1738  O   LYS A1019    10391  12983   8813    102   -477   -223       O  
ATOM   1739  CB  LYS A1019       1.536 -22.136  72.293  1.00 86.89           C  
ANISOU 1739  CB  LYS A1019    10322  13573   9120    479   -559   -435       C  
ATOM   1740  CG  LYS A1019       2.361 -23.384  72.002  1.00 98.31           C  
ANISOU 1740  CG  LYS A1019    11698  15125  10531    735   -584   -504       C  
ATOM   1741  CD  LYS A1019       3.847 -23.085  72.148  1.00111.67           C  
ANISOU 1741  CD  LYS A1019    13011  17050  12370    744   -514   -643       C  
ATOM   1742  CE  LYS A1019       4.728 -24.280  71.879  1.00125.79           C  
ANISOU 1742  CE  LYS A1019    14702  18962  14131   1032   -534   -720       C  
ATOM   1743  NZ  LYS A1019       6.149 -24.002  72.221  1.00137.02           N  
ANISOU 1743  NZ  LYS A1019    15702  20651  15707   1055   -510   -879       N  
ATOM   1744  N   ASP A1020      -1.295 -21.309  74.040  1.00 82.42           N  
ANISOU 1744  N   ASP A1020    10171  12689   8456    261   -838   -268       N  
ATOM   1745  CA  ASP A1020      -2.034 -20.245  74.718  1.00 81.80           C  
ANISOU 1745  CA  ASP A1020    10132  12535   8414     92   -861   -243       C  
ATOM   1746  C   ASP A1020      -1.107 -19.249  75.444  1.00 87.95           C  
ANISOU 1746  C   ASP A1020    10659  13417   9342    -40   -846   -371       C  
ATOM   1747  O   ASP A1020       0.116 -19.335  75.311  1.00 89.32           O  
ANISOU 1747  O   ASP A1020    10599  13737   9602    -17   -804   -477       O  
ATOM   1748  CB  ASP A1020      -3.065 -20.843  75.697  1.00 82.44           C  
ANISOU 1748  CB  ASP A1020    10381  12543   8401    155  -1039   -196       C  
ATOM   1749  CG  ASP A1020      -2.497 -21.620  76.875  1.00 98.33           C  
ANISOU 1749  CG  ASP A1020    12317  14659  10386    297  -1209   -258       C  
ATOM   1750  OD1 ASP A1020      -1.256 -21.761  76.957  1.00100.88           O  
ANISOU 1750  OD1 ASP A1020    12430  15136  10765    372  -1223   -361       O  
ATOM   1751  OD2 ASP A1020      -3.296 -22.089  77.715  1.00106.29           O  
ANISOU 1751  OD2 ASP A1020    13473  15604  11309    348  -1322   -200       O  
ATOM   1752  N   THR A1021      -1.699 -18.305  76.203  1.00 84.63           N  
ANISOU 1752  N   THR A1021    10272  12924   8959   -179   -880   -384       N  
ATOM   1753  CA  THR A1021      -0.990 -17.284  76.983  1.00 86.41           C  
ANISOU 1753  CA  THR A1021    10282  13218   9331   -333   -883   -542       C  
ATOM   1754  C   THR A1021       0.091 -17.881  77.895  1.00 91.85           C  
ANISOU 1754  C   THR A1021    10732  14137  10030   -221  -1057   -708       C  
ATOM   1755  O   THR A1021       1.202 -17.350  77.950  1.00 93.83           O  
ANISOU 1755  O   THR A1021    10702  14516  10434   -321  -1010   -871       O  
ATOM   1756  CB  THR A1021      -1.983 -16.424  77.783  1.00 96.18           C  
ANISOU 1756  CB  THR A1021    11649  14334  10562   -442   -930   -538       C  
ATOM   1757  OG1 THR A1021      -2.796 -17.273  78.603  1.00 95.02           O  
ANISOU 1757  OG1 THR A1021    11652  14201  10250   -293  -1115   -483       O  
ATOM   1758  CG2 THR A1021      -2.850 -15.537  76.890  1.00 94.05           C  
ANISOU 1758  CG2 THR A1021    11558  13855  10320   -555   -743   -401       C  
ATOM   1759  N   GLU A1022      -0.232 -18.994  78.585  1.00 87.20           N  
ANISOU 1759  N   GLU A1022    10252  13601   9281     -7  -1249   -664       N  
ATOM   1760  CA  GLU A1022       0.705 -19.688  79.475  1.00 88.54           C  
ANISOU 1760  CA  GLU A1022    10240  13994   9408    175  -1438   -785       C  
ATOM   1761  C   GLU A1022       1.740 -20.564  78.749  1.00 91.69           C  
ANISOU 1761  C   GLU A1022    10489  14514   9833    341  -1403   -807       C  
ATOM   1762  O   GLU A1022       2.790 -20.850  79.321  1.00 93.61           O  
ANISOU 1762  O   GLU A1022    10487  14986  10096    469  -1529   -949       O  
ATOM   1763  CB  GLU A1022       0.001 -20.432  80.635  1.00 89.42           C  
ANISOU 1763  CB  GLU A1022    10543  14105   9328    352  -1637   -713       C  
ATOM   1764  CG  GLU A1022      -1.337 -21.069  80.295  1.00100.11           C  
ANISOU 1764  CG  GLU A1022    12229  15236  10572    389  -1590   -504       C  
ATOM   1765  CD  GLU A1022      -2.556 -20.269  80.712  1.00123.69           C  
ANISOU 1765  CD  GLU A1022    15373  18089  13533    232  -1565   -453       C  
ATOM   1766  OE1 GLU A1022      -2.694 -19.985  81.925  1.00123.33           O  
ANISOU 1766  OE1 GLU A1022    15324  18122  13415    248  -1686   -513       O  
ATOM   1767  OE2 GLU A1022      -3.397 -19.963  79.835  1.00113.70           O  
ANISOU 1767  OE2 GLU A1022    14241  16658  12301    120  -1432   -355       O  
ATOM   1768  N   GLY A1023       1.414 -21.033  77.552  1.00 85.59           N  
ANISOU 1768  N   GLY A1023     9867  13611   9042    370  -1252   -679       N  
ATOM   1769  CA  GLY A1023       2.348 -21.816  76.766  1.00 85.96           C  
ANISOU 1769  CA  GLY A1023     9790  13761   9111    530  -1187   -708       C  
ATOM   1770  C   GLY A1023       1.900 -23.219  76.435  1.00 86.89           C  
ANISOU 1770  C   GLY A1023    10151  13773   9089    770  -1235   -590       C  
ATOM   1771  O   GLY A1023       2.544 -23.944  75.711  1.00 86.87           O  
ANISOU 1771  O   GLY A1023    10096  13821   9088    925  -1171   -610       O  
ATOM   1772  N   TYR A1024       0.749 -23.619  76.939  1.00 81.41           N  
ANISOU 1772  N   TYR A1024     9733  12916   8283    793  -1329   -474       N  
ATOM   1773  CA  TYR A1024       0.307 -24.978  76.703  1.00 81.05           C  
ANISOU 1773  CA  TYR A1024     9924  12737   8136    994  -1365   -379       C  
ATOM   1774  C   TYR A1024      -0.434 -25.123  75.421  1.00 83.42           C  
ANISOU 1774  C   TYR A1024    10406  12872   8417    915  -1220   -314       C  
ATOM   1775  O   TYR A1024      -0.957 -24.170  74.902  1.00 82.06           O  
ANISOU 1775  O   TYR A1024    10250  12659   8271    715  -1118   -290       O  
ATOM   1776  CB  TYR A1024      -0.597 -25.447  77.813  1.00 81.76           C  
ANISOU 1776  CB  TYR A1024    10226  12715   8123   1047  -1504   -281       C  
ATOM   1777  CG  TYR A1024       0.038 -25.346  79.151  1.00 85.80           C  
ANISOU 1777  CG  TYR A1024    10598  13407   8596   1161  -1669   -337       C  
ATOM   1778  CD1 TYR A1024      -0.449 -24.476  80.097  1.00 87.13           C  
ANISOU 1778  CD1 TYR A1024    10758  13611   8735   1022  -1737   -350       C  
ATOM   1779  CD2 TYR A1024       1.125 -26.116  79.472  1.00 89.04           C  
ANISOU 1779  CD2 TYR A1024    10883  13968   8981   1432  -1767   -390       C  
ATOM   1780  CE1 TYR A1024       0.126 -24.378  81.316  1.00 89.36           C  
ANISOU 1780  CE1 TYR A1024    10917  14086   8949   1141  -1904   -424       C  
ATOM   1781  CE2 TYR A1024       1.706 -26.020  80.689  1.00 91.70           C  
ANISOU 1781  CE2 TYR A1024    11084  14508   9250   1566  -1945   -452       C  
ATOM   1782  CZ  TYR A1024       1.202 -25.150  81.610  1.00 98.57           C  
ANISOU 1782  CZ  TYR A1024    11955  15422  10076   1415  -2018   -475       C  
ATOM   1783  OH  TYR A1024       1.776 -25.047  82.844  1.00102.21           O  
ANISOU 1783  OH  TYR A1024    12285  16113  10436   1564  -2213   -560       O  
ATOM   1784  N   TYR A1025      -0.491 -26.349  74.936  1.00 79.79           N  
ANISOU 1784  N   TYR A1025    10098  12315   7904   1094  -1220   -293       N  
ATOM   1785  CA  TYR A1025      -1.135 -26.673  73.665  1.00 78.50           C  
ANISOU 1785  CA  TYR A1025    10109  12019   7700   1057  -1108   -273       C  
ATOM   1786  C   TYR A1025      -2.659 -26.644  73.733  1.00 80.41           C  
ANISOU 1786  C   TYR A1025    10583  12078   7893    916  -1141   -190       C  
ATOM   1787  O   TYR A1025      -3.271 -27.337  74.543  1.00 79.17           O  
ANISOU 1787  O   TYR A1025    10571  11796   7714    958  -1239   -136       O  
ATOM   1788  CB  TYR A1025      -0.604 -27.989  73.084  1.00 81.22           C  
ANISOU 1788  CB  TYR A1025    10524  12318   8016   1296  -1092   -324       C  
ATOM   1789  CG  TYR A1025       0.824 -27.916  72.582  1.00 84.56           C  
ANISOU 1789  CG  TYR A1025    10697  12946   8486   1423  -1003   -423       C  
ATOM   1790  CD1 TYR A1025       1.835 -28.653  73.188  1.00 88.70           C  
ANISOU 1790  CD1 TYR A1025    11099  13566   9037   1674  -1085   -473       C  
ATOM   1791  CD2 TYR A1025       1.158 -27.133  71.479  1.00 85.18           C  
ANISOU 1791  CD2 TYR A1025    10661  13128   8575   1310   -822   -459       C  
ATOM   1792  CE1 TYR A1025       3.148 -28.601  72.722  1.00 91.87           C  
ANISOU 1792  CE1 TYR A1025    11229  14181   9495   1797   -998   -582       C  
ATOM   1793  CE2 TYR A1025       2.468 -27.070  71.006  1.00 88.02           C  
ANISOU 1793  CE2 TYR A1025    10770  13684   8991   1411   -705   -551       C  
ATOM   1794  CZ  TYR A1025       3.459 -27.815  71.624  1.00 97.25           C  
ANISOU 1794  CZ  TYR A1025    11781  14963  10205   1650   -796   -625       C  
ATOM   1795  OH  TYR A1025       4.750 -27.764  71.158  1.00100.46           O  
ANISOU 1795  OH  TYR A1025    11901  15590  10679   1756   -677   -732       O  
ATOM   1796  N   THR A1026      -3.257 -25.822  72.865  1.00 77.05           N  
ANISOU 1796  N   THR A1026    10182  11646   7447    758  -1048   -174       N  
ATOM   1797  CA  THR A1026      -4.690 -25.550  72.794  1.00 75.82           C  
ANISOU 1797  CA  THR A1026    10185  11372   7250    619  -1073   -113       C  
ATOM   1798  C   THR A1026      -5.221 -25.682  71.335  1.00 81.12           C  
ANISOU 1798  C   THR A1026    10968  12016   7838    612   -997   -139       C  
ATOM   1799  O   THR A1026      -4.429 -25.750  70.391  1.00 82.35           O  
ANISOU 1799  O   THR A1026    11076  12254   7960    695   -896   -188       O  
ATOM   1800  CB  THR A1026      -4.938 -24.145  73.411  1.00 84.29           C  
ANISOU 1800  CB  THR A1026    11161  12498   8366    455  -1063    -65       C  
ATOM   1801  OG1 THR A1026      -4.018 -23.895  74.480  1.00 85.97           O  
ANISOU 1801  OG1 THR A1026    11211  12810   8643    482  -1114    -99       O  
ATOM   1802  CG2 THR A1026      -6.335 -23.964  73.933  1.00 81.71           C  
ANISOU 1802  CG2 THR A1026    10960  12068   8017    352  -1128     -3       C  
ATOM   1803  N   ILE A1027      -6.565 -25.733  71.176  1.00 77.22           N  
ANISOU 1803  N   ILE A1027    10611  11429   7302    524  -1050   -118       N  
ATOM   1804  CA  ILE A1027      -7.320 -25.847  69.917  1.00 77.63           C  
ANISOU 1804  CA  ILE A1027    10769  11476   7248    518  -1032   -162       C  
ATOM   1805  C   ILE A1027      -8.790 -25.399  70.154  1.00 81.10           C  
ANISOU 1805  C   ILE A1027    11264  11872   7678    387  -1106   -121       C  
ATOM   1806  O   ILE A1027      -9.237 -25.377  71.302  1.00 79.13           O  
ANISOU 1806  O   ILE A1027    11002  11555   7507    313  -1164    -73       O  
ATOM   1807  CB  ILE A1027      -7.199 -27.285  69.303  1.00 82.28           C  
ANISOU 1807  CB  ILE A1027    11473  11985   7805    638  -1056   -285       C  
ATOM   1808  CG1 ILE A1027      -7.551 -27.305  67.798  1.00 83.66           C  
ANISOU 1808  CG1 ILE A1027    11726  12231   7831    677  -1021   -370       C  
ATOM   1809  CG2 ILE A1027      -7.976 -28.347  70.109  1.00 83.21           C  
ANISOU 1809  CG2 ILE A1027    11703  11912   8002    600  -1157   -308       C  
ATOM   1810  CD1 ILE A1027      -6.744 -28.244  66.974  1.00 90.97           C  
ANISOU 1810  CD1 ILE A1027    12702  13162   8700    839   -967   -494       C  
ATOM   1811  N   GLY A1028      -9.505 -25.051  69.079  1.00 79.30           N  
ANISOU 1811  N   GLY A1028    11087  11704   7339    383  -1103   -143       N  
ATOM   1812  CA  GLY A1028     -10.896 -24.607  69.125  1.00 79.08           C  
ANISOU 1812  CA  GLY A1028    11080  11676   7289    295  -1179   -123       C  
ATOM   1813  C   GLY A1028     -11.072 -23.349  69.951  1.00 83.30           C  
ANISOU 1813  C   GLY A1028    11540  12225   7883    218  -1148      2       C  
ATOM   1814  O   GLY A1028     -10.276 -22.410  69.825  1.00 83.19           O  
ANISOU 1814  O   GLY A1028    11479  12261   7869    232  -1043     74       O  
ATOM   1815  N   ILE A1029     -12.101 -23.329  70.822  1.00 79.43           N  
ANISOU 1815  N   ILE A1029    11039  11683   7457    127  -1223     16       N  
ATOM   1816  CA  ILE A1029     -12.338 -22.194  71.720  1.00 78.45           C  
ANISOU 1816  CA  ILE A1029    10857  11561   7391     64  -1198    110       C  
ATOM   1817  C   ILE A1029     -11.767 -22.535  73.113  1.00 82.29           C  
ANISOU 1817  C   ILE A1029    11309  11985   7974     27  -1207    123       C  
ATOM   1818  O   ILE A1029     -12.463 -23.094  73.976  1.00 81.53           O  
ANISOU 1818  O   ILE A1029    11235  11827   7917    -24  -1258    123       O  
ATOM   1819  CB  ILE A1029     -13.807 -21.656  71.723  1.00 81.36           C  
ANISOU 1819  CB  ILE A1029    11217  11956   7740     24  -1252    127       C  
ATOM   1820  CG1 ILE A1029     -14.268 -21.264  70.294  1.00 82.47           C  
ANISOU 1820  CG1 ILE A1029    11394  12197   7744    114  -1263    120       C  
ATOM   1821  CG2 ILE A1029     -13.959 -20.464  72.697  1.00 81.58           C  
ANISOU 1821  CG2 ILE A1029    11198  11967   7830    -22  -1209    210       C  
ATOM   1822  CD1 ILE A1029     -15.773 -20.995  70.125  1.00 88.83           C  
ANISOU 1822  CD1 ILE A1029    12165  13071   8514    115  -1356     98       C  
ATOM   1823  N   GLY A1030     -10.474 -22.249  73.263  1.00 79.28           N  
ANISOU 1823  N   GLY A1030    10870  11635   7618     63  -1151    129       N  
ATOM   1824  CA  GLY A1030      -9.702 -22.468  74.481  1.00 79.22           C  
ANISOU 1824  CA  GLY A1030    10808  11623   7670     72  -1177    125       C  
ATOM   1825  C   GLY A1030      -9.659 -23.884  75.025  1.00 83.88           C  
ANISOU 1825  C   GLY A1030    11469  12142   8262    136  -1242    110       C  
ATOM   1826  O   GLY A1030      -9.481 -24.062  76.233  1.00 84.68           O  
ANISOU 1826  O   GLY A1030    11564  12234   8376    153  -1283    138       O  
ATOM   1827  N   HIS A1031      -9.791 -24.902  74.157  1.00 80.17           N  
ANISOU 1827  N   HIS A1031    11081  11612   7769    186  -1246     63       N  
ATOM   1828  CA  HIS A1031      -9.747 -26.293  74.603  1.00 80.70           C  
ANISOU 1828  CA  HIS A1031    11249  11554   7858    251  -1281     52       C  
ATOM   1829  C   HIS A1031      -8.312 -26.766  74.773  1.00 83.83           C  
ANISOU 1829  C   HIS A1031    11608  11985   8258    410  -1279     36       C  
ATOM   1830  O   HIS A1031      -7.625 -27.023  73.782  1.00 84.45           O  
ANISOU 1830  O   HIS A1031    11668  12101   8320    492  -1240    -32       O  
ATOM   1831  CB  HIS A1031     -10.533 -27.225  73.662  1.00 82.53           C  
ANISOU 1831  CB  HIS A1031    11590  11680   8088    224  -1288    -28       C  
ATOM   1832  CG  HIS A1031     -10.545 -28.655  74.105  1.00 87.28           C  
ANISOU 1832  CG  HIS A1031    12325  12094   8744    271  -1294    -38       C  
ATOM   1833  ND1 HIS A1031     -11.558 -29.153  74.907  1.00 89.30           N  
ANISOU 1833  ND1 HIS A1031    12661  12210   9059    164  -1290      9       N  
ATOM   1834  CD2 HIS A1031      -9.660 -29.648  73.849  1.00 90.50           C  
ANISOU 1834  CD2 HIS A1031    12807  12418   9160    420  -1281    -82       C  
ATOM   1835  CE1 HIS A1031     -11.260 -30.426  75.110  1.00 90.39           C  
ANISOU 1835  CE1 HIS A1031    12941  12160   9244    241  -1267      6       C  
ATOM   1836  NE2 HIS A1031     -10.122 -30.767  74.503  1.00 91.45           N  
ANISOU 1836  NE2 HIS A1031    13079  12318   9348    410  -1271    -50       N  
ATOM   1837  N   LEU A1032      -7.867 -26.894  76.032  1.00 79.34           N  
ANISOU 1837  N   LEU A1032    11023  11427   7695    473  -1322     92       N  
ATOM   1838  CA  LEU A1032      -6.526 -27.370  76.376  1.00 79.82           C  
ANISOU 1838  CA  LEU A1032    11025  11553   7752    660  -1351     75       C  
ATOM   1839  C   LEU A1032      -6.432 -28.853  76.026  1.00 84.05           C  
ANISOU 1839  C   LEU A1032    11719  11921   8295    799  -1343     63       C  
ATOM   1840  O   LEU A1032      -7.366 -29.617  76.308  1.00 84.13           O  
ANISOU 1840  O   LEU A1032    11904  11742   8321    752  -1337    111       O  
ATOM   1841  CB  LEU A1032      -6.266 -27.166  77.882  1.00 80.14           C  
ANISOU 1841  CB  LEU A1032    11032  11660   7759    714  -1427    137       C  
ATOM   1842  CG  LEU A1032      -4.813 -27.127  78.349  1.00 85.99           C  
ANISOU 1842  CG  LEU A1032    11613  12574   8486    890  -1491     88       C  
ATOM   1843  CD1 LEU A1032      -4.652 -26.165  79.498  1.00 86.30           C  
ANISOU 1843  CD1 LEU A1032    11532  12767   8490    846  -1564     79       C  
ATOM   1844  CD2 LEU A1032      -4.332 -28.497  78.777  1.00 90.12           C  
ANISOU 1844  CD2 LEU A1032    12257  13015   8968   1137  -1537    139       C  
ATOM   1845  N   LEU A1033      -5.315 -29.252  75.399  1.00 80.28           N  
ANISOU 1845  N   LEU A1033    11178  11503   7821    962  -1325     -8       N  
ATOM   1846  CA  LEU A1033      -5.081 -30.644  75.022  1.00 80.79           C  
ANISOU 1846  CA  LEU A1033    11397  11400   7900   1128  -1309    -40       C  
ATOM   1847  C   LEU A1033      -4.197 -31.337  76.054  1.00 83.82           C  
ANISOU 1847  C   LEU A1033    11798  11780   8270   1373  -1368     25       C  
ATOM   1848  O   LEU A1033      -4.596 -32.356  76.616  1.00 84.37           O  
ANISOU 1848  O   LEU A1033    12080  11632   8345   1454  -1372    106       O  
ATOM   1849  CB  LEU A1033      -4.481 -30.752  73.608  1.00 81.43           C  
ANISOU 1849  CB  LEU A1033    11423  11542   7974   1191  -1240   -169       C  
ATOM   1850  CG  LEU A1033      -5.408 -30.408  72.448  1.00 85.10           C  
ANISOU 1850  CG  LEU A1033    11938  11986   8409   1018  -1192   -238       C  
ATOM   1851  CD1 LEU A1033      -4.615 -30.182  71.184  1.00 86.21           C  
ANISOU 1851  CD1 LEU A1033    11988  12269   8498   1097  -1108   -338       C  
ATOM   1852  CD2 LEU A1033      -6.457 -31.483  72.235  1.00 88.01           C  
ANISOU 1852  CD2 LEU A1033    12527  12106   8806    965  -1206   -283       C  
ATOM   1853  N   THR A1034      -3.012 -30.767  76.316  1.00 79.42           N  
ANISOU 1853  N   THR A1034    11012  11465   7697   1492  -1411    -10       N  
ATOM   1854  CA  THR A1034      -2.055 -31.280  77.290  1.00 80.72           C  
ANISOU 1854  CA  THR A1034    11137  11708   7825   1761  -1501     31       C  
ATOM   1855  C   THR A1034      -1.182 -30.168  77.876  1.00 82.71           C  
ANISOU 1855  C   THR A1034    11088  12275   8065   1758  -1579    -24       C  
ATOM   1856  O   THR A1034      -0.815 -29.218  77.170  1.00 81.39           O  
ANISOU 1856  O   THR A1034    10708  12261   7954   1613  -1520   -125       O  
ATOM   1857  CB  THR A1034      -1.244 -32.473  76.721  1.00 93.27           C  
ANISOU 1857  CB  THR A1034    12790  13215   9435   2042  -1473    -17       C  
ATOM   1858  OG1 THR A1034      -0.572 -33.135  77.791  1.00 97.62           O  
ANISOU 1858  OG1 THR A1034    13374  13789   9930   2340  -1572     65       O  
ATOM   1859  CG2 THR A1034      -0.239 -32.069  75.641  1.00 91.62           C  
ANISOU 1859  CG2 THR A1034    12336  13209   9265   2082  -1411   -168       C  
ATOM   1860  N   LYS A1035      -0.846 -30.296  79.171  1.00 78.90           N  
ANISOU 1860  N   LYS A1035    10592  11883   7502   1919  -1706     37       N  
ATOM   1861  CA  LYS A1035       0.050 -29.355  79.840  1.00 78.68           C  
ANISOU 1861  CA  LYS A1035    10265  12171   7460   1937  -1814    -58       C  
ATOM   1862  C   LYS A1035       1.518 -29.798  79.640  1.00 84.27           C  
ANISOU 1862  C   LYS A1035    10750  13078   8193   2218  -1866   -162       C  
ATOM   1863  O   LYS A1035       2.449 -29.071  79.993  1.00 84.92           O  
ANISOU 1863  O   LYS A1035    10515  13453   8299   2233  -1949   -293       O  
ATOM   1864  CB  LYS A1035      -0.336 -29.151  81.312  1.00 80.81           C  
ANISOU 1864  CB  LYS A1035    10609  12493   7601   1971  -1940     27       C  
ATOM   1865  CG  LYS A1035      -1.225 -27.928  81.521  1.00 84.95           C  
ANISOU 1865  CG  LYS A1035    11109  13025   8141   1650  -1907     10       C  
ATOM   1866  CD  LYS A1035      -1.861 -27.913  82.904  1.00 92.20           C  
ANISOU 1866  CD  LYS A1035    12180  13943   8910   1688  -1992    115       C  
ATOM   1867  CE  LYS A1035      -2.178 -26.526  83.411  1.00101.49           C  
ANISOU 1867  CE  LYS A1035    13220  15256  10086   1461  -2020     23       C  
ATOM   1868  NZ  LYS A1035      -3.388 -25.951  82.769  1.00112.64           N  
ANISOU 1868  NZ  LYS A1035    14732  16484  11583   1173  -1878     60       N  
ATOM   1869  N   SER A1036       1.700 -30.977  79.000  1.00 81.20           N  
ANISOU 1869  N   SER A1036    10512  12524   7814   2426  -1806   -129       N  
ATOM   1870  CA  SER A1036       2.977 -31.583  78.624  1.00 83.23           C  
ANISOU 1870  CA  SER A1036    10598  12924   8102   2726  -1822   -222       C  
ATOM   1871  C   SER A1036       3.659 -30.702  77.554  1.00 85.63           C  
ANISOU 1871  C   SER A1036    10580  13430   8527   2556  -1706   -393       C  
ATOM   1872  O   SER A1036       2.952 -30.020  76.804  1.00 83.20           O  
ANISOU 1872  O   SER A1036    10318  13031   8264   2254  -1579   -397       O  
ATOM   1873  CB  SER A1036       2.740 -32.981  78.065  1.00 87.75           C  
ANISOU 1873  CB  SER A1036    11473  13196   8673   2931  -1743   -150       C  
ATOM   1874  OG  SER A1036       1.857 -33.710  78.902  1.00 95.81           O  
ANISOU 1874  OG  SER A1036    12839  13951   9612   2992  -1781     31       O  
ATOM   1875  N   PRO A1037       5.010 -30.677  77.447  1.00 83.28           N  
ANISOU 1875  N   PRO A1037     9951  13412   8281   2746  -1734   -529       N  
ATOM   1876  CA  PRO A1037       5.639 -29.797  76.450  1.00 82.80           C  
ANISOU 1876  CA  PRO A1037     9583  13532   8344   2553  -1578   -676       C  
ATOM   1877  C   PRO A1037       5.841 -30.426  75.069  1.00 87.20           C  
ANISOU 1877  C   PRO A1037    10209  13992   8931   2636  -1390   -710       C  
ATOM   1878  O   PRO A1037       6.661 -29.924  74.295  1.00 88.90           O  
ANISOU 1878  O   PRO A1037    10141  14404   9234   2581  -1251   -831       O  
ATOM   1879  CB  PRO A1037       6.961 -29.415  77.115  1.00 87.13           C  
ANISOU 1879  CB  PRO A1037     9702  14456   8947   2689  -1700   -828       C  
ATOM   1880  CG  PRO A1037       7.274 -30.558  78.021  1.00 93.93           C  
ANISOU 1880  CG  PRO A1037    10669  15329   9691   3108  -1896   -766       C  
ATOM   1881  CD  PRO A1037       6.032 -31.387  78.238  1.00 87.79           C  
ANISOU 1881  CD  PRO A1037    10389  14169   8800   3146  -1899   -557       C  
ATOM   1882  N   SER A1038       5.079 -31.493  74.743  1.00 81.56           N  
ANISOU 1882  N   SER A1038     9870  12973   8147   2750  -1368   -617       N  
ATOM   1883  CA  SER A1038       5.190 -32.195  73.466  1.00 81.18           C  
ANISOU 1883  CA  SER A1038     9931  12812   8102   2851  -1208   -674       C  
ATOM   1884  C   SER A1038       3.990 -31.979  72.560  1.00 80.63           C  
ANISOU 1884  C   SER A1038    10119  12520   7997   2578  -1089   -638       C  
ATOM   1885  O   SER A1038       2.853 -32.192  72.984  1.00 77.88           O  
ANISOU 1885  O   SER A1038    10042  11937   7611   2465  -1157   -536       O  
ATOM   1886  CB  SER A1038       5.433 -33.684  73.698  1.00 87.09           C  
ANISOU 1886  CB  SER A1038    10885  13391   8817   3238  -1272   -650       C  
ATOM   1887  OG  SER A1038       5.340 -34.467  72.518  1.00 95.94           O  
ANISOU 1887  OG  SER A1038    12185  14338   9931   3329  -1127   -720       O  
ATOM   1888  N   LEU A1039       4.256 -31.563  71.302  1.00 77.24           N  
ANISOU 1888  N   LEU A1039     9593  12183   7570   2487   -906   -724       N  
ATOM   1889  CA  LEU A1039       3.247 -31.359  70.253  1.00 75.14           C  
ANISOU 1889  CA  LEU A1039     9548  11768   7235   2282   -795   -714       C  
ATOM   1890  C   LEU A1039       2.735 -32.722  69.762  1.00 80.26           C  
ANISOU 1890  C   LEU A1039    10517  12149   7828   2452   -803   -755       C  
ATOM   1891  O   LEU A1039       1.553 -32.849  69.435  1.00 78.41           O  
ANISOU 1891  O   LEU A1039    10532  11715   7545   2291   -816   -734       O  
ATOM   1892  CB  LEU A1039       3.830 -30.522  69.095  1.00 75.57           C  
ANISOU 1892  CB  LEU A1039     9405  12029   7277   2183   -583   -779       C  
ATOM   1893  CG  LEU A1039       3.016 -30.378  67.799  1.00 78.82           C  
ANISOU 1893  CG  LEU A1039    10029  12352   7566   2060   -453   -786       C  
ATOM   1894  CD1 LEU A1039       1.746 -29.589  68.019  1.00 76.01           C  
ANISOU 1894  CD1 LEU A1039     9815  11885   7179   1782   -516   -677       C  
ATOM   1895  CD2 LEU A1039       3.835 -29.713  66.730  1.00 82.88           C  
ANISOU 1895  CD2 LEU A1039    10352  13087   8051   2042   -215   -832       C  
ATOM   1896  N   ASN A1040       3.623 -33.742  69.754  1.00 79.69           N  
ANISOU 1896  N   ASN A1040    10429  12073   7778   2780   -800   -828       N  
ATOM   1897  CA  ASN A1040       3.296 -35.120  69.380  1.00 81.29           C  
ANISOU 1897  CA  ASN A1040    10939  11989   7959   2976   -799   -887       C  
ATOM   1898  C   ASN A1040       2.398 -35.763  70.456  1.00 84.73           C  
ANISOU 1898  C   ASN A1040    11643  12124   8427   2958   -941   -763       C  
ATOM   1899  O   ASN A1040       1.637 -36.682  70.146  1.00 84.95           O  
ANISOU 1899  O   ASN A1040    11977  11842   8459   2961   -930   -797       O  
ATOM   1900  CB  ASN A1040       4.565 -35.950  69.155  1.00 87.17           C  
ANISOU 1900  CB  ASN A1040    11578  12816   8728   3362   -748   -991       C  
ATOM   1901  CG  ASN A1040       5.576 -35.319  68.221  1.00123.54           C  
ANISOU 1901  CG  ASN A1040    15874  17750  13317   3393   -580  -1104       C  
ATOM   1902  OD1 ASN A1040       5.274 -34.957  67.077  1.00121.51           O  
ANISOU 1902  OD1 ASN A1040    15662  17528  12977   3249   -435  -1172       O  
ATOM   1903  ND2 ASN A1040       6.811 -35.193  68.685  1.00119.67           N  
ANISOU 1903  ND2 ASN A1040    15054  17519  12895   3595   -589  -1129       N  
ATOM   1904  N   ALA A1041       2.483 -35.271  71.710  1.00 80.71           N  
ANISOU 1904  N   ALA A1041    11018  11709   7940   2929  -1061   -629       N  
ATOM   1905  CA  ALA A1041       1.640 -35.725  72.820  1.00 80.33           C  
ANISOU 1905  CA  ALA A1041    11209  11416   7898   2900  -1170   -480       C  
ATOM   1906  C   ALA A1041       0.297 -34.992  72.766  1.00 82.04           C  
ANISOU 1906  C   ALA A1041    11519  11550   8102   2515  -1168   -430       C  
ATOM   1907  O   ALA A1041      -0.718 -35.542  73.199  1.00 81.65           O  
ANISOU 1907  O   ALA A1041    11728  11225   8070   2426  -1192   -351       O  
ATOM   1908  CB  ALA A1041       2.323 -35.458  74.150  1.00 81.72           C  
ANISOU 1908  CB  ALA A1041    11216  11775   8060   3057  -1303   -374       C  
ATOM   1909  N   ALA A1042       0.299 -33.750  72.229  1.00 76.62           N  
ANISOU 1909  N   ALA A1042    10618  11100   7396   2296  -1123   -472       N  
ATOM   1910  CA  ALA A1042      -0.894 -32.922  72.061  1.00 73.95           C  
ANISOU 1910  CA  ALA A1042    10334  10727   7037   1968  -1117   -432       C  
ATOM   1911  C   ALA A1042      -1.742 -33.473  70.917  1.00 79.63           C  
ANISOU 1911  C   ALA A1042    11265  11262   7728   1885  -1054   -530       C  
ATOM   1912  O   ALA A1042      -2.971 -33.504  71.026  1.00 78.02           O  
ANISOU 1912  O   ALA A1042    11217  10897   7530   1689  -1088   -500       O  
ATOM   1913  CB  ALA A1042      -0.498 -31.483  71.783  1.00 73.24           C  
ANISOU 1913  CB  ALA A1042     9973  10918   6937   1810  -1067   -442       C  
ATOM   1914  N   LYS A1043      -1.076 -33.939  69.834  1.00 79.23           N  
ANISOU 1914  N   LYS A1043    11208  11252   7643   2044   -964   -668       N  
ATOM   1915  CA  LYS A1043      -1.718 -34.538  68.661  1.00 80.16           C  
ANISOU 1915  CA  LYS A1043    11519  11229   7708   2010   -914   -813       C  
ATOM   1916  C   LYS A1043      -2.360 -35.885  69.006  1.00 87.40           C  
ANISOU 1916  C   LYS A1043    12721  11785   8702   2059   -961   -846       C  
ATOM   1917  O   LYS A1043      -3.448 -36.177  68.511  1.00 86.88           O  
ANISOU 1917  O   LYS A1043    12818  11559   8633   1888   -975   -933       O  
ATOM   1918  CB  LYS A1043      -0.730 -34.676  67.495  1.00 83.82           C  
ANISOU 1918  CB  LYS A1043    11899  11851   8096   2198   -791   -955       C  
ATOM   1919  CG  LYS A1043      -0.437 -33.362  66.790  1.00 91.62           C  
ANISOU 1919  CG  LYS A1043    12679  13139   8993   2079   -691   -936       C  
ATOM   1920  CD  LYS A1043       0.305 -33.574  65.489  1.00102.45           C  
ANISOU 1920  CD  LYS A1043    14022  14648  10257   2243   -538  -1079       C  
ATOM   1921  CE  LYS A1043       0.593 -32.263  64.808  1.00114.08           C  
ANISOU 1921  CE  LYS A1043    15316  16393  11637   2122   -400  -1023       C  
ATOM   1922  NZ  LYS A1043       1.041 -32.460  63.406  1.00130.48           N  
ANISOU 1922  NZ  LYS A1043    17426  18594  13555   2260   -233  -1153       N  
ATOM   1923  N   SER A1044      -1.702 -36.683  69.880  1.00 86.99           N  
ANISOU 1923  N   SER A1044    12723  11604   8724   2292   -983   -774       N  
ATOM   1924  CA  SER A1044      -2.203 -37.977  70.359  1.00 89.38           C  
ANISOU 1924  CA  SER A1044    13321  11519   9120   2361   -993   -760       C  
ATOM   1925  C   SER A1044      -3.458 -37.795  71.225  1.00 93.50           C  
ANISOU 1925  C   SER A1044    13950  11882   9693   2091  -1044   -626       C  
ATOM   1926  O   SER A1044      -4.363 -38.631  71.171  1.00 94.11           O  
ANISOU 1926  O   SER A1044    14265  11639   9855   1978  -1019   -673       O  
ATOM   1927  CB  SER A1044      -1.125 -38.715  71.145  1.00 95.29           C  
ANISOU 1927  CB  SER A1044    14093  12208   9904   2719  -1003   -672       C  
ATOM   1928  OG  SER A1044      -0.006 -39.001  70.324  1.00106.09           O  
ANISOU 1928  OG  SER A1044    15360  13708  11241   2986   -941   -815       O  
ATOM   1929  N   GLU A1045      -3.511 -36.693  72.008  1.00 89.09           N  
ANISOU 1929  N   GLU A1045    13208  11549   9095   1976  -1101   -477       N  
ATOM   1930  CA  GLU A1045      -4.654 -36.346  72.856  1.00 87.88           C  
ANISOU 1930  CA  GLU A1045    13115  11306   8971   1730  -1137   -348       C  
ATOM   1931  C   GLU A1045      -5.812 -35.790  72.033  1.00 91.44           C  
ANISOU 1931  C   GLU A1045    13545  11786   9413   1427  -1134   -453       C  
ATOM   1932  O   GLU A1045      -6.969 -35.969  72.415  1.00 90.74           O  
ANISOU 1932  O   GLU A1045    13565  11526   9387   1222  -1136   -419       O  
ATOM   1933  CB  GLU A1045      -4.255 -35.373  73.980  1.00 87.78           C  
ANISOU 1933  CB  GLU A1045    12918  11529   8904   1744  -1203   -183       C  
ATOM   1934  CG  GLU A1045      -3.672 -36.059  75.208  1.00 99.97           C  
ANISOU 1934  CG  GLU A1045    14559  12980  10443   1998  -1238    -31       C  
ATOM   1935  CD  GLU A1045      -4.556 -37.093  75.885  1.00119.90           C  
ANISOU 1935  CD  GLU A1045    17396  15132  13029   1967  -1188     87       C  
ATOM   1936  OE1 GLU A1045      -5.709 -36.756  76.239  1.00113.78           O  
ANISOU 1936  OE1 GLU A1045    16668  14287  12276   1697  -1169    146       O  
ATOM   1937  OE2 GLU A1045      -4.090 -38.243  76.064  1.00112.90           O  
ANISOU 1937  OE2 GLU A1045    16707  14015  12175   2220  -1152    125       O  
ATOM   1938  N   LEU A1046      -5.502 -35.125  70.904  1.00 88.63           N  
ANISOU 1938  N   LEU A1046    13047  11657   8973   1414  -1121   -577       N  
ATOM   1939  CA  LEU A1046      -6.500 -34.575  69.984  1.00 88.12           C  
ANISOU 1939  CA  LEU A1046    12961  11664   8856   1193  -1133   -682       C  
ATOM   1940  C   LEU A1046      -7.181 -35.726  69.232  1.00 95.83           C  
ANISOU 1940  C   LEU A1046    14139  12392   9878   1152  -1127   -875       C  
ATOM   1941  O   LEU A1046      -8.413 -35.781  69.199  1.00 95.24           O  
ANISOU 1941  O   LEU A1046    14116  12220   9850    928  -1165   -926       O  
ATOM   1942  CB  LEU A1046      -5.852 -33.561  69.013  1.00 87.34           C  
ANISOU 1942  CB  LEU A1046    12685  11874   8627   1235  -1095   -726       C  
ATOM   1943  CG  LEU A1046      -6.762 -32.835  68.010  1.00 90.95           C  
ANISOU 1943  CG  LEU A1046    13120  12460   8979   1069  -1111   -804       C  
ATOM   1944  CD1 LEU A1046      -7.780 -31.941  68.707  1.00 88.97           C  
ANISOU 1944  CD1 LEU A1046    12805  12244   8755    854  -1170   -679       C  
ATOM   1945  CD2 LEU A1046      -5.945 -31.997  67.061  1.00 93.31           C  
ANISOU 1945  CD2 LEU A1046    13293  13022   9141   1160  -1026   -816       C  
ATOM   1946  N   ASP A1047      -6.374 -36.667  68.682  1.00 95.69           N  
ANISOU 1946  N   ASP A1047    14226  12268   9863   1371  -1077  -1000       N  
ATOM   1947  CA  ASP A1047      -6.838 -37.857  67.964  1.00 98.21           C  
ANISOU 1947  CA  ASP A1047    14753  12321  10239   1362  -1062  -1223       C  
ATOM   1948  C   ASP A1047      -7.684 -38.754  68.870  1.00102.46           C  
ANISOU 1948  C   ASP A1047    15482  12486  10964   1226  -1053  -1172       C  
ATOM   1949  O   ASP A1047      -8.672 -39.313  68.403  1.00103.37           O  
ANISOU 1949  O   ASP A1047    15704  12417  11155   1036  -1064  -1351       O  
ATOM   1950  CB  ASP A1047      -5.649 -38.644  67.383  1.00102.84           C  
ANISOU 1950  CB  ASP A1047    15414  12862  10800   1671   -992  -1340       C  
ATOM   1951  CG  ASP A1047      -4.885 -37.943  66.269  1.00115.53           C  
ANISOU 1951  CG  ASP A1047    16863  14811  12224   1793   -956  -1434       C  
ATOM   1952  OD1 ASP A1047      -5.481 -37.075  65.591  1.00115.02           O  
ANISOU 1952  OD1 ASP A1047    16706  14960  12036   1631   -989  -1476       O  
ATOM   1953  OD2 ASP A1047      -3.698 -38.283  66.056  1.00123.52           O  
ANISOU 1953  OD2 ASP A1047    17847  15875  13211   2067   -883  -1462       O  
ATOM   1954  N   LYS A1048      -7.307 -38.866  70.166  1.00 98.21           N  
ANISOU 1954  N   LYS A1048    14976  11848  10490   1318  -1027   -931       N  
ATOM   1955  CA  LYS A1048      -8.020 -39.649  71.181  1.00 99.00           C  
ANISOU 1955  CA  LYS A1048    15271  11597  10746   1212   -978   -814       C  
ATOM   1956  C   LYS A1048      -9.403 -39.050  71.474  1.00100.40           C  
ANISOU 1956  C   LYS A1048    15371  11812  10966    863  -1005   -786       C  
ATOM   1957  O   LYS A1048     -10.382 -39.796  71.547  1.00101.54           O  
ANISOU 1957  O   LYS A1048    15655  11665  11261    659   -954   -860       O  
ATOM   1958  CB  LYS A1048      -7.199 -39.736  72.483  1.00101.84           C  
ANISOU 1958  CB  LYS A1048    15668  11931  11094   1446   -958   -542       C  
ATOM   1959  CG  LYS A1048      -6.429 -41.040  72.654  1.00121.62           C  
ANISOU 1959  CG  LYS A1048    18415  14124  13672   1744   -886   -528       C  
ATOM   1960  CD  LYS A1048      -5.664 -41.065  73.977  1.00132.31           C  
ANISOU 1960  CD  LYS A1048    19795  15502  14973   2006   -895   -250       C  
ATOM   1961  CE  LYS A1048      -5.106 -42.428  74.323  1.00145.60           C  
ANISOU 1961  CE  LYS A1048    21772  16816  16734   2312   -813   -184       C  
ATOM   1962  NZ  LYS A1048      -6.122 -43.304  74.969  1.00155.39           N  
ANISOU 1962  NZ  LYS A1048    23321  17600  18121   2147   -688    -70       N  
ATOM   1963  N   ALA A1049      -9.475 -37.708  71.634  1.00 93.39           N  
ANISOU 1963  N   ALA A1049    14253  11272   9961    793  -1074   -690       N  
ATOM   1964  CA  ALA A1049     -10.703 -36.960  71.930  1.00 91.21           C  
ANISOU 1964  CA  ALA A1049    13866  11088   9702    509  -1105   -652       C  
ATOM   1965  C   ALA A1049     -11.709 -36.984  70.780  1.00 95.32           C  
ANISOU 1965  C   ALA A1049    14342  11636  10238    303  -1156   -907       C  
ATOM   1966  O   ALA A1049     -12.899 -37.192  71.025  1.00 95.51           O  
ANISOU 1966  O   ALA A1049    14370  11539  10379     57  -1146   -948       O  
ATOM   1967  CB  ALA A1049     -10.368 -35.524  72.303  1.00 88.99           C  
ANISOU 1967  CB  ALA A1049    13370  11152   9291    535  -1159   -506       C  
ATOM   1968  N   ILE A1050     -11.230 -36.774  69.533  1.00 91.52           N  
ANISOU 1968  N   ILE A1050    13809  11336   9629    413  -1206  -1083       N  
ATOM   1969  CA  ILE A1050     -12.052 -36.767  68.320  1.00 91.82           C  
ANISOU 1969  CA  ILE A1050    13807  11463   9619    280  -1283  -1346       C  
ATOM   1970  C   ILE A1050     -12.377 -38.198  67.875  1.00 99.22           C  
ANISOU 1970  C   ILE A1050    14933  12069  10698    223  -1256  -1593       C  
ATOM   1971  O   ILE A1050     -13.549 -38.575  67.862  1.00100.49           O  
ANISOU 1971  O   ILE A1050    15092  12100  10989    -30  -1281  -1730       O  
ATOM   1972  CB  ILE A1050     -11.420 -35.892  67.185  1.00 93.62           C  
ANISOU 1972  CB  ILE A1050    13923  12036   9612    437  -1329  -1409       C  
ATOM   1973  CG1 ILE A1050     -11.140 -34.420  67.630  1.00 90.74           C  
ANISOU 1973  CG1 ILE A1050    13380  11955   9143    459  -1332  -1171       C  
ATOM   1974  CG2 ILE A1050     -12.210 -35.965  65.866  1.00 95.49           C  
ANISOU 1974  CG2 ILE A1050    14146  12389   9745    358  -1426  -1694       C  
ATOM   1975  CD1 ILE A1050     -12.339 -33.569  68.187  1.00 94.21           C  
ANISOU 1975  CD1 ILE A1050    13696  12485   9614    244  -1390  -1076       C  
ATOM   1976  N   GLY A1051     -11.345 -38.967  67.523  1.00 97.22           N  
ANISOU 1976  N   GLY A1051    14827  11678  10432    453  -1200  -1662       N  
ATOM   1977  CA  GLY A1051     -11.478 -40.344  67.054  1.00100.47           C  
ANISOU 1977  CA  GLY A1051    15451  11744  10979    441  -1158  -1913       C  
ATOM   1978  C   GLY A1051     -10.584 -40.673  65.870  1.00105.36           C  
ANISOU 1978  C   GLY A1051    16132  12446  11454    685  -1164  -2129       C  
ATOM   1979  O   GLY A1051      -9.972 -41.745  65.837  1.00107.71           O  
ANISOU 1979  O   GLY A1051    16631  12451  11845    846  -1081  -2211       O  
ATOM   1980  N   ARG A1052     -10.504 -39.749  64.891  1.00 99.83           N  
ANISOU 1980  N   ARG A1052    15275  12140  10515    734  -1245  -2212       N  
ATOM   1981  CA  ARG A1052      -9.698 -39.881  63.671  1.00100.70           C  
ANISOU 1981  CA  ARG A1052    15422  12407  10433    968  -1235  -2409       C  
ATOM   1982  C   ARG A1052      -8.286 -39.270  63.798  1.00103.99           C  
ANISOU 1982  C   ARG A1052    15751  13038  10724   1250  -1147  -2193       C  
ATOM   1983  O   ARG A1052      -8.028 -38.500  64.727  1.00101.09           O  
ANISOU 1983  O   ARG A1052    15256  12770  10384   1237  -1131  -1908       O  
ATOM   1984  CB  ARG A1052     -10.448 -39.273  62.465  1.00 99.08           C  
ANISOU 1984  CB  ARG A1052    15119  12514  10012    877  -1358  -2625       C  
ATOM   1985  CG  ARG A1052     -10.732 -37.774  62.575  1.00 99.78           C  
ANISOU 1985  CG  ARG A1052    14996  12966   9950    818  -1410  -2400       C  
ATOM   1986  CD  ARG A1052     -11.155 -37.178  61.251  1.00102.93           C  
ANISOU 1986  CD  ARG A1052    15337  13702  10069    849  -1509  -2579       C  
ATOM   1987  NE  ARG A1052     -11.278 -35.721  61.325  1.00105.85           N  
ANISOU 1987  NE  ARG A1052    15540  14387  10290    843  -1525  -2332       N  
ATOM   1988  CZ  ARG A1052     -10.290 -34.870  61.063  1.00118.65           C  
ANISOU 1988  CZ  ARG A1052    17109  16229  11744   1026  -1418  -2145       C  
ATOM   1989  NH1 ARG A1052      -9.095 -35.319  60.704  1.00107.43           N  
ANISOU 1989  NH1 ARG A1052    15758  14789  10272   1239  -1293  -2180       N  
ATOM   1990  NH2 ARG A1052     -10.491 -33.562  61.159  1.00102.48           N  
ANISOU 1990  NH2 ARG A1052    14933  14412   9592    996  -1421  -1927       N  
ATOM   1991  N   ASN A1053      -7.381 -39.608  62.854  1.00103.25           N  
ANISOU 1991  N   ASN A1053    15710  13026  10494   1497  -1086  -2352       N  
ATOM   1992  CA  ASN A1053      -6.023 -39.058  62.809  1.00102.80           C  
ANISOU 1992  CA  ASN A1053    15533  13203  10323   1755   -983  -2197       C  
ATOM   1993  C   ASN A1053      -6.110 -37.686  62.132  1.00104.42           C  
ANISOU 1993  C   ASN A1053    15558  13821  10297   1705   -994  -2125       C  
ATOM   1994  O   ASN A1053      -6.314 -37.588  60.920  1.00105.19           O  
ANISOU 1994  O   ASN A1053    15690  14090  10188   1742  -1006  -2319       O  
ATOM   1995  CB  ASN A1053      -5.058 -40.001  62.075  1.00110.07           C  
ANISOU 1995  CB  ASN A1053    16578  14044  11200   2046   -887  -2400       C  
ATOM   1996  CG  ASN A1053      -3.624 -39.520  62.053  1.00139.66           C  
ANISOU 1996  CG  ASN A1053    20165  18037  14861   2313   -764  -2260       C  
ATOM   1997  OD1 ASN A1053      -2.938 -39.469  63.084  1.00136.07           O  
ANISOU 1997  OD1 ASN A1053    19624  17541  14534   2410   -735  -2048       O  
ATOM   1998  ND2 ASN A1053      -3.135 -39.182  60.866  1.00130.89           N  
ANISOU 1998  ND2 ASN A1053    19006  17202  13526   2446   -686  -2388       N  
ATOM   1999  N   THR A1054      -5.991 -36.634  62.942  1.00 98.29           N  
ANISOU 1999  N   THR A1054    14609  13186   9549   1625   -989  -1847       N  
ATOM   2000  CA  THR A1054      -6.151 -35.237  62.542  1.00 96.36           C  
ANISOU 2000  CA  THR A1054    14209  13268   9134   1550   -984  -1722       C  
ATOM   2001  C   THR A1054      -4.884 -34.519  62.073  1.00100.36           C  
ANISOU 2001  C   THR A1054    14582  14039   9509   1732   -829  -1626       C  
ATOM   2002  O   THR A1054      -4.985 -33.621  61.229  1.00 99.55           O  
ANISOU 2002  O   THR A1054    14432  14186   9206   1723   -784  -1600       O  
ATOM   2003  CB  THR A1054      -6.816 -34.456  63.683  1.00102.39           C  
ANISOU 2003  CB  THR A1054    14869  14013  10020   1339  -1053  -1498       C  
ATOM   2004  OG1 THR A1054      -5.947 -34.465  64.816  1.00103.26           O  
ANISOU 2004  OG1 THR A1054    14904  14054  10276   1412  -1001  -1319       O  
ATOM   2005  CG2 THR A1054      -8.191 -35.010  64.060  1.00100.33           C  
ANISOU 2005  CG2 THR A1054    14704  13538   9881   1125  -1179  -1588       C  
ATOM   2006  N   ASN A1055      -3.710 -34.872  62.653  1.00 97.64           N  
ANISOU 2006  N   ASN A1055    14168  13650   9281   1898   -741  -1560       N  
ATOM   2007  CA  ASN A1055      -2.397 -34.248  62.396  1.00 97.93           C  
ANISOU 2007  CA  ASN A1055    14021  13933   9256   2053   -578  -1475       C  
ATOM   2008  C   ASN A1055      -2.389 -32.759  62.816  1.00 99.05           C  
ANISOU 2008  C   ASN A1055    13969  14270   9397   1888   -545  -1246       C  
ATOM   2009  O   ASN A1055      -1.708 -31.930  62.200  1.00 98.81           O  
ANISOU 2009  O   ASN A1055    13811  14472   9260   1927   -390  -1186       O  
ATOM   2010  CB  ASN A1055      -1.907 -34.456  60.939  1.00101.85           C  
ANISOU 2010  CB  ASN A1055    14572  14592   9534   2233   -446  -1650       C  
ATOM   2011  CG  ASN A1055      -1.850 -35.892  60.466  1.00129.11           C  
ANISOU 2011  CG  ASN A1055    18222  17848  12985   2410   -465  -1911       C  
ATOM   2012  OD1 ASN A1055      -1.792 -36.847  61.252  1.00126.76           O  
ANISOU 2012  OD1 ASN A1055    18005  17277  12880   2464   -529  -1943       O  
ATOM   2013  ND2 ASN A1055      -1.838 -36.073  59.155  1.00120.89           N  
ANISOU 2013  ND2 ASN A1055    17281  16936  11714   2522   -397  -2102       N  
ATOM   2014  N   GLY A1056      -3.154 -32.458  63.868  1.00 93.24           N  
ANISOU 2014  N   GLY A1056    13223  13416   8787   1704   -673  -1124       N  
ATOM   2015  CA  GLY A1056      -3.287 -31.124  64.440  1.00 90.76           C  
ANISOU 2015  CA  GLY A1056    12755  13226   8503   1536   -665   -928       C  
ATOM   2016  C   GLY A1056      -4.332 -30.219  63.817  1.00 93.33           C  
ANISOU 2016  C   GLY A1056    13130  13641   8690   1385   -687   -885       C  
ATOM   2017  O   GLY A1056      -4.431 -29.053  64.205  1.00 90.61           O  
ANISOU 2017  O   GLY A1056    12677  13382   8369   1261   -659   -724       O  
ATOM   2018  N   VAL A1057      -5.111 -30.739  62.845  1.00 91.87           N  
ANISOU 2018  N   VAL A1057    13108  13441   8358   1408   -745  -1042       N  
ATOM   2019  CA  VAL A1057      -6.152 -29.982  62.134  1.00 91.56           C  
ANISOU 2019  CA  VAL A1057    13121  13519   8147   1319   -796  -1026       C  
ATOM   2020  C   VAL A1057      -7.520 -30.628  62.356  1.00 95.61           C  
ANISOU 2020  C   VAL A1057    13735  13883   8710   1194   -993  -1153       C  
ATOM   2021  O   VAL A1057      -7.697 -31.814  62.077  1.00 96.77           O  
ANISOU 2021  O   VAL A1057    13996  13894   8877   1237  -1053  -1363       O  
ATOM   2022  CB  VAL A1057      -5.823 -29.796  60.622  1.00 97.74           C  
ANISOU 2022  CB  VAL A1057    13975  14512   8651   1478   -681  -1103       C  
ATOM   2023  CG1 VAL A1057      -6.962 -29.099  59.880  1.00 97.82           C  
ANISOU 2023  CG1 VAL A1057    14061  14657   8450   1436   -766  -1090       C  
ATOM   2024  CG2 VAL A1057      -4.516 -29.031  60.423  1.00 97.99           C  
ANISOU 2024  CG2 VAL A1057    13882  14695   8657   1561   -443   -955       C  
ATOM   2025  N   ILE A1058      -8.485 -29.838  62.846  1.00 91.08           N  
ANISOU 2025  N   ILE A1058    13109  13326   8169   1035  -1079  -1038       N  
ATOM   2026  CA  ILE A1058      -9.853 -30.299  63.105  1.00 91.15           C  
ANISOU 2026  CA  ILE A1058    13160  13227   8246    888  -1250  -1148       C  
ATOM   2027  C   ILE A1058     -10.907 -29.422  62.412  1.00 95.51           C  
ANISOU 2027  C   ILE A1058    13693  13974   8621    854  -1337  -1143       C  
ATOM   2028  O   ILE A1058     -10.646 -28.250  62.131  1.00 94.59           O  
ANISOU 2028  O   ILE A1058    13537  14021   8382    910  -1254   -968       O  
ATOM   2029  CB  ILE A1058     -10.148 -30.468  64.626  1.00 92.69           C  
ANISOU 2029  CB  ILE A1058    13304  13220   8694    734  -1286  -1037       C  
ATOM   2030  CG1 ILE A1058      -9.850 -29.189  65.429  1.00 90.84           C  
ANISOU 2030  CG1 ILE A1058    12944  13071   8501    688  -1224   -789       C  
ATOM   2031  CG2 ILE A1058      -9.437 -31.681  65.217  1.00 94.53           C  
ANISOU 2031  CG2 ILE A1058    13610  13225   9081    792  -1249  -1091       C  
ATOM   2032  CD1 ILE A1058     -11.038 -28.452  65.868  1.00 95.79           C  
ANISOU 2032  CD1 ILE A1058    13516  13727   9153    541  -1308   -715       C  
ATOM   2033  N   THR A1059     -12.100 -29.989  62.159  1.00 93.19           N  
ANISOU 2033  N   THR A1059    13424  13658   8327    764  -1501  -1337       N  
ATOM   2034  CA  THR A1059     -13.214 -29.258  61.545  1.00 93.42           C  
ANISOU 2034  CA  THR A1059    13411  13894   8190    756  -1626  -1361       C  
ATOM   2035  C   THR A1059     -13.981 -28.490  62.634  1.00 95.09           C  
ANISOU 2035  C   THR A1059    13501  14068   8562    602  -1663  -1186       C  
ATOM   2036  O   THR A1059     -13.755 -28.731  63.822  1.00 93.39           O  
ANISOU 2036  O   THR A1059    13251  13657   8574    485  -1611  -1093       O  
ATOM   2037  CB  THR A1059     -14.104 -30.177  60.675  1.00103.00           C  
ANISOU 2037  CB  THR A1059    14666  15156   9315    742  -1800  -1695       C  
ATOM   2038  OG1 THR A1059     -14.973 -30.965  61.491  1.00102.54           O  
ANISOU 2038  OG1 THR A1059    14550  14892   9519    518  -1894  -1822       O  
ATOM   2039  CG2 THR A1059     -13.305 -31.058  59.712  1.00103.65           C  
ANISOU 2039  CG2 THR A1059    14887  15238   9258    895  -1754  -1901       C  
ATOM   2040  N   LYS A1060     -14.868 -27.561  62.231  1.00 91.48           N  
ANISOU 2040  N   LYS A1060    12986  13807   7965    632  -1750  -1137       N  
ATOM   2041  CA  LYS A1060     -15.655 -26.724  63.141  1.00 89.37           C  
ANISOU 2041  CA  LYS A1060    12603  13535   7820    523  -1780   -982       C  
ATOM   2042  C   LYS A1060     -16.596 -27.522  64.061  1.00 92.19           C  
ANISOU 2042  C   LYS A1060    12869  13738   8421    306  -1873  -1106       C  
ATOM   2043  O   LYS A1060     -16.705 -27.191  65.240  1.00 89.67           O  
ANISOU 2043  O   LYS A1060    12488  13305   8278    195  -1816   -954       O  
ATOM   2044  CB  LYS A1060     -16.414 -25.653  62.352  1.00 92.80           C  
ANISOU 2044  CB  LYS A1060    13011  14221   8028    656  -1861   -925       C  
ATOM   2045  CG  LYS A1060     -16.887 -24.493  63.202  1.00101.83           C  
ANISOU 2045  CG  LYS A1060    14066  15359   9265    614  -1831   -707       C  
ATOM   2046  CD  LYS A1060     -18.109 -23.860  62.595  1.00112.67           C  
ANISOU 2046  CD  LYS A1060    15375  16957  10479    718  -1985   -739       C  
ATOM   2047  CE  LYS A1060     -18.809 -23.007  63.608  1.00123.17           C  
ANISOU 2047  CE  LYS A1060    16591  18249  11961    645  -1980   -592       C  
ATOM   2048  NZ  LYS A1060     -19.800 -22.118  62.972  1.00134.72           N  
ANISOU 2048  NZ  LYS A1060    18007  19940  13241    821  -2098   -559       N  
ATOM   2049  N   ASP A1061     -17.262 -28.567  63.527  1.00 90.80           N  
ANISOU 2049  N   ASP A1061    12689  13554   8256    239  -1999  -1388       N  
ATOM   2050  CA  ASP A1061     -18.166 -29.435  64.292  1.00 90.91           C  
ANISOU 2050  CA  ASP A1061    12621  13399   8522      3  -2054  -1528       C  
ATOM   2051  C   ASP A1061     -17.386 -30.179  65.375  1.00 91.82           C  
ANISOU 2051  C   ASP A1061    12828  13203   8857    -89  -1907  -1431       C  
ATOM   2052  O   ASP A1061     -17.916 -30.409  66.464  1.00 90.99           O  
ANISOU 2052  O   ASP A1061    12667  12944   8961   -262  -1871  -1371       O  
ATOM   2053  CB  ASP A1061     -18.878 -30.440  63.366  1.00 96.17           C  
ANISOU 2053  CB  ASP A1061    13273  14104   9162    -57  -2206  -1891       C  
ATOM   2054  CG  ASP A1061     -19.953 -29.827  62.496  1.00109.68           C  
ANISOU 2054  CG  ASP A1061    14845  16143  10685      9  -2399  -2025       C  
ATOM   2055  OD1 ASP A1061     -21.027 -29.483  63.034  1.00110.73           O  
ANISOU 2055  OD1 ASP A1061    14797  16340  10937   -116  -2467  -2020       O  
ATOM   2056  OD2 ASP A1061     -19.731 -29.713  61.273  1.00117.49           O  
ANISOU 2056  OD2 ASP A1061    15904  17341  11395    204  -2483  -2139       O  
ATOM   2057  N   GLU A1062     -16.119 -30.533  65.071  1.00 86.72           N  
ANISOU 2057  N   GLU A1062    12319  12482   8147     51  -1816  -1406       N  
ATOM   2058  CA  GLU A1062     -15.203 -31.213  65.986  1.00 85.26           C  
ANISOU 2058  CA  GLU A1062    12230  12040   8126     42  -1690  -1306       C  
ATOM   2059  C   GLU A1062     -14.801 -30.256  67.119  1.00 85.62           C  
ANISOU 2059  C   GLU A1062    12213  12096   8223     45  -1605  -1017       C  
ATOM   2060  O   GLU A1062     -14.701 -30.682  68.270  1.00 84.50           O  
ANISOU 2060  O   GLU A1062    12096  11763   8246    -33  -1545   -920       O  
ATOM   2061  CB  GLU A1062     -13.979 -31.752  65.230  1.00 87.48           C  
ANISOU 2061  CB  GLU A1062    12638  12298   8304    230  -1628  -1381       C  
ATOM   2062  CG  GLU A1062     -14.331 -32.832  64.217  1.00 98.58           C  
ANISOU 2062  CG  GLU A1062    14131  13652   9673    226  -1706  -1701       C  
ATOM   2063  CD  GLU A1062     -13.208 -33.374  63.353  1.00112.32           C  
ANISOU 2063  CD  GLU A1062    15999  15391  11285    433  -1642  -1811       C  
ATOM   2064  OE1 GLU A1062     -12.242 -32.627  63.077  1.00 90.58           O  
ANISOU 2064  OE1 GLU A1062    13232  12802   8384    604  -1552  -1656       O  
ATOM   2065  OE2 GLU A1062     -13.321 -34.540  62.907  1.00109.04           O  
ANISOU 2065  OE2 GLU A1062    15694  14812  10923    417  -1671  -2070       O  
ATOM   2066  N   ALA A1063     -14.636 -28.953  66.790  1.00 80.34           N  
ANISOU 2066  N   ALA A1063    11474  11646   7406    135  -1598   -887       N  
ATOM   2067  CA  ALA A1063     -14.322 -27.875  67.734  1.00 77.51           C  
ANISOU 2067  CA  ALA A1063    11048  11317   7086    129  -1527   -653       C  
ATOM   2068  C   ALA A1063     -15.514 -27.609  68.650  1.00 79.42           C  
ANISOU 2068  C   ALA A1063    11201  11529   7445    -29  -1572   -609       C  
ATOM   2069  O   ALA A1063     -15.307 -27.258  69.812  1.00 78.19           O  
ANISOU 2069  O   ALA A1063    11021  11304   7382    -73  -1511   -460       O  
ATOM   2070  CB  ALA A1063     -13.945 -26.603  66.986  1.00 77.87           C  
ANISOU 2070  CB  ALA A1063    11066  11563   6956    252  -1488   -550       C  
ATOM   2071  N   GLU A1064     -16.755 -27.781  68.127  1.00 75.82           N  
ANISOU 2071  N   GLU A1064    10682  11148   6977   -105  -1680   -757       N  
ATOM   2072  CA  GLU A1064     -17.997 -27.631  68.888  1.00 75.10           C  
ANISOU 2072  CA  GLU A1064    10473  11052   7009   -261  -1714   -753       C  
ATOM   2073  C   GLU A1064     -18.067 -28.720  69.969  1.00 78.61           C  
ANISOU 2073  C   GLU A1064    10966  11242   7659   -416  -1640   -754       C  
ATOM   2074  O   GLU A1064     -18.406 -28.413  71.115  1.00 77.48           O  
ANISOU 2074  O   GLU A1064    10779  11049   7610   -498  -1577   -619       O  
ATOM   2075  CB  GLU A1064     -19.219 -27.714  67.967  1.00 78.39           C  
ANISOU 2075  CB  GLU A1064    10781  11632   7372   -298  -1860   -958       C  
ATOM   2076  CG  GLU A1064     -19.894 -26.381  67.704  1.00 89.81           C  
ANISOU 2076  CG  GLU A1064    12111  13317   8697   -203  -1924   -875       C  
ATOM   2077  CD  GLU A1064     -20.844 -26.390  66.522  1.00120.19           C  
ANISOU 2077  CD  GLU A1064    15862  17393  12410   -146  -2099  -1081       C  
ATOM   2078  OE1 GLU A1064     -20.363 -26.421  65.364  1.00112.58           O  
ANISOU 2078  OE1 GLU A1064    14992  16542  11244     11  -2153  -1154       O  
ATOM   2079  OE2 GLU A1064     -22.075 -26.357  66.755  1.00120.83           O  
ANISOU 2079  OE2 GLU A1064    15766  17566  12580   -247  -2185  -1177       O  
ATOM   2080  N   LYS A1065     -17.701 -29.978  69.612  1.00 75.58           N  
ANISOU 2080  N   LYS A1065    10698  10686   7332   -437  -1631   -894       N  
ATOM   2081  CA  LYS A1065     -17.687 -31.114  70.537  1.00 75.88           C  
ANISOU 2081  CA  LYS A1065    10836  10435   7560   -556  -1537   -878       C  
ATOM   2082  C   LYS A1065     -16.736 -30.842  71.706  1.00 77.81           C  
ANISOU 2082  C   LYS A1065    11154  10600   7810   -464  -1434   -630       C  
ATOM   2083  O   LYS A1065     -17.115 -31.048  72.862  1.00 77.37           O  
ANISOU 2083  O   LYS A1065    11114  10421   7863   -563  -1355   -514       O  
ATOM   2084  CB  LYS A1065     -17.312 -32.416  69.809  1.00 80.37           C  
ANISOU 2084  CB  LYS A1065    11545  10820   8173   -546  -1540  -1077       C  
ATOM   2085  CG  LYS A1065     -17.688 -33.681  70.585  1.00 96.65           C  
ANISOU 2085  CG  LYS A1065    13716  12545  10464   -714  -1439  -1103       C  
ATOM   2086  CD  LYS A1065     -17.293 -34.959  69.853  1.00107.45           C  
ANISOU 2086  CD  LYS A1065    15246  13689  11891   -693  -1431  -1314       C  
ATOM   2087  CE  LYS A1065     -15.983 -35.548  70.321  1.00111.78           C  
ANISOU 2087  CE  LYS A1065    15996  14032  12443   -501  -1330  -1172       C  
ATOM   2088  NZ  LYS A1065     -16.111 -36.222  71.642  1.00119.00           N  
ANISOU 2088  NZ  LYS A1065    17035  14649  13530   -583  -1187   -993       N  
ATOM   2089  N   LEU A1066     -15.527 -30.333  71.407  1.00 72.96           N  
ANISOU 2089  N   LEU A1066    10568  10083   7070   -275  -1432   -557       N  
ATOM   2090  CA  LEU A1066     -14.525 -29.997  72.421  1.00 71.35           C  
ANISOU 2090  CA  LEU A1066    10394   9859   6857   -172  -1367   -365       C  
ATOM   2091  C   LEU A1066     -15.017 -28.872  73.340  1.00 75.20           C  
ANISOU 2091  C   LEU A1066    10775  10460   7339   -235  -1357   -224       C  
ATOM   2092  O   LEU A1066     -14.777 -28.929  74.547  1.00 74.74           O  
ANISOU 2092  O   LEU A1066    10752  10330   7315   -230  -1305    -93       O  
ATOM   2093  CB  LEU A1066     -13.175 -29.625  71.777  1.00 70.40           C  
ANISOU 2093  CB  LEU A1066    10273   9851   6625     15  -1362   -357       C  
ATOM   2094  CG  LEU A1066     -12.458 -30.716  70.975  1.00 76.00           C  
ANISOU 2094  CG  LEU A1066    11094  10457   7326    128  -1351   -488       C  
ATOM   2095  CD1 LEU A1066     -11.267 -30.151  70.252  1.00 75.60           C  
ANISOU 2095  CD1 LEU A1066    10996  10573   7157    295  -1324   -482       C  
ATOM   2096  CD2 LEU A1066     -12.030 -31.895  71.856  1.00 79.04           C  
ANISOU 2096  CD2 LEU A1066    11616  10592   7824    176  -1300   -441       C  
ATOM   2097  N   PHE A1067     -15.742 -27.881  72.766  1.00 71.83           N  
ANISOU 2097  N   PHE A1067    10230  10209   6852   -273  -1407   -256       N  
ATOM   2098  CA  PHE A1067     -16.318 -26.734  73.475  1.00 70.71           C  
ANISOU 2098  CA  PHE A1067     9988  10175   6704   -316  -1398   -151       C  
ATOM   2099  C   PHE A1067     -17.431 -27.158  74.434  1.00 76.83           C  
ANISOU 2099  C   PHE A1067    10737  10864   7592   -468  -1360   -134       C  
ATOM   2100  O   PHE A1067     -17.467 -26.680  75.569  1.00 76.21           O  
ANISOU 2100  O   PHE A1067    10647  10787   7522   -479  -1305    -11       O  
ATOM   2101  CB  PHE A1067     -16.856 -25.690  72.478  1.00 71.94           C  
ANISOU 2101  CB  PHE A1067    10050  10520   6765   -278  -1459   -192       C  
ATOM   2102  CG  PHE A1067     -17.630 -24.559  73.117  1.00 72.02           C  
ANISOU 2102  CG  PHE A1067     9961  10620   6783   -309  -1449   -107       C  
ATOM   2103  CD1 PHE A1067     -16.970 -23.452  73.642  1.00 73.26           C  
ANISOU 2103  CD1 PHE A1067    10116  10812   6907   -244  -1397     14       C  
ATOM   2104  CD2 PHE A1067     -19.016 -24.606  73.208  1.00 74.17           C  
ANISOU 2104  CD2 PHE A1067    10129  10941   7110   -405  -1486   -170       C  
ATOM   2105  CE1 PHE A1067     -17.683 -22.414  74.236  1.00 73.31           C  
ANISOU 2105  CE1 PHE A1067    10050  10879   6925   -258  -1380     74       C  
ATOM   2106  CE2 PHE A1067     -19.726 -23.571  73.808  1.00 76.17           C  
ANISOU 2106  CE2 PHE A1067    10288  11281   7371   -405  -1467    -99       C  
ATOM   2107  CZ  PHE A1067     -19.055 -22.482  74.314  1.00 72.94           C  
ANISOU 2107  CZ  PHE A1067     9911  10884   6919   -323  -1414     24       C  
ATOM   2108  N   ASN A1068     -18.364 -28.003  73.959  1.00 75.43           N  
ANISOU 2108  N   ASN A1068    10537  10623   7498   -593  -1383   -273       N  
ATOM   2109  CA  ASN A1068     -19.484 -28.492  74.754  1.00 76.67           C  
ANISOU 2109  CA  ASN A1068    10649  10692   7792   -773  -1316   -275       C  
ATOM   2110  C   ASN A1068     -19.001 -29.312  75.946  1.00 82.83           C  
ANISOU 2110  C   ASN A1068    11586  11251   8636   -790  -1189   -138       C  
ATOM   2111  O   ASN A1068     -19.690 -29.360  76.963  1.00 83.45           O  
ANISOU 2111  O   ASN A1068    11647  11284   8779   -894  -1089    -49       O  
ATOM   2112  CB  ASN A1068     -20.457 -29.282  73.883  1.00 78.67           C  
ANISOU 2112  CB  ASN A1068    10828  10920   8144   -921  -1370   -495       C  
ATOM   2113  CG  ASN A1068     -21.311 -28.437  72.963  1.00 96.54           C  
ANISOU 2113  CG  ASN A1068    12901  13444  10337   -905  -1501   -620       C  
ATOM   2114  OD1 ASN A1068     -21.382 -27.203  73.065  1.00 85.31           O  
ANISOU 2114  OD1 ASN A1068    11401  12199   8815   -799  -1527   -520       O  
ATOM   2115  ND2 ASN A1068     -22.014 -29.096  72.057  1.00 90.71           N  
ANISOU 2115  ND2 ASN A1068    12084  12731   9650  -1003  -1590   -853       N  
ATOM   2116  N   GLN A1069     -17.806 -29.928  75.832  1.00 80.37           N  
ANISOU 2116  N   GLN A1069    11429  10818   8289   -661  -1186   -109       N  
ATOM   2117  CA  GLN A1069     -17.164 -30.683  76.906  1.00 81.37           C  
ANISOU 2117  CA  GLN A1069    11728  10753   8436   -601  -1088     41       C  
ATOM   2118  C   GLN A1069     -16.671 -29.684  77.957  1.00 84.95           C  
ANISOU 2118  C   GLN A1069    12152  11350   8773   -492  -1082    206       C  
ATOM   2119  O   GLN A1069     -16.851 -29.915  79.156  1.00 85.55           O  
ANISOU 2119  O   GLN A1069    12307  11353   8847   -503   -989    345       O  
ATOM   2120  CB  GLN A1069     -15.976 -31.495  76.364  1.00 83.38           C  
ANISOU 2120  CB  GLN A1069    12124  10886   8672   -444  -1112      3       C  
ATOM   2121  CG  GLN A1069     -16.364 -32.795  75.658  1.00102.18           C  
ANISOU 2121  CG  GLN A1069    14607  13029  11186   -543  -1081   -150       C  
ATOM   2122  CD  GLN A1069     -15.187 -33.531  75.051  1.00123.46           C  
ANISOU 2122  CD  GLN A1069    17439  15616  13854   -358  -1102   -207       C  
ATOM   2123  OE1 GLN A1069     -15.333 -34.263  74.067  1.00120.96           O  
ANISOU 2123  OE1 GLN A1069    17169  15191  13599   -399  -1123   -400       O  
ATOM   2124  NE2 GLN A1069     -13.997 -33.389  75.627  1.00115.11           N  
ANISOU 2124  NE2 GLN A1069    16438  14593  12704   -140  -1101    -63       N  
ATOM   2125  N   ASP A1070     -16.070 -28.560  77.491  1.00 79.96           N  
ANISOU 2125  N   ASP A1070    11415  10921   8044   -393  -1170    182       N  
ATOM   2126  CA  ASP A1070     -15.549 -27.477  78.326  1.00 78.57           C  
ANISOU 2126  CA  ASP A1070    11188  10890   7775   -308  -1181    280       C  
ATOM   2127  C   ASP A1070     -16.658 -26.734  79.054  1.00 81.38           C  
ANISOU 2127  C   ASP A1070    11463  11322   8136   -413  -1137    321       C  
ATOM   2128  O   ASP A1070     -16.458 -26.349  80.202  1.00 81.24           O  
ANISOU 2128  O   ASP A1070    11469  11344   8054   -367  -1104    417       O  
ATOM   2129  CB  ASP A1070     -14.696 -26.498  77.501  1.00 79.69           C  
ANISOU 2129  CB  ASP A1070    11240  11185   7854   -217  -1252    226       C  
ATOM   2130  CG  ASP A1070     -13.395 -27.074  76.961  1.00 95.96           C  
ANISOU 2130  CG  ASP A1070    13352  13215   9893    -82  -1276    195       C  
ATOM   2131  OD1 ASP A1070     -12.836 -27.996  77.606  1.00 98.92           O  
ANISOU 2131  OD1 ASP A1070    13833  13479  10272      4  -1260    249       O  
ATOM   2132  OD2 ASP A1070     -12.911 -26.571  75.921  1.00101.90           O  
ANISOU 2132  OD2 ASP A1070    14041  14061  10614    -40  -1301    128       O  
ATOM   2133  N   VAL A1071     -17.821 -26.538  78.398  1.00 77.09           N  
ANISOU 2133  N   VAL A1071    10814  10820   7658   -536  -1143    235       N  
ATOM   2134  CA  VAL A1071     -18.987 -25.876  78.995  1.00 76.36           C  
ANISOU 2134  CA  VAL A1071    10614  10813   7587   -626  -1093    255       C  
ATOM   2135  C   VAL A1071     -19.594 -26.751  80.090  1.00 82.18           C  
ANISOU 2135  C   VAL A1071    11423  11421   8381   -727   -959    339       C  
ATOM   2136  O   VAL A1071     -19.910 -26.236  81.163  1.00 81.81           O  
ANISOU 2136  O   VAL A1071    11367  11434   8284   -721   -885    427       O  
ATOM   2137  CB  VAL A1071     -20.012 -25.372  77.938  1.00 79.48           C  
ANISOU 2137  CB  VAL A1071    10847  11328   8022   -687  -1158    130       C  
ATOM   2138  CG1 VAL A1071     -21.433 -25.297  78.489  1.00 80.06           C  
ANISOU 2138  CG1 VAL A1071    10794  11449   8177   -816  -1086    117       C  
ATOM   2139  CG2 VAL A1071     -19.590 -24.016  77.405  1.00 77.74           C  
ANISOU 2139  CG2 VAL A1071    10574  11256   7709   -560  -1231    133       C  
ATOM   2140  N   ASP A1072     -19.707 -28.072  79.841  1.00 80.47           N  
ANISOU 2140  N   ASP A1072    11299  11011   8263   -813   -909    315       N  
ATOM   2141  CA  ASP A1072     -20.224 -29.015  80.830  1.00 82.47           C  
ANISOU 2141  CA  ASP A1072    11660  11089   8586   -918   -740    420       C  
ATOM   2142  C   ASP A1072     -19.311 -29.007  82.050  1.00 85.44           C  
ANISOU 2142  C   ASP A1072    12206  11442   8817   -751   -692    607       C  
ATOM   2143  O   ASP A1072     -19.806 -28.999  83.175  1.00 85.73           O  
ANISOU 2143  O   ASP A1072    12285  11475   8813   -779   -559    731       O  
ATOM   2144  CB  ASP A1072     -20.376 -30.421  80.230  1.00 86.91           C  
ANISOU 2144  CB  ASP A1072    12318  11403   9302  -1036   -691    345       C  
ATOM   2145  CG  ASP A1072     -21.553 -30.594  79.270  1.00105.34           C  
ANISOU 2145  CG  ASP A1072    14466  13764  11795  -1247   -718    137       C  
ATOM   2146  OD1 ASP A1072     -22.124 -29.564  78.823  1.00105.11           O  
ANISOU 2146  OD1 ASP A1072    14229  13977  11732  -1250   -815     48       O  
ATOM   2147  OD2 ASP A1072     -21.892 -31.756  78.951  1.00116.80           O  
ANISOU 2147  OD2 ASP A1072    15980  14993  13405  -1398   -648     51       O  
ATOM   2148  N   ALA A1073     -17.981 -28.900  81.811  1.00 80.47           N  
ANISOU 2148  N   ALA A1073    11645  10840   8091   -563   -808    612       N  
ATOM   2149  CA  ALA A1073     -16.944 -28.799  82.833  1.00 79.88           C  
ANISOU 2149  CA  ALA A1073    11687  10804   7859   -367   -822    743       C  
ATOM   2150  C   ALA A1073     -17.074 -27.460  83.557  1.00 83.58           C  
ANISOU 2150  C   ALA A1073    12047  11497   8215   -336   -850    752       C  
ATOM   2151  O   ALA A1073     -16.951 -27.428  84.777  1.00 84.31           O  
ANISOU 2151  O   ALA A1073    12230  11624   8179   -251   -796    868       O  
ATOM   2152  CB  ALA A1073     -15.571 -28.921  82.195  1.00 79.77           C  
ANISOU 2152  CB  ALA A1073    11696  10806   7807   -199   -950    693       C  
ATOM   2153  N   ALA A1074     -17.367 -26.364  82.809  1.00 79.53           N  
ANISOU 2153  N   ALA A1074    11356  11125   7738   -391   -925    629       N  
ATOM   2154  CA  ALA A1074     -17.565 -25.011  83.353  1.00 78.79           C  
ANISOU 2154  CA  ALA A1074    11161  11207   7570   -370   -942    608       C  
ATOM   2155  C   ALA A1074     -18.828 -24.951  84.205  1.00 85.07           C  
ANISOU 2155  C   ALA A1074    11939  12017   8366   -465   -805    664       C  
ATOM   2156  O   ALA A1074     -18.855 -24.221  85.192  1.00 85.48           O  
ANISOU 2156  O   ALA A1074    11993  12178   8306   -404   -778    693       O  
ATOM   2157  CB  ALA A1074     -17.643 -23.986  82.232  1.00 78.01           C  
ANISOU 2157  CB  ALA A1074    10914  11200   7525   -394  -1027    489       C  
ATOM   2158  N   VAL A1075     -19.863 -25.727  83.828  1.00 82.68           N  
ANISOU 2158  N   VAL A1075    11608  11611   8195   -619   -712    659       N  
ATOM   2159  CA  VAL A1075     -21.120 -25.846  84.563  1.00 84.02           C  
ANISOU 2159  CA  VAL A1075    11735  11787   8403   -740   -545    708       C  
ATOM   2160  C   VAL A1075     -20.844 -26.662  85.842  1.00 90.45           C  
ANISOU 2160  C   VAL A1075    12760  12497   9110   -687   -403    889       C  
ATOM   2161  O   VAL A1075     -21.157 -26.185  86.935  1.00 91.06           O  
ANISOU 2161  O   VAL A1075    12859  12677   9064   -642   -309    962       O  
ATOM   2162  CB  VAL A1075     -22.241 -26.426  83.659  1.00 88.94           C  
ANISOU 2162  CB  VAL A1075    12221  12344   9226   -941   -502    609       C  
ATOM   2163  CG1 VAL A1075     -23.362 -27.072  84.467  1.00 91.07           C  
ANISOU 2163  CG1 VAL A1075    12481  12544   9578  -1104   -277    682       C  
ATOM   2164  CG2 VAL A1075     -22.800 -25.344  82.739  1.00 87.70           C  
ANISOU 2164  CG2 VAL A1075    11843  12367   9111   -944   -622    460       C  
ATOM   2165  N   ARG A1076     -20.178 -27.841  85.709  1.00 87.61           N  
ANISOU 2165  N   ARG A1076    12576  11941   8770   -655   -392    963       N  
ATOM   2166  CA  ARG A1076     -19.775 -28.706  86.825  1.00 88.96           C  
ANISOU 2166  CA  ARG A1076    12993  11989   8820   -551   -268   1164       C  
ATOM   2167  C   ARG A1076     -18.564 -28.051  87.512  1.00 92.32           C  
ANISOU 2167  C   ARG A1076    13484  12584   9011   -296   -410   1197       C  
ATOM   2168  O   ARG A1076     -17.450 -28.584  87.494  1.00 92.60           O  
ANISOU 2168  O   ARG A1076    13645  12563   8977   -129   -502   1242       O  
ATOM   2169  CB  ARG A1076     -19.420 -30.124  86.330  1.00 89.64           C  
ANISOU 2169  CB  ARG A1076    13247  11791   9022   -572   -224   1215       C  
ATOM   2170  CG  ARG A1076     -20.589 -30.939  85.788  1.00101.58           C  
ANISOU 2170  CG  ARG A1076    14714  13102  10780   -847    -66   1166       C  
ATOM   2171  CD  ARG A1076     -20.210 -32.403  85.663  1.00114.14           C  
ANISOU 2171  CD  ARG A1076    16546  14359  12464   -846     31   1254       C  
ATOM   2172  NE  ARG A1076     -20.727 -33.026  84.443  1.00122.93           N  
ANISOU 2172  NE  ARG A1076    17568  15309  13830  -1062     22   1065       N  
ATOM   2173  CZ  ARG A1076     -19.997 -33.275  83.359  1.00136.27           C  
ANISOU 2173  CZ  ARG A1076    19260  16951  15565   -994   -145    922       C  
ATOM   2174  NH1 ARG A1076     -18.712 -32.943  83.324  1.00119.68           N  
ANISOU 2174  NH1 ARG A1076    17223  14953  13297   -728   -305    954       N  
ATOM   2175  NH2 ARG A1076     -20.547 -33.854  82.300  1.00125.38           N  
ANISOU 2175  NH2 ARG A1076    17805  15439  14396  -1192   -152    727       N  
ATOM   2176  N   GLY A1077     -18.808 -26.871  88.070  1.00 87.75           N  
ANISOU 2176  N   GLY A1077    12798  12220   8325   -269   -435   1145       N  
ATOM   2177  CA  GLY A1077     -17.821 -26.032  88.735  1.00 86.67           C  
ANISOU 2177  CA  GLY A1077    12671  12275   7986    -73   -576   1112       C  
ATOM   2178  C   GLY A1077     -18.497 -24.834  89.359  1.00 89.04           C  
ANISOU 2178  C   GLY A1077    12865  12756   8211    -99   -538   1042       C  
ATOM   2179  O   GLY A1077     -18.273 -24.543  90.538  1.00 89.90           O  
ANISOU 2179  O   GLY A1077    13065  12990   8103     35   -522   1089       O  
ATOM   2180  N   ILE A1078     -19.356 -24.149  88.571  1.00 83.25           N  
ANISOU 2180  N   ILE A1078    11945  12042   7644   -250   -526    926       N  
ATOM   2181  CA  ILE A1078     -20.167 -23.013  89.012  1.00 82.30           C  
ANISOU 2181  CA  ILE A1078    11710  12065   7494   -274   -472    850       C  
ATOM   2182  C   ILE A1078     -21.126 -23.553  90.095  1.00 88.79           C  
ANISOU 2182  C   ILE A1078    12617  12886   8234   -308   -241    989       C  
ATOM   2183  O   ILE A1078     -21.283 -22.929  91.152  1.00 89.73           O  
ANISOU 2183  O   ILE A1078    12772  13146   8176   -216   -182    991       O  
ATOM   2184  CB  ILE A1078     -20.909 -22.362  87.802  1.00 83.37           C  
ANISOU 2184  CB  ILE A1078    11640  12206   7833   -395   -509    723       C  
ATOM   2185  CG1 ILE A1078     -19.913 -21.596  86.893  1.00 81.84           C  
ANISOU 2185  CG1 ILE A1078    11390  12030   7674   -336   -700    606       C  
ATOM   2186  CG2 ILE A1078     -22.030 -21.432  88.270  1.00 83.96           C  
ANISOU 2186  CG2 ILE A1078    11596  12401   7904   -415   -406    672       C  
ATOM   2187  CD1 ILE A1078     -20.395 -21.296  85.464  1.00 88.80           C  
ANISOU 2187  CD1 ILE A1078    12127  12886   8727   -418   -755    524       C  
ATOM   2188  N   LEU A1079     -21.687 -24.762  89.847  1.00 85.62           N  
ANISOU 2188  N   LEU A1079    12263  12314   7954   -440    -98   1102       N  
ATOM   2189  CA  LEU A1079     -22.594 -25.479  90.743  1.00 87.41           C  
ANISOU 2189  CA  LEU A1079    12577  12486   8147   -514    171   1260       C  
ATOM   2190  C   LEU A1079     -21.923 -25.878  92.066  1.00 92.44           C  
ANISOU 2190  C   LEU A1079    13482  13145   8498   -318    238   1440       C  
ATOM   2191  O   LEU A1079     -22.612 -26.018  93.077  1.00 94.08           O  
ANISOU 2191  O   LEU A1079    13769  13393   8584   -318    462   1564       O  
ATOM   2192  CB  LEU A1079     -23.196 -26.709  90.037  1.00 88.46           C  
ANISOU 2192  CB  LEU A1079    12703  12387   8520   -726    298   1311       C  
ATOM   2193  CG  LEU A1079     -24.016 -26.452  88.762  1.00 91.65           C  
ANISOU 2193  CG  LEU A1079    12834  12800   9190   -919    236   1123       C  
ATOM   2194  CD1 LEU A1079     -24.203 -27.727  87.985  1.00 92.85           C  
ANISOU 2194  CD1 LEU A1079    13013  12710   9554  -1097    288   1126       C  
ATOM   2195  CD2 LEU A1079     -25.368 -25.816  89.073  1.00 94.90           C  
ANISOU 2195  CD2 LEU A1079    13030  13365   9664  -1027    385   1066       C  
ATOM   2196  N   ARG A1080     -20.588 -26.054  92.058  1.00 88.03           N  
ANISOU 2196  N   ARG A1080    13050  12580   7816   -135     45   1452       N  
ATOM   2197  CA  ARG A1080     -19.806 -26.383  93.255  1.00 89.40           C  
ANISOU 2197  CA  ARG A1080    13465  12820   7683    108     45   1602       C  
ATOM   2198  C   ARG A1080     -19.477 -25.103  94.012  1.00 92.74           C  
ANISOU 2198  C   ARG A1080    13830  13523   7884    256    -78   1465       C  
ATOM   2199  O   ARG A1080     -19.420 -25.124  95.244  1.00 94.96           O  
ANISOU 2199  O   ARG A1080    14274  13929   7879    420     -2   1566       O  
ATOM   2200  CB  ARG A1080     -18.500 -27.105  92.894  1.00 88.49           C  
ANISOU 2200  CB  ARG A1080    13471  12609   7541    264   -130   1644       C  
ATOM   2201  CG  ARG A1080     -18.686 -28.521  92.382  1.00 98.17           C  
ANISOU 2201  CG  ARG A1080    14837  13527   8938    174      8   1800       C  
ATOM   2202  CD  ARG A1080     -17.431 -29.354  92.570  1.00109.72           C  
ANISOU 2202  CD  ARG A1080    16509  14913  10267    429   -103   1918       C  
ATOM   2203  NE  ARG A1080     -16.269 -28.805  91.866  1.00116.52           N  
ANISOU 2203  NE  ARG A1080    17222  15902  11149    535   -396   1727       N  
ATOM   2204  CZ  ARG A1080     -15.950 -29.085  90.606  1.00129.77           C  
ANISOU 2204  CZ  ARG A1080    18801  17449  13057    444   -485   1620       C  
ATOM   2205  NH1 ARG A1080     -16.712 -29.899  89.885  1.00117.27           N  
ANISOU 2205  NH1 ARG A1080    17248  15605  11704    243   -334   1656       N  
ATOM   2206  NH2 ARG A1080     -14.870 -28.549  90.055  1.00115.57           N  
ANISOU 2206  NH2 ARG A1080    16866  15786  11259    546   -717   1461       N  
ATOM   2207  N   ASN A1081     -19.246 -23.994  93.271  1.00 86.38           N  
ANISOU 2207  N   ASN A1081    12810  12808   7203    203   -260   1231       N  
ATOM   2208  CA  ASN A1081     -18.924 -22.678  93.824  1.00 85.62           C  
ANISOU 2208  CA  ASN A1081    12639  12932   6960    303   -382   1050       C  
ATOM   2209  C   ASN A1081     -20.100 -22.117  94.630  1.00 90.59           C  
ANISOU 2209  C   ASN A1081    13253  13664   7502    272   -183   1049       C  
ATOM   2210  O   ASN A1081     -21.196 -21.930  94.088  1.00 89.69           O  
ANISOU 2210  O   ASN A1081    12997  13491   7590    103    -52   1028       O  
ATOM   2211  CB  ASN A1081     -18.492 -21.706  92.721  1.00 83.02           C  
ANISOU 2211  CB  ASN A1081    12106  12604   6833    224   -567    832       C  
ATOM   2212  CG  ASN A1081     -17.797 -20.471  93.240  1.00 99.28           C  
ANISOU 2212  CG  ASN A1081    14114  14840   8766    327   -721    629       C  
ATOM   2213  OD1 ASN A1081     -18.422 -19.550  93.781  1.00 92.07           O  
ANISOU 2213  OD1 ASN A1081    13164  14022   7796    327   -655    529       O  
ATOM   2214  ND2 ASN A1081     -16.483 -20.422  93.079  1.00 89.22           N  
ANISOU 2214  ND2 ASN A1081    12825  13613   7462    413   -923    543       N  
ATOM   2215  N   ALA A1082     -19.855 -21.868  95.935  1.00 88.67           N  
ANISOU 2215  N   ALA A1082    13149  13599   6942    457   -167   1061       N  
ATOM   2216  CA  ALA A1082     -20.819 -21.347  96.907  1.00 89.93           C  
ANISOU 2216  CA  ALA A1082    13331  13894   6944    484     29   1057       C  
ATOM   2217  C   ALA A1082     -21.428 -19.985  96.530  1.00 91.40           C  
ANISOU 2217  C   ALA A1082    13304  14142   7282    399      8    822       C  
ATOM   2218  O   ALA A1082     -22.605 -19.750  96.808  1.00 92.05           O  
ANISOU 2218  O   ALA A1082    13325  14260   7391    339    223    840       O  
ATOM   2219  CB  ALA A1082     -20.171 -21.270  98.282  1.00 93.18           C  
ANISOU 2219  CB  ALA A1082    13941  14514   6949    739    -18   1070       C  
ATOM   2220  N   LYS A1083     -20.631 -19.097  95.908  1.00 84.90           N  
ANISOU 2220  N   LYS A1083    12371  13323   6562    402   -230    610       N  
ATOM   2221  CA  LYS A1083     -21.069 -17.755  95.524  1.00 83.12           C  
ANISOU 2221  CA  LYS A1083    11985  13116   6481    352   -256    396       C  
ATOM   2222  C   LYS A1083     -21.519 -17.602  94.061  1.00 84.21           C  
ANISOU 2222  C   LYS A1083    11943  13096   6956    189   -274    380       C  
ATOM   2223  O   LYS A1083     -22.021 -16.537  93.685  1.00 83.96           O  
ANISOU 2223  O   LYS A1083    11790  13060   7049    169   -271    241       O  
ATOM   2224  CB  LYS A1083     -20.009 -16.706  95.929  1.00 85.48           C  
ANISOU 2224  CB  LYS A1083    12296  13517   6666    458   -463    155       C  
ATOM   2225  CG  LYS A1083     -20.532 -15.591  96.847  1.00101.71           C  
ANISOU 2225  CG  LYS A1083    14362  15702   8581    544   -391    -25       C  
ATOM   2226  CD  LYS A1083     -21.276 -16.108  98.099  1.00114.95           C  
ANISOU 2226  CD  LYS A1083    16178  17529   9969    655   -181    107       C  
ATOM   2227  CE  LYS A1083     -21.433 -15.066  99.178  1.00126.70           C  
ANISOU 2227  CE  LYS A1083    17718  19188  11233    793   -157   -107       C  
ATOM   2228  NZ  LYS A1083     -20.289 -15.082 100.130  1.00136.42           N  
ANISOU 2228  NZ  LYS A1083    19092  20597  12145    959   -341   -214       N  
ATOM   2229  N   LEU A1084     -21.377 -18.662  93.247  1.00 78.10           N  
ANISOU 2229  N   LEU A1084    11164  12194   6315     94   -289    519       N  
ATOM   2230  CA  LEU A1084     -21.784 -18.603  91.840  1.00 74.87           C  
ANISOU 2230  CA  LEU A1084    10595  11665   6187    -41   -323    496       C  
ATOM   2231  C   LEU A1084     -23.065 -19.361  91.532  1.00 77.70           C  
ANISOU 2231  C   LEU A1084    10869  11976   6677   -172   -140    608       C  
ATOM   2232  O   LEU A1084     -23.830 -18.915  90.673  1.00 75.95           O  
ANISOU 2232  O   LEU A1084    10473  11744   6641   -245   -138    538       O  
ATOM   2233  CB  LEU A1084     -20.647 -19.003  90.887  1.00 72.96           C  
ANISOU 2233  CB  LEU A1084    10364  11320   6036    -63   -504    493       C  
ATOM   2234  CG  LEU A1084     -19.505 -17.990  90.726  1.00 76.21           C  
ANISOU 2234  CG  LEU A1084    10758  11763   6435      3   -685    328       C  
ATOM   2235  CD1 LEU A1084     -18.439 -18.528  89.815  1.00 74.68           C  
ANISOU 2235  CD1 LEU A1084    10560  11487   6329    -19   -823    344       C  
ATOM   2236  CD2 LEU A1084     -20.001 -16.668  90.169  1.00 78.07           C  
ANISOU 2236  CD2 LEU A1084    10874  11980   6808    -25   -685    192       C  
ATOM   2237  N   LYS A1085     -23.301 -20.497  92.234  1.00 75.17           N  
ANISOU 2237  N   LYS A1085    10670  11628   6263   -199     18    779       N  
ATOM   2238  CA  LYS A1085     -24.500 -21.329  92.083  1.00 75.81           C  
ANISOU 2238  CA  LYS A1085    10671  11649   6485   -360    232    883       C  
ATOM   2239  C   LYS A1085     -25.796 -20.516  92.284  1.00 80.78           C  
ANISOU 2239  C   LYS A1085    11108  12411   7174   -389    375    797       C  
ATOM   2240  O   LYS A1085     -26.638 -20.570  91.383  1.00 79.70           O  
ANISOU 2240  O   LYS A1085    10762  12255   7265   -518    391    743       O  
ATOM   2241  CB  LYS A1085     -24.450 -22.579  92.992  1.00 79.63           C  
ANISOU 2241  CB  LYS A1085    11365  12057   6833   -366    419   1101       C  
ATOM   2242  CG  LYS A1085     -25.703 -23.453  92.931  1.00 87.24           C  
ANISOU 2242  CG  LYS A1085    12245  12934   7968   -573    687   1203       C  
ATOM   2243  CD  LYS A1085     -25.568 -24.717  93.757  1.00 97.53           C  
ANISOU 2243  CD  LYS A1085    13801  14103   9153   -580    896   1448       C  
ATOM   2244  CE  LYS A1085     -26.825 -25.558  93.752  1.00113.52           C  
ANISOU 2244  CE  LYS A1085    15735  16020  11378   -824   1203   1541       C  
ATOM   2245  NZ  LYS A1085     -27.630 -25.376  94.994  1.00122.07           N  
ANISOU 2245  NZ  LYS A1085    16850  17238  12295   -797   1503   1647       N  
ATOM   2246  N   PRO A1086     -25.964 -19.718  93.382  1.00 79.19           N  
ANISOU 2246  N   PRO A1086    10956  12360   6774   -252    459    758       N  
ATOM   2247  CA  PRO A1086     -27.208 -18.941  93.542  1.00 80.49           C  
ANISOU 2247  CA  PRO A1086    10926  12653   7005   -253    604    668       C  
ATOM   2248  C   PRO A1086     -27.521 -18.003  92.374  1.00 84.43           C  
ANISOU 2248  C   PRO A1086    11212  13153   7716   -252    448    504       C  
ATOM   2249  O   PRO A1086     -28.684 -17.903  91.967  1.00 84.48           O  
ANISOU 2249  O   PRO A1086    10991  13223   7886   -317    544    466       O  
ATOM   2250  CB  PRO A1086     -26.970 -18.167  94.844  1.00 83.29           C  
ANISOU 2250  CB  PRO A1086    11421  13149   7076    -66    659    618       C  
ATOM   2251  CG  PRO A1086     -26.006 -18.987  95.592  1.00 88.21           C  
ANISOU 2251  CG  PRO A1086    12304  13744   7468     -7    646    758       C  
ATOM   2252  CD  PRO A1086     -25.075 -19.503  94.544  1.00 81.49           C  
ANISOU 2252  CD  PRO A1086    11471  12732   6758    -75    427    776       C  
ATOM   2253  N   VAL A1087     -26.474 -17.340  91.827  1.00 80.46           N  
ANISOU 2253  N   VAL A1087    10777  12585   7207   -172    213    414       N  
ATOM   2254  CA  VAL A1087     -26.566 -16.417  90.687  1.00 79.26           C  
ANISOU 2254  CA  VAL A1087    10487  12403   7224   -141     64    293       C  
ATOM   2255  C   VAL A1087     -27.009 -17.209  89.460  1.00 83.98           C  
ANISOU 2255  C   VAL A1087    10939  12946   8025   -281     19    335       C  
ATOM   2256  O   VAL A1087     -27.977 -16.821  88.805  1.00 84.20           O  
ANISOU 2256  O   VAL A1087    10762  13040   8192   -279     24    272       O  
ATOM   2257  CB  VAL A1087     -25.233 -15.657  90.431  1.00 81.14           C  
ANISOU 2257  CB  VAL A1087    10855  12559   7414    -57   -134    209       C  
ATOM   2258  CG1 VAL A1087     -25.386 -14.628  89.313  1.00 79.64           C  
ANISOU 2258  CG1 VAL A1087    10559  12316   7383     -8   -239    117       C  
ATOM   2259  CG2 VAL A1087     -24.718 -14.989  91.705  1.00 82.04           C  
ANISOU 2259  CG2 VAL A1087    11112  12739   7321     61   -111    128       C  
ATOM   2260  N   TYR A1088     -26.327 -18.344  89.192  1.00 80.42           N  
ANISOU 2260  N   TYR A1088    10591  12386   7579   -386    -28    429       N  
ATOM   2261  CA  TYR A1088     -26.588 -19.246  88.072  1.00 79.98           C  
ANISOU 2261  CA  TYR A1088    10434  12256   7699   -529    -79    446       C  
ATOM   2262  C   TYR A1088     -27.992 -19.861  88.120  1.00 86.04           C  
ANISOU 2262  C   TYR A1088    11005  13088   8600   -673     98    452       C  
ATOM   2263  O   TYR A1088     -28.590 -20.058  87.061  1.00 85.98           O  
ANISOU 2263  O   TYR A1088    10809  13099   8762   -756     26    376       O  
ATOM   2264  CB  TYR A1088     -25.507 -20.332  88.015  1.00 80.58           C  
ANISOU 2264  CB  TYR A1088    10700  12185   7732   -583   -133    542       C  
ATOM   2265  CG  TYR A1088     -25.565 -21.216  86.788  1.00 82.06           C  
ANISOU 2265  CG  TYR A1088    10819  12271   8087   -713   -212    525       C  
ATOM   2266  CD1 TYR A1088     -24.998 -20.810  85.585  1.00 82.31           C  
ANISOU 2266  CD1 TYR A1088    10820  12283   8169   -666   -409    445       C  
ATOM   2267  CD2 TYR A1088     -26.142 -22.481  86.843  1.00 84.58           C  
ANISOU 2267  CD2 TYR A1088    11126  12502   8510   -886    -76    586       C  
ATOM   2268  CE1 TYR A1088     -25.028 -21.629  84.457  1.00 83.07           C  
ANISOU 2268  CE1 TYR A1088    10869  12306   8390   -767   -487    408       C  
ATOM   2269  CE2 TYR A1088     -26.184 -23.307  85.721  1.00 85.44           C  
ANISOU 2269  CE2 TYR A1088    11179  12509   8775  -1012   -155    531       C  
ATOM   2270  CZ  TYR A1088     -25.632 -22.874  84.528  1.00 89.99           C  
ANISOU 2270  CZ  TYR A1088    11721  13098   9372   -941   -372    434       C  
ATOM   2271  OH  TYR A1088     -25.678 -23.681  83.417  1.00 88.71           O  
ANISOU 2271  OH  TYR A1088    11513  12857   9337  -1048   -455    357       O  
ATOM   2272  N   ASP A1089     -28.515 -20.153  89.337  1.00 84.00           N  
ANISOU 2272  N   ASP A1089    10780  12878   8259   -702    331    533       N  
ATOM   2273  CA  ASP A1089     -29.857 -20.714  89.538  1.00 85.99           C  
ANISOU 2273  CA  ASP A1089    10827  13197   8647   -861    552    541       C  
ATOM   2274  C   ASP A1089     -30.944 -19.705  89.161  1.00 90.39           C  
ANISOU 2274  C   ASP A1089    11091  13946   9308   -791    540    394       C  
ATOM   2275  O   ASP A1089     -31.821 -20.028  88.366  1.00 90.90           O  
ANISOU 2275  O   ASP A1089    10897  14070   9572   -913    527    310       O  
ATOM   2276  CB  ASP A1089     -30.045 -21.212  90.986  1.00 89.90           C  
ANISOU 2276  CB  ASP A1089    11468  13698   8994   -883    836    691       C  
ATOM   2277  CG  ASP A1089     -29.277 -22.474  91.357  1.00 99.63           C  
ANISOU 2277  CG  ASP A1089    12966  14732  10155   -964    904    870       C  
ATOM   2278  OD1 ASP A1089     -28.695 -23.112  90.447  1.00 99.34           O  
ANISOU 2278  OD1 ASP A1089    12975  14541  10230  -1040    750    863       O  
ATOM   2279  OD2 ASP A1089     -29.265 -22.829  92.558  1.00105.25           O  
ANISOU 2279  OD2 ASP A1089    13855  15446  10690   -931   1121   1022       O  
ATOM   2280  N   SER A1090     -30.848 -18.467  89.680  1.00 87.03           N  
ANISOU 2280  N   SER A1090    10704  13616   8747   -580    523    345       N  
ATOM   2281  CA  SER A1090     -31.788 -17.374  89.390  1.00 87.72           C  
ANISOU 2281  CA  SER A1090    10553  13868   8908   -447    509    214       C  
ATOM   2282  C   SER A1090     -31.680 -16.830  87.940  1.00 89.17           C  
ANISOU 2282  C   SER A1090    10632  14042   9206   -369    247    120       C  
ATOM   2283  O   SER A1090     -32.404 -15.900  87.558  1.00 89.84           O  
ANISOU 2283  O   SER A1090    10537  14251   9347   -216    204     26       O  
ATOM   2284  CB  SER A1090     -31.780 -16.356  90.534  1.00 92.40           C  
ANISOU 2284  CB  SER A1090    11248  14537   9322   -256    621    190       C  
ATOM   2285  OG  SER A1090     -30.556 -15.637  90.600  1.00 99.51           O  
ANISOU 2285  OG  SER A1090    12395  15328  10086   -121    457    170       O  
ATOM   2286  N   LEU A1091     -30.777 -17.421  87.142  1.00 82.93           N  
ANISOU 2286  N   LEU A1091     9967  13109   8435   -450     82    156       N  
ATOM   2287  CA  LEU A1091     -30.505 -16.989  85.776  1.00 81.13           C  
ANISOU 2287  CA  LEU A1091     9696  12862   8268   -369   -152     94       C  
ATOM   2288  C   LEU A1091     -31.078 -17.810  84.627  1.00 84.54           C  
ANISOU 2288  C   LEU A1091     9925  13342   8852   -501   -249     31       C  
ATOM   2289  O   LEU A1091     -31.173 -19.034  84.719  1.00 84.15           O  
ANISOU 2289  O   LEU A1091     9860  13235   8879   -718   -173     52       O  
ATOM   2290  CB  LEU A1091     -28.962 -16.954  85.727  1.00 78.80           C  
ANISOU 2290  CB  LEU A1091     9693  12389   7860   -342   -262    158       C  
ATOM   2291  CG  LEU A1091     -28.275 -15.641  85.316  1.00 81.96           C  
ANISOU 2291  CG  LEU A1091    10201  12738   8204   -150   -389    126       C  
ATOM   2292  CD1 LEU A1091     -28.552 -14.509  86.305  1.00 82.95           C  
ANISOU 2292  CD1 LEU A1091    10354  12905   8257      0   -283     84       C  
ATOM   2293  CD2 LEU A1091     -26.781 -15.837  85.196  1.00 82.17           C  
ANISOU 2293  CD2 LEU A1091    10453  12610   8158   -178   -484    173       C  
ATOM   2294  N   ASP A1092     -31.479 -17.118  83.558  1.00 81.34           N  
ANISOU 2294  N   ASP A1092     9375  13042   8487   -357   -415    -53       N  
ATOM   2295  CA  ASP A1092     -32.081 -17.700  82.357  1.00 82.44           C  
ANISOU 2295  CA  ASP A1092     9299  13285   8740   -429   -556   -156       C  
ATOM   2296  C   ASP A1092     -31.016 -18.201  81.374  1.00 86.15           C  
ANISOU 2296  C   ASP A1092     9951  13614   9169   -468   -725   -137       C  
ATOM   2297  O   ASP A1092     -29.851 -17.819  81.507  1.00 84.49           O  
ANISOU 2297  O   ASP A1092    10002  13252   8847   -391   -750    -43       O  
ATOM   2298  CB  ASP A1092     -33.003 -16.669  81.687  1.00 85.40           C  
ANISOU 2298  CB  ASP A1092     9446  13872   9131   -196   -667   -246       C  
ATOM   2299  CG  ASP A1092     -32.369 -15.301  81.531  1.00 92.75           C  
ANISOU 2299  CG  ASP A1092    10576  14729   9935     83   -736   -175       C  
ATOM   2300  OD1 ASP A1092     -32.321 -14.552  82.535  1.00 92.12           O  
ANISOU 2300  OD1 ASP A1092    10585  14607   9810    176   -599   -135       O  
ATOM   2301  OD2 ASP A1092     -31.900 -14.988  80.412  1.00 98.93           O  
ANISOU 2301  OD2 ASP A1092    11442  15484  10663    203   -912   -162       O  
ATOM   2302  N   ALA A1093     -31.425 -19.034  80.377  1.00 83.69           N  
ANISOU 2302  N   ALA A1093     9484  13367   8947   -584   -843   -249       N  
ATOM   2303  CA  ALA A1093     -30.573 -19.633  79.337  1.00 82.12           C  
ANISOU 2303  CA  ALA A1093     9424  13065   8712   -622  -1000   -267       C  
ATOM   2304  C   ALA A1093     -29.665 -18.635  78.613  1.00 84.94           C  
ANISOU 2304  C   ALA A1093     9969  13387   8917   -383  -1136   -197       C  
ATOM   2305  O   ALA A1093     -28.524 -18.980  78.291  1.00 83.32           O  
ANISOU 2305  O   ALA A1093     9979  13029   8651   -408  -1176   -142       O  
ATOM   2306  CB  ALA A1093     -31.423 -20.379  78.327  1.00 84.94           C  
ANISOU 2306  CB  ALA A1093     9530  13567   9176   -729  -1127   -454       C  
ATOM   2307  N   VAL A1094     -30.158 -17.405  78.364  1.00 81.89           N  
ANISOU 2307  N   VAL A1094     9505  13131   8479   -147  -1187   -192       N  
ATOM   2308  CA  VAL A1094     -29.378 -16.363  77.685  1.00 80.20           C  
ANISOU 2308  CA  VAL A1094     9480  12856   8136     81  -1274   -105       C  
ATOM   2309  C   VAL A1094     -28.328 -15.799  78.645  1.00 80.35           C  
ANISOU 2309  C   VAL A1094     9743  12673   8115     85  -1146     12       C  
ATOM   2310  O   VAL A1094     -27.142 -15.790  78.309  1.00 78.24           O  
ANISOU 2310  O   VAL A1094     9679  12263   7787     81  -1174     76       O  
ATOM   2311  CB  VAL A1094     -30.262 -15.246  77.054  1.00 86.04           C  
ANISOU 2311  CB  VAL A1094    10085  13772   8832    361  -1365   -123       C  
ATOM   2312  CG1 VAL A1094     -29.424 -14.263  76.239  1.00 84.84           C  
ANISOU 2312  CG1 VAL A1094    10166  13519   8550    582  -1426     -7       C  
ATOM   2313  CG2 VAL A1094     -31.376 -15.837  76.194  1.00 88.32           C  
ANISOU 2313  CG2 VAL A1094    10081  14319   9158    360  -1516   -279       C  
ATOM   2314  N   ARG A1095     -28.767 -15.362  79.839  1.00 76.24           N  
ANISOU 2314  N   ARG A1095     9185  12160   7625     91  -1006     20       N  
ATOM   2315  CA  ARG A1095     -27.905 -14.776  80.868  1.00 74.74           C  
ANISOU 2315  CA  ARG A1095     9197  11816   7385    103   -897     86       C  
ATOM   2316  C   ARG A1095     -26.902 -15.737  81.524  1.00 77.63           C  
ANISOU 2316  C   ARG A1095     9711  12057   7727    -83   -848    126       C  
ATOM   2317  O   ARG A1095     -25.844 -15.281  81.969  1.00 75.34           O  
ANISOU 2317  O   ARG A1095     9603  11646   7377    -58   -829    163       O  
ATOM   2318  CB  ARG A1095     -28.720 -13.978  81.886  1.00 74.92           C  
ANISOU 2318  CB  ARG A1095     9140  11907   7420    200   -770     59       C  
ATOM   2319  CG  ARG A1095     -29.186 -12.645  81.326  1.00 81.21           C  
ANISOU 2319  CG  ARG A1095     9910  12734   8211    461   -814     53       C  
ATOM   2320  CD  ARG A1095     -30.193 -11.994  82.239  1.00 87.51           C  
ANISOU 2320  CD  ARG A1095    10582  13631   9035    573   -690      0       C  
ATOM   2321  NE  ARG A1095     -30.646 -10.710  81.709  1.00 90.79           N  
ANISOU 2321  NE  ARG A1095    10992  14053   9450    858   -727      3       N  
ATOM   2322  CZ  ARG A1095     -31.909 -10.417  81.423  1.00103.52           C  
ANISOU 2322  CZ  ARG A1095    12366  15865  11104   1029   -750    -47       C  
ATOM   2323  NH1 ARG A1095     -32.866 -11.320  81.606  1.00 90.00           N  
ANISOU 2323  NH1 ARG A1095    10369  14372   9456    905   -732   -125       N  
ATOM   2324  NH2 ARG A1095     -32.226  -9.222  80.949  1.00 91.64           N  
ANISOU 2324  NH2 ARG A1095    10898  14337   9584   1328   -782    -22       N  
ATOM   2325  N   ARG A1096     -27.206 -17.059  81.547  1.00 75.54           N  
ANISOU 2325  N   ARG A1096     9371  11815   7516   -261   -830    110       N  
ATOM   2326  CA  ARG A1096     -26.299 -18.090  82.073  1.00 74.90           C  
ANISOU 2326  CA  ARG A1096     9445  11603   7410   -404   -787    166       C  
ATOM   2327  C   ARG A1096     -25.066 -18.190  81.169  1.00 78.45           C  
ANISOU 2327  C   ARG A1096    10038  11949   7818   -375   -912    185       C  
ATOM   2328  O   ARG A1096     -23.950 -18.333  81.669  1.00 77.06           O  
ANISOU 2328  O   ARG A1096    10025  11671   7583   -385   -899    236       O  
ATOM   2329  CB  ARG A1096     -26.993 -19.459  82.167  1.00 76.28           C  
ANISOU 2329  CB  ARG A1096     9518  11784   7681   -599   -719    146       C  
ATOM   2330  CG  ARG A1096     -27.839 -19.631  83.416  1.00 86.94           C  
ANISOU 2330  CG  ARG A1096    10793  13186   9053   -672   -523    174       C  
ATOM   2331  CD  ARG A1096     -28.516 -20.984  83.447  1.00 96.43           C  
ANISOU 2331  CD  ARG A1096    11897  14356  10385   -897   -422    158       C  
ATOM   2332  NE  ARG A1096     -29.465 -21.073  84.556  1.00104.23           N  
ANISOU 2332  NE  ARG A1096    12780  15416  11405   -971   -200    188       N  
ATOM   2333  CZ  ARG A1096     -30.033 -22.197  84.977  1.00119.76           C  
ANISOU 2333  CZ  ARG A1096    14699  17322  13481  -1186    -24    215       C  
ATOM   2334  NH1 ARG A1096     -29.744 -23.355  84.392  1.00107.71           N  
ANISOU 2334  NH1 ARG A1096    13230  15639  12055  -1349    -56    202       N  
ATOM   2335  NH2 ARG A1096     -30.884 -22.178  85.992  1.00107.65           N  
ANISOU 2335  NH2 ARG A1096    13069  15869  11963  -1242    208    255       N  
ATOM   2336  N   ALA A1097     -25.273 -18.072  79.841  1.00 75.74           N  
ANISOU 2336  N   ALA A1097     9626  11660   7492   -320  -1034    138       N  
ATOM   2337  CA  ALA A1097     -24.212 -18.103  78.841  1.00 74.41           C  
ANISOU 2337  CA  ALA A1097     9579  11421   7273   -276  -1132    155       C  
ATOM   2338  C   ALA A1097     -23.297 -16.888  78.954  1.00 77.52           C  
ANISOU 2338  C   ALA A1097    10103  11743   7609   -154  -1115    214       C  
ATOM   2339  O   ALA A1097     -22.106 -17.008  78.663  1.00 76.53           O  
ANISOU 2339  O   ALA A1097    10099  11529   7452   -164  -1135    242       O  
ATOM   2340  CB  ALA A1097     -24.808 -18.176  77.456  1.00 76.04           C  
ANISOU 2340  CB  ALA A1097     9681  11738   7474   -216  -1255     88       C  
ATOM   2341  N   ALA A1098     -23.842 -15.725  79.381  1.00 74.30           N  
ANISOU 2341  N   ALA A1098     9665  11365   7203    -47  -1066    219       N  
ATOM   2342  CA  ALA A1098     -23.055 -14.504  79.578  1.00 73.55           C  
ANISOU 2342  CA  ALA A1098     9696  11164   7087     44  -1025    250       C  
ATOM   2343  C   ALA A1098     -22.093 -14.704  80.764  1.00 76.14           C  
ANISOU 2343  C   ALA A1098    10117  11414   7398    -51   -971    239       C  
ATOM   2344  O   ALA A1098     -20.932 -14.300  80.686  1.00 74.25           O  
ANISOU 2344  O   ALA A1098     9977  11081   7154    -57   -975    242       O  
ATOM   2345  CB  ALA A1098     -23.973 -13.315  79.816  1.00 75.35           C  
ANISOU 2345  CB  ALA A1098     9875  11422   7332    189   -977    241       C  
ATOM   2346  N   LEU A1099     -22.572 -15.398  81.825  1.00 73.92           N  
ANISOU 2346  N   LEU A1099     9795  11187   7102   -125   -919    226       N  
ATOM   2347  CA  LEU A1099     -21.822 -15.752  83.035  1.00 73.59           C  
ANISOU 2347  CA  LEU A1099     9843  11117   6999   -180   -880    225       C  
ATOM   2348  C   LEU A1099     -20.765 -16.829  82.700  1.00 77.45           C  
ANISOU 2348  C   LEU A1099    10401  11554   7471   -249   -943    259       C  
ATOM   2349  O   LEU A1099     -19.659 -16.781  83.242  1.00 76.99           O  
ANISOU 2349  O   LEU A1099    10425  11465   7363   -244   -964    247       O  
ATOM   2350  CB  LEU A1099     -22.803 -16.244  84.119  1.00 74.55           C  
ANISOU 2350  CB  LEU A1099     9914  11320   7090   -216   -778    235       C  
ATOM   2351  CG  LEU A1099     -22.223 -16.597  85.487  1.00 79.73           C  
ANISOU 2351  CG  LEU A1099    10681  11981   7631   -231   -724    251       C  
ATOM   2352  CD1 LEU A1099     -22.479 -15.490  86.501  1.00 81.01           C  
ANISOU 2352  CD1 LEU A1099    10860  12193   7726   -144   -657    181       C  
ATOM   2353  CD2 LEU A1099     -22.810 -17.889  85.994  1.00 82.96           C  
ANISOU 2353  CD2 LEU A1099    11086  12412   8023   -320   -633    332       C  
ATOM   2354  N   ILE A1100     -21.113 -17.790  81.807  1.00 73.93           N  
ANISOU 2354  N   ILE A1100     9911  11108   7069   -303   -980    280       N  
ATOM   2355  CA  ILE A1100     -20.215 -18.858  81.342  1.00 73.09           C  
ANISOU 2355  CA  ILE A1100     9873  10939   6960   -347  -1033    301       C  
ATOM   2356  C   ILE A1100     -19.101 -18.241  80.478  1.00 77.46           C  
ANISOU 2356  C   ILE A1100    10465  11457   7507   -289  -1094    286       C  
ATOM   2357  O   ILE A1100     -17.943 -18.645  80.618  1.00 77.34           O  
ANISOU 2357  O   ILE A1100    10512  11405   7468   -288  -1119    291       O  
ATOM   2358  CB  ILE A1100     -20.987 -20.038  80.667  1.00 76.34           C  
ANISOU 2358  CB  ILE A1100    10230  11343   7433   -434  -1044    290       C  
ATOM   2359  CG1 ILE A1100     -21.757 -20.857  81.735  1.00 77.81           C  
ANISOU 2359  CG1 ILE A1100    10409  11516   7639   -530   -936    327       C  
ATOM   2360  CG2 ILE A1100     -20.052 -20.955  79.848  1.00 75.88           C  
ANISOU 2360  CG2 ILE A1100    10248  11207   7377   -446  -1110    283       C  
ATOM   2361  CD1 ILE A1100     -22.924 -21.739  81.230  1.00 84.21           C  
ANISOU 2361  CD1 ILE A1100    11103  12333   8561   -658   -910    278       C  
ATOM   2362  N   ASN A1101     -19.437 -17.216  79.651  1.00 73.91           N  
ANISOU 2362  N   ASN A1101     9980  11024   7077   -226  -1101    278       N  
ATOM   2363  CA  ASN A1101     -18.464 -16.491  78.819  1.00 73.45           C  
ANISOU 2363  CA  ASN A1101     9971  10918   7019   -178  -1109    287       C  
ATOM   2364  C   ASN A1101     -17.448 -15.799  79.726  1.00 77.55           C  
ANISOU 2364  C   ASN A1101    10529  11386   7550   -195  -1072    257       C  
ATOM   2365  O   ASN A1101     -16.269 -15.722  79.378  1.00 77.25           O  
ANISOU 2365  O   ASN A1101    10512  11312   7526   -210  -1073    246       O  
ATOM   2366  CB  ASN A1101     -19.162 -15.465  77.910  1.00 74.56           C  
ANISOU 2366  CB  ASN A1101    10098  11070   7162    -79  -1099    315       C  
ATOM   2367  CG  ASN A1101     -18.236 -14.673  77.007  1.00 96.67           C  
ANISOU 2367  CG  ASN A1101    12975  13797   9960    -30  -1060    358       C  
ATOM   2368  OD1 ASN A1101     -17.450 -13.827  77.449  1.00 88.04           O  
ANISOU 2368  OD1 ASN A1101    11925  12611   8915    -54   -990    349       O  
ATOM   2369  ND2 ASN A1101     -18.367 -14.875  75.710  1.00 90.94           N  
ANISOU 2369  ND2 ASN A1101    12264  13112   9175     39  -1093    398       N  
ATOM   2370  N   MET A1102     -17.917 -15.307  80.889  1.00 74.11           N  
ANISOU 2370  N   MET A1102    10087  10964   7105   -193  -1037    222       N  
ATOM   2371  CA  MET A1102     -17.092 -14.646  81.894  1.00 74.07           C  
ANISOU 2371  CA  MET A1102    10109  10937   7096   -210  -1022    147       C  
ATOM   2372  C   MET A1102     -16.123 -15.639  82.537  1.00 79.10           C  
ANISOU 2372  C   MET A1102    10757  11624   7674   -237  -1081    130       C  
ATOM   2373  O   MET A1102     -14.930 -15.346  82.616  1.00 79.34           O  
ANISOU 2373  O   MET A1102    10774  11648   7724   -255  -1109     66       O  
ATOM   2374  CB  MET A1102     -17.966 -13.948  82.946  1.00 76.77           C  
ANISOU 2374  CB  MET A1102    10453  11302   7415   -176   -971    101       C  
ATOM   2375  CG  MET A1102     -18.508 -12.634  82.470  1.00 80.35           C  
ANISOU 2375  CG  MET A1102    10915  11675   7940   -116   -910     90       C  
ATOM   2376  SD  MET A1102     -19.448 -11.773  83.737  1.00 85.12           S  
ANISOU 2376  SD  MET A1102    11525  12300   8518    -52   -838      6       S  
ATOM   2377  CE  MET A1102     -18.186 -10.803  84.490  1.00 82.29           C  
ANISOU 2377  CE  MET A1102    11230  11849   8187   -102   -833   -148       C  
ATOM   2378  N   VAL A1103     -16.626 -16.831  82.936  1.00 76.15           N  
ANISOU 2378  N   VAL A1103    10402  11293   7238   -237  -1092    191       N  
ATOM   2379  CA  VAL A1103     -15.841 -17.923  83.530  1.00 76.49           C  
ANISOU 2379  CA  VAL A1103    10490  11366   7208   -220  -1140    213       C  
ATOM   2380  C   VAL A1103     -14.782 -18.408  82.519  1.00 80.97           C  
ANISOU 2380  C   VAL A1103    11042  11902   7821   -215  -1193    214       C  
ATOM   2381  O   VAL A1103     -13.666 -18.754  82.907  1.00 81.00           O  
ANISOU 2381  O   VAL A1103    11044  11944   7788   -173  -1249    185       O  
ATOM   2382  CB  VAL A1103     -16.765 -19.055  84.068  1.00 80.90           C  
ANISOU 2382  CB  VAL A1103    11100  11924   7715   -230  -1093    304       C  
ATOM   2383  CG1 VAL A1103     -15.989 -20.329  84.400  1.00 81.29           C  
ANISOU 2383  CG1 VAL A1103    11232  11953   7701   -186  -1128    366       C  
ATOM   2384  CG2 VAL A1103     -17.553 -18.581  85.289  1.00 81.49           C  
ANISOU 2384  CG2 VAL A1103    11190  12062   7711   -215  -1021    299       C  
ATOM   2385  N   PHE A1104     -15.114 -18.357  81.221  1.00 77.53           N  
ANISOU 2385  N   PHE A1104    10585  11420   7452   -238  -1176    235       N  
ATOM   2386  CA  PHE A1104     -14.196 -18.721  80.144  1.00 77.10           C  
ANISOU 2386  CA  PHE A1104    10521  11346   7428   -224  -1200    232       C  
ATOM   2387  C   PHE A1104     -13.000 -17.754  80.067  1.00 80.66           C  
ANISOU 2387  C   PHE A1104    10917  11810   7922   -231  -1188    168       C  
ATOM   2388  O   PHE A1104     -11.871 -18.195  79.840  1.00 80.48           O  
ANISOU 2388  O   PHE A1104    10858  11813   7907   -209  -1213    140       O  
ATOM   2389  CB  PHE A1104     -14.952 -18.775  78.806  1.00 78.74           C  
ANISOU 2389  CB  PHE A1104    10729  11530   7657   -228  -1185    260       C  
ATOM   2390  CG  PHE A1104     -15.298 -20.171  78.353  1.00 80.53           C  
ANISOU 2390  CG  PHE A1104    10990  11735   7873   -235  -1219    271       C  
ATOM   2391  CD1 PHE A1104     -16.328 -20.881  78.956  1.00 84.09           C  
ANISOU 2391  CD1 PHE A1104    11454  12168   8330   -283  -1211    288       C  
ATOM   2392  CD2 PHE A1104     -14.600 -20.775  77.315  1.00 83.22           C  
ANISOU 2392  CD2 PHE A1104    11351  12062   8208   -201  -1238    251       C  
ATOM   2393  CE1 PHE A1104     -16.638 -22.179  78.545  1.00 85.76           C  
ANISOU 2393  CE1 PHE A1104    11702  12318   8564   -318  -1224    278       C  
ATOM   2394  CE2 PHE A1104     -14.919 -22.069  76.897  1.00 86.61           C  
ANISOU 2394  CE2 PHE A1104    11825  12444   8640   -211  -1266    231       C  
ATOM   2395  CZ  PHE A1104     -15.934 -22.763  77.517  1.00 85.03           C  
ANISOU 2395  CZ  PHE A1104    11642  12197   8469   -280  -1260    240       C  
ATOM   2396  N   GLN A1105     -13.250 -16.447  80.297  1.00 76.90           N  
ANISOU 2396  N   GLN A1105    10425  11305   7488   -264  -1138    132       N  
ATOM   2397  CA  GLN A1105     -12.234 -15.394  80.245  1.00 76.99           C  
ANISOU 2397  CA  GLN A1105    10383  11289   7580   -313  -1095     53       C  
ATOM   2398  C   GLN A1105     -11.394 -15.317  81.513  1.00 81.42           C  
ANISOU 2398  C   GLN A1105    10882  11928   8127   -329  -1162    -69       C  
ATOM   2399  O   GLN A1105     -10.165 -15.368  81.438  1.00 81.89           O  
ANISOU 2399  O   GLN A1105    10848  12035   8230   -351  -1185   -144       O  
ATOM   2400  CB  GLN A1105     -12.880 -14.027  79.971  1.00 78.31           C  
ANISOU 2400  CB  GLN A1105    10588  11352   7813   -336  -1001     62       C  
ATOM   2401  CG  GLN A1105     -11.864 -12.915  79.715  1.00 90.90           C  
ANISOU 2401  CG  GLN A1105    12147  12860   9530   -418   -911     -7       C  
ATOM   2402  CD  GLN A1105     -12.482 -11.550  79.553  1.00110.32           C  
ANISOU 2402  CD  GLN A1105    14682  15170  12066   -425   -800      8       C  
ATOM   2403  OE1 GLN A1105     -13.705 -11.375  79.538  1.00106.18           O  
ANISOU 2403  OE1 GLN A1105    14225  14627  11492   -341   -799     75       O  
ATOM   2404  NE2 GLN A1105     -11.635 -10.542  79.410  1.00103.78           N  
ANISOU 2404  NE2 GLN A1105    13838  14221  11372   -524   -693    -57       N  
ATOM   2405  N   MET A1106     -12.069 -15.148  82.662  1.00 77.33           N  
ANISOU 2405  N   MET A1106    10402  11442   7537   -308  -1191   -102       N  
ATOM   2406  CA  MET A1106     -11.473 -14.965  83.981  1.00 77.78           C  
ANISOU 2406  CA  MET A1106    10422  11600   7533   -297  -1267   -234       C  
ATOM   2407  C   MET A1106     -11.247 -16.262  84.749  1.00 81.46           C  
ANISOU 2407  C   MET A1106    10915  12188   7847   -191  -1366   -189       C  
ATOM   2408  O   MET A1106     -10.134 -16.519  85.201  1.00 82.37           O  
ANISOU 2408  O   MET A1106    10956  12414   7927   -147  -1462   -276       O  
ATOM   2409  CB  MET A1106     -12.346 -14.015  84.818  1.00 80.51           C  
ANISOU 2409  CB  MET A1106    10818  11919   7853   -305  -1227   -299       C  
ATOM   2410  CG  MET A1106     -12.379 -12.601  84.295  1.00 84.63           C  
ANISOU 2410  CG  MET A1106    11331  12296   8528   -388  -1130   -369       C  
ATOM   2411  SD  MET A1106     -13.861 -11.739  84.850  1.00 89.02           S  
ANISOU 2411  SD  MET A1106    11979  12784   9059   -342  -1051   -371       S  
ATOM   2412  CE  MET A1106     -14.877 -11.995  83.480  1.00 84.64           C  
ANISOU 2412  CE  MET A1106    11462  12151   8547   -299   -980   -172       C  
ATOM   2413  N   GLY A1107     -12.305 -17.047  84.908  1.00 76.93           N  
ANISOU 2413  N   GLY A1107    10443  11592   7193   -147  -1335    -56       N  
ATOM   2414  CA  GLY A1107     -12.293 -18.274  85.688  1.00 77.04           C  
ANISOU 2414  CA  GLY A1107    10536  11671   7064    -45  -1382     28       C  
ATOM   2415  C   GLY A1107     -13.174 -18.071  86.896  1.00 81.50           C  
ANISOU 2415  C   GLY A1107    11179  12288   7501    -14  -1345     38       C  
ATOM   2416  O   GLY A1107     -13.211 -16.961  87.439  1.00 81.06           O  
ANISOU 2416  O   GLY A1107    11088  12275   7436    -36  -1346    -90       O  
ATOM   2417  N   GLU A1108     -13.900 -19.134  87.320  1.00 79.33           N  
ANISOU 2417  N   GLU A1108    11015  11995   7132     32  -1290    186       N  
ATOM   2418  CA  GLU A1108     -14.827 -19.109  88.468  1.00 80.56           C  
ANISOU 2418  CA  GLU A1108    11256  12203   7149     65  -1210    232       C  
ATOM   2419  C   GLU A1108     -14.238 -18.538  89.752  1.00 85.42           C  
ANISOU 2419  C   GLU A1108    11891  12982   7584    168  -1286    116       C  
ATOM   2420  O   GLU A1108     -14.949 -17.872  90.504  1.00 85.32           O  
ANISOU 2420  O   GLU A1108    11904  13022   7493    172  -1221     66       O  
ATOM   2421  CB  GLU A1108     -15.507 -20.469  88.708  1.00 82.80           C  
ANISOU 2421  CB  GLU A1108    11663  12421   7374     85  -1112    424       C  
ATOM   2422  CG  GLU A1108     -14.592 -21.605  89.124  1.00 97.77           C  
ANISOU 2422  CG  GLU A1108    13669  14327   9151    221  -1176    518       C  
ATOM   2423  CD  GLU A1108     -15.338 -22.896  89.387  1.00128.26           C  
ANISOU 2423  CD  GLU A1108    17687  18068  12980    222  -1036    720       C  
ATOM   2424  OE1 GLU A1108     -15.577 -23.215  90.575  1.00128.91           O  
ANISOU 2424  OE1 GLU A1108    17903  18208  12868    321   -965    822       O  
ATOM   2425  OE2 GLU A1108     -15.695 -23.582  88.403  1.00123.19           O  
ANISOU 2425  OE2 GLU A1108    17037  17266  12502    121   -985    770       O  
ATOM   2426  N   THR A1109     -12.930 -18.765  89.970  1.00 83.17           N  
ANISOU 2426  N   THR A1109    11575  12792   7233    260  -1432     49       N  
ATOM   2427  CA  THR A1109     -12.160 -18.263  91.108  1.00 85.25           C  
ANISOU 2427  CA  THR A1109    11822  13250   7319    370  -1558   -109       C  
ATOM   2428  C   THR A1109     -12.087 -16.725  91.087  1.00 89.30           C  
ANISOU 2428  C   THR A1109    12219  13772   7940    256  -1573   -347       C  
ATOM   2429  O   THR A1109     -12.019 -16.098  92.147  1.00 90.41           O  
ANISOU 2429  O   THR A1109    12374  14046   7932    312  -1623   -498       O  
ATOM   2430  CB  THR A1109     -10.789 -18.971  91.190  1.00 96.30           C  
ANISOU 2430  CB  THR A1109    13177  14763   8648    506  -1722   -127       C  
ATOM   2431  OG1 THR A1109     -10.061 -18.474  92.313  1.00 97.55           O  
ANISOU 2431  OG1 THR A1109    13293  15151   8619    622  -1873   -311       O  
ATOM   2432  CG2 THR A1109      -9.951 -18.830  89.904  1.00 94.43           C  
ANISOU 2432  CG2 THR A1109    12777  14453   8651    406  -1764   -198       C  
ATOM   2433  N   GLY A1110     -12.127 -16.153  89.879  1.00 84.52           N  
ANISOU 2433  N   GLY A1110    11521  13012   7580    108  -1519   -373       N  
ATOM   2434  CA  GLY A1110     -12.092 -14.717  89.637  1.00 84.62           C  
ANISOU 2434  CA  GLY A1110    11453  12956   7744    -12  -1492   -559       C  
ATOM   2435  C   GLY A1110     -13.465 -14.098  89.470  1.00 88.61           C  
ANISOU 2435  C   GLY A1110    12023  13339   8305    -55  -1343   -506       C  
ATOM   2436  O   GLY A1110     -13.661 -12.946  89.864  1.00 89.09           O  
ANISOU 2436  O   GLY A1110    12080  13371   8399    -87  -1313   -666       O  
ATOM   2437  N   VAL A1111     -14.426 -14.845  88.877  1.00 84.64           N  
ANISOU 2437  N   VAL A1111    11569  12764   7825    -54  -1251   -302       N  
ATOM   2438  CA  VAL A1111     -15.812 -14.376  88.671  1.00 84.34           C  
ANISOU 2438  CA  VAL A1111    11555  12649   7841    -74  -1119   -246       C  
ATOM   2439  C   VAL A1111     -16.534 -14.226  90.028  1.00 91.45           C  
ANISOU 2439  C   VAL A1111    12525  13659   8562      6  -1062   -282       C  
ATOM   2440  O   VAL A1111     -17.320 -13.286  90.213  1.00 91.57           O  
ANISOU 2440  O   VAL A1111    12539  13641   8612     12   -978   -355       O  
ATOM   2441  CB  VAL A1111     -16.596 -15.242  87.642  1.00 86.40           C  
ANISOU 2441  CB  VAL A1111    11807  12835   8184   -108  -1058    -62       C  
ATOM   2442  CG1 VAL A1111     -18.039 -14.767  87.488  1.00 85.93           C  
ANISOU 2442  CG1 VAL A1111    11728  12746   8176   -109   -943    -28       C  
ATOM   2443  CG2 VAL A1111     -15.895 -15.240  86.281  1.00 85.13           C  
ANISOU 2443  CG2 VAL A1111    11592  12582   8172   -165  -1103    -47       C  
ATOM   2444  N   ALA A1112     -16.208 -15.119  90.995  1.00 89.81           N  
ANISOU 2444  N   ALA A1112    12391  13585   8146     91  -1104   -232       N  
ATOM   2445  CA  ALA A1112     -16.742 -15.086  92.356  1.00 91.81           C  
ANISOU 2445  CA  ALA A1112    12736  13974   8172    192  -1045   -251       C  
ATOM   2446  C   ALA A1112     -16.114 -13.925  93.162  1.00 98.99           C  
ANISOU 2446  C   ALA A1112    13636  14973   9000    232  -1135   -518       C  
ATOM   2447  O   ALA A1112     -16.533 -13.657  94.294  1.00100.86           O  
ANISOU 2447  O   ALA A1112    13951  15335   9037    327  -1091   -588       O  
ATOM   2448  CB  ALA A1112     -16.508 -16.421  93.044  1.00 93.44           C  
ANISOU 2448  CB  ALA A1112    13054  14279   8168    293  -1054    -86       C  
ATOM   2449  N   GLY A1113     -15.147 -13.232  92.547  1.00 95.82           N  
ANISOU 2449  N   GLY A1113    13139  14502   8765    149  -1242   -677       N  
ATOM   2450  CA  GLY A1113     -14.489 -12.048  93.095  1.00 97.51           C  
ANISOU 2450  CA  GLY A1113    13315  14751   8985    129  -1324   -971       C  
ATOM   2451  C   GLY A1113     -15.437 -10.862  93.122  1.00102.34           C  
ANISOU 2451  C   GLY A1113    13955  15236   9693    102  -1191  -1071       C  
ATOM   2452  O   GLY A1113     -15.334  -9.999  94.001  1.00103.92           O  
ANISOU 2452  O   GLY A1113    14183  15488   9813    133  -1213  -1309       O  
ATOM   2453  N   PHE A1114     -16.388 -10.837  92.194  1.00 97.98           N  
ANISOU 2453  N   PHE A1114    13397  14533   9299     67  -1059   -903       N  
ATOM   2454  CA  PHE A1114     -17.316  -9.714  92.078  1.00 98.88           C  
ANISOU 2454  CA  PHE A1114    13531  14515   9522     78   -932   -974       C  
ATOM   2455  C   PHE A1114     -18.631  -9.875  92.851  1.00 99.86           C  
ANISOU 2455  C   PHE A1114    13707  14743   9492    193   -802   -910       C  
ATOM   2456  O   PHE A1114     -19.578 -10.492  92.364  1.00 99.36           O  
ANISOU 2456  O   PHE A1114    13611  14677   9463    204   -708   -709       O  
ATOM   2457  CB  PHE A1114     -17.616  -9.425  90.604  1.00100.55           C  
ANISOU 2457  CB  PHE A1114    13696  14525   9984     11   -871   -848       C  
ATOM   2458  CG  PHE A1114     -16.501  -8.721  89.885  1.00104.11           C  
ANISOU 2458  CG  PHE A1114    14115  14819  10624   -103   -921   -955       C  
ATOM   2459  CD1 PHE A1114     -16.257  -7.376  90.107  1.00110.51           C  
ANISOU 2459  CD1 PHE A1114    14958  15481  11550   -140   -882  -1171       C  
ATOM   2460  CD2 PHE A1114     -15.698  -9.404  88.987  1.00106.16           C  
ANISOU 2460  CD2 PHE A1114    14313  15067  10957   -181   -985   -847       C  
ATOM   2461  CE1 PHE A1114     -15.232  -6.725  89.447  1.00112.36           C  
ANISOU 2461  CE1 PHE A1114    15159  15549  11984   -277   -890  -1266       C  
ATOM   2462  CE2 PHE A1114     -14.672  -8.758  88.324  1.00109.93           C  
ANISOU 2462  CE2 PHE A1114    14746  15410  11614   -297   -996   -939       C  
ATOM   2463  CZ  PHE A1114     -14.438  -7.417  88.554  1.00110.11           C  
ANISOU 2463  CZ  PHE A1114    14796  15276  11766   -358   -940  -1143       C  
ATOM   2464  N   THR A1115     -18.722  -9.201  93.994  1.00 94.68           N  
ANISOU 2464  N   THR A1115    13115  14170   8689    273   -785  -1109       N  
ATOM   2465  CA  THR A1115     -19.937  -9.204  94.810  1.00 94.04           C  
ANISOU 2465  CA  THR A1115    13080  14200   8452    394   -633  -1079       C  
ATOM   2466  C   THR A1115     -21.240  -8.413  94.585  1.00 94.24           C  
ANISOU 2466  C   THR A1115    13080  14135   8593    461   -464  -1082       C  
ATOM   2467  O   THR A1115     -22.332  -8.974  94.674  1.00 93.56           O  
ANISOU 2467  O   THR A1115    12952  14140   8457    511   -330   -923       O  
ATOM   2468  CB  THR A1115     -19.637  -8.762  96.258  1.00104.69           C  
ANISOU 2468  CB  THR A1115    14524  15711   9541    495   -665  -1316       C  
ATOM   2469  OG1 THR A1115     -18.815  -9.744  96.900  1.00101.86           O  
ANISOU 2469  OG1 THR A1115    14209  15547   8946    526   -788  -1269       O  
ATOM   2470  CG2 THR A1115     -20.929  -8.596  97.043  1.00106.09           C  
ANISOU 2470  CG2 THR A1115    14747  15991   9571    628   -472  -1302       C  
ATOM   2471  N   ASN A1116     -21.119  -7.113  94.315  1.00 88.85           N  
ANISOU 2471  N   ASN A1116    12417  13270   8074    465   -460  -1269       N  
ATOM   2472  CA  ASN A1116     -22.251  -6.192  94.351  1.00 88.89           C  
ANISOU 2472  CA  ASN A1116    12425  13197   8153    586   -308  -1326       C  
ATOM   2473  C   ASN A1116     -22.957  -6.496  93.041  1.00 89.99           C  
ANISOU 2473  C   ASN A1116    12458  13248   8484    574   -265  -1089       C  
ATOM   2474  O   ASN A1116     -24.185  -6.606  93.028  1.00 89.75           O  
ANISOU 2474  O   ASN A1116    12352  13297   8451    674   -142   -997       O  
ATOM   2475  CB  ASN A1116     -21.861  -4.718  94.446  1.00 88.85           C  
ANISOU 2475  CB  ASN A1116    12505  12977   8277    602   -307  -1595       C  
ATOM   2476  CG  ASN A1116     -21.458  -4.278  95.833  1.00103.92           C  
ANISOU 2476  CG  ASN A1116    14509  14997   9980    648   -334  -1886       C  
ATOM   2477  OD1 ASN A1116     -21.798  -4.903  96.844  1.00 91.00           O  
ANISOU 2477  OD1 ASN A1116    12892  13616   8066    736   -306  -1878       O  
ATOM   2478  ND2 ASN A1116     -20.762  -3.157  95.911  1.00 98.98           N  
ANISOU 2478  ND2 ASN A1116    13951  14173   9483    595   -376  -2160       N  
ATOM   2479  N   SER A1117     -22.175  -6.681  91.950  1.00 84.15           N  
ANISOU 2479  N   SER A1117    11699  12377   7899    456   -368  -1000       N  
ATOM   2480  CA  SER A1117     -22.682  -7.008  90.614  1.00 81.85           C  
ANISOU 2480  CA  SER A1117    11318  12019   7761    447   -362   -792       C  
ATOM   2481  C   SER A1117     -23.304  -8.401  90.565  1.00 82.77           C  
ANISOU 2481  C   SER A1117    11333  12327   7788    417   -350   -603       C  
ATOM   2482  O   SER A1117     -24.170  -8.638  89.730  1.00 81.43           O  
ANISOU 2482  O   SER A1117    11057  12168   7713    447   -318   -476       O  
ATOM   2483  CB  SER A1117     -21.580  -6.878  89.567  1.00 84.22           C  
ANISOU 2483  CB  SER A1117    11644  12148   8208    331   -459   -759       C  
ATOM   2484  OG  SER A1117     -21.058  -5.560  89.548  1.00 93.96           O  
ANISOU 2484  OG  SER A1117    12971  13163   9566    331   -433   -926       O  
ATOM   2485  N   LEU A1118     -22.875  -9.312  91.460  1.00 78.62           N  
ANISOU 2485  N   LEU A1118    10842  11949   7081    364   -374   -592       N  
ATOM   2486  CA  LEU A1118     -23.430 -10.658  91.547  1.00 78.14           C  
ANISOU 2486  CA  LEU A1118    10719  12028   6942    321   -325   -413       C  
ATOM   2487  C   LEU A1118     -24.700 -10.671  92.395  1.00 85.03           C  
ANISOU 2487  C   LEU A1118    11543  13044   7719    408   -147   -408       C  
ATOM   2488  O   LEU A1118     -25.547 -11.545  92.192  1.00 85.10           O  
ANISOU 2488  O   LEU A1118    11446  13134   7754    361    -59   -265       O  
ATOM   2489  CB  LEU A1118     -22.409 -11.682  92.067  1.00 77.79           C  
ANISOU 2489  CB  LEU A1118    10760  12053   6745    255   -410   -362       C  
ATOM   2490  CG  LEU A1118     -21.376 -12.214  91.064  1.00 80.67           C  
ANISOU 2490  CG  LEU A1118    11116  12320   7214    155   -555   -295       C  
ATOM   2491  CD1 LEU A1118     -20.453 -13.211  91.724  1.00 80.86           C  
ANISOU 2491  CD1 LEU A1118    11222  12433   7067    144   -631   -249       C  
ATOM   2492  CD2 LEU A1118     -22.044 -12.900  89.880  1.00 83.22           C  
ANISOU 2492  CD2 LEU A1118    11338  12596   7686     91   -534   -136       C  
ATOM   2493  N   ARG A1119     -24.844  -9.702  93.331  1.00 83.52           N  
ANISOU 2493  N   ARG A1119    11420  12885   7428    525    -82   -580       N  
ATOM   2494  CA  ARG A1119     -26.051  -9.582  94.153  1.00 85.45           C  
ANISOU 2494  CA  ARG A1119    11614  13276   7576    632    111   -596       C  
ATOM   2495  C   ARG A1119     -27.182  -8.995  93.297  1.00 89.30           C  
ANISOU 2495  C   ARG A1119    11938  13720   8272    706    179   -581       C  
ATOM   2496  O   ARG A1119     -28.334  -9.395  93.459  1.00 90.19           O  
ANISOU 2496  O   ARG A1119    11905  13975   8388    733    328   -510       O  
ATOM   2497  CB  ARG A1119     -25.809  -8.756  95.437  1.00 88.76           C  
ANISOU 2497  CB  ARG A1119    12171  13756   7798    754    154   -809       C  
ATOM   2498  CG  ARG A1119     -27.031  -8.704  96.369  1.00103.56           C  
ANISOU 2498  CG  ARG A1119    14001  15810   9536    878    383   -821       C  
ATOM   2499  CD  ARG A1119     -26.698  -8.784  97.848  1.00116.53           C  
ANISOU 2499  CD  ARG A1119    15805  17620  10850    958    440   -920       C  
ATOM   2500  NE  ARG A1119     -26.252  -7.498  98.380  1.00126.33           N  
ANISOU 2500  NE  ARG A1119    17161  18802  12036   1070    381  -1215       N  
ATOM   2501  CZ  ARG A1119     -24.985  -7.202  98.649  1.00141.15           C  
ANISOU 2501  CZ  ARG A1119    19165  20628  13836   1035    192  -1380       C  
ATOM   2502  NH1 ARG A1119     -24.664  -6.009  99.126  1.00131.50           N  
ANISOU 2502  NH1 ARG A1119    18033  19335  12595   1114    154  -1681       N  
ATOM   2503  NH2 ARG A1119     -24.029  -8.104  98.452  1.00125.86           N  
ANISOU 2503  NH2 ARG A1119    17256  18715  11851    921     40  -1263       N  
ATOM   2504  N   MET A1120     -26.844  -8.087  92.363  1.00 84.87           N  
ANISOU 2504  N   MET A1120    11393  12969   7883    743     76   -638       N  
ATOM   2505  CA  MET A1120     -27.814  -7.473  91.459  1.00 85.02           C  
ANISOU 2505  CA  MET A1120    11281  12942   8079    861    109   -611       C  
ATOM   2506  C   MET A1120     -28.314  -8.445  90.386  1.00 87.11           C  
ANISOU 2506  C   MET A1120    11370  13278   8450    775     60   -436       C  
ATOM   2507  O   MET A1120     -29.459  -8.321  89.954  1.00 87.17           O  
ANISOU 2507  O   MET A1120    11196  13378   8546    874    115   -410       O  
ATOM   2508  CB  MET A1120     -27.268  -6.178  90.853  1.00 87.52           C  
ANISOU 2508  CB  MET A1120    11717  13009   8526    948     41   -706       C  
ATOM   2509  CG  MET A1120     -27.440  -4.983  91.757  1.00 93.73           C  
ANISOU 2509  CG  MET A1120    12612  13726   9275   1101    141   -910       C  
ATOM   2510  SD  MET A1120     -26.049  -3.844  91.621  1.00 98.57           S  
ANISOU 2510  SD  MET A1120    13450  14019   9983   1049     56  -1077       S  
ATOM   2511  CE  MET A1120     -26.590  -2.536  92.721  1.00 98.58           C  
ANISOU 2511  CE  MET A1120    13557  13955   9945   1251    200  -1340       C  
ATOM   2512  N   LEU A1121     -27.480  -9.428  89.981  1.00 82.43           N  
ANISOU 2512  N   LEU A1121    10815  12657   7845    600    -47   -336       N  
ATOM   2513  CA  LEU A1121     -27.884 -10.448  89.004  1.00 81.80           C  
ANISOU 2513  CA  LEU A1121    10586  12637   7858    498    -99   -202       C  
ATOM   2514  C   LEU A1121     -28.793 -11.456  89.702  1.00 88.69           C  
ANISOU 2514  C   LEU A1121    11327  13693   8680    418     48   -148       C  
ATOM   2515  O   LEU A1121     -29.789 -11.896  89.117  1.00 89.29           O  
ANISOU 2515  O   LEU A1121    11190  13871   8866    392     76   -109       O  
ATOM   2516  CB  LEU A1121     -26.678 -11.149  88.342  1.00 79.54           C  
ANISOU 2516  CB  LEU A1121    10398  12244   7581    354   -244   -129       C  
ATOM   2517  CG  LEU A1121     -25.780 -10.290  87.437  1.00 82.62           C  
ANISOU 2517  CG  LEU A1121    10891  12452   8050    395   -363   -155       C  
ATOM   2518  CD1 LEU A1121     -24.495 -11.001  87.118  1.00 80.62           C  
ANISOU 2518  CD1 LEU A1121    10730  12126   7774    255   -471   -109       C  
ATOM   2519  CD2 LEU A1121     -26.488  -9.864  86.164  1.00 84.96           C  
ANISOU 2519  CD2 LEU A1121    11082  12730   8467    499   -406   -106       C  
ATOM   2520  N   GLN A1122     -28.468 -11.781  90.974  1.00 86.75           N  
ANISOU 2520  N   GLN A1122    11203  13497   8260    387    150   -153       N  
ATOM   2521  CA  GLN A1122     -29.263 -12.668  91.821  1.00 88.83           C  
ANISOU 2521  CA  GLN A1122    11390  13914   8446    319    344    -81       C  
ATOM   2522  C   GLN A1122     -30.620 -11.992  92.070  1.00 96.29           C  
ANISOU 2522  C   GLN A1122    12142  14999   9445    447    502   -157       C  
ATOM   2523  O   GLN A1122     -31.664 -12.619  91.864  1.00 97.39           O  
ANISOU 2523  O   GLN A1122    12057  15260   9687    370    614   -106       O  
ATOM   2524  CB  GLN A1122     -28.517 -12.961  93.145  1.00 90.86           C  
ANISOU 2524  CB  GLN A1122    11869  14199   8453    323    409    -68       C  
ATOM   2525  CG  GLN A1122     -29.394 -13.374  94.342  1.00111.45           C  
ANISOU 2525  CG  GLN A1122    14453  16977  10915    338    672    -20       C  
ATOM   2526  CD  GLN A1122     -29.879 -14.802  94.281  1.00133.30           C  
ANISOU 2526  CD  GLN A1122    17146  19771  13733    154    807    162       C  
ATOM   2527  OE1 GLN A1122     -29.092 -15.749  94.223  1.00128.99           O  
ANISOU 2527  OE1 GLN A1122    16739  19132  13140     52    744    282       O  
ATOM   2528  NE2 GLN A1122     -31.191 -14.991  94.343  1.00126.61           N  
ANISOU 2528  NE2 GLN A1122    16074  19043  12989    110   1013    179       N  
ATOM   2529  N   GLN A1123     -30.590 -10.695  92.447  1.00 94.20           N  
ANISOU 2529  N   GLN A1123    11950  14708   9133    640    506   -297       N  
ATOM   2530  CA  GLN A1123     -31.780  -9.890  92.726  1.00 96.64           C  
ANISOU 2530  CA  GLN A1123    12100  15136   9482    818    651   -391       C  
ATOM   2531  C   GLN A1123     -32.475  -9.328  91.479  1.00100.67           C  
ANISOU 2531  C   GLN A1123    12412  15634  10204    929    555   -408       C  
ATOM   2532  O   GLN A1123     -33.458  -8.595  91.601  1.00101.80           O  
ANISOU 2532  O   GLN A1123    12409  15876  10396   1118    652   -489       O  
ATOM   2533  CB  GLN A1123     -31.496  -8.818  93.789  1.00 99.46           C  
ANISOU 2533  CB  GLN A1123    12641  15468   9683    990    721   -549       C  
ATOM   2534  CG  GLN A1123     -31.333  -9.405  95.194  1.00120.29           C  
ANISOU 2534  CG  GLN A1123    15401  18237  12065    944    878   -537       C  
ATOM   2535  CD  GLN A1123     -30.624  -8.496  96.173  1.00146.01           C  
ANISOU 2535  CD  GLN A1123    18896  21453  15128   1076    866   -718       C  
ATOM   2536  OE1 GLN A1123     -30.241  -7.360  95.866  1.00142.77           O  
ANISOU 2536  OE1 GLN A1123    18565  20882  14799   1184    758   -872       O  
ATOM   2537  NE2 GLN A1123     -30.414  -8.992  97.387  1.00140.34           N  
ANISOU 2537  NE2 GLN A1123    18308  20873  14141   1070    978   -709       N  
ATOM   2538  N   LYS A1124     -31.992  -9.726  90.283  1.00 96.25           N  
ANISOU 2538  N   LYS A1124    11843  14975   9752    831    366   -329       N  
ATOM   2539  CA  LYS A1124     -32.534  -9.392  88.952  1.00 96.51           C  
ANISOU 2539  CA  LYS A1124    11708  15015   9946    933    238   -317       C  
ATOM   2540  C   LYS A1124     -32.572  -7.891  88.588  1.00101.55           C  
ANISOU 2540  C   LYS A1124    12429  15530  10626   1209    191   -389       C  
ATOM   2541  O   LYS A1124     -33.465  -7.451  87.860  1.00102.46           O  
ANISOU 2541  O   LYS A1124    12363  15731  10838   1391    156   -395       O  
ATOM   2542  CB  LYS A1124     -33.895 -10.099  88.684  1.00100.59           C  
ANISOU 2542  CB  LYS A1124    11871  15780  10568    892    308   -310       C  
ATOM   2543  CG  LYS A1124     -33.992 -11.555  89.166  1.00114.80           C  
ANISOU 2543  CG  LYS A1124    13598  17665  12355    608    419   -241       C  
ATOM   2544  CD  LYS A1124     -33.338 -12.562  88.223  1.00122.38           C  
ANISOU 2544  CD  LYS A1124    14594  18532  13373    404    254   -160       C  
ATOM   2545  CE  LYS A1124     -34.313 -13.186  87.255  1.00133.28           C  
ANISOU 2545  CE  LYS A1124    15653  20067  14921    327    194   -190       C  
ATOM   2546  NZ  LYS A1124     -35.144 -14.238  87.904  1.00143.28           N  
ANISOU 2546  NZ  LYS A1124    16717  21468  16254    112    403   -184       N  
ATOM   2547  N   ARG A1125     -31.586  -7.123  89.069  1.00 97.83           N  
ANISOU 2547  N   ARG A1125    12231  14852  10086   1243    188   -447       N  
ATOM   2548  CA  ARG A1125     -31.459  -5.694  88.793  1.00 98.98           C  
ANISOU 2548  CA  ARG A1125    12515  14803  10289   1471    172   -516       C  
ATOM   2549  C   ARG A1125     -30.322  -5.735  87.767  1.00101.49           C  
ANISOU 2549  C   ARG A1125    12989  14917  10656   1365     10   -428       C  
ATOM   2550  O   ARG A1125     -29.153  -5.918  88.122  1.00100.02           O  
ANISOU 2550  O   ARG A1125    12978  14609  10417   1198    -24   -450       O  
ATOM   2551  CB  ARG A1125     -31.216  -4.898  90.091  1.00101.61           C  
ANISOU 2551  CB  ARG A1125    13019  15060  10530   1544    303   -680       C  
ATOM   2552  CG  ARG A1125     -32.486  -4.306  90.702  1.00119.84           C  
ANISOU 2552  CG  ARG A1125    15188  17512  12835   1782    467   -776       C  
ATOM   2553  CD  ARG A1125     -33.118  -5.164  91.788  1.00135.00           C  
ANISOU 2553  CD  ARG A1125    16960  19706  14628   1693    627   -795       C  
ATOM   2554  NE  ARG A1125     -32.395  -5.082  93.061  1.00145.36           N  
ANISOU 2554  NE  ARG A1125    18489  20986  15756   1628    704   -907       N  
ATOM   2555  CZ  ARG A1125     -32.853  -5.555  94.218  1.00161.47           C  
ANISOU 2555  CZ  ARG A1125    20483  23235  17631   1609    882   -941       C  
ATOM   2556  NH1 ARG A1125     -32.128  -5.436  95.322  1.00150.04           N  
ANISOU 2556  NH1 ARG A1125    19254  21772  15981   1583    920  -1050       N  
ATOM   2557  NH2 ARG A1125     -34.039  -6.151  94.279  1.00148.94           N  
ANISOU 2557  NH2 ARG A1125    18626  21890  16077   1617   1027   -871       N  
ATOM   2558  N   TRP A1126     -30.691  -5.584  86.480  1.00 98.37           N  
ANISOU 2558  N   TRP A1126    12513  14514  10349   1479    -89   -330       N  
ATOM   2559  CA  TRP A1126     -29.788  -5.641  85.322  1.00 96.76           C  
ANISOU 2559  CA  TRP A1126    12433  14152  10181   1414   -223   -222       C  
ATOM   2560  C   TRP A1126     -29.091  -4.301  85.131  1.00102.92           C  
ANISOU 2560  C   TRP A1126    13467  14620  11016   1536   -191   -240       C  
ATOM   2561  O   TRP A1126     -27.865  -4.277  85.054  1.00101.50           O  
ANISOU 2561  O   TRP A1126    13461  14260  10846   1372   -218   -238       O  
ATOM   2562  CB  TRP A1126     -30.489  -6.068  84.024  1.00 95.43           C  
ANISOU 2562  CB  TRP A1126    12084  14132  10045   1502   -344   -115       C  
ATOM   2563  CG  TRP A1126     -31.505  -7.154  84.193  1.00 96.49           C  
ANISOU 2563  CG  TRP A1126    11918  14569  10176   1419   -349   -139       C  
ATOM   2564  CD1 TRP A1126     -32.837  -7.078  83.914  1.00101.67           C  
ANISOU 2564  CD1 TRP A1126    12307  15449  10875   1596   -355   -167       C  
ATOM   2565  CD2 TRP A1126     -31.271  -8.473  84.696  1.00 95.00           C  
ANISOU 2565  CD2 TRP A1126    11660  14481   9957   1134   -332   -141       C  
ATOM   2566  NE1 TRP A1126     -33.448  -8.275  84.199  1.00101.25           N  
ANISOU 2566  NE1 TRP A1126    12003  15627  10840   1401   -333   -202       N  
ATOM   2567  CE2 TRP A1126     -32.510  -9.149  84.688  1.00100.49           C  
ANISOU 2567  CE2 TRP A1126    12045  15437  10698   1118   -307   -173       C  
ATOM   2568  CE3 TRP A1126     -30.130  -9.156  85.149  1.00 94.16           C  
ANISOU 2568  CE3 TRP A1126    11718  14264   9792    900   -332   -118       C  
ATOM   2569  CZ2 TRP A1126     -32.643 -10.471  85.126  1.00 99.36           C  
ANISOU 2569  CZ2 TRP A1126    11784  15407  10560    855   -253   -171       C  
ATOM   2570  CZ3 TRP A1126     -30.264 -10.463  85.589  1.00 95.13           C  
ANISOU 2570  CZ3 TRP A1126    11740  14510   9895    684   -295   -101       C  
ATOM   2571  CH2 TRP A1126     -31.505 -11.110  85.565  1.00 97.38           C  
ANISOU 2571  CH2 TRP A1126    11746  15012  10241    651   -244   -121       C  
ATOM   2572  N   ASP A1127     -29.864  -3.193  85.048  1.00102.34           N  
ANISOU 2572  N   ASP A1127    13413  14477  10996   1823   -122   -263       N  
ATOM   2573  CA  ASP A1127     -29.338  -1.838  84.853  1.00103.55           C  
ANISOU 2573  CA  ASP A1127    13827  14285  11231   1960    -55   -275       C  
ATOM   2574  C   ASP A1127     -28.400  -1.435  85.991  1.00106.52           C  
ANISOU 2574  C   ASP A1127    14382  14478  11613   1791     29   -452       C  
ATOM   2575  O   ASP A1127     -27.377  -0.793  85.743  1.00105.62           O  
ANISOU 2575  O   ASP A1127    14481  14071  11579   1710     49   -465       O  
ATOM   2576  CB  ASP A1127     -30.483  -0.826  84.674  1.00108.69           C  
ANISOU 2576  CB  ASP A1127    14453  14914  11930   2335     12   -271       C  
ATOM   2577  CG  ASP A1127     -31.356  -1.088  83.457  1.00121.21           C  
ANISOU 2577  CG  ASP A1127    15865  16691  13499   2545   -103   -111       C  
ATOM   2578  OD1 ASP A1127     -30.873  -0.884  82.323  1.00121.69           O  
ANISOU 2578  OD1 ASP A1127    16061  16611  13566   2593   -171     43       O  
ATOM   2579  OD2 ASP A1127     -32.529  -1.475  83.641  1.00128.67           O  
ANISOU 2579  OD2 ASP A1127    16531  17939  14417   2669   -121   -150       O  
ATOM   2580  N   GLU A1128     -28.728  -1.869  87.226  1.00103.20           N  
ANISOU 2580  N   GLU A1128    13865  14250  11099   1727     80   -591       N  
ATOM   2581  CA  GLU A1128     -27.927  -1.639  88.429  1.00103.22           C  
ANISOU 2581  CA  GLU A1128    14004  14166  11048   1584    131   -787       C  
ATOM   2582  C   GLU A1128     -26.631  -2.454  88.373  1.00104.28           C  
ANISOU 2582  C   GLU A1128    14183  14295  11143   1290     23   -765       C  
ATOM   2583  O   GLU A1128     -25.591  -1.984  88.839  1.00103.72           O  
ANISOU 2583  O   GLU A1128    14264  14052  11092   1168     21   -908       O  
ATOM   2584  CB  GLU A1128     -28.739  -1.973  89.686  1.00105.79           C  
ANISOU 2584  CB  GLU A1128    14211  14746  11238   1637    223   -907       C  
ATOM   2585  CG  GLU A1128     -29.725  -0.881  90.069  1.00119.54           C  
ANISOU 2585  CG  GLU A1128    15964  16436  13019   1930    358  -1018       C  
ATOM   2586  CD  GLU A1128     -30.677  -1.221  91.199  1.00139.05           C  
ANISOU 2586  CD  GLU A1128    18286  19193  15355   2010    481  -1115       C  
ATOM   2587  OE1 GLU A1128     -31.899  -1.013  91.018  1.00131.36           O  
ANISOU 2587  OE1 GLU A1128    17140  18351  14420   2239    556  -1083       O  
ATOM   2588  OE2 GLU A1128     -30.209  -1.682  92.265  1.00132.87           O  
ANISOU 2588  OE2 GLU A1128    17552  18516  14415   1861    507  -1221       O  
ATOM   2589  N   ALA A1129     -26.697  -3.666  87.782  1.00 99.07           N  
ANISOU 2589  N   ALA A1129    13379  13826  10439   1182    -70   -603       N  
ATOM   2590  CA  ALA A1129     -25.546  -4.550  87.587  1.00 96.82           C  
ANISOU 2590  CA  ALA A1129    13118  13552  10119    940   -175   -556       C  
ATOM   2591  C   ALA A1129     -24.697  -4.051  86.413  1.00100.78           C  
ANISOU 2591  C   ALA A1129    13732  13812  10747    903   -220   -475       C  
ATOM   2592  O   ALA A1129     -23.489  -4.273  86.405  1.00 99.18           O  
ANISOU 2592  O   ALA A1129    13596  13532  10556    719   -272   -507       O  
ATOM   2593  CB  ALA A1129     -26.013  -5.972  87.321  1.00 96.01           C  
ANISOU 2593  CB  ALA A1129    12838  13698   9944    858   -235   -421       C  
ATOM   2594  N   ALA A1130     -25.331  -3.367  85.432  1.00 99.18           N  
ANISOU 2594  N   ALA A1130    13549  13502  10631   1095   -189   -365       N  
ATOM   2595  CA  ALA A1130     -24.672  -2.821  84.242  1.00 99.48           C  
ANISOU 2595  CA  ALA A1130    13720  13306  10770   1103   -191   -247       C  
ATOM   2596  C   ALA A1130     -23.675  -1.710  84.579  1.00105.30           C  
ANISOU 2596  C   ALA A1130    14662  13718  11629   1022    -96   -375       C  
ATOM   2597  O   ALA A1130     -22.544  -1.746  84.086  1.00104.30           O  
ANISOU 2597  O   ALA A1130    14606  13458  11565    848   -106   -346       O  
ATOM   2598  CB  ALA A1130     -25.704  -2.327  83.238  1.00101.67           C  
ANISOU 2598  CB  ALA A1130    13985  13573  11070   1383   -179    -95       C  
ATOM   2599  N   VAL A1131     -24.086  -0.739  85.420  1.00104.12           N  
ANISOU 2599  N   VAL A1131    14595  13442  11523   1139      5   -534       N  
ATOM   2600  CA  VAL A1131     -23.238   0.378  85.862  1.00105.89           C  
ANISOU 2600  CA  VAL A1131    15010  13339  11886   1051    105   -713       C  
ATOM   2601  C   VAL A1131     -22.110  -0.183  86.743  1.00108.03           C  
ANISOU 2601  C   VAL A1131    15234  13705  12107    769     26   -903       C  
ATOM   2602  O   VAL A1131     -20.955   0.227  86.599  1.00108.13           O  
ANISOU 2602  O   VAL A1131    15330  13511  12244    580     46   -987       O  
ATOM   2603  CB  VAL A1131     -24.068   1.483  86.590  1.00113.05           C  
ANISOU 2603  CB  VAL A1131    16014  14104  12836   1272    227   -864       C  
ATOM   2604  CG1 VAL A1131     -23.180   2.613  87.115  1.00115.19           C  
ANISOU 2604  CG1 VAL A1131    16483  14016  13267   1151    331  -1099       C  
ATOM   2605  CG2 VAL A1131     -25.163   2.045  85.683  1.00114.40           C  
ANISOU 2605  CG2 VAL A1131    16223  14195  13051   1598    291   -666       C  
ATOM   2606  N   ASN A1132     -22.456  -1.144  87.621  1.00103.04           N  
ANISOU 2606  N   ASN A1132    14463  13397  11292    749    -58   -960       N  
ATOM   2607  CA  ASN A1132     -21.538  -1.807  88.544  1.00102.17           C  
ANISOU 2607  CA  ASN A1132    14304  13442  11072    550   -154  -1117       C  
ATOM   2608  C   ASN A1132     -20.481  -2.677  87.833  1.00103.43           C  
ANISOU 2608  C   ASN A1132    14401  13653  11246    357   -260  -1002       C  
ATOM   2609  O   ASN A1132     -19.351  -2.780  88.322  1.00103.16           O  
ANISOU 2609  O   ASN A1132    14361  13627  11210    184   -326  -1157       O  
ATOM   2610  CB  ASN A1132     -22.317  -2.614  89.585  1.00103.95           C  
ANISOU 2610  CB  ASN A1132    14431  13986  11081    624   -179  -1148       C  
ATOM   2611  CG  ASN A1132     -21.979  -2.281  91.019  1.00134.71           C  
ANISOU 2611  CG  ASN A1132    18383  17941  14858    600   -179  -1428       C  
ATOM   2612  OD1 ASN A1132     -22.863  -2.039  91.848  1.00133.25           O  
ANISOU 2612  OD1 ASN A1132    18206  17857  14567    752    -99  -1518       O  
ATOM   2613  ND2 ASN A1132     -20.696  -2.287  91.359  1.00127.55           N  
ANISOU 2613  ND2 ASN A1132    17503  17007  13954    421   -274  -1587       N  
ATOM   2614  N   LEU A1133     -20.843  -3.294  86.689  1.00 97.73           N  
ANISOU 2614  N   LEU A1133    13620  12981  10531    399   -282   -752       N  
ATOM   2615  CA  LEU A1133     -19.904  -4.107  85.913  1.00 95.54           C  
ANISOU 2615  CA  LEU A1133    13293  12744  10266    246   -364   -640       C  
ATOM   2616  C   LEU A1133     -19.016  -3.234  85.015  1.00 99.82           C  
ANISOU 2616  C   LEU A1133    13938  12997  10994    163   -287   -620       C  
ATOM   2617  O   LEU A1133     -17.953  -3.685  84.587  1.00 98.33           O  
ANISOU 2617  O   LEU A1133    13709  12814  10839      3   -330   -600       O  
ATOM   2618  CB  LEU A1133     -20.623  -5.184  85.080  1.00 93.80           C  
ANISOU 2618  CB  LEU A1133    12971  12706   9964    315   -423   -416       C  
ATOM   2619  CG  LEU A1133     -20.960  -6.514  85.766  1.00 97.11           C  
ANISOU 2619  CG  LEU A1133    13271  13403  10223    278   -504   -403       C  
ATOM   2620  CD1 LEU A1133     -21.826  -7.372  84.868  1.00 96.32           C  
ANISOU 2620  CD1 LEU A1133    13071  13433  10094    340   -540   -221       C  
ATOM   2621  CD2 LEU A1133     -19.707  -7.304  86.115  1.00 97.87           C  
ANISOU 2621  CD2 LEU A1133    13350  13569  10265    111   -597   -453       C  
ATOM   2622  N   ALA A1134     -19.451  -1.989  84.736  1.00 98.38           N  
ANISOU 2622  N   ALA A1134    13892  12552  10938    280   -153   -619       N  
ATOM   2623  CA  ALA A1134     -18.710  -1.027  83.914  1.00 99.79           C  
ANISOU 2623  CA  ALA A1134    14208  12399  11310    210    -23   -579       C  
ATOM   2624  C   ALA A1134     -17.562  -0.370  84.698  1.00105.11           C  
ANISOU 2624  C   ALA A1134    14910  12902  12124    -18     17   -856       C  
ATOM   2625  O   ALA A1134     -16.612   0.134  84.093  1.00105.50           O  
ANISOU 2625  O   ALA A1134    15015  12723  12347   -176    116   -851       O  
ATOM   2626  CB  ALA A1134     -19.654   0.033  83.370  1.00102.56           C  
ANISOU 2626  CB  ALA A1134    14720  12515  11735    451    115   -460       C  
ATOM   2627  N   LYS A1135     -17.651  -0.383  86.042  1.00102.18           N  
ANISOU 2627  N   LYS A1135    14493  12657  11673    -37    -55  -1109       N  
ATOM   2628  CA  LYS A1135     -16.626   0.170  86.935  1.00103.81           C  
ANISOU 2628  CA  LYS A1135    14696  12770  11978   -242    -64  -1433       C  
ATOM   2629  C   LYS A1135     -15.435  -0.793  87.082  1.00106.61           C  
ANISOU 2629  C   LYS A1135    14877  13353  12276   -445   -213  -1498       C  
ATOM   2630  O   LYS A1135     -14.338  -0.358  87.446  1.00107.77           O  
ANISOU 2630  O   LYS A1135    14978  13417  12553   -652   -222  -1741       O  
ATOM   2631  CB  LYS A1135     -17.220   0.473  88.324  1.00107.12           C  
ANISOU 2631  CB  LYS A1135    15138  13284  12279   -144   -100  -1684       C  
ATOM   2632  CG  LYS A1135     -18.185   1.653  88.351  1.00121.78           C  
ANISOU 2632  CG  LYS A1135    17169  14866  14234     44     63  -1709       C  
ATOM   2633  CD  LYS A1135     -17.962   2.536  89.577  1.00134.21           C  
ANISOU 2633  CD  LYS A1135    18816  16330  15849     -6     85  -2097       C  
ATOM   2634  CE  LYS A1135     -18.829   2.160  90.757  1.00144.21           C  
ANISOU 2634  CE  LYS A1135    20046  17892  16857    170     16  -2215       C  
ATOM   2635  NZ  LYS A1135     -18.504   2.980  91.956  1.00155.24           N  
ANISOU 2635  NZ  LYS A1135    21515  19209  18259    118     19  -2627       N  
ATOM   2636  N   SER A1136     -15.672  -2.101  86.804  1.00100.47           N  
ANISOU 2636  N   SER A1136    13995  12864  11316   -379   -329  -1297       N  
ATOM   2637  CA  SER A1136     -14.722  -3.213  86.926  1.00 98.70           C  
ANISOU 2637  CA  SER A1136    13616  12887  10997   -498   -480  -1311       C  
ATOM   2638  C   SER A1136     -13.464  -3.096  86.075  1.00103.06           C  
ANISOU 2638  C   SER A1136    14106  13320  11733   -692   -440  -1304       C  
ATOM   2639  O   SER A1136     -13.479  -2.450  85.026  1.00103.34           O  
ANISOU 2639  O   SER A1136    14232  13100  11933   -711   -280  -1164       O  
ATOM   2640  CB  SER A1136     -15.417  -4.547  86.658  1.00 98.95           C  
ANISOU 2640  CB  SER A1136    13594  13169  10832   -370   -565  -1071       C  
ATOM   2641  OG  SER A1136     -15.704  -4.726  85.282  1.00103.73           O  
ANISOU 2641  OG  SER A1136    14226  13687  11502   -327   -498   -815       O  
ATOM   2642  N   ARG A1137     -12.383  -3.760  86.530  1.00 99.36           N  
ANISOU 2642  N   ARG A1137    13479  13055  11220   -815   -579  -1445       N  
ATOM   2643  CA  ARG A1137     -11.086  -3.810  85.858  1.00 99.59           C  
ANISOU 2643  CA  ARG A1137    13388  13044  11409  -1003   -557  -1471       C  
ATOM   2644  C   ARG A1137     -11.142  -4.701  84.618  1.00101.16           C  
ANISOU 2644  C   ARG A1137    13575  13298  11564   -943   -531  -1161       C  
ATOM   2645  O   ARG A1137     -10.334  -4.524  83.706  1.00101.27           O  
ANISOU 2645  O   ARG A1137    13545  13202  11732  -1066   -427  -1106       O  
ATOM   2646  CB  ARG A1137      -9.992  -4.276  86.837  1.00100.81           C  
ANISOU 2646  CB  ARG A1137    13350  13452  11501  -1102   -744  -1741       C  
ATOM   2647  CG  ARG A1137      -8.870  -3.260  87.060  1.00114.56           C  
ANISOU 2647  CG  ARG A1137    14987  15048  13492  -1348   -695  -2054       C  
ATOM   2648  CD  ARG A1137      -9.321  -1.995  87.781  1.00127.49           C  
ANISOU 2648  CD  ARG A1137    16752  16463  15227  -1386   -618  -2290       C  
ATOM   2649  NE  ARG A1137      -8.808  -0.792  87.118  1.00137.11           N  
ANISOU 2649  NE  ARG A1137    18008  17301  16787  -1604   -394  -2368       N  
ATOM   2650  CZ  ARG A1137      -9.391   0.403  87.161  1.00150.63           C  
ANISOU 2650  CZ  ARG A1137    19915  18667  18652  -1614   -222  -2431       C  
ATOM   2651  NH1 ARG A1137     -10.525   0.574  87.832  1.00136.13           N  
ANISOU 2651  NH1 ARG A1137    18230  16842  16652  -1406   -256  -2439       N  
ATOM   2652  NH2 ARG A1137      -8.851   1.434  86.527  1.00138.69           N  
ANISOU 2652  NH2 ARG A1137    18452  16782  17463  -1825      7  -2478       N  
ATOM   2653  N   TRP A1138     -12.107  -5.644  84.586  1.00 95.77           N  
ANISOU 2653  N   TRP A1138    12930  12782  10676   -761   -612   -974       N  
ATOM   2654  CA  TRP A1138     -12.376  -6.566  83.478  1.00 93.55           C  
ANISOU 2654  CA  TRP A1138    12651  12569  10325   -681   -611   -708       C  
ATOM   2655  C   TRP A1138     -12.823  -5.756  82.253  1.00 96.78           C  
ANISOU 2655  C   TRP A1138    13191  12732  10850   -644   -431   -529       C  
ATOM   2656  O   TRP A1138     -12.331  -5.986  81.143  1.00 95.39           O  
ANISOU 2656  O   TRP A1138    13008  12522  10714   -675   -365   -388       O  
ATOM   2657  CB  TRP A1138     -13.443  -7.592  83.917  1.00 90.73           C  
ANISOU 2657  CB  TRP A1138    12306  12412   9754   -523   -722   -605       C  
ATOM   2658  CG  TRP A1138     -14.218  -8.247  82.814  1.00 90.47           C  
ANISOU 2658  CG  TRP A1138    12309  12401   9664   -419   -703   -361       C  
ATOM   2659  CD1 TRP A1138     -13.737  -9.105  81.869  1.00 92.43           C  
ANISOU 2659  CD1 TRP A1138    12515  12712   9893   -433   -729   -240       C  
ATOM   2660  CD2 TRP A1138     -15.632  -8.150  82.587  1.00 89.98           C  
ANISOU 2660  CD2 TRP A1138    12313  12329   9545   -274   -673   -241       C  
ATOM   2661  NE1 TRP A1138     -14.760  -9.530  81.051  1.00 91.10           N  
ANISOU 2661  NE1 TRP A1138    12391  12567   9654   -317   -724    -66       N  
ATOM   2662  CE2 TRP A1138     -15.934  -8.958  81.467  1.00 92.85           C  
ANISOU 2662  CE2 TRP A1138    12665  12757   9858   -220   -696    -64       C  
ATOM   2663  CE3 TRP A1138     -16.675  -7.443  83.210  1.00 92.05           C  
ANISOU 2663  CE3 TRP A1138    12629  12548   9796   -175   -628   -285       C  
ATOM   2664  CZ2 TRP A1138     -17.236  -9.092  80.970  1.00 91.77           C  
ANISOU 2664  CZ2 TRP A1138    12544  12661   9662    -82   -697     56       C  
ATOM   2665  CZ3 TRP A1138     -17.960  -7.560  82.704  1.00 93.11           C  
ANISOU 2665  CZ3 TRP A1138    12776  12721   9881    -27   -613   -147       C  
ATOM   2666  CH2 TRP A1138     -18.228  -8.364  81.589  1.00 92.66           C  
ANISOU 2666  CH2 TRP A1138    12684  12743   9779     14   -656     16       C  
ATOM   2667  N   TYR A1139     -13.721  -4.777  82.486  1.00 94.23           N  
ANISOU 2667  N   TYR A1139    12996  12238  10567   -557   -345   -539       N  
ATOM   2668  CA  TYR A1139     -14.251  -3.855  81.484  1.00 94.94           C  
ANISOU 2668  CA  TYR A1139    13246  12075  10751   -468   -173   -369       C  
ATOM   2669  C   TYR A1139     -13.149  -2.901  81.032  1.00101.27           C  
ANISOU 2669  C   TYR A1139    14091  12606  11779   -651      5   -421       C  
ATOM   2670  O   TYR A1139     -13.080  -2.587  79.848  1.00101.67           O  
ANISOU 2670  O   TYR A1139    14245  12505  11880   -618    152   -216       O  
ATOM   2671  CB  TYR A1139     -15.465  -3.091  82.046  1.00 96.86           C  
ANISOU 2671  CB  TYR A1139    13601  12223  10980   -302   -139   -398       C  
ATOM   2672  CG  TYR A1139     -16.088  -2.089  81.097  1.00100.31           C  
ANISOU 2672  CG  TYR A1139    14221  12395  11498   -152     30   -217       C  
ATOM   2673  CD1 TYR A1139     -17.048  -2.481  80.170  1.00101.43           C  
ANISOU 2673  CD1 TYR A1139    14394  12635  11509     67      2     23       C  
ATOM   2674  CD2 TYR A1139     -15.762  -0.738  81.168  1.00103.95           C  
ANISOU 2674  CD2 TYR A1139    14830  12505  12163   -211    213   -297       C  
ATOM   2675  CE1 TYR A1139     -17.639  -1.558  79.307  1.00104.14           C  
ANISOU 2675  CE1 TYR A1139    14915  12760  11892    258    140    203       C  
ATOM   2676  CE2 TYR A1139     -16.351   0.195  80.315  1.00106.72           C  
ANISOU 2676  CE2 TYR A1139    15385  12587  12576    -33    381   -102       C  
ATOM   2677  CZ  TYR A1139     -17.286  -0.221  79.383  1.00113.01           C  
ANISOU 2677  CZ  TYR A1139    16215  13515  13210    220    337    159       C  
ATOM   2678  OH  TYR A1139     -17.863   0.695  78.539  1.00116.24           O  
ANISOU 2678  OH  TYR A1139    16833  13684  13648    442    487    365       O  
ATOM   2679  N   ASN A1140     -12.283  -2.455  81.964  1.00 99.31           N  
ANISOU 2679  N   ASN A1140    13762  12308  11663   -848     -2   -702       N  
ATOM   2680  CA  ASN A1140     -11.162  -1.560  81.657  1.00101.65           C  
ANISOU 2680  CA  ASN A1140    14056  12349  12218  -1081    176   -805       C  
ATOM   2681  C   ASN A1140     -10.109  -2.268  80.793  1.00104.72           C  
ANISOU 2681  C   ASN A1140    14309  12853  12628  -1200    199   -709       C  
ATOM   2682  O   ASN A1140      -9.532  -1.638  79.903  1.00106.43           O  
ANISOU 2682  O   ASN A1140    14584  12837  13016  -1313    422   -614       O  
ATOM   2683  CB  ASN A1140     -10.529  -1.016  82.941  1.00104.06           C  
ANISOU 2683  CB  ASN A1140    14263  12630  12646  -1266    119  -1185       C  
ATOM   2684  CG  ASN A1140      -9.580   0.135  82.711  1.00128.08           C  
ANISOU 2684  CG  ASN A1140    17319  15339  16007  -1526    335  -1332       C  
ATOM   2685  OD1 ASN A1140      -8.425  -0.047  82.308  1.00121.76           O  
ANISOU 2685  OD1 ASN A1140    16358  14571  15335  -1732    385  -1379       O  
ATOM   2686  ND2 ASN A1140     -10.048   1.348  82.963  1.00122.55           N  
ANISOU 2686  ND2 ASN A1140    16806  14299  15457  -1526    485  -1414       N  
ATOM   2687  N   GLN A1141      -9.874  -3.575  81.052  1.00 98.47           N  
ANISOU 2687  N   GLN A1141    13350  12406  11661  -1161    -11   -724       N  
ATOM   2688  CA  GLN A1141      -8.908  -4.409  80.328  1.00 97.45           C  
ANISOU 2688  CA  GLN A1141    13074  12429  11522  -1233    -17   -654       C  
ATOM   2689  C   GLN A1141      -9.426  -4.771  78.932  1.00 98.64           C  
ANISOU 2689  C   GLN A1141    13355  12553  11569  -1081     79   -330       C  
ATOM   2690  O   GLN A1141      -8.753  -4.479  77.944  1.00 98.98           O  
ANISOU 2690  O   GLN A1141    13414  12478  11715  -1164    266   -223       O  
ATOM   2691  CB  GLN A1141      -8.565  -5.670  81.145  1.00 97.35           C  
ANISOU 2691  CB  GLN A1141    12876  12766  11348  -1199   -274   -777       C  
ATOM   2692  CG  GLN A1141      -7.080  -6.048  81.125  1.00116.95           C  
ANISOU 2692  CG  GLN A1141    15121  15385  13931  -1362   -299   -924       C  
ATOM   2693  CD  GLN A1141      -6.547  -6.495  82.474  1.00134.94           C  
ANISOU 2693  CD  GLN A1141    17218  17909  16142  -1385   -531  -1197       C  
ATOM   2694  OE1 GLN A1141      -5.432  -6.139  82.875  1.00132.22           O  
ANISOU 2694  OE1 GLN A1141    16678  17610  15952  -1562   -545  -1445       O  
ATOM   2695  NE2 GLN A1141      -7.312  -7.298  83.203  1.00124.55           N  
ANISOU 2695  NE2 GLN A1141    15958  16774  14592  -1203   -714  -1160       N  
ATOM   2696  N   THR A1142     -10.621  -5.392  78.857  1.00 92.51           N  
ANISOU 2696  N   THR A1142    12664  11899  10588   -862    -43   -187       N  
ATOM   2697  CA  THR A1142     -11.272  -5.796  77.606  1.00 90.87           C  
ANISOU 2697  CA  THR A1142    12567  11715  10244   -688     -5     81       C  
ATOM   2698  C   THR A1142     -12.633  -5.078  77.473  1.00 93.93           C  
ANISOU 2698  C   THR A1142    13137  11970  10583   -498     34    203       C  
ATOM   2699  O   THR A1142     -13.656  -5.653  77.849  1.00 91.97           O  
ANISOU 2699  O   THR A1142    12872  11881  10192   -357   -119    214       O  
ATOM   2700  CB  THR A1142     -11.382  -7.341  77.491  1.00 93.84           C  
ANISOU 2700  CB  THR A1142    12837  12387  10432   -608   -197    118       C  
ATOM   2701  OG1 THR A1142     -11.924  -7.881  78.701  1.00 92.78           O  
ANISOU 2701  OG1 THR A1142    12636  12399  10216   -575   -377     -7       O  
ATOM   2702  CG2 THR A1142     -10.054  -8.006  77.152  1.00 89.71           C  
ANISOU 2702  CG2 THR A1142    12169  11971   9944   -727   -189     71       C  
ATOM   2703  N   PRO A1143     -12.679  -3.824  76.961  1.00 91.55           N  
ANISOU 2703  N   PRO A1143    13006  11371  10406   -485    248    295       N  
ATOM   2704  CA  PRO A1143     -13.971  -3.122  76.864  1.00 91.53           C  
ANISOU 2704  CA  PRO A1143    13174  11248  10355   -259    276    409       C  
ATOM   2705  C   PRO A1143     -14.934  -3.652  75.804  1.00 92.86           C  
ANISOU 2705  C   PRO A1143    13407  11567  10311     -1    209    644       C  
ATOM   2706  O   PRO A1143     -16.141  -3.657  76.047  1.00 91.99           O  
ANISOU 2706  O   PRO A1143    13310  11535  10106    191    108    665       O  
ATOM   2707  CB  PRO A1143     -13.577  -1.659  76.611  1.00 96.55           C  
ANISOU 2707  CB  PRO A1143    13993  11489  11202   -323    544    443       C  
ATOM   2708  CG  PRO A1143     -12.080  -1.597  76.769  1.00102.15           C  
ANISOU 2708  CG  PRO A1143    14584  12129  12097   -635    644    294       C  
ATOM   2709  CD  PRO A1143     -11.577  -2.970  76.482  1.00 95.44           C  
ANISOU 2709  CD  PRO A1143    13549  11611  11104   -669    491    302       C  
ATOM   2710  N   ASN A1144     -14.412  -4.084  74.639  1.00 88.12           N  
ANISOU 2710  N   ASN A1144    12830  11021   9630      8    265    800       N  
ATOM   2711  CA  ASN A1144     -15.239  -4.586  73.536  1.00 86.93           C  
ANISOU 2711  CA  ASN A1144    12740  11033   9256    255    190    997       C  
ATOM   2712  C   ASN A1144     -15.994  -5.870  73.881  1.00 86.78           C  
ANISOU 2712  C   ASN A1144    12551  11334   9088    312    -71    909       C  
ATOM   2713  O   ASN A1144     -17.201  -5.946  73.651  1.00 86.08           O  
ANISOU 2713  O   ASN A1144    12473  11354   8878    522   -174    971       O  
ATOM   2714  CB  ASN A1144     -14.418  -4.735  72.254  1.00 87.75           C  
ANISOU 2714  CB  ASN A1144    12921  11128   9293    247    328   1160       C  
ATOM   2715  CG  ASN A1144     -14.142  -3.444  71.526  1.00110.80           C  
ANISOU 2715  CG  ASN A1144    16077  13735  12287    301    612   1354       C  
ATOM   2716  OD1 ASN A1144     -14.199  -2.340  72.083  1.00104.64           O  
ANISOU 2716  OD1 ASN A1144    15399  12672  11687    261    748   1327       O  
ATOM   2717  ND2 ASN A1144     -13.799  -3.562  70.256  1.00105.43           N  
ANISOU 2717  ND2 ASN A1144    15507  13084  11468    392    729   1554       N  
ATOM   2718  N   ARG A1145     -15.289  -6.856  74.465  1.00 80.82           N  
ANISOU 2718  N   ARG A1145    11634  10720   8355    127   -170    761       N  
ATOM   2719  CA  ARG A1145     -15.850  -8.139  74.891  1.00 77.98           C  
ANISOU 2719  CA  ARG A1145    11128  10613   7886    139   -381    677       C  
ATOM   2720  C   ARG A1145     -16.809  -7.921  76.063  1.00 81.77           C  
ANISOU 2720  C   ARG A1145    11562  11114   8395    172   -455    576       C  
ATOM   2721  O   ARG A1145     -17.911  -8.473  76.044  1.00 81.49           O  
ANISOU 2721  O   ARG A1145    11466  11237   8260    287   -573    589       O  
ATOM   2722  CB  ARG A1145     -14.724  -9.121  75.267  1.00 74.77           C  
ANISOU 2722  CB  ARG A1145    10598  10304   7506    -42   -434    564       C  
ATOM   2723  CG  ARG A1145     -15.208 -10.456  75.813  1.00 76.34           C  
ANISOU 2723  CG  ARG A1145    10681  10708   7615    -45   -619    487       C  
ATOM   2724  CD  ARG A1145     -14.062 -11.374  76.172  1.00 76.05           C  
ANISOU 2724  CD  ARG A1145    10549  10747   7599   -175   -665    396       C  
ATOM   2725  NE  ARG A1145     -14.539 -12.679  76.631  1.00 75.50           N  
ANISOU 2725  NE  ARG A1145    10411  10829   7446   -164   -812    354       N  
ATOM   2726  CZ  ARG A1145     -13.831 -13.801  76.552  1.00 88.78           C  
ANISOU 2726  CZ  ARG A1145    12041  12593   9097   -202   -873    323       C  
ATOM   2727  NH1 ARG A1145     -12.606 -13.787  76.043  1.00 77.02           N  
ANISOU 2727  NH1 ARG A1145    10530  11087   7647   -246   -809    315       N  
ATOM   2728  NH2 ARG A1145     -14.340 -14.946  76.989  1.00 75.45           N  
ANISOU 2728  NH2 ARG A1145    10325  10994   7350   -192   -979    300       N  
ATOM   2729  N   ALA A1146     -16.395  -7.099  77.063  1.00 78.13           N  
ANISOU 2729  N   ALA A1146    11118  10497   8071     68   -377    458       N  
ATOM   2730  CA  ALA A1146     -17.186  -6.779  78.258  1.00 77.29           C  
ANISOU 2730  CA  ALA A1146    10983  10400   7985    101   -418    341       C  
ATOM   2731  C   ALA A1146     -18.502  -6.081  77.952  1.00 80.97           C  
ANISOU 2731  C   ALA A1146    11522  10826   8418    328   -392    435       C  
ATOM   2732  O   ALA A1146     -19.506  -6.454  78.550  1.00 80.21           O  
ANISOU 2732  O   ALA A1146    11335  10879   8260    405   -479    386       O  
ATOM   2733  CB  ALA A1146     -16.375  -5.965  79.247  1.00 79.01           C  
ANISOU 2733  CB  ALA A1146    11220  10453   8346    -50   -339    171       C  
ATOM   2734  N   LYS A1147     -18.517  -5.101  77.015  1.00 78.24           N  
ANISOU 2734  N   LYS A1147    11334  10288   8107    450   -263    578       N  
ATOM   2735  CA  LYS A1147     -19.747  -4.398  76.625  1.00 78.93           C  
ANISOU 2735  CA  LYS A1147    11499  10342   8148    723   -245    687       C  
ATOM   2736  C   LYS A1147     -20.782  -5.402  76.104  1.00 79.82           C  
ANISOU 2736  C   LYS A1147    11475  10761   8093    866   -421    740       C  
ATOM   2737  O   LYS A1147     -21.930  -5.360  76.546  1.00 79.87           O  
ANISOU 2737  O   LYS A1147    11393  10881   8072   1005   -486    698       O  
ATOM   2738  CB  LYS A1147     -19.473  -3.286  75.594  1.00 83.87           C  
ANISOU 2738  CB  LYS A1147    12351  10704   8811    850    -68    874       C  
ATOM   2739  CG  LYS A1147     -20.682  -2.384  75.343  1.00103.83           C  
ANISOU 2739  CG  LYS A1147    14987  13159  11305   1170    -38    982       C  
ATOM   2740  CD  LYS A1147     -20.481  -1.454  74.149  1.00119.08           C  
ANISOU 2740  CD  LYS A1147    17171  14856  13219   1349    132   1226       C  
ATOM   2741  CE  LYS A1147     -21.783  -0.923  73.582  1.00131.73           C  
ANISOU 2741  CE  LYS A1147    18849  16505  14697   1749     90   1377       C  
ATOM   2742  NZ  LYS A1147     -22.399   0.125  74.442  1.00140.79           N  
ANISOU 2742  NZ  LYS A1147    20070  17442  15981   1875    175   1305       N  
ATOM   2743  N   ARG A1148     -20.345  -6.342  75.229  1.00 73.38           N  
ANISOU 2743  N   ARG A1148    10620  10084   7178    814   -494    801       N  
ATOM   2744  CA  ARG A1148     -21.168  -7.404  74.641  1.00 71.61           C  
ANISOU 2744  CA  ARG A1148    10261  10141   6808    903   -666    812       C  
ATOM   2745  C   ARG A1148     -21.770  -8.286  75.720  1.00 74.12           C  
ANISOU 2745  C   ARG A1148    10385  10628   7147    794   -773    658       C  
ATOM   2746  O   ARG A1148     -22.952  -8.610  75.642  1.00 74.76           O  
ANISOU 2746  O   ARG A1148    10338  10893   7175    912   -872    637       O  
ATOM   2747  CB  ARG A1148     -20.350  -8.260  73.667  1.00 69.12           C  
ANISOU 2747  CB  ARG A1148     9959   9902   6403    825   -701    860       C  
ATOM   2748  CG  ARG A1148     -20.004  -7.563  72.368  1.00 76.43           C  
ANISOU 2748  CG  ARG A1148    11069  10730   7241    983   -600   1044       C  
ATOM   2749  CD  ARG A1148     -19.270  -8.477  71.398  1.00 77.60           C  
ANISOU 2749  CD  ARG A1148    11221  10990   7273    926   -632   1074       C  
ATOM   2750  NE  ARG A1148     -17.864  -8.108  71.200  1.00 84.74           N  
ANISOU 2750  NE  ARG A1148    12236  11706   8255    783   -444   1130       N  
ATOM   2751  CZ  ARG A1148     -17.444  -7.077  70.464  1.00108.33           C  
ANISOU 2751  CZ  ARG A1148    15419  14507  11236    875   -251   1304       C  
ATOM   2752  NH1 ARG A1148     -18.317  -6.260  69.884  1.00 98.21           N  
ANISOU 2752  NH1 ARG A1148    14273  13187   9855   1144   -227   1456       N  
ATOM   2753  NH2 ARG A1148     -16.147  -6.840  70.326  1.00100.94           N  
ANISOU 2753  NH2 ARG A1148    14540  13416  10398    703    -66   1330       N  
ATOM   2754  N   VAL A1149     -20.964  -8.649  76.738  1.00 68.80           N  
ANISOU 2754  N   VAL A1149     9687   9903   6550    577   -745    552       N  
ATOM   2755  CA  VAL A1149     -21.382  -9.482  77.872  1.00 67.15           C  
ANISOU 2755  CA  VAL A1149     9339   9827   6346    469   -809    432       C  
ATOM   2756  C   VAL A1149     -22.386  -8.729  78.772  1.00 72.33           C  
ANISOU 2756  C   VAL A1149     9961  10481   7039    573   -763    376       C  
ATOM   2757  O   VAL A1149     -23.455  -9.272  79.058  1.00 72.19           O  
ANISOU 2757  O   VAL A1149     9798  10639   6990    612   -817    342       O  
ATOM   2758  CB  VAL A1149     -20.161 -10.072  78.638  1.00 68.91           C  
ANISOU 2758  CB  VAL A1149     9569  10014   6600    259   -803    353       C  
ATOM   2759  CG1 VAL A1149     -20.564 -10.677  79.981  1.00 68.08           C  
ANISOU 2759  CG1 VAL A1149     9377  10011   6480    183   -829    255       C  
ATOM   2760  CG2 VAL A1149     -19.441 -11.108  77.784  1.00 67.42           C  
ANISOU 2760  CG2 VAL A1149     9368   9885   6364    185   -866    394       C  
ATOM   2761  N   ILE A1150     -22.052  -7.473  79.171  1.00 69.73           N  
ANISOU 2761  N   ILE A1150     9759   9947   6787    616   -649    355       N  
ATOM   2762  CA  ILE A1150     -22.889  -6.590  80.002  1.00 70.82           C  
ANISOU 2762  CA  ILE A1150     9900  10042   6965    741   -582    287       C  
ATOM   2763  C   ILE A1150     -24.246  -6.312  79.310  1.00 77.80           C  
ANISOU 2763  C   ILE A1150    10715  11035   7808    998   -616    370       C  
ATOM   2764  O   ILE A1150     -25.275  -6.268  79.996  1.00 78.63           O  
ANISOU 2764  O   ILE A1150    10702  11262   7912   1087   -613    300       O  
ATOM   2765  CB  ILE A1150     -22.119  -5.302  80.459  1.00 74.59           C  
ANISOU 2765  CB  ILE A1150    10553  10232   7555    716   -449    224       C  
ATOM   2766  CG1 ILE A1150     -20.894  -5.663  81.334  1.00 73.64           C  
ANISOU 2766  CG1 ILE A1150    10433  10083   7463    468   -454     86       C  
ATOM   2767  CG2 ILE A1150     -23.029  -4.314  81.210  1.00 76.88           C  
ANISOU 2767  CG2 ILE A1150    10873  10453   7886    884   -369    146       C  
ATOM   2768  CD1 ILE A1150     -19.797  -4.604  81.401  1.00 80.08           C  
ANISOU 2768  CD1 ILE A1150    11390  10621   8415    368   -341     16       C  
ATOM   2769  N   THR A1151     -24.250  -6.190  77.957  1.00 75.30           N  
ANISOU 2769  N   THR A1151    10457  10711   7442   1128   -654    512       N  
ATOM   2770  CA  THR A1151     -25.470  -5.979  77.167  1.00 77.19           C  
ANISOU 2770  CA  THR A1151    10620  11099   7611   1404   -726    589       C  
ATOM   2771  C   THR A1151     -26.374  -7.220  77.190  1.00 81.30           C  
ANISOU 2771  C   THR A1151    10874  11942   8076   1356   -871    511       C  
ATOM   2772  O   THR A1151     -27.589  -7.070  77.305  1.00 82.58           O  
ANISOU 2772  O   THR A1151    10876  12267   8233   1526   -909    474       O  
ATOM   2773  CB  THR A1151     -25.152  -5.366  75.786  1.00 86.23           C  
ANISOU 2773  CB  THR A1151    11945  12133   8687   1587   -710    770       C  
ATOM   2774  OG1 THR A1151     -24.895  -3.973  75.968  1.00 87.74           O  
ANISOU 2774  OG1 THR A1151    12352  12018   8967   1705   -543    832       O  
ATOM   2775  CG2 THR A1151     -26.283  -5.521  74.779  1.00 86.12           C  
ANISOU 2775  CG2 THR A1151    11820  12364   8539   1865   -852    840       C  
ATOM   2776  N   THR A1152     -25.781  -8.433  77.149  1.00 76.53           N  
ANISOU 2776  N   THR A1152    10213  11416   7450   1119   -934    473       N  
ATOM   2777  CA  THR A1152     -26.516  -9.703  77.221  1.00 76.49           C  
ANISOU 2777  CA  THR A1152     9976  11658   7427   1015  -1041    387       C  
ATOM   2778  C   THR A1152     -27.209  -9.827  78.590  1.00 81.91           C  
ANISOU 2778  C   THR A1152    10528  12412   8182    944   -968    284       C  
ATOM   2779  O   THR A1152     -28.327 -10.336  78.668  1.00 82.48           O  
ANISOU 2779  O   THR A1152    10375  12695   8269    961  -1012    220       O  
ATOM   2780  CB  THR A1152     -25.585 -10.901  76.962  1.00 83.69           C  
ANISOU 2780  CB  THR A1152    10914  12567   8316    785  -1091    375       C  
ATOM   2781  OG1 THR A1152     -24.573 -10.555  76.014  1.00 82.73           O  
ANISOU 2781  OG1 THR A1152    10974  12317   8142    824  -1086    472       O  
ATOM   2782  CG2 THR A1152     -26.341 -12.135  76.490  1.00 82.86           C  
ANISOU 2782  CG2 THR A1152    10610  12683   8191    716  -1217    301       C  
ATOM   2783  N   PHE A1153     -26.545  -9.335  79.657  1.00 78.85           N  
ANISOU 2783  N   PHE A1153    10271  11858   7832    866   -849    257       N  
ATOM   2784  CA  PHE A1153     -27.067  -9.327  81.022  1.00 79.28           C  
ANISOU 2784  CA  PHE A1153    10246  11963   7912    823   -755    166       C  
ATOM   2785  C   PHE A1153     -28.200  -8.323  81.181  1.00 86.86           C  
ANISOU 2785  C   PHE A1153    11129  12974   8899   1068   -703    140       C  
ATOM   2786  O   PHE A1153     -29.101  -8.546  81.992  1.00 88.17           O  
ANISOU 2786  O   PHE A1153    11131  13290   9078   1071   -644     66       O  
ATOM   2787  CB  PHE A1153     -25.956  -8.992  82.029  1.00 79.90           C  
ANISOU 2787  CB  PHE A1153    10501  11865   7991    704   -671    120       C  
ATOM   2788  CG  PHE A1153     -25.097 -10.153  82.460  1.00 79.42           C  
ANISOU 2788  CG  PHE A1153    10458  11825   7892    476   -700    111       C  
ATOM   2789  CD1 PHE A1153     -25.673 -11.339  82.908  1.00 82.02           C  
ANISOU 2789  CD1 PHE A1153    10653  12316   8197    365   -700    102       C  
ATOM   2790  CD2 PHE A1153     -23.714 -10.039  82.486  1.00 80.25           C  
ANISOU 2790  CD2 PHE A1153    10713  11783   7996    377   -711    107       C  
ATOM   2791  CE1 PHE A1153     -24.877 -12.405  83.332  1.00 81.67           C  
ANISOU 2791  CE1 PHE A1153    10659  12262   8110    191   -715    115       C  
ATOM   2792  CE2 PHE A1153     -22.919 -11.103  82.915  1.00 81.69           C  
ANISOU 2792  CE2 PHE A1153    10907  11998   8132    212   -748    100       C  
ATOM   2793  CZ  PHE A1153     -23.505 -12.279  83.337  1.00 79.57           C  
ANISOU 2793  CZ  PHE A1153    10541  11870   7824    135   -750    115       C  
ATOM   2794  N   ARG A1154     -28.136  -7.209  80.435  1.00 84.35           N  
ANISOU 2794  N   ARG A1154    10940  12520   8589   1286   -705    210       N  
ATOM   2795  CA  ARG A1154     -29.128  -6.144  80.494  1.00 86.68           C  
ANISOU 2795  CA  ARG A1154    11199  12824   8909   1575   -656    202       C  
ATOM   2796  C   ARG A1154     -30.351  -6.491  79.637  1.00 92.72           C  
ANISOU 2796  C   ARG A1154    11720  13867   9644   1754   -780    221       C  
ATOM   2797  O   ARG A1154     -31.449  -6.632  80.178  1.00 93.43           O  
ANISOU 2797  O   ARG A1154    11576  14161   9762   1818   -759    132       O  
ATOM   2798  CB  ARG A1154     -28.483  -4.803  80.093  1.00 87.59           C  
ANISOU 2798  CB  ARG A1154    11593  12631   9056   1735   -582    282       C  
ATOM   2799  CG  ARG A1154     -29.393  -3.574  80.151  1.00100.78           C  
ANISOU 2799  CG  ARG A1154    13290  14240  10761   2073   -512    288       C  
ATOM   2800  CD  ARG A1154     -28.658  -2.297  79.763  1.00112.55           C  
ANISOU 2800  CD  ARG A1154    15099  15360  12307   2195   -405    380       C  
ATOM   2801  NE  ARG A1154     -27.815  -2.465  78.575  1.00122.32           N  
ANISOU 2801  NE  ARG A1154    16476  16502  13499   2142   -451    538       N  
ATOM   2802  CZ  ARG A1154     -28.219  -2.281  77.321  1.00138.28           C  
ANISOU 2802  CZ  ARG A1154    18524  18583  15431   2392   -525    701       C  
ATOM   2803  NH1 ARG A1154     -27.381  -2.466  76.312  1.00123.97           N  
ANISOU 2803  NH1 ARG A1154    16853  16691  13557   2330   -542    838       N  
ATOM   2804  NH2 ARG A1154     -29.470  -1.908  77.067  1.00127.02           N  
ANISOU 2804  NH2 ARG A1154    16980  17321  13963   2728   -583    724       N  
ATOM   2805  N   THR A1155     -30.148  -6.653  78.316  1.00 90.05           N  
ANISOU 2805  N   THR A1155    11419  13557   9238   1830   -908    321       N  
ATOM   2806  CA  THR A1155     -31.194  -6.947  77.329  1.00 91.82           C  
ANISOU 2806  CA  THR A1155    11423  14063   9401   2023  -1069    322       C  
ATOM   2807  C   THR A1155     -31.863  -8.309  77.520  1.00 96.15           C  
ANISOU 2807  C   THR A1155    11653  14898   9980   1808  -1152    187       C  
ATOM   2808  O   THR A1155     -33.092  -8.394  77.476  1.00 98.08           O  
ANISOU 2808  O   THR A1155    11612  15405  10250   1937  -1212    101       O  
ATOM   2809  CB  THR A1155     -30.674  -6.762  75.883  1.00 98.82           C  
ANISOU 2809  CB  THR A1155    12477  14903  10167   2165  -1176    463       C  
ATOM   2810  OG1 THR A1155     -29.656  -7.727  75.606  1.00 94.51           O  
ANISOU 2810  OG1 THR A1155    12006  14308   9596   1877  -1207    466       O  
ATOM   2811  CG2 THR A1155     -30.159  -5.349  75.613  1.00 98.64           C  
ANISOU 2811  CG2 THR A1155    12769  14579  10130   2399  -1060    620       C  
ATOM   2812  N   GLY A1156     -31.054  -9.348  77.718  1.00 90.70           N  
ANISOU 2812  N   GLY A1156    11011  14150   9302   1488  -1147    166       N  
ATOM   2813  CA  GLY A1156     -31.530 -10.717  77.876  1.00 90.60           C  
ANISOU 2813  CA  GLY A1156    10754  14333   9338   1245  -1196     52       C  
ATOM   2814  C   GLY A1156     -31.671 -11.430  76.550  1.00 96.00           C  
ANISOU 2814  C   GLY A1156    11340  15176   9959   1250  -1392     22       C  
ATOM   2815  O   GLY A1156     -32.279 -12.501  76.480  1.00 96.16           O  
ANISOU 2815  O   GLY A1156    11119  15379  10039   1077  -1456   -104       O  
ATOM   2816  N   THR A1157     -31.112 -10.817  75.487  1.00 93.68           N  
ANISOU 2816  N   THR A1157    11244  14807   9543   1448  -1475    133       N  
ATOM   2817  CA  THR A1157     -31.101 -11.305  74.104  1.00 94.58           C  
ANISOU 2817  CA  THR A1157    11332  15067   9536   1517  -1664    121       C  
ATOM   2818  C   THR A1157     -29.657 -11.386  73.594  1.00 97.22           C  
ANISOU 2818  C   THR A1157    11975  15174   9788   1433  -1631    239       C  
ATOM   2819  O   THR A1157     -28.747 -10.844  74.223  1.00 95.36           O  
ANISOU 2819  O   THR A1157    11956  14681   9595   1371  -1476    334       O  
ATOM   2820  CB  THR A1157     -31.974 -10.409  73.203  1.00104.86           C  
ANISOU 2820  CB  THR A1157    12562  16557  10722   1918  -1793    159       C  
ATOM   2821  OG1 THR A1157     -31.582  -9.047  73.359  1.00104.67           O  
ANISOU 2821  OG1 THR A1157    12798  16303  10670   2151  -1665    334       O  
ATOM   2822  CG2 THR A1157     -33.464 -10.565  73.477  1.00105.31           C  
ANISOU 2822  CG2 THR A1157    12231  16926  10857   1997  -1874     -3       C  
ATOM   2823  N   TRP A1158     -29.452 -12.046  72.449  1.00 94.96           N  
ANISOU 2823  N   TRP A1158    11694  15001   9386   1437  -1776    211       N  
ATOM   2824  CA  TRP A1158     -28.126 -12.236  71.851  1.00 93.65           C  
ANISOU 2824  CA  TRP A1158    11786  14665   9133   1365  -1742    306       C  
ATOM   2825  C   TRP A1158     -27.798 -11.210  70.768  1.00 99.02           C  
ANISOU 2825  C   TRP A1158    12682  15304   9635   1671  -1748    481       C  
ATOM   2826  O   TRP A1158     -26.808 -11.376  70.047  1.00 97.88           O  
ANISOU 2826  O   TRP A1158    12728  15071   9391   1645  -1723    558       O  
ATOM   2827  CB  TRP A1158     -28.009 -13.650  71.274  1.00 92.30           C  
ANISOU 2827  CB  TRP A1158    11520  14618   8933   1177  -1869    162       C  
ATOM   2828  CG  TRP A1158     -28.381 -14.734  72.233  1.00 92.81           C  
ANISOU 2828  CG  TRP A1158    11392  14698   9172    880  -1845      9       C  
ATOM   2829  CD1 TRP A1158     -29.639 -15.102  72.609  1.00 97.42           C  
ANISOU 2829  CD1 TRP A1158    11682  15476   9857    831  -1900   -137       C  
ATOM   2830  CD2 TRP A1158     -27.481 -15.596  72.935  1.00 90.50           C  
ANISOU 2830  CD2 TRP A1158    11193  14218   8975    600  -1741      0       C  
ATOM   2831  NE1 TRP A1158     -29.581 -16.181  73.457  1.00 96.23           N  
ANISOU 2831  NE1 TRP A1158    11457  15248   9859    518  -1818   -225       N  
ATOM   2832  CE2 TRP A1158     -28.267 -16.489  73.697  1.00 95.24           C  
ANISOU 2832  CE2 TRP A1158    11579  14885   9721    392  -1726   -133       C  
ATOM   2833  CE3 TRP A1158     -26.082 -15.696  73.004  1.00 89.54           C  
ANISOU 2833  CE3 TRP A1158    11306  13884   8830    516  -1653     95       C  
ATOM   2834  CZ2 TRP A1158     -27.701 -17.475  74.510  1.00 93.06           C  
ANISOU 2834  CZ2 TRP A1158    11359  14451   9547    128  -1624   -149       C  
ATOM   2835  CZ3 TRP A1158     -25.524 -16.667  73.815  1.00 89.60           C  
ANISOU 2835  CZ3 TRP A1158    11337  13768   8938    270  -1580     57       C  
ATOM   2836  CH2 TRP A1158     -26.329 -17.559  74.536  1.00 90.82           C  
ANISOU 2836  CH2 TRP A1158    11317  13974   9216     91  -1567    -52       C  
ATOM   2837  N   ASP A1159     -28.617 -10.146  70.665  1.00 97.80           N  
ANISOU 2837  N   ASP A1159    12511  15208   9442   1974  -1760    554       N  
ATOM   2838  CA  ASP A1159     -28.495  -9.055  69.687  1.00 99.48           C  
ANISOU 2838  CA  ASP A1159    12948  15372   9480   2323  -1746    754       C  
ATOM   2839  C   ASP A1159     -27.108  -8.390  69.627  1.00101.94           C  
ANISOU 2839  C   ASP A1159    13601  15334   9799   2266  -1529    945       C  
ATOM   2840  O   ASP A1159     -26.729  -7.870  68.576  1.00102.89           O  
ANISOU 2840  O   ASP A1159    13935  15413   9745   2478  -1502   1116       O  
ATOM   2841  CB  ASP A1159     -29.619  -8.024  69.885  1.00103.83           C  
ANISOU 2841  CB  ASP A1159    13419  15996  10036   2651  -1765    795       C  
ATOM   2842  CG  ASP A1159     -31.020  -8.614  69.858  1.00114.81           C  
ANISOU 2842  CG  ASP A1159    14427  17771  11426   2727  -1978    595       C  
ATOM   2843  OD1 ASP A1159     -31.287  -9.479  68.993  1.00116.02           O  
ANISOU 2843  OD1 ASP A1159    14440  18190  11454   2719  -2177    480       O  
ATOM   2844  OD2 ASP A1159     -31.857  -8.194  70.686  1.00120.87           O  
ANISOU 2844  OD2 ASP A1159    15024  18582  12321   2796  -1943    536       O  
ATOM   2845  N   ALA A1160     -26.332  -8.473  70.729  1.00 96.40           N  
ANISOU 2845  N   ALA A1160    12939  14402   9287   1972  -1376    906       N  
ATOM   2846  CA  ALA A1160     -24.966  -7.952  70.841  1.00 95.25           C  
ANISOU 2846  CA  ALA A1160    13049  13942   9199   1846  -1173   1026       C  
ATOM   2847  C   ALA A1160     -23.952  -8.800  70.037  1.00 98.50           C  
ANISOU 2847  C   ALA A1160    13531  14379   9513   1704  -1187   1038       C  
ATOM   2848  O   ALA A1160     -22.770  -8.445  69.973  1.00 97.65           O  
ANISOU 2848  O   ALA A1160    13606  14049   9447   1598  -1019   1132       O  
ATOM   2849  CB  ALA A1160     -24.558  -7.901  72.307  1.00 93.95           C  
ANISOU 2849  CB  ALA A1160    12849  13601   9245   1590  -1059    927       C  
ATOM   2850  N   TYR A1161     -24.419  -9.911  69.427  1.00 94.88           N  
ANISOU 2850  N   TYR A1161    12917  14194   8938   1698  -1379    923       N  
ATOM   2851  CA  TYR A1161     -23.600 -10.839  68.646  1.00108.94           C  
ANISOU 2851  CA  TYR A1161    14746  16031  10615   1588  -1413    896       C  
ATOM   2852  C   TYR A1161     -24.245 -11.129  67.296  1.00137.48           C  
ANISOU 2852  C   TYR A1161    18340  19917  13977   1833  -1592    888       C  
ATOM   2853  O   TYR A1161     -23.550 -11.498  66.353  1.00 98.50           O  
ANISOU 2853  O   TYR A1161    13525  15016   8884   1855  -1585    925       O  
ATOM   2854  CB  TYR A1161     -23.387 -12.147  69.431  1.00107.35           C  
ANISOU 2854  CB  TYR A1161    14378  15860  10550   1274  -1469    704       C  
ATOM   2855  CG  TYR A1161     -22.710 -11.952  70.772  1.00106.42           C  
ANISOU 2855  CG  TYR A1161    14280  15519  10635   1055  -1320    699       C  
ATOM   2856  CD1 TYR A1161     -21.322 -11.941  70.880  1.00107.11           C  
ANISOU 2856  CD1 TYR A1161    14501  15427  10771    912  -1185    749       C  
ATOM   2857  CD2 TYR A1161     -23.456 -11.797  71.937  1.00106.52           C  
ANISOU 2857  CD2 TYR A1161    14162  15530  10781   1000  -1318    627       C  
ATOM   2858  CE1 TYR A1161     -20.693 -11.753  72.109  1.00106.25           C  
ANISOU 2858  CE1 TYR A1161    14392  15151  10828    729  -1080    716       C  
ATOM   2859  CE2 TYR A1161     -22.839 -11.602  73.172  1.00105.68           C  
ANISOU 2859  CE2 TYR A1161    14086  15247  10821    826  -1197    608       C  
ATOM   2860  CZ  TYR A1161     -21.456 -11.583  73.252  1.00111.44           C  
ANISOU 2860  CZ  TYR A1161    14945  15812  11586    694  -1093    645       C  
ATOM   2861  OH  TYR A1161     -20.839 -11.409  74.464  1.00111.51           O  
ANISOU 2861  OH  TYR A1161    14963  15686  11719    536  -1006    597       O  
ATOM   2862  N   HIS A 232     -33.239 -12.638  63.283  1.00152.47           N  
ANISOU 2862  N   HIS A 232    23824  19538  14571  -3025    827   1534       N  
ATOM   2863  CA  HIS A 232     -34.548 -12.127  62.741  1.00152.27           C  
ANISOU 2863  CA  HIS A 232    23533  19661  14664  -2922   1175   1446       C  
ATOM   2864  C   HIS A 232     -35.179 -10.878  62.213  1.00154.36           C  
ANISOU 2864  C   HIS A 232    23603  20030  15016  -2755   1404   1350       C  
ATOM   2865  O   HIS A 232     -36.227 -10.943  61.569  1.00154.12           O  
ANISOU 2865  O   HIS A 232    23275  20136  15147  -2676   1614   1306       O  
ATOM   2866  CB  HIS A 232     -35.137 -12.353  64.110  1.00156.04           C  
ANISOU 2866  CB  HIS A 232    24373  20038  14875  -3109   1386   1462       C  
ATOM   2867  CG  HIS A 232     -36.150 -13.456  64.137  1.00160.66           C  
ANISOU 2867  CG  HIS A 232    24857  20682  15505  -3215   1555   1486       C  
ATOM   2868  ND1 HIS A 232     -36.841 -13.859  63.014  1.00161.27           N  
ANISOU 2868  ND1 HIS A 232    24516  20917  15843  -3120   1621   1463       N  
ATOM   2869  CD2 HIS A 232     -36.589 -14.239  65.150  1.00164.78           C  
ANISOU 2869  CD2 HIS A 232    25652  21124  15834  -3425   1666   1536       C  
ATOM   2870  CE1 HIS A 232     -37.661 -14.844  63.335  1.00162.19           C  
ANISOU 2870  CE1 HIS A 232    24644  21049  15933  -3272   1760   1499       C  
ATOM   2871  NE2 HIS A 232     -37.528 -15.093  64.625  1.00164.76           N  
ANISOU 2871  NE2 HIS A 232    25384  21234  15985  -3459   1797   1545       N  
ATOM   2872  N   GLN A 233     -34.579  -9.727  62.503  1.00149.11           N  
ANISOU 2872  N   GLN A 233    23115  19296  14243  -2705   1361   1320       N  
ATOM   2873  CA  GLN A 233     -35.163  -8.430  62.049  1.00147.76           C  
ANISOU 2873  CA  GLN A 233    22803  19197  14142  -2535   1574   1226       C  
ATOM   2874  C   GLN A 233     -34.165  -8.081  60.944  1.00146.74           C  
ANISOU 2874  C   GLN A 233    22457  19112  14185  -2415   1284   1240       C  
ATOM   2875  O   GLN A 233     -34.585  -7.492  59.944  1.00145.05           O  
ANISOU 2875  O   GLN A 233    21947  19011  14153  -2251   1361   1188       O  
ATOM   2876  CB  GLN A 233     -35.217  -7.318  63.135  1.00151.10           C  
ANISOU 2876  CB  GLN A 233    23606  19494  14309  -2564   1740   1174       C  
ATOM   2877  CG  GLN A 233     -36.596  -7.187  63.792  1.00168.51           C  
ANISOU 2877  CG  GLN A 233    25873  21727  16426  -2574   2159   1109       C  
ATOM   2878  CD  GLN A 233     -37.592  -6.351  63.010  1.00185.81           C  
ANISOU 2878  CD  GLN A 233    27747  24048  18805  -2360   2413   1019       C  
ATOM   2879  OE1 GLN A 233     -37.367  -5.950  61.857  1.00178.71           O  
ANISOU 2879  OE1 GLN A 233    26552  23231  18119  -2204   2280   1007       O  
ATOM   2880  NE2 GLN A 233     -38.729  -6.065  63.631  1.00178.78           N  
ANISOU 2880  NE2 GLN A 233    26913  23179  17835  -2345   2788    953       N  
ATOM   2881  N   LYS A 234     -32.881  -8.472  61.089  1.00140.87           N  
ANISOU 2881  N   LYS A 234    21842  18288  13393  -2495    955   1313       N  
ATOM   2882  CA  LYS A 234     -31.809  -8.278  60.055  1.00137.68           C  
ANISOU 2882  CA  LYS A 234    21222  17938  13153  -2401    666   1336       C  
ATOM   2883  C   LYS A 234     -31.998  -9.237  58.907  1.00137.61           C  
ANISOU 2883  C   LYS A 234    20839  18059  13388  -2325    600   1348       C  
ATOM   2884  O   LYS A 234     -31.440  -9.001  57.830  1.00135.45           O  
ANISOU 2884  O   LYS A 234    20317  17868  13279  -2214    451   1343       O  
ATOM   2885  CB  LYS A 234     -30.464  -8.457  60.733  1.00140.66           C  
ANISOU 2885  CB  LYS A 234    21862  18190  13393  -2522    360   1414       C  
ATOM   2886  N   ARG A 235     -32.766 -10.329  59.122  1.00132.87           N  
ANISOU 2886  N   ARG A 235    20211  17472  12801  -2397    708   1364       N  
ATOM   2887  CA  ARG A 235     -33.088 -11.342  58.118  1.00130.50           C  
ANISOU 2887  CA  ARG A 235    19595  17277  12711  -2349    662   1373       C  
ATOM   2888  C   ARG A 235     -34.046 -10.769  57.070  1.00130.57           C  
ANISOU 2888  C   ARG A 235    19272  17438  12902  -2202    854   1302       C  
ATOM   2889  O   ARG A 235     -33.883 -11.055  55.882  1.00128.58           O  
ANISOU 2889  O   ARG A 235    18732  17282  12841  -2106    739   1296       O  
ATOM   2890  CB  ARG A 235     -33.692 -12.597  58.780  1.00132.53           C  
ANISOU 2890  CB  ARG A 235    19969  17485  12901  -2500    732   1415       C  
ATOM   2891  CG  ARG A 235     -32.663 -13.623  59.246  1.00143.50           C  
ANISOU 2891  CG  ARG A 235    21553  18750  14219  -2605    443   1500       C  
ATOM   2892  CD  ARG A 235     -32.140 -14.471  58.095  1.00151.77           C  
ANISOU 2892  CD  ARG A 235    22329  19856  15481  -2516    221   1515       C  
ATOM   2893  NE  ARG A 235     -32.094 -15.892  58.436  1.00160.55           N  
ANISOU 2893  NE  ARG A 235    23554  20879  16571  -2628    105   1579       N  
ATOM   2894  CZ  ARG A 235     -31.055 -16.501  58.999  1.00175.53           C  
ANISOU 2894  CZ  ARG A 235    25665  22642  18387  -2687   -160   1651       C  
ATOM   2895  NH1 ARG A 235     -29.959 -15.815  59.303  1.00163.29           N  
ANISOU 2895  NH1 ARG A 235    24226  21044  16774  -2658   -338   1672       N  
ATOM   2896  NH2 ARG A 235     -31.106 -17.797  59.271  1.00163.12           N  
ANISOU 2896  NH2 ARG A 235    24202  20977  16799  -2781   -258   1707       N  
ATOM   2897  N   LYS A 236     -35.025  -9.937  57.512  1.00125.88           N  
ANISOU 2897  N   LYS A 236    18727  16860  12242  -2177   1143   1248       N  
ATOM   2898  CA  LYS A 236     -36.004  -9.269  56.645  1.00123.85           C  
ANISOU 2898  CA  LYS A 236    18174  16735  12149  -2026   1335   1184       C  
ATOM   2899  C   LYS A 236     -35.312  -8.293  55.699  1.00121.97           C  
ANISOU 2899  C   LYS A 236    17804  16532  12007  -1879   1189   1161       C  
ATOM   2900  O   LYS A 236     -35.777  -8.101  54.577  1.00120.06           O  
ANISOU 2900  O   LYS A 236    17257  16410  11951  -1755   1212   1133       O  
ATOM   2901  CB  LYS A 236     -37.083  -8.550  57.471  1.00128.58           C  
ANISOU 2901  CB  LYS A 236    18890  17324  12642  -2019   1671   1130       C  
ATOM   2902  CG  LYS A 236     -38.171  -9.478  58.006  1.00145.10           C  
ANISOU 2902  CG  LYS A 236    20961  19456  14716  -2136   1888   1142       C  
ATOM   2903  CD  LYS A 236     -39.340  -8.709  58.619  1.00157.60           C  
ANISOU 2903  CD  LYS A 236    22573  21067  16240  -2091   2256   1077       C  
ATOM   2904  CE  LYS A 236     -39.234  -8.570  60.122  1.00170.76           C  
ANISOU 2904  CE  LYS A 236    24667  22593  17619  -2228   2390   1076       C  
ATOM   2905  NZ  LYS A 236     -40.353  -7.764  60.684  1.00180.90           N  
ANISOU 2905  NZ  LYS A 236    25978  23908  18848  -2160   2771    999       N  
ATOM   2906  N   ALA A 237     -34.187  -7.702  56.155  1.00115.96           N  
ANISOU 2906  N   ALA A 237    17281  15666  11113  -1910   1026   1179       N  
ATOM   2907  CA  ALA A 237     -33.347  -6.779  55.387  1.00113.06           C  
ANISOU 2907  CA  ALA A 237    16837  15316  10804  -1812    863   1171       C  
ATOM   2908  C   ALA A 237     -32.580  -7.540  54.303  1.00111.42           C  
ANISOU 2908  C   ALA A 237    16385  15190  10758  -1785    618   1208       C  
ATOM   2909  O   ALA A 237     -32.393  -7.011  53.208  1.00109.69           O  
ANISOU 2909  O   ALA A 237    15951  15056  10669  -1674    558   1189       O  
ATOM   2910  CB  ALA A 237     -32.376  -6.062  56.312  1.00114.52           C  
ANISOU 2910  CB  ALA A 237    17364  15363  10787  -1893    753   1192       C  
ATOM   2911  N   LEU A 238     -32.154  -8.784  54.610  1.00105.34           N  
ANISOU 2911  N   LEU A 238    15662  14386   9975  -1884    483   1259       N  
ATOM   2912  CA  LEU A 238     -31.447  -9.669  53.687  1.00102.58           C  
ANISOU 2912  CA  LEU A 238    15107  14097   9770  -1854    264   1288       C  
ATOM   2913  C   LEU A 238     -32.384 -10.164  52.568  1.00103.79           C  
ANISOU 2913  C   LEU A 238    14947  14378  10110  -1771    360   1252       C  
ATOM   2914  O   LEU A 238     -31.961 -10.208  51.415  1.00102.35           O  
ANISOU 2914  O   LEU A 238    14542  14280  10065  -1682    239   1242       O  
ATOM   2915  CB  LEU A 238     -30.800 -10.844  54.455  1.00103.08           C  
ANISOU 2915  CB  LEU A 238    15350  14061   9756  -1974     99   1351       C  
ATOM   2916  CG  LEU A 238     -30.108 -11.953  53.644  1.00106.48           C  
ANISOU 2916  CG  LEU A 238    15602  14527  10327  -1937   -118   1377       C  
ATOM   2917  CD1 LEU A 238     -28.817 -11.465  53.002  1.00105.53           C  
ANISOU 2917  CD1 LEU A 238    15379  14447  10269  -1862   -329   1388       C  
ATOM   2918  CD2 LEU A 238     -29.830 -13.162  54.508  1.00109.74           C  
ANISOU 2918  CD2 LEU A 238    16215  14822  10659  -2052   -232   1437       C  
ATOM   2919  N   LYS A 239     -33.647 -10.512  52.900  1.00 99.46           N  
ANISOU 2919  N   LYS A 239    14381  13847   9563  -1808    576   1235       N  
ATOM   2920  CA  LYS A 239     -34.632 -10.982  51.920  1.00 98.26           C  
ANISOU 2920  CA  LYS A 239    13938  13815   9583  -1753    664   1209       C  
ATOM   2921  C   LYS A 239     -35.109  -9.866  50.994  1.00100.48           C  
ANISOU 2921  C   LYS A 239    14008  14198   9973  -1607    751   1161       C  
ATOM   2922  O   LYS A 239     -35.368 -10.131  49.821  1.00 99.31           O  
ANISOU 2922  O   LYS A 239    13603  14151   9981  -1537    702   1147       O  
ATOM   2923  CB  LYS A 239     -35.813 -11.692  52.593  1.00102.49           C  
ANISOU 2923  CB  LYS A 239    14506  14348  10088  -1857    863   1216       C  
ATOM   2924  CG  LYS A 239     -36.267 -12.931  51.826  1.00121.16           C  
ANISOU 2924  CG  LYS A 239    16669  16775  12592  -1891    807   1228       C  
ATOM   2925  CD  LYS A 239     -37.341 -13.734  52.562  1.00135.79           C  
ANISOU 2925  CD  LYS A 239    18574  18619  14402  -2034    984   1250       C  
ATOM   2926  CE  LYS A 239     -38.717 -13.565  51.952  1.00147.31           C  
ANISOU 2926  CE  LYS A 239    19750  20218  16003  -1995   1180   1219       C  
ATOM   2927  NZ  LYS A 239     -39.697 -14.533  52.518  1.00156.70           N  
ANISOU 2927  NZ  LYS A 239    20950  21414  17173  -2160   1324   1250       N  
ATOM   2928  N   THR A 240     -35.186  -8.617  51.503  1.00 96.79           N  
ANISOU 2928  N   THR A 240    13669  13691   9414  -1561    865   1136       N  
ATOM   2929  CA  THR A 240     -35.569  -7.428  50.722  1.00 95.77           C  
ANISOU 2929  CA  THR A 240    13389  13628   9370  -1415    934   1095       C  
ATOM   2930  C   THR A 240     -34.474  -7.159  49.672  1.00 96.08           C  
ANISOU 2930  C   THR A 240    13329  13702   9474  -1358    703   1107       C  
ATOM   2931  O   THR A 240     -34.764  -6.751  48.545  1.00 94.82           O  
ANISOU 2931  O   THR A 240    12952  13634   9443  -1253    691   1087       O  
ATOM   2932  CB  THR A 240     -35.803  -6.223  51.662  1.00106.55           C  
ANISOU 2932  CB  THR A 240    14981  14906  10597  -1389   1100   1065       C  
ATOM   2933  OG1 THR A 240     -36.737  -6.590  52.680  1.00108.40           O  
ANISOU 2933  OG1 THR A 240    15318  15113  10756  -1457   1324   1054       O  
ATOM   2934  CG2 THR A 240     -36.320  -4.989  50.931  1.00105.73           C  
ANISOU 2934  CG2 THR A 240    14743  14848  10580  -1227   1183   1023       C  
ATOM   2935  N   THR A 241     -33.224  -7.444  50.048  1.00 90.81           N  
ANISOU 2935  N   THR A 241    12816  12966   8720  -1434    518   1143       N  
ATOM   2936  CA  THR A 241     -32.043  -7.308  49.208  1.00 88.43           C  
ANISOU 2936  CA  THR A 241    12431  12701   8466  -1403    303   1160       C  
ATOM   2937  C   THR A 241     -32.059  -8.378  48.106  1.00 88.65           C  
ANISOU 2937  C   THR A 241    12211  12826   8645  -1371    211   1158       C  
ATOM   2938  O   THR A 241     -31.878  -8.033  46.939  1.00 87.37           O  
ANISOU 2938  O   THR A 241    11866  12751   8579  -1290    152   1142       O  
ATOM   2939  CB  THR A 241     -30.780  -7.391  50.081  1.00 96.52           C  
ANISOU 2939  CB  THR A 241    13685  13627   9360  -1501    140   1205       C  
ATOM   2940  OG1 THR A 241     -30.852  -6.426  51.132  1.00 96.91           O  
ANISOU 2940  OG1 THR A 241    13996  13574   9252  -1544    230   1203       O  
ATOM   2941  CG2 THR A 241     -29.528  -7.173  49.295  1.00 94.44           C  
ANISOU 2941  CG2 THR A 241    13322  13413   9146  -1475    -67   1226       C  
ATOM   2942  N   VAL A 242     -32.278  -9.664  48.479  1.00 83.33           N  
ANISOU 2942  N   VAL A 242    11557  12126   7979  -1443    198   1174       N  
ATOM   2943  CA  VAL A 242     -32.312 -10.814  47.564  1.00 81.38           C  
ANISOU 2943  CA  VAL A 242    11125  11939   7854  -1427    109   1168       C  
ATOM   2944  C   VAL A 242     -33.312 -10.600  46.422  1.00 82.79           C  
ANISOU 2944  C   VAL A 242    11058  12233   8165  -1347    199   1131       C  
ATOM   2945  O   VAL A 242     -32.940 -10.796  45.264  1.00 81.09           O  
ANISOU 2945  O   VAL A 242    10682  12090   8040  -1287     91   1115       O  
ATOM   2946  CB  VAL A 242     -32.463 -12.182  48.302  1.00 85.83           C  
ANISOU 2946  CB  VAL A 242    11802  12425   8384  -1533     87   1196       C  
ATOM   2947  CG1 VAL A 242     -32.725 -13.331  47.331  1.00 85.25           C  
ANISOU 2947  CG1 VAL A 242    11552  12402   8436  -1517     19   1181       C  
ATOM   2948  CG2 VAL A 242     -31.231 -12.487  49.149  1.00 85.81           C  
ANISOU 2948  CG2 VAL A 242    12011  12315   8277  -1591    -77   1241       C  
ATOM   2949  N   ILE A 243     -34.546 -10.131  46.743  1.00 78.94           N  
ANISOU 2949  N   ILE A 243    10544  11765   7684  -1340    396   1117       N  
ATOM   2950  CA  ILE A 243     -35.594  -9.825  45.750  1.00 77.80           C  
ANISOU 2950  CA  ILE A 243    10162  11729   7671  -1261    478   1090       C  
ATOM   2951  C   ILE A 243     -35.086  -8.772  44.755  1.00 78.19           C  
ANISOU 2951  C   ILE A 243    10122  11829   7757  -1151    398   1076       C  
ATOM   2952  O   ILE A 243     -35.163  -9.003  43.552  1.00 77.31           O  
ANISOU 2952  O   ILE A 243     9829  11800   7746  -1105    319   1064       O  
ATOM   2953  CB  ILE A 243     -36.948  -9.404  46.400  1.00 82.21           C  
ANISOU 2953  CB  ILE A 243    10702  12299   8235  -1259    713   1081       C  
ATOM   2954  CG1 ILE A 243     -37.525 -10.528  47.301  1.00 83.64           C  
ANISOU 2954  CG1 ILE A 243    10955  12445   8379  -1394    803   1101       C  
ATOM   2955  CG2 ILE A 243     -37.972  -8.969  45.325  1.00 82.69           C  
ANISOU 2955  CG2 ILE A 243    10496  12476   8447  -1158    768   1061       C  
ATOM   2956  CD1 ILE A 243     -38.452 -10.037  48.443  1.00 92.95           C  
ANISOU 2956  CD1 ILE A 243    12229  13600   9487  -1420   1054   1094       C  
ATOM   2957  N   LEU A 244     -34.537  -7.648  45.268  1.00 72.80           N  
ANISOU 2957  N   LEU A 244     9594  11089   6979  -1125    412   1079       N  
ATOM   2958  CA  LEU A 244     -33.986  -6.538  44.483  1.00 71.34           C  
ANISOU 2958  CA  LEU A 244     9374  10931   6800  -1046    339   1074       C  
ATOM   2959  C   LEU A 244     -32.936  -6.985  43.457  1.00 73.17           C  
ANISOU 2959  C   LEU A 244     9509  11221   7073  -1047    152   1081       C  
ATOM   2960  O   LEU A 244     -33.001  -6.539  42.315  1.00 72.46           O  
ANISOU 2960  O   LEU A 244     9278  11205   7047   -980    112   1071       O  
ATOM   2961  CB  LEU A 244     -33.430  -5.440  45.418  1.00 71.82           C  
ANISOU 2961  CB  LEU A 244     9672  10892   6725  -1060    365   1083       C  
ATOM   2962  CG  LEU A 244     -32.777  -4.194  44.788  1.00 75.32           C  
ANISOU 2962  CG  LEU A 244    10134  11337   7146  -1007    286   1087       C  
ATOM   2963  CD1 LEU A 244     -33.814  -3.255  44.175  1.00 75.65           C  
ANISOU 2963  CD1 LEU A 244    10077  11408   7259   -888    392   1065       C  
ATOM   2964  CD2 LEU A 244     -31.965  -3.441  45.820  1.00 77.12           C  
ANISOU 2964  CD2 LEU A 244    10629  11452   7222  -1070    261   1105       C  
ATOM   2965  N   ILE A 245     -31.994  -7.865  43.851  1.00 69.08           N  
ANISOU 2965  N   ILE A 245     9065  10668   6514  -1116     41   1098       N  
ATOM   2966  CA  ILE A 245     -30.944  -8.381  42.959  1.00 67.98           C  
ANISOU 2966  CA  ILE A 245     8829  10584   6416  -1105   -119   1098       C  
ATOM   2967  C   ILE A 245     -31.516  -9.396  41.940  1.00 72.85           C  
ANISOU 2967  C   ILE A 245     9265  11272   7142  -1076   -135   1069       C  
ATOM   2968  O   ILE A 245     -31.284  -9.255  40.734  1.00 71.46           O  
ANISOU 2968  O   ILE A 245     8955  11178   7019  -1024   -193   1050       O  
ATOM   2969  CB  ILE A 245     -29.711  -8.930  43.740  1.00 70.76           C  
ANISOU 2969  CB  ILE A 245     9312  10872   6702  -1168   -243   1127       C  
ATOM   2970  CG1 ILE A 245     -29.091  -7.841  44.640  1.00 71.35           C  
ANISOU 2970  CG1 ILE A 245     9570  10879   6661  -1212   -254   1159       C  
ATOM   2971  CG2 ILE A 245     -28.662  -9.511  42.778  1.00 70.83           C  
ANISOU 2971  CG2 ILE A 245     9191  10950   6772  -1132   -388   1119       C  
ATOM   2972  CD1 ILE A 245     -28.005  -8.313  45.621  1.00 79.33           C  
ANISOU 2972  CD1 ILE A 245    10734  11812   7596  -1289   -383   1201       C  
ATOM   2973  N   LEU A 246     -32.256 -10.409  42.438  1.00 71.31           N  
ANISOU 2973  N   LEU A 246     9086  11040   6968  -1125    -85   1068       N  
ATOM   2974  CA  LEU A 246     -32.881 -11.479  41.651  1.00 71.68           C  
ANISOU 2974  CA  LEU A 246     8999  11130   7106  -1128   -104   1044       C  
ATOM   2975  C   LEU A 246     -33.855 -10.930  40.601  1.00 74.95           C  
ANISOU 2975  C   LEU A 246     9237  11637   7601  -1072    -51   1026       C  
ATOM   2976  O   LEU A 246     -33.830 -11.391  39.458  1.00 74.44           O  
ANISOU 2976  O   LEU A 246     9055  11632   7596  -1047   -129   1001       O  
ATOM   2977  CB  LEU A 246     -33.591 -12.476  42.594  1.00 73.15           C  
ANISOU 2977  CB  LEU A 246     9267  11246   7281  -1220    -42   1060       C  
ATOM   2978  CG  LEU A 246     -33.497 -13.971  42.266  1.00 78.73           C  
ANISOU 2978  CG  LEU A 246     9961  11924   8028  -1263   -138   1049       C  
ATOM   2979  CD1 LEU A 246     -32.052 -14.461  42.254  1.00 78.76           C  
ANISOU 2979  CD1 LEU A 246    10045  11879   8002  -1233   -294   1048       C  
ATOM   2980  CD2 LEU A 246     -34.260 -14.784  43.281  1.00 82.76           C  
ANISOU 2980  CD2 LEU A 246    10575  12361   8510  -1376    -63   1076       C  
ATOM   2981  N   ALA A 247     -34.679  -9.922  40.976  1.00 71.34           N  
ANISOU 2981  N   ALA A 247     8773  11188   7144  -1045     76   1035       N  
ATOM   2982  CA  ALA A 247     -35.640  -9.286  40.072  1.00 71.17           C  
ANISOU 2982  CA  ALA A 247     8587  11247   7208   -978    117   1027       C  
ATOM   2983  C   ALA A 247     -34.928  -8.514  38.974  1.00 74.91           C  
ANISOU 2983  C   ALA A 247     9017  11769   7677   -910     17   1021       C  
ATOM   2984  O   ALA A 247     -35.403  -8.511  37.842  1.00 74.31           O  
ANISOU 2984  O   ALA A 247     8800  11764   7669   -875    -28   1012       O  
ATOM   2985  CB  ALA A 247     -36.569  -8.362  40.837  1.00 72.71           C  
ANISOU 2985  CB  ALA A 247     8800  11424   7403   -942    280   1036       C  
ATOM   2986  N   PHE A 248     -33.779  -7.885  39.304  1.00 71.86           N  
ANISOU 2986  N   PHE A 248     8758  11344   7203   -908    -26   1031       N  
ATOM   2987  CA  PHE A 248     -32.956  -7.114  38.371  1.00 71.36           C  
ANISOU 2987  CA  PHE A 248     8674  11325   7115   -870   -113   1033       C  
ATOM   2988  C   PHE A 248     -32.419  -8.003  37.258  1.00 75.06           C  
ANISOU 2988  C   PHE A 248     9042  11861   7615   -875   -221   1008       C  
ATOM   2989  O   PHE A 248     -32.528  -7.634  36.089  1.00 73.92           O  
ANISOU 2989  O   PHE A 248     8808  11784   7493   -840   -262   1001       O  
ATOM   2990  CB  PHE A 248     -31.803  -6.414  39.110  1.00 73.06           C  
ANISOU 2990  CB  PHE A 248     9046  11484   7229   -899   -141   1055       C  
ATOM   2991  CG  PHE A 248     -30.947  -5.515  38.249  1.00 74.45           C  
ANISOU 2991  CG  PHE A 248     9210  11707   7370   -885   -219   1066       C  
ATOM   2992  CD1 PHE A 248     -31.253  -4.168  38.104  1.00 77.87           C  
ANISOU 2992  CD1 PHE A 248     9693  12120   7776   -849   -185   1084       C  
ATOM   2993  CD2 PHE A 248     -29.802  -6.003  37.627  1.00 76.30           C  
ANISOU 2993  CD2 PHE A 248     9396  12000   7596   -909   -320   1061       C  
ATOM   2994  CE1 PHE A 248     -30.437  -3.329  37.338  1.00 78.51           C  
ANISOU 2994  CE1 PHE A 248     9784  12236   7809   -860   -260   1104       C  
ATOM   2995  CE2 PHE A 248     -28.990  -5.162  36.862  1.00 78.75           C  
ANISOU 2995  CE2 PHE A 248     9693  12363   7865   -917   -376   1077       C  
ATOM   2996  CZ  PHE A 248     -29.312  -3.832  36.726  1.00 77.00           C  
ANISOU 2996  CZ  PHE A 248     9533  12118   7606   -903   -349   1102       C  
ATOM   2997  N   PHE A 249     -31.840  -9.166  37.618  1.00 72.27           N  
ANISOU 2997  N   PHE A 249     8721  11481   7258   -916   -267    995       N  
ATOM   2998  CA  PHE A 249     -31.295 -10.105  36.641  1.00 72.03           C  
ANISOU 2998  CA  PHE A 249     8617  11498   7253   -906   -357    960       C  
ATOM   2999  C   PHE A 249     -32.382 -10.798  35.821  1.00 76.28           C  
ANISOU 2999  C   PHE A 249     9051  12069   7860   -907   -357    934       C  
ATOM   3000  O   PHE A 249     -32.126 -11.173  34.673  1.00 75.79           O  
ANISOU 3000  O   PHE A 249     8926  12061   7809   -887   -423    901       O  
ATOM   3001  CB  PHE A 249     -30.317 -11.089  37.286  1.00 73.83           C  
ANISOU 3001  CB  PHE A 249     8919  11670   7461   -928   -418    954       C  
ATOM   3002  CG  PHE A 249     -28.971 -10.475  37.584  1.00 75.57           C  
ANISOU 3002  CG  PHE A 249     9189  11897   7626   -923   -468    976       C  
ATOM   3003  CD1 PHE A 249     -27.960 -10.478  36.630  1.00 78.99           C  
ANISOU 3003  CD1 PHE A 249     9543  12409   8060   -888   -532    954       C  
ATOM   3004  CD2 PHE A 249     -28.712  -9.892  38.819  1.00 78.57           C  
ANISOU 3004  CD2 PHE A 249     9695  12209   7949   -965   -450   1019       C  
ATOM   3005  CE1 PHE A 249     -26.705  -9.918  36.913  1.00 80.17           C  
ANISOU 3005  CE1 PHE A 249     9712  12579   8169   -899   -580    982       C  
ATOM   3006  CE2 PHE A 249     -27.456  -9.334  39.102  1.00 81.33           C  
ANISOU 3006  CE2 PHE A 249    10086  12566   8249   -981   -517   1047       C  
ATOM   3007  CZ  PHE A 249     -26.461  -9.355  38.149  1.00 79.25           C  
ANISOU 3007  CZ  PHE A 249     9715  12393   8003   -950   -584   1032       C  
ATOM   3008  N   ALA A 250     -33.607 -10.904  36.381  1.00 72.94           N  
ANISOU 3008  N   ALA A 250     8610  11622   7482   -935   -281    950       N  
ATOM   3009  CA  ALA A 250     -34.764 -11.464  35.685  1.00 73.16           C  
ANISOU 3009  CA  ALA A 250     8523  11688   7586   -955   -285    939       C  
ATOM   3010  C   ALA A 250     -35.151 -10.530  34.526  1.00 77.45           C  
ANISOU 3010  C   ALA A 250     8965  12311   8153   -900   -313    942       C  
ATOM   3011  O   ALA A 250     -35.431 -11.010  33.429  1.00 76.97           O  
ANISOU 3011  O   ALA A 250     8831  12296   8119   -908   -388    920       O  
ATOM   3012  CB  ALA A 250     -35.929 -11.623  36.645  1.00 74.59           C  
ANISOU 3012  CB  ALA A 250     8689  11841   7812  -1002   -179    965       C  
ATOM   3013  N   CYS A 251     -35.098  -9.201  34.764  1.00 74.64           N  
ANISOU 3013  N   CYS A 251     8631  11958   7773   -848   -265    970       N  
ATOM   3014  CA  CYS A 251     -35.386  -8.144  33.794  1.00 75.15           C  
ANISOU 3014  CA  CYS A 251     8633  12074   7845   -791   -298    984       C  
ATOM   3015  C   CYS A 251     -34.406  -8.197  32.623  1.00 79.00           C  
ANISOU 3015  C   CYS A 251     9133  12610   8275   -792   -398    962       C  
ATOM   3016  O   CYS A 251     -34.814  -8.166  31.456  1.00 79.20           O  
ANISOU 3016  O   CYS A 251     9088  12688   8315   -784   -465    958       O  
ATOM   3017  CB  CYS A 251     -35.342  -6.772  34.469  1.00 75.96           C  
ANISOU 3017  CB  CYS A 251     8809  12137   7916   -739   -227   1015       C  
ATOM   3018  SG  CYS A 251     -36.636  -6.494  35.705  1.00 81.27           S  
ANISOU 3018  SG  CYS A 251     9462  12764   8654   -712    -76   1032       S  
ATOM   3019  N   TRP A 252     -33.112  -8.285  32.949  1.00 74.51           N  
ANISOU 3019  N   TRP A 252     8649  12025   7637   -806   -408    951       N  
ATOM   3020  CA  TRP A 252     -32.020  -8.242  31.995  1.00 73.57           C  
ANISOU 3020  CA  TRP A 252     8537  11960   7455   -806   -472    931       C  
ATOM   3021  C   TRP A 252     -31.652  -9.494  31.218  1.00 77.57           C  
ANISOU 3021  C   TRP A 252     9012  12497   7963   -817   -526    875       C  
ATOM   3022  O   TRP A 252     -31.227  -9.358  30.071  1.00 77.09           O  
ANISOU 3022  O   TRP A 252     8935  12500   7857   -812   -566    854       O  
ATOM   3023  CB  TRP A 252     -30.796  -7.591  32.633  1.00 71.63           C  
ANISOU 3023  CB  TRP A 252     8372  11700   7144   -816   -460    952       C  
ATOM   3024  CG  TRP A 252     -30.934  -6.108  32.774  1.00 72.42           C  
ANISOU 3024  CG  TRP A 252     8523  11785   7208   -806   -437    999       C  
ATOM   3025  CD1 TRP A 252     -31.124  -5.408  33.928  1.00 75.21           C  
ANISOU 3025  CD1 TRP A 252     8963  12062   7549   -804   -381   1030       C  
ATOM   3026  CD2 TRP A 252     -30.945  -5.147  31.712  1.00 72.30           C  
ANISOU 3026  CD2 TRP A 252     8500  11815   7155   -797   -472   1018       C  
ATOM   3027  NE1 TRP A 252     -31.213  -4.063  33.656  1.00 74.85           N  
ANISOU 3027  NE1 TRP A 252     8968  12005   7465   -786   -381   1064       N  
ATOM   3028  CE2 TRP A 252     -31.107  -3.874  32.301  1.00 76.56           C  
ANISOU 3028  CE2 TRP A 252     9127  12295   7667   -784   -442   1063       C  
ATOM   3029  CE3 TRP A 252     -30.808  -5.235  30.314  1.00 73.66           C  
ANISOU 3029  CE3 TRP A 252     8623  12064   7300   -804   -528   1003       C  
ATOM   3030  CZ2 TRP A 252     -31.142  -2.695  31.540  1.00 76.29           C  
ANISOU 3030  CZ2 TRP A 252     9131  12268   7587   -776   -477   1098       C  
ATOM   3031  CZ3 TRP A 252     -30.862  -4.072  29.561  1.00 75.30           C  
ANISOU 3031  CZ3 TRP A 252     8867  12289   7456   -805   -560   1041       C  
ATOM   3032  CH2 TRP A 252     -31.019  -2.820  30.172  1.00 76.20           C  
ANISOU 3032  CH2 TRP A 252     9066  12336   7551   -791   -539   1090       C  
ATOM   3033  N   LEU A 253     -31.777 -10.695  31.817  1.00 74.57           N  
ANISOU 3033  N   LEU A 253     8646  12065   7621   -835   -524    850       N  
ATOM   3034  CA  LEU A 253     -31.408 -11.945  31.134  1.00 74.57           C  
ANISOU 3034  CA  LEU A 253     8645  12068   7619   -834   -577    790       C  
ATOM   3035  C   LEU A 253     -31.982 -12.170  29.720  1.00 76.69           C  
ANISOU 3035  C   LEU A 253     8871  12388   7880   -842   -629    757       C  
ATOM   3036  O   LEU A 253     -31.175 -12.474  28.845  1.00 75.60           O  
ANISOU 3036  O   LEU A 253     8749  12288   7689   -820   -655    708       O  
ATOM   3037  CB  LEU A 253     -31.485 -13.196  32.024  1.00 75.12           C  
ANISOU 3037  CB  LEU A 253     8765  12049   7727   -857   -582    774       C  
ATOM   3038  CG  LEU A 253     -30.442 -14.276  31.708  1.00 80.27           C  
ANISOU 3038  CG  LEU A 253     9457  12680   8361   -820   -630    714       C  
ATOM   3039  CD1 LEU A 253     -29.115 -13.995  32.408  1.00 80.41           C  
ANISOU 3039  CD1 LEU A 253     9501  12694   8356   -781   -626    729       C  
ATOM   3040  CD2 LEU A 253     -30.950 -15.649  32.083  1.00 82.95           C  
ANISOU 3040  CD2 LEU A 253     9854  12924   8738   -854   -663    690       C  
ATOM   3041  N   PRO A 254     -33.301 -11.960  29.424  1.00 73.24           N  
ANISOU 3041  N   PRO A 254     8377  11960   7489   -871   -647    783       N  
ATOM   3042  CA  PRO A 254     -33.776 -12.127  28.031  1.00 73.53           C  
ANISOU 3042  CA  PRO A 254     8389  12044   7506   -889   -723    759       C  
ATOM   3043  C   PRO A 254     -33.041 -11.235  27.021  1.00 76.43           C  
ANISOU 3043  C   PRO A 254     8777  12481   7784   -863   -738    756       C  
ATOM   3044  O   PRO A 254     -32.810 -11.665  25.889  1.00 76.41           O  
ANISOU 3044  O   PRO A 254     8805  12509   7719   -875   -786    709       O  
ATOM   3045  CB  PRO A 254     -35.264 -11.766  28.113  1.00 75.70           C  
ANISOU 3045  CB  PRO A 254     8574  12326   7863   -916   -740    811       C  
ATOM   3046  CG  PRO A 254     -35.630 -11.989  29.523  1.00 79.99           C  
ANISOU 3046  CG  PRO A 254     9104  12815   8473   -928   -661    836       C  
ATOM   3047  CD  PRO A 254     -34.422 -11.594  30.314  1.00 74.82           C  
ANISOU 3047  CD  PRO A 254     8529  12134   7766   -889   -599    836       C  
ATOM   3048  N   TYR A 255     -32.635 -10.018  27.448  1.00 71.56           N  
ANISOU 3048  N   TYR A 255     8163  11880   7147   -837   -693    805       N  
ATOM   3049  CA  TYR A 255     -31.884  -9.076  26.620  1.00 70.62           C  
ANISOU 3049  CA  TYR A 255     8075  11822   6936   -833   -700    816       C  
ATOM   3050  C   TYR A 255     -30.466  -9.570  26.408  1.00 72.95           C  
ANISOU 3050  C   TYR A 255     8401  12151   7165   -827   -669    763       C  
ATOM   3051  O   TYR A 255     -29.990  -9.525  25.276  1.00 73.66           O  
ANISOU 3051  O   TYR A 255     8512  12303   7172   -839   -682    733       O  
ATOM   3052  CB  TYR A 255     -31.894  -7.658  27.215  1.00 71.42           C  
ANISOU 3052  CB  TYR A 255     8189  11910   7035   -819   -669    886       C  
ATOM   3053  CG  TYR A 255     -31.000  -6.675  26.490  1.00 73.42           C  
ANISOU 3053  CG  TYR A 255     8493  12217   7185   -837   -675    906       C  
ATOM   3054  CD1 TYR A 255     -31.385  -6.115  25.275  1.00 75.84           C  
ANISOU 3054  CD1 TYR A 255     8820  12560   7434   -855   -737    925       C  
ATOM   3055  CD2 TYR A 255     -29.768  -6.301  27.020  1.00 74.15           C  
ANISOU 3055  CD2 TYR A 255     8616  12324   7233   -852   -627    915       C  
ATOM   3056  CE1 TYR A 255     -30.568  -5.204  24.606  1.00 77.14           C  
ANISOU 3056  CE1 TYR A 255     9048  12773   7491   -892   -738    951       C  
ATOM   3057  CE2 TYR A 255     -28.940  -5.392  26.360  1.00 75.34           C  
ANISOU 3057  CE2 TYR A 255     8809  12532   7287   -893   -628    941       C  
ATOM   3058  CZ  TYR A 255     -29.352  -4.832  25.161  1.00 84.36           C  
ANISOU 3058  CZ  TYR A 255     9983  13706   8365   -916   -677    959       C  
ATOM   3059  OH  TYR A 255     -28.534  -3.943  24.504  1.00 86.31           O  
ANISOU 3059  OH  TYR A 255    10285  14006   8501   -975   -673    991       O  
ATOM   3060  N   TYR A 256     -29.793 -10.047  27.474  1.00 67.43           N  
ANISOU 3060  N   TYR A 256     7703  11415   6502   -807   -629    753       N  
ATOM   3061  CA  TYR A 256     -28.428 -10.559  27.362  1.00 67.08           C  
ANISOU 3061  CA  TYR A 256     7660  11407   6422   -782   -604    706       C  
ATOM   3062  C   TYR A 256     -28.317 -11.797  26.478  1.00 72.01           C  
ANISOU 3062  C   TYR A 256     8297  12036   7029   -757   -622    619       C  
ATOM   3063  O   TYR A 256     -27.330 -11.942  25.762  1.00 72.07           O  
ANISOU 3063  O   TYR A 256     8298  12109   6976   -732   -591    572       O  
ATOM   3064  CB  TYR A 256     -27.741 -10.709  28.730  1.00 67.64           C  
ANISOU 3064  CB  TYR A 256     7731  11430   6538   -765   -583    727       C  
ATOM   3065  CG  TYR A 256     -27.385  -9.371  29.350  1.00 69.11           C  
ANISOU 3065  CG  TYR A 256     7929  11629   6699   -796   -563    800       C  
ATOM   3066  CD1 TYR A 256     -26.577  -8.460  28.675  1.00 71.20           C  
ANISOU 3066  CD1 TYR A 256     8181  11979   6891   -823   -551    818       C  
ATOM   3067  CD2 TYR A 256     -27.864  -9.012  30.606  1.00 69.83           C  
ANISOU 3067  CD2 TYR A 256     8063  11643   6828   -809   -553    849       C  
ATOM   3068  CE1 TYR A 256     -26.262  -7.220  29.228  1.00 71.97           C  
ANISOU 3068  CE1 TYR A 256     8313  12073   6958   -867   -545    887       C  
ATOM   3069  CE2 TYR A 256     -27.549  -7.776  31.174  1.00 70.85           C  
ANISOU 3069  CE2 TYR A 256     8234  11764   6921   -840   -539    909       C  
ATOM   3070  CZ  TYR A 256     -26.752  -6.879  30.477  1.00 79.64           C  
ANISOU 3070  CZ  TYR A 256     9341  12954   7966   -871   -543    929       C  
ATOM   3071  OH  TYR A 256     -26.429  -5.652  31.016  1.00 81.08           O  
ANISOU 3071  OH  TYR A 256     9586  13117   8105   -917   -541    990       O  
ATOM   3072  N   ILE A 257     -29.371 -12.633  26.460  1.00 69.63           N  
ANISOU 3072  N   ILE A 257     8017  11669   6772   -771   -666    598       N  
ATOM   3073  CA  ILE A 257     -29.473 -13.823  25.613  1.00 70.65           C  
ANISOU 3073  CA  ILE A 257     8193  11776   6876   -762   -700    516       C  
ATOM   3074  C   ILE A 257     -29.597 -13.372  24.149  1.00 77.03           C  
ANISOU 3074  C   ILE A 257     9024  12658   7585   -790   -718    495       C  
ATOM   3075  O   ILE A 257     -28.873 -13.890  23.291  1.00 77.86           O  
ANISOU 3075  O   ILE A 257     9172  12794   7615   -762   -695    419       O  
ATOM   3076  CB  ILE A 257     -30.629 -14.765  26.086  1.00 73.67           C  
ANISOU 3076  CB  ILE A 257     8598  12062   7332   -801   -755    515       C  
ATOM   3077  CG1 ILE A 257     -30.372 -15.341  27.512  1.00 73.91           C  
ANISOU 3077  CG1 ILE A 257     8639  12009   7435   -782   -734    531       C  
ATOM   3078  CG2 ILE A 257     -30.934 -15.888  25.082  1.00 74.98           C  
ANISOU 3078  CG2 ILE A 257     8838  12193   7458   -817   -812    436       C  
ATOM   3079  CD1 ILE A 257     -28.969 -16.025  27.776  1.00 80.84           C  
ANISOU 3079  CD1 ILE A 257     9548  12864   8304   -698   -714    477       C  
ATOM   3080  N   GLY A 258     -30.461 -12.377  23.905  1.00 73.81           N  
ANISOU 3080  N   GLY A 258     8594  12276   7174   -838   -756    564       N  
ATOM   3081  CA  GLY A 258     -30.682 -11.781  22.588  1.00 74.33           C  
ANISOU 3081  CA  GLY A 258     8697  12403   7142   -876   -795    568       C  
ATOM   3082  C   GLY A 258     -29.408 -11.213  22.001  1.00 78.54           C  
ANISOU 3082  C   GLY A 258     9253  13021   7569   -866   -724    550       C  
ATOM   3083  O   GLY A 258     -28.988 -11.609  20.910  1.00 78.62           O  
ANISOU 3083  O   GLY A 258     9324  13072   7476   -874   -711    485       O  
ATOM   3084  N   ILE A 259     -28.763 -10.331  22.757  1.00 75.13           N  
ANISOU 3084  N   ILE A 259     8773  12615   7156   -856   -670    605       N  
ATOM   3085  CA  ILE A 259     -27.480  -9.767  22.363  1.00 75.47           C  
ANISOU 3085  CA  ILE A 259     8814  12749   7114   -863   -596    600       C  
ATOM   3086  C   ILE A 259     -26.433 -10.851  22.108  1.00 79.80           C  
ANISOU 3086  C   ILE A 259     9348  13330   7643   -808   -528    503       C  
ATOM   3087  O   ILE A 259     -25.718 -10.801  21.107  1.00 80.78           O  
ANISOU 3087  O   ILE A 259     9493  13539   7662   -819   -470    460       O  
ATOM   3088  CB  ILE A 259     -26.943  -8.791  23.427  1.00 78.11           C  
ANISOU 3088  CB  ILE A 259     9102  13089   7489   -871   -566    676       C  
ATOM   3089  CG1 ILE A 259     -27.737  -7.483  23.400  1.00 78.45           C  
ANISOU 3089  CG1 ILE A 259     9182  13111   7516   -917   -615    765       C  
ATOM   3090  CG2 ILE A 259     -25.462  -8.525  23.206  1.00 79.80           C  
ANISOU 3090  CG2 ILE A 259     9278  13401   7640   -883   -487    663       C  
ATOM   3091  CD1 ILE A 259     -27.786  -6.827  22.038  1.00 88.03           C  
ANISOU 3091  CD1 ILE A 259    10460  14383   8604   -975   -639    779       C  
ATOM   3092  N   SER A 260     -26.337 -11.826  23.005  1.00 75.15           N  
ANISOU 3092  N   SER A 260     8730  12672   7152   -745   -530    469       N  
ATOM   3093  CA  SER A 260     -25.363 -12.903  22.847  1.00 75.34           C  
ANISOU 3093  CA  SER A 260     8741  12706   7177   -664   -475    376       C  
ATOM   3094  C   SER A 260     -25.439 -13.513  21.449  1.00 79.26           C  
ANISOU 3094  C   SER A 260     9322  13226   7568   -660   -457    285       C  
ATOM   3095  O   SER A 260     -24.422 -13.705  20.783  1.00 79.17           O  
ANISOU 3095  O   SER A 260     9298  13293   7490   -619   -367    219       O  
ATOM   3096  CB  SER A 260     -25.583 -13.985  23.906  1.00 78.74           C  
ANISOU 3096  CB  SER A 260     9175  13022   7722   -605   -516    356       C  
ATOM   3097  OG  SER A 260     -25.137 -13.550  25.179  1.00 87.81           O  
ANISOU 3097  OG  SER A 260    10258  14159   8947   -598   -514    424       O  
ATOM   3098  N   ILE A 261     -26.658 -13.801  21.005  1.00 75.81           N  
ANISOU 3098  N   ILE A 261     8969  12723   7112   -709   -543    281       N  
ATOM   3099  CA  ILE A 261     -26.879 -14.356  19.675  1.00 76.72           C  
ANISOU 3099  CA  ILE A 261     9199  12842   7111   -727   -552    199       C  
ATOM   3100  C   ILE A 261     -26.473 -13.360  18.592  1.00 82.37           C  
ANISOU 3100  C   ILE A 261     9942  13672   7683   -786   -502    215       C  
ATOM   3101  O   ILE A 261     -25.819 -13.724  17.616  1.00 83.97           O  
ANISOU 3101  O   ILE A 261    10209  13927   7770   -769   -424    130       O  
ATOM   3102  CB  ILE A 261     -28.351 -14.756  19.467  1.00 79.48           C  
ANISOU 3102  CB  ILE A 261     9622  13100   7476   -793   -683    213       C  
ATOM   3103  CG1 ILE A 261     -28.632 -16.112  20.116  1.00 79.51           C  
ANISOU 3103  CG1 ILE A 261     9656  12985   7569   -750   -720    159       C  
ATOM   3104  CG2 ILE A 261     -28.690 -14.789  17.984  1.00 81.62           C  
ANISOU 3104  CG2 ILE A 261    10020  13396   7595   -856   -720    169       C  
ATOM   3105  CD1 ILE A 261     -29.952 -16.175  20.853  1.00 83.56           C  
ANISOU 3105  CD1 ILE A 261    10140  13423   8188   -816   -824    232       C  
ATOM   3106  N   ASP A 262     -26.865 -12.102  18.772  1.00 78.31           N  
ANISOU 3106  N   ASP A 262     9393  13192   7171   -855   -541    324       N  
ATOM   3107  CA  ASP A 262     -26.531 -11.046  17.805  1.00 79.09           C  
ANISOU 3107  CA  ASP A 262     9537  13386   7129   -930   -510    359       C  
ATOM   3108  C   ASP A 262     -25.016 -11.022  17.560  1.00 83.61           C  
ANISOU 3108  C   ASP A 262    10060  14068   7638   -900   -356    310       C  
ATOM   3109  O   ASP A 262     -24.591 -10.924  16.408  1.00 84.05           O  
ANISOU 3109  O   ASP A 262    10192  14199   7543   -941   -291    266       O  
ATOM   3110  CB  ASP A 262     -27.005  -9.662  18.304  1.00 80.42           C  
ANISOU 3110  CB  ASP A 262     9670  13555   7333   -987   -570    488       C  
ATOM   3111  CG  ASP A 262     -27.135  -8.561  17.247  1.00 95.48           C  
ANISOU 3111  CG  ASP A 262    11668  15514   9095  -1082   -599    546       C  
ATOM   3112  OD1 ASP A 262     -26.405  -8.614  16.224  1.00 97.10           O  
ANISOU 3112  OD1 ASP A 262    11940  15799   9152  -1120   -522    496       O  
ATOM   3113  OD2 ASP A 262     -27.930  -7.619  17.465  1.00103.43           O  
ANISOU 3113  OD2 ASP A 262    12685  16481  10133  -1115   -693    642       O  
ATOM   3114  N   SER A 263     -24.214 -11.159  18.644  1.00 79.70           N  
ANISOU 3114  N   SER A 263     9436  13585   7259   -833   -300    316       N  
ATOM   3115  CA  SER A 263     -22.750 -11.171  18.613  1.00 80.12           C  
ANISOU 3115  CA  SER A 263     9393  13752   7298   -794   -164    279       C  
ATOM   3116  C   SER A 263     -22.203 -12.319  17.767  1.00 85.14           C  
ANISOU 3116  C   SER A 263    10066  14412   7870   -711    -69    142       C  
ATOM   3117  O   SER A 263     -21.401 -12.063  16.874  1.00 86.21           O  
ANISOU 3117  O   SER A 263    10201  14667   7888   -735     52    105       O  
ATOM   3118  CB  SER A 263     -22.178 -11.226  20.026  1.00 83.20           C  
ANISOU 3118  CB  SER A 263     9646  14124   7841   -734   -167    318       C  
ATOM   3119  OG  SER A 263     -22.793 -10.272  20.878  1.00 91.08           O  
ANISOU 3119  OG  SER A 263    10641  15073   8893   -800   -253    431       O  
ATOM   3120  N   PHE A 264     -22.659 -13.541  18.020  1.00 81.82           N  
ANISOU 3120  N   PHE A 264     9694  13876   7517   -622   -118     67       N  
ATOM   3121  CA  PHE A 264     -22.209 -14.701  17.259  1.00 83.45           C  
ANISOU 3121  CA  PHE A 264     9968  14074   7665   -528    -36    -74       C  
ATOM   3122  C   PHE A 264     -22.605 -14.634  15.783  1.00 88.50           C  
ANISOU 3122  C   PHE A 264    10776  14739   8109   -605    -15   -127       C  
ATOM   3123  O   PHE A 264     -21.846 -15.060  14.913  1.00 89.31           O  
ANISOU 3123  O   PHE A 264    10921  14907   8107   -557    119   -231       O  
ATOM   3124  CB  PHE A 264     -22.745 -15.991  17.886  1.00 85.14           C  
ANISOU 3124  CB  PHE A 264    10234  14128   7987   -436   -121   -131       C  
ATOM   3125  CG  PHE A 264     -22.077 -16.358  19.181  1.00 86.50           C  
ANISOU 3125  CG  PHE A 264    10269  14272   8326   -331   -120   -113       C  
ATOM   3126  CD1 PHE A 264     -20.734 -16.694  19.212  1.00 91.10           C  
ANISOU 3126  CD1 PHE A 264    10739  14933   8942   -210      0   -174       C  
ATOM   3127  CD2 PHE A 264     -22.792 -16.367  20.366  1.00 87.60           C  
ANISOU 3127  CD2 PHE A 264    10390  14308   8586   -355   -239    -32       C  
ATOM   3128  CE1 PHE A 264     -20.117 -17.032  20.401  1.00 91.64           C  
ANISOU 3128  CE1 PHE A 264    10684  14970   9166   -115    -25   -148       C  
ATOM   3129  CE2 PHE A 264     -22.181 -16.704  21.559  1.00 90.18           C  
ANISOU 3129  CE2 PHE A 264    10616  14599   9048   -271   -251    -10       C  
ATOM   3130  CZ  PHE A 264     -20.841 -17.037  21.576  1.00 89.23           C  
ANISOU 3130  CZ  PHE A 264    10389  14550   8963   -151   -157    -64       C  
ATOM   3131  N   ILE A 265     -23.798 -14.146  15.530  1.00 84.86           N  
ANISOU 3131  N   ILE A 265    10413  14224   7605   -717   -148    -58       N  
ATOM   3132  CA  ILE A 265     -24.243 -14.015  14.179  1.00 86.37           C  
ANISOU 3132  CA  ILE A 265    10777  14430   7608   -807   -163    -89       C  
ATOM   3133  C   ILE A 265     -23.153 -13.330  13.434  1.00 92.70           C  
ANISOU 3133  C   ILE A 265    11561  15386   8276   -840     -1   -100       C  
ATOM   3134  O   ILE A 265     -22.553 -13.905  12.560  1.00 94.60           O  
ANISOU 3134  O   ILE A 265    11881  15669   8394   -803    123   -214       O  
ATOM   3135  CB  ILE A 265     -25.388 -13.081  14.087  1.00 88.45           C  
ANISOU 3135  CB  ILE A 265    11087  14665   7855   -931   -317     30       C  
ATOM   3136  CG1 ILE A 265     -26.654 -13.843  13.751  1.00 88.73           C  
ANISOU 3136  CG1 ILE A 265    11254  14576   7883   -962   -472      3       C  
ATOM   3137  CG2 ILE A 265     -25.088 -12.074  13.024  1.00 89.73           C  
ANISOU 3137  CG2 ILE A 265    11330  14931   7833  -1038   -270     66       C  
ATOM   3138  CD1 ILE A 265     -27.451 -14.213  14.935  1.00 88.60           C  
ANISOU 3138  CD1 ILE A 265    11147  14459   8058   -930   -581     50       C  
ATOM   3139  N   LEU A 266     -22.909 -12.076  13.780  1.00 88.69           N  
ANISOU 3139  N   LEU A 266    10957  14958   7782   -918      2     18       N  
ATOM   3140  CA  LEU A 266     -21.885 -11.319  13.107  1.00 89.78           C  
ANISOU 3140  CA  LEU A 266    11072  15250   7790   -982    152     27       C  
ATOM   3141  C   LEU A 266     -20.475 -11.823  13.008  1.00 96.00           C  
ANISOU 3141  C   LEU A 266    11743  16155   8578   -890    359    -68       C  
ATOM   3142  O   LEU A 266     -19.799 -11.593  12.024  1.00 97.66           O  
ANISOU 3142  O   LEU A 266    11995  16483   8627   -940    505   -110       O  
ATOM   3143  CB  LEU A 266     -21.551 -10.023  13.895  1.00 88.48           C  
ANISOU 3143  CB  LEU A 266    10775  15148   7697  -1055    136    167       C  
ATOM   3144  CG  LEU A 266     -22.646  -9.029  14.272  1.00 91.33           C  
ANISOU 3144  CG  LEU A 266    11187  15426   8087  -1145    -40    299       C  
ATOM   3145  CD1 LEU A 266     -22.645  -8.821  15.746  1.00 89.47           C  
ANISOU 3145  CD1 LEU A 266    10805  15144   8047  -1092    -92    366       C  
ATOM   3146  CD2 LEU A 266     -22.457  -7.703  13.610  1.00 94.42           C  
ANISOU 3146  CD2 LEU A 266    11649  15893   8332  -1293    -29    392       C  
ATOM   3147  N   LEU A 267     -20.023 -12.529  14.028  1.00 92.46           N  
ANISOU 3147  N   LEU A 267    11143  15676   8311   -751    373   -101       N  
ATOM   3148  CA  LEU A 267     -18.706 -13.140  13.967  1.00 94.24           C  
ANISOU 3148  CA  LEU A 267    11236  16005   8566   -629    558   -198       C  
ATOM   3149  C   LEU A 267     -19.109 -14.335  13.193  1.00100.92           C  
ANISOU 3149  C   LEU A 267    12259  16756   9329   -545    574   -341       C  
ATOM   3150  O   LEU A 267     -18.284 -15.077  12.681  1.00102.32           O  
ANISOU 3150  O   LEU A 267    12424  16985   9467   -431    736   -468       O  
ATOM   3151  CB  LEU A 267     -18.231 -13.485  15.376  1.00 93.16           C  
ANISOU 3151  CB  LEU A 267    10902  15839   8658   -511    519   -171       C  
ATOM   3152  N   GLU A 268     -20.411 -14.530  13.104  1.00 97.80           N  
ANISOU 3152  N   GLU A 268    12034  16217   8909   -600    403   -322       N  
ATOM   3153  CA  GLU A 268     -20.979 -15.551  12.250  1.00 99.09           C  
ANISOU 3153  CA  GLU A 268    12414  16275   8960   -569    382   -443       C  
ATOM   3154  C   GLU A 268     -20.698 -17.028  12.378  1.00104.72           C  
ANISOU 3154  C   GLU A 268    13166  16887   9735   -392    426   -589       C  
ATOM   3155  O   GLU A 268     -20.473 -17.708  11.393  1.00106.16           O  
ANISOU 3155  O   GLU A 268    13503  17059   9774   -348    526   -722       O  
ATOM   3156  CB  GLU A 268     -20.770 -15.203  10.781  1.00102.10           C  
ANISOU 3156  CB  GLU A 268    12955  16748   9090   -665    495   -494       C  
ATOM   3157  CG  GLU A 268     -19.335 -14.954  10.395  1.00112.01           C  
ANISOU 3157  CG  GLU A 268    14087  18185  10287   -622    743   -545       C  
ATOM   3158  CD  GLU A 268     -19.217 -14.254   9.057  1.00128.23           C  
ANISOU 3158  CD  GLU A 268    16296  20346  12081   -773    843   -547       C  
ATOM   3159  OE1 GLU A 268     -18.456 -14.721   8.192  1.00114.21           O  
ANISOU 3159  OE1 GLU A 268    14579  18648  10168   -721   1046   -674       O  
ATOM   3160  OE2 GLU A 268     -19.896 -13.235   8.864  1.00121.57           O  
ANISOU 3160  OE2 GLU A 268    15525  19502  11163   -940    718   -422       O  
ATOM   3161  N   ILE A 269     -20.717 -17.499  13.617  1.00100.56           N  
ANISOU 3161  N   ILE A 269    12518  16277   9415   -295    347   -562       N  
ATOM   3162  CA  ILE A 269     -20.828 -18.907  13.944  1.00101.18           C  
ANISOU 3162  CA  ILE A 269    12672  16198   9572   -150    309   -669       C  
ATOM   3163  C   ILE A 269     -22.233 -19.457  13.762  1.00105.51           C  
ANISOU 3163  C   ILE A 269    13433  16576  10081   -235    126   -672       C  
ATOM   3164  O   ILE A 269     -22.418 -20.631  13.440  1.00106.43           O  
ANISOU 3164  O   ILE A 269    13714  16560  10164   -161    109   -790       O  
ATOM   3165  CB  ILE A 269     -20.357 -19.169  15.383  1.00103.18           C  
ANISOU 3165  CB  ILE A 269    12732  16418  10054    -34    273   -621       C  
ATOM   3166  CG1 ILE A 269     -18.952 -18.602  15.596  1.00104.17           C  
ANISOU 3166  CG1 ILE A 269    12623  16724  10233     36    434   -605       C  
ATOM   3167  CG2 ILE A 269     -20.387 -20.659  15.690  1.00104.87           C  
ANISOU 3167  CG2 ILE A 269    13045  16459  10343    122    234   -732       C  
ATOM   3168  CD1 ILE A 269     -17.987 -19.581  16.227  1.00112.30           C  
ANISOU 3168  CD1 ILE A 269    13536  17720  11411    253    491   -683       C  
ATOM   3169  N   ILE A 270     -23.223 -18.590  13.960  1.00100.98           N  
ANISOU 3169  N   ILE A 270    12852  16003   9513   -391    -14   -541       N  
ATOM   3170  CA  ILE A 270     -24.610 -18.946  13.685  1.00100.65           C  
ANISOU 3170  CA  ILE A 270    12981  15831   9432   -499   -193   -526       C  
ATOM   3171  C   ILE A 270     -24.963 -18.858  12.205  1.00107.64           C  
ANISOU 3171  C   ILE A 270    14078  16733  10088   -600   -193   -581       C  
ATOM   3172  O   ILE A 270     -24.972 -17.774  11.622  1.00107.40           O  
ANISOU 3172  O   ILE A 270    14042  16815   9951   -705   -175   -513       O  
ATOM   3173  CB  ILE A 270     -25.578 -18.058  14.488  1.00101.32           C  
ANISOU 3173  CB  ILE A 270    12959  15911   9626   -611   -342   -364       C  
ATOM   3174  CG1 ILE A 270     -25.325 -18.214  15.989  1.00100.20           C  
ANISOU 3174  CG1 ILE A 270    12646  15732   9691   -526   -352   -311       C  
ATOM   3175  CG2 ILE A 270     -27.020 -18.399  14.148  1.00101.99           C  
ANISOU 3175  CG2 ILE A 270    13186  15883   9681   -727   -527   -343       C  
ATOM   3176  CD1 ILE A 270     -26.075 -17.215  16.842  1.00104.94           C  
ANISOU 3176  CD1 ILE A 270    13130  16348  10394   -616   -450   -160       C  
ATOM   3177  N   LYS A 271     -25.254 -20.006  11.602  1.00106.49           N  
ANISOU 3177  N   LYS A 271    14142  16463   9856   -575   -224   -704       N  
ATOM   3178  CA  LYS A 271     -25.608 -20.061  10.189  1.00108.29           C  
ANISOU 3178  CA  LYS A 271    14613  16685   9849   -676   -238   -769       C  
ATOM   3179  C   LYS A 271     -27.123 -20.194  10.304  1.00112.14           C  
ANISOU 3179  C   LYS A 271    15182  17054  10372   -817   -491   -689       C  
ATOM   3180  O   LYS A 271     -27.640 -21.262  10.632  1.00112.55           O  
ANISOU 3180  O   LYS A 271    15320  16955  10487   -798   -590   -738       O  
ATOM   3181  CB  LYS A 271     -24.890 -21.224   9.501  1.00113.09           C  
ANISOU 3181  CB  LYS A 271    15402  17228  10339   -551    -99   -960       C  
ATOM   3182  N   GLN A 272     -27.830 -19.101  10.032  1.00107.91           N  
ANISOU 3182  N   GLN A 272    14614  16586   9799   -960   -599   -562       N  
ATOM   3183  CA  GLN A 272     -29.286 -19.093  10.103  1.00107.40           C  
ANISOU 3183  CA  GLN A 272    14586  16438   9783  -1095   -841   -472       C  
ATOM   3184  C   GLN A 272     -29.729 -18.098   9.036  1.00112.34           C  
ANISOU 3184  C   GLN A 272    15307  17137  10239  -1237   -918   -403       C  
ATOM   3185  O   GLN A 272     -29.064 -17.090   8.799  1.00112.50           O  
ANISOU 3185  O   GLN A 272    15269  17283  10195  -1237   -807   -360       O  
ATOM   3186  CB  GLN A 272     -29.953 -18.763  11.439  1.00106.66           C  
ANISOU 3186  CB  GLN A 272    14268  16327   9929  -1096   -941   -343       C  
ATOM   3187  CG  GLN A 272     -29.673 -19.775  12.539  1.00120.01           C  
ANISOU 3187  CG  GLN A 272    15891  17924  11782   -982   -901   -394       C  
ATOM   3188  CD  GLN A 272     -30.247 -21.144  12.231  1.00140.95           C  
ANISOU 3188  CD  GLN A 272    18742  20416  14396  -1013  -1005   -488       C  
ATOM   3189  OE1 GLN A 272     -29.688 -22.167  12.627  1.00133.42           O  
ANISOU 3189  OE1 GLN A 272    17839  19370  13484   -900   -938   -586       O  
ATOM   3190  NE2 GLN A 272     -31.369 -21.169  11.522  1.00139.59           N  
ANISOU 3190  NE2 GLN A 272    18691  20202  14146  -1169  -1184   -455       N  
ATOM   3191  N   GLY A 273     -30.857 -18.389   8.395  1.00109.49           N  
ANISOU 3191  N   GLY A 273    15102  16695   9805  -1368  -1123   -386       N  
ATOM   3192  CA  GLY A 273     -31.388 -17.525   7.357  1.00110.45           C  
ANISOU 3192  CA  GLY A 273    15337  16864   9763  -1509  -1240   -313       C  
ATOM   3193  C   GLY A 273     -31.926 -16.219   7.908  1.00112.84           C  
ANISOU 3193  C   GLY A 273    15433  17241  10199  -1546  -1332   -138       C  
ATOM   3194  O   GLY A 273     -32.420 -16.166   9.034  1.00111.41           O  
ANISOU 3194  O   GLY A 273    15049  17039  10243  -1506  -1386    -64       O  
ATOM   3195  N   CYS A 274     -31.829 -15.161   7.110  1.00109.15           N  
ANISOU 3195  N   CYS A 274    15037  16852   9584  -1622  -1346    -74       N  
ATOM   3196  CA  CYS A 274     -32.308 -13.846   7.519  1.00107.39           C  
ANISOU 3196  CA  CYS A 274    14655  16684   9465  -1651  -1437     90       C  
ATOM   3197  C   CYS A 274     -33.505 -13.997   8.454  1.00108.10           C  
ANISOU 3197  C   CYS A 274    14568  16710   9795  -1646  -1612    175       C  
ATOM   3198  O   CYS A 274     -33.656 -13.239   9.412  1.00106.57           O  
ANISOU 3198  O   CYS A 274    14166  16548   9776  -1592  -1603    273       O  
ATOM   3199  CB  CYS A 274     -32.630 -12.988   6.294  1.00109.64           C  
ANISOU 3199  CB  CYS A 274    15118  16997   9542  -1781  -1556    157       C  
ATOM   3200  SG  CYS A 274     -31.213 -12.094   5.615  1.00114.39           S  
ANISOU 3200  SG  CYS A 274    15818  17722   9924  -1793  -1324    138       S  
ATOM   3201  N   GLU A 275     -34.352 -14.981   8.168  1.00103.61           N  
ANISOU 3201  N   GLU A 275    14089  16051   9227  -1712  -1765    136       N  
ATOM   3202  CA  GLU A 275     -35.537 -15.234   8.984  1.00101.86           C  
ANISOU 3202  CA  GLU A 275    13699  15777   9226  -1730  -1927    214       C  
ATOM   3203  C   GLU A 275     -35.177 -15.145  10.472  1.00101.51           C  
ANISOU 3203  C   GLU A 275    13416  15751   9402  -1606  -1784    236       C  
ATOM   3204  O   GLU A 275     -35.760 -14.327  11.189  1.00100.13           O  
ANISOU 3204  O   GLU A 275    13051  15607   9387  -1587  -1836    353       O  
ATOM   3205  CB  GLU A 275     -36.151 -16.600   8.620  1.00104.74           C  
ANISOU 3205  CB  GLU A 275    14205  16035   9557  -1812  -2050    133       C  
ATOM   3206  CG  GLU A 275     -37.644 -16.716   8.886  1.00116.73           C  
ANISOU 3206  CG  GLU A 275    15604  17517  11232  -1910  -2293    236       C  
ATOM   3207  CD  GLU A 275     -38.537 -15.690   8.213  1.00139.29           C  
ANISOU 3207  CD  GLU A 275    18438  20419  14067  -1998  -2501    368       C  
ATOM   3208  OE1 GLU A 275     -38.364 -15.443   6.997  1.00127.91           O  
ANISOU 3208  OE1 GLU A 275    17219  18981  12401  -2073  -2567    350       O  
ATOM   3209  OE2 GLU A 275     -39.424 -15.144   8.908  1.00137.66           O  
ANISOU 3209  OE2 GLU A 275    17995  20241  14068  -1988  -2598    489       O  
ATOM   3210  N   PHE A 276     -34.143 -15.861  10.895  1.00 95.65           N  
ANISOU 3210  N   PHE A 276    12694  14995   8655  -1512  -1599    126       N  
ATOM   3211  CA  PHE A 276     -33.653 -15.763  12.270  1.00 92.81           C  
ANISOU 3211  CA  PHE A 276    12135  14651   8477  -1398  -1465    146       C  
ATOM   3212  C   PHE A 276     -33.260 -14.348  12.745  1.00 94.83           C  
ANISOU 3212  C   PHE A 276    12245  15001   8784  -1352  -1389    246       C  
ATOM   3213  O   PHE A 276     -33.593 -13.963  13.866  1.00 93.63           O  
ANISOU 3213  O   PHE A 276    11916  14849   8810  -1310  -1388    322       O  
ATOM   3214  CB  PHE A 276     -32.479 -16.723  12.481  1.00 94.41           C  
ANISOU 3214  CB  PHE A 276    12401  14826   8645  -1296  -1289     10       C  
ATOM   3215  CG  PHE A 276     -32.155 -16.975  13.926  1.00 94.23           C  
ANISOU 3215  CG  PHE A 276    12206  14782   8814  -1196  -1203     23       C  
ATOM   3216  CD1 PHE A 276     -33.080 -16.693  14.917  1.00 96.18           C  
ANISOU 3216  CD1 PHE A 276    12294  15009   9240  -1221  -1290    128       C  
ATOM   3217  CD2 PHE A 276     -30.925 -17.495  14.293  1.00 96.38           C  
ANISOU 3217  CD2 PHE A 276    12477  15055   9087  -1076  -1036    -68       C  
ATOM   3218  CE1 PHE A 276     -32.784 -16.924  16.247  1.00 95.88           C  
ANISOU 3218  CE1 PHE A 276    12127  14945   9357  -1142  -1212    142       C  
ATOM   3219  CE2 PHE A 276     -30.623 -17.729  15.622  1.00 98.05           C  
ANISOU 3219  CE2 PHE A 276    12549  15240   9467   -991   -980    -48       C  
ATOM   3220  CZ  PHE A 276     -31.554 -17.442  16.600  1.00 94.87           C  
ANISOU 3220  CZ  PHE A 276    12016  14810   9220  -1032  -1067     57       C  
ATOM   3221  N   GLU A 277     -32.563 -13.602  11.895  1.00 90.57           N  
ANISOU 3221  N   GLU A 277    11799  14535   8078  -1371  -1325    244       N  
ATOM   3222  CA  GLU A 277     -32.124 -12.255  12.239  1.00 88.93           C  
ANISOU 3222  CA  GLU A 277    11491  14406   7892  -1349  -1260    337       C  
ATOM   3223  C   GLU A 277     -33.233 -11.327  12.724  1.00 90.86           C  
ANISOU 3223  C   GLU A 277    11616  14636   8272  -1369  -1406    476       C  
ATOM   3224  O   GLU A 277     -33.191 -10.828  13.849  1.00 89.33           O  
ANISOU 3224  O   GLU A 277    11265  14447   8229  -1303  -1354    533       O  
ATOM   3225  CB  GLU A 277     -31.466 -11.581  11.033  1.00 91.75           C  
ANISOU 3225  CB  GLU A 277    12004  14834   8023  -1412  -1212    330       C  
ATOM   3226  CG  GLU A 277     -30.081 -11.022  11.314  1.00104.56           C  
ANISOU 3226  CG  GLU A 277    13570  16549   9609  -1363  -1005    317       C  
ATOM   3227  CD  GLU A 277     -29.074 -11.397  10.244  1.00127.65           C  
ANISOU 3227  CD  GLU A 277    16649  19535  12317  -1386   -862    208       C  
ATOM   3228  OE1 GLU A 277     -28.455 -10.481   9.661  1.00116.28           O  
ANISOU 3228  OE1 GLU A 277    15263  18180  10738  -1446   -789    246       O  
ATOM   3229  OE2 GLU A 277     -28.900 -12.606   9.986  1.00125.01           O  
ANISOU 3229  OE2 GLU A 277    16391  19160  11947  -1345   -817     84       O  
ATOM   3230  N   ASN A 278     -34.223 -11.098  11.867  1.00 87.92           N  
ANISOU 3230  N   ASN A 278    11323  14242   7841  -1455  -1593    529       N  
ATOM   3231  CA  ASN A 278     -35.336 -10.213  12.195  1.00 87.33           C  
ANISOU 3231  CA  ASN A 278    11130  14154   7897  -1459  -1745    660       C  
ATOM   3232  C   ASN A 278     -35.983 -10.613  13.518  1.00 87.81           C  
ANISOU 3232  C   ASN A 278    10988  14180   8195  -1397  -1740    682       C  
ATOM   3233  O   ASN A 278     -36.483  -9.764  14.255  1.00 86.63           O  
ANISOU 3233  O   ASN A 278    10697  14034   8184  -1347  -1760    774       O  
ATOM   3234  CB  ASN A 278     -36.376 -10.241  11.073  1.00 93.51           C  
ANISOU 3234  CB  ASN A 278    12019  14911   8600  -1562  -1974    701       C  
ATOM   3235  CG  ASN A 278     -36.965  -8.873  10.791  1.00120.29           C  
ANISOU 3235  CG  ASN A 278    15387  18313  12003  -1570  -2108    836       C  
ATOM   3236  OD1 ASN A 278     -37.820  -8.387  11.532  1.00114.95           O  
ANISOU 3236  OD1 ASN A 278    14532  17623  11519  -1514  -2182    923       O  
ATOM   3237  ND2 ASN A 278     -36.510  -8.243   9.714  1.00111.44           N  
ANISOU 3237  ND2 ASN A 278    14455  17213  10672  -1635  -2135    852       N  
ATOM   3238  N   THR A 279     -35.972 -11.909  13.812  1.00 82.93           N  
ANISOU 3238  N   THR A 279    10374  13520   7613  -1401  -1709    594       N  
ATOM   3239  CA  THR A 279     -36.584 -12.423  15.042  1.00 80.97           C  
ANISOU 3239  CA  THR A 279     9959  13235   7571  -1366  -1700    611       C  
ATOM   3240  C   THR A 279     -35.674 -11.970  16.186  1.00 80.47           C  
ANISOU 3240  C   THR A 279     9804  13192   7578  -1264  -1518    614       C  
ATOM   3241  O   THR A 279     -36.180 -11.528  17.208  1.00 79.05           O  
ANISOU 3241  O   THR A 279     9476  13007   7553  -1222  -1504    682       O  
ATOM   3242  CB  THR A 279     -36.697 -13.958  14.980  1.00 89.57           C  
ANISOU 3242  CB  THR A 279    11122  14258   8651  -1411  -1721    515       C  
ATOM   3243  OG1 THR A 279     -37.378 -14.343  13.781  1.00 92.89           O  
ANISOU 3243  OG1 THR A 279    11672  14657   8965  -1522  -1894    504       O  
ATOM   3244  CG2 THR A 279     -37.402 -14.547  16.196  1.00 86.76           C  
ANISOU 3244  CG2 THR A 279    10613  13859   8492  -1405  -1722    540       C  
ATOM   3245  N   VAL A 280     -34.338 -12.052  15.989  1.00 75.44           N  
ANISOU 3245  N   VAL A 280     9255  12584   6825  -1228  -1378    541       N  
ATOM   3246  CA  VAL A 280     -33.308 -11.647  16.952  1.00 73.83           C  
ANISOU 3246  CA  VAL A 280     8977  12407   6666  -1146  -1218    541       C  
ATOM   3247  C   VAL A 280     -33.406 -10.142  17.203  1.00 78.06           C  
ANISOU 3247  C   VAL A 280     9453  12979   7226  -1134  -1222    649       C  
ATOM   3248  O   VAL A 280     -33.413  -9.724  18.357  1.00 77.33           O  
ANISOU 3248  O   VAL A 280     9254  12874   7255  -1081  -1168    694       O  
ATOM   3249  CB  VAL A 280     -31.879 -12.060  16.499  1.00 77.86           C  
ANISOU 3249  CB  VAL A 280     9579  12958   7046  -1117  -1081    443       C  
ATOM   3250  CG1 VAL A 280     -30.828 -11.694  17.541  1.00 76.29           C  
ANISOU 3250  CG1 VAL A 280     9283  12792   6913  -1042   -939    451       C  
ATOM   3251  CG2 VAL A 280     -31.806 -13.548  16.181  1.00 78.61           C  
ANISOU 3251  CG2 VAL A 280     9764  12996   7110  -1112  -1081    327       C  
ATOM   3252  N   HIS A 281     -33.505  -9.341  16.126  1.00 76.18           N  
ANISOU 3252  N   HIS A 281     9307  12775   6864  -1187  -1294    690       N  
ATOM   3253  CA  HIS A 281     -33.609  -7.880  16.184  1.00 76.48           C  
ANISOU 3253  CA  HIS A 281     9331  12829   6900  -1182  -1321    794       C  
ATOM   3254  C   HIS A 281     -34.877  -7.435  16.912  1.00 79.44           C  
ANISOU 3254  C   HIS A 281     9578  13156   7450  -1141  -1417    879       C  
ATOM   3255  O   HIS A 281     -34.804  -6.523  17.737  1.00 78.26           O  
ANISOU 3255  O   HIS A 281     9367  12994   7373  -1086  -1368    938       O  
ATOM   3256  CB  HIS A 281     -33.549  -7.280  14.768  1.00 79.20           C  
ANISOU 3256  CB  HIS A 281     9830  13202   7059  -1262  -1403    819       C  
ATOM   3257  CG  HIS A 281     -33.649  -5.783  14.734  1.00 83.19           C  
ANISOU 3257  CG  HIS A 281    10355  13705   7548  -1263  -1449    930       C  
ATOM   3258  ND1 HIS A 281     -32.520  -4.988  14.653  1.00 85.08           N  
ANISOU 3258  ND1 HIS A 281    10662  13989   7677  -1288  -1340    944       N  
ATOM   3259  CD2 HIS A 281     -34.746  -4.985  14.743  1.00 85.63           C  
ANISOU 3259  CD2 HIS A 281    10629  13967   7937  -1241  -1598   1028       C  
ATOM   3260  CE1 HIS A 281     -32.963  -3.740  14.633  1.00 84.87           C  
ANISOU 3260  CE1 HIS A 281    10664  13925   7658  -1287  -1429   1051       C  
ATOM   3261  NE2 HIS A 281     -34.295  -3.689  14.696  1.00 85.56           N  
ANISOU 3261  NE2 HIS A 281    10690  13956   7864  -1245  -1583   1102       N  
ATOM   3262  N   LYS A 282     -36.034  -8.058  16.586  1.00 76.15           N  
ANISOU 3262  N   LYS A 282     9123  12713   7095  -1171  -1553    884       N  
ATOM   3263  CA  LYS A 282     -37.329  -7.754  17.199  1.00 75.81           C  
ANISOU 3263  CA  LYS A 282     8929  12643   7232  -1133  -1642    961       C  
ATOM   3264  C   LYS A 282     -37.342  -8.139  18.674  1.00 77.74           C  
ANISOU 3264  C   LYS A 282     9041  12866   7629  -1072  -1515    945       C  
ATOM   3265  O   LYS A 282     -37.947  -7.430  19.477  1.00 76.68           O  
ANISOU 3265  O   LYS A 282     8795  12717   7623  -1008  -1502   1010       O  
ATOM   3266  CB  LYS A 282     -38.473  -8.456  16.457  1.00 79.73           C  
ANISOU 3266  CB  LYS A 282     9405  13132   7755  -1204  -1820    969       C  
ATOM   3267  CG  LYS A 282     -39.096  -7.608  15.357  1.00 95.60           C  
ANISOU 3267  CG  LYS A 282    11473  15148   9703  -1236  -2004   1049       C  
ATOM   3268  CD  LYS A 282     -40.239  -8.330  14.648  1.00106.19           C  
ANISOU 3268  CD  LYS A 282    12787  16484  11077  -1320  -2203   1063       C  
ATOM   3269  CE  LYS A 282     -41.607  -7.901  15.126  1.00121.12           C  
ANISOU 3269  CE  LYS A 282    14463  18378  13181  -1273  -2317   1160       C  
ATOM   3270  NZ  LYS A 282     -41.927  -8.411  16.490  1.00131.12           N  
ANISOU 3270  NZ  LYS A 282    15541  19645  14632  -1224  -2187   1143       N  
ATOM   3271  N   TRP A 283     -36.660  -9.254  19.025  1.00 73.38           N  
ANISOU 3271  N   TRP A 283     8518  12305   7056  -1088  -1421    857       N  
ATOM   3272  CA  TRP A 283     -36.536  -9.760  20.391  1.00 72.07           C  
ANISOU 3272  CA  TRP A 283     8265  12110   7007  -1046  -1307    837       C  
ATOM   3273  C   TRP A 283     -35.775  -8.719  21.210  1.00 74.36           C  
ANISOU 3273  C   TRP A 283     8548  12404   7301   -978  -1191    870       C  
ATOM   3274  O   TRP A 283     -36.316  -8.234  22.206  1.00 74.40           O  
ANISOU 3274  O   TRP A 283     8461  12385   7422   -931  -1154    920       O  
ATOM   3275  CB  TRP A 283     -35.833 -11.135  20.394  1.00 70.96           C  
ANISOU 3275  CB  TRP A 283     8196  11947   6818  -1071  -1255    736       C  
ATOM   3276  CG  TRP A 283     -35.506 -11.699  21.748  1.00 71.38           C  
ANISOU 3276  CG  TRP A 283     8198  11959   6963  -1033  -1146    715       C  
ATOM   3277  CD1 TRP A 283     -34.393 -11.441  22.498  1.00 73.38           C  
ANISOU 3277  CD1 TRP A 283     8465  12214   7201   -977  -1027    701       C  
ATOM   3278  CD2 TRP A 283     -36.248 -12.697  22.461  1.00 71.44           C  
ANISOU 3278  CD2 TRP A 283     8151  11916   7079  -1066  -1159    706       C  
ATOM   3279  NE1 TRP A 283     -34.419 -12.184  23.654  1.00 72.34           N  
ANISOU 3279  NE1 TRP A 283     8299  12028   7159   -965   -973    687       N  
ATOM   3280  CE2 TRP A 283     -35.538 -12.977  23.651  1.00 74.53           C  
ANISOU 3280  CE2 TRP A 283     8540  12271   7507  -1021  -1045    688       C  
ATOM   3281  CE3 TRP A 283     -37.435 -13.400  22.200  1.00 74.04           C  
ANISOU 3281  CE3 TRP A 283     8436  12225   7470  -1144  -1265    716       C  
ATOM   3282  CZ2 TRP A 283     -35.994 -13.903  24.594  1.00 73.95           C  
ANISOU 3282  CZ2 TRP A 283     8439  12136   7523  -1051  -1026    683       C  
ATOM   3283  CZ3 TRP A 283     -37.892 -14.313  23.140  1.00 75.47           C  
ANISOU 3283  CZ3 TRP A 283     8573  12354   7747  -1181  -1239    711       C  
ATOM   3284  CH2 TRP A 283     -37.176 -14.556  24.321  1.00 75.37           C  
ANISOU 3284  CH2 TRP A 283     8577  12300   7761  -1134  -1117    695       C  
ATOM   3285  N   ILE A 284     -34.565  -8.321  20.735  1.00 68.80           N  
ANISOU 3285  N   ILE A 284     7944  11733   6464   -982  -1137    846       N  
ATOM   3286  CA  ILE A 284     -33.691  -7.311  21.343  1.00 66.88           C  
ANISOU 3286  CA  ILE A 284     7717  11499   6197   -947  -1044    880       C  
ATOM   3287  C   ILE A 284     -34.424  -5.985  21.595  1.00 70.75           C  
ANISOU 3287  C   ILE A 284     8181  11961   6739   -911  -1088    974       C  
ATOM   3288  O   ILE A 284     -34.196  -5.375  22.635  1.00 69.93           O  
ANISOU 3288  O   ILE A 284     8057  11826   6685   -868  -1013   1003       O  
ATOM   3289  CB  ILE A 284     -32.369  -7.133  20.547  1.00 69.57           C  
ANISOU 3289  CB  ILE A 284     8155  11899   6379   -983   -993    845       C  
ATOM   3290  CG1 ILE A 284     -31.499  -8.407  20.615  1.00 69.42           C  
ANISOU 3290  CG1 ILE A 284     8142  11898   6338   -977   -915    746       C  
ATOM   3291  CG2 ILE A 284     -31.575  -5.899  21.017  1.00 69.53           C  
ANISOU 3291  CG2 ILE A 284     8172  11906   6340   -978   -929    900       C  
ATOM   3292  CD1 ILE A 284     -30.474  -8.518  19.517  1.00 76.18           C  
ANISOU 3292  CD1 ILE A 284     9083  12825   7039  -1011   -870    691       C  
ATOM   3293  N   SER A 285     -35.315  -5.559  20.678  1.00 67.92           N  
ANISOU 3293  N   SER A 285     7831  11604   6370   -924  -1217   1020       N  
ATOM   3294  CA  SER A 285     -36.075  -4.320  20.858  1.00 68.24           C  
ANISOU 3294  CA  SER A 285     7848  11607   6474   -867  -1274   1108       C  
ATOM   3295  C   SER A 285     -37.098  -4.455  21.993  1.00 71.38           C  
ANISOU 3295  C   SER A 285     8098  11968   7053   -795  -1242   1126       C  
ATOM   3296  O   SER A 285     -37.119  -3.606  22.887  1.00 70.67           O  
ANISOU 3296  O   SER A 285     7999  11835   7016   -726  -1173   1161       O  
ATOM   3297  CB  SER A 285     -36.736  -3.882  19.554  1.00 74.35           C  
ANISOU 3297  CB  SER A 285     8670  12388   7191   -896  -1440   1157       C  
ATOM   3298  OG  SER A 285     -37.730  -4.798  19.120  1.00 86.55           O  
ANISOU 3298  OG  SER A 285    10134  13948   8803   -923  -1545   1143       O  
ATOM   3299  N   ILE A 286     -37.896  -5.550  21.985  1.00 68.05           N  
ANISOU 3299  N   ILE A 286     7575  11563   6718   -821  -1281   1099       N  
ATOM   3300  CA  ILE A 286     -38.918  -5.862  23.002  1.00 67.96           C  
ANISOU 3300  CA  ILE A 286     7408  11535   6877   -779  -1240   1114       C  
ATOM   3301  C   ILE A 286     -38.268  -6.095  24.381  1.00 70.33           C  
ANISOU 3301  C   ILE A 286     7718  11805   7200   -756  -1073   1079       C  
ATOM   3302  O   ILE A 286     -38.682  -5.472  25.360  1.00 69.67           O  
ANISOU 3302  O   ILE A 286     7582  11690   7201   -687   -994   1111       O  
ATOM   3303  CB  ILE A 286     -39.846  -7.059  22.577  1.00 71.93           C  
ANISOU 3303  CB  ILE A 286     7814  12067   7449   -850  -1333   1096       C  
ATOM   3304  CG1 ILE A 286     -40.618  -6.769  21.265  1.00 74.21           C  
ANISOU 3304  CG1 ILE A 286     8090  12381   7724   -877  -1526   1143       C  
ATOM   3305  CG2 ILE A 286     -40.825  -7.440  23.693  1.00 72.66           C  
ANISOU 3305  CG2 ILE A 286     7740  12156   7713   -829  -1265   1112       C  
ATOM   3306  CD1 ILE A 286     -41.106  -8.036  20.484  1.00 84.69           C  
ANISOU 3306  CD1 ILE A 286     9407  13732   9041   -992  -1647   1110       C  
ATOM   3307  N   THR A 287     -37.255  -6.979  24.440  1.00 66.04           N  
ANISOU 3307  N   THR A 287     7249  11267   6576   -810  -1023   1014       N  
ATOM   3308  CA  THR A 287     -36.546  -7.354  25.665  1.00 65.08           C  
ANISOU 3308  CA  THR A 287     7150  11113   6465   -802   -895    983       C  
ATOM   3309  C   THR A 287     -35.763  -6.227  26.338  1.00 70.22           C  
ANISOU 3309  C   THR A 287     7872  11737   7072   -756   -816   1010       C  
ATOM   3310  O   THR A 287     -35.658  -6.231  27.563  1.00 69.62           O  
ANISOU 3310  O   THR A 287     7796  11620   7037   -735   -722   1011       O  
ATOM   3311  CB  THR A 287     -35.715  -8.619  25.473  1.00 70.98           C  
ANISOU 3311  CB  THR A 287     7952  11866   7153   -854   -886    909       C  
ATOM   3312  OG1 THR A 287     -34.769  -8.407  24.422  1.00 71.34           O  
ANISOU 3312  OG1 THR A 287     8085  11951   7069   -871   -917    884       O  
ATOM   3313  CG2 THR A 287     -36.578  -9.843  25.196  1.00 67.82           C  
ANISOU 3313  CG2 THR A 287     7499  11461   6811   -909   -949    881       C  
ATOM   3314  N   GLU A 288     -35.220  -5.270  25.566  1.00 68.08           N  
ANISOU 3314  N   GLU A 288     7678  11483   6706   -755   -858   1036       N  
ATOM   3315  CA  GLU A 288     -34.501  -4.129  26.138  1.00 67.98           C  
ANISOU 3315  CA  GLU A 288     7750  11437   6643   -732   -802   1070       C  
ATOM   3316  C   GLU A 288     -35.507  -3.216  26.821  1.00 72.97           C  
ANISOU 3316  C   GLU A 288     8352  12008   7365   -652   -783   1121       C  
ATOM   3317  O   GLU A 288     -35.238  -2.725  27.916  1.00 71.42           O  
ANISOU 3317  O   GLU A 288     8204  11757   7175   -624   -696   1129       O  
ATOM   3318  CB  GLU A 288     -33.758  -3.352  25.049  1.00 69.78           C  
ANISOU 3318  CB  GLU A 288     8073  11698   6742   -772   -858   1092       C  
ATOM   3319  CG  GLU A 288     -32.739  -2.363  25.583  1.00 81.66           C  
ANISOU 3319  CG  GLU A 288     9677  13177   8173   -788   -804   1121       C  
ATOM   3320  CD  GLU A 288     -31.983  -1.563  24.538  1.00113.12           C  
ANISOU 3320  CD  GLU A 288    13760  17197  12023   -851   -850   1152       C  
ATOM   3321  OE1 GLU A 288     -31.012  -0.874  24.924  1.00118.99           O  
ANISOU 3321  OE1 GLU A 288    14579  17933  12698   -894   -809   1175       O  
ATOM   3322  OE2 GLU A 288     -32.350  -1.617  23.340  1.00108.81           O  
ANISOU 3322  OE2 GLU A 288    13226  16687  11431   -873   -931   1158       O  
ATOM   3323  N   ALA A 289     -36.672  -3.006  26.164  1.00 71.92           N  
ANISOU 3323  N   ALA A 289     8142  11884   7302   -612   -868   1153       N  
ATOM   3324  CA  ALA A 289     -37.772  -2.174  26.640  1.00 72.77           C  
ANISOU 3324  CA  ALA A 289     8188  11943   7517   -510   -858   1199       C  
ATOM   3325  C   ALA A 289     -38.329  -2.717  27.952  1.00 77.50           C  
ANISOU 3325  C   ALA A 289     8698  12524   8225   -480   -733   1176       C  
ATOM   3326  O   ALA A 289     -38.450  -1.956  28.913  1.00 77.57           O  
ANISOU 3326  O   ALA A 289     8746  12470   8258   -409   -639   1189       O  
ATOM   3327  CB  ALA A 289     -38.862  -2.097  25.587  1.00 74.62           C  
ANISOU 3327  CB  ALA A 289     8326  12209   7817   -483   -996   1237       C  
ATOM   3328  N   LEU A 290     -38.609  -4.035  28.011  1.00 74.29           N  
ANISOU 3328  N   LEU A 290     8198  12163   7866   -543   -727   1140       N  
ATOM   3329  CA  LEU A 290     -39.132  -4.693  29.211  1.00 74.35           C  
ANISOU 3329  CA  LEU A 290     8131  12157   7962   -544   -609   1122       C  
ATOM   3330  C   LEU A 290     -38.104  -4.708  30.346  1.00 78.57           C  
ANISOU 3330  C   LEU A 290     8795  12638   8421   -563   -495   1096       C  
ATOM   3331  O   LEU A 290     -38.491  -4.577  31.509  1.00 78.67           O  
ANISOU 3331  O   LEU A 290     8804  12609   8478   -532   -377   1097       O  
ATOM   3332  CB  LEU A 290     -39.642  -6.113  28.900  1.00 74.44           C  
ANISOU 3332  CB  LEU A 290     8036  12218   8028   -629   -654   1097       C  
ATOM   3333  CG  LEU A 290     -40.796  -6.245  27.882  1.00 79.80           C  
ANISOU 3333  CG  LEU A 290     8571  12954   8796   -633   -781   1128       C  
ATOM   3334  CD1 LEU A 290     -41.027  -7.689  27.520  1.00 79.99           C  
ANISOU 3334  CD1 LEU A 290     8547  13011   8834   -747   -840   1096       C  
ATOM   3335  CD2 LEU A 290     -42.094  -5.631  28.398  1.00 82.75           C  
ANISOU 3335  CD2 LEU A 290     8784  13338   9320   -546   -732   1174       C  
ATOM   3336  N   ALA A 291     -36.797  -4.808  30.003  1.00 75.02           N  
ANISOU 3336  N   ALA A 291     8459  12190   7854   -614   -531   1075       N  
ATOM   3337  CA  ALA A 291     -35.681  -4.803  30.957  1.00 74.03           C  
ANISOU 3337  CA  ALA A 291     8452  12022   7654   -642   -459   1058       C  
ATOM   3338  C   ALA A 291     -35.568  -3.483  31.702  1.00 79.48           C  
ANISOU 3338  C   ALA A 291     9241  12643   8314   -589   -397   1090       C  
ATOM   3339  O   ALA A 291     -35.066  -3.475  32.819  1.00 78.85           O  
ANISOU 3339  O   ALA A 291     9249  12511   8199   -607   -322   1083       O  
ATOM   3340  CB  ALA A 291     -34.378  -5.084  30.239  1.00 73.91           C  
ANISOU 3340  CB  ALA A 291     8498  12046   7539   -697   -520   1036       C  
ATOM   3341  N   PHE A 292     -36.040  -2.378  31.089  1.00 78.21           N  
ANISOU 3341  N   PHE A 292     9085  12471   8161   -525   -441   1127       N  
ATOM   3342  CA  PHE A 292     -36.012  -1.027  31.656  1.00 79.08           C  
ANISOU 3342  CA  PHE A 292     9311  12495   8238   -462   -397   1156       C  
ATOM   3343  C   PHE A 292     -36.891  -0.840  32.897  1.00 84.84           C  
ANISOU 3343  C   PHE A 292    10031  13164   9042   -387   -266   1148       C  
ATOM   3344  O   PHE A 292     -36.719   0.159  33.603  1.00 84.17           O  
ANISOU 3344  O   PHE A 292    10083  12988   8909   -343   -208   1158       O  
ATOM   3345  CB  PHE A 292     -36.326   0.042  30.592  1.00 81.67           C  
ANISOU 3345  CB  PHE A 292     9659  12815   8557   -407   -495   1199       C  
ATOM   3346  CG  PHE A 292     -35.310   0.240  29.492  1.00 82.96           C  
ANISOU 3346  CG  PHE A 292     9895  13019   8606   -489   -599   1215       C  
ATOM   3347  CD1 PHE A 292     -33.982  -0.145  29.665  1.00 85.61           C  
ANISOU 3347  CD1 PHE A 292    10298  13383   8846   -589   -584   1194       C  
ATOM   3348  CD2 PHE A 292     -35.664   0.866  28.304  1.00 85.98           C  
ANISOU 3348  CD2 PHE A 292    10282  13412   8975   -466   -711   1255       C  
ATOM   3349  CE1 PHE A 292     -33.040   0.054  28.649  1.00 86.45           C  
ANISOU 3349  CE1 PHE A 292    10456  13543   8848   -667   -655   1207       C  
ATOM   3350  CE2 PHE A 292     -34.720   1.070  27.295  1.00 88.79           C  
ANISOU 3350  CE2 PHE A 292    10720  13810   9207   -556   -789   1270       C  
ATOM   3351  CZ  PHE A 292     -33.415   0.665  27.476  1.00 86.07           C  
ANISOU 3351  CZ  PHE A 292    10425  13507   8771   -657   -749   1243       C  
ATOM   3352  N   PHE A 293     -37.796  -1.810  33.191  1.00 83.29           N  
ANISOU 3352  N   PHE A 293     9686  13011   8949   -385   -212   1130       N  
ATOM   3353  CA  PHE A 293     -38.652  -1.780  34.383  1.00 84.39           C  
ANISOU 3353  CA  PHE A 293     9798  13110   9154   -331    -60   1119       C  
ATOM   3354  C   PHE A 293     -37.826  -1.959  35.665  1.00 87.36           C  
ANISOU 3354  C   PHE A 293    10341  13419   9432   -394     35   1097       C  
ATOM   3355  O   PHE A 293     -38.367  -1.815  36.762  1.00 88.41           O  
ANISOU 3355  O   PHE A 293    10508  13503   9581   -359    175   1085       O  
ATOM   3356  CB  PHE A 293     -39.791  -2.809  34.306  1.00 87.26           C  
ANISOU 3356  CB  PHE A 293     9954  13553   9649   -343    -33   1114       C  
ATOM   3357  CG  PHE A 293     -41.044  -2.393  35.049  1.00 91.15           C  
ANISOU 3357  CG  PHE A 293    10348  14034  10250   -243    109   1117       C  
ATOM   3358  CD1 PHE A 293     -41.222  -2.724  36.391  1.00 94.69           C  
ANISOU 3358  CD1 PHE A 293    10844  14449  10685   -268    280   1094       C  
ATOM   3359  CD2 PHE A 293     -42.062  -1.700  34.398  1.00 95.55           C  
ANISOU 3359  CD2 PHE A 293    10761  14620  10924   -123     73   1146       C  
ATOM   3360  CE1 PHE A 293     -42.382  -2.341  37.077  1.00 97.44           C  
ANISOU 3360  CE1 PHE A 293    11094  14798  11131   -172    439   1091       C  
ATOM   3361  CE2 PHE A 293     -43.229  -1.327  35.083  1.00100.16           C  
ANISOU 3361  CE2 PHE A 293    11226  15205  11625    -13    218   1145       C  
ATOM   3362  CZ  PHE A 293     -43.381  -1.652  36.417  1.00 98.37           C  
ANISOU 3362  CZ  PHE A 293    11043  14953  11380    -38    413   1114       C  
ATOM   3363  N   HIS A 294     -36.505  -2.198  35.528  1.00 82.16           N  
ANISOU 3363  N   HIS A 294     9790  12758   8669   -483    -43   1094       N  
ATOM   3364  CA  HIS A 294     -35.581  -2.296  36.654  1.00 81.74           C  
ANISOU 3364  CA  HIS A 294     9901  12639   8517   -549      5   1085       C  
ATOM   3365  C   HIS A 294     -35.544  -0.950  37.423  1.00 87.67           C  
ANISOU 3365  C   HIS A 294    10825  13283   9202   -495     74   1094       C  
ATOM   3366  O   HIS A 294     -35.374  -0.949  38.646  1.00 88.34           O  
ANISOU 3366  O   HIS A 294    11043  13295   9226   -524    164   1083       O  
ATOM   3367  CB  HIS A 294     -34.177  -2.756  36.192  1.00 81.14           C  
ANISOU 3367  CB  HIS A 294     9866  12599   8365   -640   -109   1085       C  
ATOM   3368  CG  HIS A 294     -33.360  -1.711  35.488  1.00 84.00           C  
ANISOU 3368  CG  HIS A 294    10303  12959   8654   -645   -191   1111       C  
ATOM   3369  ND1 HIS A 294     -32.565  -0.825  36.190  1.00 85.64           N  
ANISOU 3369  ND1 HIS A 294    10686  13091   8764   -678   -186   1130       N  
ATOM   3370  CD2 HIS A 294     -33.206  -1.474  34.165  1.00 85.42           C  
ANISOU 3370  CD2 HIS A 294    10418  13204   8833   -641   -283   1123       C  
ATOM   3371  CE1 HIS A 294     -31.974  -0.072  35.278  1.00 84.93           C  
ANISOU 3371  CE1 HIS A 294    10622  13024   8625   -697   -271   1156       C  
ATOM   3372  NE2 HIS A 294     -32.328  -0.424  34.047  1.00 85.12           N  
ANISOU 3372  NE2 HIS A 294    10509  13134   8700   -675   -326   1153       N  
ATOM   3373  N   CYS A 295     -35.779   0.179  36.694  1.00 84.01           N  
ANISOU 3373  N   CYS A 295    10375  12800   8746   -416     30   1115       N  
ATOM   3374  CA  CYS A 295     -35.851   1.551  37.210  1.00 84.42           C  
ANISOU 3374  CA  CYS A 295    10600  12735   8742   -345     79   1123       C  
ATOM   3375  C   CYS A 295     -36.946   1.689  38.258  1.00 88.46           C  
ANISOU 3375  C   CYS A 295    11116  13189   9305   -250    251   1094       C  
ATOM   3376  O   CYS A 295     -36.834   2.515  39.167  1.00 89.25           O  
ANISOU 3376  O   CYS A 295    11413  13172   9326   -219    332   1082       O  
ATOM   3377  CB  CYS A 295     -36.090   2.536  36.070  1.00 85.45           C  
ANISOU 3377  CB  CYS A 295    10714  12859   8894   -268    -17   1155       C  
ATOM   3378  SG  CYS A 295     -34.785   2.571  34.822  1.00 88.51           S  
ANISOU 3378  SG  CYS A 295    11125  13311   9192   -389   -193   1191       S  
ATOM   3379  N   CYS A 296     -38.021   0.900  38.101  1.00 84.08           N  
ANISOU 3379  N   CYS A 296    10346  12718   8881   -208    309   1083       N  
ATOM   3380  CA  CYS A 296     -39.204   0.910  38.950  1.00 84.56           C  
ANISOU 3380  CA  CYS A 296    10347  12762   9019   -118    490   1058       C  
ATOM   3381  C   CYS A 296     -39.173  -0.102  40.088  1.00 86.99           C  
ANISOU 3381  C   CYS A 296    10688  13075   9290   -218    609   1034       C  
ATOM   3382  O   CYS A 296     -39.970   0.036  41.010  1.00 87.88           O  
ANISOU 3382  O   CYS A 296    10812  13155   9422   -162    788   1009       O  
ATOM   3383  CB  CYS A 296     -40.464   0.767  38.101  1.00 85.71           C  
ANISOU 3383  CB  CYS A 296    10224  13001   9339    -18    478   1071       C  
ATOM   3384  SG  CYS A 296     -40.565   1.943  36.727  1.00 89.84           S  
ANISOU 3384  SG  CYS A 296    10726  13507   9902     99    314   1111       S  
ATOM   3385  N   LEU A 297     -38.245  -1.083  40.055  1.00 81.54           N  
ANISOU 3385  N   LEU A 297    10026  12417   8539   -360    517   1041       N  
ATOM   3386  CA  LEU A 297     -38.121  -2.113  41.096  1.00 81.14           C  
ANISOU 3386  CA  LEU A 297    10030  12357   8443   -467    598   1028       C  
ATOM   3387  C   LEU A 297     -37.856  -1.555  42.502  1.00 85.11           C  
ANISOU 3387  C   LEU A 297    10783  12738   8815   -481    724   1011       C  
ATOM   3388  O   LEU A 297     -38.578  -1.911  43.429  1.00 85.50           O  
ANISOU 3388  O   LEU A 297    10844  12775   8866   -490    888    992       O  
ATOM   3389  CB  LEU A 297     -37.070  -3.177  40.728  1.00 79.68           C  
ANISOU 3389  CB  LEU A 297     9844  12210   8219   -593    450   1040       C  
ATOM   3390  CG  LEU A 297     -37.388  -4.142  39.581  1.00 83.66           C  
ANISOU 3390  CG  LEU A 297    10130  12825   8833   -613    352   1044       C  
ATOM   3391  CD1 LEU A 297     -36.179  -4.976  39.248  1.00 82.42           C  
ANISOU 3391  CD1 LEU A 297    10014  12682   8619   -706    216   1046       C  
ATOM   3392  CD2 LEU A 297     -38.545  -5.077  39.927  1.00 87.04           C  
ANISOU 3392  CD2 LEU A 297    10418  13299   9353   -640    455   1039       C  
ATOM   3393  N   ASN A 298     -36.837  -0.680  42.652  1.00 81.13           N  
ANISOU 3393  N   ASN A 298    10487  12146   8191   -495    648   1018       N  
ATOM   3394  CA  ASN A 298     -36.447  -0.042  43.921  1.00 81.49           C  
ANISOU 3394  CA  ASN A 298    10814  12060   8089   -523    733   1003       C  
ATOM   3395  C   ASN A 298     -37.596   0.769  44.592  1.00 86.19           C  
ANISOU 3395  C   ASN A 298    11463  12589   8696   -393    945    964       C  
ATOM   3396  O   ASN A 298     -37.895   0.477  45.753  1.00 85.91           O  
ANISOU 3396  O   ASN A 298    11546  12506   8591   -431   1097    940       O  
ATOM   3397  CB  ASN A 298     -35.162   0.790  43.743  1.00 82.17           C  
ANISOU 3397  CB  ASN A 298    11084  12076   8060   -573    582   1027       C  
ATOM   3398  CG  ASN A 298     -34.562   1.352  45.011  1.00102.65           C  
ANISOU 3398  CG  ASN A 298    13990  14529  10483   -640    620   1020       C  
ATOM   3399  OD1 ASN A 298     -34.298   0.631  45.974  1.00 99.75           O  
ANISOU 3399  OD1 ASN A 298    13725  14133  10041   -739    652   1019       O  
ATOM   3400  ND2 ASN A 298     -34.251   2.643  45.003  1.00 92.13           N  
ANISOU 3400  ND2 ASN A 298    12835  13096   9074   -604    593   1020       N  
ATOM   3401  N   PRO A 299     -38.280   1.733  43.906  1.00 83.51           N  
ANISOU 3401  N   PRO A 299    11038  12246   8444   -235    965    956       N  
ATOM   3402  CA  PRO A 299     -39.391   2.456  44.562  1.00 85.29           C  
ANISOU 3402  CA  PRO A 299    11298  12412   8698    -86   1180    912       C  
ATOM   3403  C   PRO A 299     -40.606   1.581  44.879  1.00 89.65           C  
ANISOU 3403  C   PRO A 299    11625  13068   9371    -61   1356    895       C  
ATOM   3404  O   PRO A 299     -41.323   1.867  45.839  1.00 91.15           O  
ANISOU 3404  O   PRO A 299    11886  13209   9537      5   1576    852       O  
ATOM   3405  CB  PRO A 299     -39.770   3.527  43.539  1.00 87.56           C  
ANISOU 3405  CB  PRO A 299    11506  12685   9079     77   1109    922       C  
ATOM   3406  CG  PRO A 299     -38.630   3.607  42.601  1.00 90.21           C  
ANISOU 3406  CG  PRO A 299    11875  13033   9368    -17    870    969       C  
ATOM   3407  CD  PRO A 299     -38.084   2.232  42.531  1.00 84.23           C  
ANISOU 3407  CD  PRO A 299    11015  12381   8609   -179    798    988       C  
ATOM   3408  N   ILE A 300     -40.852   0.537  44.056  1.00 84.64           N  
ANISOU 3408  N   ILE A 300    10725  12574   8862   -118   1263    927       N  
ATOM   3409  CA  ILE A 300     -41.941  -0.426  44.245  1.00 84.95           C  
ANISOU 3409  CA  ILE A 300    10533  12726   9021   -137   1396    924       C  
ATOM   3410  C   ILE A 300     -41.650  -1.249  45.510  1.00 87.93           C  
ANISOU 3410  C   ILE A 300    11077  13065   9267   -290   1509    912       C  
ATOM   3411  O   ILE A 300     -42.540  -1.409  46.344  1.00 89.36           O  
ANISOU 3411  O   ILE A 300    11232  13260   9461   -276   1731    888       O  
ATOM   3412  CB  ILE A 300     -42.149  -1.293  42.953  1.00 87.13           C  
ANISOU 3412  CB  ILE A 300    10524  13140   9442   -178   1228    964       C  
ATOM   3413  CG1 ILE A 300     -43.031  -0.588  41.874  1.00 88.52           C  
ANISOU 3413  CG1 ILE A 300    10471  13377   9786    -11   1182    977       C  
ATOM   3414  CG2 ILE A 300     -42.577  -2.742  43.225  1.00 87.94           C  
ANISOU 3414  CG2 ILE A 300    10489  13334   9590   -318   1275    975       C  
ATOM   3415  CD1 ILE A 300     -44.545  -0.275  42.222  1.00101.49           C  
ANISOU 3415  CD1 ILE A 300    11912  15072  11577    133   1390    959       C  
ATOM   3416  N   LEU A 301     -40.384  -1.695  45.681  1.00 82.68           N  
ANISOU 3416  N   LEU A 301    10596  12348   8472   -431   1359    932       N  
ATOM   3417  CA  LEU A 301     -39.934  -2.486  46.831  1.00 82.64           C  
ANISOU 3417  CA  LEU A 301    10782  12289   8329   -586   1413    934       C  
ATOM   3418  C   LEU A 301     -39.974  -1.756  48.176  1.00 88.13           C  
ANISOU 3418  C   LEU A 301    11762  12857   8866   -575   1596    897       C  
ATOM   3419  O   LEU A 301     -39.971  -2.408  49.222  1.00 88.21           O  
ANISOU 3419  O   LEU A 301    11913  12831   8770   -693   1696    896       O  
ATOM   3420  CB  LEU A 301     -38.573  -3.141  46.571  1.00 80.79           C  
ANISOU 3420  CB  LEU A 301    10638  12036   8021   -716   1183    969       C  
ATOM   3421  CG  LEU A 301     -38.615  -4.420  45.739  1.00 84.47           C  
ANISOU 3421  CG  LEU A 301    10884  12613   8600   -785   1063    995       C  
ATOM   3422  CD1 LEU A 301     -37.299  -4.656  45.033  1.00 82.85           C  
ANISOU 3422  CD1 LEU A 301    10709  12406   8365   -834    827   1018       C  
ATOM   3423  CD2 LEU A 301     -39.002  -5.624  46.588  1.00 87.61           C  
ANISOU 3423  CD2 LEU A 301    11304  13013   8970   -914   1156   1004       C  
ATOM   3424  N   TYR A 302     -40.035  -0.414  48.148  1.00 85.35           N  
ANISOU 3424  N   TYR A 302    11514  12427   8489   -436   1640    866       N  
ATOM   3425  CA  TYR A 302     -40.156   0.414  49.346  1.00 86.48           C  
ANISOU 3425  CA  TYR A 302    11943  12435   8479   -399   1825    819       C  
ATOM   3426  C   TYR A 302     -41.623   0.515  49.745  1.00 92.77           C  
ANISOU 3426  C   TYR A 302    12597  13283   9368   -279   2112    773       C  
ATOM   3427  O   TYR A 302     -41.921   0.583  50.938  1.00 94.21           O  
ANISOU 3427  O   TYR A 302    12974  13396   9424   -306   2323    734       O  
ATOM   3428  CB  TYR A 302     -39.604   1.825  49.106  1.00 87.07           C  
ANISOU 3428  CB  TYR A 302    12206  12389   8489   -298   1743    803       C  
ATOM   3429  CG  TYR A 302     -38.138   1.992  49.429  1.00 86.82           C  
ANISOU 3429  CG  TYR A 302    12458  12251   8279   -443   1553    831       C  
ATOM   3430  CD1 TYR A 302     -37.683   1.949  50.743  1.00 89.60           C  
ANISOU 3430  CD1 TYR A 302    13130  12485   8428   -560   1618    816       C  
ATOM   3431  CD2 TYR A 302     -37.216   2.285  48.430  1.00 85.68           C  
ANISOU 3431  CD2 TYR A 302    12271  12122   8161   -465   1310    874       C  
ATOM   3432  CE1 TYR A 302     -36.337   2.133  51.048  1.00 89.65           C  
ANISOU 3432  CE1 TYR A 302    13385  12398   8280   -699   1423    850       C  
ATOM   3433  CE2 TYR A 302     -35.868   2.480  48.724  1.00 85.55           C  
ANISOU 3433  CE2 TYR A 302    12488  12023   7994   -602   1136    905       C  
ATOM   3434  CZ  TYR A 302     -35.432   2.401  50.035  1.00 93.13           C  
ANISOU 3434  CZ  TYR A 302    13745  12870   8769   -718   1183    895       C  
ATOM   3435  OH  TYR A 302     -34.108   2.600  50.334  1.00 92.03           O  
ANISOU 3435  OH  TYR A 302    13822  12655   8492   -860    993    934       O  
ATOM   3436  N   ALA A 303     -42.534   0.539  48.746  1.00 89.71           N  
ANISOU 3436  N   ALA A 303    11868  13019   9198   -149   2118    781       N  
ATOM   3437  CA  ALA A 303     -43.981   0.645  48.949  1.00 91.97           C  
ANISOU 3437  CA  ALA A 303    11940  13385   9620    -16   2372    746       C  
ATOM   3438  C   ALA A 303     -44.564  -0.590  49.640  1.00 97.27           C  
ANISOU 3438  C   ALA A 303    12514  14151  10292   -165   2531    756       C  
ATOM   3439  O   ALA A 303     -45.351  -0.450  50.578  1.00 98.81           O  
ANISOU 3439  O   ALA A 303    12747  14343  10455   -128   2812    712       O  
ATOM   3440  CB  ALA A 303     -44.684   0.889  47.622  1.00 92.52           C  
ANISOU 3440  CB  ALA A 303    11661  13568   9926    134   2278    770       C  
ATOM   3441  N   PHE A 304     -44.157  -1.789  49.191  1.00 92.75           N  
ANISOU 3441  N   PHE A 304    11835  13655   9749   -335   2358    812       N  
ATOM   3442  CA  PHE A 304     -44.643  -3.061  49.722  1.00 93.60           C  
ANISOU 3442  CA  PHE A 304    11859  13845   9861   -502   2465    834       C  
ATOM   3443  C   PHE A 304     -43.837  -3.605  50.911  1.00 98.00           C  
ANISOU 3443  C   PHE A 304    12761  14290  10183   -689   2486    839       C  
ATOM   3444  O   PHE A 304     -44.403  -4.323  51.738  1.00 99.50           O  
ANISOU 3444  O   PHE A 304    12968  14510  10327   -805   2669    841       O  
ATOM   3445  CB  PHE A 304     -44.754  -4.108  48.600  1.00 94.17           C  
ANISOU 3445  CB  PHE A 304    11642  14047  10093   -582   2270    889       C  
ATOM   3446  CG  PHE A 304     -45.556  -3.680  47.388  1.00 96.22           C  
ANISOU 3446  CG  PHE A 304    11562  14420  10578   -423   2217    897       C  
ATOM   3447  CD1 PHE A 304     -44.971  -3.630  46.131  1.00 97.36           C  
ANISOU 3447  CD1 PHE A 304    11621  14582  10790   -395   1946    925       C  
ATOM   3448  CD2 PHE A 304     -46.899  -3.337  47.505  1.00101.09           C  
ANISOU 3448  CD2 PHE A 304    11942  15130  11340   -304   2436    878       C  
ATOM   3449  CE1 PHE A 304     -45.714  -3.245  45.012  1.00 98.79           C  
ANISOU 3449  CE1 PHE A 304    11511  14859  11164   -260   1878    939       C  
ATOM   3450  CE2 PHE A 304     -47.637  -2.944  46.386  1.00104.34           C  
ANISOU 3450  CE2 PHE A 304    12036  15642  11965   -155   2359    894       C  
ATOM   3451  CZ  PHE A 304     -47.039  -2.901  45.147  1.00100.43           C  
ANISOU 3451  CZ  PHE A 304    11487  15151  11520   -140   2072    927       C  
ATOM   3452  N   LEU A 305     -42.532  -3.264  51.000  1.00 92.59           N  
ANISOU 3452  N   LEU A 305    12349  13480   9352   -728   2296    846       N  
ATOM   3453  CA  LEU A 305     -41.632  -3.723  52.069  1.00102.82           C  
ANISOU 3453  CA  LEU A 305    13983  14657  10426   -902   2261    860       C  
ATOM   3454  C   LEU A 305     -40.988  -2.547  52.808  1.00112.87           C  
ANISOU 3454  C   LEU A 305    15604  15770  11513   -854   2289    822       C  
ATOM   3455  O   LEU A 305     -41.681  -1.639  53.264  1.00 72.82           O  
ANISOU 3455  O   LEU A 305    10595  10660   6416   -729   2511    763       O  
ATOM   3456  CB  LEU A 305     -40.538  -4.657  51.508  1.00100.43           C  
ANISOU 3456  CB  LEU A 305    13675  14360  10125  -1030   1962    919       C  
ATOM   3457  CG  LEU A 305     -40.952  -6.077  51.094  1.00104.55           C  
ANISOU 3457  CG  LEU A 305    13975  14989  10759  -1141   1916    960       C  
ATOM   3458  CD1 LEU A 305     -41.451  -6.123  49.660  1.00103.88           C  
ANISOU 3458  CD1 LEU A 305    13534  15037  10898  -1038   1824    966       C  
ATOM   3459  CD2 LEU A 305     -39.781  -7.018  51.196  1.00105.44           C  
ANISOU 3459  CD2 LEU A 305    14238  15040  10784  -1288   1686   1007       C  
TER    3460      LEU A 305                                                      
ATOM   3461  N   PRO B  27     -57.654  11.878  -1.659  1.00179.49           N  
ANISOU 3461  N   PRO B  27    19264  34197  14735  -2160   1106   -529       N  
ATOM   3462  CA  PRO B  27     -57.820  10.521  -1.115  1.00176.95           C  
ANISOU 3462  CA  PRO B  27    18937  33564  14734  -1558   1113  -1078       C  
ATOM   3463  C   PRO B  27     -57.346  10.390   0.334  1.00177.57           C  
ANISOU 3463  C   PRO B  27    19011  33236  15220  -1432   1162  -1119       C  
ATOM   3464  O   PRO B  27     -56.846  11.368   0.895  1.00176.83           O  
ANISOU 3464  O   PRO B  27    18898  33145  15145  -1814   1201   -738       O  
ATOM   3465  CB  PRO B  27     -57.011   9.657  -2.087  1.00183.37           C  
ANISOU 3465  CB  PRO B  27    19374  35278  15022  -1282   1244  -1511       C  
ATOM   3466  CG  PRO B  27     -57.088  10.394  -3.378  1.00191.79           C  
ANISOU 3466  CG  PRO B  27    20380  36925  15568  -1679   1243  -1223       C  
ATOM   3467  CD  PRO B  27     -57.067  11.856  -3.012  1.00186.59           C  
ANISOU 3467  CD  PRO B  27    19865  36068  14963  -2288   1206   -575       C  
ATOM   3468  N   CYS B  28     -57.508   9.182   0.936  1.00172.14           N  
ANISOU 3468  N   CYS B  28    18366  32188  14853   -910   1140  -1574       N  
ATOM   3469  CA  CYS B  28     -57.164   8.845   2.329  1.00169.14           C  
ANISOU 3469  CA  CYS B  28    18014  31369  14882   -709   1162  -1672       C  
ATOM   3470  C   CYS B  28     -57.890   9.786   3.323  1.00168.84           C  
ANISOU 3470  C   CYS B  28    18297  30559  15294  -1013   1069  -1243       C  
ATOM   3471  O   CYS B  28     -57.260  10.405   4.191  1.00167.63           O  
ANISOU 3471  O   CYS B  28    18093  30361  15239  -1213   1127  -1022       O  
ATOM   3472  CB  CYS B  28     -55.648   8.809   2.549  1.00172.22           C  
ANISOU 3472  CB  CYS B  28    17998  32466  14972   -689   1338  -1768       C  
ATOM   3473  SG  CYS B  28     -55.120   7.845   3.995  1.00173.93           S  
ANISOU 3473  SG  CYS B  28    18191  32299  15595   -216   1347  -2109       S  
ATOM   3474  N   PHE B  29     -59.231   9.905   3.154  1.00163.10           N  
ANISOU 3474  N   PHE B  29    17891  29258  14820  -1038    913  -1141       N  
ATOM   3475  CA  PHE B  29     -60.109  10.761   3.959  1.00159.29           C  
ANISOU 3475  CA  PHE B  29    17721  28056  14744  -1263    799   -783       C  
ATOM   3476  C   PHE B  29     -60.430  10.135   5.310  1.00158.47           C  
ANISOU 3476  C   PHE B  29    17760  27305  15148   -980    775   -953       C  
ATOM   3477  O   PHE B  29     -60.813  10.839   6.242  1.00154.98           O  
ANISOU 3477  O   PHE B  29    17502  26362  15020  -1140    726   -689       O  
ATOM   3478  CB  PHE B  29     -61.411  11.097   3.202  1.00160.96           C  
ANISOU 3478  CB  PHE B  29    18173  27991  14993  -1364    637   -635       C  
ATOM   3479  CG  PHE B  29     -61.251  11.589   1.781  1.00166.57           C  
ANISOU 3479  CG  PHE B  29    18781  29314  15195  -1615    633   -485       C  
ATOM   3480  CD1 PHE B  29     -60.826  12.887   1.519  1.00171.43           C  
ANISOU 3480  CD1 PHE B  29    19399  30172  15565  -2090    630    -25       C  
ATOM   3481  CD2 PHE B  29     -61.576  10.773   0.705  1.00170.91           C  
ANISOU 3481  CD2 PHE B  29    19263  30169  15505  -1398    607   -788       C  
ATOM   3482  CE1 PHE B  29     -60.691  13.345   0.203  1.00176.18           C  
ANISOU 3482  CE1 PHE B  29    19920  31351  15671  -2356    616    149       C  
ATOM   3483  CE2 PHE B  29     -61.449  11.234  -0.611  1.00177.35           C  
ANISOU 3483  CE2 PHE B  29    19984  31577  15822  -1637    602   -640       C  
ATOM   3484  CZ  PHE B  29     -61.005  12.516  -0.853  1.00177.12           C  
ANISOU 3484  CZ  PHE B  29    19947  31813  15539  -2122    611   -160       C  
ATOM   3485  N   ASN B  33     -62.852   1.922   6.880  1.00131.23           N  
ANISOU 3485  N   ASN B  33    15084  21723  13055   1307    162  -3285       N  
ATOM   3486  CA  ASN B  33     -63.137   0.506   6.677  1.00132.88           C  
ANISOU 3486  CA  ASN B  33    15473  21667  13348   1642    -25  -3705       C  
ATOM   3487  C   ASN B  33     -62.378  -0.385   7.676  1.00137.38           C  
ANISOU 3487  C   ASN B  33    16107  22003  14089   1968    -68  -3924       C  
ATOM   3488  O   ASN B  33     -61.174  -0.617   7.526  1.00139.16           O  
ANISOU 3488  O   ASN B  33    16129  22679  14067   2235      1  -4144       O  
ATOM   3489  CB  ASN B  33     -62.876   0.096   5.223  1.00136.91           C  
ANISOU 3489  CB  ASN B  33    15868  22705  13448   1825    -62  -4033       C  
ATOM   3490  N   ALA B  34     -63.097  -0.850   8.718  1.00132.10           N  
ANISOU 3490  N   ALA B  34    15708  20650  13832   1932   -185  -3845       N  
ATOM   3491  CA  ALA B  34     -62.594  -1.725   9.785  1.00131.95           C  
ANISOU 3491  CA  ALA B  34    15829  20276  14032   2198   -272  -3996       C  
ATOM   3492  C   ALA B  34     -63.629  -2.823  10.082  1.00135.63           C  
ANISOU 3492  C   ALA B  34    16664  20065  14806   2239   -522  -4125       C  
ATOM   3493  O   ALA B  34     -64.737  -2.539  10.556  1.00132.97           O  
ANISOU 3493  O   ALA B  34    16466  19329  14729   1924   -546  -3852       O  
ATOM   3494  CB  ALA B  34     -62.285  -0.915  11.043  1.00129.38           C  
ANISOU 3494  CB  ALA B  34    15436  19836  13888   2006   -123  -3641       C  
ATOM   3495  N   ASN B  35     -63.268  -4.075   9.755  1.00134.54           N  
ANISOU 3495  N   ASN B  35    16678  19825  14615   2626   -724  -4553       N  
ATOM   3496  CA  ASN B  35     -64.121  -5.254   9.922  1.00134.92           C  
ANISOU 3496  CA  ASN B  35    17111  19237  14916   2679  -1012  -4724       C  
ATOM   3497  C   ASN B  35     -64.147  -5.753  11.377  1.00136.57           C  
ANISOU 3497  C   ASN B  35    17556  18865  15471   2676  -1104  -4588       C  
ATOM   3498  O   ASN B  35     -65.222  -6.015  11.919  1.00134.49           O  
ANISOU 3498  O   ASN B  35    17530  18080  15489   2403  -1217  -4406       O  
ATOM   3499  CB  ASN B  35     -63.658  -6.366   8.964  1.00138.07           C  
ANISOU 3499  CB  ASN B  35    17611  19748  15102   3121  -1221  -5258       C  
ATOM   3500  CG  ASN B  35     -64.682  -7.430   8.634  1.00151.86           C  
ANISOU 3500  CG  ASN B  35    19736  20949  17013   3103  -1536  -5460       C  
ATOM   3501  OD1 ASN B  35     -65.829  -7.418   9.097  1.00140.25           O  
ANISOU 3501  OD1 ASN B  35    18451  19016  15823   2733  -1608  -5196       O  
ATOM   3502  ND2 ASN B  35     -64.282  -8.381   7.805  1.00146.85           N  
ANISOU 3502  ND2 ASN B  35    19218  20388  16191   3507  -1742  -5949       N  
ATOM   3503  N   PHE B  36     -62.960  -5.876  11.996  1.00133.39           N  
ANISOU 3503  N   PHE B  36    17066  18595  15020   2969  -1056  -4671       N  
ATOM   3504  CA  PHE B  36     -62.778  -6.361  13.364  1.00132.31           C  
ANISOU 3504  CA  PHE B  36    17140  17975  15159   3021  -1149  -4562       C  
ATOM   3505  C   PHE B  36     -63.349  -5.434  14.438  1.00130.20           C  
ANISOU 3505  C   PHE B  36    16827  17532  15113   2591   -973  -4075       C  
ATOM   3506  O   PHE B  36     -63.919  -5.922  15.416  1.00129.05           O  
ANISOU 3506  O   PHE B  36    16947  16842  15245   2460  -1096  -3926       O  
ATOM   3507  CB  PHE B  36     -61.293  -6.682  13.629  1.00136.68           C  
ANISOU 3507  CB  PHE B  36    17565  18808  15558   3486  -1147  -4807       C  
ATOM   3508  CG  PHE B  36     -60.930  -6.963  15.070  1.00137.71           C  
ANISOU 3508  CG  PHE B  36    17847  18553  15925   3540  -1203  -4651       C  
ATOM   3509  CD1 PHE B  36     -61.277  -8.170  15.671  1.00143.09           C  
ANISOU 3509  CD1 PHE B  36    18961  18561  16847   3667  -1514  -4751       C  
ATOM   3510  CD2 PHE B  36     -60.244  -6.021  15.828  1.00137.63           C  
ANISOU 3510  CD2 PHE B  36    17564  18843  15884   3443   -965  -4392       C  
ATOM   3511  CE1 PHE B  36     -60.949  -8.424  17.005  1.00143.44           C  
ANISOU 3511  CE1 PHE B  36    19155  18259  17087   3701  -1575  -4583       C  
ATOM   3512  CE2 PHE B  36     -59.916  -6.277  17.162  1.00139.81           C  
ANISOU 3512  CE2 PHE B  36    17979  18781  16360   3492  -1024  -4249       C  
ATOM   3513  CZ  PHE B  36     -60.262  -7.481  17.736  1.00139.87           C  
ANISOU 3513  CZ  PHE B  36    18409  18143  16592   3629  -1324  -4343       C  
ATOM   3514  N   ASN B  37     -63.177  -4.110  14.275  1.00122.92           N  
ANISOU 3514  N   ASN B  37    15582  17070  14054   2375   -700  -3831       N  
ATOM   3515  CA  ASN B  37     -63.662  -3.122  15.244  1.00118.10           C  
ANISOU 3515  CA  ASN B  37    14914  16334  13623   2009   -535  -3402       C  
ATOM   3516  C   ASN B  37     -65.197  -3.038  15.357  1.00118.58           C  
ANISOU 3516  C   ASN B  37    15137  16014  13902   1649   -590  -3190       C  
ATOM   3517  O   ASN B  37     -65.700  -2.439  16.305  1.00115.46           O  
ANISOU 3517  O   ASN B  37    14742  15440  13687   1391   -495  -2878       O  
ATOM   3518  CB  ASN B  37     -63.010  -1.750  15.015  1.00116.29           C  
ANISOU 3518  CB  ASN B  37    14339  16664  13183   1886   -274  -3216       C  
ATOM   3519  CG  ASN B  37     -61.605  -1.617  15.572  1.00131.69           C  
ANISOU 3519  CG  ASN B  37    16116  18903  15019   2106   -183  -3264       C  
ATOM   3520  OD1 ASN B  37     -60.816  -2.571  15.623  1.00126.33           O  
ANISOU 3520  OD1 ASN B  37    15484  18230  14287   2484   -306  -3563       O  
ATOM   3521  ND2 ASN B  37     -61.250  -0.408  15.977  1.00119.47           N  
ANISOU 3521  ND2 ASN B  37    14359  17611  13421   1881     16  -2980       N  
ATOM   3522  N   LYS B  38     -65.933  -3.679  14.430  1.00115.82           N  
ANISOU 3522  N   LYS B  38    14918  15557  13531   1646   -755  -3379       N  
ATOM   3523  CA  LYS B  38     -67.396  -3.723  14.455  1.00114.14           C  
ANISOU 3523  CA  LYS B  38    14836  15025  13507   1314   -835  -3216       C  
ATOM   3524  C   LYS B  38     -67.902  -5.033  15.084  1.00116.86           C  
ANISOU 3524  C   LYS B  38    15532  14785  14085   1310  -1091  -3299       C  
ATOM   3525  O   LYS B  38     -69.059  -5.411  14.905  1.00116.91           O  
ANISOU 3525  O   LYS B  38    15675  14530  14213   1068  -1224  -3259       O  
ATOM   3526  CB  LYS B  38     -67.979  -3.461  13.051  1.00118.62           C  
ANISOU 3526  CB  LYS B  38    15306  15868  13896   1241   -855  -3319       C  
ATOM   3527  CG  LYS B  38     -68.344  -1.993  12.790  1.00136.81           C  
ANISOU 3527  CG  LYS B  38    17352  18514  16117    990   -641  -3022       C  
ATOM   3528  CD  LYS B  38     -67.135  -1.074  12.514  1.00148.09           C  
ANISOU 3528  CD  LYS B  38    18526  20451  17290   1107   -440  -2987       C  
ATOM   3529  CE  LYS B  38     -67.008   0.017  13.553  1.00155.91           C  
ANISOU 3529  CE  LYS B  38    19409  21439  18391    924   -258  -2639       C  
ATOM   3530  NZ  LYS B  38     -65.754   0.802  13.387  1.00164.76           N  
ANISOU 3530  NZ  LYS B  38    20306  23023  19274   1004    -91  -2603       N  
ATOM   3531  N   ILE B  39     -67.017  -5.711  15.832  1.00112.79           N  
ANISOU 3531  N   ILE B  39    15162  14072  13621   1563  -1174  -3402       N  
ATOM   3532  CA  ILE B  39     -67.297  -6.934  16.582  1.00113.93           C  
ANISOU 3532  CA  ILE B  39    15678  13632  13979   1570  -1435  -3444       C  
ATOM   3533  C   ILE B  39     -66.600  -6.865  17.946  1.00114.14           C  
ANISOU 3533  C   ILE B  39    15734  13526  14110   1637  -1369  -3267       C  
ATOM   3534  O   ILE B  39     -67.076  -7.464  18.906  1.00113.94           O  
ANISOU 3534  O   ILE B  39    15962  13044  14287   1473  -1502  -3112       O  
ATOM   3535  CB  ILE B  39     -67.021  -8.240  15.773  1.00121.78           C  
ANISOU 3535  CB  ILE B  39    16947  14416  14908   1892  -1750  -3873       C  
ATOM   3536  CG1 ILE B  39     -68.076  -9.325  16.061  1.00124.65           C  
ANISOU 3536  CG1 ILE B  39    17710  14154  15496   1653  -2056  -3850       C  
ATOM   3537  CG2 ILE B  39     -65.596  -8.770  15.934  1.00124.67           C  
ANISOU 3537  CG2 ILE B  39    17357  14844  15168   2399  -1827  -4150       C  
ATOM   3538  CD1 ILE B  39     -69.188  -9.398  15.022  1.00132.31           C  
ANISOU 3538  CD1 ILE B  39    18691  15142  16441   1409  -2144  -3919       C  
ATOM   3539  N   PHE B  40     -65.496  -6.103  18.027  1.00108.12           N  
ANISOU 3539  N   PHE B  40    14700  13189  13191   1842  -1164  -3272       N  
ATOM   3540  CA  PHE B  40     -64.747  -5.904  19.261  1.00106.28           C  
ANISOU 3540  CA  PHE B  40    14446  12913  13024   1914  -1084  -3113       C  
ATOM   3541  C   PHE B  40     -65.479  -4.865  20.123  1.00104.34           C  
ANISOU 3541  C   PHE B  40    14076  12668  12901   1509   -872  -2706       C  
ATOM   3542  O   PHE B  40     -66.036  -5.223  21.163  1.00103.66           O  
ANISOU 3542  O   PHE B  40    14182  12203  13003   1320   -940  -2510       O  
ATOM   3543  CB  PHE B  40     -63.297  -5.475  18.952  1.00108.82           C  
ANISOU 3543  CB  PHE B  40    14496  13740  13112   2264   -956  -3288       C  
ATOM   3544  CG  PHE B  40     -62.408  -5.275  20.159  1.00109.95           C  
ANISOU 3544  CG  PHE B  40    14590  13890  13295   2369   -888  -3157       C  
ATOM   3545  CD1 PHE B  40     -62.329  -4.038  20.790  1.00110.11           C  
ANISOU 3545  CD1 PHE B  40    14376  14146  13314   2123   -633  -2852       C  
ATOM   3546  CD2 PHE B  40     -61.626  -6.315  20.647  1.00115.18           C  
ANISOU 3546  CD2 PHE B  40    15452  14322  13988   2733  -1101  -3354       C  
ATOM   3547  CE1 PHE B  40     -61.506  -3.854  21.905  1.00110.42           C  
ANISOU 3547  CE1 PHE B  40    14372  14203  13381   2211   -582  -2741       C  
ATOM   3548  CE2 PHE B  40     -60.787  -6.126  21.751  1.00117.46           C  
ANISOU 3548  CE2 PHE B  40    15684  14645  14300   2839  -1049  -3235       C  
ATOM   3549  CZ  PHE B  40     -60.735  -4.897  22.373  1.00112.22           C  
ANISOU 3549  CZ  PHE B  40    14774  14233  13631   2565   -784  -2929       C  
ATOM   3550  N   LEU B  41     -65.505  -3.588  19.661  1.00 96.57           N  
ANISOU 3550  N   LEU B  41    12783  12114  11794   1376   -633  -2584       N  
ATOM   3551  CA  LEU B  41     -66.139  -2.446  20.336  1.00 92.13           C  
ANISOU 3551  CA  LEU B  41    12082  11608  11316   1051   -437  -2242       C  
ATOM   3552  C   LEU B  41     -67.564  -2.704  20.867  1.00 93.68           C  
ANISOU 3552  C   LEU B  41    12431  11446  11717    731   -502  -2053       C  
ATOM   3553  O   LEU B  41     -67.777  -2.449  22.053  1.00 91.71           O  
ANISOU 3553  O   LEU B  41    12204  11057  11586    583   -432  -1827       O  
ATOM   3554  CB  LEU B  41     -66.100  -1.148  19.499  1.00 90.48           C  
ANISOU 3554  CB  LEU B  41    11588  11852  10939    959   -246  -2172       C  
ATOM   3555  CG  LEU B  41     -64.764  -0.690  18.904  1.00 95.64           C  
ANISOU 3555  CG  LEU B  41    12027  12968  11345   1179   -147  -2305       C  
ATOM   3556  CD1 LEU B  41     -64.977   0.462  17.952  1.00 94.97           C  
ANISOU 3556  CD1 LEU B  41    11729  13260  11095   1014    -13  -2206       C  
ATOM   3557  CD2 LEU B  41     -63.775  -0.285  19.973  1.00 96.75           C  
ANISOU 3557  CD2 LEU B  41    12086  13185  11488   1246    -45  -2195       C  
ATOM   3558  N   PRO B  42     -68.543  -3.231  20.077  1.00 90.26           N  
ANISOU 3558  N   PRO B  42    12093  10885  11318    608   -638  -2140       N  
ATOM   3559  CA  PRO B  42     -69.885  -3.466  20.647  1.00 89.24           C  
ANISOU 3559  CA  PRO B  42    12063  10478  11366    269   -693  -1944       C  
ATOM   3560  C   PRO B  42     -69.910  -4.489  21.788  1.00 92.38           C  
ANISOU 3560  C   PRO B  42    12737  10450  11914    212   -843  -1870       C  
ATOM   3561  O   PRO B  42     -70.741  -4.360  22.683  1.00 91.12           O  
ANISOU 3561  O   PRO B  42    12582  10171  11868    -77   -797  -1624       O  
ATOM   3562  CB  PRO B  42     -70.707  -3.933  19.442  1.00 92.83           C  
ANISOU 3562  CB  PRO B  42    12565  10913  11794    188   -842  -2103       C  
ATOM   3563  CG  PRO B  42     -69.703  -4.510  18.508  1.00 99.65           C  
ANISOU 3563  CG  PRO B  42    13500  11855  12507    538   -955  -2434       C  
ATOM   3564  CD  PRO B  42     -68.506  -3.623  18.651  1.00 93.68           C  
ANISOU 3564  CD  PRO B  42    12529  11454  11611    751   -749  -2417       C  
ATOM   3565  N   THR B  43     -68.992  -5.482  21.761  1.00 89.57           N  
ANISOU 3565  N   THR B  43    12606   9886  11539    499  -1028  -2083       N  
ATOM   3566  CA  THR B  43     -68.895  -6.517  22.794  1.00 90.39           C  
ANISOU 3566  CA  THR B  43    13026   9546  11772    479  -1219  -2017       C  
ATOM   3567  C   THR B  43     -68.341  -5.908  24.070  1.00 90.53           C  
ANISOU 3567  C   THR B  43    12949   9642  11806    484  -1046  -1795       C  
ATOM   3568  O   THR B  43     -68.898  -6.139  25.144  1.00 90.07           O  
ANISOU 3568  O   THR B  43    13012   9353  11856    230  -1066  -1554       O  
ATOM   3569  CB  THR B  43     -68.053  -7.707  22.310  1.00100.19           C  
ANISOU 3569  CB  THR B  43    14546  10542  12980    847  -1500  -2343       C  
ATOM   3570  OG1 THR B  43     -68.453  -8.068  20.989  1.00101.44           O  
ANISOU 3570  OG1 THR B  43    14737  10728  13078    887  -1626  -2593       O  
ATOM   3571  CG2 THR B  43     -68.167  -8.915  23.229  1.00100.85           C  
ANISOU 3571  CG2 THR B  43    15040  10067  13210    783  -1778  -2269       C  
ATOM   3572  N   ILE B  44     -67.264  -5.108  23.942  1.00 84.46           N  
ANISOU 3572  N   ILE B  44    11952   9228  10909    743   -875  -1868       N  
ATOM   3573  CA  ILE B  44     -66.611  -4.422  25.055  1.00 81.91           C  
ANISOU 3573  CA  ILE B  44    11514   9031  10577    770   -710  -1690       C  
ATOM   3574  C   ILE B  44     -67.564  -3.422  25.728  1.00 82.70           C  
ANISOU 3574  C   ILE B  44    11453   9234  10735    419   -505  -1392       C  
ATOM   3575  O   ILE B  44     -67.662  -3.428  26.958  1.00 82.21           O  
ANISOU 3575  O   ILE B  44    11458   9040  10737    297   -475  -1191       O  
ATOM   3576  CB  ILE B  44     -65.219  -3.848  24.644  1.00 84.34           C  
ANISOU 3576  CB  ILE B  44    11605   9724  10717   1103   -602  -1857       C  
ATOM   3577  CG1 ILE B  44     -64.108  -4.909  24.804  1.00 87.57           C  
ANISOU 3577  CG1 ILE B  44    12197   9980  11097   1486   -808  -2078       C  
ATOM   3578  CG2 ILE B  44     -64.848  -2.594  25.426  1.00 82.04           C  
ANISOU 3578  CG2 ILE B  44    11081   9703  10389   1009   -360  -1645       C  
ATOM   3579  CD1 ILE B  44     -63.981  -5.933  23.674  1.00 98.25           C  
ANISOU 3579  CD1 ILE B  44    13706  11224  12401   1744  -1037  -2417       C  
ATOM   3580  N   TYR B  45     -68.312  -2.624  24.930  1.00 76.98           N  
ANISOU 3580  N   TYR B  45    10531   8739   9979    270   -387  -1372       N  
ATOM   3581  CA  TYR B  45     -69.285  -1.673  25.475  1.00 74.28           C  
ANISOU 3581  CA  TYR B  45    10030   8508   9685     -9   -218  -1133       C  
ATOM   3582  C   TYR B  45     -70.372  -2.397  26.261  1.00 79.65           C  
ANISOU 3582  C   TYR B  45    10862   8911  10488   -294   -308   -973       C  
ATOM   3583  O   TYR B  45     -70.616  -2.036  27.410  1.00 78.77           O  
ANISOU 3583  O   TYR B  45    10714   8806  10408   -432   -203   -771       O  
ATOM   3584  CB  TYR B  45     -69.909  -0.781  24.382  1.00 73.91           C  
ANISOU 3584  CB  TYR B  45     9773   8731   9579    -80   -128  -1159       C  
ATOM   3585  CG  TYR B  45     -68.931   0.100  23.632  1.00 74.21           C  
ANISOU 3585  CG  TYR B  45     9640   9088   9466    117    -23  -1254       C  
ATOM   3586  CD1 TYR B  45     -67.808   0.631  24.266  1.00 75.08           C  
ANISOU 3586  CD1 TYR B  45     9687   9323   9516    251     79  -1217       C  
ATOM   3587  CD2 TYR B  45     -69.153   0.447  22.303  1.00 74.95           C  
ANISOU 3587  CD2 TYR B  45     9628   9388   9462    133    -28  -1360       C  
ATOM   3588  CE1 TYR B  45     -66.904   1.438  23.579  1.00 74.66           C  
ANISOU 3588  CE1 TYR B  45     9466   9597   9306    373    169  -1280       C  
ATOM   3589  CE2 TYR B  45     -68.254   1.251  21.605  1.00 75.07           C  
ANISOU 3589  CE2 TYR B  45     9487   9729   9308    264     65  -1416       C  
ATOM   3590  CZ  TYR B  45     -67.134   1.748  22.250  1.00 80.59           C  
ANISOU 3590  CZ  TYR B  45    10119  10553   9948    368    165  -1369       C  
ATOM   3591  OH  TYR B  45     -66.261   2.559  21.573  1.00 81.62           O  
ANISOU 3591  OH  TYR B  45    10082  11034   9895    437    253  -1397       O  
ATOM   3592  N   SER B  46     -70.968  -3.458  25.667  1.00 78.15           N  
ANISOU 3592  N   SER B  46    10853   8487  10352   -390   -513  -1065       N  
ATOM   3593  CA  SER B  46     -72.024  -4.270  26.279  1.00 79.60           C  
ANISOU 3593  CA  SER B  46    11197   8409  10637   -721   -635   -908       C  
ATOM   3594  C   SER B  46     -71.574  -4.920  27.582  1.00 84.48           C  
ANISOU 3594  C   SER B  46    12038   8764  11295   -748   -709   -764       C  
ATOM   3595  O   SER B  46     -72.364  -4.997  28.526  1.00 84.70           O  
ANISOU 3595  O   SER B  46    12072   8751  11359  -1056   -673   -528       O  
ATOM   3596  CB  SER B  46     -72.525  -5.328  25.304  1.00 85.46           C  
ANISOU 3596  CB  SER B  46    12135   8918  11419   -794   -886  -1068       C  
ATOM   3597  OG  SER B  46     -72.963  -4.726  24.097  1.00 92.66           O  
ANISOU 3597  OG  SER B  46    12838  10095  12275   -775   -825  -1193       O  
ATOM   3598  N   ILE B  47     -70.302  -5.360  27.640  1.00 81.20           N  
ANISOU 3598  N   ILE B  47    11787   8212  10854   -418   -810   -906       N  
ATOM   3599  CA  ILE B  47     -69.700  -5.970  28.825  1.00 82.11           C  
ANISOU 3599  CA  ILE B  47    12130   8075  10993   -375   -907   -788       C  
ATOM   3600  C   ILE B  47     -69.592  -4.933  29.956  1.00 83.48           C  
ANISOU 3600  C   ILE B  47    12092   8504  11123   -446   -653   -573       C  
ATOM   3601  O   ILE B  47     -70.067  -5.195  31.061  1.00 84.13           O  
ANISOU 3601  O   ILE B  47    12270   8471  11227   -693   -658   -339       O  
ATOM   3602  CB  ILE B  47     -68.363  -6.694  28.469  1.00 86.87           C  
ANISOU 3602  CB  ILE B  47    12933   8505  11568     57  -1102  -1041       C  
ATOM   3603  CG1 ILE B  47     -68.658  -8.107  27.910  1.00 91.34           C  
ANISOU 3603  CG1 ILE B  47    13871   8627  12208     50  -1450  -1181       C  
ATOM   3604  CG2 ILE B  47     -67.399  -6.766  29.668  1.00 87.31           C  
ANISOU 3604  CG2 ILE B  47    13078   8493  11604    220  -1108   -939       C  
ATOM   3605  CD1 ILE B  47     -67.565  -8.737  27.013  1.00101.68           C  
ANISOU 3605  CD1 ILE B  47    15315   9851  13468    531  -1647  -1551       C  
ATOM   3606  N   ILE B  48     -69.023  -3.747  29.655  1.00 77.22           N  
ANISOU 3606  N   ILE B  48    11019   8066  10255   -260   -441   -648       N  
ATOM   3607  CA  ILE B  48     -68.869  -2.637  30.603  1.00 74.60           C  
ANISOU 3607  CA  ILE B  48    10488   7980   9875   -298   -213   -489       C  
ATOM   3608  C   ILE B  48     -70.247  -2.119  31.038  1.00 77.99           C  
ANISOU 3608  C   ILE B  48    10778   8529  10328   -635    -81   -297       C  
ATOM   3609  O   ILE B  48     -70.428  -1.793  32.209  1.00 77.23           O  
ANISOU 3609  O   ILE B  48    10646   8492  10206   -756     21   -118       O  
ATOM   3610  CB  ILE B  48     -67.910  -1.545  30.036  1.00 75.33           C  
ANISOU 3610  CB  ILE B  48    10353   8389   9880    -45    -67   -623       C  
ATOM   3611  CG1 ILE B  48     -66.460  -2.070  30.050  1.00 76.92           C  
ANISOU 3611  CG1 ILE B  48    10656   8539  10030    282   -177   -773       C  
ATOM   3612  CG2 ILE B  48     -68.000  -0.215  30.811  1.00 73.13           C  
ANISOU 3612  CG2 ILE B  48     9866   8359   9559   -129    156   -474       C  
ATOM   3613  CD1 ILE B  48     -65.567  -1.544  28.967  1.00 83.70           C  
ANISOU 3613  CD1 ILE B  48    11335   9682  10786    525   -125   -981       C  
ATOM   3614  N   PHE B  49     -71.222  -2.121  30.113  1.00 74.78           N  
ANISOU 3614  N   PHE B  49    10289   8171   9954   -778    -99   -345       N  
ATOM   3615  CA  PHE B  49     -72.601  -1.707  30.367  1.00 74.69           C  
ANISOU 3615  CA  PHE B  49    10107   8317   9955  -1076      4   -199       C  
ATOM   3616  C   PHE B  49     -73.265  -2.568  31.470  1.00 81.02           C  
ANISOU 3616  C   PHE B  49    11053   8956  10775  -1385    -66     14       C  
ATOM   3617  O   PHE B  49     -73.762  -2.004  32.443  1.00 79.74           O  
ANISOU 3617  O   PHE B  49    10742   8991  10563  -1528     90    175       O  
ATOM   3618  CB  PHE B  49     -73.417  -1.715  29.056  1.00 76.90           C  
ANISOU 3618  CB  PHE B  49    10292   8665  10262  -1147    -51   -314       C  
ATOM   3619  CG  PHE B  49     -74.916  -1.663  29.216  1.00 79.62           C  
ANISOU 3619  CG  PHE B  49    10484   9141  10625  -1475    -14   -184       C  
ATOM   3620  CD1 PHE B  49     -75.689  -2.805  29.043  1.00 86.12           C  
ANISOU 3620  CD1 PHE B  49    11453   9771  11499  -1757   -196   -142       C  
ATOM   3621  CD2 PHE B  49     -75.557  -0.472  29.534  1.00 80.16           C  
ANISOU 3621  CD2 PHE B  49    10263   9541  10654  -1500    183   -113       C  
ATOM   3622  CE1 PHE B  49     -77.079  -2.757  29.189  1.00 88.48           C  
ANISOU 3622  CE1 PHE B  49    11564  10259  11795  -2086   -158    -18       C  
ATOM   3623  CE2 PHE B  49     -76.946  -0.424  29.680  1.00 84.53           C  
ANISOU 3623  CE2 PHE B  49    10630  10284  11205  -1772    218    -15       C  
ATOM   3624  CZ  PHE B  49     -77.697  -1.567  29.508  1.00 85.72           C  
ANISOU 3624  CZ  PHE B  49    10883  10292  11393  -2077     58     38       C  
ATOM   3625  N   LEU B  50     -73.237  -3.916  31.331  1.00 80.35           N  
ANISOU 3625  N   LEU B  50    11270   8515  10744  -1485   -312     12       N  
ATOM   3626  CA  LEU B  50     -73.825  -4.843  32.307  1.00 82.65           C  
ANISOU 3626  CA  LEU B  50    11752   8610  11041  -1828   -424    243       C  
ATOM   3627  C   LEU B  50     -73.116  -4.757  33.649  1.00 85.58           C  
ANISOU 3627  C   LEU B  50    12206   8960  11350  -1768   -363    395       C  
ATOM   3628  O   LEU B  50     -73.774  -4.539  34.663  1.00 85.78           O  
ANISOU 3628  O   LEU B  50    12128   9157  11306  -2029   -243    611       O  
ATOM   3629  CB  LEU B  50     -73.821  -6.300  31.797  1.00 86.12           C  
ANISOU 3629  CB  LEU B  50    12564   8598  11559  -1921   -755    192       C  
ATOM   3630  CG  LEU B  50     -74.635  -6.628  30.540  1.00 92.38           C  
ANISOU 3630  CG  LEU B  50    13333   9360  12407  -2053   -871     57       C  
ATOM   3631  CD1 LEU B  50     -74.240  -7.983  29.992  1.00 95.86           C  
ANISOU 3631  CD1 LEU B  50    14193   9308  12919  -2001  -1224    -73       C  
ATOM   3632  CD2 LEU B  50     -76.138  -6.603  30.813  1.00 96.79           C  
ANISOU 3632  CD2 LEU B  50    13710  10114  12950  -2534   -810    260       C  
ATOM   3633  N   THR B  51     -71.773  -4.891  33.642  1.00 81.14           N  
ANISOU 3633  N   THR B  51    11799   8237  10792  -1412   -440    269       N  
ATOM   3634  CA  THR B  51     -70.902  -4.836  34.825  1.00 80.65           C  
ANISOU 3634  CA  THR B  51    11830   8145  10669  -1293   -415    378       C  
ATOM   3635  C   THR B  51     -70.991  -3.472  35.536  1.00 82.62           C  
ANISOU 3635  C   THR B  51    11762   8801  10829  -1285   -117    450       C  
ATOM   3636  O   THR B  51     -70.973  -3.423  36.764  1.00 82.44           O  
ANISOU 3636  O   THR B  51    11767   8828  10728  -1395    -60    635       O  
ATOM   3637  CB  THR B  51     -69.458  -5.211  34.442  1.00 85.96           C  
ANISOU 3637  CB  THR B  51    12675   8626  11361   -873   -567    175       C  
ATOM   3638  OG1 THR B  51     -69.473  -6.261  33.475  1.00 87.74           O  
ANISOU 3638  OG1 THR B  51    13140   8532  11666   -816   -826     21       O  
ATOM   3639  CG2 THR B  51     -68.617  -5.624  35.638  1.00 84.65           C  
ANISOU 3639  CG2 THR B  51    12711   8305  11148   -777   -656    301       C  
ATOM   3640  N   GLY B  52     -71.106  -2.398  34.755  1.00 77.39           N  
ANISOU 3640  N   GLY B  52    10826   8410  10170  -1159     46    305       N  
ATOM   3641  CA  GLY B  52     -71.246  -1.035  35.252  1.00 75.07           C  
ANISOU 3641  CA  GLY B  52    10257   8463   9806  -1125    291    333       C  
ATOM   3642  C   GLY B  52     -72.585  -0.806  35.919  1.00 80.90           C  
ANISOU 3642  C   GLY B  52    10840   9404  10494  -1435    410    499       C  
ATOM   3643  O   GLY B  52     -72.627  -0.468  37.102  1.00 81.12           O  
ANISOU 3643  O   GLY B  52    10821   9573  10428  -1499    519    628       O  
ATOM   3644  N   ILE B  53     -73.693  -1.037  35.179  1.00 78.29           N  
ANISOU 3644  N   ILE B  53    10417   9120  10208  -1632    383    491       N  
ATOM   3645  CA  ILE B  53     -75.063  -0.863  35.673  1.00 79.13           C  
ANISOU 3645  CA  ILE B  53    10320   9492  10256  -1935    492    629       C  
ATOM   3646  C   ILE B  53     -75.396  -1.744  36.904  1.00 84.41           C  
ANISOU 3646  C   ILE B  53    11126  10105  10842  -2253    449    878       C  
ATOM   3647  O   ILE B  53     -76.114  -1.290  37.797  1.00 84.56           O  
ANISOU 3647  O   ILE B  53    10942  10447  10740  -2413    609    998       O  
ATOM   3648  CB  ILE B  53     -76.107  -0.922  34.512  1.00 83.05           C  
ANISOU 3648  CB  ILE B  53    10670  10071  10816  -2063    451    550       C  
ATOM   3649  CG1 ILE B  53     -77.305   0.036  34.728  1.00 83.54           C  
ANISOU 3649  CG1 ILE B  53    10364  10571  10807  -2154    638    573       C  
ATOM   3650  CG2 ILE B  53     -76.501  -2.357  34.086  1.00 87.20           C  
ANISOU 3650  CG2 ILE B  53    11425  10301  11404  -2344    219    614       C  
ATOM   3651  CD1 ILE B  53     -78.530  -0.496  35.561  1.00 95.76           C  
ANISOU 3651  CD1 ILE B  53    11783  12342  12259  -2566    676    776       C  
ATOM   3652  N   VAL B  54     -74.842  -2.971  36.968  1.00 81.88           N  
ANISOU 3652  N   VAL B  54    11157   9387  10568  -2325    222    951       N  
ATOM   3653  CA  VAL B  54     -75.050  -3.869  38.109  1.00 84.33           C  
ANISOU 3653  CA  VAL B  54    11663   9585  10792  -2640    137   1218       C  
ATOM   3654  C   VAL B  54     -74.122  -3.428  39.246  1.00 86.96           C  
ANISOU 3654  C   VAL B  54    12038   9976  11025  -2448    229   1275       C  
ATOM   3655  O   VAL B  54     -74.599  -3.126  40.341  1.00 87.76           O  
ANISOU 3655  O   VAL B  54    12010  10357  10976  -2633    374   1443       O  
ATOM   3656  CB  VAL B  54     -74.884  -5.372  37.736  1.00 90.69           C  
ANISOU 3656  CB  VAL B  54    12878   9892  11690  -2799   -191   1281       C  
ATOM   3657  CG1 VAL B  54     -74.816  -6.261  38.974  1.00 93.30           C  
ANISOU 3657  CG1 VAL B  54    13485  10039  11925  -3076   -317   1576       C  
ATOM   3658  CG2 VAL B  54     -76.003  -5.834  36.807  1.00 92.28           C  
ANISOU 3658  CG2 VAL B  54    13025  10080  11959  -3093   -282   1266       C  
ATOM   3659  N   GLY B  55     -72.821  -3.376  38.957  1.00 81.10           N  
ANISOU 3659  N   GLY B  55    11451   9015  10349  -2078    146   1122       N  
ATOM   3660  CA  GLY B  55     -71.778  -2.996  39.902  1.00 79.65           C  
ANISOU 3660  CA  GLY B  55    11320   8860  10085  -1861    196   1145       C  
ATOM   3661  C   GLY B  55     -72.038  -1.685  40.607  1.00 81.73           C  
ANISOU 3661  C   GLY B  55    11274   9550  10228  -1823    469   1142       C  
ATOM   3662  O   GLY B  55     -72.209  -1.670  41.828  1.00 82.09           O  
ANISOU 3662  O   GLY B  55    11320   9742  10129  -1973    539   1317       O  
ATOM   3663  N   ASN B  56     -72.079  -0.598  39.843  1.00 76.71           N  
ANISOU 3663  N   ASN B  56    10398   9107   9641  -1625    604    943       N  
ATOM   3664  CA  ASN B  56     -72.341   0.724  40.397  1.00 75.41           C  
ANISOU 3664  CA  ASN B  56     9968   9305   9379  -1546    827    898       C  
ATOM   3665  C   ASN B  56     -73.717   0.817  41.046  1.00 81.95           C  
ANISOU 3665  C   ASN B  56    10602  10444  10090  -1836    957   1030       C  
ATOM   3666  O   ASN B  56     -73.846   1.278  42.180  1.00 81.86           O  
ANISOU 3666  O   ASN B  56    10501  10679   9924  -1867   1085   1102       O  
ATOM   3667  CB  ASN B  56     -72.196   1.796  39.315  1.00 73.04           C  
ANISOU 3667  CB  ASN B  56     9495   9093   9164  -1305    895    677       C  
ATOM   3668  CG  ASN B  56     -70.755   2.012  38.897  1.00 94.99           C  
ANISOU 3668  CG  ASN B  56    12387  11712  11995  -1018    824    549       C  
ATOM   3669  OD1 ASN B  56     -69.947   2.540  39.662  1.00 90.25           O  
ANISOU 3669  OD1 ASN B  56    11799  11169  11323   -888    869    545       O  
ATOM   3670  ND2 ASN B  56     -70.424   1.602  37.678  1.00 84.77           N  
ANISOU 3670  ND2 ASN B  56    11156  10247  10805   -925    710    435       N  
ATOM   3671  N   GLY B  57     -74.745   0.378  40.325  1.00 80.44           N  
ANISOU 3671  N   GLY B  57    10328  10280   9955  -2048    923   1051       N  
ATOM   3672  CA  GLY B  57     -76.126   0.426  40.857  1.00 82.78           C  
ANISOU 3672  CA  GLY B  57    10383  10945  10125  -2346   1047   1171       C  
ATOM   3673  C   GLY B  57     -76.185  -0.197  42.238  1.00 89.18           C  
ANISOU 3673  C   GLY B  57    11295  11830  10759  -2606   1059   1417       C  
ATOM   3674  O   GLY B  57     -76.864   0.299  43.121  1.00 89.35           O  
ANISOU 3674  O   GLY B  57    11086  12264  10600  -2708   1233   1476       O  
ATOM   3675  N   LEU B  58     -75.458  -1.292  42.432  1.00 87.46           N  
ANISOU 3675  N   LEU B  58    11431  11221  10579  -2698    861   1557       N  
ATOM   3676  CA  LEU B  58     -75.307  -1.864  43.758  1.00 90.13           C  
ANISOU 3676  CA  LEU B  58    11924  11578  10743  -2912    840   1807       C  
ATOM   3677  C   LEU B  58     -74.679  -0.855  44.697  1.00 95.71           C  
ANISOU 3677  C   LEU B  58    12528  12518  11318  -2650   1003   1736       C  
ATOM   3678  O   LEU B  58     -75.200  -0.605  45.775  1.00 96.51           O  
ANISOU 3678  O   LEU B  58    12485  12982  11204  -2811   1148   1857       O  
ATOM   3679  CB  LEU B  58     -74.429  -3.099  43.731  1.00 90.94           C  
ANISOU 3679  CB  LEU B  58    12468  11155  10932  -2945    557   1928       C  
ATOM   3680  CG  LEU B  58     -75.091  -4.412  43.410  1.00 97.90           C  
ANISOU 3680  CG  LEU B  58    13566  11774  11859  -3348    343   2122       C  
ATOM   3681  CD1 LEU B  58     -73.975  -5.475  43.181  1.00 98.42           C  
ANISOU 3681  CD1 LEU B  58    14104  11238  12052  -3206     22   2139       C  
ATOM   3682  CD2 LEU B  58     -76.083  -4.770  44.518  1.00103.33           C  
ANISOU 3682  CD2 LEU B  58    14173  12772  12316  -3839    420   2436       C  
ATOM   3683  N   VAL B  59     -73.545  -0.282  44.311  1.00 92.59           N  
ANISOU 3683  N   VAL B  59    12205  11942  11034  -2262    975   1539       N  
ATOM   3684  CA  VAL B  59     -72.932   0.704  45.187  1.00 92.72           C  
ANISOU 3684  CA  VAL B  59    12137  12163  10927  -2034   1107   1463       C  
ATOM   3685  C   VAL B  59     -73.980   1.729  45.582  1.00102.03           C  
ANISOU 3685  C   VAL B  59    12970  13828  11968  -2062   1340   1392       C  
ATOM   3686  O   VAL B  59     -74.215   1.925  46.759  1.00103.52           O  
ANISOU 3686  O   VAL B  59    13086  14306  11942  -2152   1449   1485       O  
ATOM   3687  CB  VAL B  59     -71.710   1.417  44.563  1.00 93.18           C  
ANISOU 3687  CB  VAL B  59    12240  12044  11119  -1640   1069   1235       C  
ATOM   3688  CG1 VAL B  59     -71.224   2.547  45.497  1.00 91.87           C  
ANISOU 3688  CG1 VAL B  59    11970  12119  10817  -1450   1203   1151       C  
ATOM   3689  CG2 VAL B  59     -70.595   0.422  44.299  1.00 93.07           C  
ANISOU 3689  CG2 VAL B  59    12536  11621  11205  -1554    842   1276       C  
ATOM   3690  N   ILE B  60     -74.635   2.332  44.595  1.00101.14           N  
ANISOU 3690  N   ILE B  60    12647  13819  11965  -1978   1400   1225       N  
ATOM   3691  CA  ILE B  60     -75.628   3.390  44.842  1.00103.12           C  
ANISOU 3691  CA  ILE B  60    12557  14522  12101  -1921   1594   1105       C  
ATOM   3692  C   ILE B  60     -76.744   2.940  45.808  1.00114.83           C  
ANISOU 3692  C   ILE B  60    13868  16411  13352  -2260   1706   1292       C  
ATOM   3693  O   ILE B  60     -77.097   3.674  46.723  1.00115.38           O  
ANISOU 3693  O   ILE B  60    13742  16876  13220  -2188   1866   1236       O  
ATOM   3694  CB  ILE B  60     -76.246   3.910  43.530  1.00104.97           C  
ANISOU 3694  CB  ILE B  60    12615  14773  12494  -1807   1596    930       C  
ATOM   3695  CG1 ILE B  60     -75.170   4.583  42.671  1.00101.94           C  
ANISOU 3695  CG1 ILE B  60    12359  14091  12284  -1477   1518    746       C  
ATOM   3696  CG2 ILE B  60     -77.372   4.918  43.813  1.00106.77           C  
ANISOU 3696  CG2 ILE B  60    12488  15483  12596  -1727   1768    803       C  
ATOM   3697  CD1 ILE B  60     -75.596   4.934  41.270  1.00106.54           C  
ANISOU 3697  CD1 ILE B  60    12837  14617  13025  -1384   1478    609       C  
ATOM   3698  N   LEU B  61     -77.259   1.728  45.644  1.00116.98           N  
ANISOU 3698  N   LEU B  61    14221  16594  13630  -2640   1612   1513       N  
ATOM   3699  CA  LEU B  61     -78.350   1.249  46.487  1.00122.18           C  
ANISOU 3699  CA  LEU B  61    14700  17673  14051  -3036   1711   1723       C  
ATOM   3700  C   LEU B  61     -77.877   0.825  47.881  1.00130.45           C  
ANISOU 3700  C   LEU B  61    15913  18781  14872  -3189   1722   1941       C  
ATOM   3701  O   LEU B  61     -78.539   1.104  48.880  1.00132.63           O  
ANISOU 3701  O   LEU B  61    15955  19565  14872  -3324   1894   2006       O  
ATOM   3702  CB  LEU B  61     -79.091   0.093  45.809  1.00124.74           C  
ANISOU 3702  CB  LEU B  61    15072  17868  14455  -3450   1579   1906       C  
ATOM   3703  CG  LEU B  61     -79.814   0.438  44.494  1.00128.88           C  
ANISOU 3703  CG  LEU B  61    15378  18437  15153  -3371   1577   1718       C  
ATOM   3704  CD1 LEU B  61     -80.091  -0.841  43.657  1.00130.85           C  
ANISOU 3704  CD1 LEU B  61    15830  18340  15548  -3725   1359   1873       C  
ATOM   3705  CD2 LEU B  61     -81.100   1.257  44.702  1.00133.04           C  
ANISOU 3705  CD2 LEU B  61    15416  19620  15514  -3382   1792   1617       C  
ATOM   3706  N   VAL B  62     -76.738   0.154  47.954  1.00128.05           N  
ANISOU 3706  N   VAL B  62    15999  17991  14664  -3153   1534   2045       N  
ATOM   3707  CA  VAL B  62     -76.260  -0.403  49.226  1.00131.02           C  
ANISOU 3707  CA  VAL B  62    16582  18368  14831  -3322   1494   2288       C  
ATOM   3708  C   VAL B  62     -75.701   0.653  50.168  1.00137.32           C  
ANISOU 3708  C   VAL B  62    17284  19427  15464  -3016   1643   2145       C  
ATOM   3709  O   VAL B  62     -75.856   0.547  51.378  1.00139.64           O  
ANISOU 3709  O   VAL B  62    17553  20024  15478  -3188   1723   2308       O  
ATOM   3710  CB  VAL B  62     -75.191  -1.470  48.974  1.00134.02           C  
ANISOU 3710  CB  VAL B  62    17422  18126  15374  -3328   1208   2424       C  
ATOM   3711  CG1 VAL B  62     -74.371  -1.756  50.251  1.00134.86           C  
ANISOU 3711  CG1 VAL B  62    17759  18191  15290  -3337   1151   2605       C  
ATOM   3712  CG2 VAL B  62     -75.859  -2.722  48.406  1.00136.50           C  
ANISOU 3712  CG2 VAL B  62    17892  18200  15770  -3742   1030   2640       C  
ATOM   3713  N   MET B  63     -75.030   1.654  49.615  1.00132.83           N  
ANISOU 3713  N   MET B  63    16677  18736  15057  -2586   1665   1849       N  
ATOM   3714  CA  MET B  63     -74.533   2.755  50.412  1.00132.78           C  
ANISOU 3714  CA  MET B  63    16585  18952  14913  -2293   1784   1678       C  
ATOM   3715  C   MET B  63     -75.593   3.806  50.444  1.00138.32           C  
ANISOU 3715  C   MET B  63    16906  20142  15507  -2192   1993   1477       C  
ATOM   3716  O   MET B  63     -76.094   4.176  51.508  1.00139.74           O  
ANISOU 3716  O   MET B  63    16907  20784  15404  -2237   2147   1482       O  
ATOM   3717  CB  MET B  63     -73.284   3.363  49.796  1.00131.96           C  
ANISOU 3717  CB  MET B  63    16631  18484  15024  -1912   1684   1465       C  
ATOM   3718  CG  MET B  63     -72.069   2.505  49.917  1.00136.04           C  
ANISOU 3718  CG  MET B  63    17489  18587  15612  -1905   1482   1604       C  
ATOM   3719  SD  MET B  63     -70.678   3.570  50.261  1.00138.58           S  
ANISOU 3719  SD  MET B  63    17870  18843  15943  -1511   1468   1388       S  
ATOM   3720  CE  MET B  63     -69.783   3.480  48.712  1.00132.30           C  
ANISOU 3720  CE  MET B  63    17188  17606  15475  -1294   1309   1243       C  
ATOM   3721  N   GLY B  64     -75.947   4.276  49.253  1.00134.58           N  
ANISOU 3721  N   GLY B  64    16308  19579  15248  -2039   1988   1290       N  
ATOM   3722  CA  GLY B  64     -76.871   5.383  49.112  1.00135.42           C  
ANISOU 3722  CA  GLY B  64    16074  20084  15296  -1849   2143   1053       C  
ATOM   3723  C   GLY B  64     -77.922   5.333  50.185  1.00144.68           C  
ANISOU 3723  C   GLY B  64    16973  21856  16141  -2051   2320   1134       C  
ATOM   3724  O   GLY B  64     -78.189   6.334  50.844  1.00145.21           O  
ANISOU 3724  O   GLY B  64    16847  22297  16031  -1812   2453    932       O  
ATOM   3725  N   TYR B  65     -78.486   4.164  50.397  1.00144.66           N  
ANISOU 3725  N   TYR B  65    16968  21956  16040  -2496   2310   1427       N  
ATOM   3726  CA  TYR B  65     -79.583   4.070  51.326  1.00148.96           C  
ANISOU 3726  CA  TYR B  65    17202  23149  16249  -2747   2489   1526       C  
ATOM   3727  C   TYR B  65     -79.410   3.395  52.672  1.00156.40           C  
ANISOU 3727  C   TYR B  65    18249  24296  16882  -3055   2525   1806       C  
ATOM   3728  O   TYR B  65     -79.615   4.006  53.721  1.00158.02           O  
ANISOU 3728  O   TYR B  65    18269  24983  16788  -2954   2687   1721       O  
ATOM   3729  CB  TYR B  65     -80.725   3.455  50.580  1.00152.18           C  
ANISOU 3729  CB  TYR B  65    17395  23721  16705  -3069   2493   1634       C  
ATOM   3730  CG  TYR B  65     -81.142   4.358  49.471  1.00152.12           C  
ANISOU 3730  CG  TYR B  65    17179  23713  16905  -2727   2506   1324       C  
ATOM   3731  CD1 TYR B  65     -80.279   4.698  48.470  1.00149.75           C  
ANISOU 3731  CD1 TYR B  65    17120  22857  16922  -2430   2361   1173       C  
ATOM   3732  CD2 TYR B  65     -82.383   4.919  49.459  1.00155.68           C  
ANISOU 3732  CD2 TYR B  65    17182  24758  17212  -2683   2661   1177       C  
ATOM   3733  CE1 TYR B  65     -80.664   5.533  47.499  1.00148.79           C  
ANISOU 3733  CE1 TYR B  65    16828  22742  16962  -2138   2361    919       C  
ATOM   3734  CE2 TYR B  65     -82.757   5.744  48.494  1.00155.21           C  
ANISOU 3734  CE2 TYR B  65    16955  24689  17329  -2355   2648    906       C  
ATOM   3735  CZ  TYR B  65     -81.918   6.048  47.524  1.00158.73           C  
ANISOU 3735  CZ  TYR B  65    17670  24556  18083  -2098   2495    791       C  
ATOM   3736  OH  TYR B  65     -82.372   6.888  46.573  1.00159.06           O  
ANISOU 3736  OH  TYR B  65    17541  24620  18275  -1792   2475    542       O  
ATOM   3737  N   GLN B  66     -79.041   2.140  52.671  1.00153.78           N  
ANISOU 3737  N   GLN B  66    18225  23604  16601  -3422   2361   2137       N  
ATOM   3738  CA  GLN B  66     -78.908   1.485  53.927  1.00156.71           C  
ANISOU 3738  CA  GLN B  66    18717  24158  16667  -3735   2371   2433       C  
ATOM   3739  C   GLN B  66     -77.836   1.994  54.829  1.00159.12           C  
ANISOU 3739  C   GLN B  66    19204  24393  16862  -3447   2369   2355       C  
ATOM   3740  O   GLN B  66     -78.064   2.113  56.005  1.00161.62           O  
ANISOU 3740  O   GLN B  66    19408  25172  16827  -3555   2498   2437       O  
ATOM   3741  CB  GLN B  66     -78.628   0.028  53.697  1.00159.28           C  
ANISOU 3741  CB  GLN B  66    19415  24005  17100  -4153   2134   2802       C  
ATOM   3742  CG  GLN B  66     -79.708  -0.672  52.963  1.00176.68           C  
ANISOU 3742  CG  GLN B  66    21483  26281  19367  -4554   2105   2946       C  
ATOM   3743  CD  GLN B  66     -79.372  -2.118  52.686  1.00196.87           C  
ANISOU 3743  CD  GLN B  66    24478  28269  22054  -4946   1817   3289       C  
ATOM   3744  OE1 GLN B  66     -79.440  -2.981  53.564  1.00198.39           O  
ANISOU 3744  OE1 GLN B  66    24850  28511  22020  -5370   1745   3650       O  
ATOM   3745  NE2 GLN B  66     -79.009  -2.386  51.462  1.00183.32           N  
ANISOU 3745  NE2 GLN B  66    22952  26006  20693  -4799   1636   3174       N  
ATOM   3746  N   LYS B  67     -76.656   2.278  54.292  1.00151.51           N  
ANISOU 3746  N   LYS B  67    18509  22882  16176  -3098   2219   2200       N  
ATOM   3747  CA  LYS B  67     -75.482   2.523  55.128  1.00150.32           C  
ANISOU 3747  CA  LYS B  67    18591  22585  15939  -2890   2159   2185       C  
ATOM   3748  C   LYS B  67     -75.487   3.759  56.067  1.00152.99           C  
ANISOU 3748  C   LYS B  67    18716  23389  16023  -2600   2343   1931       C  
ATOM   3749  O   LYS B  67     -75.637   4.883  55.636  1.00150.54           O  
ANISOU 3749  O   LYS B  67    18218  23174  15807  -2253   2426   1593       O  
ATOM   3750  CB  LYS B  67     -74.212   2.505  54.271  1.00149.68           C  
ANISOU 3750  CB  LYS B  67    18810  21855  16208  -2605   1950   2078       C  
ATOM   3751  CG  LYS B  67     -73.478   1.209  54.219  1.00170.61           C  
ANISOU 3751  CG  LYS B  67    21846  24023  18955  -2802   1705   2366       C  
ATOM   3752  CD  LYS B  67     -72.001   1.423  53.911  1.00181.33           C  
ANISOU 3752  CD  LYS B  67    23448  24932  20518  -2439   1540   2224       C  
ATOM   3753  CE  LYS B  67     -71.382   0.298  52.987  1.00194.91           C  
ANISOU 3753  CE  LYS B  67    25485  26059  22514  -2476   1273   2344       C  
ATOM   3754  NZ  LYS B  67     -69.927   0.377  52.522  1.00201.22           N  
ANISOU 3754  NZ  LYS B  67    26489  26447  23519  -2117   1097   2197       N  
ATOM   3755  N   LYS B  68     -75.254   3.506  57.357  1.00151.10           N  
ANISOU 3755  N   LYS B  68    18553  23398  15460  -2741   2372   2102       N  
ATOM   3756  CA  LYS B  68     -75.237   4.551  58.372  1.00151.23           C  
ANISOU 3756  CA  LYS B  68    18401  23871  15190  -2493   2527   1875       C  
ATOM   3757  C   LYS B  68     -73.850   4.879  58.948  1.00151.79           C  
ANISOU 3757  C   LYS B  68    18753  23659  15260  -2243   2400   1807       C  
ATOM   3758  O   LYS B  68     -73.580   6.007  59.340  1.00150.86           O  
ANISOU 3758  O   LYS B  68    18550  23709  15062  -1906   2467   1500       O  
ATOM   3759  CB  LYS B  68     -76.254   4.269  59.476  1.00158.71           C  
ANISOU 3759  CB  LYS B  68    19102  25519  15681  -2816   2717   2050       C  
ATOM   3760  CG  LYS B  68     -77.175   5.431  59.801  1.00174.69           C  
ANISOU 3760  CG  LYS B  68    20700  28193  17482  -2565   2958   1703       C  
ATOM   3761  CD  LYS B  68     -78.268   5.587  58.787  1.00183.39           C  
ANISOU 3761  CD  LYS B  68    21495  29442  18742  -2575   3042   1585       C  
ATOM   3762  CE  LYS B  68     -79.144   6.765  59.113  1.00194.17           C  
ANISOU 3762  CE  LYS B  68    22444  31444  19888  -2254   3252   1208       C  
ATOM   3763  NZ  LYS B  68     -80.440   6.709  58.376  1.00203.40           N  
ANISOU 3763  NZ  LYS B  68    23237  32954  21094  -2364   3359   1168       N  
ATOM   3764  N   LEU B  69     -72.931   3.944  58.992  1.00146.14           N  
ANISOU 3764  N   LEU B  69    18380  22507  14640  -2378   2195   2068       N  
ATOM   3765  CA  LEU B  69     -71.638   4.421  59.385  1.00143.07           C  
ANISOU 3765  CA  LEU B  69    18192  21886  14280  -2087   2079   1940       C  
ATOM   3766  C   LEU B  69     -70.820   4.380  58.095  1.00139.84           C  
ANISOU 3766  C   LEU B  69    17947  20880  14306  -1888   1904   1838       C  
ATOM   3767  O   LEU B  69     -70.426   3.326  57.613  1.00139.16           O  
ANISOU 3767  O   LEU B  69    18088  20397  14390  -2033   1728   2062       O  
ATOM   3768  CB  LEU B  69     -71.045   3.599  60.517  1.00145.82           C  
ANISOU 3768  CB  LEU B  69    18786  22246  14374  -2290   1969   2251       C  
ATOM   3769  CG  LEU B  69     -70.104   4.386  61.410  1.00150.19           C  
ANISOU 3769  CG  LEU B  69    19405  22893  14767  -2015   1945   2074       C  
ATOM   3770  CD1 LEU B  69     -70.299   4.069  62.872  1.00154.45           C  
ANISOU 3770  CD1 LEU B  69    19959  23877  14847  -2232   2006   2286       C  
ATOM   3771  CD2 LEU B  69     -68.670   4.241  60.976  1.00149.73           C  
ANISOU 3771  CD2 LEU B  69    19621  22289  14982  -1803   1703   2048       C  
ATOM   3772  N   ARG B  70     -70.573   5.558  57.541  1.00131.19           N  
ANISOU 3772  N   ARG B  70    16739  19734  13373  -1550   1943   1490       N  
ATOM   3773  CA  ARG B  70     -69.858   5.687  56.283  1.00126.12           C  
ANISOU 3773  CA  ARG B  70    16198  18617  13106  -1362   1808   1367       C  
ATOM   3774  C   ARG B  70     -68.599   6.516  56.405  1.00124.04           C  
ANISOU 3774  C   ARG B  70    16039  18184  12906  -1067   1711   1163       C  
ATOM   3775  O   ARG B  70     -68.588   7.556  57.001  1.00123.92           O  
ANISOU 3775  O   ARG B  70    15933  18405  12747   -901   1788    951       O  
ATOM   3776  CB  ARG B  70     -70.785   6.292  55.243  1.00125.67           C  
ANISOU 3776  CB  ARG B  70    15913  18618  13218  -1285   1915   1173       C  
ATOM   3777  CG  ARG B  70     -71.259   5.351  54.150  1.00137.85           C  
ANISOU 3777  CG  ARG B  70    17477  19919  14980  -1481   1857   1328       C  
ATOM   3778  CD  ARG B  70     -71.258   6.094  52.797  1.00150.42           C  
ANISOU 3778  CD  ARG B  70    18982  21303  16866  -1252   1843   1081       C  
ATOM   3779  NE  ARG B  70     -72.038   7.338  52.778  1.00164.17           N  
ANISOU 3779  NE  ARG B  70    20471  23357  18548  -1065   1992    816       N  
ATOM   3780  CZ  ARG B  70     -73.219   7.497  52.188  1.00182.30           C  
ANISOU 3780  CZ  ARG B  70    22538  25848  20880  -1104   2090    753       C  
ATOM   3781  NH1 ARG B  70     -73.785   6.496  51.574  1.00172.49           N  
ANISOU 3781  NH1 ARG B  70    21280  24532  19728  -1364   2067    943       N  
ATOM   3782  NH2 ARG B  70     -73.835   8.652  52.216  1.00169.52           N  
ANISOU 3782  NH2 ARG B  70    20713  24493  19203   -874   2191    491       N  
ATOM   3783  N   SER B  71     -67.523   6.126  55.721  1.00115.37           N  
ANISOU 3783  N   SER B  71    15119  16674  12043   -984   1532   1193       N  
ATOM   3784  CA  SER B  71     -66.283   6.937  55.722  1.00111.73           C  
ANISOU 3784  CA  SER B  71    14722  16078  11652   -734   1433   1000       C  
ATOM   3785  C   SER B  71     -66.300   8.166  54.777  1.00109.42           C  
ANISOU 3785  C   SER B  71    14306  15716  11553   -535   1471    707       C  
ATOM   3786  O   SER B  71     -67.231   8.322  53.987  1.00108.15           O  
ANISOU 3786  O   SER B  71    14016  15570  11505   -556   1559    650       O  
ATOM   3787  CB  SER B  71     -65.071   6.055  55.408  1.00114.24           C  
ANISOU 3787  CB  SER B  71    15241  16056  12109   -705   1223   1135       C  
ATOM   3788  OG  SER B  71     -63.879   6.821  55.374  1.00121.43           O  
ANISOU 3788  OG  SER B  71    16170  16893  13075   -498   1132    957       O  
ATOM   3789  N   MET B  72     -65.275   9.028  54.857  1.00102.21           N  
ANISOU 3789  N   MET B  72    13440  14727  10669   -362   1386    535       N  
ATOM   3790  CA  MET B  72     -65.187  10.202  53.986  1.00 98.84           C  
ANISOU 3790  CA  MET B  72    12945  14195  10414   -210   1382    291       C  
ATOM   3791  C   MET B  72     -64.865   9.752  52.565  1.00 97.89           C  
ANISOU 3791  C   MET B  72    12833  13787  10572   -218   1309    336       C  
ATOM   3792  O   MET B  72     -65.368  10.340  51.608  1.00 96.38           O  
ANISOU 3792  O   MET B  72    12559  13530  10530   -170   1346    217       O  
ATOM   3793  CB  MET B  72     -64.135  11.187  54.503  1.00101.03           C  
ANISOU 3793  CB  MET B  72    13292  14467  10628    -87   1285    127       C  
ATOM   3794  CG  MET B  72     -64.601  11.999  55.693  1.00106.79           C  
ANISOU 3794  CG  MET B  72    13999  15474  11101    -21   1357    -20       C  
ATOM   3795  SD  MET B  72     -65.554  13.463  55.223  1.00110.92           S  
ANISOU 3795  SD  MET B  72    14430  16034  11680    151   1420   -326       S  
ATOM   3796  CE  MET B  72     -67.191  12.963  55.712  1.00109.73           C  
ANISOU 3796  CE  MET B  72    14097  16255  11340    103   1632   -273       C  
ATOM   3797  N   THR B  73     -64.081   8.658  52.447  1.00 92.29           N  
ANISOU 3797  N   THR B  73    12229  12920   9915   -266   1197    505       N  
ATOM   3798  CA  THR B  73     -63.704   8.000  51.195  1.00 89.60           C  
ANISOU 3798  CA  THR B  73    11910  12331   9802   -255   1112    548       C  
ATOM   3799  C   THR B  73     -64.945   7.335  50.591  1.00 91.97           C  
ANISOU 3799  C   THR B  73    12166  12599  10179   -381   1192    639       C  
ATOM   3800  O   THR B  73     -65.222   7.534  49.411  1.00 90.29           O  
ANISOU 3800  O   THR B  73    11884  12278  10143   -353   1203    558       O  
ATOM   3801  CB  THR B  73     -62.554   7.010  51.455  1.00 95.76           C  
ANISOU 3801  CB  THR B  73    12825  12986  10574   -220    950    675       C  
ATOM   3802  OG1 THR B  73     -61.434   7.731  51.967  1.00 96.04           O  
ANISOU 3802  OG1 THR B  73    12858  13099  10534   -115    879    573       O  
ATOM   3803  CG2 THR B  73     -62.139   6.236  50.211  1.00 91.89           C  
ANISOU 3803  CG2 THR B  73    12361  12263  10291   -166    849    690       C  
ATOM   3804  N   ASP B  74     -65.709   6.592  51.419  1.00 89.26           N  
ANISOU 3804  N   ASP B  74    11855  12379   9682   -545   1244    814       N  
ATOM   3805  CA  ASP B  74     -66.936   5.897  51.027  1.00 89.33           C  
ANISOU 3805  CA  ASP B  74    11812  12406   9721   -730   1312    933       C  
ATOM   3806  C   ASP B  74     -68.031   6.853  50.545  1.00 91.45           C  
ANISOU 3806  C   ASP B  74    11867  12860  10020   -701   1465    767       C  
ATOM   3807  O   ASP B  74     -68.901   6.430  49.785  1.00 91.17           O  
ANISOU 3807  O   ASP B  74    11757  12798  10083   -811   1497    810       O  
ATOM   3808  CB  ASP B  74     -67.441   4.995  52.158  1.00 94.04           C  
ANISOU 3808  CB  ASP B  74    12485  13149  10098   -957   1329   1179       C  
ATOM   3809  CG  ASP B  74     -66.493   3.878  52.543  1.00105.12           C  
ANISOU 3809  CG  ASP B  74    14140  14315  11487   -990   1137   1376       C  
ATOM   3810  OD1 ASP B  74     -65.745   3.333  51.719  1.00104.86           O  
ANISOU 3810  OD1 ASP B  74    14225  13969  11647   -888    980   1367       O  
ATOM   3811  OD2 ASP B  74     -66.534   3.582  53.752  1.00112.31           O  
ANISOU 3811  OD2 ASP B  74    15123  15390  12161  -1108   1141   1535       O  
ATOM   3812  N   LYS B  75     -67.970   8.141  50.953  1.00 86.67           N  
ANISOU 3812  N   LYS B  75    11176  12421   9333   -539   1531    566       N  
ATOM   3813  CA  LYS B  75     -68.913   9.173  50.514  1.00 85.61           C  
ANISOU 3813  CA  LYS B  75    10866  12433   9229   -440   1634    374       C  
ATOM   3814  C   LYS B  75     -68.549   9.631  49.092  1.00 84.84           C  
ANISOU 3814  C   LYS B  75    10776  12072   9387   -330   1555    260       C  
ATOM   3815  O   LYS B  75     -69.442   9.809  48.261  1.00 83.70           O  
ANISOU 3815  O   LYS B  75    10513  11946   9342   -327   1600    207       O  
ATOM   3816  CB  LYS B  75     -68.952  10.358  51.503  1.00 89.52           C  
ANISOU 3816  CB  LYS B  75    11316  13161   9536   -283   1692    185       C  
ATOM   3817  CG  LYS B  75     -70.042  11.402  51.214  1.00110.77           C  
ANISOU 3817  CG  LYS B  75    13834  16030  12225   -134   1780    -32       C  
ATOM   3818  CD  LYS B  75     -71.473  10.903  51.482  1.00126.09           C  
ANISOU 3818  CD  LYS B  75    15560  18320  14028   -256   1934     36       C  
ATOM   3819  CE  LYS B  75     -72.508  11.927  51.082  1.00138.06           C  
ANISOU 3819  CE  LYS B  75    16886  20013  15557    -54   1996   -202       C  
ATOM   3820  NZ  LYS B  75     -73.893  11.408  51.232  1.00150.09           N  
ANISOU 3820  NZ  LYS B  75    18149  21928  16950   -186   2145   -137       N  
ATOM   3821  N   TYR B  76     -67.238   9.801  48.811  1.00 78.66           N  
ANISOU 3821  N   TYR B  76    10117  11079   8690   -252   1434    232       N  
ATOM   3822  CA  TYR B  76     -66.761  10.184  47.479  1.00 75.68           C  
ANISOU 3822  CA  TYR B  76     9744  10494   8517   -182   1357    150       C  
ATOM   3823  C   TYR B  76     -66.888   9.009  46.528  1.00 77.20           C  
ANISOU 3823  C   TYR B  76     9948  10537   8847   -275   1321    271       C  
ATOM   3824  O   TYR B  76     -67.131   9.223  45.348  1.00 76.31           O  
ANISOU 3824  O   TYR B  76     9783  10333   8878   -251   1307    210       O  
ATOM   3825  CB  TYR B  76     -65.294  10.642  47.495  1.00 75.95           C  
ANISOU 3825  CB  TYR B  76     9869  10422   8568   -109   1243     97       C  
ATOM   3826  CG  TYR B  76     -65.006  11.940  48.218  1.00 78.45           C  
ANISOU 3826  CG  TYR B  76    10210  10817   8780    -24   1229    -51       C  
ATOM   3827  CD1 TYR B  76     -65.636  13.126  47.844  1.00 80.41           C  
ANISOU 3827  CD1 TYR B  76    10426  11061   9067     59   1242   -208       C  
ATOM   3828  CD2 TYR B  76     -64.023  12.009  49.200  1.00 79.85           C  
ANISOU 3828  CD2 TYR B  76    10465  11042   8831    -15   1168    -45       C  
ATOM   3829  CE1 TYR B  76     -65.352  14.329  48.487  1.00 81.99           C  
ANISOU 3829  CE1 TYR B  76    10695  11279   9179    146   1188   -362       C  
ATOM   3830  CE2 TYR B  76     -63.727  13.206  49.846  1.00 81.46           C  
ANISOU 3830  CE2 TYR B  76    10714  11295   8940     50   1128   -196       C  
ATOM   3831  CZ  TYR B  76     -64.391  14.365  49.483  1.00 90.01           C  
ANISOU 3831  CZ  TYR B  76    11791  12345  10066    130   1133   -359       C  
ATOM   3832  OH  TYR B  76     -64.101  15.541  50.125  1.00 94.53           O  
ANISOU 3832  OH  TYR B  76    12451  12918  10547    202   1058   -524       O  
ATOM   3833  N   ARG B  77     -66.709   7.772  47.030  1.00 72.76           N  
ANISOU 3833  N   ARG B  77     9479   9932   8235   -380   1282    440       N  
ATOM   3834  CA  ARG B  77     -66.808   6.559  46.215  1.00 71.57           C  
ANISOU 3834  CA  ARG B  77     9391   9595   8207   -463   1208    547       C  
ATOM   3835  C   ARG B  77     -68.216   6.308  45.665  1.00 76.66           C  
ANISOU 3835  C   ARG B  77     9930  10297   8901   -598   1285    577       C  
ATOM   3836  O   ARG B  77     -68.343   5.652  44.629  1.00 76.19           O  
ANISOU 3836  O   ARG B  77     9897  10070   8981   -636   1218    593       O  
ATOM   3837  CB  ARG B  77     -66.208   5.336  46.921  1.00 70.03           C  
ANISOU 3837  CB  ARG B  77     9374   9287   7948   -524   1097    720       C  
ATOM   3838  CG  ARG B  77     -64.682   5.380  46.951  1.00 70.97           C  
ANISOU 3838  CG  ARG B  77     9574   9310   8082   -349    974    664       C  
ATOM   3839  CD  ARG B  77     -64.061   4.181  47.632  1.00 77.51           C  
ANISOU 3839  CD  ARG B  77    10592  10008   8849   -357    829    823       C  
ATOM   3840  NE  ARG B  77     -64.182   2.967  46.826  1.00 84.12           N  
ANISOU 3840  NE  ARG B  77    11553  10593   9815   -382    703    889       N  
ATOM   3841  CZ  ARG B  77     -63.656   1.791  47.150  1.00 99.51           C  
ANISOU 3841  CZ  ARG B  77    13715  12340  11754   -357    521   1014       C  
ATOM   3842  NH1 ARG B  77     -62.961   1.654  48.272  1.00 90.34           N  
ANISOU 3842  NH1 ARG B  77    12651  11222  10453   -311    451   1103       N  
ATOM   3843  NH2 ARG B  77     -63.825   0.742  46.359  1.00 85.95           N  
ANISOU 3843  NH2 ARG B  77    12133  10361  10161   -367    385   1043       N  
ATOM   3844  N   LEU B  78     -69.264   6.867  46.322  1.00 74.46           N  
ANISOU 3844  N   LEU B  78     9512  10283   8498   -654   1420    561       N  
ATOM   3845  CA  LEU B  78     -70.637   6.775  45.814  1.00 74.97           C  
ANISOU 3845  CA  LEU B  78     9416  10478   8589   -768   1501    565       C  
ATOM   3846  C   LEU B  78     -70.932   7.948  44.868  1.00 77.64           C  
ANISOU 3846  C   LEU B  78     9627  10835   9038   -592   1526    364       C  
ATOM   3847  O   LEU B  78     -71.720   7.791  43.938  1.00 77.32           O  
ANISOU 3847  O   LEU B  78     9490  10791   9097   -641   1530    349       O  
ATOM   3848  CB  LEU B  78     -71.711   6.580  46.905  1.00 77.45           C  
ANISOU 3848  CB  LEU B  78     9608  11125   8696   -937   1628    664       C  
ATOM   3849  CG  LEU B  78     -71.967   7.714  47.876  1.00 82.74           C  
ANISOU 3849  CG  LEU B  78    10150  12103   9183   -795   1747    526       C  
ATOM   3850  CD1 LEU B  78     -73.171   8.537  47.444  1.00 83.31           C  
ANISOU 3850  CD1 LEU B  78     9976  12420   9258   -704   1847    365       C  
ATOM   3851  CD2 LEU B  78     -72.199   7.174  49.268  1.00 87.64           C  
ANISOU 3851  CD2 LEU B  78    10774  12977   9549   -967   1818    685       C  
ATOM   3852  N   HIS B  79     -70.254   9.101  45.087  1.00 72.86           N  
ANISOU 3852  N   HIS B  79     9047  10224   8412   -400   1516    220       N  
ATOM   3853  CA  HIS B  79     -70.312  10.292  44.239  1.00 71.38           C  
ANISOU 3853  CA  HIS B  79     8811   9988   8323   -235   1491     49       C  
ATOM   3854  C   HIS B  79     -69.708   9.876  42.889  1.00 74.24           C  
ANISOU 3854  C   HIS B  79     9237  10111   8858   -254   1392     74       C  
ATOM   3855  O   HIS B  79     -70.259  10.195  41.836  1.00 73.93           O  
ANISOU 3855  O   HIS B  79     9127  10044   8920   -225   1378     16       O  
ATOM   3856  CB  HIS B  79     -69.446  11.401  44.846  1.00 71.87           C  
ANISOU 3856  CB  HIS B  79     8960  10027   8321    -90   1452    -67       C  
ATOM   3857  CG  HIS B  79     -70.202  12.556  45.412  1.00 76.66           C  
ANISOU 3857  CG  HIS B  79     9490  10806   8831     58   1501   -229       C  
ATOM   3858  ND1 HIS B  79     -70.538  12.608  46.753  1.00 80.46           N  
ANISOU 3858  ND1 HIS B  79     9930  11529   9114     75   1586   -253       N  
ATOM   3859  CD2 HIS B  79     -70.591  13.708  44.820  1.00 78.37           C  
ANISOU 3859  CD2 HIS B  79     9689  10977   9113    218   1452   -387       C  
ATOM   3860  CE1 HIS B  79     -71.147  13.770  46.923  1.00 80.87           C  
ANISOU 3860  CE1 HIS B  79     9925  11686   9117    270   1592   -451       C  
ATOM   3861  NE2 HIS B  79     -71.202  14.465  45.788  1.00 80.15           N  
ANISOU 3861  NE2 HIS B  79     9860  11404   9190    366   1500   -533       N  
ATOM   3862  N   LEU B  80     -68.589   9.123  42.950  1.00 70.21           N  
ANISOU 3862  N   LEU B  80     8854   9459   8362   -288   1319    153       N  
ATOM   3863  CA  LEU B  80     -67.850   8.552  41.826  1.00 69.14           C  
ANISOU 3863  CA  LEU B  80     8777   9144   8349   -281   1224    162       C  
ATOM   3864  C   LEU B  80     -68.707   7.488  41.128  1.00 74.48           C  
ANISOU 3864  C   LEU B  80     9433   9762   9103   -396   1213    229       C  
ATOM   3865  O   LEU B  80     -68.710   7.412  39.896  1.00 73.21           O  
ANISOU 3865  O   LEU B  80     9252   9517   9047   -374   1165    177       O  
ATOM   3866  CB  LEU B  80     -66.530   7.937  42.355  1.00 69.09           C  
ANISOU 3866  CB  LEU B  80     8892   9057   8301   -251   1145    214       C  
ATOM   3867  CG  LEU B  80     -65.626   7.198  41.373  1.00 72.76           C  
ANISOU 3867  CG  LEU B  80     9409   9383   8853   -196   1038    200       C  
ATOM   3868  CD1 LEU B  80     -64.758   8.162  40.606  1.00 71.70           C  
ANISOU 3868  CD1 LEU B  80     9214   9287   8740   -110   1013     93       C  
ATOM   3869  CD2 LEU B  80     -64.753   6.207  42.104  1.00 75.90           C  
ANISOU 3869  CD2 LEU B  80     9931   9708   9201   -163    948    277       C  
ATOM   3870  N   SER B  81     -69.434   6.674  41.925  1.00 73.01           N  
ANISOU 3870  N   SER B  81     9257   9634   8849   -545   1249    351       N  
ATOM   3871  CA  SER B  81     -70.314   5.619  41.423  1.00 73.84           C  
ANISOU 3871  CA  SER B  81     9359   9685   9011   -716   1221    439       C  
ATOM   3872  C   SER B  81     -71.504   6.193  40.646  1.00 77.92           C  
ANISOU 3872  C   SER B  81     9688  10340   9577   -736   1286    362       C  
ATOM   3873  O   SER B  81     -71.937   5.573  39.676  1.00 77.67           O  
ANISOU 3873  O   SER B  81     9652  10216   9642   -818   1226    368       O  
ATOM   3874  CB  SER B  81     -70.806   4.741  42.567  1.00 78.97           C  
ANISOU 3874  CB  SER B  81    10061  10400   9542   -922   1241    619       C  
ATOM   3875  OG  SER B  81     -71.006   3.415  42.109  1.00 88.37           O  
ANISOU 3875  OG  SER B  81    11383  11387  10806  -1089   1122    732       O  
ATOM   3876  N   VAL B  82     -72.023   7.373  41.066  1.00 74.50           N  
ANISOU 3876  N   VAL B  82     9109  10123   9074   -639   1387    273       N  
ATOM   3877  CA  VAL B  82     -73.129   8.076  40.404  1.00 74.54           C  
ANISOU 3877  CA  VAL B  82     8927  10280   9114   -593   1431    177       C  
ATOM   3878  C   VAL B  82     -72.651   8.563  39.031  1.00 76.99           C  
ANISOU 3878  C   VAL B  82     9278  10416   9558   -470   1341     82       C  
ATOM   3879  O   VAL B  82     -73.378   8.432  38.043  1.00 76.39           O  
ANISOU 3879  O   VAL B  82     9115  10352   9557   -504   1313     59       O  
ATOM   3880  CB  VAL B  82     -73.696   9.219  41.295  1.00 79.33           C  
ANISOU 3880  CB  VAL B  82     9400  11146   9597   -459   1531     77       C  
ATOM   3881  CG1 VAL B  82     -74.514  10.223  40.491  1.00 79.22           C  
ANISOU 3881  CG1 VAL B  82     9240  11220   9639   -301   1523    -67       C  
ATOM   3882  CG2 VAL B  82     -74.536   8.655  42.436  1.00 81.51           C  
ANISOU 3882  CG2 VAL B  82     9554  11704   9710   -621   1642    173       C  
ATOM   3883  N   ALA B  83     -71.404   9.079  38.977  1.00 72.86           N  
ANISOU 3883  N   ALA B  83     8880   9757   9046   -353   1291     40       N  
ATOM   3884  CA  ALA B  83     -70.752   9.574  37.761  1.00 71.24           C  
ANISOU 3884  CA  ALA B  83     8718   9427   8924   -269   1210    -26       C  
ATOM   3885  C   ALA B  83     -70.543   8.446  36.751  1.00 74.35           C  
ANISOU 3885  C   ALA B  83     9153   9702   9396   -346   1142      5       C  
ATOM   3886  O   ALA B  83     -70.900   8.616  35.590  1.00 73.57           O  
ANISOU 3886  O   ALA B  83     9005   9593   9356   -334   1102    -41       O  
ATOM   3887  CB  ALA B  83     -69.420  10.231  38.104  1.00 71.09           C  
ANISOU 3887  CB  ALA B  83     8801   9343   8865   -188   1176    -52       C  
ATOM   3888  N   ASP B  84     -69.997   7.294  37.193  1.00 71.29           N  
ANISOU 3888  N   ASP B  84     8871   9218   8998   -410   1109     76       N  
ATOM   3889  CA  ASP B  84     -69.754   6.134  36.331  1.00 71.53           C  
ANISOU 3889  CA  ASP B  84     8980   9101   9095   -448   1012     77       C  
ATOM   3890  C   ASP B  84     -71.046   5.468  35.851  1.00 75.88           C  
ANISOU 3890  C   ASP B  84     9478   9655   9699   -600    998    108       C  
ATOM   3891  O   ASP B  84     -71.069   4.921  34.749  1.00 75.43           O  
ANISOU 3891  O   ASP B  84     9451   9504   9706   -606    913     55       O  
ATOM   3892  CB  ASP B  84     -68.794   5.122  36.992  1.00 74.51           C  
ANISOU 3892  CB  ASP B  84     9519   9341   9448   -434    940    132       C  
ATOM   3893  CG  ASP B  84     -67.333   5.565  37.046  1.00 89.27           C  
ANISOU 3893  CG  ASP B  84    11420  11220  11279   -272    914     70       C  
ATOM   3894  OD1 ASP B  84     -66.832   6.100  36.029  1.00 90.16           O  
ANISOU 3894  OD1 ASP B  84    11472  11380  11406   -188    899    -24       O  
ATOM   3895  OD2 ASP B  84     -66.667   5.298  38.074  1.00 96.81           O  
ANISOU 3895  OD2 ASP B  84    12455  12153  12174   -243    897    125       O  
ATOM   3896  N   LEU B  85     -72.124   5.543  36.658  1.00 73.52           N  
ANISOU 3896  N   LEU B  85     9080   9500   9353   -726   1080    182       N  
ATOM   3897  CA  LEU B  85     -73.429   4.987  36.298  1.00 74.71           C  
ANISOU 3897  CA  LEU B  85     9131   9722   9531   -910   1074    224       C  
ATOM   3898  C   LEU B  85     -74.055   5.835  35.189  1.00 77.90           C  
ANISOU 3898  C   LEU B  85     9380  10234   9985   -821   1080    113       C  
ATOM   3899  O   LEU B  85     -74.531   5.284  34.197  1.00 78.27           O  
ANISOU 3899  O   LEU B  85     9411  10232  10095   -902   1003     90       O  
ATOM   3900  CB  LEU B  85     -74.355   4.897  37.527  1.00 76.51           C  
ANISOU 3900  CB  LEU B  85     9250  10165   9654  -1075   1176    335       C  
ATOM   3901  CG  LEU B  85     -75.737   4.264  37.331  1.00 83.57           C  
ANISOU 3901  CG  LEU B  85    10004  11203  10544  -1327   1178    406       C  
ATOM   3902  CD1 LEU B  85     -75.655   2.740  37.219  1.00 85.24           C  
ANISOU 3902  CD1 LEU B  85    10417  11171  10799  -1572   1041    533       C  
ATOM   3903  CD2 LEU B  85     -76.650   4.630  38.474  1.00 88.89           C  
ANISOU 3903  CD2 LEU B  85    10475  12228  11073  -1424   1322    469       C  
ATOM   3904  N   LEU B  86     -73.989   7.175  35.339  1.00 73.01           N  
ANISOU 3904  N   LEU B  86     8676   9733   9332   -647   1143     40       N  
ATOM   3905  CA  LEU B  86     -74.496   8.174  34.395  1.00 72.01           C  
ANISOU 3905  CA  LEU B  86     8437   9684   9239   -526   1123    -54       C  
ATOM   3906  C   LEU B  86     -73.967   7.931  32.966  1.00 74.07           C  
ANISOU 3906  C   LEU B  86     8776   9801   9567   -504   1019    -97       C  
ATOM   3907  O   LEU B  86     -74.736   8.034  32.006  1.00 74.46           O  
ANISOU 3907  O   LEU B  86     8732   9910   9651   -515    973   -136       O  
ATOM   3908  CB  LEU B  86     -74.095   9.577  34.884  1.00 71.32           C  
ANISOU 3908  CB  LEU B  86     8357   9634   9106   -336   1155   -115       C  
ATOM   3909  CG  LEU B  86     -75.105  10.695  34.656  1.00 76.78           C  
ANISOU 3909  CG  LEU B  86     8906  10475   9793   -198   1153   -198       C  
ATOM   3910  CD1 LEU B  86     -76.134  10.743  35.778  1.00 78.67           C  
ANISOU 3910  CD1 LEU B  86     8974  10967   9948   -199   1255   -212       C  
ATOM   3911  CD2 LEU B  86     -74.404  12.032  34.569  1.00 78.24           C  
ANISOU 3911  CD2 LEU B  86     9202  10555   9970    -20   1096   -260       C  
ATOM   3912  N   PHE B  87     -72.675   7.555  32.841  1.00 68.19           N  
ANISOU 3912  N   PHE B  87     8183   8905   8820   -470    980    -99       N  
ATOM   3913  CA  PHE B  87     -72.028   7.255  31.565  1.00 66.70           C  
ANISOU 3913  CA  PHE B  87     8055   8634   8653   -433    893   -159       C  
ATOM   3914  C   PHE B  87     -72.390   5.868  31.017  1.00 71.73           C  
ANISOU 3914  C   PHE B  87     8741   9175   9338   -544    813   -172       C  
ATOM   3915  O   PHE B  87     -72.691   5.766  29.827  1.00 71.16           O  
ANISOU 3915  O   PHE B  87     8638   9116   9284   -544    747   -237       O  
ATOM   3916  CB  PHE B  87     -70.501   7.446  31.652  1.00 67.09           C  
ANISOU 3916  CB  PHE B  87     8202   8632   8656   -333    884   -179       C  
ATOM   3917  CG  PHE B  87     -69.730   6.925  30.461  1.00 68.09           C  
ANISOU 3917  CG  PHE B  87     8370   8734   8769   -284    807   -257       C  
ATOM   3918  CD1 PHE B  87     -68.906   5.813  30.579  1.00 71.23           C  
ANISOU 3918  CD1 PHE B  87     8868   9035   9161   -240    752   -296       C  
ATOM   3919  CD2 PHE B  87     -69.852   7.528  29.211  1.00 69.64           C  
ANISOU 3919  CD2 PHE B  87     8504   9016   8939   -264    776   -301       C  
ATOM   3920  CE1 PHE B  87     -68.207   5.319  29.469  1.00 72.26           C  
ANISOU 3920  CE1 PHE B  87     9016   9185   9255   -151    679   -409       C  
ATOM   3921  CE2 PHE B  87     -69.161   7.026  28.101  1.00 72.37           C  
ANISOU 3921  CE2 PHE B  87     8866   9398   9235   -215    715   -389       C  
ATOM   3922  CZ  PHE B  87     -68.341   5.929  28.239  1.00 70.85           C  
ANISOU 3922  CZ  PHE B  87     8752   9136   9032   -147    672   -458       C  
ATOM   3923  N   VAL B  88     -72.349   4.805  31.864  1.00 69.49           N  
ANISOU 3923  N   VAL B  88     8559   8778   9066   -645    794   -107       N  
ATOM   3924  CA  VAL B  88     -72.657   3.425  31.435  1.00 70.74           C  
ANISOU 3924  CA  VAL B  88     8826   8777   9274   -770    674   -111       C  
ATOM   3925  C   VAL B  88     -74.025   3.259  30.781  1.00 74.94           C  
ANISOU 3925  C   VAL B  88     9239   9392   9843   -930    645   -112       C  
ATOM   3926  O   VAL B  88     -74.183   2.407  29.909  1.00 75.89           O  
ANISOU 3926  O   VAL B  88     9438   9392  10003   -990    520   -174       O  
ATOM   3927  CB  VAL B  88     -72.307   2.287  32.435  1.00 76.17           C  
ANISOU 3927  CB  VAL B  88     9701   9275   9966   -861    612    -19       C  
ATOM   3928  CG1 VAL B  88     -70.817   2.264  32.764  1.00 75.36           C  
ANISOU 3928  CG1 VAL B  88     9722   9082   9830   -659    590    -60       C  
ATOM   3929  CG2 VAL B  88     -73.149   2.355  33.701  1.00 76.86           C  
ANISOU 3929  CG2 VAL B  88     9717   9473  10011  -1049    706    138       C  
ATOM   3930  N   ILE B  89     -74.993   4.111  31.187  1.00 70.54           N  
ANISOU 3930  N   ILE B  89     8483   9057   9263   -975    750    -65       N  
ATOM   3931  CA  ILE B  89     -76.368   4.195  30.675  1.00 70.90           C  
ANISOU 3931  CA  ILE B  89     8343   9273   9325  -1099    741    -69       C  
ATOM   3932  C   ILE B  89     -76.372   4.646  29.180  1.00 73.04           C  
ANISOU 3932  C   ILE B  89     8575   9562   9617   -978    667   -187       C  
ATOM   3933  O   ILE B  89     -77.244   4.219  28.422  1.00 73.83           O  
ANISOU 3933  O   ILE B  89     8600   9709   9741  -1097    589   -215       O  
ATOM   3934  CB  ILE B  89     -77.211   5.112  31.624  1.00 74.01           C  
ANISOU 3934  CB  ILE B  89     8519   9939   9661  -1091    877    -20       C  
ATOM   3935  CG1 ILE B  89     -77.522   4.392  32.955  1.00 75.57           C  
ANISOU 3935  CG1 ILE B  89     8723  10185   9806  -1301    937    114       C  
ATOM   3936  CG2 ILE B  89     -78.493   5.650  30.969  1.00 75.56           C  
ANISOU 3936  CG2 ILE B  89     8471  10378   9860  -1095    872    -70       C  
ATOM   3937  CD1 ILE B  89     -77.838   5.317  34.148  1.00 82.18           C  
ANISOU 3937  CD1 ILE B  89     9402  11277  10545  -1219   1090    136       C  
ATOM   3938  N   THR B  90     -75.391   5.482  28.767  1.00 66.91           N  
ANISOU 3938  N   THR B  90     7850   8761   8813   -772    682   -243       N  
ATOM   3939  CA  THR B  90     -75.273   5.969  27.384  1.00 65.94           C  
ANISOU 3939  CA  THR B  90     7705   8678   8672   -674    615   -327       C  
ATOM   3940  C   THR B  90     -74.573   4.959  26.470  1.00 68.60           C  
ANISOU 3940  C   THR B  90     8183   8880   9003   -675    510   -417       C  
ATOM   3941  O   THR B  90     -74.640   5.102  25.248  1.00 68.60           O  
ANISOU 3941  O   THR B  90     8157   8939   8968   -634    442   -493       O  
ATOM   3942  CB  THR B  90     -74.569   7.346  27.304  1.00 75.01           C  
ANISOU 3942  CB  THR B  90     8851   9881   9769   -502    660   -323       C  
ATOM   3943  OG1 THR B  90     -73.173   7.211  27.586  1.00 75.88           O  
ANISOU 3943  OG1 THR B  90     9091   9898   9842   -439    681   -329       O  
ATOM   3944  CG2 THR B  90     -75.220   8.406  28.184  1.00 72.56           C  
ANISOU 3944  CG2 THR B  90     8435   9674   9460   -445    732   -276       C  
ATOM   3945  N   LEU B  91     -73.883   3.957  27.053  1.00 63.92           N  
ANISOU 3945  N   LEU B  91     7746   8113   8429   -697    483   -419       N  
ATOM   3946  CA  LEU B  91     -73.165   2.941  26.278  1.00 63.53           C  
ANISOU 3946  CA  LEU B  91     7849   7922   8369   -640    362   -542       C  
ATOM   3947  C   LEU B  91     -73.977   2.193  25.194  1.00 67.52           C  
ANISOU 3947  C   LEU B  91     8365   8392   8895   -742    227   -633       C  
ATOM   3948  O   LEU B  91     -73.448   2.081  24.091  1.00 67.19           O  
ANISOU 3948  O   LEU B  91     8357   8380   8793   -621    161   -771       O  
ATOM   3949  CB  LEU B  91     -72.280   2.024  27.136  1.00 63.76           C  
ANISOU 3949  CB  LEU B  91     8063   7747   8415   -601    322   -536       C  
ATOM   3950  CG  LEU B  91     -70.964   2.640  27.636  1.00 66.14           C  
ANISOU 3950  CG  LEU B  91     8369   8107   8655   -418    406   -535       C  
ATOM   3951  CD1 LEU B  91     -70.468   1.929  28.850  1.00 66.73           C  
ANISOU 3951  CD1 LEU B  91     8588   8009   8756   -420    384   -468       C  
ATOM   3952  CD2 LEU B  91     -69.890   2.604  26.569  1.00 67.87           C  
ANISOU 3952  CD2 LEU B  91     8598   8401   8788   -227    360   -694       C  
ATOM   3953  N   PRO B  92     -75.267   1.788  25.390  1.00 64.24           N  
ANISOU 3953  N   PRO B  92     7893   7973   8543   -966    188   -566       N  
ATOM   3954  CA  PRO B  92     -76.019   1.159  24.277  1.00 65.36           C  
ANISOU 3954  CA  PRO B  92     8036   8101   8695  -1074     44   -662       C  
ATOM   3955  C   PRO B  92     -75.976   1.948  22.958  1.00 68.80           C  
ANISOU 3955  C   PRO B  92     8362   8726   9053   -933     38   -764       C  
ATOM   3956  O   PRO B  92     -75.947   1.334  21.895  1.00 69.30           O  
ANISOU 3956  O   PRO B  92     8498   8748   9083   -920    -92   -905       O  
ATOM   3957  CB  PRO B  92     -77.451   1.077  24.813  1.00 68.13           C  
ANISOU 3957  CB  PRO B  92     8239   8549   9098  -1340     56   -538       C  
ATOM   3958  CG  PRO B  92     -77.309   1.030  26.266  1.00 72.30           C  
ANISOU 3958  CG  PRO B  92     8792   9033   9644  -1411    156   -393       C  
ATOM   3959  CD  PRO B  92     -76.081   1.821  26.623  1.00 65.79           C  
ANISOU 3959  CD  PRO B  92     8008   8211   8779  -1150    266   -406       C  
ATOM   3960  N   PHE B  93     -75.934   3.301  23.032  1.00 64.66           N  
ANISOU 3960  N   PHE B  93     7688   8394   8485   -827    160   -694       N  
ATOM   3961  CA  PHE B  93     -75.854   4.198  21.869  1.00 64.66           C  
ANISOU 3961  CA  PHE B  93     7605   8569   8393   -711    148   -740       C  
ATOM   3962  C   PHE B  93     -74.510   4.067  21.156  1.00 68.24           C  
ANISOU 3962  C   PHE B  93     8169   9022   8739   -558    132   -848       C  
ATOM   3963  O   PHE B  93     -74.467   4.141  19.927  1.00 68.41           O  
ANISOU 3963  O   PHE B  93     8171   9160   8660   -516     64   -938       O  
ATOM   3964  CB  PHE B  93     -76.090   5.668  22.277  1.00 65.58           C  
ANISOU 3964  CB  PHE B  93     7592   8828   8499   -640    248   -621       C  
ATOM   3965  CG  PHE B  93     -77.383   5.924  23.020  1.00 68.26           C  
ANISOU 3965  CG  PHE B  93     7777   9247   8914   -731    279   -543       C  
ATOM   3966  CD1 PHE B  93     -78.610   5.805  22.377  1.00 72.97           C  
ANISOU 3966  CD1 PHE B  93     8232   9970   9522   -819    194   -567       C  
ATOM   3967  CD2 PHE B  93     -77.372   6.304  24.355  1.00 69.99           C  
ANISOU 3967  CD2 PHE B  93     7965   9458   9169   -720    392   -458       C  
ATOM   3968  CE1 PHE B  93     -79.801   6.032  23.065  1.00 74.75           C  
ANISOU 3968  CE1 PHE B  93     8264  10345   9794   -894    229   -510       C  
ATOM   3969  CE2 PHE B  93     -78.565   6.547  25.039  1.00 73.75           C  
ANISOU 3969  CE2 PHE B  93     8260  10080   9679   -785    433   -408       C  
ATOM   3970  CZ  PHE B  93     -79.771   6.410  24.389  1.00 73.45           C  
ANISOU 3970  CZ  PHE B  93     8058  10199   9651   -869    354   -435       C  
ATOM   3971  N   TRP B  94     -73.417   3.873  21.932  1.00 63.78           N  
ANISOU 3971  N   TRP B  94     7698   8363   8173   -473    194   -844       N  
ATOM   3972  CA  TRP B  94     -72.052   3.712  21.423  1.00 63.53           C  
ANISOU 3972  CA  TRP B  94     7730   8386   8025   -311    192   -957       C  
ATOM   3973  C   TRP B  94     -71.939   2.435  20.601  1.00 69.16           C  
ANISOU 3973  C   TRP B  94     8555   9014   8709   -263     48  -1157       C  
ATOM   3974  O   TRP B  94     -71.291   2.444  19.552  1.00 69.40           O  
ANISOU 3974  O   TRP B  94     8566   9211   8593   -140     21  -1292       O  
ATOM   3975  CB  TRP B  94     -71.035   3.678  22.580  1.00 61.45           C  
ANISOU 3975  CB  TRP B  94     7526   8041   7783   -234    270   -912       C  
ATOM   3976  CG  TRP B  94     -70.755   5.001  23.234  1.00 60.58           C  
ANISOU 3976  CG  TRP B  94     7330   8035   7654   -238    396   -762       C  
ATOM   3977  CD1 TRP B  94     -71.636   5.781  23.927  1.00 62.93           C  
ANISOU 3977  CD1 TRP B  94     7564   8320   8027   -326    452   -627       C  
ATOM   3978  CD2 TRP B  94     -69.474   5.639  23.352  1.00 59.68           C  
ANISOU 3978  CD2 TRP B  94     7192   8047   7437   -146    465   -747       C  
ATOM   3979  NE1 TRP B  94     -70.995   6.895  24.422  1.00 61.37           N  
ANISOU 3979  NE1 TRP B  94     7340   8191   7786   -284    534   -539       N  
ATOM   3980  CE2 TRP B  94     -69.663   6.827  24.093  1.00 62.59           C  
ANISOU 3980  CE2 TRP B  94     7518   8429   7833   -202    543   -595       C  
ATOM   3981  CE3 TRP B  94     -68.183   5.329  22.892  1.00 61.20           C  
ANISOU 3981  CE3 TRP B  94     7381   8372   7501    -20    460   -858       C  
ATOM   3982  CZ2 TRP B  94     -68.609   7.703  24.383  1.00 61.09           C  
ANISOU 3982  CZ2 TRP B  94     7309   8343   7559   -178    602   -535       C  
ATOM   3983  CZ3 TRP B  94     -67.142   6.201  23.175  1.00 61.97           C  
ANISOU 3983  CZ3 TRP B  94     7413   8630   7502     -3    539   -790       C  
ATOM   3984  CH2 TRP B  94     -67.359   7.371  23.911  1.00 61.37           C  
ANISOU 3984  CH2 TRP B  94     7322   8527   7469   -101    603   -621       C  
ATOM   3985  N   ALA B  95     -72.585   1.345  21.076  1.00 67.32           N  
ANISOU 3985  N   ALA B  95     8445   8532   8601   -371    -55  -1177       N  
ATOM   3986  CA  ALA B  95     -72.593   0.034  20.421  1.00 69.75           C  
ANISOU 3986  CA  ALA B  95     8921   8672   8911   -343   -241  -1373       C  
ATOM   3987  C   ALA B  95     -73.371   0.055  19.095  1.00 75.30           C  
ANISOU 3987  C   ALA B  95     9557   9506   9548   -403   -330  -1473       C  
ATOM   3988  O   ALA B  95     -72.899  -0.515  18.109  1.00 76.65           O  
ANISOU 3988  O   ALA B  95     9803   9706   9613   -265   -437  -1688       O  
ATOM   3989  CB  ALA B  95     -73.157  -1.027  21.357  1.00 71.74           C  
ANISOU 3989  CB  ALA B  95     9346   8598   9315   -511   -348  -1313       C  
ATOM   3990  N   VAL B  96     -74.543   0.724  19.067  1.00 71.14           N  
ANISOU 3990  N   VAL B  96     8878   9087   9067   -585   -293  -1332       N  
ATOM   3991  CA  VAL B  96     -75.372   0.846  17.865  1.00 72.22           C  
ANISOU 3991  CA  VAL B  96     8929   9373   9139   -650   -383  -1401       C  
ATOM   3992  C   VAL B  96     -74.641   1.707  16.817  1.00 76.39           C  
ANISOU 3992  C   VAL B  96     9370  10179   9475   -477   -327  -1456       C  
ATOM   3993  O   VAL B  96     -74.547   1.306  15.656  1.00 77.56           O  
ANISOU 3993  O   VAL B  96     9549  10420   9499   -417   -432  -1630       O  
ATOM   3994  CB  VAL B  96     -76.810   1.351  18.177  1.00 75.73           C  
ANISOU 3994  CB  VAL B  96     9205   9894   9676   -860   -367  -1240       C  
ATOM   3995  CG1 VAL B  96     -77.604   1.600  16.897  1.00 76.55           C  
ANISOU 3995  CG1 VAL B  96     9201  10188   9697   -898   -468  -1306       C  
ATOM   3996  CG2 VAL B  96     -77.553   0.369  19.076  1.00 76.77           C  
ANISOU 3996  CG2 VAL B  96     9407   9808   9953  -1090   -436  -1186       C  
ATOM   3997  N   ASP B  97     -74.073   2.851  17.248  1.00 71.49           N  
ANISOU 3997  N   ASP B  97     8658   9691   8815   -411   -174  -1310       N  
ATOM   3998  CA  ASP B  97     -73.308   3.764  16.393  1.00 71.13           C  
ANISOU 3998  CA  ASP B  97     8539   9914   8574   -307   -116  -1303       C  
ATOM   3999  C   ASP B  97     -72.092   3.064  15.759  1.00 77.22           C  
ANISOU 3999  C   ASP B  97     9376  10780   9186   -139   -140  -1514       C  
ATOM   4000  O   ASP B  97     -71.670   3.450  14.670  1.00 78.14           O  
ANISOU 4000  O   ASP B  97     9426  11171   9094    -83   -139  -1570       O  
ATOM   4001  CB  ASP B  97     -72.898   5.019  17.190  1.00 70.72           C  
ANISOU 4001  CB  ASP B  97     8422   9914   8536   -305     24  -1098       C  
ATOM   4002  CG  ASP B  97     -71.749   5.811  16.606  1.00 79.11           C  
ANISOU 4002  CG  ASP B  97     9444  11218   9396   -235     90  -1070       C  
ATOM   4003  OD1 ASP B  97     -70.586   5.517  16.965  1.00 79.93           O  
ANISOU 4003  OD1 ASP B  97     9571  11352   9446   -143    152  -1132       O  
ATOM   4004  OD2 ASP B  97     -72.011   6.715  15.777  1.00 82.20           O  
ANISOU 4004  OD2 ASP B  97     9777  11784   9669   -283     67   -978       O  
ATOM   4005  N   ALA B  98     -71.539   2.043  16.441  1.00 74.37           N  
ANISOU 4005  N   ALA B  98     9141  10211   8906    -48   -169  -1630       N  
ATOM   4006  CA  ALA B  98     -70.397   1.280  15.951  1.00 75.81           C  
ANISOU 4006  CA  ALA B  98     9384  10474   8948    172   -213  -1870       C  
ATOM   4007  C   ALA B  98     -70.829   0.283  14.855  1.00 83.06           C  
ANISOU 4007  C   ALA B  98    10396  11361   9801    220   -394  -2121       C  
ATOM   4008  O   ALA B  98     -70.433   0.461  13.700  1.00 83.89           O  
ANISOU 4008  O   ALA B  98    10421  11772   9681    318   -398  -2254       O  
ATOM   4009  CB  ALA B  98     -69.700   0.571  17.105  1.00 76.33           C  
ANISOU 4009  CB  ALA B  98     9573  10298   9131    281   -216  -1901       C  
ATOM   4010  N   VAL B  99     -71.677  -0.724  15.204  1.00 80.80           N  
ANISOU 4010  N   VAL B  99    10279  10724   9696    119   -550  -2173       N  
ATOM   4011  CA  VAL B  99     -72.165  -1.769  14.285  1.00 83.11           C  
ANISOU 4011  CA  VAL B  99    10709  10909   9958    133   -764  -2418       C  
ATOM   4012  C   VAL B  99     -72.993  -1.249  13.118  1.00 87.52           C  
ANISOU 4012  C   VAL B  99    11140  11713  10399     18   -793  -2417       C  
ATOM   4013  O   VAL B  99     -72.873  -1.765  12.005  1.00 90.20           O  
ANISOU 4013  O   VAL B  99    11526  12165  10580    129   -914  -2665       O  
ATOM   4014  CB  VAL B  99     -72.872  -2.974  14.970  1.00 88.12           C  
ANISOU 4014  CB  VAL B  99    11584  11084  10812     -8   -954  -2444       C  
ATOM   4015  CG1 VAL B  99     -71.891  -3.825  15.751  1.00 88.76           C  
ANISOU 4015  CG1 VAL B  99    11870  10901  10954    189  -1018  -2547       C  
ATOM   4016  CG2 VAL B  99     -74.050  -2.546  15.845  1.00 86.28           C  
ANISOU 4016  CG2 VAL B  99    11273  10746  10765   -330   -895  -2150       C  
ATOM   4017  N   ALA B 100     -73.867  -0.271  13.388  1.00 81.03           N  
ANISOU 4017  N   ALA B 100    10167  10970   9652   -185   -702  -2157       N  
ATOM   4018  CA  ALA B 100     -74.780   0.294  12.407  1.00 80.66           C  
ANISOU 4018  CA  ALA B 100     9994  11135   9516   -299   -747  -2117       C  
ATOM   4019  C   ALA B 100     -74.750   1.818  12.454  1.00 81.31           C  
ANISOU 4019  C   ALA B 100     9894  11467   9535   -323   -585  -1869       C  
ATOM   4020  O   ALA B 100     -73.812   2.400  12.995  1.00 79.82           O  
ANISOU 4020  O   ALA B 100     9678  11337   9314   -237   -441  -1775       O  
ATOM   4021  CB  ALA B 100     -76.187  -0.224  12.674  1.00 82.13           C  
ANISOU 4021  CB  ALA B 100    10204  11115   9887   -538   -879  -2072       C  
ATOM   4022  N   ASN B 101     -75.773   2.454  11.885  1.00 76.51           N  
ANISOU 4022  N   ASN B 101     9175  10991   8905   -439   -634  -1766       N  
ATOM   4023  CA  ASN B 101     -75.970   3.895  11.799  1.00 74.68           C  
ANISOU 4023  CA  ASN B 101     8809  10947   8617   -462   -550  -1535       C  
ATOM   4024  C   ASN B 101     -76.273   4.546  13.181  1.00 77.41           C  
ANISOU 4024  C   ASN B 101     9108  11138   9166   -513   -439  -1323       C  
ATOM   4025  O   ASN B 101     -76.512   3.834  14.165  1.00 77.38           O  
ANISOU 4025  O   ASN B 101     9149  10911   9339   -571   -428  -1339       O  
ATOM   4026  CB  ASN B 101     -77.161   4.113  10.860  1.00 73.95           C  
ANISOU 4026  CB  ASN B 101     8632  10987   8476   -550   -689  -1527       C  
ATOM   4027  CG  ASN B 101     -77.193   5.401  10.098  1.00 87.24           C  
ANISOU 4027  CG  ASN B 101    10236  12922   9990   -526   -687  -1368       C  
ATOM   4028  OD1 ASN B 101     -76.672   6.432  10.520  1.00 76.99           O  
ANISOU 4028  OD1 ASN B 101     8926  11652   8673   -494   -582  -1184       O  
ATOM   4029  ND2 ASN B 101     -77.845   5.369   8.957  1.00 82.06           N  
ANISOU 4029  ND2 ASN B 101     9541  12436   9203   -557   -827  -1426       N  
ATOM   4030  N   TRP B 102     -76.278   5.904  13.237  1.00 72.24           N  
ANISOU 4030  N   TRP B 102     8380  10600   8470   -495   -377  -1125       N  
ATOM   4031  CA  TRP B 102     -76.672   6.688  14.411  1.00 70.17           C  
ANISOU 4031  CA  TRP B 102     8067  10226   8368   -509   -297   -948       C  
ATOM   4032  C   TRP B 102     -78.098   7.202  14.124  1.00 73.18           C  
ANISOU 4032  C   TRP B 102     8325  10680   8801   -550   -400   -879       C  
ATOM   4033  O   TRP B 102     -78.276   8.115  13.315  1.00 73.01           O  
ANISOU 4033  O   TRP B 102     8278  10802   8661   -509   -469   -796       O  
ATOM   4034  CB  TRP B 102     -75.692   7.845  14.690  1.00 68.09           C  
ANISOU 4034  CB  TRP B 102     7838  10007   8025   -446   -197   -799       C  
ATOM   4035  CG  TRP B 102     -76.198   8.834  15.705  1.00 68.43           C  
ANISOU 4035  CG  TRP B 102     7845   9949   8204   -430   -156   -637       C  
ATOM   4036  CD1 TRP B 102     -76.966   9.934  15.463  1.00 71.81           C  
ANISOU 4036  CD1 TRP B 102     8230  10425   8629   -396   -236   -516       C  
ATOM   4037  CD2 TRP B 102     -75.998   8.790  17.124  1.00 67.38           C  
ANISOU 4037  CD2 TRP B 102     7726   9657   8218   -419    -45   -602       C  
ATOM   4038  NE1 TRP B 102     -77.262  10.575  16.641  1.00 70.46           N  
ANISOU 4038  NE1 TRP B 102     8041  10135   8594   -343   -181   -432       N  
ATOM   4039  CE2 TRP B 102     -76.673   9.900  17.677  1.00 71.00           C  
ANISOU 4039  CE2 TRP B 102     8137  10090   8748   -369    -54   -478       C  
ATOM   4040  CE3 TRP B 102     -75.267   7.948  17.982  1.00 68.22           C  
ANISOU 4040  CE3 TRP B 102     7891   9641   8388   -427     49   -665       C  
ATOM   4041  CZ2 TRP B 102     -76.664  10.174  19.050  1.00 69.61           C  
ANISOU 4041  CZ2 TRP B 102     7957   9798   8692   -337     42   -431       C  
ATOM   4042  CZ3 TRP B 102     -75.256   8.222  19.344  1.00 68.78           C  
ANISOU 4042  CZ3 TRP B 102     7963   9592   8579   -418    142   -589       C  
ATOM   4043  CH2 TRP B 102     -75.949   9.324  19.865  1.00 69.16           C  
ANISOU 4043  CH2 TRP B 102     7950   9644   8683   -378    147   -479       C  
ATOM   4044  N   TYR B 103     -79.098   6.608  14.795  1.00 69.22           N  
ANISOU 4044  N   TYR B 103     7739  10098   8462   -638   -419   -905       N  
ATOM   4045  CA  TYR B 103     -80.523   6.900  14.623  1.00 70.15           C  
ANISOU 4045  CA  TYR B 103     7687  10333   8633   -680   -516   -872       C  
ATOM   4046  C   TYR B 103     -81.151   7.844  15.661  1.00 73.15           C  
ANISOU 4046  C   TYR B 103     7942  10729   9124   -612   -452   -742       C  
ATOM   4047  O   TYR B 103     -82.243   8.368  15.439  1.00 74.91           O  
ANISOU 4047  O   TYR B 103     8004  11100   9360   -574   -539   -714       O  
ATOM   4048  CB  TYR B 103     -81.308   5.587  14.662  1.00 73.16           C  
ANISOU 4048  CB  TYR B 103     8020  10678   9098   -863   -593   -989       C  
ATOM   4049  CG  TYR B 103     -80.761   4.463  13.810  1.00 76.15           C  
ANISOU 4049  CG  TYR B 103     8552  10986   9395   -918   -682  -1164       C  
ATOM   4050  CD1 TYR B 103     -80.019   3.429  14.379  1.00 77.49           C  
ANISOU 4050  CD1 TYR B 103     8885  10933   9623   -958   -646  -1251       C  
ATOM   4051  CD2 TYR B 103     -81.078   4.370  12.457  1.00 78.73           C  
ANISOU 4051  CD2 TYR B 103     8866  11466   9584   -919   -828  -1261       C  
ATOM   4052  CE1 TYR B 103     -79.579   2.350  13.615  1.00 79.14           C  
ANISOU 4052  CE1 TYR B 103     9251  11058   9760   -967   -761  -1451       C  
ATOM   4053  CE2 TYR B 103     -80.642   3.296  11.683  1.00 80.97           C  
ANISOU 4053  CE2 TYR B 103     9292  11694   9781   -947   -927  -1463       C  
ATOM   4054  CZ  TYR B 103     -79.897   2.285  12.269  1.00 87.65           C  
ANISOU 4054  CZ  TYR B 103    10309  12301  10695   -958   -898  -1568       C  
ATOM   4055  OH  TYR B 103     -79.462   1.231  11.505  1.00 90.91           O  
ANISOU 4055  OH  TYR B 103    10883  12640  11019   -937  -1023  -1801       O  
ATOM   4056  N   PHE B 104     -80.485   8.025  16.790  1.00 67.06           N  
ANISOU 4056  N   PHE B 104     7235   9825   8421   -577   -311   -686       N  
ATOM   4057  CA  PHE B 104     -80.927   8.771  17.970  1.00 66.19           C  
ANISOU 4057  CA  PHE B 104     7028   9715   8407   -502   -230   -601       C  
ATOM   4058  C   PHE B 104     -81.169  10.290  17.878  1.00 69.72           C  
ANISOU 4058  C   PHE B 104     7452  10216   8822   -306   -281   -511       C  
ATOM   4059  O   PHE B 104     -81.638  10.889  18.851  1.00 69.50           O  
ANISOU 4059  O   PHE B 104     7337  10204   8868   -206   -233   -481       O  
ATOM   4060  CB  PHE B 104     -80.084   8.359  19.192  1.00 66.50           C  
ANISOU 4060  CB  PHE B 104     7165   9589   8512   -539    -79   -583       C  
ATOM   4061  CG  PHE B 104     -79.741   6.883  19.170  1.00 67.81           C  
ANISOU 4061  CG  PHE B 104     7418   9646   8702   -701    -79   -670       C  
ATOM   4062  CD1 PHE B 104     -78.459   6.456  18.844  1.00 69.12           C  
ANISOU 4062  CD1 PHE B 104     7765   9695   8803   -669    -62   -724       C  
ATOM   4063  CD2 PHE B 104     -80.723   5.919  19.396  1.00 70.51           C  
ANISOU 4063  CD2 PHE B 104     7661  10013   9116   -885   -124   -705       C  
ATOM   4064  CE1 PHE B 104     -78.154   5.093  18.792  1.00 70.26           C  
ANISOU 4064  CE1 PHE B 104     8019   9707   8970   -767   -103   -832       C  
ATOM   4065  CE2 PHE B 104     -80.417   4.558  19.334  1.00 73.42           C  
ANISOU 4065  CE2 PHE B 104     8167  10220   9510  -1038   -174   -784       C  
ATOM   4066  CZ  PHE B 104     -79.135   4.156  19.042  1.00 70.52           C  
ANISOU 4066  CZ  PHE B 104     8007   9696   9092   -953   -171   -857       C  
ATOM   4067  N   GLY B 105     -80.891  10.895  16.729  1.00 66.66           N  
ANISOU 4067  N   GLY B 105     7151   9860   8315   -248   -395   -472       N  
ATOM   4068  CA  GLY B 105     -81.148  12.318  16.525  1.00 67.61           C  
ANISOU 4068  CA  GLY B 105     7303   9986   8400    -72   -500   -371       C  
ATOM   4069  C   GLY B 105     -80.122  13.289  17.067  1.00 71.60           C  
ANISOU 4069  C   GLY B 105     7996  10320   8889      0   -452   -265       C  
ATOM   4070  O   GLY B 105     -79.089  12.879  17.601  1.00 69.70           O  
ANISOU 4070  O   GLY B 105     7846   9987   8652    -85   -317   -268       O  
ATOM   4071  N   ASN B 106     -80.407  14.597  16.921  1.00 70.21           N  
ANISOU 4071  N   ASN B 106     7893  10092   8691    159   -589   -173       N  
ATOM   4072  CA  ASN B 106     -79.500  15.681  17.309  1.00 69.99           C  
ANISOU 4072  CA  ASN B 106     8083   9873   8637    205   -603    -54       C  
ATOM   4073  C   ASN B 106     -79.331  15.965  18.799  1.00 73.94           C  
ANISOU 4073  C   ASN B 106     8594  10246   9255    290   -490    -87       C  
ATOM   4074  O   ASN B 106     -78.198  16.198  19.225  1.00 72.14           O  
ANISOU 4074  O   ASN B 106     8520   9888   9001    212   -416    -26       O  
ATOM   4075  CB  ASN B 106     -79.779  16.955  16.523  1.00 72.63           C  
ANISOU 4075  CB  ASN B 106     8561  10143   8893    320   -837     72       C  
ATOM   4076  CG  ASN B 106     -78.548  17.510  15.860  1.00 93.10           C  
ANISOU 4076  CG  ASN B 106    11392  12652  11330    164   -882    240       C  
ATOM   4077  OD1 ASN B 106     -78.162  17.094  14.762  1.00 86.31           O  
ANISOU 4077  OD1 ASN B 106    10539  11938  10317     15   -896    281       O  
ATOM   4078  ND2 ASN B 106     -77.893  18.451  16.521  1.00 85.39           N  
ANISOU 4078  ND2 ASN B 106    10608  11466  10372    179   -908    336       N  
ATOM   4079  N   PHE B 107     -80.437  15.970  19.584  1.00 72.30           N  
ANISOU 4079  N   PHE B 107     8206  10112   9154    446   -477   -187       N  
ATOM   4080  CA  PHE B 107     -80.381  16.230  21.032  1.00 71.87           C  
ANISOU 4080  CA  PHE B 107     8138   9986   9184    544   -367   -238       C  
ATOM   4081  C   PHE B 107     -79.577  15.169  21.775  1.00 75.20           C  
ANISOU 4081  C   PHE B 107     8547  10397   9630    354   -155   -260       C  
ATOM   4082  O   PHE B 107     -78.729  15.514  22.603  1.00 73.33           O  
ANISOU 4082  O   PHE B 107     8440  10020   9402    354    -81   -233       O  
ATOM   4083  CB  PHE B 107     -81.781  16.394  21.654  1.00 75.31           C  
ANISOU 4083  CB  PHE B 107     8333  10597   9686    751   -387   -356       C  
ATOM   4084  CG  PHE B 107     -81.739  16.735  23.127  1.00 76.88           C  
ANISOU 4084  CG  PHE B 107     8513  10763   9934    874   -277   -424       C  
ATOM   4085  CD1 PHE B 107     -81.912  15.748  24.094  1.00 79.43           C  
ANISOU 4085  CD1 PHE B 107     8653  11237  10288    753    -76   -483       C  
ATOM   4086  CD2 PHE B 107     -81.473  18.034  23.551  1.00 79.89           C  
ANISOU 4086  CD2 PHE B 107     9091  10947  10318   1093   -389   -421       C  
ATOM   4087  CE1 PHE B 107     -81.839  16.058  25.460  1.00 80.20           C  
ANISOU 4087  CE1 PHE B 107     8736  11338  10401    858     31   -543       C  
ATOM   4088  CE2 PHE B 107     -81.405  18.343  24.916  1.00 82.72           C  
ANISOU 4088  CE2 PHE B 107     9441  11285  10703   1216   -293   -508       C  
ATOM   4089  CZ  PHE B 107     -81.594  17.354  25.861  1.00 79.83           C  
ANISOU 4089  CZ  PHE B 107     8864  11119  10350   1102    -73   -569       C  
ATOM   4090  N   LEU B 108     -79.843  13.885  21.470  1.00 72.96           N  
ANISOU 4090  N   LEU B 108     8125  10242   9355    193    -83   -310       N  
ATOM   4091  CA  LEU B 108     -79.143  12.754  22.066  1.00 71.79           C  
ANISOU 4091  CA  LEU B 108     7990  10057   9231     23     75   -332       C  
ATOM   4092  C   LEU B 108     -77.668  12.697  21.674  1.00 75.78           C  
ANISOU 4092  C   LEU B 108     8692  10439   9662    -61    100   -280       C  
ATOM   4093  O   LEU B 108     -76.891  12.103  22.408  1.00 74.48           O  
ANISOU 4093  O   LEU B 108     8575  10207   9516   -131    217   -291       O  
ATOM   4094  CB  LEU B 108     -79.867  11.436  21.781  1.00 72.48           C  
ANISOU 4094  CB  LEU B 108     7923  10271   9347   -130     91   -400       C  
ATOM   4095  CG  LEU B 108     -80.635  10.851  22.970  1.00 77.99           C  
ANISOU 4095  CG  LEU B 108     8450  11066  10117   -189    196   -432       C  
ATOM   4096  CD1 LEU B 108     -81.928  11.621  23.254  1.00 79.89           C  
ANISOU 4096  CD1 LEU B 108     8472  11511  10371    -32    152   -465       C  
ATOM   4097  CD2 LEU B 108     -80.981   9.418  22.722  1.00 81.96           C  
ANISOU 4097  CD2 LEU B 108     8889  11609  10643   -419    198   -466       C  
ATOM   4098  N   CYS B 109     -77.270  13.354  20.559  1.00 73.82           N  
ANISOU 4098  N   CYS B 109     8548  10188   9312    -55    -13   -214       N  
ATOM   4099  CA  CYS B 109     -75.866  13.431  20.148  1.00 73.34           C  
ANISOU 4099  CA  CYS B 109     8633  10091   9142   -147     14   -155       C  
ATOM   4100  C   CYS B 109     -75.139  14.393  21.071  1.00 75.79           C  
ANISOU 4100  C   CYS B 109     9070  10263   9466   -111     43    -77       C  
ATOM   4101  O   CYS B 109     -73.998  14.128  21.455  1.00 75.07           O  
ANISOU 4101  O   CYS B 109     9036  10149   9337   -190    136    -66       O  
ATOM   4102  CB  CYS B 109     -75.726  13.852  18.690  1.00 75.24           C  
ANISOU 4102  CB  CYS B 109     8930  10423   9235   -190   -113    -88       C  
ATOM   4103  SG  CYS B 109     -74.015  13.879  18.101  1.00 79.12           S  
ANISOU 4103  SG  CYS B 109     9534  10989   9538   -334    -63    -19       S  
ATOM   4104  N   LYS B 110     -75.814  15.504  21.431  1.00 71.45           N  
ANISOU 4104  N   LYS B 110     8562   9623   8965     25    -57    -40       N  
ATOM   4105  CA  LYS B 110     -75.300  16.503  22.354  1.00 70.47           C  
ANISOU 4105  CA  LYS B 110     8580   9332   8862     81    -69      9       C  
ATOM   4106  C   LYS B 110     -75.278  15.886  23.757  1.00 73.68           C  
ANISOU 4106  C   LYS B 110     8901   9735   9359    110     95    -83       C  
ATOM   4107  O   LYS B 110     -74.235  15.906  24.411  1.00 72.28           O  
ANISOU 4107  O   LYS B 110     8811   9489   9164     41    171    -58       O  
ATOM   4108  CB  LYS B 110     -76.172  17.765  22.333  1.00 73.74           C  
ANISOU 4108  CB  LYS B 110     9072   9636   9308    273   -254     30       C  
ATOM   4109  CG  LYS B 110     -76.087  18.554  21.043  1.00 79.24           C  
ANISOU 4109  CG  LYS B 110     9919  10288   9903    233   -453    165       C  
ATOM   4110  CD  LYS B 110     -77.114  19.673  21.011  1.00 86.93           C  
ANISOU 4110  CD  LYS B 110    10970  11138  10923    476   -670    163       C  
ATOM   4111  CE  LYS B 110     -77.255  20.296  19.647  1.00100.23           C  
ANISOU 4111  CE  LYS B 110    12786  12794  12501    443   -889    304       C  
ATOM   4112  NZ  LYS B 110     -76.009  20.984  19.211  1.00111.08           N  
ANISOU 4112  NZ  LYS B 110    14422  14033  13751    217   -967    501       N  
ATOM   4113  N   ALA B 111     -76.411  15.271  24.177  1.00 70.97           N  
ANISOU 4113  N   ALA B 111     8373   9500   9092    184    148   -179       N  
ATOM   4114  CA  ALA B 111     -76.570  14.633  25.488  1.00 70.38           C  
ANISOU 4114  CA  ALA B 111     8200   9464   9077    185    298   -245       C  
ATOM   4115  C   ALA B 111     -75.548  13.523  25.773  1.00 72.74           C  
ANISOU 4115  C   ALA B 111     8532   9742   9365     20    422   -235       C  
ATOM   4116  O   ALA B 111     -75.046  13.449  26.894  1.00 71.41           O  
ANISOU 4116  O   ALA B 111     8400   9525   9209     18    515   -238       O  
ATOM   4117  CB  ALA B 111     -77.993  14.128  25.675  1.00 72.32           C  
ANISOU 4117  CB  ALA B 111     8216   9890   9371    231    320   -322       C  
ATOM   4118  N   VAL B 112     -75.218  12.688  24.766  1.00 69.34           N  
ANISOU 4118  N   VAL B 112     8099   9349   8898    -92    408   -236       N  
ATOM   4119  CA  VAL B 112     -74.228  11.612  24.910  1.00 68.59           C  
ANISOU 4119  CA  VAL B 112     8047   9228   8785   -195    488   -256       C  
ATOM   4120  C   VAL B 112     -72.804  12.203  25.036  1.00 72.38           C  
ANISOU 4120  C   VAL B 112     8654   9657   9190   -204    505   -203       C  
ATOM   4121  O   VAL B 112     -71.992  11.708  25.831  1.00 70.37           O  
ANISOU 4121  O   VAL B 112     8432   9366   8938   -225    585   -214       O  
ATOM   4122  CB  VAL B 112     -74.405  10.507  23.826  1.00 72.94           C  
ANISOU 4122  CB  VAL B 112     8559   9839   9315   -273    447   -318       C  
ATOM   4123  CG1 VAL B 112     -73.135   9.685  23.606  1.00 72.35           C  
ANISOU 4123  CG1 VAL B 112     8565   9744   9181   -309    478   -362       C  
ATOM   4124  CG2 VAL B 112     -75.574   9.593  24.181  1.00 73.43           C  
ANISOU 4124  CG2 VAL B 112     8508   9926   9464   -335    456   -363       C  
ATOM   4125  N   HIS B 113     -72.544  13.310  24.310  1.00 70.46           N  
ANISOU 4125  N   HIS B 113     8481   9416   8873   -201    414   -131       N  
ATOM   4126  CA  HIS B 113     -71.273  14.027  24.372  1.00 70.62           C  
ANISOU 4126  CA  HIS B 113     8611   9415   8805   -262    408    -53       C  
ATOM   4127  C   HIS B 113     -71.105  14.715  25.738  1.00 75.67           C  
ANISOU 4127  C   HIS B 113     9322   9927   9502   -212    435    -37       C  
ATOM   4128  O   HIS B 113     -70.021  14.654  26.323  1.00 74.29           O  
ANISOU 4128  O   HIS B 113     9187   9751   9290   -269    491    -22       O  
ATOM   4129  CB  HIS B 113     -71.156  15.034  23.217  1.00 72.49           C  
ANISOU 4129  CB  HIS B 113     8929   9679   8936   -322    277     53       C  
ATOM   4130  CG  HIS B 113     -70.570  14.439  21.974  1.00 76.36           C  
ANISOU 4130  CG  HIS B 113     9367  10358   9288   -419    281     51       C  
ATOM   4131  ND1 HIS B 113     -71.370  13.851  21.007  1.00 78.70           N  
ANISOU 4131  ND1 HIS B 113     9588  10741   9571   -392    239     -7       N  
ATOM   4132  CD2 HIS B 113     -69.276  14.339  21.588  1.00 78.33           C  
ANISOU 4132  CD2 HIS B 113     9612  10760   9392   -530    321     81       C  
ATOM   4133  CE1 HIS B 113     -70.542  13.425  20.068  1.00 78.55           C  
ANISOU 4133  CE1 HIS B 113     9539  10910   9396   -473    255    -21       C  
ATOM   4134  NE2 HIS B 113     -69.274  13.705  20.366  1.00 78.81           N  
ANISOU 4134  NE2 HIS B 113     9597  11010   9337   -553    310     31       N  
ATOM   4135  N   VAL B 114     -72.195  15.316  26.264  1.00 74.42           N  
ANISOU 4135  N   VAL B 114     9162   9692   9422    -87    392    -63       N  
ATOM   4136  CA  VAL B 114     -72.179  16.000  27.560  1.00 74.97           C  
ANISOU 4136  CA  VAL B 114     9298   9658   9530     -2    405    -84       C  
ATOM   4137  C   VAL B 114     -71.946  15.083  28.752  1.00 78.88           C  
ANISOU 4137  C   VAL B 114     9722  10193  10055    -11    555   -139       C  
ATOM   4138  O   VAL B 114     -71.191  15.442  29.657  1.00 78.48           O  
ANISOU 4138  O   VAL B 114     9754  10082   9984    -18    582   -132       O  
ATOM   4139  CB  VAL B 114     -73.299  17.054  27.802  1.00 80.50           C  
ANISOU 4139  CB  VAL B 114    10026  10282  10276    185    295   -125       C  
ATOM   4140  CG1 VAL B 114     -73.339  18.097  26.692  1.00 81.72           C  
ANISOU 4140  CG1 VAL B 114    10321  10335  10392    189    102    -40       C  
ATOM   4141  CG2 VAL B 114     -74.664  16.421  28.013  1.00 80.73           C  
ANISOU 4141  CG2 VAL B 114     9852  10455  10365    295    354   -219       C  
ATOM   4142  N   ILE B 115     -72.584  13.896  28.743  1.00 75.15           N  
ANISOU 4142  N   ILE B 115     9115   9816   9624    -30    634   -182       N  
ATOM   4143  CA  ILE B 115     -72.465  12.907  29.814  1.00 74.09           C  
ANISOU 4143  CA  ILE B 115     8935   9706   9509    -67    752   -204       C  
ATOM   4144  C   ILE B 115     -71.029  12.379  29.897  1.00 76.66           C  
ANISOU 4144  C   ILE B 115     9339   9997   9790   -143    782   -178       C  
ATOM   4145  O   ILE B 115     -70.494  12.264  30.997  1.00 75.76           O  
ANISOU 4145  O   ILE B 115     9263   9858   9664   -140    840   -173       O  
ATOM   4146  CB  ILE B 115     -73.569  11.816  29.698  1.00 77.63           C  
ANISOU 4146  CB  ILE B 115     9246  10245  10006   -116    789   -231       C  
ATOM   4147  CG1 ILE B 115     -74.948  12.406  30.102  1.00 79.13           C  
ANISOU 4147  CG1 ILE B 115     9305  10544  10216    -19    790   -271       C  
ATOM   4148  CG2 ILE B 115     -73.241  10.597  30.557  1.00 78.32           C  
ANISOU 4148  CG2 ILE B 115     9343  10315  10101   -211    872   -215       C  
ATOM   4149  CD1 ILE B 115     -76.177  11.748  29.502  1.00 85.50           C  
ANISOU 4149  CD1 ILE B 115     9945  11486  11056    -74    773   -292       C  
ATOM   4150  N   TYR B 116     -70.393  12.135  28.737  1.00 73.27           N  
ANISOU 4150  N   TYR B 116     8923   9600   9316   -194    737   -172       N  
ATOM   4151  CA  TYR B 116     -69.007  11.669  28.628  1.00 72.87           C  
ANISOU 4151  CA  TYR B 116     8903   9587   9197   -232    756   -174       C  
ATOM   4152  C   TYR B 116     -68.027  12.723  29.185  1.00 76.55           C  
ANISOU 4152  C   TYR B 116     9439  10043   9602   -257    747   -119       C  
ATOM   4153  O   TYR B 116     -67.132  12.380  29.960  1.00 75.32           O  
ANISOU 4153  O   TYR B 116     9295   9902   9421   -258    790   -127       O  
ATOM   4154  CB  TYR B 116     -68.692  11.321  27.160  1.00 74.68           C  
ANISOU 4154  CB  TYR B 116     9098   9920   9357   -263    709   -199       C  
ATOM   4155  CG  TYR B 116     -67.322  10.730  26.899  1.00 76.52           C  
ANISOU 4155  CG  TYR B 116     9315  10266   9494   -263    728   -241       C  
ATOM   4156  CD1 TYR B 116     -66.847   9.660  27.651  1.00 78.36           C  
ANISOU 4156  CD1 TYR B 116     9558  10457   9758   -199    762   -303       C  
ATOM   4157  CD2 TYR B 116     -66.550  11.164  25.828  1.00 77.97           C  
ANISOU 4157  CD2 TYR B 116     9461  10625   9539   -317    699   -225       C  
ATOM   4158  CE1 TYR B 116     -65.601   9.092  27.396  1.00 79.96           C  
ANISOU 4158  CE1 TYR B 116     9727  10787   9866   -144    762   -371       C  
ATOM   4159  CE2 TYR B 116     -65.307  10.594  25.552  1.00 79.69           C  
ANISOU 4159  CE2 TYR B 116     9612  11023   9642   -290    722   -291       C  
ATOM   4160  CZ  TYR B 116     -64.836   9.555  26.338  1.00 88.65           C  
ANISOU 4160  CZ  TYR B 116    10749  12111  10821   -179    750   -379       C  
ATOM   4161  OH  TYR B 116     -63.605   8.993  26.076  1.00 91.41           O  
ANISOU 4161  OH  TYR B 116    11019  12660  11052   -100    757   -471       O  
ATOM   4162  N   THR B 117     -68.238  14.007  28.820  1.00 73.81           N  
ANISOU 4162  N   THR B 117     9154   9655   9234   -281    667    -63       N  
ATOM   4163  CA  THR B 117     -67.464  15.167  29.273  1.00 73.57           C  
ANISOU 4163  CA  THR B 117     9231   9570   9152   -340    612     -1       C  
ATOM   4164  C   THR B 117     -67.558  15.254  30.807  1.00 76.63           C  
ANISOU 4164  C   THR B 117     9655   9873   9587   -265    661    -45       C  
ATOM   4165  O   THR B 117     -66.529  15.196  31.482  1.00 76.26           O  
ANISOU 4165  O   THR B 117     9627   9855   9493   -314    688    -37       O  
ATOM   4166  CB  THR B 117     -67.988  16.423  28.546  1.00 81.30           C  
ANISOU 4166  CB  THR B 117    10315  10455  10121   -361    474     67       C  
ATOM   4167  OG1 THR B 117     -67.671  16.320  27.160  1.00 80.99           O  
ANISOU 4167  OG1 THR B 117    10241  10537   9992   -468    435    129       O  
ATOM   4168  CG2 THR B 117     -67.437  17.722  29.111  1.00 80.88           C  
ANISOU 4168  CG2 THR B 117    10430  10263  10037   -422    370    126       C  
ATOM   4169  N   VAL B 118     -68.800  15.332  31.342  1.00 72.54           N  
ANISOU 4169  N   VAL B 118     9121   9298   9143   -143    676    -99       N  
ATOM   4170  CA  VAL B 118     -69.105  15.382  32.773  1.00 72.11           C  
ANISOU 4170  CA  VAL B 118     9074   9219   9105    -58    735   -155       C  
ATOM   4171  C   VAL B 118     -68.388  14.241  33.499  1.00 75.02           C  
ANISOU 4171  C   VAL B 118     9398   9654   9451   -105    837   -149       C  
ATOM   4172  O   VAL B 118     -67.667  14.515  34.451  1.00 74.75           O  
ANISOU 4172  O   VAL B 118     9424   9605   9374   -111    846   -151       O  
ATOM   4173  CB  VAL B 118     -70.639  15.409  33.038  1.00 76.66           C  
ANISOU 4173  CB  VAL B 118     9564   9829   9732     75    758   -222       C  
ATOM   4174  CG1 VAL B 118     -70.979  15.032  34.482  1.00 76.58           C  
ANISOU 4174  CG1 VAL B 118     9501   9893   9701    130    865   -272       C  
ATOM   4175  CG2 VAL B 118     -71.231  16.770  32.683  1.00 77.69           C  
ANISOU 4175  CG2 VAL B 118     9781   9863   9876    193    622   -254       C  
ATOM   4176  N   ASN B 119     -68.529  12.985  33.003  1.00 70.89           N  
ANISOU 4176  N   ASN B 119     8794   9185   8955   -136    884   -145       N  
ATOM   4177  CA  ASN B 119     -67.880  11.801  33.575  1.00 70.02           C  
ANISOU 4177  CA  ASN B 119     8679   9096   8832   -158    937   -138       C  
ATOM   4178  C   ASN B 119     -66.353  11.910  33.570  1.00 73.69           C  
ANISOU 4178  C   ASN B 119     9176   9598   9226   -184    910   -127       C  
ATOM   4179  O   ASN B 119     -65.738  11.651  34.604  1.00 73.53           O  
ANISOU 4179  O   ASN B 119     9184   9581   9172   -169    934   -121       O  
ATOM   4180  CB  ASN B 119     -68.344  10.504  32.900  1.00 69.18           C  
ANISOU 4180  CB  ASN B 119     8524   8988   8771   -181    941   -150       C  
ATOM   4181  CG  ASN B 119     -67.693   9.258  33.469  1.00 89.23           C  
ANISOU 4181  CG  ASN B 119    11108  11492  11305   -180    949   -144       C  
ATOM   4182  OD1 ASN B 119     -66.724   8.727  32.919  1.00 83.66           O  
ANISOU 4182  OD1 ASN B 119    10415  10801  10571   -145    907   -180       O  
ATOM   4183  ND2 ASN B 119     -68.172   8.791  34.610  1.00 80.14           N  
ANISOU 4183  ND2 ASN B 119     9981  10310  10161   -206    992   -101       N  
ATOM   4184  N   LEU B 120     -65.748  12.306  32.428  1.00 70.13           N  
ANISOU 4184  N   LEU B 120     8705   9212   8730   -232    860   -119       N  
ATOM   4185  CA  LEU B 120     -64.294  12.447  32.299  1.00 70.19           C  
ANISOU 4185  CA  LEU B 120     8690   9338   8642   -281    838   -108       C  
ATOM   4186  C   LEU B 120     -63.718  13.362  33.372  1.00 74.64           C  
ANISOU 4186  C   LEU B 120     9319   9875   9167   -325    819    -77       C  
ATOM   4187  O   LEU B 120     -62.817  12.951  34.104  1.00 74.30           O  
ANISOU 4187  O   LEU B 120     9254   9898   9078   -308    834    -89       O  
ATOM   4188  CB  LEU B 120     -63.888  12.950  30.896  1.00 70.69           C  
ANISOU 4188  CB  LEU B 120     8707   9524   8628   -372    791    -80       C  
ATOM   4189  CG  LEU B 120     -63.858  11.918  29.762  1.00 75.39           C  
ANISOU 4189  CG  LEU B 120     9212  10235   9197   -323    802   -143       C  
ATOM   4190  CD1 LEU B 120     -63.883  12.599  28.416  1.00 76.08           C  
ANISOU 4190  CD1 LEU B 120     9272  10434   9202   -425    757    -97       C  
ATOM   4191  CD2 LEU B 120     -62.633  11.020  29.849  1.00 78.44           C  
ANISOU 4191  CD2 LEU B 120     9513  10785   9506   -252    820   -215       C  
ATOM   4192  N   TYR B 121     -64.278  14.577  33.496  1.00 72.16           N  
ANISOU 4192  N   TYR B 121     9098   9450   8872   -361    767    -52       N  
ATOM   4193  CA  TYR B 121     -63.827  15.564  34.468  1.00 72.89           C  
ANISOU 4193  CA  TYR B 121     9289   9477   8927   -402    716    -44       C  
ATOM   4194  C   TYR B 121     -64.093  15.160  35.911  1.00 75.46           C  
ANISOU 4194  C   TYR B 121     9634   9770   9267   -299    779    -96       C  
ATOM   4195  O   TYR B 121     -63.149  15.104  36.698  1.00 75.35           O  
ANISOU 4195  O   TYR B 121     9626   9812   9191   -329    775    -95       O  
ATOM   4196  CB  TYR B 121     -64.346  16.976  34.132  1.00 75.76           C  
ANISOU 4196  CB  TYR B 121     9791   9689   9306   -443    599    -19       C  
ATOM   4197  CG  TYR B 121     -63.835  17.517  32.808  1.00 79.52           C  
ANISOU 4197  CG  TYR B 121    10279  10211   9725   -609    513     77       C  
ATOM   4198  CD1 TYR B 121     -62.483  17.446  32.477  1.00 82.23           C  
ANISOU 4198  CD1 TYR B 121    10548  10738   9957   -780    508    138       C  
ATOM   4199  CD2 TYR B 121     -64.696  18.131  31.903  1.00 81.26           C  
ANISOU 4199  CD2 TYR B 121    10573  10324   9980   -600    429    113       C  
ATOM   4200  CE1 TYR B 121     -62.007  17.941  31.264  1.00 84.79           C  
ANISOU 4200  CE1 TYR B 121    10861  11165  10189   -968    439    244       C  
ATOM   4201  CE2 TYR B 121     -64.230  18.632  30.686  1.00 83.36           C  
ANISOU 4201  CE2 TYR B 121    10861  10647  10164   -779    342    228       C  
ATOM   4202  CZ  TYR B 121     -62.883  18.536  30.372  1.00 92.87           C  
ANISOU 4202  CZ  TYR B 121    11984  12061  11242   -979    356    299       C  
ATOM   4203  OH  TYR B 121     -62.414  19.027  29.176  1.00 96.62           O  
ANISOU 4203  OH  TYR B 121    12460  12653  11599  -1190    282    429       O  
ATOM   4204  N   SER B 122     -65.349  14.807  36.242  1.00 71.06           N  
ANISOU 4204  N   SER B 122     9062   9166   8770   -192    838   -134       N  
ATOM   4205  CA  SER B 122     -65.747  14.406  37.594  1.00 70.47           C  
ANISOU 4205  CA  SER B 122     8990   9108   8678   -117    910   -167       C  
ATOM   4206  C   SER B 122     -64.948  13.222  38.150  1.00 73.79           C  
ANISOU 4206  C   SER B 122     9378   9599   9062   -133    955   -130       C  
ATOM   4207  O   SER B 122     -64.256  13.401  39.152  1.00 73.69           O  
ANISOU 4207  O   SER B 122     9408   9612   8979   -134    945   -134       O  
ATOM   4208  CB  SER B 122     -67.246  14.144  37.671  1.00 72.94           C  
ANISOU 4208  CB  SER B 122     9243   9433   9037    -39    973   -197       C  
ATOM   4209  OG  SER B 122     -67.587  13.070  36.814  1.00 78.72           O  
ANISOU 4209  OG  SER B 122     9894  10189   9826    -77   1004   -159       O  
ATOM   4210  N   SER B 123     -64.992  12.041  37.479  1.00 69.60           N  
ANISOU 4210  N   SER B 123     8789   9082   8572   -135    977   -104       N  
ATOM   4211  CA  SER B 123     -64.301  10.822  37.932  1.00 69.07           C  
ANISOU 4211  CA  SER B 123     8726   9037   8483   -111    979    -78       C  
ATOM   4212  C   SER B 123     -62.867  11.040  38.419  1.00 72.21           C  
ANISOU 4212  C   SER B 123     9128   9510   8797   -105    933    -82       C  
ATOM   4213  O   SER B 123     -62.517  10.542  39.489  1.00 72.44           O  
ANISOU 4213  O   SER B 123     9197   9547   8778    -70    932    -58       O  
ATOM   4214  CB  SER B 123     -64.384   9.696  36.903  1.00 72.12           C  
ANISOU 4214  CB  SER B 123     9082   9397   8926    -91    959    -85       C  
ATOM   4215  OG  SER B 123     -63.760  10.020  35.670  1.00 80.23           O  
ANISOU 4215  OG  SER B 123    10047  10497   9941    -96    921   -125       O  
ATOM   4216  N   VAL B 124     -62.066  11.830  37.675  1.00 67.67           N  
ANISOU 4216  N   VAL B 124     8509   9014   8189   -160    887    -99       N  
ATOM   4217  CA  VAL B 124     -60.681  12.116  38.051  1.00 67.53           C  
ANISOU 4217  CA  VAL B 124     8455   9124   8079   -191    837   -101       C  
ATOM   4218  C   VAL B 124     -60.590  13.116  39.210  1.00 71.43           C  
ANISOU 4218  C   VAL B 124     9035   9584   8524   -243    814    -99       C  
ATOM   4219  O   VAL B 124     -59.835  12.882  40.154  1.00 71.45           O  
ANISOU 4219  O   VAL B 124     9037   9654   8456   -220    792    -99       O  
ATOM   4220  CB  VAL B 124     -59.756  12.430  36.841  1.00 71.46           C  
ANISOU 4220  CB  VAL B 124     8840   9790   8523   -268    798   -106       C  
ATOM   4221  CG1 VAL B 124     -60.169  13.709  36.102  1.00 71.16           C  
ANISOU 4221  CG1 VAL B 124     8846   9702   8492   -415    768    -69       C  
ATOM   4222  CG2 VAL B 124     -58.284  12.469  37.252  1.00 72.20           C  
ANISOU 4222  CG2 VAL B 124     8839  10090   8505   -294    751   -115       C  
ATOM   4223  N   TRP B 125     -61.418  14.143  39.194  1.00 67.48           N  
ANISOU 4223  N   TRP B 125     8616   8969   8054   -282    806   -112       N  
ATOM   4224  CA  TRP B 125     -61.414  15.144  40.248  1.00 67.56           C  
ANISOU 4224  CA  TRP B 125     8734   8923   8014   -301    762   -148       C  
ATOM   4225  C   TRP B 125     -62.104  14.734  41.537  1.00 70.31           C  
ANISOU 4225  C   TRP B 125     9121   9259   8334   -192    829   -179       C  
ATOM   4226  O   TRP B 125     -62.026  15.422  42.526  1.00 70.04           O  
ANISOU 4226  O   TRP B 125     9168   9213   8230   -182    797   -231       O  
ATOM   4227  CB  TRP B 125     -62.027  16.437  39.734  1.00 66.92           C  
ANISOU 4227  CB  TRP B 125     8754   8701   7971   -344    690   -173       C  
ATOM   4228  CG  TRP B 125     -61.086  17.194  38.908  1.00 69.02           C  
ANISOU 4228  CG  TRP B 125     9033   8985   8205   -521    585   -119       C  
ATOM   4229  CD1 TRP B 125     -60.920  17.103  37.569  1.00 71.70           C  
ANISOU 4229  CD1 TRP B 125     9300   9382   8560   -608    576    -55       C  
ATOM   4230  CD2 TRP B 125     -60.133  18.150  39.368  1.00 70.12           C  
ANISOU 4230  CD2 TRP B 125     9257   9118   8269   -672    466   -112       C  
ATOM   4231  NE1 TRP B 125     -59.927  17.950  37.160  1.00 72.46           N  
ANISOU 4231  NE1 TRP B 125     9420   9531   8581   -821    469      9       N  
ATOM   4232  CE2 TRP B 125     -59.428  18.604  38.253  1.00 74.90           C  
ANISOU 4232  CE2 TRP B 125     9828   9788   8841   -875    393    -22       C  
ATOM   4233  CE3 TRP B 125     -59.807  18.663  40.621  1.00 72.23           C  
ANISOU 4233  CE3 TRP B 125     9625   9343   8475   -672    407   -174       C  
ATOM   4234  CZ2 TRP B 125     -58.426  19.541  38.352  1.00 75.63           C  
ANISOU 4234  CZ2 TRP B 125     9983   9904   8851  -1109    259     27       C  
ATOM   4235  CZ3 TRP B 125     -58.821  19.588  40.712  1.00 75.00           C  
ANISOU 4235  CZ3 TRP B 125    10049   9689   8757   -879    266   -147       C  
ATOM   4236  CH2 TRP B 125     -58.140  20.020  39.592  1.00 76.39           C  
ANISOU 4236  CH2 TRP B 125    10189   9928   8909  -1110    191    -39       C  
ATOM   4237  N   ILE B 126     -62.804  13.624  41.513  1.00 66.30           N  
ANISOU 4237  N   ILE B 126     8563   8766   7864   -130    915   -146       N  
ATOM   4238  CA  ILE B 126     -63.338  12.995  42.723  1.00 66.77           C  
ANISOU 4238  CA  ILE B 126     8640   8865   7863    -77    983   -129       C  
ATOM   4239  C   ILE B 126     -62.136  12.271  43.357  1.00 71.32           C  
ANISOU 4239  C   ILE B 126     9225   9506   8368    -78    942    -80       C  
ATOM   4240  O   ILE B 126     -61.887  12.435  44.554  1.00 71.82           O  
ANISOU 4240  O   ILE B 126     9339   9625   8325    -66    936    -86       O  
ATOM   4241  CB  ILE B 126     -64.553  12.053  42.441  1.00 69.65           C  
ANISOU 4241  CB  ILE B 126     8956   9221   8286    -66   1068    -83       C  
ATOM   4242  CG1 ILE B 126     -65.783  12.864  41.977  1.00 70.14           C  
ANISOU 4242  CG1 ILE B 126     8983   9269   8397    -34   1101   -150       C  
ATOM   4243  CG2 ILE B 126     -64.909  11.216  43.688  1.00 70.86           C  
ANISOU 4243  CG2 ILE B 126     9132   9447   8347    -75   1127    -15       C  
ATOM   4244  CD1 ILE B 126     -66.801  12.098  41.134  1.00 76.74           C  
ANISOU 4244  CD1 ILE B 126     9737  10100   9319    -58   1149   -112       C  
ATOM   4245  N   LEU B 127     -61.341  11.552  42.523  1.00 67.07           N  
ANISOU 4245  N   LEU B 127     8630   8981   7873    -72    899    -51       N  
ATOM   4246  CA  LEU B 127     -60.126  10.862  42.963  1.00 67.47           C  
ANISOU 4246  CA  LEU B 127     8665   9111   7858    -26    833    -26       C  
ATOM   4247  C   LEU B 127     -59.111  11.850  43.523  1.00 71.55           C  
ANISOU 4247  C   LEU B 127     9170   9733   8281    -79    769    -65       C  
ATOM   4248  O   LEU B 127     -58.301  11.479  44.376  1.00 71.71           O  
ANISOU 4248  O   LEU B 127     9193   9838   8214    -38    717    -49       O  
ATOM   4249  CB  LEU B 127     -59.491  10.049  41.828  1.00 67.51           C  
ANISOU 4249  CB  LEU B 127     8587   9148   7916     34    790    -38       C  
ATOM   4250  CG  LEU B 127     -60.270   8.846  41.312  1.00 72.33           C  
ANISOU 4250  CG  LEU B 127     9236   9631   8612     92    806     -9       C  
ATOM   4251  CD1 LEU B 127     -59.664   8.356  40.053  1.00 72.67           C  
ANISOU 4251  CD1 LEU B 127     9194   9726   8692    165    760    -71       C  
ATOM   4252  CD2 LEU B 127     -60.302   7.715  42.321  1.00 75.43           C  
ANISOU 4252  CD2 LEU B 127     9741   9946   8974    154    764     68       C  
ATOM   4253  N   ALA B 128     -59.166  13.110  43.044  1.00 68.00           N  
ANISOU 4253  N   ALA B 128     8726   9266   7847   -180    751   -110       N  
ATOM   4254  CA  ALA B 128     -58.329  14.199  43.532  1.00 68.63           C  
ANISOU 4254  CA  ALA B 128     8830   9403   7843   -282    665   -145       C  
ATOM   4255  C   ALA B 128     -58.819  14.586  44.931  1.00 72.67           C  
ANISOU 4255  C   ALA B 128     9463   9869   8281   -241    672   -187       C  
ATOM   4256  O   ALA B 128     -57.993  14.740  45.833  1.00 73.69           O  
ANISOU 4256  O   ALA B 128     9606  10088   8305   -263    608   -201       O  
ATOM   4257  CB  ALA B 128     -58.390  15.391  42.585  1.00 69.45           C  
ANISOU 4257  CB  ALA B 128     8959   9440   7987   -420    614   -159       C  
ATOM   4258  N   PHE B 129     -60.159  14.659  45.128  1.00 67.38           N  
ANISOU 4258  N   PHE B 129     8855   9103   7644   -172    753   -213       N  
ATOM   4259  CA  PHE B 129     -60.764  14.974  46.421  1.00 67.50           C  
ANISOU 4259  CA  PHE B 129     8954   9135   7559   -109    784   -273       C  
ATOM   4260  C   PHE B 129     -60.541  13.858  47.445  1.00 71.22           C  
ANISOU 4260  C   PHE B 129     9412   9720   7928    -66    823   -196       C  
ATOM   4261  O   PHE B 129     -60.344  14.164  48.621  1.00 71.70           O  
ANISOU 4261  O   PHE B 129     9533   9858   7852    -50    801   -236       O  
ATOM   4262  CB  PHE B 129     -62.248  15.329  46.268  1.00 69.20           C  
ANISOU 4262  CB  PHE B 129     9185   9290   7816    -32    863   -333       C  
ATOM   4263  CG  PHE B 129     -62.523  16.809  46.141  1.00 71.56           C  
ANISOU 4263  CG  PHE B 129     9588   9473   8128    -12    776   -464       C  
ATOM   4264  CD1 PHE B 129     -62.146  17.510  44.999  1.00 74.41           C  
ANISOU 4264  CD1 PHE B 129     9985   9700   8588   -101    675   -454       C  
ATOM   4265  CD2 PHE B 129     -63.197  17.495  47.142  1.00 75.27           C  
ANISOU 4265  CD2 PHE B 129    10134   9966   8499    105    779   -602       C  
ATOM   4266  CE1 PHE B 129     -62.415  18.879  44.876  1.00 76.37           C  
ANISOU 4266  CE1 PHE B 129    10382   9783   8852    -88    551   -559       C  
ATOM   4267  CE2 PHE B 129     -63.478  18.861  47.010  1.00 79.22           C  
ANISOU 4267  CE2 PHE B 129    10771  10311   9019    165    658   -747       C  
ATOM   4268  CZ  PHE B 129     -63.083  19.543  45.880  1.00 76.87           C  
ANISOU 4268  CZ  PHE B 129    10545   9824   8837     62    531   -715       C  
ATOM   4269  N   ILE B 130     -60.526  12.576  46.994  1.00 66.92           N  
ANISOU 4269  N   ILE B 130     8813   9172   7441    -48    855    -87       N  
ATOM   4270  CA  ILE B 130     -60.259  11.415  47.853  1.00 67.64           C  
ANISOU 4270  CA  ILE B 130     8934   9320   7447    -13    849     17       C  
ATOM   4271  C   ILE B 130     -58.816  11.499  48.370  1.00 72.70           C  
ANISOU 4271  C   ILE B 130     9568  10054   8001      1    732      7       C  
ATOM   4272  O   ILE B 130     -58.603  11.377  49.574  1.00 74.14           O  
ANISOU 4272  O   ILE B 130     9809  10318   8042     17    708     33       O  
ATOM   4273  CB  ILE B 130     -60.551  10.046  47.167  1.00 70.77           C  
ANISOU 4273  CB  ILE B 130     9320   9629   7940     10    860    122       C  
ATOM   4274  CG1 ILE B 130     -61.986   9.969  46.613  1.00 70.86           C  
ANISOU 4274  CG1 ILE B 130     9313   9577   8033    -34    967    133       C  
ATOM   4275  CG2 ILE B 130     -60.317   8.902  48.145  1.00 73.47           C  
ANISOU 4275  CG2 ILE B 130     9750   9981   8185     36    814    249       C  
ATOM   4276  CD1 ILE B 130     -62.365   8.662  45.804  1.00 77.00           C  
ANISOU 4276  CD1 ILE B 130    10102  10235   8920    -44    956    223       C  
ATOM   4277  N   SER B 131     -57.839  11.733  47.466  1.00 68.88           N  
ANISOU 4277  N   SER B 131     8993   9599   7581    -15    660    -29       N  
ATOM   4278  CA  SER B 131     -56.417  11.870  47.804  1.00 69.51           C  
ANISOU 4278  CA  SER B 131     9009   9826   7575    -18    544    -48       C  
ATOM   4279  C   SER B 131     -56.157  13.125  48.644  1.00 74.78           C  
ANISOU 4279  C   SER B 131     9732  10544   8137   -115    496   -126       C  
ATOM   4280  O   SER B 131     -55.292  13.099  49.520  1.00 75.49           O  
ANISOU 4280  O   SER B 131     9815  10762   8106   -109    410   -128       O  
ATOM   4281  CB  SER B 131     -55.558  11.873  46.548  1.00 71.86           C  
ANISOU 4281  CB  SER B 131     9155  10209   7941    -37    500    -73       C  
ATOM   4282  OG  SER B 131     -55.974  12.894  45.659  1.00 78.44           O  
ANISOU 4282  OG  SER B 131     9981  10978   8845   -166    534   -114       O  
ATOM   4283  N   LEU B 132     -56.939  14.203  48.403  1.00 71.38           N  
ANISOU 4283  N   LEU B 132     9372  10001   7748   -187    532   -199       N  
ATOM   4284  CA  LEU B 132     -56.875  15.467  49.150  1.00 72.01           C  
ANISOU 4284  CA  LEU B 132     9558  10063   7741   -258    462   -305       C  
ATOM   4285  C   LEU B 132     -57.423  15.283  50.570  1.00 75.55           C  
ANISOU 4285  C   LEU B 132    10098  10563   8046   -165    504   -332       C  
ATOM   4286  O   LEU B 132     -56.835  15.805  51.520  1.00 76.49           O  
ANISOU 4286  O   LEU B 132    10274  10757   8031   -194    415   -397       O  
ATOM   4287  CB  LEU B 132     -57.646  16.577  48.410  1.00 71.70           C  
ANISOU 4287  CB  LEU B 132     9597   9848   7796   -310    460   -382       C  
ATOM   4288  CG  LEU B 132     -57.513  17.993  48.942  1.00 77.83           C  
ANISOU 4288  CG  LEU B 132    10527  10536   8511   -384    334   -509       C  
ATOM   4289  CD1 LEU B 132     -56.320  18.693  48.327  1.00 78.92           C  
ANISOU 4289  CD1 LEU B 132    10644  10680   8661   -603    185   -484       C  
ATOM   4290  CD2 LEU B 132     -58.766  18.785  48.659  1.00 79.78           C  
ANISOU 4290  CD2 LEU B 132    10894  10594   8824   -303    352   -608       C  
ATOM   4291  N   ASP B 133     -58.545  14.547  50.706  1.00 70.72           N  
ANISOU 4291  N   ASP B 133     9491   9935   7442    -76    635   -280       N  
ATOM   4292  CA  ASP B 133     -59.175  14.268  51.995  1.00 71.76           C  
ANISOU 4292  CA  ASP B 133     9683  10175   7408    -14    700   -278       C  
ATOM   4293  C   ASP B 133     -58.250  13.389  52.833  1.00 76.86           C  
ANISOU 4293  C   ASP B 133    10331  10943   7929     -8    635   -169       C  
ATOM   4294  O   ASP B 133     -58.024  13.677  54.011  1.00 78.04           O  
ANISOU 4294  O   ASP B 133    10543  11213   7897      2    597   -212       O  
ATOM   4295  CB  ASP B 133     -60.533  13.593  51.786  1.00 73.16           C  
ANISOU 4295  CB  ASP B 133     9830  10347   7622     22    851   -211       C  
ATOM   4296  CG  ASP B 133     -61.453  13.728  52.967  1.00 84.67           C  
ANISOU 4296  CG  ASP B 133    11318  11965   8889     65    943   -255       C  
ATOM   4297  OD1 ASP B 133     -61.313  12.931  53.915  1.00 86.95           O  
ANISOU 4297  OD1 ASP B 133    11630  12386   9022     44    958   -140       O  
ATOM   4298  OD2 ASP B 133     -62.335  14.620  52.934  1.00 90.13           O  
ANISOU 4298  OD2 ASP B 133    12005  12667   9572    131    995   -407       O  
ATOM   4299  N   ARG B 134     -57.657  12.366  52.189  1.00 72.81           N  
ANISOU 4299  N   ARG B 134     9755  10398   7510      7    598    -48       N  
ATOM   4300  CA  ARG B 134     -56.700  11.423  52.769  1.00 73.57           C  
ANISOU 4300  CA  ARG B 134     9853  10579   7520     59    498     57       C  
ATOM   4301  C   ARG B 134     -55.466  12.159  53.332  1.00 78.22           C  
ANISOU 4301  C   ARG B 134    10413  11305   8002     32    364    -29       C  
ATOM   4302  O   ARG B 134     -54.917  11.736  54.355  1.00 79.23           O  
ANISOU 4302  O   ARG B 134    10579  11550   7977     75    285     24       O  
ATOM   4303  CB  ARG B 134     -56.321  10.356  51.716  1.00 72.95           C  
ANISOU 4303  CB  ARG B 134     9710  10417   7591    126    462    142       C  
ATOM   4304  CG  ARG B 134     -55.344   9.252  52.156  1.00 85.47           C  
ANISOU 4304  CG  ARG B 134    11307  12055   9113    243    324    238       C  
ATOM   4305  CD  ARG B 134     -55.795   8.387  53.331  1.00 96.44           C  
ANISOU 4305  CD  ARG B 134    12853  13430  10361    261    309    390       C  
ATOM   4306  NE  ARG B 134     -57.078   7.718  53.106  1.00101.15           N  
ANISOU 4306  NE  ARG B 134    13537  13882  11015    204    416    500       N  
ATOM   4307  CZ  ARG B 134     -58.131   7.834  53.909  1.00111.27           C  
ANISOU 4307  CZ  ARG B 134    14889  15217  12172     98    527    561       C  
ATOM   4308  NH1 ARG B 134     -59.255   7.189  53.630  1.00105.38           N  
ANISOU 4308  NH1 ARG B 134    14188  14376  11475     16    616    670       N  
ATOM   4309  NH2 ARG B 134     -58.069   8.594  54.997  1.00 86.12           N  
ANISOU 4309  NH2 ARG B 134    11715  12210   8796     70    548    505       N  
ATOM   4310  N   TYR B 135     -55.065  13.277  52.683  1.00 74.02           N  
ANISOU 4310  N   TYR B 135     9826  10757   7540    -61    324   -148       N  
ATOM   4311  CA  TYR B 135     -53.957  14.129  53.117  1.00 74.71           C  
ANISOU 4311  CA  TYR B 135     9886  10966   7533   -151    185   -234       C  
ATOM   4312  C   TYR B 135     -54.328  14.780  54.459  1.00 80.33           C  
ANISOU 4312  C   TYR B 135    10741  11713   8066   -157    170   -321       C  
ATOM   4313  O   TYR B 135     -53.573  14.666  55.422  1.00 81.18           O  
ANISOU 4313  O   TYR B 135    10856  11973   8017   -149     70   -318       O  
ATOM   4314  CB  TYR B 135     -53.615  15.177  52.031  1.00 74.96           C  
ANISOU 4314  CB  TYR B 135     9861  10941   7680   -305    141   -309       C  
ATOM   4315  CG  TYR B 135     -52.828  16.372  52.527  1.00 78.23           C  
ANISOU 4315  CG  TYR B 135    10313  11414   7997   -468     -6   -411       C  
ATOM   4316  CD1 TYR B 135     -51.438  16.365  52.525  1.00 81.52           C  
ANISOU 4316  CD1 TYR B 135    10579  12044   8351   -566   -137   -394       C  
ATOM   4317  CD2 TYR B 135     -53.474  17.523  52.973  1.00 79.56           C  
ANISOU 4317  CD2 TYR B 135    10666  11431   8133   -523    -34   -539       C  
ATOM   4318  CE1 TYR B 135     -50.709  17.460  52.987  1.00 84.15           C  
ANISOU 4318  CE1 TYR B 135    10951  12433   8591   -762   -292   -479       C  
ATOM   4319  CE2 TYR B 135     -52.755  18.621  53.443  1.00 82.17           C  
ANISOU 4319  CE2 TYR B 135    11074  11772   8377   -687   -205   -642       C  
ATOM   4320  CZ  TYR B 135     -51.372  18.585  53.447  1.00 90.33           C  
ANISOU 4320  CZ  TYR B 135    11960  13012   9349   -832   -334   -600       C  
ATOM   4321  OH  TYR B 135     -50.655  19.663  53.901  1.00 93.28           O  
ANISOU 4321  OH  TYR B 135    12410  13399   9634  -1039   -519   -692       O  
ATOM   4322  N   LEU B 136     -55.515  15.414  54.521  1.00 77.22           N  
ANISOU 4322  N   LEU B 136    10451  11204   7684   -143    266   -409       N  
ATOM   4323  CA  LEU B 136     -56.045  16.090  55.709  1.00 78.97           C  
ANISOU 4323  CA  LEU B 136    10801  11477   7726   -106    269   -538       C  
ATOM   4324  C   LEU B 136     -56.342  15.117  56.857  1.00 84.11           C  
ANISOU 4324  C   LEU B 136    11472  12301   8184    -23    335   -435       C  
ATOM   4325  O   LEU B 136     -56.334  15.521  58.021  1.00 85.27           O  
ANISOU 4325  O   LEU B 136    11699  12579   8120     -1    300   -524       O  
ATOM   4326  CB  LEU B 136     -57.307  16.887  55.345  1.00 78.74           C  
ANISOU 4326  CB  LEU B 136    10843  11310   7764    -57    358   -668       C  
ATOM   4327  CG  LEU B 136     -57.100  18.104  54.452  1.00 83.18           C  
ANISOU 4327  CG  LEU B 136    11463  11670   8470   -145    248   -786       C  
ATOM   4328  CD1 LEU B 136     -58.348  18.416  53.687  1.00 82.41           C  
ANISOU 4328  CD1 LEU B 136    11386  11424   8500    -64    347   -837       C  
ATOM   4329  CD2 LEU B 136     -56.626  19.317  55.256  1.00 87.65           C  
ANISOU 4329  CD2 LEU B 136    12184  12209   8911   -193     78   -973       C  
ATOM   4330  N   ALA B 137     -56.604  13.842  56.525  1.00 80.08           N  
ANISOU 4330  N   ALA B 137    10907  11784   7734     11    413   -244       N  
ATOM   4331  CA  ALA B 137     -56.870  12.798  57.505  1.00 81.39           C  
ANISOU 4331  CA  ALA B 137    11119  12080   7725     47    451    -89       C  
ATOM   4332  C   ALA B 137     -55.575  12.346  58.192  1.00 87.24           C  
ANISOU 4332  C   ALA B 137    11868  12933   8348     64    285    -16       C  
ATOM   4333  O   ALA B 137     -55.588  12.108  59.399  1.00 88.84           O  
ANISOU 4333  O   ALA B 137    12145  13292   8317     76    265     32       O  
ATOM   4334  CB  ALA B 137     -57.552  11.618  56.832  1.00 81.20           C  
ANISOU 4334  CB  ALA B 137    11074  11953   7826     50    544     94       C  
ATOM   4335  N   ILE B 138     -54.459  12.249  57.435  1.00 83.74           N  
ANISOU 4335  N   ILE B 138    11328  12449   8041     70    164    -13       N  
ATOM   4336  CA  ILE B 138     -53.162  11.803  57.959  1.00 85.44           C  
ANISOU 4336  CA  ILE B 138    11504  12801   8156    118    -10     41       C  
ATOM   4337  C   ILE B 138     -52.275  12.951  58.457  1.00 90.93           C  
ANISOU 4337  C   ILE B 138    12168  13634   8746     35   -135   -122       C  
ATOM   4338  O   ILE B 138     -51.859  12.938  59.619  1.00 92.61           O  
ANISOU 4338  O   ILE B 138    12436  14005   8747     51   -227   -120       O  
ATOM   4339  CB  ILE B 138     -52.440  10.822  56.981  1.00 88.10           C  
ANISOU 4339  CB  ILE B 138    11730  13087   8657    214    -83    137       C  
ATOM   4340  CG1 ILE B 138     -53.180   9.457  56.929  1.00 88.61           C  
ANISOU 4340  CG1 ILE B 138    11901  13011   8758    301    -34    326       C  
ATOM   4341  CG2 ILE B 138     -50.954  10.629  57.352  1.00 90.27           C  
ANISOU 4341  CG2 ILE B 138    11900  13556   8843    284   -282    131       C  
ATOM   4342  CD1 ILE B 138     -52.931   8.616  55.664  1.00 95.12           C  
ANISOU 4342  CD1 ILE B 138    12650  13699   9792    405    -63    367       C  
ATOM   4343  N   VAL B 139     -51.983  13.925  57.580  1.00 86.71           N  
ANISOU 4343  N   VAL B 139    11559  13038   8350    -74   -155   -250       N  
ATOM   4344  CA  VAL B 139     -51.128  15.079  57.887  1.00 87.82           C  
ANISOU 4344  CA  VAL B 139    11684  13269   8415   -213   -300   -396       C  
ATOM   4345  C   VAL B 139     -51.766  16.026  58.920  1.00 93.41           C  
ANISOU 4345  C   VAL B 139    12574  13956   8960   -242   -298   -548       C  
ATOM   4346  O   VAL B 139     -51.038  16.668  59.674  1.00 95.35           O  
ANISOU 4346  O   VAL B 139    12852  14316   9062   -320   -448   -649       O  
ATOM   4347  CB  VAL B 139     -50.662  15.810  56.591  1.00 90.63           C  
ANISOU 4347  CB  VAL B 139    11927  13556   8954   -367   -335   -450       C  
ATOM   4348  CG1 VAL B 139     -49.705  16.961  56.895  1.00 92.29           C  
ANISOU 4348  CG1 VAL B 139    12127  13858   9080   -572   -516   -570       C  
ATOM   4349  CG2 VAL B 139     -50.014  14.833  55.611  1.00 89.58           C  
ANISOU 4349  CG2 VAL B 139    11588  13510   8940   -301   -331   -332       C  
ATOM   4350  N   HIS B 140     -53.109  16.085  58.988  1.00 89.18           N  
ANISOU 4350  N   HIS B 140    12145  13308   8431   -168   -138   -578       N  
ATOM   4351  CA  HIS B 140     -53.798  16.987  59.912  1.00 90.51           C  
ANISOU 4351  CA  HIS B 140    12468  13489   8433   -143   -127   -762       C  
ATOM   4352  C   HIS B 140     -54.788  16.299  60.864  1.00 95.31           C  
ANISOU 4352  C   HIS B 140    13127  14240   8846    -18     21   -703       C  
ATOM   4353  O   HIS B 140     -55.904  16.787  61.069  1.00 95.84           O  
ANISOU 4353  O   HIS B 140    13259  14297   8859     51    135   -829       O  
ATOM   4354  CB  HIS B 140     -54.433  18.151  59.130  1.00 90.70           C  
ANISOU 4354  CB  HIS B 140    12570  13282   8611   -178   -117   -933       C  
ATOM   4355  CG  HIS B 140     -53.455  18.847  58.237  1.00 93.98           C  
ANISOU 4355  CG  HIS B 140    12951  13576   9181   -360   -273   -955       C  
ATOM   4356  ND1 HIS B 140     -52.590  19.810  58.726  1.00 97.79           N  
ANISOU 4356  ND1 HIS B 140    13514  14070   9570   -501   -479  -1088       N  
ATOM   4357  CD2 HIS B 140     -53.196  18.655  56.923  1.00 94.01           C  
ANISOU 4357  CD2 HIS B 140    12837  13484   9397   -445   -253   -848       C  
ATOM   4358  CE1 HIS B 140     -51.861  20.193  57.693  1.00 96.66           C  
ANISOU 4358  CE1 HIS B 140    13297  13846   9586   -694   -574  -1040       C  
ATOM   4359  NE2 HIS B 140     -52.187  19.526  56.588  1.00 94.70           N  
ANISOU 4359  NE2 HIS B 140    12921  13547   9514   -657   -436   -899       N  
ATOM   4360  N   ALA B 141     -54.348  15.192  61.484  1.00 92.01           N  
ANISOU 4360  N   ALA B 141    12678  13981   8300      8      1   -513       N  
ATOM   4361  CA  ALA B 141     -55.154  14.422  62.428  1.00 93.01           C  
ANISOU 4361  CA  ALA B 141    12857  14274   8209     66    119   -395       C  
ATOM   4362  C   ALA B 141     -55.177  15.097  63.797  1.00100.01           C  
ANISOU 4362  C   ALA B 141    13839  15379   8781     88     74   -555       C  
ATOM   4363  O   ALA B 141     -55.779  16.155  63.955  1.00100.39           O  
ANISOU 4363  O   ALA B 141    13943  15421   8782    126    112   -798       O  
ATOM   4364  CB  ALA B 141     -54.605  13.010  62.553  1.00 93.88           C  
ANISOU 4364  CB  ALA B 141    12946  14424   8301     79     64   -118       C  
ATOM   4365  N   GLN B 145     -57.738  20.265  63.030  1.00122.48           N  
ANISOU 4365  N   GLN B 145    17023  17733  11782    374     56  -1728       N  
ATOM   4366  CA  GLN B 145     -59.169  19.981  63.146  1.00122.55           C  
ANISOU 4366  CA  GLN B 145    16952  17905  11706    540    283  -1760       C  
ATOM   4367  C   GLN B 145     -59.754  19.313  61.878  1.00123.10           C  
ANISOU 4367  C   GLN B 145    16887  17837  12048    503    428  -1557       C  
ATOM   4368  O   GLN B 145     -58.988  18.740  61.097  1.00120.81           O  
ANISOU 4368  O   GLN B 145    16547  17396  11958    354    383  -1344       O  
ATOM   4369  CB  GLN B 145     -59.955  21.244  63.569  1.00126.40           C  
ANISOU 4369  CB  GLN B 145    17564  18388  12075    759    240  -2143       C  
ATOM   4370  CG  GLN B 145     -60.978  20.997  64.681  1.00143.82           C  
ANISOU 4370  CG  GLN B 145    19689  21021  13935    937    424  -2249       C  
ATOM   4371  CD  GLN B 145     -60.365  20.966  66.063  1.00166.09           C  
ANISOU 4371  CD  GLN B 145    22578  24114  16414    922    353  -2309       C  
ATOM   4372  OE1 GLN B 145     -60.290  21.982  66.762  1.00164.47           O  
ANISOU 4372  OE1 GLN B 145    22525  23926  16039   1060    214  -2639       O  
ATOM   4373  NE2 GLN B 145     -59.921  19.796  66.500  1.00157.49           N  
ANISOU 4373  NE2 GLN B 145    21399  23232  15209    765    424  -1997       N  
ATOM   4374  N   ARG B 146     -61.098  19.371  61.679  1.00118.55           N  
ANISOU 4374  N   ARG B 146    16235  17345  11463    647    597  -1637       N  
ATOM   4375  CA  ARG B 146     -61.798  18.708  60.574  1.00115.09           C  
ANISOU 4375  CA  ARG B 146    15659  16822  11246    614    741  -1459       C  
ATOM   4376  C   ARG B 146     -62.481  19.611  59.520  1.00115.97           C  
ANISOU 4376  C   ARG B 146    15795  16686  11582    731    716  -1633       C  
ATOM   4377  O   ARG B 146     -63.709  19.727  59.524  1.00116.41           O  
ANISOU 4377  O   ARG B 146    15758  16890  11581    890    851  -1741       O  
ATOM   4378  CB  ARG B 146     -62.778  17.653  61.123  1.00116.16           C  
ANISOU 4378  CB  ARG B 146    15637  17309  11189    614    972  -1301       C  
ATOM   4379  CG  ARG B 146     -63.021  16.468  60.196  1.00123.89           C  
ANISOU 4379  CG  ARG B 146    16500  18208  12366    472   1077   -997       C  
ATOM   4380  CD  ARG B 146     -64.345  15.775  60.475  1.00137.86           C  
ANISOU 4380  CD  ARG B 146    18109  20285  13985    465   1298   -903       C  
ATOM   4381  NE  ARG B 146     -64.432  15.213  61.828  1.00155.73           N  
ANISOU 4381  NE  ARG B 146    20359  22919  15894    407   1372   -808       N  
ATOM   4382  CZ  ARG B 146     -65.265  15.645  62.774  1.00176.46           C  
ANISOU 4382  CZ  ARG B 146    22907  25929  18211    521   1487   -985       C  
ATOM   4383  NH1 ARG B 146     -66.087  16.661  62.534  1.00167.67           N  
ANISOU 4383  NH1 ARG B 146    21729  24867  17112    741   1528  -1294       N  
ATOM   4384  NH2 ARG B 146     -65.281  15.066  63.966  1.00163.96           N  
ANISOU 4384  NH2 ARG B 146    21312  24701  16286    431   1552   -861       N  
ATOM   4385  N   PRO B 147     -61.729  20.164  58.532  1.00109.15           N  
ANISOU 4385  N   PRO B 147    15031  15471  10972    638    548  -1628       N  
ATOM   4386  CA  PRO B 147     -62.376  20.930  57.445  1.00107.29           C  
ANISOU 4386  CA  PRO B 147    14834  14979  10952    727    508  -1742       C  
ATOM   4387  C   PRO B 147     -62.757  20.012  56.266  1.00105.03           C  
ANISOU 4387  C   PRO B 147    14384  14643  10878    639    644  -1500       C  
ATOM   4388  O   PRO B 147     -63.028  20.484  55.160  1.00103.40           O  
ANISOU 4388  O   PRO B 147    14204  14201  10881    651    592  -1521       O  
ATOM   4389  CB  PRO B 147     -61.306  21.961  57.065  1.00109.42           C  
ANISOU 4389  CB  PRO B 147    15310  14924  11342    613    244  -1825       C  
ATOM   4390  CG  PRO B 147     -59.985  21.357  57.520  1.00113.82           C  
ANISOU 4390  CG  PRO B 147    15840  15577  11830    405    189  -1658       C  
ATOM   4391  CD  PRO B 147     -60.264  20.127  58.352  1.00109.62           C  
ANISOU 4391  CD  PRO B 147    15155  15385  11111    437    381  -1513       C  
ATOM   4392  N   ARG B 148     -62.784  18.682  56.522  1.00 98.42           N  
ANISOU 4392  N   ARG B 148    13402  14019   9975    546    798  -1267       N  
ATOM   4393  CA  ARG B 148     -63.110  17.605  55.583  1.00 94.98           C  
ANISOU 4393  CA  ARG B 148    12827  13557   9704    451    917  -1031       C  
ATOM   4394  C   ARG B 148     -64.611  17.482  55.351  1.00 98.89           C  
ANISOU 4394  C   ARG B 148    13193  14189  10194    563   1082  -1074       C  
ATOM   4395  O   ARG B 148     -65.023  17.084  54.257  1.00 96.52           O  
ANISOU 4395  O   ARG B 148    12811  13775  10087    519   1130   -968       O  
ATOM   4396  CB  ARG B 148     -62.554  16.268  56.086  1.00 92.43           C  
ANISOU 4396  CB  ARG B 148    12452  13376   9292    320    969   -781       C  
ATOM   4397  CG  ARG B 148     -61.040  16.168  56.041  1.00 94.94           C  
ANISOU 4397  CG  ARG B 148    12837  13579   9657    216    809   -704       C  
ATOM   4398  CD  ARG B 148     -60.525  15.104  56.986  1.00 98.64           C  
ANISOU 4398  CD  ARG B 148    13301  14227   9951    161    817   -528       C  
ATOM   4399  NE  ARG B 148     -60.617  13.754  56.424  1.00100.94           N  
ANISOU 4399  NE  ARG B 148    13527  14477  10347     93    877   -281       N  
ATOM   4400  CZ  ARG B 148     -61.060  12.691  57.089  1.00116.44           C  
ANISOU 4400  CZ  ARG B 148    15487  16588  12168     49    956   -101       C  
ATOM   4401  NH1 ARG B 148     -61.468  12.805  58.347  1.00107.80           N  
ANISOU 4401  NH1 ARG B 148    14416  15746  10797     60   1012   -129       N  
ATOM   4402  NH2 ARG B 148     -61.101  11.504  56.496  1.00100.74           N  
ANISOU 4402  NH2 ARG B 148    13484  14494  10299    -16    965    111       N  
ATOM   4403  N   LYS B 149     -65.425  17.804  56.392  1.00 97.84           N  
ANISOU 4403  N   LYS B 149    13019  14341   9816    708   1168  -1237       N  
ATOM   4404  CA  LYS B 149     -66.892  17.804  56.340  1.00 98.76           C  
ANISOU 4404  CA  LYS B 149    12966  14688   9868    839   1327  -1323       C  
ATOM   4405  C   LYS B 149     -67.346  18.796  55.268  1.00102.15           C  
ANISOU 4405  C   LYS B 149    13433  14864  10515    998   1235  -1501       C  
ATOM   4406  O   LYS B 149     -68.227  18.471  54.473  1.00101.30           O  
ANISOU 4406  O   LYS B 149    13180  14787  10522   1010   1328  -1444       O  
ATOM   4407  CB  LYS B 149     -67.494  18.182  57.710  1.00104.81           C  
ANISOU 4407  CB  LYS B 149    13684  15845  10295   1001   1408  -1524       C  
ATOM   4408  CG  LYS B 149     -67.593  17.028  58.722  1.00120.59           C  
ANISOU 4408  CG  LYS B 149    15573  18215  12029    833   1563  -1306       C  
ATOM   4409  CD  LYS B 149     -68.884  16.197  58.584  1.00129.22           C  
ANISOU 4409  CD  LYS B 149    16417  19631  13051    758   1778  -1168       C  
ATOM   4410  CE  LYS B 149     -70.039  16.697  59.422  1.00139.69           C  
ANISOU 4410  CE  LYS B 149    17560  21443  14072    953   1920  -1404       C  
ATOM   4411  NZ  LYS B 149     -71.323  16.054  59.024  1.00146.83           N  
ANISOU 4411  NZ  LYS B 149    18188  22645  14955    874   2108  -1293       N  
ATOM   4412  N   LEU B 150     -66.684  19.975  55.211  1.00 98.92           N  
ANISOU 4412  N   LEU B 150    13238  14180  10166   1090   1027  -1694       N  
ATOM   4413  CA  LEU B 150     -66.920  21.029  54.224  1.00 98.45           C  
ANISOU 4413  CA  LEU B 150    13293  13804  10308   1217    874  -1845       C  
ATOM   4414  C   LEU B 150     -66.671  20.506  52.810  1.00 98.45           C  
ANISOU 4414  C   LEU B 150    13252  13578  10577   1032    871  -1608       C  
ATOM   4415  O   LEU B 150     -67.494  20.737  51.925  1.00 97.91           O  
ANISOU 4415  O   LEU B 150    13126  13435  10640   1131    878  -1642       O  
ATOM   4416  CB  LEU B 150     -65.988  22.224  54.494  1.00 99.86           C  
ANISOU 4416  CB  LEU B 150    13756  13695  10491   1242    618  -2022       C  
ATOM   4417  CG  LEU B 150     -66.644  23.586  54.711  1.00107.81           C  
ANISOU 4417  CG  LEU B 150    14924  14584  11454   1554    462  -2375       C  
ATOM   4418  CD1 LEU B 150     -65.656  24.564  55.315  1.00109.94           C  
ANISOU 4418  CD1 LEU B 150    15487  14621  11664   1531    212  -2538       C  
ATOM   4419  CD2 LEU B 150     -67.216  24.151  53.417  1.00109.34           C  
ANISOU 4419  CD2 LEU B 150    15168  14491  11884   1646    362  -2396       C  
ATOM   4420  N   LEU B 151     -65.551  19.778  52.615  1.00 92.34           N  
ANISOU 4420  N   LEU B 151    12492  12728   9864    787    857  -1381       N  
ATOM   4421  CA  LEU B 151     -65.154  19.206  51.327  1.00 89.25           C  
ANISOU 4421  CA  LEU B 151    12055  12163   9693    616    852  -1171       C  
ATOM   4422  C   LEU B 151     -66.146  18.179  50.777  1.00 91.52           C  
ANISOU 4422  C   LEU B 151    12144  12591  10039    606   1030  -1037       C  
ATOM   4423  O   LEU B 151     -66.628  18.344  49.654  1.00 89.70           O  
ANISOU 4423  O   LEU B 151    11880  12228   9974    625   1015  -1026       O  
ATOM   4424  CB  LEU B 151     -63.751  18.569  51.401  1.00 87.81           C  
ANISOU 4424  CB  LEU B 151    11897  11950   9518    409    803   -995       C  
ATOM   4425  CG  LEU B 151     -62.517  19.462  51.429  1.00 92.23           C  
ANISOU 4425  CG  LEU B 151    12618  12333  10091    312    600  -1052       C  
ATOM   4426  CD1 LEU B 151     -61.290  18.611  51.539  1.00 91.08           C  
ANISOU 4426  CD1 LEU B 151    12415  12263   9928    145    588   -877       C  
ATOM   4427  CD2 LEU B 151     -62.399  20.314  50.171  1.00 93.61           C  
ANISOU 4427  CD2 LEU B 151    12883  12235  10452    253    466  -1067       C  
ATOM   4428  N   ALA B 152     -66.433  17.120  51.562  1.00 88.37           N  
ANISOU 4428  N   ALA B 152    11627  12455   9494    551   1181   -922       N  
ATOM   4429  CA  ALA B 152     -67.314  16.016  51.183  1.00 87.69           C  
ANISOU 4429  CA  ALA B 152    11369  12511   9438    476   1334   -765       C  
ATOM   4430  C   ALA B 152     -68.813  16.365  51.130  1.00 93.07           C  
ANISOU 4430  C   ALA B 152    11897  13392  10073    627   1437   -899       C  
ATOM   4431  O   ALA B 152     -69.551  15.750  50.350  1.00 91.84           O  
ANISOU 4431  O   ALA B 152    11607  13268  10019    563   1513   -798       O  
ATOM   4432  CB  ALA B 152     -67.079  14.829  52.102  1.00 88.95           C  
ANISOU 4432  CB  ALA B 152    11496  12861   9439    334   1421   -577       C  
ATOM   4433  N   GLU B 153     -69.262  17.338  51.950  1.00 91.85           N  
ANISOU 4433  N   GLU B 153    11753  13389   9756    838   1429  -1143       N  
ATOM   4434  CA  GLU B 153     -70.676  17.724  52.001  1.00 93.71           C  
ANISOU 4434  CA  GLU B 153    11810  13883   9912   1037   1522  -1313       C  
ATOM   4435  C   GLU B 153     -71.045  18.970  51.192  1.00 98.19           C  
ANISOU 4435  C   GLU B 153    12455  14223  10628   1281   1374  -1537       C  
ATOM   4436  O   GLU B 153     -72.191  19.075  50.759  1.00 98.92           O  
ANISOU 4436  O   GLU B 153    12374  14470  10739   1420   1433  -1619       O  
ATOM   4437  CB  GLU B 153     -71.180  17.844  53.450  1.00 98.09           C  
ANISOU 4437  CB  GLU B 153    12269  14857  10145   1154   1634  -1456       C  
ATOM   4438  CG  GLU B 153     -71.174  16.534  54.220  1.00108.39           C  
ANISOU 4438  CG  GLU B 153    13459  16455  11268    899   1796  -1203       C  
ATOM   4439  CD  GLU B 153     -71.822  16.598  55.590  1.00135.18           C  
ANISOU 4439  CD  GLU B 153    16712  20346  14303    986   1933  -1321       C  
ATOM   4440  OE1 GLU B 153     -72.790  15.839  55.822  1.00136.64           O  
ANISOU 4440  OE1 GLU B 153    16655  20921  14342    868   2112  -1203       O  
ATOM   4441  OE2 GLU B 153     -71.368  17.407  56.431  1.00129.99           O  
ANISOU 4441  OE2 GLU B 153    16182  19714  13495   1157   1858  -1531       O  
ATOM   4442  N   LYS B 154     -70.109  19.921  51.007  1.00 94.19           N  
ANISOU 4442  N   LYS B 154    12211  13362  10215   1326   1167  -1632       N  
ATOM   4443  CA  LYS B 154     -70.417  21.158  50.280  1.00 94.53           C  
ANISOU 4443  CA  LYS B 154    12391  13136  10390   1544    981  -1827       C  
ATOM   4444  C   LYS B 154     -69.494  21.718  49.182  1.00 96.19           C  
ANISOU 4444  C   LYS B 154    12835  12887  10827   1416    770  -1739       C  
ATOM   4445  O   LYS B 154     -69.979  22.457  48.320  1.00 96.77           O  
ANISOU 4445  O   LYS B 154    12981  12759  11029   1552    641  -1820       O  
ATOM   4446  CB  LYS B 154     -70.492  22.373  51.236  1.00 99.87           C  
ANISOU 4446  CB  LYS B 154    13230  13802  10912   1829    847  -2153       C  
ATOM   4447  CG  LYS B 154     -71.464  22.233  52.421  1.00115.68           C  
ANISOU 4447  CG  LYS B 154    15021  16296  12636   2048   1018  -2343       C  
ATOM   4448  CD  LYS B 154     -72.914  22.566  52.061  1.00127.44           C  
ANISOU 4448  CD  LYS B 154    16308  17999  14114   2352   1063  -2529       C  
ATOM   4449  CE  LYS B 154     -73.823  22.558  53.267  1.00141.60           C  
ANISOU 4449  CE  LYS B 154    17871  20338  15591   2587   1224  -2753       C  
ATOM   4450  NZ  LYS B 154     -75.188  23.054  52.936  1.00151.96           N  
ANISOU 4450  NZ  LYS B 154    18977  21880  16879   2945   1234  -2992       N  
ATOM   4451  N   VAL B 155     -68.176  21.375  49.219  1.00 90.11           N  
ANISOU 4451  N   VAL B 155    12171  11982  10085   1154    729  -1570       N  
ATOM   4452  CA  VAL B 155     -67.139  21.858  48.283  1.00 88.33           C  
ANISOU 4452  CA  VAL B 155    12134  11405  10024    973    543  -1466       C  
ATOM   4453  C   VAL B 155     -67.235  20.985  47.016  1.00 89.66           C  
ANISOU 4453  C   VAL B 155    12156  11562  10350    818    632  -1243       C  
ATOM   4454  O   VAL B 155     -67.253  21.534  45.916  1.00 88.45           O  
ANISOU 4454  O   VAL B 155    12088  11182  10336    795    508  -1214       O  
ATOM   4455  CB  VAL B 155     -65.687  21.946  48.851  1.00 91.71           C  
ANISOU 4455  CB  VAL B 155    12699  11756  10393    772    449  -1409       C  
ATOM   4456  CG1 VAL B 155     -64.708  22.481  47.806  1.00 90.71           C  
ANISOU 4456  CG1 VAL B 155    12721  11334  10411    555    265  -1294       C  
ATOM   4457  CG2 VAL B 155     -65.628  22.812  50.106  1.00 94.09           C  
ANISOU 4457  CG2 VAL B 155    13157  12066  10525    926    346  -1650       C  
ATOM   4458  N   VAL B 156     -67.356  19.649  47.182  1.00 85.44           N  
ANISOU 4458  N   VAL B 156    11421  11262   9782    719    827  -1093       N  
ATOM   4459  CA  VAL B 156     -67.485  18.647  46.109  1.00 83.46           C  
ANISOU 4459  CA  VAL B 156    11032  11019   9658    584    914   -903       C  
ATOM   4460  C   VAL B 156     -68.450  19.048  44.944  1.00 89.18           C  
ANISOU 4460  C   VAL B 156    11716  11653  10514    681    877   -937       C  
ATOM   4461  O   VAL B 156     -68.228  18.651  43.795  1.00 87.79           O  
ANISOU 4461  O   VAL B 156    11513  11381  10464    556    863   -804       O  
ATOM   4462  CB  VAL B 156     -67.752  17.221  46.682  1.00 86.39           C  
ANISOU 4462  CB  VAL B 156    11235  11642   9949    501   1100   -773       C  
ATOM   4463  CG1 VAL B 156     -69.162  17.086  47.250  1.00 87.75           C  
ANISOU 4463  CG1 VAL B 156    11248  12079  10014    636   1233   -861       C  
ATOM   4464  CG2 VAL B 156     -67.463  16.128  45.656  1.00 84.19           C  
ANISOU 4464  CG2 VAL B 156    10884  11305   9799    337   1136   -581       C  
ATOM   4465  N   TYR B 157     -69.486  19.853  45.243  1.00 87.83           N  
ANISOU 4465  N   TYR B 157    11542  11530  10300    924    848  -1131       N  
ATOM   4466  CA  TYR B 157     -70.455  20.309  44.246  1.00 88.06           C  
ANISOU 4466  CA  TYR B 157    11531  11491  10436   1064    789  -1185       C  
ATOM   4467  C   TYR B 157     -69.915  21.532  43.506  1.00 92.12           C  
ANISOU 4467  C   TYR B 157    12308  11642  11051   1079    540  -1219       C  
ATOM   4468  O   TYR B 157     -69.833  21.523  42.278  1.00 90.22           O  
ANISOU 4468  O   TYR B 157    12089  11258  10934    976    476  -1097       O  
ATOM   4469  CB  TYR B 157     -71.820  20.598  44.915  1.00 91.54           C  
ANISOU 4469  CB  TYR B 157    11823  12192  10768   1352    857  -1393       C  
ATOM   4470  CG  TYR B 157     -72.449  19.376  45.555  1.00 92.76           C  
ANISOU 4470  CG  TYR B 157    11701  12740  10805   1274   1100  -1320       C  
ATOM   4471  CD1 TYR B 157     -72.205  19.058  46.887  1.00 95.41           C  
ANISOU 4471  CD1 TYR B 157    12008  13291  10952   1250   1206  -1346       C  
ATOM   4472  CD2 TYR B 157     -73.261  18.519  44.818  1.00 92.79           C  
ANISOU 4472  CD2 TYR B 157    11487  12895  10872   1188   1208  -1204       C  
ATOM   4473  CE1 TYR B 157     -72.746  17.912  47.469  1.00 96.16           C  
ANISOU 4473  CE1 TYR B 157    11878  13738  10922   1123   1411  -1234       C  
ATOM   4474  CE2 TYR B 157     -73.815  17.376  45.391  1.00 93.89           C  
ANISOU 4474  CE2 TYR B 157    11401  13373  10900   1053   1406  -1104       C  
ATOM   4475  CZ  TYR B 157     -73.555  17.075  46.717  1.00101.10           C  
ANISOU 4475  CZ  TYR B 157    12302  14490  11621   1012   1506  -1107       C  
ATOM   4476  OH  TYR B 157     -74.107  15.952  47.283  1.00102.17           O  
ANISOU 4476  OH  TYR B 157    12238  14954  11628    837   1682   -973       O  
ATOM   4477  N   VAL B 158     -69.504  22.555  44.273  1.00 91.00           N  
ANISOU 4477  N   VAL B 158    12381  11353  10840   1178    391  -1373       N  
ATOM   4478  CA  VAL B 158     -68.954  23.838  43.818  1.00 92.21           C  
ANISOU 4478  CA  VAL B 158    12846  11128  11060   1169    111  -1414       C  
ATOM   4479  C   VAL B 158     -67.639  23.641  43.045  1.00 94.30           C  
ANISOU 4479  C   VAL B 158    13192  11242  11395    807     55  -1176       C  
ATOM   4480  O   VAL B 158     -67.408  24.323  42.044  1.00 94.58           O  
ANISOU 4480  O   VAL B 158    13392  11026  11519    712   -126  -1096       O  
ATOM   4481  CB  VAL B 158     -68.788  24.814  45.030  1.00 98.72           C  
ANISOU 4481  CB  VAL B 158    13881  11860  11769   1343    -29  -1653       C  
ATOM   4482  CG1 VAL B 158     -68.053  26.102  44.649  1.00100.07           C  
ANISOU 4482  CG1 VAL B 158    14424  11593  12004   1257   -353  -1668       C  
ATOM   4483  CG2 VAL B 158     -70.139  25.134  45.675  1.00100.89           C  
ANISOU 4483  CG2 VAL B 158    14061  12316  11955   1750      8  -1926       C  
ATOM   4484  N   GLY B 159     -66.812  22.708  43.514  1.00 88.93           N  
ANISOU 4484  N   GLY B 159    12388  10745  10656    619    203  -1066       N  
ATOM   4485  CA  GLY B 159     -65.501  22.423  42.943  1.00 87.39           C  
ANISOU 4485  CA  GLY B 159    12210  10506  10489    309    172   -873       C  
ATOM   4486  C   GLY B 159     -65.429  21.356  41.873  1.00 89.42           C  
ANISOU 4486  C   GLY B 159    12271  10885  10818    178    304   -692       C  
ATOM   4487  O   GLY B 159     -64.545  21.423  41.016  1.00 88.83           O  
ANISOU 4487  O   GLY B 159    12223  10755  10774    -40    235   -555       O  
ATOM   4488  N   VAL B 160     -66.310  20.339  41.929  1.00 84.80           N  
ANISOU 4488  N   VAL B 160    11485  10491  10244    290    488   -691       N  
ATOM   4489  CA  VAL B 160     -66.275  19.242  40.959  1.00 82.81           C  
ANISOU 4489  CA  VAL B 160    11068  10338  10058    180    597   -545       C  
ATOM   4490  C   VAL B 160     -67.476  19.186  40.013  1.00 86.70           C  
ANISOU 4490  C   VAL B 160    11482  10822  10636    282    614   -551       C  
ATOM   4491  O   VAL B 160     -67.280  19.284  38.801  1.00 86.32           O  
ANISOU 4491  O   VAL B 160    11450  10694  10654    184    550   -461       O  
ATOM   4492  CB  VAL B 160     -65.913  17.871  41.606  1.00 85.66           C  
ANISOU 4492  CB  VAL B 160    11285  10896  10368    126    758   -477       C  
ATOM   4493  CG1 VAL B 160     -66.121  16.698  40.645  1.00 84.06           C  
ANISOU 4493  CG1 VAL B 160    10939  10763  10239     64    848   -368       C  
ATOM   4494  CG2 VAL B 160     -64.486  17.880  42.135  1.00 85.48           C  
ANISOU 4494  CG2 VAL B 160    11319  10884  10274     -3    708   -436       C  
ATOM   4495  N   TRP B 161     -68.698  19.012  40.553  1.00 83.06           N  
ANISOU 4495  N   TRP B 161    10917  10487  10157    467    703   -654       N  
ATOM   4496  CA  TRP B 161     -69.925  18.872  39.767  1.00 82.69           C  
ANISOU 4496  CA  TRP B 161    10748  10493  10176    571    727   -672       C  
ATOM   4497  C   TRP B 161     -70.356  20.078  38.938  1.00 87.74           C  
ANISOU 4497  C   TRP B 161    11522  10936  10880    691    540   -730       C  
ATOM   4498  O   TRP B 161     -70.709  19.892  37.772  1.00 87.17           O  
ANISOU 4498  O   TRP B 161    11397  10841  10882    652    514   -654       O  
ATOM   4499  CB  TRP B 161     -71.076  18.323  40.612  1.00 82.13           C  
ANISOU 4499  CB  TRP B 161    10485  10683  10037    704    879   -758       C  
ATOM   4500  CG  TRP B 161     -70.931  16.869  40.933  1.00 81.72           C  
ANISOU 4500  CG  TRP B 161    10293  10802   9956    535   1044   -632       C  
ATOM   4501  CD1 TRP B 161     -70.581  16.327  42.132  1.00 84.79           C  
ANISOU 4501  CD1 TRP B 161    10666  11317  10232    485   1140   -613       C  
ATOM   4502  CD2 TRP B 161     -71.104  15.771  40.030  1.00 80.18           C  
ANISOU 4502  CD2 TRP B 161     9991  10636   9839    393   1100   -504       C  
ATOM   4503  NE1 TRP B 161     -70.535  14.957  42.037  1.00 83.39           N  
ANISOU 4503  NE1 TRP B 161    10396  11222  10066    320   1238   -467       N  
ATOM   4504  CE2 TRP B 161     -70.858  14.587  40.758  1.00 83.92           C  
ANISOU 4504  CE2 TRP B 161    10410  11223  10254    264   1214   -411       C  
ATOM   4505  CE3 TRP B 161     -71.464  15.670  38.676  1.00 80.57           C  
ANISOU 4505  CE3 TRP B 161     9999  10620   9993    364   1049   -464       C  
ATOM   4506  CZ2 TRP B 161     -70.948  13.316  40.176  1.00 82.42           C  
ANISOU 4506  CZ2 TRP B 161    10152  11045  10120    115   1258   -290       C  
ATOM   4507  CZ3 TRP B 161     -71.564  14.411  38.103  1.00 81.09           C  
ANISOU 4507  CZ3 TRP B 161     9973  10735  10105    219   1113   -360       C  
ATOM   4508  CH2 TRP B 161     -71.302  13.252  38.847  1.00 81.46           C  
ANISOU 4508  CH2 TRP B 161     9991  10857  10105     99   1207   -280       C  
ATOM   4509  N   ILE B 162     -70.347  21.296  39.514  1.00 85.53           N  
ANISOU 4509  N   ILE B 162    11432  10498  10566    843    388   -867       N  
ATOM   4510  CA  ILE B 162     -70.717  22.502  38.762  1.00 86.89           C  
ANISOU 4510  CA  ILE B 162    11794  10420  10801    968    156   -915       C  
ATOM   4511  C   ILE B 162     -69.691  22.797  37.645  1.00 90.13           C  
ANISOU 4511  C   ILE B 162    12368  10618  11261    695     22   -722       C  
ATOM   4512  O   ILE B 162     -70.130  22.938  36.504  1.00 89.97           O  
ANISOU 4512  O   ILE B 162    12350  10534  11300    695    -55   -648       O  
ATOM   4513  CB  ILE B 162     -71.082  23.729  39.652  1.00 92.93           C  
ANISOU 4513  CB  ILE B 162    12752  11039  11518   1244    -10  -1142       C  
ATOM   4514  CG1 ILE B 162     -72.169  23.401  40.724  1.00 94.90           C  
ANISOU 4514  CG1 ILE B 162    12779  11601  11675   1526    150  -1348       C  
ATOM   4515  CG2 ILE B 162     -71.454  24.966  38.822  1.00 95.69           C  
ANISOU 4515  CG2 ILE B 162    13349  11068  11942   1386   -298  -1180       C  
ATOM   4516  CD1 ILE B 162     -73.569  22.773  40.231  1.00102.09           C  
ANISOU 4516  CD1 ILE B 162    13383  12798  12609   1679    279  -1375       C  
ATOM   4517  N   PRO B 163     -68.346  22.797  37.892  1.00 86.01           N  
ANISOU 4517  N   PRO B 163    11940  10044  10695    447      6   -625       N  
ATOM   4518  CA  PRO B 163     -67.396  23.032  36.788  1.00 85.35           C  
ANISOU 4518  CA  PRO B 163    11955   9853  10623    163   -100   -434       C  
ATOM   4519  C   PRO B 163     -67.456  21.991  35.670  1.00 87.12           C  
ANISOU 4519  C   PRO B 163    11968  10261  10874     52     35   -302       C  
ATOM   4520  O   PRO B 163     -67.263  22.349  34.506  1.00 86.92           O  
ANISOU 4520  O   PRO B 163    12012  10158  10855    -83    -73   -177       O  
ATOM   4521  CB  PRO B 163     -66.031  23.022  37.488  1.00 86.83           C  
ANISOU 4521  CB  PRO B 163    12192  10065  10735    -54    -96   -390       C  
ATOM   4522  CG  PRO B 163     -66.331  23.365  38.895  1.00 92.42           C  
ANISOU 4522  CG  PRO B 163    12970  10741  11404    144   -101   -578       C  
ATOM   4523  CD  PRO B 163     -67.612  22.646  39.165  1.00 87.48           C  
ANISOU 4523  CD  PRO B 163    12139  10299  10799    404     70   -685       C  
ATOM   4524  N   ALA B 164     -67.759  20.717  36.011  1.00 81.90           N  
ANISOU 4524  N   ALA B 164    11069   9834  10216    106    254   -330       N  
ATOM   4525  CA  ALA B 164     -67.873  19.623  35.045  1.00 80.27           C  
ANISOU 4525  CA  ALA B 164    10678   9786  10036     28    370   -242       C  
ATOM   4526  C   ALA B 164     -68.996  19.899  34.055  1.00 85.80           C  
ANISOU 4526  C   ALA B 164    11363  10441  10795    137    301   -246       C  
ATOM   4527  O   ALA B 164     -68.841  19.613  32.867  1.00 85.54           O  
ANISOU 4527  O   ALA B 164    11291  10447  10766     20    286   -145       O  
ATOM   4528  CB  ALA B 164     -68.116  18.306  35.760  1.00 79.72           C  
ANISOU 4528  CB  ALA B 164    10420   9907   9964     74    567   -280       C  
ATOM   4529  N   LEU B 165     -70.099  20.509  34.537  1.00 83.73           N  
ANISOU 4529  N   LEU B 165    11131  10122  10563    376    245   -375       N  
ATOM   4530  CA  LEU B 165     -71.248  20.884  33.715  1.00 84.36           C  
ANISOU 4530  CA  LEU B 165    11190  10170  10695    533    152   -404       C  
ATOM   4531  C   LEU B 165     -70.922  22.112  32.875  1.00 88.20           C  
ANISOU 4531  C   LEU B 165    11936  10393  11184    484    -99   -322       C  
ATOM   4532  O   LEU B 165     -71.190  22.110  31.679  1.00 87.67           O  
ANISOU 4532  O   LEU B 165    11860  10319  11131    433   -167   -227       O  
ATOM   4533  CB  LEU B 165     -72.498  21.117  34.581  1.00 86.05           C  
ANISOU 4533  CB  LEU B 165    11313  10468  10915    836    174   -593       C  
ATOM   4534  CG  LEU B 165     -73.064  19.876  35.280  1.00 90.29           C  
ANISOU 4534  CG  LEU B 165    11572  11306  11429    847    413   -640       C  
ATOM   4535  CD1 LEU B 165     -73.857  20.260  36.517  1.00 92.53           C  
ANISOU 4535  CD1 LEU B 165    11789  11713  11653   1098    451   -828       C  
ATOM   4536  CD2 LEU B 165     -73.910  19.030  34.324  1.00 92.57           C  
ANISOU 4536  CD2 LEU B 165    11653  11756  11764    813    478   -591       C  
ATOM   4537  N   LEU B 166     -70.293  23.137  33.482  1.00 85.33           N  
ANISOU 4537  N   LEU B 166    11820   9808  10795    467   -251   -343       N  
ATOM   4538  CA  LEU B 166     -69.898  24.361  32.775  1.00 86.95           C  
ANISOU 4538  CA  LEU B 166    12328   9715  10994    365   -527   -237       C  
ATOM   4539  C   LEU B 166     -68.935  24.043  31.624  1.00 90.27           C  
ANISOU 4539  C   LEU B 166    12732  10206  11359     14   -515     -6       C  
ATOM   4540  O   LEU B 166     -68.971  24.706  30.588  1.00 91.03           O  
ANISOU 4540  O   LEU B 166    12986  10160  11439    -80   -701    127       O  
ATOM   4541  CB  LEU B 166     -69.279  25.396  33.738  1.00 88.60           C  
ANISOU 4541  CB  LEU B 166    12815   9672  11179    357   -694   -302       C  
ATOM   4542  CG  LEU B 166     -70.162  25.916  34.884  1.00 94.65           C  
ANISOU 4542  CG  LEU B 166    13639  10358  11966    734   -748   -563       C  
ATOM   4543  CD1 LEU B 166     -69.315  26.532  35.973  1.00 95.86           C  
ANISOU 4543  CD1 LEU B 166    13999  10353  12071    668   -835   -636       C  
ATOM   4544  CD2 LEU B 166     -71.208  26.914  34.394  1.00 99.12           C  
ANISOU 4544  CD2 LEU B 166    14389  10686  12587   1025  -1006   -647       C  
ATOM   4545  N   LEU B 167     -68.118  22.988  31.795  1.00 85.33           N  
ANISOU 4545  N   LEU B 167    11904   9828  10689   -159   -300     34       N  
ATOM   4546  CA  LEU B 167     -67.150  22.501  30.812  1.00 84.65           C  
ANISOU 4546  CA  LEU B 167    11732   9909  10522   -451   -245    204       C  
ATOM   4547  C   LEU B 167     -67.815  21.707  29.673  1.00 89.63           C  
ANISOU 4547  C   LEU B 167    12185  10707  11163   -410   -164    235       C  
ATOM   4548  O   LEU B 167     -67.129  21.246  28.753  1.00 88.97           O  
ANISOU 4548  O   LEU B 167    12011  10799  10995   -611   -115    347       O  
ATOM   4549  CB  LEU B 167     -66.098  21.637  31.529  1.00 82.87           C  
ANISOU 4549  CB  LEU B 167    11349   9889  10247   -567    -65    186       C  
ATOM   4550  CG  LEU B 167     -64.666  22.188  31.699  1.00 87.78           C  
ANISOU 4550  CG  LEU B 167    12068  10517  10770   -854   -142    293       C  
ATOM   4551  CD1 LEU B 167     -64.596  23.717  31.675  1.00 90.06           C  
ANISOU 4551  CD1 LEU B 167    12679  10492  11047   -961   -415    365       C  
ATOM   4552  CD2 LEU B 167     -64.041  21.646  32.958  1.00 88.71           C  
ANISOU 4552  CD2 LEU B 167    12093  10737  10876   -824    -19    199       C  
ATOM   4553  N   THR B 168     -69.151  21.578  29.721  1.00 87.29           N  
ANISOU 4553  N   THR B 168    11830  10383  10954   -150   -159    124       N  
ATOM   4554  CA  THR B 168     -69.912  20.843  28.715  1.00 86.57           C  
ANISOU 4554  CA  THR B 168    11572  10442  10878   -103   -101    133       C  
ATOM   4555  C   THR B 168     -70.593  21.734  27.644  1.00 91.28           C  
ANISOU 4555  C   THR B 168    12309  10901  11472    -56   -317    210       C  
ATOM   4556  O   THR B 168     -71.148  21.206  26.677  1.00 90.43           O  
ANISOU 4556  O   THR B 168    12077  10926  11357    -44   -295    233       O  
ATOM   4557  CB  THR B 168     -70.728  19.720  29.382  1.00 92.98           C  
ANISOU 4557  CB  THR B 168    12151  11417  11759     63     90    -11       C  
ATOM   4558  OG1 THR B 168     -70.588  18.539  28.607  1.00 91.98           O  
ANISOU 4558  OG1 THR B 168    11854  11482  11612    -44    209     21       O  
ATOM   4559  CG2 THR B 168     -72.202  20.074  29.614  1.00 91.29           C  
ANISOU 4559  CG2 THR B 168    11895  11176  11617    334     33   -129       C  
ATOM   4560  N   ILE B 169     -70.519  23.077  27.813  1.00 89.45           N  
ANISOU 4560  N   ILE B 169    12359  10388  11240    -33   -549    252       N  
ATOM   4561  CA  ILE B 169     -71.052  24.081  26.880  1.00 91.71           C  
ANISOU 4561  CA  ILE B 169    12855  10473  11517     10   -814    350       C  
ATOM   4562  C   ILE B 169     -70.432  23.915  25.459  1.00 96.41           C  
ANISOU 4562  C   ILE B 169    13448  11194  11987   -291   -839    568       C  
ATOM   4563  O   ILE B 169     -71.213  23.839  24.509  1.00 96.95           O  
ANISOU 4563  O   ILE B 169    13476  11311  12050   -210   -907    600       O  
ATOM   4564  CB  ILE B 169     -70.997  25.534  27.458  1.00 97.39           C  
ANISOU 4564  CB  ILE B 169    13933  10810  12263     90  -1091    343       C  
ATOM   4565  CG1 ILE B 169     -71.784  25.634  28.792  1.00 98.14           C  
ANISOU 4565  CG1 ILE B 169    13985  10852  12453    454  -1054     81       C  
ATOM   4566  CG2 ILE B 169     -71.511  26.573  26.441  1.00100.74           C  
ANISOU 4566  CG2 ILE B 169    14622  10980  12674    131  -1410    470       C  
ATOM   4567  CD1 ILE B 169     -71.394  26.820  29.742  1.00108.12           C  
ANISOU 4567  CD1 ILE B 169    15577  11775  13729    514  -1266     13       C  
ATOM   4568  N   PRO B 170     -69.087  23.739  25.269  1.00 92.39           N  
ANISOU 4568  N   PRO B 170    12932  10810  11360   -625   -766    702       N  
ATOM   4569  CA  PRO B 170     -68.561  23.502  23.904  1.00 92.57           C  
ANISOU 4569  CA  PRO B 170    12900  11045  11228   -888   -763    883       C  
ATOM   4570  C   PRO B 170     -68.982  22.150  23.304  1.00 94.46           C  
ANISOU 4570  C   PRO B 170    12834  11596  11460   -800   -556    786       C  
ATOM   4571  O   PRO B 170     -68.893  21.960  22.094  1.00 94.51           O  
ANISOU 4571  O   PRO B 170    12793  11774  11342   -931   -575    892       O  
ATOM   4572  CB  PRO B 170     -67.039  23.571  24.092  1.00 94.47           C  
ANISOU 4572  CB  PRO B 170    13143  11410  11340  -1223   -705    997       C  
ATOM   4573  CG  PRO B 170     -66.832  24.234  25.417  1.00 99.24           C  
ANISOU 4573  CG  PRO B 170    13917  11752  12038  -1166   -777    925       C  
ATOM   4574  CD  PRO B 170     -67.979  23.774  26.244  1.00 93.37           C  
ANISOU 4574  CD  PRO B 170    13077  10936  11462   -778   -690    692       C  
ATOM   4575  N   ASP B 171     -69.438  21.210  24.150  1.00 89.33           N  
ANISOU 4575  N   ASP B 171    11994  11017  10930   -594   -373    590       N  
ATOM   4576  CA  ASP B 171     -69.930  19.897  23.725  1.00 87.50           C  
ANISOU 4576  CA  ASP B 171    11511  11018  10716   -510   -208    482       C  
ATOM   4577  C   ASP B 171     -71.434  19.982  23.425  1.00 89.39           C  
ANISOU 4577  C   ASP B 171    11722  11194  11049   -281   -295    413       C  
ATOM   4578  O   ASP B 171     -71.948  19.175  22.654  1.00 88.62           O  
ANISOU 4578  O   ASP B 171    11470  11266  10937   -261   -243    373       O  
ATOM   4579  CB  ASP B 171     -69.603  18.816  24.767  1.00 87.97           C  
ANISOU 4579  CB  ASP B 171    11405  11178  10840   -456      5    342       C  
ATOM   4580  CG  ASP B 171     -68.110  18.628  24.986  1.00102.91           C  
ANISOU 4580  CG  ASP B 171    13282  13188  12629   -652     86    393       C  
ATOM   4581  OD1 ASP B 171     -67.529  17.712  24.363  1.00104.05           O  
ANISOU 4581  OD1 ASP B 171    13280  13570  12686   -729    190    376       O  
ATOM   4582  OD2 ASP B 171     -67.520  19.404  25.780  1.00109.62           O  
ANISOU 4582  OD2 ASP B 171    14263  13908  13479   -717     34    436       O  
ATOM   4583  N   PHE B 172     -72.123  20.988  24.004  1.00 84.99           N  
ANISOU 4583  N   PHE B 172    11314  10402  10576    -99   -447    385       N  
ATOM   4584  CA  PHE B 172     -73.537  21.258  23.751  1.00 85.03           C  
ANISOU 4584  CA  PHE B 172    11287  10366  10655    154   -564    311       C  
ATOM   4585  C   PHE B 172     -73.648  21.953  22.391  1.00 88.79           C  
ANISOU 4585  C   PHE B 172    11915  10783  11038     78   -782    477       C  
ATOM   4586  O   PHE B 172     -74.553  21.652  21.616  1.00 89.45           O  
ANISOU 4586  O   PHE B 172    11884  10979  11122    179   -826    452       O  
ATOM   4587  CB  PHE B 172     -74.120  22.204  24.824  1.00 88.24           C  
ANISOU 4587  CB  PHE B 172    11819  10551  11156    414   -680    203       C  
ATOM   4588  CG  PHE B 172     -74.833  21.596  26.009  1.00 89.17           C  
ANISOU 4588  CG  PHE B 172    11724  10794  11365    621   -510      0       C  
ATOM   4589  CD1 PHE B 172     -74.620  22.085  27.293  1.00 92.66           C  
ANISOU 4589  CD1 PHE B 172    12255  11114  11839    730   -499    -98       C  
ATOM   4590  CD2 PHE B 172     -75.775  20.587  25.835  1.00 90.95           C  
ANISOU 4590  CD2 PHE B 172    11662  11269  11624    696   -380    -91       C  
ATOM   4591  CE1 PHE B 172     -75.307  21.550  28.388  1.00 93.19           C  
ANISOU 4591  CE1 PHE B 172    12113  11344  11952    909   -338   -274       C  
ATOM   4592  CE2 PHE B 172     -76.449  20.041  26.935  1.00 93.61           C  
ANISOU 4592  CE2 PHE B 172    11794  11757  12016    838   -226   -249       C  
ATOM   4593  CZ  PHE B 172     -76.212  20.529  28.202  1.00 91.88           C  
ANISOU 4593  CZ  PHE B 172    11653  11448  11808    946   -199   -335       C  
ATOM   4594  N   ILE B 173     -72.718  22.884  22.111  1.00 84.48           N  
ANISOU 4594  N   ILE B 173    11630  10071  10397   -127   -931    658       N  
ATOM   4595  CA  ILE B 173     -72.680  23.696  20.898  1.00 85.75           C  
ANISOU 4595  CA  ILE B 173    11996  10144  10440   -256  -1169    868       C  
ATOM   4596  C   ILE B 173     -72.184  22.928  19.655  1.00 87.79           C  
ANISOU 4596  C   ILE B 173    12108  10720  10529   -503  -1065    976       C  
ATOM   4597  O   ILE B 173     -72.883  22.888  18.638  1.00 88.18           O  
ANISOU 4597  O   ILE B 173    12133  10847  10526   -452  -1165   1019       O  
ATOM   4598  CB  ILE B 173     -71.872  25.020  21.157  1.00 90.76           C  
ANISOU 4598  CB  ILE B 173    12994  10463  11029   -429  -1391   1040       C  
ATOM   4599  CG1 ILE B 173     -72.381  25.839  22.387  1.00 92.00           C  
ANISOU 4599  CG1 ILE B 173    13331  10283  11343   -142  -1528    894       C  
ATOM   4600  CG2 ILE B 173     -71.708  25.889  19.901  1.00 94.23           C  
ANISOU 4600  CG2 ILE B 173    13688  10800  11316   -639  -1658   1313       C  
ATOM   4601  CD1 ILE B 173     -73.843  26.376  22.391  1.00101.97           C  
ANISOU 4601  CD1 ILE B 173    14653  11374  12716    277  -1732    765       C  
ATOM   4602  N   PHE B 174     -70.975  22.345  19.733  1.00 82.33           N  
ANISOU 4602  N   PHE B 174    11314  10229   9738   -749   -878   1006       N  
ATOM   4603  CA  PHE B 174     -70.314  21.701  18.597  1.00 81.83           C  
ANISOU 4603  CA  PHE B 174    11116  10500   9474   -978   -783   1089       C  
ATOM   4604  C   PHE B 174     -70.783  20.318  18.135  1.00 84.79           C  
ANISOU 4604  C   PHE B 174    11211  11150   9855   -863   -606    915       C  
ATOM   4605  O   PHE B 174     -70.696  20.045  16.934  1.00 85.36           O  
ANISOU 4605  O   PHE B 174    11227  11449   9758   -975   -623    979       O  
ATOM   4606  CB  PHE B 174     -68.786  21.852  18.672  1.00 83.51           C  
ANISOU 4606  CB  PHE B 174    11347  10855   9530  -1297   -709   1215       C  
ATOM   4607  CG  PHE B 174     -68.345  23.304  18.676  1.00 87.17           C  
ANISOU 4607  CG  PHE B 174    12129  11066   9927  -1512   -951   1455       C  
ATOM   4608  CD1 PHE B 174     -68.041  23.954  19.866  1.00 89.61           C  
ANISOU 4608  CD1 PHE B 174    12599  11093  10355  -1501  -1009   1437       C  
ATOM   4609  CD2 PHE B 174     -68.282  24.033  17.494  1.00 91.77           C  
ANISOU 4609  CD2 PHE B 174    12877  11669  10322  -1733  -1147   1704       C  
ATOM   4610  CE1 PHE B 174     -67.665  25.300  19.872  1.00 93.04           C  
ANISOU 4610  CE1 PHE B 174    13372  11242  10737  -1711  -1272   1653       C  
ATOM   4611  CE2 PHE B 174     -67.914  25.382  17.504  1.00 97.02           C  
ANISOU 4611  CE2 PHE B 174    13885  12046  10930  -1960  -1411   1948       C  
ATOM   4612  CZ  PHE B 174     -67.600  26.003  18.690  1.00 94.93           C  
ANISOU 4612  CZ  PHE B 174    13793  11476  10800  -1950  -1479   1917       C  
ATOM   4613  N   ALA B 175     -71.330  19.479  19.046  1.00 79.21           N  
ANISOU 4613  N   ALA B 175    10348  10419   9327   -655   -462    703       N  
ATOM   4614  CA  ALA B 175     -71.839  18.141  18.702  1.00 77.27           C  
ANISOU 4614  CA  ALA B 175     9875  10377   9108   -566   -328    537       C  
ATOM   4615  C   ALA B 175     -73.123  18.210  17.875  1.00 81.46           C  
ANISOU 4615  C   ALA B 175    10378  10916   9655   -442   -464    525       C  
ATOM   4616  O   ALA B 175     -74.112  18.812  18.304  1.00 81.14           O  
ANISOU 4616  O   ALA B 175    10387  10702   9742   -258   -579    505       O  
ATOM   4617  CB  ALA B 175     -72.058  17.306  19.953  1.00 76.03           C  
ANISOU 4617  CB  ALA B 175     9594  10171   9123   -432   -166    361       C  
ATOM   4618  N   ASN B 176     -73.080  17.624  16.666  1.00 79.04           N  
ANISOU 4618  N   ASN B 176     9989  10841   9202   -529   -463    525       N  
ATOM   4619  CA  ASN B 176     -74.192  17.584  15.710  1.00 80.16           C  
ANISOU 4619  CA  ASN B 176    10088  11047   9321   -443   -596    515       C  
ATOM   4620  C   ASN B 176     -74.209  16.271  14.915  1.00 83.08           C  
ANISOU 4620  C   ASN B 176    10282  11679   9606   -485   -498    375       C  
ATOM   4621  O   ASN B 176     -73.217  15.540  14.906  1.00 81.50           O  
ANISOU 4621  O   ASN B 176    10024  11620   9322   -581   -353    310       O  
ATOM   4622  CB  ASN B 176     -74.130  18.789  14.752  1.00 84.06           C  
ANISOU 4622  CB  ASN B 176    10780  11503   9654   -535   -818    744       C  
ATOM   4623  CG  ASN B 176     -74.417  20.116  15.413  1.00112.53           C  
ANISOU 4623  CG  ASN B 176    14606  14786  13363   -440   -995    859       C  
ATOM   4624  OD1 ASN B 176     -75.575  20.523  15.577  1.00109.32           O  
ANISOU 4624  OD1 ASN B 176    14213  14242  13080   -206  -1138    811       O  
ATOM   4625  ND2 ASN B 176     -73.364  20.808  15.837  1.00104.65           N  
ANISOU 4625  ND2 ASN B 176    13780  13670  12314   -607  -1002    994       N  
ATOM   4626  N   VAL B 177     -75.344  15.977  14.252  1.00 80.74           N  
ANISOU 4626  N   VAL B 177     9902  11448   9327   -395   -597    311       N  
ATOM   4627  CA  VAL B 177     -75.527  14.782  13.417  1.00 80.45           C  
ANISOU 4627  CA  VAL B 177     9727  11630   9211   -428   -555    163       C  
ATOM   4628  C   VAL B 177     -75.356  15.209  11.962  1.00 86.14           C  
ANISOU 4628  C   VAL B 177    10510  12543   9678   -527   -684    281       C  
ATOM   4629  O   VAL B 177     -76.001  16.169  11.534  1.00 86.99           O  
ANISOU 4629  O   VAL B 177    10708  12586   9759   -488   -870    426       O  
ATOM   4630  CB  VAL B 177     -76.898  14.083  13.668  1.00 83.74           C  
ANISOU 4630  CB  VAL B 177     9990  12025   9801   -308   -581     10       C  
ATOM   4631  CG1 VAL B 177     -77.066  12.839  12.795  1.00 83.73           C  
ANISOU 4631  CG1 VAL B 177     9886  12209   9719   -366   -571   -152       C  
ATOM   4632  CG2 VAL B 177     -77.066  13.721  15.140  1.00 81.89           C  
ANISOU 4632  CG2 VAL B 177     9694  11636   9782   -244   -451    -74       C  
ATOM   4633  N   SER B 178     -74.483  14.517  11.213  1.00 83.35           N  
ANISOU 4633  N   SER B 178    10111  12438   9122   -639   -598    217       N  
ATOM   4634  CA  SER B 178     -74.240  14.837   9.806  1.00 85.81           C  
ANISOU 4634  CA  SER B 178    10458  13004   9140   -754   -698    323       C  
ATOM   4635  C   SER B 178     -74.231  13.602   8.911  1.00 90.29           C  
ANISOU 4635  C   SER B 178    10897  13840   9568   -745   -655    103       C  
ATOM   4636  O   SER B 178     -73.831  12.525   9.349  1.00 88.76           O  
ANISOU 4636  O   SER B 178    10620  13661   9444   -694   -518   -110       O  
ATOM   4637  CB  SER B 178     -72.938  15.619   9.643  1.00 90.99           C  
ANISOU 4637  CB  SER B 178    11212  13775   9586   -946   -660    523       C  
ATOM   4638  OG  SER B 178     -71.815  14.767   9.485  1.00101.15           O  
ANISOU 4638  OG  SER B 178    12381  15334  10718  -1006   -483    385       O  
ATOM   4639  N   GLU B 179     -74.636  13.772   7.648  1.00 89.11           N  
ANISOU 4639  N   GLU B 179    10754  13895   9208   -788   -791    151       N  
ATOM   4640  CA  GLU B 179     -74.631  12.688   6.673  1.00 90.29           C  
ANISOU 4640  CA  GLU B 179    10802  14319   9184   -777   -780    -67       C  
ATOM   4641  C   GLU B 179     -73.221  12.554   6.080  1.00 96.11           C  
ANISOU 4641  C   GLU B 179    11512  15400   9605   -886   -659    -75       C  
ATOM   4642  O   GLU B 179     -72.673  13.532   5.564  1.00 98.25           O  
ANISOU 4642  O   GLU B 179    11850  15836   9646  -1046   -695    171       O  
ATOM   4643  CB  GLU B 179     -75.681  12.935   5.575  1.00 93.70           C  
ANISOU 4643  CB  GLU B 179    11240  14858   9502   -772   -984    -20       C  
ATOM   4644  CG  GLU B 179     -76.041  11.691   4.776  1.00105.46           C  
ANISOU 4644  CG  GLU B 179    12628  16542  10900   -726  -1007   -301       C  
ATOM   4645  CD  GLU B 179     -77.172  11.814   3.767  1.00129.78           C  
ANISOU 4645  CD  GLU B 179    15692  19728  13890   -714  -1218   -286       C  
ATOM   4646  OE1 GLU B 179     -77.565  12.953   3.422  1.00130.01           O  
ANISOU 4646  OE1 GLU B 179    15802  19744  13852   -744  -1364    -29       O  
ATOM   4647  OE2 GLU B 179     -77.654  10.755   3.303  1.00120.96           O  
ANISOU 4647  OE2 GLU B 179    14497  18700  12763   -675  -1259   -537       O  
ATOM   4648  N   ALA B 180     -72.624  11.350   6.193  1.00 91.19           N  
ANISOU 4648  N   ALA B 180    10793  14889   8966   -799   -528   -356       N  
ATOM   4649  CA  ALA B 180     -71.299  11.009   5.661  1.00 91.76           C  
ANISOU 4649  CA  ALA B 180    10783  15350   8733   -836   -403   -448       C  
ATOM   4650  C   ALA B 180     -71.188   9.494   5.512  1.00 94.68           C  
ANISOU 4650  C   ALA B 180    11076  15788   9110   -652   -361   -835       C  
ATOM   4651  O   ALA B 180     -71.571   8.766   6.430  1.00 92.45           O  
ANISOU 4651  O   ALA B 180    10820  15178   9129   -537   -348   -983       O  
ATOM   4652  CB  ALA B 180     -70.199  11.533   6.574  1.00 91.36           C  
ANISOU 4652  CB  ALA B 180    10727  15274   8713   -910   -263   -314       C  
ATOM   4653  N   ASP B 181     -70.684   9.025   4.348  1.00 93.09           N  
ANISOU 4653  N   ASP B 181    10797  16011   8564   -627   -357  -1000       N  
ATOM   4654  CA  ASP B 181     -70.513   7.611   3.974  1.00 93.68           C  
ANISOU 4654  CA  ASP B 181    10827  16190   8578   -426   -357  -1403       C  
ATOM   4655  C   ASP B 181     -71.862   6.846   3.956  1.00 96.02           C  
ANISOU 4655  C   ASP B 181    11207  16161   9116   -356   -519  -1565       C  
ATOM   4656  O   ASP B 181     -71.950   5.729   4.481  1.00 94.68           O  
ANISOU 4656  O   ASP B 181    11081  15754   9141   -216   -534  -1825       O  
ATOM   4657  CB  ASP B 181     -69.443   6.917   4.857  1.00 94.73           C  
ANISOU 4657  CB  ASP B 181    10914  16283   8795   -273   -217  -1589       C  
ATOM   4658  CG  ASP B 181     -68.612   5.864   4.146  1.00108.65           C  
ANISOU 4658  CG  ASP B 181    12590  18404  10289    -66   -188  -1961       C  
ATOM   4659  OD1 ASP B 181     -67.366   5.965   4.188  1.00111.28           O  
ANISOU 4659  OD1 ASP B 181    12790  19079  10413    -23    -49  -1992       O  
ATOM   4660  OD2 ASP B 181     -69.204   4.924   3.570  1.00114.43           O  
ANISOU 4660  OD2 ASP B 181    13382  19080  11016     64   -315  -2238       O  
ATOM   4661  N   ASP B 182     -72.914   7.471   3.342  1.00 92.68           N  
ANISOU 4661  N   ASP B 182    10810  15734   8669   -470   -659  -1397       N  
ATOM   4662  CA  ASP B 182     -74.303   6.969   3.224  1.00 92.37           C  
ANISOU 4662  CA  ASP B 182    10811  15461   8826   -456   -829  -1494       C  
ATOM   4663  C   ASP B 182     -74.854   6.559   4.608  1.00 93.46           C  
ANISOU 4663  C   ASP B 182    10986  15140   9386   -429   -810  -1511       C  
ATOM   4664  O   ASP B 182     -75.619   5.601   4.750  1.00 93.38           O  
ANISOU 4664  O   ASP B 182    11002  14930   9548   -404   -908  -1704       O  
ATOM   4665  CB  ASP B 182     -74.401   5.828   2.186  1.00 96.71           C  
ANISOU 4665  CB  ASP B 182    11359  16203   9181   -363   -930  -1844       C  
ATOM   4666  CG  ASP B 182     -75.816   5.493   1.737  1.00107.64           C  
ANISOU 4666  CG  ASP B 182    12764  17465  10670   -409  -1135  -1909       C  
ATOM   4667  OD1 ASP B 182     -76.583   6.432   1.433  1.00108.62           O  
ANISOU 4667  OD1 ASP B 182    12862  17628  10780   -510  -1223  -1660       O  
ATOM   4668  OD2 ASP B 182     -76.150   4.292   1.675  1.00113.18           O  
ANISOU 4668  OD2 ASP B 182    13514  18030  11459   -345  -1228  -2210       O  
ATOM   4669  N   ARG B 183     -74.432   7.316   5.631  1.00 87.41           N  
ANISOU 4669  N   ARG B 183    10226  14224   8763   -459   -689  -1295       N  
ATOM   4670  CA  ARG B 183     -74.706   7.084   7.042  1.00 84.51           C  
ANISOU 4670  CA  ARG B 183     9884  13484   8742   -439   -631  -1275       C  
ATOM   4671  C   ARG B 183     -74.833   8.418   7.772  1.00 86.72           C  
ANISOU 4671  C   ARG B 183    10169  13646   9134   -503   -588   -962       C  
ATOM   4672  O   ARG B 183     -74.492   9.466   7.218  1.00 87.10           O  
ANISOU 4672  O   ARG B 183    10231  13874   8988   -571   -601   -761       O  
ATOM   4673  CB  ARG B 183     -73.506   6.319   7.629  1.00 83.08           C  
ANISOU 4673  CB  ARG B 183     9725  13276   8566   -338   -499  -1444       C  
ATOM   4674  CG  ARG B 183     -73.842   5.334   8.722  1.00 89.50           C  
ANISOU 4674  CG  ARG B 183    10597  13728   9680   -293   -501  -1574       C  
ATOM   4675  CD  ARG B 183     -72.634   5.085   9.597  1.00 93.03           C  
ANISOU 4675  CD  ARG B 183    11068  14117  10163   -199   -361  -1614       C  
ATOM   4676  NE  ARG B 183     -72.701   5.862  10.832  1.00 96.60           N  
ANISOU 4676  NE  ARG B 183    11518  14368  10819   -264   -268  -1379       N  
ATOM   4677  CZ  ARG B 183     -72.220   5.449  11.998  1.00107.62           C  
ANISOU 4677  CZ  ARG B 183    12957  15554  12381   -212   -187  -1401       C  
ATOM   4678  NH1 ARG B 183     -72.326   6.216  13.074  1.00 94.31           N  
ANISOU 4678  NH1 ARG B 183    11266  13714  10854   -269   -109  -1196       N  
ATOM   4679  NH2 ARG B 183     -71.631   4.264  12.099  1.00 92.53           N  
ANISOU 4679  NH2 ARG B 183    11108  13579  10470    -85   -204  -1638       N  
ATOM   4680  N   TYR B 184     -75.306   8.371   9.027  1.00 81.27           N  
ANISOU 4680  N   TYR B 184     9483  12652   8743   -488   -548   -924       N  
ATOM   4681  CA  TYR B 184     -75.380   9.534   9.897  1.00 79.57           C  
ANISOU 4681  CA  TYR B 184     9289  12290   8654   -507   -508   -682       C  
ATOM   4682  C   TYR B 184     -74.235   9.391  10.898  1.00 81.83           C  
ANISOU 4682  C   TYR B 184     9606  12486   8998   -487   -344   -690       C  
ATOM   4683  O   TYR B 184     -74.107   8.355  11.553  1.00 80.30           O  
ANISOU 4683  O   TYR B 184     9412  12158   8939   -438   -287   -855       O  
ATOM   4684  CB  TYR B 184     -76.738   9.630  10.621  1.00 80.19           C  
ANISOU 4684  CB  TYR B 184     9317  12161   8992   -485   -574   -649       C  
ATOM   4685  CG  TYR B 184     -77.947   9.731   9.710  1.00 83.95           C  
ANISOU 4685  CG  TYR B 184     9727  12743   9426   -491   -749   -654       C  
ATOM   4686  CD1 TYR B 184     -78.299  10.940   9.116  1.00 86.97           C  
ANISOU 4686  CD1 TYR B 184    10134  13206   9703   -474   -868   -462       C  
ATOM   4687  CD2 TYR B 184     -78.786   8.639   9.510  1.00 85.65           C  
ANISOU 4687  CD2 TYR B 184     9868  12956   9720   -521   -820   -839       C  
ATOM   4688  CE1 TYR B 184     -79.427  11.047   8.303  1.00 89.40           C  
ANISOU 4688  CE1 TYR B 184    10373  13623   9972   -457  -1046   -466       C  
ATOM   4689  CE2 TYR B 184     -79.917   8.733   8.700  1.00 88.40           C  
ANISOU 4689  CE2 TYR B 184    10131  13428  10028   -535   -990   -848       C  
ATOM   4690  CZ  TYR B 184     -80.236   9.940   8.101  1.00 96.47           C  
ANISOU 4690  CZ  TYR B 184    11158  14558  10938   -487  -1099   -665       C  
ATOM   4691  OH  TYR B 184     -81.354  10.037   7.310  1.00 99.70           O  
ANISOU 4691  OH  TYR B 184    11476  15103  11303   -478  -1284   -674       O  
ATOM   4692  N   ILE B 185     -73.369  10.397  10.956  1.00 78.96           N  
ANISOU 4692  N   ILE B 185     9281  12205   8516   -540   -289   -508       N  
ATOM   4693  CA  ILE B 185     -72.235  10.438  11.872  1.00 78.06           C  
ANISOU 4693  CA  ILE B 185     9181  12046   8432   -538   -146   -489       C  
ATOM   4694  C   ILE B 185     -72.581  11.468  12.940  1.00 81.82           C  
ANISOU 4694  C   ILE B 185     9720  12273   9097   -556   -147   -296       C  
ATOM   4695  O   ILE B 185     -73.053  12.560  12.611  1.00 82.09           O  
ANISOU 4695  O   ILE B 185     9813  12282   9096   -600   -254   -113       O  
ATOM   4696  CB  ILE B 185     -70.896  10.787  11.136  1.00 82.67           C  
ANISOU 4696  CB  ILE B 185     9739  12966   8707   -619    -86   -438       C  
ATOM   4697  CG1 ILE B 185     -70.631   9.902   9.883  1.00 85.38           C  
ANISOU 4697  CG1 ILE B 185    10008  13631   8803   -575   -103   -645       C  
ATOM   4698  CG2 ILE B 185     -69.691  10.807  12.094  1.00 82.49           C  
ANISOU 4698  CG2 ILE B 185     9698  12937   8708   -620     55   -428       C  
ATOM   4699  CD1 ILE B 185     -70.279   8.378  10.094  1.00 94.21           C  
ANISOU 4699  CD1 ILE B 185    11089  14732   9974   -403    -54   -974       C  
ATOM   4700  N   CYS B 186     -72.357  11.112  14.214  1.00 77.64           N  
ANISOU 4700  N   CYS B 186     9192  11551   8755   -505    -47   -345       N  
ATOM   4701  CA  CYS B 186     -72.587  11.989  15.359  1.00 76.30           C  
ANISOU 4701  CA  CYS B 186     9078  11159   8753   -495    -32   -207       C  
ATOM   4702  C   CYS B 186     -71.273  12.247  16.100  1.00 77.47           C  
ANISOU 4702  C   CYS B 186     9260  11308   8866   -537     80   -156       C  
ATOM   4703  O   CYS B 186     -70.731  11.332  16.724  1.00 75.80           O  
ANISOU 4703  O   CYS B 186     9011  11077   8711   -486    180   -287       O  
ATOM   4704  CB  CYS B 186     -73.671  11.422  16.279  1.00 76.00           C  
ANISOU 4704  CB  CYS B 186     8994  10927   8956   -415    -22   -295       C  
ATOM   4705  SG  CYS B 186     -73.522  11.904  18.028  1.00 78.51           S  
ANISOU 4705  SG  CYS B 186     9349  11022   9458   -372     73   -230       S  
ATOM   4706  N   ASP B 187     -70.749  13.483  15.981  1.00 74.30           N  
ANISOU 4706  N   ASP B 187     8941  10932   8359   -643     39     39       N  
ATOM   4707  CA  ASP B 187     -69.565  13.988  16.690  1.00 74.06           C  
ANISOU 4707  CA  ASP B 187     8947  10903   8288   -727    114    126       C  
ATOM   4708  C   ASP B 187     -69.514  15.515  16.771  1.00 76.46           C  
ANISOU 4708  C   ASP B 187     9405  11085   8562   -847      0    362       C  
ATOM   4709  O   ASP B 187     -70.471  16.169  16.364  1.00 76.92           O  
ANISOU 4709  O   ASP B 187     9549  11025   8653   -817   -143    447       O  
ATOM   4710  CB  ASP B 187     -68.223  13.338  16.262  1.00 77.05           C  
ANISOU 4710  CB  ASP B 187     9217  11594   8465   -782    221     45       C  
ATOM   4711  CG  ASP B 187     -67.629  13.796  14.953  1.00 91.28           C  
ANISOU 4711  CG  ASP B 187    10987  13728   9966   -943    184    149       C  
ATOM   4712  OD1 ASP B 187     -68.348  13.775  13.940  1.00 93.44           O  
ANISOU 4712  OD1 ASP B 187    11268  14075  10159   -942     96    153       O  
ATOM   4713  OD2 ASP B 187     -66.413  14.071  14.922  1.00 98.77           O  
ANISOU 4713  OD2 ASP B 187    11878  14911  10738  -1074    250    214       O  
ATOM   4714  N   ARG B 188     -68.439  16.075  17.350  1.00 71.00           N  
ANISOU 4714  N   ARG B 188     8760  10399   7818   -972     41    460       N  
ATOM   4715  CA  ARG B 188     -68.277  17.522  17.492  1.00 70.93           C  
ANISOU 4715  CA  ARG B 188     8941  10229   7780  -1117    -96    686       C  
ATOM   4716  C   ARG B 188     -67.650  18.109  16.227  1.00 74.62           C  
ANISOU 4716  C   ARG B 188     9443  10946   7964  -1367   -176    878       C  
ATOM   4717  O   ARG B 188     -66.509  17.782  15.881  1.00 74.21           O  
ANISOU 4717  O   ARG B 188     9263  11224   7711  -1519    -69    882       O  
ATOM   4718  CB  ARG B 188     -67.448  17.869  18.745  1.00 69.79           C  
ANISOU 4718  CB  ARG B 188     8843   9964   7709  -1168    -38    705       C  
ATOM   4719  CG  ARG B 188     -68.052  17.405  20.063  1.00 73.73           C  
ANISOU 4719  CG  ARG B 188     9324  10232   8457   -946     34    545       C  
ATOM   4720  CD  ARG B 188     -66.976  17.104  21.088  1.00 82.39           C  
ANISOU 4720  CD  ARG B 188    10369  11370   9567   -983    158    496       C  
ATOM   4721  NE  ARG B 188     -66.237  15.877  20.775  1.00 90.48           N  
ANISOU 4721  NE  ARG B 188    11201  12682  10497   -964    301    366       N  
ATOM   4722  CZ  ARG B 188     -64.954  15.682  21.058  1.00103.57           C  
ANISOU 4722  CZ  ARG B 188    12769  14536  12045  -1053    384    358       C  
ATOM   4723  NH1 ARG B 188     -64.364  14.538  20.734  1.00 82.95           N  
ANISOU 4723  NH1 ARG B 188     9986  12182   9349   -971    489    207       N  
ATOM   4724  NH2 ARG B 188     -64.247  16.631  21.661  1.00 96.74           N  
ANISOU 4724  NH2 ARG B 188    11988  13618  11150  -1213    345    489       N  
ATOM   4725  N   PHE B 189     -68.418  18.947  15.521  1.00 71.96           N  
ANISOU 4725  N   PHE B 189     9265  10485   7592  -1402   -369   1033       N  
ATOM   4726  CA  PHE B 189     -67.980  19.593  14.287  1.00 74.14           C  
ANISOU 4726  CA  PHE B 189     9610  10974   7584  -1662   -479   1258       C  
ATOM   4727  C   PHE B 189     -67.603  21.039  14.577  1.00 81.83           C  
ANISOU 4727  C   PHE B 189    10854  11706   8532  -1884   -662   1531       C  
ATOM   4728  O   PHE B 189     -68.474  21.867  14.864  1.00 82.01           O  
ANISOU 4728  O   PHE B 189    11103  11346   8709  -1771   -862   1602       O  
ATOM   4729  CB  PHE B 189     -69.057  19.482  13.188  1.00 76.14           C  
ANISOU 4729  CB  PHE B 189     9876  11269   7786  -1565   -598   1261       C  
ATOM   4730  CG  PHE B 189     -69.356  18.062  12.768  1.00 75.50           C  
ANISOU 4730  CG  PHE B 189     9555  11435   7697  -1397   -448    997       C  
ATOM   4731  CD1 PHE B 189     -68.594  17.434  11.790  1.00 78.81           C  
ANISOU 4731  CD1 PHE B 189     9817  12290   7837  -1515   -349    954       C  
ATOM   4732  CD2 PHE B 189     -70.402  17.352  13.348  1.00 75.21           C  
ANISOU 4732  CD2 PHE B 189     9452  11208   7918  -1130   -419    787       C  
ATOM   4733  CE1 PHE B 189     -68.863  16.114  11.412  1.00 78.71           C  
ANISOU 4733  CE1 PHE B 189     9623  12463   7822  -1340   -244    683       C  
ATOM   4734  CE2 PHE B 189     -70.663  16.031  12.974  1.00 77.03           C  
ANISOU 4734  CE2 PHE B 189     9500  11621   8145  -1011   -315    552       C  
ATOM   4735  CZ  PHE B 189     -69.902  15.429  11.996  1.00 76.16           C  
ANISOU 4735  CZ  PHE B 189     9276  11888   7774  -1103   -242    494       C  
ATOM   4736  N   TYR B 190     -66.289  21.322  14.551  1.00 80.85           N  
ANISOU 4736  N   TYR B 190    10701  11808   8211  -2192   -605   1668       N  
ATOM   4737  CA  TYR B 190     -65.717  22.643  14.828  1.00 83.20           C  
ANISOU 4737  CA  TYR B 190    11256  11902   8452  -2487   -783   1942       C  
ATOM   4738  C   TYR B 190     -65.526  23.445  13.525  1.00 92.50           C  
ANISOU 4738  C   TYR B 190    12579  13232   9334  -2823   -963   2259       C  
ATOM   4739  O   TYR B 190     -65.324  22.832  12.473  1.00 92.56           O  
ANISOU 4739  O   TYR B 190    12388  13680   9103  -2894   -860   2249       O  
ATOM   4740  CB  TYR B 190     -64.394  22.510  15.619  1.00 83.44           C  
ANISOU 4740  CB  TYR B 190    11158  12112   8433  -2670   -630   1922       C  
ATOM   4741  CG  TYR B 190     -64.549  21.777  16.937  1.00 81.56           C  
ANISOU 4741  CG  TYR B 190    10810  11711   8467  -2361   -476   1644       C  
ATOM   4742  CD1 TYR B 190     -64.269  20.418  17.039  1.00 81.31           C  
ANISOU 4742  CD1 TYR B 190    10475  11981   8437  -2181   -235   1394       C  
ATOM   4743  CD2 TYR B 190     -65.008  22.436  18.073  1.00 81.54           C  
ANISOU 4743  CD2 TYR B 190    11026  11246   8708  -2237   -591   1626       C  
ATOM   4744  CE1 TYR B 190     -64.422  19.736  18.246  1.00 78.24           C  
ANISOU 4744  CE1 TYR B 190    10013  11432   8283  -1924   -115   1172       C  
ATOM   4745  CE2 TYR B 190     -65.185  21.760  19.280  1.00 79.49           C  
ANISOU 4745  CE2 TYR B 190    10663  10871   8668  -1970   -448   1386       C  
ATOM   4746  CZ  TYR B 190     -64.889  20.411  19.362  1.00 83.23           C  
ANISOU 4746  CZ  TYR B 190    10844  11642   9136  -1833   -212   1179       C  
ATOM   4747  OH  TYR B 190     -65.063  19.752  20.553  1.00 81.71           O  
ANISOU 4747  OH  TYR B 190    10578  11323   9143  -1600    -92    978       O  
ATOM   4748  N   PRO B 191     -65.611  24.801  13.547  1.00 93.06           N  
ANISOU 4748  N   PRO B 191    13014  12943   9403  -3028  -1251   2541       N  
ATOM   4749  CA  PRO B 191     -65.454  25.558  12.290  1.00 97.15           C  
ANISOU 4749  CA  PRO B 191    13701  13591   9621  -3378  -1447   2880       C  
ATOM   4750  C   PRO B 191     -64.009  25.708  11.818  1.00104.41           C  
ANISOU 4750  C   PRO B 191    14492  14990  10188  -3884  -1355   3098       C  
ATOM   4751  O   PRO B 191     -63.775  25.996  10.643  1.00107.64           O  
ANISOU 4751  O   PRO B 191    14921  15701  10276  -4186  -1429   3344       O  
ATOM   4752  CB  PRO B 191     -66.087  26.913  12.611  1.00100.89           C  
ANISOU 4752  CB  PRO B 191    14645  13440  10250  -3381  -1818   3081       C  
ATOM   4753  CG  PRO B 191     -65.900  27.078  14.072  1.00103.28           C  
ANISOU 4753  CG  PRO B 191    15008  13413  10819  -3245  -1788   2924       C  
ATOM   4754  CD  PRO B 191     -65.850  25.704  14.693  1.00 94.63           C  
ANISOU 4754  CD  PRO B 191    13510  12592   9851  -2952  -1433   2562       C  
ATOM   4755  N   ASN B 192     -63.052  25.521  12.735  1.00 99.90           N  
ANISOU 4755  N   ASN B 192    13777  14523   9658  -3981  -1197   3012       N  
ATOM   4756  CA  ASN B 192     -61.624  25.658  12.470  1.00102.35           C  
ANISOU 4756  CA  ASN B 192    13915  15327   9647  -4453  -1098   3191       C  
ATOM   4757  C   ASN B 192     -60.817  24.637  13.284  1.00104.03           C  
ANISOU 4757  C   ASN B 192    13749  15864   9915  -4301   -790   2892       C  
ATOM   4758  O   ASN B 192     -61.356  24.003  14.196  1.00100.07           O  
ANISOU 4758  O   ASN B 192    13202  15095   9724  -3881   -696   2597       O  
ATOM   4759  CB  ASN B 192     -61.181  27.090  12.818  1.00107.37           C  
ANISOU 4759  CB  ASN B 192    14930  15608  10258  -4886  -1385   3541       C  
ATOM   4760  CG  ASN B 192     -59.998  27.607  12.036  1.00142.37           C  
ANISOU 4760  CG  ASN B 192    19297  20530  14268  -5517  -1407   3890       C  
ATOM   4761  OD1 ASN B 192     -59.212  26.855  11.443  1.00139.16           O  
ANISOU 4761  OD1 ASN B 192    18477  20832  13567  -5642  -1149   3834       O  
ATOM   4762  ND2 ASN B 192     -59.833  28.921  12.036  1.00139.83           N  
ANISOU 4762  ND2 ASN B 192    19386  19849  13894  -5936  -1730   4258       N  
ATOM   4763  N   ASP B 193     -59.521  24.490  12.956  1.00102.85           N  
ANISOU 4763  N   ASP B 193    13320  16311   9445  -4649   -645   2978       N  
ATOM   4764  CA  ASP B 193     -58.607  23.587  13.657  1.00100.89           C  
ANISOU 4764  CA  ASP B 193    12703  16428   9202  -4527   -381   2717       C  
ATOM   4765  C   ASP B 193     -58.006  24.264  14.891  1.00102.97           C  
ANISOU 4765  C   ASP B 193    13099  16409   9617  -4705   -461   2791       C  
ATOM   4766  O   ASP B 193     -57.375  23.594  15.719  1.00100.77           O  
ANISOU 4766  O   ASP B 193    12572  16303   9414  -4551   -282   2568       O  
ATOM   4767  CB  ASP B 193     -57.527  23.048  12.707  1.00105.76           C  
ANISOU 4767  CB  ASP B 193    12907  17890   9387  -4753   -184   2726       C  
ATOM   4768  CG  ASP B 193     -58.100  22.201  11.587  1.00118.16           C  
ANISOU 4768  CG  ASP B 193    14320  19758  10816  -4502    -85   2568       C  
ATOM   4769  OD1 ASP B 193     -58.049  22.651  10.414  1.00122.37           O  
ANISOU 4769  OD1 ASP B 193    14876  20596  11022  -4811   -157   2813       O  
ATOM   4770  OD2 ASP B 193     -58.631  21.099  11.884  1.00120.20           O  
ANISOU 4770  OD2 ASP B 193    14456  19926  11287  -4013     47   2210       O  
ATOM   4771  N   LEU B 194     -58.238  25.592  15.028  1.00100.14           N  
ANISOU 4771  N   LEU B 194    13160  15580   9309  -5007   -756   3095       N  
ATOM   4772  CA  LEU B 194     -57.803  26.383  16.179  1.00 99.64           C  
ANISOU 4772  CA  LEU B 194    13309  15149   9402  -5183   -895   3173       C  
ATOM   4773  C   LEU B 194     -58.663  26.011  17.389  1.00 98.35           C  
ANISOU 4773  C   LEU B 194    13256  14458   9653  -4653   -875   2862       C  
ATOM   4774  O   LEU B 194     -58.134  25.891  18.494  1.00 96.30           O  
ANISOU 4774  O   LEU B 194    12927  14145   9516  -4607   -808   2732       O  
ATOM   4775  CB  LEU B 194     -57.910  27.895  15.903  1.00103.34           C  
ANISOU 4775  CB  LEU B 194    14254  15203   9809  -5627  -1264   3571       C  
ATOM   4776  CG  LEU B 194     -57.159  28.465  14.702  1.00112.39           C  
ANISOU 4776  CG  LEU B 194    15373  16802  10526  -6239  -1343   3961       C  
ATOM   4777  CD1 LEU B 194     -57.538  29.907  14.489  1.00116.18           C  
ANISOU 4777  CD1 LEU B 194    16422  16708  11015  -6586  -1762   4338       C  
ATOM   4778  CD2 LEU B 194     -55.643  28.338  14.859  1.00116.40           C  
ANISOU 4778  CD2 LEU B 194    15521  17947  10760  -6668  -1177   4031       C  
ATOM   4779  N   TRP B 195     -59.991  25.813  17.164  1.00 92.40           N  
ANISOU 4779  N   TRP B 195    12652  13363   9093  -4263   -932   2747       N  
ATOM   4780  CA  TRP B 195     -60.970  25.404  18.176  1.00 88.26           C  
ANISOU 4780  CA  TRP B 195    12198  12409   8929  -3756   -901   2458       C  
ATOM   4781  C   TRP B 195     -60.612  24.024  18.701  1.00 87.63           C  
ANISOU 4781  C   TRP B 195    11724  12667   8904  -3477   -586   2146       C  
ATOM   4782  O   TRP B 195     -60.635  23.817  19.911  1.00 84.73           O  
ANISOU 4782  O   TRP B 195    11362  12083   8750  -3271   -534   1970       O  
ATOM   4783  CB  TRP B 195     -62.386  25.384  17.591  1.00 86.54           C  
ANISOU 4783  CB  TRP B 195    12132  11918   8833  -3449  -1008   2417       C  
ATOM   4784  CG  TRP B 195     -62.971  26.739  17.334  1.00 90.67           C  
ANISOU 4784  CG  TRP B 195    13104  11960   9386  -3580  -1365   2667       C  
ATOM   4785  CD1 TRP B 195     -62.988  27.413  16.149  1.00 96.83           C  
ANISOU 4785  CD1 TRP B 195    14058  12791   9942  -3883  -1558   2971       C  
ATOM   4786  CD2 TRP B 195     -63.683  27.556  18.272  1.00 90.59           C  
ANISOU 4786  CD2 TRP B 195    13443  11336   9641  -3371  -1594   2618       C  
ATOM   4787  NE1 TRP B 195     -63.653  28.610  16.293  1.00 98.55           N  
ANISOU 4787  NE1 TRP B 195    14739  12421  10283  -3875  -1917   3126       N  
ATOM   4788  CE2 TRP B 195     -64.092  28.723  17.586  1.00 97.98           C  
ANISOU 4788  CE2 TRP B 195    14776  11937  10513  -3544  -1945   2895       C  
ATOM   4789  CE3 TRP B 195     -64.002  27.424  19.635  1.00 89.58           C  
ANISOU 4789  CE3 TRP B 195    13334  10922   9780  -3048  -1545   2361       C  
ATOM   4790  CZ2 TRP B 195     -64.803  29.751  18.216  1.00 98.66           C  
ANISOU 4790  CZ2 TRP B 195    15284  11395  10806  -3364  -2261   2895       C  
ATOM   4791  CZ3 TRP B 195     -64.710  28.440  20.257  1.00 92.53           C  
ANISOU 4791  CZ3 TRP B 195    14094  10723  10339  -2881  -1831   2355       C  
ATOM   4792  CH2 TRP B 195     -65.103  29.588  19.551  1.00 96.71           C  
ANISOU 4792  CH2 TRP B 195    15022  10909  10814  -3019  -2192   2605       C  
ATOM   4793  N   VAL B 196     -60.235  23.100  17.787  1.00 84.26           N  
ANISOU 4793  N   VAL B 196    10973  12778   8266  -3474   -395   2079       N  
ATOM   4794  CA  VAL B 196     -59.797  21.731  18.083  1.00 82.08           C  
ANISOU 4794  CA  VAL B 196    10331  12858   7996  -3213   -125   1787       C  
ATOM   4795  C   VAL B 196     -58.577  21.821  18.998  1.00 87.49           C  
ANISOU 4795  C   VAL B 196    10890  13711   8642  -3382    -59   1782       C  
ATOM   4796  O   VAL B 196     -58.498  21.104  19.992  1.00 84.97           O  
ANISOU 4796  O   VAL B 196    10464  13323   8499  -3106     58   1553       O  
ATOM   4797  CB  VAL B 196     -59.501  20.926  16.781  1.00 87.08           C  
ANISOU 4797  CB  VAL B 196    10676  14061   8348  -3223     15   1735       C  
ATOM   4798  CG1 VAL B 196     -58.820  19.587  17.072  1.00 85.43           C  
ANISOU 4798  CG1 VAL B 196    10108  14243   8111  -2972    254   1435       C  
ATOM   4799  CG2 VAL B 196     -60.774  20.705  15.967  1.00 86.31           C  
ANISOU 4799  CG2 VAL B 196    10691  13789   8315  -3013    -49   1698       C  
ATOM   4800  N   VAL B 197     -57.671  22.758  18.692  1.00 87.98           N  
ANISOU 4800  N   VAL B 197    10987  13970   8472  -3860   -160   2054       N  
ATOM   4801  CA  VAL B 197     -56.467  23.027  19.470  1.00 89.14           C  
ANISOU 4801  CA  VAL B 197    11018  14306   8544  -4109   -136   2097       C  
ATOM   4802  C   VAL B 197     -56.808  23.596  20.869  1.00 91.34           C  
ANISOU 4802  C   VAL B 197    11588  13993   9125  -4009   -268   2056       C  
ATOM   4803  O   VAL B 197     -56.216  23.151  21.855  1.00 89.71           O  
ANISOU 4803  O   VAL B 197    11226  13869   8990  -3900   -164   1896       O  
ATOM   4804  CB  VAL B 197     -55.483  23.877  18.618  1.00 97.91           C  
ANISOU 4804  CB  VAL B 197    12079  15830   9290  -4706   -220   2428       C  
ATOM   4805  CG1 VAL B 197     -54.707  24.894  19.442  1.00 99.73           C  
ANISOU 4805  CG1 VAL B 197    12465  15911   9518  -5106   -378   2616       C  
ATOM   4806  CG2 VAL B 197     -54.538  22.973  17.837  1.00 99.17           C  
ANISOU 4806  CG2 VAL B 197    11749  16806   9125  -4745     18   2334       C  
ATOM   4807  N   VAL B 198     -57.804  24.518  20.950  1.00 88.31           N  
ANISOU 4807  N   VAL B 198    11617  13028   8909  -3996   -501   2171       N  
ATOM   4808  CA  VAL B 198     -58.269  25.133  22.205  1.00 87.04           C  
ANISOU 4808  CA  VAL B 198    11760  12293   9017  -3858   -650   2107       C  
ATOM   4809  C   VAL B 198     -58.799  24.045  23.146  1.00 86.46           C  
ANISOU 4809  C   VAL B 198    11534  12138   9179  -3353   -457   1773       C  
ATOM   4810  O   VAL B 198     -58.305  23.907  24.269  1.00 85.25           O  
ANISOU 4810  O   VAL B 198    11332  11951   9109  -3299   -407   1659       O  
ATOM   4811  CB  VAL B 198     -59.329  26.271  21.990  1.00 92.36           C  
ANISOU 4811  CB  VAL B 198    12897  12384   9812  -3859   -952   2256       C  
ATOM   4812  CG1 VAL B 198     -59.956  26.723  23.310  1.00 91.05           C  
ANISOU 4812  CG1 VAL B 198    13000  11667   9928  -3585  -1076   2099       C  
ATOM   4813  CG2 VAL B 198     -58.736  27.470  21.264  1.00 96.47           C  
ANISOU 4813  CG2 VAL B 198    13653  12888  10112  -4411  -1201   2623       C  
ATOM   4814  N   PHE B 199     -59.793  23.276  22.676  1.00 80.37           N  
ANISOU 4814  N   PHE B 199    10692  11346   8500  -3014   -362   1634       N  
ATOM   4815  CA  PHE B 199     -60.444  22.248  23.474  1.00 76.89           C  
ANISOU 4815  CA  PHE B 199    10138  10804   8274  -2576   -204   1353       C  
ATOM   4816  C   PHE B 199     -59.625  21.014  23.789  1.00 80.57           C  
ANISOU 4816  C   PHE B 199    10261  11665   8685  -2464     28   1178       C  
ATOM   4817  O   PHE B 199     -59.842  20.413  24.840  1.00 77.74           O  
ANISOU 4817  O   PHE B 199     9869  11171   8496  -2201    112    997       O  
ATOM   4818  CB  PHE B 199     -61.864  21.950  22.976  1.00 77.37           C  
ANISOU 4818  CB  PHE B 199    10271  10659   8467  -2283   -222   1274       C  
ATOM   4819  CG  PHE B 199     -62.732  23.186  22.868  1.00 80.42           C  
ANISOU 4819  CG  PHE B 199    11011  10608   8938  -2306   -480   1409       C  
ATOM   4820  CD1 PHE B 199     -62.769  24.127  23.896  1.00 84.15           C  
ANISOU 4820  CD1 PHE B 199    11744  10699   9530  -2316   -640   1422       C  
ATOM   4821  CD2 PHE B 199     -63.508  23.414  21.741  1.00 83.63           C  
ANISOU 4821  CD2 PHE B 199    11502  10978   9297  -2295   -585   1507       C  
ATOM   4822  CE1 PHE B 199     -63.556  25.278  23.786  1.00 86.87           C  
ANISOU 4822  CE1 PHE B 199    12441  10617   9951  -2292   -914   1521       C  
ATOM   4823  CE2 PHE B 199     -64.310  24.555  21.642  1.00 88.29           C  
ANISOU 4823  CE2 PHE B 199    12433  11148   9965  -2274   -856   1623       C  
ATOM   4824  CZ  PHE B 199     -64.323  25.483  22.661  1.00 87.11           C  
ANISOU 4824  CZ  PHE B 199    12552  10606   9939  -2262  -1025   1624       C  
ATOM   4825  N   GLN B 200     -58.655  20.660  22.930  1.00 80.61           N  
ANISOU 4825  N   GLN B 200    10017  12173   8440  -2657    117   1231       N  
ATOM   4826  CA  GLN B 200     -57.778  19.520  23.192  1.00 80.90           C  
ANISOU 4826  CA  GLN B 200     9725  12610   8403  -2520    307   1048       C  
ATOM   4827  C   GLN B 200     -56.819  19.830  24.330  1.00 88.40           C  
ANISOU 4827  C   GLN B 200    10644  13587   9359  -2641    297   1054       C  
ATOM   4828  O   GLN B 200     -56.591  18.953  25.156  1.00 86.89           O  
ANISOU 4828  O   GLN B 200    10320  13433   9260  -2384    405    862       O  
ATOM   4829  CB  GLN B 200     -57.016  19.076  21.941  1.00 84.28           C  
ANISOU 4829  CB  GLN B 200     9867  13622   8532  -2651    402   1067       C  
ATOM   4830  CG  GLN B 200     -57.751  18.011  21.138  1.00102.68           C  
ANISOU 4830  CG  GLN B 200    12102  16031  10880  -2344    495    890       C  
ATOM   4831  CD  GLN B 200     -57.424  16.610  21.591  1.00123.19           C  
ANISOU 4831  CD  GLN B 200    14478  18794  13534  -1993    642    605       C  
ATOM   4832  OE1 GLN B 200     -57.678  16.213  22.738  1.00115.93           O  
ANISOU 4832  OE1 GLN B 200    13633  17578  12838  -1779    657    489       O  
ATOM   4833  NE2 GLN B 200     -56.881  15.812  20.681  1.00117.97           N  
ANISOU 4833  NE2 GLN B 200    13556  18607  12659  -1911    740    479       N  
ATOM   4834  N   PHE B 201     -56.305  21.084  24.405  1.00 89.25           N  
ANISOU 4834  N   PHE B 201    10902  13637   9373  -3038    142   1280       N  
ATOM   4835  CA  PHE B 201     -55.398  21.543  25.463  1.00 91.03           C  
ANISOU 4835  CA  PHE B 201    11127  13869   9592  -3215     93   1307       C  
ATOM   4836  C   PHE B 201     -56.133  21.637  26.804  1.00 94.44           C  
ANISOU 4836  C   PHE B 201    11796  13786  10302  -2949     41   1177       C  
ATOM   4837  O   PHE B 201     -55.577  21.237  27.831  1.00 93.61           O  
ANISOU 4837  O   PHE B 201    11583  13744  10239  -2848    102   1056       O  
ATOM   4838  CB  PHE B 201     -54.770  22.902  25.103  1.00 96.70           C  
ANISOU 4838  CB  PHE B 201    11994  14612  10137  -3753    -98   1600       C  
ATOM   4839  CG  PHE B 201     -53.617  23.326  25.990  1.00100.31           C  
ANISOU 4839  CG  PHE B 201    12381  15212  10521  -4020   -147   1642       C  
ATOM   4840  CD1 PHE B 201     -53.844  24.023  27.171  1.00103.37           C  
ANISOU 4840  CD1 PHE B 201    13065  15120  11092  -4016   -301   1625       C  
ATOM   4841  CD2 PHE B 201     -52.303  23.055  25.627  1.00105.11           C  
ANISOU 4841  CD2 PHE B 201    12612  16467  10857  -4276    -49   1689       C  
ATOM   4842  CE1 PHE B 201     -52.779  24.426  27.982  1.00106.28           C  
ANISOU 4842  CE1 PHE B 201    13374  15624  11385  -4280   -364   1660       C  
ATOM   4843  CE2 PHE B 201     -51.238  23.466  26.436  1.00109.94           C  
ANISOU 4843  CE2 PHE B 201    13137  17243  11392  -4544   -107   1732       C  
ATOM   4844  CZ  PHE B 201     -51.484  24.147  27.607  1.00107.69           C  
ANISOU 4844  CZ  PHE B 201    13170  16445  11303  -4554   -269   1722       C  
ATOM   4845  N   GLN B 202     -57.377  22.174  26.786  1.00 91.12           N  
ANISOU 4845  N   GLN B 202    11681  12889  10050  -2826    -77   1199       N  
ATOM   4846  CA  GLN B 202     -58.259  22.327  27.949  1.00 89.42           C  
ANISOU 4846  CA  GLN B 202    11686  12217  10074  -2549   -126   1065       C  
ATOM   4847  C   GLN B 202     -58.583  20.954  28.543  1.00 91.86           C  
ANISOU 4847  C   GLN B 202    11793  12613  10497  -2163     79    833       C  
ATOM   4848  O   GLN B 202     -58.683  20.829  29.757  1.00 90.80           O  
ANISOU 4848  O   GLN B 202    11710  12312  10477  -2004     96    718       O  
ATOM   4849  CB  GLN B 202     -59.553  23.053  27.547  1.00 90.75           C  
ANISOU 4849  CB  GLN B 202    12150  11970  10360  -2455   -282   1116       C  
ATOM   4850  CG  GLN B 202     -60.407  23.534  28.716  1.00 98.11           C  
ANISOU 4850  CG  GLN B 202    13329  12453  11494  -2211   -378    991       C  
ATOM   4851  CD  GLN B 202     -61.809  23.873  28.277  1.00116.96           C  
ANISOU 4851  CD  GLN B 202    15900  14537  14002  -1989   -478    972       C  
ATOM   4852  OE1 GLN B 202     -62.599  23.001  27.885  1.00109.50           O  
ANISOU 4852  OE1 GLN B 202    14802  13686  13118  -1746   -343    875       O  
ATOM   4853  NE2 GLN B 202     -62.162  25.148  28.365  1.00112.13           N  
ANISOU 4853  NE2 GLN B 202    15630  13545  13429  -2057   -738   1053       N  
ATOM   4854  N   HIS B 203     -58.720  19.929  27.692  1.00 88.43           N  
ANISOU 4854  N   HIS B 203    11146  12437  10016  -2028    217    770       N  
ATOM   4855  CA  HIS B 203     -58.998  18.572  28.141  1.00 86.69           C  
ANISOU 4855  CA  HIS B 203    10767  12277   9893  -1695    377    570       C  
ATOM   4856  C   HIS B 203     -57.753  17.925  28.745  1.00 89.66           C  
ANISOU 4856  C   HIS B 203    10926  12959  10180  -1690    464    494       C  
ATOM   4857  O   HIS B 203     -57.867  17.295  29.789  1.00 87.92           O  
ANISOU 4857  O   HIS B 203    10702  12630  10073  -1475    518    372       O  
ATOM   4858  CB  HIS B 203     -59.612  17.729  27.009  1.00 87.53           C  
ANISOU 4858  CB  HIS B 203    10765  12506   9986  -1551    454    512       C  
ATOM   4859  CG  HIS B 203     -59.316  16.261  27.090  1.00 90.44           C  
ANISOU 4859  CG  HIS B 203    10921  13087  10356  -1313    594    333       C  
ATOM   4860  ND1 HIS B 203     -59.859  15.468  28.086  1.00 90.78           N  
ANISOU 4860  ND1 HIS B 203    11001  12923  10570  -1061    647    203       N  
ATOM   4861  CD2 HIS B 203     -58.548  15.488  26.285  1.00 93.40           C  
ANISOU 4861  CD2 HIS B 203    11065  13852  10569  -1290    669    264       C  
ATOM   4862  CE1 HIS B 203     -59.399  14.248  27.860  1.00 90.32           C  
ANISOU 4862  CE1 HIS B 203    10771  13080  10466   -899    727     72       C  
ATOM   4863  NE2 HIS B 203     -58.610  14.212  26.785  1.00 92.20           N  
ANISOU 4863  NE2 HIS B 203    10839  13683  10509  -1000    743     82       N  
ATOM   4864  N   ILE B 204     -56.580  18.079  28.108  1.00 87.63           N  
ANISOU 4864  N   ILE B 204    10479  13109   9709  -1925    471    571       N  
ATOM   4865  CA  ILE B 204     -55.321  17.509  28.601  1.00 88.20           C  
ANISOU 4865  CA  ILE B 204    10301  13543   9668  -1912    539    492       C  
ATOM   4866  C   ILE B 204     -54.969  18.109  29.976  1.00 92.59           C  
ANISOU 4866  C   ILE B 204    10979  13908  10294  -1990    462    512       C  
ATOM   4867  O   ILE B 204     -54.617  17.367  30.893  1.00 91.15           O  
ANISOU 4867  O   ILE B 204    10705  13768  10157  -1783    516    384       O  
ATOM   4868  CB  ILE B 204     -54.160  17.625  27.550  1.00 93.90           C  
ANISOU 4868  CB  ILE B 204    10745  14827  10104  -2168    566    570       C  
ATOM   4869  CG1 ILE B 204     -54.489  16.933  26.186  1.00 94.63           C  
ANISOU 4869  CG1 ILE B 204    10702  15153  10098  -2051    649    512       C  
ATOM   4870  CG2 ILE B 204     -52.812  17.144  28.096  1.00 95.63           C  
ANISOU 4870  CG2 ILE B 204    10673  15470  10192  -2151    618    481       C  
ATOM   4871  CD1 ILE B 204     -54.875  15.377  26.181  1.00100.68           C  
ANISOU 4871  CD1 ILE B 204    11366  15923  10964  -1592    756    254       C  
ATOM   4872  N   MET B 205     -55.129  19.438  30.126  1.00 90.85           N  
ANISOU 4872  N   MET B 205    10996  13440  10085  -2269    313    666       N  
ATOM   4873  CA  MET B 205     -54.840  20.149  31.373  1.00 91.23           C  
ANISOU 4873  CA  MET B 205    11201  13276  10187  -2364    207    675       C  
ATOM   4874  C   MET B 205     -55.852  19.841  32.487  1.00 91.25           C  
ANISOU 4874  C   MET B 205    11384  12888  10400  -2033    228    533       C  
ATOM   4875  O   MET B 205     -55.465  19.261  33.503  1.00 89.92           O  
ANISOU 4875  O   MET B 205    11133  12778  10253  -1883    281    427       O  
ATOM   4876  CB  MET B 205     -54.707  21.663  31.134  1.00 96.29           C  
ANISOU 4876  CB  MET B 205    12081  13737  10769  -2765      4    873       C  
ATOM   4877  CG  MET B 205     -53.724  22.321  32.069  1.00102.37           C  
ANISOU 4877  CG  MET B 205    12878  14546  11473  -3014   -107    910       C  
ATOM   4878  SD  MET B 205     -52.110  22.642  31.306  1.00110.81           S  
ANISOU 4878  SD  MET B 205    13649  16212  12240  -3512   -130   1091       S  
ATOM   4879  CE  MET B 205     -51.142  23.110  32.764  1.00108.77           C  
ANISOU 4879  CE  MET B 205    13406  15957  11962  -3677   -243   1055       C  
ATOM   4880  N   VAL B 206     -57.140  20.213  32.287  1.00 85.66           N  
ANISOU 4880  N   VAL B 206    10900  11820   9826  -1918    183    534       N  
ATOM   4881  CA  VAL B 206     -58.231  20.025  33.256  1.00 83.07           C  
ANISOU 4881  CA  VAL B 206    10723  11170   9670  -1624    205    406       C  
ATOM   4882  C   VAL B 206     -58.521  18.544  33.551  1.00 84.70           C  
ANISOU 4882  C   VAL B 206    10751  11496   9936  -1327    381    275       C  
ATOM   4883  O   VAL B 206     -58.621  18.167  34.716  1.00 84.05           O  
ANISOU 4883  O   VAL B 206    10690  11339   9907  -1173    420    186       O  
ATOM   4884  CB  VAL B 206     -59.517  20.834  32.895  1.00 86.42           C  
ANISOU 4884  CB  VAL B 206    11395  11241  10200  -1564     98    430       C  
ATOM   4885  CG1 VAL B 206     -60.613  20.645  33.938  1.00 84.82           C  
ANISOU 4885  CG1 VAL B 206    11291  10800  10138  -1259    136    281       C  
ATOM   4886  CG2 VAL B 206     -59.208  22.321  32.724  1.00 88.51           C  
ANISOU 4886  CG2 VAL B 206    11906  11310  10413  -1850   -128    562       C  
ATOM   4887  N   GLY B 207     -58.641  17.732  32.508  1.00 80.26           N  
ANISOU 4887  N   GLY B 207    10036  11107   9351  -1264    466    269       N  
ATOM   4888  CA  GLY B 207     -58.940  16.309  32.641  1.00 78.66           C  
ANISOU 4888  CA  GLY B 207     9708  10971   9208  -1003    592    152       C  
ATOM   4889  C   GLY B 207     -57.737  15.654  33.297  1.00 82.94           C  
ANISOU 4889  C   GLY B 207    10094  11750   9668   -967    627    100       C  
ATOM   4890  O   GLY B 207     -57.877  15.100  34.393  1.00 82.77           O  
ANISOU 4890  O   GLY B 207    10109  11628   9713   -807    656     34       O  
ATOM   4891  N   LEU B 208     -56.555  15.675  32.643  1.00 79.97           N  
ANISOU 4891  N   LEU B 208     9528  11723   9133  -1108    622    129       N  
ATOM   4892  CA  LEU B 208     -55.371  15.038  33.230  1.00 80.21           C  
ANISOU 4892  CA  LEU B 208     9374  12028   9073  -1038    642     61       C  
ATOM   4893  C   LEU B 208     -54.182  15.662  33.971  1.00 84.48           C  
ANISOU 4893  C   LEU B 208     9838  12759   9501  -1222    577    102       C  
ATOM   4894  O   LEU B 208     -53.729  15.070  34.953  1.00 84.09           O  
ANISOU 4894  O   LEU B 208     9741  12751   9459  -1066    581     27       O  
ATOM   4895  CB  LEU B 208     -54.881  14.248  31.990  1.00 81.12           C  
ANISOU 4895  CB  LEU B 208     9256  12492   9073   -966    701      0       C  
ATOM   4896  CG  LEU B 208     -53.739  13.228  32.182  1.00 86.85           C  
ANISOU 4896  CG  LEU B 208     9736  13569   9694   -774    726   -128       C  
ATOM   4897  CD1 LEU B 208     -54.157  12.060  33.080  1.00 86.07           C  
ANISOU 4897  CD1 LEU B 208     9735  13231   9737   -446    731   -240       C  
ATOM   4898  CD2 LEU B 208     -53.259  12.703  30.845  1.00 89.85           C  
ANISOU 4898  CD2 LEU B 208     9881  14336   9921   -721    773   -204       C  
ATOM   4899  N   ILE B 209     -53.674  16.829  33.511  1.00 81.70           N  
ANISOU 4899  N   ILE B 209     9484  12522   9037  -1568    501    230       N  
ATOM   4900  CA  ILE B 209     -52.516  17.496  34.124  1.00 82.88           C  
ANISOU 4900  CA  ILE B 209     9553  12876   9063  -1811    419    284       C  
ATOM   4901  C   ILE B 209     -52.880  18.044  35.507  1.00 85.04           C  
ANISOU 4901  C   ILE B 209    10073  12791   9446  -1797    337    268       C  
ATOM   4902  O   ILE B 209     -52.294  17.608  36.497  1.00 85.07           O  
ANISOU 4902  O   ILE B 209     9999  12895   9430  -1687    337    195       O  
ATOM   4903  CB  ILE B 209     -51.829  18.563  33.210  1.00 88.36           C  
ANISOU 4903  CB  ILE B 209    10179  13812   9583  -2248    342    452       C  
ATOM   4904  CG1 ILE B 209     -51.323  17.949  31.887  1.00 89.84           C  
ANISOU 4904  CG1 ILE B 209    10061  14472   9603  -2253    442    447       C  
ATOM   4905  CG2 ILE B 209     -50.690  19.289  33.953  1.00 91.03           C  
ANISOU 4905  CG2 ILE B 209    10453  14334   9802  -2543    234    514       C  
ATOM   4906  CD1 ILE B 209     -51.021  18.983  30.764  1.00 99.90           C  
ANISOU 4906  CD1 ILE B 209    11317  15937  10703  -2696    379    652       C  
ATOM   4907  N   LEU B 210     -53.844  18.984  35.567  1.00 79.92           N  
ANISOU 4907  N   LEU B 210     9720  11744   8900  -1881    257    324       N  
ATOM   4908  CA  LEU B 210     -54.294  19.635  36.800  1.00 79.05           C  
ANISOU 4908  CA  LEU B 210     9865  11293   8876  -1851    167    282       C  
ATOM   4909  C   LEU B 210     -54.669  18.690  37.966  1.00 79.48           C  
ANISOU 4909  C   LEU B 210     9916  11274   9007  -1520    257    148       C  
ATOM   4910  O   LEU B 210     -54.122  18.903  39.048  1.00 79.50           O  
ANISOU 4910  O   LEU B 210     9947  11294   8966  -1549    198    111       O  
ATOM   4911  CB  LEU B 210     -55.356  20.716  36.529  1.00 79.35           C  
ANISOU 4911  CB  LEU B 210    10210  10930   9009  -1918     57    329       C  
ATOM   4912  CG  LEU B 210     -55.078  22.118  37.094  1.00 85.96           C  
ANISOU 4912  CG  LEU B 210    11300  11540   9820  -2175   -155    375       C  
ATOM   4913  CD1 LEU B 210     -53.905  22.797  36.379  1.00 88.39           C  
ANISOU 4913  CD1 LEU B 210    11529  12083   9970  -2616   -267    543       C  
ATOM   4914  CD2 LEU B 210     -56.305  22.992  36.963  1.00 88.66           C  
ANISOU 4914  CD2 LEU B 210    11965  11443  10280  -2101   -270    365       C  
ATOM   4915  N   PRO B 211     -55.502  17.620  37.810  1.00 73.27           N  
ANISOU 4915  N   PRO B 211     9094  10430   8314  -1238    384     86       N  
ATOM   4916  CA  PRO B 211     -55.749  16.734  38.961  1.00 71.58           C  
ANISOU 4916  CA  PRO B 211     8890  10166   8142   -989    446      0       C  
ATOM   4917  C   PRO B 211     -54.569  15.814  39.274  1.00 74.50           C  
ANISOU 4917  C   PRO B 211     9047  10843   8419   -915    463    -29       C  
ATOM   4918  O   PRO B 211     -54.329  15.540  40.446  1.00 73.95           O  
ANISOU 4918  O   PRO B 211     9008  10764   8326   -822    445    -66       O  
ATOM   4919  CB  PRO B 211     -57.007  15.954  38.570  1.00 71.84           C  
ANISOU 4919  CB  PRO B 211     8962  10040   8294   -782    548    -28       C  
ATOM   4920  CG  PRO B 211     -57.099  16.047  37.108  1.00 76.21           C  
ANISOU 4920  CG  PRO B 211     9443  10664   8850   -868    559     18       C  
ATOM   4921  CD  PRO B 211     -56.229  17.155  36.608  1.00 73.71           C  
ANISOU 4921  CD  PRO B 211     9108  10470   8428  -1159    458    102       C  
ATOM   4922  N   GLY B 212     -53.828  15.392  38.239  1.00 70.93           N  
ANISOU 4922  N   GLY B 212     8376  10681   7894   -946    486    -19       N  
ATOM   4923  CA  GLY B 212     -52.645  14.541  38.357  1.00 71.46           C  
ANISOU 4923  CA  GLY B 212     8202  11093   7855   -837    485    -73       C  
ATOM   4924  C   GLY B 212     -51.605  15.120  39.292  1.00 76.21           C  
ANISOU 4924  C   GLY B 212     8747  11862   8349   -984    392    -62       C  
ATOM   4925  O   GLY B 212     -51.030  14.396  40.111  1.00 76.56           O  
ANISOU 4925  O   GLY B 212     8711  12026   8354   -806    371   -119       O  
ATOM   4926  N   ILE B 213     -51.410  16.451  39.211  1.00 72.67           N  
ANISOU 4926  N   ILE B 213     8371  11387   7852  -1315    312     18       N  
ATOM   4927  CA  ILE B 213     -50.507  17.213  40.066  1.00 73.49           C  
ANISOU 4927  CA  ILE B 213     8463  11606   7855  -1528    195     37       C  
ATOM   4928  C   ILE B 213     -51.056  17.264  41.497  1.00 74.75           C  
ANISOU 4928  C   ILE B 213     8851  11469   8080  -1388    161    -20       C  
ATOM   4929  O   ILE B 213     -50.303  16.992  42.431  1.00 75.77           O  
ANISOU 4929  O   ILE B 213     8900  11759   8131  -1337    112    -60       O  
ATOM   4930  CB  ILE B 213     -50.210  18.606  39.435  1.00 78.45           C  
ANISOU 4930  CB  ILE B 213     9147  12245   8416  -1957     90    155       C  
ATOM   4931  CG1 ILE B 213     -48.958  18.539  38.530  1.00 81.42           C  
ANISOU 4931  CG1 ILE B 213     9172  13152   8610  -2170     95    213       C  
ATOM   4932  CG2 ILE B 213     -50.046  19.719  40.480  1.00 80.20           C  
ANISOU 4932  CG2 ILE B 213     9585  12265   8621  -2174    -69    167       C  
ATOM   4933  CD1 ILE B 213     -49.162  18.011  37.103  1.00 88.62           C  
ANISOU 4933  CD1 ILE B 213     9924  14249   9499  -2109    210    232       C  
ATOM   4934  N   VAL B 214     -52.369  17.570  41.663  1.00 67.74           N  
ANISOU 4934  N   VAL B 214     8227  10193   7319  -1307    190    -32       N  
ATOM   4935  CA  VAL B 214     -53.052  17.630  42.965  1.00 65.90           C  
ANISOU 4935  CA  VAL B 214     8200   9717   7124  -1161    181    -98       C  
ATOM   4936  C   VAL B 214     -52.907  16.277  43.686  1.00 68.69           C  
ANISOU 4936  C   VAL B 214     8454  10187   7460   -888    252   -134       C  
ATOM   4937  O   VAL B 214     -52.463  16.246  44.834  1.00 68.70           O  
ANISOU 4937  O   VAL B 214     8480  10241   7382   -855    195   -166       O  
ATOM   4938  CB  VAL B 214     -54.532  18.081  42.821  1.00 67.74           C  
ANISOU 4938  CB  VAL B 214     8663   9599   7477  -1086    218   -119       C  
ATOM   4939  CG1 VAL B 214     -55.313  17.866  44.110  1.00 67.09           C  
ANISOU 4939  CG1 VAL B 214     8723   9364   7403   -886    255   -200       C  
ATOM   4940  CG2 VAL B 214     -54.628  19.535  42.380  1.00 68.55           C  
ANISOU 4940  CG2 VAL B 214     8936   9522   7588  -1334     84    -91       C  
ATOM   4941  N   ILE B 215     -53.225  15.170  42.970  1.00 63.78           N  
ANISOU 4941  N   ILE B 215     7734   9599   6901   -704    350   -126       N  
ATOM   4942  CA  ILE B 215     -53.132  13.771  43.412  1.00 62.74           C  
ANISOU 4942  CA  ILE B 215     7544   9525   6770   -442    386   -143       C  
ATOM   4943  C   ILE B 215     -51.688  13.414  43.816  1.00 68.52           C  
ANISOU 4943  C   ILE B 215     8084  10576   7376   -409    299   -166       C  
ATOM   4944  O   ILE B 215     -51.490  12.816  44.876  1.00 68.94           O  
ANISOU 4944  O   ILE B 215     8179  10631   7385   -261    259   -172       O  
ATOM   4945  CB  ILE B 215     -53.712  12.827  42.314  1.00 64.33           C  
ANISOU 4945  CB  ILE B 215     7700   9675   7068   -297    469   -144       C  
ATOM   4946  CG1 ILE B 215     -55.260  12.887  42.285  1.00 62.71           C  
ANISOU 4946  CG1 ILE B 215     7684   9162   6982   -273    551   -124       C  
ATOM   4947  CG2 ILE B 215     -53.212  11.386  42.464  1.00 65.42           C  
ANISOU 4947  CG2 ILE B 215     7753   9914   7190    -41    447   -173       C  
ATOM   4948  CD1 ILE B 215     -55.922  12.579  40.948  1.00 65.23           C  
ANISOU 4948  CD1 ILE B 215     7971   9421   7394   -252    614   -122       C  
ATOM   4949  N   LEU B 216     -50.690  13.783  42.984  1.00 66.29           N  
ANISOU 4949  N   LEU B 216     7578  10594   7016   -553    264   -171       N  
ATOM   4950  CA  LEU B 216     -49.286  13.503  43.294  1.00 68.50           C  
ANISOU 4950  CA  LEU B 216     7617  11253   7158   -525    179   -206       C  
ATOM   4951  C   LEU B 216     -48.808  14.282  44.503  1.00 73.94           C  
ANISOU 4951  C   LEU B 216     8371  11965   7760   -682     76   -197       C  
ATOM   4952  O   LEU B 216     -48.027  13.748  45.290  1.00 74.69           O  
ANISOU 4952  O   LEU B 216     8363  12249   7766   -546      1   -228       O  
ATOM   4953  CB  LEU B 216     -48.353  13.813  42.109  1.00 70.22           C  
ANISOU 4953  CB  LEU B 216     7540  11863   7276   -689    178   -209       C  
ATOM   4954  CG  LEU B 216     -48.144  12.751  41.030  1.00 75.38           C  
ANISOU 4954  CG  LEU B 216     7991  12727   7924   -449    239   -279       C  
ATOM   4955  CD1 LEU B 216     -46.910  13.076  40.215  1.00 77.74           C  
ANISOU 4955  CD1 LEU B 216     7928  13564   8046   -611    223   -298       C  
ATOM   4956  CD2 LEU B 216     -48.030  11.337  41.616  1.00 78.57           C  
ANISOU 4956  CD2 LEU B 216     8401  13098   8355    -36    202   -362       C  
ATOM   4957  N   SER B 217     -49.256  15.554  44.629  1.00 70.43           N  
ANISOU 4957  N   SER B 217     8105  11322   7334   -955     48   -164       N  
ATOM   4958  CA  SER B 217     -48.881  16.453  45.715  1.00 71.36           C  
ANISOU 4958  CA  SER B 217     8327  11416   7369  -1133    -72   -177       C  
ATOM   4959  C   SER B 217     -49.284  15.869  47.068  1.00 76.92           C  
ANISOU 4959  C   SER B 217     9182  11980   8062   -896    -73   -216       C  
ATOM   4960  O   SER B 217     -48.424  15.728  47.936  1.00 78.09           O  
ANISOU 4960  O   SER B 217     9248  12329   8094   -878   -169   -239       O  
ATOM   4961  CB  SER B 217     -49.479  17.841  45.505  1.00 72.42           C  
ANISOU 4961  CB  SER B 217     8690  11277   7551  -1410   -121   -156       C  
ATOM   4962  OG  SER B 217     -48.818  18.522  44.454  1.00 73.06           O  
ANISOU 4962  OG  SER B 217     8634  11540   7585  -1719   -171    -85       O  
ATOM   4963  N   CYS B 218     -50.567  15.457  47.207  1.00 73.26           N  
ANISOU 4963  N   CYS B 218     8913  11219   7703   -721     32   -214       N  
ATOM   4964  CA  CYS B 218     -51.138  14.852  48.410  1.00 73.88           C  
ANISOU 4964  CA  CYS B 218     9142  11174   7754   -523     55   -222       C  
ATOM   4965  C   CYS B 218     -50.352  13.626  48.849  1.00 80.22           C  
ANISOU 4965  C   CYS B 218     9812  12180   8487   -315     10   -197       C  
ATOM   4966  O   CYS B 218     -49.854  13.614  49.970  1.00 81.30           O  
ANISOU 4966  O   CYS B 218     9974  12413   8504   -289    -78   -207       O  
ATOM   4967  CB  CYS B 218     -52.614  14.531  48.206  1.00 72.94           C  
ANISOU 4967  CB  CYS B 218     9184  10780   7750   -409    188   -204       C  
ATOM   4968  SG  CYS B 218     -53.664  15.991  47.989  1.00 76.67           S  
ANISOU 4968  SG  CYS B 218     9851  10994   8286   -568    206   -262       S  
ATOM   4969  N   TYR B 219     -50.170  12.637  47.950  1.00 77.36           N  
ANISOU 4969  N   TYR B 219     9312  11891   8190   -156     46   -180       N  
ATOM   4970  CA  TYR B 219     -49.392  11.426  48.234  1.00 78.63           C  
ANISOU 4970  CA  TYR B 219     9361  12221   8296     95    -33   -177       C  
ATOM   4971  C   TYR B 219     -47.912  11.659  48.502  1.00 85.47           C  
ANISOU 4971  C   TYR B 219     9988  13464   9021     61   -164   -223       C  
ATOM   4972  O   TYR B 219     -47.325  10.905  49.272  1.00 86.62           O  
ANISOU 4972  O   TYR B 219    10105  13721   9085    260   -268   -221       O  
ATOM   4973  CB  TYR B 219     -49.603  10.353  47.163  1.00 79.25           C  
ANISOU 4973  CB  TYR B 219     9377  12256   8477    298     13   -184       C  
ATOM   4974  CG  TYR B 219     -50.929   9.643  47.316  1.00 79.60           C  
ANISOU 4974  CG  TYR B 219     9668  11950   8628    397     89   -118       C  
ATOM   4975  CD1 TYR B 219     -51.845   9.603  46.272  1.00 79.98           C  
ANISOU 4975  CD1 TYR B 219     9755  11829   8806    362    198   -118       C  
ATOM   4976  CD2 TYR B 219     -51.285   9.043  48.521  1.00 80.89           C  
ANISOU 4976  CD2 TYR B 219    10016  11975   8742    493     46    -41       C  
ATOM   4977  CE1 TYR B 219     -53.076   8.965  46.415  1.00 80.00           C  
ANISOU 4977  CE1 TYR B 219     9957  11544   8895    415    263    -51       C  
ATOM   4978  CE2 TYR B 219     -52.523   8.431  48.686  1.00 80.96           C  
ANISOU 4978  CE2 TYR B 219    10232  11705   8823    521    119     43       C  
ATOM   4979  CZ  TYR B 219     -53.413   8.386  47.628  1.00 87.12           C  
ANISOU 4979  CZ  TYR B 219    11029  12332   9741    479    226     34       C  
ATOM   4980  OH  TYR B 219     -54.619   7.753  47.796  1.00 87.33           O  
ANISOU 4980  OH  TYR B 219    11233  12120   9827    479    288    122       O  
ATOM   4981  N   CYS B 220     -47.316  12.703  47.895  1.00 83.68           N  
ANISOU 4981  N   CYS B 220     9595  13443   8755   -207   -175   -252       N  
ATOM   4982  CA  CYS B 220     -45.916  13.062  48.107  1.00 86.80           C  
ANISOU 4982  CA  CYS B 220     9728  14251   9000   -315   -299   -289       C  
ATOM   4983  C   CYS B 220     -45.729  13.550  49.543  1.00 89.60           C  
ANISOU 4983  C   CYS B 220    10218  14572   9254   -396   -406   -288       C  
ATOM   4984  O   CYS B 220     -44.715  13.231  50.163  1.00 91.58           O  
ANISOU 4984  O   CYS B 220    10304  15114   9378   -310   -530   -314       O  
ATOM   4985  CB  CYS B 220     -45.459  14.107  47.088  1.00 88.99           C  
ANISOU 4985  CB  CYS B 220     9829  14733   9250   -658   -285   -284       C  
ATOM   4986  SG  CYS B 220     -43.805  14.796  47.394  1.00 96.94           S  
ANISOU 4986  SG  CYS B 220    10509  16274  10052   -921   -443   -306       S  
ATOM   4987  N   ILE B 221     -46.715  14.295  50.075  1.00 83.10           N  
ANISOU 4987  N   ILE B 221     9686  13415   8473   -532   -367   -275       N  
ATOM   4988  CA  ILE B 221     -46.670  14.803  51.446  1.00 83.38           C  
ANISOU 4988  CA  ILE B 221     9879  13404   8396   -597   -462   -300       C  
ATOM   4989  C   ILE B 221     -46.997  13.679  52.452  1.00 86.30           C  
ANISOU 4989  C   ILE B 221    10368  13701   8722   -293   -463   -263       C  
ATOM   4990  O   ILE B 221     -46.332  13.580  53.485  1.00 87.52           O  
ANISOU 4990  O   ILE B 221    10503  14019   8731   -252   -587   -273       O  
ATOM   4991  CB  ILE B 221     -47.513  16.102  51.647  1.00 85.91           C  
ANISOU 4991  CB  ILE B 221    10458  13434   8751   -832   -447   -338       C  
ATOM   4992  CG1 ILE B 221     -47.203  17.157  50.550  1.00 86.43           C  
ANISOU 4992  CG1 ILE B 221    10447  13527   8867  -1151   -476   -335       C  
ATOM   4993  CG2 ILE B 221     -47.243  16.701  53.037  1.00 89.11           C  
ANISOU 4993  CG2 ILE B 221    10995  13858   9006   -907   -576   -403       C  
ATOM   4994  CD1 ILE B 221     -48.305  18.214  50.272  1.00 89.66           C  
ANISOU 4994  CD1 ILE B 221    11135  13556   9375  -1297   -447   -360       C  
ATOM   4995  N   ILE B 222     -47.998  12.825  52.130  1.00 80.76           N  
ANISOU 4995  N   ILE B 222     9791  12763   8133   -104   -342   -206       N  
ATOM   4996  CA  ILE B 222     -48.437  11.684  52.947  1.00 80.27           C  
ANISOU 4996  CA  ILE B 222     9875  12590   8035    139   -345   -128       C  
ATOM   4997  C   ILE B 222     -47.264  10.734  53.191  1.00 86.71           C  
ANISOU 4997  C   ILE B 222    10526  13651   8768    357   -498   -113       C  
ATOM   4998  O   ILE B 222     -46.947  10.442  54.347  1.00 88.17           O  
ANISOU 4998  O   ILE B 222    10785  13901   8814    439   -607    -77       O  
ATOM   4999  CB  ILE B 222     -49.667  10.952  52.322  1.00 81.14           C  
ANISOU 4999  CB  ILE B 222    10119  12415   8294    244   -203    -62       C  
ATOM   5000  CG1 ILE B 222     -50.947  11.811  52.412  1.00 79.80           C  
ANISOU 5000  CG1 ILE B 222    10126  12025   8168     85    -67    -79       C  
ATOM   5001  CG2 ILE B 222     -49.893   9.566  52.968  1.00 82.56           C  
ANISOU 5001  CG2 ILE B 222    10430  12498   8439    475   -252     51       C  
ATOM   5002  CD1 ILE B 222     -52.046  11.454  51.355  1.00 82.17           C  
ANISOU 5002  CD1 ILE B 222    10472  12108   8642    110     75    -47       C  
ATOM   5003  N   ILE B 223     -46.598  10.291  52.105  1.00 83.71           N  
ANISOU 5003  N   ILE B 223     9915  13435   8454    463   -517   -155       N  
ATOM   5004  CA  ILE B 223     -45.462   9.369  52.194  1.00 86.02           C  
ANISOU 5004  CA  ILE B 223    10020  13992   8673    732   -675   -180       C  
ATOM   5005  C   ILE B 223     -44.215   9.971  52.871  1.00 92.41           C  
ANISOU 5005  C   ILE B 223    10620  15184   9309    639   -821   -235       C  
ATOM   5006  O   ILE B 223     -43.333   9.222  53.293  1.00 94.36           O  
ANISOU 5006  O   ILE B 223    10743  15647   9462    888   -980   -249       O  
ATOM   5007  CB  ILE B 223     -45.179   8.562  50.893  1.00 89.25           C  
ANISOU 5007  CB  ILE B 223    10249  14481   9180    949   -660   -241       C  
ATOM   5008  CG1 ILE B 223     -44.467   9.388  49.814  1.00 90.33           C  
ANISOU 5008  CG1 ILE B 223    10058  14962   9302    757   -609   -337       C  
ATOM   5009  CG2 ILE B 223     -46.425   7.848  50.360  1.00 87.50           C  
ANISOU 5009  CG2 ILE B 223    10268  13858   9119   1045   -552   -182       C  
ATOM   5010  CD1 ILE B 223     -43.020   8.981  49.626  1.00103.90           C  
ANISOU 5010  CD1 ILE B 223    11412  17168  10897    949   -748   -437       C  
ATOM   5011  N   SER B 224     -44.168  11.316  52.997  1.00 88.57           N  
ANISOU 5011  N   SER B 224    10113  14761   8780    286   -791   -267       N  
ATOM   5012  CA  SER B 224     -43.088  12.029  53.679  1.00 90.57           C  
ANISOU 5012  CA  SER B 224    10199  15345   8867    120   -938   -316       C  
ATOM   5013  C   SER B 224     -43.314  11.976  55.199  1.00 93.31           C  
ANISOU 5013  C   SER B 224    10784  15579   9092    169  -1026   -279       C  
ATOM   5014  O   SER B 224     -42.374  11.679  55.934  1.00 95.16           O  
ANISOU 5014  O   SER B 224    10892  16084   9180    277  -1193   -291       O  
ATOM   5015  CB  SER B 224     -42.992  13.473  53.192  1.00 94.90           C  
ANISOU 5015  CB  SER B 224    10689  15948   9422   -303   -905   -357       C  
ATOM   5016  OG  SER B 224     -42.666  13.538  51.812  1.00104.20           O  
ANISOU 5016  OG  SER B 224    11619  17303  10667   -380   -835   -372       O  
ATOM   5017  N   LYS B 225     -44.569  12.215  55.654  1.00 87.02           N  
ANISOU 5017  N   LYS B 225    10311  14418   8336    110   -914   -237       N  
ATOM   5018  CA  LYS B 225     -44.997  12.171  57.061  1.00 86.96           C  
ANISOU 5018  CA  LYS B 225    10547  14306   8189    147   -958   -199       C  
ATOM   5019  C   LYS B 225     -44.900  10.761  57.654  1.00 90.79           C  
ANISOU 5019  C   LYS B 225    11097  14786   8612    469  -1041    -85       C  
ATOM   5020  O   LYS B 225     -44.549  10.620  58.826  1.00 92.26           O  
ANISOU 5020  O   LYS B 225    11354  15081   8618    522  -1169    -54       O  
ATOM   5021  CB  LYS B 225     -46.433  12.709  57.214  1.00 87.54           C  
ANISOU 5021  CB  LYS B 225    10899  14047   8317     33   -791   -198       C  
ATOM   5022  CG  LYS B 225     -46.513  14.121  57.787  1.00104.66           C  
ANISOU 5022  CG  LYS B 225    13165  16207  10395   -225   -824   -317       C  
ATOM   5023  CD  LYS B 225     -46.310  15.196  56.716  1.00115.15           C  
ANISOU 5023  CD  LYS B 225    14393  17512  11845   -481   -811   -398       C  
ATOM   5024  CE  LYS B 225     -45.918  16.525  57.313  1.00126.14           C  
ANISOU 5024  CE  LYS B 225    15856  18943  13127   -747   -944   -518       C  
ATOM   5025  NZ  LYS B 225     -45.598  17.524  56.259  1.00132.77           N  
ANISOU 5025  NZ  LYS B 225    16613  19761  14072  -1038   -974   -556       N  
ATOM   5026  N   LEU B 226     -45.205   9.728  56.842  1.00 85.64           N  
ANISOU 5026  N   LEU B 226    10445  13993   8102    679   -991    -22       N  
ATOM   5027  CA  LEU B 226     -45.153   8.319  57.234  1.00 86.41           C  
ANISOU 5027  CA  LEU B 226    10652  14006   8172    991  -1103     95       C  
ATOM   5028  C   LEU B 226     -43.716   7.810  57.446  1.00 92.10           C  
ANISOU 5028  C   LEU B 226    11146  15057   8791   1220  -1335     53       C  
ATOM   5029  O   LEU B 226     -42.743   8.435  57.018  1.00 92.08           O  
ANISOU 5029  O   LEU B 226    10835  15390   8763   1142  -1379    -72       O  
ATOM   5030  CB  LEU B 226     -45.877   7.461  56.182  1.00 85.06           C  
ANISOU 5030  CB  LEU B 226    10555  13565   8197   1128  -1006    141       C  
ATOM   5031  CG  LEU B 226     -47.298   6.974  56.521  1.00 88.65           C  
ANISOU 5031  CG  LEU B 226    11337  13656   8692   1087   -891    290       C  
ATOM   5032  CD1 LEU B 226     -48.310   8.103  56.460  1.00 86.38           C  
ANISOU 5032  CD1 LEU B 226    11112  13275   8434    799   -680    248       C  
ATOM   5033  CD2 LEU B 226     -47.741   5.883  55.557  1.00 90.92           C  
ANISOU 5033  CD2 LEU B 226    11693  13699   9153   1265   -879    338       C  
ATOM   5034  N   ASN B1002     -44.793   4.063  66.469  1.00 93.97           N  
ANISOU 5034  N   ASN B1002    12080  14047   9577   -616    469   1699       N  
ATOM   5035  CA  ASN B1002     -46.215   3.965  66.821  1.00 93.48           C  
ANISOU 5035  CA  ASN B1002    12042  14005   9471   -501    388   1823       C  
ATOM   5036  C   ASN B1002     -46.492   4.264  68.305  1.00 96.46           C  
ANISOU 5036  C   ASN B1002    12417  14299   9936   -346    330   1823       C  
ATOM   5037  O   ASN B1002     -47.361   5.084  68.606  1.00 95.84           O  
ANISOU 5037  O   ASN B1002    12378  14196   9842   -254    286   1923       O  
ATOM   5038  CB  ASN B1002     -46.824   2.625  66.370  1.00 95.93           C  
ANISOU 5038  CB  ASN B1002    12299  14427   9724   -526    374   1798       C  
ATOM   5039  CG  ASN B1002     -46.087   1.393  66.854  1.00126.86           C  
ANISOU 5039  CG  ASN B1002    16139  18324  13737   -522    373   1635       C  
ATOM   5040  OD1 ASN B1002     -46.172   1.003  68.029  1.00122.18           O  
ANISOU 5040  OD1 ASN B1002    15528  17672  13223   -427    311   1621       O  
ATOM   5041  ND2 ASN B1002     -45.365   0.739  65.949  1.00119.34           N  
ANISOU 5041  ND2 ASN B1002    15142  17423  12777   -626    431   1503       N  
ATOM   5042  N   ILE B1003     -45.753   3.604  69.224  1.00 92.79           N  
ANISOU 5042  N   ILE B1003    11901  13795   9559   -315    320   1703       N  
ATOM   5043  CA  ILE B1003     -45.837   3.830  70.676  1.00 91.99           C  
ANISOU 5043  CA  ILE B1003    11804  13635   9511   -197    267   1686       C  
ATOM   5044  C   ILE B1003     -45.181   5.188  71.016  1.00 96.85           C  
ANISOU 5044  C   ILE B1003    12472  14139  10187   -178    277   1663       C  
ATOM   5045  O   ILE B1003     -45.685   5.909  71.876  1.00 96.72           O  
ANISOU 5045  O   ILE B1003    12490  14083  10177    -71    241   1685       O  
ATOM   5046  CB  ILE B1003     -45.282   2.630  71.522  1.00 94.30           C  
ANISOU 5046  CB  ILE B1003    12045  13917   9866   -184    217   1591       C  
ATOM   5047  CG1 ILE B1003     -45.537   2.832  73.046  1.00 94.32           C  
ANISOU 5047  CG1 ILE B1003    12069  13899   9868    -84    157   1598       C  
ATOM   5048  CG2 ILE B1003     -43.806   2.307  71.199  1.00 95.16           C  
ANISOU 5048  CG2 ILE B1003    12103  13972  10082   -253    237   1445       C  
ATOM   5049  CD1 ILE B1003     -45.244   1.635  73.963  1.00100.13           C  
ANISOU 5049  CD1 ILE B1003    12784  14628  10633    -82     71   1563       C  
ATOM   5050  N   PHE B1004     -44.079   5.535  70.309  1.00 93.99           N  
ANISOU 5050  N   PHE B1004    12109  13735   9867   -294    330   1608       N  
ATOM   5051  CA  PHE B1004     -43.344   6.791  70.460  1.00 94.57           C  
ANISOU 5051  CA  PHE B1004    12234  13694  10006   -326    338   1593       C  
ATOM   5052  C   PHE B1004     -44.262   7.968  70.153  1.00 99.77           C  
ANISOU 5052  C   PHE B1004    12994  14290  10625   -285    307   1733       C  
ATOM   5053  O   PHE B1004     -44.308   8.922  70.929  1.00 99.64           O  
ANISOU 5053  O   PHE B1004    13030  14157  10672   -200    259   1723       O  
ATOM   5054  CB  PHE B1004     -42.089   6.787  69.563  1.00 97.08           C  
ANISOU 5054  CB  PHE B1004    12509  14027  10351   -501    420   1518       C  
ATOM   5055  CG  PHE B1004     -41.305   8.078  69.494  1.00 99.74           C  
ANISOU 5055  CG  PHE B1004    12900  14254  10744   -593    438   1524       C  
ATOM   5056  CD1 PHE B1004     -40.437   8.440  70.518  1.00102.95           C  
ANISOU 5056  CD1 PHE B1004    13278  14566  11271   -563    403   1411       C  
ATOM   5057  CD2 PHE B1004     -41.406   8.912  68.386  1.00102.91           C  
ANISOU 5057  CD2 PHE B1004    13387  14644  11072   -732    476   1651       C  
ATOM   5058  CE1 PHE B1004     -39.703   9.628  70.445  1.00105.17           C  
ANISOU 5058  CE1 PHE B1004    13609  14735  11614   -670    412   1414       C  
ATOM   5059  CE2 PHE B1004     -40.677  10.102  68.317  1.00107.13           C  
ANISOU 5059  CE2 PHE B1004    13985  15057  11662   -847    479   1676       C  
ATOM   5060  CZ  PHE B1004     -39.828  10.450  69.345  1.00105.47           C  
ANISOU 5060  CZ  PHE B1004    13739  14749  11588   -817    451   1550       C  
ATOM   5061  N   GLU B1005     -45.036   7.853  69.060  1.00 97.54           N  
ANISOU 5061  N   GLU B1005    12736  14082  10244   -331    316   1854       N  
ATOM   5062  CA  GLU B1005     -46.012   8.837  68.588  1.00 98.86           C  
ANISOU 5062  CA  GLU B1005    12990  14193  10377   -286    254   2007       C  
ATOM   5063  C   GLU B1005     -47.091   9.069  69.651  1.00103.71           C  
ANISOU 5063  C   GLU B1005    13587  14789  11029    -76    184   2002       C  
ATOM   5064  O   GLU B1005     -47.503  10.208  69.867  1.00104.16           O  
ANISOU 5064  O   GLU B1005    13709  14722  11147     17    117   2045       O  
ATOM   5065  CB  GLU B1005     -46.651   8.363  67.269  1.00100.56           C  
ANISOU 5065  CB  GLU B1005    13213  14534  10462   -378    261   2122       C  
ATOM   5066  CG  GLU B1005     -45.648   7.934  66.210  1.00112.18           C  
ANISOU 5066  CG  GLU B1005    14678  16086  11861   -593    356   2087       C  
ATOM   5067  CD  GLU B1005     -45.102   9.037  65.327  1.00135.31           C  
ANISOU 5067  CD  GLU B1005    17717  18945  14749   -761    367   2193       C  
ATOM   5068  OE1 GLU B1005     -44.277   9.844  65.814  1.00128.07           O  
ANISOU 5068  OE1 GLU B1005    16834  17896  13933   -791    373   2158       O  
ATOM   5069  OE2 GLU B1005     -45.469   9.066  64.130  1.00132.82           O  
ANISOU 5069  OE2 GLU B1005    17458  18715  14292   -884    365   2316       O  
ATOM   5070  N   MET B1006     -47.512   7.985  70.333  1.00100.37           N  
ANISOU 5070  N   MET B1006    13072  14489  10574    -10    200   1941       N  
ATOM   5071  CA  MET B1006     -48.511   7.988  71.401  1.00100.66           C  
ANISOU 5071  CA  MET B1006    13062  14573  10610    155    166   1917       C  
ATOM   5072  C   MET B1006     -48.034   8.837  72.593  1.00105.91           C  
ANISOU 5072  C   MET B1006    13761  15124  11358    247    149   1807       C  
ATOM   5073  O   MET B1006     -48.798   9.658  73.103  1.00106.37           O  
ANISOU 5073  O   MET B1006    13824  15147  11445    390    110   1792       O  
ATOM   5074  CB  MET B1006     -48.811   6.538  71.835  1.00101.97           C  
ANISOU 5074  CB  MET B1006    13142  14893  10710    138    190   1889       C  
ATOM   5075  CG  MET B1006     -49.744   6.423  73.011  1.00105.70           C  
ANISOU 5075  CG  MET B1006    13557  15458  11148    260    179   1861       C  
ATOM   5076  SD  MET B1006     -49.631   4.825  73.826  1.00109.10           S  
ANISOU 5076  SD  MET B1006    13932  16005  11514    193    185   1832       S  
ATOM   5077  CE  MET B1006     -51.330   4.635  74.345  1.00106.48           C  
ANISOU 5077  CE  MET B1006    13507  15865  11086    270    194   1885       C  
ATOM   5078  N   LEU B1007     -46.773   8.646  73.018  1.00102.77           N  
ANISOU 5078  N   LEU B1007    13374  14671  11003    171    169   1714       N  
ATOM   5079  CA  LEU B1007     -46.190   9.374  74.144  1.00103.38           C  
ANISOU 5079  CA  LEU B1007    13485  14646  11150    233    142   1597       C  
ATOM   5080  C   LEU B1007     -45.670  10.762  73.770  1.00109.21           C  
ANISOU 5080  C   LEU B1007    14316  15189  11988    208    111   1602       C  
ATOM   5081  O   LEU B1007     -45.457  11.596  74.651  1.00109.58           O  
ANISOU 5081  O   LEU B1007    14404  15129  12103    285     71   1504       O  
ATOM   5082  CB  LEU B1007     -45.148   8.523  74.871  1.00102.74           C  
ANISOU 5082  CB  LEU B1007    13364  14595  11077    173    145   1496       C  
ATOM   5083  CG  LEU B1007     -45.741   7.567  75.908  1.00107.37           C  
ANISOU 5083  CG  LEU B1007    13901  15321  11574    238    129   1474       C  
ATOM   5084  CD1 LEU B1007     -46.070   6.208  75.300  1.00106.78           C  
ANISOU 5084  CD1 LEU B1007    13770  15359  11442    169    145   1551       C  
ATOM   5085  CD2 LEU B1007     -44.803   7.391  77.069  1.00110.71           C  
ANISOU 5085  CD2 LEU B1007    14330  15717  12018    234     81   1362       C  
ATOM   5086  N   ARG B1008     -45.518  11.017  72.456  1.00106.75           N  
ANISOU 5086  N   ARG B1008    14049  14836  11677     89    123   1720       N  
ATOM   5087  CA  ARG B1008     -45.114  12.301  71.883  1.00108.36           C  
ANISOU 5087  CA  ARG B1008    14363  14850  11959     20     81   1781       C  
ATOM   5088  C   ARG B1008     -46.288  13.286  72.044  1.00115.32           C  
ANISOU 5088  C   ARG B1008    15304  15625  12889    196    -15   1831       C  
ATOM   5089  O   ARG B1008     -46.061  14.476  72.264  1.00116.72           O  
ANISOU 5089  O   ARG B1008    15574  15595  13179    226    -88   1812       O  
ATOM   5090  CB  ARG B1008     -44.730  12.096  70.399  1.00107.83           C  
ANISOU 5090  CB  ARG B1008    14322  14825  11824   -184    128   1911       C  
ATOM   5091  CG  ARG B1008     -44.571  13.344  69.534  1.00117.41           C  
ANISOU 5091  CG  ARG B1008    15673  15867  13072   -294     71   2050       C  
ATOM   5092  CD  ARG B1008     -45.778  13.518  68.629  1.00123.57           C  
ANISOU 5092  CD  ARG B1008    16506  16665  13781   -250      0   2229       C  
ATOM   5093  NE  ARG B1008     -45.465  14.309  67.443  1.00128.96           N  
ANISOU 5093  NE  ARG B1008    17322  17248  14430   -443    -39   2406       N  
ATOM   5094  CZ  ARG B1008     -45.200  13.790  66.249  1.00139.72           C  
ANISOU 5094  CZ  ARG B1008    18690  18755  15641   -649     31   2504       C  
ATOM   5095  NH1 ARG B1008     -45.216  12.475  66.070  1.00119.99           N  
ANISOU 5095  NH1 ARG B1008    16066  16485  13038   -668    136   2422       N  
ATOM   5096  NH2 ARG B1008     -44.922  14.583  65.223  1.00129.37           N  
ANISOU 5096  NH2 ARG B1008    17518  17363  14275   -849    -10   2682       N  
ATOM   5097  N   ILE B1009     -47.534  12.774  71.936  1.00112.55           N  
ANISOU 5097  N   ILE B1009    14885  15410  12469    314    -23   1880       N  
ATOM   5098  CA  ILE B1009     -48.782  13.531  72.080  1.00114.28           C  
ANISOU 5098  CA  ILE B1009    15106  15573  12741    510   -113   1902       C  
ATOM   5099  C   ILE B1009     -49.141  13.693  73.571  1.00120.70           C  
ANISOU 5099  C   ILE B1009    15854  16416  13590    696   -104   1710       C  
ATOM   5100  O   ILE B1009     -49.444  14.804  74.013  1.00122.18           O  
ANISOU 5100  O   ILE B1009    16085  16445  13894    841   -183   1635       O  
ATOM   5101  CB  ILE B1009     -49.938  12.851  71.273  1.00116.94           C  
ANISOU 5101  CB  ILE B1009    15370  16078  12984    535   -122   2029       C  
ATOM   5102  CG1 ILE B1009     -49.631  12.813  69.755  1.00117.61           C  
ANISOU 5102  CG1 ILE B1009    15538  16141  13007    345   -142   2214       C  
ATOM   5103  CG2 ILE B1009     -51.298  13.517  71.549  1.00119.09           C  
ANISOU 5103  CG2 ILE B1009    15590  16331  13328    768   -215   2016       C  
ATOM   5104  CD1 ILE B1009     -50.367  11.711  68.964  1.00123.49           C  
ANISOU 5104  CD1 ILE B1009    16201  17102  13617    294   -115   2304       C  
ATOM   5105  N   ASP B1010     -49.126  12.577  74.327  1.00117.40           N  
ANISOU 5105  N   ASP B1010    15338  16202  13066    686    -18   1631       N  
ATOM   5106  CA  ASP B1010     -49.512  12.528  75.737  1.00118.18           C  
ANISOU 5106  CA  ASP B1010    15370  16398  13134    821      9   1464       C  
ATOM   5107  C   ASP B1010     -48.552  13.208  76.713  1.00125.38           C  
ANISOU 5107  C   ASP B1010    16352  17178  14110    830    -10   1305       C  
ATOM   5108  O   ASP B1010     -49.001  14.007  77.535  1.00126.25           O  
ANISOU 5108  O   ASP B1010    16459  17245  14264    987    -37   1162       O  
ATOM   5109  CB  ASP B1010     -49.830  11.083  76.174  1.00118.24           C  
ANISOU 5109  CB  ASP B1010    15274  16662  12991    769     86   1472       C  
ATOM   5110  CG  ASP B1010     -50.946  10.390  75.402  1.00124.45           C  
ANISOU 5110  CG  ASP B1010    15972  17604  13711    770    100   1598       C  
ATOM   5111  OD1 ASP B1010     -51.735  11.092  74.727  1.00125.92           O  
ANISOU 5111  OD1 ASP B1010    16149  17736  13959    863     46   1656       O  
ATOM   5112  OD2 ASP B1010     -51.040   9.150  75.485  1.00127.30           O  
ANISOU 5112  OD2 ASP B1010    16275  18128  13967    677    146   1639       O  
ATOM   5113  N   GLU B1011     -47.248  12.884  76.644  1.00123.59           N  
ANISOU 5113  N   GLU B1011    16171  16896  13891    668      2   1308       N  
ATOM   5114  CA  GLU B1011     -46.251  13.443  77.562  1.00125.23           C  
ANISOU 5114  CA  GLU B1011    16434  16992  14158    654    -27   1158       C  
ATOM   5115  C   GLU B1011     -45.406  14.588  76.983  1.00132.26           C  
ANISOU 5115  C   GLU B1011    17434  17619  15199    574    -88   1175       C  
ATOM   5116  O   GLU B1011     -44.693  15.265  77.732  1.00132.99           O  
ANISOU 5116  O   GLU B1011    17578  17587  15364    573   -132   1039       O  
ATOM   5117  CB  GLU B1011     -45.379  12.332  78.169  1.00125.50           C  
ANISOU 5117  CB  GLU B1011    16422  17152  14110    548      3   1116       C  
ATOM   5118  CG  GLU B1011     -45.011  12.582  79.624  1.00139.10           C  
ANISOU 5118  CG  GLU B1011    18160  18889  15803    604    -30    937       C  
ATOM   5119  CD  GLU B1011     -44.137  11.532  80.282  1.00164.06           C  
ANISOU 5119  CD  GLU B1011    21289  22155  18893    507    -44    909       C  
ATOM   5120  OE1 GLU B1011     -42.995  11.319  79.810  1.00163.54           O  
ANISOU 5120  OE1 GLU B1011    21219  22007  18912    383    -64    927       O  
ATOM   5121  OE2 GLU B1011     -44.577  10.955  81.303  1.00157.99           O  
ANISOU 5121  OE2 GLU B1011    20494  21550  17985    552    -42    862       O  
ATOM   5122  N   GLY B1012     -45.506  14.806  75.674  1.00130.20           N  
ANISOU 5122  N   GLY B1012    17216  17281  14974    490    -99   1344       N  
ATOM   5123  CA  GLY B1012     -44.782  15.871  74.986  1.00131.94           C  
ANISOU 5123  CA  GLY B1012    17555  17260  15317    371   -158   1408       C  
ATOM   5124  C   GLY B1012     -43.341  15.549  74.645  1.00136.21           C  
ANISOU 5124  C   GLY B1012    18089  17800  15863    139   -106   1413       C  
ATOM   5125  O   GLY B1012     -42.664  14.827  75.386  1.00134.60           O  
ANISOU 5125  O   GLY B1012    17807  17707  15628    115    -66   1294       O  
ATOM   5126  N   LEU B1013     -42.864  16.103  73.517  1.00134.66           N  
ANISOU 5126  N   LEU B1013    17973  17485  15707    -39   -115   1553       N  
ATOM   5127  CA  LEU B1013     -41.499  15.909  73.036  1.00135.05           C  
ANISOU 5127  CA  LEU B1013    17998  17552  15765   -284    -49   1554       C  
ATOM   5128  C   LEU B1013     -40.730  17.228  73.019  1.00143.03           C  
ANISOU 5128  C   LEU B1013    19124  18312  16911   -410   -120   1555       C  
ATOM   5129  O   LEU B1013     -41.247  18.246  72.550  1.00144.33           O  
ANISOU 5129  O   LEU B1013    19426  18277  17134   -403   -214   1678       O  
ATOM   5130  CB  LEU B1013     -41.504  15.234  71.646  1.00134.58           C  
ANISOU 5130  CB  LEU B1013    17908  17637  15588   -446     38   1710       C  
ATOM   5131  CG  LEU B1013     -40.155  14.927  70.967  1.00139.36           C  
ANISOU 5131  CG  LEU B1013    18452  18320  16179   -711    140   1695       C  
ATOM   5132  CD1 LEU B1013     -39.375  13.853  71.709  1.00138.06           C  
ANISOU 5132  CD1 LEU B1013    18124  18305  16029   -688    200   1506       C  
ATOM   5133  CD2 LEU B1013     -40.367  14.481  69.543  1.00141.70           C  
ANISOU 5133  CD2 LEU B1013    18750  18753  16338   -861    217   1847       C  
ATOM   5134  N   ARG B1014     -39.504  17.201  73.566  1.00141.29           N  
ANISOU 5134  N   ARG B1014    18844  18088  16751   -525    -95   1418       N  
ATOM   5135  CA  ARG B1014     -38.583  18.337  73.638  1.00143.90           C  
ANISOU 5135  CA  ARG B1014    19259  18201  17216   -685   -154   1393       C  
ATOM   5136  C   ARG B1014     -37.194  17.844  73.210  1.00149.53           C  
ANISOU 5136  C   ARG B1014    19848  19044  17922   -943    -47   1356       C  
ATOM   5137  O   ARG B1014     -36.662  16.917  73.825  1.00147.76           O  
ANISOU 5137  O   ARG B1014    19473  18985  17685   -901     -2   1205       O  
ATOM   5138  CB  ARG B1014     -38.544  18.949  75.064  1.00144.51           C  
ANISOU 5138  CB  ARG B1014    19370  18136  17402   -524   -259   1195       C  
ATOM   5139  CG  ARG B1014     -39.887  19.463  75.619  1.00154.58           C  
ANISOU 5139  CG  ARG B1014    20732  19303  18696   -249   -353   1166       C  
ATOM   5140  CD  ARG B1014     -40.369  20.760  74.981  1.00165.60           C  
ANISOU 5140  CD  ARG B1014    22305  20406  20211   -258   -472   1299       C  
ATOM   5141  NE  ARG B1014     -39.709  21.942  75.543  1.00174.12           N  
ANISOU 5141  NE  ARG B1014    23491  21204  21461   -314   -586   1190       N  
ATOM   5142  CZ  ARG B1014     -39.848  23.178  75.071  1.00188.16           C  
ANISOU 5142  CZ  ARG B1014    25444  22664  23384   -366   -721   1296       C  
ATOM   5143  NH1 ARG B1014     -39.215  24.189  75.648  1.00175.83           N  
ANISOU 5143  NH1 ARG B1014    23978  20843  21988   -425   -831   1177       N  
ATOM   5144  NH2 ARG B1014     -40.618  23.411  74.014  1.00174.70           N  
ANISOU 5144  NH2 ARG B1014    23828  20884  21665   -366   -768   1526       N  
ATOM   5145  N   LEU B1015     -36.626  18.434  72.142  1.00149.27           N  
ANISOU 5145  N   LEU B1015    19872  18949  17896  -1212    -11   1495       N  
ATOM   5146  CA  LEU B1015     -35.318  18.034  71.604  1.00150.32           C  
ANISOU 5146  CA  LEU B1015    19864  19236  18017  -1482    114   1449       C  
ATOM   5147  C   LEU B1015     -34.117  18.820  72.173  1.00157.87           C  
ANISOU 5147  C   LEU B1015    20799  20059  19126  -1644     72   1331       C  
ATOM   5148  O   LEU B1015     -33.060  18.892  71.536  1.00158.42           O  
ANISOU 5148  O   LEU B1015    20781  20210  19203  -1928    167   1334       O  
ATOM   5149  CB  LEU B1015     -35.331  18.044  70.061  1.00151.42           C  
ANISOU 5149  CB  LEU B1015    20042  19466  18025  -1724    215   1654       C  
ATOM   5150  CG  LEU B1015     -36.282  17.063  69.367  1.00154.44           C  
ANISOU 5150  CG  LEU B1015    20399  20040  18240  -1615    279   1741       C  
ATOM   5151  CD1 LEU B1015     -36.495  17.449  67.919  1.00156.28           C  
ANISOU 5151  CD1 LEU B1015    20746  20297  18336  -1849    322   1979       C  
ATOM   5152  CD2 LEU B1015     -35.776  15.636  69.461  1.00155.18           C  
ANISOU 5152  CD2 LEU B1015    20265  20406  18288  -1581    405   1565       C  
ATOM   5153  N   LYS B1016     -34.275  19.377  73.390  1.00156.43           N  
ANISOU 5153  N   LYS B1016    20682  19696  19059  -1471    -65   1206       N  
ATOM   5154  CA  LYS B1016     -33.244  20.140  74.102  1.00158.64           C  
ANISOU 5154  CA  LYS B1016    20952  19832  19491  -1592   -138   1069       C  
ATOM   5155  C   LYS B1016     -33.374  19.928  75.616  1.00163.29           C  
ANISOU 5155  C   LYS B1016    21508  20408  20128  -1336   -239    850       C  
ATOM   5156  O   LYS B1016     -34.484  19.698  76.107  1.00161.57           O  
ANISOU 5156  O   LYS B1016    21352  20190  19845  -1073   -281    843       O  
ATOM   5157  CB  LYS B1016     -33.329  21.636  73.749  1.00163.67           C  
ANISOU 5157  CB  LYS B1016    21809  20149  20231  -1740   -244   1204       C  
ATOM   5158  CG  LYS B1016     -31.992  22.370  73.851  1.00179.10           C  
ANISOU 5158  CG  LYS B1016    23731  22000  22319  -2033   -264   1137       C  
ATOM   5159  CD  LYS B1016     -32.031  23.750  73.193  1.00191.10           C  
ANISOU 5159  CD  LYS B1016    25479  23209  23921  -2254   -358   1335       C  
ATOM   5160  CE  LYS B1016     -31.481  23.761  71.782  1.00201.65           C  
ANISOU 5160  CE  LYS B1016    26797  24663  25158  -2624   -223   1547       C  
ATOM   5161  NZ  LYS B1016     -32.430  23.173  70.796  1.00208.05           N  
ANISOU 5161  NZ  LYS B1016    27650  25615  25782  -2555   -147   1741       N  
ATOM   5162  N   ILE B1017     -32.236  19.998  76.346  1.00162.19           N  
ANISOU 5162  N   ILE B1017    21261  20276  20087  -1429   -277    671       N  
ATOM   5163  CA  ILE B1017     -32.161  19.820  77.805  1.00162.44           C  
ANISOU 5163  CA  ILE B1017    21261  20314  20146  -1235   -386    457       C  
ATOM   5164  C   ILE B1017     -33.006  20.886  78.515  1.00169.39           C  
ANISOU 5164  C   ILE B1017    22347  20943  21069  -1073   -517    417       C  
ATOM   5165  O   ILE B1017     -32.806  22.083  78.293  1.00171.22           O  
ANISOU 5165  O   ILE B1017    22712  20919  21427  -1204   -590    449       O  
ATOM   5166  CB  ILE B1017     -30.690  19.766  78.330  1.00166.78           C  
ANISOU 5166  CB  ILE B1017    21649  20915  20805  -1398   -423    283       C  
ATOM   5167  CG1 ILE B1017     -29.851  18.694  77.600  1.00166.70           C  
ANISOU 5167  CG1 ILE B1017    21401  21160  20777  -1534   -292    286       C  
ATOM   5168  CG2 ILE B1017     -30.635  19.540  79.846  1.00167.18           C  
ANISOU 5168  CG2 ILE B1017    21682  20989  20850  -1205   -556     77       C  
ATOM   5169  CD1 ILE B1017     -28.913  19.237  76.533  1.00176.53           C  
ANISOU 5169  CD1 ILE B1017    22579  22396  22099  -1874   -194    352       C  
ATOM   5170  N   TYR B1018     -33.966  20.437  79.344  1.00166.20           N  
ANISOU 5170  N   TYR B1018    21967  20617  20565   -794   -547    341       N  
ATOM   5171  CA  TYR B1018     -34.886  21.309  80.076  1.00167.84           C  
ANISOU 5171  CA  TYR B1018    22333  20640  20797   -595   -651    255       C  
ATOM   5172  C   TYR B1018     -34.984  20.979  81.573  1.00172.53           C  
ANISOU 5172  C   TYR B1018    22895  21346  21313   -412   -715     25       C  
ATOM   5173  O   TYR B1018     -34.525  19.920  82.008  1.00170.84           O  
ANISOU 5173  O   TYR B1018    22546  21360  21004   -413   -688    -22       O  
ATOM   5174  CB  TYR B1018     -36.280  21.306  79.405  1.00168.58           C  
ANISOU 5174  CB  TYR B1018    22509  20718  20828   -437   -610    414       C  
ATOM   5175  CG  TYR B1018     -36.992  19.968  79.417  1.00168.08           C  
ANISOU 5175  CG  TYR B1018    22333  20946  20584   -292   -509    461       C  
ATOM   5176  CD1 TYR B1018     -37.916  19.656  80.411  1.00169.49           C  
ANISOU 5176  CD1 TYR B1018    22508  21232  20657    -48   -524    343       C  
ATOM   5177  CD2 TYR B1018     -36.790  19.038  78.400  1.00167.43           C  
ANISOU 5177  CD2 TYR B1018    22151  21033  20430   -411   -396    621       C  
ATOM   5178  CE1 TYR B1018     -38.589  18.434  80.418  1.00168.19           C  
ANISOU 5178  CE1 TYR B1018    22249  21325  20329     55   -439    404       C  
ATOM   5179  CE2 TYR B1018     -37.453  17.810  78.399  1.00166.28           C  
ANISOU 5179  CE2 TYR B1018    21915  21127  20137   -288   -321    663       C  
ATOM   5180  CZ  TYR B1018     -38.358  17.516  79.407  1.00173.36           C  
ANISOU 5180  CZ  TYR B1018    22817  22113  20939    -63   -347    568       C  
ATOM   5181  OH  TYR B1018     -39.023  16.312  79.408  1.00172.63           O  
ANISOU 5181  OH  TYR B1018    22643  22248  20702     28   -280    626       O  
ATOM   5182  N   LYS B1019     -35.580  21.884  82.342  1.00171.28           N  
ANISOU 5182  N   LYS B1019    22862  21024  21191   -260   -808   -120       N  
ATOM   5183  CA  LYS B1019     -35.738  21.685  83.778  1.00171.51           C  
ANISOU 5183  CA  LYS B1019    22880  21173  21113   -102   -864   -351       C  
ATOM   5184  C   LYS B1019     -37.097  21.074  84.103  1.00175.17           C  
ANISOU 5184  C   LYS B1019    23333  21825  21400    139   -793   -345       C  
ATOM   5185  O   LYS B1019     -38.134  21.711  83.920  1.00175.30           O  
ANISOU 5185  O   LYS B1019    23430  21724  21452    291   -794   -348       O  
ATOM   5186  CB  LYS B1019     -35.564  23.009  84.525  1.00176.49           C  
ANISOU 5186  CB  LYS B1019    23640  21546  21873    -79  -1000   -568       C  
ATOM   5187  CG  LYS B1019     -35.341  22.854  86.020  1.00190.07           C  
ANISOU 5187  CG  LYS B1019    25343  23402  23473      6  -1071   -830       C  
ATOM   5188  CD  LYS B1019     -35.832  24.074  86.782  1.00201.45           C  
ANISOU 5188  CD  LYS B1019    26925  24632  24986    145  -1171  -1074       C  
ATOM   5189  CE  LYS B1019     -34.686  24.784  87.484  1.00212.90           C  
ANISOU 5189  CE  LYS B1019    28416  25935  26542     -1  -1314  -1274       C  
ATOM   5190  NZ  LYS B1019     -34.636  24.455  88.936  1.00221.77           N  
ANISOU 5190  NZ  LYS B1019    29520  27274  27470     93  -1365  -1525       N  
ATOM   5191  N   ASP B1020     -37.084  19.836  84.586  1.00171.10           N  
ANISOU 5191  N   ASP B1020    22710  21596  20704    168   -744   -337       N  
ATOM   5192  CA  ASP B1020     -38.314  19.138  84.938  1.00170.31           C  
ANISOU 5192  CA  ASP B1020    22584  21710  20415    353   -669   -319       C  
ATOM   5193  C   ASP B1020     -39.074  19.887  86.028  1.00176.82           C  
ANISOU 5193  C   ASP B1020    23482  22520  21180    535   -708   -553       C  
ATOM   5194  O   ASP B1020     -38.608  20.910  86.531  1.00178.35           O  
ANISOU 5194  O   ASP B1020    23757  22524  21483    524   -806   -736       O  
ATOM   5195  CB  ASP B1020     -37.998  17.791  85.592  1.00170.76           C  
ANISOU 5195  CB  ASP B1020    22544  22047  20289    327   -659   -306       C  
ATOM   5196  N   THR B1021     -40.254  19.384  86.373  1.00173.52           N  
ANISOU 5196  N   THR B1021    23028  22310  20592    695   -626   -560       N  
ATOM   5197  CA  THR B1021     -41.152  20.071  87.293  1.00175.59           C  
ANISOU 5197  CA  THR B1021    23329  22599  20790    886   -627   -798       C  
ATOM   5198  C   THR B1021     -40.697  19.938  88.743  1.00181.32           C  
ANISOU 5198  C   THR B1021    24069  23487  21338    871   -678  -1021       C  
ATOM   5199  O   THR B1021     -41.202  20.629  89.628  1.00183.16           O  
ANISOU 5199  O   THR B1021    24342  23737  21514   1002   -689  -1278       O  
ATOM   5200  CB  THR B1021     -42.590  19.537  87.166  1.00182.47           C  
ANISOU 5200  CB  THR B1021    24123  23683  21526   1045   -506   -738       C  
ATOM   5201  OG1 THR B1021     -43.046  19.700  85.817  1.00181.02           O  
ANISOU 5201  OG1 THR B1021    23933  23348  21499   1063   -482   -533       O  
ATOM   5202  CG2 THR B1021     -43.522  20.287  88.106  1.00183.08           C  
ANISOU 5202  CG2 THR B1021    24207  23809  21545   1250   -491  -1024       C  
ATOM   5203  N   GLU B1022     -39.740  19.046  88.979  1.00177.10           N  
ANISOU 5203  N   GLU B1022    23498  23075  20717    713   -718   -932       N  
ATOM   5204  CA  GLU B1022     -39.216  18.821  90.320  1.00178.26           C  
ANISOU 5204  CA  GLU B1022    23666  23384  20679    672   -798  -1104       C  
ATOM   5205  C   GLU B1022     -37.725  19.135  90.391  1.00183.22           C  
ANISOU 5205  C   GLU B1022    24315  23845  21456    509   -942  -1148       C  
ATOM   5206  O   GLU B1022     -37.019  18.645  91.272  1.00183.12           O  
ANISOU 5206  O   GLU B1022    24294  23971  21311    430  -1038  -1209       O  
ATOM   5207  CB  GLU B1022     -39.471  17.378  90.760  1.00178.13           C  
ANISOU 5207  CB  GLU B1022    23588  23694  20401    637   -757   -965       C  
ATOM   5208  CG  GLU B1022     -39.434  17.173  92.266  1.00188.39           C  
ANISOU 5208  CG  GLU B1022    24930  25226  21425    630   -816  -1141       C  
ATOM   5209  CD  GLU B1022     -39.905  18.393  93.033  1.00206.74           C  
ANISOU 5209  CD  GLU B1022    27322  27511  23718    750   -809  -1460       C  
ATOM   5210  OE1 GLU B1022     -40.844  19.068  92.560  1.00198.50           O  
ANISOU 5210  OE1 GLU B1022    26269  26375  22777    898   -712  -1523       O  
ATOM   5211  OE2 GLU B1022     -39.337  18.677  94.108  1.00199.42           O  
ANISOU 5211  OE2 GLU B1022    26456  26642  22671    703   -914  -1659       O  
ATOM   5212  N   GLY B1023     -37.253  19.953  89.456  1.00180.51           N  
ANISOU 5212  N   GLY B1023    23994  23209  21382    447   -966  -1108       N  
ATOM   5213  CA  GLY B1023     -35.853  20.332  89.411  1.00181.37           C  
ANISOU 5213  CA  GLY B1023    24100  23156  21655    269  -1087  -1149       C  
ATOM   5214  C   GLY B1023     -34.950  19.173  89.037  1.00184.17           C  
ANISOU 5214  C   GLY B1023    24331  23641  22005    127  -1099   -973       C  
ATOM   5215  O   GLY B1023     -34.238  18.631  89.882  1.00184.19           O  
ANISOU 5215  O   GLY B1023    24294  23779  21909     72  -1204  -1042       O  
ATOM   5216  N   TYR B1024     -34.980  18.793  87.764  1.00179.42           N  
ANISOU 5216  N   TYR B1024    23664  22996  21510     72  -1003   -756       N  
ATOM   5217  CA  TYR B1024     -34.159  17.692  87.273  1.00177.78           C  
ANISOU 5217  CA  TYR B1024    23319  22901  21327    -45  -1001   -612       C  
ATOM   5218  C   TYR B1024     -33.986  17.767  85.760  1.00180.68           C  
ANISOU 5218  C   TYR B1024    23635  23154  21861   -149   -897   -437       C  
ATOM   5219  O   TYR B1024     -34.964  17.865  85.018  1.00179.33           O  
ANISOU 5219  O   TYR B1024    23510  22954  21674    -77   -792   -314       O  
ATOM   5220  CB  TYR B1024     -34.774  16.348  87.667  1.00177.46           C  
ANISOU 5220  CB  TYR B1024    23236  23120  21069     48   -971   -517       C  
ATOM   5221  CG  TYR B1024     -34.402  15.888  89.059  1.00180.15           C  
ANISOU 5221  CG  TYR B1024    23587  23617  21244     59  -1110   -636       C  
ATOM   5222  CD1 TYR B1024     -35.211  15.004  89.759  1.00181.56           C  
ANISOU 5222  CD1 TYR B1024    23792  24021  21171    145  -1098   -584       C  
ATOM   5223  CD2 TYR B1024     -33.240  16.339  89.672  1.00182.57           C  
ANISOU 5223  CD2 TYR B1024    23881  23854  21633    -37  -1263   -789       C  
ATOM   5224  CE1 TYR B1024     -34.875  14.581  91.031  1.00183.33           C  
ANISOU 5224  CE1 TYR B1024    24048  24397  21214    130  -1240   -667       C  
ATOM   5225  CE2 TYR B1024     -32.895  15.921  90.944  1.00184.57           C  
ANISOU 5225  CE2 TYR B1024    24156  24257  21718    -35  -1414   -887       C  
ATOM   5226  CZ  TYR B1024     -33.716  15.043  91.618  1.00191.23           C  
ANISOU 5226  CZ  TYR B1024    25042  25322  22293     46  -1404   -817       C  
ATOM   5227  OH  TYR B1024     -33.377  14.625  92.884  1.00193.62           O  
ANISOU 5227  OH  TYR B1024    25386  25782  22399     24  -1568   -889       O  
ATOM   5228  N   TYR B1025     -32.737  17.719  85.309  1.00177.75           N  
ANISOU 5228  N   TYR B1025    23158  22737  21640   -328   -929   -431       N  
ATOM   5229  CA  TYR B1025     -32.434  17.784  83.884  1.00177.17           C  
ANISOU 5229  CA  TYR B1025    23025  22594  21699   -470   -820   -280       C  
ATOM   5230  C   TYR B1025     -32.890  16.577  83.059  1.00179.18           C  
ANISOU 5230  C   TYR B1025    23191  23018  21871   -432   -701   -109       C  
ATOM   5231  O   TYR B1025     -32.444  15.460  83.288  1.00177.89           O  
ANISOU 5231  O   TYR B1025    22903  23015  21671   -422   -728   -115       O  
ATOM   5232  CB  TYR B1025     -30.918  17.993  83.682  1.00179.61           C  
ANISOU 5232  CB  TYR B1025    23207  22859  22179   -688   -870   -351       C  
ATOM   5233  N   THR B1026     -33.766  16.817  82.089  1.00175.28           N  
ANISOU 5233  N   THR B1026    22765  22471  21362   -412   -591     40       N  
ATOM   5234  CA  THR B1026     -34.259  15.769  81.185  1.00173.22           C  
ANISOU 5234  CA  THR B1026    22433  22357  21025   -391   -477    200       C  
ATOM   5235  C   THR B1026     -34.213  16.186  79.702  1.00176.83           C  
ANISOU 5235  C   THR B1026    22898  22736  21555   -543   -368    348       C  
ATOM   5236  O   THR B1026     -34.104  17.375  79.394  1.00178.00           O  
ANISOU 5236  O   THR B1026    23147  22689  21795   -636   -387    364       O  
ATOM   5237  CB  THR B1026     -35.670  15.300  81.609  1.00180.96           C  
ANISOU 5237  CB  THR B1026    23482  23437  21837   -186   -457    250       C  
ATOM   5238  OG1 THR B1026     -36.466  16.426  81.992  1.00181.62           O  
ANISOU 5238  OG1 THR B1026    23706  23381  21920    -84   -485    200       O  
ATOM   5239  CG2 THR B1026     -35.639  14.276  82.736  1.00179.30           C  
ANISOU 5239  CG2 THR B1026    23221  23401  21504    -95   -528    179       C  
ATOM   5240  N   ILE B1027     -34.293  15.192  78.791  1.00171.78           N  
ANISOU 5240  N   ILE B1027    22160  22244  20863   -577   -265    455       N  
ATOM   5241  CA  ILE B1027     -34.291  15.370  77.332  1.00171.81           C  
ANISOU 5241  CA  ILE B1027    22163  22238  20879   -733   -148    602       C  
ATOM   5242  C   ILE B1027     -35.131  14.266  76.645  1.00173.72           C  
ANISOU 5242  C   ILE B1027    22367  22644  20994   -652    -60    717       C  
ATOM   5243  O   ILE B1027     -35.075  13.106  77.057  1.00172.30           O  
ANISOU 5243  O   ILE B1027    22084  22609  20772   -565    -70    662       O  
ATOM   5244  CB  ILE B1027     -32.846  15.532  76.756  1.00176.40           C  
ANISOU 5244  CB  ILE B1027    22614  22833  21576   -986   -100    547       C  
ATOM   5245  CG1 ILE B1027     -32.859  16.075  75.305  1.00177.93           C  
ANISOU 5245  CG1 ILE B1027    22856  22994  21755  -1195     14    712       C  
ATOM   5246  CG2 ILE B1027     -31.997  14.253  76.907  1.00176.46           C  
ANISOU 5246  CG2 ILE B1027    22402  23036  21609   -984    -84    427       C  
ATOM   5247  CD1 ILE B1027     -31.608  16.824  74.865  1.00186.70           C  
ANISOU 5247  CD1 ILE B1027    23908  24051  22978  -1483     47    679       C  
ATOM   5248  N   GLY B1028     -35.911  14.651  75.633  1.00169.91           N  
ANISOU 5248  N   GLY B1028    21978  22123  20458   -685      2    881       N  
ATOM   5249  CA  GLY B1028     -36.782  13.743  74.891  1.00168.04           C  
ANISOU 5249  CA  GLY B1028    21721  22029  20099   -626     77    997       C  
ATOM   5250  C   GLY B1028     -38.164  13.696  75.502  1.00170.43           C  
ANISOU 5250  C   GLY B1028    22108  22328  20321   -402     24   1037       C  
ATOM   5251  O   GLY B1028     -38.828  14.733  75.601  1.00170.77           O  
ANISOU 5251  O   GLY B1028    22275  22222  20387   -336    -27   1081       O  
ATOM   5252  N   ILE B1029     -38.600  12.496  75.935  1.00165.30           N  
ANISOU 5252  N   ILE B1029    21382  21837  19585   -287     31   1013       N  
ATOM   5253  CA  ILE B1029     -39.897  12.302  76.596  1.00164.30           C  
ANISOU 5253  CA  ILE B1029    21302  21761  19363    -96     -1   1038       C  
ATOM   5254  C   ILE B1029     -39.399  11.940  78.014  1.00168.01           C  
ANISOU 5254  C   ILE B1029    21736  22270  19830    -31    -76    889       C  
ATOM   5255  O   ILE B1029     -39.159  10.772  78.332  1.00166.80           O  
ANISOU 5255  O   ILE B1029    21502  22239  19634    -25    -89    870       O  
ATOM   5256  CB  ILE B1029     -40.848  11.301  75.854  1.00166.05           C  
ANISOU 5256  CB  ILE B1029    21485  22131  19475    -63     60   1162       C  
ATOM   5257  CG1 ILE B1029     -40.859  11.547  74.325  1.00166.77           C  
ANISOU 5257  CG1 ILE B1029    21597  22202  19565   -196    127   1292       C  
ATOM   5258  CG2 ILE B1029     -42.275  11.377  76.422  1.00166.44           C  
ANISOU 5258  CG2 ILE B1029    21574  22229  19437    113     39   1194       C  
ATOM   5259  CD1 ILE B1029     -41.494  10.442  73.480  1.00172.79           C  
ANISOU 5259  CD1 ILE B1029    22305  23122  20225   -208    186   1383       C  
ATOM   5260  N   GLY B1030     -39.215  12.978  78.831  1.00165.55           N  
ANISOU 5260  N   GLY B1030    21497  21837  19569      8   -141    786       N  
ATOM   5261  CA  GLY B1030     -38.750  12.873  80.210  1.00165.68           C  
ANISOU 5261  CA  GLY B1030    21504  21882  19564     58   -229    637       C  
ATOM   5262  C   GLY B1030     -37.659  11.882  80.569  1.00168.65           C  
ANISOU 5262  C   GLY B1030    21775  22340  19962    -13   -280    581       C  
ATOM   5263  O   GLY B1030     -37.710  11.280  81.647  1.00168.14           O  
ANISOU 5263  O   GLY B1030    21706  22370  19808     54   -357    528       O  
ATOM   5264  N   HIS B1031     -36.656  11.714  79.682  1.00164.81           N  
ANISOU 5264  N   HIS B1031    21200  21827  19594   -154   -247    586       N  
ATOM   5265  CA  HIS B1031     -35.537  10.795  79.904  1.00164.46           C  
ANISOU 5265  CA  HIS B1031    21021  21847  19618   -208   -305    508       C  
ATOM   5266  C   HIS B1031     -34.420  11.439  80.740  1.00169.55           C  
ANISOU 5266  C   HIS B1031    21643  22414  20364   -261   -413    355       C  
ATOM   5267  O   HIS B1031     -33.817  12.429  80.319  1.00170.06           O  
ANISOU 5267  O   HIS B1031    21709  22369  20536   -380   -385    316       O  
ATOM   5268  CB  HIS B1031     -35.015  10.220  78.573  1.00164.88           C  
ANISOU 5268  CB  HIS B1031    20953  21948  19746   -323   -205    545       C  
ATOM   5269  CG  HIS B1031     -33.826   9.321  78.718  1.00168.61           C  
ANISOU 5269  CG  HIS B1031    21257  22476  20330   -359   -268    429       C  
ATOM   5270  ND1 HIS B1031     -33.950   8.033  79.205  1.00169.76           N  
ANISOU 5270  ND1 HIS B1031    21356  22696  20448   -258   -358    429       N  
ATOM   5271  CD2 HIS B1031     -32.526   9.557  78.432  1.00171.61           C  
ANISOU 5271  CD2 HIS B1031    21498  22843  20862   -484   -265    309       C  
ATOM   5272  CE1 HIS B1031     -32.728   7.528  79.201  1.00169.98           C  
ANISOU 5272  CE1 HIS B1031    21220  22736  20628   -299   -421    302       C  
ATOM   5273  NE2 HIS B1031     -31.837   8.409  78.745  1.00171.52           N  
ANISOU 5273  NE2 HIS B1031    21339  22897  20933   -433   -358    215       N  
ATOM   5274  N   LEU B1032     -34.164  10.867  81.932  1.00166.38           N  
ANISOU 5274  N   LEU B1032    21228  22070  19918   -188   -550    281       N  
ATOM   5275  CA  LEU B1032     -33.151  11.333  82.882  1.00167.71           C  
ANISOU 5275  CA  LEU B1032    21374  22190  20159   -225   -688    131       C  
ATOM   5276  C   LEU B1032     -31.733  11.018  82.403  1.00172.19           C  
ANISOU 5276  C   LEU B1032    21754  22756  20917   -343   -717     47       C  
ATOM   5277  O   LEU B1032     -31.478   9.919  81.903  1.00170.94           O  
ANISOU 5277  O   LEU B1032    21472  22676  20803   -334   -706     72       O  
ATOM   5278  CB  LEU B1032     -33.401  10.713  84.273  1.00167.97           C  
ANISOU 5278  CB  LEU B1032    21461  22312  20048   -120   -837    104       C  
ATOM   5279  CG  LEU B1032     -32.538  11.225  85.433  1.00174.42           C  
ANISOU 5279  CG  LEU B1032    22288  23097  20887   -145  -1004    -51       C  
ATOM   5280  CD1 LEU B1032     -33.134  12.474  86.053  1.00175.52           C  
ANISOU 5280  CD1 LEU B1032    22579  23172  20937   -112   -988   -131       C  
ATOM   5281  CD2 LEU B1032     -32.359  10.155  86.489  1.00177.30           C  
ANISOU 5281  CD2 LEU B1032    22646  23572  21148    -89  -1182    -43       C  
ATOM   5282  N   LEU B1033     -30.812  11.984  82.585  1.00170.48           N  
ANISOU 5282  N   LEU B1033    21505  22450  20821   -454   -759    -72       N  
ATOM   5283  CA  LEU B1033     -29.398  11.865  82.218  1.00171.53           C  
ANISOU 5283  CA  LEU B1033    21432  22596  21146   -585   -784   -184       C  
ATOM   5284  C   LEU B1033     -28.545  11.598  83.469  1.00176.87           C  
ANISOU 5284  C   LEU B1033    22040  23291  21871   -547  -1005   -322       C  
ATOM   5285  O   LEU B1033     -27.860  10.576  83.532  1.00176.74           O  
ANISOU 5285  O   LEU B1033    21857  23351  21943   -514  -1097   -371       O  
ATOM   5286  CB  LEU B1033     -28.911  13.126  81.470  1.00172.82           C  
ANISOU 5286  CB  LEU B1033    21591  22655  21417   -779   -679   -206       C  
ATOM   5287  CG  LEU B1033     -29.611  13.456  80.146  1.00176.68           C  
ANISOU 5287  CG  LEU B1033    22149  23122  21861   -853   -483    -54       C  
ATOM   5288  CD1 LEU B1033     -29.693  14.953  79.930  1.00178.15           C  
ANISOU 5288  CD1 LEU B1033    22475  23131  22082   -981   -455    -24       C  
ATOM   5289  CD2 LEU B1033     -28.928  12.781  78.970  1.00179.06           C  
ANISOU 5289  CD2 LEU B1033    22248  23547  22240   -976   -355    -59       C  
ATOM   5290  N   THR B1034     -28.610  12.506  84.469  1.00174.63           N  
ANISOU 5290  N   THR B1034    21888  22933  21530   -543  -1107   -392       N  
ATOM   5291  CA  THR B1034     -27.877  12.410  85.739  1.00176.01           C  
ANISOU 5291  CA  THR B1034    22033  23128  21713   -519  -1335   -522       C  
ATOM   5292  C   THR B1034     -28.674  13.012  86.919  1.00180.51           C  
ANISOU 5292  C   THR B1034    22826  23677  22083   -437  -1414   -548       C  
ATOM   5293  O   THR B1034     -29.695  13.671  86.700  1.00179.46           O  
ANISOU 5293  O   THR B1034    22846  23489  21854   -400  -1286   -494       O  
ATOM   5294  CB  THR B1034     -26.432  12.955  85.594  1.00185.88           C  
ANISOU 5294  CB  THR B1034    23100  24336  23190   -681  -1395   -677       C  
ATOM   5295  OG1 THR B1034     -25.651  12.530  86.712  1.00187.05           O  
ANISOU 5295  OG1 THR B1034    23173  24533  23363   -642  -1642   -790       O  
ATOM   5296  CG2 THR B1034     -26.369  14.478  85.454  1.00185.43           C  
ANISOU 5296  CG2 THR B1034    23143  24132  23181   -821  -1330   -732       C  
ATOM   5297  N   LYS B1035     -28.192  12.754  88.133  1.00178.38           N  
ANISOU 5297  N   LYS B1035    22561  23462  21755   -406  -1628   -639       N  
ATOM   5298  CA  LYS B1035     -28.751  13.319  89.353  1.00179.07           C  
ANISOU 5298  CA  LYS B1035    22836  23564  21638   -351  -1717   -711       C  
ATOM   5299  C   LYS B1035     -27.809  14.409  89.848  1.00184.99           C  
ANISOU 5299  C   LYS B1035    23572  24214  22503   -462  -1831   -906       C  
ATOM   5300  O   LYS B1035     -26.923  14.166  90.667  1.00186.02           O  
ANISOU 5300  O   LYS B1035    23634  24393  22652   -491  -2043  -1004       O  
ATOM   5301  CB  LYS B1035     -28.920  12.239  90.421  1.00181.71           C  
ANISOU 5301  CB  LYS B1035    23214  24052  21777   -266  -1892   -661       C  
ATOM   5302  CG  LYS B1035     -30.067  11.278  90.155  1.00191.71           C  
ANISOU 5302  CG  LYS B1035    24544  25414  22881   -170  -1787   -470       C  
ATOM   5303  CD  LYS B1035     -30.017  10.084  91.095  1.00200.60           C  
ANISOU 5303  CD  LYS B1035    25697  26668  23854   -128  -1992   -387       C  
ATOM   5304  CE  LYS B1035     -31.093  10.178  92.164  1.00209.66           C  
ANISOU 5304  CE  LYS B1035    27046  27951  24665    -89  -1992   -362       C  
ATOM   5305  NZ  LYS B1035     -30.661  11.018  93.316  1.00220.07           N  
ANISOU 5305  NZ  LYS B1035    28446  29295  25877   -128  -2133   -545       N  
ATOM   5306  N   SER B1036     -28.012  15.611  89.324  1.00181.82           N  
ANISOU 5306  N   SER B1036    23238  23658  22187   -528  -1707   -954       N  
ATOM   5307  CA  SER B1036     -27.116  16.752  89.539  1.00183.71           C  
ANISOU 5307  CA  SER B1036    23462  23758  22582   -669  -1791  -1126       C  
ATOM   5308  C   SER B1036     -27.846  18.069  89.195  1.00187.48           C  
ANISOU 5308  C   SER B1036    24111  24042  23080   -683  -1671  -1152       C  
ATOM   5309  O   SER B1036     -28.482  18.147  88.140  1.00185.47           O  
ANISOU 5309  O   SER B1036    23880  23728  22861   -675  -1495  -1007       O  
ATOM   5310  CB  SER B1036     -25.750  16.721  88.853  1.00188.13           C  
ANISOU 5310  CB  SER B1036    23789  24289  23402   -844  -1815  -1160       C  
ATOM   5311  OG  SER B1036     -24.952  15.638  89.301  1.00197.18           O  
ANISOU 5311  OG  SER B1036    24763  25582  24574   -815  -1977  -1185       O  
ATOM   5312  N   PRO B1037     -27.727  19.131  90.040  1.00186.01           N  
ANISOU 5312  N   PRO B1037    24045  23740  22889   -708  -1783  -1343       N  
ATOM   5313  CA  PRO B1037     -28.385  20.411  89.714  1.00186.46           C  
ANISOU 5313  CA  PRO B1037    24267  23569  23008   -707  -1702  -1384       C  
ATOM   5314  C   PRO B1037     -27.619  21.263  88.691  1.00190.80           C  
ANISOU 5314  C   PRO B1037    24766  23902  23827   -925  -1663  -1350       C  
ATOM   5315  O   PRO B1037     -28.128  22.301  88.262  1.00191.00           O  
ANISOU 5315  O   PRO B1037    24936  23701  23936   -942  -1613  -1342       O  
ATOM   5316  CB  PRO B1037     -28.499  21.118  91.077  1.00190.46           C  
ANISOU 5316  CB  PRO B1037    24915  24047  23405   -646  -1853  -1632       C  
ATOM   5317  CG  PRO B1037     -27.853  20.193  92.093  1.00195.42           C  
ANISOU 5317  CG  PRO B1037    25453  24906  23890   -642  -2015  -1694       C  
ATOM   5318  CD  PRO B1037     -27.013  19.226  91.328  1.00189.71           C  
ANISOU 5318  CD  PRO B1037    24513  24269  23298   -733  -2004  -1538       C  
ATOM   5319  N   SER B1038     -26.398  20.828  88.308  1.00187.46           N  
ANISOU 5319  N   SER B1038    24133  23549  23543  -1098  -1692  -1333       N  
ATOM   5320  CA  SER B1038     -25.528  21.493  87.329  1.00188.36           C  
ANISOU 5320  CA  SER B1038    24155  23522  23891  -1355  -1639  -1296       C  
ATOM   5321  C   SER B1038     -25.990  21.215  85.886  1.00189.97           C  
ANISOU 5321  C   SER B1038    24333  23730  24117  -1395  -1424  -1062       C  
ATOM   5322  O   SER B1038     -26.809  20.318  85.672  1.00187.23           O  
ANISOU 5322  O   SER B1038    23992  23522  23625  -1222  -1333   -944       O  
ATOM   5323  CB  SER B1038     -24.080  21.051  87.523  1.00193.00           C  
ANISOU 5323  CB  SER B1038    24489  24236  24605  -1510  -1744  -1396       C  
ATOM   5324  OG  SER B1038     -23.948  19.643  87.417  1.00199.57           O  
ANISOU 5324  OG  SER B1038    25146  25309  25372  -1404  -1721  -1327       O  
ATOM   5325  N   LEU B1039     -25.464  21.979  84.902  1.00187.44           N  
ANISOU 5325  N   LEU B1039    23989  23265  23964  -1643  -1349   -990       N  
ATOM   5326  CA  LEU B1039     -25.837  21.842  83.491  1.00185.93           C  
ANISOU 5326  CA  LEU B1039    23791  23080  23776  -1726  -1154   -766       C  
ATOM   5327  C   LEU B1039     -24.885  20.974  82.654  1.00189.16           C  
ANISOU 5327  C   LEU B1039    23919  23708  24244  -1887  -1039   -723       C  
ATOM   5328  O   LEU B1039     -25.358  20.116  81.906  1.00186.71           O  
ANISOU 5328  O   LEU B1039    23554  23543  23842  -1812   -898   -591       O  
ATOM   5329  CB  LEU B1039     -26.038  23.227  82.843  1.00187.91           C  
ANISOU 5329  CB  LEU B1039    24229  23031  24136  -1903  -1138   -674       C  
ATOM   5330  CG  LEU B1039     -26.657  23.253  81.438  1.00191.74           C  
ANISOU 5330  CG  LEU B1039    24779  23487  24585  -1975   -967   -416       C  
ATOM   5331  CD1 LEU B1039     -28.176  23.235  81.499  1.00190.28           C  
ANISOU 5331  CD1 LEU B1039    24793  23231  24271  -1694   -956   -327       C  
ATOM   5332  CD2 LEU B1039     -26.194  24.466  80.670  1.00196.89           C  
ANISOU 5332  CD2 LEU B1039    25525  23898  25385  -2289   -966   -316       C  
ATOM   5333  N   ASN B1040     -23.564  21.209  82.758  1.00187.76           N  
ANISOU 5333  N   ASN B1040    23553  23561  24224  -2108  -1095   -851       N  
ATOM   5334  CA  ASN B1040     -22.546  20.491  81.982  1.00187.96           C  
ANISOU 5334  CA  ASN B1040    23273  23806  24337  -2275   -983   -862       C  
ATOM   5335  C   ASN B1040     -22.383  18.991  82.306  1.00190.12           C  
ANISOU 5335  C   ASN B1040    23340  24332  24564  -2065  -1008   -932       C  
ATOM   5336  O   ASN B1040     -21.866  18.248  81.465  1.00189.50           O  
ANISOU 5336  O   ASN B1040    23029  24438  24533  -2139   -877   -924       O  
ATOM   5337  CB  ASN B1040     -21.203  21.229  82.024  1.00192.21           C  
ANISOU 5337  CB  ASN B1040    23650  24312  25071  -2581  -1039   -992       C  
ATOM   5338  CG  ASN B1040     -20.312  20.984  80.824  1.00217.66           C  
ANISOU 5338  CG  ASN B1040    26606  27713  28383  -2854   -849   -961       C  
ATOM   5339  OD1 ASN B1040     -20.769  20.845  79.679  1.00210.53           O  
ANISOU 5339  OD1 ASN B1040    25738  26860  27395  -2927   -650   -787       O  
ATOM   5340  ND2 ASN B1040     -19.009  20.970  81.056  1.00211.60           N  
ANISOU 5340  ND2 ASN B1040    25557  27060  27781  -3028   -905  -1140       N  
ATOM   5341  N   ALA B1041     -22.829  18.547  83.506  1.00185.71           N  
ANISOU 5341  N   ALA B1041    22871  23781  23909  -1811  -1179  -1003       N  
ATOM   5342  CA  ALA B1041     -22.756  17.145  83.945  1.00184.16           C  
ANISOU 5342  CA  ALA B1041    22529  23780  23665  -1606  -1253  -1043       C  
ATOM   5343  C   ALA B1041     -23.741  16.235  83.190  1.00185.72           C  
ANISOU 5343  C   ALA B1041    22771  24064  23729  -1458  -1096   -874       C  
ATOM   5344  O   ALA B1041     -23.437  15.060  82.964  1.00184.45           O  
ANISOU 5344  O   ALA B1041    22422  24064  23597  -1377  -1090   -891       O  
ATOM   5345  CB  ALA B1041     -22.994  17.048  85.445  1.00184.92           C  
ANISOU 5345  CB  ALA B1041    22747  23855  23658  -1425  -1486  -1137       C  
ATOM   5346  N   ALA B1042     -24.914  16.780  82.809  1.00181.35           N  
ANISOU 5346  N   ALA B1042    22461  23396  23048  -1419   -988   -723       N  
ATOM   5347  CA  ALA B1042     -25.962  16.065  82.076  1.00178.89           C  
ANISOU 5347  CA  ALA B1042    22215  23152  22602  -1294   -843   -556       C  
ATOM   5348  C   ALA B1042     -25.685  16.013  80.573  1.00182.74           C  
ANISOU 5348  C   ALA B1042    22586  23702  23145  -1479   -635   -465       C  
ATOM   5349  O   ALA B1042     -26.081  15.049  79.917  1.00180.66           O  
ANISOU 5349  O   ALA B1042    22260  23568  22814  -1400   -531   -390       O  
ATOM   5350  CB  ALA B1042     -27.315  16.707  82.341  1.00178.74           C  
ANISOU 5350  CB  ALA B1042    22481  22995  22437  -1168   -834   -453       C  
ATOM   5351  N   LYS B1043     -25.004  17.044  80.034  1.00181.41           N  
ANISOU 5351  N   LYS B1043    22394  23449  23085  -1742   -577   -474       N  
ATOM   5352  CA  LYS B1043     -24.641  17.160  78.616  1.00182.00           C  
ANISOU 5352  CA  LYS B1043    22366  23600  23187  -1982   -374   -388       C  
ATOM   5353  C   LYS B1043     -23.664  16.062  78.176  1.00186.72           C  
ANISOU 5353  C   LYS B1043    22628  24449  23868  -2024   -299   -519       C  
ATOM   5354  O   LYS B1043     -23.723  15.619  77.027  1.00185.89           O  
ANISOU 5354  O   LYS B1043    22437  24481  23712  -2110   -112   -454       O  
ATOM   5355  CB  LYS B1043     -24.072  18.555  78.306  1.00186.78           C  
ANISOU 5355  CB  LYS B1043    23032  24047  23889  -2285   -359   -366       C  
ATOM   5356  CG  LYS B1043     -25.113  19.674  78.366  1.00198.18           C  
ANISOU 5356  CG  LYS B1043    24813  25217  25271  -2261   -406   -212       C  
ATOM   5357  CD  LYS B1043     -24.581  20.999  77.828  1.00209.25           C  
ANISOU 5357  CD  LYS B1043    26292  26439  26773  -2594   -389   -145       C  
ATOM   5358  CE  LYS B1043     -24.802  21.163  76.341  1.00219.01           C  
ANISOU 5358  CE  LYS B1043    27570  27717  27928  -2812   -200     75       C  
ATOM   5359  NZ  LYS B1043     -24.144  22.387  75.819  1.00231.94           N  
ANISOU 5359  NZ  LYS B1043    29270  29198  29660  -3187   -189    155       N  
ATOM   5360  N   SER B1044     -22.781  15.622  79.097  1.00184.63           N  
ANISOU 5360  N   SER B1044    22173  24245  23733  -1953   -458   -715       N  
ATOM   5361  CA  SER B1044     -21.795  14.561  78.871  1.00185.34           C  
ANISOU 5361  CA  SER B1044    21919  24550  23951  -1943   -443   -883       C  
ATOM   5362  C   SER B1044     -22.464  13.183  78.887  1.00187.12           C  
ANISOU 5362  C   SER B1044    22137  24863  24098  -1668   -461   -855       C  
ATOM   5363  O   SER B1044     -22.047  12.299  78.136  1.00186.88           O  
ANISOU 5363  O   SER B1044    21878  25000  24128  -1669   -356   -935       O  
ATOM   5364  CB  SER B1044     -20.693  14.623  79.925  1.00190.80           C  
ANISOU 5364  CB  SER B1044    22430  25246  24818  -1944   -655  -1088       C  
ATOM   5365  OG  SER B1044     -19.654  13.699  79.649  1.00200.11           O  
ANISOU 5365  OG  SER B1044    23244  26625  26164  -1941   -649  -1273       O  
ATOM   5366  N   GLU B1045     -23.505  13.009  79.738  1.00181.88           N  
ANISOU 5366  N   GLU B1045    21719  24089  23298  -1445   -591   -752       N  
ATOM   5367  CA  GLU B1045     -24.282  11.770  79.891  1.00179.65           C  
ANISOU 5367  CA  GLU B1045    21479  23859  22921  -1201   -633   -690       C  
ATOM   5368  C   GLU B1045     -25.047  11.381  78.613  1.00182.08           C  
ANISOU 5368  C   GLU B1045    21827  24235  23121  -1219   -412   -560       C  
ATOM   5369  O   GLU B1045     -25.308  10.194  78.398  1.00180.75           O  
ANISOU 5369  O   GLU B1045    21588  24151  22939  -1075   -412   -564       O  
ATOM   5370  CB  GLU B1045     -25.247  11.877  81.086  1.00179.75           C  
ANISOU 5370  CB  GLU B1045    21754  23760  22782  -1017   -794   -602       C  
ATOM   5371  CG  GLU B1045     -24.569  11.770  82.443  1.00192.11           C  
ANISOU 5371  CG  GLU B1045    23271  25308  24414   -943  -1052   -734       C  
ATOM   5372  CD  GLU B1045     -24.521  10.383  83.058  1.00211.54           C  
ANISOU 5372  CD  GLU B1045    25656  27841  26881   -747  -1227   -753       C  
ATOM   5373  OE1 GLU B1045     -24.941  10.243  84.230  1.00204.08           O  
ANISOU 5373  OE1 GLU B1045    24864  26862  25813   -626  -1410   -719       O  
ATOM   5374  OE2 GLU B1045     -24.052   9.440  82.382  1.00206.16           O  
ANISOU 5374  OE2 GLU B1045    24764  27246  26323   -720  -1190   -806       O  
ATOM   5375  N   LEU B1046     -25.400  12.381  77.776  1.00178.67           N  
ANISOU 5375  N   LEU B1046    21518  23755  22615  -1402   -245   -441       N  
ATOM   5376  CA  LEU B1046     -26.113  12.207  76.507  1.00177.43           C  
ANISOU 5376  CA  LEU B1046    21421  23662  22333  -1460    -43   -301       C  
ATOM   5377  C   LEU B1046     -25.230  11.481  75.484  1.00181.87           C  
ANISOU 5377  C   LEU B1046    21695  24431  22978  -1579    107   -432       C  
ATOM   5378  O   LEU B1046     -25.686  10.509  74.880  1.00180.28           O  
ANISOU 5378  O   LEU B1046    21456  24330  22711  -1483    183   -417       O  
ATOM   5379  CB  LEU B1046     -26.573  13.575  75.968  1.00178.14           C  
ANISOU 5379  CB  LEU B1046    21721  23623  22342  -1645     48   -137       C  
ATOM   5380  CG  LEU B1046     -27.489  13.562  74.746  1.00181.97           C  
ANISOU 5380  CG  LEU B1046    22328  24145  22667  -1700    215     51       C  
ATOM   5381  CD1 LEU B1046     -28.689  14.443  74.965  1.00181.35           C  
ANISOU 5381  CD1 LEU B1046    22551  23868  22484  -1629    160    238       C  
ATOM   5382  CD2 LEU B1046     -26.745  14.002  73.499  1.00186.39           C  
ANISOU 5382  CD2 LEU B1046    22776  24813  23230  -2018    402     62       C  
ATOM   5383  N   ASP B1047     -23.968  11.944  75.313  1.00180.24           N  
ANISOU 5383  N   ASP B1047    21272  24294  22916  -1788    149   -581       N  
ATOM   5384  CA  ASP B1047     -22.973  11.382  74.388  1.00181.41           C  
ANISOU 5384  CA  ASP B1047    21098  24671  23158  -1927    308   -758       C  
ATOM   5385  C   ASP B1047     -22.650   9.912  74.699  1.00183.87           C  
ANISOU 5385  C   ASP B1047    21189  25079  23594  -1681    209   -946       C  
ATOM   5386  O   ASP B1047     -22.304   9.158  73.786  1.00184.11           O  
ANISOU 5386  O   ASP B1047    21008  25293  23654  -1709    356  -1073       O  
ATOM   5387  CB  ASP B1047     -21.687  12.230  74.382  1.00186.08           C  
ANISOU 5387  CB  ASP B1047    21491  25314  23896  -2196    341   -891       C  
ATOM   5388  CG  ASP B1047     -21.901  13.718  74.160  1.00195.99           C  
ANISOU 5388  CG  ASP B1047    22973  26429  25066  -2456    396   -707       C  
ATOM   5389  OD1 ASP B1047     -22.493  14.087  73.124  1.00196.16           O  
ANISOU 5389  OD1 ASP B1047    23141  26469  24922  -2609    568   -529       O  
ATOM   5390  OD2 ASP B1047     -21.448  14.513  75.009  1.00202.63           O  
ANISOU 5390  OD2 ASP B1047    23845  27133  26012  -2514    253   -744       O  
ATOM   5391  N   LYS B1048     -22.780   9.513  75.985  1.00178.78           N  
ANISOU 5391  N   LYS B1048    20604  24308  23016  -1445    -49   -963       N  
ATOM   5392  CA  LYS B1048     -22.565   8.149  76.479  1.00177.99           C  
ANISOU 5392  CA  LYS B1048    20353  24234  23040  -1194   -216  -1095       C  
ATOM   5393  C   LYS B1048     -23.595   7.180  75.885  1.00178.90           C  
ANISOU 5393  C   LYS B1048    20578  24368  23029  -1053   -145   -995       C  
ATOM   5394  O   LYS B1048     -23.254   6.034  75.586  1.00178.96           O  
ANISOU 5394  O   LYS B1048    20389  24453  23155   -933   -167  -1146       O  
ATOM   5395  CB  LYS B1048     -22.652   8.115  78.015  1.00180.00           C  
ANISOU 5395  CB  LYS B1048    20729  24337  23326  -1018   -515  -1065       C  
ATOM   5396  CG  LYS B1048     -21.374   8.553  78.725  1.00195.53           C  
ANISOU 5396  CG  LYS B1048    22490  26312  25491  -1088   -663  -1247       C  
ATOM   5397  CD  LYS B1048     -21.573   8.748  80.232  1.00204.07           C  
ANISOU 5397  CD  LYS B1048    23749  27250  26536   -957   -946  -1192       C  
ATOM   5398  CE  LYS B1048     -21.575   7.461  81.030  1.00212.60           C  
ANISOU 5398  CE  LYS B1048    24792  28305  27680   -702  -1203  -1221       C  
ATOM   5399  NZ  LYS B1048     -21.695   7.716  82.490  1.00220.43           N  
ANISOU 5399  NZ  LYS B1048    25957  29193  28602   -619  -1473  -1167       N  
ATOM   5400  N   ALA B1049     -24.851   7.649  75.717  1.00172.50           N  
ANISOU 5400  N   ALA B1049    20071  23477  21994  -1062    -73   -754       N  
ATOM   5401  CA  ALA B1049     -25.961   6.866  75.173  1.00169.92           C  
ANISOU 5401  CA  ALA B1049    19875  23162  21524   -952    -10   -633       C  
ATOM   5402  C   ALA B1049     -26.151   7.076  73.667  1.00172.90           C  
ANISOU 5402  C   ALA B1049    20228  23675  21789  -1138    261   -602       C  
ATOM   5403  O   ALA B1049     -26.327   6.096  72.941  1.00172.18           O  
ANISOU 5403  O   ALA B1049    20050  23683  21687  -1081    337   -667       O  
ATOM   5404  CB  ALA B1049     -27.247   7.192  75.921  1.00168.51           C  
ANISOU 5404  CB  ALA B1049    20014  22842  21172   -840   -105   -404       C  
ATOM   5405  N   ILE B1050     -26.115   8.344  73.203  1.00169.30           N  
ANISOU 5405  N   ILE B1050    19863  23218  21246  -1368    393   -502       N  
ATOM   5406  CA  ILE B1050     -26.304   8.723  71.796  1.00169.29           C  
ANISOU 5406  CA  ILE B1050    19880  23343  21099  -1591    636   -428       C  
ATOM   5407  C   ILE B1050     -25.159   8.248  70.890  1.00174.69           C  
ANISOU 5407  C   ILE B1050    20236  24264  21874  -1741    805   -671       C  
ATOM   5408  O   ILE B1050     -25.417   7.586  69.881  1.00174.19           O  
ANISOU 5408  O   ILE B1050    20119  24350  21714  -1765    952   -708       O  
ATOM   5409  CB  ILE B1050     -26.654  10.239  71.642  1.00172.56           C  
ANISOU 5409  CB  ILE B1050    20521  23643  21400  -1793    682   -216       C  
ATOM   5410  CG1 ILE B1050     -27.969  10.621  72.384  1.00170.56           C  
ANISOU 5410  CG1 ILE B1050    20580  23181  21046  -1614    541     -2       C  
ATOM   5411  CG2 ILE B1050     -26.664  10.707  70.180  1.00174.65           C  
ANISOU 5411  CG2 ILE B1050    20801  24047  21511  -2076    915   -125       C  
ATOM   5412  CD1 ILE B1050     -29.272   9.901  71.959  1.00174.68           C  
ANISOU 5412  CD1 ILE B1050    21242  23721  21407  -1463    564    136       C  
ATOM   5413  N   GLY B1051     -23.924   8.588  71.260  1.00172.87           N  
ANISOU 5413  N   GLY B1051    19781  24079  21824  -1841    782   -850       N  
ATOM   5414  CA  GLY B1051     -22.726   8.202  70.520  1.00175.09           C  
ANISOU 5414  CA  GLY B1051    19699  24606  22219  -1984    941  -1122       C  
ATOM   5415  C   GLY B1051     -22.194   9.231  69.539  1.00180.38           C  
ANISOU 5415  C   GLY B1051    20317  25434  22785  -2371   1183  -1091       C  
ATOM   5416  O   GLY B1051     -21.339   8.898  68.712  1.00182.35           O  
ANISOU 5416  O   GLY B1051    20270  25945  23069  -2526   1374  -1311       O  
ATOM   5417  N   ARG B1052     -22.692  10.484  69.616  1.00175.77           N  
ANISOU 5417  N   ARG B1052    20017  24694  22074  -2539   1173   -823       N  
ATOM   5418  CA  ARG B1052     -22.260  11.591  68.755  1.00177.52           C  
ANISOU 5418  CA  ARG B1052    20252  25012  22186  -2939   1364   -728       C  
ATOM   5419  C   ARG B1052     -22.286  12.933  69.489  1.00180.46           C  
ANISOU 5419  C   ARG B1052    20837  25132  22598  -3053   1227   -551       C  
ATOM   5420  O   ARG B1052     -23.091  13.120  70.406  1.00177.60           O  
ANISOU 5420  O   ARG B1052    20716  24517  22247  -2825   1026   -423       O  
ATOM   5421  CB  ARG B1052     -23.067  11.652  67.436  1.00177.42           C  
ANISOU 5421  CB  ARG B1052    20412  25110  21889  -3099   1558   -538       C  
ATOM   5422  CG  ARG B1052     -24.477  12.236  67.554  1.00185.11           C  
ANISOU 5422  CG  ARG B1052    21801  25830  22702  -3013   1445   -199       C  
ATOM   5423  CD  ARG B1052     -25.042  12.636  66.207  1.00195.23           C  
ANISOU 5423  CD  ARG B1052    23250  27218  23710  -3266   1620     15       C  
ATOM   5424  NE  ARG B1052     -26.236  13.473  66.343  1.00202.72           N  
ANISOU 5424  NE  ARG B1052    24578  27897  24547  -3223   1488    342       N  
ATOM   5425  CZ  ARG B1052     -26.234  14.803  66.297  1.00218.64           C  
ANISOU 5425  CZ  ARG B1052    26793  29741  26541  -3450   1447    553       C  
ATOM   5426  NH1 ARG B1052     -25.097  15.466  66.118  1.00209.68           N  
ANISOU 5426  NH1 ARG B1052    25520  28681  25469  -3770   1536    490       N  
ATOM   5427  NH2 ARG B1052     -27.366  15.479  66.431  1.00202.91           N  
ANISOU 5427  NH2 ARG B1052    25128  27492  24477  -3360   1307    820       N  
ATOM   5428  N   ASN B1053     -21.412  13.866  69.071  1.00179.35           N  
ANISOU 5428  N   ASN B1053    20605  25067  22475  -3418   1343   -554       N  
ATOM   5429  CA  ASN B1053     -21.320  15.207  69.648  1.00179.74           C  
ANISOU 5429  CA  ASN B1053    20845  24871  22577  -3579   1221   -402       C  
ATOM   5430  C   ASN B1053     -22.508  16.043  69.167  1.00181.89           C  
ANISOU 5430  C   ASN B1053    21525  24941  22645  -3655   1213    -54       C  
ATOM   5431  O   ASN B1053     -22.759  16.121  67.960  1.00182.35           O  
ANISOU 5431  O   ASN B1053    21640  25140  22504  -3872   1396     82       O  
ATOM   5432  CB  ASN B1053     -19.982  15.868  69.289  1.00184.43           C  
ANISOU 5432  CB  ASN B1053    21194  25622  23260  -3975   1349   -516       C  
ATOM   5433  CG  ASN B1053     -18.766  15.086  69.736  1.00207.97           C  
ANISOU 5433  CG  ASN B1053    23737  28813  26470  -3899   1347   -879       C  
ATOM   5434  OD1 ASN B1053     -18.549  14.842  70.930  1.00200.90           O  
ANISOU 5434  OD1 ASN B1053    22782  27784  25767  -3647   1120  -1008       O  
ATOM   5435  ND2 ASN B1053     -17.936  14.689  68.783  1.00201.28           N  
ANISOU 5435  ND2 ASN B1053    22564  28310  25603  -4121   1593  -1059       N  
ATOM   5436  N   THR B1054     -23.266  16.621  70.118  1.00176.15           N  
ANISOU 5436  N   THR B1054    21072  23893  21962  -3460    992     76       N  
ATOM   5437  CA  THR B1054     -24.467  17.413  69.830  1.00174.83           C  
ANISOU 5437  CA  THR B1054    21285  23493  21651  -3460    934    381       C  
ATOM   5438  C   THR B1054     -24.337  18.878  70.250  1.00179.27           C  
ANISOU 5438  C   THR B1054    22053  23761  22302  -3641    803    508       C  
ATOM   5439  O   THR B1054     -24.695  19.764  69.470  1.00180.51           O  
ANISOU 5439  O   THR B1054    22428  23805  22353  -3878    835    754       O  
ATOM   5440  CB  THR B1054     -25.716  16.760  70.447  1.00180.30           C  
ANISOU 5440  CB  THR B1054    22135  24074  22298  -3046    802    423       C  
ATOM   5441  OG1 THR B1054     -25.564  16.705  71.867  1.00178.93           O  
ANISOU 5441  OG1 THR B1054    21936  23761  22287  -2811    609    275       O  
ATOM   5442  CG2 THR B1054     -25.999  15.367  69.884  1.00177.61           C  
ANISOU 5442  CG2 THR B1054    21644  23984  21856  -2895    921    342       C  
ATOM   5443  N   ASN B1055     -23.842  19.126  71.487  1.00174.72           N  
ANISOU 5443  N   ASN B1055    21418  23047  21919  -3528    635    342       N  
ATOM   5444  CA  ASN B1055     -23.655  20.452  72.098  1.00175.72           C  
ANISOU 5444  CA  ASN B1055    21723  22875  22169  -3660    478    398       C  
ATOM   5445  C   ASN B1055     -24.968  21.273  72.207  1.00177.68           C  
ANISOU 5445  C   ASN B1055    22362  22792  22356  -3526    339    633       C  
ATOM   5446  O   ASN B1055     -24.958  22.501  72.071  1.00179.48           O  
ANISOU 5446  O   ASN B1055    22793  22767  22635  -3739    261    777       O  
ATOM   5447  CB  ASN B1055     -22.499  21.236  71.432  1.00179.10           C  
ANISOU 5447  CB  ASN B1055    22035  23366  22648  -4136    589    416       C  
ATOM   5448  CG  ASN B1055     -21.152  20.546  71.490  1.00197.02           C  
ANISOU 5448  CG  ASN B1055    23885  25949  25026  -4250    701    138       C  
ATOM   5449  OD1 ASN B1055     -20.667  20.143  72.554  1.00188.90           O  
ANISOU 5449  OD1 ASN B1055    22688  24928  24159  -4051    571    -94       O  
ATOM   5450  ND2 ASN B1055     -20.496  20.432  70.346  1.00188.96           N  
ANISOU 5450  ND2 ASN B1055    22679  25200  23917  -4585    937    149       N  
ATOM   5451  N   GLY B1056     -26.074  20.569  72.471  1.00170.25           N  
ANISOU 5451  N   GLY B1056    21510  21853  21323  -3172    298    658       N  
ATOM   5452  CA  GLY B1056     -27.401  21.155  72.624  1.00168.57           C  
ANISOU 5452  CA  GLY B1056    21614  21375  21060  -2981    172    836       C  
ATOM   5453  C   GLY B1056     -28.506  20.455  71.854  1.00168.99           C  
ANISOU 5453  C   GLY B1056    21740  21541  20927  -2830    255    991       C  
ATOM   5454  O   GLY B1056     -29.310  19.728  72.447  1.00166.05           O  
ANISOU 5454  O   GLY B1056    21375  21201  20516  -2499    205    932       O  
ATOM   5455  N   VAL B1057     -28.558  20.685  70.523  1.00165.69           N  
ANISOU 5455  N   VAL B1057    21383  21190  20380  -3095    378   1197       N  
ATOM   5456  CA  VAL B1057     -29.587  20.153  69.612  1.00163.64           C  
ANISOU 5456  CA  VAL B1057    21212  21035  19927  -3011    450   1372       C  
ATOM   5457  C   VAL B1057     -29.424  18.654  69.288  1.00163.92           C  
ANISOU 5457  C   VAL B1057    20997  21423  19860  -2917    613   1228       C  
ATOM   5458  O   VAL B1057     -28.358  18.229  68.831  1.00164.70           O  
ANISOU 5458  O   VAL B1057    20865  21759  19955  -3130    768   1103       O  
ATOM   5459  CB  VAL B1057     -29.761  21.015  68.319  1.00170.25           C  
ANISOU 5459  CB  VAL B1057    22245  21802  20642  -3339    488   1669       C  
ATOM   5460  CG1 VAL B1057     -31.045  20.648  67.570  1.00168.79           C  
ANISOU 5460  CG1 VAL B1057    22206  21652  20275  -3196    487   1865       C  
ATOM   5461  CG2 VAL B1057     -29.738  22.513  68.627  1.00172.56           C  
ANISOU 5461  CG2 VAL B1057    22776  21714  21076  -3468    307   1800       C  
ATOM   5462  N   ILE B1058     -30.510  17.873  69.505  1.00156.26           N  
ANISOU 5462  N   ILE B1058    20072  20483  18817  -2600    574   1239       N  
ATOM   5463  CA  ILE B1058     -30.603  16.434  69.207  1.00153.26           C  
ANISOU 5463  CA  ILE B1058    19505  20381  18346  -2473    690   1127       C  
ATOM   5464  C   ILE B1058     -31.756  16.167  68.213  1.00154.64           C  
ANISOU 5464  C   ILE B1058    19821  20613  18322  -2441    733   1331       C  
ATOM   5465  O   ILE B1058     -32.744  16.909  68.209  1.00154.24           O  
ANISOU 5465  O   ILE B1058    20005  20356  18243  -2364    615   1525       O  
ATOM   5466  CB  ILE B1058     -30.671  15.529  70.477  1.00153.81           C  
ANISOU 5466  CB  ILE B1058    19454  20466  18519  -2148    595    921       C  
ATOM   5467  CG1 ILE B1058     -31.994  15.698  71.258  1.00152.22           C  
ANISOU 5467  CG1 ILE B1058    19454  20083  18301  -1852    443   1010       C  
ATOM   5468  CG2 ILE B1058     -29.446  15.723  71.380  1.00155.49           C  
ANISOU 5468  CG2 ILE B1058    19508  20655  18917  -2198    542    714       C  
ATOM   5469  CD1 ILE B1058     -32.529  14.413  71.882  1.00155.91           C  
ANISOU 5469  CD1 ILE B1058    19833  20666  18739  -1570    414    910       C  
ATOM   5470  N   THR B1059     -31.619  15.127  67.365  1.00149.17           N  
ANISOU 5470  N   THR B1059    18978  20196  17504  -2497    889   1271       N  
ATOM   5471  CA  THR B1059     -32.635  14.770  66.364  1.00147.58           C  
ANISOU 5471  CA  THR B1059    18889  20087  17100  -2488    934   1441       C  
ATOM   5472  C   THR B1059     -33.770  13.932  66.961  1.00146.74           C  
ANISOU 5472  C   THR B1059    18809  19955  16989  -2133    838   1423       C  
ATOM   5473  O   THR B1059     -33.624  13.400  68.063  1.00144.75           O  
ANISOU 5473  O   THR B1059    18457  19673  16869  -1919    771   1255       O  
ATOM   5474  CB  THR B1059     -32.002  14.084  65.139  1.00156.34           C  
ANISOU 5474  CB  THR B1059    19835  21512  18056  -2729   1149   1371       C  
ATOM   5475  OG1 THR B1059     -31.228  12.960  65.562  1.00154.61           O  
ANISOU 5475  OG1 THR B1059    19336  21465  17944  -2620   1222   1072       O  
ATOM   5476  CG2 THR B1059     -31.156  15.035  64.300  1.00158.36           C  
ANISOU 5476  CG2 THR B1059    20115  21819  18237  -3138   1258   1469       C  
ATOM   5477  N   LYS B1060     -34.878  13.822  66.236  1.00141.60           N  
ANISOU 5477  N   LYS B1060    18294  19327  16182  -2093    825   1602       N  
ATOM   5478  CA  LYS B1060     -36.019  13.039  66.695  1.00138.47           C  
ANISOU 5478  CA  LYS B1060    17917  18929  15767  -1795    746   1600       C  
ATOM   5479  C   LYS B1060     -35.683  11.552  66.725  1.00139.36           C  
ANISOU 5479  C   LYS B1060    17818  19256  15877  -1712    834   1392       C  
ATOM   5480  O   LYS B1060     -36.190  10.807  67.563  1.00136.94           O  
ANISOU 5480  O   LYS B1060    17475  18930  15628  -1467    757   1318       O  
ATOM   5481  CB  LYS B1060     -37.235  13.286  65.800  1.00141.39           C  
ANISOU 5481  CB  LYS B1060    18459  19289  15973  -1798    706   1839       C  
ATOM   5482  CG  LYS B1060     -38.568  13.195  66.524  1.00154.76           C  
ANISOU 5482  CG  LYS B1060    20235  20866  17699  -1495    564   1898       C  
ATOM   5483  CD  LYS B1060     -39.727  13.139  65.542  1.00166.31           C  
ANISOU 5483  CD  LYS B1060    21809  22382  19000  -1492    532   2097       C  
ATOM   5484  CE  LYS B1060     -40.185  14.534  65.148  1.00180.92           C  
ANISOU 5484  CE  LYS B1060    23872  24020  20849  -1564    408   2332       C  
ATOM   5485  NZ  LYS B1060     -41.053  15.148  66.191  1.00190.13           N  
ANISOU 5485  NZ  LYS B1060    25115  24962  22162  -1289    245   2344       N  
ATOM   5486  N   ASP B1061     -34.782  11.107  65.869  1.00135.87           N  
ANISOU 5486  N   ASP B1061    17230  19015  15379  -1917    991   1282       N  
ATOM   5487  CA  ASP B1061     -34.483   9.691  65.823  1.00134.11           C  
ANISOU 5487  CA  ASP B1061    16808  18972  15178  -1824   1058   1067       C  
ATOM   5488  C   ASP B1061     -33.480   9.211  66.856  1.00135.76           C  
ANISOU 5488  C   ASP B1061    16824  19161  15598  -1718   1023    827       C  
ATOM   5489  O   ASP B1061     -33.496   8.054  67.236  1.00134.31           O  
ANISOU 5489  O   ASP B1061    16523  19026  15482  -1545    988    680       O  
ATOM   5490  CB  ASP B1061     -34.076   9.320  64.421  1.00137.65           C  
ANISOU 5490  CB  ASP B1061    17171  19666  15464  -2059   1241   1018       C  
ATOM   5491  CG  ASP B1061     -34.977   9.954  63.405  1.00148.50           C  
ANISOU 5491  CG  ASP B1061    18756  21051  16614  -2200   1250   1284       C  
ATOM   5492  OD1 ASP B1061     -35.164  11.182  63.485  1.00149.67           O  
ANISOU 5492  OD1 ASP B1061    19077  21031  16757  -2287   1177   1488       O  
ATOM   5493  OD2 ASP B1061     -35.526   9.233  62.553  1.00154.83           O  
ANISOU 5493  OD2 ASP B1061    19560  22013  17256  -2215   1306   1292       O  
ATOM   5494  N   GLU B1062     -32.613  10.096  67.317  1.00131.80           N  
ANISOU 5494  N   GLU B1062    16296  18574  15207  -1827   1010    794       N  
ATOM   5495  CA  GLU B1062     -31.804   9.821  68.497  1.00130.46           C  
ANISOU 5495  CA  GLU B1062    15981  18343  15244  -1700    919    601       C  
ATOM   5496  C   GLU B1062     -32.671   9.757  69.749  1.00129.72           C  
ANISOU 5496  C   GLU B1062    16018  18072  15199  -1430    734    666       C  
ATOM   5497  O   GLU B1062     -32.398   8.984  70.667  1.00128.48           O  
ANISOU 5497  O   GLU B1062    15758  17903  15155  -1259    637    527       O  
ATOM   5498  CB  GLU B1062     -30.718  10.887  68.663  1.00133.99           C  
ANISOU 5498  CB  GLU B1062    16378  18742  15789  -1907    943    561       C  
ATOM   5499  CG  GLU B1062     -29.305  10.330  68.716  1.00148.02           C  
ANISOU 5499  CG  GLU B1062    17854  20673  17715  -1981   1012    287       C  
ATOM   5500  CD  GLU B1062     -28.388  10.967  67.690  1.00175.52           C  
ANISOU 5500  CD  GLU B1062    21233  24310  21147  -2331   1200    262       C  
ATOM   5501  OE1 GLU B1062     -28.715  12.069  67.202  1.00174.42           O  
ANISOU 5501  OE1 GLU B1062    21290  24090  20890  -2531   1228    483       O  
ATOM   5502  OE2 GLU B1062     -27.341  10.366  67.372  1.00171.65           O  
ANISOU 5502  OE2 GLU B1062    20460  24022  20736  -2413   1313     20       O  
ATOM   5503  N   ALA B1063     -33.719  10.574  69.778  1.00123.68           N  
ANISOU 5503  N   ALA B1063    15476  17175  14342  -1395    680    874       N  
ATOM   5504  CA  ALA B1063     -34.635  10.604  70.912  1.00120.83           C  
ANISOU 5504  CA  ALA B1063    15233  16678  13999  -1154    531    926       C  
ATOM   5505  C   ALA B1063     -35.392   9.287  71.037  1.00120.92           C  
ANISOU 5505  C   ALA B1063    15206  16783  13954   -975    507    911       C  
ATOM   5506  O   ALA B1063     -35.498   8.721  72.125  1.00119.58           O  
ANISOU 5506  O   ALA B1063    15011  16582  13841   -804    400    842       O  
ATOM   5507  CB  ALA B1063     -35.607  11.766  70.777  1.00121.70           C  
ANISOU 5507  CB  ALA B1063    15562  16638  14041  -1150    485   1127       C  
ATOM   5508  N   GLU B1064     -35.916   8.803  69.915  1.00115.47           N  
ANISOU 5508  N   GLU B1064    14523  16210  13142  -1033    598    983       N  
ATOM   5509  CA  GLU B1064     -36.658   7.540  69.895  1.00112.92           C  
ANISOU 5509  CA  GLU B1064    14168  15969  12766   -894    576    973       C  
ATOM   5510  C   GLU B1064     -35.779   6.409  70.444  1.00113.56           C  
ANISOU 5510  C   GLU B1064    14072  16094  12982   -823    538    766       C  
ATOM   5511  O   GLU B1064     -36.299   5.509  71.105  1.00111.99           O  
ANISOU 5511  O   GLU B1064    13876  15879  12797   -665    440    760       O  
ATOM   5512  CB  GLU B1064     -37.146   7.216  68.470  1.00114.69           C  
ANISOU 5512  CB  GLU B1064    14408  16327  12840  -1009    686   1048       C  
ATOM   5513  CG  GLU B1064     -38.294   6.214  68.430  1.00123.16           C  
ANISOU 5513  CG  GLU B1064    15510  17448  13836   -871    640   1102       C  
ATOM   5514  CD  GLU B1064     -38.862   5.836  67.072  1.00138.40           C  
ANISOU 5514  CD  GLU B1064    17462  19516  15609   -974    725   1167       C  
ATOM   5515  OE1 GLU B1064     -38.278   6.224  66.032  1.00129.32           O  
ANISOU 5515  OE1 GLU B1064    16293  18460  14384  -1173    842   1155       O  
ATOM   5516  OE2 GLU B1064     -39.895   5.129  67.053  1.00128.95           O  
ANISOU 5516  OE2 GLU B1064    16299  18346  14349   -873    674   1228       O  
ATOM   5517  N   LYS B1065     -34.451   6.470  70.180  1.00109.04           N  
ANISOU 5517  N   LYS B1065    13341  15574  12515   -945    603    600       N  
ATOM   5518  CA  LYS B1065     -33.449   5.509  70.657  1.00107.98           C  
ANISOU 5518  CA  LYS B1065    13009  15469  12549   -875    548    378       C  
ATOM   5519  C   LYS B1065     -33.434   5.473  72.186  1.00107.98           C  
ANISOU 5519  C   LYS B1065    13048  15334  12646   -709    360    375       C  
ATOM   5520  O   LYS B1065     -33.379   4.390  72.769  1.00106.96           O  
ANISOU 5520  O   LYS B1065    12856  15188  12594   -571    242    302       O  
ATOM   5521  CB  LYS B1065     -32.050   5.856  70.100  1.00112.43           C  
ANISOU 5521  CB  LYS B1065    13381  16128  13208  -1055    664    202       C  
ATOM   5522  CG  LYS B1065     -31.568   4.931  68.981  1.00128.01           C  
ANISOU 5522  CG  LYS B1065    15170  18285  15184  -1126    800     25       C  
ATOM   5523  N   LEU B1066     -33.527   6.656  72.824  1.00102.43           N  
ANISOU 5523  N   LEU B1066    12461  14530  11926   -730    320    460       N  
ATOM   5524  CA  LEU B1066     -33.577   6.810  74.277  1.00100.76           C  
ANISOU 5524  CA  LEU B1066    12312  14211  11760   -596    154    458       C  
ATOM   5525  C   LEU B1066     -34.933   6.350  74.813  1.00100.58           C  
ANISOU 5525  C   LEU B1066    12434  14170  11612   -445     84    597       C  
ATOM   5526  O   LEU B1066     -34.996   5.799  75.916  1.00 99.67           O  
ANISOU 5526  O   LEU B1066    12331  14027  11514   -326    -57    577       O  
ATOM   5527  CB  LEU B1066     -33.332   8.275  74.687  1.00101.62           C  
ANISOU 5527  CB  LEU B1066    12510  14217  11883   -674    146    485       C  
ATOM   5528  CG  LEU B1066     -31.941   8.869  74.443  1.00108.10           C  
ANISOU 5528  CG  LEU B1066    13191  15043  12839   -844    188    350       C  
ATOM   5529  CD1 LEU B1066     -31.974  10.374  74.583  1.00109.19           C  
ANISOU 5529  CD1 LEU B1066    13466  15053  12967   -949    192    424       C  
ATOM   5530  CD2 LEU B1066     -30.901   8.293  75.401  1.00110.94           C  
ANISOU 5530  CD2 LEU B1066    13391  15406  13357   -773     50    168       C  
ATOM   5531  N   PHE B1067     -36.013   6.579  74.026  1.00 94.56           N  
ANISOU 5531  N   PHE B1067    11776  13438  10716   -464    176    742       N  
ATOM   5532  CA  PHE B1067     -37.391   6.205  74.367  1.00 92.30           C  
ANISOU 5532  CA  PHE B1067    11601  13163  10304   -343    137    875       C  
ATOM   5533  C   PHE B1067     -37.586   4.683  74.415  1.00 94.73           C  
ANISOU 5533  C   PHE B1067    11844  13532  10616   -278     83    852       C  
ATOM   5534  O   PHE B1067     -38.296   4.196  75.296  1.00 93.33           O  
ANISOU 5534  O   PHE B1067    11729  13352  10381   -178    -11    916       O  
ATOM   5535  CB  PHE B1067     -38.398   6.878  73.411  1.00 93.53           C  
ANISOU 5535  CB  PHE B1067    11859  13336  10343   -387    232   1024       C  
ATOM   5536  CG  PHE B1067     -39.838   6.459  73.603  1.00 93.61           C  
ANISOU 5536  CG  PHE B1067    11945  13390  10235   -275    206   1147       C  
ATOM   5537  CD1 PHE B1067     -40.609   7.003  74.623  1.00 95.89           C  
ANISOU 5537  CD1 PHE B1067    12319  13640  10477   -160    144   1192       C  
ATOM   5538  CD2 PHE B1067     -40.425   5.525  72.758  1.00 95.07           C  
ANISOU 5538  CD2 PHE B1067    12101  13669  10352   -293    247   1199       C  
ATOM   5539  CE1 PHE B1067     -41.937   6.607  74.804  1.00 95.91           C  
ANISOU 5539  CE1 PHE B1067    12358  13716  10370    -70    135   1290       C  
ATOM   5540  CE2 PHE B1067     -41.746   5.115  72.955  1.00 96.88           C  
ANISOU 5540  CE2 PHE B1067    12379  13951  10479   -208    219   1308       C  
ATOM   5541  CZ  PHE B1067     -42.497   5.672  73.966  1.00 94.48           C  
ANISOU 5541  CZ  PHE B1067    12142  13625  10132   -101    169   1357       C  
ATOM   5542  N   ASN B1068     -36.964   3.945  73.470  1.00 91.64           N  
ANISOU 5542  N   ASN B1068    11331  13197  10292   -344    141    755       N  
ATOM   5543  CA  ASN B1068     -37.026   2.482  73.402  1.00 91.38           C  
ANISOU 5543  CA  ASN B1068    11229  13186  10303   -284     75    704       C  
ATOM   5544  C   ASN B1068     -36.335   1.845  74.613  1.00 96.03           C  
ANISOU 5544  C   ASN B1068    11769  13696  11022   -189   -105    621       C  
ATOM   5545  O   ASN B1068     -36.811   0.826  75.117  1.00 94.88           O  
ANISOU 5545  O   ASN B1068    11658  13521  10870   -114   -226    671       O  
ATOM   5546  CB  ASN B1068     -36.413   1.969  72.100  1.00 92.96           C  
ANISOU 5546  CB  ASN B1068    11295  13467  10558   -372    187    568       C  
ATOM   5547  CG  ASN B1068     -37.115   2.427  70.842  1.00112.01           C  
ANISOU 5547  CG  ASN B1068    13768  15975  12814   -483    343    663       C  
ATOM   5548  OD1 ASN B1068     -38.250   2.930  70.860  1.00103.36           O  
ANISOU 5548  OD1 ASN B1068    12813  14876  11583   -468    349    844       O  
ATOM   5549  ND2 ASN B1068     -36.440   2.262  69.715  1.00104.61           N  
ANISOU 5549  ND2 ASN B1068    12718  15140  11891   -599    469    532       N  
ATOM   5550  N   GLN B1069     -35.241   2.478  75.100  1.00 94.28           N  
ANISOU 5550  N   GLN B1069    11476  13437  10909   -208   -140    511       N  
ATOM   5551  CA  GLN B1069     -34.476   2.070  76.288  1.00 95.13           C  
ANISOU 5551  CA  GLN B1069    11537  13470  11137   -127   -333    433       C  
ATOM   5552  C   GLN B1069     -35.337   2.192  77.552  1.00 98.97           C  
ANISOU 5552  C   GLN B1069    12193  13925  11486    -57   -450    583       C  
ATOM   5553  O   GLN B1069     -35.148   1.425  78.497  1.00 99.16           O  
ANISOU 5553  O   GLN B1069    12228  13902  11546     12   -636    590       O  
ATOM   5554  CB  GLN B1069     -33.221   2.944  76.454  1.00 97.68           C  
ANISOU 5554  CB  GLN B1069    11749  13781  11585   -188   -326    290       C  
ATOM   5555  CG  GLN B1069     -32.140   2.711  75.404  1.00114.67           C  
ANISOU 5555  CG  GLN B1069    13684  15995  13892   -265   -225     99       C  
ATOM   5556  CD  GLN B1069     -30.970   3.645  75.581  1.00136.37           C  
ANISOU 5556  CD  GLN B1069    16317  18748  16752   -355   -207    -28       C  
ATOM   5557  OE1 GLN B1069     -31.106   4.873  75.571  1.00131.04           O  
ANISOU 5557  OE1 GLN B1069    15734  18061  15995   -456   -124     44       O  
ATOM   5558  NE2 GLN B1069     -29.780   3.080  75.716  1.00132.67           N  
ANISOU 5558  NE2 GLN B1069    15631  18288  16490   -325   -294   -230       N  
ATOM   5559  N   ASP B1070     -36.269   3.168  77.564  1.00 95.01           N  
ANISOU 5559  N   ASP B1070    11819  13455  10827    -77   -347    698       N  
ATOM   5560  CA  ASP B1070     -37.187   3.416  78.677  1.00 94.62           C  
ANISOU 5560  CA  ASP B1070    11911  13416  10622    -18   -412    811       C  
ATOM   5561  C   ASP B1070     -38.429   2.534  78.609  1.00 97.10           C  
ANISOU 5561  C   ASP B1070    12292  13791  10811     10   -410    952       C  
ATOM   5562  O   ASP B1070     -39.001   2.236  79.656  1.00 97.46           O  
ANISOU 5562  O   ASP B1070    12421  13867  10742     46   -501   1032       O  
ATOM   5563  CB  ASP B1070     -37.562   4.903  78.778  1.00 96.79           C  
ANISOU 5563  CB  ASP B1070    12270  13684  10823    -31   -319    826       C  
ATOM   5564  CG  ASP B1070     -36.376   5.829  78.983  1.00110.49           C  
ANISOU 5564  CG  ASP B1070    13957  15346  12678    -81   -339    695       C  
ATOM   5565  OD1 ASP B1070     -35.586   5.590  79.934  1.00112.31           O  
ANISOU 5565  OD1 ASP B1070    14154  15552  12968    -58   -484    612       O  
ATOM   5566  OD2 ASP B1070     -36.257   6.817  78.222  1.00116.13           O  
ANISOU 5566  OD2 ASP B1070    14676  16025  13422   -154   -226    687       O  
ATOM   5567  N   VAL B1071     -38.843   2.114  77.386  1.00 91.85           N  
ANISOU 5567  N   VAL B1071    11590  13158  10152    -24   -306    982       N  
ATOM   5568  CA  VAL B1071     -39.979   1.201  77.166  1.00 90.29           C  
ANISOU 5568  CA  VAL B1071    11435  13014   9856    -18   -307   1105       C  
ATOM   5569  C   VAL B1071     -39.544  -0.199  77.619  1.00 93.96           C  
ANISOU 5569  C   VAL B1071    11872  13418  10411      0   -477   1088       C  
ATOM   5570  O   VAL B1071     -40.292  -0.864  78.336  1.00 92.89           O  
ANISOU 5570  O   VAL B1071    11815  13300  10178      4   -567   1210       O  
ATOM   5571  CB  VAL B1071     -40.506   1.248  75.703  1.00 93.05           C  
ANISOU 5571  CB  VAL B1071    11758  13417  10181    -70   -160   1129       C  
ATOM   5572  CG1 VAL B1071     -41.419   0.065  75.383  1.00 92.34           C  
ANISOU 5572  CG1 VAL B1071    11683  13367  10036    -78   -189   1216       C  
ATOM   5573  CG2 VAL B1071     -41.232   2.556  75.442  1.00 92.42           C  
ANISOU 5573  CG2 VAL B1071    11743  13378   9995    -73    -46   1202       C  
ATOM   5574  N   ASP B1072     -38.297  -0.601  77.259  1.00 91.50           N  
ANISOU 5574  N   ASP B1072    11442  13030  10292      8   -531    932       N  
ATOM   5575  CA  ASP B1072     -37.665  -1.856  77.673  1.00 92.40           C  
ANISOU 5575  CA  ASP B1072    11512  13042  10553     53   -730    882       C  
ATOM   5576  C   ASP B1072     -37.644  -1.924  79.206  1.00 97.03           C  
ANISOU 5576  C   ASP B1072    12197  13594  11077     81   -916    974       C  
ATOM   5577  O   ASP B1072     -37.907  -2.982  79.781  1.00 97.48           O  
ANISOU 5577  O   ASP B1072    12318  13591  11131     88  -1089   1070       O  
ATOM   5578  CB  ASP B1072     -36.219  -1.934  77.136  1.00 95.26           C  
ANISOU 5578  CB  ASP B1072    11697  13352  11147     75   -742    656       C  
ATOM   5579  CG  ASP B1072     -36.067  -2.246  75.659  1.00104.55           C  
ANISOU 5579  CG  ASP B1072    12757  14572  12396     39   -593    529       C  
ATOM   5580  OD1 ASP B1072     -36.947  -2.936  75.102  1.00105.12           O  
ANISOU 5580  OD1 ASP B1072    12880  14657  12401     24   -565    601       O  
ATOM   5581  OD2 ASP B1072     -35.034  -1.856  75.074  1.00109.60           O  
ANISOU 5581  OD2 ASP B1072    13245  15242  13157     15   -509    346       O  
ATOM   5582  N   ALA B1073     -37.362  -0.771  79.854  1.00 93.46           N  
ANISOU 5582  N   ALA B1073    11769  13180  10560     81   -885    949       N  
ATOM   5583  CA  ALA B1073     -37.321  -0.604  81.301  1.00 94.07           C  
ANISOU 5583  CA  ALA B1073    11944  13261  10536     93  -1036   1012       C  
ATOM   5584  C   ALA B1073     -38.727  -0.733  81.905  1.00 98.19           C  
ANISOU 5584  C   ALA B1073    12612  13887  10811     59  -1009   1198       C  
ATOM   5585  O   ALA B1073     -38.891  -1.426  82.913  1.00 98.70           O  
ANISOU 5585  O   ALA B1073    12764  13950  10788     39  -1178   1304       O  
ATOM   5586  CB  ALA B1073     -36.711   0.746  81.652  1.00 94.90           C  
ANISOU 5586  CB  ALA B1073    12031  13385  10642     94   -981    904       C  
ATOM   5587  N   ALA B1074     -39.739  -0.095  81.272  1.00 94.37           N  
ANISOU 5587  N   ALA B1074    12145  13498  10214     44   -805   1240       N  
ATOM   5588  CA  ALA B1074     -41.132  -0.143  81.720  1.00 94.54           C  
ANISOU 5588  CA  ALA B1074    12259  13650  10014     15   -746   1387       C  
ATOM   5589  C   ALA B1074     -41.688  -1.564  81.640  1.00101.30           C  
ANISOU 5589  C   ALA B1074    13144  14495  10851    -40   -839   1521       C  
ATOM   5590  O   ALA B1074     -42.364  -1.997  82.572  1.00102.32           O  
ANISOU 5590  O   ALA B1074    13362  14704  10811    -96   -907   1653       O  
ATOM   5591  CB  ALA B1074     -41.988   0.809  80.904  1.00 94.11           C  
ANISOU 5591  CB  ALA B1074    12185  13674   9900     32   -537   1383       C  
ATOM   5592  N   VAL B1075     -41.358  -2.299  80.553  1.00 98.52           N  
ANISOU 5592  N   VAL B1075    12719  14045  10670    -37   -847   1478       N  
ATOM   5593  CA  VAL B1075     -41.766  -3.690  80.320  1.00 99.02           C  
ANISOU 5593  CA  VAL B1075    12805  14049  10768    -86   -953   1575       C  
ATOM   5594  C   VAL B1075     -41.163  -4.602  81.402  1.00104.60           C  
ANISOU 5594  C   VAL B1075    13580  14641  11520    -98  -1218   1637       C  
ATOM   5595  O   VAL B1075     -41.911  -5.341  82.046  1.00105.28           O  
ANISOU 5595  O   VAL B1075    13771  14753  11478   -184  -1314   1813       O  
ATOM   5596  CB  VAL B1075     -41.404  -4.157  78.883  1.00102.83           C  
ANISOU 5596  CB  VAL B1075    13184  14450  11436    -66   -899   1456       C  
ATOM   5597  CG1 VAL B1075     -41.612  -5.659  78.705  1.00103.59           C  
ANISOU 5597  CG1 VAL B1075    13306  14433  11619   -102  -1054   1516       C  
ATOM   5598  CG2 VAL B1075     -42.197  -3.382  77.836  1.00101.45           C  
ANISOU 5598  CG2 VAL B1075    12976  14400  11171    -84   -669   1452       C  
ATOM   5599  N   ARG B1076     -39.827  -4.511  81.624  1.00101.47           N  
ANISOU 5599  N   ARG B1076    13126  14129  11301    -25  -1344   1501       N  
ATOM   5600  CA  ARG B1076     -39.078  -5.294  82.619  1.00102.86           C  
ANISOU 5600  CA  ARG B1076    13354  14173  11555    -14  -1634   1545       C  
ATOM   5601  C   ARG B1076     -39.653  -5.145  84.034  1.00107.13           C  
ANISOU 5601  C   ARG B1076    14052  14824  11829    -98  -1717   1726       C  
ATOM   5602  O   ARG B1076     -39.741  -6.136  84.763  1.00108.06           O  
ANISOU 5602  O   ARG B1076    14280  14867  11911   -162  -1942   1884       O  
ATOM   5603  CB  ARG B1076     -37.587  -4.918  82.600  1.00103.61           C  
ANISOU 5603  CB  ARG B1076    13323  14172  11871     85  -1719   1341       C  
ATOM   5604  CG  ARG B1076     -36.650  -6.120  82.635  1.00116.09           C  
ANISOU 5604  CG  ARG B1076    14852  15540  13716    152  -1999   1287       C  
ATOM   5605  CD  ARG B1076     -36.041  -6.392  81.271  1.00126.86           C  
ANISOU 5605  CD  ARG B1076    16029  16832  15340    229  -1908   1065       C  
ATOM   5606  NE  ARG B1076     -35.708  -7.808  81.091  1.00136.69           N  
ANISOU 5606  NE  ARG B1076    17253  17870  16814    286  -2145   1042       N  
ATOM   5607  CZ  ARG B1076     -35.413  -8.368  79.922  1.00148.61           C  
ANISOU 5607  CZ  ARG B1076    18624  19307  18532    345  -2089    857       C  
ATOM   5608  NH1 ARG B1076     -35.406  -7.642  78.810  1.00134.24           N  
ANISOU 5608  NH1 ARG B1076    16682  17629  16695    332  -1797    701       N  
ATOM   5609  NH2 ARG B1076     -35.129  -9.662  79.853  1.00134.17           N  
ANISOU 5609  NH2 ARG B1076    16787  17263  16927    412  -2334    824       N  
ATOM   5610  N   GLY B1077     -40.058  -3.918  84.380  1.00102.64           N  
ANISOU 5610  N   GLY B1077    13498  14430  11073   -105  -1535   1697       N  
ATOM   5611  CA  GLY B1077     -40.653  -3.571  85.668  1.00103.04           C  
ANISOU 5611  CA  GLY B1077    13674  14639  10837   -183  -1554   1814       C  
ATOM   5612  C   GLY B1077     -42.053  -4.123  85.855  1.00105.82           C  
ANISOU 5612  C   GLY B1077    14109  15128  10969   -305  -1487   2008       C  
ATOM   5613  O   GLY B1077     -42.398  -4.580  86.950  1.00106.75           O  
ANISOU 5613  O   GLY B1077    14352  15326  10885   -418  -1609   2166       O  
ATOM   5614  N   ILE B1078     -42.867  -4.079  84.778  1.00100.16           N  
ANISOU 5614  N   ILE B1078    13322  14454  10282   -299  -1294   2001       N  
ATOM   5615  CA  ILE B1078     -44.234  -4.610  84.734  1.00 99.80           C  
ANISOU 5615  CA  ILE B1078    13313  14542  10064   -416  -1212   2164       C  
ATOM   5616  C   ILE B1078     -44.152  -6.132  84.927  1.00104.39           C  
ANISOU 5616  C   ILE B1078    13982  14975  10707   -521  -1451   2332       C  
ATOM   5617  O   ILE B1078     -44.904  -6.690  85.733  1.00105.04           O  
ANISOU 5617  O   ILE B1078    14167  15161  10580   -677  -1510   2524       O  
ATOM   5618  CB  ILE B1078     -44.941  -4.196  83.397  1.00101.03           C  
ANISOU 5618  CB  ILE B1078    13357  14745  10284   -367   -987   2095       C  
ATOM   5619  CG1 ILE B1078     -45.466  -2.745  83.470  1.00100.68           C  
ANISOU 5619  CG1 ILE B1078    13264  14878  10112   -299   -771   2000       C  
ATOM   5620  CG2 ILE B1078     -46.074  -5.160  83.010  1.00101.75           C  
ANISOU 5620  CG2 ILE B1078    13459  14889  10311   -487   -971   2251       C  
ATOM   5621  CD1 ILE B1078     -45.737  -2.082  82.109  1.00107.36           C  
ANISOU 5621  CD1 ILE B1078    14008  15713  11071   -217   -596   1905       C  
ATOM   5622  N   LEU B1079     -43.195  -6.779  84.217  1.00100.76           N  
ANISOU 5622  N   LEU B1079    13478  14270  10538   -440  -1595   2247       N  
ATOM   5623  CA  LEU B1079     -42.944  -8.222  84.263  1.00102.19           C  
ANISOU 5623  CA  LEU B1079    13732  14238  10858   -498  -1859   2363       C  
ATOM   5624  C   LEU B1079     -42.520  -8.727  85.649  1.00108.68           C  
ANISOU 5624  C   LEU B1079    14704  15002  11588   -577  -2136   2522       C  
ATOM   5625  O   LEU B1079     -42.675  -9.917  85.929  1.00110.11           O  
ANISOU 5625  O   LEU B1079    14996  15040  11800   -682  -2361   2701       O  
ATOM   5626  CB  LEU B1079     -41.908  -8.637  83.199  1.00101.81           C  
ANISOU 5626  CB  LEU B1079    13568  13955  11160   -356  -1936   2167       C  
ATOM   5627  CG  LEU B1079     -42.347  -8.629  81.730  1.00104.80           C  
ANISOU 5627  CG  LEU B1079    13834  14348  11638   -324  -1734   2050       C  
ATOM   5628  CD1 LEU B1079     -41.149  -8.780  80.822  1.00105.05           C  
ANISOU 5628  CD1 LEU B1079    13730  14210  11974   -181  -1774   1807       C  
ATOM   5629  CD2 LEU B1079     -43.359  -9.733  81.429  1.00107.39           C  
ANISOU 5629  CD2 LEU B1079    14232  14635  11935   -452  -1785   2207       C  
ATOM   5630  N   ARG B1080     -41.982  -7.826  86.503  1.00105.41           N  
ANISOU 5630  N   ARG B1080    14302  14689  11060   -536  -2137   2463       N  
ATOM   5631  CA  ARG B1080     -41.549  -8.131  87.871  1.00107.18           C  
ANISOU 5631  CA  ARG B1080    14673  14900  11152   -615  -2395   2605       C  
ATOM   5632  C   ARG B1080     -42.645  -7.854  88.892  1.00111.01           C  
ANISOU 5632  C   ARG B1080    15278  15671  11229   -801  -2291   2781       C  
ATOM   5633  O   ARG B1080     -42.683  -8.518  89.928  1.00113.46           O  
ANISOU 5633  O   ARG B1080    15752  15985  11374   -952  -2511   2992       O  
ATOM   5634  CB  ARG B1080     -40.270  -7.368  88.233  1.00107.62           C  
ANISOU 5634  CB  ARG B1080    14669  14905  11318   -475  -2481   2423       C  
ATOM   5635  CG  ARG B1080     -39.015  -8.056  87.722  1.00120.03           C  
ANISOU 5635  CG  ARG B1080    16156  16178  13271   -337  -2724   2312       C  
ATOM   5636  CD  ARG B1080     -37.753  -7.459  88.310  1.00131.86           C  
ANISOU 5636  CD  ARG B1080    17604  17636  14860   -234  -2869   2170       C  
ATOM   5637  NE  ARG B1080     -37.466  -6.131  87.767  1.00140.29           N  
ANISOU 5637  NE  ARG B1080    18522  18823  15961   -139  -2597   1932       N  
ATOM   5638  CZ  ARG B1080     -36.732  -5.907  86.682  1.00157.03           C  
ANISOU 5638  CZ  ARG B1080    20454  20842  18369    -11  -2510   1711       C  
ATOM   5639  NH1 ARG B1080     -36.208  -6.920  86.002  1.00146.33           N  
ANISOU 5639  NH1 ARG B1080    19018  19278  17302     62  -2658   1660       N  
ATOM   5640  NH2 ARG B1080     -36.518  -4.666  86.265  1.00145.56           N  
ANISOU 5640  NH2 ARG B1080    18894  19497  16915     35  -2274   1533       N  
ATOM   5641  N   ASN B1081     -43.525  -6.873  88.605  1.00105.02           N  
ANISOU 5641  N   ASN B1081    14435  15157  10310   -792  -1964   2690       N  
ATOM   5642  CA  ASN B1081     -44.656  -6.505  89.457  1.00105.40           C  
ANISOU 5642  CA  ASN B1081    14545  15521   9982   -948  -1808   2796       C  
ATOM   5643  C   ASN B1081     -45.721  -7.605  89.357  1.00110.86           C  
ANISOU 5643  C   ASN B1081    15296  16252  10574  -1146  -1824   3032       C  
ATOM   5644  O   ASN B1081     -46.357  -7.756  88.311  1.00108.90           O  
ANISOU 5644  O   ASN B1081    14948  15988  10440  -1123  -1678   3003       O  
ATOM   5645  CB  ASN B1081     -45.220  -5.140  89.045  1.00102.04           C  
ANISOU 5645  CB  ASN B1081    13983  15299   9490   -836  -1479   2594       C  
ATOM   5646  CG  ASN B1081     -46.162  -4.524  90.046  1.00116.21           C  
ANISOU 5646  CG  ASN B1081    15807  17431  10917   -944  -1317   2613       C  
ATOM   5647  OD1 ASN B1081     -47.282  -5.000  90.270  1.00108.23           O  
ANISOU 5647  OD1 ASN B1081    14811  16611   9702  -1109  -1231   2762       O  
ATOM   5648  ND2 ASN B1081     -45.747  -3.409  90.625  1.00107.56           N  
ANISOU 5648  ND2 ASN B1081    14702  16430   9738   -851  -1255   2437       N  
ATOM   5649  N   ALA B1082     -45.881  -8.390  90.446  1.00111.02           N  
ANISOU 5649  N   ALA B1082    15489  16317  10378  -1359  -2019   3274       N  
ATOM   5650  CA  ALA B1082     -46.799  -9.533  90.577  1.00112.77           C  
ANISOU 5650  CA  ALA B1082    15806  16562  10478  -1606  -2088   3545       C  
ATOM   5651  C   ALA B1082     -48.270  -9.266  90.212  1.00115.98           C  
ANISOU 5651  C   ALA B1082    16101  17260  10704  -1710  -1771   3554       C  
ATOM   5652  O   ALA B1082     -48.953 -10.188  89.761  1.00116.13           O  
ANISOU 5652  O   ALA B1082    16135  17225  10764  -1854  -1801   3710       O  
ATOM   5653  CB  ALA B1082     -46.702 -10.120  91.977  1.00116.91           C  
ANISOU 5653  CB  ALA B1082    16543  17149  10727  -1838  -2323   3799       C  
ATOM   5654  N   LYS B1083     -48.752  -8.022  90.410  1.00111.16           N  
ANISOU 5654  N   LYS B1083    15375  16948   9914  -1634  -1487   3377       N  
ATOM   5655  CA  LYS B1083     -50.133  -7.636  90.113  1.00110.21           C  
ANISOU 5655  CA  LYS B1083    15114  17124   9635  -1697  -1188   3348       C  
ATOM   5656  C   LYS B1083     -50.362  -7.336  88.624  1.00109.68           C  
ANISOU 5656  C   LYS B1083    14879  16943   9851  -1511  -1045   3193       C  
ATOM   5657  O   LYS B1083     -51.388  -7.749  88.078  1.00109.72           O  
ANISOU 5657  O   LYS B1083    14807  17043   9840  -1612   -939   3268       O  
ATOM   5658  CB  LYS B1083     -50.565  -6.446  90.985  1.00113.76           C  
ANISOU 5658  CB  LYS B1083    15504  17930   9789  -1677   -966   3202       C  
ATOM   5659  CG  LYS B1083     -52.077  -6.278  91.072  1.00131.66           C  
ANISOU 5659  CG  LYS B1083    17640  20565  11820  -1810   -699   3216       C  
ATOM   5660  CD  LYS B1083     -52.483  -5.160  92.007  1.00144.13           C  
ANISOU 5660  CD  LYS B1083    19154  22500  13109  -1784   -490   3041       C  
ATOM   5661  CE  LYS B1083     -53.981  -5.106  92.168  1.00158.08           C  
ANISOU 5661  CE  LYS B1083    20767  24656  14640  -1931   -236   3050       C  
ATOM   5662  NZ  LYS B1083     -54.388  -4.064  93.145  1.00170.82           N  
ANISOU 5662  NZ  LYS B1083    22306  26636  15961  -1907    -30   2847       N  
ATOM   5663  N   LEU B1084     -49.415  -6.624  87.979  1.00102.28           N  
ANISOU 5663  N   LEU B1084    13887  15817   9158  -1262  -1046   2986       N  
ATOM   5664  CA  LEU B1084     -49.495  -6.213  86.572  1.00 98.64           C  
ANISOU 5664  CA  LEU B1084    13283  15255   8941  -1090   -915   2833       C  
ATOM   5665  C   LEU B1084     -49.077  -7.296  85.571  1.00101.05           C  
ANISOU 5665  C   LEU B1084    13607  15268   9519  -1091  -1076   2888       C  
ATOM   5666  O   LEU B1084     -49.702  -7.394  84.516  1.00 99.38           O  
ANISOU 5666  O   LEU B1084    13299  15061   9401  -1072   -966   2859       O  
ATOM   5667  CB  LEU B1084     -48.694  -4.920  86.325  1.00 96.82           C  
ANISOU 5667  CB  LEU B1084    12987  14973   8826   -859   -830   2593       C  
ATOM   5668  CG  LEU B1084     -49.036  -3.696  87.194  1.00101.76           C  
ANISOU 5668  CG  LEU B1084    13583  15849   9230   -812   -669   2475       C  
ATOM   5669  CD1 LEU B1084     -47.832  -2.796  87.361  1.00101.34           C  
ANISOU 5669  CD1 LEU B1084    13549  15664   9292   -650   -719   2297       C  
ATOM   5670  CD2 LEU B1084     -50.191  -2.903  86.617  1.00102.23           C  
ANISOU 5670  CD2 LEU B1084    13493  16103   9248   -743   -417   2381       C  
ATOM   5671  N   LYS B1085     -48.017  -8.085  85.889  1.00 98.32           N  
ANISOU 5671  N   LYS B1085    13380  14669   9309  -1101  -1346   2948       N  
ATOM   5672  CA  LYS B1085     -47.460  -9.171  85.058  1.00 97.89           C  
ANISOU 5672  CA  LYS B1085    13348  14305   9542  -1080  -1538   2964       C  
ATOM   5673  C   LYS B1085     -48.498 -10.109  84.366  1.00102.76           C  
ANISOU 5673  C   LYS B1085    13954  14915  10175  -1226  -1520   3088       C  
ATOM   5674  O   LYS B1085     -48.425 -10.214  83.138  1.00100.23           O  
ANISOU 5674  O   LYS B1085    13542  14479  10061  -1127  -1468   2961       O  
ATOM   5675  CB  LYS B1085     -46.365  -9.955  85.825  1.00101.41           C  
ANISOU 5675  CB  LYS B1085    13934  14510  10086  -1098  -1868   3050       C  
ATOM   5676  CG  LYS B1085     -45.715 -11.127  85.074  1.00108.55           C  
ANISOU 5676  CG  LYS B1085    14858  15066  11319  -1053  -2103   3039       C  
ATOM   5677  CD  LYS B1085     -46.141 -12.500  85.624  1.00119.34           C  
ANISOU 5677  CD  LYS B1085    16396  16302  12647  -1272  -2358   3316       C  
ATOM   5678  CE  LYS B1085     -45.270 -13.037  86.748  1.00132.68           C  
ANISOU 5678  CE  LYS B1085    18249  17819  14346  -1310  -2696   3456       C  
ATOM   5679  NZ  LYS B1085     -45.595 -12.438  88.075  1.00139.29           N  
ANISOU 5679  NZ  LYS B1085    19179  18935  14810  -1449  -2648   3598       N  
ATOM   5680  N   PRO B1086     -49.455 -10.784  85.081  1.00102.29           N  
ANISOU 5680  N   PRO B1086    13981  14986   9898  -1473  -1558   3325       N  
ATOM   5681  CA  PRO B1086     -50.393 -11.686  84.377  1.00102.84           C  
ANISOU 5681  CA  PRO B1086    14034  15031  10010  -1622  -1556   3433       C  
ATOM   5682  C   PRO B1086     -51.320 -11.030  83.351  1.00106.10           C  
ANISOU 5682  C   PRO B1086    14265  15637  10410  -1560  -1281   3307       C  
ATOM   5683  O   PRO B1086     -51.594 -11.641  82.314  1.00105.39           O  
ANISOU 5683  O   PRO B1086    14136  15426  10482  -1573  -1303   3284       O  
ATOM   5684  CB  PRO B1086     -51.172 -12.358  85.515  1.00107.16           C  
ANISOU 5684  CB  PRO B1086    14705  15723  10286  -1923  -1633   3716       C  
ATOM   5685  CG  PRO B1086     -51.055 -11.432  86.656  1.00111.91           C  
ANISOU 5685  CG  PRO B1086    15324  16571  10626  -1915  -1539   3706       C  
ATOM   5686  CD  PRO B1086     -49.700 -10.810  86.539  1.00106.02           C  
ANISOU 5686  CD  PRO B1086    14575  15637  10070  -1653  -1613   3508       C  
ATOM   5687  N   VAL B1087     -51.798  -9.800  83.640  1.00102.53           N  
ANISOU 5687  N   VAL B1087    13707  15475   9774  -1489  -1042   3219       N  
ATOM   5688  CA  VAL B1087     -52.696  -9.024  82.767  1.00101.09           C  
ANISOU 5688  CA  VAL B1087    13349  15486   9575  -1408   -799   3103       C  
ATOM   5689  C   VAL B1087     -51.961  -8.608  81.478  1.00103.00           C  
ANISOU 5689  C   VAL B1087    13527  15537  10071  -1190   -777   2905       C  
ATOM   5690  O   VAL B1087     -52.502  -8.787  80.385  1.00101.86           O  
ANISOU 5690  O   VAL B1087    13302  15391  10011  -1187   -717   2871       O  
ATOM   5691  CB  VAL B1087     -53.334  -7.811  83.510  1.00105.08           C  
ANISOU 5691  CB  VAL B1087    13762  16322   9842  -1368   -581   3042       C  
ATOM   5692  CG1 VAL B1087     -54.298  -7.041  82.606  1.00103.75           C  
ANISOU 5692  CG1 VAL B1087    13407  16328   9684  -1271   -370   2932       C  
ATOM   5693  CG2 VAL B1087     -54.042  -8.256  84.789  1.00107.45           C  
ANISOU 5693  CG2 VAL B1087    14116  16855   9856  -1613   -583   3224       C  
ATOM   5694  N   TYR B1088     -50.721  -8.086  81.618  1.00 98.65           N  
ANISOU 5694  N   TYR B1088    13014  14840   9630  -1030   -831   2779       N  
ATOM   5695  CA  TYR B1088     -49.858  -7.642  80.522  1.00 96.61           C  
ANISOU 5695  CA  TYR B1088    12698  14420   9591   -848   -804   2588       C  
ATOM   5696  C   TYR B1088     -49.645  -8.756  79.491  1.00101.44           C  
ANISOU 5696  C   TYR B1088    13317  14822  10405   -879   -922   2572       C  
ATOM   5697  O   TYR B1088     -49.793  -8.502  78.297  1.00100.15           O  
ANISOU 5697  O   TYR B1088    13067  14663  10323   -815   -818   2462       O  
ATOM   5698  CB  TYR B1088     -48.513  -7.127  81.075  1.00 97.16           C  
ANISOU 5698  CB  TYR B1088    12811  14366   9739   -723   -883   2481       C  
ATOM   5699  CG  TYR B1088     -47.595  -6.522  80.033  1.00 96.89           C  
ANISOU 5699  CG  TYR B1088    12699  14210   9903   -560   -825   2279       C  
ATOM   5700  CD1 TYR B1088     -47.716  -5.187  79.659  1.00 97.51           C  
ANISOU 5700  CD1 TYR B1088    12702  14406   9940   -455   -637   2172       C  
ATOM   5701  CD2 TYR B1088     -46.581  -7.273  79.448  1.00 97.60           C  
ANISOU 5701  CD2 TYR B1088    12790  14068  10225   -516   -965   2189       C  
ATOM   5702  CE1 TYR B1088     -46.874  -4.623  78.702  1.00 96.49           C  
ANISOU 5702  CE1 TYR B1088    12513  14179   9969   -346   -581   2010       C  
ATOM   5703  CE2 TYR B1088     -45.736  -6.723  78.485  1.00 97.35           C  
ANISOU 5703  CE2 TYR B1088    12670  13966  10351   -395   -889   1995       C  
ATOM   5704  CZ  TYR B1088     -45.889  -5.397  78.112  1.00102.49           C  
ANISOU 5704  CZ  TYR B1088    13261  14750  10931   -328   -693   1921       C  
ATOM   5705  OH  TYR B1088     -45.065  -4.850  77.161  1.00101.61           O  
ANISOU 5705  OH  TYR B1088    13074  14582  10951   -249   -615   1754       O  
ATOM   5706  N   ASP B1089     -49.339  -9.987  79.953  1.00100.18           N  
ANISOU 5706  N   ASP B1089    13267  14480  10318   -986  -1149   2683       N  
ATOM   5707  CA  ASP B1089     -49.119 -11.151  79.090  1.00100.85           C  
ANISOU 5707  CA  ASP B1089    13371  14332  10614  -1014  -1294   2652       C  
ATOM   5708  C   ASP B1089     -50.375 -11.560  78.317  1.00105.34           C  
ANISOU 5708  C   ASP B1089    13891  15009  11124  -1141  -1209   2713       C  
ATOM   5709  O   ASP B1089     -50.259 -12.027  77.184  1.00104.89           O  
ANISOU 5709  O   ASP B1089    13795  14832  11225  -1109  -1227   2595       O  
ATOM   5710  CB  ASP B1089     -48.549 -12.334  79.892  1.00104.85           C  
ANISOU 5710  CB  ASP B1089    14024  14593  11222  -1096  -1592   2775       C  
ATOM   5711  CG  ASP B1089     -47.128 -12.146  80.409  1.00115.65           C  
ANISOU 5711  CG  ASP B1089    15421  15792  12728   -947  -1736   2676       C  
ATOM   5712  OD1 ASP B1089     -46.583 -11.025  80.272  1.00114.66           O  
ANISOU 5712  OD1 ASP B1089    15206  15763  12595   -799  -1586   2519       O  
ATOM   5713  OD2 ASP B1089     -46.563 -13.116  80.957  1.00123.04           O  
ANISOU 5713  OD2 ASP B1089    16469  16491  13790   -983  -2014   2760       O  
ATOM   5714  N   SER B1090     -51.569 -11.350  78.915  1.00102.56           N  
ANISOU 5714  N   SER B1090    13524  14905  10539  -1285  -1107   2877       N  
ATOM   5715  CA  SER B1090     -52.861 -11.663  78.295  1.00102.76           C  
ANISOU 5715  CA  SER B1090    13477  15077  10491  -1419  -1022   2945       C  
ATOM   5716  C   SER B1090     -53.249 -10.621  77.241  1.00105.44           C  
ANISOU 5716  C   SER B1090    13667  15578  10816  -1282   -811   2796       C  
ATOM   5717  O   SER B1090     -53.960 -10.955  76.288  1.00105.48           O  
ANISOU 5717  O   SER B1090    13610  15622  10848  -1339   -782   2783       O  
ATOM   5718  CB  SER B1090     -53.956 -11.765  79.350  1.00107.61           C  
ANISOU 5718  CB  SER B1090    14097  15930  10861  -1624   -978   3155       C  
ATOM   5719  OG  SER B1090     -54.374 -10.486  79.798  1.00115.08           O  
ANISOU 5719  OG  SER B1090    14940  17159  11627  -1538   -767   3109       O  
ATOM   5720  N   LEU B1091     -52.802  -9.357  77.435  1.00100.20           N  
ANISOU 5720  N   LEU B1091    12959  15003  10109  -1113   -683   2693       N  
ATOM   5721  CA  LEU B1091     -53.078  -8.234  76.533  1.00 98.00           C  
ANISOU 5721  CA  LEU B1091    12565  14851   9818   -976   -508   2573       C  
ATOM   5722  C   LEU B1091     -52.330  -8.356  75.207  1.00100.04           C  
ANISOU 5722  C   LEU B1091    12815  14943  10251   -890   -528   2420       C  
ATOM   5723  O   LEU B1091     -51.380  -9.131  75.087  1.00 99.37           O  
ANISOU 5723  O   LEU B1091    12798  14640  10320   -885   -661   2356       O  
ATOM   5724  CB  LEU B1091     -52.739  -6.878  77.196  1.00 97.21           C  
ANISOU 5724  CB  LEU B1091    12444  14851   9642   -833   -395   2510       C  
ATOM   5725  CG  LEU B1091     -53.651  -6.355  78.317  1.00102.54           C  
ANISOU 5725  CG  LEU B1091    13076  15773  10110   -877   -301   2594       C  
ATOM   5726  CD1 LEU B1091     -52.994  -5.199  79.045  1.00102.13           C  
ANISOU 5726  CD1 LEU B1091    13041  15741  10021   -733   -241   2498       C  
ATOM   5727  CD2 LEU B1091     -54.996  -5.902  77.787  1.00104.71           C  
ANISOU 5727  CD2 LEU B1091    13206  16275  10304   -881   -168   2607       C  
ATOM   5728  N   ASP B1092     -52.776  -7.572  74.216  1.00 96.00           N  
ANISOU 5728  N   ASP B1092    12217  14548   9710   -824   -400   2355       N  
ATOM   5729  CA  ASP B1092     -52.210  -7.479  72.869  1.00 95.03           C  
ANISOU 5729  CA  ASP B1092    12076  14341   9688   -764   -377   2213       C  
ATOM   5730  C   ASP B1092     -51.276  -6.259  72.789  1.00 97.10           C  
ANISOU 5730  C   ASP B1092    12334  14582   9977   -617   -287   2105       C  
ATOM   5731  O   ASP B1092     -51.382  -5.366  73.632  1.00 96.71           O  
ANISOU 5731  O   ASP B1092    12280  14609   9854   -553   -230   2145       O  
ATOM   5732  CB  ASP B1092     -53.339  -7.373  71.828  1.00 97.03           C  
ANISOU 5732  CB  ASP B1092    12253  14746   9866   -813   -315   2241       C  
ATOM   5733  CG  ASP B1092     -54.431  -6.395  72.214  1.00107.93           C  
ANISOU 5733  CG  ASP B1092    13552  16347  11111   -779   -214   2335       C  
ATOM   5734  OD1 ASP B1092     -55.436  -6.836  72.810  1.00109.71           O  
ANISOU 5734  OD1 ASP B1092    13732  16696  11256   -881   -227   2449       O  
ATOM   5735  OD2 ASP B1092     -54.263  -5.185  71.953  1.00113.48           O  
ANISOU 5735  OD2 ASP B1092    14230  17094  11795   -652   -126   2288       O  
ATOM   5736  N   ALA B1093     -50.377  -6.223  71.775  1.00 92.19           N  
ANISOU 5736  N   ALA B1093    11708  13866   9453   -578   -270   1960       N  
ATOM   5737  CA  ALA B1093     -49.390  -5.157  71.547  1.00 90.86           C  
ANISOU 5737  CA  ALA B1093    11533  13669   9321   -479   -187   1853       C  
ATOM   5738  C   ALA B1093     -49.946  -3.727  71.628  1.00 93.33           C  
ANISOU 5738  C   ALA B1093    11828  14108   9526   -412    -78   1918       C  
ATOM   5739  O   ALA B1093     -49.294  -2.858  72.211  1.00 92.25           O  
ANISOU 5739  O   ALA B1093    11707  13933   9409   -335    -47   1882       O  
ATOM   5740  CB  ALA B1093     -48.683  -5.373  70.221  1.00 91.71           C  
ANISOU 5740  CB  ALA B1093    11616  13732   9497   -496   -154   1701       C  
ATOM   5741  N   VAL B1094     -51.148  -3.489  71.059  1.00 89.80           N  
ANISOU 5741  N   VAL B1094    11342  13799   8980   -437    -39   2003       N  
ATOM   5742  CA  VAL B1094     -51.809  -2.174  71.069  1.00 89.31           C  
ANISOU 5742  CA  VAL B1094    11252  13838   8842   -354     33   2060       C  
ATOM   5743  C   VAL B1094     -52.181  -1.787  72.502  1.00 92.01           C  
ANISOU 5743  C   VAL B1094    11583  14233   9143   -294     40   2104       C  
ATOM   5744  O   VAL B1094     -51.882  -0.673  72.929  1.00 91.27           O  
ANISOU 5744  O   VAL B1094    11503  14120   9056   -193     83   2070       O  
ATOM   5745  CB  VAL B1094     -53.044  -2.096  70.130  1.00 93.94           C  
ANISOU 5745  CB  VAL B1094    11781  14561   9350   -385     41   2138       C  
ATOM   5746  CG1 VAL B1094     -53.472  -0.645  69.911  1.00 93.86           C  
ANISOU 5746  CG1 VAL B1094    11755  14600   9309   -275     85   2175       C  
ATOM   5747  CG2 VAL B1094     -52.778  -2.784  68.793  1.00 94.08           C  
ANISOU 5747  CG2 VAL B1094    11816  14556   9373   -481     21   2088       C  
ATOM   5748  N   ARG B1095     -52.821  -2.721  73.234  1.00 88.30           N  
ANISOU 5748  N   ARG B1095    11094  13833   8624   -374     -4   2175       N  
ATOM   5749  CA  ARG B1095     -53.247  -2.541  74.620  1.00 88.30           C  
ANISOU 5749  CA  ARG B1095    11080  13930   8542   -361     11   2219       C  
ATOM   5750  C   ARG B1095     -52.077  -2.552  75.621  1.00 92.48           C  
ANISOU 5750  C   ARG B1095    11695  14337   9106   -338    -35   2169       C  
ATOM   5751  O   ARG B1095     -52.129  -1.823  76.614  1.00 92.72           O  
ANISOU 5751  O   ARG B1095    11727  14433   9069   -276      4   2150       O  
ATOM   5752  CB  ARG B1095     -54.345  -3.541  74.982  1.00 87.49           C  
ANISOU 5752  CB  ARG B1095    10928  13965   8351   -497    -16   2331       C  
ATOM   5753  CG  ARG B1095     -55.733  -3.010  74.677  1.00 92.86           C  
ANISOU 5753  CG  ARG B1095    11475  14853   8954   -471     59   2369       C  
ATOM   5754  CD  ARG B1095     -56.678  -4.125  74.304  1.00101.27           C  
ANISOU 5754  CD  ARG B1095    12482  16013   9984   -633     17   2463       C  
ATOM   5755  NE  ARG B1095     -57.968  -3.607  73.849  1.00112.39           N  
ANISOU 5755  NE  ARG B1095    13739  17622  11344   -599     72   2484       N  
ATOM   5756  CZ  ARG B1095     -58.852  -4.307  73.144  1.00129.67           C  
ANISOU 5756  CZ  ARG B1095    15849  19899  13519   -713     35   2545       C  
ATOM   5757  NH1 ARG B1095     -58.590  -5.561  72.793  1.00117.66           N  
ANISOU 5757  NH1 ARG B1095    14403  18270  12032   -873    -55   2584       N  
ATOM   5758  NH2 ARG B1095     -60.002  -3.757  72.780  1.00118.55           N  
ANISOU 5758  NH2 ARG B1095    14285  18680  12081   -663     72   2556       N  
ATOM   5759  N   ARG B1096     -51.007  -3.336  75.337  1.00 88.26           N  
ANISOU 5759  N   ARG B1096    11222  13628   8685   -378   -123   2124       N  
ATOM   5760  CA  ARG B1096     -49.791  -3.390  76.158  1.00 87.70           C  
ANISOU 5760  CA  ARG B1096    11218  13425   8680   -348   -197   2066       C  
ATOM   5761  C   ARG B1096     -49.131  -2.008  76.165  1.00 91.37           C  
ANISOU 5761  C   ARG B1096    11680  13863   9175   -227   -121   1964       C  
ATOM   5762  O   ARG B1096     -48.625  -1.575  77.200  1.00 91.56           O  
ANISOU 5762  O   ARG B1096    11740  13870   9179   -187   -145   1933       O  
ATOM   5763  CB  ARG B1096     -48.810  -4.442  75.616  1.00 86.09           C  
ANISOU 5763  CB  ARG B1096    11041  13037   8633   -384   -308   2003       C  
ATOM   5764  CG  ARG B1096     -49.131  -5.855  76.066  1.00 91.19           C  
ANISOU 5764  CG  ARG B1096    11733  13631   9282   -500   -449   2105       C  
ATOM   5765  CD  ARG B1096     -48.109  -6.847  75.562  1.00 95.99           C  
ANISOU 5765  CD  ARG B1096    12361  14028  10084   -500   -579   2006       C  
ATOM   5766  NE  ARG B1096     -48.519  -8.221  75.852  1.00105.27           N  
ANISOU 5766  NE  ARG B1096    13595  15118  11286   -618   -735   2113       N  
ATOM   5767  CZ  ARG B1096     -47.893  -9.306  75.409  1.00122.15           C  
ANISOU 5767  CZ  ARG B1096    15752  17053  13605   -627   -880   2036       C  
ATOM   5768  NH1 ARG B1096     -46.817  -9.194  74.640  1.00113.38           N  
ANISOU 5768  NH1 ARG B1096    14584  15839  12657   -524   -866   1831       N  
ATOM   5769  NH2 ARG B1096     -48.343 -10.513  75.723  1.00109.76           N  
ANISOU 5769  NH2 ARG B1096    14255  15384  12064   -747  -1040   2154       N  
ATOM   5770  N   ALA B1097     -49.196  -1.305  75.014  1.00 87.20           N  
ANISOU 5770  N   ALA B1097    11116  13335   8680   -188    -39   1922       N  
ATOM   5771  CA  ALA B1097     -48.671   0.043  74.807  1.00 86.80           C  
ANISOU 5771  CA  ALA B1097    11073  13241   8665   -101     28   1849       C  
ATOM   5772  C   ALA B1097     -49.473   1.088  75.587  1.00 91.66           C  
ANISOU 5772  C   ALA B1097    11679  13953   9192    -14     78   1870       C  
ATOM   5773  O   ALA B1097     -48.924   2.134  75.939  1.00 91.35           O  
ANISOU 5773  O   ALA B1097    11670  13850   9190     60     97   1797       O  
ATOM   5774  CB  ALA B1097     -48.681   0.375  73.328  1.00 87.23           C  
ANISOU 5774  CB  ALA B1097    11110  13284   8749   -120     83   1840       C  
ATOM   5775  N   ALA B1098     -50.769   0.810  75.846  1.00 89.17           N  
ANISOU 5775  N   ALA B1098    11313  13796   8773    -25     99   1950       N  
ATOM   5776  CA  ALA B1098     -51.655   1.695  76.607  1.00 89.97           C  
ANISOU 5776  CA  ALA B1098    11369  14025   8791     66    156   1937       C  
ATOM   5777  C   ALA B1098     -51.349   1.586  78.102  1.00 94.65           C  
ANISOU 5777  C   ALA B1098    11998  14662   9304     57    138   1900       C  
ATOM   5778  O   ALA B1098     -51.383   2.594  78.809  1.00 94.71           O  
ANISOU 5778  O   ALA B1098    12006  14697   9282    156    177   1812       O  
ATOM   5779  CB  ALA B1098     -53.110   1.350  76.334  1.00 91.34           C  
ANISOU 5779  CB  ALA B1098    11440  14380   8884     42    189   2018       C  
ATOM   5780  N   LEU B1099     -51.026   0.365  78.569  1.00 91.53           N  
ANISOU 5780  N   LEU B1099    11644  14260   8873    -65     63   1965       N  
ATOM   5781  CA  LEU B1099     -50.673   0.077  79.957  1.00 92.50           C  
ANISOU 5781  CA  LEU B1099    11826  14423   8898   -110     11   1966       C  
ATOM   5782  C   LEU B1099     -49.331   0.741  80.303  1.00 96.91           C  
ANISOU 5782  C   LEU B1099    12453  14823   9546    -37    -37   1852       C  
ATOM   5783  O   LEU B1099     -49.181   1.262  81.409  1.00 97.13           O  
ANISOU 5783  O   LEU B1099    12514  14910   9482     -8    -38   1793       O  
ATOM   5784  CB  LEU B1099     -50.631  -1.449  80.173  1.00 92.90           C  
ANISOU 5784  CB  LEU B1099    11920  14456   8920   -267    -99   2093       C  
ATOM   5785  CG  LEU B1099     -50.612  -1.965  81.614  1.00 98.93           C  
ANISOU 5785  CG  LEU B1099    12755  15307   9527   -368   -169   2163       C  
ATOM   5786  CD1 LEU B1099     -51.948  -1.745  82.309  1.00100.60           C  
ANISOU 5786  CD1 LEU B1099    12897  15802   9526   -420    -51   2203       C  
ATOM   5787  CD2 LEU B1099     -50.288  -3.441  81.646  1.00101.46           C  
ANISOU 5787  CD2 LEU B1099    13151  15513   9888   -511   -330   2293       C  
ATOM   5788  N   ILE B1100     -48.385   0.763  79.331  1.00 93.31           N  
ANISOU 5788  N   ILE B1100    12006  14189   9260    -18    -69   1806       N  
ATOM   5789  CA  ILE B1100     -47.061   1.394  79.435  1.00 93.26           C  
ANISOU 5789  CA  ILE B1100    12035  14031   9367     33   -107   1692       C  
ATOM   5790  C   ILE B1100     -47.226   2.922  79.562  1.00 99.15           C  
ANISOU 5790  C   ILE B1100    12780  14785  10107    138    -23   1602       C  
ATOM   5791  O   ILE B1100     -46.487   3.551  80.328  1.00 99.08           O  
ANISOU 5791  O   ILE B1100    12813  14722  10113    174    -57   1507       O  
ATOM   5792  CB  ILE B1100     -46.143   0.953  78.249  1.00 95.31           C  
ANISOU 5792  CB  ILE B1100    12272  14145   9795      3   -133   1657       C  
ATOM   5793  CG1 ILE B1100     -45.595  -0.471  78.481  1.00 95.91           C  
ANISOU 5793  CG1 ILE B1100    12362  14154   9927    -67   -268   1687       C  
ATOM   5794  CG2 ILE B1100     -44.990   1.942  77.985  1.00 95.58           C  
ANISOU 5794  CG2 ILE B1100    12305  14060   9950     45   -115   1534       C  
ATOM   5795  CD1 ILE B1100     -45.235  -1.246  77.219  1.00102.88           C  
ANISOU 5795  CD1 ILE B1100    13198  14954  10939   -104   -275   1658       C  
ATOM   5796  N   ASN B1101     -48.218   3.503  78.842  1.00 97.07           N  
ANISOU 5796  N   ASN B1101    12471  14580   9830    190     65   1629       N  
ATOM   5797  CA  ASN B1101     -48.531   4.938  78.875  1.00 98.20           C  
ANISOU 5797  CA  ASN B1101    12614  14702   9994    307    120   1552       C  
ATOM   5798  C   ASN B1101     -48.894   5.370  80.298  1.00104.64           C  
ANISOU 5798  C   ASN B1101    13435  15629  10692    367    132   1466       C  
ATOM   5799  O   ASN B1101     -48.415   6.410  80.760  1.00104.99           O  
ANISOU 5799  O   ASN B1101    13521  15590  10781    443    125   1345       O  
ATOM   5800  CB  ASN B1101     -49.653   5.281  77.888  1.00 99.57           C  
ANISOU 5800  CB  ASN B1101    12730  14928  10175    356    175   1617       C  
ATOM   5801  CG  ASN B1101     -49.795   6.757  77.605  1.00125.05           C  
ANISOU 5801  CG  ASN B1101    15975  18055  13485    478    189   1554       C  
ATOM   5802  OD1 ASN B1101     -50.337   7.523  78.410  1.00122.40           O  
ANISOU 5802  OD1 ASN B1101    15620  17767  13121    592    208   1462       O  
ATOM   5803  ND2 ASN B1101     -49.331   7.184  76.440  1.00116.04           N  
ANISOU 5803  ND2 ASN B1101    14873  16772  12444    450    175   1599       N  
ATOM   5804  N   MET B1102     -49.693   4.536  81.001  1.00102.42           N  
ANISOU 5804  N   MET B1102    13118  15543  10254    312    148   1525       N  
ATOM   5805  CA  MET B1102     -50.110   4.745  82.390  1.00104.01           C  
ANISOU 5805  CA  MET B1102    13317  15914  10287    327    176   1450       C  
ATOM   5806  C   MET B1102     -48.919   4.621  83.349  1.00109.26           C  
ANISOU 5806  C   MET B1102    14081  16509  10923    278     82   1397       C  
ATOM   5807  O   MET B1102     -48.783   5.448  84.251  1.00110.22           O  
ANISOU 5807  O   MET B1102    14230  16667  10981    341     94   1259       O  
ATOM   5808  CB  MET B1102     -51.209   3.743  82.776  1.00107.00           C  
ANISOU 5808  CB  MET B1102    13631  16533  10492    225    218   1560       C  
ATOM   5809  CG  MET B1102     -52.589   4.178  82.348  1.00111.34           C  
ANISOU 5809  CG  MET B1102    14047  17236  11023    305    327   1544       C  
ATOM   5810  SD  MET B1102     -53.859   2.909  82.581  1.00116.26           S  
ANISOU 5810  SD  MET B1102    14569  18139  11464    142    378   1691       S  
ATOM   5811  CE  MET B1102     -54.190   3.091  84.306  1.00115.16           C  
ANISOU 5811  CE  MET B1102    14420  18264  11070    100    450   1592       C  
ATOM   5812  N   VAL B1103     -48.062   3.585  83.151  1.00105.23           N  
ANISOU 5812  N   VAL B1103    13619  15895  10467    173    -26   1493       N  
ATOM   5813  CA  VAL B1103     -46.865   3.302  83.961  1.00105.31           C  
ANISOU 5813  CA  VAL B1103    13712  15822  10480    124   -157   1463       C  
ATOM   5814  C   VAL B1103     -45.854   4.458  83.870  1.00110.46           C  
ANISOU 5814  C   VAL B1103    14385  16310  11274    211   -173   1308       C  
ATOM   5815  O   VAL B1103     -45.220   4.800  84.867  1.00110.60           O  
ANISOU 5815  O   VAL B1103    14457  16325  11240    212   -243   1218       O  
ATOM   5816  CB  VAL B1103     -46.276   1.889  83.651  1.00108.18           C  
ANISOU 5816  CB  VAL B1103    14098  16092  10913     18   -287   1591       C  
ATOM   5817  CG1 VAL B1103     -44.881   1.693  84.252  1.00108.22           C  
ANISOU 5817  CG1 VAL B1103    14162  15965  10993      2   -449   1542       C  
ATOM   5818  CG2 VAL B1103     -47.220   0.791  84.141  1.00108.66           C  
ANISOU 5818  CG2 VAL B1103    14174  16313  10798   -101   -304   1749       C  
ATOM   5819  N   PHE B1104     -45.775   5.105  82.699  1.00108.05           N  
ANISOU 5819  N   PHE B1104    14042  15882  11131    267   -110   1282       N  
ATOM   5820  CA  PHE B1104     -44.914   6.267  82.463  1.00108.67           C  
ANISOU 5820  CA  PHE B1104    14142  15796  11352    321   -116   1157       C  
ATOM   5821  C   PHE B1104     -45.419   7.500  83.238  1.00114.75           C  
ANISOU 5821  C   PHE B1104    14938  16605  12055    423    -71   1024       C  
ATOM   5822  O   PHE B1104     -44.616   8.347  83.634  1.00115.21           O  
ANISOU 5822  O   PHE B1104    15042  16550  12184    447   -116    897       O  
ATOM   5823  CB  PHE B1104     -44.871   6.589  80.961  1.00109.55           C  
ANISOU 5823  CB  PHE B1104    14220  15790  11614    322    -57   1201       C  
ATOM   5824  CG  PHE B1104     -43.578   6.244  80.262  1.00110.52           C  
ANISOU 5824  CG  PHE B1104    14326  15779  11886    242   -103   1192       C  
ATOM   5825  CD1 PHE B1104     -43.344   4.957  79.791  1.00112.84           C  
ANISOU 5825  CD1 PHE B1104    14577  16092  12203    173   -137   1263       C  
ATOM   5826  CD2 PHE B1104     -42.619   7.221  80.018  1.00113.09           C  
ANISOU 5826  CD2 PHE B1104    14666  15962  12341    230   -109   1099       C  
ATOM   5827  CE1 PHE B1104     -42.160   4.647  79.113  1.00113.48           C  
ANISOU 5827  CE1 PHE B1104    14613  16072  12435    113   -166   1214       C  
ATOM   5828  CE2 PHE B1104     -41.437   6.910  79.337  1.00115.60           C  
ANISOU 5828  CE2 PHE B1104    14934  16194  12793    144   -129   1071       C  
ATOM   5829  CZ  PHE B1104     -41.215   5.625  78.891  1.00113.01           C  
ANISOU 5829  CZ  PHE B1104    14545  15906  12486     96   -152   1116       C  
ATOM   5830  N   GLN B1105     -46.749   7.582  83.449  1.00112.08           N  
ANISOU 5830  N   GLN B1105    14559  16433  11594    484     16   1035       N  
ATOM   5831  CA  GLN B1105     -47.434   8.685  84.115  1.00113.69           C  
ANISOU 5831  CA  GLN B1105    14755  16699  11741    607     73    880       C  
ATOM   5832  C   GLN B1105     -47.338   8.919  85.631  1.00121.04           C  
ANISOU 5832  C   GLN B1105    15726  17763  12501    614     57    732       C  
ATOM   5833  O   GLN B1105     -46.953  10.008  86.049  1.00121.94           O  
ANISOU 5833  O   GLN B1105    15883  17777  12673    693     36    557       O  
ATOM   5834  CB  GLN B1105     -48.936   8.636  83.806  1.00115.15           C  
ANISOU 5834  CB  GLN B1105    14841  17051  11860    676    176    919       C  
ATOM   5835  CG  GLN B1105     -49.639   9.982  83.878  1.00128.16           C  
ANISOU 5835  CG  GLN B1105    16453  18672  13572    855    224    755       C  
ATOM   5836  CD  GLN B1105     -51.024   9.939  83.274  1.00147.44           C  
ANISOU 5836  CD  GLN B1105    18771  21238  16011    935    300    807       C  
ATOM   5837  OE1 GLN B1105     -51.526   8.891  82.845  1.00142.54           O  
ANISOU 5837  OE1 GLN B1105    18091  20748  15319    841    328    966       O  
ATOM   5838  NE2 GLN B1105     -51.679  11.090  83.221  1.00140.73           N  
ANISOU 5838  NE2 GLN B1105    17874  20340  15257   1116    317    665       N  
ATOM   5839  N   MET B1106     -47.716   7.915  86.446  1.00119.00           N  
ANISOU 5839  N   MET B1106    15462  17731  12023    516     62    803       N  
ATOM   5840  CA  MET B1106     -47.749   8.017  87.908  1.00121.17           C  
ANISOU 5840  CA  MET B1106    15778  18191  12071    488     56    683       C  
ATOM   5841  C   MET B1106     -46.892   6.916  88.563  1.00125.25           C  
ANISOU 5841  C   MET B1106    16381  18734  12475    325    -81    807       C  
ATOM   5842  O   MET B1106     -46.731   6.906  89.791  1.00126.55           O  
ANISOU 5842  O   MET B1106    16608  19044  12432    268   -122    736       O  
ATOM   5843  CB  MET B1106     -49.143   8.132  88.576  1.00125.50           C  
ANISOU 5843  CB  MET B1106    16241  19042  12401    522    200    604       C  
ATOM   5844  CG  MET B1106     -50.339   7.978  87.633  1.00128.71           C  
ANISOU 5844  CG  MET B1106    16517  19518  12870    577    310    688       C  
ATOM   5845  SD  MET B1106     -50.714   6.268  87.172  1.00131.70           S  
ANISOU 5845  SD  MET B1106    16872  20005  13164    383    294    986       S  
ATOM   5846  CE  MET B1106     -52.291   6.504  86.363  1.00128.67           C  
ANISOU 5846  CE  MET B1106    16306  19761  12821    482    440    986       C  
ATOM   5847  N   GLY B1107     -46.335   6.029  87.740  1.00120.15           N  
ANISOU 5847  N   GLY B1107    15739  17943  11969    256   -164    977       N  
ATOM   5848  CA  GLY B1107     -45.503   4.919  88.192  1.00119.98           C  
ANISOU 5848  CA  GLY B1107    15788  17893  11905    126   -328   1103       C  
ATOM   5849  C   GLY B1107     -46.258   3.607  88.269  1.00124.20           C  
ANISOU 5849  C   GLY B1107    16322  18573  12294     -1   -335   1309       C  
ATOM   5850  O   GLY B1107     -47.456   3.564  87.979  1.00123.52           O  
ANISOU 5850  O   GLY B1107    16164  18638  12129      2   -193   1347       O  
ATOM   5851  N   GLU B1108     -45.561   2.530  88.669  1.00121.90           N  
ANISOU 5851  N   GLU B1108    16108  18228  11981   -116   -515   1445       N  
ATOM   5852  CA  GLU B1108     -46.125   1.182  88.787  1.00122.78           C  
ANISOU 5852  CA  GLU B1108    16250  18426  11976   -265   -571   1665       C  
ATOM   5853  C   GLU B1108     -47.120   1.021  89.935  1.00130.22           C  
ANISOU 5853  C   GLU B1108    17229  19677  12571   -389   -503   1720       C  
ATOM   5854  O   GLU B1108     -48.121   0.324  89.761  1.00130.28           O  
ANISOU 5854  O   GLU B1108    17202  19820  12477   -492   -432   1860       O  
ATOM   5855  CB  GLU B1108     -45.012   0.138  88.905  1.00124.40           C  
ANISOU 5855  CB  GLU B1108    16536  18440  12291   -334   -822   1783       C  
ATOM   5856  CG  GLU B1108     -44.340  -0.175  87.581  1.00134.46           C  
ANISOU 5856  CG  GLU B1108    17739  19461  13888   -257   -862   1771       C  
ATOM   5857  CD  GLU B1108     -43.081  -1.015  87.670  1.00158.27           C  
ANISOU 5857  CD  GLU B1108    20797  22269  17071   -273  -1114   1812       C  
ATOM   5858  OE1 GLU B1108     -42.983  -1.871  88.580  1.00153.89           O  
ANISOU 5858  OE1 GLU B1108    20347  21734  16389   -383  -1299   1955       O  
ATOM   5859  OE2 GLU B1108     -42.200  -0.835  86.800  1.00154.62           O  
ANISOU 5859  OE2 GLU B1108    20253  21623  16870   -181  -1132   1703       O  
ATOM   5860  N   THR B1109     -46.836   1.638  91.108  1.00129.25           N  
ANISOU 5860  N   THR B1109    17173  19681  12255   -399   -525   1604       N  
ATOM   5861  CA  THR B1109     -47.688   1.579  92.306  1.00131.88           C  
ANISOU 5861  CA  THR B1109    17542  20352  12216   -533   -446   1619       C  
ATOM   5862  C   THR B1109     -49.056   2.247  92.055  1.00136.63           C  
ANISOU 5862  C   THR B1109    17995  21182  12737   -465   -176   1499       C  
ATOM   5863  O   THR B1109     -50.076   1.768  92.562  1.00138.14           O  
ANISOU 5863  O   THR B1109    18155  21659  12671   -611    -75   1585       O  
ATOM   5864  CB  THR B1109     -46.937   2.132  93.539  1.00142.34           C  
ANISOU 5864  CB  THR B1109    18974  21745  13364   -550   -546   1491       C  
ATOM   5865  OG1 THR B1109     -45.621   1.575  93.584  1.00141.55           O  
ANISOU 5865  OG1 THR B1109    18976  21397  13410   -574   -814   1587       O  
ATOM   5866  CG2 THR B1109     -47.654   1.835  94.855  1.00143.97           C  
ANISOU 5866  CG2 THR B1109    19248  22316  13137   -743   -501   1544       C  
ATOM   5867  N   GLY B1110     -49.057   3.317  91.256  1.00131.80           N  
ANISOU 5867  N   GLY B1110    17287  20438  12354   -255    -75   1311       N  
ATOM   5868  CA  GLY B1110     -50.259   4.047  90.865  1.00131.80           C  
ANISOU 5868  CA  GLY B1110    17132  20590  12356   -139    142   1180       C  
ATOM   5869  C   GLY B1110     -51.175   3.216  89.988  1.00134.45           C  
ANISOU 5869  C   GLY B1110    17372  20973  12740   -204    206   1362       C  
ATOM   5870  O   GLY B1110     -52.379   3.140  90.246  1.00135.35           O  
ANISOU 5870  O   GLY B1110    17374  21370  12682   -253    358   1354       O  
ATOM   5871  N   VAL B1111     -50.592   2.552  88.969  1.00128.85           N  
ANISOU 5871  N   VAL B1111    16696  20001  12259   -216     89   1515       N  
ATOM   5872  CA  VAL B1111     -51.298   1.677  88.023  1.00127.64           C  
ANISOU 5872  CA  VAL B1111    16472  19843  12182   -285    114   1689       C  
ATOM   5873  C   VAL B1111     -51.782   0.399  88.732  1.00133.41           C  
ANISOU 5873  C   VAL B1111    17253  20760  12676   -533     69   1899       C  
ATOM   5874  O   VAL B1111     -52.875  -0.088  88.425  1.00133.38           O  
ANISOU 5874  O   VAL B1111    17150  20919  12607   -621    165   1992       O  
ATOM   5875  CB  VAL B1111     -50.478   1.396  86.731  1.00128.94           C  
ANISOU 5875  CB  VAL B1111    16660  19683  12649   -222      8   1748       C  
ATOM   5876  CG1 VAL B1111     -51.309   0.648  85.689  1.00127.94           C  
ANISOU 5876  CG1 VAL B1111    16450  19568  12595   -276     49   1884       C  
ATOM   5877  CG2 VAL B1111     -49.953   2.693  86.134  1.00127.61           C  
ANISOU 5877  CG2 VAL B1111    16463  19344  12678    -23     47   1563       C  
ATOM   5878  N   ALA B1112     -50.995  -0.106  89.715  1.00131.54           N  
ANISOU 5878  N   ALA B1112    17170  20506  12304   -659    -86   1979       N  
ATOM   5879  CA  ALA B1112     -51.353  -1.283  90.517  1.00133.57           C  
ANISOU 5879  CA  ALA B1112    17514  20921  12314   -923   -164   2206       C  
ATOM   5880  C   ALA B1112     -52.548  -0.991  91.440  1.00140.45           C  
ANISOU 5880  C   ALA B1112    18305  22214  12844  -1035     36   2156       C  
ATOM   5881  O   ALA B1112     -53.277  -1.914  91.800  1.00141.22           O  
ANISOU 5881  O   ALA B1112    18412  22500  12743  -1272     48   2350       O  
ATOM   5882  CB  ALA B1112     -50.161  -1.760  91.329  1.00135.14           C  
ANISOU 5882  CB  ALA B1112    17903  20980  12463  -1007   -407   2296       C  
ATOM   5883  N   GLY B1113     -52.756   0.290  91.764  1.00138.35           N  
ANISOU 5883  N   GLY B1113    17949  22090  12527   -867    194   1887       N  
ATOM   5884  CA  GLY B1113     -53.858   0.774  92.590  1.00141.15           C  
ANISOU 5884  CA  GLY B1113    18185  22857  12588   -918    412   1752       C  
ATOM   5885  C   GLY B1113     -55.231   0.523  91.992  1.00146.32           C  
ANISOU 5885  C   GLY B1113    18639  23712  13242   -956    588   1789       C  
ATOM   5886  O   GLY B1113     -56.206   0.367  92.733  1.00148.58           O  
ANISOU 5886  O   GLY B1113    18831  24383  13238  -1114    743   1780       O  
ATOM   5887  N   PHE B1114     -55.317   0.473  90.644  1.00141.23           N  
ANISOU 5887  N   PHE B1114    17920  22829  12912   -825    565   1828       N  
ATOM   5888  CA  PHE B1114     -56.557   0.193  89.916  1.00141.52           C  
ANISOU 5888  CA  PHE B1114    17765  23015  12992   -852    694   1876       C  
ATOM   5889  C   PHE B1114     -56.765  -1.333  89.918  1.00146.52           C  
ANISOU 5889  C   PHE B1114    18477  23667  13527  -1156    594   2189       C  
ATOM   5890  O   PHE B1114     -56.438  -2.019  88.943  1.00144.17           O  
ANISOU 5890  O   PHE B1114    18232  23095  13452  -1165    461   2337       O  
ATOM   5891  CB  PHE B1114     -56.506   0.769  88.483  1.00140.77           C  
ANISOU 5891  CB  PHE B1114    17584  22652  13249   -605    684   1799       C  
ATOM   5892  CG  PHE B1114     -56.056   2.208  88.367  1.00141.85           C  
ANISOU 5892  CG  PHE B1114    17701  22658  13536   -320    716   1537       C  
ATOM   5893  CD1 PHE B1114     -56.929   3.253  88.642  1.00146.87           C  
ANISOU 5893  CD1 PHE B1114    18162  23513  14131   -162    885   1296       C  
ATOM   5894  CD2 PHE B1114     -54.769   2.518  87.953  1.00142.10           C  
ANISOU 5894  CD2 PHE B1114    17880  22341  13769   -213    571   1523       C  
ATOM   5895  CE1 PHE B1114     -56.511   4.583  88.527  1.00147.50           C  
ANISOU 5895  CE1 PHE B1114    18241  23428  14374     99    887   1059       C  
ATOM   5896  CE2 PHE B1114     -54.353   3.848  87.840  1.00144.62           C  
ANISOU 5896  CE2 PHE B1114    18194  22524  14233     20    590   1298       C  
ATOM   5897  CZ  PHE B1114     -55.227   4.871  88.125  1.00144.41           C  
ANISOU 5897  CZ  PHE B1114    18018  22681  14170    174    738   1074       C  
ATOM   5898  N   THR B1115     -57.274  -1.852  91.055  1.00146.10           N  
ANISOU 5898  N   THR B1115    18443  23938  13129  -1417    652   2282       N  
ATOM   5899  CA  THR B1115     -57.504  -3.272  91.349  1.00147.25           C  
ANISOU 5899  CA  THR B1115    18694  24137  13119  -1759    549   2596       C  
ATOM   5900  C   THR B1115     -58.490  -3.963  90.395  1.00150.37           C  
ANISOU 5900  C   THR B1115    18944  24559  13630  -1853    596   2723       C  
ATOM   5901  O   THR B1115     -58.080  -4.845  89.636  1.00148.42           O  
ANISOU 5901  O   THR B1115    18802  24007  13583  -1908    414   2906       O  
ATOM   5902  CB  THR B1115     -57.888  -3.455  92.834  1.00160.36           C  
ANISOU 5902  CB  THR B1115    20397  26191  14341  -2026    632   2644       C  
ATOM   5903  OG1 THR B1115     -57.028  -2.660  93.651  1.00161.66           O  
ANISOU 5903  OG1 THR B1115    20674  26346  14405  -1905    600   2477       O  
ATOM   5904  CG2 THR B1115     -57.835  -4.916  93.284  1.00160.70           C  
ANISOU 5904  CG2 THR B1115    20628  26217  14214  -2402    457   3010       C  
ATOM   5905  N   ASN B1116     -59.783  -3.579  90.461  1.00148.21           N  
ANISOU 5905  N   ASN B1116    18420  24660  13234  -1875    833   2608       N  
ATOM   5906  CA  ASN B1116     -60.868  -4.144  89.654  1.00147.92           C  
ANISOU 5906  CA  ASN B1116    18203  24721  13277  -1978    899   2701       C  
ATOM   5907  C   ASN B1116     -60.662  -3.921  88.159  1.00147.72           C  
ANISOU 5907  C   ASN B1116    18131  24363  13632  -1728    819   2651       C  
ATOM   5908  O   ASN B1116     -61.014  -4.792  87.363  1.00146.72           O  
ANISOU 5908  O   ASN B1116    17989  24135  13623  -1850    742   2815       O  
ATOM   5909  CB  ASN B1116     -62.226  -3.586  90.096  1.00151.36           C  
ANISOU 5909  CB  ASN B1116    18342  25649  13517  -2005   1176   2529       C  
ATOM   5910  CG  ASN B1116     -62.552  -3.825  91.550  1.00176.80           C  
ANISOU 5910  CG  ASN B1116    21584  29273  16318  -2292   1293   2568       C  
ATOM   5911  OD1 ASN B1116     -62.369  -4.921  92.090  1.00171.90           O  
ANISOU 5911  OD1 ASN B1116    21147  28659  15508  -2631   1178   2853       O  
ATOM   5912  ND2 ASN B1116     -63.066  -2.802  92.210  1.00170.80           N  
ANISOU 5912  ND2 ASN B1116    20636  28861  15399  -2168   1518   2277       N  
ATOM   5913  N   SER B1117     -60.073  -2.770  87.785  1.00141.79           N  
ANISOU 5913  N   SER B1117    17371  23441  13062  -1399    829   2430       N  
ATOM   5914  CA  SER B1117     -59.789  -2.409  86.399  1.00138.61           C  
ANISOU 5914  CA  SER B1117    16941  22735  12988  -1165    759   2375       C  
ATOM   5915  C   SER B1117     -58.866  -3.432  85.723  1.00140.09           C  
ANISOU 5915  C   SER B1117    17331  22556  13341  -1252    538   2572       C  
ATOM   5916  O   SER B1117     -59.152  -3.844  84.599  1.00138.20           O  
ANISOU 5916  O   SER B1117    17040  22193  13277  -1244    492   2633       O  
ATOM   5917  CB  SER B1117     -59.187  -1.009  86.323  1.00140.93           C  
ANISOU 5917  CB  SER B1117    17234  22903  13409   -847    790   2130       C  
ATOM   5918  OG  SER B1117     -60.077  -0.039  86.851  1.00151.77           O  
ANISOU 5918  OG  SER B1117    18405  24586  14676   -730    981   1911       O  
ATOM   5919  N   LEU B1118     -57.801  -3.878  86.432  1.00136.58           N  
ANISOU 5919  N   LEU B1118    17105  21953  12835  -1340    395   2662       N  
ATOM   5920  CA  LEU B1118     -56.827  -4.853  85.931  1.00134.88           C  
ANISOU 5920  CA  LEU B1118    17076  21383  12790  -1403    168   2817       C  
ATOM   5921  C   LEU B1118     -57.419  -6.223  85.582  1.00139.92           C  
ANISOU 5921  C   LEU B1118    17732  22006  13427  -1659     81   3043       C  
ATOM   5922  O   LEU B1118     -57.162  -6.715  84.481  1.00138.07           O  
ANISOU 5922  O   LEU B1118    17517  21520  13422  -1616    -21   3072       O  
ATOM   5923  CB  LEU B1118     -55.632  -5.001  86.887  1.00135.20           C  
ANISOU 5923  CB  LEU B1118    17324  21284  12761  -1435     15   2857       C  
ATOM   5924  CG  LEU B1118     -54.545  -3.937  86.782  1.00138.02           C  
ANISOU 5924  CG  LEU B1118    17721  21460  13263  -1171     -3   2657       C  
ATOM   5925  CD1 LEU B1118     -53.725  -3.883  88.050  1.00139.44           C  
ANISOU 5925  CD1 LEU B1118    18055  21650  13276  -1228   -103   2668       C  
ATOM   5926  CD2 LEU B1118     -53.634  -4.190  85.582  1.00138.12           C  
ANISOU 5926  CD2 LEU B1118    17781  21106  13592  -1045   -138   2646       C  
ATOM   5927  N   ARG B1119     -58.210  -6.830  86.501  1.00139.12           N  
ANISOU 5927  N   ARG B1119    17621  22176  13061  -1938    125   3194       N  
ATOM   5928  CA  ARG B1119     -58.841  -8.142  86.278  1.00140.09           C  
ANISOU 5928  CA  ARG B1119    17767  22295  13166  -2227     39   3426       C  
ATOM   5929  C   ARG B1119     -59.823  -8.143  85.099  1.00142.96           C  
ANISOU 5929  C   ARG B1119    17926  22722  13670  -2187    134   3376       C  
ATOM   5930  O   ARG B1119     -59.816  -9.091  84.317  1.00141.96           O  
ANISOU 5930  O   ARG B1119    17855  22383  13701  -2286     -6   3494       O  
ATOM   5931  CB  ARG B1119     -59.445  -8.748  87.567  1.00143.44           C  
ANISOU 5931  CB  ARG B1119    18237  23014  13249  -2572     68   3616       C  
ATOM   5932  CG  ARG B1119     -60.568  -7.943  88.221  1.00155.35           C  
ANISOU 5932  CG  ARG B1119    19515  25017  14493  -2608    356   3488       C  
ATOM   5933  CD  ARG B1119     -61.040  -8.581  89.511  1.00167.59           C  
ANISOU 5933  CD  ARG B1119    21131  26872  15676  -2984    386   3683       C  
ATOM   5934  NE  ARG B1119     -62.256  -7.943  90.021  1.00178.10           N  
ANISOU 5934  NE  ARG B1119    22192  28716  16761  -3045    684   3542       N  
ATOM   5935  CZ  ARG B1119     -62.892  -8.315  91.129  1.00195.94           C  
ANISOU 5935  CZ  ARG B1119    24437  31359  18653  -3382    791   3661       C  
ATOM   5936  NH1 ARG B1119     -63.992  -7.681  91.513  1.00186.62           N  
ANISOU 5936  NH1 ARG B1119    22969  30661  17275  -3406   1082   3482       N  
ATOM   5937  NH2 ARG B1119     -62.434  -9.323  91.861  1.00183.52           N  
ANISOU 5937  NH2 ARG B1119    23130  29695  16905  -3700    603   3957       N  
ATOM   5938  N   MET B1120     -60.600  -7.047  84.935  1.00139.30           N  
ANISOU 5938  N   MET B1120    17229  22525  13172  -2019    350   3183       N  
ATOM   5939  CA  MET B1120     -61.560  -6.864  83.840  1.00138.45           C  
ANISOU 5939  CA  MET B1120    16906  22504  13195  -1946    434   3116       C  
ATOM   5940  C   MET B1120     -60.845  -6.805  82.489  1.00137.84           C  
ANISOU 5940  C   MET B1120    16896  22065  13412  -1744    308   3061       C  
ATOM   5941  O   MET B1120     -61.374  -7.318  81.503  1.00137.07           O  
ANISOU 5941  O   MET B1120    16727  21923  13430  -1797    267   3107       O  
ATOM   5942  CB  MET B1120     -62.416  -5.606  84.057  1.00141.90           C  
ANISOU 5942  CB  MET B1120    17088  23273  13554  -1768    660   2902       C  
ATOM   5943  CG  MET B1120     -63.511  -5.794  85.089  1.00149.28           C  
ANISOU 5943  CG  MET B1120    17862  24652  14205  -2003    826   2934       C  
ATOM   5944  SD  MET B1120     -64.681  -4.414  85.161  1.00155.26           S  
ANISOU 5944  SD  MET B1120    18256  25805  14930  -1769   1084   2640       S  
ATOM   5945  CE  MET B1120     -63.789  -3.277  86.198  1.00151.88           C  
ANISOU 5945  CE  MET B1120    17936  25371  14399  -1557   1147   2437       C  
ATOM   5946  N   LEU B1121     -59.629  -6.209  82.459  1.00131.27           N  
ANISOU 5946  N   LEU B1121    16200  20991  12686  -1534    247   2960       N  
ATOM   5947  CA  LEU B1121     -58.787  -6.116  81.260  1.00127.94           C  
ANISOU 5947  CA  LEU B1121    15851  20243  12517  -1360    142   2896       C  
ATOM   5948  C   LEU B1121     -58.305  -7.516  80.849  1.00130.11           C  
ANISOU 5948  C   LEU B1121    16277  20262  12897  -1532    -52   3045       C  
ATOM   5949  O   LEU B1121     -58.230  -7.812  79.658  1.00128.29           O  
ANISOU 5949  O   LEU B1121    16036  19871  12838  -1487   -112   3017       O  
ATOM   5950  CB  LEU B1121     -57.587  -5.171  81.485  1.00126.45           C  
ANISOU 5950  CB  LEU B1121    15761  19889  12397  -1137    131   2756       C  
ATOM   5951  CG  LEU B1121     -57.884  -3.666  81.602  1.00130.87           C  
ANISOU 5951  CG  LEU B1121    16192  20597  12934   -910    288   2570       C  
ATOM   5952  CD1 LEU B1121     -56.709  -2.927  82.210  1.00130.14           C  
ANISOU 5952  CD1 LEU B1121    16223  20366  12857   -772    261   2463       C  
ATOM   5953  CD2 LEU B1121     -58.268  -3.048  80.257  1.00132.26           C  
ANISOU 5953  CD2 LEU B1121    16254  20721  13277   -744    322   2489       C  
ATOM   5954  N   GLN B1122     -58.009  -8.382  81.840  1.00127.20           N  
ANISOU 5954  N   GLN B1122    16052  19857  12421  -1735   -162   3199       N  
ATOM   5955  CA  GLN B1122     -57.591  -9.763  81.598  1.00127.07           C  
ANISOU 5955  CA  GLN B1122    16190  19575  12516  -1906   -378   3348       C  
ATOM   5956  C   GLN B1122     -58.813 -10.598  81.212  1.00132.10           C  
ANISOU 5956  C   GLN B1122    16737  20341  13114  -2140   -369   3475       C  
ATOM   5957  O   GLN B1122     -58.706 -11.466  80.344  1.00131.45           O  
ANISOU 5957  O   GLN B1122    16706  20035  13203  -2197   -506   3508       O  
ATOM   5958  CB  GLN B1122     -56.886 -10.349  82.828  1.00129.70           C  
ANISOU 5958  CB  GLN B1122    16718  19814  12749  -2044   -530   3493       C  
ATOM   5959  CG  GLN B1122     -56.109 -11.632  82.531  1.00140.53           C  
ANISOU 5959  CG  GLN B1122    18272  20809  14314  -2132   -804   3602       C  
ATOM   5960  CD  GLN B1122     -55.126 -12.016  83.609  1.00159.26           C  
ANISOU 5960  CD  GLN B1122    20844  23021  16648  -2182   -997   3708       C  
ATOM   5961  OE1 GLN B1122     -55.169 -11.532  84.748  1.00156.17           O  
ANISOU 5961  OE1 GLN B1122    20480  22835  16021  -2237   -934   3757       O  
ATOM   5962  NE2 GLN B1122     -54.218 -12.917  83.270  1.00150.31           N  
ANISOU 5962  NE2 GLN B1122    19850  21515  15748  -2163  -1249   3737       N  
ATOM   5963  N   GLN B1123     -59.983 -10.300  81.826  1.00129.97           N  
ANISOU 5963  N   GLN B1123    16313  20444  12624  -2271   -201   3520       N  
ATOM   5964  CA  GLN B1123     -61.267 -10.958  81.545  1.00131.17           C  
ANISOU 5964  CA  GLN B1123    16331  20790  12717  -2508   -161   3629       C  
ATOM   5965  C   GLN B1123     -61.852 -10.479  80.193  1.00133.12           C  
ANISOU 5965  C   GLN B1123    16391  21075  13115  -2342    -87   3483       C  
ATOM   5966  O   GLN B1123     -62.960 -10.887  79.828  1.00134.25           O  
ANISOU 5966  O   GLN B1123    16385  21395  13229  -2505    -49   3539       O  
ATOM   5967  CB  GLN B1123     -62.275 -10.721  82.691  1.00134.94           C  
ANISOU 5967  CB  GLN B1123    16673  21696  12901  -2698     16   3694       C  
ATOM   5968  CG  GLN B1123     -61.967 -11.467  83.995  1.00147.14           C  
ANISOU 5968  CG  GLN B1123    18411  23253  14244  -2976    -75   3906       C  
ATOM   5969  CD  GLN B1123     -62.393 -12.912  83.996  1.00163.84           C  
ANISOU 5969  CD  GLN B1123    20624  25278  16351  -3341   -234   4161       C  
ATOM   5970  OE1 GLN B1123     -63.545 -13.256  83.708  1.00160.33           O  
ANISOU 5970  OE1 GLN B1123    20011  25052  15857  -3535   -151   4216       O  
ATOM   5971  NE2 GLN B1123     -61.486 -13.788  84.394  1.00154.89           N  
ANISOU 5971  NE2 GLN B1123    19765  23822  15264  -3455   -479   4329       N  
ATOM   5972  N   LYS B1124     -61.093  -9.623  79.460  1.00126.24           N  
ANISOU 5972  N   LYS B1124    15532  20038  12395  -2037    -79   3308       N  
ATOM   5973  CA  LYS B1124     -61.409  -9.040  78.147  1.00124.15           C  
ANISOU 5973  CA  LYS B1124    15136  19768  12266  -1854    -36   3175       C  
ATOM   5974  C   LYS B1124     -62.657  -8.141  78.153  1.00128.34           C  
ANISOU 5974  C   LYS B1124    15404  20655  12703  -1787    141   3104       C  
ATOM   5975  O   LYS B1124     -63.346  -8.025  77.137  1.00127.55           O  
ANISOU 5975  O   LYS B1124    15167  20614  12682  -1745    145   3064       O  
ATOM   5976  CB  LYS B1124     -61.445 -10.110  77.031  1.00126.33           C  
ANISOU 5976  CB  LYS B1124    15467  19844  12690  -1970   -185   3222       C  
ATOM   5977  CG  LYS B1124     -60.136 -10.875  76.862  1.00139.81           C  
ANISOU 5977  CG  LYS B1124    17405  21175  14543  -1966   -365   3228       C  
ATOM   5978  CD  LYS B1124     -59.450 -10.555  75.543  1.00148.11           C  
ANISOU 5978  CD  LYS B1124    18477  22031  15766  -1765   -396   3067       C  
ATOM   5979  CE  LYS B1124     -58.029 -11.067  75.480  1.00159.41           C  
ANISOU 5979  CE  LYS B1124    20095  23125  17347  -1705   -538   3015       C  
ATOM   5980  NZ  LYS B1124     -57.092 -10.249  76.302  1.00167.39           N  
ANISOU 5980  NZ  LYS B1124    21167  24102  18333  -1547   -496   2965       N  
ATOM   5981  N   ARG B1125     -62.917  -7.481  79.296  1.00126.05           N  
ANISOU 5981  N   ARG B1125    15040  20604  12251  -1764    278   3069       N  
ATOM   5982  CA  ARG B1125     -64.046  -6.568  79.492  1.00127.31           C  
ANISOU 5982  CA  ARG B1125    14930  21113  12328  -1673    453   2960       C  
ATOM   5983  C   ARG B1125     -63.578  -5.113  79.343  1.00130.41           C  
ANISOU 5983  C   ARG B1125    15299  21451  12802  -1328    517   2766       C  
ATOM   5984  O   ARG B1125     -63.301  -4.435  80.335  1.00130.39           O  
ANISOU 5984  O   ARG B1125    15308  21539  12696  -1244    607   2680       O  
ATOM   5985  CB  ARG B1125     -64.714  -6.810  80.859  1.00129.71           C  
ANISOU 5985  CB  ARG B1125    15146  21751  12385  -1891    579   3019       C  
ATOM   5986  CG  ARG B1125     -65.608  -8.043  80.901  1.00140.32           C  
ANISOU 5986  CG  ARG B1125    16425  23245  13646  -2246    553   3201       C  
ATOM   5987  CD  ARG B1125     -65.542  -8.752  82.242  1.00149.04           C  
ANISOU 5987  CD  ARG B1125    17640  24475  14512  -2547    571   3360       C  
ATOM   5988  NE  ARG B1125     -66.096  -7.946  83.332  1.00156.62           N  
ANISOU 5988  NE  ARG B1125    18429  25831  15248  -2529    788   3246       N  
ATOM   5989  CZ  ARG B1125     -66.129  -8.324  84.606  1.00171.87           C  
ANISOU 5989  CZ  ARG B1125    20427  27963  16912  -2782    849   3353       C  
ATOM   5990  NH1 ARG B1125     -66.649  -7.525  85.528  1.00162.20           N  
ANISOU 5990  NH1 ARG B1125    19025  27123  15479  -2747   1066   3203       N  
ATOM   5991  NH2 ARG B1125     -65.641  -9.504  84.970  1.00157.85           N  
ANISOU 5991  NH2 ARG B1125    18900  26004  15073  -3073    683   3606       N  
ATOM   5992  N   TRP B1126     -63.472  -4.648  78.090  1.00126.02           N  
ANISOU 5992  N   TRP B1126    14724  20735  12422  -1144    456   2703       N  
ATOM   5993  CA  TRP B1126     -63.020  -3.292  77.765  1.00124.89           C  
ANISOU 5993  CA  TRP B1126    14581  20490  12381   -838    483   2549       C  
ATOM   5994  C   TRP B1126     -64.086  -2.253  78.079  1.00131.74           C  
ANISOU 5994  C   TRP B1126    15195  21639  13221   -680    609   2414       C  
ATOM   5995  O   TRP B1126     -63.762  -1.196  78.625  1.00131.43           O  
ANISOU 5995  O   TRP B1126    15158  21594  13185   -483    673   2275       O  
ATOM   5996  CB  TRP B1126     -62.568  -3.191  76.297  1.00121.69           C  
ANISOU 5996  CB  TRP B1126    14254  19835  12147   -736    368   2553       C  
ATOM   5997  CG  TRP B1126     -61.893  -4.425  75.772  1.00121.58           C  
ANISOU 5997  CG  TRP B1126    14412  19608  12174   -914    246   2661       C  
ATOM   5998  CD1 TRP B1126     -62.342  -5.241  74.777  1.00124.63           C  
ANISOU 5998  CD1 TRP B1126    14773  19972  12610  -1039    162   2728       C  
ATOM   5999  CD2 TRP B1126     -60.686  -5.022  76.266  1.00120.48           C  
ANISOU 5999  CD2 TRP B1126    14485  19251  12042   -986    180   2696       C  
ATOM   6000  NE1 TRP B1126     -61.474  -6.293  74.597  1.00123.26           N  
ANISOU 6000  NE1 TRP B1126    14785  19567  12483  -1172     54   2785       N  
ATOM   6001  CE2 TRP B1126     -60.452  -6.187  75.504  1.00124.04           C  
ANISOU 6001  CE2 TRP B1126    15025  19539  12565  -1136     57   2771       C  
ATOM   6002  CE3 TRP B1126     -59.768  -4.677  77.274  1.00121.36           C  
ANISOU 6002  CE3 TRP B1126    14715  19285  12113   -930    198   2660       C  
ATOM   6003  CZ2 TRP B1126     -59.335  -7.003  75.709  1.00122.75           C  
ANISOU 6003  CZ2 TRP B1126    15054  19127  12460  -1210    -52   2802       C  
ATOM   6004  CZ3 TRP B1126     -58.667  -5.491  77.481  1.00122.18           C  
ANISOU 6004  CZ3 TRP B1126    15008  19154  12260  -1015     83   2711       C  
ATOM   6005  CH2 TRP B1126     -58.457  -6.638  76.703  1.00122.60           C  
ANISOU 6005  CH2 TRP B1126    15136  19038  12410  -1144    -42   2778       C  
ATOM   6006  N   ASP B1127     -65.359  -2.570  77.750  1.00130.64           N  
ANISOU 6006  N   ASP B1127    14827  21744  13066   -766    638   2440       N  
ATOM   6007  CA  ASP B1127     -66.533  -1.724  77.970  1.00132.85           C  
ANISOU 6007  CA  ASP B1127    14810  22324  13345   -623    746   2299       C  
ATOM   6008  C   ASP B1127     -66.778  -1.490  79.463  1.00139.48           C  
ANISOU 6008  C   ASP B1127    15558  23435  14001   -667    917   2201       C  
ATOM   6009  O   ASP B1127     -67.170  -0.391  79.853  1.00140.09           O  
ANISOU 6009  O   ASP B1127    15474  23651  14101   -440   1010   2004       O  
ATOM   6010  CB  ASP B1127     -67.769  -2.364  77.315  1.00136.19           C  
ANISOU 6010  CB  ASP B1127    15008  22955  13783   -765    724   2368       C  
ATOM   6011  CG  ASP B1127     -68.936  -1.417  77.145  1.00147.74           C  
ANISOU 6011  CG  ASP B1127    16145  24665  15322   -556    779   2211       C  
ATOM   6012  OD1 ASP B1127     -68.925  -0.633  76.170  1.00147.21           O  
ANISOU 6012  OD1 ASP B1127    16069  24438  15425   -317    671   2164       O  
ATOM   6013  OD2 ASP B1127     -69.871  -1.472  77.976  1.00155.56           O  
ANISOU 6013  OD2 ASP B1127    16886  26017  16202   -638    925   2136       O  
ATOM   6014  N   GLU B1128     -66.516  -2.517  80.291  1.00137.74           N  
ANISOU 6014  N   GLU B1128    15455  23280  13599   -958    945   2334       N  
ATOM   6015  CA  GLU B1128     -66.697  -2.473  81.741  1.00140.49           C  
ANISOU 6015  CA  GLU B1128    15752  23911  13716  -1071   1102   2276       C  
ATOM   6016  C   GLU B1128     -65.562  -1.757  82.482  1.00144.67           C  
ANISOU 6016  C   GLU B1128    16482  24277  14207   -919   1110   2176       C  
ATOM   6017  O   GLU B1128     -65.842  -0.948  83.368  1.00145.73           O  
ANISOU 6017  O   GLU B1128    16498  24637  14237   -810   1253   1988       O  
ATOM   6018  CB  GLU B1128     -66.943  -3.880  82.305  1.00143.36           C  
ANISOU 6018  CB  GLU B1128    16170  24414  13886  -1479   1104   2494       C  
ATOM   6019  CG  GLU B1128     -68.359  -4.382  82.064  1.00157.20           C  
ANISOU 6019  CG  GLU B1128    17633  26497  15601  -1661   1178   2532       C  
ATOM   6020  CD  GLU B1128     -68.654  -5.801  82.517  1.00181.05           C  
ANISOU 6020  CD  GLU B1128    20712  29630  18447  -2098   1160   2772       C  
ATOM   6021  OE1 GLU B1128     -69.208  -6.574  81.702  1.00176.62           O  
ANISOU 6021  OE1 GLU B1128    20087  29044  17976  -2253   1074   2892       O  
ATOM   6022  OE2 GLU B1128     -68.362  -6.135  83.688  1.00176.53           O  
ANISOU 6022  OE2 GLU B1128    20255  29174  17644  -2298   1223   2845       O  
ATOM   6023  N   ALA B1129     -64.293  -2.035  82.115  1.00139.96           N  
ANISOU 6023  N   ALA B1129    16173  23301  13702   -906    958   2277       N  
ATOM   6024  CA  ALA B1129     -63.114  -1.416  82.740  1.00139.26           C  
ANISOU 6024  CA  ALA B1129    16282  23030  13599   -777    937   2193       C  
ATOM   6025  C   ALA B1129     -62.938   0.069  82.366  1.00143.56           C  
ANISOU 6025  C   ALA B1129    16771  23465  14311   -424    958   1973       C  
ATOM   6026  O   ALA B1129     -62.120   0.763  82.981  1.00142.66           O  
ANISOU 6026  O   ALA B1129    16777  23246  14180   -304    964   1860       O  
ATOM   6027  CB  ALA B1129     -61.858  -2.204  82.389  1.00137.73           C  
ANISOU 6027  CB  ALA B1129    16371  22480  13481   -870    762   2354       C  
ATOM   6028  N   ALA B1130     -63.715   0.551  81.373  1.00141.02           N  
ANISOU 6028  N   ALA B1130    16272  23159  14151   -269    951   1919       N  
ATOM   6029  CA  ALA B1130     -63.676   1.926  80.873  1.00140.85           C  
ANISOU 6029  CA  ALA B1130    16198  23005  14315     57    932   1744       C  
ATOM   6030  C   ALA B1130     -64.216   2.963  81.860  1.00147.65           C  
ANISOU 6030  C   ALA B1130    16888  24096  15118    231   1072   1493       C  
ATOM   6031  O   ALA B1130     -63.563   3.987  82.074  1.00146.51           O  
ANISOU 6031  O   ALA B1130    16835  23775  15055    439   1053   1346       O  
ATOM   6032  CB  ALA B1130     -64.422   2.022  79.553  1.00141.46           C  
ANISOU 6032  CB  ALA B1130    16139  23047  14562    144    854   1790       C  
ATOM   6033  N   VAL B1131     -65.406   2.704  82.447  1.00147.62           N  
ANISOU 6033  N   VAL B1131    16624  24490  14976    140   1214   1427       N  
ATOM   6034  CA  VAL B1131     -66.078   3.615  83.388  1.00150.57           C  
ANISOU 6034  CA  VAL B1131    16780  25149  15281    299   1373   1146       C  
ATOM   6035  C   VAL B1131     -65.311   3.750  84.715  1.00155.70           C  
ANISOU 6035  C   VAL B1131    17585  25854  15719    232   1458   1054       C  
ATOM   6036  O   VAL B1131     -65.380   4.804  85.351  1.00156.91           O  
ANISOU 6036  O   VAL B1131    17660  26081  15877    444   1538    784       O  
ATOM   6037  CB  VAL B1131     -67.581   3.264  83.605  1.00157.41           C  
ANISOU 6037  CB  VAL B1131    17289  26465  16054    203   1517   1085       C  
ATOM   6038  CG1 VAL B1131     -68.340   4.439  84.222  1.00160.31           C  
ANISOU 6038  CG1 VAL B1131    17380  27078  16453    471   1654    735       C  
ATOM   6039  CG2 VAL B1131     -68.249   2.835  82.299  1.00156.53           C  
ANISOU 6039  CG2 VAL B1131    17058  26299  16116    191   1403   1234       C  
ATOM   6040  N   ASN B1132     -64.570   2.695  85.111  1.00151.67           N  
ANISOU 6040  N   ASN B1132    17301  25292  15036    -54   1418   1273       N  
ATOM   6041  CA  ASN B1132     -63.774   2.650  86.342  1.00152.24           C  
ANISOU 6041  CA  ASN B1132    17552  25408  14886   -162   1458   1239       C  
ATOM   6042  C   ASN B1132     -62.646   3.686  86.382  1.00155.26           C  
ANISOU 6042  C   ASN B1132    18119  25466  15405     82   1372   1097       C  
ATOM   6043  O   ASN B1132     -62.397   4.275  87.435  1.00156.27           O  
ANISOU 6043  O   ASN B1132    18272  25713  15392    131   1451    907       O  
ATOM   6044  CB  ASN B1132     -63.210   1.246  86.559  1.00152.03           C  
ANISOU 6044  CB  ASN B1132    17738  25326  14702   -504   1371   1540       C  
ATOM   6045  CG  ASN B1132     -64.252   0.215  86.899  1.00174.50           C  
ANISOU 6045  CG  ASN B1132    20432  28530  17339   -811   1471   1679       C  
ATOM   6046  OD1 ASN B1132     -65.126  -0.118  86.092  1.00168.14           O  
ANISOU 6046  OD1 ASN B1132    19448  27799  16639   -839   1478   1739       O  
ATOM   6047  ND2 ASN B1132     -64.149  -0.353  88.090  1.00168.05           N  
ANISOU 6047  ND2 ASN B1132    19699  27937  16214  -1075   1533   1751       N  
ATOM   6048  N   LEU B1133     -61.974   3.906  85.239  1.00149.82           N  
ANISOU 6048  N   LEU B1133    17558  24386  14979    214   1213   1182       N  
ATOM   6049  CA  LEU B1133     -60.858   4.848  85.121  1.00148.61           C  
ANISOU 6049  CA  LEU B1133    17584  23899  14982    413   1117   1079       C  
ATOM   6050  C   LEU B1133     -61.290   6.323  84.981  1.00154.49           C  
ANISOU 6050  C   LEU B1133    18192  24605  15902    739   1149    807       C  
ATOM   6051  O   LEU B1133     -60.450   7.219  85.099  1.00153.35           O  
ANISOU 6051  O   LEU B1133    18184  24217  15864    894   1086    685       O  
ATOM   6052  CB  LEU B1133     -59.896   4.427  83.992  1.00145.59           C  
ANISOU 6052  CB  LEU B1133    17396  23140  14781    381    947   1285       C  
ATOM   6053  CG  LEU B1133     -59.189   3.072  84.146  1.00149.00           C  
ANISOU 6053  CG  LEU B1133    18001  23514  15098    107    870   1518       C  
ATOM   6054  CD1 LEU B1133     -58.738   2.544  82.808  1.00146.74           C  
ANISOU 6054  CD1 LEU B1133    17801  22953  15000     81    741   1687       C  
ATOM   6055  CD2 LEU B1133     -58.008   3.154  85.113  1.00151.23           C  
ANISOU 6055  CD2 LEU B1133    18481  23697  15283     65    823   1481       C  
ATOM   6056  N   ALA B1134     -62.596   6.567  84.749  1.00153.86           N  
ANISOU 6056  N   ALA B1134    17838  24756  15864    840   1232    707       N  
ATOM   6057  CA  ALA B1134     -63.183   7.907  84.637  1.00156.02           C  
ANISOU 6057  CA  ALA B1134    17945  25011  16327   1166   1246    435       C  
ATOM   6058  C   ALA B1134     -63.449   8.499  86.035  1.00163.93           C  
ANISOU 6058  C   ALA B1134    18840  26287  17158   1235   1406    125       C  
ATOM   6059  O   ALA B1134     -63.383   9.718  86.213  1.00164.52           O  
ANISOU 6059  O   ALA B1134    18892  26236  17383   1507   1387   -135       O  
ATOM   6060  CB  ALA B1134     -64.477   7.843  83.843  1.00157.97           C  
ANISOU 6060  CB  ALA B1134    17917  25411  16692   1245   1253    448       C  
ATOM   6061  N   LYS B1135     -63.752   7.622  87.017  1.00162.75           N  
ANISOU 6061  N   LYS B1135    18636  26514  16688    974   1557    154       N  
ATOM   6062  CA  LYS B1135     -64.018   7.977  88.415  1.00165.96           C  
ANISOU 6062  CA  LYS B1135    18947  27261  16848    965   1735   -120       C  
ATOM   6063  C   LYS B1135     -62.715   8.253  89.174  1.00169.81           C  
ANISOU 6063  C   LYS B1135    19724  27564  17233    932   1677   -161       C  
ATOM   6064  O   LYS B1135     -62.732   8.968  90.179  1.00171.92           O  
ANISOU 6064  O   LYS B1135    19950  27993  17377   1024   1778   -457       O  
ATOM   6065  CB  LYS B1135     -64.787   6.845  89.122  1.00170.07           C  
ANISOU 6065  CB  LYS B1135    19327  28259  17032    637   1907    -18       C  
ATOM   6066  CG  LYS B1135     -66.242   6.715  88.705  1.00185.68           C  
ANISOU 6066  CG  LYS B1135    20944  30543  19064    669   2018    -77       C  
ATOM   6067  CD  LYS B1135     -66.943   5.623  89.502  1.00197.42           C  
ANISOU 6067  CD  LYS B1135    22302  32518  20192    301   2200     24       C  
ATOM   6068  CE  LYS B1135     -68.395   5.468  89.117  1.00210.37           C  
ANISOU 6068  CE  LYS B1135    23554  34494  21884    309   2318    -44       C  
ATOM   6069  NZ  LYS B1135     -68.555   4.827  87.782  1.00215.51           N  
ANISOU 6069  NZ  LYS B1135    24219  34909  22755    264   2153    246       N  
ATOM   6070  N   SER B1136     -61.597   7.666  88.696  1.00163.59           N  
ANISOU 6070  N   SER B1136    19212  26452  16495    798   1512    119       N  
ATOM   6071  CA  SER B1136     -60.252   7.752  89.275  1.00162.52           C  
ANISOU 6071  CA  SER B1136    19355  26111  16286    738   1418    136       C  
ATOM   6072  C   SER B1136     -59.665   9.172  89.369  1.00167.51           C  
ANISOU 6072  C   SER B1136    20054  26483  17109   1022   1359   -138       C  
ATOM   6073  O   SER B1136     -60.132  10.088  88.686  1.00167.73           O  
ANISOU 6073  O   SER B1136    19963  26366  17401   1284   1336   -281       O  
ATOM   6074  CB  SER B1136     -59.296   6.832  88.520  1.00162.63           C  
ANISOU 6074  CB  SER B1136    19588  25823  16382    574   1248    474       C  
ATOM   6075  OG  SER B1136     -58.943   7.351  87.247  1.00169.08           O  
ANISOU 6075  OG  SER B1136    20447  26267  17528    755   1121    521       O  
ATOM   6076  N   ARG B1137     -58.615   9.326  90.211  1.00164.24           N  
ANISOU 6076  N   ARG B1137    19843  25992  16568    956   1311   -196       N  
ATOM   6077  CA  ARG B1137     -57.868  10.570  90.438  1.00164.55           C  
ANISOU 6077  CA  ARG B1137    19990  25772  16760   1167   1236   -442       C  
ATOM   6078  C   ARG B1137     -57.125  10.996  89.167  1.00166.30           C  
ANISOU 6078  C   ARG B1137    20336  25514  17337   1290   1057   -308       C  
ATOM   6079  O   ARG B1137     -56.925  12.192  88.947  1.00166.50           O  
ANISOU 6079  O   ARG B1137    20380  25294  17586   1518    996   -504       O  
ATOM   6080  CB  ARG B1137     -56.860  10.388  91.586  1.00164.88           C  
ANISOU 6080  CB  ARG B1137    20229  25862  16557   1007   1203   -475       C  
ATOM   6081  CG  ARG B1137     -57.488  10.309  92.977  1.00177.03           C  
ANISOU 6081  CG  ARG B1137    21671  27870  17722    909   1380   -682       C  
ATOM   6082  CD  ARG B1137     -56.935   9.159  93.806  1.00184.99           C  
ANISOU 6082  CD  ARG B1137    22841  29062  18386    575   1352   -457       C  
ATOM   6083  NE  ARG B1137     -55.507   9.309  94.099  1.00191.74           N  
ANISOU 6083  NE  ARG B1137    23948  29636  19267    542   1170   -423       N  
ATOM   6084  CZ  ARG B1137     -55.018   9.856  95.208  1.00207.43           C  
ANISOU 6084  CZ  ARG B1137    26027  31720  21065    537   1169   -650       C  
ATOM   6085  NH1 ARG B1137     -53.709   9.946  95.387  1.00193.46           N  
ANISOU 6085  NH1 ARG B1137    24473  29686  19347    501    983   -601       N  
ATOM   6086  NH2 ARG B1137     -55.837  10.320  96.146  1.00196.92           N  
ANISOU 6086  NH2 ARG B1137    24561  30770  19489    567   1354   -947       N  
ATOM   6087  N   TRP B1138     -56.710  10.003  88.351  1.00160.64           N  
ANISOU 6087  N   TRP B1138    19707  24669  16660   1122    973     19       N  
ATOM   6088  CA  TRP B1138     -56.000  10.159  87.080  1.00158.08           C  
ANISOU 6088  CA  TRP B1138    19495  23951  16616   1172    825    186       C  
ATOM   6089  C   TRP B1138     -56.837  10.950  86.059  1.00162.27           C  
ANISOU 6089  C   TRP B1138    19891  24366  17400   1396    812    132       C  
ATOM   6090  O   TRP B1138     -56.293  11.828  85.383  1.00161.26           O  
ANISOU 6090  O   TRP B1138    19857  23902  17513   1531    699    110       O  
ATOM   6091  CB  TRP B1138     -55.568   8.774  86.552  1.00154.55           C  
ANISOU 6091  CB  TRP B1138    19132  23479  16111    934    767    507       C  
ATOM   6092  CG  TRP B1138     -55.168   8.697  85.103  1.00153.26           C  
ANISOU 6092  CG  TRP B1138    19024  23017  16192    955    660    687       C  
ATOM   6093  CD1 TRP B1138     -54.289   9.506  84.445  1.00155.14           C  
ANISOU 6093  CD1 TRP B1138    19377  22919  16649   1053    557    667       C  
ATOM   6094  CD2 TRP B1138     -55.558   7.684  84.168  1.00151.70           C  
ANISOU 6094  CD2 TRP B1138    18782  22846  16013    838    646    919       C  
ATOM   6095  NE1 TRP B1138     -54.172   9.110  83.134  1.00152.78           N  
ANISOU 6095  NE1 TRP B1138    19097  22462  16489   1010    496    865       N  
ATOM   6096  CE2 TRP B1138     -54.920   7.978  82.942  1.00153.91           C  
ANISOU 6096  CE2 TRP B1138    19147  22817  16514    885    544   1013       C  
ATOM   6097  CE3 TRP B1138     -56.409   6.569  84.236  1.00153.32           C  
ANISOU 6097  CE3 TRP B1138    18881  23310  16062    684    710   1052       C  
ATOM   6098  CZ2 TRP B1138     -55.093   7.188  81.800  1.00151.78           C  
ANISOU 6098  CZ2 TRP B1138    18863  22502  16305    795    507   1214       C  
ATOM   6099  CZ3 TRP B1138     -56.590   5.796  83.099  1.00153.28           C  
ANISOU 6099  CZ3 TRP B1138    18863  23232  16143    600    660   1254       C  
ATOM   6100  CH2 TRP B1138     -55.944   6.111  81.897  1.00152.18           C  
ANISOU 6100  CH2 TRP B1138    18810  22796  16215    664    561   1322       C  
ATOM   6101  N   TYR B1139     -58.152  10.662  85.972  1.00159.98           N  
ANISOU 6101  N   TYR B1139    19378  24354  17054   1427    916    115       N  
ATOM   6102  CA  TYR B1139     -59.065  11.377  85.076  1.00160.62           C  
ANISOU 6102  CA  TYR B1139    19301  24358  17369   1651    885     57       C  
ATOM   6103  C   TYR B1139     -59.326  12.801  85.596  1.00166.65           C  
ANISOU 6103  C   TYR B1139    19999  25054  18265   1933    889   -287       C  
ATOM   6104  O   TYR B1139     -59.421  13.732  84.795  1.00166.59           O  
ANISOU 6104  O   TYR B1139    19998  24763  18536   2141    767   -322       O  
ATOM   6105  CB  TYR B1139     -60.386  10.604  84.900  1.00162.86           C  
ANISOU 6105  CB  TYR B1139    19340  24985  17555   1590    990    123       C  
ATOM   6106  CG  TYR B1139     -61.277  11.151  83.803  1.00165.47           C  
ANISOU 6106  CG  TYR B1139    19513  25222  18135   1795    917    125       C  
ATOM   6107  CD1 TYR B1139     -61.076  10.796  82.471  1.00165.14           C  
ANISOU 6107  CD1 TYR B1139    19555  24959  18231   1740    787    392       C  
ATOM   6108  CD2 TYR B1139     -62.330  12.014  84.096  1.00169.51           C  
ANISOU 6108  CD2 TYR B1139    19786  25877  18744   2046    969   -150       C  
ATOM   6109  CE1 TYR B1139     -61.887  11.302  81.456  1.00166.62           C  
ANISOU 6109  CE1 TYR B1139    19614  25062  18631   1918    692    413       C  
ATOM   6110  CE2 TYR B1139     -63.150  12.524  83.090  1.00171.35           C  
ANISOU 6110  CE2 TYR B1139    19873  26010  19224   2248    865   -141       C  
ATOM   6111  CZ  TYR B1139     -62.925  12.164  81.771  1.00176.14           C  
ANISOU 6111  CZ  TYR B1139    20587  26391  19949   2175    719    156       C  
ATOM   6112  OH  TYR B1139     -63.733  12.656  80.775  1.00178.18           O  
ANISOU 6112  OH  TYR B1139    20713  26556  20431   2361    592    185       O  
ATOM   6113  N   ASN B1140     -59.429  12.957  86.937  1.00164.84           N  
ANISOU 6113  N   ASN B1140    19720  25083  17831   1929   1016   -538       N  
ATOM   6114  CA  ASN B1140     -59.663  14.226  87.637  1.00167.38           C  
ANISOU 6114  CA  ASN B1140    19973  25385  18239   2185   1040   -922       C  
ATOM   6115  C   ASN B1140     -58.554  15.257  87.368  1.00169.59           C  
ANISOU 6115  C   ASN B1140    20485  25198  18755   2302    866   -975       C  
ATOM   6116  O   ASN B1140     -58.859  16.433  87.155  1.00171.25           O  
ANISOU 6116  O   ASN B1140    20650  25199  19218   2572    788  -1186       O  
ATOM   6117  CB  ASN B1140     -59.831  13.976  89.145  1.00170.33           C  
ANISOU 6117  CB  ASN B1140    20281  26164  18274   2082   1221  -1149       C  
ATOM   6118  CG  ASN B1140     -60.047  15.220  89.978  1.00196.25           C  
ANISOU 6118  CG  ASN B1140    23489  29466  21609   2332   1264  -1592       C  
ATOM   6119  OD1 ASN B1140     -61.016  15.967  89.795  1.00193.71           O  
ANISOU 6119  OD1 ASN B1140    22949  29178  21472   2598   1289  -1830       O  
ATOM   6120  ND2 ASN B1140     -59.155  15.452  90.928  1.00187.81           N  
ANISOU 6120  ND2 ASN B1140    22595  28380  20385   2257   1263  -1727       N  
ATOM   6121  N   GLN B1141     -57.282  14.810  87.370  1.00162.70           N  
ANISOU 6121  N   GLN B1141    19850  24157  17811   2098    794   -784       N  
ATOM   6122  CA  GLN B1141     -56.112  15.660  87.137  1.00161.43           C  
ANISOU 6122  CA  GLN B1141    19909  23580  17847   2146    638   -806       C  
ATOM   6123  C   GLN B1141     -55.968  16.073  85.664  1.00163.11           C  
ANISOU 6123  C   GLN B1141    20188  23421  18364   2219    484   -601       C  
ATOM   6124  O   GLN B1141     -56.152  17.249  85.347  1.00164.46           O  
ANISOU 6124  O   GLN B1141    20367  23333  18787   2439    383   -745       O  
ATOM   6125  CB  GLN B1141     -54.830  14.989  87.667  1.00160.88           C  
ANISOU 6125  CB  GLN B1141    20032  23498  17596   1898    616   -684       C  
ATOM   6126  CG  GLN B1141     -54.644  15.121  89.177  1.00177.16           C  
ANISOU 6126  CG  GLN B1141    22110  25792  19413   1866    697   -948       C  
ATOM   6127  CD  GLN B1141     -53.519  14.256  89.683  1.00192.32           C  
ANISOU 6127  CD  GLN B1141    24195  27744  21132   1609    656   -784       C  
ATOM   6128  OE1 GLN B1141     -53.733  13.137  90.161  1.00186.52           O  
ANISOU 6128  OE1 GLN B1141    23429  27310  20129   1420    734   -651       O  
ATOM   6129  NE2 GLN B1141     -52.293  14.753  89.599  1.00183.59           N  
ANISOU 6129  NE2 GLN B1141    23266  26326  20163   1589    519   -789       N  
ATOM   6130  N   THR B1142     -55.655  15.111  84.771  1.00156.13           N  
ANISOU 6130  N   THR B1142    19358  22511  17452   2030    458   -272       N  
ATOM   6131  CA  THR B1142     -55.487  15.360  83.333  1.00154.14           C  
ANISOU 6131  CA  THR B1142    19179  21959  17430   2048    326    -51       C  
ATOM   6132  C   THR B1142     -56.557  14.599  82.520  1.00155.74           C  
ANISOU 6132  C   THR B1142    19219  22348  17607   2033    361    127       C  
ATOM   6133  O   THR B1142     -56.325  13.446  82.145  1.00153.01           O  
ANISOU 6133  O   THR B1142    18895  22110  17131   1824    395    352       O  
ATOM   6134  CB  THR B1142     -54.028  15.098  82.881  1.00159.99           C  
ANISOU 6134  CB  THR B1142    20134  22460  18193   1848    247    138       C  
ATOM   6135  OG1 THR B1142     -53.626  13.788  83.289  1.00157.98           O  
ANISOU 6135  OG1 THR B1142    19888  22428  17709   1629    326    260       O  
ATOM   6136  CG2 THR B1142     -53.049  16.140  83.423  1.00159.22           C  
ANISOU 6136  CG2 THR B1142    20188  22106  18202   1894    169    -37       C  
ATOM   6137  N   PRO B1143     -57.744  15.208  82.258  1.00153.03           N  
ANISOU 6137  N   PRO B1143    18702  22046  17396   2256    343     16       N  
ATOM   6138  CA  PRO B1143     -58.793  14.481  81.516  1.00151.81           C  
ANISOU 6138  CA  PRO B1143    18374  22090  17216   2236    367    174       C  
ATOM   6139  C   PRO B1143     -58.548  14.307  80.014  1.00151.60           C  
ANISOU 6139  C   PRO B1143    18452  21835  17313   2160    230    472       C  
ATOM   6140  O   PRO B1143     -59.156  13.423  79.409  1.00150.48           O  
ANISOU 6140  O   PRO B1143    18208  21869  17097   2063    255    639       O  
ATOM   6141  CB  PRO B1143     -60.058  15.289  81.805  1.00157.03           C  
ANISOU 6141  CB  PRO B1143    18802  22862  18002   2520    376    -80       C  
ATOM   6142  CG  PRO B1143     -59.573  16.672  82.031  1.00163.61           C  
ANISOU 6142  CG  PRO B1143    19754  23362  19047   2723    260   -280       C  
ATOM   6143  CD  PRO B1143     -58.198  16.562  82.644  1.00157.66           C  
ANISOU 6143  CD  PRO B1143    19229  22500  18176   2545    286   -276       C  
ATOM   6144  N   ASN B1144     -57.677  15.146  79.416  1.00145.78           N  
ANISOU 6144  N   ASN B1144    17918  20723  16750   2185     89    533       N  
ATOM   6145  CA  ASN B1144     -57.359  15.077  77.988  1.00143.19           C  
ANISOU 6145  CA  ASN B1144    17709  20185  16511   2089    -36    810       C  
ATOM   6146  C   ASN B1144     -56.561  13.804  77.661  1.00140.81           C  
ANISOU 6146  C   ASN B1144    17493  19976  16031   1802     36   1012       C  
ATOM   6147  O   ASN B1144     -56.969  13.044  76.780  1.00139.28           O  
ANISOU 6147  O   ASN B1144    17254  19881  15787   1705     28   1196       O  
ATOM   6148  CB  ASN B1144     -56.633  16.348  77.524  1.00145.76           C  
ANISOU 6148  CB  ASN B1144    18229  20100  17051   2162   -198    819       C  
ATOM   6149  CG  ASN B1144     -56.954  16.788  76.110  1.00172.73           C  
ANISOU 6149  CG  ASN B1144    21705  23313  20614   2190   -370   1036       C  
ATOM   6150  OD1 ASN B1144     -57.970  16.410  75.511  1.00168.53           O  
ANISOU 6150  OD1 ASN B1144    21032  22930  20074   2241   -399   1127       O  
ATOM   6151  ND2 ASN B1144     -56.094  17.625  75.550  1.00165.57           N  
ANISOU 6151  ND2 ASN B1144    21010  22061  19837   2142   -500   1131       N  
ATOM   6152  N   ARG B1145     -55.461  13.552  78.410  1.00133.62           N  
ANISOU 6152  N   ARG B1145    16696  19043  15032   1677     97    957       N  
ATOM   6153  CA  ARG B1145     -54.605  12.369  78.264  1.00129.58           C  
ANISOU 6153  CA  ARG B1145    16258  18598  14379   1432    150   1104       C  
ATOM   6154  C   ARG B1145     -55.347  11.083  78.673  1.00131.03           C  
ANISOU 6154  C   ARG B1145    16297  19114  14373   1342    256   1141       C  
ATOM   6155  O   ARG B1145     -55.291  10.096  77.939  1.00128.88           O  
ANISOU 6155  O   ARG B1145    16030  18895  14045   1190    257   1318       O  
ATOM   6156  CB  ARG B1145     -53.295  12.532  79.072  1.00127.12           C  
ANISOU 6156  CB  ARG B1145    16081  18173  14046   1354    159   1009       C  
ATOM   6157  CG  ARG B1145     -52.374  11.310  79.022  1.00126.17           C  
ANISOU 6157  CG  ARG B1145    16018  18111  13809   1130    193   1131       C  
ATOM   6158  CD  ARG B1145     -51.086  11.497  79.793  1.00121.57           C  
ANISOU 6158  CD  ARG B1145    15549  17419  13225   1064    176   1035       C  
ATOM   6159  NE  ARG B1145     -50.288  10.268  79.807  1.00113.85           N  
ANISOU 6159  NE  ARG B1145    14599  16504  12155    880    187   1136       N  
ATOM   6160  CZ  ARG B1145     -48.977  10.228  80.019  1.00119.20           C  
ANISOU 6160  CZ  ARG B1145    15365  17055  12869    786    146   1111       C  
ATOM   6161  NH1 ARG B1145     -48.296  11.348  80.231  1.00106.90           N  
ANISOU 6161  NH1 ARG B1145    13886  15309  11424    834    100    999       N  
ATOM   6162  NH2 ARG B1145     -48.333   9.069  80.013  1.00 98.48           N  
ANISOU 6162  NH2 ARG B1145    12746  14484  10187    646    138   1190       N  
ATOM   6163  N   ALA B1146     -56.042  11.113  79.834  1.00127.84           N  
ANISOU 6163  N   ALA B1146    15768  18936  13871   1424    345    967       N  
ATOM   6164  CA  ALA B1146     -56.785   9.989  80.412  1.00127.02           C  
ANISOU 6164  CA  ALA B1146    15526  19169  13568   1316    455    991       C  
ATOM   6165  C   ALA B1146     -57.784   9.309  79.478  1.00128.94           C  
ANISOU 6165  C   ALA B1146    15636  19544  13810   1274    451   1146       C  
ATOM   6166  O   ALA B1146     -57.761   8.083  79.382  1.00127.08           O  
ANISOU 6166  O   ALA B1146    15399  19436  13449   1079    482   1289       O  
ATOM   6167  CB  ALA B1146     -57.462  10.404  81.707  1.00130.12           C  
ANISOU 6167  CB  ALA B1146    15787  19792  13859   1426    558    752       C  
ATOM   6168  N   LYS B1147     -58.633  10.094  78.775  1.00125.72           N  
ANISOU 6168  N   LYS B1147    15125  19088  13554   1456    390   1119       N  
ATOM   6169  CA  LYS B1147     -59.658   9.582  77.853  1.00125.01           C  
ANISOU 6169  CA  LYS B1147    14892  19125  13479   1437    362   1251       C  
ATOM   6170  C   LYS B1147     -59.081   8.816  76.658  1.00124.75           C  
ANISOU 6170  C   LYS B1147    14992  18966  13443   1256    290   1488       C  
ATOM   6171  O   LYS B1147     -59.633   7.777  76.296  1.00123.51           O  
ANISOU 6171  O   LYS B1147    14748  18984  13197   1121    312   1602       O  
ATOM   6172  CB  LYS B1147     -60.607  10.700  77.389  1.00129.78           C  
ANISOU 6172  CB  LYS B1147    15366  19673  14271   1696    274   1162       C  
ATOM   6173  CG  LYS B1147     -62.028  10.210  77.126  1.00145.71           C  
ANISOU 6173  CG  LYS B1147    17124  21974  16265   1721    297   1178       C  
ATOM   6174  CD  LYS B1147     -62.946  11.316  76.622  1.00159.00           C  
ANISOU 6174  CD  LYS B1147    18667  23581  18165   1999    173   1091       C  
ATOM   6175  CE  LYS B1147     -63.166  11.257  75.126  1.00167.81           C  
ANISOU 6175  CE  LYS B1147    19827  24559  19373   1976      3   1318       C  
ATOM   6176  NZ  LYS B1147     -64.129  12.297  74.674  1.00178.27           N  
ANISOU 6176  NZ  LYS B1147    21006  25811  20916   2255   -151   1245       N  
ATOM   6177  N   ARG B1148     -57.962   9.309  76.074  1.00119.17           N  
ANISOU 6177  N   ARG B1148    14485  17969  12825   1238    210   1547       N  
ATOM   6178  CA  ARG B1148     -57.273   8.684  74.933  1.00116.62           C  
ANISOU 6178  CA  ARG B1148    14288  17528  12492   1066    157   1733       C  
ATOM   6179  C   ARG B1148     -56.670   7.318  75.256  1.00117.68           C  
ANISOU 6179  C   ARG B1148    14462  17760  12490    853    226   1787       C  
ATOM   6180  O   ARG B1148     -56.645   6.449  74.382  1.00116.26           O  
ANISOU 6180  O   ARG B1148    14298  17601  12275    715    203   1916       O  
ATOM   6181  CB  ARG B1148     -56.201   9.610  74.352  1.00115.96           C  
ANISOU 6181  CB  ARG B1148    14391  17144  12525   1080     78   1760       C  
ATOM   6182  CG  ARG B1148     -56.773  10.593  73.349  1.00126.72           C  
ANISOU 6182  CG  ARG B1148    15761  18371  14017   1204    -50   1832       C  
ATOM   6183  CD  ARG B1148     -55.719  11.479  72.712  1.00134.26           C  
ANISOU 6183  CD  ARG B1148    16914  19030  15067   1169   -132   1894       C  
ATOM   6184  NE  ARG B1148     -55.156  12.457  73.647  1.00140.89           N  
ANISOU 6184  NE  ARG B1148    17820  19707  16004   1279   -134   1737       N  
ATOM   6185  CZ  ARG B1148     -55.683  13.651  73.904  1.00156.50           C  
ANISOU 6185  CZ  ARG B1148    19782  21550  18131   1491   -223   1642       C  
ATOM   6186  NH1 ARG B1148     -56.818  14.025  73.322  1.00145.24           N  
ANISOU 6186  NH1 ARG B1148    18262  20139  16785   1635   -326   1691       N  
ATOM   6187  NH2 ARG B1148     -55.092  14.471  74.760  1.00143.33           N  
ANISOU 6187  NH2 ARG B1148    18185  19728  16546   1571   -225   1482       N  
ATOM   6188  N   VAL B1149     -56.183   7.134  76.501  1.00113.28           N  
ANISOU 6188  N   VAL B1149    13928  17252  11860    828    293   1685       N  
ATOM   6189  CA  VAL B1149     -55.588   5.877  76.978  1.00111.55           C  
ANISOU 6189  CA  VAL B1149    13758  17100  11525    641    325   1737       C  
ATOM   6190  C   VAL B1149     -56.694   4.815  77.164  1.00115.40           C  
ANISOU 6190  C   VAL B1149    14108  17849  11892    543    370   1805       C  
ATOM   6191  O   VAL B1149     -56.499   3.659  76.784  1.00113.86           O  
ANISOU 6191  O   VAL B1149    13944  17663  11653    377    346   1919       O  
ATOM   6192  CB  VAL B1149     -54.709   6.073  78.249  1.00115.54           C  
ANISOU 6192  CB  VAL B1149    14346  17572  11983    640    350   1623       C  
ATOM   6193  CG1 VAL B1149     -53.994   4.782  78.644  1.00114.31           C  
ANISOU 6193  CG1 VAL B1149    14260  17436  11737    455    334   1700       C  
ATOM   6194  CG2 VAL B1149     -53.691   7.194  78.050  1.00115.11           C  
ANISOU 6194  CG2 VAL B1149    14411  17263  12062    728    301   1548       C  
ATOM   6195  N   ILE B1150     -57.863   5.232  77.702  1.00113.54           N  
ANISOU 6195  N   ILE B1150    13707  17819  11616    645    430   1723       N  
ATOM   6196  CA  ILE B1150     -59.047   4.383  77.915  1.00114.16           C  
ANISOU 6196  CA  ILE B1150    13615  18180  11581    548    488   1772       C  
ATOM   6197  C   ILE B1150     -59.627   3.936  76.552  1.00116.83           C  
ANISOU 6197  C   ILE B1150    13898  18510  11984    502    419   1904       C  
ATOM   6198  O   ILE B1150     -60.007   2.771  76.408  1.00115.78           O  
ANISOU 6198  O   ILE B1150    13725  18498  11770    322    422   2011       O  
ATOM   6199  CB  ILE B1150     -60.095   5.085  78.838  1.00119.69           C  
ANISOU 6199  CB  ILE B1150    14122  19122  12232    686    586   1605       C  
ATOM   6200  CG1 ILE B1150     -59.509   5.384  80.241  1.00120.60           C  
ANISOU 6200  CG1 ILE B1150    14305  19282  12237    693    660   1467       C  
ATOM   6201  CG2 ILE B1150     -61.391   4.264  78.963  1.00121.98           C  
ANISOU 6201  CG2 ILE B1150    14200  19734  12413    571    656   1652       C  
ATOM   6202  CD1 ILE B1150     -60.159   6.581  80.976  1.00129.43           C  
ANISOU 6202  CD1 ILE B1150    15280  20522  13374    914    736   1224       C  
ATOM   6203  N   THR B1151     -59.642   4.849  75.554  1.00113.49           N  
ANISOU 6203  N   THR B1151    13493  17929  11700    648    340   1906       N  
ATOM   6204  CA  THR B1151     -60.115   4.580  74.189  1.00113.37           C  
ANISOU 6204  CA  THR B1151    13448  17893  11733    611    253   2029       C  
ATOM   6205  C   THR B1151     -59.220   3.533  73.501  1.00115.42           C  
ANISOU 6205  C   THR B1151    13861  18038  11956    411    218   2143       C  
ATOM   6206  O   THR B1151     -59.728   2.706  72.736  1.00114.96           O  
ANISOU 6206  O   THR B1151    13755  18058  11866    294    180   2236       O  
ATOM   6207  CB  THR B1151     -60.260   5.888  73.392  1.00123.90           C  
ANISOU 6207  CB  THR B1151    14796  19071  13209    807    156   2017       C  
ATOM   6208  OG1 THR B1151     -60.956   6.847  74.190  1.00127.03           O  
ANISOU 6208  OG1 THR B1151    15055  19544  13667   1015    184   1867       O  
ATOM   6209  CG2 THR B1151     -61.006   5.698  72.075  1.00122.54           C  
ANISOU 6209  CG2 THR B1151    14563  18933  13063    783     52   2142       C  
ATOM   6210  N   THR B1152     -57.903   3.545  73.813  1.00110.65           N  
ANISOU 6210  N   THR B1152    13422  17258  11363    375    229   2114       N  
ATOM   6211  CA  THR B1152     -56.931   2.568  73.309  1.00108.98           C  
ANISOU 6211  CA  THR B1152    13335  16932  11139    210    202   2173       C  
ATOM   6212  C   THR B1152     -57.246   1.189  73.913  1.00113.37           C  
ANISOU 6212  C   THR B1152    13850  17623  11603     48    219   2218       C  
ATOM   6213  O   THR B1152     -57.221   0.202  73.179  1.00112.76           O  
ANISOU 6213  O   THR B1152    13794  17529  11521    -86    174   2285       O  
ATOM   6214  CB  THR B1152     -55.486   3.035  73.552  1.00115.18           C  
ANISOU 6214  CB  THR B1152    14270  17512  11981    232    203   2110       C  
ATOM   6215  OG1 THR B1152     -55.352   4.392  73.124  1.00115.57           O  
ANISOU 6215  OG1 THR B1152    14355  17444  12114    369    183   2081       O  
ATOM   6216  CG2 THR B1152     -54.460   2.173  72.821  1.00112.32           C  
ANISOU 6216  CG2 THR B1152    14007  17031  11640     94    173   2137       C  
ATOM   6217  N   PHE B1153     -57.598   1.133  75.226  1.00110.66           N  
ANISOU 6217  N   PHE B1153    13449  17419  11179     48    279   2181       N  
ATOM   6218  CA  PHE B1153     -58.000  -0.104  75.914  1.00110.79           C  
ANISOU 6218  CA  PHE B1153    13432  17576  11086   -132    289   2251       C  
ATOM   6219  C   PHE B1153     -59.350  -0.601  75.376  1.00114.73           C  
ANISOU 6219  C   PHE B1153    13772  18270  11551   -207    292   2321       C  
ATOM   6220  O   PHE B1153     -59.541  -1.809  75.230  1.00113.83           O  
ANISOU 6220  O   PHE B1153    13667  18183  11400   -394    251   2415       O  
ATOM   6221  CB  PHE B1153     -58.116   0.112  77.438  1.00113.71           C  
ANISOU 6221  CB  PHE B1153    13777  18089  11340   -128    365   2195       C  
ATOM   6222  CG  PHE B1153     -56.827   0.225  78.217  1.00114.58           C  
ANISOU 6222  CG  PHE B1153    14045  18044  11445   -120    340   2149       C  
ATOM   6223  CD1 PHE B1153     -55.968  -0.863  78.339  1.00116.96           C  
ANISOU 6223  CD1 PHE B1153    14475  18214  11749   -266    252   2229       C  
ATOM   6224  CD2 PHE B1153     -56.512   1.393  78.901  1.00117.08           C  
ANISOU 6224  CD2 PHE B1153    14373  18350  11762     35    388   2015       C  
ATOM   6225  CE1 PHE B1153     -54.787  -0.764  79.082  1.00117.49           C  
ANISOU 6225  CE1 PHE B1153    14671  18146  11822   -252    207   2184       C  
ATOM   6226  CE2 PHE B1153     -55.329   1.492  79.639  1.00119.43           C  
ANISOU 6226  CE2 PHE B1153    14808  18516  12053     33    351   1968       C  
ATOM   6227  CZ  PHE B1153     -54.476   0.413  79.729  1.00116.78           C  
ANISOU 6227  CZ  PHE B1153    14590  18063  11720   -111    259   2058       C  
ATOM   6228  N   ARG B1154     -60.274   0.340  75.090  1.00112.45           N  
ANISOU 6228  N   ARG B1154    13333  18101  11292    -57    323   2270       N  
ATOM   6229  CA  ARG B1154     -61.624   0.084  74.586  1.00113.85           C  
ANISOU 6229  CA  ARG B1154    13318  18484  11456    -92    318   2313       C  
ATOM   6230  C   ARG B1154     -61.645  -0.595  73.211  1.00117.02           C  
ANISOU 6230  C   ARG B1154    13763  18797  11903   -193    216   2408       C  
ATOM   6231  O   ARG B1154     -62.197  -1.691  73.073  1.00116.64           O  
ANISOU 6231  O   ARG B1154    13660  18853  11804   -378    194   2485       O  
ATOM   6232  CB  ARG B1154     -62.426   1.399  74.519  1.00115.97           C  
ANISOU 6232  CB  ARG B1154    13425  18845  11791    142    339   2213       C  
ATOM   6233  CG  ARG B1154     -63.375   1.636  75.686  1.00129.25           C  
ANISOU 6233  CG  ARG B1154    14901  20812  13396    181    456   2113       C  
ATOM   6234  CD  ARG B1154     -64.221   2.873  75.434  1.00140.66           C  
ANISOU 6234  CD  ARG B1154    16164  22325  14955    438    444   1995       C  
ATOM   6235  NE  ARG B1154     -65.272   3.034  76.441  1.00151.34           N  
ANISOU 6235  NE  ARG B1154    17264  23999  16238    475    570   1866       N  
ATOM   6236  CZ  ARG B1154     -66.218   3.968  76.403  1.00166.55           C  
ANISOU 6236  CZ  ARG B1154    18965  26050  18268    698    572   1727       C  
ATOM   6237  NH1 ARG B1154     -66.266   4.836  75.400  1.00152.80           N  
ANISOU 6237  NH1 ARG B1154    17239  24112  16706    903    429   1730       N  
ATOM   6238  NH2 ARG B1154     -67.129   4.035  77.365  1.00155.62           N  
ANISOU 6238  NH2 ARG B1154    17330  24992  16806    714    712   1582       N  
ATOM   6239  N   THR B1155     -61.052   0.067  72.203  1.00113.14           N  
ANISOU 6239  N   THR B1155    13373  18121  11495    -88    152   2401       N  
ATOM   6240  CA  THR B1155     -61.036  -0.379  70.808  1.00112.64           C  
ANISOU 6240  CA  THR B1155    13357  17991  11451   -168     59   2468       C  
ATOM   6241  C   THR B1155     -59.897  -1.325  70.422  1.00114.81           C  
ANISOU 6241  C   THR B1155    13807  18092  11724   -313     33   2478       C  
ATOM   6242  O   THR B1155     -60.093  -2.181  69.555  1.00114.35           O  
ANISOU 6242  O   THR B1155    13757  18041  11651   -445    -28   2516       O  
ATOM   6243  CB  THR B1155     -61.091   0.829  69.856  1.00121.53           C  
ANISOU 6243  CB  THR B1155    14498  19039  12640     -5     -3   2470       C  
ATOM   6244  OG1 THR B1155     -60.045   1.748  70.189  1.00119.90           O  
ANISOU 6244  OG1 THR B1155    14423  18650  12484    110     27   2414       O  
ATOM   6245  CG2 THR B1155     -62.445   1.533  69.872  1.00121.99           C  
ANISOU 6245  CG2 THR B1155    14349  19272  12731    133    -32   2466       C  
ATOM   6246  N   GLY B1156     -58.724  -1.141  71.029  1.00110.15           N  
ANISOU 6246  N   GLY B1156    13343  17347  11161   -280     69   2424       N  
ATOM   6247  CA  GLY B1156     -57.528  -1.917  70.713  1.00108.84           C  
ANISOU 6247  CA  GLY B1156    13322  17007  11027   -379     40   2399       C  
ATOM   6248  C   GLY B1156     -56.908  -1.439  69.413  1.00112.31           C  
ANISOU 6248  C   GLY B1156    13839  17337  11496   -352     17   2373       C  
ATOM   6249  O   GLY B1156     -56.257  -2.214  68.705  1.00111.56           O  
ANISOU 6249  O   GLY B1156    13814  17158  11414   -454    -11   2338       O  
ATOM   6250  N   THR B1157     -57.136  -0.145  69.085  1.00108.80           N  
ANISOU 6250  N   THR B1157    13381  16897  11061   -219     23   2386       N  
ATOM   6251  CA  THR B1157     -56.665   0.538  67.876  1.00108.17           C  
ANISOU 6251  CA  THR B1157    13383  16734  10982   -206     -3   2398       C  
ATOM   6252  C   THR B1157     -55.956   1.857  68.223  1.00110.50           C  
ANISOU 6252  C   THR B1157    13750  16900  11335    -79     25   2371       C  
ATOM   6253  O   THR B1157     -56.064   2.350  69.350  1.00109.86           O  
ANISOU 6253  O   THR B1157    13633  16815  11292     30     57   2334       O  
ATOM   6254  CB  THR B1157     -57.844   0.809  66.916  1.00118.31           C  
ANISOU 6254  CB  THR B1157    14592  18141  12220   -196    -80   2487       C  
ATOM   6255  OG1 THR B1157     -58.785   1.667  67.559  1.00120.03           O  
ANISOU 6255  OG1 THR B1157    14696  18432  12477    -39    -93   2509       O  
ATOM   6256  CG2 THR B1157     -58.539  -0.461  66.430  1.00117.27           C  
ANISOU 6256  CG2 THR B1157    14394  18133  12031   -342   -122   2508       C  
ATOM   6257  N   TRP B1158     -55.259   2.439  67.232  1.00106.35           N  
ANISOU 6257  N   TRP B1158    13328  16278  10804   -109     13   2389       N  
ATOM   6258  CA  TRP B1158     -54.533   3.703  67.369  1.00105.92           C  
ANISOU 6258  CA  TRP B1158    13360  16078  10808    -28     24   2380       C  
ATOM   6259  C   TRP B1158     -55.361   4.902  66.857  1.00110.85           C  
ANISOU 6259  C   TRP B1158    13985  16687  11448     80    -65   2482       C  
ATOM   6260  O   TRP B1158     -54.806   5.978  66.606  1.00110.67           O  
ANISOU 6260  O   TRP B1158    14064  16520  11467    112    -89   2511       O  
ATOM   6261  CB  TRP B1158     -53.186   3.612  66.639  1.00104.09           C  
ANISOU 6261  CB  TRP B1158    13238  15753  10559   -158     69   2341       C  
ATOM   6262  CG  TRP B1158     -52.285   2.538  67.172  1.00103.83           C  
ANISOU 6262  CG  TRP B1158    13195  15700  10555   -228    128   2221       C  
ATOM   6263  CD1 TRP B1158     -52.069   1.306  66.632  1.00106.46           C  
ANISOU 6263  CD1 TRP B1158    13511  16085  10853   -347    137   2168       C  
ATOM   6264  CD2 TRP B1158     -51.501   2.596  68.370  1.00102.93           C  
ANISOU 6264  CD2 TRP B1158    13087  15497  10524   -173    162   2134       C  
ATOM   6265  NE1 TRP B1158     -51.177   0.599  67.405  1.00105.19           N  
ANISOU 6265  NE1 TRP B1158    13345  15853  10769   -358    162   2058       N  
ATOM   6266  CE2 TRP B1158     -50.814   1.367  68.481  1.00106.29           C  
ANISOU 6266  CE2 TRP B1158    13500  15915  10972   -258    175   2045       C  
ATOM   6267  CE3 TRP B1158     -51.302   3.575  69.358  1.00104.12           C  
ANISOU 6267  CE3 TRP B1158    13257  15567  10736    -57    168   2112       C  
ATOM   6268  CZ2 TRP B1158     -49.943   1.091  69.541  1.00105.06           C  
ANISOU 6268  CZ2 TRP B1158    13348  15674  10895   -231    179   1957       C  
ATOM   6269  CZ3 TRP B1158     -50.440   3.300  70.405  1.00104.95           C  
ANISOU 6269  CZ3 TRP B1158    13368  15609  10897    -45    187   2016       C  
ATOM   6270  CH2 TRP B1158     -49.765   2.076  70.485  1.00105.00           C  
ANISOU 6270  CH2 TRP B1158    13362  15611  10922   -132    186   1951       C  
ATOM   6271  N   ASP B1159     -56.695   4.707  66.737  1.00108.24           N  
ANISOU 6271  N   ASP B1159    13534  16496  11097    136   -128   2535       N  
ATOM   6272  CA  ASP B1159     -57.686   5.676  66.254  1.00109.57           C  
ANISOU 6272  CA  ASP B1159    13663  16668  11300    261   -248   2627       C  
ATOM   6273  C   ASP B1159     -57.768   6.967  67.079  1.00113.33           C  
ANISOU 6273  C   ASP B1159    14135  17017  11907    466   -272   2583       C  
ATOM   6274  O   ASP B1159     -57.963   8.034  66.499  1.00114.27           O  
ANISOU 6274  O   ASP B1159    14317  17017  12085    549   -390   2666       O  
ATOM   6275  CB  ASP B1159     -59.073   5.018  66.127  1.00112.34           C  
ANISOU 6275  CB  ASP B1159    13839  17226  11619    275   -299   2656       C  
ATOM   6276  CG  ASP B1159     -59.151   3.803  65.210  1.00122.75           C  
ANISOU 6276  CG  ASP B1159    15162  18659  12817     78   -308   2695       C  
ATOM   6277  OD1 ASP B1159     -58.406   3.764  64.201  1.00123.18           O  
ANISOU 6277  OD1 ASP B1159    15356  18650  12796    -48   -321   2736       O  
ATOM   6278  OD2 ASP B1159     -59.995   2.917  65.471  1.00128.92           O  
ANISOU 6278  OD2 ASP B1159    15804  19604  13576     39   -303   2679       O  
ATOM   6279  N   ALA B1160     -57.605   6.875  68.421  1.00108.76           N  
ANISOU 6279  N   ALA B1160    13497  16456  11373    541   -175   2452       N  
ATOM   6280  CA  ALA B1160     -57.610   8.028  69.337  1.00109.25           C  
ANISOU 6280  CA  ALA B1160    13552  16407  11552    732   -182   2360       C  
ATOM   6281  C   ALA B1160     -56.358   8.901  69.124  1.00112.55           C  
ANISOU 6281  C   ALA B1160    14163  16576  12026    704   -198   2371       C  
ATOM   6282  O   ALA B1160     -56.256  10.004  69.666  1.00113.18           O  
ANISOU 6282  O   ALA B1160    14276  16506  12220    850   -236   2307       O  
ATOM   6283  CB  ALA B1160     -57.687   7.554  70.781  1.00109.39           C  
ANISOU 6283  CB  ALA B1160    13469  16546  11549    770    -64   2217       C  
ATOM   6284  N   TYR B1161     -55.443   8.346  68.359  1.00107.65           N  
ANISOU 6284  N   TYR B1161    13649  15926  11325    509   -165   2432       N  
ATOM   6285  CA  TYR B1161     -54.214   9.001  68.043  1.00107.41           C  
ANISOU 6285  CA  TYR B1161    13780  15707  11324    428   -160   2448       C  
ATOM   6286  C   TYR B1161     -54.246   9.161  66.546  1.00113.29           C  
ANISOU 6286  C   TYR B1161    14614  16435  11995    303   -239   2611       C  
ATOM   6287  O   TYR B1161     -53.316   9.672  65.940  1.00113.45           O  
ANISOU 6287  O   TYR B1161    14773  16332  12001    180   -240   2667       O  
ATOM   6288  CB  TYR B1161     -53.055   8.129  68.484  1.00106.63           C  
ANISOU 6288  CB  TYR B1161    13700  15628  11185    295    -38   2351       C  
ATOM   6289  CG  TYR B1161     -52.927   8.019  69.985  1.00107.41           C  
ANISOU 6289  CG  TYR B1161    13739  15739  11332    396     19   2209       C  
ATOM   6290  CD1 TYR B1161     -51.977   8.742  70.663  1.00109.26           C  
ANISOU 6290  CD1 TYR B1161    14048  15821  11645    423     37   2123       C  
ATOM   6291  CD2 TYR B1161     -53.754   7.195  70.718  1.00107.66           C  
ANISOU 6291  CD2 TYR B1161    13643  15946  11317    442     52   2167       C  
ATOM   6292  CE1 TYR B1161     -51.852   8.653  72.021  1.00109.52           C  
ANISOU 6292  CE1 TYR B1161    14038  15880  11696    503     78   1993       C  
ATOM   6293  CE2 TYR B1161     -53.632   7.102  72.082  1.00108.21           C  
ANISOU 6293  CE2 TYR B1161    13673  16049  11393    506    104   2050       C  
ATOM   6294  CZ  TYR B1161     -52.681   7.839  72.724  1.00115.85           C  
ANISOU 6294  CZ  TYR B1161    14724  16868  12427    542    113   1961       C  
ATOM   6295  OH  TYR B1161     -52.538   7.767  74.079  1.00117.48           O  
ANISOU 6295  OH  TYR B1161    14902  17119  12615    596    154   1843       O  
ATOM   6296  N   GLY B1200     -55.150   8.530  65.724  1.00110.68           N  
ANISOU 6296  N   GLY B1200    14030  14022  14003     19   -145     35       N  
ATOM   6297  CA  GLY B1200     -55.541   9.183  64.488  1.00110.28           C  
ANISOU 6297  CA  GLY B1200    13979  13971  13952     18   -145     35       C  
ATOM   6298  C   GLY B1200     -54.896   8.552  63.270  1.00113.63           C  
ANISOU 6298  C   GLY B1200    14403  14396  14378     18   -146     34       C  
ATOM   6299  O   GLY B1200     -55.195   7.411  62.918  1.00113.19           O  
ANISOU 6299  O   GLY B1200    14346  14338  14322     17   -146     34       O  
ATOM   6300  N   SER B1201     -54.007   9.299  62.624  1.00109.74           N  
ANISOU 6300  N   SER B1201    13910  13903  13884     18   -146     33       N  
ATOM   6301  CA  SER B1201     -53.314   8.812  61.437  1.00109.13           C  
ANISOU 6301  CA  SER B1201    13831  13825  13807     18   -147     33       C  
ATOM   6302  C   SER B1201     -52.680   7.646  60.683  1.00111.62           C  
ANISOU 6302  C   SER B1201    14147  14141  14123     18   -147     32       C  
ATOM   6303  O   SER B1201     -52.877   7.495  59.477  1.00111.54           O  
ANISOU 6303  O   SER B1201    14136  14132  14114     18   -148     31       O  
ATOM   6304  CB  SER B1201     -52.209   9.786  61.023  1.00112.76           C  
ANISOU 6304  CB  SER B1201    14291  14285  14266     18   -147     33       C  
ATOM   6305  OG  SER B1201     -52.402  11.058  61.616  1.00121.15           O  
ANISOU 6305  OG  SER B1201    15354  15348  15329     18   -147     33       O  
ATOM   6306  N   LYS B 230     -51.843   6.921  61.414  1.00120.35           N  
ANISOU 6306  N   LYS B 230    16558  16942  12229   3572   -871   -537       N  
ATOM   6307  CA  LYS B 230     -51.260   5.679  60.969  1.00118.54           C  
ANISOU 6307  CA  LYS B 230    16384  16487  12169   3281   -798   -353       C  
ATOM   6308  C   LYS B 230     -51.715   4.813  62.118  1.00123.57           C  
ANISOU 6308  C   LYS B 230    17081  17375  12496   3274   -675   -174       C  
ATOM   6309  O   LYS B 230     -52.010   5.316  63.203  1.00125.66           O  
ANISOU 6309  O   LYS B 230    17372  17893  12478   3529   -702   -237       O  
ATOM   6310  CB  LYS B 230     -49.735   5.701  60.885  1.00119.90           C  
ANISOU 6310  CB  LYS B 230    16698  16270  12588   3306  -1007   -426       C  
ATOM   6311  CG  LYS B 230     -49.047   6.070  62.189  1.00136.31           C  
ANISOU 6311  CG  LYS B 230    18940  18327  14525   3581  -1184   -514       C  
ATOM   6312  CD  LYS B 230     -48.496   7.485  62.142  1.00144.80           C  
ANISOU 6312  CD  LYS B 230    20029  19263  15725   3815  -1433   -750       C  
ATOM   6313  CE  LYS B 230     -47.558   7.752  63.307  1.00156.16           C  
ANISOU 6313  CE  LYS B 230    21646  20589  17098   4065  -1652   -845       C  
ATOM   6314  NZ  LYS B 230     -46.791   6.536  63.693  1.00164.56           N  
ANISOU 6314  NZ  LYS B 230    22834  21509  18181   3944  -1623   -705       N  
ATOM   6315  N   GLY B 231     -51.790   3.515  61.887  1.00118.36           N  
ANISOU 6315  N   GLY B 231    16445  16655  11873   2986   -556     53       N  
ATOM   6316  CA  GLY B 231     -52.390   2.638  62.855  1.00119.94           C  
ANISOU 6316  CA  GLY B 231    16682  17116  11776   2906   -427    279       C  
ATOM   6317  C   GLY B 231     -52.453   1.493  61.907  1.00121.13           C  
ANISOU 6317  C   GLY B 231    16818  17070  12136   2551   -356    458       C  
ATOM   6318  O   GLY B 231     -51.613   1.389  61.045  1.00118.65           O  
ANISOU 6318  O   GLY B 231    16547  16409  12124   2488   -463    373       O  
ATOM   6319  N   HIS B 232     -53.448   0.641  62.038  1.00118.13           N  
ANISOU 6319  N   HIS B 232    16366  16922  11595   2320   -188    704       N  
ATOM   6320  CA  HIS B 232     -53.468  -0.594  61.281  1.00116.94           C  
ANISOU 6320  CA  HIS B 232    16246  16550  11636   1983   -171    894       C  
ATOM   6321  C   HIS B 232     -54.517  -0.585  60.205  1.00118.41           C  
ANISOU 6321  C   HIS B 232    16213  16864  11913   1797    -25    922       C  
ATOM   6322  O   HIS B 232     -54.246  -0.795  59.040  1.00116.02           O  
ANISOU 6322  O   HIS B 232    15889  16299  11896   1680    -68    860       O  
ATOM   6323  CB  HIS B 232     -53.787  -1.722  62.245  1.00120.84           C  
ANISOU 6323  CB  HIS B 232    16850  17163  11901   1802   -133   1202       C  
ATOM   6324  CG  HIS B 232     -54.343  -1.245  63.553  1.00126.93           C  
ANISOU 6324  CG  HIS B 232    17584  18372  12270   1977    -37   1256       C  
ATOM   6325  ND1 HIS B 232     -53.995  -1.807  64.760  1.00131.02           N  
ANISOU 6325  ND1 HIS B 232    18288  18935  12560   1996    -91   1422       N  
ATOM   6326  CD2 HIS B 232     -55.208  -0.246  63.838  1.00129.49           C  
ANISOU 6326  CD2 HIS B 232    17709  19126  12365   2169     95   1146       C  
ATOM   6327  CE1 HIS B 232     -54.633  -1.182  65.730  1.00132.65           C  
ANISOU 6327  CE1 HIS B 232    18397  19604  12399   2189     22   1422       C  
ATOM   6328  NE2 HIS B 232     -55.375  -0.231  65.198  1.00132.20           N  
ANISOU 6328  NE2 HIS B 232    18103  19792  12335   2308    130   1244       N  
ATOM   6329  N   GLN B 233     -55.733  -0.343  60.639  1.00115.52           N  
ANISOU 6329  N   GLN B 233    15676  16937  11280   1786    148   1011       N  
ATOM   6330  CA  GLN B 233     -56.940  -0.431  59.815  1.00114.66           C  
ANISOU 6330  CA  GLN B 233    15337  17032  11196   1594    307   1078       C  
ATOM   6331  C   GLN B 233     -56.854   0.777  58.866  1.00113.48           C  
ANISOU 6331  C   GLN B 233    15082  16806  11228   1788    270    774       C  
ATOM   6332  O   GLN B 233     -57.290   0.686  57.715  1.00111.56           O  
ANISOU 6332  O   GLN B 233    14724  16488  11178   1636    314    754       O  
ATOM   6333  CB  GLN B 233     -58.212  -0.343  60.684  1.00119.28           C  
ANISOU 6333  CB  GLN B 233    15738  18181  11401   1585    498   1226       C  
ATOM   6334  CG  GLN B 233     -59.500  -0.816  59.999  1.00135.15           C  
ANISOU 6334  CG  GLN B 233    17515  20419  13417   1297    663   1387       C  
ATOM   6335  CD  GLN B 233     -59.664  -2.321  59.971  1.00153.12           C  
ANISOU 6335  CD  GLN B 233    19866  22564  15749    891    662   1738       C  
ATOM   6336  OE1 GLN B 233     -59.306  -3.043  60.914  1.00148.18           O  
ANISOU 6336  OE1 GLN B 233    19403  21922  14976    804    616   1954       O  
ATOM   6337  NE2 GLN B 233     -60.245  -2.829  58.890  1.00144.92           N  
ANISOU 6337  NE2 GLN B 233    18718  21423  14923    632    691   1809       N  
ATOM   6338  N   LYS B 234     -56.274   1.896  59.365  1.00107.62           N  
ANISOU 6338  N   LYS B 234    14397  16069  10426   2120    164    545       N  
ATOM   6339  CA  LYS B 234     -56.085   3.167  58.666  1.00104.53           C  
ANISOU 6339  CA  LYS B 234    13944  15589  10182   2328     74    266       C  
ATOM   6340  C   LYS B 234     -55.103   3.084  57.487  1.00103.72           C  
ANISOU 6340  C   LYS B 234    13915  15043  10449   2228    -47    187       C  
ATOM   6341  O   LYS B 234     -55.299   3.788  56.488  1.00101.53           O  
ANISOU 6341  O   LYS B 234    13537  14714  10327   2245    -63     48       O  
ATOM   6342  CB  LYS B 234     -55.645   4.240  59.648  1.00107.77           C  
ANISOU 6342  CB  LYS B 234    14433  16085  10429   2691    -58     75       C  
ATOM   6343  N   ARG B 235     -54.051   2.236  57.603  1.00 98.34           N  
ANISOU 6343  N   ARG B 235    13404  14065   9894   2134   -140    269       N  
ATOM   6344  CA  ARG B 235     -53.064   2.025  56.533  1.00 95.02           C  
ANISOU 6344  CA  ARG B 235    13033  13276   9793   2047   -248    198       C  
ATOM   6345  C   ARG B 235     -53.729   1.281  55.367  1.00 96.33           C  
ANISOU 6345  C   ARG B 235    13090  13412  10098   1786   -144    294       C  
ATOM   6346  O   ARG B 235     -53.596   1.694  54.213  1.00 93.80           O  
ANISOU 6346  O   ARG B 235    12688  12977   9974   1763   -163    179       O  
ATOM   6347  CB  ARG B 235     -51.861   1.216  57.034  1.00 95.17           C  
ANISOU 6347  CB  ARG B 235    13249  13031   9878   2038   -380    249       C  
ATOM   6348  CG  ARG B 235     -50.916   1.974  57.953  1.00105.84           C  
ANISOU 6348  CG  ARG B 235    14720  14320  11176   2300   -531    116       C  
ATOM   6349  CD  ARG B 235     -49.469   1.497  57.843  1.00117.31           C  
ANISOU 6349  CD  ARG B 235    16310  15436  12826   2306   -700     68       C  
ATOM   6350  NE  ARG B 235     -49.332   0.075  57.499  1.00129.49           N  
ANISOU 6350  NE  ARG B 235    17924  16822  14453   2093   -695    213       N  
ATOM   6351  CZ  ARG B 235     -49.353  -0.926  58.375  1.00148.27           C  
ANISOU 6351  CZ  ARG B 235    20457  19183  16696   2028   -717    380       C  
ATOM   6352  NH1 ARG B 235     -49.535  -0.685  59.668  1.00138.80           N  
ANISOU 6352  NH1 ARG B 235    19342  18154  15243   2157   -711    436       N  
ATOM   6353  NH2 ARG B 235     -49.212  -2.179  57.963  1.00135.70           N  
ANISOU 6353  NH2 ARG B 235    18943  17405  15211   1838   -765    495       N  
ATOM   6354  N   LYS B 236     -54.468   0.194  55.690  1.00 93.38           N  
ANISOU 6354  N   LYS B 236    12716  13149   9614   1583    -47    516       N  
ATOM   6355  CA  LYS B 236     -55.209  -0.644  54.745  1.00 92.44           C  
ANISOU 6355  CA  LYS B 236    12506  13007   9608   1320     30    637       C  
ATOM   6356  C   LYS B 236     -56.245   0.203  53.990  1.00 93.16           C  
ANISOU 6356  C   LYS B 236    12382  13317   9696   1337    149    539       C  
ATOM   6357  O   LYS B 236     -56.424   0.017  52.785  1.00 90.91           O  
ANISOU 6357  O   LYS B 236    12025  12912   9605   1219    155    503       O  
ATOM   6358  CB  LYS B 236     -55.892  -1.797  55.502  1.00 97.85           C  
ANISOU 6358  CB  LYS B 236    13230  13820  10129   1102     91    921       C  
ATOM   6359  CG  LYS B 236     -55.988  -3.102  54.710  1.00111.31           C  
ANISOU 6359  CG  LYS B 236    14980  15288  12025    821     32   1067       C  
ATOM   6360  CD  LYS B 236     -56.919  -4.121  55.372  1.00122.61           C  
ANISOU 6360  CD  LYS B 236    16410  16883  13292    554     92   1384       C  
ATOM   6361  CE  LYS B 236     -56.248  -4.947  56.444  1.00133.60           C  
ANISOU 6361  CE  LYS B 236    18036  18139  14586    512    -32   1554       C  
ATOM   6362  NZ  LYS B 236     -57.246  -5.621  57.317  1.00145.11           N  
ANISOU 6362  NZ  LYS B 236    19460  19874  15802    272     59   1885       N  
ATOM   6363  N   ALA B 237     -56.882   1.164  54.707  1.00 89.41           N  
ANISOU 6363  N   ALA B 237    11813  13164   8996   1517    221    473       N  
ATOM   6364  CA  ALA B 237     -57.877   2.118  54.203  1.00 88.40           C  
ANISOU 6364  CA  ALA B 237    11491  13277   8820   1600    305    346       C  
ATOM   6365  C   ALA B 237     -57.263   3.073  53.176  1.00 88.05           C  
ANISOU 6365  C   ALA B 237    11453  13005   8998   1720    189    123       C  
ATOM   6366  O   ALA B 237     -57.952   3.513  52.253  1.00 86.36           O  
ANISOU 6366  O   ALA B 237    11106  12852   8856   1693    232     45       O  
ATOM   6367  CB  ALA B 237     -58.456   2.917  55.362  1.00 91.13           C  
ANISOU 6367  CB  ALA B 237    11772  13999   8855   1832    352    290       C  
ATOM   6368  N   LEU B 238     -55.965   3.399  53.364  1.00 82.62           N  
ANISOU 6368  N   LEU B 238    10916  12066   8410   1844     36     33       N  
ATOM   6369  CA  LEU B 238     -55.160   4.268  52.508  1.00 79.57           C  
ANISOU 6369  CA  LEU B 238    10548  11454   8230   1929    -97   -137       C  
ATOM   6370  C   LEU B 238     -54.616   3.479  51.303  1.00 79.77           C  
ANISOU 6370  C   LEU B 238    10577  11232   8499   1729   -104    -95       C  
ATOM   6371  O   LEU B 238     -54.616   4.018  50.200  1.00 77.83           O  
ANISOU 6371  O   LEU B 238    10256  10920   8395   1709   -125   -185       O  
ATOM   6372  CB  LEU B 238     -54.047   4.954  53.347  1.00 79.64           C  
ANISOU 6372  CB  LEU B 238    10694  11344   8222   2142   -267   -238       C  
ATOM   6373  CG  LEU B 238     -52.714   5.350  52.688  1.00 82.53           C  
ANISOU 6373  CG  LEU B 238    11121  11411   8826   2153   -428   -330       C  
ATOM   6374  CD1 LEU B 238     -52.833   6.638  51.910  1.00 81.71           C  
ANISOU 6374  CD1 LEU B 238    10945  11286   8814   2225   -518   -468       C  
ATOM   6375  CD2 LEU B 238     -51.638   5.519  53.732  1.00 85.31           C  
ANISOU 6375  CD2 LEU B 238    11617  11649   9146   2307   -575   -367       C  
ATOM   6376  N   LYS B 239     -54.198   2.199  51.505  1.00 75.55           N  
ANISOU 6376  N   LYS B 239    10133  10573   8000   1594   -100     38       N  
ATOM   6377  CA  LYS B 239     -53.693   1.301  50.448  1.00 73.76           C  
ANISOU 6377  CA  LYS B 239     9919  10127   7981   1440   -133     60       C  
ATOM   6378  C   LYS B 239     -54.782   1.095  49.395  1.00 76.17           C  
ANISOU 6378  C   LYS B 239    10085  10517   8339   1293    -28     86       C  
ATOM   6379  O   LYS B 239     -54.485   1.062  48.198  1.00 74.15           O  
ANISOU 6379  O   LYS B 239     9783  10138   8252   1246    -56     14       O  
ATOM   6380  CB  LYS B 239     -53.262  -0.057  51.042  1.00 77.44           C  
ANISOU 6380  CB  LYS B 239    10528  10459   8439   1342   -182    198       C  
ATOM   6381  CG  LYS B 239     -52.494  -0.960  50.069  1.00 92.02           C  
ANISOU 6381  CG  LYS B 239    12416  12055  10492   1257   -278    169       C  
ATOM   6382  CD  LYS B 239     -52.304  -2.368  50.634  1.00104.52           C  
ANISOU 6382  CD  LYS B 239    14156  13494  12064   1149   -361    313       C  
ATOM   6383  CE  LYS B 239     -51.446  -3.252  49.756  1.00113.69           C  
ANISOU 6383  CE  LYS B 239    15374  14406  13417   1127   -502    240       C  
ATOM   6384  NZ  LYS B 239     -51.192  -4.577  50.387  1.00123.47           N  
ANISOU 6384  NZ  LYS B 239    16802  15464  14647   1047   -641    365       N  
ATOM   6385  N   THR B 240     -56.046   0.989  49.867  1.00 73.41           N  
ANISOU 6385  N   THR B 240     9654  10407   7831   1229     92    186       N  
ATOM   6386  CA  THR B 240     -57.277   0.838  49.089  1.00 72.84           C  
ANISOU 6386  CA  THR B 240     9429  10471   7774   1094    199    221       C  
ATOM   6387  C   THR B 240     -57.446   2.040  48.159  1.00 73.69           C  
ANISOU 6387  C   THR B 240     9437  10609   7953   1205    193     41       C  
ATOM   6388  O   THR B 240     -57.728   1.864  46.977  1.00 72.23           O  
ANISOU 6388  O   THR B 240     9183  10356   7905   1110    206     10       O  
ATOM   6389  CB  THR B 240     -58.442   0.664  50.069  1.00 83.77           C  
ANISOU 6389  CB  THR B 240    10731  12169   8929   1042    323    359       C  
ATOM   6390  OG1 THR B 240     -58.280  -0.585  50.742  1.00 85.91           O  
ANISOU 6390  OG1 THR B 240    11109  12372   9162    879    306    567       O  
ATOM   6391  CG2 THR B 240     -59.797   0.724  49.403  1.00 82.80           C  
ANISOU 6391  CG2 THR B 240    10414  12251   8794    935    437    373       C  
ATOM   6392  N   THR B 241     -57.225   3.249  48.695  1.00 69.57           N  
ANISOU 6392  N   THR B 241     8926  10166   7340   1411    145    -79       N  
ATOM   6393  CA  THR B 241     -57.299   4.519  47.975  1.00 68.16           C  
ANISOU 6393  CA  THR B 241     8691   9989   7218   1531     85   -243       C  
ATOM   6394  C   THR B 241     -56.187   4.636  46.899  1.00 70.01           C  
ANISOU 6394  C   THR B 241     8970   9963   7666   1491    -15   -299       C  
ATOM   6395  O   THR B 241     -56.461   5.111  45.797  1.00 68.35           O  
ANISOU 6395  O   THR B 241     8689   9733   7547   1461    -22   -364       O  
ATOM   6396  CB  THR B 241     -57.305   5.676  48.987  1.00 77.31           C  
ANISOU 6396  CB  THR B 241     9880  11275   8219   1770      7   -349       C  
ATOM   6397  OG1 THR B 241     -58.313   5.433  49.972  1.00 78.76           O  
ANISOU 6397  OG1 THR B 241     9996  11759   8172   1808    121   -289       O  
ATOM   6398  CG2 THR B 241     -57.553   7.015  48.342  1.00 75.66           C  
ANISOU 6398  CG2 THR B 241     9630  11067   8052   1897    -95   -512       C  
ATOM   6399  N   VAL B 242     -54.953   4.190  47.214  1.00 66.53           N  
ANISOU 6399  N   VAL B 242     8637   9350   7292   1494    -90   -272       N  
ATOM   6400  CA  VAL B 242     -53.814   4.224  46.286  1.00 65.07           C  
ANISOU 6400  CA  VAL B 242     8465   8978   7281   1462   -175   -319       C  
ATOM   6401  C   VAL B 242     -54.052   3.264  45.109  1.00 70.37           C  
ANISOU 6401  C   VAL B 242     9075   9601   8060   1310   -111   -287       C  
ATOM   6402  O   VAL B 242     -53.848   3.672  43.963  1.00 69.48           O  
ANISOU 6402  O   VAL B 242     8896   9459   8045   1285   -130   -347       O  
ATOM   6403  CB  VAL B 242     -52.436   4.002  46.976  1.00 68.32           C  
ANISOU 6403  CB  VAL B 242     8985   9248   7725   1527   -281   -320       C  
ATOM   6404  CG1 VAL B 242     -51.284   4.157  45.987  1.00 66.89           C  
ANISOU 6404  CG1 VAL B 242     8767   8946   7702   1500   -360   -375       C  
ATOM   6405  CG2 VAL B 242     -52.239   4.956  48.148  1.00 68.63           C  
ANISOU 6405  CG2 VAL B 242     9093   9325   7657   1694   -367   -363       C  
ATOM   6406  N   ILE B 243     -54.514   2.012  45.384  1.00 68.57           N  
ANISOU 6406  N   ILE B 243     8875   9367   7810   1207    -56   -187       N  
ATOM   6407  CA  ILE B 243     -54.820   1.008  44.348  1.00 68.81           C  
ANISOU 6407  CA  ILE B 243     8867   9331   7947   1075    -35   -163       C  
ATOM   6408  C   ILE B 243     -55.804   1.587  43.318  1.00 73.43           C  
ANISOU 6408  C   ILE B 243     9324  10021   8554   1039     33   -213       C  
ATOM   6409  O   ILE B 243     -55.487   1.597  42.125  1.00 72.98           O  
ANISOU 6409  O   ILE B 243     9222   9903   8602   1024      7   -282       O  
ATOM   6410  CB  ILE B 243     -55.319  -0.343  44.937  1.00 73.40           C  
ANISOU 6410  CB  ILE B 243     9513   9877   8498    949    -25    -22       C  
ATOM   6411  CG1 ILE B 243     -54.190  -1.087  45.680  1.00 74.22           C  
ANISOU 6411  CG1 ILE B 243     9769   9817   8613    984   -136     11       C  
ATOM   6412  CG2 ILE B 243     -55.939  -1.238  43.842  1.00 74.50           C  
ANISOU 6412  CG2 ILE B 243     9602   9955   8748    813    -28     -4       C  
ATOM   6413  CD1 ILE B 243     -54.674  -2.027  46.804  1.00 83.49           C  
ANISOU 6413  CD1 ILE B 243    11041  10994   9687    879   -138    189       C  
ATOM   6414  N   LEU B 244     -56.968   2.103  43.797  1.00 69.91           N  
ANISOU 6414  N   LEU B 244     8814   9755   7994   1044    113   -191       N  
ATOM   6415  CA  LEU B 244     -58.028   2.708  42.983  1.00 69.04           C  
ANISOU 6415  CA  LEU B 244     8583   9763   7885   1031    167   -250       C  
ATOM   6416  C   LEU B 244     -57.515   3.808  42.045  1.00 71.08           C  
ANISOU 6416  C   LEU B 244     8825   9967   8213   1112     98   -369       C  
ATOM   6417  O   LEU B 244     -57.788   3.752  40.848  1.00 70.31           O  
ANISOU 6417  O   LEU B 244     8670   9847   8198   1056    106   -407       O  
ATOM   6418  CB  LEU B 244     -59.167   3.237  43.880  1.00 70.25           C  
ANISOU 6418  CB  LEU B 244     8665  10156   7870   1083    241   -237       C  
ATOM   6419  CG  LEU B 244     -60.409   3.812  43.182  1.00 75.03           C  
ANISOU 6419  CG  LEU B 244     9133  10916   8457   1086    291   -310       C  
ATOM   6420  CD1 LEU B 244     -61.242   2.714  42.531  1.00 76.00           C  
ANISOU 6420  CD1 LEU B 244     9173  11051   8651    900    361   -227       C  
ATOM   6421  CD2 LEU B 244     -61.281   4.563  44.166  1.00 78.70           C  
ANISOU 6421  CD2 LEU B 244     9526  11648   8729   1213    333   -348       C  
ATOM   6422  N   ILE B 245     -56.765   4.785  42.586  1.00 67.06           N  
ANISOU 6422  N   ILE B 245     8374   9434   7670   1232     14   -415       N  
ATOM   6423  CA  ILE B 245     -56.209   5.917  41.840  1.00 66.11           C  
ANISOU 6423  CA  ILE B 245     8253   9254   7612   1281    -85   -490       C  
ATOM   6424  C   ILE B 245     -55.246   5.463  40.749  1.00 70.22           C  
ANISOU 6424  C   ILE B 245     8758   9669   8255   1200   -104   -481       C  
ATOM   6425  O   ILE B 245     -55.366   5.935  39.619  1.00 69.92           O  
ANISOU 6425  O   ILE B 245     8665   9639   8263   1165   -119   -512       O  
ATOM   6426  CB  ILE B 245     -55.626   7.013  42.781  1.00 69.38           C  
ANISOU 6426  CB  ILE B 245     8743   9646   7973   1418   -210   -530       C  
ATOM   6427  CG1 ILE B 245     -56.764   7.699  43.579  1.00 70.72           C  
ANISOU 6427  CG1 ILE B 245     8900   9970   7999   1546   -211   -590       C  
ATOM   6428  CG2 ILE B 245     -54.800   8.053  42.002  1.00 68.87           C  
ANISOU 6428  CG2 ILE B 245     8689   9478   8001   1415   -348   -560       C  
ATOM   6429  CD1 ILE B 245     -56.363   8.435  44.866  1.00 77.32           C  
ANISOU 6429  CD1 ILE B 245     9825  10814   8740   1720   -327   -636       C  
ATOM   6430  N   LEU B 246     -54.330   4.523  41.068  1.00 66.92           N  
ANISOU 6430  N   LEU B 246     8383   9172   7873   1182   -109   -445       N  
ATOM   6431  CA  LEU B 246     -53.360   3.991  40.097  1.00 66.03           C  
ANISOU 6431  CA  LEU B 246     8236   9003   7850   1143   -132   -462       C  
ATOM   6432  C   LEU B 246     -54.060   3.206  38.988  1.00 67.86           C  
ANISOU 6432  C   LEU B 246     8407   9255   8123   1073    -72   -479       C  
ATOM   6433  O   LEU B 246     -53.841   3.492  37.814  1.00 66.14           O  
ANISOU 6433  O   LEU B 246     8119   9072   7939   1057    -78   -518       O  
ATOM   6434  CB  LEU B 246     -52.272   3.124  40.773  1.00 66.66           C  
ANISOU 6434  CB  LEU B 246     8381   8997   7951   1175   -179   -450       C  
ATOM   6435  CG  LEU B 246     -51.301   3.810  41.744  1.00 71.72           C  
ANISOU 6435  CG  LEU B 246     9077   9599   8573   1252   -264   -448       C  
ATOM   6436  CD1 LEU B 246     -50.537   2.777  42.542  1.00 72.62           C  
ANISOU 6436  CD1 LEU B 246     9275   9624   8693   1291   -305   -439       C  
ATOM   6437  CD2 LEU B 246     -50.332   4.743  41.019  1.00 73.35           C  
ANISOU 6437  CD2 LEU B 246     9207   9828   8834   1246   -334   -472       C  
ATOM   6438  N   ALA B 247     -54.945   2.264  39.371  1.00 65.70           N  
ANISOU 6438  N   ALA B 247     8158   8968   7838   1024    -25   -440       N  
ATOM   6439  CA  ALA B 247     -55.727   1.435  38.448  1.00 66.46           C  
ANISOU 6439  CA  ALA B 247     8208   9057   7986    952      3   -451       C  
ATOM   6440  C   ALA B 247     -56.571   2.275  37.474  1.00 71.07           C  
ANISOU 6440  C   ALA B 247     8705   9732   8567    941     42   -499       C  
ATOM   6441  O   ALA B 247     -56.778   1.851  36.336  1.00 71.18           O  
ANISOU 6441  O   ALA B 247     8673   9738   8635    917     38   -544       O  
ATOM   6442  CB  ALA B 247     -56.610   0.469  39.222  1.00 68.35           C  
ANISOU 6442  CB  ALA B 247     8485   9275   8210    867     29   -361       C  
ATOM   6443  N   PHE B 248     -57.039   3.466  37.913  1.00 67.46           N  
ANISOU 6443  N   PHE B 248     8235   9355   8042    980     56   -504       N  
ATOM   6444  CA  PHE B 248     -57.796   4.401  37.083  1.00 66.90           C  
ANISOU 6444  CA  PHE B 248     8105   9353   7962    989     57   -559       C  
ATOM   6445  C   PHE B 248     -56.882   4.930  35.982  1.00 70.41           C  
ANISOU 6445  C   PHE B 248     8535   9772   8445    993      1   -586       C  
ATOM   6446  O   PHE B 248     -57.278   4.940  34.819  1.00 69.90           O  
ANISOU 6446  O   PHE B 248     8421   9735   8403    967     10   -622       O  
ATOM   6447  CB  PHE B 248     -58.337   5.563  37.927  1.00 68.84           C  
ANISOU 6447  CB  PHE B 248     8364   9674   8120   1068     33   -579       C  
ATOM   6448  CG  PHE B 248     -59.148   6.585  37.161  1.00 70.41           C  
ANISOU 6448  CG  PHE B 248     8523   9925   8305   1100     -6   -652       C  
ATOM   6449  CD1 PHE B 248     -60.531   6.493  37.096  1.00 74.17           C  
ANISOU 6449  CD1 PHE B 248     8925  10510   8747   1102     50   -694       C  
ATOM   6450  CD2 PHE B 248     -58.530   7.671  36.549  1.00 72.23           C  
ANISOU 6450  CD2 PHE B 248     8790  10100   8555   1123   -116   -672       C  
ATOM   6451  CE1 PHE B 248     -61.280   7.459  36.419  1.00 75.20           C  
ANISOU 6451  CE1 PHE B 248     9030  10682   8863   1154     -9   -781       C  
ATOM   6452  CE2 PHE B 248     -59.279   8.624  35.856  1.00 75.09           C  
ANISOU 6452  CE2 PHE B 248     9144  10485   8904   1153   -186   -734       C  
ATOM   6453  CZ  PHE B 248     -60.647   8.515  35.801  1.00 73.75           C  
ANISOU 6453  CZ  PHE B 248     8911  10411   8699   1184   -136   -802       C  
ATOM   6454  N   PHE B 249     -55.667   5.375  36.356  1.00 67.05           N  
ANISOU 6454  N   PHE B 249     8145   9314   8018   1020    -58   -560       N  
ATOM   6455  CA  PHE B 249     -54.674   5.887  35.418  1.00 66.85           C  
ANISOU 6455  CA  PHE B 249     8080   9308   8012    997   -108   -552       C  
ATOM   6456  C   PHE B 249     -54.179   4.794  34.483  1.00 70.74           C  
ANISOU 6456  C   PHE B 249     8512   9833   8533    985    -69   -581       C  
ATOM   6457  O   PHE B 249     -53.957   5.070  33.305  1.00 70.51           O  
ANISOU 6457  O   PHE B 249     8416   9883   8492    962    -71   -589       O  
ATOM   6458  CB  PHE B 249     -53.502   6.561  36.151  1.00 68.95           C  
ANISOU 6458  CB  PHE B 249     8379   9540   8279   1013   -193   -508       C  
ATOM   6459  CG  PHE B 249     -53.823   7.930  36.702  1.00 71.04           C  
ANISOU 6459  CG  PHE B 249     8704   9768   8520   1040   -296   -497       C  
ATOM   6460  CD1 PHE B 249     -54.099   8.996  35.851  1.00 74.95           C  
ANISOU 6460  CD1 PHE B 249     9191  10273   9013    998   -375   -484       C  
ATOM   6461  CD2 PHE B 249     -53.820   8.163  38.071  1.00 73.53           C  
ANISOU 6461  CD2 PHE B 249     9096  10034   8807   1121   -342   -506       C  
ATOM   6462  CE1 PHE B 249     -54.397  10.265  36.363  1.00 76.49           C  
ANISOU 6462  CE1 PHE B 249     9466  10403   9195   1043   -524   -492       C  
ATOM   6463  CE2 PHE B 249     -54.114   9.433  38.582  1.00 76.90           C  
ANISOU 6463  CE2 PHE B 249     9588  10423   9207   1185   -477   -527       C  
ATOM   6464  CZ  PHE B 249     -54.400  10.474  37.725  1.00 75.43           C  
ANISOU 6464  CZ  PHE B 249     9404  10222   9035   1149   -580   -526       C  
ATOM   6465  N   ALA B 250     -54.053   3.552  34.996  1.00 67.51           N  
ANISOU 6465  N   ALA B 250     8133   9366   8151   1010    -51   -599       N  
ATOM   6466  CA  ALA B 250     -53.621   2.379  34.235  1.00 68.15           C  
ANISOU 6466  CA  ALA B 250     8180   9450   8262   1039    -59   -659       C  
ATOM   6467  C   ALA B 250     -54.575   2.082  33.064  1.00 73.85           C  
ANISOU 6467  C   ALA B 250     8858  10205   8996   1024    -36   -710       C  
ATOM   6468  O   ALA B 250     -54.115   1.681  31.993  1.00 74.24           O  
ANISOU 6468  O   ALA B 250     8847  10325   9036   1070    -53   -776       O  
ATOM   6469  CB  ALA B 250     -53.514   1.173  35.151  1.00 69.32           C  
ANISOU 6469  CB  ALA B 250     8411   9480   8446   1060    -92   -658       C  
ATOM   6470  N   CYS B 251     -55.893   2.319  33.262  1.00 70.61           N  
ANISOU 6470  N   CYS B 251     8466   9769   8593    973     -1   -689       N  
ATOM   6471  CA  CYS B 251     -56.939   2.137  32.252  1.00 70.67           C  
ANISOU 6471  CA  CYS B 251     8433   9797   8620    955     12   -738       C  
ATOM   6472  C   CYS B 251     -56.757   3.131  31.102  1.00 75.40           C  
ANISOU 6472  C   CYS B 251     8977  10501   9171    968     12   -760       C  
ATOM   6473  O   CYS B 251     -56.671   2.719  29.946  1.00 76.42           O  
ANISOU 6473  O   CYS B 251     9061  10682   9293   1001      1   -821       O  
ATOM   6474  CB  CYS B 251     -58.324   2.270  32.879  1.00 71.06           C  
ANISOU 6474  CB  CYS B 251     8488   9832   8677    899     50   -708       C  
ATOM   6475  SG  CYS B 251     -58.770   0.921  33.999  1.00 75.97           S  
ANISOU 6475  SG  CYS B 251     9158  10361   9346    831     49   -642       S  
ATOM   6476  N   TRP B 252     -56.680   4.435  31.430  1.00 71.29           N  
ANISOU 6476  N   TRP B 252     8471  10009   8609    945      2   -707       N  
ATOM   6477  CA  TRP B 252     -56.536   5.526  30.469  1.00 70.70           C  
ANISOU 6477  CA  TRP B 252     8368  10009   8485    924    -31   -688       C  
ATOM   6478  C   TRP B 252     -55.167   5.675  29.806  1.00 75.20           C  
ANISOU 6478  C   TRP B 252     8878  10685   9009    912    -44   -647       C  
ATOM   6479  O   TRP B 252     -55.095   6.203  28.696  1.00 74.34           O  
ANISOU 6479  O   TRP B 252     8726  10675   8845    883    -56   -625       O  
ATOM   6480  CB  TRP B 252     -56.993   6.842  31.094  1.00 68.90           C  
ANISOU 6480  CB  TRP B 252     8198   9741   8240    908    -90   -651       C  
ATOM   6481  CG  TRP B 252     -58.478   6.915  31.240  1.00 69.51           C  
ANISOU 6481  CG  TRP B 252     8287   9799   8326    933    -78   -714       C  
ATOM   6482  CD1 TRP B 252     -59.203   6.692  32.373  1.00 72.42           C  
ANISOU 6482  CD1 TRP B 252     8668  10151   8697    962    -48   -732       C  
ATOM   6483  CD2 TRP B 252     -59.429   7.140  30.191  1.00 69.41           C  
ANISOU 6483  CD2 TRP B 252     8252   9813   8306    935    -91   -770       C  
ATOM   6484  NE1 TRP B 252     -60.548   6.812  32.105  1.00 72.02           N  
ANISOU 6484  NE1 TRP B 252     8585  10137   8642    978    -38   -798       N  
ATOM   6485  CE2 TRP B 252     -60.715   7.079  30.769  1.00 73.37           C  
ANISOU 6485  CE2 TRP B 252     8742  10316   8818    966    -71   -829       C  
ATOM   6486  CE3 TRP B 252     -59.318   7.399  28.814  1.00 70.64           C  
ANISOU 6486  CE3 TRP B 252     8390  10014   8436    917   -118   -773       C  
ATOM   6487  CZ2 TRP B 252     -61.882   7.276  30.021  1.00 72.75           C  
ANISOU 6487  CZ2 TRP B 252     8634  10264   8742    984    -87   -906       C  
ATOM   6488  CZ3 TRP B 252     -60.475   7.585  28.073  1.00 72.04           C  
ANISOU 6488  CZ3 TRP B 252     8562  10197   8613    938   -138   -845       C  
ATOM   6489  CH2 TRP B 252     -61.737   7.528  28.676  1.00 72.63           C  
ANISOU 6489  CH2 TRP B 252     8625  10255   8717    973   -128   -918       C  
ATOM   6490  N   LEU B 253     -54.094   5.222  30.474  1.00 73.42           N  
ANISOU 6490  N   LEU B 253     8640  10461   8795    933    -43   -631       N  
ATOM   6491  CA  LEU B 253     -52.714   5.325  29.980  1.00 74.60           C  
ANISOU 6491  CA  LEU B 253     8696  10755   8894    925    -51   -595       C  
ATOM   6492  C   LEU B 253     -52.454   4.863  28.531  1.00 79.35           C  
ANISOU 6492  C   LEU B 253     9189  11539   9420    964    -18   -646       C  
ATOM   6493  O   LEU B 253     -51.882   5.665  27.790  1.00 79.47           O  
ANISOU 6493  O   LEU B 253     9125  11713   9356    896    -22   -562       O  
ATOM   6494  CB  LEU B 253     -51.696   4.735  30.984  1.00 75.05           C  
ANISOU 6494  CB  LEU B 253     8754  10779   8982    971    -65   -605       C  
ATOM   6495  CG  LEU B 253     -50.218   4.619  30.582  1.00 81.06           C  
ANISOU 6495  CG  LEU B 253     9387  11720   9692    989    -70   -598       C  
ATOM   6496  CD1 LEU B 253     -49.602   5.982  30.267  1.00 82.09           C  
ANISOU 6496  CD1 LEU B 253     9449  11962   9778    860   -103   -456       C  
ATOM   6497  CD2 LEU B 253     -49.427   3.998  31.698  1.00 83.77           C  
ANISOU 6497  CD2 LEU B 253     9760  11986  10081   1053   -103   -632       C  
ATOM   6498  N   PRO B 254     -52.843   3.635  28.082  1.00 76.10           N  
ANISOU 6498  N   PRO B 254     8773  11118   9022   1069     -4   -773       N  
ATOM   6499  CA  PRO B 254     -52.541   3.238  26.691  1.00 77.00           C  
ANISOU 6499  CA  PRO B 254     8782  11432   9041   1145     10   -845       C  
ATOM   6500  C   PRO B 254     -53.190   4.132  25.636  1.00 81.69           C  
ANISOU 6500  C   PRO B 254     9361  12111   9565   1080     25   -791       C  
ATOM   6501  O   PRO B 254     -52.579   4.400  24.606  1.00 82.07           O  
ANISOU 6501  O   PRO B 254     9300  12394   9488   1084     47   -765       O  
ATOM   6502  CB  PRO B 254     -53.041   1.791  26.614  1.00 78.77           C  
ANISOU 6502  CB  PRO B 254     9051  11549   9328   1274    -31   -999       C  
ATOM   6503  CG  PRO B 254     -53.121   1.331  28.032  1.00 82.28           C  
ANISOU 6503  CG  PRO B 254     9597  11783   9882   1251    -60   -982       C  
ATOM   6504  CD  PRO B 254     -53.533   2.542  28.795  1.00 76.83           C  
ANISOU 6504  CD  PRO B 254     8955  11026   9210   1121    -23   -851       C  
ATOM   6505  N   TYR B 255     -54.407   4.618  25.924  1.00 78.58           N  
ANISOU 6505  N   TYR B 255     9070  11548   9240   1021      9   -771       N  
ATOM   6506  CA  TYR B 255     -55.177   5.516  25.069  1.00 78.87           C  
ANISOU 6506  CA  TYR B 255     9126  11611   9229    965     -7   -731       C  
ATOM   6507  C   TYR B 255     -54.466   6.863  24.937  1.00 87.88           C  
ANISOU 6507  C   TYR B 255    10249  12844  10297    837    -40   -566       C  
ATOM   6508  O   TYR B 255     -54.410   7.395  23.828  1.00 88.44           O  
ANISOU 6508  O   TYR B 255    10281  13058  10265    794    -50   -508       O  
ATOM   6509  CB  TYR B 255     -56.617   5.653  25.608  1.00 77.99           C  
ANISOU 6509  CB  TYR B 255     9116  11304   9214    955    -31   -773       C  
ATOM   6510  CG  TYR B 255     -57.436   6.772  25.001  1.00 77.99           C  
ANISOU 6510  CG  TYR B 255     9162  11292   9180    904    -82   -738       C  
ATOM   6511  CD1 TYR B 255     -57.977   6.654  23.723  1.00 80.07           C  
ANISOU 6511  CD1 TYR B 255     9407  11626   9389    943    -88   -795       C  
ATOM   6512  CD2 TYR B 255     -57.721   7.926  25.727  1.00 77.66           C  
ANISOU 6512  CD2 TYR B 255     9196  11151   9160    841   -151   -669       C  
ATOM   6513  CE1 TYR B 255     -58.749   7.674  23.167  1.00 80.22           C  
ANISOU 6513  CE1 TYR B 255     9486  11618   9377    904   -157   -769       C  
ATOM   6514  CE2 TYR B 255     -58.496   8.950  25.184  1.00 78.32           C  
ANISOU 6514  CE2 TYR B 255     9343  11199   9217    815   -239   -656       C  
ATOM   6515  CZ  TYR B 255     -59.003   8.823  23.901  1.00 85.83           C  
ANISOU 6515  CZ  TYR B 255    10278  12219  10115    839   -239   -700       C  
ATOM   6516  OH  TYR B 255     -59.742   9.844  23.351  1.00 86.80           O  
ANISOU 6516  OH  TYR B 255    10477  12294  10207    818   -347   -689       O  
ATOM   6517  N   TYR B 256     -53.899   7.377  26.023  1.00 87.71           N  
ANISOU 6517  N   TYR B 256    10256  12744  10325    773    -74   -484       N  
ATOM   6518  CA  TYR B 256     -53.154   8.632  25.969  1.00 89.94           C  
ANISOU 6518  CA  TYR B 256    10526  13083  10563    632   -146   -313       C  
ATOM   6519  C   TYR B 256     -51.962   8.551  25.012  1.00 96.00           C  
ANISOU 6519  C   TYR B 256    11131  14140  11203    586    -99   -232       C  
ATOM   6520  O   TYR B 256     -51.715   9.473  24.235  1.00 96.72           O  
ANISOU 6520  O   TYR B 256    11193  14351  11207    454   -144    -84       O  
ATOM   6521  CB  TYR B 256     -52.679   9.033  27.367  1.00 92.12           C  
ANISOU 6521  CB  TYR B 256    10857  13218  10926    599   -207   -265       C  
ATOM   6522  CG  TYR B 256     -53.697   9.827  28.155  1.00 95.35           C  
ANISOU 6522  CG  TYR B 256    11416  13407  11406    601   -305   -277       C  
ATOM   6523  CD1 TYR B 256     -54.094  11.090  27.737  1.00 98.23           C  
ANISOU 6523  CD1 TYR B 256    11857  13714  11752    515   -439   -193       C  
ATOM   6524  CD2 TYR B 256     -54.260   9.313  29.315  1.00 95.97           C  
ANISOU 6524  CD2 TYR B 256    11559  13352  11555    697   -280   -376       C  
ATOM   6525  CE1 TYR B 256     -55.023  11.820  28.454  1.00 99.56           C  
ANISOU 6525  CE1 TYR B 256    12157  13699  11972    560   -556   -241       C  
ATOM   6526  CE2 TYR B 256     -55.190  10.036  30.038  1.00 97.07           C  
ANISOU 6526  CE2 TYR B 256    11806  13350  11727    729   -365   -408       C  
ATOM   6527  CZ  TYR B 256     -55.568  11.288  29.603  1.00107.89           C  
ANISOU 6527  CZ  TYR B 256    13246  14668  13080    678   -508   -358       C  
ATOM   6528  OH  TYR B 256     -56.494  12.011  30.320  1.00112.50           O  
ANISOU 6528  OH  TYR B 256    13934  15126  13684    752   -619   -425       O  
ATOM   6529  N   ILE B 257     -51.206   7.480  25.053  1.00 93.64           N  
ANISOU 6529  N   ILE B 257    10723  13977  10881    691    -22   -323       N  
ATOM   6530  CA  ILE B 257     -50.202   7.356  24.035  1.00 95.57           C  
ANISOU 6530  CA  ILE B 257    10784  14558  10970    684     32   -277       C  
ATOM   6531  C   ILE B 257     -50.760   7.328  22.624  1.00100.99           C  
ANISOU 6531  C   ILE B 257    11438  15405  11528    716     63   -298       C  
ATOM   6532  O   ILE B 257     -50.121   7.789  21.681  1.00102.60           O  
ANISOU 6532  O   ILE B 257    11513  15899  11572    635     89   -177       O  
ATOM   6533  CB  ILE B 257     -49.637   5.958  23.987  1.00 99.00           C  
ANISOU 6533  CB  ILE B 257    11116  15124  11376    879     93   -458       C  
ATOM   6534  N   GLY B 258     -51.984   6.830  22.488  1.00 96.30           N  
ANISOU 6534  N   GLY B 258    10960  14630  10998    821     56   -439       N  
ATOM   6535  CA  GLY B 258     -52.686   6.867  21.222  1.00 96.65           C  
ANISOU 6535  CA  GLY B 258    11008  14772  10943    859     62   -471       C  
ATOM   6536  C   GLY B 258     -53.148   8.243  20.799  1.00100.69           C  
ANISOU 6536  C   GLY B 258    11599  15243  11417    686     -8   -298       C  
ATOM   6537  O   GLY B 258     -53.212   8.534  19.625  1.00101.50           O  
ANISOU 6537  O   GLY B 258    11661  15530  11374    665     -2   -245       O  
ATOM   6538  N   ILE B 259     -53.483   9.098  21.749  1.00 96.09           N  
ANISOU 6538  N   ILE B 259    11141  14414  10956    575    -95   -216       N  
ATOM   6539  CA  ILE B 259     -53.855  10.439  21.387  1.00 96.28           C  
ANISOU 6539  CA  ILE B 259    11260  14369  10951    421   -213    -57       C  
ATOM   6540  C   ILE B 259     -52.547  10.979  20.955  1.00103.01           C  
ANISOU 6540  C   ILE B 259    11983  15478  11679    260   -211    154       C  
ATOM   6541  O   ILE B 259     -52.362  11.390  19.831  1.00103.84           O  
ANISOU 6541  O   ILE B 259    12034  15792  11629    175   -213    276       O  
ATOM   6542  CB  ILE B 259     -54.019  11.202  22.655  1.00 98.14           C  
ANISOU 6542  CB  ILE B 259    11620  14340  11329    352   -328    -12       C  
ATOM   6543  CG1 ILE B 259     -55.476  11.256  23.025  1.00 96.77           C  
ANISOU 6543  CG1 ILE B 259    11590  13924  11254    451   -383   -156       C  
ATOM   6544  CG2 ILE B 259     -53.472  12.587  22.452  1.00100.23           C  
ANISOU 6544  CG2 ILE B 259    11923  14609  11552    140   -478    227       C  
ATOM   6545  CD1 ILE B 259     -56.283  10.582  22.019  1.00103.59           C  
ANISOU 6545  CD1 ILE B 259    12435  14857  12067    557   -317   -281       C  
ATOM   6546  N   SER B 260     -51.634  10.992  21.907  1.00100.78           N  
ANISOU 6546  N   SER B 260    11645  15184  11462    209   -212    206       N  
ATOM   6547  CA  SER B 260     -50.284  11.439  21.686  1.00102.62           C  
ANISOU 6547  CA  SER B 260    11719  15673  11598     44   -209    409       C  
ATOM   6548  C   SER B 260     -49.441  11.112  20.477  1.00109.45           C  
ANISOU 6548  C   SER B 260    12361  16982  12242     24    -93    482       C  
ATOM   6549  O   SER B 260     -48.615  11.907  20.076  1.00111.03           O  
ANISOU 6549  O   SER B 260    12456  17390  12341   -191   -129    726       O  
ATOM   6550  CB  SER B 260     -49.402  10.703  22.673  1.00104.70           C  
ANISOU 6550  CB  SER B 260    11885  15963  11934    124   -145    325       C  
ATOM   6551  N   ILE B 261     -49.652   9.945  19.892  1.00106.70           N  
ANISOU 6551  N   ILE B 261    11936  16792  11813    249     30    273       N  
ATOM   6552  CA  ILE B 261     -48.895   9.549  18.720  1.00109.34           C  
ANISOU 6552  CA  ILE B 261    12047  17591  11907    291    140    297       C  
ATOM   6553  C   ILE B 261     -49.506  10.124  17.469  1.00118.19           C  
ANISOU 6553  C   ILE B 261    13209  18825  12874    221    120    401       C  
ATOM   6554  O   ILE B 261     -48.833  10.706  16.640  1.00120.30           O  
ANISOU 6554  O   ILE B 261    13336  19429  12943     62    143    617       O  
ATOM   6555  CB  ILE B 261     -49.253   8.105  18.439  1.00111.31           C  
ANISOU 6555  CB  ILE B 261    12267  17888  12137    604    220    -10       C  
ATOM   6556  CG1 ILE B 261     -48.197   7.165  19.015  1.00111.58           C  
ANISOU 6556  CG1 ILE B 261    12142  18076  12176    746    278   -140       C  
ATOM   6557  CG2 ILE B 261     -49.406   7.913  16.962  1.00113.36           C  
ANISOU 6557  CG2 ILE B 261    12436  18471  12164    691    276    -34       C  
ATOM   6558  CD1 ILE B 261     -48.578   5.705  18.989  1.00114.41           C  
ANISOU 6558  CD1 ILE B 261    12525  18373  12571   1055    291   -454       C  
ATOM   6559  N   ASP B 262     -50.817   9.952  17.336  1.00116.08           N  
ANISOU 6559  N   ASP B 262    13131  18280  12693    335     73    253       N  
ATOM   6560  CA  ASP B 262     -51.545  10.472  16.185  1.00118.04           C  
ANISOU 6560  CA  ASP B 262    13455  18582  12814    296     33    321       C  
ATOM   6561  C   ASP B 262     -52.124  11.848  16.493  1.00123.74           C  
ANISOU 6561  C   ASP B 262    14378  18999  13637     69   -141    515       C  
ATOM   6562  O   ASP B 262     -52.619  12.540  15.603  1.00124.73           O  
ANISOU 6562  O   ASP B 262    14589  19145  13659    -20   -218    630       O  
ATOM   6563  CB  ASP B 262     -52.663   9.510  15.777  1.00119.02           C  
ANISOU 6563  CB  ASP B 262    13662  18586  12973    558     55     38       C  
ATOM   6564  CG  ASP B 262     -53.403   9.969  14.537  1.00133.46           C  
ANISOU 6564  CG  ASP B 262    15565  20484  14660    548     11     83       C  
ATOM   6565  OD1 ASP B 262     -54.099  11.004  14.607  1.00133.29           O  
ANISOU 6565  OD1 ASP B 262    15718  20218  14707    398   -119    205       O  
ATOM   6566  OD2 ASP B 262     -53.289   9.296  13.491  1.00143.21           O  
ANISOU 6566  OD2 ASP B 262    16690  22016  15707    710     87    -17       O  
ATOM   6567  N   SER B 263     -52.057  12.237  17.762  1.00120.28           N  
ANISOU 6567  N   SER B 263    14029  18276  13397     -6   -225    539       N  
ATOM   6568  CA  SER B 263     -52.563  13.525  18.200  1.00120.38           C  
ANISOU 6568  CA  SER B 263    14243  17976  13521   -180   -432    684       C  
ATOM   6569  C   SER B 263     -51.650  14.593  17.638  1.00127.68           C  
ANISOU 6569  C   SER B 263    15108  19092  14313   -473   -523   1024       C  
ATOM   6570  O   SER B 263     -52.021  15.763  17.544  1.00127.74           O  
ANISOU 6570  O   SER B 263    15287  18898  14351   -648   -734   1194       O  
ATOM   6571  CB  SER B 263     -52.592  13.603  19.727  1.00122.15           C  
ANISOU 6571  CB  SER B 263    14553  17896  13963   -156   -499    610       C  
ATOM   6572  N   PHE B 264     -50.443  14.186  17.260  1.00126.63           N  
ANISOU 6572  N   PHE B 264    14725  19361  14028   -530   -380   1126       N  
ATOM   6573  CA  PHE B 264     -49.464  15.110  16.697  1.00129.59           C  
ANISOU 6573  CA  PHE B 264    14986  19997  14254   -840   -441   1481       C  
ATOM   6574  C   PHE B 264     -49.345  14.932  15.188  1.00136.38           C  
ANISOU 6574  C   PHE B 264    15709  21286  14822   -850   -326   1570       C  
ATOM   6575  O   PHE B 264     -48.806  15.793  14.492  1.00138.63           O  
ANISOU 6575  O   PHE B 264    15934  21791  14948  -1130   -392   1896       O  
ATOM   6576  CB  PHE B 264     -48.099  14.912  17.359  1.00132.09           C  
ANISOU 6576  CB  PHE B 264    15080  20521  14586   -929   -370   1568       C  
ATOM   6577  CG  PHE B 264     -47.966  15.595  18.690  1.00132.52           C  
ANISOU 6577  CG  PHE B 264    15274  20192  14886  -1044   -555   1625       C  
ATOM   6578  CD1 PHE B 264     -49.008  16.348  19.205  1.00134.20           C  
ANISOU 6578  CD1 PHE B 264    15782  19937  15270  -1050   -771   1593       C  
ATOM   6579  CD2 PHE B 264     -46.798  15.485  19.427  1.00135.17           C  
ANISOU 6579  CD2 PHE B 264    15438  20646  15273  -1122   -526   1691       C  
ATOM   6580  CE1 PHE B 264     -48.888  16.978  20.429  1.00134.45           C  
ANISOU 6580  CE1 PHE B 264    15944  19633  15509  -1119   -960   1621       C  
ATOM   6581  CE2 PHE B 264     -46.673  16.113  20.651  1.00137.21           C  
ANISOU 6581  CE2 PHE B 264    15832  20548  15752  -1207   -713   1732       C  
ATOM   6582  CZ  PHE B 264     -47.719  16.860  21.153  1.00134.03           C  
ANISOU 6582  CZ  PHE B 264    15732  19686  15509  -1199   -932   1694       C  
ATOM   6583  N   ILE B 265     -49.852  13.810  14.687  1.00132.70           N  
ANISOU 6583  N   ILE B 265    15197  20941  14280   -548   -171   1287       N  
ATOM   6584  CA  ILE B 265     -49.805  13.517  13.260  1.00134.99           C  
ANISOU 6584  CA  ILE B 265    15361  21649  14279   -488    -61   1314       C  
ATOM   6585  C   ILE B 265     -50.789  14.387  12.485  1.00139.71           C  
ANISOU 6585  C   ILE B 265    16183  22073  14828   -593   -213   1435       C  
ATOM   6586  O   ILE B 265     -52.003  14.251  12.635  1.00137.02           O  
ANISOU 6586  O   ILE B 265    16057  21372  14632   -432   -289   1225       O  
ATOM   6587  CB  ILE B 265     -50.112  12.035  12.977  1.00137.17           C  
ANISOU 6587  CB  ILE B 265    15551  22056  14511   -102    100    943       C  
ATOM   6588  CG1 ILE B 265     -48.837  11.295  12.569  1.00140.11           C  
ANISOU 6588  CG1 ILE B 265    15592  22987  14656    -13    278    928       C  
ATOM   6589  CG2 ILE B 265     -51.176  11.908  11.899  1.00137.60           C  
ANISOU 6589  CG2 ILE B 265    15728  22097  14455     38     79    837       C  
ATOM   6590  CD1 ILE B 265     -49.034   9.809  12.359  1.00146.59           C  
ANISOU 6590  CD1 ILE B 265    16339  23914  15446    387    383    545       C  
ATOM   6591  N   LEU B 266     -50.258  15.281  11.657  1.00139.83           N  
ANISOU 6591  N   LEU B 266    16141  22356  14632   -874   -265   1783       N  
ATOM   6592  CA  LEU B 266     -51.088  16.174  10.858  1.00140.98           C  
ANISOU 6592  CA  LEU B 266    16507  22352  14707   -999   -436   1935       C  
ATOM   6593  C   LEU B 266     -51.146  17.569  11.472  1.00145.12           C  
ANISOU 6593  C   LEU B 266    17246  22491  15401  -1323   -724   2210       C  
ATOM   6594  O   LEU B 266     -50.904  17.743  12.666  1.00143.12           O  
ANISOU 6594  O   LEU B 266    17030  21968  15381  -1366   -800   2182       O  
ATOM   6595  CB  LEU B 266     -52.501  15.604  10.713  1.00138.71           C  
ANISOU 6595  CB  LEU B 266    16415  21766  14521   -686   -453   1587       C  
ATOM   6596  CG  LEU B 266     -53.459  15.862  11.877  1.00140.54           C  
ANISOU 6596  CG  LEU B 266    16894  21418  15086   -619   -618   1411       C  
ATOM   6597  CD1 LEU B 266     -53.959  17.298  11.854  1.00141.63           C  
ANISOU 6597  CD1 LEU B 266    17294  21234  15287   -859   -914   1637       C  
ATOM   6598  CD2 LEU B 266     -54.624  14.884  11.842  1.00140.50           C  
ANISOU 6598  CD2 LEU B 266    16965  21244  15176   -277   -551   1027       C  
ATOM   6599  N   GLN B 272     -45.886   7.706   9.417  1.00159.98           N  
ANISOU 6599  N   GLN B 272    16992  27744  16047    970    840    331       N  
ATOM   6600  CA  GLN B 272     -45.350   8.001   8.090  1.00163.43           C  
ANISOU 6600  CA  GLN B 272    17186  28849  16061    940    949    500       C  
ATOM   6601  C   GLN B 272     -46.445   8.167   7.035  1.00166.33           C  
ANISOU 6601  C   GLN B 272    17743  29145  16309   1012    903    482       C  
ATOM   6602  O   GLN B 272     -46.660   9.284   6.566  1.00166.78           O  
ANISOU 6602  O   GLN B 272    17874  29220  16274    690    875    827       O  
ATOM   6603  CB  GLN B 272     -44.304   6.952   7.663  1.00167.64           C  
ANISOU 6603  CB  GLN B 272    17363  30017  16315   1281   1072    257       C  
ATOM   6604  CG  GLN B 272     -42.898   7.228   8.201  1.00187.91           C  
ANISOU 6604  CG  GLN B 272    19615  32966  18818   1091   1163    443       C  
ATOM   6605  CD  GLN B 272     -41.867   6.189   7.808  1.00212.07           C  
ANISOU 6605  CD  GLN B 272    22308  36674  21596   1462   1270    169       C  
ATOM   6606  OE1 GLN B 272     -41.886   5.613   6.709  1.00210.63           O  
ANISOU 6606  OE1 GLN B 272    21990  36949  21090   1772   1324    -15       O  
ATOM   6607  NE2 GLN B 272     -40.898   5.967   8.686  1.00204.00           N  
ANISOU 6607  NE2 GLN B 272    21104  35735  20671   1447   1290    135       N  
ATOM   6608  N   GLY B 273     -47.130   7.070   6.693  1.00161.73           N  
ANISOU 6608  N   GLY B 273    17252  28455  15743   1426    866     86       N  
ATOM   6609  CA  GLY B 273     -48.187   7.048   5.684  1.00161.71           C  
ANISOU 6609  CA  GLY B 273    17422  28383  15636   1562    808      2       C  
ATOM   6610  C   GLY B 273     -49.542   6.555   6.155  1.00161.73           C  
ANISOU 6610  C   GLY B 273    17755  27709  15987   1722    660   -269       C  
ATOM   6611  O   GLY B 273     -49.785   6.451   7.361  1.00158.27           O  
ANISOU 6611  O   GLY B 273    17451  26791  15895   1651    598   -325       O  
ATOM   6612  N   CYS B 274     -50.444   6.265   5.190  1.00158.31           N  
ANISOU 6612  N   CYS B 274    17444  27255  15453   1933    600   -429       N  
ATOM   6613  CA  CYS B 274     -51.811   5.790   5.446  1.00154.97           C  
ANISOU 6613  CA  CYS B 274    17307  26244  15329   2086    452   -681       C  
ATOM   6614  C   CYS B 274     -51.876   4.361   5.999  1.00156.64           C  
ANISOU 6614  C   CYS B 274    17518  26268  15730   2431    389  -1078       C  
ATOM   6615  O   CYS B 274     -52.808   4.049   6.740  1.00153.30           O  
ANISOU 6615  O   CYS B 274    17309  25292  15645   2441    279  -1212       O  
ATOM   6616  CB  CYS B 274     -52.701   5.963   4.215  1.00156.20           C  
ANISOU 6616  CB  CYS B 274    17584  26451  15315   2192    392   -717       C  
ATOM   6617  SG  CYS B 274     -53.096   7.689   3.812  1.00160.65           S  
ANISOU 6617  SG  CYS B 274    18295  26949  15795   1753    368   -266       S  
ATOM   6618  N   GLU B 275     -50.888   3.507   5.646  1.00154.99           N  
ANISOU 6618  N   GLU B 275    17066  26529  15295   2712    444  -1260       N  
ATOM   6619  CA  GLU B 275     -50.767   2.112   6.097  1.00154.09           C  
ANISOU 6619  CA  GLU B 275    16940  26286  15322   3063    347  -1640       C  
ATOM   6620  C   GLU B 275     -50.654   2.052   7.626  1.00153.79           C  
ANISOU 6620  C   GLU B 275    16985  25807  15641   2885    325  -1601       C  
ATOM   6621  O   GLU B 275     -51.373   1.282   8.268  1.00151.30           O  
ANISOU 6621  O   GLU B 275    16851  25015  15621   3000    190  -1813       O  
ATOM   6622  CB  GLU B 275     -49.541   1.442   5.432  1.00159.24           C  
ANISOU 6622  CB  GLU B 275    17280  27611  15614   3373    412  -1803       C  
ATOM   6623  CG  GLU B 275     -49.208   0.040   5.922  1.00171.51           C  
ANISOU 6623  CG  GLU B 275    18808  29069  17289   3744    281  -2192       C  
ATOM   6624  CD  GLU B 275     -50.087  -1.068   5.380  1.00195.94           C  
ANISOU 6624  CD  GLU B 275    22067  31929  20452   4134     67  -2573       C  
ATOM   6625  OE1 GLU B 275     -49.656  -1.752   4.425  1.00196.07           O  
ANISOU 6625  OE1 GLU B 275    21932  32398  20169   4526     19  -2828       O  
ATOM   6626  OE2 GLU B 275     -51.197  -1.267   5.926  1.00190.27           O  
ANISOU 6626  OE2 GLU B 275    21620  30588  20086   4055    -66  -2623       O  
ATOM   6627  N   PHE B 276     -49.757   2.881   8.189  1.00149.28           N  
ANISOU 6627  N   PHE B 276    16280  25407  15034   2592    449  -1314       N  
ATOM   6628  CA  PHE B 276     -49.502   2.987   9.620  1.00146.04           C  
ANISOU 6628  CA  PHE B 276    15927  24646  14917   2404    441  -1238       C  
ATOM   6629  C   PHE B 276     -50.581   3.801  10.341  1.00144.56           C  
ANISOU 6629  C   PHE B 276    16008  23891  15025   2112    386  -1065       C  
ATOM   6630  O   PHE B 276     -50.919   3.467  11.476  1.00141.73           O  
ANISOU 6630  O   PHE B 276    15785  23102  14964   2085    323  -1141       O  
ATOM   6631  CB  PHE B 276     -48.089   3.549   9.871  1.00149.71           C  
ANISOU 6631  CB  PHE B 276    16125  25542  15215   2225    574  -1013       C  
ATOM   6632  CG  PHE B 276     -47.765   3.926  11.298  1.00149.34           C  
ANISOU 6632  CG  PHE B 276    16136  25164  15444   1982    568   -875       C  
ATOM   6633  CD1 PHE B 276     -47.738   2.963  12.301  1.00150.94           C  
ANISOU 6633  CD1 PHE B 276    16413  25055  15884   2153    489  -1113       C  
ATOM   6634  CD2 PHE B 276     -47.470   5.240  11.635  1.00151.61           C  
ANISOU 6634  CD2 PHE B 276    16411  25445  15748   1586    617   -504       C  
ATOM   6635  CE1 PHE B 276     -47.457   3.317  13.623  1.00150.11           C  
ANISOU 6635  CE1 PHE B 276    16369  24652  16016   1943    481   -988       C  
ATOM   6636  CE2 PHE B 276     -47.166   5.589  12.955  1.00152.76           C  
ANISOU 6636  CE2 PHE B 276    16615  25284  16143   1389    591   -396       C  
ATOM   6637  CZ  PHE B 276     -47.152   4.624  13.937  1.00149.18           C  
ANISOU 6637  CZ  PHE B 276    16229  24548  15906   1577    536   -642       C  
ATOM   6638  N   GLU B 277     -51.137   4.841   9.683  1.00139.64           N  
ANISOU 6638  N   GLU B 277    15466  23280  14310   1912    396   -846       N  
ATOM   6639  CA  GLU B 277     -52.185   5.696  10.258  1.00136.09           C  
ANISOU 6639  CA  GLU B 277    15266  22334  14108   1666    320   -702       C  
ATOM   6640  C   GLU B 277     -53.509   4.948  10.486  1.00135.23           C  
ANISOU 6640  C   GLU B 277    15367  21770  14246   1844    204   -967       C  
ATOM   6641  O   GLU B 277     -54.270   5.321  11.382  1.00132.14           O  
ANISOU 6641  O   GLU B 277    15148  20945  14116   1696    145   -924       O  
ATOM   6642  CB  GLU B 277     -52.392   6.964   9.410  1.00138.80           C  
ANISOU 6642  CB  GLU B 277    15648  22821  14270   1431    322   -414       C  
ATOM   6643  N   ASN B 278     -53.764   3.884   9.693  1.00131.40           N  
ANISOU 6643  N   ASN B 278    14855  21402  13671   2165    159  -1243       N  
ATOM   6644  CA  ASN B 278     -54.953   3.038   9.806  1.00129.04           C  
ANISOU 6644  CA  ASN B 278    14726  20707  13597   2341     27  -1500       C  
ATOM   6645  C   ASN B 278     -54.903   2.239  11.102  1.00128.82           C  
ANISOU 6645  C   ASN B 278    14742  20360  13846   2366    -19  -1619       C  
ATOM   6646  O   ASN B 278     -55.922   2.131  11.779  1.00126.66           O  
ANISOU 6646  O   ASN B 278    14630  19659  13837   2297    -94  -1658       O  
ATOM   6647  CB  ASN B 278     -55.079   2.093   8.603  1.00132.99           C  
ANISOU 6647  CB  ASN B 278    15178  21435  13917   2691    -43  -1765       C  
ATOM   6648  CG  ASN B 278     -55.673   2.724   7.367  1.00161.94           C  
ANISOU 6648  CG  ASN B 278    18890  25254  17386   2695    -50  -1704       C  
ATOM   6649  OD1 ASN B 278     -56.733   3.357   7.404  1.00157.20           O  
ANISOU 6649  OD1 ASN B 278    18461  24342  16927   2545   -103  -1625       O  
ATOM   6650  ND2 ASN B 278     -55.030   2.516   6.228  1.00156.98           N  
ANISOU 6650  ND2 ASN B 278    18107  25121  16415   2896     -9  -1760       N  
ATOM   6651  N   THR B 279     -53.714   1.706  11.452  1.00124.18           N  
ANISOU 6651  N   THR B 279    13999  20000  13184   2460     24  -1667       N  
ATOM   6652  CA  THR B 279     -53.477   0.922  12.671  1.00121.66           C  
ANISOU 6652  CA  THR B 279    13715  19416  13093   2493    -28  -1769       C  
ATOM   6653  C   THR B 279     -53.462   1.793  13.931  1.00120.14           C  
ANISOU 6653  C   THR B 279    13589  18977  13082   2181     35  -1534       C  
ATOM   6654  O   THR B 279     -53.854   1.314  14.996  1.00117.99           O  
ANISOU 6654  O   THR B 279    13428  18349  13054   2155    -25  -1591       O  
ATOM   6655  CB  THR B 279     -52.209   0.060  12.548  1.00132.70           C  
ANISOU 6655  CB  THR B 279    14930  21154  14335   2735    -30  -1930       C  
ATOM   6656  OG1 THR B 279     -51.103   0.884  12.185  1.00134.23           O  
ANISOU 6656  OG1 THR B 279    14914  21819  14270   2627    122  -1736       O  
ATOM   6657  CG2 THR B 279     -52.370  -1.083  11.549  1.00133.27           C  
ANISOU 6657  CG2 THR B 279    14985  21358  14294   3114   -164  -2247       C  
ATOM   6658  N   VAL B 280     -53.013   3.065  13.808  1.00114.62           N  
ANISOU 6658  N   VAL B 280    12826  18467  12257   1945    135  -1265       N  
ATOM   6659  CA  VAL B 280     -52.954   4.043  14.902  1.00111.70           C  
ANISOU 6659  CA  VAL B 280    12522  17882  12035   1660    163  -1038       C  
ATOM   6660  C   VAL B 280     -54.375   4.386  15.348  1.00112.29           C  
ANISOU 6660  C   VAL B 280    12811  17526  12327   1566     89  -1037       C  
ATOM   6661  O   VAL B 280     -54.705   4.156  16.507  1.00110.07           O  
ANISOU 6661  O   VAL B 280    12620  16940  12262   1521     60  -1066       O  
ATOM   6662  CB  VAL B 280     -52.117   5.307  14.533  1.00116.55           C  
ANISOU 6662  CB  VAL B 280    13021  18804  12459   1428    238   -745       C  
ATOM   6663  CG1 VAL B 280     -52.309   6.437  15.541  1.00114.69           C  
ANISOU 6663  CG1 VAL B 280    12907  18279  12393   1144    204   -525       C  
ATOM   6664  CG2 VAL B 280     -50.643   4.967  14.408  1.00118.36           C  
ANISOU 6664  CG2 VAL B 280    13003  19463  12506   1491    322   -734       C  
ATOM   6665  N   HIS B 281     -55.226   4.873  14.415  1.00108.79           N  
ANISOU 6665  N   HIS B 281    12440  17082  11814   1555     55  -1019       N  
ATOM   6666  CA  HIS B 281     -56.617   5.235  14.692  1.00106.75           C  
ANISOU 6666  CA  HIS B 281    12359  16466  11735   1490    -22  -1040       C  
ATOM   6667  C   HIS B 281     -57.465   4.027  15.128  1.00107.31           C  
ANISOU 6667  C   HIS B 281    12497  16270  12008   1646    -85  -1274       C  
ATOM   6668  O   HIS B 281     -58.484   4.215  15.797  1.00105.41           O  
ANISOU 6668  O   HIS B 281    12367  15731  11952   1569   -130  -1282       O  
ATOM   6669  CB  HIS B 281     -57.239   5.989  13.503  1.00108.76           C  
ANISOU 6669  CB  HIS B 281    12668  16806  11847   1464    -60   -980       C  
ATOM   6670  CG  HIS B 281     -58.418   6.850  13.872  1.00111.27           C  
ANISOU 6670  CG  HIS B 281    13154  16809  12315   1337   -145   -929       C  
ATOM   6671  ND1 HIS B 281     -58.319   7.843  14.839  1.00112.22           N  
ANISOU 6671  ND1 HIS B 281    13337  16771  12529   1137   -168   -760       N  
ATOM   6672  CD2 HIS B 281     -59.673   6.867  13.359  1.00112.81           C  
ANISOU 6672  CD2 HIS B 281    13454  16843  12565   1406   -227  -1042       C  
ATOM   6673  CE1 HIS B 281     -59.517   8.404  14.896  1.00110.92           C  
ANISOU 6673  CE1 HIS B 281    13311  16368  12466   1110   -264   -791       C  
ATOM   6674  NE2 HIS B 281     -60.361   7.855  14.022  1.00111.50           N  
ANISOU 6674  NE2 HIS B 281    13408  16436  12522   1260   -296   -955       N  
ATOM   6675  N   LYS B 282     -57.017   2.796  14.782  1.00103.18           N  
ANISOU 6675  N   LYS B 282    11898  15862  11443   1863   -106  -1458       N  
ATOM   6676  CA  LYS B 282     -57.660   1.535  15.150  1.00101.76           C  
ANISOU 6676  CA  LYS B 282    11782  15431  11452   2003   -208  -1666       C  
ATOM   6677  C   LYS B 282     -57.437   1.255  16.635  1.00102.80           C  
ANISOU 6677  C   LYS B 282    11945  15346  11770   1900   -197  -1619       C  
ATOM   6678  O   LYS B 282     -58.389   0.915  17.334  1.00101.31           O  
ANISOU 6678  O   LYS B 282    11849  14861  11782   1845   -251  -1651       O  
ATOM   6679  CB  LYS B 282     -57.116   0.371  14.304  1.00106.07           C  
ANISOU 6679  CB  LYS B 282    12251  16171  11880   2286   -280  -1883       C  
ATOM   6680  CG  LYS B 282     -58.102  -0.781  14.129  1.00120.89           C  
ANISOU 6680  CG  LYS B 282    14224  17783  13925   2441   -449  -2102       C  
ATOM   6681  CD  LYS B 282     -57.460  -2.022  13.505  1.00133.67           C  
ANISOU 6681  CD  LYS B 282    15789  19546  15453   2749   -574  -2344       C  
ATOM   6682  CE  LYS B 282     -57.503  -2.049  11.991  1.00147.30           C  
ANISOU 6682  CE  LYS B 282    17464  21552  16953   2967   -611  -2474       C  
ATOM   6683  NZ  LYS B 282     -56.408  -1.251  11.375  1.00157.33           N  
ANISOU 6683  NZ  LYS B 282    18573  23296  17909   2972   -449  -2356       N  
ATOM   6684  N   TRP B 283     -56.194   1.418  17.117  1.00 98.81           N  
ANISOU 6684  N   TRP B 283    11352  15006  11187   1868   -126  -1534       N  
ATOM   6685  CA  TRP B 283     -55.847   1.193  18.519  1.00 97.47           C  
ANISOU 6685  CA  TRP B 283    11212  14653  11167   1783   -117  -1486       C  
ATOM   6686  C   TRP B 283     -56.408   2.246  19.482  1.00 96.18           C  
ANISOU 6686  C   TRP B 283    11132  14296  11116   1556    -73  -1311       C  
ATOM   6687  O   TRP B 283     -56.688   1.914  20.633  1.00 94.55           O  
ANISOU 6687  O   TRP B 283    10990  13866  11067   1502    -89  -1305       O  
ATOM   6688  CB  TRP B 283     -54.339   0.962  18.699  1.00 98.10           C  
ANISOU 6688  CB  TRP B 283    11166  14976  11133   1849    -76  -1481       C  
ATOM   6689  CG  TRP B 283     -53.992  -0.485  18.912  1.00100.47           C  
ANISOU 6689  CG  TRP B 283    11470  15212  11493   2058   -184  -1688       C  
ATOM   6690  CD1 TRP B 283     -53.985  -1.477  17.973  1.00105.25           C  
ANISOU 6690  CD1 TRP B 283    12048  15915  12028   2309   -290  -1906       C  
ATOM   6691  CD2 TRP B 283     -53.649  -1.107  20.157  1.00100.11           C  
ANISOU 6691  CD2 TRP B 283    11481  14961  11595   2044   -232  -1702       C  
ATOM   6692  NE1 TRP B 283     -53.652  -2.679  18.557  1.00105.42           N  
ANISOU 6692  NE1 TRP B 283    12115  15784  12155   2451   -424  -2059       N  
ATOM   6693  CE2 TRP B 283     -53.439  -2.480  19.897  1.00105.62           C  
ANISOU 6693  CE2 TRP B 283    12194  15623  12313   2283   -385  -1928       C  
ATOM   6694  CE3 TRP B 283     -53.477  -0.633  21.467  1.00100.03           C  
ANISOU 6694  CE3 TRP B 283    11519  14794  11693   1867   -180  -1552       C  
ATOM   6695  CZ2 TRP B 283     -53.081  -3.386  20.905  1.00105.17           C  
ANISOU 6695  CZ2 TRP B 283    12211  15360  12387   2327   -493  -1989       C  
ATOM   6696  CZ3 TRP B 283     -53.129  -1.529  22.466  1.00101.67           C  
ANISOU 6696  CZ3 TRP B 283    11789  14823  12017   1914   -260  -1612       C  
ATOM   6697  CH2 TRP B 283     -52.924  -2.886  22.181  1.00103.80           C  
ANISOU 6697  CH2 TRP B 283    12083  15047  12310   2133   -417  -1820       C  
ATOM   6698  N   ILE B 284     -56.621   3.490  18.998  1.00 90.07           N  
ANISOU 6698  N   ILE B 284    10363  13605  10253   1437    -39  -1176       N  
ATOM   6699  CA  ILE B 284     -57.208   4.602  19.762  1.00 87.47           C  
ANISOU 6699  CA  ILE B 284    10124  13102  10010   1261    -42  -1039       C  
ATOM   6700  C   ILE B 284     -58.687   4.279  20.085  1.00 88.98           C  
ANISOU 6700  C   ILE B 284    10408  13040  10359   1276    -92  -1140       C  
ATOM   6701  O   ILE B 284     -59.190   4.673  21.138  1.00 87.54           O  
ANISOU 6701  O   ILE B 284    10284  12690  10287   1187    -94  -1092       O  
ATOM   6702  CB  ILE B 284     -57.004   5.960  19.014  1.00 90.86           C  
ANISOU 6702  CB  ILE B 284    10551  13678  10295   1143    -45   -876       C  
ATOM   6703  CG1 ILE B 284     -55.518   6.368  19.005  1.00 91.91           C  
ANISOU 6703  CG1 ILE B 284    10569  14055  10297   1064      6   -727       C  
ATOM   6704  CG2 ILE B 284     -57.864   7.102  19.583  1.00 90.78           C  
ANISOU 6704  CG2 ILE B 284    10664  13456  10373   1013   -110   -789       C  
ATOM   6705  CD1 ILE B 284     -55.127   7.227  17.828  1.00 99.96           C  
ANISOU 6705  CD1 ILE B 284    11535  15331  11115    981      8   -581       C  
ATOM   6706  N   SER B 285     -59.352   3.522  19.191  1.00 85.05           N  
ANISOU 6706  N   SER B 285     9911  12539   9866   1398   -138  -1285       N  
ATOM   6707  CA  SER B 285     -60.736   3.072  19.346  1.00 83.72           C  
ANISOU 6707  CA  SER B 285     9798  12163   9848   1410   -196  -1385       C  
ATOM   6708  C   SER B 285     -60.821   1.968  20.406  1.00 84.89           C  
ANISOU 6708  C   SER B 285     9955  12148  10153   1408   -214  -1430       C  
ATOM   6709  O   SER B 285     -61.696   2.024  21.273  1.00 83.62           O  
ANISOU 6709  O   SER B 285     9824  11834  10115   1318   -213  -1404       O  
ATOM   6710  CB  SER B 285     -61.284   2.565  18.015  1.00 88.54           C  
ANISOU 6710  CB  SER B 285    10404  12821  10415   1545   -266  -1526       C  
ATOM   6711  OG  SER B 285     -61.143   3.542  16.997  1.00 99.02           O  
ANISOU 6711  OG  SER B 285    11731  14319  11572   1544   -254  -1468       O  
ATOM   6712  N   ILE B 286     -59.887   0.987  20.339  1.00 80.54           N  
ANISOU 6712  N   ILE B 286     9373  11648   9580   1512   -239  -1495       N  
ATOM   6713  CA  ILE B 286     -59.742  -0.163  21.244  1.00 79.84           C  
ANISOU 6713  CA  ILE B 286     9313  11402   9622   1524   -294  -1534       C  
ATOM   6714  C   ILE B 286     -59.390   0.303  22.666  1.00 80.65           C  
ANISOU 6714  C   ILE B 286     9434  11442   9767   1389   -218  -1393       C  
ATOM   6715  O   ILE B 286     -60.061  -0.090  23.625  1.00 79.77           O  
ANISOU 6715  O   ILE B 286     9366  11161   9783   1303   -233  -1359       O  
ATOM   6716  CB  ILE B 286     -58.664  -1.147  20.690  1.00 84.46           C  
ANISOU 6716  CB  ILE B 286     9863  12092  10135   1710   -368  -1660       C  
ATOM   6717  CG1 ILE B 286     -59.082  -1.770  19.336  1.00 86.52           C  
ANISOU 6717  CG1 ILE B 286    10118  12399  10358   1885   -479  -1834       C  
ATOM   6718  CG2 ILE B 286     -58.286  -2.226  21.716  1.00 85.22           C  
ANISOU 6718  CG2 ILE B 286    10011  12015  10353   1720   -449  -1683       C  
ATOM   6719  CD1 ILE B 286     -57.891  -2.239  18.445  1.00 96.45           C  
ANISOU 6719  CD1 ILE B 286    11297  13911  11438   2113   -516  -1966       C  
ATOM   6720  N   THR B 287     -58.323   1.118  22.793  1.00 75.13           N  
ANISOU 6720  N   THR B 287     8696  10897   8954   1367   -144  -1304       N  
ATOM   6721  CA  THR B 287     -57.829   1.627  24.074  1.00 73.05           C  
ANISOU 6721  CA  THR B 287     8453  10587   8717   1265    -91  -1182       C  
ATOM   6722  C   THR B 287     -58.807   2.497  24.858  1.00 74.29           C  
ANISOU 6722  C   THR B 287     8659  10636   8932   1144    -62  -1099       C  
ATOM   6723  O   THR B 287     -58.788   2.440  26.084  1.00 74.14           O  
ANISOU 6723  O   THR B 287     8673  10524   8971   1089    -44  -1042       O  
ATOM   6724  CB  THR B 287     -56.426   2.211  23.958  1.00 76.89           C  
ANISOU 6724  CB  THR B 287     8871  11262   9080   1269    -47  -1113       C  
ATOM   6725  OG1 THR B 287     -56.389   3.167  22.904  1.00 75.52           O  
ANISOU 6725  OG1 THR B 287     8653  11256   8784   1244    -25  -1063       O  
ATOM   6726  CG2 THR B 287     -55.383   1.149  23.736  1.00 75.44           C  
ANISOU 6726  CG2 THR B 287     8631  11175   8859   1408    -81  -1213       C  
ATOM   6727  N   GLU B 288     -59.650   3.286  24.167  1.00 68.78           N  
ANISOU 6727  N   GLU B 288     7966   9963   8205   1124    -68  -1104       N  
ATOM   6728  CA  GLU B 288     -60.681   4.122  24.785  1.00 67.67           C  
ANISOU 6728  CA  GLU B 288     7861   9744   8105   1054    -67  -1069       C  
ATOM   6729  C   GLU B 288     -61.797   3.206  25.279  1.00 71.72           C  
ANISOU 6729  C   GLU B 288     8367  10148   8735   1041    -73  -1128       C  
ATOM   6730  O   GLU B 288     -62.367   3.447  26.345  1.00 71.30           O  
ANISOU 6730  O   GLU B 288     8318  10053   8719    986    -47  -1087       O  
ATOM   6731  CB  GLU B 288     -61.250   5.121  23.762  1.00 69.17           C  
ANISOU 6731  CB  GLU B 288     8066   9988   8230   1058   -107  -1081       C  
ATOM   6732  CG  GLU B 288     -62.219   6.139  24.347  1.00 77.62           C  
ANISOU 6732  CG  GLU B 288     9175  10995   9322   1023   -140  -1071       C  
ATOM   6733  CD  GLU B 288     -63.027   6.935  23.341  1.00 94.37           C  
ANISOU 6733  CD  GLU B 288    11327  13129  11401   1047   -212  -1118       C  
ATOM   6734  OE1 GLU B 288     -63.363   8.098  23.655  1.00 81.62           O  
ANISOU 6734  OE1 GLU B 288     9768  11481   9762   1032   -282  -1093       O  
ATOM   6735  OE2 GLU B 288     -63.338   6.399  22.251  1.00 88.01           O  
ANISOU 6735  OE2 GLU B 288    10499  12354  10585   1095   -223  -1191       O  
ATOM   6736  N   ALA B 289     -62.106   2.161  24.489  1.00 68.79           N  
ANISOU 6736  N   ALA B 289     7979   9745   8413   1092   -121  -1220       N  
ATOM   6737  CA  ALA B 289     -63.125   1.168  24.806  1.00 68.72           C  
ANISOU 6737  CA  ALA B 289     7958   9621   8531   1052   -161  -1257       C  
ATOM   6738  C   ALA B 289     -62.696   0.361  26.026  1.00 70.93           C  
ANISOU 6738  C   ALA B 289     8262   9818   8872    992   -154  -1184       C  
ATOM   6739  O   ALA B 289     -63.514   0.145  26.919  1.00 70.48           O  
ANISOU 6739  O   ALA B 289     8187   9714   8879    892   -135  -1126       O  
ATOM   6740  CB  ALA B 289     -63.359   0.257  23.615  1.00 70.36           C  
ANISOU 6740  CB  ALA B 289     8162   9792   8779   1137   -260  -1378       C  
ATOM   6741  N   LEU B 290     -61.407  -0.031  26.091  1.00 66.73           N  
ANISOU 6741  N   LEU B 290     7761   9291   8303   1052   -169  -1182       N  
ATOM   6742  CA  LEU B 290     -60.863  -0.774  27.232  1.00 66.79           C  
ANISOU 6742  CA  LEU B 290     7813   9206   8358   1011   -184  -1117       C  
ATOM   6743  C   LEU B 290     -60.710   0.119  28.469  1.00 68.34           C  
ANISOU 6743  C   LEU B 290     8016   9442   8508    939    -88  -1003       C  
ATOM   6744  O   LEU B 290     -60.814  -0.381  29.586  1.00 67.48           O  
ANISOU 6744  O   LEU B 290     7938   9261   8439    869    -84   -927       O  
ATOM   6745  CB  LEU B 290     -59.523  -1.452  26.889  1.00 67.59           C  
ANISOU 6745  CB  LEU B 290     7938   9315   8429   1131   -250  -1182       C  
ATOM   6746  CG  LEU B 290     -59.554  -2.602  25.879  1.00 73.78           C  
ANISOU 6746  CG  LEU B 290     8736  10038   9261   1245   -394  -1323       C  
ATOM   6747  CD1 LEU B 290     -58.164  -2.924  25.406  1.00 74.48           C  
ANISOU 6747  CD1 LEU B 290     8810  10229   9262   1410   -438  -1417       C  
ATOM   6748  CD2 LEU B 290     -60.220  -3.853  26.458  1.00 77.26           C  
ANISOU 6748  CD2 LEU B 290     9247  10254   9853   1169   -527  -1306       C  
ATOM   6749  N   ALA B 291     -60.482   1.438  28.264  1.00 64.07           N  
ANISOU 6749  N   ALA B 291     7456   9010   7879    958    -33   -987       N  
ATOM   6750  CA  ALA B 291     -60.337   2.432  29.329  1.00 63.44           C  
ANISOU 6750  CA  ALA B 291     7394   8960   7752    923     17   -905       C  
ATOM   6751  C   ALA B 291     -61.608   2.550  30.144  1.00 69.59           C  
ANISOU 6751  C   ALA B 291     8153   9737   8553    865     50   -881       C  
ATOM   6752  O   ALA B 291     -61.521   2.836  31.336  1.00 69.84           O  
ANISOU 6752  O   ALA B 291     8203   9781   8553    846     83   -818       O  
ATOM   6753  CB  ALA B 291     -59.977   3.788  28.752  1.00 63.55           C  
ANISOU 6753  CB  ALA B 291     7405   9057   7684    946     12   -898       C  
ATOM   6754  N   PHE B 292     -62.782   2.279  29.521  1.00 67.47           N  
ANISOU 6754  N   PHE B 292     7832   9472   8329    843     38   -936       N  
ATOM   6755  CA  PHE B 292     -64.098   2.329  30.173  1.00 68.10           C  
ANISOU 6755  CA  PHE B 292     7848   9604   8423    784     74   -921       C  
ATOM   6756  C   PHE B 292     -64.279   1.332  31.319  1.00 74.32           C  
ANISOU 6756  C   PHE B 292     8626  10367   9246    683    102   -820       C  
ATOM   6757  O   PHE B 292     -65.277   1.412  32.034  1.00 74.27           O  
ANISOU 6757  O   PHE B 292     8541  10461   9218    624    152   -781       O  
ATOM   6758  CB  PHE B 292     -65.245   2.253  29.154  1.00 70.24           C  
ANISOU 6758  CB  PHE B 292     8052   9892   8743    782     41  -1008       C  
ATOM   6759  CG  PHE B 292     -65.277   3.362  28.127  1.00 71.27           C  
ANISOU 6759  CG  PHE B 292     8200  10061   8819    872      6  -1094       C  
ATOM   6760  CD1 PHE B 292     -64.822   4.638  28.439  1.00 73.82           C  
ANISOU 6760  CD1 PHE B 292     8569  10427   9052    924      2  -1081       C  
ATOM   6761  CD2 PHE B 292     -65.818   3.146  26.864  1.00 73.86           C  
ANISOU 6761  CD2 PHE B 292     8508  10368   9186    900    -48  -1183       C  
ATOM   6762  CE1 PHE B 292     -64.851   5.661  27.488  1.00 74.48           C  
ANISOU 6762  CE1 PHE B 292     8689  10524   9086    982    -62  -1132       C  
ATOM   6763  CE2 PHE B 292     -65.867   4.177  25.920  1.00 76.18           C  
ANISOU 6763  CE2 PHE B 292     8832  10697   9415    974    -91  -1245       C  
ATOM   6764  CZ  PHE B 292     -65.383   5.427  26.238  1.00 73.63           C  
ANISOU 6764  CZ  PHE B 292     8564  10408   9004   1003   -101  -1209       C  
ATOM   6765  N   PHE B 293     -63.283   0.445  31.530  1.00 72.98           N  
ANISOU 6765  N   PHE B 293     8533  10084   9114    669     62   -774       N  
ATOM   6766  CA  PHE B 293     -63.213  -0.523  32.624  1.00 74.94           C  
ANISOU 6766  CA  PHE B 293     8813  10271   9389    571     56   -658       C  
ATOM   6767  C   PHE B 293     -63.038   0.221  33.966  1.00 79.50           C  
ANISOU 6767  C   PHE B 293     9396  10954   9857    579    142   -583       C  
ATOM   6768  O   PHE B 293     -63.280  -0.367  35.022  1.00 79.92           O  
ANISOU 6768  O   PHE B 293     9452  11020   9892    486    165   -467       O  
ATOM   6769  CB  PHE B 293     -62.050  -1.507  32.381  1.00 77.47           C  
ANISOU 6769  CB  PHE B 293     9235  10432   9769    605    -45   -670       C  
ATOM   6770  CG  PHE B 293     -61.829  -2.569  33.431  1.00 80.96           C  
ANISOU 6770  CG  PHE B 293     9751  10764  10246    510    -98   -552       C  
ATOM   6771  CD1 PHE B 293     -62.591  -3.730  33.439  1.00 86.27           C  
ANISOU 6771  CD1 PHE B 293    10431  11327  11021    374   -192   -483       C  
ATOM   6772  CD2 PHE B 293     -60.828  -2.428  34.386  1.00 83.61           C  
ANISOU 6772  CD2 PHE B 293    10161  11088  10520    548    -80   -501       C  
ATOM   6773  CE1 PHE B 293     -62.374  -4.722  34.402  1.00 88.90           C  
ANISOU 6773  CE1 PHE B 293    10854  11538  11385    263   -271   -348       C  
ATOM   6774  CE2 PHE B 293     -60.618  -3.417  35.357  1.00 87.98           C  
ANISOU 6774  CE2 PHE B 293    10804  11529  11098    461   -146   -384       C  
ATOM   6775  CZ  PHE B 293     -61.389  -4.559  35.354  1.00 87.85           C  
ANISOU 6775  CZ  PHE B 293    10804  11400  11175    313   -245   -301       C  
ATOM   6776  N   HIS B 294     -62.662   1.527  33.912  1.00 75.86           N  
ANISOU 6776  N   HIS B 294     8940  10569   9316    689    169   -644       N  
ATOM   6777  CA  HIS B 294     -62.501   2.409  35.071  1.00 76.17           C  
ANISOU 6777  CA  HIS B 294     8992  10701   9248    742    211   -612       C  
ATOM   6778  C   HIS B 294     -63.827   2.557  35.839  1.00 82.65           C  
ANISOU 6778  C   HIS B 294     9711  11695   9999    707    281   -584       C  
ATOM   6779  O   HIS B 294     -63.815   2.815  37.044  1.00 83.33           O  
ANISOU 6779  O   HIS B 294     9799  11880   9984    733    322   -532       O  
ATOM   6780  CB  HIS B 294     -61.920   3.784  34.658  1.00 75.94           C  
ANISOU 6780  CB  HIS B 294     8997  10683   9175    856    170   -688       C  
ATOM   6781  CG  HIS B 294     -62.905   4.729  34.026  1.00 79.46           C  
ANISOU 6781  CG  HIS B 294     9385  11212   9595    904    153   -777       C  
ATOM   6782  ND1 HIS B 294     -63.661   5.602  34.790  1.00 81.82           N  
ANISOU 6782  ND1 HIS B 294     9648  11637   9803    978    155   -817       N  
ATOM   6783  CD2 HIS B 294     -63.188   4.943  32.719  1.00 80.88           C  
ANISOU 6783  CD2 HIS B 294     9548  11368   9816    910    114   -846       C  
ATOM   6784  CE1 HIS B 294     -64.391   6.293  33.929  1.00 81.18           C  
ANISOU 6784  CE1 HIS B 294     9532  11587   9724   1024    108   -913       C  
ATOM   6785  NE2 HIS B 294     -64.141   5.932  32.674  1.00 80.90           N  
ANISOU 6785  NE2 HIS B 294     9511  11458   9767    976     86   -924       N  
ATOM   6786  N   CYS B 295     -64.960   2.369  35.129  1.00 80.03           N  
ANISOU 6786  N   CYS B 295     9277  11421   9711    656    290   -625       N  
ATOM   6787  CA  CYS B 295     -66.312   2.410  35.680  1.00 81.47           C  
ANISOU 6787  CA  CYS B 295     9314  11810   9831    610    358   -606       C  
ATOM   6788  C   CYS B 295     -66.520   1.196  36.571  1.00 86.47           C  
ANISOU 6788  C   CYS B 295     9919  12467  10467    440    402   -433       C  
ATOM   6789  O   CYS B 295     -67.130   1.310  37.637  1.00 87.51           O  
ANISOU 6789  O   CYS B 295     9959  12815  10477    415    484   -362       O  
ATOM   6790  CB  CYS B 295     -67.349   2.458  34.563  1.00 82.22           C  
ANISOU 6790  CB  CYS B 295     9310  11936   9995    594    336   -699       C  
ATOM   6791  SG  CYS B 295     -67.095   3.802  33.378  1.00 84.87           S  
ANISOU 6791  SG  CYS B 295     9707  12213  10327    766    254   -875       S  
ATOM   6792  N   CYS B 296     -65.965   0.044  36.143  1.00 82.72           N  
ANISOU 6792  N   CYS B 296     9532  11775  10121    334    329   -366       N  
ATOM   6793  CA  CYS B 296     -66.041  -1.244  36.831  1.00 84.08           C  
ANISOU 6793  CA  CYS B 296     9726  11888  10331    150    307   -187       C  
ATOM   6794  C   CYS B 296     -64.972  -1.421  37.921  1.00 86.27           C  
ANISOU 6794  C   CYS B 296    10133  12107  10538    172    307    -95       C  
ATOM   6795  O   CYS B 296     -64.971  -2.447  38.594  1.00 86.89           O  
ANISOU 6795  O   CYS B 296    10254  12128  10632     19    274     69       O  
ATOM   6796  CB  CYS B 296     -66.005  -2.388  35.819  1.00 85.05           C  
ANISOU 6796  CB  CYS B 296     9902  11779  10635     54    172   -187       C  
ATOM   6797  SG  CYS B 296     -67.273  -2.276  34.530  1.00 89.43           S  
ANISOU 6797  SG  CYS B 296    10313  12383  11284     30    149   -297       S  
ATOM   6798  N   LEU B 297     -64.089  -0.421  38.118  1.00 80.51           N  
ANISOU 6798  N   LEU B 297     9469  11386   9734    350    326   -191       N  
ATOM   6799  CA  LEU B 297     -63.031  -0.479  39.126  1.00 79.49           C  
ANISOU 6799  CA  LEU B 297     9461  11201   9542    395    315   -128       C  
ATOM   6800  C   LEU B 297     -63.536  -0.362  40.552  1.00 82.97           C  
ANISOU 6800  C   LEU B 297     9855  11851   9820    361    405     -8       C  
ATOM   6801  O   LEU B 297     -63.255  -1.255  41.355  1.00 83.83           O  
ANISOU 6801  O   LEU B 297    10037  11903   9910    253    385    144       O  
ATOM   6802  CB  LEU B 297     -61.936   0.555  38.849  1.00 77.73           C  
ANISOU 6802  CB  LEU B 297     9310  10920   9305    577    285   -258       C  
ATOM   6803  CG  LEU B 297     -60.826   0.099  37.921  1.00 81.49           C  
ANISOU 6803  CG  LEU B 297     9873  11190   9898    607    190   -318       C  
ATOM   6804  CD1 LEU B 297     -59.967   1.255  37.529  1.00 80.13           C  
ANISOU 6804  CD1 LEU B 297     9720  11022   9703    745    174   -421       C  
ATOM   6805  CD2 LEU B 297     -59.965  -0.986  38.569  1.00 85.03           C  
ANISOU 6805  CD2 LEU B 297    10440  11489  10378    565    120   -233       C  
ATOM   6806  N   ASN B 298     -64.270   0.731  40.866  1.00 78.17           N  
ANISOU 6806  N   ASN B 298     9128  11491   9081    467    488    -82       N  
ATOM   6807  CA  ASN B 298     -64.867   1.003  42.185  1.00 79.04           C  
ANISOU 6807  CA  ASN B 298     9156  11885   8992    484    584     -4       C  
ATOM   6808  C   ASN B 298     -65.733  -0.180  42.726  1.00 83.25           C  
ANISOU 6808  C   ASN B 298     9595  12545   9492    238    645    215       C  
ATOM   6809  O   ASN B 298     -65.455  -0.620  43.847  1.00 83.44           O  
ANISOU 6809  O   ASN B 298     9671  12628   9404    183    671    367       O  
ATOM   6810  CB  ASN B 298     -65.616   2.354  42.183  1.00 80.20           C  
ANISOU 6810  CB  ASN B 298     9177  12278   9018    671    625   -171       C  
ATOM   6811  CG  ASN B 298     -66.223   2.790  43.498  1.00 99.07           C  
ANISOU 6811  CG  ASN B 298    11462  15013  11168    760    713   -145       C  
ATOM   6812  OD1 ASN B 298     -65.595   2.740  44.557  1.00 95.18           O  
ANISOU 6812  OD1 ASN B 298    11057  14543  10565    809    719    -75       O  
ATOM   6813  ND2 ASN B 298     -67.435   3.314  43.436  1.00 89.38           N  
ANISOU 6813  ND2 ASN B 298    10041  14080   9841    817    773   -229       N  
ATOM   6814  N   PRO B 299     -66.699  -0.766  41.954  1.00 79.72           N  
ANISOU 6814  N   PRO B 299     9024  12118   9148     71    648    256       N  
ATOM   6815  CA  PRO B 299     -67.472  -1.912  42.477  1.00 81.76           C  
ANISOU 6815  CA  PRO B 299     9195  12479   9390   -205    676    501       C  
ATOM   6816  C   PRO B 299     -66.675  -3.196  42.712  1.00 85.04           C  
ANISOU 6816  C   PRO B 299     9802  12595   9913   -377    553    681       C  
ATOM   6817  O   PRO B 299     -66.932  -3.886  43.697  1.00 86.94           O  
ANISOU 6817  O   PRO B 299    10033  12943  10058   -558    577    913       O  
ATOM   6818  CB  PRO B 299     -68.542  -2.135  41.404  1.00 84.00           C  
ANISOU 6818  CB  PRO B 299     9324  12790   9804   -317    662    462       C  
ATOM   6819  CG  PRO B 299     -68.599  -0.862  40.640  1.00 86.62           C  
ANISOU 6819  CG  PRO B 299     9615  13165  10130    -68    679    196       C  
ATOM   6820  CD  PRO B 299     -67.190  -0.393  40.612  1.00 80.12           C  
ANISOU 6820  CD  PRO B 299     9003  12111   9326    113    614     95       C  
ATOM   6821  N   ILE B 300     -65.733  -3.523  41.803  1.00 79.12           N  
ANISOU 6821  N   ILE B 300     9222  11490   9350   -317    410    573       N  
ATOM   6822  CA  ILE B 300     -64.862  -4.702  41.880  1.00 79.31           C  
ANISOU 6822  CA  ILE B 300     9448  11195   9491   -418    245    679       C  
ATOM   6823  C   ILE B 300     -63.953  -4.600  43.118  1.00 84.00           C  
ANISOU 6823  C   ILE B 300    10174  11797   9946   -345    262    752       C  
ATOM   6824  O   ILE B 300     -63.714  -5.607  43.794  1.00 85.03           O  
ANISOU 6824  O   ILE B 300    10422  11807  10079   -502    171    945       O  
ATOM   6825  CB  ILE B 300     -64.080  -4.888  40.535  1.00 80.52           C  
ANISOU 6825  CB  ILE B 300     9711  11045   9839   -301    100    487       C  
ATOM   6826  CG1 ILE B 300     -64.946  -5.542  39.408  1.00 81.76           C  
ANISOU 6826  CG1 ILE B 300     9794  11109  10162   -432      9    475       C  
ATOM   6827  CG2 ILE B 300     -62.704  -5.554  40.682  1.00 80.68           C  
ANISOU 6827  CG2 ILE B 300     9952  10780   9925   -236    -54    476       C  
ATOM   6828  CD1 ILE B 300     -65.476  -7.012  39.616  1.00 93.57           C  
ANISOU 6828  CD1 ILE B 300    11334  12450  11769   -719   -150    700       C  
ATOM   6829  N   LEU B 301     -63.495  -3.371  43.430  1.00 79.91           N  
ANISOU 6829  N   LEU B 301     9642  11414   9307   -110    358    603       N  
ATOM   6830  CA  LEU B 301     -62.631  -3.067  44.575  1.00 80.00           C  
ANISOU 6830  CA  LEU B 301     9768  11447   9181      5    371    631       C  
ATOM   6831  C   LEU B 301     -63.324  -3.337  45.912  1.00 87.02           C  
ANISOU 6831  C   LEU B 301    10595  12603   9865   -122    467    851       C  
ATOM   6832  O   LEU B 301     -62.670  -3.815  46.837  1.00 88.02           O  
ANISOU 6832  O   LEU B 301    10866  12655   9922   -146    419    973       O  
ATOM   6833  CB  LEU B 301     -62.118  -1.611  44.495  1.00 78.01           C  
ANISOU 6833  CB  LEU B 301     9500  11273   8865    277    419    414       C  
ATOM   6834  CG  LEU B 301     -60.658  -1.308  44.901  1.00 81.39           C  
ANISOU 6834  CG  LEU B 301    10099  11529   9297    441    338    339       C  
ATOM   6835  CD1 LEU B 301     -60.480  -1.274  46.400  1.00 82.86           C  
ANISOU 6835  CD1 LEU B 301    10344  11845   9295    476    373    450       C  
ATOM   6836  CD2 LEU B 301     -59.654  -2.245  44.235  1.00 82.98           C  
ANISOU 6836  CD2 LEU B 301    10442  11407   9681    400    192    325       C  
ATOM   6837  N   TYR B 302     -64.640  -3.054  46.007  1.00 84.91           N  
ANISOU 6837  N   TYR B 302    10107  12667   9489   -202    599    903       N  
ATOM   6838  CA  TYR B 302     -65.434  -3.296  47.216  1.00 87.60           C  
ANISOU 6838  CA  TYR B 302    10331  13352   9600   -336    716   1125       C  
ATOM   6839  C   TYR B 302     -65.644  -4.785  47.481  1.00 95.68           C  
ANISOU 6839  C   TYR B 302    11419  14248  10688   -676    629   1430       C  
ATOM   6840  O   TYR B 302     -65.730  -5.179  48.646  1.00 98.10           O  
ANISOU 6840  O   TYR B 302    11742  14721  10811   -789    671   1653       O  
ATOM   6841  CB  TYR B 302     -66.795  -2.583  47.147  1.00 89.14           C  
ANISOU 6841  CB  TYR B 302    10236  13972   9662   -315    874   1074       C  
ATOM   6842  CG  TYR B 302     -66.781  -1.160  47.666  1.00 89.02           C  
ANISOU 6842  CG  TYR B 302    10151  14231   9444     10    965    863       C  
ATOM   6843  CD1 TYR B 302     -66.486  -0.884  48.998  1.00 92.01           C  
ANISOU 6843  CD1 TYR B 302    10563  14821   9575    123   1021    923       C  
ATOM   6844  CD2 TYR B 302     -67.116  -0.093  46.838  1.00 87.74           C  
ANISOU 6844  CD2 TYR B 302     9893  14117   9327    210    970    603       C  
ATOM   6845  CE1 TYR B 302     -66.476   0.424  49.482  1.00 91.51           C  
ANISOU 6845  CE1 TYR B 302    10449  14992   9329    449   1061    707       C  
ATOM   6846  CE2 TYR B 302     -67.118   1.219  47.313  1.00 87.99           C  
ANISOU 6846  CE2 TYR B 302     9882  14366   9182    518    999    400       C  
ATOM   6847  CZ  TYR B 302     -66.796   1.473  48.637  1.00 93.78           C  
ANISOU 6847  CZ  TYR B 302    10654  15295   9682    645   1037    444       C  
ATOM   6848  OH  TYR B 302     -66.791   2.761  49.117  1.00 90.56           O  
ANISOU 6848  OH  TYR B 302    10219  15084   9104    974   1024    224       O  
ATOM   6849  N   ALA B 303     -65.727  -5.605  46.409  1.00 92.64           N  
ANISOU 6849  N   ALA B 303    11080  13565  10555   -835    486   1442       N  
ATOM   6850  CA  ALA B 303     -65.940  -7.054  46.490  1.00 95.29           C  
ANISOU 6850  CA  ALA B 303    11501  13704  11001  -1165    333   1717       C  
ATOM   6851  C   ALA B 303     -64.833  -7.804  47.244  1.00101.01           C  
ANISOU 6851  C   ALA B 303    12503  14155  11722  -1190    179   1841       C  
ATOM   6852  O   ALA B 303     -63.648  -7.483  47.102  1.00 98.09           O  
ANISOU 6852  O   ALA B 303    12303  13563  11404   -949    109   1645       O  
ATOM   6853  CB  ALA B 303     -66.130  -7.640  45.100  1.00 95.26           C  
ANISOU 6853  CB  ALA B 303    11514  13403  11277  -1248    171   1631       C  
ATOM   6854  N   PHE B 304     -65.250  -8.806  48.053  1.00101.96           N  
ANISOU 6854  N   PHE B 304    12658  14305  11775  -1499    117   2180       N  
ATOM   6855  CA  PHE B 304     -64.424  -9.686  48.897  1.00144.91           C  
ANISOU 6855  CA  PHE B 304    18363  19503  17192  -1593    -54   2369       C  
ATOM   6856  C   PHE B 304     -63.487  -8.962  49.867  1.00173.36           C  
ANISOU 6856  C   PHE B 304    22071  23199  20598  -1326     35   2275       C  
ATOM   6857  O   PHE B 304     -63.452  -9.301  51.050  1.00134.96           O  
ANISOU 6857  O   PHE B 304    17277  18458  15543  -1438     49   2513       O  
ATOM   6858  CB  PHE B 304     -63.681 -10.757  48.074  1.00146.35           C  
ANISOU 6858  CB  PHE B 304    18797  19141  17667  -1638   -380   2321       C  
ATOM   6859  CG  PHE B 304     -64.506 -11.983  47.753  1.00150.78           C  
ANISOU 6859  CG  PHE B 304    19365  19543  18381  -2016   -576   2583       C  
ATOM   6860  CD1 PHE B 304     -64.561 -13.055  48.637  1.00157.26           C  
ANISOU 6860  CD1 PHE B 304    20341  20250  19159  -2318   -746   2937       C  
ATOM   6861  CD2 PHE B 304     -65.208 -12.076  46.556  1.00152.36           C  
ANISOU 6861  CD2 PHE B 304    19431  19685  18774  -2075   -619   2482       C  
ATOM   6862  CE1 PHE B 304     -65.318 -14.194  48.337  1.00161.38           C  
ANISOU 6862  CE1 PHE B 304    20881  20594  19842  -2694   -969   3201       C  
ATOM   6863  CE2 PHE B 304     -65.965 -13.215  46.257  1.00158.33           C  
ANISOU 6863  CE2 PHE B 304    20199  20269  19691  -2430   -835   2725       C  
ATOM   6864  CZ  PHE B 304     -66.014 -14.266  47.149  1.00160.08           C  
ANISOU 6864  CZ  PHE B 304    20574  20367  19881  -2747  -1017   3088       C  
TER    6865      PHE B 304                                                      
ATOM   6866  N   PRO C  27     -59.928  39.145   5.448  1.00149.42           N  
ANISOU 6866  N   PRO C  27    19830  24587  12354  -2181  -1483  -1206       N  
ATOM   6867  CA  PRO C  27     -58.600  39.303   4.842  1.00149.21           C  
ANISOU 6867  CA  PRO C  27    19985  24578  12128  -2160  -1297  -1123       C  
ATOM   6868  C   PRO C  27     -58.056  40.726   5.010  1.00151.65           C  
ANISOU 6868  C   PRO C  27    20342  24821  12457  -2026  -1266   -739       C  
ATOM   6869  O   PRO C  27     -58.197  41.565   4.115  1.00152.98           O  
ANISOU 6869  O   PRO C  27    20570  25198  12356  -1963  -1383   -534       O  
ATOM   6870  CB  PRO C  27     -58.830  38.902   3.381  1.00154.57           C  
ANISOU 6870  CB  PRO C  27    20742  25598  12389  -2220  -1403  -1265       C  
ATOM   6871  CG  PRO C  27     -59.974  37.938   3.432  1.00160.23           C  
ANISOU 6871  CG  PRO C  27    21332  26382  13165  -2331  -1559  -1567       C  
ATOM   6872  CD  PRO C  27     -60.784  38.226   4.674  1.00153.71           C  
ANISOU 6872  CD  PRO C  27    20326  25362  12716  -2300  -1635  -1495       C  
ATOM   6873  N   CYS C  28     -57.439  40.997   6.181  1.00145.25           N  
ANISOU 6873  N   CYS C  28    19513  23710  11967  -1986  -1112   -641       N  
ATOM   6874  CA  CYS C  28     -56.868  42.307   6.512  1.00143.70           C  
ANISOU 6874  CA  CYS C  28    19358  23395  11847  -1879  -1065   -302       C  
ATOM   6875  C   CYS C  28     -55.450  42.479   5.984  1.00148.29           C  
ANISOU 6875  C   CYS C  28    20084  23984  12276  -1893   -851   -215       C  
ATOM   6876  O   CYS C  28     -54.546  41.739   6.381  1.00146.31           O  
ANISOU 6876  O   CYS C  28    19856  23597  12139  -1943   -649   -370       O  
ATOM   6877  CB  CYS C  28     -56.956  42.596   8.011  1.00140.51           C  
ANISOU 6877  CB  CYS C  28    18858  22687  11843  -1831  -1025   -243       C  
ATOM   6878  SG  CYS C  28     -56.856  44.357   8.432  1.00143.36           S  
ANISOU 6878  SG  CYS C  28    19232  22921  12318  -1688  -1075    159       S  
ATOM   6879  N   PHE C  29     -55.267  43.468   5.088  1.00147.40           N  
ANISOU 6879  N   PHE C  29    20067  24032  11907  -1845   -895     43       N  
ATOM   6880  CA  PHE C  29     -53.991  43.808   4.453  1.00148.43           C  
ANISOU 6880  CA  PHE C  29    20331  24209  11856  -1867   -694    171       C  
ATOM   6881  C   PHE C  29     -52.968  44.371   5.451  1.00149.55           C  
ANISOU 6881  C   PHE C  29    20462  24062  12297  -1846   -509    319       C  
ATOM   6882  O   PHE C  29     -53.270  45.295   6.204  1.00147.75           O  
ANISOU 6882  O   PHE C  29    20191  23661  12286  -1775   -588    523       O  
ATOM   6883  CB  PHE C  29     -54.216  44.792   3.293  1.00153.52           C  
ANISOU 6883  CB  PHE C  29    21088  25089  12154  -1824   -808    441       C  
ATOM   6884  CG  PHE C  29     -54.875  44.198   2.071  1.00158.40           C  
ANISOU 6884  CG  PHE C  29    21754  26045  12386  -1861   -949    288       C  
ATOM   6885  CD1 PHE C  29     -54.111  43.672   1.036  1.00163.76           C  
ANISOU 6885  CD1 PHE C  29    22557  26928  12735  -1936   -796    178       C  
ATOM   6886  CD2 PHE C  29     -56.259  44.190   1.941  1.00161.79           C  
ANISOU 6886  CD2 PHE C  29    22096  26601  12775  -1818  -1236    248       C  
ATOM   6887  CE1 PHE C  29     -54.722  43.128  -0.100  1.00167.88           C  
ANISOU 6887  CE1 PHE C  29    23135  27773  12879  -1973   -934     20       C  
ATOM   6888  CE2 PHE C  29     -56.868  43.644   0.806  1.00167.75           C  
ANISOU 6888  CE2 PHE C  29    22890  27684  13165  -1858  -1386     93       C  
ATOM   6889  CZ  PHE C  29     -56.096  43.118  -0.206  1.00167.94           C  
ANISOU 6889  CZ  PHE C  29    23056  27903  12850  -1937  -1238    -21       C  
ATOM   6890  N   PHE C  36     -48.145  57.544  16.550  1.00 80.48           N  
ANISOU 6890  N   PHE C  36    11809  11963   6805  -1573   -233   2371       N  
ATOM   6891  CA  PHE C  36     -48.501  57.965  17.906  1.00 79.08           C  
ANISOU 6891  CA  PHE C  36    11605  11542   6900  -1496   -308   2283       C  
ATOM   6892  C   PHE C  36     -47.988  57.003  18.978  1.00 80.59           C  
ANISOU 6892  C   PHE C  36    11678  11723   7218  -1535   -248   2016       C  
ATOM   6893  O   PHE C  36     -47.488  57.461  20.001  1.00 79.67           O  
ANISOU 6893  O   PHE C  36    11553  11400   7317  -1562   -232   1969       O  
ATOM   6894  CB  PHE C  36     -50.014  58.208  18.055  1.00 81.07           C  
ANISOU 6894  CB  PHE C  36    11864  11778   7160  -1311   -483   2297       C  
ATOM   6895  CG  PHE C  36     -50.400  58.923  19.329  1.00 81.83           C  
ANISOU 6895  CG  PHE C  36    11962  11605   7525  -1222   -548   2250       C  
ATOM   6896  CD1 PHE C  36     -50.344  60.310  19.413  1.00 86.85           C  
ANISOU 6896  CD1 PHE C  36    12711  11992   8295  -1194   -580   2443       C  
ATOM   6897  CD2 PHE C  36     -50.819  58.211  20.447  1.00 81.84           C  
ANISOU 6897  CD2 PHE C  36    11862  11593   7640  -1168   -570   2010       C  
ATOM   6898  CE1 PHE C  36     -50.690  60.969  20.597  1.00 87.33           C  
ANISOU 6898  CE1 PHE C  36    12780  11800   8599  -1108   -634   2375       C  
ATOM   6899  CE2 PHE C  36     -51.166  58.872  21.630  1.00 84.24           C  
ANISOU 6899  CE2 PHE C  36    12176  11663   8170  -1085   -617   1954       C  
ATOM   6900  CZ  PHE C  36     -51.095  60.245  21.697  1.00 84.10           C  
ANISOU 6900  CZ  PHE C  36    12266  11404   8283  -1053   -650   2126       C  
ATOM   6901  N   ASN C  37     -48.112  55.683  18.756  1.00 75.73           N  
ANISOU 6901  N   ASN C  37    10983  11322   6468  -1536   -222   1842       N  
ATOM   6902  CA  ASN C  37     -47.605  54.674  19.690  1.00 73.47           C  
ANISOU 6902  CA  ASN C  37    10602  11031   6283  -1563   -165   1604       C  
ATOM   6903  C   ASN C  37     -46.075  54.654  19.700  1.00 78.23           C  
ANISOU 6903  C   ASN C  37    11172  11614   6938  -1698    -22   1598       C  
ATOM   6904  O   ASN C  37     -45.477  54.253  20.690  1.00 76.52           O  
ANISOU 6904  O   ASN C  37    10888  11315   6869  -1716      6   1449       O  
ATOM   6905  CB  ASN C  37     -48.155  53.294  19.345  1.00 73.57           C  
ANISOU 6905  CB  ASN C  37    10558  11257   6140  -1533   -171   1434       C  
ATOM   6906  CG  ASN C  37     -49.526  53.019  19.899  1.00 93.40           C  
ANISOU 6906  CG  ASN C  37    13043  13758   8687  -1417   -295   1342       C  
ATOM   6907  OD1 ASN C  37     -50.389  53.903  19.986  1.00 90.94           O  
ANISOU 6907  OD1 ASN C  37    12764  13366   8424  -1329   -400   1454       O  
ATOM   6908  ND2 ASN C  37     -49.771  51.765  20.235  1.00 81.53           N  
ANISOU 6908  ND2 ASN C  37    11476  12340   7161  -1414   -280   1137       N  
ATOM   6909  N   LYS C  38     -45.445  55.125  18.614  1.00 78.00           N  
ANISOU 6909  N   LYS C  38    11186  11664   6788  -1792     66   1766       N  
ATOM   6910  CA  LYS C  38     -43.989  55.216  18.476  1.00 79.17           C  
ANISOU 6910  CA  LYS C  38    11283  11815   6983  -1935    219   1781       C  
ATOM   6911  C   LYS C  38     -43.419  56.333  19.360  1.00 85.39           C  
ANISOU 6911  C   LYS C  38    12081  12342   8021  -1994    209   1851       C  
ATOM   6912  O   LYS C  38     -42.213  56.368  19.579  1.00 85.77           O  
ANISOU 6912  O   LYS C  38    12051  12368   8170  -2111    313   1816       O  
ATOM   6913  CB  LYS C  38     -43.581  55.403  17.000  1.00 83.62           C  
ANISOU 6913  CB  LYS C  38    11897  12557   7319  -2025    332   1950       C  
ATOM   6914  CG  LYS C  38     -43.950  54.218  16.123  1.00 92.86           C  
ANISOU 6914  CG  LYS C  38    13050  13999   8233  -1987    358   1841       C  
ATOM   6915  CD  LYS C  38     -42.996  54.027  14.963  1.00104.43           C  
ANISOU 6915  CD  LYS C  38    14509  15662   9508  -2105    538   1901       C  
ATOM   6916  CE  LYS C  38     -43.050  52.605  14.454  1.00117.35           C  
ANISOU 6916  CE  LYS C  38    16092  17535  10962  -2072    588   1691       C  
ATOM   6917  NZ  LYS C  38     -42.247  51.668  15.290  1.00123.71           N  
ANISOU 6917  NZ  LYS C  38    16761  18313  11932  -2073    660   1453       N  
ATOM   6918  N   ILE C  39     -44.288  57.228  19.875  1.00 83.22           N  
ANISOU 6918  N   ILE C  39    11894  11874   7854  -1911     82   1933       N  
ATOM   6919  CA  ILE C  39     -43.931  58.337  20.768  1.00 84.35           C  
ANISOU 6919  CA  ILE C  39    12070  11740   8237  -1951     52   1978       C  
ATOM   6920  C   ILE C  39     -44.604  58.203  22.147  1.00 88.63           C  
ANISOU 6920  C   ILE C  39    12595  12143   8936  -1830    -67   1805       C  
ATOM   6921  O   ILE C  39     -43.957  58.457  23.164  1.00 87.50           O  
ANISOU 6921  O   ILE C  39    12417  11850   8977  -1879    -69   1708       O  
ATOM   6922  CB  ILE C  39     -44.134  59.737  20.097  1.00 90.14           C  
ANISOU 6922  CB  ILE C  39    12947  12325   8977  -1983     39   2256       C  
ATOM   6923  CG1 ILE C  39     -43.883  60.912  21.072  1.00 91.41           C  
ANISOU 6923  CG1 ILE C  39    13161  12165   9406  -2017     -4   2282       C  
ATOM   6924  CG2 ILE C  39     -45.486  59.879  19.402  1.00 91.15           C  
ANISOU 6924  CG2 ILE C  39    13170  12517   8946  -1832    -69   2379       C  
ATOM   6925  CD1 ILE C  39     -42.472  61.362  21.188  1.00 99.45           C  
ANISOU 6925  CD1 ILE C  39    14133  13097  10556  -2221    113   2304       C  
ATOM   6926  N   PHE C  40     -45.883  57.779  22.173  1.00 86.32           N  
ANISOU 6926  N   PHE C  40    12321  11917   8560  -1681   -162   1759       N  
ATOM   6927  CA  PHE C  40     -46.659  57.607  23.398  1.00 85.50           C  
ANISOU 6927  CA  PHE C  40    12203  11709   8574  -1563   -255   1602       C  
ATOM   6928  C   PHE C  40     -46.234  56.397  24.216  1.00 87.96           C  
ANISOU 6928  C   PHE C  40    12418  12099   8904  -1573   -223   1373       C  
ATOM   6929  O   PHE C  40     -46.193  56.513  25.439  1.00 86.92           O  
ANISOU 6929  O   PHE C  40    12282  11826   8917  -1544   -263   1256       O  
ATOM   6930  CB  PHE C  40     -48.163  57.562  23.100  1.00 88.05           C  
ANISOU 6930  CB  PHE C  40    12552  12094   8809  -1411   -355   1632       C  
ATOM   6931  CG  PHE C  40     -49.076  57.685  24.299  1.00 89.58           C  
ANISOU 6931  CG  PHE C  40    12740  12161   9136  -1285   -439   1508       C  
ATOM   6932  CD1 PHE C  40     -49.406  58.931  24.818  1.00 94.78           C  
ANISOU 6932  CD1 PHE C  40    13476  12585   9953  -1221   -499   1581       C  
ATOM   6933  CD2 PHE C  40     -49.661  56.558  24.866  1.00 90.47           C  
ANISOU 6933  CD2 PHE C  40    12777  12387   9210  -1229   -449   1320       C  
ATOM   6934  CE1 PHE C  40     -50.270  59.045  25.917  1.00 95.35           C  
ANISOU 6934  CE1 PHE C  40    13538  12553  10137  -1096   -560   1453       C  
ATOM   6935  CE2 PHE C  40     -50.540  56.676  25.951  1.00 92.86           C  
ANISOU 6935  CE2 PHE C  40    13074  12590   9621  -1119   -506   1211       C  
ATOM   6936  CZ  PHE C  40     -50.821  57.914  26.483  1.00 92.27           C  
ANISOU 6936  CZ  PHE C  40    13065  12298   9695  -1050   -557   1271       C  
ATOM   6937  N   LEU C  41     -45.964  55.231  23.572  1.00 84.26           N  
ANISOU 6937  N   LEU C  41    11885  11847   8283  -1603   -157   1305       N  
ATOM   6938  CA  LEU C  41     -45.537  54.017  24.291  1.00 82.56           C  
ANISOU 6938  CA  LEU C  41    11593  11692   8085  -1600   -126   1101       C  
ATOM   6939  C   LEU C  41     -44.198  54.213  25.012  1.00 86.39           C  
ANISOU 6939  C   LEU C  41    12026  12080   8717  -1685    -85   1047       C  
ATOM   6940  O   LEU C  41     -44.171  53.968  26.221  1.00 85.08           O  
ANISOU 6940  O   LEU C  41    11849  11820   8656  -1642   -134    916       O  
ATOM   6941  CB  LEU C  41     -45.523  52.745  23.427  1.00 82.56           C  
ANISOU 6941  CB  LEU C  41    11545  11918   7904  -1608    -62   1029       C  
ATOM   6942  CG  LEU C  41     -46.853  52.243  22.849  1.00 87.80           C  
ANISOU 6942  CG  LEU C  41    12232  12707   8420  -1532   -116   1018       C  
ATOM   6943  CD1 LEU C  41     -46.617  51.051  21.936  1.00 88.43           C  
ANISOU 6943  CD1 LEU C  41    12275  12997   8327  -1566    -41    935       C  
ATOM   6944  CD2 LEU C  41     -47.841  51.870  23.944  1.00 89.19           C  
ANISOU 6944  CD2 LEU C  41    12406  12807   8676  -1439   -194    893       C  
ATOM   6945  N   PRO C  42     -43.111  54.735  24.366  1.00 83.78           N  
ANISOU 6945  N   PRO C  42    11664  11763   8403  -1808     -1   1150       N  
ATOM   6946  CA  PRO C  42     -41.864  54.976  25.120  1.00 83.46           C  
ANISOU 6946  CA  PRO C  42    11549  11634   8526  -1895     21   1086       C  
ATOM   6947  C   PRO C  42     -42.000  55.990  26.262  1.00 86.33           C  
ANISOU 6947  C   PRO C  42    11969  11760   9072  -1888    -76   1075       C  
ATOM   6948  O   PRO C  42     -41.151  55.991  27.147  1.00 86.11           O  
ANISOU 6948  O   PRO C  42    11879  11668   9172  -1931    -96    969       O  
ATOM   6949  CB  PRO C  42     -40.877  55.450  24.046  1.00 87.23           C  
ANISOU 6949  CB  PRO C  42    11984  12184   8977  -2040    142   1222       C  
ATOM   6950  CG  PRO C  42     -41.724  55.968  22.953  1.00 92.81           C  
ANISOU 6950  CG  PRO C  42    12798  12924   9540  -2027    150   1406       C  
ATOM   6951  CD  PRO C  42     -42.935  55.094  22.942  1.00 86.91           C  
ANISOU 6951  CD  PRO C  42    12085  12273   8665  -1883     81   1323       C  
ATOM   6952  N   THR C  43     -43.062  56.827  26.262  1.00 82.09           N  
ANISOU 6952  N   THR C  43    11545  11098   8546  -1823   -143   1170       N  
ATOM   6953  CA  THR C  43     -43.325  57.780  27.347  1.00 81.38           C  
ANISOU 6953  CA  THR C  43    11525  10775   8622  -1794   -232   1139       C  
ATOM   6954  C   THR C  43     -43.802  56.995  28.562  1.00 83.23           C  
ANISOU 6954  C   THR C  43    11747  11011   8864  -1684   -297    944       C  
ATOM   6955  O   THR C  43     -43.338  57.265  29.664  1.00 83.29           O  
ANISOU 6955  O   THR C  43    11754  10898   8992  -1700   -345    836       O  
ATOM   6956  CB  THR C  43     -44.355  58.849  26.944  1.00 86.29           C  
ANISOU 6956  CB  THR C  43    12267  11265   9255  -1730   -278   1294       C  
ATOM   6957  OG1 THR C  43     -44.021  59.383  25.665  1.00 88.46           O  
ANISOU 6957  OG1 THR C  43    12569  11573   9467  -1821   -211   1500       O  
ATOM   6958  CG2 THR C  43     -44.456  59.976  27.962  1.00 82.73           C  
ANISOU 6958  CG2 THR C  43    11895  10546   8993  -1716   -350   1264       C  
ATOM   6959  N   ILE C  44     -44.707  56.016  28.354  1.00 77.87           N  
ANISOU 6959  N   ILE C  44    11063  10473   8051  -1583   -297    898       N  
ATOM   6960  CA  ILE C  44     -45.241  55.143  29.402  1.00 75.83           C  
ANISOU 6960  CA  ILE C  44    10803  10232   7777  -1488   -335    731       C  
ATOM   6961  C   ILE C  44     -44.130  54.193  29.859  1.00 79.60           C  
ANISOU 6961  C   ILE C  44    11204  10783   8258  -1532   -308    612       C  
ATOM   6962  O   ILE C  44     -44.003  53.930  31.058  1.00 79.20           O  
ANISOU 6962  O   ILE C  44    11166  10668   8257  -1494   -357    488       O  
ATOM   6963  CB  ILE C  44     -46.516  54.400  28.927  1.00 78.07           C  
ANISOU 6963  CB  ILE C  44    11093  10644   7928  -1395   -332    727       C  
ATOM   6964  CG1 ILE C  44     -47.640  55.394  28.573  1.00 79.45           C  
ANISOU 6964  CG1 ILE C  44    11324  10746   8116  -1324   -381    840       C  
ATOM   6965  CG2 ILE C  44     -47.000  53.376  29.968  1.00 77.28           C  
ANISOU 6965  CG2 ILE C  44    10991  10567   7806  -1324   -345    562       C  
ATOM   6966  CD1 ILE C  44     -48.809  54.763  27.911  1.00 88.42           C  
ANISOU 6966  CD1 ILE C  44    12437  12034   9123  -1251   -390    849       C  
ATOM   6967  N   TYR C  45     -43.297  53.726  28.913  1.00 76.25           N  
ANISOU 6967  N   TYR C  45    10702  10491   7778  -1607   -232    652       N  
ATOM   6968  CA  TYR C  45     -42.165  52.862  29.227  1.00 75.91           C  
ANISOU 6968  CA  TYR C  45    10566  10523   7754  -1634   -204    546       C  
ATOM   6969  C   TYR C  45     -41.165  53.577  30.133  1.00 80.99           C  
ANISOU 6969  C   TYR C  45    11173  11044   8554  -1698   -258    504       C  
ATOM   6970  O   TYR C  45     -40.710  52.980  31.104  1.00 80.49           O  
ANISOU 6970  O   TYR C  45    11080  10978   8524  -1657   -308    378       O  
ATOM   6971  CB  TYR C  45     -41.505  52.308  27.954  1.00 77.82           C  
ANISOU 6971  CB  TYR C  45    10724  10937   7908  -1695    -95    592       C  
ATOM   6972  CG  TYR C  45     -42.376  51.323  27.201  1.00 79.21           C  
ANISOU 6972  CG  TYR C  45    10927  11249   7919  -1631    -56    576       C  
ATOM   6973  CD1 TYR C  45     -43.186  50.415  27.880  1.00 79.74           C  
ANISOU 6973  CD1 TYR C  45    11038  11311   7948  -1533    -98    464       C  
ATOM   6974  CD2 TYR C  45     -42.366  51.275  25.810  1.00 81.06           C  
ANISOU 6974  CD2 TYR C  45    11148  11623   8030  -1679     29    667       C  
ATOM   6975  CE1 TYR C  45     -43.969  49.490  27.196  1.00 79.83           C  
ANISOU 6975  CE1 TYR C  45    11067  11441   7823  -1496    -64    433       C  
ATOM   6976  CE2 TYR C  45     -43.158  50.362  25.113  1.00 81.67           C  
ANISOU 6976  CE2 TYR C  45    11249  11832   7949  -1630     52    631       C  
ATOM   6977  CZ  TYR C  45     -43.956  49.468  25.812  1.00 88.73           C  
ANISOU 6977  CZ  TYR C  45    12175  12708   8829  -1543      3    508       C  
ATOM   6978  OH  TYR C  45     -44.748  48.562  25.148  1.00 91.65           O  
ANISOU 6978  OH  TYR C  45    12563  13198   9060  -1515     23    457       O  
ATOM   6979  N   SER C  46     -40.904  54.873  29.873  1.00 78.74           N  
ANISOU 6979  N   SER C  46    10906  10648   8364  -1794   -258    609       N  
ATOM   6980  CA  SER C  46     -40.005  55.709  30.671  1.00 79.54           C  
ANISOU 6980  CA  SER C  46    10976  10617   8628  -1881   -314    566       C  
ATOM   6981  C   SER C  46     -40.566  55.984  32.074  1.00 82.43           C  
ANISOU 6981  C   SER C  46    11436  10838   9047  -1799   -430    452       C  
ATOM   6982  O   SER C  46     -39.825  55.840  33.047  1.00 82.67           O  
ANISOU 6982  O   SER C  46    11422  10847   9143  -1812   -499    329       O  
ATOM   6983  CB  SER C  46     -39.696  57.016  29.952  1.00 85.24           C  
ANISOU 6983  CB  SER C  46    11716  11235   9438  -2016   -272    719       C  
ATOM   6984  OG  SER C  46     -39.106  56.768  28.686  1.00 95.14           O  
ANISOU 6984  OG  SER C  46    12886  12638  10626  -2103   -150    824       O  
ATOM   6985  N   ILE C  47     -41.870  56.353  32.179  1.00 77.61           N  
ANISOU 6985  N   ILE C  47    10947  10144   8398  -1708   -451    486       N  
ATOM   6986  CA  ILE C  47     -42.558  56.624  33.448  1.00 76.74           C  
ANISOU 6986  CA  ILE C  47    10932   9908   8316  -1618   -534    376       C  
ATOM   6987  C   ILE C  47     -42.511  55.369  34.333  1.00 79.55           C  
ANISOU 6987  C   ILE C  47    11272  10366   8589  -1538   -562    235       C  
ATOM   6988  O   ILE C  47     -42.118  55.460  35.498  1.00 79.92           O  
ANISOU 6988  O   ILE C  47    11342  10348   8676  -1529   -640    117       O  
ATOM   6989  CB  ILE C  47     -44.011  57.164  33.231  1.00 79.66           C  
ANISOU 6989  CB  ILE C  47    11405  10202   8660  -1520   -531    443       C  
ATOM   6990  CG1 ILE C  47     -44.003  58.577  32.600  1.00 81.58           C  
ANISOU 6990  CG1 ILE C  47    11699  10287   9013  -1584   -529    582       C  
ATOM   6991  CG2 ILE C  47     -44.815  57.162  34.552  1.00 80.14           C  
ANISOU 6991  CG2 ILE C  47    11549  10182   8718  -1408   -587    305       C  
ATOM   6992  CD1 ILE C  47     -45.352  59.057  32.006  1.00 88.69           C  
ANISOU 6992  CD1 ILE C  47    12673  11147   9879  -1477   -525    694       C  
ATOM   6993  N   ILE C  48     -42.864  54.203  33.760  1.00 74.21           N  
ANISOU 6993  N   ILE C  48    10563   9841   7791  -1486   -502    249       N  
ATOM   6994  CA  ILE C  48     -42.853  52.920  34.468  1.00 72.40           C  
ANISOU 6994  CA  ILE C  48    10335   9694   7480  -1410   -515    139       C  
ATOM   6995  C   ILE C  48     -41.428  52.431  34.804  1.00 75.11           C  
ANISOU 6995  C   ILE C  48    10583  10089   7865  -1448   -549     74       C  
ATOM   6996  O   ILE C  48     -41.252  51.772  35.830  1.00 74.11           O  
ANISOU 6996  O   ILE C  48    10487   9965   7708  -1383   -608    -24       O  
ATOM   6997  CB  ILE C  48     -43.810  51.881  33.804  1.00 74.47           C  
ANISOU 6997  CB  ILE C  48    10608  10071   7616  -1348   -443    162       C  
ATOM   6998  CG1 ILE C  48     -45.269  52.102  34.266  1.00 74.64           C  
ANISOU 6998  CG1 ILE C  48    10723  10037   7601  -1270   -449    149       C  
ATOM   6999  CG2 ILE C  48     -43.406  50.426  34.070  1.00 74.22           C  
ANISOU 6999  CG2 ILE C  48    10554  10132   7516  -1305   -426     82       C  
ATOM   7000  CD1 ILE C  48     -46.090  53.135  33.524  1.00 81.18           C  
ANISOU 7000  CD1 ILE C  48    11566  10822   8457  -1270   -440    253       C  
ATOM   7001  N   PHE C  49     -40.415  52.818  33.990  1.00 71.42           N  
ANISOU 7001  N   PHE C  49    10003   9663   7472  -1553   -515    132       N  
ATOM   7002  CA  PHE C  49     -39.016  52.467  34.243  1.00 71.40           C  
ANISOU 7002  CA  PHE C  49     9872   9723   7535  -1592   -547     68       C  
ATOM   7003  C   PHE C  49     -38.478  53.225  35.460  1.00 76.09           C  
ANISOU 7003  C   PHE C  49    10477  10205   8230  -1624   -673    -20       C  
ATOM   7004  O   PHE C  49     -37.956  52.593  36.378  1.00 75.96           O  
ANISOU 7004  O   PHE C  49    10439  10221   8200  -1563   -759   -122       O  
ATOM   7005  CB  PHE C  49     -38.127  52.716  33.007  1.00 74.01           C  
ANISOU 7005  CB  PHE C  49    10063  10140   7917  -1708   -453    151       C  
ATOM   7006  CG  PHE C  49     -36.635  52.727  33.267  1.00 76.60           C  
ANISOU 7006  CG  PHE C  49    10224  10519   8360  -1778   -487     87       C  
ATOM   7007  CD1 PHE C  49     -35.923  53.921  33.289  1.00 80.83           C  
ANISOU 7007  CD1 PHE C  49    10695  10979   9039  -1926   -508    112       C  
ATOM   7008  CD2 PHE C  49     -35.941  51.543  33.495  1.00 78.39           C  
ANISOU 7008  CD2 PHE C  49    10353  10867   8566  -1694   -501     -1       C  
ATOM   7009  CE1 PHE C  49     -34.543  53.929  33.531  1.00 82.89           C  
ANISOU 7009  CE1 PHE C  49    10772  11304   9419  -2002   -543     41       C  
ATOM   7010  CE2 PHE C  49     -34.561  51.553  33.731  1.00 82.27           C  
ANISOU 7010  CE2 PHE C  49    10661  11423   9174  -1745   -543    -66       C  
ATOM   7011  CZ  PHE C  49     -33.873  52.745  33.745  1.00 81.66           C  
ANISOU 7011  CZ  PHE C  49    10499  11290   9238  -1904   -564    -48       C  
ATOM   7012  N   LEU C  50     -38.599  54.568  35.464  1.00 73.25           N  
ANISOU 7012  N   LEU C  50    10158   9709   7965  -1716   -691     19       N  
ATOM   7013  CA  LEU C  50     -38.097  55.417  36.552  1.00 74.25           C  
ANISOU 7013  CA  LEU C  50    10302   9715   8196  -1768   -811    -79       C  
ATOM   7014  C   LEU C  50     -38.754  55.091  37.891  1.00 77.52           C  
ANISOU 7014  C   LEU C  50    10849  10084   8522  -1644   -903   -196       C  
ATOM   7015  O   LEU C  50     -38.055  54.952  38.891  1.00 77.33           O  
ANISOU 7015  O   LEU C  50    10803  10069   8510  -1636  -1018   -312       O  
ATOM   7016  CB  LEU C  50     -38.239  56.924  36.229  1.00 75.53           C  
ANISOU 7016  CB  LEU C  50    10513   9704   8481  -1887   -798    -11       C  
ATOM   7017  CG  LEU C  50     -37.597  57.452  34.934  1.00 81.23           C  
ANISOU 7017  CG  LEU C  50    11130  10444   9289  -2037   -696    127       C  
ATOM   7018  CD1 LEU C  50     -38.133  58.825  34.586  1.00 82.08           C  
ANISOU 7018  CD1 LEU C  50    11350  10352   9485  -2109   -674    228       C  
ATOM   7019  CD2 LEU C  50     -36.072  57.469  35.019  1.00 85.78           C  
ANISOU 7019  CD2 LEU C  50    11521  11090   9982  -2168   -724     68       C  
ATOM   7020  N   THR C  51     -40.084  54.930  37.896  1.00 73.70           N  
ANISOU 7020  N   THR C  51    10493   9568   7942  -1547   -852   -165       N  
ATOM   7021  CA  THR C  51     -40.853  54.612  39.101  1.00 73.46           C  
ANISOU 7021  CA  THR C  51    10597   9504   7812  -1434   -903   -263       C  
ATOM   7022  C   THR C  51     -40.562  53.180  39.585  1.00 77.39           C  
ANISOU 7022  C   THR C  51    11081  10129   8194  -1347   -925   -311       C  
ATOM   7023  O   THR C  51     -40.459  52.949  40.792  1.00 76.83           O  
ANISOU 7023  O   THR C  51    11085  10046   8061  -1289  -1015   -410       O  
ATOM   7024  CB  THR C  51     -42.350  54.892  38.863  1.00 80.96           C  
ANISOU 7024  CB  THR C  51    11653  10395   8713  -1366   -825   -213       C  
ATOM   7025  OG1 THR C  51     -42.508  56.175  38.252  1.00 81.01           O  
ANISOU 7025  OG1 THR C  51    11665  10277   8837  -1435   -808   -142       O  
ATOM   7026  CG2 THR C  51     -43.172  54.834  40.139  1.00 79.11           C  
ANISOU 7026  CG2 THR C  51    11554  10111   8393  -1268   -857   -321       C  
ATOM   7027  N   GLY C  52     -40.404  52.258  38.633  1.00 74.22           N  
ANISOU 7027  N   GLY C  52    10595   9841   7762  -1336   -846   -240       N  
ATOM   7028  CA  GLY C  52     -40.114  50.851  38.889  1.00 73.55           C  
ANISOU 7028  CA  GLY C  52    10500   9857   7589  -1249   -852   -270       C  
ATOM   7029  C   GLY C  52     -38.746  50.610  39.495  1.00 78.46           C  
ANISOU 7029  C   GLY C  52    11029  10524   8258  -1247   -968   -341       C  
ATOM   7030  O   GLY C  52     -38.655  50.077  40.607  1.00 78.55           O  
ANISOU 7030  O   GLY C  52    11118  10535   8191  -1162  -1058   -409       O  
ATOM   7031  N   ILE C  53     -37.676  51.018  38.775  1.00 75.12           N  
ANISOU 7031  N   ILE C  53    10436  10148   7958  -1343   -966   -322       N  
ATOM   7032  CA  ILE C  53     -36.282  50.853  39.194  1.00 75.94           C  
ANISOU 7032  CA  ILE C  53    10396  10319   8138  -1353  -1075   -392       C  
ATOM   7033  C   ILE C  53     -35.998  51.431  40.600  1.00 79.32           C  
ANISOU 7033  C   ILE C  53    10887  10683   8570  -1351  -1245   -500       C  
ATOM   7034  O   ILE C  53     -35.446  50.724  41.445  1.00 78.89           O  
ANISOU 7034  O   ILE C  53    10826  10686   8464  -1258  -1362   -566       O  
ATOM   7035  CB  ILE C  53     -35.287  51.318  38.072  1.00 80.24           C  
ANISOU 7035  CB  ILE C  53    10732  10930   8826  -1484  -1009   -349       C  
ATOM   7036  CG1 ILE C  53     -33.936  50.550  38.079  1.00 81.90           C  
ANISOU 7036  CG1 ILE C  53    10746  11277   9097  -1447  -1061   -404       C  
ATOM   7037  CG2 ILE C  53     -35.143  52.853  37.920  1.00 82.16           C  
ANISOU 7037  CG2 ILE C  53    10954  11068   9194  -1651  -1016   -331       C  
ATOM   7038  CD1 ILE C  53     -32.861  50.926  39.171  1.00 91.94           C  
ANISOU 7038  CD1 ILE C  53    11916  12561  10454  -1467  -1251   -518       C  
ATOM   7039  N   VAL C  54     -36.429  52.686  40.847  1.00 75.60           N  
ANISOU 7039  N   VAL C  54    10490  10087   8146  -1441  -1261   -519       N  
ATOM   7040  CA  VAL C  54     -36.245  53.425  42.101  1.00 76.14           C  
ANISOU 7040  CA  VAL C  54    10633  10079   8219  -1460  -1412   -641       C  
ATOM   7041  C   VAL C  54     -37.022  52.765  43.250  1.00 78.47           C  
ANISOU 7041  C   VAL C  54    11120  10369   8328  -1315  -1461   -693       C  
ATOM   7042  O   VAL C  54     -36.434  52.481  44.299  1.00 78.53           O  
ANISOU 7042  O   VAL C  54    11145  10420   8274  -1263  -1610   -784       O  
ATOM   7043  CB  VAL C  54     -36.591  54.933  41.909  1.00 80.54           C  
ANISOU 7043  CB  VAL C  54    11235  10477   8890  -1591  -1387   -644       C  
ATOM   7044  CG1 VAL C  54     -36.698  55.677  43.242  1.00 81.47           C  
ANISOU 7044  CG1 VAL C  54    11479  10493   8982  -1593  -1522   -789       C  
ATOM   7045  CG2 VAL C  54     -35.584  55.614  40.982  1.00 81.45           C  
ANISOU 7045  CG2 VAL C  54    11161  10594   9190  -1760  -1360   -600       C  
ATOM   7046  N   GLY C  55     -38.317  52.519  43.015  1.00 73.34           N  
ANISOU 7046  N   GLY C  55    10602   9677   7586  -1255  -1335   -629       N  
ATOM   7047  CA  GLY C  55     -39.237  51.893  43.959  1.00 72.44           C  
ANISOU 7047  CA  GLY C  55    10672   9558   7295  -1135  -1330   -657       C  
ATOM   7048  C   GLY C  55     -38.793  50.519  44.415  1.00 76.67           C  
ANISOU 7048  C   GLY C  55    11219  10193   7719  -1026  -1381   -650       C  
ATOM   7049  O   GLY C  55     -38.592  50.308  45.613  1.00 77.32           O  
ANISOU 7049  O   GLY C  55    11401  10287   7691   -961  -1499   -722       O  
ATOM   7050  N   ASN C  56     -38.588  49.589  43.459  1.00 72.62           N  
ANISOU 7050  N   ASN C  56    10610   9750   7234  -1001  -1300   -567       N  
ATOM   7051  CA  ASN C  56     -38.129  48.224  43.743  1.00 72.62           C  
ANISOU 7051  CA  ASN C  56    10616   9821   7154   -885  -1339   -550       C  
ATOM   7052  C   ASN C  56     -36.719  48.192  44.322  1.00 79.77           C  
ANISOU 7052  C   ASN C  56    11410  10792   8107   -860  -1521   -615       C  
ATOM   7053  O   ASN C  56     -36.456  47.407  45.233  1.00 80.31           O  
ANISOU 7053  O   ASN C  56    11562  10888   8064   -743  -1624   -631       O  
ATOM   7054  CB  ASN C  56     -38.249  47.328  42.522  1.00 69.72           C  
ANISOU 7054  CB  ASN C  56    10173   9498   6821   -870  -1202   -468       C  
ATOM   7055  CG  ASN C  56     -39.658  47.221  42.015  1.00 86.35           C  
ANISOU 7055  CG  ASN C  56    12383  11559   8867   -887  -1045   -413       C  
ATOM   7056  OD1 ASN C  56     -40.592  46.886  42.754  1.00 77.63           O  
ANISOU 7056  OD1 ASN C  56    11444  10412   7640   -837  -1018   -415       O  
ATOM   7057  ND2 ASN C  56     -39.841  47.511  40.737  1.00 79.04           N  
ANISOU 7057  ND2 ASN C  56    11356  10655   8021   -961   -939   -361       N  
ATOM   7058  N   GLY C  57     -35.851  49.079  43.827  1.00 77.95           N  
ANISOU 7058  N   GLY C  57    10995  10584   8037   -973  -1563   -650       N  
ATOM   7059  CA  GLY C  57     -34.488  49.243  44.319  1.00 79.71           C  
ANISOU 7059  CA  GLY C  57    11067  10882   8338   -979  -1742   -731       C  
ATOM   7060  C   GLY C  57     -34.505  49.608  45.788  1.00 84.60           C  
ANISOU 7060  C   GLY C  57    11827  11475   8844   -944  -1915   -828       C  
ATOM   7061  O   GLY C  57     -33.746  49.035  46.574  1.00 85.51           O  
ANISOU 7061  O   GLY C  57    11921  11667   8900   -846  -2080   -870       O  
ATOM   7062  N   LEU C  58     -35.435  50.514  46.177  1.00 80.76           N  
ANISOU 7062  N   LEU C  58    11495  10882   8307  -1007  -1876   -863       N  
ATOM   7063  CA  LEU C  58     -35.618  50.934  47.566  1.00 81.85           C  
ANISOU 7063  CA  LEU C  58    11799  10991   8312   -979  -2013   -970       C  
ATOM   7064  C   LEU C  58     -36.165  49.801  48.438  1.00 87.59           C  
ANISOU 7064  C   LEU C  58    12724  11748   8809   -817  -2025   -933       C  
ATOM   7065  O   LEU C  58     -35.623  49.564  49.512  1.00 88.59           O  
ANISOU 7065  O   LEU C  58    12909  11932   8818   -745  -2202   -996       O  
ATOM   7066  CB  LEU C  58     -36.475  52.201  47.674  1.00 81.15           C  
ANISOU 7066  CB  LEU C  58    11817  10770   8246  -1078  -1946  -1027       C  
ATOM   7067  CG  LEU C  58     -35.702  53.504  47.563  1.00 86.44           C  
ANISOU 7067  CG  LEU C  58    12359  11387   9096  -1236  -2036  -1125       C  
ATOM   7068  CD1 LEU C  58     -36.591  54.619  47.099  1.00 85.69           C  
ANISOU 7068  CD1 LEU C  58    12335  11136   9086  -1327  -1907  -1119       C  
ATOM   7069  CD2 LEU C  58     -35.026  53.861  48.872  1.00 90.57           C  
ANISOU 7069  CD2 LEU C  58    12924  11942   9548  -1236  -2260  -1286       C  
ATOM   7070  N   VAL C  59     -37.185  49.067  47.949  1.00 84.15           N  
ANISOU 7070  N   VAL C  59    12385  11281   8309   -766  -1843   -826       N  
ATOM   7071  CA  VAL C  59     -37.773  47.916  48.647  1.00 84.57           C  
ANISOU 7071  CA  VAL C  59    12630  11344   8159   -634  -1816   -768       C  
ATOM   7072  C   VAL C  59     -36.672  46.856  48.899  1.00 92.36           C  
ANISOU 7072  C   VAL C  59    13555  12414   9124   -516  -1959   -736       C  
ATOM   7073  O   VAL C  59     -36.543  46.378  50.023  1.00 93.27           O  
ANISOU 7073  O   VAL C  59    13817  12555   9065   -413  -2080   -744       O  
ATOM   7074  CB  VAL C  59     -39.021  47.355  47.894  1.00 86.15           C  
ANISOU 7074  CB  VAL C  59    12901  11493   8340   -633  -1587   -667       C  
ATOM   7075  CG1 VAL C  59     -39.491  46.028  48.481  1.00 85.97           C  
ANISOU 7075  CG1 VAL C  59    13056  11470   8139   -517  -1547   -592       C  
ATOM   7076  CG2 VAL C  59     -40.167  48.365  47.897  1.00 85.12           C  
ANISOU 7076  CG2 VAL C  59    12849  11289   8205   -710  -1473   -705       C  
ATOM   7077  N   ILE C  60     -35.844  46.558  47.877  1.00 91.04           N  
ANISOU 7077  N   ILE C  60    13167  12295   9130   -525  -1951   -705       N  
ATOM   7078  CA  ILE C  60     -34.731  45.608  47.973  1.00 93.32           C  
ANISOU 7078  CA  ILE C  60    13353  12663   9440   -400  -2081   -685       C  
ATOM   7079  C   ILE C  60     -33.623  46.086  48.933  1.00102.80           C  
ANISOU 7079  C   ILE C  60    14478  13948  10633   -379  -2341   -788       C  
ATOM   7080  O   ILE C  60     -33.125  45.284  49.720  1.00103.68           O  
ANISOU 7080  O   ILE C  60    14650  14108  10635   -228  -2493   -770       O  
ATOM   7081  CB  ILE C  60     -34.232  45.190  46.558  1.00 95.59           C  
ANISOU 7081  CB  ILE C  60    13421  12986   9915   -416  -1970   -641       C  
ATOM   7082  CG1 ILE C  60     -35.016  43.971  46.050  1.00 94.59           C  
ANISOU 7082  CG1 ILE C  60    13415  12802   9724   -333  -1803   -538       C  
ATOM   7083  CG2 ILE C  60     -32.717  44.934  46.483  1.00 98.01           C  
ANISOU 7083  CG2 ILE C  60    13488  13405  10346   -352  -2128   -684       C  
ATOM   7084  CD1 ILE C  60     -35.771  44.212  44.782  1.00 98.97           C  
ANISOU 7084  CD1 ILE C  60    13922  13323  10359   -446  -1589   -503       C  
ATOM   7085  N   LEU C  61     -33.259  47.380  48.885  1.00102.77           N  
ANISOU 7085  N   LEU C  61    14351  13954  10744   -529  -2400   -893       N  
ATOM   7086  CA  LEU C  61     -32.221  47.942  49.756  1.00106.29           C  
ANISOU 7086  CA  LEU C  61    14706  14481  11198   -542  -2653  -1017       C  
ATOM   7087  C   LEU C  61     -32.700  48.067  51.214  1.00113.23           C  
ANISOU 7087  C   LEU C  61    15848  15347  11828   -482  -2778  -1073       C  
ATOM   7088  O   LEU C  61     -31.944  47.747  52.130  1.00115.08           O  
ANISOU 7088  O   LEU C  61    16087  15675  11963   -383  -3005  -1117       O  
ATOM   7089  CB  LEU C  61     -31.721  49.300  49.208  1.00106.99           C  
ANISOU 7089  CB  LEU C  61    14592  14560  11500   -748  -2658  -1115       C  
ATOM   7090  CG  LEU C  61     -30.466  49.918  49.849  1.00114.79           C  
ANISOU 7090  CG  LEU C  61    15406  15645  12565   -803  -2914  -1259       C  
ATOM   7091  CD1 LEU C  61     -29.199  49.169  49.440  1.00116.45           C  
ANISOU 7091  CD1 LEU C  61    15340  16000  12905   -724  -3011  -1242       C  
ATOM   7092  CD2 LEU C  61     -30.324  51.377  49.456  1.00118.00           C  
ANISOU 7092  CD2 LEU C  61    15702  15981  13152  -1035  -2884  -1355       C  
ATOM   7093  N   VAL C  62     -33.958  48.508  51.415  1.00109.80           N  
ANISOU 7093  N   VAL C  62    15626  14807  11285   -533  -2629  -1071       N  
ATOM   7094  CA  VAL C  62     -34.569  48.712  52.731  1.00111.15           C  
ANISOU 7094  CA  VAL C  62    16059  14963  11209   -492  -2696  -1132       C  
ATOM   7095  C   VAL C  62     -35.062  47.401  53.375  1.00117.37           C  
ANISOU 7095  C   VAL C  62    17071  15767  11758   -321  -2672  -1011       C  
ATOM   7096  O   VAL C  62     -34.547  47.025  54.430  1.00118.91           O  
ANISOU 7096  O   VAL C  62    17363  16040  11779   -215  -2870  -1032       O  
ATOM   7097  CB  VAL C  62     -35.628  49.853  52.693  1.00113.86           C  
ANISOU 7097  CB  VAL C  62    16508  15193  11561   -617  -2548  -1204       C  
ATOM   7098  CG1 VAL C  62     -36.570  49.820  53.893  1.00114.32           C  
ANISOU 7098  CG1 VAL C  62    16861  15232  11342   -553  -2527  -1240       C  
ATOM   7099  CG2 VAL C  62     -34.958  51.219  52.563  1.00114.68           C  
ANISOU 7099  CG2 VAL C  62    16455  15272  11845   -773  -2653  -1354       C  
ATOM   7100  N   MET C  63     -36.035  46.701  52.745  1.00114.11           N  
ANISOU 7100  N   MET C  63    16742  15280  11336   -299  -2440   -884       N  
ATOM   7101  CA  MET C  63     -36.581  45.444  53.276  1.00115.11           C  
ANISOU 7101  CA  MET C  63    17089  15391  11256   -164  -2384   -757       C  
ATOM   7102  C   MET C  63     -35.637  44.241  53.166  1.00122.97           C  
ANISOU 7102  C   MET C  63    18017  16432  12274    -15  -2502   -662       C  
ATOM   7103  O   MET C  63     -35.901  43.193  53.761  1.00123.25           O  
ANISOU 7103  O   MET C  63    18253  16445  12130    110  -2500   -554       O  
ATOM   7104  CB  MET C  63     -37.994  45.152  52.741  1.00115.30           C  
ANISOU 7104  CB  MET C  63    17227  15319  11261   -210  -2102   -675       C  
ATOM   7105  CG  MET C  63     -39.104  45.637  53.665  1.00119.20           C  
ANISOU 7105  CG  MET C  63    17952  15786  11554   -242  -2014   -721       C  
ATOM   7106  SD  MET C  63     -39.301  47.441  53.711  1.00123.46           S  
ANISOU 7106  SD  MET C  63    18419  16305  12187   -381  -2027   -905       S  
ATOM   7107  CE  MET C  63     -40.434  47.605  55.062  1.00121.23           C  
ANISOU 7107  CE  MET C  63    18441  16017  11605   -352  -1947   -955       C  
ATOM   7108  N   GLY C  64     -34.537  44.419  52.435  1.00122.42           N  
ANISOU 7108  N   GLY C  64    17669  16422  12424    -29  -2599   -703       N  
ATOM   7109  CA  GLY C  64     -33.486  43.419  52.290  1.00124.82           C  
ANISOU 7109  CA  GLY C  64    17855  16782  12788    123  -2729   -644       C  
ATOM   7110  C   GLY C  64     -32.616  43.382  53.529  1.00134.84           C  
ANISOU 7110  C   GLY C  64    19167  18154  13914    238  -3025   -690       C  
ATOM   7111  O   GLY C  64     -32.117  42.317  53.909  1.00136.15           O  
ANISOU 7111  O   GLY C  64    19385  18342  14004    423  -3142   -600       O  
ATOM   7112  N   TYR C  65     -32.447  44.558  54.177  1.00134.55           N  
ANISOU 7112  N   TYR C  65    19116  18173  13833    133  -3154   -834       N  
ATOM   7113  CA  TYR C  65     -31.698  44.717  55.423  1.00138.29           C  
ANISOU 7113  CA  TYR C  65    19640  18761  14144    213  -3452   -911       C  
ATOM   7114  C   TYR C  65     -32.585  45.328  56.536  1.00144.16           C  
ANISOU 7114  C   TYR C  65    20674  19482  14619    161  -3447   -975       C  
ATOM   7115  O   TYR C  65     -32.301  46.400  57.082  1.00144.84           O  
ANISOU 7115  O   TYR C  65    20729  19621  14683     63  -3585  -1142       O  
ATOM   7116  CB  TYR C  65     -30.346  45.443  55.207  1.00141.40           C  
ANISOU 7116  CB  TYR C  65    19698  19277  14749    150  -3668  -1055       C  
ATOM   7117  CG  TYR C  65     -29.470  45.492  56.445  1.00146.93           C  
ANISOU 7117  CG  TYR C  65    20417  20119  15290    248  -4009  -1139       C  
ATOM   7118  CD1 TYR C  65     -29.036  44.323  57.065  1.00150.86           C  
ANISOU 7118  CD1 TYR C  65    21010  20678  15632    484  -4174  -1024       C  
ATOM   7119  CD2 TYR C  65     -29.072  46.708  56.993  1.00149.35           C  
ANISOU 7119  CD2 TYR C  65    20653  20494  15601    108  -4177  -1334       C  
ATOM   7120  CE1 TYR C  65     -28.249  44.363  58.215  1.00155.21           C  
ANISOU 7120  CE1 TYR C  65    21584  21374  16014    587  -4508  -1094       C  
ATOM   7121  CE2 TYR C  65     -28.281  46.760  58.140  1.00153.61           C  
ANISOU 7121  CE2 TYR C  65    21208  21180  15976    192  -4508  -1426       C  
ATOM   7122  CZ  TYR C  65     -27.864  45.585  58.743  1.00162.84           C  
ANISOU 7122  CZ  TYR C  65    22467  22430  16976    436  -4680  -1302       C  
ATOM   7123  OH  TYR C  65     -27.097  45.633  59.881  1.00166.48           O  
ANISOU 7123  OH  TYR C  65    22950  23049  17255    531  -5025  -1386       O  
ATOM   7124  N   GLN C  66     -33.659  44.619  56.863  1.00141.33           N  
ANISOU 7124  N   GLN C  66    20598  19043  14060    224  -3277   -849       N  
ATOM   7125  CA  GLN C  66     -34.556  45.018  57.941  1.00142.57           C  
ANISOU 7125  CA  GLN C  66    21045  19189  13935    197  -3239   -893       C  
ATOM   7126  C   GLN C  66     -35.040  43.946  58.906  1.00149.36           C  
ANISOU 7126  C   GLN C  66    22227  20047  14478    346  -3233   -745       C  
ATOM   7127  O   GLN C  66     -36.242  43.718  59.042  1.00148.12           O  
ANISOU 7127  O   GLN C  66    22281  19807  14188    313  -2997   -675       O  
ATOM   7128  CB  GLN C  66     -35.776  45.752  57.384  1.00141.52           C  
ANISOU 7128  CB  GLN C  66    20947  18948  13877     41  -2956   -934       C  
ATOM   7129  CG  GLN C  66     -37.007  45.673  58.272  1.00157.95           C  
ANISOU 7129  CG  GLN C  66    23347  20995  15673     48  -2807   -911       C  
ATOM   7130  CD  GLN C  66     -38.175  46.467  57.721  1.00175.16           C  
ANISOU 7130  CD  GLN C  66    25523  23080  17949    -89  -2546   -968       C  
ATOM   7131  OE1 GLN C  66     -38.095  47.686  57.568  1.00169.38           O  
ANISOU 7131  OE1 GLN C  66    24683  22334  17338   -199  -2573  -1126       O  
ATOM   7132  NE2 GLN C  66     -39.269  45.778  57.419  1.00167.48           N  
ANISOU 7132  NE2 GLN C  66    24666  22036  16931    -84  -2296   -841       N  
ATOM   7133  N   LYS C  67     -34.099  43.279  59.566  1.00149.22           N  
ANISOU 7133  N   LYS C  67    22238  20118  14341    509  -3490   -691       N  
ATOM   7134  CA  LYS C  67     -34.432  42.127  60.403  1.00150.75           C  
ANISOU 7134  CA  LYS C  67    22740  20293  14246    668  -3496   -511       C  
ATOM   7135  C   LYS C  67     -35.351  42.235  61.624  1.00156.04           C  
ANISOU 7135  C   LYS C  67    23768  20977  14543    659  -3432   -501       C  
ATOM   7136  O   LYS C  67     -35.601  41.252  62.327  1.00157.23           O  
ANISOU 7136  O   LYS C  67    24189  21109  14443    785  -3430   -331       O  
ATOM   7137  CB  LYS C  67     -33.218  41.177  60.377  1.00155.15           C  
ANISOU 7137  CB  LYS C  67    23189  20900  14862    868  -3738   -410       C  
ATOM   7138  CG  LYS C  67     -33.115  40.362  59.088  1.00167.67           C  
ANISOU 7138  CG  LYS C  67    24598  22375  16733    903  -3585   -300       C  
ATOM   7139  CD  LYS C  67     -31.991  39.326  59.135  1.00179.49           C  
ANISOU 7139  CD  LYS C  67    26018  23905  18276   1134  -3809   -194       C  
ATOM   7140  CE  LYS C  67     -30.697  39.804  58.516  1.00189.65           C  
ANISOU 7140  CE  LYS C  67    26903  25311  19844   1141  -4002   -329       C  
ATOM   7141  NZ  LYS C  67     -29.926  40.686  59.434  1.00200.79           N  
ANISOU 7141  NZ  LYS C  67    28243  26901  21147   1131  -4310   -484       N  
ATOM   7142  N   LYS C  68     -35.793  43.460  61.878  1.00152.18           N  
ANISOU 7142  N   LYS C  68    23279  20520  14023    514  -3385   -689       N  
ATOM   7143  CA  LYS C  68     -36.592  43.775  63.045  1.00153.42           C  
ANISOU 7143  CA  LYS C  68    23745  20716  13834    495  -3328   -733       C  
ATOM   7144  C   LYS C  68     -38.085  43.578  62.969  1.00154.86           C  
ANISOU 7144  C   LYS C  68    24116  20794  13928    420  -2968   -656       C  
ATOM   7145  O   LYS C  68     -38.678  42.908  63.807  1.00156.04           O  
ANISOU 7145  O   LYS C  68    24564  20949  13776    481  -2885   -534       O  
ATOM   7146  CB  LYS C  68     -36.468  45.262  63.385  1.00156.70           C  
ANISOU 7146  CB  LYS C  68    24082  21197  14258    370  -3423  -1001       C  
ATOM   7147  N   LEU C  69     -38.677  44.190  61.953  1.00147.61           N  
ANISOU 7147  N   LEU C  69    23016  19788  13279    284  -2759   -728       N  
ATOM   7148  CA  LEU C  69     -40.115  44.319  61.843  1.00145.56           C  
ANISOU 7148  CA  LEU C  69    22876  19454  12976    191  -2430   -715       C  
ATOM   7149  C   LEU C  69     -40.604  43.415  60.705  1.00145.80           C  
ANISOU 7149  C   LEU C  69    22814  19366  13216    174  -2214   -545       C  
ATOM   7150  O   LEU C  69     -41.733  43.550  60.227  1.00143.93           O  
ANISOU 7150  O   LEU C  69    22575  19061  13050     79  -1943   -541       O  
ATOM   7151  CB  LEU C  69     -40.579  45.768  61.649  1.00144.71           C  
ANISOU 7151  CB  LEU C  69    22662  19336  12987     59  -2350   -935       C  
ATOM   7152  CG  LEU C  69     -39.631  46.867  62.148  1.00151.08           C  
ANISOU 7152  CG  LEU C  69    23389  20224  13792     39  -2625  -1150       C  
ATOM   7153  CD1 LEU C  69     -39.186  47.769  61.016  1.00149.44           C  
ANISOU 7153  CD1 LEU C  69    22866  19953  13960    -70  -2652  -1260       C  
ATOM   7154  CD2 LEU C  69     -40.252  47.682  63.266  1.00155.13           C  
ANISOU 7154  CD2 LEU C  69    24119  20786  14038     10  -2590  -1318       C  
ATOM   7155  N   ARG C  70     -39.753  42.485  60.286  1.00140.89           N  
ANISOU 7155  N   ARG C  70    22115  18725  12694    273  -2342   -416       N  
ATOM   7156  CA  ARG C  70     -40.087  41.551  59.218  1.00137.77           C  
ANISOU 7156  CA  ARG C  70    21641  18215  12491    268  -2164   -270       C  
ATOM   7157  C   ARG C  70     -41.438  40.883  59.427  1.00138.83           C  
ANISOU 7157  C   ARG C  70    22000  18270  12479    222  -1874   -151       C  
ATOM   7158  O   ARG C  70     -41.685  40.263  60.445  1.00140.66           O  
ANISOU 7158  O   ARG C  70    22507  18510  12427    285  -1867    -47       O  
ATOM   7159  CB  ARG C  70     -39.003  40.490  59.083  1.00139.02           C  
ANISOU 7159  CB  ARG C  70    21765  18361  12695    422  -2351   -141       C  
ATOM   7160  N   SER C  71     -42.287  41.005  58.419  1.00130.66           N  
ANISOU 7160  N   SER C  71    20836  17164  11646    106  -1639   -162       N  
ATOM   7161  CA  SER C  71     -43.693  40.597  58.426  1.00128.72           C  
ANISOU 7161  CA  SER C  71    20727  16857  11325     20  -1338    -92       C  
ATOM   7162  C   SER C  71     -43.733  39.536  57.321  1.00127.99           C  
ANISOU 7162  C   SER C  71    20542  16651  11437     15  -1239     35       C  
ATOM   7163  O   SER C  71     -42.938  39.601  56.380  1.00126.57           O  
ANISOU 7163  O   SER C  71    20138  16462  11492     38  -1348      5       O  
ATOM   7164  CB  SER C  71     -44.699  41.711  58.136  1.00130.96           C  
ANISOU 7164  CB  SER C  71    20910  17163  11686   -108  -1158   -237       C  
ATOM   7165  OG  SER C  71     -45.981  41.218  57.779  1.00139.26           O  
ANISOU 7165  OG  SER C  71    21999  18156  12755   -197   -871   -168       O  
ATOM   7166  N   MET C  72     -44.659  38.567  57.435  1.00122.13           N  
ANISOU 7166  N   MET C  72    19973  15826  10606    -24  -1024    167       N  
ATOM   7167  CA  MET C  72     -44.828  37.490  56.457  1.00119.56           C  
ANISOU 7167  CA  MET C  72    19595  15375  10456    -44   -910    277       C  
ATOM   7168  C   MET C  72     -45.168  37.997  55.053  1.00117.48           C  
ANISOU 7168  C   MET C  72    19048  15109  10482   -150   -809    178       C  
ATOM   7169  O   MET C  72     -44.631  37.475  54.079  1.00115.29           O  
ANISOU 7169  O   MET C  72    18633  14774  10397   -123   -847    204       O  
ATOM   7170  CB  MET C  72     -45.866  36.471  56.938  1.00122.94           C  
ANISOU 7170  CB  MET C  72    20274  15712  10728   -101   -683    420       C  
ATOM   7171  CG  MET C  72     -45.284  35.405  57.828  1.00128.94           C  
ANISOU 7171  CG  MET C  72    21304  16400  11287     30   -790    594       C  
ATOM   7172  SD  MET C  72     -44.233  34.244  56.925  1.00132.68           S  
ANISOU 7172  SD  MET C  72    21702  16731  11980    157   -923    695       S  
ATOM   7173  CE  MET C  72     -43.732  33.204  58.238  1.00132.96           C  
ANISOU 7173  CE  MET C  72    22100  16693  11727    322  -1048    904       C  
ATOM   7174  N   THR C  73     -46.032  39.031  54.962  1.00111.43           N  
ANISOU 7174  N   THR C  73    18196  14407   9737   -257   -686     62       N  
ATOM   7175  CA  THR C  73     -46.455  39.660  53.705  1.00108.09           C  
ANISOU 7175  CA  THR C  73    17519  13993   9559   -353   -597    -27       C  
ATOM   7176  C   THR C  73     -45.258  40.338  53.031  1.00108.99           C  
ANISOU 7176  C   THR C  73    17417  14144   9850   -306   -802   -104       C  
ATOM   7177  O   THR C  73     -45.112  40.245  51.812  1.00107.03           O  
ANISOU 7177  O   THR C  73    16981  13875   9810   -341   -776   -108       O  
ATOM   7178  CB  THR C  73     -47.613  40.650  53.951  1.00116.44           C  
ANISOU 7178  CB  THR C  73    18558  15108  10577   -444   -442   -127       C  
ATOM   7179  OG1 THR C  73     -48.520  40.112  54.920  1.00119.25           O  
ANISOU 7179  OG1 THR C  73    19137  15459  10714   -472   -277    -65       O  
ATOM   7180  CG2 THR C  73     -48.365  41.007  52.673  1.00112.42           C  
ANISOU 7180  CG2 THR C  73    17828  14595  10292   -543   -306   -175       C  
ATOM   7181  N   ASP C  74     -44.392  40.980  53.839  1.00105.06           N  
ANISOU 7181  N   ASP C  74    16950  13710   9259   -234  -1005   -165       N  
ATOM   7182  CA  ASP C  74     -43.176  41.665  53.400  1.00103.64           C  
ANISOU 7182  CA  ASP C  74    16571  13576   9232   -201  -1212   -246       C  
ATOM   7183  C   ASP C  74     -42.134  40.686  52.844  1.00105.11           C  
ANISOU 7183  C   ASP C  74    16679  13735   9524   -110  -1323   -163       C  
ATOM   7184  O   ASP C  74     -41.342  41.075  51.984  1.00103.57           O  
ANISOU 7184  O   ASP C  74    16256  13568   9526   -117  -1408   -215       O  
ATOM   7185  CB  ASP C  74     -42.587  42.491  54.545  1.00107.29           C  
ANISOU 7185  CB  ASP C  74    17108  14115   9544   -157  -1402   -341       C  
ATOM   7186  CG  ASP C  74     -43.508  43.559  55.099  1.00119.13           C  
ANISOU 7186  CG  ASP C  74    18675  15638  10950   -233  -1304   -454       C  
ATOM   7187  OD1 ASP C  74     -44.540  43.918  54.513  1.00118.14           O  
ANISOU 7187  OD1 ASP C  74    18490  15483  10916   -319  -1107   -477       O  
ATOM   7188  OD2 ASP C  74     -43.105  44.191  56.117  1.00127.87           O  
ANISOU 7188  OD2 ASP C  74    19876  16805  11906   -200  -1449   -547       O  
ATOM   7189  N   LYS C  75     -42.151  39.417  53.324  1.00101.41           N  
ANISOU 7189  N   LYS C  75    16401  13202   8927    -23  -1309    -32       N  
ATOM   7190  CA  LYS C  75     -41.257  38.342  52.877  1.00100.92           C  
ANISOU 7190  CA  LYS C  75    16300  13087   8958     91  -1397     54       C  
ATOM   7191  C   LYS C  75     -41.549  37.985  51.410  1.00100.22           C  
ANISOU 7191  C   LYS C  75    16041  12942   9097     19  -1242     53       C  
ATOM   7192  O   LYS C  75     -40.606  37.867  50.623  1.00 99.44           O  
ANISOU 7192  O   LYS C  75    15754  12861   9169     72  -1331     28       O  
ATOM   7193  CB  LYS C  75     -41.353  37.109  53.807  1.00105.88           C  
ANISOU 7193  CB  LYS C  75    17216  13630   9384    198  -1402    206       C  
ATOM   7194  CG  LYS C  75     -40.354  35.983  53.506  1.00125.72           C  
ANISOU 7194  CG  LYS C  75    19715  16070  11983    356  -1521    296       C  
ATOM   7195  CD  LYS C  75     -38.913  36.319  53.918  1.00138.21           C  
ANISOU 7195  CD  LYS C  75    21184  17757  13574    502  -1820    252       C  
ATOM   7196  CE  LYS C  75     -37.886  35.464  53.214  1.00147.82           C  
ANISOU 7196  CE  LYS C  75    22264  18927  14972    646  -1915    289       C  
ATOM   7197  NZ  LYS C  75     -37.726  35.837  51.782  1.00154.17           N  
ANISOU 7197  NZ  LYS C  75    22776  19757  16045    557  -1822    188       N  
ATOM   7198  N   TYR C  76     -42.849  37.850  51.040  1.00 93.56           N  
ANISOU 7198  N   TYR C  76    15250  12047   8251   -104  -1011     68       N  
ATOM   7199  CA  TYR C  76     -43.264  37.589  49.656  1.00 90.39           C  
ANISOU 7199  CA  TYR C  76    14695  11610   8039   -188   -864     52       C  
ATOM   7200  C   TYR C  76     -43.148  38.885  48.837  1.00 90.26           C  
ANISOU 7200  C   TYR C  76    14434  11690   8171   -269   -883    -61       C  
ATOM   7201  O   TYR C  76     -42.853  38.818  47.644  1.00 88.77           O  
ANISOU 7201  O   TYR C  76    14068  11509   8150   -294   -856    -84       O  
ATOM   7202  CB  TYR C  76     -44.712  37.092  49.565  1.00 90.86           C  
ANISOU 7202  CB  TYR C  76    14871  11603   8048   -303   -630     93       C  
ATOM   7203  CG  TYR C  76     -45.042  35.823  50.316  1.00 94.24           C  
ANISOU 7203  CG  TYR C  76    15559  11912   8335   -266   -562    218       C  
ATOM   7204  CD1 TYR C  76     -44.862  34.574  49.727  1.00 96.53           C  
ANISOU 7204  CD1 TYR C  76    15888  12077   8710   -234   -517    284       C  
ATOM   7205  CD2 TYR C  76     -45.658  35.870  51.560  1.00 96.42           C  
ANISOU 7205  CD2 TYR C  76    16052  12191   8394   -280   -512    267       C  
ATOM   7206  CE1 TYR C  76     -45.217  33.402  50.394  1.00 99.01           C  
ANISOU 7206  CE1 TYR C  76    16461  12252   8908   -213   -440    410       C  
ATOM   7207  CE2 TYR C  76     -46.007  34.708  52.242  1.00 99.05           C  
ANISOU 7207  CE2 TYR C  76    16640  12405   8588   -263   -430    402       C  
ATOM   7208  CZ  TYR C  76     -45.786  33.475  51.656  1.00106.53           C  
ANISOU 7208  CZ  TYR C  76    17631  13208   9636   -232   -396    479       C  
ATOM   7209  OH  TYR C  76     -46.133  32.336  52.340  1.00109.46           O  
ANISOU 7209  OH  TYR C  76    18275  13435   9879   -223   -311    624       O  
ATOM   7210  N   ARG C  77     -43.393  40.062  49.473  1.00 84.94           N  
ANISOU 7210  N   ARG C  77    13764  11080   7429   -310   -921   -131       N  
ATOM   7211  CA  ARG C  77     -43.300  41.373  48.817  1.00 82.71           C  
ANISOU 7211  CA  ARG C  77    13283  10861   7284   -386   -943   -228       C  
ATOM   7212  C   ARG C  77     -41.885  41.705  48.327  1.00 85.75           C  
ANISOU 7212  C   ARG C  77    13479  11294   7808   -344  -1114   -266       C  
ATOM   7213  O   ARG C  77     -41.732  42.544  47.438  1.00 85.01           O  
ANISOU 7213  O   ARG C  77    13202  11234   7864   -419  -1102   -317       O  
ATOM   7214  CB  ARG C  77     -43.894  42.498  49.679  1.00 81.88           C  
ANISOU 7214  CB  ARG C  77    13249  10784   7077   -428   -941   -303       C  
ATOM   7215  CG  ARG C  77     -45.404  42.627  49.527  1.00 87.48           C  
ANISOU 7215  CG  ARG C  77    14004  11476   7760   -512   -729   -303       C  
ATOM   7216  CD  ARG C  77     -45.993  43.601  50.526  1.00 98.18           C  
ANISOU 7216  CD  ARG C  77    15455  12855   8994   -525   -715   -385       C  
ATOM   7217  NE  ARG C  77     -46.101  44.957  49.983  1.00104.49           N  
ANISOU 7217  NE  ARG C  77    16101  13666   9935   -577   -728   -479       N  
ATOM   7218  CZ  ARG C  77     -46.486  46.021  50.684  1.00116.85           C  
ANISOU 7218  CZ  ARG C  77    17717  15237  11445   -584   -732   -579       C  
ATOM   7219  NH1 ARG C  77     -46.773  45.908  51.974  1.00102.93           N  
ANISOU 7219  NH1 ARG C  77    16147  13492   9470   -544   -723   -608       N  
ATOM   7220  NH2 ARG C  77     -46.557  47.212  50.105  1.00103.45           N  
ANISOU 7220  NH2 ARG C  77    15887  13520   9899   -626   -745   -651       N  
ATOM   7221  N   LEU C  78     -40.864  41.022  48.873  1.00 82.17           N  
ANISOU 7221  N   LEU C  78    13066  10846   7309   -223  -1266   -234       N  
ATOM   7222  CA  LEU C  78     -39.481  41.180  48.438  1.00 81.91           C  
ANISOU 7222  CA  LEU C  78    12833  10873   7417   -172  -1424   -271       C  
ATOM   7223  C   LEU C  78     -39.291  40.378  47.134  1.00 84.10           C  
ANISOU 7223  C   LEU C  78    12982  11127   7845   -164  -1322   -234       C  
ATOM   7224  O   LEU C  78     -38.633  40.871  46.219  1.00 83.10           O  
ANISOU 7224  O   LEU C  78    12634  11060   7879   -205  -1338   -282       O  
ATOM   7225  CB  LEU C  78     -38.502  40.720  49.531  1.00 84.00           C  
ANISOU 7225  CB  LEU C  78    13178  11165   7574    -26  -1636   -253       C  
ATOM   7226  CG  LEU C  78     -37.072  41.225  49.394  1.00 89.28           C  
ANISOU 7226  CG  LEU C  78    13620  11929   8373     12  -1836   -327       C  
ATOM   7227  CD1 LEU C  78     -36.582  41.786  50.690  1.00 91.30           C  
ANISOU 7227  CD1 LEU C  78    13951  12247   8491     54  -2047   -383       C  
ATOM   7228  CD2 LEU C  78     -36.148  40.124  48.943  1.00 92.25           C  
ANISOU 7228  CD2 LEU C  78    13903  12307   8843    151  -1894   -276       C  
ATOM   7229  N   HIS C  79     -39.893  39.164  47.042  1.00 80.08           N  
ANISOU 7229  N   HIS C  79    12618  10529   7281   -123  -1205   -156       N  
ATOM   7230  CA  HIS C  79     -39.846  38.310  45.843  1.00 79.10           C  
ANISOU 7230  CA  HIS C  79    12408  10368   7281   -118  -1094   -138       C  
ATOM   7231  C   HIS C  79     -40.484  39.046  44.671  1.00 79.83           C  
ANISOU 7231  C   HIS C  79    12355  10504   7474   -267   -957   -185       C  
ATOM   7232  O   HIS C  79     -39.881  39.144  43.603  1.00 78.18           O  
ANISOU 7232  O   HIS C  79    11959  10348   7400   -281   -943   -218       O  
ATOM   7233  CB  HIS C  79     -40.594  36.984  46.078  1.00 80.51           C  
ANISOU 7233  CB  HIS C  79    12803  10415   7370    -82   -982    -55       C  
ATOM   7234  CG  HIS C  79     -39.809  35.969  46.844  1.00 86.03           C  
ANISOU 7234  CG  HIS C  79    13630  11045   8011     92  -1105     13       C  
ATOM   7235  ND1 HIS C  79     -39.822  35.941  48.227  1.00 89.34           N  
ANISOU 7235  ND1 HIS C  79    14246  11449   8252    159  -1208     73       N  
ATOM   7236  CD2 HIS C  79     -39.025  34.963  46.392  1.00 88.88           C  
ANISOU 7236  CD2 HIS C  79    13955  11349   8467    220  -1138     33       C  
ATOM   7237  CE1 HIS C  79     -39.044  34.927  48.569  1.00 90.66           C  
ANISOU 7237  CE1 HIS C  79    14491  11546   8408    328  -1314    141       C  
ATOM   7238  NE2 HIS C  79     -38.542  34.310  47.498  1.00 90.76           N  
ANISOU 7238  NE2 HIS C  79    14365  11526   8595    376  -1274    116       N  
ATOM   7239  N   LEU C  80     -41.696  39.595  44.909  1.00 75.82           N  
ANISOU 7239  N   LEU C  80    11934   9984   6891   -369   -857   -185       N  
ATOM   7240  CA  LEU C  80     -42.517  40.376  43.983  1.00 74.14           C  
ANISOU 7240  CA  LEU C  80    11617   9809   6746   -498   -739   -216       C  
ATOM   7241  C   LEU C  80     -41.709  41.552  43.428  1.00 78.46           C  
ANISOU 7241  C   LEU C  80    11963  10435   7412   -537   -821   -265       C  
ATOM   7242  O   LEU C  80     -41.709  41.777  42.216  1.00 77.35           O  
ANISOU 7242  O   LEU C  80    11682  10336   7373   -600   -751   -271       O  
ATOM   7243  CB  LEU C  80     -43.779  40.860  44.733  1.00 73.68           C  
ANISOU 7243  CB  LEU C  80    11690   9729   6575   -558   -663   -216       C  
ATOM   7244  CG  LEU C  80     -44.753  41.805  44.033  1.00 76.54           C  
ANISOU 7244  CG  LEU C  80    11960  10127   6993   -667   -562   -246       C  
ATOM   7245  CD1 LEU C  80     -45.542  41.094  42.953  1.00 75.63           C  
ANISOU 7245  CD1 LEU C  80    11806  10010   6920   -728   -419   -225       C  
ATOM   7246  CD2 LEU C  80     -45.711  42.385  45.035  1.00 78.89           C  
ANISOU 7246  CD2 LEU C  80    12377  10412   7184   -687   -522   -266       C  
ATOM   7247  N   SER C  81     -40.976  42.249  44.317  1.00 75.89           N  
ANISOU 7247  N   SER C  81    11634  10133   7069   -503   -972   -299       N  
ATOM   7248  CA  SER C  81     -40.123  43.374  43.969  1.00 75.98           C  
ANISOU 7248  CA  SER C  81    11467  10204   7199   -555  -1062   -350       C  
ATOM   7249  C   SER C  81     -38.916  42.935  43.131  1.00 81.22           C  
ANISOU 7249  C   SER C  81    11946  10926   7988   -519  -1099   -352       C  
ATOM   7250  O   SER C  81     -38.575  43.636  42.183  1.00 80.53           O  
ANISOU 7250  O   SER C  81    11690  10888   8020   -604  -1065   -367       O  
ATOM   7251  CB  SER C  81     -39.664  44.097  45.228  1.00 80.50           C  
ANISOU 7251  CB  SER C  81    12094  10781   7710   -532  -1224   -405       C  
ATOM   7252  OG  SER C  81     -39.576  45.490  44.990  1.00 88.51           O  
ANISOU 7252  OG  SER C  81    13007  11805   8817   -637  -1248   -460       O  
ATOM   7253  N   VAL C  82     -38.277  41.784  43.466  1.00 79.54           N  
ANISOU 7253  N   VAL C  82    11767  10706   7750   -389  -1160   -334       N  
ATOM   7254  CA  VAL C  82     -37.131  41.229  42.719  1.00 80.41           C  
ANISOU 7254  CA  VAL C  82    11698  10873   7982   -324  -1185   -348       C  
ATOM   7255  C   VAL C  82     -37.580  40.858  41.295  1.00 85.23           C  
ANISOU 7255  C   VAL C  82    12240  11489   8652   -385  -1003   -336       C  
ATOM   7256  O   VAL C  82     -36.861  41.138  40.330  1.00 84.91           O  
ANISOU 7256  O   VAL C  82    12003  11530   8727   -422   -973   -363       O  
ATOM   7257  CB  VAL C  82     -36.459  40.036  43.460  1.00 85.34           C  
ANISOU 7257  CB  VAL C  82    12398  11465   8561   -143  -1295   -327       C  
ATOM   7258  CG1 VAL C  82     -35.516  39.255  42.546  1.00 85.66           C  
ANISOU 7258  CG1 VAL C  82    12269  11546   8731    -56  -1272   -345       C  
ATOM   7259  CG2 VAL C  82     -35.716  40.507  44.708  1.00 86.60           C  
ANISOU 7259  CG2 VAL C  82    12566  11666   8673    -80  -1511   -352       C  
ATOM   7260  N   ALA C  83     -38.793  40.261  41.185  1.00 82.28           N  
ANISOU 7260  N   ALA C  83    12031  11040   8192   -407   -879   -300       N  
ATOM   7261  CA  ALA C  83     -39.448  39.852  39.936  1.00 81.34           C  
ANISOU 7261  CA  ALA C  83    11884  10926   8097   -472   -715   -298       C  
ATOM   7262  C   ALA C  83     -39.766  41.067  39.067  1.00 85.45           C  
ANISOU 7262  C   ALA C  83    12281  11520   8666   -609   -657   -302       C  
ATOM   7263  O   ALA C  83     -39.639  40.989  37.845  1.00 85.18           O  
ANISOU 7263  O   ALA C  83    12134  11547   8682   -654   -568   -311       O  
ATOM   7264  CB  ALA C  83     -40.729  39.088  40.244  1.00 81.39           C  
ANISOU 7264  CB  ALA C  83    12090  10836   8000   -485   -620   -267       C  
ATOM   7265  N   ASP C  84     -40.159  42.191  39.705  1.00 82.23           N  
ANISOU 7265  N   ASP C  84    11905  11103   8236   -669   -709   -295       N  
ATOM   7266  CA  ASP C  84     -40.495  43.444  39.031  1.00 81.74           C  
ANISOU 7266  CA  ASP C  84    11754  11078   8224   -787   -671   -285       C  
ATOM   7267  C   ASP C  84     -39.277  44.306  38.707  1.00 85.83           C  
ANISOU 7267  C   ASP C  84    12095  11657   8857   -828   -740   -301       C  
ATOM   7268  O   ASP C  84     -39.325  45.046  37.730  1.00 85.32           O  
ANISOU 7268  O   ASP C  84    11934  11634   8850   -924   -676   -274       O  
ATOM   7269  CB  ASP C  84     -41.585  44.228  39.794  1.00 83.73           C  
ANISOU 7269  CB  ASP C  84    12129  11272   8414   -825   -674   -280       C  
ATOM   7270  CG  ASP C  84     -42.938  43.524  39.923  1.00 98.86           C  
ANISOU 7270  CG  ASP C  84    14183  13148  10232   -820   -571   -263       C  
ATOM   7271  OD1 ASP C  84     -43.175  42.533  39.188  1.00100.12           O  
ANISOU 7271  OD1 ASP C  84    14339  13321  10382   -816   -486   -253       O  
ATOM   7272  OD2 ASP C  84     -43.758  43.961  40.760  1.00106.44           O  
ANISOU 7272  OD2 ASP C  84    15248  14065  11129   -826   -569   -270       O  
ATOM   7273  N   LEU C  85     -38.182  44.192  39.487  1.00 83.52           N  
ANISOU 7273  N   LEU C  85    11756  11378   8600   -762   -871   -340       N  
ATOM   7274  CA  LEU C  85     -36.934  44.929  39.240  1.00 84.35           C  
ANISOU 7274  CA  LEU C  85    11666  11553   8832   -812   -942   -369       C  
ATOM   7275  C   LEU C  85     -36.207  44.341  38.025  1.00 88.75           C  
ANISOU 7275  C   LEU C  85    12056  12202   9463   -805   -850   -366       C  
ATOM   7276  O   LEU C  85     -35.611  45.088  37.246  1.00 89.10           O  
ANISOU 7276  O   LEU C  85    11938  12313   9603   -905   -811   -360       O  
ATOM   7277  CB  LEU C  85     -36.016  44.945  40.486  1.00 85.72           C  
ANISOU 7277  CB  LEU C  85    11825  11731   9014   -737  -1128   -425       C  
ATOM   7278  CG  LEU C  85     -34.663  45.678  40.375  1.00 91.86           C  
ANISOU 7278  CG  LEU C  85    12377  12589   9937   -797  -1222   -474       C  
ATOM   7279  CD1 LEU C  85     -34.837  47.195  40.255  1.00 91.89           C  
ANISOU 7279  CD1 LEU C  85    12350  12556  10007   -964  -1221   -478       C  
ATOM   7280  CD2 LEU C  85     -33.777  45.354  41.555  1.00 96.39           C  
ANISOU 7280  CD2 LEU C  85    12932  13191  10502   -689  -1420   -534       C  
ATOM   7281  N   LEU C  86     -36.285  43.004  37.859  1.00 84.79           N  
ANISOU 7281  N   LEU C  86    11607  11696   8915   -691   -802   -372       N  
ATOM   7282  CA  LEU C  86     -35.692  42.260  36.747  1.00 84.81           C  
ANISOU 7282  CA  LEU C  86    11479  11775   8968   -658   -701   -392       C  
ATOM   7283  C   LEU C  86     -36.349  42.673  35.421  1.00 86.66           C  
ANISOU 7283  C   LEU C  86    11689  12055   9182   -783   -543   -356       C  
ATOM   7284  O   LEU C  86     -35.666  42.773  34.401  1.00 86.80           O  
ANISOU 7284  O   LEU C  86    11547  12175   9258   -825   -462   -366       O  
ATOM   7285  CB  LEU C  86     -35.856  40.745  36.992  1.00 85.03           C  
ANISOU 7285  CB  LEU C  86    11625  11741   8942   -507   -688   -410       C  
ATOM   7286  CG  LEU C  86     -35.130  39.795  36.037  1.00 90.68           C  
ANISOU 7286  CG  LEU C  86    12221  12515   9716   -429   -600   -459       C  
ATOM   7287  CD1 LEU C  86     -33.615  39.825  36.252  1.00 92.60           C  
ANISOU 7287  CD1 LEU C  86    12255  12846  10084   -343   -696   -506       C  
ATOM   7288  CD2 LEU C  86     -35.635  38.387  36.214  1.00 93.46           C  
ANISOU 7288  CD2 LEU C  86    12745  12757  10007   -309   -565   -470       C  
ATOM   7289  N   PHE C  87     -37.665  42.950  35.463  1.00 80.73           N  
ANISOU 7289  N   PHE C  87    11091  11241   8344   -839   -505   -314       N  
ATOM   7290  CA  PHE C  87     -38.455  43.371  34.314  1.00 79.05           C  
ANISOU 7290  CA  PHE C  87    10876  11068   8090   -943   -385   -270       C  
ATOM   7291  C   PHE C  87     -38.249  44.845  33.975  1.00 81.69           C  
ANISOU 7291  C   PHE C  87    11123  11432   8485  -1066   -393   -216       C  
ATOM   7292  O   PHE C  87     -38.043  45.159  32.801  1.00 81.53           O  
ANISOU 7292  O   PHE C  87    11009  11495   8472  -1142   -299   -180       O  
ATOM   7293  CB  PHE C  87     -39.944  43.049  34.528  1.00 79.55           C  
ANISOU 7293  CB  PHE C  87    11113  11061   8051   -944   -351   -253       C  
ATOM   7294  CG  PHE C  87     -40.852  43.529  33.422  1.00 80.42           C  
ANISOU 7294  CG  PHE C  87    11220  11222   8113  -1038   -259   -207       C  
ATOM   7295  CD1 PHE C  87     -41.627  44.672  33.583  1.00 83.03           C  
ANISOU 7295  CD1 PHE C  87    11588  11520   8440  -1102   -284   -150       C  
ATOM   7296  CD2 PHE C  87     -40.916  42.854  32.210  1.00 82.60           C  
ANISOU 7296  CD2 PHE C  87    11457  11582   8344  -1054   -156   -224       C  
ATOM   7297  CE1 PHE C  87     -42.448  45.129  32.550  1.00 83.57           C  
ANISOU 7297  CE1 PHE C  87    11649  11641   8463  -1170   -219    -95       C  
ATOM   7298  CE2 PHE C  87     -41.741  43.312  31.182  1.00 84.99           C  
ANISOU 7298  CE2 PHE C  87    11759  11950   8582  -1135    -92   -178       C  
ATOM   7299  CZ  PHE C  87     -42.507  44.439  31.361  1.00 82.59           C  
ANISOU 7299  CZ  PHE C  87    11488  11615   8278  -1187   -130   -106       C  
ATOM   7300  N   VAL C  88     -38.324  45.749  34.981  1.00 77.09           N  
ANISOU 7300  N   VAL C  88    10584  10770   7936  -1089   -499   -209       N  
ATOM   7301  CA  VAL C  88     -38.150  47.192  34.753  1.00 76.89           C  
ANISOU 7301  CA  VAL C  88    10499  10730   7985  -1209   -513   -161       C  
ATOM   7302  C   VAL C  88     -36.804  47.546  34.108  1.00 81.51           C  
ANISOU 7302  C   VAL C  88    10887  11405   8679  -1282   -490   -160       C  
ATOM   7303  O   VAL C  88     -36.704  48.546  33.402  1.00 81.20           O  
ANISOU 7303  O   VAL C  88    10792  11373   8686  -1403   -438    -92       O  
ATOM   7304  CB  VAL C  88     -38.535  48.126  35.935  1.00 80.42           C  
ANISOU 7304  CB  VAL C  88    11043  11061   8451  -1223   -624   -177       C  
ATOM   7305  CG1 VAL C  88     -40.009  47.990  36.301  1.00 78.75           C  
ANISOU 7305  CG1 VAL C  88    11003  10781   8137  -1179   -600   -163       C  
ATOM   7306  CG2 VAL C  88     -37.633  47.921  37.149  1.00 81.10           C  
ANISOU 7306  CG2 VAL C  88    11107  11134   8573  -1164   -763   -259       C  
ATOM   7307  N   ILE C  89     -35.794  46.686  34.316  1.00 79.01           N  
ANISOU 7307  N   ILE C  89    10464  11156   8401  -1203   -519   -229       N  
ATOM   7308  CA  ILE C  89     -34.455  46.815  33.758  1.00 80.52           C  
ANISOU 7308  CA  ILE C  89    10435  11456   8701  -1251   -488   -249       C  
ATOM   7309  C   ILE C  89     -34.435  46.581  32.233  1.00 83.66           C  
ANISOU 7309  C   ILE C  89    10761  11963   9061  -1303   -308   -205       C  
ATOM   7310  O   ILE C  89     -33.571  47.126  31.551  1.00 84.15           O  
ANISOU 7310  O   ILE C  89    10658  12112   9201  -1405   -239   -184       O  
ATOM   7311  CB  ILE C  89     -33.481  45.910  34.571  1.00 84.94           C  
ANISOU 7311  CB  ILE C  89    10907  12053   9313  -1114   -594   -343       C  
ATOM   7312  CG1 ILE C  89     -32.475  46.741  35.377  1.00 86.92           C  
ANISOU 7312  CG1 ILE C  89    11024  12311   9692  -1170   -735   -387       C  
ATOM   7313  CG2 ILE C  89     -32.805  44.791  33.760  1.00 87.14           C  
ANISOU 7313  CG2 ILE C  89    11059  12444   9604  -1024   -494   -386       C  
ATOM   7314  CD1 ILE C  89     -32.952  47.108  36.781  1.00 95.25           C  
ANISOU 7314  CD1 ILE C  89    12236  13249  10705  -1137   -903   -413       C  
ATOM   7315  N   THR C  90     -35.389  45.781  31.712  1.00 78.93           N  
ANISOU 7315  N   THR C  90    10287  11365   8336  -1244   -230   -196       N  
ATOM   7316  CA  THR C  90     -35.493  45.460  30.286  1.00 78.72           C  
ANISOU 7316  CA  THR C  90    10223  11450   8235  -1282    -69   -171       C  
ATOM   7317  C   THR C  90     -36.307  46.488  29.499  1.00 81.27           C  
ANISOU 7317  C   THR C  90    10614  11770   8494  -1410    -10    -54       C  
ATOM   7318  O   THR C  90     -36.298  46.449  28.270  1.00 81.20           O  
ANISOU 7318  O   THR C  90    10570  11871   8413  -1464    117    -15       O  
ATOM   7319  CB  THR C  90     -36.012  44.024  30.058  1.00 87.11           C  
ANISOU 7319  CB  THR C  90    11375  12521   9202  -1161    -22   -241       C  
ATOM   7320  OG1 THR C  90     -37.384  43.924  30.444  1.00 86.20           O  
ANISOU 7320  OG1 THR C  90    11448  12308   8997  -1148    -61   -215       O  
ATOM   7321  CG2 THR C  90     -35.159  42.961  30.749  1.00 85.97           C  
ANISOU 7321  CG2 THR C  90    11173  12366   9126  -1014    -76   -342       C  
ATOM   7322  N   LEU C  91     -37.007  47.407  30.198  1.00 76.97           N  
ANISOU 7322  N   LEU C  91    10173  11103   7969  -1447   -102      1       N  
ATOM   7323  CA  LEU C  91     -37.829  48.450  29.577  1.00 76.61           C  
ANISOU 7323  CA  LEU C  91    10204  11026   7880  -1541    -70    121       C  
ATOM   7324  C   LEU C  91     -37.092  49.416  28.634  1.00 82.07           C  
ANISOU 7324  C   LEU C  91    10791  11776   8616  -1682     16    219       C  
ATOM   7325  O   LEU C  91     -37.668  49.736  27.592  1.00 82.09           O  
ANISOU 7325  O   LEU C  91    10844  11826   8520  -1733     95    319       O  
ATOM   7326  CB  LEU C  91     -38.721  49.176  30.582  1.00 75.91           C  
ANISOU 7326  CB  LEU C  91    10243  10783   7816  -1527   -181    139       C  
ATOM   7327  CG  LEU C  91     -39.970  48.408  31.036  1.00 79.30           C  
ANISOU 7327  CG  LEU C  91    10809  11174   8147  -1424   -208     97       C  
ATOM   7328  CD1 LEU C  91     -40.470  48.927  32.357  1.00 79.03           C  
ANISOU 7328  CD1 LEU C  91    10870  11002   8155  -1389   -317     70       C  
ATOM   7329  CD2 LEU C  91     -41.076  48.465  29.991  1.00 81.07           C  
ANISOU 7329  CD2 LEU C  91    11094  11449   8261  -1442   -141    172       C  
ATOM   7330  N   PRO C  92     -35.821  49.851  28.891  1.00 79.55           N  
ANISOU 7330  N   PRO C  92    10321  11470   8434  -1755     10    198       N  
ATOM   7331  CA  PRO C  92     -35.126  50.696  27.900  1.00 80.81           C  
ANISOU 7331  CA  PRO C  92    10381  11694   8630  -1910    123    300       C  
ATOM   7332  C   PRO C  92     -35.032  50.041  26.511  1.00 84.61           C  
ANISOU 7332  C   PRO C  92    10820  12353   8975  -1916    289    328       C  
ATOM   7333  O   PRO C  92     -35.047  50.757  25.515  1.00 85.31           O  
ANISOU 7333  O   PRO C  92    10918  12486   9010  -2032    392    457       O  
ATOM   7334  CB  PRO C  92     -33.745  50.923  28.531  1.00 83.84           C  
ANISOU 7334  CB  PRO C  92    10576  12089   9189  -1967     84    225       C  
ATOM   7335  CG  PRO C  92     -33.956  50.741  29.971  1.00 87.23           C  
ANISOU 7335  CG  PRO C  92    11065  12403   9674  -1867    -92    126       C  
ATOM   7336  CD  PRO C  92     -34.961  49.632  30.071  1.00 81.13           C  
ANISOU 7336  CD  PRO C  92    10431  11636   8759  -1709   -103     85       C  
ATOM   7337  N   PHE C  93     -34.990  48.683  26.441  1.00 80.13           N  
ANISOU 7337  N   PHE C  93    10228  11879   8339  -1788    316    208       N  
ATOM   7338  CA  PHE C  93     -34.967  47.930  25.175  1.00 80.34           C  
ANISOU 7338  CA  PHE C  93    10233  12072   8222  -1775    469    196       C  
ATOM   7339  C   PHE C  93     -36.341  48.004  24.495  1.00 82.72           C  
ANISOU 7339  C   PHE C  93    10713  12370   8346  -1774    477    278       C  
ATOM   7340  O   PHE C  93     -36.404  48.144  23.274  1.00 83.30           O  
ANISOU 7340  O   PHE C  93    10794  12568   8288  -1840    597    352       O  
ATOM   7341  CB  PHE C  93     -34.577  46.452  25.385  1.00 81.92           C  
ANISOU 7341  CB  PHE C  93    10374  12334   8418  -1627    483     29       C  
ATOM   7342  CG  PHE C  93     -33.279  46.182  26.107  1.00 84.39           C  
ANISOU 7342  CG  PHE C  93    10502  12661   8900  -1582    449    -68       C  
ATOM   7343  CD1 PHE C  93     -32.060  46.291  25.447  1.00 89.53           C  
ANISOU 7343  CD1 PHE C  93    10946  13459   9613  -1646    577    -85       C  
ATOM   7344  CD2 PHE C  93     -33.277  45.746  27.426  1.00 85.37           C  
ANISOU 7344  CD2 PHE C  93    10653  12670   9113  -1466    290   -147       C  
ATOM   7345  CE1 PHE C  93     -30.860  46.022  26.111  1.00 91.53           C  
ANISOU 7345  CE1 PHE C  93    10999  13745  10035  -1593    533   -185       C  
ATOM   7346  CE2 PHE C  93     -32.079  45.467  28.087  1.00 89.34           C  
ANISOU 7346  CE2 PHE C  93    10979  13202   9764  -1406    235   -236       C  
ATOM   7347  CZ  PHE C  93     -30.878  45.611  27.427  1.00 89.61           C  
ANISOU 7347  CZ  PHE C  93    10786  13385   9877  -1467    351   -259       C  
ATOM   7348  N   TRP C  94     -37.435  47.902  25.296  1.00 77.05           N  
ANISOU 7348  N   TRP C  94    10131  11524   7619  -1698    350    263       N  
ATOM   7349  CA  TRP C  94     -38.830  47.992  24.854  1.00 75.94           C  
ANISOU 7349  CA  TRP C  94    10140  11373   7342  -1684    325    327       C  
ATOM   7350  C   TRP C  94     -39.108  49.365  24.227  1.00 80.65           C  
ANISOU 7350  C   TRP C  94    10780  11951   7914  -1792    338    509       C  
ATOM   7351  O   TRP C  94     -39.783  49.436  23.196  1.00 81.71           O  
ANISOU 7351  O   TRP C  94    10981  12174   7892  -1810    381    589       O  
ATOM   7352  CB  TRP C  94     -39.786  47.810  26.043  1.00 73.00           C  
ANISOU 7352  CB  TRP C  94     9870  10856   7010  -1597    193    277       C  
ATOM   7353  CG  TRP C  94     -40.002  46.403  26.510  1.00 73.36           C  
ANISOU 7353  CG  TRP C  94     9941  10903   7029  -1489    179    132       C  
ATOM   7354  CD1 TRP C  94     -39.143  45.640  27.246  1.00 76.23           C  
ANISOU 7354  CD1 TRP C  94    10244  11242   7480  -1420    163     24       C  
ATOM   7355  CD2 TRP C  94     -41.225  45.660  26.424  1.00 72.04           C  
ANISOU 7355  CD2 TRP C  94     9879  10735   6757  -1438    164     87       C  
ATOM   7356  NE1 TRP C  94     -39.737  44.443  27.576  1.00 75.01           N  
ANISOU 7356  NE1 TRP C  94    10169  11056   7274  -1328    149    -74       N  
ATOM   7357  CE2 TRP C  94     -41.011  44.423  27.071  1.00 75.57           C  
ANISOU 7357  CE2 TRP C  94    10338  11144   7232  -1350    157    -44       C  
ATOM   7358  CE3 TRP C  94     -42.475  45.908  25.835  1.00 72.87           C  
ANISOU 7358  CE3 TRP C  94    10062  10873   6752  -1459    152    144       C  
ATOM   7359  CZ2 TRP C  94     -41.996  43.432  27.134  1.00 74.00           C  
ANISOU 7359  CZ2 TRP C  94    10232  10925   6958  -1306    155   -118       C  
ATOM   7360  CZ3 TRP C  94     -43.452  44.930  25.906  1.00 73.68           C  
ANISOU 7360  CZ3 TRP C  94    10232  10979   6784  -1414    141     57       C  
ATOM   7361  CH2 TRP C  94     -43.209  43.707  26.547  1.00 73.78           C  
ANISOU 7361  CH2 TRP C  94    10262  10940   6831  -1349    150    -73       C  
ATOM   7362  N   ALA C  95     -38.601  50.451  24.865  1.00 76.16           N  
ANISOU 7362  N   ALA C  95    10182  11256   7499  -1861    291    574       N  
ATOM   7363  CA  ALA C  95     -38.771  51.831  24.409  1.00 76.38           C  
ANISOU 7363  CA  ALA C  95    10265  11214   7543  -1965    298    754       C  
ATOM   7364  C   ALA C  95     -38.061  52.060  23.077  1.00 81.30           C  
ANISOU 7364  C   ALA C  95    10828  11985   8077  -2080    454    859       C  
ATOM   7365  O   ALA C  95     -38.678  52.602  22.161  1.00 81.96           O  
ANISOU 7365  O   ALA C  95    11009  12100   8034  -2115    484   1009       O  
ATOM   7366  CB  ALA C  95     -38.253  52.803  25.457  1.00 77.36           C  
ANISOU 7366  CB  ALA C  95    10365  11160   7869  -2023    218    760       C  
ATOM   7367  N   VAL C  96     -36.778  51.618  22.967  1.00 77.80           N  
ANISOU 7367  N   VAL C  96    10224  11646   7692  -2129    554    779       N  
ATOM   7368  CA  VAL C  96     -35.930  51.737  21.771  1.00 79.17           C  
ANISOU 7368  CA  VAL C  96    10310  11983   7787  -2244    734    853       C  
ATOM   7369  C   VAL C  96     -36.579  51.044  20.571  1.00 83.46           C  
ANISOU 7369  C   VAL C  96    10932  12700   8077  -2198    816    868       C  
ATOM   7370  O   VAL C  96     -36.731  51.677  19.528  1.00 84.56           O  
ANISOU 7370  O   VAL C  96    11138  12909   8083  -2286    900   1031       O  
ATOM   7371  CB  VAL C  96     -34.461  51.275  22.019  1.00 83.37           C  
ANISOU 7371  CB  VAL C  96    10622  12604   8452  -2278    819    728       C  
ATOM   7372  CG1 VAL C  96     -33.688  51.110  20.707  1.00 85.19           C  
ANISOU 7372  CG1 VAL C  96    10754  13048   8566  -2369   1035    767       C  
ATOM   7373  CG2 VAL C  96     -33.733  52.243  22.944  1.00 83.68           C  
ANISOU 7373  CG2 VAL C  96    10573  12495   8725  -2379    750    747       C  
ATOM   7374  N   ASP C  97     -36.978  49.766  20.734  1.00 79.12           N  
ANISOU 7374  N   ASP C  97    10390  12213   7460  -2065    786    700       N  
ATOM   7375  CA  ASP C  97     -37.636  48.958  19.705  1.00 79.73           C  
ANISOU 7375  CA  ASP C  97    10541  12449   7304  -2016    844    665       C  
ATOM   7376  C   ASP C  97     -38.840  49.697  19.076  1.00 84.42           C  
ANISOU 7376  C   ASP C  97    11296  13034   7745  -2037    782    834       C  
ATOM   7377  O   ASP C  97     -38.925  49.794  17.844  1.00 85.43           O  
ANISOU 7377  O   ASP C  97    11469  13320   7672  -2089    876    922       O  
ATOM   7378  CB  ASP C  97     -38.046  47.586  20.285  1.00 80.41           C  
ANISOU 7378  CB  ASP C  97    10635  12523   7393  -1875    781    459       C  
ATOM   7379  CG  ASP C  97     -38.884  46.720  19.359  1.00 95.41           C  
ANISOU 7379  CG  ASP C  97    12625  14557   9071  -1829    810    395       C  
ATOM   7380  OD1 ASP C  97     -40.125  46.884  19.356  1.00 96.27           O  
ANISOU 7380  OD1 ASP C  97    12851  14625   9101  -1805    703    443       O  
ATOM   7381  OD2 ASP C  97     -38.304  45.854  18.666  1.00102.78           O  
ANISOU 7381  OD2 ASP C  97    13501  15636   9913  -1815    937    279       O  
ATOM   7382  N   ALA C  98     -39.726  50.253  19.935  1.00 79.99           N  
ANISOU 7382  N   ALA C  98    10818  12295   7281  -1991    624    881       N  
ATOM   7383  CA  ALA C  98     -40.936  50.990  19.560  1.00 79.96           C  
ANISOU 7383  CA  ALA C  98    10950  12253   7180  -1976    533   1032       C  
ATOM   7384  C   ALA C  98     -40.683  52.214  18.661  1.00 86.73           C  
ANISOU 7384  C   ALA C  98    11860  13121   7971  -2087    596   1269       C  
ATOM   7385  O   ALA C  98     -41.462  52.459  17.740  1.00 87.18           O  
ANISOU 7385  O   ALA C  98    12019  13265   7840  -2076    577   1390       O  
ATOM   7386  CB  ALA C  98     -41.700  51.401  20.807  1.00 78.92           C  
ANISOU 7386  CB  ALA C  98    10865  11913   7208  -1903    377   1016       C  
ATOM   7387  N   VAL C  99     -39.608  52.973  18.918  1.00 84.73           N  
ANISOU 7387  N   VAL C  99    11540  12783   7871  -2199    668   1338       N  
ATOM   7388  CA  VAL C  99     -39.305  54.165  18.130  1.00 87.11           C  
ANISOU 7388  CA  VAL C  99    11902  13063   8132  -2326    743   1576       C  
ATOM   7389  C   VAL C  99     -38.378  53.850  16.975  1.00 94.66           C  
ANISOU 7389  C   VAL C  99    12794  14241   8932  -2430    945   1606       C  
ATOM   7390  O   VAL C  99     -38.704  54.155  15.827  1.00 96.25           O  
ANISOU 7390  O   VAL C  99    13098  14558   8913  -2467   1003   1766       O  
ATOM   7391  CB  VAL C  99     -38.727  55.344  18.953  1.00 91.42           C  
ANISOU 7391  CB  VAL C  99    12430  13374   8931  -2421    716   1660       C  
ATOM   7392  CG1 VAL C  99     -39.061  56.669  18.296  1.00 93.19           C  
ANISOU 7392  CG1 VAL C  99    12800  13494   9115  -2499    720   1932       C  
ATOM   7393  CG2 VAL C  99     -39.195  55.330  20.398  1.00 89.16           C  
ANISOU 7393  CG2 VAL C  99    12143  12896   8837  -2321    550   1528       C  
ATOM   7394  N   ALA C 100     -37.247  53.203  17.238  1.00 92.26           N  
ANISOU 7394  N   ALA C 100    12320  14014   8722  -2467   1053   1450       N  
ATOM   7395  CA  ALA C 100     -36.247  52.998  16.187  1.00 94.59           C  
ANISOU 7395  CA  ALA C 100    12528  14518   8893  -2575   1273   1473       C  
ATOM   7396  C   ALA C 100     -36.100  51.489  16.451  1.00 98.63           C  
ANISOU 7396  C   ALA C 100    12937  15151   9389  -2447   1280   1202       C  
ATOM   7397  O   ALA C 100     -36.847  50.905  17.235  1.00 96.89           O  
ANISOU 7397  O   ALA C 100    12753  14839   9220  -2315   1127   1078       O  
ATOM   7398  CB  ALA C 100     -34.859  53.370  16.707  1.00 96.21           C  
ANISOU 7398  CB  ALA C 100    12547  14676   9333  -2699   1371   1443       C  
ATOM   7399  N   ASN C 101     -35.138  50.879  15.767  1.00 97.01           N  
ANISOU 7399  N   ASN C 101    12607  15143   9109  -2487   1470   1116       N  
ATOM   7400  CA  ASN C 101     -35.047  49.435  15.565  1.00 96.46           C  
ANISOU 7400  CA  ASN C 101    12478  15223   8949  -2367   1520    883       C  
ATOM   7401  C   ASN C 101     -34.478  48.501  16.643  1.00 99.24           C  
ANISOU 7401  C   ASN C 101    12680  15511   9514  -2255   1471    654       C  
ATOM   7402  O   ASN C 101     -34.028  48.977  17.690  1.00 98.07           O  
ANISOU 7402  O   ASN C 101    12447  15211   9605  -2274   1389    659       O  
ATOM   7403  CB  ASN C 101     -33.995  49.664  14.434  1.00100.50           C  
ANISOU 7403  CB  ASN C 101    12898  15943   9343  -2500   1773    950       C  
ATOM   7404  CG  ASN C 101     -33.488  48.460  13.689  1.00123.25           C  
ANISOU 7404  CG  ASN C 101    15697  19053  12078  -2439   1939    755       C  
ATOM   7405  OD1 ASN C 101     -34.214  47.830  12.913  1.00116.92           O  
ANISOU 7405  OD1 ASN C 101    15021  18374  11028  -2378   1946    702       O  
ATOM   7406  ND2 ASN C 101     -32.193  48.188  13.831  1.00115.35           N  
ANISOU 7406  ND2 ASN C 101    14477  18128  11224  -2464   2087    648       N  
ATOM   7407  N   TRP C 102     -34.488  47.182  16.392  1.00 96.04           N  
ANISOU 7407  N   TRP C 102    12254  15216   9021  -2137   1516    452       N  
ATOM   7408  CA  TRP C 102     -33.895  46.235  17.326  1.00 95.40           C  
ANISOU 7408  CA  TRP C 102    12042  15076   9129  -2015   1478    247       C  
ATOM   7409  C   TRP C 102     -32.403  46.052  16.992  1.00101.79           C  
ANISOU 7409  C   TRP C 102    12626  16031  10018  -2051   1670    172       C  
ATOM   7410  O   TRP C 102     -32.055  45.300  16.079  1.00102.88           O  
ANISOU 7410  O   TRP C 102    12725  16352  10013  -2019   1834     64       O  
ATOM   7411  CB  TRP C 102     -34.649  44.897  17.362  1.00 93.13           C  
ANISOU 7411  CB  TRP C 102    11850  14786   8750  -1864   1420     65       C  
ATOM   7412  CG  TRP C 102     -34.130  44.002  18.447  1.00 93.43           C  
ANISOU 7412  CG  TRP C 102    11789  14718   8992  -1727   1355   -110       C  
ATOM   7413  CD1 TRP C 102     -33.151  43.059  18.332  1.00 97.62           C  
ANISOU 7413  CD1 TRP C 102    12177  15333   9580  -1638   1467   -283       C  
ATOM   7414  CD2 TRP C 102     -34.453  44.078  19.843  1.00 91.42           C  
ANISOU 7414  CD2 TRP C 102    11562  14255   8919  -1664   1164   -112       C  
ATOM   7415  NE1 TRP C 102     -32.874  42.512  19.562  1.00 96.18           N  
ANISOU 7415  NE1 TRP C 102    11940  15002   9601  -1513   1342   -381       N  
ATOM   7416  CE2 TRP C 102     -33.662  43.116  20.509  1.00 95.62           C  
ANISOU 7416  CE2 TRP C 102    11979  14756   9598  -1533   1158   -278       C  
ATOM   7417  CE3 TRP C 102     -35.370  44.836  20.595  1.00 90.93           C  
ANISOU 7417  CE3 TRP C 102    11620  14032   8899  -1692    999      6       C  
ATOM   7418  CZ2 TRP C 102     -33.764  42.887  21.888  1.00 93.35           C  
ANISOU 7418  CZ2 TRP C 102    11706  14288   9474  -1439    988   -317       C  
ATOM   7419  CZ3 TRP C 102     -35.459  44.617  21.962  1.00 90.82           C  
ANISOU 7419  CZ3 TRP C 102    11611  13847   9050  -1606    848    -49       C  
ATOM   7420  CH2 TRP C 102     -34.658  43.658  22.594  1.00 91.56           C  
ANISOU 7420  CH2 TRP C 102    11603  13920   9266  -1485    841   -202       C  
ATOM   7421  N   TYR C 103     -31.531  46.757  17.732  1.00 98.78           N  
ANISOU 7421  N   TYR C 103    12088  15576   9866  -2120   1649    219       N  
ATOM   7422  CA  TYR C 103     -30.079  46.716  17.544  1.00100.90           C  
ANISOU 7422  CA  TYR C 103    12101  15981  10255  -2168   1816    154       C  
ATOM   7423  C   TYR C 103     -29.409  45.589  18.340  1.00103.36           C  
ANISOU 7423  C   TYR C 103    12252  16281  10738  -1988   1767    -72       C  
ATOM   7424  O   TYR C 103     -28.357  45.087  17.939  1.00105.26           O  
ANISOU 7424  O   TYR C 103    12289  16682  11022  -1959   1928   -189       O  
ATOM   7425  CB  TYR C 103     -29.442  48.061  17.950  1.00103.38           C  
ANISOU 7425  CB  TYR C 103    12308  16224  10749  -2350   1808    309       C  
ATOM   7426  CG  TYR C 103     -29.958  49.278  17.208  1.00106.31           C  
ANISOU 7426  CG  TYR C 103    12832  16576  10984  -2532   1862    557       C  
ATOM   7427  CD1 TYR C 103     -30.808  50.188  17.830  1.00106.76           C  
ANISOU 7427  CD1 TYR C 103    13054  16415  11093  -2572   1681    700       C  
ATOM   7428  CD2 TYR C 103     -29.549  49.551  15.905  1.00109.76           C  
ANISOU 7428  CD2 TYR C 103    13250  17210  11245  -2660   2100    653       C  
ATOM   7429  CE1 TYR C 103     -31.262  51.327  17.163  1.00108.58           C  
ANISOU 7429  CE1 TYR C 103    13433  16608  11217  -2722   1722    939       C  
ATOM   7430  CE2 TYR C 103     -30.006  50.678  15.223  1.00111.75           C  
ANISOU 7430  CE2 TYR C 103    13661  17433  11365  -2821   2145    905       C  
ATOM   7431  CZ  TYR C 103     -30.861  51.565  15.858  1.00117.51           C  
ANISOU 7431  CZ  TYR C 103    14557  17927  12164  -2845   1948   1050       C  
ATOM   7432  OH  TYR C 103     -31.310  52.680  15.193  1.00119.94           O  
ANISOU 7432  OH  TYR C 103    15030  18186  12354  -2984   1983   1308       O  
ATOM   7433  N   PHE C 104     -30.030  45.206  19.465  1.00 96.31           N  
ANISOU 7433  N   PHE C 104    11454  15199   9939  -1863   1549   -127       N  
ATOM   7434  CA  PHE C 104     -29.583  44.246  20.481  1.00 94.97           C  
ANISOU 7434  CA  PHE C 104    11188  14957   9940  -1680   1439   -300       C  
ATOM   7435  C   PHE C 104     -29.308  42.783  20.083  1.00 98.11           C  
ANISOU 7435  C   PHE C 104    11547  15443  10288  -1501   1532   -502       C  
ATOM   7436  O   PHE C 104     -28.687  42.048  20.858  1.00 97.28           O  
ANISOU 7436  O   PHE C 104    11324  15291  10346  -1347   1462   -633       O  
ATOM   7437  CB  PHE C 104     -30.439  44.380  21.753  1.00 94.37           C  
ANISOU 7437  CB  PHE C 104    11265  14653   9940  -1622   1193   -268       C  
ATOM   7438  CG  PHE C 104     -30.905  45.801  21.983  1.00 95.63           C  
ANISOU 7438  CG  PHE C 104    11505  14714  10116  -1789   1117    -80       C  
ATOM   7439  CD1 PHE C 104     -32.200  46.188  21.654  1.00 97.52           C  
ANISOU 7439  CD1 PHE C 104    11972  14886  10196  -1830   1073     34       C  
ATOM   7440  CD2 PHE C 104     -30.024  46.774  22.455  1.00 98.90           C  
ANISOU 7440  CD2 PHE C 104    11759  15108  10709  -1908   1096    -21       C  
ATOM   7441  CE1 PHE C 104     -32.616  47.515  21.824  1.00 98.14           C  
ANISOU 7441  CE1 PHE C 104    12129  14861  10300  -1965   1009    208       C  
ATOM   7442  CE2 PHE C 104     -30.441  48.102  22.617  1.00101.38           C  
ANISOU 7442  CE2 PHE C 104    12163  15309  11048  -2064   1037    147       C  
ATOM   7443  CZ  PHE C 104     -31.733  48.460  22.305  1.00 98.16           C  
ANISOU 7443  CZ  PHE C 104    11993  14819  10484  -2081    995    263       C  
ATOM   7444  N   GLY C 105     -29.723  42.388  18.886  1.00 95.32           N  
ANISOU 7444  N   GLY C 105    11290  15215   9713  -1517   1685   -528       N  
ATOM   7445  CA  GLY C 105     -29.467  41.048  18.368  1.00 96.44           C  
ANISOU 7445  CA  GLY C 105    11409  15441   9794  -1361   1798   -734       C  
ATOM   7446  C   GLY C 105     -30.366  39.935  18.862  1.00 99.20           C  
ANISOU 7446  C   GLY C 105    11946  15628  10118  -1201   1665   -849       C  
ATOM   7447  O   GLY C 105     -31.330  40.180  19.591  1.00 96.66           O  
ANISOU 7447  O   GLY C 105    11786  15139   9802  -1214   1487   -765       O  
ATOM   7448  N   ASN C 106     -30.037  38.692  18.456  1.00 97.39           N  
ANISOU 7448  N   ASN C 106    11693  15444   9868  -1050   1766  -1050       N  
ATOM   7449  CA  ASN C 106     -30.783  37.467  18.754  1.00 96.36           C  
ANISOU 7449  CA  ASN C 106    11739  15160   9712   -902   1683  -1188       C  
ATOM   7450  C   ASN C 106     -30.776  37.032  20.215  1.00 98.82           C  
ANISOU 7450  C   ASN C 106    12068  15248  10232   -762   1484  -1202       C  
ATOM   7451  O   ASN C 106     -31.815  36.582  20.708  1.00 96.71           O  
ANISOU 7451  O   ASN C 106    12005  14811   9929   -731   1359  -1202       O  
ATOM   7452  CB  ASN C 106     -30.325  36.327  17.853  1.00100.83           C  
ANISOU 7452  CB  ASN C 106    12273  15830  10208   -785   1865  -1405       C  
ATOM   7453  CG  ASN C 106     -31.462  35.542  17.255  1.00127.45           C  
ANISOU 7453  CG  ASN C 106    15885  19156  13384   -781   1870  -1503       C  
ATOM   7454  OD1 ASN C 106     -32.191  36.019  16.377  1.00122.98           O  
ANISOU 7454  OD1 ASN C 106    15429  18705  12593   -926   1916  -1437       O  
ATOM   7455  ND2 ASN C 106     -31.622  34.309  17.701  1.00119.55           N  
ANISOU 7455  ND2 ASN C 106    14971  17987  12466   -616   1819  -1664       N  
ATOM   7456  N   PHE C 107     -29.612  37.136  20.901  1.00 96.23           N  
ANISOU 7456  N   PHE C 107    11523  14927  10114   -679   1453  -1217       N  
ATOM   7457  CA  PHE C 107     -29.481  36.743  22.309  1.00 94.82           C  
ANISOU 7457  CA  PHE C 107    11352  14556  10119   -534   1254  -1223       C  
ATOM   7458  C   PHE C 107     -30.359  37.570  23.232  1.00 96.69           C  
ANISOU 7458  C   PHE C 107    11730  14653  10354   -637   1066  -1060       C  
ATOM   7459  O   PHE C 107     -31.173  36.992  23.950  1.00 94.81           O  
ANISOU 7459  O   PHE C 107    11682  14235  10109   -563    941  -1066       O  
ATOM   7460  CB  PHE C 107     -28.015  36.744  22.793  1.00 98.21           C  
ANISOU 7460  CB  PHE C 107    11495  15057  10765   -425   1247  -1277       C  
ATOM   7461  CG  PHE C 107     -27.882  36.552  24.289  1.00 98.62           C  
ANISOU 7461  CG  PHE C 107    11558  14932  10981   -295   1012  -1251       C  
ATOM   7462  CD1 PHE C 107     -27.616  37.632  25.125  1.00100.90           C  
ANISOU 7462  CD1 PHE C 107    11756  15215  11366   -394    872  -1129       C  
ATOM   7463  CD2 PHE C 107     -28.096  35.306  24.870  1.00100.40           C  
ANISOU 7463  CD2 PHE C 107    11916  14984  11247    -84    927  -1342       C  
ATOM   7464  CE1 PHE C 107     -27.539  37.463  26.511  1.00101.04           C  
ANISOU 7464  CE1 PHE C 107    11806  15083  11500   -277    647  -1108       C  
ATOM   7465  CE2 PHE C 107     -28.013  35.139  26.255  1.00102.42           C  
ANISOU 7465  CE2 PHE C 107    12211  15082  11623     35    709  -1298       C  
ATOM   7466  CZ  PHE C 107     -27.734  36.217  27.064  1.00 99.93           C  
ANISOU 7466  CZ  PHE C 107    11798  14789  11382    -60    568  -1185       C  
ATOM   7467  N   LEU C 108     -30.180  38.911  23.225  1.00 93.60           N  
ANISOU 7467  N   LEU C 108    11248  14338   9976   -809   1056   -918       N  
ATOM   7468  CA  LEU C 108     -30.944  39.844  24.058  1.00 91.83           C  
ANISOU 7468  CA  LEU C 108    11143  13989   9759   -911    891   -770       C  
ATOM   7469  C   LEU C 108     -32.442  39.800  23.769  1.00 94.22           C  
ANISOU 7469  C   LEU C 108    11700  14214   9885   -970    869   -718       C  
ATOM   7470  O   LEU C 108     -33.232  40.045  24.683  1.00 92.13           O  
ANISOU 7470  O   LEU C 108    11570  13800   9636   -975    718   -651       O  
ATOM   7471  CB  LEU C 108     -30.409  41.289  23.959  1.00 92.61           C  
ANISOU 7471  CB  LEU C 108    11099  14176   9915  -1090    909   -641       C  
ATOM   7472  CG  LEU C 108     -29.169  41.693  24.797  1.00 98.59           C  
ANISOU 7472  CG  LEU C 108    11621  14950  10890  -1072    830   -656       C  
ATOM   7473  CD1 LEU C 108     -29.198  41.112  26.220  1.00 97.69           C  
ANISOU 7473  CD1 LEU C 108    11558  14674  10885   -906    617   -708       C  
ATOM   7474  CD2 LEU C 108     -27.872  41.360  24.084  1.00104.22           C  
ANISOU 7474  CD2 LEU C 108    12067  15854  11676  -1039    997   -756       C  
ATOM   7475  N   CYS C 109     -32.829  39.443  22.517  1.00 91.27           N  
ANISOU 7475  N   CYS C 109    11384  13953   9341  -1010   1018   -762       N  
ATOM   7476  CA  CYS C 109     -34.218  39.282  22.070  1.00 89.88           C  
ANISOU 7476  CA  CYS C 109    11422  13741   8988  -1063   1003   -740       C  
ATOM   7477  C   CYS C 109     -34.910  38.188  22.893  1.00 92.07           C  
ANISOU 7477  C   CYS C 109    11850  13832   9299   -939    896   -830       C  
ATOM   7478  O   CYS C 109     -36.059  38.355  23.298  1.00 89.96           O  
ANISOU 7478  O   CYS C 109    11737  13464   8981   -984    798   -768       O  
ATOM   7479  CB  CYS C 109     -34.259  38.967  20.578  1.00 91.81           C  
ANISOU 7479  CB  CYS C 109    11674  14166   9045  -1110   1181   -806       C  
ATOM   7480  SG  CYS C 109     -35.925  38.800  19.888  1.00 94.87           S  
ANISOU 7480  SG  CYS C 109    12294  14553   9200  -1187   1151   -792       S  
ATOM   7481  N   LYS C 110     -34.187  37.083  23.153  1.00 89.09           N  
ANISOU 7481  N   LYS C 110    11424  13407   9019   -780    922   -972       N  
ATOM   7482  CA  LYS C 110     -34.655  35.952  23.951  1.00 88.05           C  
ANISOU 7482  CA  LYS C 110    11437  13080   8940   -650    836  -1053       C  
ATOM   7483  C   LYS C 110     -34.716  36.341  25.439  1.00 90.40           C  
ANISOU 7483  C   LYS C 110    11762  13226   9359   -614    656   -952       C  
ATOM   7484  O   LYS C 110     -35.692  36.009  26.115  1.00 88.52           O  
ANISOU 7484  O   LYS C 110    11700  12836   9097   -610    568   -929       O  
ATOM   7485  CB  LYS C 110     -33.730  34.733  23.762  1.00 92.16           C  
ANISOU 7485  CB  LYS C 110    11890  13587   9542   -472    917  -1223       C  
ATOM   7486  CG  LYS C 110     -33.631  34.222  22.333  1.00102.62           C  
ANISOU 7486  CG  LYS C 110    13197  15054  10739   -488   1104  -1358       C  
ATOM   7487  CD  LYS C 110     -32.745  32.992  22.249  1.00110.64           C  
ANISOU 7487  CD  LYS C 110    14155  16027  11858   -288   1180  -1540       C  
ATOM   7488  CE  LYS C 110     -32.498  32.554  20.829  1.00120.40           C  
ANISOU 7488  CE  LYS C 110    15354  17427  12967   -297   1384  -1694       C  
ATOM   7489  NZ  LYS C 110     -33.722  31.997  20.197  1.00127.04           N  
ANISOU 7489  NZ  LYS C 110    16415  18219  13633   -377   1408  -1769       N  
ATOM   7490  N   ALA C 111     -33.671  37.050  25.934  1.00 87.09           N  
ANISOU 7490  N   ALA C 111    11166  12861   9065   -599    608   -900       N  
ATOM   7491  CA  ALA C 111     -33.533  37.501  27.321  1.00 85.78           C  
ANISOU 7491  CA  ALA C 111    11002  12583   9007   -566    433   -822       C  
ATOM   7492  C   ALA C 111     -34.665  38.432  27.747  1.00 87.24           C  
ANISOU 7492  C   ALA C 111    11323  12703   9119   -700    350   -696       C  
ATOM   7493  O   ALA C 111     -35.218  38.239  28.826  1.00 85.49           O  
ANISOU 7493  O   ALA C 111    11233  12335   8912   -653    229   -668       O  
ATOM   7494  CB  ALA C 111     -32.184  38.170  27.530  1.00 87.86           C  
ANISOU 7494  CB  ALA C 111    11021  12953   9407   -559    412   -810       C  
ATOM   7495  N   VAL C 112     -35.032  39.414  26.895  1.00 83.65           N  
ANISOU 7495  N   VAL C 112    10845  12356   8581   -858    420   -619       N  
ATOM   7496  CA  VAL C 112     -36.132  40.342  27.190  1.00 81.82           C  
ANISOU 7496  CA  VAL C 112    10732  12067   8288   -971    349   -503       C  
ATOM   7497  C   VAL C 112     -37.471  39.614  27.185  1.00 85.25           C  
ANISOU 7497  C   VAL C 112    11359  12416   8616   -959    341   -531       C  
ATOM   7498  O   VAL C 112     -38.358  39.963  27.962  1.00 83.54           O  
ANISOU 7498  O   VAL C 112    11254  12097   8390   -983    249   -471       O  
ATOM   7499  CB  VAL C 112     -36.159  41.625  26.317  1.00 85.58           C  
ANISOU 7499  CB  VAL C 112    11143  12660   8713  -1129    411   -394       C  
ATOM   7500  CG1 VAL C 112     -34.953  42.514  26.592  1.00 86.38           C  
ANISOU 7500  CG1 VAL C 112    11066  12807   8949  -1175    397   -351       C  
ATOM   7501  CG2 VAL C 112     -36.276  41.305  24.830  1.00 86.28           C  
ANISOU 7501  CG2 VAL C 112    11223  12899   8661  -1175    567   -424       C  
ATOM   7502  N   HIS C 113     -37.602  38.591  26.315  1.00 83.04           N  
ANISOU 7502  N   HIS C 113    11111  12181   8260   -926    445   -635       N  
ATOM   7503  CA  HIS C 113     -38.806  37.777  26.174  1.00 82.44           C  
ANISOU 7503  CA  HIS C 113    11199  12034   8091   -932    452   -689       C  
ATOM   7504  C   HIS C 113     -39.003  36.864  27.379  1.00 86.84           C  
ANISOU 7504  C   HIS C 113    11870  12401   8724   -825    373   -729       C  
ATOM   7505  O   HIS C 113     -40.122  36.772  27.892  1.00 85.60           O  
ANISOU 7505  O   HIS C 113    11846  12149   8530   -865    324   -700       O  
ATOM   7506  CB  HIS C 113     -38.772  36.978  24.863  1.00 84.30           C  
ANISOU 7506  CB  HIS C 113    11431  12374   8224   -936    585   -809       C  
ATOM   7507  CG  HIS C 113     -39.378  37.714  23.708  1.00 87.66           C  
ANISOU 7507  CG  HIS C 113    11853  12960   8496  -1069    638   -755       C  
ATOM   7508  ND1 HIS C 113     -38.687  38.714  23.044  1.00 90.03           N  
ANISOU 7508  ND1 HIS C 113    12029  13410   8769  -1134    696   -671       N  
ATOM   7509  CD2 HIS C 113     -40.604  37.586  23.149  1.00 88.81           C  
ANISOU 7509  CD2 HIS C 113    12101  13134   8508  -1146    633   -767       C  
ATOM   7510  CE1 HIS C 113     -39.506  39.150  22.103  1.00 89.35           C  
ANISOU 7510  CE1 HIS C 113    11994  13434   8521  -1235    721   -623       C  
ATOM   7511  NE2 HIS C 113     -40.670  38.502  22.125  1.00 89.03           N  
ANISOU 7511  NE2 HIS C 113    12080  13335   8413  -1241    676   -684       N  
ATOM   7512  N   VAL C 114     -37.912  36.216  27.849  1.00 84.67           N  
ANISOU 7512  N   VAL C 114    11539  12075   8557   -687    361   -787       N  
ATOM   7513  CA  VAL C 114     -37.968  35.317  29.005  1.00 84.24           C  
ANISOU 7513  CA  VAL C 114    11605  11834   8570   -567    281   -806       C  
ATOM   7514  C   VAL C 114     -38.281  36.036  30.303  1.00 86.77           C  
ANISOU 7514  C   VAL C 114    11980  12074   8916   -580    148   -694       C  
ATOM   7515  O   VAL C 114     -39.154  35.580  31.037  1.00 86.25           O  
ANISOU 7515  O   VAL C 114    12078  11872   8819   -578    110   -674       O  
ATOM   7516  CB  VAL C 114     -36.835  34.256  29.125  1.00 89.74           C  
ANISOU 7516  CB  VAL C 114    12254  12478   9368   -386    296   -902       C  
ATOM   7517  CG1 VAL C 114     -36.814  33.327  27.916  1.00 90.64           C  
ANISOU 7517  CG1 VAL C 114    12374  12626   9438   -367    440  -1041       C  
ATOM   7518  CG2 VAL C 114     -35.468  34.887  29.358  1.00 90.52           C  
ANISOU 7518  CG2 VAL C 114    12142  12679   9573   -319    249   -880       C  
ATOM   7519  N   ILE C 115     -37.617  37.188  30.552  1.00 82.84           N  
ANISOU 7519  N   ILE C 115    11347  11661   8468   -612     88   -627       N  
ATOM   7520  CA  ILE C 115     -37.808  38.039  31.736  1.00 81.66           C  
ANISOU 7520  CA  ILE C 115    11234  11452   8340   -633    -41   -539       C  
ATOM   7521  C   ILE C 115     -39.266  38.536  31.823  1.00 84.70           C  
ANISOU 7521  C   ILE C 115    11750  11800   8633   -747    -36   -480       C  
ATOM   7522  O   ILE C 115     -39.846  38.519  32.908  1.00 83.63           O  
ANISOU 7522  O   ILE C 115    11737  11556   8481   -728   -109   -446       O  
ATOM   7523  CB  ILE C 115     -36.741  39.170  31.777  1.00 85.14           C  
ANISOU 7523  CB  ILE C 115    11487  11996   8866   -667    -90   -504       C  
ATOM   7524  CG1 ILE C 115     -35.355  38.599  32.156  1.00 86.97           C  
ANISOU 7524  CG1 ILE C 115    11592  12244   9209   -523   -142   -564       C  
ATOM   7525  CG2 ILE C 115     -37.141  40.292  32.730  1.00 85.14           C  
ANISOU 7525  CG2 ILE C 115    11533  11947   8869   -734   -202   -425       C  
ATOM   7526  CD1 ILE C 115     -34.132  39.452  31.747  1.00 94.26           C  
ANISOU 7526  CD1 ILE C 115    12269  13313  10232   -570   -134   -568       C  
ATOM   7527  N   TYR C 116     -39.865  38.911  30.673  1.00 81.95           N  
ANISOU 7527  N   TYR C 116    11373  11547   8215   -854     52   -473       N  
ATOM   7528  CA  TYR C 116     -41.261  39.349  30.561  1.00 81.29           C  
ANISOU 7528  CA  TYR C 116    11382  11456   8051   -951     58   -427       C  
ATOM   7529  C   TYR C 116     -42.217  38.211  30.951  1.00 85.11           C  
ANISOU 7529  C   TYR C 116    12017  11830   8491   -929     78   -478       C  
ATOM   7530  O   TYR C 116     -43.221  38.462  31.612  1.00 84.03           O  
ANISOU 7530  O   TYR C 116    11968  11633   8327   -967     46   -439       O  
ATOM   7531  CB  TYR C 116     -41.556  39.854  29.135  1.00 83.20           C  
ANISOU 7531  CB  TYR C 116    11554  11842   8217  -1049    137   -411       C  
ATOM   7532  CG  TYR C 116     -43.018  40.118  28.835  1.00 85.05           C  
ANISOU 7532  CG  TYR C 116    11862  12088   8363  -1129    140   -380       C  
ATOM   7533  CD1 TYR C 116     -43.687  41.194  29.411  1.00 86.41           C  
ANISOU 7533  CD1 TYR C 116    12055  12229   8549  -1166     72   -291       C  
ATOM   7534  CD2 TYR C 116     -43.717  39.325  27.931  1.00 86.40           C  
ANISOU 7534  CD2 TYR C 116    12071  12314   8444  -1166    206   -452       C  
ATOM   7535  CE1 TYR C 116     -45.021  41.462  29.113  1.00 87.10           C  
ANISOU 7535  CE1 TYR C 116    12183  12342   8568  -1223     70   -266       C  
ATOM   7536  CE2 TYR C 116     -45.055  39.578  27.630  1.00 87.13           C  
ANISOU 7536  CE2 TYR C 116    12203  12440   8461  -1239    193   -431       C  
ATOM   7537  CZ  TYR C 116     -45.702  40.654  28.218  1.00 94.98           C  
ANISOU 7537  CZ  TYR C 116    13200  13410   9479  -1260    125   -333       C  
ATOM   7538  OH  TYR C 116     -47.023  40.908  27.934  1.00 96.96           O  
ANISOU 7538  OH  TYR C 116    13467  13704   9670  -1314    108   -316       O  
ATOM   7539  N   THR C 117     -41.884  36.966  30.550  1.00 82.41           N  
ANISOU 7539  N   THR C 117    11704  11455   8152   -870    139   -571       N  
ATOM   7540  CA  THR C 117     -42.634  35.742  30.852  1.00 81.95           C  
ANISOU 7540  CA  THR C 117    11797  11267   8073   -857    171   -629       C  
ATOM   7541  C   THR C 117     -42.476  35.412  32.349  1.00 85.16           C  
ANISOU 7541  C   THR C 117    12313  11519   8526   -767     94   -582       C  
ATOM   7542  O   THR C 117     -43.473  35.125  33.012  1.00 84.32           O  
ANISOU 7542  O   THR C 117    12337  11317   8384   -809     96   -559       O  
ATOM   7543  CB  THR C 117     -42.164  34.612  29.919  1.00 89.15           C  
ANISOU 7543  CB  THR C 117    12704  12181   8987   -812    259   -749       C  
ATOM   7544  OG1 THR C 117     -42.344  35.008  28.558  1.00 87.11           O  
ANISOU 7544  OG1 THR C 117    12355  12089   8652   -901    327   -787       O  
ATOM   7545  CG2 THR C 117     -42.869  33.301  30.173  1.00 88.87           C  
ANISOU 7545  CG2 THR C 117    12834  11985   8949   -809    299   -818       C  
ATOM   7546  N   VAL C 118     -41.229  35.486  32.873  1.00 81.89           N  
ANISOU 7546  N   VAL C 118    11838  11093   8182   -649     25   -567       N  
ATOM   7547  CA  VAL C 118     -40.906  35.243  34.286  1.00 81.98           C  
ANISOU 7547  CA  VAL C 118    11947  10983   8220   -547    -74   -516       C  
ATOM   7548  C   VAL C 118     -41.703  36.213  35.192  1.00 84.48           C  
ANISOU 7548  C   VAL C 118    12322  11294   8484   -621   -132   -436       C  
ATOM   7549  O   VAL C 118     -42.400  35.749  36.094  1.00 84.12           O  
ANISOU 7549  O   VAL C 118    12436  11133   8391   -616   -138   -404       O  
ATOM   7550  CB  VAL C 118     -39.370  35.245  34.574  1.00 86.81           C  
ANISOU 7550  CB  VAL C 118    12442  11623   8920   -405   -159   -525       C  
ATOM   7551  CG1 VAL C 118     -39.078  35.217  36.076  1.00 86.98           C  
ANISOU 7551  CG1 VAL C 118    12560  11549   8940   -307   -293   -461       C  
ATOM   7552  CG2 VAL C 118     -38.677  34.072  33.880  1.00 87.91           C  
ANISOU 7552  CG2 VAL C 118    12556  11732   9116   -296    -94   -615       C  
ATOM   7553  N   ASN C 119     -41.639  37.539  34.910  1.00 79.54           N  
ANISOU 7553  N   ASN C 119    11573  10783   7866   -694   -160   -405       N  
ATOM   7554  CA  ASN C 119     -42.371  38.586  35.640  1.00 78.00           C  
ANISOU 7554  CA  ASN C 119    11417  10585   7634   -758   -207   -348       C  
ATOM   7555  C   ASN C 119     -43.888  38.394  35.541  1.00 80.79           C  
ANISOU 7555  C   ASN C 119    11868  10911   7919   -846   -128   -344       C  
ATOM   7556  O   ASN C 119     -44.590  38.657  36.516  1.00 80.82           O  
ANISOU 7556  O   ASN C 119    11968  10859   7881   -858   -148   -312       O  
ATOM   7557  CB  ASN C 119     -41.987  39.982  35.122  1.00 76.91           C  
ANISOU 7557  CB  ASN C 119    11130  10556   7537   -823   -236   -321       C  
ATOM   7558  CG  ASN C 119     -42.888  41.117  35.588  1.00 93.36           C  
ANISOU 7558  CG  ASN C 119    13249  12632   9594   -893   -262   -275       C  
ATOM   7559  OD1 ASN C 119     -43.963  41.373  35.027  1.00 83.04           O  
ANISOU 7559  OD1 ASN C 119    11952  11353   8247   -966   -200   -261       O  
ATOM   7560  ND2 ASN C 119     -42.462  41.833  36.615  1.00 84.96           N  
ANISOU 7560  ND2 ASN C 119    12197  11531   8552   -866   -361   -260       N  
ATOM   7561  N   LEU C 120     -44.387  37.971  34.363  1.00 75.99           N  
ANISOU 7561  N   LEU C 120    11223  10355   7293   -911    -39   -386       N  
ATOM   7562  CA  LEU C 120     -45.814  37.784  34.102  1.00 74.77           C  
ANISOU 7562  CA  LEU C 120    11121  10203   7084  -1006     29   -398       C  
ATOM   7563  C   LEU C 120     -46.465  36.715  34.958  1.00 77.39           C  
ANISOU 7563  C   LEU C 120    11612  10401   7391  -1003     68   -411       C  
ATOM   7564  O   LEU C 120     -47.516  36.972  35.549  1.00 75.88           O  
ANISOU 7564  O   LEU C 120    11473  10192   7166  -1060     90   -386       O  
ATOM   7565  CB  LEU C 120     -46.069  37.522  32.608  1.00 74.95           C  
ANISOU 7565  CB  LEU C 120    11066  10329   7084  -1073     96   -455       C  
ATOM   7566  CG  LEU C 120     -46.969  38.528  31.894  1.00 79.13           C  
ANISOU 7566  CG  LEU C 120    11513  10981   7573  -1162     97   -423       C  
ATOM   7567  CD1 LEU C 120     -46.477  39.969  32.069  1.00 78.79           C  
ANISOU 7567  CD1 LEU C 120    11392  10985   7561  -1145     29   -340       C  
ATOM   7568  CD2 LEU C 120     -47.059  38.211  30.434  1.00 82.33           C  
ANISOU 7568  CD2 LEU C 120    11853  11500   7927  -1216    147   -479       C  
ATOM   7569  N   TYR C 121     -45.835  35.532  35.043  1.00 74.37           N  
ANISOU 7569  N   TYR C 121    11307   9918   7031   -934     85   -445       N  
ATOM   7570  CA  TYR C 121     -46.367  34.418  35.817  1.00 74.80           C  
ANISOU 7570  CA  TYR C 121    11537   9817   7068   -934    131   -441       C  
ATOM   7571  C   TYR C 121     -46.045  34.490  37.307  1.00 78.15           C  
ANISOU 7571  C   TYR C 121    12081  10148   7466   -848     64   -361       C  
ATOM   7572  O   TYR C 121     -46.917  34.180  38.120  1.00 77.91           O  
ANISOU 7572  O   TYR C 121    12182  10037   7384   -897    111   -325       O  
ATOM   7573  CB  TYR C 121     -45.950  33.067  35.217  1.00 77.28           C  
ANISOU 7573  CB  TYR C 121    11909  10035   7421   -896    185   -514       C  
ATOM   7574  CG  TYR C 121     -46.464  32.833  33.812  1.00 79.37           C  
ANISOU 7574  CG  TYR C 121    12092  10385   7681   -999    261   -614       C  
ATOM   7575  CD1 TYR C 121     -47.826  32.680  33.562  1.00 81.47           C  
ANISOU 7575  CD1 TYR C 121    12380  10665   7911  -1146    327   -646       C  
ATOM   7576  CD2 TYR C 121     -45.588  32.720  32.739  1.00 80.57           C  
ANISOU 7576  CD2 TYR C 121    12143  10614   7857   -950    268   -685       C  
ATOM   7577  CE1 TYR C 121     -48.304  32.469  32.269  1.00 83.06           C  
ANISOU 7577  CE1 TYR C 121    12505  10962   8093  -1241    375   -746       C  
ATOM   7578  CE2 TYR C 121     -46.053  32.502  31.444  1.00 81.75           C  
ANISOU 7578  CE2 TYR C 121    12232  10856   7973  -1043    334   -784       C  
ATOM   7579  CZ  TYR C 121     -47.412  32.381  31.212  1.00 89.87           C  
ANISOU 7579  CZ  TYR C 121    13288  11902   8957  -1188    376   -814       C  
ATOM   7580  OH  TYR C 121     -47.858  32.160  29.931  1.00 91.46           O  
ANISOU 7580  OH  TYR C 121    13430  12210   9112  -1279    420   -920       O  
ATOM   7581  N   SER C 122     -44.810  34.904  37.672  1.00 74.17           N  
ANISOU 7581  N   SER C 122    11526   9665   6990   -729    -44   -335       N  
ATOM   7582  CA  SER C 122     -44.388  34.981  39.072  1.00 74.14           C  
ANISOU 7582  CA  SER C 122    11634   9593   6945   -636   -136   -267       C  
ATOM   7583  C   SER C 122     -45.124  36.034  39.888  1.00 75.79           C  
ANISOU 7583  C   SER C 122    11866   9846   7083   -697   -154   -228       C  
ATOM   7584  O   SER C 122     -45.680  35.679  40.925  1.00 76.21           O  
ANISOU 7584  O   SER C 122    12082   9817   7056   -698   -132   -182       O  
ATOM   7585  CB  SER C 122     -42.879  35.142  39.200  1.00 79.10           C  
ANISOU 7585  CB  SER C 122    12174  10251   7629   -498   -261   -267       C  
ATOM   7586  OG  SER C 122     -42.480  36.430  38.763  1.00 90.21           O  
ANISOU 7586  OG  SER C 122    13400  11799   9075   -538   -311   -285       O  
ATOM   7587  N   SER C 123     -45.164  37.308  39.421  1.00 69.94           N  
ANISOU 7587  N   SER C 123    10975   9228   6371   -750   -181   -247       N  
ATOM   7588  CA  SER C 123     -45.836  38.393  40.152  1.00 68.98           C  
ANISOU 7588  CA  SER C 123    10870   9140   6201   -793   -198   -227       C  
ATOM   7589  C   SER C 123     -47.252  38.023  40.638  1.00 73.52           C  
ANISOU 7589  C   SER C 123    11562   9671   6702   -869    -85   -216       C  
ATOM   7590  O   SER C 123     -47.550  38.198  41.826  1.00 74.10           O  
ANISOU 7590  O   SER C 123    11754   9707   6694   -849    -93   -188       O  
ATOM   7591  CB  SER C 123     -45.816  39.707  39.374  1.00 70.29           C  
ANISOU 7591  CB  SER C 123    10868   9414   6426   -846   -222   -244       C  
ATOM   7592  OG  SER C 123     -46.784  39.748  38.340  1.00 78.48           O  
ANISOU 7592  OG  SER C 123    11837  10506   7476   -938   -128   -261       O  
ATOM   7593  N   VAL C 124     -48.081  37.438  39.745  1.00 69.03           N  
ANISOU 7593  N   VAL C 124    10961   9110   6157   -957     23   -245       N  
ATOM   7594  CA  VAL C 124     -49.434  36.998  40.089  1.00 68.98           C  
ANISOU 7594  CA  VAL C 124    11034   9073   6104  -1051    142   -245       C  
ATOM   7595  C   VAL C 124     -49.426  35.812  41.078  1.00 75.02           C  
ANISOU 7595  C   VAL C 124    12006   9694   6805  -1027    186   -200       C  
ATOM   7596  O   VAL C 124     -50.204  35.828  42.033  1.00 75.35           O  
ANISOU 7596  O   VAL C 124    12151   9710   6770  -1065    251   -169       O  
ATOM   7597  CB  VAL C 124     -50.365  36.809  38.857  1.00 72.16           C  
ANISOU 7597  CB  VAL C 124    11322   9544   6551  -1165    225   -301       C  
ATOM   7598  CG1 VAL C 124     -49.996  35.573  38.033  1.00 72.42           C  
ANISOU 7598  CG1 VAL C 124    11380   9517   6620  -1180    258   -341       C  
ATOM   7599  CG2 VAL C 124     -51.835  36.777  39.267  1.00 72.30           C  
ANISOU 7599  CG2 VAL C 124    11358   9577   6537  -1269    334   -310       C  
ATOM   7600  N   TRP C 125     -48.520  34.820  40.878  1.00 72.56           N  
ANISOU 7600  N   TRP C 125    11759   9286   6522   -955    153   -191       N  
ATOM   7601  CA  TRP C 125     -48.397  33.652  41.763  1.00 73.78           C  
ANISOU 7601  CA  TRP C 125    12130   9278   6624   -912    181   -128       C  
ATOM   7602  C   TRP C 125     -47.857  34.014  43.150  1.00 77.83           C  
ANISOU 7602  C   TRP C 125    12766   9770   7036   -805     87    -51       C  
ATOM   7603  O   TRP C 125     -48.147  33.310  44.120  1.00 78.41           O  
ANISOU 7603  O   TRP C 125    13041   9733   7017   -799    133     23       O  
ATOM   7604  CB  TRP C 125     -47.642  32.487  41.100  1.00 73.38           C  
ANISOU 7604  CB  TRP C 125    12115   9118   6650   -850    174   -149       C  
ATOM   7605  CG  TRP C 125     -48.528  31.628  40.246  1.00 74.87           C  
ANISOU 7605  CG  TRP C 125    12311   9250   6887   -983    308   -210       C  
ATOM   7606  CD1 TRP C 125     -48.607  31.633  38.884  1.00 77.32           C  
ANISOU 7606  CD1 TRP C 125    12469   9639   7269  -1042    333   -311       C  
ATOM   7607  CD2 TRP C 125     -49.520  30.696  40.702  1.00 76.07           C  
ANISOU 7607  CD2 TRP C 125    12626   9268   7010  -1095    437   -183       C  
ATOM   7608  NE1 TRP C 125     -49.573  30.747  38.460  1.00 77.50           N  
ANISOU 7608  NE1 TRP C 125    12546   9586   7313  -1180    454   -362       N  
ATOM   7609  CE2 TRP C 125     -50.149  30.157  39.555  1.00 80.03           C  
ANISOU 7609  CE2 TRP C 125    13054   9769   7585  -1223    525   -285       C  
ATOM   7610  CE3 TRP C 125     -49.932  30.252  41.971  1.00 78.64           C  
ANISOU 7610  CE3 TRP C 125    13158   9474   7248  -1109    493    -81       C  
ATOM   7611  CZ2 TRP C 125     -51.165  29.195  39.640  1.00 80.54           C  
ANISOU 7611  CZ2 TRP C 125    13230   9710   7659  -1374    662   -297       C  
ATOM   7612  CZ3 TRP C 125     -50.942  29.303  42.053  1.00 81.27           C  
ANISOU 7612  CZ3 TRP C 125    13610   9684   7586  -1260    645    -75       C  
ATOM   7613  CH2 TRP C 125     -51.542  28.780  40.899  1.00 81.95           C  
ANISOU 7613  CH2 TRP C 125    13606   9763   7769  -1395    727   -187       C  
ATOM   7614  N   ILE C 126     -47.120  35.141  43.249  1.00 73.25           N  
ANISOU 7614  N   ILE C 126    12070   9298   6463   -735    -41    -70       N  
ATOM   7615  CA  ILE C 126     -46.627  35.663  44.523  1.00 73.57           C  
ANISOU 7615  CA  ILE C 126    12205   9348   6400   -647   -150    -26       C  
ATOM   7616  C   ILE C 126     -47.842  36.236  45.257  1.00 77.50           C  
ANISOU 7616  C   ILE C 126    12769   9881   6798   -739    -52    -23       C  
ATOM   7617  O   ILE C 126     -48.012  35.947  46.439  1.00 78.97           O  
ANISOU 7617  O   ILE C 126    13143  10017   6847   -711    -41     37       O  
ATOM   7618  CB  ILE C 126     -45.453  36.669  44.356  1.00 76.13           C  
ANISOU 7618  CB  ILE C 126    12373   9770   6783   -566   -315    -66       C  
ATOM   7619  CG1 ILE C 126     -44.184  35.943  43.851  1.00 77.18           C  
ANISOU 7619  CG1 ILE C 126    12453   9868   7003   -452   -405    -65       C  
ATOM   7620  CG2 ILE C 126     -45.152  37.386  45.676  1.00 77.23           C  
ANISOU 7620  CG2 ILE C 126    12602   9938   6806   -506   -426    -49       C  
ATOM   7621  CD1 ILE C 126     -43.244  36.775  42.995  1.00 83.24           C  
ANISOU 7621  CD1 ILE C 126    12989  10749   7891   -435   -491   -127       C  
ATOM   7622  N   LEU C 127     -48.737  36.950  44.528  1.00 72.39           N  
ANISOU 7622  N   LEU C 127    11974   9320   6212   -845     31    -83       N  
ATOM   7623  CA  LEU C 127     -49.993  37.482  45.073  1.00 72.09           C  
ANISOU 7623  CA  LEU C 127    11957   9326   6106   -928    144    -98       C  
ATOM   7624  C   LEU C 127     -50.936  36.345  45.454  1.00 77.98           C  
ANISOU 7624  C   LEU C 127    12848   9989   6791  -1014    306    -54       C  
ATOM   7625  O   LEU C 127     -51.715  36.500  46.395  1.00 78.13           O  
ANISOU 7625  O   LEU C 127    12964  10020   6703  -1053    399    -37       O  
ATOM   7626  CB  LEU C 127     -50.709  38.419  44.087  1.00 70.61           C  
ANISOU 7626  CB  LEU C 127    11564   9246   6020  -1002    182   -167       C  
ATOM   7627  CG  LEU C 127     -49.996  39.684  43.621  1.00 74.04           C  
ANISOU 7627  CG  LEU C 127    11851   9753   6526   -949     54   -204       C  
ATOM   7628  CD1 LEU C 127     -50.918  40.507  42.801  1.00 72.98           C  
ANISOU 7628  CD1 LEU C 127    11558   9704   6467  -1016    108   -246       C  
ATOM   7629  CD2 LEU C 127     -49.498  40.526  44.791  1.00 77.26           C  
ANISOU 7629  CD2 LEU C 127    12337  10163   6856   -874    -40   -211       C  
ATOM   7630  N   ALA C 128     -50.865  35.208  44.717  1.00 75.93           N  
ANISOU 7630  N   ALA C 128    12605   9644   6602  -1052    350    -42       N  
ATOM   7631  CA  ALA C 128     -51.653  33.999  44.978  1.00 77.62           C  
ANISOU 7631  CA  ALA C 128    12965   9744   6784  -1151    502      2       C  
ATOM   7632  C   ALA C 128     -51.153  33.338  46.265  1.00 84.86           C  
ANISOU 7632  C   ALA C 128    14140  10538   7564  -1068    481    113       C  
ATOM   7633  O   ALA C 128     -51.961  32.823  47.045  1.00 85.86           O  
ANISOU 7633  O   ALA C 128    14422  10605   7596  -1150    619    173       O  
ATOM   7634  CB  ALA C 128     -51.549  33.031  43.811  1.00 78.27           C  
ANISOU 7634  CB  ALA C 128    13001   9751   6986  -1199    529    -35       C  
ATOM   7635  N   PHE C 129     -49.823  33.391  46.498  1.00 82.36           N  
ANISOU 7635  N   PHE C 129    13864  10197   7234   -906    307    146       N  
ATOM   7636  CA  PHE C 129     -49.184  32.864  47.699  1.00 84.07           C  
ANISOU 7636  CA  PHE C 129    14315  10317   7311   -792    237    256       C  
ATOM   7637  C   PHE C 129     -49.487  33.761  48.883  1.00 88.37           C  
ANISOU 7637  C   PHE C 129    14932  10957   7688   -782    228    270       C  
ATOM   7638  O   PHE C 129     -49.744  33.244  49.973  1.00 90.54           O  
ANISOU 7638  O   PHE C 129    15437  11165   7800   -777    284    367       O  
ATOM   7639  CB  PHE C 129     -47.673  32.690  47.491  1.00 86.24           C  
ANISOU 7639  CB  PHE C 129    14562  10562   7641   -615     38    267       C  
ATOM   7640  CG  PHE C 129     -47.260  31.263  47.213  1.00 89.55           C  
ANISOU 7640  CG  PHE C 129    15108  10798   8119   -560     52    329       C  
ATOM   7641  CD1 PHE C 129     -47.685  30.608  46.061  1.00 92.55           C  
ANISOU 7641  CD1 PHE C 129    15413  11113   8641   -656    164    269       C  
ATOM   7642  CD2 PHE C 129     -46.425  30.582  48.090  1.00 93.87           C  
ANISOU 7642  CD2 PHE C 129    15854  11233   8580   -401    -58    441       C  
ATOM   7643  CE1 PHE C 129     -47.304  29.286  45.807  1.00 95.04           C  
ANISOU 7643  CE1 PHE C 129    15858  11234   9020   -600    182    310       C  
ATOM   7644  CE2 PHE C 129     -46.035  29.263  47.828  1.00 98.27           C  
ANISOU 7644  CE2 PHE C 129    16537  11595   9206   -331    -48    500       C  
ATOM   7645  CZ  PHE C 129     -46.483  28.623  46.692  1.00 95.96           C  
ANISOU 7645  CZ  PHE C 129    16176  11221   9065   -433     80    428       C  
ATOM   7646  N   ILE C 130     -49.504  35.102  48.663  1.00 82.54           N  
ANISOU 7646  N   ILE C 130    14010  10367   6984   -783    170    171       N  
ATOM   7647  CA  ILE C 130     -49.840  36.112  49.681  1.00 82.55           C  
ANISOU 7647  CA  ILE C 130    14055  10464   6845   -776    166    144       C  
ATOM   7648  C   ILE C 130     -51.299  35.891  50.161  1.00 87.38           C  
ANISOU 7648  C   ILE C 130    14750  11080   7370   -909    397    159       C  
ATOM   7649  O   ILE C 130     -51.586  36.048  51.350  1.00 87.87           O  
ANISOU 7649  O   ILE C 130    14977  11164   7247   -898    442    192       O  
ATOM   7650  CB  ILE C 130     -49.548  37.560  49.174  1.00 83.75           C  
ANISOU 7650  CB  ILE C 130    13987  10739   7095   -755     61     29       C  
ATOM   7651  CG1 ILE C 130     -48.038  37.808  49.059  1.00 83.63           C  
ANISOU 7651  CG1 ILE C 130    13920  10731   7126   -629   -163     22       C  
ATOM   7652  CG2 ILE C 130     -50.152  38.618  50.086  1.00 85.03           C  
ANISOU 7652  CG2 ILE C 130    14183  10986   7140   -767     98    -28       C  
ATOM   7653  CD1 ILE C 130     -47.640  38.961  48.110  1.00 90.09           C  
ANISOU 7653  CD1 ILE C 130    14493  11634   8104   -639   -247    -73       C  
ATOM   7654  N   SER C 131     -52.183  35.459  49.237  1.00 83.68           N  
ANISOU 7654  N   SER C 131    14169  10597   7030  -1039    542    133       N  
ATOM   7655  CA  SER C 131     -53.583  35.134  49.500  1.00 84.56           C  
ANISOU 7655  CA  SER C 131    14310  10717   7103  -1188    770    138       C  
ATOM   7656  C   SER C 131     -53.711  33.871  50.355  1.00 90.91           C  
ANISOU 7656  C   SER C 131    15386  11381   7774  -1225    875    270       C  
ATOM   7657  O   SER C 131     -54.591  33.818  51.214  1.00 92.43           O  
ANISOU 7657  O   SER C 131    15685  11598   7837  -1307   1041    301       O  
ATOM   7658  CB  SER C 131     -54.348  34.965  48.194  1.00 87.41           C  
ANISOU 7658  CB  SER C 131    14459  11104   7648  -1313    857     66       C  
ATOM   7659  OG  SER C 131     -54.342  36.181  47.467  1.00 96.05           O  
ANISOU 7659  OG  SER C 131    15322  12328   8845  -1278    772    -35       O  
ATOM   7660  N   LEU C 132     -52.836  32.864  50.131  1.00 87.56           N  
ANISOU 7660  N   LEU C 132    15079  10807   7382  -1161    787    351       N  
ATOM   7661  CA  LEU C 132     -52.817  31.625  50.919  1.00 89.64           C  
ANISOU 7661  CA  LEU C 132    15630  10901   7527  -1173    863    500       C  
ATOM   7662  C   LEU C 132     -52.362  31.922  52.354  1.00 95.23           C  
ANISOU 7662  C   LEU C 132    16556  11636   7991  -1057    792    588       C  
ATOM   7663  O   LEU C 132     -52.893  31.339  53.305  1.00 96.76           O  
ANISOU 7663  O   LEU C 132    16979  11767   8016  -1117    932    701       O  
ATOM   7664  CB  LEU C 132     -51.880  30.586  50.288  1.00 89.89           C  
ANISOU 7664  CB  LEU C 132    15723  10761   7671  -1091    757    551       C  
ATOM   7665  CG  LEU C 132     -52.413  29.821  49.091  1.00 94.51           C  
ANISOU 7665  CG  LEU C 132    16204  11257   8448  -1227    868    494       C  
ATOM   7666  CD1 LEU C 132     -51.275  29.284  48.256  1.00 94.54           C  
ANISOU 7666  CD1 LEU C 132    16174  11161   8584  -1099    717    477       C  
ATOM   7667  CD2 LEU C 132     -53.313  28.677  49.524  1.00 99.56           C  
ANISOU 7667  CD2 LEU C 132    17047  11734   9046  -1386   1080    588       C  
ATOM   7668  N   ASP C 133     -51.381  32.842  52.496  1.00 90.77           N  
ANISOU 7668  N   ASP C 133    15917  11172   7401   -902    575    534       N  
ATOM   7669  CA  ASP C 133     -50.825  33.291  53.772  1.00 91.57           C  
ANISOU 7669  CA  ASP C 133    16190  11330   7274   -781    459    581       C  
ATOM   7670  C   ASP C 133     -51.929  33.918  54.621  1.00 95.23           C  
ANISOU 7670  C   ASP C 133    16707  11905   7573   -879    636    547       C  
ATOM   7671  O   ASP C 133     -52.065  33.553  55.785  1.00 96.99           O  
ANISOU 7671  O   ASP C 133    17186  12108   7559   -867    694    653       O  
ATOM   7672  CB  ASP C 133     -49.678  34.290  53.532  1.00 92.01           C  
ANISOU 7672  CB  ASP C 133    16085  11486   7389   -638    203    484       C  
ATOM   7673  CG  ASP C 133     -48.871  34.614  54.770  1.00101.57           C  
ANISOU 7673  CG  ASP C 133    17469  12746   8376   -498     29    525       C  
ATOM   7674  OD1 ASP C 133     -49.100  35.690  55.363  1.00101.86           O  
ANISOU 7674  OD1 ASP C 133    17484  12913   8306   -503     17    432       O  
ATOM   7675  OD2 ASP C 133     -48.000  33.800  55.137  1.00107.69           O  
ANISOU 7675  OD2 ASP C 133    18401  13430   9087   -374   -104    641       O  
ATOM   7676  N   ARG C 134     -52.753  34.810  54.016  1.00 89.59           N  
ANISOU 7676  N   ARG C 134    15754  11306   6982   -974    735    406       N  
ATOM   7677  CA  ARG C 134     -53.881  35.485  54.677  1.00 89.72           C  
ANISOU 7677  CA  ARG C 134    15766  11440   6884  -1059    920    343       C  
ATOM   7678  C   ARG C 134     -54.970  34.497  55.106  1.00 95.41           C  
ANISOU 7678  C   ARG C 134    16632  12100   7520  -1214   1190    442       C  
ATOM   7679  O   ARG C 134     -55.632  34.723  56.119  1.00 97.10           O  
ANISOU 7679  O   ARG C 134    16968  12388   7539  -1255   1340    450       O  
ATOM   7680  CB  ARG C 134     -54.472  36.606  53.800  1.00 86.17           C  
ANISOU 7680  CB  ARG C 134    15009  11109   6622  -1102    946    177       C  
ATOM   7681  CG  ARG C 134     -53.509  37.755  53.487  1.00 91.34           C  
ANISOU 7681  CG  ARG C 134    15530  11825   7350   -973    710     77       C  
ATOM   7682  CD  ARG C 134     -53.240  38.671  54.665  1.00 95.88           C  
ANISOU 7682  CD  ARG C 134    16221  12482   7728   -884    641     21       C  
ATOM   7683  NE  ARG C 134     -51.886  38.500  55.194  1.00100.64           N  
ANISOU 7683  NE  ARG C 134    16970  13048   8223   -755    409     77       N  
ATOM   7684  CZ  ARG C 134     -51.599  38.308  56.478  1.00114.75           C  
ANISOU 7684  CZ  ARG C 134    19008  14847   9744   -693    374    135       C  
ATOM   7685  NH1 ARG C 134     -50.340  38.172  56.870  1.00103.58           N  
ANISOU 7685  NH1 ARG C 134    17694  13413   8251   -566    135    180       N  
ATOM   7686  NH2 ARG C 134     -52.571  38.257  57.381  1.00 99.35           N  
ANISOU 7686  NH2 ARG C 134    17205  12943   7599   -757    579    148       N  
ATOM   7687  N   TYR C 135     -55.141  33.399  54.344  1.00 90.76           N  
ANISOU 7687  N   TYR C 135    16035  11375   7075  -1308   1258    509       N  
ATOM   7688  CA  TYR C 135     -56.092  32.341  54.662  1.00 92.07           C  
ANISOU 7688  CA  TYR C 135    16343  11448   7192  -1478   1509    611       C  
ATOM   7689  C   TYR C 135     -55.567  31.607  55.899  1.00 97.38           C  
ANISOU 7689  C   TYR C 135    17380  12013   7606  -1410   1497    795       C  
ATOM   7690  O   TYR C 135     -56.269  31.547  56.904  1.00 98.76           O  
ANISOU 7690  O   TYR C 135    17715  12231   7578  -1487   1682    854       O  
ATOM   7691  CB  TYR C 135     -56.289  31.399  53.449  1.00 92.75           C  
ANISOU 7691  CB  TYR C 135    16324  11400   7516  -1590   1552    612       C  
ATOM   7692  CG  TYR C 135     -56.760  30.003  53.798  1.00 97.50           C  
ANISOU 7692  CG  TYR C 135    17156  11816   8073  -1732   1738    759       C  
ATOM   7693  CD1 TYR C 135     -58.104  29.740  54.040  1.00101.07           C  
ANISOU 7693  CD1 TYR C 135    17589  12300   8514  -1949   2019    757       C  
ATOM   7694  CD2 TYR C 135     -55.866  28.940  53.861  1.00 99.61           C  
ANISOU 7694  CD2 TYR C 135    17653  11867   8329  -1650   1636    899       C  
ATOM   7695  CE1 TYR C 135     -58.541  28.462  54.388  1.00104.65           C  
ANISOU 7695  CE1 TYR C 135    18265  12567   8932  -2103   2204    900       C  
ATOM   7696  CE2 TYR C 135     -56.290  27.657  54.203  1.00103.37           C  
ANISOU 7696  CE2 TYR C 135    18366  12139   8769  -1782   1810   1047       C  
ATOM   7697  CZ  TYR C 135     -57.630  27.420  54.463  1.00113.20           C  
ANISOU 7697  CZ  TYR C 135    19603  13411   9997  -2020   2098   1050       C  
ATOM   7698  OH  TYR C 135     -58.053  26.151  54.790  1.00117.88           O  
ANISOU 7698  OH  TYR C 135    20436  13786  10567  -2174   2281   1200       O  
ATOM   7699  N   LEU C 136     -54.306  31.126  55.844  1.00 93.61           N  
ANISOU 7699  N   LEU C 136    17026  11414   7127  -1250   1270    882       N  
ATOM   7700  CA  LEU C 136     -53.634  30.403  56.931  1.00 95.69           C  
ANISOU 7700  CA  LEU C 136    17636  11567   7156  -1144   1200   1071       C  
ATOM   7701  C   LEU C 136     -53.461  31.226  58.213  1.00 99.89           C  
ANISOU 7701  C   LEU C 136    18308  12255   7393  -1049   1146   1072       C  
ATOM   7702  O   LEU C 136     -53.406  30.644  59.294  1.00102.35           O  
ANISOU 7702  O   LEU C 136    18931  12510   7449  -1026   1189   1237       O  
ATOM   7703  CB  LEU C 136     -52.271  29.848  56.479  1.00 95.34           C  
ANISOU 7703  CB  LEU C 136    17629  11386   7209   -962    940   1131       C  
ATOM   7704  CG  LEU C 136     -52.273  28.667  55.508  1.00100.08           C  
ANISOU 7704  CG  LEU C 136    18223  11771   8032  -1024    993   1180       C  
ATOM   7705  CD1 LEU C 136     -50.891  28.443  54.955  1.00 99.51           C  
ANISOU 7705  CD1 LEU C 136    18105  11623   8080   -819    725   1179       C  
ATOM   7706  CD2 LEU C 136     -52.765  27.383  56.180  1.00105.49           C  
ANISOU 7706  CD2 LEU C 136    19235  12249   8599  -1120   1176   1382       C  
ATOM   7707  N   ALA C 137     -53.373  32.562  58.094  1.00 93.70           N  
ANISOU 7707  N   ALA C 137    17310  11656   6636   -997   1051    891       N  
ATOM   7708  CA  ALA C 137     -53.216  33.457  59.238  1.00 94.24           C  
ANISOU 7708  CA  ALA C 137    17488  11877   6440   -912    992    847       C  
ATOM   7709  C   ALA C 137     -54.550  33.796  59.909  1.00 98.48           C  
ANISOU 7709  C   ALA C 137    18063  12527   6830  -1056   1287    807       C  
ATOM   7710  O   ALA C 137     -54.581  33.973  61.124  1.00100.10           O  
ANISOU 7710  O   ALA C 137    18495  12807   6732  -1018   1320    850       O  
ATOM   7711  CB  ALA C 137     -52.512  34.733  58.809  1.00 92.72           C  
ANISOU 7711  CB  ALA C 137    17060  11807   6362   -799    764    664       C  
ATOM   7712  N   ILE C 138     -55.635  33.912  59.121  1.00 93.61           N  
ANISOU 7712  N   ILE C 138    17212  11935   6419  -1215   1497    715       N  
ATOM   7713  CA  ILE C 138     -56.967  34.278  59.613  1.00 94.67           C  
ANISOU 7713  CA  ILE C 138    17312  12194   6465  -1354   1791    650       C  
ATOM   7714  C   ILE C 138     -57.836  33.069  59.961  1.00102.04           C  
ANISOU 7714  C   ILE C 138    18418  13030   7322  -1537   2075    811       C  
ATOM   7715  O   ILE C 138     -58.398  33.045  61.061  1.00103.61           O  
ANISOU 7715  O   ILE C 138    18807  13301   7260  -1590   2266    864       O  
ATOM   7716  CB  ILE C 138     -57.653  35.319  58.678  1.00 95.17           C  
ANISOU 7716  CB  ILE C 138    17002  12379   6780  -1396   1834    438       C  
ATOM   7717  CG1 ILE C 138     -57.012  36.715  58.848  1.00 94.12           C  
ANISOU 7717  CG1 ILE C 138    16778  12363   6619  -1232   1625    280       C  
ATOM   7718  CG2 ILE C 138     -59.168  35.383  58.883  1.00 97.11           C  
ANISOU 7718  CG2 ILE C 138    17151  12726   7022  -1566   2168    383       C  
ATOM   7719  CD1 ILE C 138     -56.921  37.528  57.586  1.00 97.25           C  
ANISOU 7719  CD1 ILE C 138    16845  12787   7318  -1204   1503    135       C  
ATOM   7720  N   VAL C 139     -57.952  32.083  59.035  1.00 99.50           N  
ANISOU 7720  N   VAL C 139    18037  12545   7223  -1642   2112    882       N  
ATOM   7721  CA  VAL C 139     -58.742  30.859  59.234  1.00102.23           C  
ANISOU 7721  CA  VAL C 139    18539  12760   7543  -1841   2376   1033       C  
ATOM   7722  C   VAL C 139     -58.239  30.069  60.447  1.00111.09           C  
ANISOU 7722  C   VAL C 139    20086  13769   8355  -1789   2380   1263       C  
ATOM   7723  O   VAL C 139     -59.055  29.725  61.304  1.00114.42           O  
ANISOU 7723  O   VAL C 139    20679  14214   8582  -1926   2647   1356       O  
ATOM   7724  CB  VAL C 139     -58.998  30.036  57.945  1.00104.75           C  
ANISOU 7724  CB  VAL C 139    18695  12927   8178  -1973   2408   1025       C  
ATOM   7725  CG1 VAL C 139     -59.799  28.767  58.235  1.00107.38           C  
ANISOU 7725  CG1 VAL C 139    19212  13104   8484  -2198   2685   1179       C  
ATOM   7726  CG2 VAL C 139     -59.731  30.893  56.915  1.00102.17           C  
ANISOU 7726  CG2 VAL C 139    17962  12759   8100  -2042   2443    804       C  
ATOM   7727  N   HIS C 140     -56.901  29.896  60.592  1.00107.59           N  
ANISOU 7727  N   HIS C 140    19803  13233   7842  -1579   2083   1349       N  
ATOM   7728  CA  HIS C 140     -56.322  29.315  61.808  1.00110.62           C  
ANISOU 7728  CA  HIS C 140    20588  13542   7899  -1481   2033   1564       C  
ATOM   7729  C   HIS C 140     -54.908  29.726  62.182  1.00113.22           C  
ANISOU 7729  C   HIS C 140    21015  13903   8102  -1213   1673   1576       C  
ATOM   7730  O   HIS C 140     -53.936  29.213  61.624  1.00112.07           O  
ANISOU 7730  O   HIS C 140    20873  13612   8099  -1087   1448   1633       O  
ATOM   7731  CB  HIS C 140     -56.612  27.829  62.059  1.00114.49           C  
ANISOU 7731  CB  HIS C 140    21370  13789   8344  -1607   2208   1811       C  
ATOM   7732  CG  HIS C 140     -57.223  27.644  63.413  1.00121.58           C  
ANISOU 7732  CG  HIS C 140    22571  14743   8882  -1691   2438   1957       C  
ATOM   7733  ND1 HIS C 140     -56.440  27.560  64.553  1.00125.86           N  
ANISOU 7733  ND1 HIS C 140    23452  15292   9076  -1518   2289   2115       N  
ATOM   7734  CD2 HIS C 140     -58.526  27.656  63.781  1.00125.14           C  
ANISOU 7734  CD2 HIS C 140    23003  15281   9263  -1922   2796   1943       C  
ATOM   7735  CE1 HIS C 140     -57.289  27.466  65.564  1.00128.36           C  
ANISOU 7735  CE1 HIS C 140    23973  15687   9110  -1654   2572   2207       C  
ATOM   7736  NE2 HIS C 140     -58.555  27.518  65.149  1.00128.44           N  
ANISOU 7736  NE2 HIS C 140    23772  15747   9281  -1901   2893   2106       N  
ATOM   7737  N   ALA C 141     -54.815  30.633  63.172  1.00109.86           N  
ANISOU 7737  N   ALA C 141    20670  13673   7400  -1129   1628   1514       N  
ATOM   7738  CA  ALA C 141     -53.566  31.159  63.721  1.00109.54           C  
ANISOU 7738  CA  ALA C 141    20723  13707   7192   -894   1294   1501       C  
ATOM   7739  C   ALA C 141     -52.942  30.176  64.719  1.00116.73           C  
ANISOU 7739  C   ALA C 141    22045  14500   7807   -789   1206   1767       C  
ATOM   7740  O   ALA C 141     -53.655  29.452  65.415  1.00119.17           O  
ANISOU 7740  O   ALA C 141    22619  14747   7915   -908   1452   1941       O  
ATOM   7741  CB  ALA C 141     -53.818  32.498  64.397  1.00110.17           C  
ANISOU 7741  CB  ALA C 141    20739  14035   7088   -867   1300   1312       C  
ATOM   7742  N   GLN C 145     -50.475  24.141  63.878  1.00138.58           N  
ANISOU 7742  N   GLN C 145    25758  15991  10905   -455    880   2787       N  
ATOM   7743  CA  GLN C 145     -49.388  23.913  62.928  1.00136.65           C  
ANISOU 7743  CA  GLN C 145    25330  15640  10950   -262    608   2722       C  
ATOM   7744  C   GLN C 145     -48.814  25.233  62.388  1.00137.22           C  
ANISOU 7744  C   GLN C 145    25016  15977  11147   -168    393   2445       C  
ATOM   7745  O   GLN C 145     -49.384  26.297  62.650  1.00136.11           O  
ANISOU 7745  O   GLN C 145    24741  16072  10902   -273    480   2294       O  
ATOM   7746  CB  GLN C 145     -49.872  23.017  61.773  1.00137.01           C  
ANISOU 7746  CB  GLN C 145    25283  15430  11344   -415    790   2707       C  
ATOM   7747  N   ARG C 146     -47.681  25.165  61.643  1.00131.58           N  
ANISOU 7747  N   ARG C 146    24123  15215  10655     30    122   2380       N  
ATOM   7748  CA  ARG C 146     -47.038  26.339  61.037  1.00127.54           C  
ANISOU 7748  CA  ARG C 146    23242  14925  10293    112    -84   2132       C  
ATOM   7749  C   ARG C 146     -46.659  26.140  59.536  1.00126.83           C  
ANISOU 7749  C   ARG C 146    22846  14740  10603    124   -126   1997       C  
ATOM   7750  O   ARG C 146     -45.472  26.070  59.191  1.00126.07           O  
ANISOU 7750  O   ARG C 146    22643  14632  10624    337   -388   1973       O  
ATOM   7751  CB  ARG C 146     -45.874  26.865  61.914  1.00128.76           C  
ANISOU 7751  CB  ARG C 146    23459  15237  10228    360   -422   2152       C  
ATOM   7752  CG  ARG C 146     -45.272  28.220  61.490  1.00133.85           C  
ANISOU 7752  CG  ARG C 146    23744  16128  10984    411   -620   1894       C  
ATOM   7753  CD  ARG C 146     -46.240  29.402  61.474  1.00138.69           C  
ANISOU 7753  CD  ARG C 146    24195  16936  11566    210   -438   1704       C  
ATOM   7754  NE  ARG C 146     -46.853  29.657  62.781  1.00149.32           N  
ANISOU 7754  NE  ARG C 146    25809  18385  12539    157   -335   1775       N  
ATOM   7755  CZ  ARG C 146     -46.309  30.396  63.745  1.00164.86           C  
ANISOU 7755  CZ  ARG C 146    27857  20538  14246    272   -535   1733       C  
ATOM   7756  NH1 ARG C 146     -45.126  30.972  63.566  1.00152.53           N  
ANISOU 7756  NH1 ARG C 146    26111  19077  12767    439   -858   1621       N  
ATOM   7757  NH2 ARG C 146     -46.942  30.560  64.899  1.00152.88           N  
ANISOU 7757  NH2 ARG C 146    26600  19111  12376    213   -408   1796       N  
ATOM   7758  N   PRO C 147     -47.658  26.054  58.620  1.00120.33           N  
ANISOU 7758  N   PRO C 147    21868  13865   9988   -104    131   1898       N  
ATOM   7759  CA  PRO C 147     -47.326  25.899  57.192  1.00117.38           C  
ANISOU 7759  CA  PRO C 147    21215  13423   9961    -99     95   1759       C  
ATOM   7760  C   PRO C 147     -47.024  27.236  56.502  1.00116.48           C  
ANISOU 7760  C   PRO C 147    20723  13556   9977    -93    -20   1521       C  
ATOM   7761  O   PRO C 147     -46.719  27.252  55.308  1.00114.04           O  
ANISOU 7761  O   PRO C 147    20168  13230   9932    -89    -53   1396       O  
ATOM   7762  CB  PRO C 147     -48.576  25.217  56.607  1.00119.14           C  
ANISOU 7762  CB  PRO C 147    21462  13494  10314   -356    410   1762       C  
ATOM   7763  CG  PRO C 147     -49.640  25.273  57.694  1.00125.57           C  
ANISOU 7763  CG  PRO C 147    22498  14349  10864   -520    629   1870       C  
ATOM   7764  CD  PRO C 147     -49.120  26.108  58.818  1.00121.95           C  
ANISOU 7764  CD  PRO C 147    22126  14088  10120   -374    459   1897       C  
ATOM   7765  N   ARG C 148     -47.111  28.357  57.255  1.00111.68           N  
ANISOU 7765  N   ARG C 148    20084  13170   9178    -94    -74   1457       N  
ATOM   7766  CA  ARG C 148     -46.862  29.719  56.783  1.00108.38           C  
ANISOU 7766  CA  ARG C 148    19349  12974   8855    -96   -180   1245       C  
ATOM   7767  C   ARG C 148     -45.384  29.979  56.507  1.00112.70           C  
ANISOU 7767  C   ARG C 148    19749  13572   9500    120   -491   1194       C  
ATOM   7768  O   ARG C 148     -45.059  30.627  55.508  1.00110.02           O  
ANISOU 7768  O   ARG C 148    19107  13317   9379    107   -547   1036       O  
ATOM   7769  CB  ARG C 148     -47.406  30.752  57.778  1.00106.87           C  
ANISOU 7769  CB  ARG C 148    19212  12973   8420   -156   -137   1193       C  
ATOM   7770  CG  ARG C 148     -48.904  30.973  57.672  1.00111.41           C  
ANISOU 7770  CG  ARG C 148    19758  13580   8994   -389    175   1143       C  
ATOM   7771  CD  ARG C 148     -49.379  32.040  58.640  1.00119.05           C  
ANISOU 7771  CD  ARG C 148    20766  14738   9730   -423    216   1068       C  
ATOM   7772  NE  ARG C 148     -49.127  33.395  58.147  1.00123.79           N  
ANISOU 7772  NE  ARG C 148    21076  15504  10455   -405    101    858       N  
ATOM   7773  CZ  ARG C 148     -49.076  34.477  58.916  1.00139.88           C  
ANISOU 7773  CZ  ARG C 148    23120  17703  12325   -371     31    756       C  
ATOM   7774  NH1 ARG C 148     -49.260  34.379  60.227  1.00134.35           N  
ANISOU 7774  NH1 ARG C 148    22697  17046  11302   -347     64    837       N  
ATOM   7775  NH2 ARG C 148     -48.856  35.669  58.378  1.00122.67           N  
ANISOU 7775  NH2 ARG C 148    20680  15636  10293   -367    -65    570       N  
ATOM   7776  N   LYS C 149     -44.493  29.487  57.393  1.00112.36           N  
ANISOU 7776  N   LYS C 149    19914  13487   9290    317   -692   1333       N  
ATOM   7777  CA  LYS C 149     -43.046  29.646  57.239  1.00112.51           C  
ANISOU 7777  CA  LYS C 149    19791  13563   9396    536   -999   1294       C  
ATOM   7778  C   LYS C 149     -42.523  28.781  56.097  1.00116.21           C  
ANISOU 7778  C   LYS C 149    20135  13870  10149    609  -1010   1295       C  
ATOM   7779  O   LYS C 149     -41.627  29.220  55.377  1.00114.68           O  
ANISOU 7779  O   LYS C 149    19666  13764  10142    697  -1166   1170       O  
ATOM   7780  CB  LYS C 149     -42.302  29.343  58.551  1.00118.23           C  
ANISOU 7780  CB  LYS C 149    20775  14301   9848    734  -1222   1444       C  
ATOM   7781  CG  LYS C 149     -41.287  30.419  58.953  1.00132.98           C  
ANISOU 7781  CG  LYS C 149    22475  16396  11657    855  -1516   1319       C  
ATOM   7782  CD  LYS C 149     -39.932  30.293  58.240  1.00142.02           C  
ANISOU 7782  CD  LYS C 149    23371  17550  13040   1040  -1760   1261       C  
ATOM   7783  CE  LYS C 149     -38.862  29.663  59.101  1.00154.55           C  
ANISOU 7783  CE  LYS C 149    25120  19119  14482   1304  -2044   1404       C  
ATOM   7784  NZ  LYS C 149     -39.062  28.198  59.271  1.00164.75           N  
ANISOU 7784  NZ  LYS C 149    26709  20153  15736   1396  -1959   1633       N  
ATOM   7785  N   LEU C 150     -43.107  27.571  55.912  1.00113.80           N  
ANISOU 7785  N   LEU C 150    20029  13329   9880    560   -829   1424       N  
ATOM   7786  CA  LEU C 150     -42.739  26.638  54.840  1.00113.11           C  
ANISOU 7786  CA  LEU C 150    19864  13057  10055    618   -806   1417       C  
ATOM   7787  C   LEU C 150     -43.036  27.234  53.466  1.00112.32           C  
ANISOU 7787  C   LEU C 150    19427  13045  10203    472   -699   1209       C  
ATOM   7788  O   LEU C 150     -42.197  27.114  52.576  1.00111.28           O  
ANISOU 7788  O   LEU C 150    19094  12910  10279    580   -800   1123       O  
ATOM   7789  CB  LEU C 150     -43.421  25.263  55.016  1.00115.41           C  
ANISOU 7789  CB  LEU C 150    20471  13059  10322    564   -617   1592       C  
ATOM   7790  CG  LEU C 150     -42.999  24.128  54.054  1.00120.78           C  
ANISOU 7790  CG  LEU C 150    21137  13498  11253    650   -601   1596       C  
ATOM   7791  CD1 LEU C 150     -41.581  23.637  54.341  1.00123.13           C  
ANISOU 7791  CD1 LEU C 150    21476  13735  11572    974   -878   1678       C  
ATOM   7792  CD2 LEU C 150     -43.962  22.960  54.136  1.00124.94           C  
ANISOU 7792  CD2 LEU C 150    21954  13744  11773    509   -359   1732       C  
ATOM   7793  N   LEU C 151     -44.197  27.910  53.305  1.00106.33           N  
ANISOU 7793  N   LEU C 151    18601  12382   9417    238   -502   1128       N  
ATOM   7794  CA  LEU C 151     -44.573  28.559  52.045  1.00103.13           C  
ANISOU 7794  CA  LEU C 151    17889  12078   9219     97   -408    945       C  
ATOM   7795  C   LEU C 151     -43.591  29.680  51.674  1.00105.57           C  
ANISOU 7795  C   LEU C 151    17913  12589   9609    192   -610    809       C  
ATOM   7796  O   LEU C 151     -43.013  29.645  50.589  1.00103.99           O  
ANISOU 7796  O   LEU C 151    17499  12397   9616    231   -651    715       O  
ATOM   7797  CB  LEU C 151     -46.012  29.116  52.084  1.00101.92           C  
ANISOU 7797  CB  LEU C 151    17722  12000   9004   -146   -180    896       C  
ATOM   7798  CG  LEU C 151     -47.202  28.153  52.023  1.00107.41           C  
ANISOU 7798  CG  LEU C 151    18587  12525   9698   -322     77    970       C  
ATOM   7799  CD1 LEU C 151     -48.495  28.929  52.107  1.00106.36           C  
ANISOU 7799  CD1 LEU C 151    18374  12527   9509   -533    266    897       C  
ATOM   7800  CD2 LEU C 151     -47.220  27.337  50.732  1.00109.07           C  
ANISOU 7800  CD2 LEU C 151    18699  12594  10149   -367    150    908       C  
ATOM   7801  N   ALA C 152     -43.377  30.640  52.595  1.00102.66           N  
ANISOU 7801  N   ALA C 152    17553  12378   9074    226   -734    797       N  
ATOM   7802  CA  ALA C 152     -42.496  31.796  52.412  1.00101.56           C  
ANISOU 7802  CA  ALA C 152    17165  12427   8996    288   -925    669       C  
ATOM   7803  C   ALA C 152     -41.008  31.465  52.268  1.00107.09           C  
ANISOU 7803  C   ALA C 152    17768  13128   9794    505  -1163    675       C  
ATOM   7804  O   ALA C 152     -40.323  32.113  51.474  1.00105.72           O  
ANISOU 7804  O   ALA C 152    17314  13064   9790    517  -1247    551       O  
ATOM   7805  CB  ALA C 152     -42.700  32.793  53.544  1.00102.73           C  
ANISOU 7805  CB  ALA C 152    17390  12716   8926    264   -991    651       C  
ATOM   7806  N   GLU C 153     -40.505  30.483  53.037  1.00106.14           N  
ANISOU 7806  N   GLU C 153    17873  12889   9566    677  -1270    822       N  
ATOM   7807  CA  GLU C 153     -39.086  30.129  53.020  1.00107.52           C  
ANISOU 7807  CA  GLU C 153    17956  13070   9825    912  -1513    835       C  
ATOM   7808  C   GLU C 153     -38.687  29.025  52.050  1.00110.36           C  
ANISOU 7808  C   GLU C 153    18266  13264  10401   1008  -1465    849       C  
ATOM   7809  O   GLU C 153     -37.543  29.022  51.595  1.00109.86           O  
ANISOU 7809  O   GLU C 153    17994  13257  10489   1164  -1625    785       O  
ATOM   7810  CB  GLU C 153     -38.576  29.833  54.440  1.00112.30           C  
ANISOU 7810  CB  GLU C 153    18806  13675  10188   1088  -1717    976       C  
ATOM   7811  CG  GLU C 153     -37.309  30.584  54.822  1.00128.48           C  
ANISOU 7811  CG  GLU C 153    20665  15918  12232   1237  -2021    898       C  
ATOM   7812  CD  GLU C 153     -37.346  32.102  54.758  1.00157.86           C  
ANISOU 7812  CD  GLU C 153    24164  19856  15958   1090  -2055    723       C  
ATOM   7813  OE1 GLU C 153     -36.367  32.692  54.246  1.00157.20           O  
ANISOU 7813  OE1 GLU C 153    23785  19901  16045   1139  -2208    600       O  
ATOM   7814  OE2 GLU C 153     -38.345  32.703  55.218  1.00154.37           O  
ANISOU 7814  OE2 GLU C 153    23841  19451  15360    927  -1924    708       O  
ATOM   7815  N   LYS C 154     -39.597  28.085  51.742  1.00106.82           N  
ANISOU 7815  N   LYS C 154    18002  12612   9972    917  -1247    920       N  
ATOM   7816  CA  LYS C 154     -39.269  26.972  50.849  1.00107.25           C  
ANISOU 7816  CA  LYS C 154    18043  12481  10227   1006  -1191    921       C  
ATOM   7817  C   LYS C 154     -40.212  26.554  49.717  1.00109.30           C  
ANISOU 7817  C   LYS C 154    18268  12628  10631    814   -931    845       C  
ATOM   7818  O   LYS C 154     -39.732  26.052  48.700  1.00108.86           O  
ANISOU 7818  O   LYS C 154    18079  12509  10775    879   -912    762       O  
ATOM   7819  CB  LYS C 154     -39.144  25.638  51.622  1.00112.90           C  
ANISOU 7819  CB  LYS C 154    19097  12945  10854   1169  -1225   1119       C  
ATOM   7820  CG  LYS C 154     -38.011  25.575  52.655  1.00130.99           C  
ANISOU 7820  CG  LYS C 154    21461  15283  13027   1439  -1516   1226       C  
ATOM   7821  CD  LYS C 154     -36.628  25.354  52.033  1.00142.20           C  
ANISOU 7821  CD  LYS C 154    22635  16734  14659   1680  -1704   1146       C  
ATOM   7822  CE  LYS C 154     -35.518  25.295  53.062  1.00154.47           C  
ANISOU 7822  CE  LYS C 154    24237  18353  16100   1953  -2013   1246       C  
ATOM   7823  NZ  LYS C 154     -35.177  26.639  53.609  1.00159.78           N  
ANISOU 7823  NZ  LYS C 154    24736  19320  16653   1906  -2181   1160       N  
ATOM   7824  N   VAL C 155     -41.486  26.893  49.754  1.00104.33           N  
ANISOU 7824  N   VAL C 155    17702  12016   9921    576   -740    837       N  
ATOM   7825  CA  VAL C 155     -42.511  26.493  48.772  1.00103.12           C  
ANISOU 7825  CA  VAL C 155    17527  11770   9885    374   -500    766       C  
ATOM   7826  C   VAL C 155     -42.565  27.612  47.708  1.00104.73           C  
ANISOU 7826  C   VAL C 155    17394  12194  10206    261   -478    583       C  
ATOM   7827  O   VAL C 155     -42.973  27.355  46.575  1.00103.34           O  
ANISOU 7827  O   VAL C 155    17108  11986  10169    153   -347    484       O  
ATOM   7828  CB  VAL C 155     -43.918  26.085  49.319  1.00107.62           C  
ANISOU 7828  CB  VAL C 155    18341  12223  10328    172   -287    860       C  
ATOM   7829  CG1 VAL C 155     -44.829  25.567  48.205  1.00106.51           C  
ANISOU 7829  CG1 VAL C 155    18146  11985  10339    -23    -72    767       C  
ATOM   7830  CG2 VAL C 155     -43.804  25.036  50.427  1.00110.58           C  
ANISOU 7830  CG2 VAL C 155    19070  12380  10565    284   -311   1067       C  
ATOM   7831  N   VAL C 156     -42.104  28.824  48.053  1.00100.65           N  
ANISOU 7831  N   VAL C 156    16721  11889   9632    290   -616    540       N  
ATOM   7832  CA  VAL C 156     -42.077  29.965  47.138  1.00 98.24           C  
ANISOU 7832  CA  VAL C 156    16116  11780   9429    193   -610    391       C  
ATOM   7833  C   VAL C 156     -41.223  29.722  45.867  1.00102.58           C  
ANISOU 7833  C   VAL C 156    16446  12345  10183    267   -636    287       C  
ATOM   7834  O   VAL C 156     -41.613  30.168  44.793  1.00100.72           O  
ANISOU 7834  O   VAL C 156    16033  12194  10041    137   -534    181       O  
ATOM   7835  CB  VAL C 156     -41.754  31.295  47.878  1.00101.49           C  
ANISOU 7835  CB  VAL C 156    16440  12383   9740    203   -752    370       C  
ATOM   7836  CG1 VAL C 156     -40.273  31.410  48.238  1.00102.53           C  
ANISOU 7836  CG1 VAL C 156    16486  12577   9896    411   -994    372       C  
ATOM   7837  CG2 VAL C 156     -42.233  32.511  47.092  1.00 98.90           C  
ANISOU 7837  CG2 VAL C 156    15882  12215   9482     42   -683    247       C  
ATOM   7838  N   TYR C 157     -40.095  28.990  45.981  1.00101.35           N  
ANISOU 7838  N   TYR C 157    16308  12113  10089    483   -765    319       N  
ATOM   7839  CA  TYR C 157     -39.203  28.724  44.844  1.00101.37           C  
ANISOU 7839  CA  TYR C 157    16097  12138  10280    576   -782    213       C  
ATOM   7840  C   TYR C 157     -39.679  27.583  43.934  1.00106.61           C  
ANISOU 7840  C   TYR C 157    16841  12622  11045    537   -610    173       C  
ATOM   7841  O   TYR C 157     -39.749  27.763  42.714  1.00105.07           O  
ANISOU 7841  O   TYR C 157    16463  12501  10958    452   -515     46       O  
ATOM   7842  CB  TYR C 157     -37.751  28.506  45.308  1.00104.26           C  
ANISOU 7842  CB  TYR C 157    16400  12523  10690    836   -999    240       C  
ATOM   7843  CG  TYR C 157     -37.227  29.613  46.198  1.00105.68           C  
ANISOU 7843  CG  TYR C 157    16493  12886  10774    866  -1187    257       C  
ATOM   7844  CD1 TYR C 157     -37.148  29.446  47.577  1.00109.49           C  
ANISOU 7844  CD1 TYR C 157    17193  13323  11087    968  -1323    385       C  
ATOM   7845  CD2 TYR C 157     -36.843  30.840  45.666  1.00104.77           C  
ANISOU 7845  CD2 TYR C 157    16095  12985  10728    781  -1224    144       C  
ATOM   7846  CE1 TYR C 157     -36.681  30.467  48.406  1.00110.60           C  
ANISOU 7846  CE1 TYR C 157    17260  13635  11126    987  -1504    379       C  
ATOM   7847  CE2 TYR C 157     -36.378  31.870  46.483  1.00105.90           C  
ANISOU 7847  CE2 TYR C 157    16164  13279  10794    791  -1397    142       C  
ATOM   7848  CZ  TYR C 157     -36.298  31.679  47.854  1.00114.80           C  
ANISOU 7848  CZ  TYR C 157    17503  14367  11750    894  -1541    249       C  
ATOM   7849  OH  TYR C 157     -35.839  32.693  48.662  1.00114.61           O  
ANISOU 7849  OH  TYR C 157    17410  14496  11639    898  -1720    225       O  
ATOM   7850  N   VAL C 158     -40.011  26.424  44.530  1.00105.52           N  
ANISOU 7850  N   VAL C 158    16986  12243  10863    591   -571    282       N  
ATOM   7851  CA  VAL C 158     -40.489  25.224  43.829  1.00106.29           C  
ANISOU 7851  CA  VAL C 158    17209  12120  11055    551   -413    250       C  
ATOM   7852  C   VAL C 158     -41.887  25.456  43.219  1.00108.41           C  
ANISOU 7852  C   VAL C 158    17471  12416  11305    265   -214    183       C  
ATOM   7853  O   VAL C 158     -42.170  24.962  42.128  1.00107.66           O  
ANISOU 7853  O   VAL C 158    17322  12266  11318    188    -95     67       O  
ATOM   7854  CB  VAL C 158     -40.449  23.975  44.765  1.00112.99           C  
ANISOU 7854  CB  VAL C 158    18388  12683  11859    684   -434    409       C  
ATOM   7855  CG1 VAL C 158     -41.019  22.728  44.085  1.00113.84           C  
ANISOU 7855  CG1 VAL C 158    18650  12529  12073    616   -261    371       C  
ATOM   7856  CG2 VAL C 158     -39.031  23.706  45.265  1.00114.81           C  
ANISOU 7856  CG2 VAL C 158    18601  12897  12124    994   -651    467       C  
ATOM   7857  N   GLY C 159     -42.726  26.210  43.924  1.00104.14           N  
ANISOU 7857  N   GLY C 159    16975  11968  10625    120   -186    245       N  
ATOM   7858  CA  GLY C 159     -44.099  26.487  43.517  1.00102.55           C  
ANISOU 7858  CA  GLY C 159    16757  11808  10398   -137    -12    195       C  
ATOM   7859  C   GLY C 159     -44.171  27.588  42.480  1.00103.99           C  
ANISOU 7859  C   GLY C 159    16647  12229  10637   -232     -6     58       C  
ATOM   7860  O   GLY C 159     -44.880  27.419  41.486  1.00103.21           O  
ANISOU 7860  O   GLY C 159    16476  12139  10599   -380    120    -41       O  
ATOM   7861  N   VAL C 160     -43.485  28.735  42.705  1.00 99.17           N  
ANISOU 7861  N   VAL C 160    15872  11808   9998   -160   -140     53       N  
ATOM   7862  CA  VAL C 160     -43.500  29.864  41.759  1.00 96.80           C  
ANISOU 7862  CA  VAL C 160    15308  11723   9748   -247   -138    -54       C  
ATOM   7863  C   VAL C 160     -42.361  30.128  40.758  1.00100.28           C  
ANISOU 7863  C   VAL C 160    15523  12273  10308   -150   -206   -148       C  
ATOM   7864  O   VAL C 160     -42.637  30.334  39.575  1.00 99.28           O  
ANISOU 7864  O   VAL C 160    15253  12231  10238   -249   -121   -245       O  
ATOM   7865  CB  VAL C 160     -43.785  31.135  42.622  1.00 99.58           C  
ANISOU 7865  CB  VAL C 160    15630  12214   9993   -293   -203     -9       C  
ATOM   7866  CG1 VAL C 160     -43.784  32.409  41.783  1.00 97.45           C  
ANISOU 7866  CG1 VAL C 160    15110  12142   9772   -375   -213    -94       C  
ATOM   7867  CG2 VAL C 160     -45.095  31.008  43.393  1.00 99.58           C  
ANISOU 7867  CG2 VAL C 160    15808  12150   9878   -425    -89     55       C  
ATOM   7868  N   TRP C 161     -41.098  30.128  41.234  1.00 97.36           N  
ANISOU 7868  N   TRP C 161    15113  11913   9965     40   -356   -119       N  
ATOM   7869  CA  TRP C 161     -39.898  30.414  40.437  1.00 96.89           C  
ANISOU 7869  CA  TRP C 161    14820  11973  10022    141   -422   -203       C  
ATOM   7870  C   TRP C 161     -39.519  29.307  39.455  1.00102.05           C  
ANISOU 7870  C   TRP C 161    15459  12531  10786    217   -341   -287       C  
ATOM   7871  O   TRP C 161     -39.272  29.611  38.288  1.00101.30           O  
ANISOU 7871  O   TRP C 161    15174  12558  10759    171   -279   -392       O  
ATOM   7872  CB  TRP C 161     -38.714  30.822  41.320  1.00 96.33           C  
ANISOU 7872  CB  TRP C 161    14685  11964   9951    310   -618   -156       C  
ATOM   7873  CG  TRP C 161     -38.881  32.180  41.930  1.00 95.85           C  
ANISOU 7873  CG  TRP C 161    14558  12049   9812    219   -697   -132       C  
ATOM   7874  CD1 TRP C 161     -39.307  32.465  43.193  1.00 98.92           C  
ANISOU 7874  CD1 TRP C 161    15112  12408  10064    211   -765    -46       C  
ATOM   7875  CD2 TRP C 161     -38.688  33.440  41.275  1.00 94.26           C  
ANISOU 7875  CD2 TRP C 161    14124  12031   9659    114   -701   -199       C  
ATOM   7876  NE1 TRP C 161     -39.366  33.827  43.376  1.00 97.11           N  
ANISOU 7876  NE1 TRP C 161    14763  12329   9806    117   -818    -74       N  
ATOM   7877  CE2 TRP C 161     -38.989  34.451  42.215  1.00 97.55           C  
ANISOU 7877  CE2 TRP C 161    14577  12506   9981     55   -782   -160       C  
ATOM   7878  CE3 TRP C 161     -38.268  33.816  39.988  1.00 94.65           C  
ANISOU 7878  CE3 TRP C 161    13949  12198   9817     65   -638   -286       C  
ATOM   7879  CZ2 TRP C 161     -38.891  35.814  41.907  1.00 95.65           C  
ANISOU 7879  CZ2 TRP C 161    14161  12411   9772    -51   -807   -204       C  
ATOM   7880  CZ3 TRP C 161     -38.164  35.165  39.685  1.00 94.91           C  
ANISOU 7880  CZ3 TRP C 161    13811  12384   9869    -45   -659   -310       C  
ATOM   7881  CH2 TRP C 161     -38.476  36.147  40.636  1.00 95.00           C  
ANISOU 7881  CH2 TRP C 161    13867  12425   9804   -101   -746   -270       C  
ATOM   7882  N   ILE C 162     -39.464  28.039  39.910  1.00100.22           N  
ANISOU 7882  N   ILE C 162    15434  12076  10568    334   -336   -241       N  
ATOM   7883  CA  ILE C 162     -39.155  26.891  39.047  1.00101.45           C  
ANISOU 7883  CA  ILE C 162    15612  12099  10835    416   -253   -331       C  
ATOM   7884  C   ILE C 162     -40.195  26.731  37.900  1.00104.16           C  
ANISOU 7884  C   ILE C 162    15946  12447  11182    208    -73   -441       C  
ATOM   7885  O   ILE C 162     -39.759  26.679  36.747  1.00103.78           O  
ANISOU 7885  O   ILE C 162    15741  12484  11208    220    -16   -572       O  
ATOM   7886  CB  ILE C 162     -38.838  25.589  39.862  1.00107.27           C  
ANISOU 7886  CB  ILE C 162    16596  12567  11596    603   -300   -243       C  
ATOM   7887  CG1 ILE C 162     -37.340  25.501  40.219  1.00109.69           C  
ANISOU 7887  CG1 ILE C 162    16792  12906  11980    879   -471   -228       C  
ATOM   7888  CG2 ILE C 162     -39.310  24.293  39.179  1.00109.10           C  
ANISOU 7888  CG2 ILE C 162    16984  12568  11903    579   -151   -316       C  
ATOM   7889  CD1 ILE C 162     -36.970  26.082  41.578  1.00118.92           C  
ANISOU 7889  CD1 ILE C 162    18003  14135  13047    965   -658    -87       C  
ATOM   7890  N   PRO C 163     -41.541  26.732  38.154  1.00 99.73           N  
ANISOU 7890  N   PRO C 163    15526  11830  10537     12     16   -401       N  
ATOM   7891  CA  PRO C 163     -42.498  26.601  37.040  1.00 98.79           C  
ANISOU 7891  CA  PRO C 163    15371  11741  10424   -182    162   -517       C  
ATOM   7892  C   PRO C 163     -42.435  27.756  36.049  1.00101.02           C  
ANISOU 7892  C   PRO C 163    15398  12292  10695   -269    167   -598       C  
ATOM   7893  O   PRO C 163     -42.591  27.525  34.850  1.00100.33           O  
ANISOU 7893  O   PRO C 163    15232  12256  10633   -337    254   -725       O  
ATOM   7894  CB  PRO C 163     -43.860  26.537  37.745  1.00100.14           C  
ANISOU 7894  CB  PRO C 163    15710  11828  10509   -359    230   -438       C  
ATOM   7895  CG  PRO C 163     -43.555  26.121  39.133  1.00105.76           C  
ANISOU 7895  CG  PRO C 163    16622  12381  11182   -234    156   -287       C  
ATOM   7896  CD  PRO C 163     -42.262  26.796  39.440  1.00101.19           C  
ANISOU 7896  CD  PRO C 163    15904  11929  10615    -42     -4   -258       C  
ATOM   7897  N   ALA C 164     -42.166  28.983  36.544  1.00 97.00           N  
ANISOU 7897  N   ALA C 164    14770  11945  10141   -264     72   -525       N  
ATOM   7898  CA  ALA C 164     -42.050  30.190  35.725  1.00 95.85           C  
ANISOU 7898  CA  ALA C 164    14398  12036   9986   -343     67   -569       C  
ATOM   7899  C   ALA C 164     -40.874  30.111  34.741  1.00102.26           C  
ANISOU 7899  C   ALA C 164    15037  12940  10877   -239     70   -664       C  
ATOM   7900  O   ALA C 164     -40.982  30.627  33.626  1.00101.45           O  
ANISOU 7900  O   ALA C 164    14792  12994  10761   -332    132   -735       O  
ATOM   7901  CB  ALA C 164     -41.929  31.420  36.605  1.00 95.44           C  
ANISOU 7901  CB  ALA C 164    14288  12088   9889   -347    -40   -472       C  
ATOM   7902  N   LEU C 165     -39.778  29.434  35.136  1.00101.45           N  
ANISOU 7902  N   LEU C 165    14948  12745  10851    -40      8   -664       N  
ATOM   7903  CA  LEU C 165     -38.610  29.231  34.280  1.00102.97           C  
ANISOU 7903  CA  LEU C 165    14970  13018  11134     83     24   -765       C  
ATOM   7904  C   LEU C 165     -38.877  28.099  33.282  1.00108.99           C  
ANISOU 7904  C   LEU C 165    15805  13682  11925     77    159   -898       C  
ATOM   7905  O   LEU C 165     -38.370  28.132  32.159  1.00108.87           O  
ANISOU 7905  O   LEU C 165    15640  13791  11936     87    233  -1015       O  
ATOM   7906  CB  LEU C 165     -37.357  28.943  35.120  1.00104.70           C  
ANISOU 7906  CB  LEU C 165    15159  13186  11436    314   -107   -722       C  
ATOM   7907  CG  LEU C 165     -36.782  30.138  35.889  1.00109.02           C  
ANISOU 7907  CG  LEU C 165    15572  13878  11972    327   -251   -636       C  
ATOM   7908  CD1 LEU C 165     -36.099  29.688  37.161  1.00110.86           C  
ANISOU 7908  CD1 LEU C 165    15893  13999  12229    523   -408   -553       C  
ATOM   7909  CD2 LEU C 165     -35.813  30.940  35.028  1.00111.67           C  
ANISOU 7909  CD2 LEU C 165    15618  14436  12376    325   -240   -708       C  
ATOM   7910  N   LEU C 166     -39.692  27.108  33.691  1.00107.09           N  
ANISOU 7910  N   LEU C 166    15801  13216  11674     50    199   -886       N  
ATOM   7911  CA  LEU C 166     -40.093  25.981  32.847  1.00108.54           C  
ANISOU 7911  CA  LEU C 166    16088  13266  11886     18    323  -1022       C  
ATOM   7912  C   LEU C 166     -41.023  26.468  31.731  1.00111.51           C  
ANISOU 7912  C   LEU C 166    16387  13804  12178   -204    419  -1112       C  
ATOM   7913  O   LEU C 166     -40.942  25.980  30.604  1.00112.01           O  
ANISOU 7913  O   LEU C 166    16414  13895  12248   -220    512  -1267       O  
ATOM   7914  CB  LEU C 166     -40.779  24.880  33.696  1.00109.90           C  
ANISOU 7914  CB  LEU C 166    16543  13140  12073     16    337   -963       C  
ATOM   7915  CG  LEU C 166     -39.947  23.642  34.144  1.00117.36           C  
ANISOU 7915  CG  LEU C 166    17632  13830  13129    251    310   -963       C  
ATOM   7916  CD1 LEU C 166     -39.649  22.684  32.985  1.00119.31           C  
ANISOU 7916  CD1 LEU C 166    17878  13993  13460    305    421  -1160       C  
ATOM   7917  CD2 LEU C 166     -38.687  24.019  34.935  1.00120.03           C  
ANISOU 7917  CD2 LEU C 166    17872  14224  13511    484    159   -865       C  
ATOM   7918  N   LEU C 167     -41.866  27.468  32.046  1.00106.57           N  
ANISOU 7918  N   LEU C 167    15731  13296  11466   -360    389  -1019       N  
ATOM   7919  CA  LEU C 167     -42.823  28.102  31.136  1.00105.45           C  
ANISOU 7919  CA  LEU C 167    15507  13323  11236   -560    446  -1069       C  
ATOM   7920  C   LEU C 167     -42.160  29.129  30.202  1.00109.27           C  
ANISOU 7920  C   LEU C 167    15767  14065  11687   -559    443  -1096       C  
ATOM   7921  O   LEU C 167     -42.791  29.598  29.249  1.00108.39           O  
ANISOU 7921  O   LEU C 167    15584  14107  11493   -698    489  -1145       O  
ATOM   7922  CB  LEU C 167     -43.920  28.778  31.971  1.00104.07           C  
ANISOU 7922  CB  LEU C 167    15385  13158  11001   -692    409   -948       C  
ATOM   7923  CG  LEU C 167     -45.262  28.051  32.130  1.00109.15           C  
ANISOU 7923  CG  LEU C 167    16184  13666  11622   -845    479   -973       C  
ATOM   7924  CD1 LEU C 167     -45.104  26.647  32.737  1.00111.23           C  
ANISOU 7924  CD1 LEU C 167    16661  13644  11958   -768    513   -981       C  
ATOM   7925  CD2 LEU C 167     -46.186  28.863  32.994  1.00109.65           C  
ANISOU 7925  CD2 LEU C 167    16258  13774  11630   -948    448   -853       C  
ATOM   7926  N   THR C 168     -40.888  29.465  30.473  1.00106.13           N  
ANISOU 7926  N   THR C 168    15257  13716  11352   -406    387  -1061       N  
ATOM   7927  CA  THR C 168     -40.095  30.418  29.700  1.00105.39           C  
ANISOU 7927  CA  THR C 168    14946  13850  11246   -402    395  -1073       C  
ATOM   7928  C   THR C 168     -39.313  29.737  28.546  1.00109.90           C  
ANISOU 7928  C   THR C 168    15440  14476  11841   -325    499  -1229       C  
ATOM   7929  O   THR C 168     -38.792  30.426  27.667  1.00109.63           O  
ANISOU 7929  O   THR C 168    15238  14646  11771   -355    546  -1256       O  
ATOM   7930  CB  THR C 168     -39.299  31.319  30.671  1.00113.31           C  
ANISOU 7930  CB  THR C 168    15852  14898  12303   -324    276   -949       C  
ATOM   7931  OG1 THR C 168     -39.471  32.684  30.306  1.00113.54           O  
ANISOU 7931  OG1 THR C 168    15751  15113  12277   -448    263   -887       O  
ATOM   7932  CG2 THR C 168     -37.818  30.954  30.789  1.00112.04           C  
ANISOU 7932  CG2 THR C 168    15579  14738  12253   -129    247   -989       C  
ATOM   7933  N   ILE C 169     -39.253  28.383  28.561  1.00107.06           N  
ANISOU 7933  N   ILE C 169    15215  13924  11539   -228    544  -1333       N  
ATOM   7934  CA  ILE C 169     -38.589  27.521  27.570  1.00108.29           C  
ANISOU 7934  CA  ILE C 169    15337  14081  11728   -132    652  -1510       C  
ATOM   7935  C   ILE C 169     -39.140  27.722  26.136  1.00111.62           C  
ANISOU 7935  C   ILE C 169    15712  14682  12017   -290    763  -1629       C  
ATOM   7936  O   ILE C 169     -38.318  27.884  25.233  1.00111.82           O  
ANISOU 7936  O   ILE C 169    15592  14872  12024   -241    842  -1716       O  
ATOM   7937  CB  ILE C 169     -38.514  26.031  28.043  1.00113.11           C  
ANISOU 7937  CB  ILE C 169    16140  14396  12442      8    664  -1582       C  
ATOM   7938  CG1 ILE C 169     -37.711  25.911  29.370  1.00113.92           C  
ANISOU 7938  CG1 ILE C 169    16260  14365  12660    204    540  -1455       C  
ATOM   7939  CG2 ILE C 169     -37.936  25.104  26.954  1.00116.02           C  
ANISOU 7939  CG2 ILE C 169    16490  14749  12844    105    789  -1796       C  
ATOM   7940  CD1 ILE C 169     -37.841  24.576  30.144  1.00122.10           C  
ANISOU 7940  CD1 ILE C 169    17538  15073  13784    329    520  -1451       C  
ATOM   7941  N   PRO C 170     -40.481  27.787  25.879  1.00107.73           N  
ANISOU 7941  N   PRO C 170    15321  14190  11420   -480    769  -1632       N  
ATOM   7942  CA  PRO C 170     -40.944  28.047  24.498  1.00107.93           C  
ANISOU 7942  CA  PRO C 170    15292  14417  11300   -617    849  -1738       C  
ATOM   7943  C   PRO C 170     -40.494  29.413  23.973  1.00111.09           C  
ANISOU 7943  C   PRO C 170    15502  15089  11619   -660    846  -1644       C  
ATOM   7944  O   PRO C 170     -40.164  29.525  22.798  1.00111.46           O  
ANISOU 7944  O   PRO C 170    15467  15315  11568   -685    937  -1738       O  
ATOM   7945  CB  PRO C 170     -42.475  27.971  24.604  1.00108.87           C  
ANISOU 7945  CB  PRO C 170    15533  14482  11349   -801    815  -1725       C  
ATOM   7946  CG  PRO C 170     -42.747  27.244  25.869  1.00113.20           C  
ANISOU 7946  CG  PRO C 170    16238  14755  12018   -752    770  -1669       C  
ATOM   7947  CD  PRO C 170     -41.634  27.629  26.791  1.00108.33           C  
ANISOU 7947  CD  PRO C 170    15555  14106  11501   -579    706  -1544       C  
ATOM   7948  N   ASP C 171     -40.439  30.433  24.859  1.00106.66           N  
ANISOU 7948  N   ASP C 171    14880  14550  11098   -669    747  -1460       N  
ATOM   7949  CA  ASP C 171     -39.999  31.797  24.544  1.00105.97           C  
ANISOU 7949  CA  ASP C 171    14626  14674  10963   -716    734  -1347       C  
ATOM   7950  C   ASP C 171     -38.507  31.851  24.191  1.00110.56           C  
ANISOU 7950  C   ASP C 171    15046  15353  11608   -594    800  -1389       C  
ATOM   7951  O   ASP C 171     -38.092  32.771  23.491  1.00110.34           O  
ANISOU 7951  O   ASP C 171    14882  15526  11516   -656    846  -1343       O  
ATOM   7952  CB  ASP C 171     -40.327  32.767  25.700  1.00106.56           C  
ANISOU 7952  CB  ASP C 171    14699  14705  11086   -749    609  -1165       C  
ATOM   7953  CG  ASP C 171     -41.753  33.311  25.725  1.00120.13           C  
ANISOU 7953  CG  ASP C 171    16490  16442  12712   -901    563  -1095       C  
ATOM   7954  OD1 ASP C 171     -41.918  34.532  25.951  1.00119.92           O  
ANISOU 7954  OD1 ASP C 171    16397  16498  12669   -959    504   -963       O  
ATOM   7955  OD2 ASP C 171     -42.704  32.510  25.561  1.00128.08           O  
ANISOU 7955  OD2 ASP C 171    17615  17372  13678   -959    583  -1178       O  
ATOM   7956  N   PHE C 172     -37.711  30.862  24.653  1.00107.85           N  
ANISOU 7956  N   PHE C 172    14716  14868  11393   -420    809  -1474       N  
ATOM   7957  CA  PHE C 172     -36.285  30.759  24.333  1.00109.09           C  
ANISOU 7957  CA  PHE C 172    14701  15117  11633   -281    877  -1541       C  
ATOM   7958  C   PHE C 172     -36.119  30.279  22.881  1.00113.05           C  
ANISOU 7958  C   PHE C 172    15172  15753  12029   -298   1045  -1715       C  
ATOM   7959  O   PHE C 172     -35.464  30.949  22.082  1.00113.09           O  
ANISOU 7959  O   PHE C 172    15014  15979  11978   -334   1135  -1715       O  
ATOM   7960  CB  PHE C 172     -35.566  29.782  25.292  1.00112.34           C  
ANISOU 7960  CB  PHE C 172    15145  15323  12216    -64    820  -1580       C  
ATOM   7961  CG  PHE C 172     -34.953  30.368  26.544  1.00113.76           C  
ANISOU 7961  CG  PHE C 172    15244  15466  12513     16    675  -1437       C  
ATOM   7962  CD1 PHE C 172     -35.337  29.916  27.803  1.00116.63           C  
ANISOU 7962  CD1 PHE C 172    15768  15609  12936     85    548  -1361       C  
ATOM   7963  CD2 PHE C 172     -33.952  31.333  26.464  1.00116.52           C  
ANISOU 7963  CD2 PHE C 172    15359  16002  12911     19    669  -1386       C  
ATOM   7964  CE1 PHE C 172     -34.746  30.436  28.962  1.00117.32           C  
ANISOU 7964  CE1 PHE C 172    15791  15677  13110    165    402  -1241       C  
ATOM   7965  CE2 PHE C 172     -33.374  31.864  27.625  1.00119.19           C  
ANISOU 7965  CE2 PHE C 172    15619  16312  13356     85    520  -1275       C  
ATOM   7966  CZ  PHE C 172     -33.773  31.410  28.865  1.00116.79           C  
ANISOU 7966  CZ  PHE C 172    15483  15801  13092    164    381  -1208       C  
ATOM   7967  N   ILE C 173     -36.741  29.133  22.544  1.00109.51           N  
ANISOU 7967  N   ILE C 173    14891  15170  11546   -286   1091  -1865       N  
ATOM   7968  CA  ILE C 173     -36.681  28.509  21.216  1.00110.87           C  
ANISOU 7968  CA  ILE C 173    15075  15444  11608   -296   1243  -2066       C  
ATOM   7969  C   ILE C 173     -37.433  29.263  20.103  1.00113.14           C  
ANISOU 7969  C   ILE C 173    15357  15963  11669   -498   1290  -2053       C  
ATOM   7970  O   ILE C 173     -37.033  29.168  18.939  1.00114.53           O  
ANISOU 7970  O   ILE C 173    15474  16316  11725   -507   1426  -2179       O  
ATOM   7971  CB  ILE C 173     -37.009  26.984  21.247  1.00115.47           C  
ANISOU 7971  CB  ILE C 173    15844  15781  12248   -210   1274  -2252       C  
ATOM   7972  CG1 ILE C 173     -38.388  26.695  21.883  1.00114.46           C  
ANISOU 7972  CG1 ILE C 173    15919  15462  12107   -335   1172  -2195       C  
ATOM   7973  CG2 ILE C 173     -35.890  26.186  21.931  1.00117.83           C  
ANISOU 7973  CG2 ILE C 173    16111  15907  12754     41   1274  -2302       C  
ATOM   7974  CD1 ILE C 173     -39.189  25.611  21.191  1.00122.88           C  
ANISOU 7974  CD1 ILE C 173    17157  16423  13108   -406   1237  -2399       C  
ATOM   7975  N   PHE C 174     -38.502  30.010  20.453  1.00106.63           N  
ANISOU 7975  N   PHE C 174    14592  15143  10778   -649   1179  -1902       N  
ATOM   7976  CA  PHE C 174     -39.307  30.742  19.470  1.00105.65           C  
ANISOU 7976  CA  PHE C 174    14472  15227  10442   -825   1192  -1868       C  
ATOM   7977  C   PHE C 174     -38.942  32.202  19.189  1.00107.85           C  
ANISOU 7977  C   PHE C 174    14607  15718  10652   -897   1191  -1686       C  
ATOM   7978  O   PHE C 174     -39.234  32.680  18.091  1.00108.05           O  
ANISOU 7978  O   PHE C 174    14622  15950  10484  -1003   1246  -1684       O  
ATOM   7979  CB  PHE C 174     -40.820  30.538  19.681  1.00106.24           C  
ANISOU 7979  CB  PHE C 174    14698  15208  10459   -951   1094  -1861       C  
ATOM   7980  CG  PHE C 174     -41.310  29.139  19.372  1.00108.94           C  
ANISOU 7980  CG  PHE C 174    15186  15412  10795   -948   1137  -2082       C  
ATOM   7981  CD1 PHE C 174     -41.973  28.388  20.335  1.00111.30           C  
ANISOU 7981  CD1 PHE C 174    15619  15451  11219   -947   1068  -2093       C  
ATOM   7982  CD2 PHE C 174     -41.096  28.567  18.121  1.00112.69           C  
ANISOU 7982  CD2 PHE C 174    15674  16007  11135   -954   1254  -2284       C  
ATOM   7983  CE1 PHE C 174     -42.419  27.093  20.052  1.00113.59           C  
ANISOU 7983  CE1 PHE C 174    16053  15586  11519   -962   1114  -2298       C  
ATOM   7984  CE2 PHE C 174     -41.537  27.271  17.842  1.00116.92           C  
ANISOU 7984  CE2 PHE C 174    16354  16394  11676   -959   1292  -2508       C  
ATOM   7985  CZ  PHE C 174     -42.197  26.544  18.807  1.00114.54           C  
ANISOU 7985  CZ  PHE C 174    16184  15817  11520   -968   1220  -2511       C  
ATOM   7986  N   ALA C 175     -38.295  32.901  20.144  1.00102.44           N  
ANISOU 7986  N   ALA C 175    13821  14985  10117   -845   1128  -1536       N  
ATOM   7987  CA  ALA C 175     -37.898  34.298  19.937  1.00101.36           C  
ANISOU 7987  CA  ALA C 175    13554  15017   9943   -925   1130  -1364       C  
ATOM   7988  C   ALA C 175     -36.593  34.415  19.140  1.00106.09           C  
ANISOU 7988  C   ALA C 175    13990  15793  10528   -883   1287  -1418       C  
ATOM   7989  O   ALA C 175     -35.547  33.917  19.564  1.00106.51           O  
ANISOU 7989  O   ALA C 175    13941  15792  10735   -745   1324  -1492       O  
ATOM   7990  CB  ALA C 175     -37.795  35.037  21.264  1.00100.38           C  
ANISOU 7990  CB  ALA C 175    13392  14769   9978   -908    995  -1201       C  
ATOM   7991  N   ASN C 176     -36.679  35.059  17.963  1.00102.66           N  
ANISOU 7991  N   ASN C 176    13529  15579   9899  -1000   1381  -1380       N  
ATOM   7992  CA  ASN C 176     -35.576  35.294  17.028  1.00104.10           C  
ANISOU 7992  CA  ASN C 176    13564  15970  10017  -1002   1560  -1416       C  
ATOM   7993  C   ASN C 176     -35.771  36.639  16.332  1.00108.30           C  
ANISOU 7993  C   ASN C 176    14072  16686  10392  -1166   1586  -1223       C  
ATOM   7994  O   ASN C 176     -36.873  37.192  16.357  1.00106.40           O  
ANISOU 7994  O   ASN C 176    13948  16422  10058  -1260   1470  -1104       O  
ATOM   7995  CB  ASN C 176     -35.495  34.169  15.994  1.00104.28           C  
ANISOU 7995  CB  ASN C 176    13639  16077   9904   -948   1705  -1651       C  
ATOM   7996  CG  ASN C 176     -34.712  32.971  16.461  1.00118.71           C  
ANISOU 7996  CG  ASN C 176    15423  17767  11914   -757   1751  -1842       C  
ATOM   7997  OD1 ASN C 176     -33.484  32.925  16.356  1.00112.24           O  
ANISOU 7997  OD1 ASN C 176    14428  17030  11189   -666   1869  -1893       O  
ATOM   7998  ND2 ASN C 176     -35.405  31.958  16.963  1.00107.69           N  
ANISOU 7998  ND2 ASN C 176    14183  16158  10576   -691   1664  -1952       N  
ATOM   7999  N   VAL C 177     -34.702  37.167  15.716  1.00107.04           N  
ANISOU 7999  N   VAL C 177    13760  16705  10208  -1199   1742  -1187       N  
ATOM   8000  CA  VAL C 177     -34.745  38.448  15.013  1.00107.33           C  
ANISOU 8000  CA  VAL C 177    13778  16905  10097  -1359   1791   -988       C  
ATOM   8001  C   VAL C 177     -34.788  38.212  13.501  1.00113.14           C  
ANISOU 8001  C   VAL C 177    14564  17879  10544  -1414   1962  -1065       C  
ATOM   8002  O   VAL C 177     -33.962  37.468  12.970  1.00114.39           O  
ANISOU 8002  O   VAL C 177    14639  18141  10681  -1342   2133  -1243       O  
ATOM   8003  CB  VAL C 177     -33.591  39.403  15.443  1.00111.69           C  
ANISOU 8003  CB  VAL C 177    14131  17482  10823  -1402   1840   -855       C  
ATOM   8004  CG1 VAL C 177     -33.682  40.748  14.722  1.00112.29           C  
ANISOU 8004  CG1 VAL C 177    14218  17694  10754  -1581   1895   -629       C  
ATOM   8005  CG2 VAL C 177     -33.586  39.621  16.954  1.00109.34           C  
ANISOU 8005  CG2 VAL C 177    13799  16958  10786  -1346   1653   -796       C  
ATOM   8006  N   SER C 178     -35.765  38.838  12.823  1.00109.88           N  
ANISOU 8006  N   SER C 178    14290  17556   9904  -1531   1910   -936       N  
ATOM   8007  CA  SER C 178     -35.945  38.775  11.372  1.00112.26           C  
ANISOU 8007  CA  SER C 178    14669  18102   9884  -1600   2041   -974       C  
ATOM   8008  C   SER C 178     -35.630  40.150  10.763  1.00118.33           C  
ANISOU 8008  C   SER C 178    15407  19024  10529  -1743   2120   -716       C  
ATOM   8009  O   SER C 178     -35.438  41.112  11.508  1.00116.79           O  
ANISOU 8009  O   SER C 178    15148  18715  10512  -1790   2046   -523       O  
ATOM   8010  CB  SER C 178     -37.367  38.342  11.028  1.00115.12           C  
ANISOU 8010  CB  SER C 178    15221  18456  10062  -1617   1900  -1033       C  
ATOM   8011  OG  SER C 178     -38.320  39.319  11.415  1.00122.01           O  
ANISOU 8011  OG  SER C 178    16166  19256  10936  -1688   1717   -808       O  
ATOM   8012  N   GLU C 179     -35.572  40.242   9.421  1.00118.03           N  
ANISOU 8012  N   GLU C 179    15426  19235  10183  -1815   2270   -713       N  
ATOM   8013  CA  GLU C 179     -35.280  41.495   8.715  1.00119.69           C  
ANISOU 8013  CA  GLU C 179    15637  19599  10240  -1958   2366   -456       C  
ATOM   8014  C   GLU C 179     -36.507  42.035   7.969  1.00124.67           C  
ANISOU 8014  C   GLU C 179    16472  20318  10579  -2032   2244   -302       C  
ATOM   8015  O   GLU C 179     -37.521  41.338   7.871  1.00123.44           O  
ANISOU 8015  O   GLU C 179    16433  20147  10320  -1979   2107   -433       O  
ATOM   8016  CB  GLU C 179     -34.094  41.315   7.751  1.00124.28           C  
ANISOU 8016  CB  GLU C 179    16113  20422  10686  -1991   2664   -535       C  
ATOM   8017  CG  GLU C 179     -32.822  40.839   8.427  1.00135.26           C  
ANISOU 8017  CG  GLU C 179    17270  21752  12371  -1907   2787   -682       C  
ATOM   8018  CD  GLU C 179     -31.560  41.081   7.626  1.00159.58           C  
ANISOU 8018  CD  GLU C 179    20193  25065  15374  -1976   3087   -681       C  
ATOM   8019  OE1 GLU C 179     -31.092  42.242   7.596  1.00154.07           O  
ANISOU 8019  OE1 GLU C 179    19426  24401  14714  -2118   3153   -440       O  
ATOM   8020  OE2 GLU C 179     -31.027  40.108   7.046  1.00155.58           O  
ANISOU 8020  OE2 GLU C 179    19631  24700  14782  -1889   3266   -927       O  
ATOM   8021  N   ALA C 180     -36.416  43.282   7.453  1.00123.24           N  
ANISOU 8021  N   ALA C 180    16329  20223  10273  -2156   2287    -20       N  
ATOM   8022  CA  ALA C 180     -37.476  43.953   6.687  1.00123.91           C  
ANISOU 8022  CA  ALA C 180    16602  20404  10073  -2218   2172    172       C  
ATOM   8023  C   ALA C 180     -36.884  45.002   5.744  1.00129.90           C  
ANISOU 8023  C   ALA C 180    17391  21336  10627  -2353   2347    424       C  
ATOM   8024  O   ALA C 180     -36.074  44.670   4.881  1.00131.79           O  
ANISOU 8024  O   ALA C 180    17594  21793  10687  -2392   2587    341       O  
ATOM   8025  CB  ALA C 180     -38.490  44.599   7.626  1.00122.03           C  
ANISOU 8025  CB  ALA C 180    16419  19935  10012  -2195   1904    327       C  
ATOM   8026  N   ARG C 183     -35.476  47.052   8.415  1.00116.17           N  
ANISOU 8026  N   ARG C 183    15347  19043   9751  -2457   2279    772       N  
ATOM   8027  CA  ARG C 183     -35.691  47.045   9.860  1.00113.13           C  
ANISOU 8027  CA  ARG C 183    14893  18386   9706  -2381   2089    721       C  
ATOM   8028  C   ARG C 183     -35.590  45.649  10.483  1.00114.19           C  
ANISOU 8028  C   ARG C 183    14937  18481   9969  -2236   2059    408       C  
ATOM   8029  O   ARG C 183     -35.975  44.657   9.858  1.00113.89           O  
ANISOU 8029  O   ARG C 183    14963  18573   9736  -2168   2084    229       O  
ATOM   8030  CB  ARG C 183     -37.054  47.670  10.213  1.00113.16           C  
ANISOU 8030  CB  ARG C 183    15062  18238   9697  -2354   1837    877       C  
ATOM   8031  CG  ARG C 183     -36.943  49.028  10.902  1.00125.18           C  
ANISOU 8031  CG  ARG C 183    16581  19553  11430  -2434   1765   1119       C  
ATOM   8032  CD  ARG C 183     -38.068  49.277  11.897  1.00132.18           C  
ANISOU 8032  CD  ARG C 183    17543  20214  12466  -2345   1505   1145       C  
ATOM   8033  NE  ARG C 183     -37.838  48.591  13.173  1.00137.74           N  
ANISOU 8033  NE  ARG C 183    18128  20764  13442  -2257   1432    942       N  
ATOM   8034  CZ  ARG C 183     -38.580  48.752  14.265  1.00147.44           C  
ANISOU 8034  CZ  ARG C 183    19388  21785  14848  -2185   1238    935       C  
ATOM   8035  NH1 ARG C 183     -38.292  48.085  15.374  1.00128.84           N  
ANISOU 8035  NH1 ARG C 183    16936  19310  12709  -2108   1187    758       N  
ATOM   8036  NH2 ARG C 183     -39.616  49.585  14.257  1.00134.51           N  
ANISOU 8036  NH2 ARG C 183    17880  20061  13167  -2181   1095   1107       N  
ATOM   8037  N   TYR C 184     -35.090  45.587  11.729  1.00108.29           N  
ANISOU 8037  N   TYR C 184    14053  17544   9548  -2187   1994    344       N  
ATOM   8038  CA  TYR C 184     -34.979  44.347  12.491  1.00106.31           C  
ANISOU 8038  CA  TYR C 184    13730  17210   9454  -2040   1943     83       C  
ATOM   8039  C   TYR C 184     -36.158  44.258  13.448  1.00105.98           C  
ANISOU 8039  C   TYR C 184    13800  16957   9511  -1966   1692     84       C  
ATOM   8040  O   TYR C 184     -36.444  45.220  14.165  1.00104.39           O  
ANISOU 8040  O   TYR C 184    13616  16600   9446  -2007   1567    251       O  
ATOM   8041  CB  TYR C 184     -33.654  44.279  13.272  1.00107.91           C  
ANISOU 8041  CB  TYR C 184    13707  17354   9938  -2019   2020     11       C  
ATOM   8042  CG  TYR C 184     -32.411  44.132  12.421  1.00112.78           C  
ANISOU 8042  CG  TYR C 184    14166  18189  10494  -2068   2287    -48       C  
ATOM   8043  CD1 TYR C 184     -32.237  43.030  11.589  1.00116.36           C  
ANISOU 8043  CD1 TYR C 184    14621  18815  10775  -1989   2433   -256       C  
ATOM   8044  CD2 TYR C 184     -31.362  45.041  12.523  1.00115.22           C  
ANISOU 8044  CD2 TYR C 184    14308  18526  10945  -2190   2400     79       C  
ATOM   8045  CE1 TYR C 184     -31.087  42.881  10.815  1.00120.82           C  
ANISOU 8045  CE1 TYR C 184    15030  19594  11284  -2023   2697   -325       C  
ATOM   8046  CE2 TYR C 184     -30.201  44.898  11.764  1.00119.33           C  
ANISOU 8046  CE2 TYR C 184    14658  19262  11422  -2241   2663     18       C  
ATOM   8047  CZ  TYR C 184     -30.069  43.817  10.906  1.00129.34           C  
ANISOU 8047  CZ  TYR C 184    15930  20714  12499  -2150   2817   -184       C  
ATOM   8048  OH  TYR C 184     -28.927  43.667  10.153  1.00133.39           O  
ANISOU 8048  OH  TYR C 184    16265  21451  12965  -2192   3095   -257       O  
ATOM   8049  N   ILE C 185     -36.863  43.120  13.437  1.00100.70           N  
ANISOU 8049  N   ILE C 185    13209  16281   8771  -1865   1628   -106       N  
ATOM   8050  CA  ILE C 185     -38.027  42.906  14.297  1.00 97.74           C  
ANISOU 8050  CA  ILE C 185    12932  15726   8477  -1803   1415   -124       C  
ATOM   8051  C   ILE C 185     -37.774  41.730  15.239  1.00 99.25           C  
ANISOU 8051  C   ILE C 185    13072  15779   8860  -1678   1382   -340       C  
ATOM   8052  O   ILE C 185     -37.453  40.628  14.789  1.00 99.51           O  
ANISOU 8052  O   ILE C 185    13092  15885   8831  -1615   1483   -540       O  
ATOM   8053  CB  ILE C 185     -39.366  42.797  13.489  1.00101.12           C  
ANISOU 8053  CB  ILE C 185    13524  16249   8649  -1824   1329   -110       C  
ATOM   8054  CG1 ILE C 185     -39.603  44.006  12.532  1.00103.06           C  
ANISOU 8054  CG1 ILE C 185    13837  16631   8690  -1931   1348    134       C  
ATOM   8055  CG2 ILE C 185     -40.578  42.570  14.402  1.00 99.90           C  
ANISOU 8055  CG2 ILE C 185    13442  15918   8596  -1769   1123   -137       C  
ATOM   8056  CD1 ILE C 185     -39.763  45.458  13.189  1.00110.55           C  
ANISOU 8056  CD1 ILE C 185    14791  17424   9787  -1983   1244    398       C  
ATOM   8057  N   CYS C 186     -37.898  41.987  16.551  1.00 93.39           N  
ANISOU 8057  N   CYS C 186    12310  14829   8344  -1638   1244   -296       N  
ATOM   8058  CA  CYS C 186     -37.707  40.990  17.597  1.00 91.71           C  
ANISOU 8058  CA  CYS C 186    12069  14459   8316  -1517   1189   -457       C  
ATOM   8059  C   CYS C 186     -39.050  40.591  18.207  1.00 93.08           C  
ANISOU 8059  C   CYS C 186    12382  14493   8491  -1484   1030   -485       C  
ATOM   8060  O   CYS C 186     -39.737  41.434  18.788  1.00 91.49           O  
ANISOU 8060  O   CYS C 186    12226  14201   8337  -1521    906   -344       O  
ATOM   8061  CB  CYS C 186     -36.726  41.493  18.656  1.00 91.31           C  
ANISOU 8061  CB  CYS C 186    11885  14300   8509  -1494   1159   -401       C  
ATOM   8062  SG  CYS C 186     -36.799  40.603  20.236  1.00 93.39           S  
ANISOU 8062  SG  CYS C 186    12164  14329   8989  -1348   1017   -518       S  
ATOM   8063  N   ASP C 187     -39.421  39.303  18.041  1.00 89.23           N  
ANISOU 8063  N   ASP C 187    11961  13988   7955  -1420   1045   -676       N  
ATOM   8064  CA  ASP C 187     -40.623  38.655  18.582  1.00 87.74           C  
ANISOU 8064  CA  ASP C 187    11892  13669   7777  -1398    926   -744       C  
ATOM   8065  C   ASP C 187     -40.586  37.141  18.394  1.00 90.83           C  
ANISOU 8065  C   ASP C 187    12333  14020   8157  -1327    986   -976       C  
ATOM   8066  O   ASP C 187     -39.716  36.633  17.688  1.00 91.32           O  
ANISOU 8066  O   ASP C 187    12343  14181   8172  -1289   1123  -1091       O  
ATOM   8067  CB  ASP C 187     -41.930  39.249  18.026  1.00 89.85           C  
ANISOU 8067  CB  ASP C 187    12244  14016   7879  -1490    841   -650       C  
ATOM   8068  CG  ASP C 187     -42.135  39.080  16.544  1.00107.23           C  
ANISOU 8068  CG  ASP C 187    14480  16436   9827  -1548    919   -702       C  
ATOM   8069  OD1 ASP C 187     -41.331  39.636  15.769  1.00110.02           O  
ANISOU 8069  OD1 ASP C 187    14778  16939  10087  -1582   1028   -631       O  
ATOM   8070  OD2 ASP C 187     -43.138  38.444  16.155  1.00115.10           O  
ANISOU 8070  OD2 ASP C 187    15560  17464  10710  -1571    867   -808       O  
ATOM   8071  N   ARG C 188     -41.524  36.423  19.039  1.00 86.10           N  
ANISOU 8071  N   ARG C 188    11837  13268   7609  -1311    895  -1048       N  
ATOM   8072  CA  ARG C 188     -41.634  34.965  18.961  1.00 86.28           C  
ANISOU 8072  CA  ARG C 188    11937  13202   7643  -1256    940  -1264       C  
ATOM   8073  C   ARG C 188     -42.219  34.576  17.605  1.00 90.07           C  
ANISOU 8073  C   ARG C 188    12474  13851   7896  -1334    993  -1386       C  
ATOM   8074  O   ARG C 188     -43.300  35.051  17.244  1.00 88.91           O  
ANISOU 8074  O   ARG C 188    12369  13787   7625  -1432    910  -1322       O  
ATOM   8075  CB  ARG C 188     -42.503  34.419  20.111  1.00 85.56           C  
ANISOU 8075  CB  ARG C 188    11944  12889   7678  -1243    832  -1276       C  
ATOM   8076  CG  ARG C 188     -41.934  34.671  21.510  1.00 95.47           C  
ANISOU 8076  CG  ARG C 188    13167  13974   9133  -1156    772  -1175       C  
ATOM   8077  CD  ARG C 188     -43.007  34.646  22.588  1.00103.27           C  
ANISOU 8077  CD  ARG C 188    14248  14802  10190  -1185    660  -1115       C  
ATOM   8078  NE  ARG C 188     -43.952  35.758  22.451  1.00110.35           N  
ANISOU 8078  NE  ARG C 188    15128  15794  11007  -1288    585   -982       N  
ATOM   8079  CZ  ARG C 188     -45.152  35.803  23.021  1.00122.12           C  
ANISOU 8079  CZ  ARG C 188    16681  17210  12508  -1342    507   -951       C  
ATOM   8080  NH1 ARG C 188     -45.938  36.855  22.839  1.00108.74           N  
ANISOU 8080  NH1 ARG C 188    14955  15612  10751  -1410    440   -833       N  
ATOM   8081  NH2 ARG C 188     -45.579  34.795  23.771  1.00106.85           N  
ANISOU 8081  NH2 ARG C 188    14842  15105  10653  -1326    502  -1033       N  
ATOM   8082  N   PHE C 189     -41.479  33.753  16.839  1.00 87.73           N  
ANISOU 8082  N   PHE C 189    12172  13620   7542  -1283   1128  -1564       N  
ATOM   8083  CA  PHE C 189     -41.885  33.289  15.513  1.00 88.87           C  
ANISOU 8083  CA  PHE C 189    12377  13936   7453  -1348   1192  -1716       C  
ATOM   8084  C   PHE C 189     -42.246  31.818  15.549  1.00 94.27           C  
ANISOU 8084  C   PHE C 189    13171  14470   8179  -1317   1209  -1963       C  
ATOM   8085  O   PHE C 189     -41.372  30.958  15.667  1.00 94.94           O  
ANISOU 8085  O   PHE C 189    13251  14454   8368  -1201   1309  -2108       O  
ATOM   8086  CB  PHE C 189     -40.813  33.593  14.455  1.00 92.12           C  
ANISOU 8086  CB  PHE C 189    12707  14570   7727  -1333   1354  -1736       C  
ATOM   8087  CG  PHE C 189     -40.695  35.062  14.128  1.00 93.06           C  
ANISOU 8087  CG  PHE C 189    12753  14859   7747  -1411   1342  -1491       C  
ATOM   8088  CD1 PHE C 189     -41.662  35.700  13.358  1.00 96.47           C  
ANISOU 8088  CD1 PHE C 189    13249  15451   7956  -1523   1270  -1399       C  
ATOM   8089  CD2 PHE C 189     -39.612  35.807  14.577  1.00 94.58           C  
ANISOU 8089  CD2 PHE C 189    12815  15046   8073  -1374   1398  -1352       C  
ATOM   8090  CE1 PHE C 189     -41.558  37.062  13.064  1.00 97.27           C  
ANISOU 8090  CE1 PHE C 189    13305  15679   7973  -1587   1257  -1156       C  
ATOM   8091  CE2 PHE C 189     -39.509  37.168  14.279  1.00 97.31           C  
ANISOU 8091  CE2 PHE C 189    13111  15521   8343  -1462   1394  -1123       C  
ATOM   8092  CZ  PHE C 189     -40.474  37.781  13.510  1.00 95.79           C  
ANISOU 8092  CZ  PHE C 189    13004  15465   7929  -1563   1329  -1020       C  
ATOM   8093  N   TYR C 190     -43.551  31.542  15.497  1.00 91.18           N  
ANISOU 8093  N   TYR C 190    12873  14048   7723  -1419   1105  -2009       N  
ATOM   8094  CA  TYR C 190     -44.105  30.194  15.563  1.00 92.42           C  
ANISOU 8094  CA  TYR C 190    13148  14043   7926  -1432   1106  -2235       C  
ATOM   8095  C   TYR C 190     -44.272  29.626  14.153  1.00100.56           C  
ANISOU 8095  C   TYR C 190    14233  15251   8724  -1492   1177  -2456       C  
ATOM   8096  O   TYR C 190     -44.427  30.420  13.222  1.00101.35           O  
ANISOU 8096  O   TYR C 190    14294  15613   8600  -1560   1170  -2387       O  
ATOM   8097  CB  TYR C 190     -45.451  30.201  16.316  1.00 92.15           C  
ANISOU 8097  CB  TYR C 190    13167  13885   7961  -1532    961  -2174       C  
ATOM   8098  CG  TYR C 190     -45.422  30.925  17.647  1.00 91.18           C  
ANISOU 8098  CG  TYR C 190    12998  13628   8020  -1488    885  -1949       C  
ATOM   8099  CD1 TYR C 190     -45.821  32.254  17.749  1.00 91.74           C  
ANISOU 8099  CD1 TYR C 190    12991  13827   8039  -1535    797  -1734       C  
ATOM   8100  CD2 TYR C 190     -45.008  30.276  18.807  1.00 91.03           C  
ANISOU 8100  CD2 TYR C 190    13024  13346   8216  -1393    897  -1954       C  
ATOM   8101  CE1 TYR C 190     -45.811  32.921  18.971  1.00 90.30           C  
ANISOU 8101  CE1 TYR C 190    12775  13518   8015  -1497    730  -1552       C  
ATOM   8102  CE2 TYR C 190     -44.983  30.937  20.034  1.00 89.76           C  
ANISOU 8102  CE2 TYR C 190    12832  13077   8197  -1355    823  -1760       C  
ATOM   8103  CZ  TYR C 190     -45.397  32.257  20.113  1.00 95.39           C  
ANISOU 8103  CZ  TYR C 190    13466  13924   8855  -1411    742  -1571       C  
ATOM   8104  OH  TYR C 190     -45.392  32.915  21.316  1.00 94.27           O  
ANISOU 8104  OH  TYR C 190    13301  13673   8843  -1375    672  -1402       O  
ATOM   8105  N   PRO C 191     -44.234  28.279  13.954  1.00 99.52           N  
ANISOU 8105  N   PRO C 191    14202  14980   8630  -1467   1244  -2720       N  
ATOM   8106  CA  PRO C 191     -44.362  27.733  12.587  1.00102.46           C  
ANISOU 8106  CA  PRO C 191    14635  15529   8767  -1525   1315  -2958       C  
ATOM   8107  C   PRO C 191     -45.717  27.983  11.915  1.00107.59           C  
ANISOU 8107  C   PRO C 191    15322  16350   9209  -1702   1185  -2981       C  
ATOM   8108  O   PRO C 191     -45.764  28.141  10.694  1.00108.89           O  
ANISOU 8108  O   PRO C 191    15497  16774   9103  -1754   1214  -3070       O  
ATOM   8109  CB  PRO C 191     -44.065  26.238  12.768  1.00105.71           C  
ANISOU 8109  CB  PRO C 191    15156  15685   9323  -1451   1400  -3226       C  
ATOM   8110  CG  PRO C 191     -43.390  26.130  14.109  1.00108.08           C  
ANISOU 8110  CG  PRO C 191    15429  15722   9916  -1309   1405  -3096       C  
ATOM   8111  CD  PRO C 191     -44.031  27.193  14.932  1.00100.75           C  
ANISOU 8111  CD  PRO C 191    14438  14807   9037  -1380   1264  -2817       C  
ATOM   8112  N   ASN C 192     -46.806  28.033  12.714  1.00103.29           N  
ANISOU 8112  N   ASN C 192    14789  15674   8782  -1789   1042  -2900       N  
ATOM   8113  CA  ASN C 192     -48.176  28.285  12.247  1.00103.69           C  
ANISOU 8113  CA  ASN C 192    14841  15875   8681  -1950    895  -2911       C  
ATOM   8114  C   ASN C 192     -49.050  28.932  13.338  1.00105.47           C  
ANISOU 8114  C   ASN C 192    15007  16002   9063  -1996    758  -2695       C  
ATOM   8115  O   ASN C 192     -48.540  29.260  14.413  1.00102.66           O  
ANISOU 8115  O   ASN C 192    14622  15480   8906  -1904    780  -2529       O  
ATOM   8116  CB  ASN C 192     -48.818  27.006  11.668  1.00107.00           C  
ANISOU 8116  CB  ASN C 192    15369  16242   9044  -2056    894  -3234       C  
ATOM   8117  CG  ASN C 192     -48.746  25.790  12.559  1.00129.48           C  
ANISOU 8117  CG  ASN C 192    18312  18728  12156  -2034    951  -3375       C  
ATOM   8118  OD1 ASN C 192     -48.988  25.853  13.764  1.00123.52           O  
ANISOU 8118  OD1 ASN C 192    17547  17761  11623  -2022    911  -3229       O  
ATOM   8119  ND2 ASN C 192     -48.451  24.639  11.973  1.00123.74           N  
ANISOU 8119  ND2 ASN C 192    17695  17917  11404  -2032   1047  -3668       N  
ATOM   8120  N   ASP C 193     -50.354  29.132  13.058  1.00103.10           N  
ANISOU 8120  N   ASP C 193    14682  15822   8670  -2132    617  -2704       N  
ATOM   8121  CA  ASP C 193     -51.276  29.753  14.014  1.00101.26           C  
ANISOU 8121  CA  ASP C 193    14377  15524   8573  -2175    495  -2520       C  
ATOM   8122  C   ASP C 193     -51.730  28.830  15.151  1.00103.20           C  
ANISOU 8122  C   ASP C 193    14676  15466   9070  -2219    509  -2595       C  
ATOM   8123  O   ASP C 193     -52.217  29.327  16.171  1.00100.64           O  
ANISOU 8123  O   ASP C 193    14301  15048   8890  -2221    453  -2427       O  
ATOM   8124  CB  ASP C 193     -52.457  30.447  13.307  1.00104.41           C  
ANISOU 8124  CB  ASP C 193    14697  16187   8787  -2279    334  -2475       C  
ATOM   8125  CG  ASP C 193     -52.161  31.890  12.923  1.00116.31           C  
ANISOU 8125  CG  ASP C 193    16132  17907  10155  -2205    287  -2220       C  
ATOM   8126  OD1 ASP C 193     -51.636  32.115  11.808  1.00119.01           O  
ANISOU 8126  OD1 ASP C 193    16498  18457  10262  -2187    324  -2243       O  
ATOM   8127  OD2 ASP C 193     -52.457  32.796  13.738  1.00119.72           O  
ANISOU 8127  OD2 ASP C 193    16492  18289  10708  -2168    221  -1998       O  
ATOM   8128  N   LEU C 194     -51.538  27.498  14.994  1.00100.97           N  
ANISOU 8128  N   LEU C 194    14508  15019   8838  -2249    594  -2844       N  
ATOM   8129  CA  LEU C 194     -51.891  26.497  16.012  1.00100.45           C  
ANISOU 8129  CA  LEU C 194    14526  14634   9005  -2297    628  -2919       C  
ATOM   8130  C   LEU C 194     -51.045  26.669  17.279  1.00102.37           C  
ANISOU 8130  C   LEU C 194    14793  14652   9452  -2146    691  -2732       C  
ATOM   8131  O   LEU C 194     -51.596  26.648  18.381  1.00100.95           O  
ANISOU 8131  O   LEU C 194    14621  14306   9431  -2182    662  -2628       O  
ATOM   8132  CB  LEU C 194     -51.764  25.053  15.481  1.00102.79           C  
ANISOU 8132  CB  LEU C 194    14960  14785   9311  -2349    711  -3227       C  
ATOM   8133  CG  LEU C 194     -52.645  24.628  14.307  1.00109.53           C  
ANISOU 8133  CG  LEU C 194    15816  15820   9980  -2521    646  -3469       C  
ATOM   8134  CD1 LEU C 194     -52.319  23.212  13.890  1.00112.09           C  
ANISOU 8134  CD1 LEU C 194    16296  15953  10341  -2547    749  -3777       C  
ATOM   8135  CD2 LEU C 194     -54.131  24.736  14.637  1.00111.91           C  
ANISOU 8135  CD2 LEU C 194    16039  16155  10326  -2709    518  -3452       C  
ATOM   8136  N   TRP C 195     -49.715  26.862  17.115  1.00 98.45           N  
ANISOU 8136  N   TRP C 195    14297  14169   8941  -1982    774  -2693       N  
ATOM   8137  CA  TRP C 195     -48.773  27.078  18.214  1.00 96.63           C  
ANISOU 8137  CA  TRP C 195    14069  13763   8884  -1825    817  -2526       C  
ATOM   8138  C   TRP C 195     -49.134  28.346  18.977  1.00 97.77           C  
ANISOU 8138  C   TRP C 195    14112  13980   9058  -1825    724  -2262       C  
ATOM   8139  O   TRP C 195     -49.096  28.339  20.203  1.00 95.77           O  
ANISOU 8139  O   TRP C 195    13887  13533   8969  -1779    715  -2144       O  
ATOM   8140  CB  TRP C 195     -47.327  27.150  17.699  1.00 96.19           C  
ANISOU 8140  CB  TRP C 195    13987  13774   8787  -1666    917  -2552       C  
ATOM   8141  CG  TRP C 195     -46.775  25.832  17.236  1.00 99.50           C  
ANISOU 8141  CG  TRP C 195    14515  14055   9235  -1612   1028  -2807       C  
ATOM   8142  CD1 TRP C 195     -46.946  25.258  16.011  1.00104.79           C  
ANISOU 8142  CD1 TRP C 195    15230  14843   9744  -1680   1074  -3046       C  
ATOM   8143  CD2 TRP C 195     -45.931  24.943  17.982  1.00 99.98           C  
ANISOU 8143  CD2 TRP C 195    14660  13832   9495  -1463   1103  -2853       C  
ATOM   8144  NE1 TRP C 195     -46.281  24.055  15.954  1.00106.06           N  
ANISOU 8144  NE1 TRP C 195    15499  14795  10004  -1585   1183  -3252       N  
ATOM   8145  CE2 TRP C 195     -45.647  23.837  17.150  1.00106.39           C  
ANISOU 8145  CE2 TRP C 195    15566  14583  10273  -1443   1200  -3130       C  
ATOM   8146  CE3 TRP C 195     -45.398  24.966  19.283  1.00 99.77           C  
ANISOU 8146  CE3 TRP C 195    14646  13595   9667  -1336   1088  -2689       C  
ATOM   8147  CZ2 TRP C 195     -44.853  22.765  17.573  1.00106.98           C  
ANISOU 8147  CZ2 TRP C 195    15743  14380  10524  -1290   1286  -3240       C  
ATOM   8148  CZ3 TRP C 195     -44.611  23.903  19.701  1.00102.63           C  
ANISOU 8148  CZ3 TRP C 195    15109  13698  10189  -1185   1160  -2786       C  
ATOM   8149  CH2 TRP C 195     -44.345  22.819  18.852  1.00105.82           C  
ANISOU 8149  CH2 TRP C 195    15602  14031  10573  -1157   1259  -3055       C  
ATOM   8150  N   VAL C 196     -49.540  29.411  18.245  1.00 94.34           N  
ANISOU 8150  N   VAL C 196    13573  13817   8455  -1877    653  -2174       N  
ATOM   8151  CA  VAL C 196     -49.958  30.721  18.778  1.00 92.22           C  
ANISOU 8151  CA  VAL C 196    13206  13637   8196  -1876    559  -1936       C  
ATOM   8152  C   VAL C 196     -51.153  30.538  19.720  1.00 95.05           C  
ANISOU 8152  C   VAL C 196    13574  13867   8675  -1968    496  -1909       C  
ATOM   8153  O   VAL C 196     -51.152  31.082  20.826  1.00 93.29           O  
ANISOU 8153  O   VAL C 196    13333  13540   8573  -1918    474  -1745       O  
ATOM   8154  CB  VAL C 196     -50.283  31.739  17.640  1.00 96.47           C  
ANISOU 8154  CB  VAL C 196    13656  14481   8517  -1919    491  -1870       C  
ATOM   8155  CG1 VAL C 196     -50.595  33.129  18.192  1.00 94.34           C  
ANISOU 8155  CG1 VAL C 196    13297  14271   8277  -1893    401  -1620       C  
ATOM   8156  CG2 VAL C 196     -49.154  31.814  16.615  1.00 97.57           C  
ANISOU 8156  CG2 VAL C 196    13797  14764   8512  -1853    581  -1914       C  
ATOM   8157  N   VAL C 197     -52.144  29.743  19.285  1.00 92.19           N  
ANISOU 8157  N   VAL C 197    13238  13513   8277  -2108    474  -2083       N  
ATOM   8158  CA  VAL C 197     -53.364  29.457  20.036  1.00 91.54           C  
ANISOU 8158  CA  VAL C 197    13148  13332   8301  -2228    433  -2090       C  
ATOM   8159  C   VAL C 197     -53.095  28.612  21.292  1.00 93.73           C  
ANISOU 8159  C   VAL C 197    13546  13291   8778  -2201    517  -2084       C  
ATOM   8160  O   VAL C 197     -53.647  28.931  22.346  1.00 91.76           O  
ANISOU 8160  O   VAL C 197    13278  12957   8631  -2221    499  -1958       O  
ATOM   8161  CB  VAL C 197     -54.472  28.900  19.105  1.00 97.84           C  
ANISOU 8161  CB  VAL C 197    13916  14260   8999  -2402    378  -2288       C  
ATOM   8162  CG1 VAL C 197     -55.658  28.372  19.893  1.00 98.09           C  
ANISOU 8162  CG1 VAL C 197    13939  14162   9170  -2548    367  -2329       C  
ATOM   8163  CG2 VAL C 197     -54.936  29.973  18.127  1.00 97.97           C  
ANISOU 8163  CG2 VAL C 197    13801  14600   8822  -2414    258  -2224       C  
ATOM   8164  N   VAL C 198     -52.222  27.578  21.190  1.00 91.23           N  
ANISOU 8164  N   VAL C 198    13355  12800   8508  -2142    609  -2211       N  
ATOM   8165  CA  VAL C 198     -51.833  26.704  22.315  1.00 90.92           C  
ANISOU 8165  CA  VAL C 198    13456  12442   8646  -2089    684  -2197       C  
ATOM   8166  C   VAL C 198     -51.242  27.541  23.467  1.00 92.81           C  
ANISOU 8166  C   VAL C 198    13674  12627   8964  -1950    666  -1960       C  
ATOM   8167  O   VAL C 198     -51.703  27.420  24.603  1.00 91.95           O  
ANISOU 8167  O   VAL C 198    13618  12360   8959  -1977    670  -1867       O  
ATOM   8168  CB  VAL C 198     -50.899  25.528  21.882  1.00 96.46           C  
ANISOU 8168  CB  VAL C 198    14289  12978   9382  -2012    776  -2375       C  
ATOM   8169  CG1 VAL C 198     -50.243  24.847  23.081  1.00 96.15           C  
ANISOU 8169  CG1 VAL C 198    14389  12624   9520  -1894    834  -2304       C  
ATOM   8170  CG2 VAL C 198     -51.653  24.500  21.051  1.00 98.60           C  
ANISOU 8170  CG2 VAL C 198    14624  13221   9617  -2178    800  -2628       C  
ATOM   8171  N   PHE C 199     -50.261  28.408  23.160  1.00 88.72           N  
ANISOU 8171  N   PHE C 199    13075  12249   8386  -1817    648  -1869       N  
ATOM   8172  CA  PHE C 199     -49.626  29.263  24.155  1.00 87.18           C  
ANISOU 8172  CA  PHE C 199    12847  12021   8258  -1693    619  -1666       C  
ATOM   8173  C   PHE C 199     -50.527  30.387  24.665  1.00 91.16           C  
ANISOU 8173  C   PHE C 199    13260  12630   8745  -1754    541  -1513       C  
ATOM   8174  O   PHE C 199     -50.409  30.757  25.836  1.00 89.41           O  
ANISOU 8174  O   PHE C 199    13061  12301   8608  -1696    524  -1378       O  
ATOM   8175  CB  PHE C 199     -48.271  29.794  23.664  1.00 88.75           C  
ANISOU 8175  CB  PHE C 199    12977  12326   8418  -1552    634  -1630       C  
ATOM   8176  CG  PHE C 199     -47.261  28.722  23.325  1.00 91.73           C  
ANISOU 8176  CG  PHE C 199    13428  12588   8837  -1451    719  -1775       C  
ATOM   8177  CD1 PHE C 199     -46.872  27.781  24.274  1.00 95.28           C  
ANISOU 8177  CD1 PHE C 199    14003  12767   9432  -1365    749  -1786       C  
ATOM   8178  CD2 PHE C 199     -46.670  28.675  22.071  1.00 94.72           C  
ANISOU 8178  CD2 PHE C 199    13754  13128   9106  -1428    773  -1894       C  
ATOM   8179  CE1 PHE C 199     -45.941  26.789  23.956  1.00 97.68           C  
ANISOU 8179  CE1 PHE C 199    14373  12952   9790  -1247    824  -1923       C  
ATOM   8180  CE2 PHE C 199     -45.734  27.688  21.758  1.00 99.12           C  
ANISOU 8180  CE2 PHE C 199    14370  13580   9711  -1319    863  -2044       C  
ATOM   8181  CZ  PHE C 199     -45.377  26.751  22.702  1.00 97.69           C  
ANISOU 8181  CZ  PHE C 199    14306  13118   9694  -1222    884  -2060       C  
ATOM   8182  N   GLN C 200     -51.442  30.909  23.809  1.00 89.64           N  
ANISOU 8182  N   GLN C 200    12971  12646   8444  -1862    488  -1541       N  
ATOM   8183  CA  GLN C 200     -52.384  31.973  24.196  1.00 89.11           C  
ANISOU 8183  CA  GLN C 200    12805  12686   8368  -1907    411  -1411       C  
ATOM   8184  C   GLN C 200     -53.383  31.478  25.241  1.00 93.79           C  
ANISOU 8184  C   GLN C 200    13441  13129   9064  -1995    432  -1413       C  
ATOM   8185  O   GLN C 200     -53.808  32.249  26.104  1.00 91.95           O  
ANISOU 8185  O   GLN C 200    13165  12895   8876  -1977    403  -1283       O  
ATOM   8186  CB  GLN C 200     -53.131  32.547  22.979  1.00 91.44           C  
ANISOU 8186  CB  GLN C 200    12986  13239   8520  -1985    338  -1445       C  
ATOM   8187  CG  GLN C 200     -53.137  34.078  22.915  1.00114.86           C  
ANISOU 8187  CG  GLN C 200    15844  16359  11436  -1920    258  -1262       C  
ATOM   8188  CD  GLN C 200     -53.770  34.750  24.119  1.00136.35           C  
ANISOU 8188  CD  GLN C 200    18533  19008  14267  -1905    226  -1134       C  
ATOM   8189  OE1 GLN C 200     -53.085  35.181  25.057  1.00127.99           O  
ANISOU 8189  OE1 GLN C 200    17509  17831  13288  -1812    244  -1023       O  
ATOM   8190  NE2 GLN C 200     -55.090  34.868  24.113  1.00132.70           N  
ANISOU 8190  NE2 GLN C 200    17991  18625  13803  -1994    177  -1157       N  
ATOM   8191  N   PHE C 201     -53.740  30.187  25.162  1.00 92.69           N  
ANISOU 8191  N   PHE C 201    13393  12859   8964  -2094    493  -1566       N  
ATOM   8192  CA  PHE C 201     -54.643  29.541  26.105  1.00 93.28           C  
ANISOU 8192  CA  PHE C 201    13528  12774   9140  -2203    541  -1578       C  
ATOM   8193  C   PHE C 201     -53.898  29.219  27.405  1.00 95.76           C  
ANISOU 8193  C   PHE C 201    13985  12845   9553  -2097    598  -1470       C  
ATOM   8194  O   PHE C 201     -54.502  29.296  28.475  1.00 95.27           O  
ANISOU 8194  O   PHE C 201    13951  12699   9550  -2137    624  -1384       O  
ATOM   8195  CB  PHE C 201     -55.260  28.272  25.492  1.00 97.58           C  
ANISOU 8195  CB  PHE C 201    14129  13251   9697  -2366    586  -1784       C  
ATOM   8196  CG  PHE C 201     -56.333  27.637  26.346  1.00100.62           C  
ANISOU 8196  CG  PHE C 201    14554  13492  10185  -2521    646  -1800       C  
ATOM   8197  CD1 PHE C 201     -56.080  26.469  27.053  1.00105.00           C  
ANISOU 8197  CD1 PHE C 201    15298  13753  10844  -2547    747  -1828       C  
ATOM   8198  CD2 PHE C 201     -57.595  28.215  26.452  1.00103.39           C  
ANISOU 8198  CD2 PHE C 201    14750  14000  10533  -2639    609  -1779       C  
ATOM   8199  CE1 PHE C 201     -57.074  25.878  27.840  1.00107.15           C  
ANISOU 8199  CE1 PHE C 201    15616  13889  11207  -2711    822  -1830       C  
ATOM   8200  CE2 PHE C 201     -58.587  27.627  27.246  1.00107.36           C  
ANISOU 8200  CE2 PHE C 201    15273  14383  11135  -2798    686  -1797       C  
ATOM   8201  CZ  PHE C 201     -58.319  26.464  27.934  1.00106.45           C  
ANISOU 8201  CZ  PHE C 201    15358  13975  11114  -2843    799  -1818       C  
ATOM   8202  N   GLN C 202     -52.591  28.865  27.303  1.00 91.52           N  
ANISOU 8202  N   GLN C 202    13533  12213   9028  -1957    617  -1477       N  
ATOM   8203  CA  GLN C 202     -51.696  28.539  28.420  1.00 90.70           C  
ANISOU 8203  CA  GLN C 202    13560  11896   9006  -1822    644  -1380       C  
ATOM   8204  C   GLN C 202     -51.460  29.789  29.257  1.00 93.64           C  
ANISOU 8204  C   GLN C 202    13865  12345   9370  -1730    583  -1199       C  
ATOM   8205  O   GLN C 202     -51.489  29.722  30.483  1.00 92.49           O  
ANISOU 8205  O   GLN C 202    13810  12059   9271  -1697    596  -1098       O  
ATOM   8206  CB  GLN C 202     -50.356  28.000  27.890  1.00 92.45           C  
ANISOU 8206  CB  GLN C 202    13831  12056   9240  -1681    662  -1450       C  
ATOM   8207  CG  GLN C 202     -49.496  27.298  28.934  1.00106.68           C  
ANISOU 8207  CG  GLN C 202    15788  13607  11139  -1543    687  -1386       C  
ATOM   8208  CD  GLN C 202     -48.131  26.951  28.395  1.00128.64           C  
ANISOU 8208  CD  GLN C 202    18568  16367  13942  -1376    695  -1452       C  
ATOM   8209  OE1 GLN C 202     -47.236  27.800  28.308  1.00124.15           O  
ANISOU 8209  OE1 GLN C 202    17887  15933  13352  -1258    648  -1382       O  
ATOM   8210  NE2 GLN C 202     -47.934  25.691  28.033  1.00122.53           N  
ANISOU 8210  NE2 GLN C 202    17916  15418  13221  -1365    761  -1593       N  
ATOM   8211  N   HIS C 203     -51.254  30.928  28.582  1.00 90.84           N  
ANISOU 8211  N   HIS C 203    13362  12206   8947  -1696    519  -1161       N  
ATOM   8212  CA  HIS C 203     -51.050  32.226  29.209  1.00 89.84           C  
ANISOU 8212  CA  HIS C 203    13162  12158   8815  -1621    456  -1009       C  
ATOM   8213  C   HIS C 203     -52.312  32.697  29.929  1.00 93.81           C  
ANISOU 8213  C   HIS C 203    13637  12681   9326  -1709    451   -951       C  
ATOM   8214  O   HIS C 203     -52.206  33.198  31.041  1.00 92.79           O  
ANISOU 8214  O   HIS C 203    13543  12489   9226  -1650    438   -844       O  
ATOM   8215  CB  HIS C 203     -50.554  33.255  28.179  1.00 90.38           C  
ANISOU 8215  CB  HIS C 203    13095  12434   8813  -1582    402   -985       C  
ATOM   8216  CG  HIS C 203     -50.513  34.655  28.704  1.00 92.83           C  
ANISOU 8216  CG  HIS C 203    13328  12817   9126  -1532    336   -840       C  
ATOM   8217  ND1 HIS C 203     -49.572  35.046  29.638  1.00 94.07           N  
ANISOU 8217  ND1 HIS C 203    13518  12887   9338  -1422    311   -750       N  
ATOM   8218  CD2 HIS C 203     -51.316  35.706  28.421  1.00 94.39           C  
ANISOU 8218  CD2 HIS C 203    13423  13156   9284  -1575    285   -782       C  
ATOM   8219  CE1 HIS C 203     -49.838  36.315  29.895  1.00 92.83           C  
ANISOU 8219  CE1 HIS C 203    13286  12809   9174  -1414    255   -651       C  
ATOM   8220  NE2 HIS C 203     -50.869  36.758  29.177  1.00 93.26           N  
ANISOU 8220  NE2 HIS C 203    13262  12996   9178  -1496    240   -661       N  
ATOM   8221  N   ILE C 204     -53.495  32.515  29.312  1.00 91.60           N  
ANISOU 8221  N   ILE C 204    13289  12495   9020  -1849    462  -1034       N  
ATOM   8222  CA  ILE C 204     -54.793  32.877  29.889  1.00 91.64           C  
ANISOU 8222  CA  ILE C 204    13235  12540   9044  -1941    471  -1004       C  
ATOM   8223  C   ILE C 204     -55.086  32.023  31.132  1.00 95.85           C  
ANISOU 8223  C   ILE C 204    13911  12867   9643  -1986    562   -987       C  
ATOM   8224  O   ILE C 204     -55.524  32.565  32.146  1.00 95.16           O  
ANISOU 8224  O   ILE C 204    13821  12764   9569  -1974    578   -898       O  
ATOM   8225  CB  ILE C 204     -55.918  32.806  28.799  1.00 95.99           C  
ANISOU 8225  CB  ILE C 204    13654  13264   9555  -2078    446  -1115       C  
ATOM   8226  CG1 ILE C 204     -56.005  34.112  27.953  1.00 96.12           C  
ANISOU 8226  CG1 ILE C 204    13514  13509   9496  -2022    340  -1059       C  
ATOM   8227  CG2 ILE C 204     -57.294  32.370  29.338  1.00 97.59           C  
ANISOU 8227  CG2 ILE C 204    13823  13445   9812  -2228    503  -1161       C  
ATOM   8228  CD1 ILE C 204     -56.502  35.446  28.692  1.00104.60           C  
ANISOU 8228  CD1 ILE C 204    14499  14646  10597  -1957    296   -924       C  
ATOM   8229  N   MET C 205     -54.798  30.707  31.058  1.00 93.35           N  
ANISOU 8229  N   MET C 205    13729  12380   9358  -2028    627  -1069       N  
ATOM   8230  CA  MET C 205     -55.040  29.749  32.136  1.00 94.01           C  
ANISOU 8230  CA  MET C 205    13981  12241   9499  -2081    722  -1044       C  
ATOM   8231  C   MET C 205     -54.063  29.863  33.317  1.00 94.05           C  
ANISOU 8231  C   MET C 205    14125  12102   9508  -1922    714   -908       C  
ATOM   8232  O   MET C 205     -54.511  29.989  34.458  1.00 93.29           O  
ANISOU 8232  O   MET C 205    14095  11944   9409  -1940    758   -817       O  
ATOM   8233  CB  MET C 205     -55.091  28.315  31.589  1.00 98.72           C  
ANISOU 8233  CB  MET C 205    14687  12684  10139  -2181    788  -1181       C  
ATOM   8234  CG  MET C 205     -55.901  27.372  32.459  1.00104.90           C  
ANISOU 8234  CG  MET C 205    15601  13274  10983  -2325    903  -1175       C  
ATOM   8235  SD  MET C 205     -55.362  25.640  32.388  1.00112.22           S  
ANISOU 8235  SD  MET C 205    16771  13879  11987  -2350    985  -1259       S  
ATOM   8236  CE  MET C 205     -53.831  25.731  33.349  1.00108.11           C  
ANISOU 8236  CE  MET C 205    16411  13207  11459  -2080    941  -1096       C  
ATOM   8237  N   VAL C 206     -52.745  29.796  33.051  1.00 88.24           N  
ANISOU 8237  N   VAL C 206    13429  11326   8773  -1770    660   -900       N  
ATOM   8238  CA  VAL C 206     -51.708  29.868  34.089  1.00 86.74           C  
ANISOU 8238  CA  VAL C 206    13353  11017   8587  -1607    625   -783       C  
ATOM   8239  C   VAL C 206     -51.541  31.291  34.641  1.00 88.48           C  
ANISOU 8239  C   VAL C 206    13477  11375   8767  -1530    548   -679       C  
ATOM   8240  O   VAL C 206     -51.381  31.457  35.849  1.00 88.79           O  
ANISOU 8240  O   VAL C 206    13614  11336   8788  -1470    539   -580       O  
ATOM   8241  CB  VAL C 206     -50.359  29.243  33.639  1.00 90.58           C  
ANISOU 8241  CB  VAL C 206    13893  11414   9109  -1465    594   -824       C  
ATOM   8242  CG1 VAL C 206     -49.315  29.314  34.747  1.00 90.08           C  
ANISOU 8242  CG1 VAL C 206    13929  11244   9054  -1291    536   -705       C  
ATOM   8243  CG2 VAL C 206     -50.546  27.797  33.178  1.00 92.15           C  
ANISOU 8243  CG2 VAL C 206    14216  11438   9360  -1534    677   -938       C  
ATOM   8244  N   GLY C 207     -51.573  32.287  33.758  1.00 82.60           N  
ANISOU 8244  N   GLY C 207    12556  10826   8000  -1534    492   -703       N  
ATOM   8245  CA  GLY C 207     -51.414  33.692  34.118  1.00 80.26           C  
ANISOU 8245  CA  GLY C 207    12166  10649   7682  -1469    418   -617       C  
ATOM   8246  C   GLY C 207     -52.616  34.341  34.772  1.00 81.65           C  
ANISOU 8246  C   GLY C 207    12306  10877   7840  -1541    444   -579       C  
ATOM   8247  O   GLY C 207     -52.444  35.186  35.653  1.00 80.17           O  
ANISOU 8247  O   GLY C 207    12128  10694   7638  -1472    407   -502       O  
ATOM   8248  N   LEU C 208     -53.839  33.979  34.345  1.00 77.93           N  
ANISOU 8248  N   LEU C 208    11781  10454   7373  -1680    508   -646       N  
ATOM   8249  CA  LEU C 208     -55.048  34.587  34.906  1.00 77.41           C  
ANISOU 8249  CA  LEU C 208    11648  10459   7304  -1746    544   -625       C  
ATOM   8250  C   LEU C 208     -56.039  33.652  35.630  1.00 80.70           C  
ANISOU 8250  C   LEU C 208    12149  10780   7735  -1875    670   -647       C  
ATOM   8251  O   LEU C 208     -56.400  33.941  36.773  1.00 79.84           O  
ANISOU 8251  O   LEU C 208    12095  10636   7606  -1865    720   -584       O  
ATOM   8252  CB  LEU C 208     -55.753  35.506  33.878  1.00 77.19           C  
ANISOU 8252  CB  LEU C 208    11418  10635   7274  -1778    487   -659       C  
ATOM   8253  CG  LEU C 208     -57.098  36.136  34.293  1.00 82.33           C  
ANISOU 8253  CG  LEU C 208    11958  11381   7941  -1834    521   -657       C  
ATOM   8254  CD1 LEU C 208     -56.935  37.126  35.451  1.00 81.90           C  
ANISOU 8254  CD1 LEU C 208    11939  11300   7880  -1729    513   -570       C  
ATOM   8255  CD2 LEU C 208     -57.779  36.792  33.116  1.00 84.65           C  
ANISOU 8255  CD2 LEU C 208    12060  11869   8235  -1860    449   -696       C  
ATOM   8256  N   ILE C 209     -56.517  32.590  34.953  1.00 77.57           N  
ANISOU 8256  N   ILE C 209    11757  10348   7369  -2007    726   -742       N  
ATOM   8257  CA  ILE C 209     -57.526  31.670  35.489  1.00 78.70           C  
ANISOU 8257  CA  ILE C 209    11961  10399   7541  -2169    856   -773       C  
ATOM   8258  C   ILE C 209     -57.130  30.886  36.767  1.00 82.81           C  
ANISOU 8258  C   ILE C 209    12721  10695   8048  -2149    942   -684       C  
ATOM   8259  O   ILE C 209     -57.841  30.981  37.772  1.00 82.68           O  
ANISOU 8259  O   ILE C 209    12740  10662   8011  -2205   1035   -630       O  
ATOM   8260  CB  ILE C 209     -58.231  30.834  34.378  1.00 82.79           C  
ANISOU 8260  CB  ILE C 209    12402  10951   8103  -2338    883   -917       C  
ATOM   8261  CG1 ILE C 209     -59.052  31.766  33.448  1.00 82.58           C  
ANISOU 8261  CG1 ILE C 209    12123  11183   8070  -2373    807   -979       C  
ATOM   8262  CG2 ILE C 209     -59.121  29.723  34.977  1.00 85.50           C  
ANISOU 8262  CG2 ILE C 209    12837  11153   8497  -2526   1032   -948       C  
ATOM   8263  CD1 ILE C 209     -59.554  31.147  32.131  1.00 90.66           C  
ANISOU 8263  CD1 ILE C 209    13048  12292   9105  -2509    780  -1132       C  
ATOM   8264  N   LEU C 210     -56.011  30.128  36.725  1.00 78.94           N  
ANISOU 8264  N   LEU C 210    12391  10039   7563  -2061    913   -667       N  
ATOM   8265  CA  LEU C 210     -55.514  29.330  37.855  1.00 79.09           C  
ANISOU 8265  CA  LEU C 210    12654   9833   7562  -2014    968   -569       C  
ATOM   8266  C   LEU C 210     -55.203  30.131  39.132  1.00 81.60           C  
ANISOU 8266  C   LEU C 210    13039  10167   7798  -1895    942   -438       C  
ATOM   8267  O   LEU C 210     -55.781  29.779  40.162  1.00 82.15           O  
ANISOU 8267  O   LEU C 210    13236  10152   7826  -1963   1049   -370       O  
ATOM   8268  CB  LEU C 210     -54.358  28.382  37.454  1.00 79.53           C  
ANISOU 8268  CB  LEU C 210    12847   9716   7655  -1915    926   -587       C  
ATOM   8269  CG  LEU C 210     -54.679  26.880  37.249  1.00 85.98           C  
ANISOU 8269  CG  LEU C 210    13816  10313   8538  -2042   1031   -646       C  
ATOM   8270  CD1 LEU C 210     -54.896  26.161  38.574  1.00 87.69           C  
ANISOU 8270  CD1 LEU C 210    14269  10316   8731  -2075   1132   -518       C  
ATOM   8271  CD2 LEU C 210     -55.862  26.661  36.310  1.00 88.69           C  
ANISOU 8271  CD2 LEU C 210    14014  10752   8931  -2261   1094   -792       C  
ATOM   8272  N   PRO C 211     -54.370  31.214  39.126  1.00 76.28           N  
ANISOU 8272  N   PRO C 211    12286   9604   7093  -1735    813   -407       N  
ATOM   8273  CA  PRO C 211     -54.155  31.961  40.382  1.00 75.35           C  
ANISOU 8273  CA  PRO C 211    12239   9499   6891  -1640    788   -308       C  
ATOM   8274  C   PRO C 211     -55.351  32.813  40.800  1.00 77.62           C  
ANISOU 8274  C   PRO C 211    12420   9923   7150  -1724    860   -317       C  
ATOM   8275  O   PRO C 211     -55.568  32.987  41.994  1.00 77.94           O  
ANISOU 8275  O   PRO C 211    12572   9935   7109  -1708    913   -248       O  
ATOM   8276  CB  PRO C 211     -52.905  32.797  40.107  1.00 75.84           C  
ANISOU 8276  CB  PRO C 211    12232   9628   6955  -1471    628   -297       C  
ATOM   8277  CG  PRO C 211     -52.832  32.921  38.644  1.00 79.61           C  
ANISOU 8277  CG  PRO C 211    12540  10204   7505  -1502    591   -389       C  
ATOM   8278  CD  PRO C 211     -53.605  31.807  38.009  1.00 76.27           C  
ANISOU 8278  CD  PRO C 211    12136   9718   7127  -1649    694   -464       C  
ATOM   8279  N   GLY C 212     -56.131  33.291  39.827  1.00 72.80           N  
ANISOU 8279  N   GLY C 212    11599   9461   6599  -1806    864   -403       N  
ATOM   8280  CA  GLY C 212     -57.343  34.079  40.053  1.00 72.52           C  
ANISOU 8280  CA  GLY C 212    11422   9568   6564  -1875    929   -430       C  
ATOM   8281  C   GLY C 212     -58.345  33.360  40.933  1.00 77.90           C  
ANISOU 8281  C   GLY C 212    12191  10186   7221  -2013   1104   -414       C  
ATOM   8282  O   GLY C 212     -58.933  33.973  41.831  1.00 77.61           O  
ANISOU 8282  O   GLY C 212    12145  10210   7133  -2008   1174   -389       O  
ATOM   8283  N   ILE C 213     -58.503  32.033  40.702  1.00 75.98           N  
ANISOU 8283  N   ILE C 213    12048   9808   7013  -2139   1185   -430       N  
ATOM   8284  CA  ILE C 213     -59.354  31.129  41.477  1.00 78.03           C  
ANISOU 8284  CA  ILE C 213    12423   9966   7260  -2300   1368   -402       C  
ATOM   8285  C   ILE C 213     -58.774  31.011  42.891  1.00 82.50           C  
ANISOU 8285  C   ILE C 213    13238  10405   7702  -2206   1403   -266       C  
ATOM   8286  O   ILE C 213     -59.526  31.159  43.854  1.00 83.58           O  
ANISOU 8286  O   ILE C 213    13414  10572   7772  -2271   1537   -226       O  
ATOM   8287  CB  ILE C 213     -59.524  29.747  40.773  1.00 82.72           C  
ANISOU 8287  CB  ILE C 213    13077  10415   7937  -2456   1427   -459       C  
ATOM   8288  CG1 ILE C 213     -60.454  29.875  39.546  1.00 83.45           C  
ANISOU 8288  CG1 ILE C 213    12907  10672   8127  -2594   1419   -607       C  
ATOM   8289  CG2 ILE C 213     -60.046  28.667  41.743  1.00 85.86           C  
ANISOU 8289  CG2 ILE C 213    13680  10630   8313  -2605   1614   -386       C  
ATOM   8290  CD1 ILE C 213     -60.306  28.778  38.488  1.00 92.83           C  
ANISOU 8290  CD1 ILE C 213    14123  11755   9395  -2697   1404   -706       C  
ATOM   8291  N   VAL C 214     -57.441  30.784  43.011  1.00 77.60           N  
ANISOU 8291  N   VAL C 214    12776   9663   7045  -2048   1279   -201       N  
ATOM   8292  CA  VAL C 214     -56.732  30.686  44.299  1.00 77.60           C  
ANISOU 8292  CA  VAL C 214    13016   9555   6915  -1929   1266    -70       C  
ATOM   8293  C   VAL C 214     -57.008  31.944  45.143  1.00 80.87           C  
ANISOU 8293  C   VAL C 214    13373  10125   7228  -1863   1263    -57       C  
ATOM   8294  O   VAL C 214     -57.450  31.818  46.284  1.00 81.62           O  
ANISOU 8294  O   VAL C 214    13613  10193   7208  -1900   1381     14       O  
ATOM   8295  CB  VAL C 214     -55.212  30.401  44.118  1.00 80.54           C  
ANISOU 8295  CB  VAL C 214    13497   9815   7289  -1747   1096    -27       C  
ATOM   8296  CG1 VAL C 214     -54.468  30.414  45.453  1.00 80.99           C  
ANISOU 8296  CG1 VAL C 214    13779   9793   7200  -1607   1046    104       C  
ATOM   8297  CG2 VAL C 214     -54.984  29.077  43.397  1.00 81.31           C  
ANISOU 8297  CG2 VAL C 214    13679   9732   7483  -1802   1123    -47       C  
ATOM   8298  N   ILE C 215     -56.822  33.142  44.543  1.00 75.71           N  
ANISOU 8298  N   ILE C 215    12514   9631   6622  -1777   1143   -131       N  
ATOM   8299  CA  ILE C 215     -57.058  34.453  45.158  1.00 75.02           C  
ANISOU 8299  CA  ILE C 215    12350   9682   6471  -1704   1123   -147       C  
ATOM   8300  C   ILE C 215     -58.527  34.625  45.601  1.00 80.89           C  
ANISOU 8300  C   ILE C 215    13014  10519   7200  -1836   1313   -184       C  
ATOM   8301  O   ILE C 215     -58.756  34.932  46.773  1.00 81.41           O  
ANISOU 8301  O   ILE C 215    13191  10601   7141  -1811   1392   -146       O  
ATOM   8302  CB  ILE C 215     -56.510  35.611  44.259  1.00 75.92           C  
ANISOU 8302  CB  ILE C 215    12270   9912   6666  -1596    954   -211       C  
ATOM   8303  CG1 ILE C 215     -54.959  35.580  44.211  1.00 75.15           C  
ANISOU 8303  CG1 ILE C 215    12264   9735   6553  -1451    783   -166       C  
ATOM   8304  CG2 ILE C 215     -57.008  36.994  44.718  1.00 76.17           C  
ANISOU 8304  CG2 ILE C 215    12195  10076   6672  -1542    954   -252       C  
ATOM   8305  CD1 ILE C 215     -54.290  36.070  42.917  1.00 77.75           C  
ANISOU 8305  CD1 ILE C 215    12422  10126   6992  -1399    648   -217       C  
ATOM   8306  N   LEU C 216     -59.507  34.405  44.686  1.00 78.23           N  
ANISOU 8306  N   LEU C 216    12484  10255   6983  -1975   1387   -264       N  
ATOM   8307  CA  LEU C 216     -60.945  34.522  44.989  1.00 79.72           C  
ANISOU 8307  CA  LEU C 216    12548  10552   7188  -2109   1568   -314       C  
ATOM   8308  C   LEU C 216     -61.404  33.532  46.064  1.00 86.58           C  
ANISOU 8308  C   LEU C 216    13619  11314   7963  -2237   1770   -237       C  
ATOM   8309  O   LEU C 216     -62.184  33.906  46.942  1.00 87.06           O  
ANISOU 8309  O   LEU C 216    13669  11457   7953  -2273   1917   -240       O  
ATOM   8310  CB  LEU C 216     -61.809  34.349  43.724  1.00 79.77           C  
ANISOU 8310  CB  LEU C 216    12303  10658   7347  -2238   1579   -417       C  
ATOM   8311  CG  LEU C 216     -61.989  35.571  42.815  1.00 83.06           C  
ANISOU 8311  CG  LEU C 216    12463  11249   7845  -2143   1445   -496       C  
ATOM   8312  CD1 LEU C 216     -62.436  35.150  41.429  1.00 82.98           C  
ANISOU 8312  CD1 LEU C 216    12270  11305   7954  -2251   1399   -578       C  
ATOM   8313  CD2 LEU C 216     -63.002  36.555  43.393  1.00 86.40           C  
ANISOU 8313  CD2 LEU C 216    12736  11824   8269  -2119   1535   -541       C  
ATOM   8314  N   SER C 217     -60.910  32.276  45.994  1.00 84.99           N  
ANISOU 8314  N   SER C 217    13610  10923   7761  -2302   1782   -168       N  
ATOM   8315  CA  SER C 217     -61.244  31.210  46.938  1.00 87.67           C  
ANISOU 8315  CA  SER C 217    14180  11117   8014  -2431   1968    -68       C  
ATOM   8316  C   SER C 217     -60.752  31.522  48.338  1.00 93.20           C  
ANISOU 8316  C   SER C 217    15111  11788   8512  -2309   1983     45       C  
ATOM   8317  O   SER C 217     -61.545  31.428  49.269  1.00 94.78           O  
ANISOU 8317  O   SER C 217    15380  12020   8613  -2406   2179     83       O  
ATOM   8318  CB  SER C 217     -60.720  29.860  46.461  1.00 92.39           C  
ANISOU 8318  CB  SER C 217    14941  11491   8674  -2497   1950    -21       C  
ATOM   8319  OG  SER C 217     -61.236  29.554  45.175  1.00101.42           O  
ANISOU 8319  OG  SER C 217    15875  12672   9988  -2625   1941   -146       O  
ATOM   8320  N   CYS C 218     -59.472  31.945  48.490  1.00 89.39           N  
ANISOU 8320  N   CYS C 218    14733  11268   7962  -2101   1780     87       N  
ATOM   8321  CA  CYS C 218     -58.893  32.330  49.785  1.00 90.22           C  
ANISOU 8321  CA  CYS C 218    15051  11366   7862  -1967   1749    177       C  
ATOM   8322  C   CYS C 218     -59.724  33.448  50.407  1.00 97.08           C  
ANISOU 8322  C   CYS C 218    15803  12425   8659  -1966   1849    105       C  
ATOM   8323  O   CYS C 218     -60.107  33.343  51.571  1.00 98.42           O  
ANISOU 8323  O   CYS C 218    16138  12601   8655  -1999   1996    168       O  
ATOM   8324  CB  CYS C 218     -57.428  32.737  49.640  1.00 88.62           C  
ANISOU 8324  CB  CYS C 218    14899  11129   7643  -1755   1490    195       C  
ATOM   8325  SG  CYS C 218     -56.296  31.353  49.357  1.00 92.66           S  
ANISOU 8325  SG  CYS C 218    15622  11399   8185  -1701   1385    307       S  
ATOM   8326  N   TYR C 219     -60.087  34.460  49.592  1.00 94.24           N  
ANISOU 8326  N   TYR C 219    15157  12216   8434  -1938   1787    -28       N  
ATOM   8327  CA  TYR C 219     -60.894  35.595  50.016  1.00 95.12           C  
ANISOU 8327  CA  TYR C 219    15122  12501   8518  -1914   1869   -119       C  
ATOM   8328  C   TYR C 219     -62.350  35.352  50.323  1.00102.76           C  
ANISOU 8328  C   TYR C 219    15991  13557   9496  -2085   2132   -156       C  
ATOM   8329  O   TYR C 219     -62.855  35.989  51.243  1.00104.15           O  
ANISOU 8329  O   TYR C 219    16181  13834   9559  -2056   2250   -187       O  
ATOM   8330  CB  TYR C 219     -60.666  36.825  49.152  1.00 94.45           C  
ANISOU 8330  CB  TYR C 219    14803  12522   8562  -1792   1696   -226       C  
ATOM   8331  CG  TYR C 219     -59.462  37.593  49.634  1.00 95.92           C  
ANISOU 8331  CG  TYR C 219    15112  12682   8653  -1607   1508   -210       C  
ATOM   8332  CD1 TYR C 219     -58.278  37.601  48.902  1.00 96.42           C  
ANISOU 8332  CD1 TYR C 219    15174  12676   8786  -1518   1293   -188       C  
ATOM   8333  CD2 TYR C 219     -59.469  38.232  50.872  1.00 97.88           C  
ANISOU 8333  CD2 TYR C 219    15487  12972   8730  -1532   1550   -220       C  
ATOM   8334  CE1 TYR C 219     -57.148  38.274  49.363  1.00 97.05           C  
ANISOU 8334  CE1 TYR C 219    15350  12735   8789  -1367   1118   -179       C  
ATOM   8335  CE2 TYR C 219     -58.343  38.895  51.350  1.00 98.31           C  
ANISOU 8335  CE2 TYR C 219    15657  13002   8695  -1378   1366   -218       C  
ATOM   8336  CZ  TYR C 219     -57.188  38.922  50.588  1.00104.75           C  
ANISOU 8336  CZ  TYR C 219    16446  13752   9602  -1301   1147   -197       C  
ATOM   8337  OH  TYR C 219     -56.094  39.596  51.060  1.00105.65           O  
ANISOU 8337  OH  TYR C 219    16647  13853   9641  -1166    965   -206       O  
ATOM   8338  N   CYS C 220     -63.032  34.433  49.610  1.00100.78           N  
ANISOU 8338  N   CYS C 220    15642  13275   9376  -2269   2234   -163       N  
ATOM   8339  CA  CYS C 220     -64.430  34.145  49.937  1.00103.42           C  
ANISOU 8339  CA  CYS C 220    15865  13700   9730  -2457   2497   -201       C  
ATOM   8340  C   CYS C 220     -64.544  33.299  51.227  1.00109.20           C  
ANISOU 8340  C   CYS C 220    16892  14329  10269  -2556   2703    -70       C  
ATOM   8341  O   CYS C 220     -65.593  33.303  51.872  1.00110.90           O  
ANISOU 8341  O   CYS C 220    17055  14644  10437  -2677   2944    -91       O  
ATOM   8342  CB  CYS C 220     -65.193  33.537  48.759  1.00104.54           C  
ANISOU 8342  CB  CYS C 220    15776  13865  10081  -2636   2533   -274       C  
ATOM   8343  SG  CYS C 220     -64.682  31.857  48.309  1.00109.34           S  
ANISOU 8343  SG  CYS C 220    16594  14218  10731  -2789   2530   -179       S  
ATOM   8344  N   ILE C 221     -63.429  32.629  51.620  1.00105.10           N  
ANISOU 8344  N   ILE C 221    16682  13620   9630  -2488   2602     68       N  
ATOM   8345  CA  ILE C 221     -63.297  31.815  52.836  1.00107.05           C  
ANISOU 8345  CA  ILE C 221    17265  13742   9666  -2542   2747    229       C  
ATOM   8346  C   ILE C 221     -63.026  32.732  54.043  1.00110.08           C  
ANISOU 8346  C   ILE C 221    17780  14231   9813  -2386   2745    241       C  
ATOM   8347  O   ILE C 221     -63.655  32.543  55.087  1.00112.05           O  
ANISOU 8347  O   ILE C 221    18163  14520   9892  -2474   2973    297       O  
ATOM   8348  CB  ILE C 221     -62.245  30.665  52.666  1.00110.29           C  
ANISOU 8348  CB  ILE C 221    17940  13897  10068  -2520   2624    371       C  
ATOM   8349  CG1 ILE C 221     -62.734  29.610  51.638  1.00111.20           C  
ANISOU 8349  CG1 ILE C 221    17961  13894  10398  -2722   2694    348       C  
ATOM   8350  CG2 ILE C 221     -61.933  29.984  54.012  1.00113.38           C  
ANISOU 8350  CG2 ILE C 221    18714  14160  10206  -2518   2725    562       C  
ATOM   8351  CD1 ILE C 221     -61.657  28.598  51.106  1.00118.07           C  
ANISOU 8351  CD1 ILE C 221    19019  14513  11328  -2669   2535    433       C  
ATOM   8352  N   ILE C 222     -62.105  33.722  53.894  1.00103.73           N  
ANISOU 8352  N   ILE C 222    16940  13476   8998  -2166   2497    182       N  
ATOM   8353  CA  ILE C 222     -61.762  34.707  54.935  1.00103.70           C  
ANISOU 8353  CA  ILE C 222    17043  13570   8787  -2008   2454    157       C  
ATOM   8354  C   ILE C 222     -63.005  35.534  55.305  1.00108.03           C  
ANISOU 8354  C   ILE C 222    17404  14316   9328  -2059   2667     27       C  
ATOM   8355  O   ILE C 222     -63.338  35.610  56.488  1.00109.49           O  
ANISOU 8355  O   ILE C 222    17753  14558   9289  -2070   2833     56       O  
ATOM   8356  CB  ILE C 222     -60.522  35.586  54.565  1.00104.39           C  
ANISOU 8356  CB  ILE C 222    17099  13656   8908  -1791   2139    104       C  
ATOM   8357  CG1 ILE C 222     -59.240  34.729  54.426  1.00104.22           C  
ANISOU 8357  CG1 ILE C 222    17284  13454   8861  -1721   1945    238       C  
ATOM   8358  CG2 ILE C 222     -60.305  36.723  55.590  1.00105.56           C  
ANISOU 8358  CG2 ILE C 222    17323  13917   8866  -1648   2100     36       C  
ATOM   8359  CD1 ILE C 222     -58.114  35.369  53.562  1.00107.09           C  
ANISOU 8359  CD1 ILE C 222    17520  13809   9361  -1563   1652    176       C  
ATOM   8360  N   ILE C 223     -63.715  36.089  54.286  1.00102.77           N  
ANISOU 8360  N   ILE C 223    16394  13755   8901  -2090   2668   -111       N  
ATOM   8361  CA  ILE C 223     -64.965  36.857  54.431  1.00103.18           C  
ANISOU 8361  CA  ILE C 223    16204  13996   9003  -2126   2858   -249       C  
ATOM   8362  C   ILE C 223     -66.050  36.005  55.131  1.00109.00           C  
ANISOU 8362  C   ILE C 223    16992  14767   9655  -2340   3193   -197       C  
ATOM   8363  O   ILE C 223     -66.749  36.518  56.009  1.00110.71           O  
ANISOU 8363  O   ILE C 223    17195  15121   9749  -2336   3390   -258       O  
ATOM   8364  CB  ILE C 223     -65.437  37.457  53.066  1.00104.35           C  
ANISOU 8364  CB  ILE C 223    15981  14232   9436  -2112   2758   -379       C  
ATOM   8365  CG1 ILE C 223     -64.490  38.589  52.595  1.00102.18           C  
ANISOU 8365  CG1 ILE C 223    15658  13951   9214  -1892   2474   -440       C  
ATOM   8366  CG2 ILE C 223     -66.897  37.957  53.121  1.00106.76           C  
ANISOU 8366  CG2 ILE C 223    16006  14729   9830  -2178   2979   -509       C  
ATOM   8367  CD1 ILE C 223     -64.543  38.925  51.066  1.00108.53           C  
ANISOU 8367  CD1 ILE C 223    16179  14782  10275  -1873   2307   -505       C  
ATOM   8368  N   SER C 224     -66.149  34.705  54.773  1.00105.03           N  
ANISOU 8368  N   SER C 224    16562  14131   9212  -2526   3263    -86       N  
ATOM   8369  CA  SER C 224     -67.098  33.765  55.380  1.00107.38           C  
ANISOU 8369  CA  SER C 224    16931  14425   9445  -2763   3581    -14       C  
ATOM   8370  C   SER C 224     -66.836  33.593  56.879  1.00111.52           C  
ANISOU 8370  C   SER C 224    17808  14923   9641  -2738   3719    111       C  
ATOM   8371  O   SER C 224     -67.716  33.904  57.681  1.00113.03           O  
ANISOU 8371  O   SER C 224    17963  15265   9719  -2800   3974     65       O  
ATOM   8372  CB  SER C 224     -67.055  32.412  54.673  1.00111.65           C  
ANISOU 8372  CB  SER C 224    17525  14780  10119  -2954   3589     83       C  
ATOM   8373  OG  SER C 224     -67.938  31.475  55.272  1.00124.27           O  
ANISOU 8373  OG  SER C 224    19209  16348  11662  -3205   3903    165       O  
ATOM   8374  N   LYS C 225     -65.617  33.146  57.255  1.00106.58           N  
ANISOU 8374  N   LYS C 225    17515  14124   8857  -2633   3543    261       N  
ATOM   8375  CA  LYS C 225     -65.248  32.939  58.656  1.00108.27           C  
ANISOU 8375  CA  LYS C 225    18095  14309   8733  -2591   3629    398       C  
ATOM   8376  C   LYS C 225     -64.700  34.209  59.338  1.00109.94           C  
ANISOU 8376  C   LYS C 225    18355  14653   8764  -2354   3490    302       C  
ATOM   8377  O   LYS C 225     -63.643  34.186  59.977  1.00109.66           O  
ANISOU 8377  O   LYS C 225    18605  14543   8518  -2212   3318    397       O  
ATOM   8378  CB  LYS C 225     -64.342  31.702  58.831  1.00111.60           C  
ANISOU 8378  CB  LYS C 225    18864  14478   9060  -2609   3536    622       C  
ATOM   8379  CG  LYS C 225     -64.484  31.005  60.200  1.00131.32           C  
ANISOU 8379  CG  LYS C 225    21735  16926  11236  -2692   3754    814       C  
ATOM   8380  CD  LYS C 225     -65.702  30.065  60.314  1.00142.49           C  
ANISOU 8380  CD  LYS C 225    23136  18308  12697  -2997   4118    885       C  
ATOM   8381  CE  LYS C 225     -65.383  28.619  60.002  1.00151.92           C  
ANISOU 8381  CE  LYS C 225    24546  19214  13963  -3130   4118   1079       C  
ATOM   8382  NZ  LYS C 225     -65.271  28.365  58.538  1.00156.46           N  
ANISOU 8382  NZ  LYS C 225    24865  19694  14889  -3165   3955    978       N  
ATOM   8383  N   LEU C 226     -65.455  35.316  59.197  1.00104.44           N  
ANISOU 8383  N   LEU C 226    17372  14152   8159  -2314   3564    103       N  
ATOM   8384  CA  LEU C 226     -65.182  36.630  59.782  1.00102.87           C  
ANISOU 8384  CA  LEU C 226    17171  14086   7831  -2112   3475    -35       C  
ATOM   8385  C   LEU C 226     -66.506  37.187  60.331  1.00108.82           C  
ANISOU 8385  C   LEU C 226    17759  15043   8546  -2177   3791   -169       C  
ATOM   8386  O   LEU C 226     -66.814  38.370  60.158  1.00107.32           O  
ANISOU 8386  O   LEU C 226    17345  14982   8450  -2051   3756   -359       O  
ATOM   8387  CB  LEU C 226     -64.562  37.573  58.732  1.00 98.97           C  
ANISOU 8387  CB  LEU C 226    16449  13585   7570  -1945   3169   -164       C  
ATOM   8388  CG  LEU C 226     -63.437  38.494  59.211  1.00101.72           C  
ANISOU 8388  CG  LEU C 226    16946  13928   7775  -1724   2916   -213       C  
ATOM   8389  CD1 LEU C 226     -62.101  37.783  59.206  1.00100.43           C  
ANISOU 8389  CD1 LEU C 226    17032  13596   7529  -1668   2675    -53       C  
ATOM   8390  CD2 LEU C 226     -63.329  39.711  58.329  1.00101.42           C  
ANISOU 8390  CD2 LEU C 226    16626  13939   7971  -1593   2734   -386       C  
ATOM   8391  N   SER C 227     -67.292  36.301  60.990  1.00108.78           N  
ANISOU 8391  N   SER C 227    17864  15058   8408  -2378   4109    -65       N  
ATOM   8392  CA  SER C 227     -68.596  36.597  61.592  1.00111.37           C  
ANISOU 8392  CA  SER C 227    18048  15584   8682  -2478   4464   -169       C  
ATOM   8393  C   SER C 227     -68.807  35.763  62.851  1.00118.36           C  
ANISOU 8393  C   SER C 227    19272  16464   9235  -2618   4740     -2       C  
ATOM   8394  O   SER C 227     -68.139  35.984  63.860  1.00118.82           O  
ANISOU 8394  O   SER C 227    19647  16524   8974  -2496   4689     50       O  
ATOM   8395  CB  SER C 227     -69.718  36.328  60.594  1.00114.98           C  
ANISOU 8395  CB  SER C 227    18116  16104   9469  -2653   4609   -245       C  
ATOM   8396  OG  SER C 227     -69.551  37.088  59.407  1.00120.28           O  
ANISOU 8396  OG  SER C 227    18485  16787  10429  -2522   4353   -383       O  
ATOM   8397  N   ASN C1002     -66.728  42.258  70.102  1.00 73.83           N  
ANISOU 8397  N   ASN C1002    10683  11756   5613    183  -1222   -233       N  
ATOM   8398  CA  ASN C1002     -67.456  42.952  71.160  1.00 72.44           C  
ANISOU 8398  CA  ASN C1002    10474  11405   5643    230  -1311   -157       C  
ATOM   8399  C   ASN C1002     -67.066  42.435  72.578  1.00 74.55           C  
ANISOU 8399  C   ASN C1002    10647  11633   6046    365  -1192   -211       C  
ATOM   8400  O   ASN C1002     -65.887  42.151  72.807  1.00 73.63           O  
ANISOU 8400  O   ASN C1002    10479  11636   5861    387  -1073   -236       O  
ATOM   8401  CB  ASN C1002     -68.978  42.911  70.878  1.00 74.54           C  
ANISOU 8401  CB  ASN C1002    10776  11520   6025    235  -1464   -151       C  
ATOM   8402  CG  ASN C1002     -69.566  41.531  70.690  1.00101.38           C  
ANISOU 8402  CG  ASN C1002    14176  14884   9461    303  -1431   -278       C  
ATOM   8403  OD1 ASN C1002     -69.138  40.750  69.831  1.00 98.08           O  
ANISOU 8403  OD1 ASN C1002    13807  14568   8890    277  -1376   -368       O  
ATOM   8404  ND2 ASN C1002     -70.602  41.221  71.464  1.00 93.61           N  
ANISOU 8404  ND2 ASN C1002    13134  13751   8681    380  -1465   -295       N  
ATOM   8405  N   ILE C1003     -68.036  42.356  73.521  1.00 70.51           N  
ANISOU 8405  N   ILE C1003    10103  10969   5717    443  -1227   -219       N  
ATOM   8406  CA  ILE C1003     -67.837  41.844  74.884  1.00 69.63           C  
ANISOU 8406  CA  ILE C1003     9921  10826   5710    546  -1131   -251       C  
ATOM   8407  C   ILE C1003     -67.462  40.346  74.858  1.00 74.00           C  
ANISOU 8407  C   ILE C1003    10455  11406   6258    626  -1033   -337       C  
ATOM   8408  O   ILE C1003     -66.610  39.917  75.636  1.00 73.22           O  
ANISOU 8408  O   ILE C1003    10301  11349   6170    689   -948   -341       O  
ATOM   8409  CB  ILE C1003     -69.060  42.159  75.815  1.00 72.40           C  
ANISOU 8409  CB  ILE C1003    10239  11037   6231    587  -1177   -244       C  
ATOM   8410  CG1 ILE C1003     -68.772  41.797  77.307  1.00 71.90           C  
ANISOU 8410  CG1 ILE C1003    10118  10976   6224    659  -1077   -257       C  
ATOM   8411  CG2 ILE C1003     -70.389  41.554  75.284  1.00 73.73           C  
ANISOU 8411  CG2 ILE C1003    10411  11112   6493    595  -1245   -278       C  
ATOM   8412  CD1 ILE C1003     -69.804  42.262  78.341  1.00 78.35           C  
ANISOU 8412  CD1 ILE C1003    10894  11707   7168    686  -1082   -267       C  
ATOM   8413  N   PHE C1004     -68.092  39.570  73.954  1.00 71.98           N  
ANISOU 8413  N   PHE C1004    10244  11111   5995    620  -1066   -405       N  
ATOM   8414  CA  PHE C1004     -67.847  38.142  73.768  1.00 72.88           C  
ANISOU 8414  CA  PHE C1004    10359  11206   6125    694   -998   -509       C  
ATOM   8415  C   PHE C1004     -66.371  37.896  73.408  1.00 78.58           C  
ANISOU 8415  C   PHE C1004    11053  12076   6729    726   -890   -563       C  
ATOM   8416  O   PHE C1004     -65.676  37.158  74.113  1.00 77.86           O  
ANISOU 8416  O   PHE C1004    10898  11974   6709    828   -815   -588       O  
ATOM   8417  CB  PHE C1004     -68.787  37.598  72.680  1.00 75.73           C  
ANISOU 8417  CB  PHE C1004    10793  11509   6471    648  -1079   -585       C  
ATOM   8418  CG  PHE C1004     -68.662  36.121  72.402  1.00 78.56           C  
ANISOU 8418  CG  PHE C1004    11175  11808   6867    717  -1032   -719       C  
ATOM   8419  CD1 PHE C1004     -69.235  35.184  73.256  1.00 81.86           C  
ANISOU 8419  CD1 PHE C1004    11567  12069   7469    779  -1035   -720       C  
ATOM   8420  CD2 PHE C1004     -67.986  35.665  71.276  1.00 82.18           C  
ANISOU 8420  CD2 PHE C1004    11683  12363   7176    713   -984   -851       C  
ATOM   8421  CE1 PHE C1004     -69.123  33.816  72.992  1.00 84.07           C  
ANISOU 8421  CE1 PHE C1004    11879  12251   7812    840  -1016   -841       C  
ATOM   8422  CE2 PHE C1004     -67.873  34.298  71.016  1.00 86.33           C  
ANISOU 8422  CE2 PHE C1004    12236  12804   7761    792   -947  -1008       C  
ATOM   8423  CZ  PHE C1004     -68.445  33.383  71.872  1.00 84.34           C  
ANISOU 8423  CZ  PHE C1004    11967  12358   7722    858   -975   -997       C  
ATOM   8424  N   GLU C1005     -65.885  38.579  72.349  1.00 76.66           N  
ANISOU 8424  N   GLU C1005    10841  11978   6307    631   -888   -564       N  
ATOM   8425  CA  GLU C1005     -64.501  38.487  71.877  1.00 77.42           C  
ANISOU 8425  CA  GLU C1005    10885  12260   6271    636   -768   -617       C  
ATOM   8426  C   GLU C1005     -63.518  39.004  72.931  1.00 80.38           C  
ANISOU 8426  C   GLU C1005    11153  12695   6693    666   -718   -529       C  
ATOM   8427  O   GLU C1005     -62.390  38.523  72.987  1.00 80.46           O  
ANISOU 8427  O   GLU C1005    11068  12813   6690    735   -612   -585       O  
ATOM   8428  CB  GLU C1005     -64.315  39.192  70.519  1.00 80.04           C  
ANISOU 8428  CB  GLU C1005    11283  12756   6374    484   -779   -609       C  
ATOM   8429  CG  GLU C1005     -65.364  38.840  69.467  1.00 91.33           C  
ANISOU 8429  CG  GLU C1005    12835  14137   7730    423   -869   -675       C  
ATOM   8430  CD  GLU C1005     -65.337  37.488  68.770  1.00108.53           C  
ANISOU 8430  CD  GLU C1005    15048  16320   9870    494   -799   -884       C  
ATOM   8431  OE1 GLU C1005     -64.565  36.591  69.185  1.00 97.04           O  
ANISOU 8431  OE1 GLU C1005    13511  14861   8497    634   -676   -999       O  
ATOM   8432  OE2 GLU C1005     -66.116  37.326  67.803  1.00102.36           O  
ANISOU 8432  OE2 GLU C1005    14377  15531   8985    409   -886   -938       O  
ATOM   8433  N   MET C1006     -63.968  39.945  73.787  1.00 76.59           N  
ANISOU 8433  N   MET C1006    10681  12139   6280    621   -800   -406       N  
ATOM   8434  CA  MET C1006     -63.203  40.515  74.901  1.00 76.44           C  
ANISOU 8434  CA  MET C1006    10584  12157   6303    630   -784   -325       C  
ATOM   8435  C   MET C1006     -62.967  39.416  75.965  1.00 82.04           C  
ANISOU 8435  C   MET C1006    11227  12803   7141    773   -739   -356       C  
ATOM   8436  O   MET C1006     -61.855  39.282  76.482  1.00 81.74           O  
ANISOU 8436  O   MET C1006    11092  12857   7110    816   -691   -338       O  
ATOM   8437  CB  MET C1006     -63.970  41.710  75.503  1.00 77.58           C  
ANISOU 8437  CB  MET C1006    10778  12203   6495    557   -890   -232       C  
ATOM   8438  CG  MET C1006     -63.242  42.407  76.621  1.00 80.55           C  
ANISOU 8438  CG  MET C1006    11099  12613   6893    541   -891   -168       C  
ATOM   8439  SD  MET C1006     -64.337  42.888  77.969  1.00 83.22           S  
ANISOU 8439  SD  MET C1006    11472  12789   7357    570   -954   -152       S  
ATOM   8440  CE  MET C1006     -63.396  44.246  78.676  1.00 79.73           C  
ANISOU 8440  CE  MET C1006    11014  12407   6874    473   -996    -89       C  
ATOM   8441  N   LEU C1007     -64.010  38.619  76.253  1.00 79.81           N  
ANISOU 8441  N   LEU C1007    10993  12366   6966    834   -768   -387       N  
ATOM   8442  CA  LEU C1007     -63.935  37.517  77.204  1.00 80.35           C  
ANISOU 8442  CA  LEU C1007    11023  12348   7159    946   -748   -387       C  
ATOM   8443  C   LEU C1007     -63.353  36.230  76.594  1.00 87.35           C  
ANISOU 8443  C   LEU C1007    11880  13223   8086   1054   -692   -497       C  
ATOM   8444  O   LEU C1007     -62.983  35.320  77.337  1.00 87.71           O  
ANISOU 8444  O   LEU C1007    11879  13199   8247   1157   -688   -482       O  
ATOM   8445  CB  LEU C1007     -65.279  37.290  77.899  1.00 79.67           C  
ANISOU 8445  CB  LEU C1007    10988  12110   7171    937   -798   -351       C  
ATOM   8446  CG  LEU C1007     -65.394  38.014  79.228  1.00 83.65           C  
ANISOU 8446  CG  LEU C1007    11474  12626   7684    906   -812   -257       C  
ATOM   8447  CD1 LEU C1007     -66.360  39.180  79.149  1.00 82.99           C  
ANISOU 8447  CD1 LEU C1007    11428  12517   7588    825   -856   -250       C  
ATOM   8448  CD2 LEU C1007     -65.737  37.055  80.336  1.00 86.67           C  
ANISOU 8448  CD2 LEU C1007    11847  12925   8157    953   -806   -206       C  
ATOM   8449  N   ARG C1008     -63.246  36.169  75.247  1.00 85.56           N  
ANISOU 8449  N   ARG C1008    11682  13065   7761   1029   -655   -609       N  
ATOM   8450  CA  ARG C1008     -62.624  35.054  74.529  1.00 87.17           C  
ANISOU 8450  CA  ARG C1008    11857  13279   7986   1136   -582   -764       C  
ATOM   8451  C   ARG C1008     -61.098  35.208  74.709  1.00 92.77           C  
ANISOU 8451  C   ARG C1008    12418  14158   8674   1196   -496   -763       C  
ATOM   8452  O   ARG C1008     -60.394  34.216  74.905  1.00 93.46           O  
ANISOU 8452  O   ARG C1008    12419  14209   8881   1345   -454   -836       O  
ATOM   8453  CB  ARG C1008     -63.023  35.079  73.040  1.00 87.49           C  
ANISOU 8453  CB  ARG C1008    11985  13379   7879   1062   -564   -893       C  
ATOM   8454  CG  ARG C1008     -62.426  33.942  72.222  1.00 98.08           C  
ANISOU 8454  CG  ARG C1008    13306  14735   9223   1173   -473  -1103       C  
ATOM   8455  CD  ARG C1008     -62.981  33.874  70.818  1.00106.46           C  
ANISOU 8455  CD  ARG C1008    14485  15848  10117   1083   -471  -1242       C  
ATOM   8456  NE  ARG C1008     -62.075  33.126  69.948  1.00114.80           N  
ANISOU 8456  NE  ARG C1008    15498  17014  11106   1172   -336  -1467       N  
ATOM   8457  CZ  ARG C1008     -61.359  33.670  68.971  1.00127.65           C  
ANISOU 8457  CZ  ARG C1008    17097  18904  12499   1091   -223  -1536       C  
ATOM   8458  NH1 ARG C1008     -61.463  34.967  68.704  1.00112.24           N  
ANISOU 8458  NH1 ARG C1008    15174  17107  10364    906   -256  -1374       N  
ATOM   8459  NH2 ARG C1008     -60.550  32.919  68.238  1.00117.48           N  
ANISOU 8459  NH2 ARG C1008    15752  17724  11160   1189    -75  -1772       N  
ATOM   8460  N   ILE C1009     -60.610  36.467  74.672  1.00 89.64           N  
ANISOU 8460  N   ILE C1009    11982  13932   8146   1077   -484   -671       N  
ATOM   8461  CA  ILE C1009     -59.208  36.833  74.886  1.00 90.77           C  
ANISOU 8461  CA  ILE C1009    11967  14258   8262   1088   -417   -640       C  
ATOM   8462  C   ILE C1009     -58.855  36.592  76.371  1.00 95.42           C  
ANISOU 8462  C   ILE C1009    12482  14770   9004   1172   -481   -530       C  
ATOM   8463  O   ILE C1009     -57.743  36.150  76.670  1.00 96.50           O  
ANISOU 8463  O   ILE C1009    12466  14983   9216   1273   -444   -542       O  
ATOM   8464  CB  ILE C1009     -58.936  38.304  74.420  1.00 93.59           C  
ANISOU 8464  CB  ILE C1009    12330  14790   8440    896   -415   -550       C  
ATOM   8465  CG1 ILE C1009     -59.060  38.433  72.883  1.00 95.05           C  
ANISOU 8465  CG1 ILE C1009    12576  15097   8442    803   -347   -645       C  
ATOM   8466  CG2 ILE C1009     -57.568  38.829  74.891  1.00 95.20           C  
ANISOU 8466  CG2 ILE C1009    12362  15171   8638    872   -376   -478       C  
ATOM   8467  CD1 ILE C1009     -59.353  39.862  72.355  1.00100.78           C  
ANISOU 8467  CD1 ILE C1009    13387  15903   9001    584   -409   -516       C  
ATOM   8468  N   ASP C1010     -59.816  36.856  77.285  1.00 91.09           N  
ANISOU 8468  N   ASP C1010    12033  14081   8497   1129   -577   -427       N  
ATOM   8469  CA  ASP C1010     -59.627  36.700  78.727  1.00 90.87           C  
ANISOU 8469  CA  ASP C1010    11967  13996   8562   1171   -645   -311       C  
ATOM   8470  C   ASP C1010     -59.843  35.280  79.261  1.00 97.31           C  
ANISOU 8470  C   ASP C1010    12787  14644   9541   1312   -676   -316       C  
ATOM   8471  O   ASP C1010     -58.888  34.679  79.754  1.00 97.79           O  
ANISOU 8471  O   ASP C1010    12735  14722   9699   1418   -691   -287       O  
ATOM   8472  CB  ASP C1010     -60.441  37.744  79.520  1.00 90.68           C  
ANISOU 8472  CB  ASP C1010    12035  13938   8482   1047   -712   -213       C  
ATOM   8473  CG  ASP C1010     -59.896  39.165  79.477  1.00 94.68           C  
ANISOU 8473  CG  ASP C1010    12517  14583   8875    917   -725   -165       C  
ATOM   8474  OD1 ASP C1010     -58.697  39.338  79.162  1.00 95.65           O  
ANISOU 8474  OD1 ASP C1010    12522  14857   8964    910   -688   -165       O  
ATOM   8475  OD2 ASP C1010     -60.655  40.099  79.798  1.00 96.80           O  
ANISOU 8475  OD2 ASP C1010    12874  14803   9105    822   -774   -130       O  
ATOM   8476  N   GLU C1011     -61.079  34.745  79.172  1.00 95.22           N  
ANISOU 8476  N   GLU C1011    12642  14211   9325   1306   -701   -339       N  
ATOM   8477  CA  GLU C1011     -61.411  33.412  79.689  1.00 96.87           C  
ANISOU 8477  CA  GLU C1011    12878  14233   9698   1406   -748   -319       C  
ATOM   8478  C   GLU C1011     -61.188  32.229  78.734  1.00104.46           C  
ANISOU 8478  C   GLU C1011    13829  15091  10772   1536   -716   -477       C  
ATOM   8479  O   GLU C1011     -60.854  31.137  79.200  1.00105.77           O  
ANISOU 8479  O   GLU C1011    13964  15118  11107   1658   -763   -456       O  
ATOM   8480  CB  GLU C1011     -62.816  33.375  80.307  1.00 97.35           C  
ANISOU 8480  CB  GLU C1011    13050  14165   9773   1318   -796   -240       C  
ATOM   8481  CG  GLU C1011     -62.925  34.153  81.607  1.00109.55           C  
ANISOU 8481  CG  GLU C1011    14595  15781  11247   1233   -827    -94       C  
ATOM   8482  CD  GLU C1011     -64.095  33.849  82.529  1.00137.57           C  
ANISOU 8482  CD  GLU C1011    18217  19228  14826   1166   -856      0       C  
ATOM   8483  OE1 GLU C1011     -65.069  33.199  82.084  1.00139.64           O  
ANISOU 8483  OE1 GLU C1011    18533  19355  15167   1156   -858    -40       O  
ATOM   8484  OE2 GLU C1011     -64.044  34.288  83.702  1.00130.74           O  
ANISOU 8484  OE2 GLU C1011    17350  18433  13892   1108   -873    109       O  
ATOM   8485  N   GLY C1012     -61.391  32.443  77.435  1.00102.31           N  
ANISOU 8485  N   GLY C1012    13592  14875  10404   1505   -649   -631       N  
ATOM   8486  CA  GLY C1012     -61.218  31.405  76.423  1.00104.46           C  
ANISOU 8486  CA  GLY C1012    13872  15070  10747   1615   -604   -828       C  
ATOM   8487  C   GLY C1012     -62.480  30.621  76.129  1.00109.51           C  
ANISOU 8487  C   GLY C1012    14653  15493  11464   1590   -665   -884       C  
ATOM   8488  O   GLY C1012     -63.172  30.187  77.055  1.00108.84           O  
ANISOU 8488  O   GLY C1012    14615  15243  11497   1571   -751   -755       O  
ATOM   8489  N   LEU C1013     -62.776  30.429  74.827  1.00107.53           N  
ANISOU 8489  N   LEU C1013    14469  15255  11132   1571   -623  -1076       N  
ATOM   8490  CA  LEU C1013     -63.953  29.702  74.336  1.00108.29           C  
ANISOU 8490  CA  LEU C1013    14699  15160  11286   1528   -692  -1160       C  
ATOM   8491  C   LEU C1013     -63.662  28.216  74.082  1.00116.74           C  
ANISOU 8491  C   LEU C1013    15786  16022  12549   1682   -704  -1327       C  
ATOM   8492  O   LEU C1013     -62.596  27.871  73.562  1.00117.95           O  
ANISOU 8492  O   LEU C1013    15862  16243  12710   1817   -614  -1492       O  
ATOM   8493  CB  LEU C1013     -64.503  30.378  73.059  1.00107.99           C  
ANISOU 8493  CB  LEU C1013    14743  15255  11033   1397   -673  -1267       C  
ATOM   8494  CG  LEU C1013     -65.735  29.754  72.389  1.00112.94           C  
ANISOU 8494  CG  LEU C1013    15503  15720  11687   1324   -762  -1366       C  
ATOM   8495  CD1 LEU C1013     -67.010  30.164  73.084  1.00111.28           C  
ANISOU 8495  CD1 LEU C1013    15324  15421  11534   1202   -868  -1181       C  
ATOM   8496  CD2 LEU C1013     -65.809  30.135  70.933  1.00116.38           C  
ANISOU 8496  CD2 LEU C1013    16012  16312  11895   1239   -731  -1528       C  
ATOM   8497  N   ARG C1014     -64.622  27.345  74.449  1.00115.26           N  
ANISOU 8497  N   ARG C1014    15690  15574  12529   1658   -814  -1288       N  
ATOM   8498  CA  ARG C1014     -64.536  25.901  74.247  1.00118.23           C  
ANISOU 8498  CA  ARG C1014    16113  15686  13125   1784   -863  -1435       C  
ATOM   8499  C   ARG C1014     -65.875  25.349  73.762  1.00123.93           C  
ANISOU 8499  C   ARG C1014    16980  16220  13888   1662   -961  -1497       C  
ATOM   8500  O   ARG C1014     -66.858  25.364  74.502  1.00122.19           O  
ANISOU 8500  O   ARG C1014    16793  15900  13734   1540  -1050  -1306       O  
ATOM   8501  CB  ARG C1014     -64.057  25.173  75.518  1.00119.56           C  
ANISOU 8501  CB  ARG C1014    16221  15672  13536   1897   -937  -1264       C  
ATOM   8502  CG  ARG C1014     -62.554  25.264  75.762  1.00132.33           C  
ANISOU 8502  CG  ARG C1014    17681  17410  15189   2075   -866  -1282       C  
ATOM   8503  CD  ARG C1014     -61.944  23.910  76.082  1.00145.06           C  
ANISOU 8503  CD  ARG C1014    19263  18747  17107   2277   -943  -1331       C  
ATOM   8504  NE  ARG C1014     -60.496  24.000  76.288  1.00153.42           N  
ANISOU 8504  NE  ARG C1014    20136  19932  18225   2460   -883  -1353       N  
ATOM   8505  CZ  ARG C1014     -59.586  23.857  75.327  1.00166.91           C  
ANISOU 8505  CZ  ARG C1014    21745  21746  19929   2613   -756  -1627       C  
ATOM   8506  NH1 ARG C1014     -58.295  23.959  75.610  1.00154.25           N  
ANISOU 8506  NH1 ARG C1014    19939  20268  18401   2772   -707  -1623       N  
ATOM   8507  NH2 ARG C1014     -59.961  23.612  74.077  1.00153.28           N  
ANISOU 8507  NH2 ARG C1014    20110  20015  18113   2601   -674  -1911       N  
ATOM   8508  N   LEU C1015     -65.905  24.870  72.508  1.00123.77           N  
ANISOU 8508  N   LEU C1015    17038  16170  13818   1685   -940  -1776       N  
ATOM   8509  CA  LEU C1015     -67.095  24.300  71.865  1.00125.08           C  
ANISOU 8509  CA  LEU C1015    17346  16166  14012   1564  -1047  -1879       C  
ATOM   8510  C   LEU C1015     -67.434  22.921  72.437  1.00132.71           C  
ANISOU 8510  C   LEU C1015    18370  16760  15293   1614  -1171  -1862       C  
ATOM   8511  O   LEU C1015     -68.591  22.504  72.390  1.00132.27           O  
ANISOU 8511  O   LEU C1015    18406  16536  15313   1471  -1291  -1829       O  
ATOM   8512  CB  LEU C1015     -66.886  24.198  70.345  1.00126.97           C  
ANISOU 8512  CB  LEU C1015    17663  16507  14071   1572   -985  -2204       C  
ATOM   8513  CG  LEU C1015     -66.359  25.438  69.617  1.00130.77           C  
ANISOU 8513  CG  LEU C1015    18099  17359  14230   1521   -856  -2239       C  
ATOM   8514  CD1 LEU C1015     -65.774  25.063  68.271  1.00133.86           C  
ANISOU 8514  CD1 LEU C1015    18545  17853  14463   1578   -756  -2583       C  
ATOM   8515  CD2 LEU C1015     -67.436  26.515  69.472  1.00130.91           C  
ANISOU 8515  CD2 LEU C1015    18158  17509  14072   1304   -934  -2066       C  
ATOM   8516  N   LYS C1016     -66.413  22.217  72.958  1.00132.75           N  
ANISOU 8516  N   LYS C1016    18314  16632  15494   1812  -1155  -1877       N  
ATOM   8517  CA  LYS C1016     -66.509  20.886  73.563  1.00135.70           C  
ANISOU 8517  CA  LYS C1016    18737  16625  16197   1886  -1288  -1837       C  
ATOM   8518  C   LYS C1016     -66.685  20.960  75.090  1.00140.57           C  
ANISOU 8518  C   LYS C1016    19299  17183  16930   1830  -1363  -1462       C  
ATOM   8519  O   LYS C1016     -66.208  21.912  75.717  1.00138.09           O  
ANISOU 8519  O   LYS C1016    18876  17114  16477   1832  -1286  -1294       O  
ATOM   8520  CB  LYS C1016     -65.291  20.018  73.174  1.00141.24           C  
ANISOU 8520  CB  LYS C1016    19402  17191  17073   2152  -1248  -2088       C  
ATOM   8521  CG  LYS C1016     -63.922  20.671  73.413  1.00155.44           C  
ANISOU 8521  CG  LYS C1016    21020  19248  18794   2319  -1109  -2073       C  
ATOM   8522  CD  LYS C1016     -62.827  20.023  72.573  1.00167.44           C  
ANISOU 8522  CD  LYS C1016    22482  20731  20408   2566  -1013  -2425       C  
ATOM   8523  CE  LYS C1016     -61.519  20.769  72.673  1.00175.21           C  
ANISOU 8523  CE  LYS C1016    23259  22024  21289   2701   -858  -2422       C  
ATOM   8524  NZ  LYS C1016     -60.484  20.182  71.784  1.00186.37           N  
ANISOU 8524  NZ  LYS C1016    24586  23445  22780   2939   -731  -2794       N  
ATOM   8525  N   ILE C1017     -67.366  19.948  75.677  1.00140.30           N  
ANISOU 8525  N   ILE C1017    19347  16824  17137   1764  -1516  -1332       N  
ATOM   8526  CA  ILE C1017     -67.642  19.850  77.119  1.00140.42           C  
ANISOU 8526  CA  ILE C1017    19334  16766  17252   1676  -1597   -968       C  
ATOM   8527  C   ILE C1017     -66.358  19.620  77.925  1.00147.57           C  
ANISOU 8527  C   ILE C1017    20148  17643  18279   1872  -1610   -853       C  
ATOM   8528  O   ILE C1017     -65.538  18.777  77.555  1.00149.72           O  
ANISOU 8528  O   ILE C1017    20416  17713  18755   2079  -1649  -1025       O  
ATOM   8529  CB  ILE C1017     -68.749  18.799  77.441  1.00145.27           C  
ANISOU 8529  CB  ILE C1017    20065  17048  18084   1517  -1760   -850       C  
ATOM   8530  CG1 ILE C1017     -70.026  19.061  76.607  1.00145.14           C  
ANISOU 8530  CG1 ILE C1017    20112  17081  17954   1318  -1762   -967       C  
ATOM   8531  CG2 ILE C1017     -69.070  18.759  78.949  1.00145.50           C  
ANISOU 8531  CG2 ILE C1017    20065  17055  18162   1389  -1823   -453       C  
ATOM   8532  CD1 ILE C1017     -71.045  17.941  76.584  1.00155.43           C  
ANISOU 8532  CD1 ILE C1017    21528  18044  19485   1165  -1926   -936       C  
ATOM   8533  N   TYR C1018     -66.199  20.377  79.026  1.00144.20           N  
ANISOU 8533  N   TYR C1018    19641  17418  17731   1807  -1585   -574       N  
ATOM   8534  CA  TYR C1018     -65.041  20.315  79.916  1.00145.56           C  
ANISOU 8534  CA  TYR C1018    19716  17610  17981   1954  -1619   -416       C  
ATOM   8535  C   TYR C1018     -65.425  20.465  81.393  1.00150.88           C  
ANISOU 8535  C   TYR C1018    20395  18316  18616   1795  -1694    -35       C  
ATOM   8536  O   TYR C1018     -66.327  21.239  81.724  1.00148.46           O  
ANISOU 8536  O   TYR C1018    20104  18195  18111   1594  -1629     75       O  
ATOM   8537  CB  TYR C1018     -63.989  21.376  79.515  1.00145.26           C  
ANISOU 8537  CB  TYR C1018    19539  17904  17748   2076  -1468   -549       C  
ATOM   8538  CG  TYR C1018     -64.456  22.813  79.638  1.00143.77           C  
ANISOU 8538  CG  TYR C1018    19323  18057  17247   1905  -1352   -474       C  
ATOM   8539  CD1 TYR C1018     -64.135  23.578  80.756  1.00144.22           C  
ANISOU 8539  CD1 TYR C1018    19310  18306  17183   1849  -1346   -235       C  
ATOM   8540  CD2 TYR C1018     -65.187  23.421  78.621  1.00143.31           C  
ANISOU 8540  CD2 TYR C1018    19311  18121  17018   1804  -1263   -651       C  
ATOM   8541  CE1 TYR C1018     -64.560  24.902  80.874  1.00142.15           C  
ANISOU 8541  CE1 TYR C1018    19027  18324  16660   1706  -1248   -191       C  
ATOM   8542  CE2 TYR C1018     -65.626  24.740  78.733  1.00141.58           C  
ANISOU 8542  CE2 TYR C1018    19065  18177  16552   1662  -1180   -579       C  
ATOM   8543  CZ  TYR C1018     -65.302  25.481  79.857  1.00146.97           C  
ANISOU 8543  CZ  TYR C1018    19678  19023  17139   1622  -1167   -361       C  
ATOM   8544  OH  TYR C1018     -65.717  26.788  79.959  1.00144.74           O  
ANISOU 8544  OH  TYR C1018    19373  18982  16638   1498  -1091   -317       O  
ATOM   8545  N   LYS C1019     -64.719  19.738  82.276  1.00150.88           N  
ANISOU 8545  N   LYS C1019    20377  18145  18804   1889  -1831    161       N  
ATOM   8546  CA  LYS C1019     -64.912  19.821  83.723  1.00151.14           C  
ANISOU 8546  CA  LYS C1019    20423  18228  18778   1740  -1914    534       C  
ATOM   8547  C   LYS C1019     -64.088  21.098  83.954  1.00154.30           C  
ANISOU 8547  C   LYS C1019    20693  19001  18932   1792  -1795    523       C  
ATOM   8548  O   LYS C1019     -62.929  21.163  83.536  1.00154.42           O  
ANISOU 8548  O   LYS C1019    20602  19059  19012   2003  -1778    380       O  
ATOM   8549  CB  LYS C1019     -64.465  18.514  84.408  1.00156.95           C  
ANISOU 8549  CB  LYS C1019    21202  18613  19818   1820  -2135    737       C  
ATOM   8550  CG  LYS C1019     -65.098  18.300  85.774  1.00172.17           C  
ANISOU 8550  CG  LYS C1019    23205  20523  21688   1584  -2241   1138       C  
ATOM   8551  CD  LYS C1019     -64.672  16.984  86.408  1.00185.26           C  
ANISOU 8551  CD  LYS C1019    24924  21809  23659   1648  -2492   1370       C  
ATOM   8552  CE  LYS C1019     -63.761  17.198  87.592  1.00196.11           C  
ANISOU 8552  CE  LYS C1019    26235  23315  24964   1677  -2597   1661       C  
ATOM   8553  NZ  LYS C1019     -63.605  15.961  88.400  1.00209.57           N  
ANISOU 8553  NZ  LYS C1019    28026  24667  26935   1661  -2870   1981       N  
ATOM   8554  N   ASP C1020     -64.657  22.058  84.680  1.00149.90           N  
ANISOU 8554  N   ASP C1020    20138  18703  18116   1599  -1720    679       N  
ATOM   8555  CA  ASP C1020     -63.914  23.220  85.151  1.00148.56           C  
ANISOU 8555  CA  ASP C1020    19867  18853  17724   1613  -1646    718       C  
ATOM   8556  C   ASP C1020     -62.989  22.798  86.276  1.00155.37           C  
ANISOU 8556  C   ASP C1020    20693  19679  18661   1671  -1798    969       C  
ATOM   8557  O   ASP C1020     -63.080  21.680  86.749  1.00157.29           O  
ANISOU 8557  O   ASP C1020    21001  19656  19104   1672  -1957   1141       O  
ATOM   8558  CB  ASP C1020     -64.868  24.275  85.677  1.00148.19           C  
ANISOU 8558  CB  ASP C1020    19848  19050  17406   1392  -1537    800       C  
ATOM   8559  CG  ASP C1020     -66.102  23.679  86.288  1.00158.40           C  
ANISOU 8559  CG  ASP C1020    21240  20218  18725   1195  -1578    980       C  
ATOM   8560  OD1 ASP C1020     -66.317  23.869  87.499  1.00158.84           O  
ANISOU 8560  OD1 ASP C1020    21316  20389  18647   1051  -1596   1219       O  
ATOM   8561  OD2 ASP C1020     -66.860  23.024  85.553  1.00165.12           O  
ANISOU 8561  OD2 ASP C1020    22148  20869  19720   1170  -1591    880       O  
ATOM   8562  N   THR C1021     -62.103  23.685  86.714  1.00152.01           N  
ANISOU 8562  N   THR C1021    20167  19511  18080   1706  -1772   1005       N  
ATOM   8563  CA  THR C1021     -61.138  23.321  87.746  1.00154.25           C  
ANISOU 8563  CA  THR C1021    20400  19778  18430   1765  -1942   1243       C  
ATOM   8564  C   THR C1021     -61.778  22.566  88.893  1.00161.12           C  
ANISOU 8564  C   THR C1021    21396  20506  19317   1600  -2089   1567       C  
ATOM   8565  O   THR C1021     -61.218  21.601  89.393  1.00163.54           O  
ANISOU 8565  O   THR C1021    21705  20600  19831   1682  -2289   1754       O  
ATOM   8566  CB  THR C1021     -60.437  24.532  88.325  1.00160.04           C  
ANISOU 8566  CB  THR C1021    21042  20848  18919   1724  -1900   1288       C  
ATOM   8567  OG1 THR C1021     -60.656  25.657  87.473  1.00156.71           O  
ANISOU 8567  OG1 THR C1021    20583  20632  18326   1699  -1703   1042       O  
ATOM   8568  CG2 THR C1021     -58.957  24.262  88.436  1.00160.03           C  
ANISOU 8568  CG2 THR C1021    20886  20838  19079   1927  -2027   1318       C  
ATOM   8569  N   GLU C1022     -62.950  23.022  89.324  1.00157.21           N  
ANISOU 8569  N   GLU C1022    20996  20134  18603   1361  -1991   1642       N  
ATOM   8570  CA  GLU C1022     -63.724  22.321  90.343  1.00159.25           C  
ANISOU 8570  CA  GLU C1022    21375  20287  18845   1159  -2091   1943       C  
ATOM   8571  C   GLU C1022     -64.764  21.483  89.617  1.00164.22           C  
ANISOU 8571  C   GLU C1022    22085  20646  19666   1114  -2077   1866       C  
ATOM   8572  O   GLU C1022     -65.164  21.831  88.506  1.00162.14           O  
ANISOU 8572  O   GLU C1022    21796  20390  19420   1168  -1943   1582       O  
ATOM   8573  CB  GLU C1022     -64.402  23.314  91.286  1.00159.37           C  
ANISOU 8573  CB  GLU C1022    21424  20627  18502    918  -1970   2054       C  
ATOM   8574  CG  GLU C1022     -63.447  24.025  92.231  1.00171.31           C  
ANISOU 8574  CG  GLU C1022    22892  22391  19807    912  -2024   2176       C  
ATOM   8575  CD  GLU C1022     -64.133  24.519  93.489  1.00197.68           C  
ANISOU 8575  CD  GLU C1022    26312  25974  22823    645  -1970   2371       C  
ATOM   8576  OE1 GLU C1022     -65.371  24.383  93.586  1.00195.73           O  
ANISOU 8576  OE1 GLU C1022    26129  25723  22515    472  -1862   2397       O  
ATOM   8577  OE2 GLU C1022     -63.435  25.043  94.382  1.00194.66           O  
ANISOU 8577  OE2 GLU C1022    25921  25800  22241    603  -2032   2489       O  
ATOM   8578  N   GLY C1023     -65.202  20.378  90.213  1.00163.71           N  
ANISOU 8578  N   GLY C1023    22122  20338  19743   1000  -2230   2123       N  
ATOM   8579  CA  GLY C1023     -66.103  19.499  89.468  1.00164.56           C  
ANISOU 8579  CA  GLY C1023    22304  20149  20073    960  -2246   2040       C  
ATOM   8580  C   GLY C1023     -67.306  19.567  88.543  1.00167.46           C  
ANISOU 8580  C   GLY C1023    22696  20476  20456    865  -2113   1829       C  
ATOM   8581  O   GLY C1023     -67.656  18.548  87.940  1.00168.70           O  
ANISOU 8581  O   GLY C1023    22919  20300  20877    885  -2211   1775       O  
ATOM   8582  N   TYR C1024     -67.925  20.735  88.395  1.00161.58           N  
ANISOU 8582  N   TYR C1024    21898  20043  19452    768  -1913   1701       N  
ATOM   8583  CA  TYR C1024     -69.126  20.866  87.559  1.00160.31           C  
ANISOU 8583  CA  TYR C1024    21742  19866  19302    665  -1805   1522       C  
ATOM   8584  C   TYR C1024     -68.856  20.784  86.049  1.00162.72           C  
ANISOU 8584  C   TYR C1024    22034  20038  19754    860  -1790   1178       C  
ATOM   8585  O   TYR C1024     -67.709  20.867  85.610  1.00162.03           O  
ANISOU 8585  O   TYR C1024    21905  19941  19717   1083  -1808   1039       O  
ATOM   8586  CB  TYR C1024     -69.861  22.169  87.885  1.00159.33           C  
ANISOU 8586  CB  TYR C1024    21552  20105  18883    522  -1611   1493       C  
ATOM   8587  CG  TYR C1024     -70.633  22.128  89.184  1.00162.47           C  
ANISOU 8587  CG  TYR C1024    21968  20630  19133    267  -1581   1780       C  
ATOM   8588  CD1 TYR C1024     -70.224  22.873  90.282  1.00164.09           C  
ANISOU 8588  CD1 TYR C1024    22153  21113  19080    214  -1525   1916       C  
ATOM   8589  CD2 TYR C1024     -71.771  21.344  89.313  1.00165.08           C  
ANISOU 8589  CD2 TYR C1024    22336  20819  19569     61  -1605   1909       C  
ATOM   8590  CE1 TYR C1024     -70.926  22.839  91.471  1.00166.27           C  
ANISOU 8590  CE1 TYR C1024    22450  21540  19183    -32  -1477   2162       C  
ATOM   8591  CE2 TYR C1024     -72.481  21.303  90.499  1.00167.48           C  
ANISOU 8591  CE2 TYR C1024    22645  21275  19717   -193  -1554   2175       C  
ATOM   8592  CZ  TYR C1024     -72.054  22.052  91.574  1.00174.63           C  
ANISOU 8592  CZ  TYR C1024    23535  22474  20343   -236  -1481   2294       C  
ATOM   8593  OH  TYR C1024     -72.756  22.015  92.757  1.00177.66           O  
ANISOU 8593  OH  TYR C1024    23927  23041  20533   -499  -1410   2542       O  
ATOM   8594  N   TYR C1025     -69.923  20.625  85.263  1.00158.62           N  
ANISOU 8594  N   TYR C1025    21541  19435  19292    762  -1755   1040       N  
ATOM   8595  CA  TYR C1025     -69.817  20.575  83.800  1.00157.70           C  
ANISOU 8595  CA  TYR C1025    21432  19223  19266    904  -1738    706       C  
ATOM   8596  C   TYR C1025     -70.062  21.951  83.177  1.00158.11           C  
ANISOU 8596  C   TYR C1025    21406  19590  19078    903  -1572    517       C  
ATOM   8597  O   TYR C1025     -71.106  22.563  83.414  1.00156.54           O  
ANISOU 8597  O   TYR C1025    21175  19548  18756    729  -1495    573       O  
ATOM   8598  CB  TYR C1025     -70.748  19.506  83.203  1.00160.80           C  
ANISOU 8598  CB  TYR C1025    21913  19305  19878    802  -1840    652       C  
ATOM   8599  CG  TYR C1025     -70.219  18.092  83.332  1.00165.75           C  
ANISOU 8599  CG  TYR C1025    22633  19538  20808    890  -2029    722       C  
ATOM   8600  CD1 TYR C1025     -70.712  17.227  84.304  1.00170.03           C  
ANISOU 8600  CD1 TYR C1025    23240  19882  21481    713  -2159   1037       C  
ATOM   8601  CD2 TYR C1025     -69.239  17.611  82.467  1.00167.57           C  
ANISOU 8601  CD2 TYR C1025    22882  19587  21202   1148  -2078    470       C  
ATOM   8602  CE1 TYR C1025     -70.235  15.921  84.421  1.00174.01           C  
ANISOU 8602  CE1 TYR C1025    23839  19982  22296    794  -2362   1118       C  
ATOM   8603  CE2 TYR C1025     -68.750  16.309  82.578  1.00171.76           C  
ANISOU 8603  CE2 TYR C1025    23490  19721  22051   1255  -2263    514       C  
ATOM   8604  CZ  TYR C1025     -69.253  15.466  83.556  1.00181.10           C  
ANISOU 8604  CZ  TYR C1025    24750  20676  23385   1080  -2420    847       C  
ATOM   8605  OH  TYR C1025     -68.779  14.180  83.666  1.00185.28           O  
ANISOU 8605  OH  TYR C1025    25364  20774  24257   1186  -2631    907       O  
ATOM   8606  N   THR C1026     -69.078  22.437  82.398  1.00153.27           N  
ANISOU 8606  N   THR C1026    20755  19069  18411   1096  -1520    302       N  
ATOM   8607  CA  THR C1026     -69.084  23.761  81.766  1.00150.29           C  
ANISOU 8607  CA  THR C1026    20315  18975  17813   1108  -1386    140       C  
ATOM   8608  C   THR C1026     -68.818  23.676  80.246  1.00153.63           C  
ANISOU 8608  C   THR C1026    20761  19351  18259   1224  -1368   -167       C  
ATOM   8609  O   THR C1026     -68.165  22.739  79.786  1.00155.20           O  
ANISOU 8609  O   THR C1026    20996  19347  18626   1366  -1430   -285       O  
ATOM   8610  CB  THR C1026     -68.087  24.673  82.522  1.00157.23           C  
ANISOU 8610  CB  THR C1026    21114  20094  18531   1177  -1324    234       C  
ATOM   8611  OG1 THR C1026     -68.285  24.525  83.931  1.00157.05           O  
ANISOU 8611  OG1 THR C1026    21097  20090  18486   1066  -1361    511       O  
ATOM   8612  CG2 THR C1026     -68.219  26.143  82.160  1.00153.73           C  
ANISOU 8612  CG2 THR C1026    20614  19936  17862   1143  -1200    134       C  
ATOM   8613  N   ILE C1027     -69.339  24.658  79.476  1.00148.01           N  
ANISOU 8613  N   ILE C1027    20032  18829  17378   1161  -1289   -296       N  
ATOM   8614  CA  ILE C1027     -69.205  24.765  78.015  1.00147.83           C  
ANISOU 8614  CA  ILE C1027    20041  18826  17301   1222  -1265   -570       C  
ATOM   8615  C   ILE C1027     -69.154  26.244  77.545  1.00149.49           C  
ANISOU 8615  C   ILE C1027    20198  19336  17267   1191  -1167   -625       C  
ATOM   8616  O   ILE C1027     -69.920  27.070  78.037  1.00147.46           O  
ANISOU 8616  O   ILE C1027    19903  19198  16925   1070  -1147   -501       O  
ATOM   8617  CB  ILE C1027     -70.285  23.901  77.287  1.00152.39           C  
ANISOU 8617  CB  ILE C1027    20712  19185  18003   1123  -1360   -676       C  
ATOM   8618  CG1 ILE C1027     -69.995  23.754  75.775  1.00153.82           C  
ANISOU 8618  CG1 ILE C1027    20955  19361  18127   1198  -1350   -985       C  
ATOM   8619  CG2 ILE C1027     -71.727  24.372  77.580  1.00151.98           C  
ANISOU 8619  CG2 ILE C1027    20638  19193  17915    914  -1380   -548       C  
ATOM   8620  CD1 ILE C1027     -70.526  22.483  75.138  1.00162.59           C  
ANISOU 8620  CD1 ILE C1027    22181  20177  19421   1172  -1466  -1136       C  
ATOM   8621  N   GLY C1028     -68.243  26.551  76.620  1.00146.53           N  
ANISOU 8621  N   GLY C1028    19813  19073  16790   1299  -1105   -807       N  
ATOM   8622  CA  GLY C1028     -68.068  27.893  76.066  1.00144.92           C  
ANISOU 8622  CA  GLY C1028    19572  19131  16360   1261  -1028   -850       C  
ATOM   8623  C   GLY C1028     -67.198  28.788  76.921  1.00148.08           C  
ANISOU 8623  C   GLY C1028    19878  19712  16673   1300   -962   -716       C  
ATOM   8624  O   GLY C1028     -66.032  28.468  77.171  1.00148.39           O  
ANISOU 8624  O   GLY C1028    19861  19764  16755   1429   -932   -727       O  
ATOM   8625  N   ILE C1029     -67.763  29.926  77.362  1.00143.56           N  
ANISOU 8625  N   ILE C1029    19281  19275  15990   1190   -949   -599       N  
ATOM   8626  CA  ILE C1029     -67.087  30.893  78.233  1.00142.54           C  
ANISOU 8626  CA  ILE C1029    19079  19312  15768   1196   -901   -477       C  
ATOM   8627  C   ILE C1029     -67.820  30.944  79.593  1.00146.91           C  
ANISOU 8627  C   ILE C1029    19622  19829  16368   1118   -923   -296       C  
ATOM   8628  O   ILE C1029     -68.746  31.741  79.786  1.00145.46           O  
ANISOU 8628  O   ILE C1029    19433  19705  16130   1018   -914   -258       O  
ATOM   8629  CB  ILE C1029     -66.877  32.296  77.565  1.00144.45           C  
ANISOU 8629  CB  ILE C1029    19302  19755  15827   1144   -858   -523       C  
ATOM   8630  CG1 ILE C1029     -66.180  32.176  76.190  1.00145.72           C  
ANISOU 8630  CG1 ILE C1029    19477  19984  15906   1191   -820   -696       C  
ATOM   8631  CG2 ILE C1029     -66.087  33.240  78.491  1.00144.36           C  
ANISOU 8631  CG2 ILE C1029    19222  19891  15737   1144   -824   -410       C  
ATOM   8632  CD1 ILE C1029     -66.282  33.401  75.273  1.00151.35           C  
ANISOU 8632  CD1 ILE C1029    20210  20861  16435   1094   -808   -727       C  
ATOM   8633  N   GLY C1030     -67.418  30.042  80.489  1.00145.34           N  
ANISOU 8633  N   GLY C1030    19418  19530  16274   1166   -955   -189       N  
ATOM   8634  CA  GLY C1030     -67.945  29.917  81.844  1.00145.74           C  
ANISOU 8634  CA  GLY C1030    19468  19566  16342   1082   -970      0       C  
ATOM   8635  C   GLY C1030     -69.427  29.626  81.996  1.00151.01           C  
ANISOU 8635  C   GLY C1030    20161  20147  17069    951   -981     44       C  
ATOM   8636  O   GLY C1030     -70.031  30.058  82.984  1.00150.24           O  
ANISOU 8636  O   GLY C1030    20037  20134  16912    853   -942    161       O  
ATOM   8637  N   HIS C1031     -70.028  28.886  81.040  1.00149.35           N  
ANISOU 8637  N   HIS C1031    19995  19780  16973    942  -1029    -59       N  
ATOM   8638  CA  HIS C1031     -71.448  28.531  81.112  1.00150.24           C  
ANISOU 8638  CA  HIS C1031    20111  19805  17167    805  -1054    -16       C  
ATOM   8639  C   HIS C1031     -71.668  27.164  81.773  1.00157.05           C  
ANISOU 8639  C   HIS C1031    21016  20464  18191    757  -1122    119       C  
ATOM   8640  O   HIS C1031     -71.483  26.122  81.139  1.00157.98           O  
ANISOU 8640  O   HIS C1031    21199  20373  18454    807  -1204     44       O  
ATOM   8641  CB  HIS C1031     -72.144  28.628  79.740  1.00151.07           C  
ANISOU 8641  CB  HIS C1031    20238  19870  17293    778  -1093   -188       C  
ATOM   8642  CG  HIS C1031     -73.607  28.305  79.790  1.00155.24           C  
ANISOU 8642  CG  HIS C1031    20740  20321  17922    631  -1133   -143       C  
ATOM   8643  ND1 HIS C1031     -74.549  29.272  80.088  1.00156.25           N  
ANISOU 8643  ND1 HIS C1031    20775  20590  18002    546  -1086   -104       N  
ATOM   8644  CD2 HIS C1031     -74.238  27.121  79.607  1.00158.77           C  
ANISOU 8644  CD2 HIS C1031    21229  20564  18532    556  -1217   -132       C  
ATOM   8645  CE1 HIS C1031     -75.718  28.652  80.068  1.00156.84           C  
ANISOU 8645  CE1 HIS C1031    20819  20567  18208    421  -1134    -67       C  
ATOM   8646  NE2 HIS C1031     -75.580  27.355  79.790  1.00158.75           N  
ANISOU 8646  NE2 HIS C1031    21145  20598  18573    409  -1218    -74       N  
ATOM   8647  N   LEU C1032     -72.071  27.182  83.054  1.00154.83           N  
ANISOU 8647  N   LEU C1032    20704  20242  17880    650  -1090    317       N  
ATOM   8648  CA  LEU C1032     -72.351  25.985  83.849  1.00157.01           C  
ANISOU 8648  CA  LEU C1032    21023  20351  18284    560  -1157    506       C  
ATOM   8649  C   LEU C1032     -73.659  25.341  83.373  1.00162.36           C  
ANISOU 8649  C   LEU C1032    21703  20883  19102    419  -1201    490       C  
ATOM   8650  O   LEU C1032     -74.524  26.031  82.828  1.00160.67           O  
ANISOU 8650  O   LEU C1032    21425  20770  18852    363  -1155    386       O  
ATOM   8651  CB  LEU C1032     -72.448  26.368  85.338  1.00157.30           C  
ANISOU 8651  CB  LEU C1032    21025  20560  18183    454  -1089    718       C  
ATOM   8652  CG  LEU C1032     -72.226  25.254  86.359  1.00164.39           C  
ANISOU 8652  CG  LEU C1032    21983  21326  19150    381  -1173    968       C  
ATOM   8653  CD1 LEU C1032     -71.271  25.703  87.446  1.00164.51           C  
ANISOU 8653  CD1 LEU C1032    22001  21508  18998    414  -1158   1103       C  
ATOM   8654  CD2 LEU C1032     -73.543  24.802  86.969  1.00168.50           C  
ANISOU 8654  CD2 LEU C1032    22485  21838  19700    150  -1144   1126       C  
ATOM   8655  N   LEU C1033     -73.791  24.019  83.565  1.00161.89           N  
ANISOU 8655  N   LEU C1033    21714  20574  19223    360  -1309    600       N  
ATOM   8656  CA  LEU C1033     -74.985  23.273  83.169  1.00163.52           C  
ANISOU 8656  CA  LEU C1033    21928  20615  19588    202  -1375    605       C  
ATOM   8657  C   LEU C1033     -75.680  22.665  84.397  1.00169.96           C  
ANISOU 8657  C   LEU C1033    22727  21405  20444     -9  -1376    889       C  
ATOM   8658  O   LEU C1033     -76.786  23.100  84.731  1.00169.64           O  
ANISOU 8658  O   LEU C1033    22581  21521  20351   -173  -1287    944       O  
ATOM   8659  CB  LEU C1033     -74.653  22.213  82.098  1.00165.05           C  
ANISOU 8659  CB  LEU C1033    22232  20502  19979    289  -1517    447       C  
ATOM   8660  CG  LEU C1033     -73.984  22.735  80.817  1.00168.50           C  
ANISOU 8660  CG  LEU C1033    22690  20987  20347    473  -1501    157       C  
ATOM   8661  CD1 LEU C1033     -73.070  21.696  80.215  1.00170.39           C  
ANISOU 8661  CD1 LEU C1033    23035  20961  20743    629  -1602     25       C  
ATOM   8662  CD2 LEU C1033     -75.008  23.224  79.804  1.00170.48           C  
ANISOU 8662  CD2 LEU C1033    22907  21306  20561    385  -1502     -2       C  
ATOM   8663  N   THR C1034     -75.014  21.697  85.085  1.00168.82           N  
ANISOU 8663  N   THR C1034    22675  21079  20390     -4  -1474   1076       N  
ATOM   8664  CA  THR C1034     -75.483  21.002  86.301  1.00171.08           C  
ANISOU 8664  CA  THR C1034    22978  21327  20700   -217  -1500   1392       C  
ATOM   8665  C   THR C1034     -74.372  20.146  86.950  1.00177.03           C  
ANISOU 8665  C   THR C1034    23844  21887  21533   -138  -1639   1581       C  
ATOM   8666  O   THR C1034     -73.260  20.067  86.419  1.00175.96           O  
ANISOU 8666  O   THR C1034    23752  21642  21462     98  -1706   1441       O  
ATOM   8667  CB  THR C1034     -76.780  20.179  86.035  1.00180.90           C  
ANISOU 8667  CB  THR C1034    24211  22397  22125   -443  -1561   1450       C  
ATOM   8668  OG1 THR C1034     -77.363  19.805  87.285  1.00182.07           O  
ANISOU 8668  OG1 THR C1034    24338  22615  22226   -690  -1530   1767       O  
ATOM   8669  CG2 THR C1034     -76.540  18.936  85.166  1.00181.14           C  
ANISOU 8669  CG2 THR C1034    24372  22014  22440   -385  -1764   1366       C  
ATOM   8670  N   LYS C1035     -74.697  19.499  88.090  1.00176.23           N  
ANISOU 8670  N   LYS C1035    23778  21749  21431   -344  -1685   1907       N  
ATOM   8671  CA  LYS C1035     -73.825  18.574  88.821  1.00178.43           C  
ANISOU 8671  CA  LYS C1035    24168  21818  21809   -318  -1858   2156       C  
ATOM   8672  C   LYS C1035     -74.178  17.137  88.399  1.00185.32           C  
ANISOU 8672  C   LYS C1035    25146  22253  23016   -391  -2057   2226       C  
ATOM   8673  O   LYS C1035     -75.343  16.736  88.487  1.00186.22           O  
ANISOU 8673  O   LYS C1035    25248  22322  23185   -644  -2049   2332       O  
ATOM   8674  CB  LYS C1035     -73.913  18.779  90.356  1.00182.06           C  
ANISOU 8674  CB  LYS C1035    24625  22520  22030   -518  -1804   2493       C  
ATOM   8675  CG  LYS C1035     -75.327  18.829  90.956  1.00197.54           C  
ANISOU 8675  CG  LYS C1035    26522  24657  23877   -844  -1674   2651       C  
ATOM   8676  CD  LYS C1035     -75.829  20.261  91.164  1.00203.59           C  
ANISOU 8676  CD  LYS C1035    27144  25856  24354   -867  -1414   2497       C  
ATOM   8677  CE  LYS C1035     -77.311  20.324  91.451  1.00213.85           C  
ANISOU 8677  CE  LYS C1035    28332  27314  25607  -1144  -1268   2564       C  
ATOM   8678  NZ  LYS C1035     -77.637  19.889  92.835  1.00224.97           N  
ANISOU 8678  NZ  LYS C1035    29769  28856  26855  -1426  -1236   2924       N  
ATOM   8679  N   SER C1036     -73.188  16.390  87.873  1.00183.28           N  
ANISOU 8679  N   SER C1036    24975  21668  22995   -165  -2231   2138       N  
ATOM   8680  CA  SER C1036     -73.407  15.026  87.379  1.00186.31           C  
ANISOU 8680  CA  SER C1036    25475  21586  23730   -193  -2439   2150       C  
ATOM   8681  C   SER C1036     -72.179  14.115  87.547  1.00192.93           C  
ANISOU 8681  C   SER C1036    26410  22084  24812     18  -2657   2233       C  
ATOM   8682  O   SER C1036     -71.058  14.570  87.302  1.00191.03           O  
ANISOU 8682  O   SER C1036    26124  21927  24533    295  -2631   2070       O  
ATOM   8683  CB  SER C1036     -73.825  15.063  85.910  1.00188.84           C  
ANISOU 8683  CB  SER C1036    25786  21802  24162   -104  -2409   1761       C  
ATOM   8684  OG  SER C1036     -74.163  13.779  85.412  1.00200.87           O  
ANISOU 8684  OG  SER C1036    27428  22878  26015   -161  -2606   1743       O  
ATOM   8685  N   PRO C1037     -72.358  12.821  87.918  1.00193.61           N  
ANISOU 8685  N   PRO C1037    26618  21768  25175   -103  -2884   2478       N  
ATOM   8686  CA  PRO C1037     -71.190  11.928  88.028  1.00196.21           C  
ANISOU 8686  CA  PRO C1037    27029  21731  25790    128  -3118   2543       C  
ATOM   8687  C   PRO C1037     -70.671  11.477  86.660  1.00200.72           C  
ANISOU 8687  C   PRO C1037    27626  21996  26642    427  -3175   2117       C  
ATOM   8688  O   PRO C1037     -69.490  11.148  86.537  1.00201.40           O  
ANISOU 8688  O   PRO C1037    27709  21906  26909    720  -3282   2034       O  
ATOM   8689  CB  PRO C1037     -71.712  10.737  88.849  1.00202.11           C  
ANISOU 8689  CB  PRO C1037    27909  22142  26743   -137  -3346   2957       C  
ATOM   8690  CG  PRO C1037     -73.143  11.057  89.199  1.00205.93           C  
ANISOU 8690  CG  PRO C1037    28361  22869  27015   -522  -3200   3107       C  
ATOM   8691  CD  PRO C1037     -73.605  12.101  88.242  1.00197.60           C  
ANISOU 8691  CD  PRO C1037    27185  22120  25775   -453  -2953   2712       C  
ATOM   8692  N   SER C1038     -71.553  11.472  85.635  1.00196.79           N  
ANISOU 8692  N   SER C1038    27143  21454  26175    349  -3103   1838       N  
ATOM   8693  CA  SER C1038     -71.236  11.066  84.264  1.00197.25           C  
ANISOU 8693  CA  SER C1038    27243  21257  26447    584  -3136   1400       C  
ATOM   8694  C   SER C1038     -71.810  12.039  83.210  1.00198.05           C  
ANISOU 8694  C   SER C1038    27270  21675  26306    572  -2919   1050       C  
ATOM   8695  O   SER C1038     -72.491  13.006  83.559  1.00194.85           O  
ANISOU 8695  O   SER C1038    26773  21653  25606    391  -2754   1153       O  
ATOM   8696  CB  SER C1038     -71.715   9.638  84.012  1.00204.79           C  
ANISOU 8696  CB  SER C1038    28357  21664  27792    487  -3381   1429       C  
ATOM   8697  OG  SER C1038     -71.159   9.107  82.820  1.00214.24           O  
ANISOU 8697  OG  SER C1038    29609  22566  29225    762  -3440   1003       O  
ATOM   8698  N   LEU C1039     -71.518  11.773  81.920  1.00195.35           N  
ANISOU 8698  N   LEU C1039    26969  21167  26088    768  -2926    633       N  
ATOM   8699  CA  LEU C1039     -71.935  12.560  80.751  1.00192.72           C  
ANISOU 8699  CA  LEU C1039    26594  21083  25548    780  -2763    276       C  
ATOM   8700  C   LEU C1039     -73.459  12.633  80.507  1.00196.52           C  
ANISOU 8700  C   LEU C1039    27089  21611  25967    457  -2761    312       C  
ATOM   8701  O   LEU C1039     -73.909  13.510  79.765  1.00193.60           O  
ANISOU 8701  O   LEU C1039    26657  21528  25375    427  -2625    108       O  
ATOM   8702  CB  LEU C1039     -71.200  12.062  79.481  1.00194.31           C  
ANISOU 8702  CB  LEU C1039    26860  21063  25908   1055  -2792   -169       C  
ATOM   8703  CG  LEU C1039     -71.488  10.625  79.003  1.00203.11           C  
ANISOU 8703  CG  LEU C1039    28139  21635  27397   1041  -3015   -297       C  
ATOM   8704  CD1 LEU C1039     -71.612  10.570  77.494  1.00203.71           C  
ANISOU 8704  CD1 LEU C1039    28279  21677  27446   1126  -2972   -785       C  
ATOM   8705  CD2 LEU C1039     -70.418   9.652  79.479  1.00208.55           C  
ANISOU 8705  CD2 LEU C1039    28872  21942  28424   1276  -3178   -227       C  
ATOM   8706  N   ASN C1040     -74.235  11.710  81.116  1.00196.06           N  
ANISOU 8706  N   ASN C1040    27105  21271  26116    212  -2923    581       N  
ATOM   8707  CA  ASN C1040     -75.691  11.578  80.976  1.00196.53           C  
ANISOU 8707  CA  ASN C1040    27163  21327  26182   -118  -2953    652       C  
ATOM   8708  C   ASN C1040     -76.536  12.818  81.304  1.00197.72           C  
ANISOU 8708  C   ASN C1040    27146  21964  26013   -299  -2752    763       C  
ATOM   8709  O   ASN C1040     -77.504  13.084  80.586  1.00196.57           O  
ANISOU 8709  O   ASN C1040    26960  21908  25821   -442  -2731    615       O  
ATOM   8710  CB  ASN C1040     -76.208  10.349  81.739  1.00200.77           C  
ANISOU 8710  CB  ASN C1040    27800  21478  27006   -356  -3164    979       C  
ATOM   8711  CG  ASN C1040     -75.836   9.006  81.141  1.00226.10           C  
ANISOU 8711  CG  ASN C1040    31189  24120  30598   -249  -3405    811       C  
ATOM   8712  OD1 ASN C1040     -75.410   8.888  79.983  1.00219.65           O  
ANISOU 8712  OD1 ASN C1040    30432  23184  29843    -31  -3415    391       O  
ATOM   8713  ND2 ASN C1040     -76.029   7.948  81.916  1.00220.35           N  
ANISOU 8713  ND2 ASN C1040    30560  23025  30139   -416  -3610   1135       N  
ATOM   8714  N   ALA C1041     -76.193  13.560  82.379  1.00193.08           N  
ANISOU 8714  N   ALA C1041    26461  21680  25219   -294  -2619   1012       N  
ATOM   8715  CA  ALA C1041     -76.957  14.746  82.793  1.00190.53           C  
ANISOU 8715  CA  ALA C1041    25976  21805  24611   -445  -2421   1106       C  
ATOM   8716  C   ALA C1041     -76.396  16.103  82.320  1.00191.54           C  
ANISOU 8716  C   ALA C1041    26011  22297  24470   -230  -2239    874       C  
ATOM   8717  O   ALA C1041     -77.123  17.102  82.356  1.00189.07           O  
ANISOU 8717  O   ALA C1041    25568  22308  23962   -331  -2096    869       O  
ATOM   8718  CB  ALA C1041     -77.173  14.741  84.299  1.00192.01           C  
ANISOU 8718  CB  ALA C1041    26118  22123  24715   -638  -2380   1520       C  
ATOM   8719  N   ALA C1042     -75.125  16.138  81.863  1.00188.02           N  
ANISOU 8719  N   ALA C1042    25619  21791  24028     61  -2247    684       N  
ATOM   8720  CA  ALA C1042     -74.470  17.354  81.369  1.00184.83           C  
ANISOU 8720  CA  ALA C1042    25138  21705  23384    256  -2089    474       C  
ATOM   8721  C   ALA C1042     -75.068  17.821  80.034  1.00187.88           C  
ANISOU 8721  C   ALA C1042    25512  22176  23698    247  -2056    169       C  
ATOM   8722  O   ALA C1042     -75.454  18.986  79.916  1.00184.80           O  
ANISOU 8722  O   ALA C1042    25016  22107  23091    213  -1927    135       O  
ATOM   8723  CB  ALA C1042     -72.973  17.123  81.227  1.00185.91           C  
ANISOU 8723  CB  ALA C1042    25318  21742  23577    545  -2115    363       C  
ATOM   8724  N   LYS C1043     -75.167  16.901  79.046  1.00186.99           N  
ANISOU 8724  N   LYS C1043    25513  21763  23771    271  -2189    -51       N  
ATOM   8725  CA  LYS C1043     -75.720  17.145  77.706  1.00186.63           C  
ANISOU 8725  CA  LYS C1043    25490  21758  23663    245  -2201   -347       C  
ATOM   8726  C   LYS C1043     -77.218  17.451  77.753  1.00190.84           C  
ANISOU 8726  C   LYS C1043    25939  22402  24170    -31  -2216   -236       C  
ATOM   8727  O   LYS C1043     -77.707  18.202  76.908  1.00188.97           O  
ANISOU 8727  O   LYS C1043    25655  22357  23788    -59  -2184   -400       O  
ATOM   8728  CB  LYS C1043     -75.472  15.936  76.787  1.00191.96           C  
ANISOU 8728  CB  LYS C1043    26326  22053  24557    318  -2355   -603       C  
ATOM   8729  CG  LYS C1043     -74.020  15.751  76.374  1.00204.79           C  
ANISOU 8729  CG  LYS C1043    28005  23611  26196    626  -2316   -825       C  
ATOM   8730  CD  LYS C1043     -73.790  14.408  75.699  1.00216.86           C  
ANISOU 8730  CD  LYS C1043    29691  24709  27998    705  -2474  -1060       C  
ATOM   8731  CE  LYS C1043     -72.330  14.175  75.406  1.00227.23           C  
ANISOU 8731  CE  LYS C1043    31022  25954  29363   1030  -2422  -1275       C  
ATOM   8732  NZ  LYS C1043     -72.096  12.833  74.814  1.00240.80           N  
ANISOU 8732  NZ  LYS C1043    32890  27222  31382   1131  -2575  -1525       N  
ATOM   8733  N   SER C1044     -77.940  16.860  78.732  1.00189.56           N  
ANISOU 8733  N   SER C1044    25748  22123  24153   -242  -2271     53       N  
ATOM   8734  CA  SER C1044     -79.384  17.021  78.945  1.00189.99           C  
ANISOU 8734  CA  SER C1044    25686  22277  24224   -523  -2278    194       C  
ATOM   8735  C   SER C1044     -79.789  18.492  79.096  1.00191.25           C  
ANISOU 8735  C   SER C1044    25667  22861  24139   -526  -2104    212       C  
ATOM   8736  O   SER C1044     -80.707  18.944  78.407  1.00190.24           O  
ANISOU 8736  O   SER C1044    25455  22845  23983   -626  -2124    108       O  
ATOM   8737  CB  SER C1044     -79.839  16.215  80.160  1.00195.90           C  
ANISOU 8737  CB  SER C1044    26424  22882  25129   -736  -2323    538       C  
ATOM   8738  OG  SER C1044     -79.505  14.842  80.036  1.00207.48           O  
ANISOU 8738  OG  SER C1044    28062  23912  26859   -740  -2514    540       O  
ATOM   8739  N   GLU C1045     -79.076  19.240  79.966  1.00186.44           N  
ANISOU 8739  N   GLU C1045    25002  22471  23364   -409  -1952    334       N  
ATOM   8740  CA  GLU C1045     -79.318  20.666  80.216  1.00183.84           C  
ANISOU 8740  CA  GLU C1045    24519  22516  22816   -385  -1786    343       C  
ATOM   8741  C   GLU C1045     -78.855  21.526  79.036  1.00185.91           C  
ANISOU 8741  C   GLU C1045    24800  22901  22937   -208  -1770     68       C  
ATOM   8742  O   GLU C1045     -79.415  22.601  78.806  1.00183.98           O  
ANISOU 8742  O   GLU C1045    24436  22893  22574   -227  -1703     26       O  
ATOM   8743  CB  GLU C1045     -78.644  21.130  81.525  1.00184.24           C  
ANISOU 8743  CB  GLU C1045    24532  22739  22730   -330  -1650    545       C  
ATOM   8744  CG  GLU C1045     -79.042  20.350  82.774  1.00197.43           C  
ANISOU 8744  CG  GLU C1045    26194  24335  24486   -526  -1656    851       C  
ATOM   8745  CD  GLU C1045     -80.523  20.213  83.076  1.00217.42           C  
ANISOU 8745  CD  GLU C1045    28591  26929  27089   -801  -1635    979       C  
ATOM   8746  OE1 GLU C1045     -81.245  21.235  83.026  1.00210.42           O  
ANISOU 8746  OE1 GLU C1045    27540  26314  26098   -834  -1515    920       O  
ATOM   8747  OE2 GLU C1045     -80.958  19.080  83.386  1.00212.32           O  
ANISOU 8747  OE2 GLU C1045    27995  26056  26621   -988  -1743   1147       O  
ATOM   8748  N   LEU C1046     -77.838  21.045  78.290  1.00182.91           N  
ANISOU 8748  N   LEU C1046    24565  22357  22575    -37  -1833   -117       N  
ATOM   8749  CA  LEU C1046     -77.280  21.713  77.115  1.00181.39           C  
ANISOU 8749  CA  LEU C1046    24412  22276  22230    115  -1815   -378       C  
ATOM   8750  C   LEU C1046     -78.252  21.652  75.929  1.00185.39           C  
ANISOU 8750  C   LEU C1046    24935  22747  22757     -4  -1930   -547       C  
ATOM   8751  O   LEU C1046     -78.600  22.700  75.386  1.00183.47           O  
ANISOU 8751  O   LEU C1046    24621  22727  22362     -9  -1901   -612       O  
ATOM   8752  CB  LEU C1046     -75.904  21.108  76.751  1.00182.29           C  
ANISOU 8752  CB  LEU C1046    24654  22238  22368    325  -1826   -531       C  
ATOM   8753  CG  LEU C1046     -75.234  21.575  75.449  1.00186.59           C  
ANISOU 8753  CG  LEU C1046    25256  22886  22754    469  -1799   -823       C  
ATOM   8754  CD1 LEU C1046     -74.673  22.986  75.577  1.00184.15           C  
ANISOU 8754  CD1 LEU C1046    24856  22905  22208    558  -1655   -794       C  
ATOM   8755  CD2 LEU C1046     -74.132  20.619  75.038  1.00191.00           C  
ANISOU 8755  CD2 LEU C1046    25930  23229  23414    649  -1827  -1006       C  
ATOM   8756  N   ASP C1047     -78.697  20.430  75.549  1.00183.84           N  
ANISOU 8756  N   ASP C1047    24835  22261  22756   -107  -2081   -608       N  
ATOM   8757  CA  ASP C1047     -79.614  20.158  74.432  1.00184.65           C  
ANISOU 8757  CA  ASP C1047    24974  22288  22898   -244  -2230   -774       C  
ATOM   8758  C   ASP C1047     -80.936  20.935  74.485  1.00186.26           C  
ANISOU 8758  C   ASP C1047    25001  22691  23080   -425  -2245   -659       C  
ATOM   8759  O   ASP C1047     -81.444  21.339  73.434  1.00185.93           O  
ANISOU 8759  O   ASP C1047    24957  22729  22957   -472  -2336   -808       O  
ATOM   8760  CB  ASP C1047     -79.873  18.647  74.292  1.00189.75           C  
ANISOU 8760  CB  ASP C1047    25748  22553  23795   -347  -2395   -819       C  
ATOM   8761  CG  ASP C1047     -78.771  17.885  73.580  1.00201.26           C  
ANISOU 8761  CG  ASP C1047    27397  23792  25281   -160  -2435  -1083       C  
ATOM   8762  OD1 ASP C1047     -77.618  17.915  74.064  1.00200.94           O  
ANISOU 8762  OD1 ASP C1047    27376  23756  25217     41  -2330  -1062       O  
ATOM   8763  OD2 ASP C1047     -79.068  17.228  72.562  1.00209.18           O  
ANISOU 8763  OD2 ASP C1047    28523  24616  26340   -217  -2577  -1318       O  
ATOM   8764  N   LYS C1048     -81.482  21.147  75.701  1.00181.00           N  
ANISOU 8764  N   LYS C1048    24179  22113  22480   -524  -2157   -398       N  
ATOM   8765  CA  LYS C1048     -82.734  21.878  75.907  1.00179.75           C  
ANISOU 8765  CA  LYS C1048    23810  22152  22335   -675  -2142   -287       C  
ATOM   8766  C   LYS C1048     -82.544  23.386  75.688  1.00179.00           C  
ANISOU 8766  C   LYS C1048    23622  22353  22036   -540  -2041   -337       C  
ATOM   8767  O   LYS C1048     -83.366  24.010  75.011  1.00178.52           O  
ANISOU 8767  O   LYS C1048    23462  22404  21963   -601  -2118   -393       O  
ATOM   8768  CB  LYS C1048     -83.321  21.583  77.299  1.00183.02           C  
ANISOU 8768  CB  LYS C1048    24086  22586  22867   -825  -2051    -13       C  
ATOM   8769  CG  LYS C1048     -84.839  21.732  77.364  1.00197.53           C  
ANISOU 8769  CG  LYS C1048    25707  24518  24827  -1047  -2089     76       C  
ATOM   8770  CD  LYS C1048     -85.399  21.409  78.747  1.00208.12           C  
ANISOU 8770  CD  LYS C1048    26907  25913  26257  -1217  -1970    345       C  
ATOM   8771  CE  LYS C1048     -85.707  22.638  79.573  1.00215.63           C  
ANISOU 8771  CE  LYS C1048    27643  27199  27087  -1173  -1761    431       C  
ATOM   8772  NZ  LYS C1048     -84.481  23.254  80.148  1.00220.92           N  
ANISOU 8772  NZ  LYS C1048    28408  27974  27556   -962  -1616    433       N  
ATOM   8773  N   ALA C1049     -81.454  23.959  76.244  1.00171.79           N  
ANISOU 8773  N   ALA C1049    22743  21551  20978   -363  -1890   -311       N  
ATOM   8774  CA  ALA C1049     -81.113  25.381  76.142  1.00168.31           C  
ANISOU 8774  CA  ALA C1049    22236  21361  20352   -234  -1794   -345       C  
ATOM   8775  C   ALA C1049     -80.796  25.823  74.708  1.00169.74           C  
ANISOU 8775  C   ALA C1049    22516  21577  20400   -162  -1892   -551       C  
ATOM   8776  O   ALA C1049     -81.080  26.967  74.353  1.00168.13           O  
ANISOU 8776  O   ALA C1049    22230  21551  20099   -137  -1892   -563       O  
ATOM   8777  CB  ALA C1049     -79.949  25.707  77.064  1.00167.43           C  
ANISOU 8777  CB  ALA C1049    22158  21327  20130    -88  -1636   -271       C  
ATOM   8778  N   ILE C1050     -80.219  24.921  73.892  1.00166.07           N  
ANISOU 8778  N   ILE C1050    22229  20941  19928   -132  -1976   -714       N  
ATOM   8779  CA  ILE C1050     -79.866  25.191  72.492  1.00165.35           C  
ANISOU 8779  CA  ILE C1050    22256  20895  19674    -86  -2058   -927       C  
ATOM   8780  C   ILE C1050     -81.123  25.207  71.597  1.00168.76           C  
ANISOU 8780  C   ILE C1050    22653  21322  20148   -256  -2247   -977       C  
ATOM   8781  O   ILE C1050     -81.348  26.183  70.875  1.00167.63           O  
ANISOU 8781  O   ILE C1050    22481  21346  19863   -259  -2301  -1008       O  
ATOM   8782  CB  ILE C1050     -78.746  24.220  71.978  1.00169.56           C  
ANISOU 8782  CB  ILE C1050    22981  21265  20177     23  -2054  -1119       C  
ATOM   8783  CG1 ILE C1050     -77.431  24.292  72.816  1.00168.59           C  
ANISOU 8783  CG1 ILE C1050    22867  21170  20020    207  -1886  -1064       C  
ATOM   8784  CG2 ILE C1050     -78.476  24.357  70.472  1.00171.19           C  
ANISOU 8784  CG2 ILE C1050    23320  21533  20191     35  -2130  -1366       C  
ATOM   8785  CD1 ILE C1050     -76.746  25.681  73.024  1.00173.02           C  
ANISOU 8785  CD1 ILE C1050    23357  22005  20379    315  -1750  -1006       C  
ATOM   8786  N   GLY C1051     -81.913  24.135  71.661  1.00165.93           N  
ANISOU 8786  N   GLY C1051    22295  20764  19988   -406  -2362   -967       N  
ATOM   8787  CA  GLY C1051     -83.135  23.979  70.878  1.00166.85           C  
ANISOU 8787  CA  GLY C1051    22366  20851  20177   -591  -2565  -1008       C  
ATOM   8788  C   GLY C1051     -83.031  22.958  69.761  1.00171.20           C  
ANISOU 8788  C   GLY C1051    23123  21213  20713   -655  -2728  -1241       C  
ATOM   8789  O   GLY C1051     -83.864  22.955  68.849  1.00172.18           O  
ANISOU 8789  O   GLY C1051    23250  21347  20824   -798  -2920  -1319       O  
ATOM   8790  N   ARG C1052     -81.999  22.086  69.826  1.00166.95           N  
ANISOU 8790  N   ARG C1052    22755  20498  20182   -543  -2662  -1365       N  
ATOM   8791  CA  ARG C1052     -81.713  21.013  68.862  1.00168.59           C  
ANISOU 8791  CA  ARG C1052    23177  20491  20389   -563  -2784  -1634       C  
ATOM   8792  C   ARG C1052     -80.765  19.958  69.464  1.00171.49           C  
ANISOU 8792  C   ARG C1052    23655  20603  20902   -435  -2700  -1679       C  
ATOM   8793  O   ARG C1052     -80.321  20.110  70.606  1.00169.39           O  
ANISOU 8793  O   ARG C1052    23302  20352  20708   -343  -2558  -1481       O  
ATOM   8794  CB  ARG C1052     -81.156  21.582  67.532  1.00168.54           C  
ANISOU 8794  CB  ARG C1052    23302  20663  20072   -494  -2799  -1874       C  
ATOM   8795  CG  ARG C1052     -79.738  22.148  67.605  1.00176.81           C  
ANISOU 8795  CG  ARG C1052    24392  21863  20925   -264  -2587  -1931       C  
ATOM   8796  CD  ARG C1052     -79.495  23.183  66.521  1.00185.74           C  
ANISOU 8796  CD  ARG C1052    25569  23275  21729   -256  -2590  -2032       C  
ATOM   8797  NE  ARG C1052     -79.315  24.526  67.079  1.00191.75           N  
ANISOU 8797  NE  ARG C1052    26182  24277  22397   -189  -2474  -1815       N  
ATOM   8798  CZ  ARG C1052     -80.303  25.385  67.318  1.00205.06           C  
ANISOU 8798  CZ  ARG C1052    27715  26074  24125   -289  -2554  -1617       C  
ATOM   8799  NH1 ARG C1052     -80.042  26.579  67.831  1.00188.73           N  
ANISOU 8799  NH1 ARG C1052    25531  24193  21986   -208  -2444  -1454       N  
ATOM   8800  NH2 ARG C1052     -81.561  25.053  67.050  1.00194.46           N  
ANISOU 8800  NH2 ARG C1052    26322  24648  22915   -468  -2750  -1590       N  
ATOM   8801  N   ASN C1053     -80.461  18.894  68.691  1.00169.50           N  
ANISOU 8801  N   ASN C1053    23597  20109  20696   -427  -2802  -1946       N  
ATOM   8802  CA  ASN C1053     -79.542  17.827  69.094  1.00170.12           C  
ANISOU 8802  CA  ASN C1053    23792  19902  20945   -282  -2758  -2032       C  
ATOM   8803  C   ASN C1053     -78.113  18.366  68.996  1.00171.06           C  
ANISOU 8803  C   ASN C1053    23934  20190  20869    -15  -2559  -2143       C  
ATOM   8804  O   ASN C1053     -77.698  18.830  67.929  1.00170.64           O  
ANISOU 8804  O   ASN C1053    23955  20321  20561     43  -2524  -2376       O  
ATOM   8805  CB  ASN C1053     -79.737  16.579  68.216  1.00174.59           C  
ANISOU 8805  CB  ASN C1053    24555  20149  21634   -354  -2939  -2322       C  
ATOM   8806  CG  ASN C1053     -78.733  15.473  68.451  1.00198.42           C  
ANISOU 8806  CG  ASN C1053    27706  22841  24845   -171  -2913  -2468       C  
ATOM   8807  OD1 ASN C1053     -78.656  14.878  69.533  1.00192.66           O  
ANISOU 8807  OD1 ASN C1053    26938  21887  24375   -161  -2920  -2249       O  
ATOM   8808  ND2 ASN C1053     -77.952  15.161  67.428  1.00191.25           N  
ANISOU 8808  ND2 ASN C1053    26953  21899  23815    -24  -2889  -2844       N  
ATOM   8809  N   THR C1054     -77.380  18.340  70.121  1.00165.34           N  
ANISOU 8809  N   THR C1054    23139  19431  20252    127  -2433  -1959       N  
ATOM   8810  CA  THR C1054     -76.011  18.853  70.188  1.00163.24           C  
ANISOU 8810  CA  THR C1054    22858  19329  19837    371  -2248  -2026       C  
ATOM   8811  C   THR C1054     -74.970  17.761  69.973  1.00168.37           C  
ANISOU 8811  C   THR C1054    23628  19714  20629    566  -2239  -2261       C  
ATOM   8812  O   THR C1054     -74.037  17.961  69.191  1.00168.27           O  
ANISOU 8812  O   THR C1054    23661  19830  20446    728  -2133  -2518       O  
ATOM   8813  CB  THR C1054     -75.756  19.611  71.508  1.00168.66           C  
ANISOU 8813  CB  THR C1054    23383  20175  20525    418  -2122  -1698       C  
ATOM   8814  OG1 THR C1054     -75.660  18.683  72.592  1.00168.48           O  
ANISOU 8814  OG1 THR C1054    23359  19882  20773    428  -2162  -1521       O  
ATOM   8815  CG2 THR C1054     -76.809  20.675  71.802  1.00165.75           C  
ANISOU 8815  CG2 THR C1054    22878  20046  20055    248  -2121  -1486       C  
ATOM   8816  N   ASN C1055     -75.124  16.617  70.692  1.00165.90           N  
ANISOU 8816  N   ASN C1055    23359  19035  20642    549  -2349  -2163       N  
ATOM   8817  CA  ASN C1055     -74.213  15.459  70.715  1.00167.97           C  
ANISOU 8817  CA  ASN C1055    23722  18963  21138    744  -2379  -2336       C  
ATOM   8818  C   ASN C1055     -72.863  15.857  71.380  1.00168.70           C  
ANISOU 8818  C   ASN C1055    23710  19185  21203   1001  -2211  -2255       C  
ATOM   8819  O   ASN C1055     -71.814  15.260  71.111  1.00170.16           O  
ANISOU 8819  O   ASN C1055    23936  19225  21493   1233  -2175  -2477       O  
ATOM   8820  CB  ASN C1055     -74.049  14.826  69.307  1.00172.12           C  
ANISOU 8820  CB  ASN C1055    24414  19361  21624    796  -2431  -2792       C  
ATOM   8821  CG  ASN C1055     -73.599  13.383  69.300  1.00199.48           C  
ANISOU 8821  CG  ASN C1055    28008  22359  25426    926  -2541  -2983       C  
ATOM   8822  OD1 ASN C1055     -72.477  13.062  68.890  1.00194.62           O  
ANISOU 8822  OD1 ASN C1055    27422  21693  24831   1186  -2447  -3261       O  
ATOM   8823  ND2 ASN C1055     -74.475  12.474  69.716  1.00192.96           N  
ANISOU 8823  ND2 ASN C1055    27256  21175  24885    747  -2746  -2849       N  
ATOM   8824  N   GLY C1056     -72.936  16.859  72.263  1.00160.69           N  
ANISOU 8824  N   GLY C1056    22552  18441  20063    952  -2119  -1942       N  
ATOM   8825  CA  GLY C1056     -71.801  17.407  72.999  1.00158.12           C  
ANISOU 8825  CA  GLY C1056    22111  18282  19683   1142  -1978  -1814       C  
ATOM   8826  C   GLY C1056     -71.016  18.472  72.257  1.00158.25           C  
ANISOU 8826  C   GLY C1056    22067  18663  19396   1262  -1803  -1991       C  
ATOM   8827  O   GLY C1056     -69.995  18.950  72.761  1.00156.41           O  
ANISOU 8827  O   GLY C1056    21730  18583  19113   1418  -1686  -1914       O  
ATOM   8828  N   VAL C1057     -71.484  18.846  71.046  1.00153.54           N  
ANISOU 8828  N   VAL C1057    21538  18212  18590   1170  -1797  -2217       N  
ATOM   8829  CA  VAL C1057     -70.841  19.831  70.166  1.00151.58           C  
ANISOU 8829  CA  VAL C1057    21257  18312  18023   1236  -1646  -2390       C  
ATOM   8830  C   VAL C1057     -71.798  20.998  69.843  1.00151.15           C  
ANISOU 8830  C   VAL C1057    21177  18530  17723   1027  -1661  -2268       C  
ATOM   8831  O   VAL C1057     -72.985  20.773  69.593  1.00151.16           O  
ANISOU 8831  O   VAL C1057    21235  18433  17766    842  -1803  -2246       O  
ATOM   8832  CB  VAL C1057     -70.286  19.176  68.860  1.00158.64           C  
ANISOU 8832  CB  VAL C1057    22268  19150  18857   1346  -1615  -2818       C  
ATOM   8833  CG1 VAL C1057     -69.301  20.102  68.147  1.00157.78           C  
ANISOU 8833  CG1 VAL C1057    22098  19414  18437   1444  -1420  -2966       C  
ATOM   8834  CG2 VAL C1057     -69.636  17.817  69.129  1.00161.49           C  
ANISOU 8834  CG2 VAL C1057    22672  19140  19547   1541  -1658  -2965       C  
ATOM   8835  N   ILE C1058     -71.260  22.237  69.841  1.00143.91           N  
ANISOU 8835  N   ILE C1058    20166  17944  16570   1060  -1528  -2188       N  
ATOM   8836  CA  ILE C1058     -71.951  23.501  69.523  1.00140.78           C  
ANISOU 8836  CA  ILE C1058    19733  17815  15942    903  -1535  -2071       C  
ATOM   8837  C   ILE C1058     -70.999  24.440  68.759  1.00141.55           C  
ANISOU 8837  C   ILE C1058    19813  18224  15743    968  -1395  -2183       C  
ATOM   8838  O   ILE C1058     -69.788  24.217  68.783  1.00141.85           O  
ANISOU 8838  O   ILE C1058    19818  18299  15778   1140  -1266  -2294       O  
ATOM   8839  CB  ILE C1058     -72.551  24.203  70.783  1.00141.39           C  
ANISOU 8839  CB  ILE C1058    19684  17938  16099    827  -1545  -1731       C  
ATOM   8840  CG1 ILE C1058     -71.541  24.276  71.956  1.00140.61           C  
ANISOU 8840  CG1 ILE C1058    19490  17850  16084    978  -1433  -1580       C  
ATOM   8841  CG2 ILE C1058     -73.887  23.582  71.205  1.00142.89           C  
ANISOU 8841  CG2 ILE C1058    19882  17918  16494    668  -1693  -1613       C  
ATOM   8842  CD1 ILE C1058     -71.492  25.609  72.666  1.00144.51           C  
ANISOU 8842  CD1 ILE C1058    19869  18585  16453    950  -1356  -1362       C  
ATOM   8843  N   THR C1059     -71.539  25.480  68.088  1.00134.99           N  
ANISOU 8843  N   THR C1059    18996  17618  14678    824  -1428  -2140       N  
ATOM   8844  CA  THR C1059     -70.733  26.471  67.351  1.00133.36           C  
ANISOU 8844  CA  THR C1059    18780  17719  14170    835  -1312  -2198       C  
ATOM   8845  C   THR C1059     -70.764  27.834  68.072  1.00132.43           C  
ANISOU 8845  C   THR C1059    18545  17777  13995    796  -1282  -1915       C  
ATOM   8846  O   THR C1059     -71.364  27.938  69.146  1.00130.24           O  
ANISOU 8846  O   THR C1059    18192  17391  13903    779  -1331  -1710       O  
ATOM   8847  CB  THR C1059     -71.136  26.553  65.856  1.00140.43           C  
ANISOU 8847  CB  THR C1059    19813  18736  14807    701  -1381  -2395       C  
ATOM   8848  OG1 THR C1059     -72.485  27.004  65.736  1.00136.90           O  
ANISOU 8848  OG1 THR C1059    19383  18269  14362    518  -1567  -2246       O  
ATOM   8849  CG2 THR C1059     -70.937  25.234  65.110  1.00141.99           C  
ANISOU 8849  CG2 THR C1059    20138  18777  15037    756  -1385  -2730       C  
ATOM   8850  N   LYS C1060     -70.115  28.869  67.490  1.00127.47           N  
ANISOU 8850  N   LYS C1060    17905  17420  13109    771  -1200  -1909       N  
ATOM   8851  CA  LYS C1060     -70.063  30.234  68.031  1.00124.55           C  
ANISOU 8851  CA  LYS C1060    17444  17207  12673    727  -1183  -1669       C  
ATOM   8852  C   LYS C1060     -71.456  30.873  68.163  1.00126.53           C  
ANISOU 8852  C   LYS C1060    17690  17412  12974    587  -1349  -1499       C  
ATOM   8853  O   LYS C1060     -71.669  31.683  69.066  1.00124.04           O  
ANISOU 8853  O   LYS C1060    17279  17112  12738    588  -1349  -1301       O  
ATOM   8854  CB  LYS C1060     -69.163  31.122  67.162  1.00127.52           C  
ANISOU 8854  CB  LYS C1060    17833  17864  12754    690  -1088  -1709       C  
ATOM   8855  CG  LYS C1060     -67.704  31.146  67.603  1.00140.27           C  
ANISOU 8855  CG  LYS C1060    19347  19586  14362    830   -902  -1736       C  
ATOM   8856  CD  LYS C1060     -66.818  31.983  66.672  1.00151.01           C  
ANISOU 8856  CD  LYS C1060    20709  21247  15419    762   -796  -1775       C  
ATOM   8857  CE  LYS C1060     -66.764  33.457  67.014  1.00158.84           C  
ANISOU 8857  CE  LYS C1060    21649  22376  16328    661   -823  -1524       C  
ATOM   8858  NZ  LYS C1060     -67.880  34.223  66.391  1.00167.07           N  
ANISOU 8858  NZ  LYS C1060    22788  23432  17258    484   -997  -1413       N  
ATOM   8859  N   ASP C1061     -72.387  30.511  67.252  1.00124.18           N  
ANISOU 8859  N   ASP C1061    17487  17064  12632    471  -1494  -1590       N  
ATOM   8860  CA  ASP C1061     -73.778  30.974  67.196  1.00123.30           C  
ANISOU 8860  CA  ASP C1061    17355  16905  12587    338  -1677  -1458       C  
ATOM   8861  C   ASP C1061     -74.505  30.609  68.499  1.00124.78           C  
ANISOU 8861  C   ASP C1061    17429  16908  13075    370  -1693  -1326       C  
ATOM   8862  O   ASP C1061     -75.143  31.470  69.107  1.00123.19           O  
ANISOU 8862  O   ASP C1061    17122  16731  12953    339  -1732  -1148       O  
ATOM   8863  CB  ASP C1061     -74.491  30.330  65.979  1.00127.54           C  
ANISOU 8863  CB  ASP C1061    18020  17404  13034    214  -1832  -1622       C  
ATOM   8864  CG  ASP C1061     -75.733  31.040  65.458  1.00136.93           C  
ANISOU 8864  CG  ASP C1061    19201  18628  14197     55  -2049  -1501       C  
ATOM   8865  OD1 ASP C1061     -76.628  31.356  66.276  1.00136.50           O  
ANISOU 8865  OD1 ASP C1061    19016  18483  14364     44  -2119  -1332       O  
ATOM   8866  OD2 ASP C1061     -75.850  31.201  64.222  1.00143.23           O  
ANISOU 8866  OD2 ASP C1061    20119  19543  14759    -61  -2156  -1586       O  
ATOM   8867  N   GLU C1062     -74.363  29.347  68.941  1.00120.99           N  
ANISOU 8867  N   GLU C1062    16968  16245  12758    432  -1656  -1413       N  
ATOM   8868  CA  GLU C1062     -74.983  28.820  70.157  1.00119.74           C  
ANISOU 8868  CA  GLU C1062    16719  15915  12863    436  -1663  -1283       C  
ATOM   8869  C   GLU C1062     -74.262  29.270  71.439  1.00119.75           C  
ANISOU 8869  C   GLU C1062    16622  15965  12913    545  -1519  -1132       C  
ATOM   8870  O   GLU C1062     -74.929  29.613  72.416  1.00117.94           O  
ANISOU 8870  O   GLU C1062    16288  15721  12804    510  -1518   -965       O  
ATOM   8871  CB  GLU C1062     -75.086  27.286  70.090  1.00123.20           C  
ANISOU 8871  CB  GLU C1062    17237  16114  13459    441  -1708  -1415       C  
ATOM   8872  CG  GLU C1062     -76.078  26.781  69.054  1.00136.87           C  
ANISOU 8872  CG  GLU C1062    19052  17762  15189    296  -1883  -1541       C  
ATOM   8873  CD  GLU C1062     -75.476  26.221  67.780  1.00162.14           C  
ANISOU 8873  CD  GLU C1062    22416  20968  18220    316  -1896  -1820       C  
ATOM   8874  OE1 GLU C1062     -74.824  26.990  67.037  1.00156.09           O  
ANISOU 8874  OE1 GLU C1062    21689  20424  17195    337  -1835  -1887       O  
ATOM   8875  OE2 GLU C1062     -75.689  25.018  67.507  1.00159.79           O  
ANISOU 8875  OE2 GLU C1062    22211  20456  18045    295  -1970  -1979       O  
ATOM   8876  N   ALA C1063     -72.908  29.264  71.424  1.00114.83           N  
ANISOU 8876  N   ALA C1063    16023  15415  12191    670  -1397  -1200       N  
ATOM   8877  CA  ALA C1063     -72.042  29.647  72.545  1.00112.46           C  
ANISOU 8877  CA  ALA C1063    15640  15175  11916    772  -1277  -1076       C  
ATOM   8878  C   ALA C1063     -72.225  31.108  72.960  1.00113.78           C  
ANISOU 8878  C   ALA C1063    15727  15508  11994    731  -1257   -925       C  
ATOM   8879  O   ALA C1063     -72.180  31.403  74.158  1.00112.60           O  
ANISOU 8879  O   ALA C1063    15499  15364  11919    757  -1204   -786       O  
ATOM   8880  CB  ALA C1063     -70.587  29.374  72.202  1.00113.67           C  
ANISOU 8880  CB  ALA C1063    15817  15393  11981    904  -1170  -1204       C  
ATOM   8881  N   GLU C1064     -72.445  32.016  71.980  1.00109.22           N  
ANISOU 8881  N   GLU C1064    15180  15059  11260    659  -1311   -953       N  
ATOM   8882  CA  GLU C1064     -72.684  33.436  72.254  1.00107.17           C  
ANISOU 8882  CA  GLU C1064    14858  14916  10945    620  -1324   -820       C  
ATOM   8883  C   GLU C1064     -74.067  33.601  72.874  1.00109.30           C  
ANISOU 8883  C   GLU C1064    15045  15099  11385    560  -1401   -720       C  
ATOM   8884  O   GLU C1064     -74.214  34.382  73.812  1.00107.54           O  
ANISOU 8884  O   GLU C1064    14736  14913  11214    579  -1358   -612       O  
ATOM   8885  CB  GLU C1064     -72.522  34.303  70.991  1.00109.01           C  
ANISOU 8885  CB  GLU C1064    15157  15289  10972    548  -1386   -852       C  
ATOM   8886  CG  GLU C1064     -72.310  35.779  71.304  1.00117.47           C  
ANISOU 8886  CG  GLU C1064    16180  16468  11985    532  -1384   -718       C  
ATOM   8887  CD  GLU C1064     -71.832  36.685  70.184  1.00137.40           C  
ANISOU 8887  CD  GLU C1064    18776  19142  14289    452  -1428   -708       C  
ATOM   8888  OE1 GLU C1064     -71.576  36.186  69.064  1.00136.53           O  
ANISOU 8888  OE1 GLU C1064    18758  19097  14019    404  -1441   -822       O  
ATOM   8889  OE2 GLU C1064     -71.700  37.905  70.436  1.00128.43           O  
ANISOU 8889  OE2 GLU C1064    17609  18057  13131    428  -1451   -588       O  
ATOM   8890  N   LYS C1065     -75.056  32.807  72.400  1.00106.24           N  
ANISOU 8890  N   LYS C1065    14676  14599  11093    487  -1508   -771       N  
ATOM   8891  CA  LYS C1065     -76.430  32.792  72.917  1.00105.85           C  
ANISOU 8891  CA  LYS C1065    14518  14473  11225    417  -1578   -687       C  
ATOM   8892  C   LYS C1065     -76.497  32.333  74.380  1.00108.13           C  
ANISOU 8892  C   LYS C1065    14722  14705  11656    449  -1465   -595       C  
ATOM   8893  O   LYS C1065     -77.444  32.688  75.082  1.00107.72           O  
ANISOU 8893  O   LYS C1065    14546  14661  11723    408  -1461   -508       O  
ATOM   8894  CB  LYS C1065     -77.355  31.948  72.025  1.00109.94           C  
ANISOU 8894  CB  LYS C1065    15077  14887  11807    313  -1728   -767       C  
ATOM   8895  CG  LYS C1065     -77.869  32.707  70.809  1.00123.28           C  
ANISOU 8895  CG  LYS C1065    16795  16653  13390    236  -1888   -789       C  
ATOM   8896  CD  LYS C1065     -79.088  32.042  70.192  1.00132.63           C  
ANISOU 8896  CD  LYS C1065    17968  17741  14683    112  -2064   -827       C  
ATOM   8897  CE  LYS C1065     -79.758  32.942  69.185  1.00141.07           C  
ANISOU 8897  CE  LYS C1065    19030  18891  15678     32  -2252   -797       C  
ATOM   8898  NZ  LYS C1065     -80.986  32.321  68.626  1.00151.16           N  
ANISOU 8898  NZ  LYS C1065    20275  20084  17074   -100  -2447   -823       N  
ATOM   8899  N   LEU C1066     -75.476  31.573  74.834  1.00103.64           N  
ANISOU 8899  N   LEU C1066    14215  14094  11071    522  -1374   -612       N  
ATOM   8900  CA  LEU C1066     -75.325  31.097  76.213  1.00102.81           C  
ANISOU 8900  CA  LEU C1066    14059  13945  11060    545  -1281   -501       C  
ATOM   8901  C   LEU C1066     -74.611  32.170  77.042  1.00103.21           C  
ANISOU 8901  C   LEU C1066    14062  14143  11009    613  -1176   -428       C  
ATOM   8902  O   LEU C1066     -74.963  32.385  78.202  1.00102.14           O  
ANISOU 8902  O   LEU C1066    13848  14042  10918    592  -1109   -324       O  
ATOM   8903  CB  LEU C1066     -74.525  29.776  76.268  1.00104.03           C  
ANISOU 8903  CB  LEU C1066    14303  13959  11266    601  -1272   -542       C  
ATOM   8904  CG  LEU C1066     -75.166  28.540  75.628  1.00110.89           C  
ANISOU 8904  CG  LEU C1066    15236  14633  12264    532  -1380   -623       C  
ATOM   8905  CD1 LEU C1066     -74.128  27.472  75.347  1.00112.20           C  
ANISOU 8905  CD1 LEU C1066    15508  14663  12462    635  -1378   -730       C  
ATOM   8906  CD2 LEU C1066     -76.295  27.976  76.486  1.00114.55           C  
ANISOU 8906  CD2 LEU C1066    15626  14996  12901    409  -1407   -485       C  
ATOM   8907  N   PHE C1067     -73.612  32.842  76.436  1.00 97.84           N  
ANISOU 8907  N   PHE C1067    13431  13561  10182    677  -1160   -488       N  
ATOM   8908  CA  PHE C1067     -72.834  33.923  77.048  1.00 95.72           C  
ANISOU 8908  CA  PHE C1067    13131  13427   9813    726  -1084   -435       C  
ATOM   8909  C   PHE C1067     -73.736  35.124  77.369  1.00 97.34           C  
ANISOU 8909  C   PHE C1067    13258  13689  10040    682  -1099   -387       C  
ATOM   8910  O   PHE C1067     -73.572  35.739  78.425  1.00 95.86           O  
ANISOU 8910  O   PHE C1067    13020  13564   9839    701  -1026   -329       O  
ATOM   8911  CB  PHE C1067     -71.677  34.338  76.117  1.00 97.23           C  
ANISOU 8911  CB  PHE C1067    13382  13710   9851    770  -1077   -510       C  
ATOM   8912  CG  PHE C1067     -70.760  35.411  76.655  1.00 97.52           C  
ANISOU 8912  CG  PHE C1067    13389  13877   9787    801  -1015   -455       C  
ATOM   8913  CD1 PHE C1067     -69.750  35.099  77.558  1.00100.28           C  
ANISOU 8913  CD1 PHE C1067    13715  14257  10129    867   -941   -412       C  
ATOM   8914  CD2 PHE C1067     -70.878  36.728  76.226  1.00 98.87           C  
ANISOU 8914  CD2 PHE C1067    13558  14127   9880    756  -1055   -438       C  
ATOM   8915  CE1 PHE C1067     -68.893  36.090  78.043  1.00100.33           C  
ANISOU 8915  CE1 PHE C1067    13692  14385  10043    877   -902   -365       C  
ATOM   8916  CE2 PHE C1067     -70.020  37.717  76.711  1.00100.91           C  
ANISOU 8916  CE2 PHE C1067    13797  14484  10058    766  -1013   -391       C  
ATOM   8917  CZ  PHE C1067     -69.036  37.391  77.616  1.00 98.75           C  
ANISOU 8917  CZ  PHE C1067    13497  14254   9769    822   -934   -361       C  
ATOM   8918  N   ASN C1068     -74.693  35.436  76.460  1.00 93.47           N  
ANISOU 8918  N   ASN C1068    12755  13170   9590    627  -1205   -421       N  
ATOM   8919  CA  ASN C1068     -75.671  36.517  76.598  1.00 92.59           C  
ANISOU 8919  CA  ASN C1068    12549  13080   9549    603  -1251   -391       C  
ATOM   8920  C   ASN C1068     -76.544  36.307  77.833  1.00 95.63           C  
ANISOU 8920  C   ASN C1068    12813  13454  10069    589  -1170   -345       C  
ATOM   8921  O   ASN C1068     -76.876  37.281  78.510  1.00 94.81           O  
ANISOU 8921  O   ASN C1068    12625  13402   9997    614  -1125   -334       O  
ATOM   8922  CB  ASN C1068     -76.550  36.618  75.349  1.00 93.33           C  
ANISOU 8922  CB  ASN C1068    12648  13132   9683    542  -1411   -422       C  
ATOM   8923  CG  ASN C1068     -75.828  37.016  74.087  1.00109.92           C  
ANISOU 8923  CG  ASN C1068    14868  15281  11616    526  -1493   -456       C  
ATOM   8924  OD1 ASN C1068     -74.656  37.415  74.096  1.00101.21           O  
ANISOU 8924  OD1 ASN C1068    13827  14255  10374    562  -1425   -455       O  
ATOM   8925  ND2 ASN C1068     -76.521  36.897  72.962  1.00101.75           N  
ANISOU 8925  ND2 ASN C1068    13865  14218  10578    454  -1645   -481       N  
ATOM   8926  N   GLN C1069     -76.892  35.032  78.130  1.00 92.36           N  
ANISOU 8926  N   GLN C1069    12393  12971   9731    541  -1149   -322       N  
ATOM   8927  CA  GLN C1069     -77.682  34.622  79.297  1.00 92.62           C  
ANISOU 8927  CA  GLN C1069    12316  13010   9866    491  -1059   -256       C  
ATOM   8928  C   GLN C1069     -76.887  34.892  80.584  1.00 94.45           C  
ANISOU 8928  C   GLN C1069    12558  13333   9997    531   -921   -203       C  
ATOM   8929  O   GLN C1069     -77.433  35.457  81.529  1.00 94.13           O  
ANISOU 8929  O   GLN C1069    12416  13377   9971    517   -828   -187       O  
ATOM   8930  CB  GLN C1069     -78.051  33.125  79.216  1.00 95.25           C  
ANISOU 8930  CB  GLN C1069    12674  13225  10294    408  -1094   -221       C  
ATOM   8931  CG  GLN C1069     -79.005  32.748  78.075  1.00111.74           C  
ANISOU 8931  CG  GLN C1069    14741  15223  12492    336  -1240   -275       C  
ATOM   8932  CD  GLN C1069     -79.127  31.253  77.856  1.00130.86           C  
ANISOU 8932  CD  GLN C1069    17232  17493  14997    257  -1297   -267       C  
ATOM   8933  OE1 GLN C1069     -78.899  30.432  78.754  1.00125.72           O  
ANISOU 8933  OE1 GLN C1069    16598  16791  14380    228  -1227   -181       O  
ATOM   8934  NE2 GLN C1069     -79.528  30.864  76.654  1.00124.83           N  
ANISOU 8934  NE2 GLN C1069    16516  16642  14271    209  -1444   -353       N  
ATOM   8935  N   ASP C1070     -75.590  34.504  80.601  1.00 89.58           N  
ANISOU 8935  N   ASP C1070    12056  12708   9273    582   -911   -189       N  
ATOM   8936  CA  ASP C1070     -74.679  34.698  81.733  1.00 88.51           C  
ANISOU 8936  CA  ASP C1070    11942  12658   9028    614   -818   -130       C  
ATOM   8937  C   ASP C1070     -74.346  36.160  81.964  1.00 89.64           C  
ANISOU 8937  C   ASP C1070    12066  12911   9082    659   -786   -176       C  
ATOM   8938  O   ASP C1070     -74.103  36.549  83.108  1.00 89.45           O  
ANISOU 8938  O   ASP C1070    12024  12978   8983    655   -700   -144       O  
ATOM   8939  CB  ASP C1070     -73.413  33.843  81.597  1.00 90.65           C  
ANISOU 8939  CB  ASP C1070    12312  12878   9252    667   -842   -103       C  
ATOM   8940  CG  ASP C1070     -73.673  32.350  81.703  1.00107.25           C  
ANISOU 8940  CG  ASP C1070    14445  14841  11465    626   -874    -40       C  
ATOM   8941  OD1 ASP C1070     -74.425  31.937  82.620  1.00109.63           O  
ANISOU 8941  OD1 ASP C1070    14699  15141  11815    537   -832     60       O  
ATOM   8942  OD2 ASP C1070     -73.116  31.594  80.885  1.00115.61           O  
ANISOU 8942  OD2 ASP C1070    15574  15791  12562    677   -939    -95       O  
ATOM   8943  N   VAL C1071     -74.353  36.974  80.890  1.00 84.36           N  
ANISOU 8943  N   VAL C1071    11410  12228   8415    688   -866   -247       N  
ATOM   8944  CA  VAL C1071     -74.152  38.422  80.995  1.00 83.05           C  
ANISOU 8944  CA  VAL C1071    11231  12122   8201    719   -867   -286       C  
ATOM   8945  C   VAL C1071     -75.434  39.012  81.606  1.00 87.27           C  
ANISOU 8945  C   VAL C1071    11645  12667   8848    710   -826   -320       C  
ATOM   8946  O   VAL C1071     -75.342  39.796  82.547  1.00 87.06           O  
ANISOU 8946  O   VAL C1071    11591  12706   8781    730   -749   -351       O  
ATOM   8947  CB  VAL C1071     -73.755  39.093  79.652  1.00 85.94           C  
ANISOU 8947  CB  VAL C1071    11656  12465   8531    730   -981   -318       C  
ATOM   8948  CG1 VAL C1071     -73.872  40.615  79.727  1.00 85.58           C  
ANISOU 8948  CG1 VAL C1071    11590  12430   8498    747  -1016   -343       C  
ATOM   8949  CG2 VAL C1071     -72.342  38.699  79.253  1.00 85.12           C  
ANISOU 8949  CG2 VAL C1071    11641  12403   8298    747   -974   -306       C  
ATOM   8950  N   ASP C1072     -76.619  38.580  81.113  1.00 83.89           N  
ANISOU 8950  N   ASP C1072    11135  12179   8561    677   -872   -326       N  
ATOM   8951  CA  ASP C1072     -77.922  39.022  81.608  1.00 84.24           C  
ANISOU 8951  CA  ASP C1072    11020  12242   8746    673   -828   -365       C  
ATOM   8952  C   ASP C1072     -78.068  38.760  83.104  1.00 86.69           C  
ANISOU 8952  C   ASP C1072    11272  12658   9006    643   -650   -351       C  
ATOM   8953  O   ASP C1072     -78.542  39.641  83.817  1.00 87.33           O  
ANISOU 8953  O   ASP C1072    11260  12806   9115    677   -565   -429       O  
ATOM   8954  CB  ASP C1072     -79.067  38.366  80.817  1.00 87.32           C  
ANISOU 8954  CB  ASP C1072    11323  12561   9295    621   -919   -353       C  
ATOM   8955  CG  ASP C1072     -80.447  38.931  81.111  1.00102.87           C  
ANISOU 8955  CG  ASP C1072    13087  14551  11447    631   -897   -401       C  
ATOM   8956  OD1 ASP C1072     -80.584  40.177  81.165  1.00104.56           O  
ANISOU 8956  OD1 ASP C1072    13250  14766  11713    716   -914   -471       O  
ATOM   8957  OD2 ASP C1072     -81.398  38.129  81.253  1.00110.78           O  
ANISOU 8957  OD2 ASP C1072    13971  15560  12561    555   -872   -372       O  
ATOM   8958  N   ALA C1073     -77.615  37.578  83.580  1.00 81.41           N  
ANISOU 8958  N   ALA C1073    10668  12005   8258    578   -601   -256       N  
ATOM   8959  CA  ALA C1073     -77.647  37.192  84.996  1.00 81.37           C  
ANISOU 8959  CA  ALA C1073    10638  12115   8163    516   -450   -201       C  
ATOM   8960  C   ALA C1073     -76.688  38.059  85.819  1.00 82.89           C  
ANISOU 8960  C   ALA C1073    10901  12406   8186    562   -388   -238       C  
ATOM   8961  O   ALA C1073     -77.002  38.401  86.962  1.00 82.81           O  
ANISOU 8961  O   ALA C1073    10839  12524   8100    530   -254   -268       O  
ATOM   8962  CB  ALA C1073     -77.284  35.724  85.150  1.00 82.41           C  
ANISOU 8962  CB  ALA C1073    10847  12195   8269    439   -466    -62       C  
ATOM   8963  N   ALA C1074     -75.528  38.426  85.219  1.00 77.49           N  
ANISOU 8963  N   ALA C1074    10331  11675   7435    624   -484   -245       N  
ATOM   8964  CA  ALA C1074     -74.511  39.276  85.840  1.00 76.23           C  
ANISOU 8964  CA  ALA C1074    10242  11593   7130    655   -462   -277       C  
ATOM   8965  C   ALA C1074     -75.028  40.708  85.912  1.00 80.11           C  
ANISOU 8965  C   ALA C1074    10674  12092   7671    705   -445   -419       C  
ATOM   8966  O   ALA C1074     -74.966  41.308  86.980  1.00 80.96           O  
ANISOU 8966  O   ALA C1074    10778  12298   7686    698   -350   -485       O  
ATOM   8967  CB  ALA C1074     -73.208  39.216  85.054  1.00 75.53           C  
ANISOU 8967  CB  ALA C1074    10256  11456   6985    693   -568   -240       C  
ATOM   8968  N   VAL C1075     -75.586  41.234  84.797  1.00 75.69           N  
ANISOU 8968  N   VAL C1075    10071  11424   7264    753   -545   -469       N  
ATOM   8969  CA  VAL C1075     -76.149  42.586  84.721  1.00 75.73           C  
ANISOU 8969  CA  VAL C1075    10014  11386   7376    818   -568   -593       C  
ATOM   8970  C   VAL C1075     -77.286  42.730  85.741  1.00 81.41           C  
ANISOU 8970  C   VAL C1075    10587  12185   8159    825   -417   -691       C  
ATOM   8971  O   VAL C1075     -77.215  43.630  86.579  1.00 81.72           O  
ANISOU 8971  O   VAL C1075    10621  12274   8154    860   -339   -811       O  
ATOM   8972  CB  VAL C1075     -76.527  43.020  83.275  1.00 78.93           C  
ANISOU 8972  CB  VAL C1075    10406  11653   7932    855   -740   -587       C  
ATOM   8973  CG1 VAL C1075     -77.220  44.378  83.258  1.00 79.70           C  
ANISOU 8973  CG1 VAL C1075    10423  11672   8187    935   -786   -701       C  
ATOM   8974  CG2 VAL C1075     -75.292  43.062  82.381  1.00 77.40           C  
ANISOU 8974  CG2 VAL C1075    10357  11425   7625    834   -854   -512       C  
ATOM   8975  N   ARG C1076     -78.255  41.782  85.750  1.00 78.83           N  
ANISOU 8975  N   ARG C1076    10147  11888   7916    777   -361   -643       N  
ATOM   8976  CA  ARG C1076     -79.363  41.754  86.721  1.00 80.52           C  
ANISOU 8976  CA  ARG C1076    10195  12220   8180    757   -186   -720       C  
ATOM   8977  C   ARG C1076     -78.851  41.712  88.172  1.00 84.33           C  
ANISOU 8977  C   ARG C1076    10736  12875   8433    700    -15   -740       C  
ATOM   8978  O   ARG C1076     -79.440  42.358  89.041  1.00 85.76           O  
ANISOU 8978  O   ARG C1076    10817  13162   8605    723    133   -887       O  
ATOM   8979  CB  ARG C1076     -80.339  40.599  86.435  1.00 81.28           C  
ANISOU 8979  CB  ARG C1076    10170  12323   8390    674   -171   -625       C  
ATOM   8980  CG  ARG C1076     -81.317  40.903  85.304  1.00 93.18           C  
ANISOU 8980  CG  ARG C1076    11542  13710  10152    730   -305   -661       C  
ATOM   8981  CD  ARG C1076     -82.319  39.781  85.087  1.00107.59           C  
ANISOU 8981  CD  ARG C1076    13235  15549  12096    627   -296   -576       C  
ATOM   8982  NE  ARG C1076     -81.838  38.771  84.140  1.00114.65           N  
ANISOU 8982  NE  ARG C1076    14265  16330  12967    561   -449   -448       N  
ATOM   8983  CZ  ARG C1076     -81.296  37.608  84.491  1.00127.22           C  
ANISOU 8983  CZ  ARG C1076    15967  17934  14437    461   -411   -329       C  
ATOM   8984  NH1 ARG C1076     -81.149  37.292  85.773  1.00113.28           N  
ANISOU 8984  NH1 ARG C1076    14201  16302  12539    395   -239   -287       N  
ATOM   8985  NH2 ARG C1076     -80.894  36.751  83.561  1.00111.53           N  
ANISOU 8985  NH2 ARG C1076    14095  15822  12458    427   -553   -255       N  
ATOM   8986  N   GLY C1077     -77.743  40.995  88.393  1.00 78.79           N  
ANISOU 8986  N   GLY C1077    10191  12198   7548    632    -47   -603       N  
ATOM   8987  CA  GLY C1077     -77.075  40.879  89.685  1.00 78.84           C  
ANISOU 8987  CA  GLY C1077    10283  12363   7310    561     63   -580       C  
ATOM   8988  C   GLY C1077     -76.362  42.152  90.100  1.00 82.37           C  
ANISOU 8988  C   GLY C1077    10808  12830   7659    622     55   -725       C  
ATOM   8989  O   GLY C1077     -76.337  42.482  91.288  1.00 83.61           O  
ANISOU 8989  O   GLY C1077    10978  13142   7647    579    186   -807       O  
ATOM   8990  N   ILE C1078     -75.780  42.882  89.123  1.00 77.38           N  
ANISOU 8990  N   ILE C1078    10235  12046   7120    706   -102   -756       N  
ATOM   8991  CA  ILE C1078     -75.095  44.165  89.335  1.00 77.13           C  
ANISOU 8991  CA  ILE C1078    10281  11986   7039    754   -147   -884       C  
ATOM   8992  C   ILE C1078     -76.130  45.237  89.694  1.00 83.07           C  
ANISOU 8992  C   ILE C1078    10922  12724   7919    833    -61  -1107       C  
ATOM   8993  O   ILE C1078     -75.879  46.052  90.582  1.00 84.02           O  
ANISOU 8993  O   ILE C1078    11085  12903   7933    840      4  -1260       O  
ATOM   8994  CB  ILE C1078     -74.248  44.575  88.090  1.00 78.48           C  
ANISOU 8994  CB  ILE C1078    10535  12001   7284    792   -341   -822       C  
ATOM   8995  CG1 ILE C1078     -72.967  43.717  87.969  1.00 77.37           C  
ANISOU 8995  CG1 ILE C1078    10500  11904   6992    731   -402   -653       C  
ATOM   8996  CG2 ILE C1078     -73.893  46.073  88.107  1.00 79.88           C  
ANISOU 8996  CG2 ILE C1078    10762  12093   7496    840   -410   -963       C  
ATOM   8997  CD1 ILE C1078     -72.404  43.600  86.521  1.00 80.46           C  
ANISOU 8997  CD1 ILE C1078    10930  12178   7465    754   -550   -565       C  
ATOM   8998  N   LEU C1079     -77.288  45.227  89.001  1.00 80.14           N  
ANISOU 8998  N   LEU C1079    10400  12269   7782    898    -70  -1137       N  
ATOM   8999  CA  LEU C1079     -78.379  46.186  89.197  1.00 81.81           C  
ANISOU 8999  CA  LEU C1079    10460  12442   8183   1005     -4  -1349       C  
ATOM   9000  C   LEU C1079     -79.070  46.070  90.557  1.00 87.82           C  
ANISOU 9000  C   LEU C1079    11115  13415   8836    975    250  -1490       C  
ATOM   9001  O   LEU C1079     -79.452  47.091  91.125  1.00 89.04           O  
ANISOU 9001  O   LEU C1079    11214  13574   9045   1062    335  -1726       O  
ATOM   9002  CB  LEU C1079     -79.392  46.122  88.038  1.00 81.80           C  
ANISOU 9002  CB  LEU C1079    10309  12302   8470   1075   -112  -1313       C  
ATOM   9003  CG  LEU C1079     -78.841  46.436  86.628  1.00 84.60           C  
ANISOU 9003  CG  LEU C1079    10764  12456   8923   1103   -366  -1198       C  
ATOM   9004  CD1 LEU C1079     -79.688  45.794  85.562  1.00 84.61           C  
ANISOU 9004  CD1 LEU C1079    10655  12391   9103   1101   -465  -1092       C  
ATOM   9005  CD2 LEU C1079     -78.684  47.937  86.383  1.00 86.85           C  
ANISOU 9005  CD2 LEU C1079    11085  12571   9343   1207   -487  -1325       C  
ATOM   9006  N   ARG C1080     -79.201  44.843  91.093  1.00 84.76           N  
ANISOU 9006  N   ARG C1080    10711  13204   8291    844    372  -1350       N  
ATOM   9007  CA  ARG C1080     -79.819  44.609  92.403  1.00 87.03           C  
ANISOU 9007  CA  ARG C1080    10908  13736   8424    770    626  -1444       C  
ATOM   9008  C   ARG C1080     -78.900  45.013  93.558  1.00 91.67           C  
ANISOU 9008  C   ARG C1080    11662  14464   8704    709    701  -1525       C  
ATOM   9009  O   ARG C1080     -79.387  45.317  94.650  1.00 94.13           O  
ANISOU 9009  O   ARG C1080    11913  14969   8882    682    911  -1700       O  
ATOM   9010  CB  ARG C1080     -80.295  43.158  92.546  1.00 87.58           C  
ANISOU 9010  CB  ARG C1080    10910  13929   8437    623    707  -1232       C  
ATOM   9011  CG  ARG C1080     -81.598  42.877  91.796  1.00100.06           C  
ANISOU 9011  CG  ARG C1080    12258  15449  10310    661    712  -1230       C  
ATOM   9012  CD  ARG C1080     -82.016  41.422  91.874  1.00110.99           C  
ANISOU 9012  CD  ARG C1080    13593  16923  11657    493    762  -1006       C  
ATOM   9013  NE  ARG C1080     -81.051  40.536  91.215  1.00118.72           N  
ANISOU 9013  NE  ARG C1080    14761  17766  12583    436    570   -777       N  
ATOM   9014  CZ  ARG C1080     -81.197  39.221  91.096  1.00134.36           C  
ANISOU 9014  CZ  ARG C1080    16748  19745  14558    302    548   -566       C  
ATOM   9015  NH1 ARG C1080     -82.276  38.618  91.582  1.00126.19           N  
ANISOU 9015  NH1 ARG C1080    15543  18845  13559    183    700   -525       N  
ATOM   9016  NH2 ARG C1080     -80.267  38.498  90.486  1.00118.88           N  
ANISOU 9016  NH2 ARG C1080    14957  17643  12570    283    374   -400       N  
ATOM   9017  N   ASN C1081     -77.575  45.030  93.307  1.00 85.96           N  
ANISOU 9017  N   ASN C1081    11138  13658   7865    683    528  -1408       N  
ATOM   9018  CA  ASN C1081     -76.542  45.434  94.265  1.00 85.94           C  
ANISOU 9018  CA  ASN C1081    11305  13764   7585    617    536  -1460       C  
ATOM   9019  C   ASN C1081     -76.588  46.967  94.420  1.00 90.51           C  
ANISOU 9019  C   ASN C1081    11893  14251   8246    734    533  -1757       C  
ATOM   9020  O   ASN C1081     -76.580  47.691  93.419  1.00 88.36           O  
ANISOU 9020  O   ASN C1081    11606  13744   8222    852    380  -1800       O  
ATOM   9021  CB  ASN C1081     -75.160  44.968  93.778  1.00 83.34           C  
ANISOU 9021  CB  ASN C1081    11139  13355   7172    568    334  -1236       C  
ATOM   9022  CG  ASN C1081     -74.098  44.902  94.849  1.00101.78           C  
ANISOU 9022  CG  ASN C1081    13628  15850   9193    453    331  -1195       C  
ATOM   9023  OD1 ASN C1081     -73.282  45.815  95.013  1.00 94.67           O  
ANISOU 9023  OD1 ASN C1081    12831  14909   8228    467    242  -1301       O  
ATOM   9024  ND2 ASN C1081     -74.052  43.795  95.574  1.00 93.75           N  
ANISOU 9024  ND2 ASN C1081    12634  15007   7978    323    402  -1019       N  
ATOM   9025  N   ALA C1082     -76.673  47.451  95.675  1.00 90.07           N  
ANISOU 9025  N   ALA C1082    11867  14376   7979    693    698  -1965       N  
ATOM   9026  CA  ALA C1082     -76.743  48.884  95.993  1.00 91.74           C  
ANISOU 9026  CA  ALA C1082    12098  14500   8257    801    712  -2290       C  
ATOM   9027  C   ALA C1082     -75.423  49.647  95.737  1.00 94.16           C  
ANISOU 9027  C   ALA C1082    12603  14646   8529    792    487  -2282       C  
ATOM   9028  O   ALA C1082     -75.460  50.846  95.453  1.00 94.38           O  
ANISOU 9028  O   ALA C1082    12644  14473   8744    905    405  -2486       O  
ATOM   9029  CB  ALA C1082     -77.204  49.080  97.429  1.00 95.72           C  
ANISOU 9029  CB  ALA C1082    12586  15274   8511    743    971  -2530       C  
ATOM   9030  N   LYS C1083     -74.272  48.957  95.852  1.00 88.94           N  
ANISOU 9030  N   LYS C1083    12081  14066   7647    657    382  -2044       N  
ATOM   9031  CA  LYS C1083     -72.948  49.540  95.638  1.00 88.01           C  
ANISOU 9031  CA  LYS C1083    12124  13837   7480    619    173  -2001       C  
ATOM   9032  C   LYS C1083     -72.624  49.702  94.149  1.00 90.35           C  
ANISOU 9032  C   LYS C1083    12404  13878   8046    693    -29  -1852       C  
ATOM   9033  O   LYS C1083     -72.131  50.754  93.733  1.00 90.65           O  
ANISOU 9033  O   LYS C1083    12510  13732   8199    726   -176  -1935       O  
ATOM   9034  CB  LYS C1083     -71.867  48.664  96.293  1.00 90.43           C  
ANISOU 9034  CB  LYS C1083    12546  14339   7472    456    132  -1788       C  
ATOM   9035  CG  LYS C1083     -71.717  48.857  97.794  1.00113.63           C  
ANISOU 9035  CG  LYS C1083    15578  17518  10078    342    249  -1939       C  
ATOM   9036  CD  LYS C1083     -70.390  48.291  98.308  1.00125.78           C  
ANISOU 9036  CD  LYS C1083    17251  19192  11348    189    115  -1723       C  
ATOM   9037  CE  LYS C1083     -69.305  49.339  98.480  1.00135.34           C  
ANISOU 9037  CE  LYS C1083    18591  20329  12501    148    -55  -1836       C  
ATOM   9038  NZ  LYS C1083     -68.709  49.764  97.181  1.00137.79           N  
ANISOU 9038  NZ  LYS C1083    18883  20381  13089    224   -247  -1745       N  
ATOM   9039  N   LEU C1084     -72.884  48.644  93.357  1.00 84.34           N  
ANISOU 9039  N   LEU C1084    11563  13110   7371    700    -42  -1627       N  
ATOM   9040  CA  LEU C1084     -72.573  48.565  91.932  1.00 81.38           C  
ANISOU 9040  CA  LEU C1084    11179  12547   7195    745   -215  -1464       C  
ATOM   9041  C   LEU C1084     -73.527  49.283  90.984  1.00 85.21           C  
ANISOU 9041  C   LEU C1084    11566  12822   7988    874   -268  -1559       C  
ATOM   9042  O   LEU C1084     -73.060  49.771  89.959  1.00 83.56           O  
ANISOU 9042  O   LEU C1084    11401  12440   7907    892   -444  -1483       O  
ATOM   9043  CB  LEU C1084     -72.394  47.098  91.504  1.00 79.49           C  
ANISOU 9043  CB  LEU C1084    10913  12385   6905    694   -217  -1208       C  
ATOM   9044  CG  LEU C1084     -71.212  46.333  92.110  1.00 82.78           C  
ANISOU 9044  CG  LEU C1084    11427  12950   7078    583   -246  -1046       C  
ATOM   9045  CD1 LEU C1084     -71.529  44.856  92.222  1.00 82.11           C  
ANISOU 9045  CD1 LEU C1084    11295  12962   6941    541   -175   -864       C  
ATOM   9046  CD2 LEU C1084     -69.946  46.541  91.299  1.00 83.02           C  
ANISOU 9046  CD2 LEU C1084    11525  12890   7131    571   -426   -931       C  
ATOM   9047  N   LYS C1085     -74.848  49.317  91.282  1.00 83.91           N  
ANISOU 9047  N   LYS C1085    11257  12680   7943    954   -124  -1706       N  
ATOM   9048  CA  LYS C1085     -75.859  49.962  90.415  1.00 84.53           C  
ANISOU 9048  CA  LYS C1085    11211  12559   8346   1091   -189  -1790       C  
ATOM   9049  C   LYS C1085     -75.587  51.445  90.058  1.00 89.37           C  
ANISOU 9049  C   LYS C1085    11894  12932   9132   1169   -351  -1926       C  
ATOM   9050  O   LYS C1085     -75.647  51.753  88.862  1.00 88.05           O  
ANISOU 9050  O   LYS C1085    11719  12570   9164   1211   -534  -1816       O  
ATOM   9051  CB  LYS C1085     -77.300  49.756  90.928  1.00 88.83           C  
ANISOU 9051  CB  LYS C1085    11554  13199   8997   1165      9  -1941       C  
ATOM   9052  CG  LYS C1085     -78.379  50.007  89.874  1.00101.13           C  
ANISOU 9052  CG  LYS C1085    12944  14578  10901   1292    -83  -1944       C  
ATOM   9053  CD  LYS C1085     -79.731  50.333  90.513  1.00112.23           C  
ANISOU 9053  CD  LYS C1085    14131  16045  12468   1405    104  -2186       C  
ATOM   9054  CE  LYS C1085     -80.839  50.541  89.502  1.00119.42           C  
ANISOU 9054  CE  LYS C1085    14845  16788  13742   1533     -5  -2177       C  
ATOM   9055  NZ  LYS C1085     -80.797  51.894  88.882  1.00124.29           N  
ANISOU 9055  NZ  LYS C1085    15494  17111  14621   1672   -215  -2277       N  
ATOM   9056  N   PRO C1086     -75.284  52.371  91.017  1.00 87.61           N  
ANISOU 9056  N   PRO C1086    11749  12704   8834   1177   -306  -2154       N  
ATOM   9057  CA  PRO C1086     -75.034  53.771  90.627  1.00 88.65           C  
ANISOU 9057  CA  PRO C1086    11956  12561   9165   1242   -487  -2271       C  
ATOM   9058  C   PRO C1086     -73.800  53.936  89.746  1.00 91.62           C  
ANISOU 9058  C   PRO C1086    12481  12828   9503   1134   -713  -2042       C  
ATOM   9059  O   PRO C1086     -73.784  54.800  88.868  1.00 91.57           O  
ANISOU 9059  O   PRO C1086    12505  12570   9719   1174   -907  -2010       O  
ATOM   9060  CB  PRO C1086     -74.874  54.491  91.966  1.00 92.83           C  
ANISOU 9060  CB  PRO C1086    12556  13153   9563   1241   -371  -2567       C  
ATOM   9061  CG  PRO C1086     -74.444  53.442  92.916  1.00 96.61           C  
ANISOU 9061  CG  PRO C1086    13072  13955   9681   1107   -200  -2502       C  
ATOM   9062  CD  PRO C1086     -75.156  52.204  92.479  1.00 90.75           C  
ANISOU 9062  CD  PRO C1086    12184  13337   8961   1113   -106  -2315       C  
ATOM   9063  N   VAL C1087     -72.785  53.083  89.977  1.00 87.28           N  
ANISOU 9063  N   VAL C1087    12011  12472   8677    994   -687  -1873       N  
ATOM   9064  CA  VAL C1087     -71.532  53.031  89.226  1.00 85.66           C  
ANISOU 9064  CA  VAL C1087    11914  12235   8398    880   -855  -1651       C  
ATOM   9065  C   VAL C1087     -71.839  52.556  87.804  1.00 89.02           C  
ANISOU 9065  C   VAL C1087    12277  12578   8967    905   -951  -1445       C  
ATOM   9066  O   VAL C1087     -71.459  53.234  86.849  1.00 88.70           O  
ANISOU 9066  O   VAL C1087    12292  12369   9041    878  -1131  -1351       O  
ATOM   9067  CB  VAL C1087     -70.485  52.116  89.918  1.00 88.36           C  
ANISOU 9067  CB  VAL C1087    12314  12824   8434    753   -787  -1539       C  
ATOM   9068  CG1 VAL C1087     -69.137  52.176  89.200  1.00 86.68           C  
ANISOU 9068  CG1 VAL C1087    12180  12590   8163    643   -949  -1343       C  
ATOM   9069  CG2 VAL C1087     -70.329  52.466  91.399  1.00 90.14           C  
ANISOU 9069  CG2 VAL C1087    12601  13172   8477    714   -685  -1744       C  
ATOM   9070  N   TYR C1088     -72.553  51.411  87.674  1.00 85.23           N  
ANISOU 9070  N   TYR C1088    11690  12218   8474    941   -836  -1376       N  
ATOM   9071  CA  TYR C1088     -72.941  50.799  86.402  1.00 84.03           C  
ANISOU 9071  CA  TYR C1088    11481  12016   8431    957   -913  -1204       C  
ATOM   9072  C   TYR C1088     -73.704  51.765  85.497  1.00 89.06           C  
ANISOU 9072  C   TYR C1088    12079  12415   9343   1041  -1068  -1233       C  
ATOM   9073  O   TYR C1088     -73.310  51.947  84.345  1.00 87.87           O  
ANISOU 9073  O   TYR C1088    11984  12169   9233    992  -1234  -1073       O  
ATOM   9074  CB  TYR C1088     -73.755  49.520  86.641  1.00 85.01           C  
ANISOU 9074  CB  TYR C1088    11491  12286   8524    979   -760  -1175       C  
ATOM   9075  CG  TYR C1088     -73.989  48.702  85.390  1.00 86.21           C  
ANISOU 9075  CG  TYR C1088    11606  12409   8739    969   -840  -1001       C  
ATOM   9076  CD1 TYR C1088     -72.994  47.872  84.879  1.00 86.74           C  
ANISOU 9076  CD1 TYR C1088    11750  12554   8654    887   -873   -835       C  
ATOM   9077  CD2 TYR C1088     -75.213  48.742  84.726  1.00 87.98           C  
ANISOU 9077  CD2 TYR C1088    11714  12534   9181   1044   -886  -1017       C  
ATOM   9078  CE1 TYR C1088     -73.203  47.117  83.724  1.00 87.12           C  
ANISOU 9078  CE1 TYR C1088    11779  12578   8744    875   -940   -711       C  
ATOM   9079  CE2 TYR C1088     -75.440  47.978  83.579  1.00 88.08           C  
ANISOU 9079  CE2 TYR C1088    11707  12527   9230   1018   -972   -871       C  
ATOM   9080  CZ  TYR C1088     -74.430  47.167  83.081  1.00 93.33           C  
ANISOU 9080  CZ  TYR C1088    12471  13270   9721    931   -993   -729       C  
ATOM   9081  OH  TYR C1088     -74.638  46.419  81.949  1.00 91.28           O  
ANISOU 9081  OH  TYR C1088    12207  12994   9481    904  -1072   -619       O  
ATOM   9082  N   ASP C1089     -74.766  52.407  86.030  1.00 87.57           N  
ANISOU 9082  N   ASP C1089    11793  12137   9342   1164  -1018  -1436       N  
ATOM   9083  CA  ASP C1089     -75.593  53.363  85.292  1.00 88.78           C  
ANISOU 9083  CA  ASP C1089    11886  12041   9804   1273  -1180  -1477       C  
ATOM   9084  C   ASP C1089     -74.815  54.577  84.775  1.00 92.63           C  
ANISOU 9084  C   ASP C1089    12521  12310  10366   1228  -1400  -1430       C  
ATOM   9085  O   ASP C1089     -75.061  55.017  83.652  1.00 92.77           O  
ANISOU 9085  O   ASP C1089    12544  12148  10554   1236  -1604  -1298       O  
ATOM   9086  CB  ASP C1089     -76.824  53.786  86.112  1.00 93.07           C  
ANISOU 9086  CB  ASP C1089    12270  12550  10543   1432  -1054  -1739       C  
ATOM   9087  CG  ASP C1089     -77.928  52.740  86.168  1.00102.64           C  
ANISOU 9087  CG  ASP C1089    13288  13916  11796   1479   -904  -1735       C  
ATOM   9088  OD1 ASP C1089     -78.418  52.327  85.088  1.00101.50           O  
ANISOU 9088  OD1 ASP C1089    13076  13715  11774   1483  -1027  -1573       O  
ATOM   9089  OD2 ASP C1089     -78.341  52.375  87.288  1.00110.52           O  
ANISOU 9089  OD2 ASP C1089    14198  15091  12702   1499   -671  -1895       O  
ATOM   9090  N   SER C1090     -73.856  55.084  85.570  1.00 89.11           N  
ANISOU 9090  N   SER C1090    12197  11882   9778   1157  -1374  -1517       N  
ATOM   9091  CA  SER C1090     -73.018  56.228  85.193  1.00 89.70           C  
ANISOU 9091  CA  SER C1090    12417  11754   9910   1079  -1579  -1470       C  
ATOM   9092  C   SER C1090     -72.017  55.881  84.084  1.00 91.92           C  
ANISOU 9092  C   SER C1090    12786  12087  10052    916  -1704  -1176       C  
ATOM   9093  O   SER C1090     -71.708  56.740  83.254  1.00 92.52           O  
ANISOU 9093  O   SER C1090    12943  11969  10240    852  -1915  -1056       O  
ATOM   9094  CB  SER C1090     -72.280  56.782  86.408  1.00 93.88           C  
ANISOU 9094  CB  SER C1090    13045  12313  10312   1030  -1514  -1656       C  
ATOM   9095  OG  SER C1090     -71.244  55.912  86.836  1.00 99.48           O  
ANISOU 9095  OG  SER C1090    13804  13287  10708    895  -1410  -1558       O  
ATOM   9096  N   LEU C1091     -71.506  54.630  84.085  1.00 86.06           N  
ANISOU 9096  N   LEU C1091    12025  11604   9068    846  -1573  -1065       N  
ATOM   9097  CA  LEU C1091     -70.523  54.135  83.112  1.00 84.09           C  
ANISOU 9097  CA  LEU C1091    11833  11454   8663    706  -1640   -826       C  
ATOM   9098  C   LEU C1091     -71.061  54.037  81.681  1.00 88.14           C  
ANISOU 9098  C   LEU C1091    12327  11882   9281    705  -1774   -660       C  
ATOM   9099  O   LEU C1091     -72.250  53.798  81.477  1.00 88.28           O  
ANISOU 9099  O   LEU C1091    12250  11842   9449    820  -1771   -705       O  
ATOM   9100  CB  LEU C1091     -69.930  52.778  83.554  1.00 82.11           C  
ANISOU 9100  CB  LEU C1091    11550  11477   8169    669  -1464   -782       C  
ATOM   9101  CG  LEU C1091     -68.994  52.774  84.777  1.00 86.33           C  
ANISOU 9101  CG  LEU C1091    12129  12142   8530    609  -1376   -863       C  
ATOM   9102  CD1 LEU C1091     -68.806  51.369  85.308  1.00 84.86           C  
ANISOU 9102  CD1 LEU C1091    11889  12187   8166    616  -1214   -828       C  
ATOM   9103  CD2 LEU C1091     -67.641  53.407  84.464  1.00 88.52           C  
ANISOU 9103  CD2 LEU C1091    12494  12413   8727    460  -1497   -755       C  
ATOM   9104  N   ASP C1092     -70.173  54.235  80.695  1.00 84.58           N  
ANISOU 9104  N   ASP C1092    11960  11440   8735    561  -1895   -467       N  
ATOM   9105  CA  ASP C1092     -70.482  54.139  79.266  1.00 84.48           C  
ANISOU 9105  CA  ASP C1092    11961  11388   8749    513  -2031   -286       C  
ATOM   9106  C   ASP C1092     -70.508  52.660  78.841  1.00 86.79           C  
ANISOU 9106  C   ASP C1092    12198  11902   8878    516  -1899   -235       C  
ATOM   9107  O   ASP C1092     -70.036  51.811  79.600  1.00 85.80           O  
ANISOU 9107  O   ASP C1092    12038  11945   8617    532  -1725   -301       O  
ATOM   9108  CB  ASP C1092     -69.451  54.927  78.446  1.00 87.08           C  
ANISOU 9108  CB  ASP C1092    12407  11677   9002    329  -2186   -102       C  
ATOM   9109  CG  ASP C1092     -68.016  54.560  78.760  1.00 96.69           C  
ANISOU 9109  CG  ASP C1092    13648  13105   9985    203  -2072    -65       C  
ATOM   9110  OD1 ASP C1092     -67.414  55.220  79.637  1.00 98.10           O  
ANISOU 9110  OD1 ASP C1092    13861  13238  10175    167  -2073   -142       O  
ATOM   9111  OD2 ASP C1092     -67.505  53.594  78.150  1.00101.02           O  
ANISOU 9111  OD2 ASP C1092    14172  13862  10349    148  -1984     26       O  
ATOM   9112  N   ALA C1093     -71.056  52.356  77.643  1.00 82.96           N  
ANISOU 9112  N   ALA C1093    11710  11403   8407    497  -1999   -120       N  
ATOM   9113  CA  ALA C1093     -71.181  50.996  77.099  1.00 81.56           C  
ANISOU 9113  CA  ALA C1093    11495  11396   8097    496  -1905    -88       C  
ATOM   9114  C   ALA C1093     -69.915  50.125  77.212  1.00 83.75           C  
ANISOU 9114  C   ALA C1093    11793  11894   8136    426  -1751    -67       C  
ATOM   9115  O   ALA C1093     -69.992  49.015  77.739  1.00 82.21           O  
ANISOU 9115  O   ALA C1093    11538  11805   7892    493  -1602   -141       O  
ATOM   9116  CB  ALA C1093     -71.657  51.051  75.658  1.00 83.24           C  
ANISOU 9116  CB  ALA C1093    11747  11568   8312    431  -2076     51       C  
ATOM   9117  N   VAL C1094     -68.759  50.642  76.741  1.00 80.47           N  
ANISOU 9117  N   VAL C1094    11448  11537   7589    290  -1795     39       N  
ATOM   9118  CA  VAL C1094     -67.450  49.964  76.747  1.00 79.24           C  
ANISOU 9118  CA  VAL C1094    11285  11592   7230    222  -1665     65       C  
ATOM   9119  C   VAL C1094     -66.963  49.681  78.183  1.00 81.51           C  
ANISOU 9119  C   VAL C1094    11522  11937   7512    287  -1536    -41       C  
ATOM   9120  O   VAL C1094     -66.499  48.570  78.461  1.00 80.30           O  
ANISOU 9120  O   VAL C1094    11318  11931   7263    327  -1405    -68       O  
ATOM   9121  CB  VAL C1094     -66.385  50.731  75.906  1.00 84.16           C  
ANISOU 9121  CB  VAL C1094    11972  12276   7731     40  -1745    212       C  
ATOM   9122  CG1 VAL C1094     -65.117  49.900  75.716  1.00 83.55           C  
ANISOU 9122  CG1 VAL C1094    11846  12444   7456    -15  -1598    228       C  
ATOM   9123  CG2 VAL C1094     -66.948  51.158  74.551  1.00 85.10           C  
ANISOU 9123  CG2 VAL C1094    12163  12329   7841    -48  -1904    340       C  
ATOM   9124  N   ARG C1095     -67.086  50.681  79.088  1.00 77.65           N  
ANISOU 9124  N   ARG C1095    11053  11323   7127    297  -1585   -105       N  
ATOM   9125  CA  ARG C1095     -66.694  50.557  80.499  1.00 76.42           C  
ANISOU 9125  CA  ARG C1095    10870  11223   6943    338  -1485   -211       C  
ATOM   9126  C   ARG C1095     -67.625  49.655  81.308  1.00 78.85           C  
ANISOU 9126  C   ARG C1095    11116  11554   7291    472  -1362   -323       C  
ATOM   9127  O   ARG C1095     -67.185  49.067  82.296  1.00 78.02           O  
ANISOU 9127  O   ARG C1095    10984  11563   7095    490  -1257   -365       O  
ATOM   9128  CB  ARG C1095     -66.515  51.928  81.160  1.00 76.33           C  
ANISOU 9128  CB  ARG C1095    10916  11073   7011    292  -1579   -269       C  
ATOM   9129  CG  ARG C1095     -65.178  52.549  80.823  1.00 84.79           C  
ANISOU 9129  CG  ARG C1095    12029  12196   7990    126  -1654   -156       C  
ATOM   9130  CD  ARG C1095     -64.921  53.815  81.594  1.00 91.50           C  
ANISOU 9130  CD  ARG C1095    12945  12902   8918     67  -1753   -229       C  
ATOM   9131  NE  ARG C1095     -63.654  54.413  81.181  1.00 96.17           N  
ANISOU 9131  NE  ARG C1095    13565  13543   9432   -122  -1837    -96       N  
ATOM   9132  CZ  ARG C1095     -63.542  55.535  80.482  1.00110.05           C  
ANISOU 9132  CZ  ARG C1095    15401  15138  11275   -248  -2005      6       C  
ATOM   9133  NH1 ARG C1095     -64.626  56.212  80.122  1.00 98.18           N  
ANISOU 9133  NH1 ARG C1095    13958  13390   9957   -184  -2125    -13       N  
ATOM   9134  NH2 ARG C1095     -62.348  55.997  80.147  1.00 98.68           N  
ANISOU 9134  NH2 ARG C1095    13969  13774   9750   -445  -2064    139       N  
ATOM   9135  N   ARG C1096     -68.899  49.525  80.885  1.00 75.21           N  
ANISOU 9135  N   ARG C1096    10625  10992   6961    550  -1386   -352       N  
ATOM   9136  CA  ARG C1096     -69.855  48.633  81.541  1.00 74.46           C  
ANISOU 9136  CA  ARG C1096    10453  10928   6911    651  -1268   -437       C  
ATOM   9137  C   ARG C1096     -69.394  47.189  81.316  1.00 78.16           C  
ANISOU 9137  C   ARG C1096    10900  11544   7254    644  -1177   -370       C  
ATOM   9138  O   ARG C1096     -69.346  46.408  82.272  1.00 77.59           O  
ANISOU 9138  O   ARG C1096    10795  11558   7128    675  -1062   -403       O  
ATOM   9139  CB  ARG C1096     -71.291  48.870  81.036  1.00 73.39           C  
ANISOU 9139  CB  ARG C1096    10263  10654   6967    724  -1335   -472       C  
ATOM   9140  CG  ARG C1096     -71.965  50.048  81.732  1.00 79.68           C  
ANISOU 9140  CG  ARG C1096    11037  11306   7931    792  -1369   -603       C  
ATOM   9141  CD  ARG C1096     -73.460  50.082  81.498  1.00 83.87           C  
ANISOU 9141  CD  ARG C1096    11459  11733   8676    894  -1398   -662       C  
ATOM   9142  NE  ARG C1096     -73.819  50.805  80.279  1.00 87.83           N  
ANISOU 9142  NE  ARG C1096    11985  12072   9316    884  -1610   -568       N  
ATOM   9143  CZ  ARG C1096     -74.508  51.941  80.254  1.00 95.59           C  
ANISOU 9143  CZ  ARG C1096    12938  12854  10527    958  -1736   -628       C  
ATOM   9144  NH1 ARG C1096     -74.926  52.499  81.386  1.00 71.58           N  
ANISOU 9144  NH1 ARG C1096     9838   9758   7603   1060  -1648   -821       N  
ATOM   9145  NH2 ARG C1096     -74.788  52.525  79.100  1.00 88.17           N  
ANISOU 9145  NH2 ARG C1096    12031  11768   9703    933  -1957   -501       N  
ATOM   9146  N   ALA C1097     -68.946  46.886  80.073  1.00 74.64           N  
ANISOU 9146  N   ALA C1097    10482  11127   6749    593  -1233   -277       N  
ATOM   9147  CA  ALA C1097     -68.393  45.594  79.659  1.00 73.72           C  
ANISOU 9147  CA  ALA C1097    10353  11127   6530    594  -1161   -237       C  
ATOM   9148  C   ALA C1097     -67.098  45.267  80.426  1.00 77.46           C  
ANISOU 9148  C   ALA C1097    10813  11727   6890    580  -1085   -220       C  
ATOM   9149  O   ALA C1097     -66.827  44.088  80.672  1.00 76.71           O  
ANISOU 9149  O   ALA C1097    10686  11700   6761    626  -1008   -215       O  
ATOM   9150  CB  ALA C1097     -68.134  45.592  78.158  1.00 74.61           C  
ANISOU 9150  CB  ALA C1097    10506  11260   6582    530  -1234   -170       C  
ATOM   9151  N   ALA C1098     -66.309  46.305  80.809  1.00 74.63           N  
ANISOU 9151  N   ALA C1098    10478  11387   6492    514  -1127   -206       N  
ATOM   9152  CA  ALA C1098     -65.078  46.142  81.596  1.00 74.88           C  
ANISOU 9152  CA  ALA C1098    10484  11542   6426    487  -1086   -185       C  
ATOM   9153  C   ALA C1098     -65.412  45.714  83.036  1.00 79.11           C  
ANISOU 9153  C   ALA C1098    11006  12095   6958    542  -1020   -239       C  
ATOM   9154  O   ALA C1098     -64.690  44.904  83.616  1.00 78.29           O  
ANISOU 9154  O   ALA C1098    10867  12095   6785    557   -976   -201       O  
ATOM   9155  CB  ALA C1098     -64.276  47.434  81.604  1.00 76.41           C  
ANISOU 9155  CB  ALA C1098    10708  11733   6590    377  -1170   -158       C  
ATOM   9156  N   LEU C1099     -66.528  46.236  83.589  1.00 76.67           N  
ANISOU 9156  N   LEU C1099    10716  11690   6723    571  -1014   -326       N  
ATOM   9157  CA  LEU C1099     -67.015  45.907  84.928  1.00 77.15           C  
ANISOU 9157  CA  LEU C1099    10767  11791   6755    603   -930   -390       C  
ATOM   9158  C   LEU C1099     -67.607  44.502  84.962  1.00 81.28           C  
ANISOU 9158  C   LEU C1099    11248  12342   7294    656   -850   -349       C  
ATOM   9159  O   LEU C1099     -67.357  43.770  85.918  1.00 81.39           O  
ANISOU 9159  O   LEU C1099    11256  12444   7226    652   -793   -314       O  
ATOM   9160  CB  LEU C1099     -68.039  46.953  85.401  1.00 78.03           C  
ANISOU 9160  CB  LEU C1099    10893  11802   6955    625   -929   -524       C  
ATOM   9161  CG  LEU C1099     -68.347  46.985  86.897  1.00 83.32           C  
ANISOU 9161  CG  LEU C1099    11565  12546   7545    627   -833   -625       C  
ATOM   9162  CD1 LEU C1099     -67.207  47.611  87.682  1.00 83.94           C  
ANISOU 9162  CD1 LEU C1099    11707  12697   7491    548   -878   -644       C  
ATOM   9163  CD2 LEU C1099     -69.611  47.763  87.158  1.00 86.94           C  
ANISOU 9163  CD2 LEU C1099    11997  12905   8131    686   -796   -784       C  
ATOM   9164  N   ILE C1100     -68.372  44.123  83.916  1.00 77.83           N  
ANISOU 9164  N   ILE C1100    10788  11824   6958    691   -865   -340       N  
ATOM   9165  CA  ILE C1100     -68.978  42.793  83.758  1.00 77.89           C  
ANISOU 9165  CA  ILE C1100    10762  11825   7007    726   -814   -304       C  
ATOM   9166  C   ILE C1100     -67.862  41.738  83.685  1.00 81.83           C  
ANISOU 9166  C   ILE C1100    11265  12391   7434    734   -807   -220       C  
ATOM   9167  O   ILE C1100     -68.015  40.645  84.236  1.00 81.87           O  
ANISOU 9167  O   ILE C1100    11258  12407   7443    751   -762   -173       O  
ATOM   9168  CB  ILE C1100     -69.945  42.769  82.531  1.00 81.17           C  
ANISOU 9168  CB  ILE C1100    11161  12137   7542    744   -867   -322       C  
ATOM   9169  CG1 ILE C1100     -71.227  43.580  82.838  1.00 82.52           C  
ANISOU 9169  CG1 ILE C1100    11285  12236   7832    764   -866   -404       C  
ATOM   9170  CG2 ILE C1100     -70.305  41.333  82.090  1.00 81.80           C  
ANISOU 9170  CG2 ILE C1100    11224  12197   7659    761   -844   -284       C  
ATOM   9171  CD1 ILE C1100     -71.840  44.269  81.669  1.00 89.81           C  
ANISOU 9171  CD1 ILE C1100    12205  13052   8867    771   -983   -414       C  
ATOM   9172  N   ASN C1101     -66.725  42.101  83.053  1.00 78.17           N  
ANISOU 9172  N   ASN C1101    10812  11973   6917    718   -854   -196       N  
ATOM   9173  CA  ASN C1101     -65.549  41.247  82.923  1.00 78.17           C  
ANISOU 9173  CA  ASN C1101    10783  12045   6872    745   -847   -139       C  
ATOM   9174  C   ASN C1101     -65.013  40.891  84.312  1.00 83.15           C  
ANISOU 9174  C   ASN C1101    11401  12747   7446    744   -833    -83       C  
ATOM   9175  O   ASN C1101     -64.743  39.717  84.566  1.00 82.94           O  
ANISOU 9175  O   ASN C1101    11352  12718   7442    793   -823    -22       O  
ATOM   9176  CB  ASN C1101     -64.475  41.934  82.070  1.00 78.17           C  
ANISOU 9176  CB  ASN C1101    10769  12113   6817    705   -883   -132       C  
ATOM   9177  CG  ASN C1101     -63.433  41.005  81.495  1.00103.73           C  
ANISOU 9177  CG  ASN C1101    13948  15424  10043    755   -856   -110       C  
ATOM   9178  OD1 ASN C1101     -62.773  40.233  82.197  1.00 98.29           O  
ANISOU 9178  OD1 ASN C1101    13209  14774   9362    808   -846    -69       O  
ATOM   9179  ND2 ASN C1101     -63.226  41.100  80.198  1.00 98.44           N  
ANISOU 9179  ND2 ASN C1101    13276  14778   9348    738   -850   -140       N  
ATOM   9180  N   MET C1102     -64.917  41.897  85.218  1.00 80.82           N  
ANISOU 9180  N   MET C1102    11129  12500   7079    685   -846   -104       N  
ATOM   9181  CA  MET C1102     -64.460  41.741  86.606  1.00 81.64           C  
ANISOU 9181  CA  MET C1102    11239  12694   7085    654   -848    -57       C  
ATOM   9182  C   MET C1102     -65.412  40.839  87.403  1.00 86.80           C  
ANISOU 9182  C   MET C1102    11909  13332   7738    663   -787    -25       C  
ATOM   9183  O   MET C1102     -64.950  40.058  88.238  1.00 87.52           O  
ANISOU 9183  O   MET C1102    12001  13483   7769    654   -803     77       O  
ATOM   9184  CB  MET C1102     -64.337  43.105  87.298  1.00 84.39           C  
ANISOU 9184  CB  MET C1102    11630  13083   7351    578   -873   -132       C  
ATOM   9185  CG  MET C1102     -63.071  43.850  86.954  1.00 88.33           C  
ANISOU 9185  CG  MET C1102    12109  13635   7819    527   -954   -113       C  
ATOM   9186  SD  MET C1102     -63.016  45.512  87.684  1.00 93.48           S  
ANISOU 9186  SD  MET C1102    12832  14282   8405    425  -1008   -222       S  
ATOM   9187  CE  MET C1102     -62.328  45.156  89.282  1.00 91.07           C  
ANISOU 9187  CE  MET C1102    12541  14129   7933    370  -1033   -181       C  
ATOM   9188  N   VAL C1103     -66.733  40.938  87.128  1.00 83.11           N  
ANISOU 9188  N   VAL C1103    11446  12787   7344    671   -727    -95       N  
ATOM   9189  CA  VAL C1103     -67.783  40.136  87.766  1.00 83.64           C  
ANISOU 9189  CA  VAL C1103    11507  12847   7424    656   -653    -65       C  
ATOM   9190  C   VAL C1103     -67.621  38.645  87.415  1.00 88.78           C  
ANISOU 9190  C   VAL C1103    12148  13436   8148    691   -677     52       C  
ATOM   9191  O   VAL C1103     -67.725  37.802  88.305  1.00 89.55           O  
ANISOU 9191  O   VAL C1103    12259  13562   8205    654   -662    157       O  
ATOM   9192  CB  VAL C1103     -69.205  40.702  87.482  1.00 87.38           C  
ANISOU 9192  CB  VAL C1103    11951  13261   7989    660   -591   -178       C  
ATOM   9193  CG1 VAL C1103     -70.308  39.761  87.971  1.00 87.91           C  
ANISOU 9193  CG1 VAL C1103    11981  13329   8091    629   -508   -135       C  
ATOM   9194  CG2 VAL C1103     -69.372  42.079  88.115  1.00 87.73           C  
ANISOU 9194  CG2 VAL C1103    12009  13352   7974    639   -564   -306       C  
ATOM   9195  N   PHE C1104     -67.309  38.322  86.146  1.00 85.12           N  
ANISOU 9195  N   PHE C1104    11669  12887   7784    754   -721     33       N  
ATOM   9196  CA  PHE C1104     -67.093  36.929  85.747  1.00 85.59           C  
ANISOU 9196  CA  PHE C1104    11725  12861   7933    804   -750    105       C  
ATOM   9197  C   PHE C1104     -65.861  36.304  86.414  1.00 90.19           C  
ANISOU 9197  C   PHE C1104    12300  13488   8479    834   -804    217       C  
ATOM   9198  O   PHE C1104     -65.873  35.109  86.716  1.00 91.31           O  
ANISOU 9198  O   PHE C1104    12452  13553   8689    855   -834    316       O  
ATOM   9199  CB  PHE C1104     -67.025  36.778  84.217  1.00 87.02           C  
ANISOU 9199  CB  PHE C1104    11899  12963   8203    863   -773     22       C  
ATOM   9200  CG  PHE C1104     -68.363  36.799  83.510  1.00 88.46           C  
ANISOU 9200  CG  PHE C1104    12087  13058   8466    838   -760    -45       C  
ATOM   9201  CD1 PHE C1104     -68.565  37.602  82.393  1.00 90.40           C  
ANISOU 9201  CD1 PHE C1104    12337  13297   8715    837   -785   -133       C  
ATOM   9202  CD2 PHE C1104     -69.421  36.013  83.958  1.00 91.38           C  
ANISOU 9202  CD2 PHE C1104    12453  13359   8910    800   -737     -2       C  
ATOM   9203  CE1 PHE C1104     -69.797  37.617  81.734  1.00 91.08           C  
ANISOU 9203  CE1 PHE C1104    12419  13304   8884    812   -803   -181       C  
ATOM   9204  CE2 PHE C1104     -70.660  36.040  83.306  1.00 94.11           C  
ANISOU 9204  CE2 PHE C1104    12778  13632   9345    770   -739    -60       C  
ATOM   9205  CZ  PHE C1104     -70.837  36.839  82.195  1.00 91.19           C  
ANISOU 9205  CZ  PHE C1104    12409  13254   8986    784   -781   -151       C  
ATOM   9206  N   GLN C1105     -64.825  37.121  86.674  1.00 85.84           N  
ANISOU 9206  N   GLN C1105    11729  13051   7835    829   -834    212       N  
ATOM   9207  CA  GLN C1105     -63.568  36.689  87.280  1.00 86.46           C  
ANISOU 9207  CA  GLN C1105    11772  13192   7886    858   -908    318       C  
ATOM   9208  C   GLN C1105     -63.648  36.520  88.800  1.00 92.22           C  
ANISOU 9208  C   GLN C1105    12545  13997   8499    778   -936    441       C  
ATOM   9209  O   GLN C1105     -63.157  35.521  89.330  1.00 93.07           O  
ANISOU 9209  O   GLN C1105    12645  14079   8638    803  -1011    583       O  
ATOM   9210  CB  GLN C1105     -62.442  37.666  86.912  1.00 87.29           C  
ANISOU 9210  CB  GLN C1105    11822  13405   7940    859   -937    268       C  
ATOM   9211  CG  GLN C1105     -61.038  37.098  87.121  1.00102.41           C  
ANISOU 9211  CG  GLN C1105    13647  15374   9888    923  -1019    357       C  
ATOM   9212  CD  GLN C1105     -59.932  38.088  86.835  1.00120.51           C  
ANISOU 9212  CD  GLN C1105    15863  17797  12129    894  -1044    321       C  
ATOM   9213  OE1 GLN C1105     -60.126  39.140  86.210  1.00116.92           O  
ANISOU 9213  OE1 GLN C1105    15426  17367  11631    834  -1003    228       O  
ATOM   9214  NE2 GLN C1105     -58.728  37.766  87.283  1.00110.98           N  
ANISOU 9214  NE2 GLN C1105    14558  16671  10940    928  -1128    409       N  
ATOM   9215  N   MET C1106     -64.240  37.508  89.495  1.00 88.90           N  
ANISOU 9215  N   MET C1106    12170  13667   7940    680   -882    383       N  
ATOM   9216  CA  MET C1106     -64.335  37.546  90.956  1.00 89.76           C  
ANISOU 9216  CA  MET C1106    12332  13893   7878    578   -888    466       C  
ATOM   9217  C   MET C1106     -65.754  37.351  91.493  1.00 92.62           C  
ANISOU 9217  C   MET C1106    12737  14257   8197    503   -776    456       C  
ATOM   9218  O   MET C1106     -65.942  36.631  92.471  1.00 94.08           O  
ANISOU 9218  O   MET C1106    12961  14494   8290    426   -782    597       O  
ATOM   9219  CB  MET C1106     -63.764  38.874  91.493  1.00 92.46           C  
ANISOU 9219  CB  MET C1106    12693  14369   8068    513   -909    379       C  
ATOM   9220  CG  MET C1106     -62.425  39.278  90.877  1.00 96.14           C  
ANISOU 9220  CG  MET C1106    13094  14853   8583    560  -1005    374       C  
ATOM   9221  SD  MET C1106     -61.708  40.793  91.570  1.00101.26           S  
ANISOU 9221  SD  MET C1106    13771  15639   9065    451  -1061    288       S  
ATOM   9222  CE  MET C1106     -62.919  41.968  91.097  1.00 96.94           C  
ANISOU 9222  CE  MET C1106    13276  15014   8543    436   -948     82       C  
ATOM   9223  N   GLY C1107     -66.721  38.024  90.878  1.00 86.66           N  
ANISOU 9223  N   GLY C1107    11964  13458   7505    516   -682    300       N  
ATOM   9224  CA  GLY C1107     -68.114  38.016  91.306  1.00 86.45           C  
ANISOU 9224  CA  GLY C1107    11935  13452   7460    454   -558    255       C  
ATOM   9225  C   GLY C1107     -68.497  39.392  91.802  1.00 89.39           C  
ANISOU 9225  C   GLY C1107    12315  13924   7726    420   -479     80       C  
ATOM   9226  O   GLY C1107     -67.622  40.146  92.235  1.00 88.39           O  
ANISOU 9226  O   GLY C1107    12229  13874   7481    400   -533     41       O  
ATOM   9227  N   GLU C1108     -69.801  39.733  91.734  1.00 86.54           N  
ANISOU 9227  N   GLU C1108    11905  13551   7424    416   -360    -37       N  
ATOM   9228  CA  GLU C1108     -70.352  41.029  92.176  1.00 87.10           C  
ANISOU 9228  CA  GLU C1108    11967  13687   7442    411   -272   -241       C  
ATOM   9229  C   GLU C1108     -69.870  41.441  93.567  1.00 91.85           C  
ANISOU 9229  C   GLU C1108    12642  14469   7786    318   -240   -268       C  
ATOM   9230  O   GLU C1108     -69.467  42.587  93.753  1.00 91.36           O  
ANISOU 9230  O   GLU C1108    12619  14423   7671    328   -264   -417       O  
ATOM   9231  CB  GLU C1108     -71.893  41.076  92.065  1.00 89.26           C  
ANISOU 9231  CB  GLU C1108    12141  13945   7830    422   -137   -341       C  
ATOM   9232  CG  GLU C1108     -72.632  39.898  92.689  1.00103.73           C  
ANISOU 9232  CG  GLU C1108    13938  15862   9614    327    -38   -208       C  
ATOM   9233  CD  GLU C1108     -74.071  39.709  92.244  1.00128.79           C  
ANISOU 9233  CD  GLU C1108    16979  18992  12965    339     61   -265       C  
ATOM   9234  OE1 GLU C1108     -74.964  39.677  93.122  1.00125.63           O  
ANISOU 9234  OE1 GLU C1108    16511  18738  12483    261    224   -308       O  
ATOM   9235  OE2 GLU C1108     -74.303  39.544  91.024  1.00122.24           O  
ANISOU 9235  OE2 GLU C1108    16107  17996  12344    414    -25   -261       O  
ATOM   9236  N   THR C1109     -69.850  40.477  94.510  1.00 89.55           N  
ANISOU 9236  N   THR C1109    12385  14305   7334    214   -209   -108       N  
ATOM   9237  CA  THR C1109     -69.387  40.627  95.895  1.00 91.14           C  
ANISOU 9237  CA  THR C1109    12673  14709   7245     93   -194    -86       C  
ATOM   9238  C   THR C1109     -67.917  41.085  95.970  1.00 93.84           C  
ANISOU 9238  C   THR C1109    13085  15059   7510     97   -366    -58       C  
ATOM   9239  O   THR C1109     -67.580  41.935  96.797  1.00 95.00           O  
ANISOU 9239  O   THR C1109    13300  15331   7465     31   -364   -177       O  
ATOM   9240  CB  THR C1109     -69.702  39.357  96.720  1.00101.36           C  
ANISOU 9240  CB  THR C1109    13991  16117   8406    -33   -154    138       C  
ATOM   9241  OG1 THR C1109     -69.106  39.471  98.009  1.00103.49           O  
ANISOU 9241  OG1 THR C1109    14363  16592   8368   -164   -178    190       O  
ATOM   9242  CG2 THR C1109     -69.225  38.061  96.044  1.00 99.68           C  
ANISOU 9242  CG2 THR C1109    13769  15748   8358      6   -292    385       C  
ATOM   9243  N   GLY C1110     -67.078  40.522  95.098  1.00 87.69           N  
ANISOU 9243  N   GLY C1110    12280  14154   6885    171   -506     82       N  
ATOM   9244  CA  GLY C1110     -65.661  40.848  94.994  1.00 86.65           C  
ANISOU 9244  CA  GLY C1110    12168  14027   6729    183   -669    126       C  
ATOM   9245  C   GLY C1110     -65.449  42.248  94.464  1.00 88.76           C  
ANISOU 9245  C   GLY C1110    12432  14239   7054    220   -682    -78       C  
ATOM   9246  O   GLY C1110     -64.756  43.045  95.099  1.00 89.06           O  
ANISOU 9246  O   GLY C1110    12525  14366   6950    151   -747   -144       O  
ATOM   9247  N   VAL C1111     -66.086  42.566  93.313  1.00 83.28           N  
ANISOU 9247  N   VAL C1111    11684  13393   6568    314   -635   -174       N  
ATOM   9248  CA  VAL C1111     -66.037  43.882  92.657  1.00 81.81           C  
ANISOU 9248  CA  VAL C1111    11498  13112   6475    348   -661   -343       C  
ATOM   9249  C   VAL C1111     -66.555  44.959  93.624  1.00 86.82           C  
ANISOU 9249  C   VAL C1111    12191  13809   6987    295   -589   -549       C  
ATOM   9250  O   VAL C1111     -65.994  46.056  93.658  1.00 86.68           O  
ANISOU 9250  O   VAL C1111    12219  13761   6956    269   -665   -661       O  
ATOM   9251  CB  VAL C1111     -66.779  43.922  91.286  1.00 83.68           C  
ANISOU 9251  CB  VAL C1111    11672  13181   6943    446   -636   -380       C  
ATOM   9252  CG1 VAL C1111     -66.413  45.176  90.496  1.00 82.80           C  
ANISOU 9252  CG1 VAL C1111    11572  12963   6927    461   -717   -480       C  
ATOM   9253  CG2 VAL C1111     -66.485  42.681  90.450  1.00 82.32           C  
ANISOU 9253  CG2 VAL C1111    11451  12960   6867    496   -672   -214       C  
ATOM   9254  N   ALA C1112     -67.579  44.620  94.449  1.00 84.66           N  
ANISOU 9254  N   ALA C1112    11917  13632   6618    269   -441   -601       N  
ATOM   9255  CA  ALA C1112     -68.163  45.514  95.460  1.00 86.72           C  
ANISOU 9255  CA  ALA C1112    12223  13985   6740    226   -333   -827       C  
ATOM   9256  C   ALA C1112     -67.164  45.855  96.588  1.00 92.57           C  
ANISOU 9256  C   ALA C1112    13077  14885   7212    102   -408   -840       C  
ATOM   9257  O   ALA C1112     -67.339  46.863  97.277  1.00 94.11           O  
ANISOU 9257  O   ALA C1112    13333  15123   7300     68   -363  -1069       O  
ATOM   9258  CB  ALA C1112     -69.439  44.911  96.039  1.00 88.63           C  
ANISOU 9258  CB  ALA C1112    12412  14335   6927    209   -137   -854       C  
ATOM   9259  N   GLY C1113     -66.126  45.030  96.742  1.00 88.36           N  
ANISOU 9259  N   GLY C1113    12562  14423   6586     43   -535   -605       N  
ATOM   9260  CA  GLY C1113     -65.067  45.234  97.722  1.00 89.48           C  
ANISOU 9260  CA  GLY C1113    12795  14717   6487    -81   -653   -569       C  
ATOM   9261  C   GLY C1113     -64.227  46.453  97.401  1.00 93.22           C  
ANISOU 9261  C   GLY C1113    13298  15103   7018    -89   -784   -699       C  
ATOM   9262  O   GLY C1113     -63.828  47.188  98.306  1.00 94.68           O  
ANISOU 9262  O   GLY C1113    13577  15386   7009   -193   -831   -826       O  
ATOM   9263  N   PHE C1114     -63.988  46.698  96.097  1.00 88.20           N  
ANISOU 9263  N   PHE C1114    12588  14282   6641      5   -844   -671       N  
ATOM   9264  CA  PHE C1114     -63.205  47.822  95.582  1.00 87.92           C  
ANISOU 9264  CA  PHE C1114    12568  14140   6699    -17   -974   -753       C  
ATOM   9265  C   PHE C1114     -63.993  49.141  95.687  1.00 93.47           C  
ANISOU 9265  C   PHE C1114    13334  14724   7457      1   -913  -1040       C  
ATOM   9266  O   PHE C1114     -64.302  49.766  94.669  1.00 91.63           O  
ANISOU 9266  O   PHE C1114    13068  14296   7450     76   -930  -1097       O  
ATOM   9267  CB  PHE C1114     -62.750  47.536  94.138  1.00 87.62           C  
ANISOU 9267  CB  PHE C1114    12429  13973   6890     60  -1039   -607       C  
ATOM   9268  CG  PHE C1114     -61.756  46.409  93.991  1.00 88.78           C  
ANISOU 9268  CG  PHE C1114    12500  14214   7018     59  -1120   -365       C  
ATOM   9269  CD1 PHE C1114     -60.390  46.644  94.104  1.00 92.68           C  
ANISOU 9269  CD1 PHE C1114    12966  14781   7469    -20  -1275   -282       C  
ATOM   9270  CD2 PHE C1114     -62.181  45.117  93.705  1.00 90.12           C  
ANISOU 9270  CD2 PHE C1114    12614  14385   7242    141  -1052   -226       C  
ATOM   9271  CE1 PHE C1114     -59.468  45.601  93.951  1.00 93.44           C  
ANISOU 9271  CE1 PHE C1114    12962  14956   7587      5  -1353    -71       C  
ATOM   9272  CE2 PHE C1114     -61.256  44.075  93.559  1.00 92.89           C  
ANISOU 9272  CE2 PHE C1114    12891  14790   7615    165  -1138    -21       C  
ATOM   9273  CZ  PHE C1114     -59.907  44.324  93.683  1.00 91.67           C  
ANISOU 9273  CZ  PHE C1114    12691  14713   7428    108  -1284     51       C  
ATOM   9274  N   THR C1115     -64.300  49.561  96.932  1.00 93.49           N  
ANISOU 9274  N   THR C1115    13430  14844   7248    -70   -851  -1222       N  
ATOM   9275  CA  THR C1115     -65.078  50.764  97.262  1.00 95.55           C  
ANISOU 9275  CA  THR C1115    13753  15007   7544    -41   -776  -1541       C  
ATOM   9276  C   THR C1115     -64.570  52.052  96.600  1.00100.50           C  
ANISOU 9276  C   THR C1115    14417  15407   8360    -44   -929  -1648       C  
ATOM   9277  O   THR C1115     -65.293  52.630  95.781  1.00 99.89           O  
ANISOU 9277  O   THR C1115    14303  15117   8534     68   -905  -1741       O  
ATOM   9278  CB  THR C1115     -65.290  50.894  98.779  1.00106.54           C  
ANISOU 9278  CB  THR C1115    15248  16611   8623   -139   -684  -1719       C  
ATOM   9279  OG1 THR C1115     -65.661  49.623  99.315  1.00107.35           O  
ANISOU 9279  OG1 THR C1115    15317  16925   8547   -168   -566  -1553       O  
ATOM   9280  CG2 THR C1115     -66.349  51.934  99.132  1.00107.33           C  
ANISOU 9280  CG2 THR C1115    15381  16624   8776    -67   -543  -2084       C  
ATOM   9281  N   ASN C1116     -63.335  52.483  96.946  1.00 97.83           N  
ANISOU 9281  N   ASN C1116    14148  15111   7911   -183  -1102  -1614       N  
ATOM   9282  CA  ASN C1116     -62.696  53.690  96.418  1.00 98.32           C  
ANISOU 9282  CA  ASN C1116    14255  14972   8129   -236  -1272  -1684       C  
ATOM   9283  C   ASN C1116     -62.677  53.691  94.888  1.00101.14           C  
ANISOU 9283  C   ASN C1116    14516  15146   8766   -161  -1322  -1516       C  
ATOM   9284  O   ASN C1116     -63.144  54.652  94.273  1.00100.98           O  
ANISOU 9284  O   ASN C1116    14521  14887   8959   -111  -1358  -1634       O  
ATOM   9285  CB  ASN C1116     -61.286  53.843  96.984  1.00100.14           C  
ANISOU 9285  CB  ASN C1116    14534  15328   8188   -418  -1453  -1602       C  
ATOM   9286  CG  ASN C1116     -61.269  53.920  98.485  1.00134.28           C  
ANISOU 9286  CG  ASN C1116    18976  19841  12204   -519  -1431  -1771       C  
ATOM   9287  OD1 ASN C1116     -61.502  54.976  99.076  1.00132.79           O  
ANISOU 9287  OD1 ASN C1116    18909  19570  11976   -561  -1444  -2059       O  
ATOM   9288  ND2 ASN C1116     -61.019  52.795  99.134  1.00128.25           N  
ANISOU 9288  ND2 ASN C1116    18187  19329  11212   -561  -1401  -1600       N  
ATOM   9289  N   SER C1117     -62.204  52.580  94.286  1.00 96.35           N  
ANISOU 9289  N   SER C1117    13804  14649   8158   -146  -1321  -1248       N  
ATOM   9290  CA  SER C1117     -62.113  52.378  92.840  1.00 94.32           C  
ANISOU 9290  CA  SER C1117    13454  14276   8106    -89  -1351  -1078       C  
ATOM   9291  C   SER C1117     -63.474  52.550  92.158  1.00 98.80           C  
ANISOU 9291  C   SER C1117    14005  14670   8864     54  -1251  -1169       C  
ATOM   9292  O   SER C1117     -63.542  53.222  91.127  1.00 98.30           O  
ANISOU 9292  O   SER C1117    13937  14421   8991     67  -1331  -1146       O  
ATOM   9293  CB  SER C1117     -61.517  51.007  92.525  1.00 95.84           C  
ANISOU 9293  CB  SER C1117    13539  14636   8241    -71  -1331   -833       C  
ATOM   9294  OG  SER C1117     -60.268  50.815  93.171  1.00104.68           O  
ANISOU 9294  OG  SER C1117    14647  15918   9210   -188  -1439   -738       O  
ATOM   9295  N   LEU C1118     -64.557  51.989  92.753  1.00 95.97           N  
ANISOU 9295  N   LEU C1118    13632  14378   8455    147  -1089  -1266       N  
ATOM   9296  CA  LEU C1118     -65.917  52.108  92.216  1.00 95.60           C  
ANISOU 9296  CA  LEU C1118    13538  14188   8596    285   -993  -1362       C  
ATOM   9297  C   LEU C1118     -66.397  53.555  92.259  1.00102.16           C  
ANISOU 9297  C   LEU C1118    14432  14800   9583    318  -1047  -1598       C  
ATOM   9298  O   LEU C1118     -66.891  54.050  91.245  1.00101.42           O  
ANISOU 9298  O   LEU C1118    14310  14500   9726    390  -1109  -1584       O  
ATOM   9299  CB  LEU C1118     -66.916  51.199  92.956  1.00 95.82           C  
ANISOU 9299  CB  LEU C1118    13517  14365   8524    349   -800  -1413       C  
ATOM   9300  CG  LEU C1118     -66.849  49.689  92.703  1.00 98.77           C  
ANISOU 9300  CG  LEU C1118    13816  14877   8834    356   -742  -1180       C  
ATOM   9301  CD1 LEU C1118     -67.685  48.946  93.731  1.00 99.96           C  
ANISOU 9301  CD1 LEU C1118    13947  15194   8838    360   -567  -1230       C  
ATOM   9302  CD2 LEU C1118     -67.288  49.323  91.284  1.00 99.29           C  
ANISOU 9302  CD2 LEU C1118    13799  14806   9118    444   -764  -1062       C  
ATOM   9303  N   ARG C1119     -66.218  54.243  93.415  1.00101.57           N  
ANISOU 9303  N   ARG C1119    14453  14761   9378    260  -1042  -1813       N  
ATOM   9304  CA  ARG C1119     -66.616  55.644  93.599  1.00103.76           C  
ANISOU 9304  CA  ARG C1119    14806  14810   9809    295  -1099  -2080       C  
ATOM   9305  C   ARG C1119     -65.851  56.571  92.648  1.00106.77           C  
ANISOU 9305  C   ARG C1119    15238  14957  10371    222  -1326  -1980       C  
ATOM   9306  O   ARG C1119     -66.421  57.557  92.182  1.00107.44           O  
ANISOU 9306  O   ARG C1119    15347  14770  10705    296  -1402  -2099       O  
ATOM   9307  CB  ARG C1119     -66.472  56.089  95.067  1.00107.82           C  
ANISOU 9307  CB  ARG C1119    15425  15437  10102    228  -1046  -2343       C  
ATOM   9308  CG  ARG C1119     -67.240  57.370  95.397  1.00125.10           C  
ANISOU 9308  CG  ARG C1119    17672  17398  12464    322  -1038  -2695       C  
ATOM   9309  CD  ARG C1119     -67.346  57.617  96.888  1.00143.56           C  
ANISOU 9309  CD  ARG C1119    20100  19899  14547    277   -919  -2998       C  
ATOM   9310  NE  ARG C1119     -68.588  57.075  97.444  1.00159.55           N  
ANISOU 9310  NE  ARG C1119    22030  22082  16512    402   -654  -3153       N  
ATOM   9311  CZ  ARG C1119     -68.688  55.903  98.064  1.00177.84           C  
ANISOU 9311  CZ  ARG C1119    24303  24719  18548    345   -494  -3036       C  
ATOM   9312  NH1 ARG C1119     -69.856  55.496  98.539  1.00168.54           N  
ANISOU 9312  NH1 ARG C1119    23028  23679  17331    439   -249  -3178       N  
ATOM   9313  NH2 ARG C1119     -67.619  55.129  98.217  1.00164.82           N  
ANISOU 9313  NH2 ARG C1119    22699  23255  16671    190   -584  -2768       N  
ATOM   9314  N   MET C1120     -64.582  56.228  92.330  1.00101.59           N  
ANISOU 9314  N   MET C1120    14586  14409   9605     76  -1435  -1747       N  
ATOM   9315  CA  MET C1120     -63.737  56.986  91.404  1.00101.00           C  
ANISOU 9315  CA  MET C1120    14542  14169   9664    -36  -1634  -1606       C  
ATOM   9316  C   MET C1120     -64.271  56.895  89.976  1.00101.46           C  
ANISOU 9316  C   MET C1120    14532  14084   9936     44  -1659  -1443       C  
ATOM   9317  O   MET C1120     -64.271  57.906  89.271  1.00101.85           O  
ANISOU 9317  O   MET C1120    14633  13887  10179     10  -1810  -1428       O  
ATOM   9318  CB  MET C1120     -62.278  56.525  91.487  1.00102.90           C  
ANISOU 9318  CB  MET C1120    14760  14614   9724   -205  -1710  -1407       C  
ATOM   9319  CG  MET C1120     -61.534  57.149  92.633  1.00108.96           C  
ANISOU 9319  CG  MET C1120    15626  15429  10344   -345  -1799  -1552       C  
ATOM   9320  SD  MET C1120     -59.986  56.297  92.980  1.00113.04           S  
ANISOU 9320  SD  MET C1120    16068  16253  10628   -506  -1862  -1323       S  
ATOM   9321  CE  MET C1120     -59.575  57.025  94.560  1.00112.76           C  
ANISOU 9321  CE  MET C1120    16177  16271  10394   -642  -1947  -1570       C  
ATOM   9322  N   LEU C1121     -64.764  55.696  89.571  1.00 94.44           N  
ANISOU 9322  N   LEU C1121    13538  13337   9008    142  -1526  -1323       N  
ATOM   9323  CA  LEU C1121     -65.377  55.449  88.260  1.00 92.16           C  
ANISOU 9323  CA  LEU C1121    13186  12948   8885    219  -1539  -1183       C  
ATOM   9324  C   LEU C1121     -66.709  56.198  88.197  1.00 96.96           C  
ANISOU 9324  C   LEU C1121    13799  13319   9723    361  -1544  -1364       C  
ATOM   9325  O   LEU C1121     -67.014  56.835  87.187  1.00 97.10           O  
ANISOU 9325  O   LEU C1121    13829  13124   9942    375  -1676  -1289       O  
ATOM   9326  CB  LEU C1121     -65.624  53.948  88.042  1.00 89.81           C  
ANISOU 9326  CB  LEU C1121    12785  12855   8484    287  -1394  -1057       C  
ATOM   9327  CG  LEU C1121     -64.403  53.061  87.875  1.00 92.64           C  
ANISOU 9327  CG  LEU C1121    13103  13424   8673    192  -1391   -864       C  
ATOM   9328  CD1 LEU C1121     -64.760  51.619  88.137  1.00 91.39           C  
ANISOU 9328  CD1 LEU C1121    12869  13440   8417    274  -1243   -811       C  
ATOM   9329  CD2 LEU C1121     -63.782  53.218  86.497  1.00 93.80           C  
ANISOU 9329  CD2 LEU C1121    13230  13527   8884    117  -1493   -674       C  
ATOM   9330  N   GLN C1122     -67.475  56.144  89.307  1.00 94.03           N  
ANISOU 9330  N   GLN C1122    13415  12994   9318    460  -1403  -1602       N  
ATOM   9331  CA  GLN C1122     -68.757  56.818  89.519  1.00 95.50           C  
ANISOU 9331  CA  GLN C1122    13575  12993   9719    619  -1367  -1836       C  
ATOM   9332  C   GLN C1122     -68.571  58.350  89.415  1.00101.43           C  
ANISOU 9332  C   GLN C1122    14434  13435  10671    597  -1560  -1959       C  
ATOM   9333  O   GLN C1122     -69.461  59.037  88.908  1.00102.41           O  
ANISOU 9333  O   GLN C1122    14529  13305  11076    721  -1636  -2033       O  
ATOM   9334  CB  GLN C1122     -69.304  56.429  90.901  1.00 97.91           C  
ANISOU 9334  CB  GLN C1122    13852  13484   9867    679  -1152  -2073       C  
ATOM   9335  CG  GLN C1122     -70.807  56.591  91.089  1.00113.69           C  
ANISOU 9335  CG  GLN C1122    15739  15403  12055    868  -1025  -2286       C  
ATOM   9336  CD  GLN C1122     -71.227  56.415  92.536  1.00138.48           C  
ANISOU 9336  CD  GLN C1122    18868  18742  15007    893   -805  -2551       C  
ATOM   9337  OE1 GLN C1122     -70.492  55.891  93.387  1.00133.05           O  
ANISOU 9337  OE1 GLN C1122    18249  18291  14012    767   -736  -2527       O  
ATOM   9338  NE2 GLN C1122     -72.434  56.854  92.853  1.00135.94           N  
ANISOU 9338  NE2 GLN C1122    18450  18340  14862   1056   -690  -2809       N  
ATOM   9339  N   GLN C1123     -67.405  58.866  89.880  1.00 98.10           N  
ANISOU 9339  N   GLN C1123    14130  13023  10120    433  -1658  -1967       N  
ATOM   9340  CA  GLN C1123     -67.035  60.287  89.827  1.00100.07           C  
ANISOU 9340  CA  GLN C1123    14505  12976  10543    366  -1864  -2063       C  
ATOM   9341  C   GLN C1123     -66.263  60.640  88.538  1.00102.82           C  
ANISOU 9341  C   GLN C1123    14887  13196  10985    220  -2076  -1756       C  
ATOM   9342  O   GLN C1123     -65.867  61.797  88.359  1.00104.37           O  
ANISOU 9342  O   GLN C1123    15192  13132  11332    126  -2276  -1772       O  
ATOM   9343  CB  GLN C1123     -66.210  60.691  91.061  1.00103.07           C  
ANISOU 9343  CB  GLN C1123    14997  13436  10729    241  -1869  -2249       C  
ATOM   9344  CG  GLN C1123     -67.016  60.839  92.350  1.00121.43           C  
ANISOU 9344  CG  GLN C1123    17337  15805  12997    368  -1700  -2624       C  
ATOM   9345  CD  GLN C1123     -66.152  61.134  93.558  1.00145.34           C  
ANISOU 9345  CD  GLN C1123    20489  18955  15777    219  -1712  -2794       C  
ATOM   9346  OE1 GLN C1123     -64.946  60.847  93.600  1.00139.05           O  
ANISOU 9346  OE1 GLN C1123    19729  18313  14791     27  -1801  -2604       O  
ATOM   9347  NE2 GLN C1123     -66.762  61.700  94.587  1.00143.37           N  
ANISOU 9347  NE2 GLN C1123    20298  18657  15518    304  -1621  -3171       N  
ATOM   9348  N   LYS C1124     -66.055  59.641  87.647  1.00 96.36           N  
ANISOU 9348  N   LYS C1124    13981  12561  10072    190  -2030  -1482       N  
ATOM   9349  CA  LYS C1124     -65.354  59.756  86.356  1.00 94.98           C  
ANISOU 9349  CA  LYS C1124    13815  12348   9925     45  -2180  -1179       C  
ATOM   9350  C   LYS C1124     -63.865  60.170  86.474  1.00 98.81           C  
ANISOU 9350  C   LYS C1124    14365  12895  10283   -195  -2290  -1069       C  
ATOM   9351  O   LYS C1124     -63.329  60.854  85.600  1.00 98.79           O  
ANISOU 9351  O   LYS C1124    14411  12758  10368   -346  -2462   -886       O  
ATOM   9352  CB  LYS C1124     -66.149  60.611  85.340  1.00 98.26           C  
ANISOU 9352  CB  LYS C1124    14262  12439  10634    101  -2352  -1116       C  
ATOM   9353  CG  LYS C1124     -67.551  60.078  85.067  1.00108.52           C  
ANISOU 9353  CG  LYS C1124    15458  13715  12059    322  -2257  -1177       C  
ATOM   9354  CD  LYS C1124     -68.054  60.454  83.685  1.00118.05           C  
ANISOU 9354  CD  LYS C1124    16667  14723  13465    326  -2437   -971       C  
ATOM   9355  CE  LYS C1124     -69.256  59.639  83.264  1.00127.72           C  
ANISOU 9355  CE  LYS C1124    17764  16007  14756    502  -2342   -969       C  
ATOM   9356  NZ  LYS C1124     -68.909  58.216  82.988  1.00133.51           N  
ANISOU 9356  NZ  LYS C1124    18424  17075  15229    460  -2174   -834       N  
ATOM   9357  N   ARG C1125     -63.204  59.724  87.556  1.00 95.52           N  
ANISOU 9357  N   ARG C1125    13940  12699   9653   -244  -2196  -1166       N  
ATOM   9358  CA  ARG C1125     -61.786  59.982  87.848  1.00 95.96           C  
ANISOU 9358  CA  ARG C1125    14024  12862   9575   -465  -2290  -1080       C  
ATOM   9359  C   ARG C1125     -60.991  58.752  87.383  1.00 97.30           C  
ANISOU 9359  C   ARG C1125    14061  13353   9555   -517  -2191   -845       C  
ATOM   9360  O   ARG C1125     -60.412  58.024  88.193  1.00 95.74           O  
ANISOU 9360  O   ARG C1125    13814  13397   9167   -535  -2110   -865       O  
ATOM   9361  CB  ARG C1125     -61.582  60.283  89.352  1.00 97.62           C  
ANISOU 9361  CB  ARG C1125    14309  13111   9672   -486  -2276  -1342       C  
ATOM   9362  CG  ARG C1125     -62.438  61.439  89.871  1.00111.61           C  
ANISOU 9362  CG  ARG C1125    16205  14566  11636   -400  -2343  -1636       C  
ATOM   9363  CD  ARG C1125     -62.225  61.698  91.346  1.00125.57           C  
ANISOU 9363  CD  ARG C1125    18059  16404  13248   -432  -2313  -1919       C  
ATOM   9364  NE  ARG C1125     -61.236  62.753  91.577  1.00140.21           N  
ANISOU 9364  NE  ARG C1125    20027  18113  15132   -649  -2529  -1946       N  
ATOM   9365  CZ  ARG C1125     -60.899  63.221  92.776  1.00161.13           C  
ANISOU 9365  CZ  ARG C1125    22785  20778  17660   -727  -2566  -2196       C  
ATOM   9366  NH1 ARG C1125     -59.991  64.182  92.888  1.00151.14           N  
ANISOU 9366  NH1 ARG C1125    21621  19361  16443   -942  -2785  -2204       N  
ATOM   9367  NH2 ARG C1125     -61.462  62.727  93.873  1.00151.36           N  
ANISOU 9367  NH2 ARG C1125    21558  19716  16236   -610  -2388  -2437       N  
ATOM   9368  N   TRP C1126     -61.018  58.516  86.051  1.00 93.16           N  
ANISOU 9368  N   TRP C1126    13482  12824   9089   -533  -2205   -628       N  
ATOM   9369  CA  TRP C1126     -60.424  57.374  85.343  1.00 91.06           C  
ANISOU 9369  CA  TRP C1126    13087  12826   8684   -551  -2102   -424       C  
ATOM   9370  C   TRP C1126     -59.000  56.977  85.738  1.00 96.05           C  
ANISOU 9370  C   TRP C1126    13633  13709   9151   -693  -2095   -334       C  
ATOM   9371  O   TRP C1126     -58.786  55.819  86.095  1.00 94.34           O  
ANISOU 9371  O   TRP C1126    13321  13718   8807   -609  -1967   -320       O  
ATOM   9372  CB  TRP C1126     -60.585  57.496  83.812  1.00 89.25           C  
ANISOU 9372  CB  TRP C1126    12848  12531   8533   -596  -2151   -225       C  
ATOM   9373  CG  TRP C1126     -61.934  57.972  83.332  1.00 90.44           C  
ANISOU 9373  CG  TRP C1126    13071  12421   8871   -473  -2207   -279       C  
ATOM   9374  CD1 TRP C1126     -62.177  59.028  82.505  1.00 94.75           C  
ANISOU 9374  CD1 TRP C1126    13703  12718   9578   -558  -2386   -181       C  
ATOM   9375  CD2 TRP C1126     -63.217  57.386  83.619  1.00 89.27           C  
ANISOU 9375  CD2 TRP C1126    12898  12237   8782   -248  -2097   -422       C  
ATOM   9376  NE1 TRP C1126     -63.527  59.146  82.266  1.00 94.10           N  
ANISOU 9376  NE1 TRP C1126    13645  12443   9667   -383  -2407   -260       N  
ATOM   9377  CE2 TRP C1126     -64.189  58.154  82.940  1.00 94.02           C  
ANISOU 9377  CE2 TRP C1126    13558  12568   9599   -194  -2222   -416       C  
ATOM   9378  CE3 TRP C1126     -63.644  56.294  84.397  1.00 89.11           C  
ANISOU 9378  CE3 TRP C1126    12807  12388   8663   -101  -1915   -541       C  
ATOM   9379  CZ2 TRP C1126     -65.556  57.856  83.003  1.00 93.03           C  
ANISOU 9379  CZ2 TRP C1126    13396  12352   9598     12  -2162   -537       C  
ATOM   9380  CZ3 TRP C1126     -65.000  56.013  84.473  1.00 90.12           C  
ANISOU 9380  CZ3 TRP C1126    12913  12430   8901     81  -1845   -656       C  
ATOM   9381  CH2 TRP C1126     -65.939  56.788  83.784  1.00 91.74           C  
ANISOU 9381  CH2 TRP C1126    13151  12378   9327    141  -1963   -662       C  
ATOM   9382  N   ASP C1127     -58.043  57.930  85.698  1.00 95.45           N  
ANISOU 9382  N   ASP C1127    13586  13584   9097   -908  -2246   -268       N  
ATOM   9383  CA  ASP C1127     -56.633  57.703  86.049  1.00 96.32           C  
ANISOU 9383  CA  ASP C1127    13591  13926   9082  -1065  -2271   -175       C  
ATOM   9384  C   ASP C1127     -56.438  57.264  87.500  1.00100.85           C  
ANISOU 9384  C   ASP C1127    14162  14626   9530  -1014  -2242   -327       C  
ATOM   9385  O   ASP C1127     -55.609  56.396  87.762  1.00 99.80           O  
ANISOU 9385  O   ASP C1127    13894  14748   9276  -1025  -2192   -241       O  
ATOM   9386  CB  ASP C1127     -55.784  58.944  85.730  1.00100.68           C  
ANISOU 9386  CB  ASP C1127    14183  14365   9707  -1329  -2457    -80       C  
ATOM   9387  CG  ASP C1127     -55.657  59.257  84.248  1.00114.38           C  
ANISOU 9387  CG  ASP C1127    15893  16061  11505  -1443  -2486    141       C  
ATOM   9388  OD1 ASP C1127     -56.493  58.762  83.457  1.00114.55           O  
ANISOU 9388  OD1 ASP C1127    15917  16061  11545  -1301  -2394    178       O  
ATOM   9389  OD2 ASP C1127     -54.740  60.021  83.881  1.00122.86           O  
ANISOU 9389  OD2 ASP C1127    16950  17130  12601  -1692  -2609    281       O  
ATOM   9390  N   GLU C1128     -57.218  57.843  88.428  1.00 99.12           N  
ANISOU 9390  N   GLU C1128    14088  14234   9339   -953  -2272   -556       N  
ATOM   9391  CA  GLU C1128     -57.192  57.515  89.854  1.00 99.99           C  
ANISOU 9391  CA  GLU C1128    14231  14463   9296   -917  -2242   -722       C  
ATOM   9392  C   GLU C1128     -57.637  56.063  90.093  1.00103.43           C  
ANISOU 9392  C   GLU C1128    14579  15104   9614   -736  -2060   -693       C  
ATOM   9393  O   GLU C1128     -56.995  55.350  90.872  1.00103.27           O  
ANISOU 9393  O   GLU C1128    14500  15303   9436   -758  -2049   -658       O  
ATOM   9394  CB  GLU C1128     -58.084  58.483  90.646  1.00103.05           C  
ANISOU 9394  CB  GLU C1128    14795  14614   9744   -875  -2281  -1004       C  
ATOM   9395  CG  GLU C1128     -57.547  59.904  90.718  1.00117.71           C  
ANISOU 9395  CG  GLU C1128    16763  16253  11708  -1068  -2490  -1069       C  
ATOM   9396  CD  GLU C1128     -58.385  60.907  91.492  1.00145.03           C  
ANISOU 9396  CD  GLU C1128    20399  19452  15255  -1013  -2535  -1386       C  
ATOM   9397  OE1 GLU C1128     -58.198  62.123  91.264  1.00145.99           O  
ANISOU 9397  OE1 GLU C1128    20624  19301  15544  -1135  -2714  -1432       O  
ATOM   9398  OE2 GLU C1128     -59.209  60.488  92.337  1.00140.50           O  
ANISOU 9398  OE2 GLU C1128    19857  18944  14583   -855  -2392  -1592       O  
ATOM   9399  N   ALA C1129     -58.721  55.630  89.406  1.00 99.26           N  
ANISOU 9399  N   ALA C1129    14044  14495   9177   -569  -1940   -692       N  
ATOM   9400  CA  ALA C1129     -59.287  54.279  89.503  1.00 97.60           C  
ANISOU 9400  CA  ALA C1129    13760  14431   8892   -404  -1775   -660       C  
ATOM   9401  C   ALA C1129     -58.376  53.218  88.875  1.00101.08           C  
ANISOU 9401  C   ALA C1129    14048  15075   9283   -412  -1742   -442       C  
ATOM   9402  O   ALA C1129     -58.361  52.079  89.343  1.00100.32           O  
ANISOU 9402  O   ALA C1129    13891  15135   9092   -325  -1657   -403       O  
ATOM   9403  CB  ALA C1129     -60.666  54.237  88.860  1.00 97.31           C  
ANISOU 9403  CB  ALA C1129    13749  14232   8991   -251  -1686   -719       C  
ATOM   9404  N   ALA C1130     -57.618  53.598  87.826  1.00 97.82           N  
ANISOU 9404  N   ALA C1130    13571  14656   8938   -519  -1808   -303       N  
ATOM   9405  CA  ALA C1130     -56.695  52.710  87.110  1.00 97.11           C  
ANISOU 9405  CA  ALA C1130    13316  14763   8818   -526  -1762   -125       C  
ATOM   9406  C   ALA C1130     -55.463  52.327  87.949  1.00101.50           C  
ANISOU 9406  C   ALA C1130    13766  15526   9273   -600  -1820    -68       C  
ATOM   9407  O   ALA C1130     -55.013  51.181  87.877  1.00100.09           O  
ANISOU 9407  O   ALA C1130    13453  15513   9062   -513  -1753     23       O  
ATOM   9408  CB  ALA C1130     -56.270  53.343  85.792  1.00 98.28           C  
ANISOU 9408  CB  ALA C1130    13429  14870   9041   -647  -1804     -5       C  
ATOM   9409  N   VAL C1131     -54.923  53.281  88.737  1.00 99.76           N  
ANISOU 9409  N   VAL C1131    13604  15282   9017   -759  -1960   -124       N  
ATOM   9410  CA  VAL C1131     -53.766  53.054  89.616  1.00100.83           C  
ANISOU 9410  CA  VAL C1131    13646  15609   9056   -854  -2057    -72       C  
ATOM   9411  C   VAL C1131     -54.210  52.222  90.837  1.00103.37           C  
ANISOU 9411  C   VAL C1131    14019  16011   9246   -740  -2021   -141       C  
ATOM   9412  O   VAL C1131     -53.493  51.307  91.252  1.00103.09           O  
ANISOU 9412  O   VAL C1131    13859  16162   9149   -712  -2041    -32       O  
ATOM   9413  CB  VAL C1131     -53.049  54.378  90.028  1.00107.06           C  
ANISOU 9413  CB  VAL C1131    14491  16341   9846  -1089  -2240   -112       C  
ATOM   9414  CG1 VAL C1131     -51.825  54.101  90.901  1.00108.44           C  
ANISOU 9414  CG1 VAL C1131    14548  16732   9923  -1198  -2361    -43       C  
ATOM   9415  CG2 VAL C1131     -52.644  55.195  88.804  1.00107.35           C  
ANISOU 9415  CG2 VAL C1131    14485  16294  10009  -1230  -2280     -9       C  
ATOM   9416  N   ASN C1132     -55.401  52.535  91.386  1.00 98.82           N  
ANISOU 9416  N   ASN C1132    13616  15298   8634   -676  -1967   -315       N  
ATOM   9417  CA  ASN C1132     -55.988  51.839  92.526  1.00 98.47           C  
ANISOU 9417  CA  ASN C1132    13640  15334   8441   -593  -1909   -388       C  
ATOM   9418  C   ASN C1132     -56.249  50.354  92.250  1.00 99.75           C  
ANISOU 9418  C   ASN C1132    13701  15592   8607   -431  -1788   -256       C  
ATOM   9419  O   ASN C1132     -56.076  49.534  93.156  1.00100.20           O  
ANISOU 9419  O   ASN C1132    13746  15789   8535   -411  -1801   -200       O  
ATOM   9420  CB  ASN C1132     -57.266  52.536  92.976  1.00100.40           C  
ANISOU 9420  CB  ASN C1132    14057  15416   8674   -552  -1841   -617       C  
ATOM   9421  CG  ASN C1132     -57.028  53.691  93.911  1.00123.49           C  
ANISOU 9421  CG  ASN C1132    17114  18294  11512   -698  -1962   -797       C  
ATOM   9422  OD1 ASN C1132     -56.242  54.605  93.631  1.00119.33           O  
ANISOU 9422  OD1 ASN C1132    16588  17697  11054   -844  -2107   -786       O  
ATOM   9423  ND2 ASN C1132     -57.728  53.684  95.038  1.00113.28           N  
ANISOU 9423  ND2 ASN C1132    15938  17041  10061   -674  -1900   -975       N  
ATOM   9424  N   LEU C1133     -56.662  50.009  91.011  1.00 93.18           N  
ANISOU 9424  N   LEU C1133    12808  14678   7920   -326  -1689   -202       N  
ATOM   9425  CA  LEU C1133     -56.916  48.621  90.614  1.00 90.98           C  
ANISOU 9425  CA  LEU C1133    12441  14454   7674   -174  -1584    -96       C  
ATOM   9426  C   LEU C1133     -55.609  47.878  90.291  1.00 94.14           C  
ANISOU 9426  C   LEU C1133    12659  15006   8104   -170  -1637     70       C  
ATOM   9427  O   LEU C1133     -55.541  46.662  90.462  1.00 93.52           O  
ANISOU 9427  O   LEU C1133    12511  14994   8027    -59  -1604    160       O  
ATOM   9428  CB  LEU C1133     -57.917  48.534  89.447  1.00 89.26           C  
ANISOU 9428  CB  LEU C1133    12239  14092   7583    -70  -1468   -128       C  
ATOM   9429  CG  LEU C1133     -59.377  48.912  89.750  1.00 93.39           C  
ANISOU 9429  CG  LEU C1133    12894  14475   8116    -15  -1392   -281       C  
ATOM   9430  CD1 LEU C1133     -60.165  49.097  88.470  1.00 92.33           C  
ANISOU 9430  CD1 LEU C1133    12761  14193   8128     51  -1337   -294       C  
ATOM   9431  CD2 LEU C1133     -60.058  47.879  90.640  1.00 95.77           C  
ANISOU 9431  CD2 LEU C1133    13215  14844   8328     67  -1304   -285       C  
ATOM   9432  N   ALA C1134     -54.572  48.615  89.845  1.00 90.60           N  
ANISOU 9432  N   ALA C1134    12124  14607   7694   -295  -1724    112       N  
ATOM   9433  CA  ALA C1134     -53.247  48.069  89.547  1.00 90.61           C  
ANISOU 9433  CA  ALA C1134    11913  14774   7740   -303  -1772    252       C  
ATOM   9434  C   ALA C1134     -52.535  47.733  90.856  1.00 93.95           C  
ANISOU 9434  C   ALA C1134    12299  15331   8065   -345  -1908    311       C  
ATOM   9435  O   ALA C1134     -51.760  46.778  90.904  1.00 93.62           O  
ANISOU 9435  O   ALA C1134    12090  15412   8071   -267  -1940    433       O  
ATOM   9436  CB  ALA C1134     -52.433  49.071  88.746  1.00 92.25           C  
ANISOU 9436  CB  ALA C1134    12038  15007   8004   -459  -1819    279       C  
ATOM   9437  N   LYS C1135     -52.815  48.514  91.920  1.00 90.59           N  
ANISOU 9437  N   LYS C1135    12034  14880   7506   -465  -1998    217       N  
ATOM   9438  CA  LYS C1135     -52.268  48.282  93.254  1.00 91.69           C  
ANISOU 9438  CA  LYS C1135    12182  15155   7502   -534  -2143    263       C  
ATOM   9439  C   LYS C1135     -53.319  47.496  94.041  1.00 95.75           C  
ANISOU 9439  C   LYS C1135    12834  15649   7899   -433  -2066    237       C  
ATOM   9440  O   LYS C1135     -54.053  48.052  94.862  1.00 95.45           O  
ANISOU 9440  O   LYS C1135    12978  15578   7711   -499  -2056     99       O  
ATOM   9441  CB  LYS C1135     -51.862  49.600  93.940  1.00 94.97           C  
ANISOU 9441  CB  LYS C1135    12693  15575   7816   -750  -2291    161       C  
ATOM   9442  CG  LYS C1135     -50.724  49.419  94.934  1.00107.07           C  
ANISOU 9442  CG  LYS C1135    14139  17297   9245   -863  -2495    266       C  
ATOM   9443  CD  LYS C1135     -50.134  50.750  95.360  1.00118.12           C  
ANISOU 9443  CD  LYS C1135    15599  18696  10586  -1097  -2658    173       C  
ATOM   9444  CE  LYS C1135     -48.946  50.570  96.269  1.00132.20           C  
ANISOU 9444  CE  LYS C1135    17273  20680  12277  -1223  -2885    289       C  
ATOM   9445  NZ  LYS C1135     -48.372  51.875  96.693  1.00144.65           N  
ANISOU 9445  NZ  LYS C1135    18916  22247  13796  -1473  -3061    188       N  
ATOM   9446  N   SER C1136     -53.445  46.203  93.689  1.00 92.52           N  
ANISOU 9446  N   SER C1136    12332  15248   7572   -269  -1995    359       N  
ATOM   9447  CA  SER C1136     -54.389  45.236  94.259  1.00 92.34           C  
ANISOU 9447  CA  SER C1136    12406  15203   7475   -173  -1919    387       C  
ATOM   9448  C   SER C1136     -53.892  43.803  94.018  1.00 97.58           C  
ANISOU 9448  C   SER C1136    12919  15899   8259    -29  -1944    575       C  
ATOM   9449  O   SER C1136     -53.074  43.576  93.119  1.00 96.88           O  
ANISOU 9449  O   SER C1136    12649  15822   8339     39  -1953    629       O  
ATOM   9450  CB  SER C1136     -55.784  45.421  93.658  1.00 93.43           C  
ANISOU 9450  CB  SER C1136    12655  15185   7659    -99  -1732    249       C  
ATOM   9451  OG  SER C1136     -55.882  44.922  92.334  1.00 96.90           O  
ANISOU 9451  OG  SER C1136    12992  15536   8290     29  -1637    281       O  
ATOM   9452  N   ARG C1137     -54.399  42.840  94.811  1.00 95.53           N  
ANISOU 9452  N   ARG C1137    12732  15648   7917     13  -1951    669       N  
ATOM   9453  CA  ARG C1137     -54.018  41.429  94.706  1.00 96.11           C  
ANISOU 9453  CA  ARG C1137    12689  15707   8121    153  -2000    853       C  
ATOM   9454  C   ARG C1137     -54.516  40.760  93.409  1.00 96.95           C  
ANISOU 9454  C   ARG C1137    12733  15662   8441    325  -1844    817       C  
ATOM   9455  O   ARG C1137     -53.916  39.782  92.961  1.00 96.58           O  
ANISOU 9455  O   ARG C1137    12541  15586   8568    462  -1882    919       O  
ATOM   9456  CB  ARG C1137     -54.404  40.646  95.979  1.00 99.74           C  
ANISOU 9456  CB  ARG C1137    13266  16214   8417    112  -2079    994       C  
ATOM   9457  CG  ARG C1137     -55.840  40.110  96.004  1.00114.46           C  
ANISOU 9457  CG  ARG C1137    15270  17973  10246    149  -1914    963       C  
ATOM   9458  CD  ARG C1137     -55.911  38.601  96.213  1.00129.72           C  
ANISOU 9458  CD  ARG C1137    17180  19838  12269    244  -1971   1176       C  
ATOM   9459  NE  ARG C1137     -54.993  37.857  95.344  1.00140.73           N  
ANISOU 9459  NE  ARG C1137    18382  21151  13938    414  -2041   1257       N  
ATOM   9460  CZ  ARG C1137     -53.918  37.201  95.773  1.00160.02           C  
ANISOU 9460  CZ  ARG C1137    20707  23637  16456    458  -2242   1445       C  
ATOM   9461  NH1 ARG C1137     -53.133  36.570  94.915  1.00149.16           N  
ANISOU 9461  NH1 ARG C1137    19136  22186  15353    635  -2275   1474       N  
ATOM   9462  NH2 ARG C1137     -53.615  37.182  97.067  1.00149.75           N  
ANISOU 9462  NH2 ARG C1137    19477  22465  14955    325  -2416   1597       N  
ATOM   9463  N   TRP C1138     -55.603  41.301  92.816  1.00 91.56           N  
ANISOU 9463  N   TRP C1138    12156  14881   7750    321  -1681    661       N  
ATOM   9464  CA  TRP C1138     -56.196  40.845  91.557  1.00 89.74           C  
ANISOU 9464  CA  TRP C1138    11895  14515   7686    450  -1540    601       C  
ATOM   9465  C   TRP C1138     -55.182  41.047  90.424  1.00 93.90           C  
ANISOU 9465  C   TRP C1138    12250  15074   8355    500  -1539    581       C  
ATOM   9466  O   TRP C1138     -54.980  40.137  89.617  1.00 93.11           O  
ANISOU 9466  O   TRP C1138    12047  14923   8409    640  -1493    602       O  
ATOM   9467  CB  TRP C1138     -57.513  41.608  91.289  1.00 86.86           C  
ANISOU 9467  CB  TRP C1138    11672  14063   7268    406  -1407    445       C  
ATOM   9468  CG  TRP C1138     -58.007  41.599  89.868  1.00 86.27           C  
ANISOU 9468  CG  TRP C1138    11569  13873   7336    490  -1292    360       C  
ATOM   9469  CD1 TRP C1138     -58.330  40.508  89.116  1.00 88.61           C  
ANISOU 9469  CD1 TRP C1138    11825  14078   7764    617  -1231    387       C  
ATOM   9470  CD2 TRP C1138     -58.330  42.748  89.069  1.00 85.05           C  
ANISOU 9470  CD2 TRP C1138    11447  13673   7194    437  -1241    236       C  
ATOM   9471  NE1 TRP C1138     -58.785  40.904  87.878  1.00 86.72           N  
ANISOU 9471  NE1 TRP C1138    11588  13767   7594    641  -1143    283       N  
ATOM   9472  CE2 TRP C1138     -58.807  42.273  87.826  1.00 87.74           C  
ANISOU 9472  CE2 TRP C1138    11761  13920   7654    530  -1153    206       C  
ATOM   9473  CE3 TRP C1138     -58.247  44.136  89.277  1.00 86.43           C  
ANISOU 9473  CE3 TRP C1138    11679  13862   7298    313  -1280    152       C  
ATOM   9474  CZ2 TRP C1138     -59.210  43.136  86.799  1.00 86.04           C  
ANISOU 9474  CZ2 TRP C1138    11576  13644   7473    497  -1110    119       C  
ATOM   9475  CZ3 TRP C1138     -58.640  44.991  88.256  1.00 86.96           C  
ANISOU 9475  CZ3 TRP C1138    11772  13838   7429    290  -1240     69       C  
ATOM   9476  CH2 TRP C1138     -59.109  44.491  87.032  1.00 86.50           C  
ANISOU 9476  CH2 TRP C1138    11686  13707   7474    378  -1160     65       C  
ATOM   9477  N   TYR C1139     -54.524  42.225  90.395  1.00 91.42           N  
ANISOU 9477  N   TYR C1139    11901  14850   7983    374  -1589    535       N  
ATOM   9478  CA  TYR C1139     -53.503  42.560  89.407  1.00 91.92           C  
ANISOU 9478  CA  TYR C1139    11791  14986   8149    372  -1583    530       C  
ATOM   9479  C   TYR C1139     -52.262  41.696  89.617  1.00 97.82           C  
ANISOU 9479  C   TYR C1139    12328  15841   8998    456  -1682    655       C  
ATOM   9480  O   TYR C1139     -51.697  41.207  88.639  1.00 97.94           O  
ANISOU 9480  O   TYR C1139    12175  15881   9156    564  -1614    646       O  
ATOM   9481  CB  TYR C1139     -53.149  44.060  89.465  1.00 93.89           C  
ANISOU 9481  CB  TYR C1139    12071  15291   8314    182  -1636    473       C  
ATOM   9482  CG  TYR C1139     -52.087  44.481  88.468  1.00 97.20           C  
ANISOU 9482  CG  TYR C1139    12304  15809   8819    136  -1625    489       C  
ATOM   9483  CD1 TYR C1139     -52.436  44.964  87.211  1.00 98.46           C  
ANISOU 9483  CD1 TYR C1139    12481  15917   9014    116  -1506    422       C  
ATOM   9484  CD2 TYR C1139     -50.733  44.406  88.786  1.00100.13           C  
ANISOU 9484  CD2 TYR C1139    12474  16343   9228     96  -1737    583       C  
ATOM   9485  CE1 TYR C1139     -51.464  45.345  86.287  1.00101.01           C  
ANISOU 9485  CE1 TYR C1139    12633  16361   9386     46  -1478    449       C  
ATOM   9486  CE2 TYR C1139     -49.752  44.774  87.868  1.00102.14           C  
ANISOU 9486  CE2 TYR C1139    12530  16719   9560     41  -1704    599       C  
ATOM   9487  CZ  TYR C1139     -50.122  45.252  86.622  1.00110.19           C  
ANISOU 9487  CZ  TYR C1139    13579  17698  10589      7  -1565    533       C  
ATOM   9488  OH  TYR C1139     -49.155  45.627  85.720  1.00113.92           O  
ANISOU 9488  OH  TYR C1139    13856  18320  11107    -76  -1517    560       O  
ATOM   9489  N   ASN C1140     -51.831  41.535  90.890  1.00 95.71           N  
ANISOU 9489  N   ASN C1140    12066  15647   8654    405  -1846    764       N  
ATOM   9490  CA  ASN C1140     -50.663  40.747  91.289  1.00 97.23           C  
ANISOU 9490  CA  ASN C1140    12058  15934   8952    481  -1991    908       C  
ATOM   9491  C   ASN C1140     -50.810  39.277  90.873  1.00100.48           C  
ANISOU 9491  C   ASN C1140    12400  16233   9546    707  -1946    958       C  
ATOM   9492  O   ASN C1140     -49.840  38.681  90.400  1.00100.95           O  
ANISOU 9492  O   ASN C1140    12229  16338   9792    836  -1972    995       O  
ATOM   9493  CB  ASN C1140     -50.423  40.884  92.796  1.00100.48           C  
ANISOU 9493  CB  ASN C1140    12546  16430   9202    359  -2192   1023       C  
ATOM   9494  CG  ASN C1140     -49.229  40.117  93.324  1.00137.80           C  
ANISOU 9494  CG  ASN C1140    17068  21252  14038    426  -2390   1200       C  
ATOM   9495  OD1 ASN C1140     -48.107  40.218  92.811  1.00140.04           O  
ANISOU 9495  OD1 ASN C1140    17102  21637  14469    458  -2430   1216       O  
ATOM   9496  ND2 ASN C1140     -49.445  39.346  94.383  1.00129.89           N  
ANISOU 9496  ND2 ASN C1140    16158  20229  12967    440  -2527   1349       N  
ATOM   9497  N   GLN C1141     -52.035  38.721  91.006  1.00 96.08           N  
ANISOU 9497  N   GLN C1141    12032  15524   8951    752  -1871    945       N  
ATOM   9498  CA  GLN C1141     -52.360  37.337  90.652  1.00 96.31           C  
ANISOU 9498  CA  GLN C1141    12041  15401   9151    942  -1838    985       C  
ATOM   9499  C   GLN C1141     -52.507  37.135  89.127  1.00 99.37           C  
ANISOU 9499  C   GLN C1141    12355  15718   9683   1065  -1657    829       C  
ATOM   9500  O   GLN C1141     -51.847  36.252  88.572  1.00100.15           O  
ANISOU 9500  O   GLN C1141    12286  15786   9981   1237  -1656    828       O  
ATOM   9501  CB  GLN C1141     -53.605  36.857  91.421  1.00 97.18           C  
ANISOU 9501  CB  GLN C1141    12376  15394   9155    904  -1835   1045       C  
ATOM   9502  CG  GLN C1141     -53.654  35.344  91.658  1.00120.07           C  
ANISOU 9502  CG  GLN C1141    15259  18147  12216   1051  -1916   1187       C  
ATOM   9503  CD  GLN C1141     -54.711  34.921  92.660  1.00144.94           C  
ANISOU 9503  CD  GLN C1141    18615  21230  15226    958  -1946   1303       C  
ATOM   9504  OE1 GLN C1141     -55.817  35.477  92.732  1.00139.44           O  
ANISOU 9504  OE1 GLN C1141    18074  20531  14375    849  -1818   1211       O  
ATOM   9505  NE2 GLN C1141     -54.393  33.910  93.461  1.00140.91           N  
ANISOU 9505  NE2 GLN C1141    18099  20667  14774    996  -2119   1517       N  
ATOM   9506  N   THR C1142     -53.349  37.957  88.457  1.00 93.88           N  
ANISOU 9506  N   THR C1142    11782  15001   8887    978  -1514    693       N  
ATOM   9507  CA  THR C1142     -53.585  37.884  87.006  1.00 92.60           C  
ANISOU 9507  CA  THR C1142    11586  14794   8806   1053  -1352    550       C  
ATOM   9508  C   THR C1142     -53.141  39.201  86.334  1.00 95.56           C  
ANISOU 9508  C   THR C1142    11907  15306   9093    918  -1294    475       C  
ATOM   9509  O   THR C1142     -53.981  40.068  86.082  1.00 93.71           O  
ANISOU 9509  O   THR C1142    11822  15032   8751    806  -1238    409       O  
ATOM   9510  CB  THR C1142     -55.054  37.529  86.696  1.00 99.09           C  
ANISOU 9510  CB  THR C1142    12597  15442   9610   1073  -1260    485       C  
ATOM   9511  OG1 THR C1142     -55.909  38.538  87.243  1.00 95.85           O  
ANISOU 9511  OG1 THR C1142    12348  15034   9034    917  -1256    470       O  
ATOM   9512  CG2 THR C1142     -55.451  36.148  87.212  1.00 99.87           C  
ANISOU 9512  CG2 THR C1142    12738  15390   9819   1192  -1314    570       C  
ATOM   9513  N   PRO C1143     -51.833  39.383  86.043  1.00 92.93           N  
ANISOU 9513  N   PRO C1143    11355  15133   8820    919  -1315    493       N  
ATOM   9514  CA  PRO C1143     -51.386  40.658  85.459  1.00 92.23           C  
ANISOU 9514  CA  PRO C1143    11219  15179   8645    752  -1273    453       C  
ATOM   9515  C   PRO C1143     -51.844  40.948  84.035  1.00 94.35           C  
ANISOU 9515  C   PRO C1143    11526  15435   8887    737  -1108    339       C  
ATOM   9516  O   PRO C1143     -52.109  42.109  83.731  1.00 93.50           O  
ANISOU 9516  O   PRO C1143    11508  15344   8673    568  -1097    325       O  
ATOM   9517  CB  PRO C1143     -49.866  40.584  85.572  1.00 96.30           C  
ANISOU 9517  CB  PRO C1143    11458  15882   9251    764  -1337    517       C  
ATOM   9518  CG  PRO C1143     -49.559  39.129  85.554  1.00102.24           C  
ANISOU 9518  CG  PRO C1143    12081  16581  10183   1003  -1336    525       C  
ATOM   9519  CD  PRO C1143     -50.693  38.472  86.279  1.00 96.69           C  
ANISOU 9519  CD  PRO C1143    11603  15676   9461   1063  -1390    562       C  
ATOM   9520  N   ASN C1144     -51.928  39.912  83.172  1.00 90.30           N  
ANISOU 9520  N   ASN C1144    10955  14886   8471    904   -995    258       N  
ATOM   9521  CA  ASN C1144     -52.323  40.057  81.761  1.00 88.97           C  
ANISOU 9521  CA  ASN C1144    10823  14729   8252    889   -842    144       C  
ATOM   9522  C   ASN C1144     -53.776  40.488  81.566  1.00 89.71           C  
ANISOU 9522  C   ASN C1144    11170  14661   8253    818   -832    112       C  
ATOM   9523  O   ASN C1144     -54.034  41.413  80.794  1.00 88.57           O  
ANISOU 9523  O   ASN C1144    11091  14554   8009    682   -791     91       O  
ATOM   9524  CB  ASN C1144     -52.001  38.795  80.964  1.00 87.67           C  
ANISOU 9524  CB  ASN C1144    10534  14569   8209   1091   -731     36       C  
ATOM   9525  CG  ASN C1144     -50.549  38.415  81.024  1.00 95.42           C  
ANISOU 9525  CG  ASN C1144    11225  15720   9310   1180   -724     45       C  
ATOM   9526  OD1 ASN C1144     -49.651  39.246  80.858  1.00 82.22           O  
ANISOU 9526  OD1 ASN C1144     9402  14251   7586   1049   -709     84       O  
ATOM   9527  ND2 ASN C1144     -50.290  37.147  81.275  1.00 89.35           N  
ANISOU 9527  ND2 ASN C1144    10361  14862   8725   1402   -747     16       N  
ATOM   9528  N   ARG C1145     -54.713  39.835  82.286  1.00 84.39           N  
ANISOU 9528  N   ARG C1145    10628  13814   7623    901   -881    123       N  
ATOM   9529  CA  ARG C1145     -56.145  40.128  82.254  1.00 81.82           C  
ANISOU 9529  CA  ARG C1145    10509  13336   7242    854   -877     92       C  
ATOM   9530  C   ARG C1145     -56.438  41.489  82.900  1.00 85.23           C  
ANISOU 9530  C   ARG C1145    11038  13771   7576    688   -950    134       C  
ATOM   9531  O   ARG C1145     -57.133  42.303  82.291  1.00 83.95           O  
ANISOU 9531  O   ARG C1145    10978  13558   7361    601   -931     96       O  
ATOM   9532  CB  ARG C1145     -56.934  39.008  82.954  1.00 79.45           C  
ANISOU 9532  CB  ARG C1145    10286  12879   7021    971   -904    109       C  
ATOM   9533  CG  ARG C1145     -58.451  39.120  82.833  1.00 81.49           C  
ANISOU 9533  CG  ARG C1145    10718  12991   7254    939   -882     67       C  
ATOM   9534  CD  ARG C1145     -59.093  37.789  83.142  1.00 83.55           C  
ANISOU 9534  CD  ARG C1145    11020  13110   7616   1053   -884     77       C  
ATOM   9535  NE  ARG C1145     -60.551  37.858  83.203  1.00 83.92           N  
ANISOU 9535  NE  ARG C1145    11202  13034   7650   1010   -868     53       N  
ATOM   9536  CZ  ARG C1145     -61.328  36.824  83.508  1.00 95.58           C  
ANISOU 9536  CZ  ARG C1145    12731  14379   9206   1064   -872     75       C  
ATOM   9537  NH1 ARG C1145     -60.791  35.640  83.783  1.00 83.39           N  
ANISOU 9537  NH1 ARG C1145    11136  12780   7767   1169   -907    126       N  
ATOM   9538  NH2 ARG C1145     -62.646  36.965  83.548  1.00 79.50           N  
ANISOU 9538  NH2 ARG C1145    10786  12257   7163   1011   -851     52       N  
ATOM   9539  N   ALA C1146     -55.890  41.737  84.116  1.00 82.60           N  
ANISOU 9539  N   ALA C1146    10674  13490   7221    646  -1047    208       N  
ATOM   9540  CA  ALA C1146     -56.094  42.979  84.870  1.00 81.88           C  
ANISOU 9540  CA  ALA C1146    10679  13393   7038    495  -1124    218       C  
ATOM   9541  C   ALA C1146     -55.667  44.229  84.118  1.00 85.60           C  
ANISOU 9541  C   ALA C1146    11135  13919   7469    346  -1131    208       C  
ATOM   9542  O   ALA C1146     -56.457  45.166  84.051  1.00 84.31           O  
ANISOU 9542  O   ALA C1146    11109  13653   7273    262  -1151    168       O  
ATOM   9543  CB  ALA C1146     -55.411  42.911  86.224  1.00 83.47           C  
ANISOU 9543  CB  ALA C1146    10840  13672   7204    467  -1236    294       C  
ATOM   9544  N   LYS C1147     -54.455  44.228  83.514  1.00 83.15           N  
ANISOU 9544  N   LYS C1147    10653  13766   7174    315  -1112    247       N  
ATOM   9545  CA  LYS C1147     -53.915  45.357  82.746  1.00 83.48           C  
ANISOU 9545  CA  LYS C1147    10662  13887   7172    143  -1115    271       C  
ATOM   9546  C   LYS C1147     -54.853  45.770  81.591  1.00 85.63           C  
ANISOU 9546  C   LYS C1147    11062  14061   7413    106  -1054    231       C  
ATOM   9547  O   LYS C1147     -55.080  46.965  81.392  1.00 84.69           O  
ANISOU 9547  O   LYS C1147    11037  13881   7259    -48  -1118    255       O  
ATOM   9548  CB  LYS C1147     -52.494  45.047  82.246  1.00 87.93           C  
ANISOU 9548  CB  LYS C1147    10981  14667   7760    133  -1069    315       C  
ATOM   9549  CG  LYS C1147     -51.669  46.282  81.907  1.00109.30           C  
ANISOU 9549  CG  LYS C1147    13620  17491  10418    -95  -1111    382       C  
ATOM   9550  CD  LYS C1147     -50.230  45.913  81.553  1.00124.05           C  
ANISOU 9550  CD  LYS C1147    15203  19607  12325   -101  -1054    423       C  
ATOM   9551  CE  LYS C1147     -49.499  47.006  80.802  1.00136.62           C  
ANISOU 9551  CE  LYS C1147    16713  21341  13855   -343  -1042    495       C  
ATOM   9552  NZ  LYS C1147     -49.043  48.108  81.693  1.00145.43           N  
ANISOU 9552  NZ  LYS C1147    17848  22441  14968   -542  -1215    574       N  
ATOM   9553  N   ARG C1148     -55.431  44.780  80.879  1.00 81.46           N  
ANISOU 9553  N   ARG C1148    10547  13499   6906    244   -955    174       N  
ATOM   9554  CA  ARG C1148     -56.378  45.009  79.785  1.00 80.80           C  
ANISOU 9554  CA  ARG C1148    10584  13330   6786    218   -915    139       C  
ATOM   9555  C   ARG C1148     -57.670  45.660  80.312  1.00 85.00           C  
ANISOU 9555  C   ARG C1148    11296  13657   7343    200   -999    120       C  
ATOM   9556  O   ARG C1148     -58.102  46.674  79.762  1.00 85.00           O  
ANISOU 9556  O   ARG C1148    11389  13585   7322     84  -1053    144       O  
ATOM   9557  CB  ARG C1148     -56.696  43.698  79.045  1.00 79.65           C  
ANISOU 9557  CB  ARG C1148    10414  13189   6662    374   -806     60       C  
ATOM   9558  CG  ARG C1148     -55.608  43.243  78.074  1.00 87.54           C  
ANISOU 9558  CG  ARG C1148    11250  14390   7620    382   -692     35       C  
ATOM   9559  CD  ARG C1148     -56.032  42.060  77.209  1.00 88.99           C  
ANISOU 9559  CD  ARG C1148    11446  14554   7814    523   -589    -81       C  
ATOM   9560  NE  ARG C1148     -56.214  40.824  77.978  1.00 89.24           N  
ANISOU 9560  NE  ARG C1148    11452  14476   7980    718   -594   -129       N  
ATOM   9561  CZ  ARG C1148     -55.319  39.843  78.058  1.00 99.03           C  
ANISOU 9561  CZ  ARG C1148    12529  15788   9308    860   -537   -177       C  
ATOM   9562  NH1 ARG C1148     -54.160  39.936  77.415  1.00 85.66           N  
ANISOU 9562  NH1 ARG C1148    10659  14307   7580    839   -444   -206       N  
ATOM   9563  NH2 ARG C1148     -55.574  38.763  78.782  1.00 83.06           N  
ANISOU 9563  NH2 ARG C1148    10511  13627   7420   1021   -574   -190       N  
ATOM   9564  N   VAL C1149     -58.255  45.097  81.397  1.00 81.21           N  
ANISOU 9564  N   VAL C1149    10856  13089   6912    308  -1012     83       N  
ATOM   9565  CA  VAL C1149     -59.480  45.587  82.052  1.00 80.14           C  
ANISOU 9565  CA  VAL C1149    10856  12788   6805    312  -1059     38       C  
ATOM   9566  C   VAL C1149     -59.264  47.006  82.619  1.00 85.25           C  
ANISOU 9566  C   VAL C1149    11558  13398   7434    176  -1158     44       C  
ATOM   9567  O   VAL C1149     -60.139  47.862  82.475  1.00 84.85           O  
ANISOU 9567  O   VAL C1149    11612  13203   7424    140  -1206      5       O  
ATOM   9568  CB  VAL C1149     -60.018  44.589  83.123  1.00 83.32           C  
ANISOU 9568  CB  VAL C1149    11269  13154   7234    432  -1029     11       C  
ATOM   9569  CG1 VAL C1149     -61.302  45.100  83.771  1.00 82.72           C  
ANISOU 9569  CG1 VAL C1149    11305  12944   7180    433  -1044    -55       C  
ATOM   9570  CG2 VAL C1149     -60.253  43.204  82.525  1.00 82.69           C  
ANISOU 9570  CG2 VAL C1149    11149  13067   7202    558   -954      3       C  
ATOM   9571  N   ILE C1150     -58.087  47.251  83.230  1.00 83.18           N  
ANISOU 9571  N   ILE C1150    11219  13256   7131    101  -1203     88       N  
ATOM   9572  CA  ILE C1150     -57.695  48.549  83.789  1.00 84.05           C  
ANISOU 9572  CA  ILE C1150    11377  13335   7224    -49  -1313     87       C  
ATOM   9573  C   ILE C1150     -57.628  49.588  82.665  1.00 88.07           C  
ANISOU 9573  C   ILE C1150    11922  13788   7752   -184  -1359    137       C  
ATOM   9574  O   ILE C1150     -58.268  50.635  82.778  1.00 87.68           O  
ANISOU 9574  O   ILE C1150    11995  13568   7751   -245  -1444     98       O  
ATOM   9575  CB  ILE C1150     -56.377  48.436  84.622  1.00 88.33           C  
ANISOU 9575  CB  ILE C1150    11805  14040   7717   -109  -1364    138       C  
ATOM   9576  CG1 ILE C1150     -56.650  47.769  85.992  1.00 88.59           C  
ANISOU 9576  CG1 ILE C1150    11866  14083   7710    -19  -1372     98       C  
ATOM   9577  CG2 ILE C1150     -55.678  49.799  84.798  1.00 90.47           C  
ANISOU 9577  CG2 ILE C1150    12094  14304   7976   -309  -1487    161       C  
ATOM   9578  CD1 ILE C1150     -55.456  47.068  86.636  1.00 97.48           C  
ANISOU 9578  CD1 ILE C1150    12848  15383   8805    -10  -1414    181       C  
ATOM   9579  N   THR C1151     -56.898  49.271  81.567  1.00 84.95           N  
ANISOU 9579  N   THR C1151    11422  13534   7321   -228  -1302    220       N  
ATOM   9580  CA  THR C1151     -56.754  50.152  80.396  1.00 85.35           C  
ANISOU 9580  CA  THR C1151    11503  13574   7352   -386  -1338    304       C  
ATOM   9581  C   THR C1151     -58.079  50.414  79.681  1.00 86.14           C  
ANISOU 9581  C   THR C1151    11746  13491   7491   -349  -1363    285       C  
ATOM   9582  O   THR C1151     -58.241  51.480  79.088  1.00 86.06           O  
ANISOU 9582  O   THR C1151    11820  13379   7498   -489  -1463    356       O  
ATOM   9583  CB  THR C1151     -55.618  49.710  79.461  1.00 97.91           C  
ANISOU 9583  CB  THR C1151    12932  15406   8864   -452  -1243    383       C  
ATOM   9584  OG1 THR C1151     -55.756  48.321  79.158  1.00 98.48           O  
ANISOU 9584  OG1 THR C1151    12929  15565   8924   -269  -1109    320       O  
ATOM   9585  CG2 THR C1151     -54.238  49.999  80.048  1.00 98.53           C  
ANISOU 9585  CG2 THR C1151    12860  15645   8933   -566  -1276    439       C  
ATOM   9586  N   THR C1152     -59.035  49.462  79.771  1.00 80.39           N  
ANISOU 9586  N   THR C1152    11042  12710   6793   -170  -1293    201       N  
ATOM   9587  CA  THR C1152     -60.380  49.617  79.211  1.00 79.37           C  
ANISOU 9587  CA  THR C1152    11024  12410   6723   -118  -1328    174       C  
ATOM   9588  C   THR C1152     -61.104  50.693  80.044  1.00 83.01           C  
ANISOU 9588  C   THR C1152    11586  12659   7295   -127  -1442    117       C  
ATOM   9589  O   THR C1152     -61.712  51.590  79.465  1.00 82.65           O  
ANISOU 9589  O   THR C1152    11627  12456   7319   -184  -1549    152       O  
ATOM   9590  CB  THR C1152     -61.121  48.260  79.140  1.00 85.34           C  
ANISOU 9590  CB  THR C1152    11757  13180   7490     56  -1225    100       C  
ATOM   9591  OG1 THR C1152     -60.282  47.283  78.517  1.00 84.14           O  
ANISOU 9591  OG1 THR C1152    11505  13213   7253     77  -1120    118       O  
ATOM   9592  CG2 THR C1152     -62.433  48.348  78.367  1.00 83.27           C  
ANISOU 9592  CG2 THR C1152    11581  12774   7285     90  -1270     88       C  
ATOM   9593  N   PHE C1153     -60.969  50.638  81.395  1.00 79.73           N  
ANISOU 9593  N   PHE C1153    11159  12246   6891    -77  -1426     30       N  
ATOM   9594  CA  PHE C1153     -61.540  51.623  82.327  1.00 79.88           C  
ANISOU 9594  CA  PHE C1153    11267  12090   6994    -79  -1509    -72       C  
ATOM   9595  C   PHE C1153     -60.830  52.972  82.221  1.00 84.97           C  
ANISOU 9595  C   PHE C1153    11963  12657   7663   -258  -1649    -19       C  
ATOM   9596  O   PHE C1153     -61.443  54.007  82.469  1.00 85.32           O  
ANISOU 9596  O   PHE C1153    12105  12488   7823   -271  -1752    -88       O  
ATOM   9597  CB  PHE C1153     -61.444  51.131  83.777  1.00 81.33           C  
ANISOU 9597  CB  PHE C1153    11429  12348   7125    -10  -1446   -175       C  
ATOM   9598  CG  PHE C1153     -62.529  50.198  84.256  1.00 81.91           C  
ANISOU 9598  CG  PHE C1153    11495  12412   7213    148  -1339   -258       C  
ATOM   9599  CD1 PHE C1153     -63.873  50.506  84.060  1.00 84.82           C  
ANISOU 9599  CD1 PHE C1153    11910  12618   7701    228  -1340   -339       C  
ATOM   9600  CD2 PHE C1153     -62.214  49.060  84.985  1.00 83.49           C  
ANISOU 9600  CD2 PHE C1153    11637  12761   7324    207  -1252   -249       C  
ATOM   9601  CE1 PHE C1153     -64.878  49.663  84.543  1.00 84.97           C  
ANISOU 9601  CE1 PHE C1153    11902  12647   7737    351  -1234   -411       C  
ATOM   9602  CE2 PHE C1153     -63.219  48.218  85.463  1.00 85.68           C  
ANISOU 9602  CE2 PHE C1153    11912  13029   7614    321  -1159   -304       C  
ATOM   9603  CZ  PHE C1153     -64.543  48.525  85.239  1.00 83.64           C  
ANISOU 9603  CZ  PHE C1153    11687  12630   7462    385  -1141   -388       C  
ATOM   9604  N   ARG C1154     -59.533  52.951  81.874  1.00 81.96           N  
ANISOU 9604  N   ARG C1154    11507  12444   7192   -395  -1653     98       N  
ATOM   9605  CA  ARG C1154     -58.691  54.133  81.724  1.00 83.20           C  
ANISOU 9605  CA  ARG C1154    11691  12560   7362   -605  -1783    181       C  
ATOM   9606  C   ARG C1154     -59.037  54.901  80.437  1.00 87.73           C  
ANISOU 9606  C   ARG C1154    12340  13004   7989   -712  -1877    307       C  
ATOM   9607  O   ARG C1154     -59.195  56.123  80.485  1.00 88.60           O  
ANISOU 9607  O   ARG C1154    12557  12900   8206   -818  -2034    321       O  
ATOM   9608  CB  ARG C1154     -57.204  53.714  81.719  1.00 83.70           C  
ANISOU 9608  CB  ARG C1154    11604  12885   7312   -714  -1736    277       C  
ATOM   9609  CG  ARG C1154     -56.205  54.824  82.037  1.00 96.48           C  
ANISOU 9609  CG  ARG C1154    13224  14492   8942   -939  -1871    336       C  
ATOM   9610  CD  ARG C1154     -54.774  54.408  81.716  1.00110.72           C  
ANISOU 9610  CD  ARG C1154    14837  16578  10652  -1057  -1816    458       C  
ATOM   9611  NE  ARG C1154     -54.215  53.479  82.703  1.00123.27           N  
ANISOU 9611  NE  ARG C1154    16304  18339  12194   -949  -1754    395       N  
ATOM   9612  CZ  ARG C1154     -53.357  53.815  83.666  1.00139.08           C  
ANISOU 9612  CZ  ARG C1154    18254  20406  14185  -1050  -1847    387       C  
ATOM   9613  NH1 ARG C1154     -52.943  55.073  83.788  1.00128.75           N  
ANISOU 9613  NH1 ARG C1154    17008  18996  12914  -1268  -1998    420       N  
ATOM   9614  NH2 ARG C1154     -52.908  52.901  84.513  1.00123.62           N  
ANISOU 9614  NH2 ARG C1154    16188  18602  12181   -945  -1810    354       N  
ATOM   9615  N   THR C1155     -59.156  54.188  79.297  1.00 83.55           N  
ANISOU 9615  N   THR C1155    11766  12596   7385   -691  -1794    397       N  
ATOM   9616  CA  THR C1155     -59.389  54.790  77.980  1.00 84.36           C  
ANISOU 9616  CA  THR C1155    11939  12632   7483   -821  -1882    548       C  
ATOM   9617  C   THR C1155     -60.826  54.788  77.455  1.00 88.19           C  
ANISOU 9617  C   THR C1155    12519  12927   8062   -700  -1938    524       C  
ATOM   9618  O   THR C1155     -61.170  55.639  76.631  1.00 89.35           O  
ANISOU 9618  O   THR C1155    12760  12929   8258   -812  -2087    650       O  
ATOM   9619  CB  THR C1155     -58.413  54.211  76.942  1.00 91.14           C  
ANISOU 9619  CB  THR C1155    12689  13778   8161   -938  -1770    676       C  
ATOM   9620  OG1 THR C1155     -58.627  52.803  76.827  1.00 87.79           O  
ANISOU 9620  OG1 THR C1155    12181  13508   7666   -756  -1600    583       O  
ATOM   9621  CG2 THR C1155     -56.953  54.509  77.277  1.00 90.61           C  
ANISOU 9621  CG2 THR C1155    12508  13885   8032  -1108  -1753    742       C  
ATOM   9622  N   GLY C1156     -61.633  53.824  77.892  1.00 82.89           N  
ANISOU 9622  N   GLY C1156    11814  12263   7416   -488  -1834    385       N  
ATOM   9623  CA  GLY C1156     -63.014  53.678  77.434  1.00 82.05           C  
ANISOU 9623  CA  GLY C1156    11761  12006   7407   -366  -1878    353       C  
ATOM   9624  C   GLY C1156     -63.120  53.192  76.000  1.00 85.32           C  
ANISOU 9624  C   GLY C1156    12183  12532   7704   -425  -1869    475       C  
ATOM   9625  O   GLY C1156     -64.172  53.340  75.375  1.00 85.03           O  
ANISOU 9625  O   GLY C1156    12205  12360   7743   -385  -1968    504       O  
ATOM   9626  N   THR C1157     -62.020  52.613  75.471  1.00 81.84           N  
ANISOU 9626  N   THR C1157    11672  12349   7074   -520  -1753    539       N  
ATOM   9627  CA  THR C1157     -61.889  52.087  74.109  1.00 82.22           C  
ANISOU 9627  CA  THR C1157    11721  12565   6952   -598  -1706    628       C  
ATOM   9628  C   THR C1157     -61.492  50.617  74.122  1.00 85.80           C  
ANISOU 9628  C   THR C1157    12064  13237   7298   -476  -1501    514       C  
ATOM   9629  O   THR C1157     -60.836  50.160  75.062  1.00 84.59           O  
ANISOU 9629  O   THR C1157    11813  13160   7165   -401  -1402    435       O  
ATOM   9630  CB  THR C1157     -60.845  52.887  73.319  1.00 91.15           C  
ANISOU 9630  CB  THR C1157    12866  13820   7949   -856  -1749    810       C  
ATOM   9631  OG1 THR C1157     -59.583  52.812  73.984  1.00 88.27           O  
ANISOU 9631  OG1 THR C1157    12380  13614   7542   -904  -1645    789       O  
ATOM   9632  CG2 THR C1157     -61.256  54.341  73.094  1.00 92.75           C  
ANISOU 9632  CG2 THR C1157    13200  13776   8263  -1001  -1987    959       C  
ATOM   9633  N   TRP C1158     -61.842  49.891  73.046  1.00 83.34           N  
ANISOU 9633  N   TRP C1158    11773  13023   6872   -467  -1453    511       N  
ATOM   9634  CA  TRP C1158     -61.534  48.468  72.886  1.00 82.79           C  
ANISOU 9634  CA  TRP C1158    11615  13127   6715   -347  -1273    387       C  
ATOM   9635  C   TRP C1158     -60.053  48.180  72.640  1.00 89.04           C  
ANISOU 9635  C   TRP C1158    12282  14185   7364   -424  -1124    396       C  
ATOM   9636  O   TRP C1158     -59.651  47.018  72.701  1.00 88.71           O  
ANISOU 9636  O   TRP C1158    12143  14268   7296   -296   -975    276       O  
ATOM   9637  CB  TRP C1158     -62.420  47.830  71.804  1.00 81.53           C  
ANISOU 9637  CB  TRP C1158    11530  12971   6479   -323  -1285    355       C  
ATOM   9638  CG  TRP C1158     -63.864  47.760  72.204  1.00 81.37           C  
ANISOU 9638  CG  TRP C1158    11569  12714   6632   -200  -1395    308       C  
ATOM   9639  CD1 TRP C1158     -64.906  48.433  71.638  1.00 84.89           C  
ANISOU 9639  CD1 TRP C1158    12115  13010   7130   -253  -1572    390       C  
ATOM   9640  CD2 TRP C1158     -64.414  47.014  73.298  1.00 79.56           C  
ANISOU 9640  CD2 TRP C1158    11288  12384   6560    -13  -1339    182       C  
ATOM   9641  NE1 TRP C1158     -66.078  48.129  72.292  1.00 83.26           N  
ANISOU 9641  NE1 TRP C1158    11897  12624   7113    -98  -1616    303       N  
ATOM   9642  CE2 TRP C1158     -65.804  47.264  73.319  1.00 83.28           C  
ANISOU 9642  CE2 TRP C1158    11813  12661   7170     39  -1466    178       C  
ATOM   9643  CE3 TRP C1158     -63.869  46.139  74.252  1.00 79.71           C  
ANISOU 9643  CE3 TRP C1158    11213  12461   6614    109  -1202     86       C  
ATOM   9644  CZ2 TRP C1158     -66.653  46.683  74.263  1.00 81.49           C  
ANISOU 9644  CZ2 TRP C1158    11542  12321   7100    192  -1433     76       C  
ATOM   9645  CZ3 TRP C1158     -64.711  45.562  75.184  1.00 80.15           C  
ANISOU 9645  CZ3 TRP C1158    11251  12391   6812    250  -1189      5       C  
ATOM   9646  CH2 TRP C1158     -66.085  45.834  75.185  1.00 80.66           C  
ANISOU 9646  CH2 TRP C1158    11363  12286   6997    284  -1290     -4       C  
ATOM   9647  N   ASP C1159     -59.248  49.248  72.414  1.00 87.19           N  
ANISOU 9647  N   ASP C1159    12039  14024   7064   -629  -1173    538       N  
ATOM   9648  CA  ASP C1159     -57.801  49.268  72.146  1.00 88.45           C  
ANISOU 9648  CA  ASP C1159    12058  14452   7097   -754  -1050    582       C  
ATOM   9649  C   ASP C1159     -56.962  48.183  72.841  1.00 92.32           C  
ANISOU 9649  C   ASP C1159    12364  15086   7628   -587   -885    446       C  
ATOM   9650  O   ASP C1159     -56.103  47.581  72.196  1.00 92.63           O  
ANISOU 9650  O   ASP C1159    12275  15374   7547   -601   -725    404       O  
ATOM   9651  CB  ASP C1159     -57.227  50.670  72.423  1.00 91.33           C  
ANISOU 9651  CB  ASP C1159    12438  14773   7490   -971  -1175    749       C  
ATOM   9652  CG  ASP C1159     -57.738  51.782  71.515  1.00103.40           C  
ANISOU 9652  CG  ASP C1159    14129  16198   8959  -1183  -1341    930       C  
ATOM   9653  OD1 ASP C1159     -58.781  51.583  70.853  1.00104.50           O  
ANISOU 9653  OD1 ASP C1159    14389  16244   9071  -1137  -1401    926       O  
ATOM   9654  OD2 ASP C1159     -57.107  52.860  71.485  1.00109.37           O  
ANISOU 9654  OD2 ASP C1159    14894  16954   9708  -1403  -1431   1088       O  
ATOM   9655  N   ALA C1160     -57.238  47.914  74.136  1.00 88.93           N  
ANISOU 9655  N   ALA C1160    11920  14503   7367   -428   -926    375       N  
ATOM   9656  CA  ALA C1160     -56.551  46.902  74.951  1.00 89.15           C  
ANISOU 9656  CA  ALA C1160    11791  14620   7463   -262   -821    276       C  
ATOM   9657  C   ALA C1160     -56.680  45.491  74.358  1.00 94.95           C  
ANISOU 9657  C   ALA C1160    12479  15431   8168    -94   -681    141       C  
ATOM   9658  O   ALA C1160     -55.734  44.702  74.430  1.00 95.42           O  
ANISOU 9658  O   ALA C1160    12370  15649   8238     -5   -561     75       O  
ATOM   9659  CB  ALA C1160     -57.109  46.917  76.365  1.00 88.29           C  
ANISOU 9659  CB  ALA C1160    11730  14313   7503   -149   -914    243       C  
ATOM   9660  N   TYR C1161     -57.780  45.270  73.653  1.00 92.27           N  
ANISOU 9660  N   TYR C1161    12280  14986   7790    -72   -705    103       N  
ATOM   9661  CA  TYR C1161     -58.046  44.003  72.995  1.00 92.98           C  
ANISOU 9661  CA  TYR C1161    12363  15116   7848     64   -597    -38       C  
ATOM   9662  C   TYR C1161     -57.842  44.082  71.496  1.00101.54           C  
ANISOU 9662  C   TYR C1161    13474  16385   8720    -67   -521    -48       C  
ATOM   9663  O   TYR C1161     -57.263  43.185  70.906  1.00103.22           O  
ANISOU 9663  O   TYR C1161    13596  16763   8862      4   -367   -178       O  
ATOM   9664  CB  TYR C1161     -59.451  43.534  73.348  1.00 92.18           C  
ANISOU 9664  CB  TYR C1161    12391  14776   7858    182   -681    -90       C  
ATOM   9665  CG  TYR C1161     -59.658  43.500  74.844  1.00 91.42           C  
ANISOU 9665  CG  TYR C1161    12273  14532   7930    283   -739    -75       C  
ATOM   9666  CD1 TYR C1161     -59.704  42.299  75.533  1.00 92.48           C  
ANISOU 9666  CD1 TYR C1161    12354  14609   8173    461   -690   -159       C  
ATOM   9667  CD2 TYR C1161     -59.758  44.675  75.571  1.00 91.42           C  
ANISOU 9667  CD2 TYR C1161    12311  14453   7971    190   -846     22       C  
ATOM   9668  CE1 TYR C1161     -59.862  42.273  76.887  1.00 92.16           C  
ANISOU 9668  CE1 TYR C1161    12304  14468   8246    524   -741   -128       C  
ATOM   9669  CE2 TYR C1161     -59.919  44.654  76.927  1.00 91.21           C  
ANISOU 9669  CE2 TYR C1161    12273  14325   8056    266   -886     17       C  
ATOM   9670  CZ  TYR C1161     -59.968  43.453  77.574  1.00 97.31           C  
ANISOU 9670  CZ  TYR C1161    12996  15075   8903    425   -830    -48       C  
ATOM   9671  OH  TYR C1161     -60.124  43.433  78.924  1.00 95.47           O  
ANISOU 9671  OH  TYR C1161    12762  14767   8744    475   -870    -36       O  
ATOM   9672  N   GLY C1200     -58.276  45.151  70.880  1.00 95.28           N  
ANISOU 9672  N   GLY C1200    11976  12075  12151    113    -18    -82       N  
ATOM   9673  CA  GLY C1200     -57.964  45.389  69.485  1.00 95.66           C  
ANISOU 9673  CA  GLY C1200    12024  12124  12198    113    -17    -82       C  
ATOM   9674  C   GLY C1200     -56.829  46.039  68.954  1.00100.82           C  
ANISOU 9674  C   GLY C1200    12677  12777  12853    113    -16    -82       C  
ATOM   9675  O   GLY C1200     -57.113  46.854  67.968  1.00100.68           O  
ANISOU 9675  O   GLY C1200    12660  12760  12834    112    -15    -82       O  
ATOM   9676  N   SER C1201     -55.683  46.127  69.626  1.00 97.99           N  
ANISOU 9676  N   SER C1201    12318  12418  12495    113    -16    -83       N  
ATOM   9677  CA  SER C1201     -54.270  45.882  69.631  1.00 98.16           C  
ANISOU 9677  CA  SER C1201    12339  12440  12518    113    -16    -84       C  
ATOM   9678  C   SER C1201     -53.305  45.022  69.882  1.00103.22           C  
ANISOU 9678  C   SER C1201    12979  13080  13160    113    -16    -85       C  
ATOM   9679  O   SER C1201     -52.245  45.388  69.012  1.00103.78           O  
ANISOU 9679  O   SER C1201    13049  13150  13231    113    -15    -87       O  
ATOM   9680  CB  SER C1201     -53.604  46.721  70.700  1.00101.34           C  
ANISOU 9680  CB  SER C1201    12740  12842  12922    113    -16    -85       C  
ATOM   9681  N   LYS C 230     -53.694  43.765  69.407  1.00135.84           N  
ANISOU 9681  N   LYS C 230    24999  17324   9292  -3664   -628   -767       N  
ATOM   9682  CA  LYS C 230     -53.271  42.448  68.945  1.00133.33           C  
ANISOU 9682  CA  LYS C 230    24019  17327   9314  -3452   -818   -491       C  
ATOM   9683  C   LYS C 230     -53.695  42.208  67.500  1.00132.87           C  
ANISOU 9683  C   LYS C 230    23598  17147   9741  -3038   -685   -510       C  
ATOM   9684  O   LYS C 230     -52.859  41.954  66.632  1.00131.88           O  
ANISOU 9684  O   LYS C 230    23079  17200   9829  -3059   -878   -370       O  
ATOM   9685  CB  LYS C 230     -53.842  41.354  69.850  1.00136.43           C  
ANISOU 9685  CB  LYS C 230    24298  17833   9705  -3259   -753   -372       C  
ATOM   9686  N   GLY C 231     -54.997  42.290  67.250  1.00126.37           N  
ANISOU 9686  N   GLY C 231    22910  16021   9083  -2673   -350   -662       N  
ATOM   9687  CA  GLY C 231     -55.532  42.084  65.916  1.00121.96           C  
ANISOU 9687  CA  GLY C 231    22041  15345   8952  -2304   -214   -678       C  
ATOM   9688  C   GLY C 231     -55.612  43.370  65.119  1.00123.82           C  
ANISOU 9688  C   GLY C 231    22519  15331   9195  -2367   -100   -856       C  
ATOM   9689  O   GLY C 231     -56.622  43.649  64.473  1.00121.29           O  
ANISOU 9689  O   GLY C 231    22237  14760   9089  -2072    169   -947       O  
ATOM   9690  N   HIS C 232     -54.542  44.157  65.164  1.00121.51           N  
ANISOU 9690  N   HIS C 232    22376  15117   8675  -2761   -308   -882       N  
ATOM   9691  CA  HIS C 232     -54.490  45.427  64.440  1.00121.29           C  
ANISOU 9691  CA  HIS C 232    22577  14863   8643  -2856   -216  -1044       C  
ATOM   9692  C   HIS C 232     -53.444  45.376  63.335  1.00123.07           C  
ANISOU 9692  C   HIS C 232    22399  15288   9072  -2929   -472   -932       C  
ATOM   9693  O   HIS C 232     -53.610  46.048  62.317  1.00121.38           O  
ANISOU 9693  O   HIS C 232    22164  14917   9039  -2830   -368  -1020       O  
ATOM   9694  CB  HIS C 232     -54.085  46.574  65.391  1.00126.03           C  
ANISOU 9694  CB  HIS C 232    23758  15345   8781  -3301   -229  -1193       C  
ATOM   9695  CG  HIS C 232     -53.423  47.741  64.720  1.00130.35           C  
ANISOU 9695  CG  HIS C 232    24443  15799   9284  -3544   -294  -1291       C  
ATOM   9696  ND1 HIS C 232     -52.050  47.904  64.741  1.00133.63           N  
ANISOU 9696  ND1 HIS C 232    24759  16475   9541  -3940   -662  -1184       N  
ATOM   9697  CD2 HIS C 232     -53.972  48.759  64.015  1.00131.72           C  
ANISOU 9697  CD2 HIS C 232    24817  15656   9572  -3431    -30  -1454       C  
ATOM   9698  CE1 HIS C 232     -51.812  49.016  64.066  1.00133.57           C  
ANISOU 9698  CE1 HIS C 232    24913  16292   9547  -4056   -616  -1310       C  
ATOM   9699  NE2 HIS C 232     -52.937  49.564  63.610  1.00132.72           N  
ANISOU 9699  NE2 HIS C 232    24986  15838   9604  -3757   -234  -1476       N  
ATOM   9700  N   GLN C 233     -52.373  44.577  63.542  1.00119.25           N  
ANISOU 9700  N   GLN C 233    21587  15151   8571  -3095   -788   -712       N  
ATOM   9701  CA  GLN C 233     -51.296  44.368  62.573  1.00117.52           C  
ANISOU 9701  CA  GLN C 233    20950  15143   8558  -3151  -1026   -547       C  
ATOM   9702  C   GLN C 233     -51.790  43.274  61.615  1.00115.97           C  
ANISOU 9702  C   GLN C 233    20290  14984   8791  -2717   -917   -460       C  
ATOM   9703  O   GLN C 233     -51.497  43.330  60.418  1.00113.56           O  
ANISOU 9703  O   GLN C 233    19726  14683   8740  -2609   -937   -437       O  
ATOM   9704  CB  GLN C 233     -49.987  43.947  63.262  1.00121.24           C  
ANISOU 9704  CB  GLN C 233    21260  15963   8842  -3505  -1375   -294       C  
ATOM   9705  CG  GLN C 233     -48.728  44.329  62.478  1.00138.09           C  
ANISOU 9705  CG  GLN C 233    23165  18251  11053  -3716  -1626   -150       C  
ATOM   9706  CD  GLN C 233     -47.424  43.865  63.101  1.00161.67           C  
ANISOU 9706  CD  GLN C 233    25927  21604  13896  -4054  -1970    177       C  
ATOM   9707  OE1 GLN C 233     -46.430  43.642  62.398  1.00156.53           O  
ANISOU 9707  OE1 GLN C 233    24902  21137  13436  -4096  -2153    409       O  
ATOM   9708  NE2 GLN C 233     -47.368  43.742  64.425  1.00157.57           N  
ANISOU 9708  NE2 GLN C 233    25628  21206  13035  -4318  -2066    232       N  
ATOM   9709  N   LYS C 234     -52.567  42.304  62.149  1.00110.42           N  
ANISOU 9709  N   LYS C 234    19507  14294   8155  -2480   -791   -421       N  
ATOM   9710  CA  LYS C 234     -53.174  41.208  61.391  1.00106.42           C  
ANISOU 9710  CA  LYS C 234    18618  13799   8019  -2089   -663   -355       C  
ATOM   9711  C   LYS C 234     -54.292  41.740  60.484  1.00106.72           C  
ANISOU 9711  C   LYS C 234    18757  13556   8237  -1830   -404   -537       C  
ATOM   9712  O   LYS C 234     -54.470  41.239  59.372  1.00104.44           O  
ANISOU 9712  O   LYS C 234    18154  13278   8252  -1611   -357   -502       O  
ATOM   9713  CB  LYS C 234     -53.725  40.157  62.342  1.00109.00           C  
ANISOU 9713  CB  LYS C 234    18885  14199   8330  -1943   -599   -268       C  
ATOM   9714  N   ARG C 235     -55.027  42.765  60.958  1.00102.79           N  
ANISOU 9714  N   ARG C 235    18702  12806   7547  -1872   -225   -712       N  
ATOM   9715  CA  ARG C 235     -56.116  43.421  60.232  1.00100.53           C  
ANISOU 9715  CA  ARG C 235    18541  12244   7412  -1651     46   -840       C  
ATOM   9716  C   ARG C 235     -55.551  44.376  59.166  1.00101.84           C  
ANISOU 9716  C   ARG C 235    18681  12366   7647  -1768    -10   -899       C  
ATOM   9717  O   ARG C 235     -56.147  44.512  58.096  1.00 98.50           O  
ANISOU 9717  O   ARG C 235    18110  11844   7471  -1557    125   -917       O  
ATOM   9718  CB  ARG C 235     -57.026  44.167  61.222  1.00103.10           C  
ANISOU 9718  CB  ARG C 235    19361  12303   7511  -1657    297   -968       C  
ATOM   9719  CG  ARG C 235     -58.456  44.384  60.737  1.00113.81           C  
ANISOU 9719  CG  ARG C 235    20767  13397   9078  -1325    630  -1001       C  
ATOM   9720  CD  ARG C 235     -59.385  44.869  61.845  1.00127.72           C  
ANISOU 9720  CD  ARG C 235    22987  14898  10642  -1282    913  -1074       C  
ATOM   9721  NE  ARG C 235     -58.993  46.175  62.383  1.00140.17           N  
ANISOU 9721  NE  ARG C 235    25051  16295  11912  -1580    982  -1226       N  
ATOM   9722  CZ  ARG C 235     -58.511  46.371  63.608  1.00159.35           C  
ANISOU 9722  CZ  ARG C 235    27836  18741  13970  -1866    913  -1295       C  
ATOM   9723  NH1 ARG C 235     -58.366  45.350  64.445  1.00146.83           N  
ANISOU 9723  NH1 ARG C 235    26146  17359  12284  -1874    770  -1207       N  
ATOM   9724  NH2 ARG C 235     -58.178  47.590  64.007  1.00150.36           N  
ANISOU 9724  NH2 ARG C 235    27165  17416  12550  -2161    991  -1449       N  
ATOM   9725  N   LYS C 236     -54.407  45.039  59.471  1.00 99.64           N  
ANISOU 9725  N   LYS C 236    18542  12173   7143  -2118   -219   -910       N  
ATOM   9726  CA  LYS C 236     -53.712  45.960  58.567  1.00 98.73           C  
ANISOU 9726  CA  LYS C 236    18404  12037   7071  -2264   -307   -950       C  
ATOM   9727  C   LYS C 236     -53.115  45.189  57.407  1.00 98.27           C  
ANISOU 9727  C   LYS C 236    17846  12184   7308  -2141   -458   -809       C  
ATOM   9728  O   LYS C 236     -53.171  45.667  56.274  1.00 96.43           O  
ANISOU 9728  O   LYS C 236    17499  11883   7259  -2055   -406   -847       O  
ATOM   9729  CB  LYS C 236     -52.606  46.746  59.302  1.00104.47           C  
ANISOU 9729  CB  LYS C 236    19401  12828   7465  -2699   -520   -968       C  
ATOM   9730  CG  LYS C 236     -52.902  48.239  59.491  1.00123.32           C  
ANISOU 9730  CG  LYS C 236    22277  14923   9658  -2866   -344  -1171       C  
ATOM   9731  CD  LYS C 236     -52.679  49.060  58.208  1.00133.28           C  
ANISOU 9731  CD  LYS C 236    23418  16101  11121  -2830   -321  -1211       C  
ATOM   9732  CE  LYS C 236     -52.894  50.541  58.402  1.00146.06           C  
ANISOU 9732  CE  LYS C 236    25508  17423  12564  -3005   -130  -1395       C  
ATOM   9733  NZ  LYS C 236     -51.692  51.205  58.974  1.00157.69           N  
ANISOU 9733  NZ  LYS C 236    27214  18977  13725  -3467   -382  -1417       N  
ATOM   9734  N   ALA C 237     -52.570  43.981  57.692  1.00 93.32           N  
ANISOU 9734  N   ALA C 237    16925  11798   6733  -2126   -617   -636       N  
ATOM   9735  CA  ALA C 237     -51.982  43.076  56.701  1.00 90.86           C  
ANISOU 9735  CA  ALA C 237    16154  11668   6703  -2000   -716   -482       C  
ATOM   9736  C   ALA C 237     -53.033  42.666  55.672  1.00 91.61           C  
ANISOU 9736  C   ALA C 237    16084  11644   7078  -1667   -501   -546       C  
ATOM   9737  O   ALA C 237     -52.749  42.678  54.475  1.00 89.30           O  
ANISOU 9737  O   ALA C 237    15570  11376   6982  -1602   -514   -527       O  
ATOM   9738  CB  ALA C 237     -51.410  41.844  57.385  1.00 92.00           C  
ANISOU 9738  CB  ALA C 237    16058  12046   6851  -2018   -847   -275       C  
ATOM   9739  N   LEU C 238     -54.259  42.366  56.147  1.00 88.14           N  
ANISOU 9739  N   LEU C 238    15772  11076   6641  -1477   -303   -611       N  
ATOM   9740  CA  LEU C 238     -55.416  41.985  55.338  1.00 85.97           C  
ANISOU 9740  CA  LEU C 238    15374  10691   6599  -1189   -100   -646       C  
ATOM   9741  C   LEU C 238     -55.776  43.086  54.327  1.00 88.33           C  
ANISOU 9741  C   LEU C 238    15747  10840   6973  -1172      1   -739       C  
ATOM   9742  O   LEU C 238     -55.836  42.798  53.132  1.00 86.54           O  
ANISOU 9742  O   LEU C 238    15265  10657   6959  -1066     11   -712       O  
ATOM   9743  CB  LEU C 238     -56.612  41.628  56.254  1.00 86.46           C  
ANISOU 9743  CB  LEU C 238    15604  10635   6610  -1025     80   -667       C  
ATOM   9744  CG  LEU C 238     -57.953  41.319  55.584  1.00 89.82           C  
ANISOU 9744  CG  LEU C 238    15937  10938   7251   -748    293   -669       C  
ATOM   9745  CD1 LEU C 238     -57.934  39.967  54.885  1.00 88.29           C  
ANISOU 9745  CD1 LEU C 238    15367  10891   7288   -606    252   -578       C  
ATOM   9746  CD2 LEU C 238     -59.078  41.373  56.587  1.00 93.43           C  
ANISOU 9746  CD2 LEU C 238    16644  11233   7621   -620    486   -681       C  
ATOM   9747  N   LYS C 239     -55.959  44.339  54.798  1.00 85.56           N  
ANISOU 9747  N   LYS C 239    15748  10315   6444  -1294     82   -841       N  
ATOM   9748  CA  LYS C 239     -56.282  45.496  53.958  1.00 84.91           C  
ANISOU 9748  CA  LYS C 239    15755  10078   6431  -1287    205   -911       C  
ATOM   9749  C   LYS C 239     -55.194  45.766  52.909  1.00 87.86           C  
ANISOU 9749  C   LYS C 239    15907  10582   6893  -1407     19   -887       C  
ATOM   9750  O   LYS C 239     -55.520  45.928  51.731  1.00 85.49           O  
ANISOU 9750  O   LYS C 239    15426  10269   6790  -1290     86   -876       O  
ATOM   9751  CB  LYS C 239     -56.551  46.741  54.817  1.00 89.78           C  
ANISOU 9751  CB  LYS C 239    16826  10464   6822  -1419    351  -1022       C  
ATOM   9752  CG  LYS C 239     -58.016  47.166  54.810  1.00107.30           C  
ANISOU 9752  CG  LYS C 239    19203  12436   9131  -1196    688  -1032       C  
ATOM   9753  CD  LYS C 239     -58.505  47.643  56.179  1.00121.64           C  
ANISOU 9753  CD  LYS C 239    21472  14041  10705  -1249    876  -1107       C  
ATOM   9754  CE  LYS C 239     -59.249  46.570  56.946  1.00130.70           C  
ANISOU 9754  CE  LYS C 239    22592  15214  11855  -1069    941  -1041       C  
ATOM   9755  NZ  LYS C 239     -59.773  47.081  58.240  1.00142.77           N  
ANISOU 9755  NZ  LYS C 239    24585  16517  13145  -1109   1157  -1112       N  
ATOM   9756  N   THR C 240     -53.907  45.755  53.329  1.00 85.74           N  
ANISOU 9756  N   THR C 240    15633  10458   6486  -1641   -219   -851       N  
ATOM   9757  CA  THR C 240     -52.746  45.970  52.454  1.00 85.16           C  
ANISOU 9757  CA  THR C 240    15347  10519   6492  -1763   -410   -791       C  
ATOM   9758  C   THR C 240     -52.783  44.967  51.305  1.00 87.35           C  
ANISOU 9758  C   THR C 240    15236  10914   7039  -1562   -405   -705       C  
ATOM   9759  O   THR C 240     -52.664  45.360  50.146  1.00 86.33           O  
ANISOU 9759  O   THR C 240    14968  10781   7053  -1525   -394   -714       O  
ATOM   9760  CB  THR C 240     -51.433  45.858  53.251  1.00 92.97           C  
ANISOU 9760  CB  THR C 240    16351  11675   7297  -2035   -670   -693       C  
ATOM   9761  OG1 THR C 240     -51.512  46.657  54.431  1.00 95.47           O  
ANISOU 9761  OG1 THR C 240    17074  11881   7318  -2248   -663   -787       O  
ATOM   9762  CG2 THR C 240     -50.214  46.255  52.430  1.00 90.54           C  
ANISOU 9762  CG2 THR C 240    15857  11483   7061  -2176   -862   -605       C  
ATOM   9763  N   THR C 241     -52.995  43.683  51.636  1.00 83.02           N  
ANISOU 9763  N   THR C 241    14533  10459   6553  -1439   -394   -630       N  
ATOM   9764  CA  THR C 241     -53.081  42.592  50.679  1.00 80.83           C  
ANISOU 9764  CA  THR C 241    13935  10270   6508  -1266   -355   -562       C  
ATOM   9765  C   THR C 241     -54.241  42.842  49.731  1.00 83.95           C  
ANISOU 9765  C   THR C 241    14314  10547   7035  -1103   -175   -643       C  
ATOM   9766  O   THR C 241     -54.032  42.804  48.516  1.00 82.76           O  
ANISOU 9766  O   THR C 241    13975  10441   7028  -1073   -179   -630       O  
ATOM   9767  CB  THR C 241     -53.165  41.265  51.422  1.00 88.07           C  
ANISOU 9767  CB  THR C 241    14744  11276   7444  -1180   -348   -474       C  
ATOM   9768  OG1 THR C 241     -52.043  41.170  52.299  1.00 88.66           O  
ANISOU 9768  OG1 THR C 241    14818  11483   7386  -1363   -529   -357       O  
ATOM   9769  CG2 THR C 241     -53.177  40.077  50.490  1.00 85.76           C  
ANISOU 9769  CG2 THR C 241    14151  11052   7380  -1025   -283   -410       C  
ATOM   9770  N   VAL C 242     -55.433  43.173  50.284  1.00 81.11           N  
ANISOU 9770  N   VAL C 242    14158  10041   6619  -1014    -16   -702       N  
ATOM   9771  CA  VAL C 242     -56.644  43.489  49.519  1.00 80.16           C  
ANISOU 9771  CA  VAL C 242    14024   9813   6621   -870    164   -721       C  
ATOM   9772  C   VAL C 242     -56.366  44.602  48.485  1.00 83.81           C  
ANISOU 9772  C   VAL C 242    14462  10248   7135   -942    159   -746       C  
ATOM   9773  O   VAL C 242     -56.637  44.393  47.303  1.00 81.82           O  
ANISOU 9773  O   VAL C 242    14002  10051   7035   -878    186   -714       O  
ATOM   9774  CB  VAL C 242     -57.871  43.779  50.432  1.00 84.89           C  
ANISOU 9774  CB  VAL C 242    14863  10241   7150   -766    355   -733       C  
ATOM   9775  CG1 VAL C 242     -59.016  44.431  49.658  1.00 84.33           C  
ANISOU 9775  CG1 VAL C 242    14784  10052   7205   -650    546   -698       C  
ATOM   9776  CG2 VAL C 242     -58.358  42.507  51.113  1.00 84.27           C  
ANISOU 9776  CG2 VAL C 242    14722  10207   7089   -641    379   -685       C  
ATOM   9777  N   ILE C 243     -55.769  45.738  48.920  1.00 82.01           N  
ANISOU 9777  N   ILE C 243    14444   9945   6772  -1096    114   -801       N  
ATOM   9778  CA  ILE C 243     -55.417  46.862  48.038  1.00 82.15           C  
ANISOU 9778  CA  ILE C 243    14447   9929   6839  -1172    108   -823       C  
ATOM   9779  C   ILE C 243     -54.413  46.409  46.971  1.00 86.60           C  
ANISOU 9779  C   ILE C 243    14718  10672   7515  -1211    -62   -774       C  
ATOM   9780  O   ILE C 243     -54.641  46.674  45.792  1.00 85.78           O  
ANISOU 9780  O   ILE C 243    14455  10589   7546  -1159    -16   -756       O  
ATOM   9781  CB  ILE C 243     -54.937  48.133  48.811  1.00 87.18           C  
ANISOU 9781  CB  ILE C 243    15399  10433   7293  -1355    100   -900       C  
ATOM   9782  CG1 ILE C 243     -55.993  48.623  49.832  1.00 88.81           C  
ANISOU 9782  CG1 ILE C 243    15938  10419   7388  -1304    332   -952       C  
ATOM   9783  CG2 ILE C 243     -54.549  49.268  47.843  1.00 87.68           C  
ANISOU 9783  CG2 ILE C 243    15418  10462   7434  -1422     98   -913       C  
ATOM   9784  CD1 ILE C 243     -55.417  49.326  51.055  1.00 95.39           C  
ANISOU 9784  CD1 ILE C 243    17142  11147   7956  -1527    294  -1046       C  
ATOM   9785  N   LEU C 244     -53.333  45.702  47.379  1.00 84.16           N  
ANISOU 9785  N   LEU C 244    14330  10492   7156  -1300   -238   -728       N  
ATOM   9786  CA  LEU C 244     -52.286  45.192  46.479  1.00 83.50           C  
ANISOU 9786  CA  LEU C 244    13981  10560   7187  -1326   -368   -649       C  
ATOM   9787  C   LEU C 244     -52.847  44.278  45.380  1.00 85.56           C  
ANISOU 9787  C   LEU C 244    14016  10871   7622  -1169   -266   -632       C  
ATOM   9788  O   LEU C 244     -52.460  44.420  44.221  1.00 84.36           O  
ANISOU 9788  O   LEU C 244    13706  10771   7574  -1172   -284   -613       O  
ATOM   9789  CB  LEU C 244     -51.164  44.495  47.280  1.00 84.71           C  
ANISOU 9789  CB  LEU C 244    14081  10834   7271  -1428   -533   -544       C  
ATOM   9790  CG  LEU C 244     -49.970  43.893  46.515  1.00 89.38           C  
ANISOU 9790  CG  LEU C 244    14398  11567   7994  -1445   -639   -406       C  
ATOM   9791  CD1 LEU C 244     -49.225  44.944  45.691  1.00 89.72           C  
ANISOU 9791  CD1 LEU C 244    14403  11616   8069  -1543   -731   -396       C  
ATOM   9792  CD2 LEU C 244     -49.009  43.212  47.475  1.00 93.39           C  
ANISOU 9792  CD2 LEU C 244    14847  12196   8442  -1540   -775   -246       C  
ATOM   9793  N   ILE C 245     -53.769  43.368  45.743  1.00 81.89           N  
ANISOU 9793  N   ILE C 245    13552  10386   7176  -1050   -158   -638       N  
ATOM   9794  CA  ILE C 245     -54.420  42.466  44.794  1.00 80.69           C  
ANISOU 9794  CA  ILE C 245    13229  10272   7157   -939    -58   -630       C  
ATOM   9795  C   ILE C 245     -55.416  43.239  43.903  1.00 84.03           C  
ANISOU 9795  C   ILE C 245    13652  10644   7630   -907     43   -654       C  
ATOM   9796  O   ILE C 245     -55.342  43.117  42.678  1.00 83.23           O  
ANISOU 9796  O   ILE C 245    13395  10612   7617   -918     49   -643       O  
ATOM   9797  CB  ILE C 245     -55.020  41.208  45.505  1.00 83.69           C  
ANISOU 9797  CB  ILE C 245    13599  10652   7546   -838     13   -612       C  
ATOM   9798  CG1 ILE C 245     -53.999  40.051  45.551  1.00 84.37           C  
ANISOU 9798  CG1 ILE C 245    13530  10834   7691   -842    -37   -543       C  
ATOM   9799  CG2 ILE C 245     -56.318  40.719  44.856  1.00 83.46           C  
ANISOU 9799  CG2 ILE C 245    13514  10599   7599   -740    148   -622       C  
ATOM   9800  CD1 ILE C 245     -53.123  39.996  46.771  1.00 92.91           C  
ANISOU 9800  CD1 ILE C 245    14662  11960   8681   -909   -151   -470       C  
ATOM   9801  N   LEU C 246     -56.317  44.044  44.520  1.00 80.58           N  
ANISOU 9801  N   LEU C 246    13389  10088   7139   -874    137   -664       N  
ATOM   9802  CA  LEU C 246     -57.335  44.850  43.830  1.00 80.09           C  
ANISOU 9802  CA  LEU C 246    13317   9971   7142   -833    263   -627       C  
ATOM   9803  C   LEU C 246     -56.718  45.839  42.832  1.00 83.58           C  
ANISOU 9803  C   LEU C 246    13679  10450   7630   -915    213   -628       C  
ATOM   9804  O   LEU C 246     -57.266  46.022  41.744  1.00 82.22           O  
ANISOU 9804  O   LEU C 246    13360  10331   7549   -901    268   -570       O  
ATOM   9805  CB  LEU C 246     -58.227  45.604  44.846  1.00 81.16           C  
ANISOU 9805  CB  LEU C 246    13684   9935   7218   -773    411   -614       C  
ATOM   9806  CG  LEU C 246     -59.764  45.469  44.756  1.00 85.74           C  
ANISOU 9806  CG  LEU C 246    14241  10458   7881   -642    592   -505       C  
ATOM   9807  CD1 LEU C 246     -60.319  45.946  43.410  1.00 85.60           C  
ANISOU 9807  CD1 LEU C 246    14030  10505   7990   -646    647   -398       C  
ATOM   9808  CD2 LEU C 246     -60.249  44.078  45.142  1.00 87.41           C  
ANISOU 9808  CD2 LEU C 246    14391  10719   8100   -563    585   -484       C  
ATOM   9809  N   ALA C 247     -55.581  46.458  43.193  1.00 81.27           N  
ANISOU 9809  N   ALA C 247    13470  10141   7267  -1016    100   -675       N  
ATOM   9810  CA  ALA C 247     -54.892  47.399  42.314  1.00 81.50           C  
ANISOU 9810  CA  ALA C 247    13421  10201   7344  -1092     40   -671       C  
ATOM   9811  C   ALA C 247     -54.248  46.672  41.128  1.00 85.60           C  
ANISOU 9811  C   ALA C 247    13695  10875   7952  -1102    -47   -643       C  
ATOM   9812  O   ALA C 247     -54.327  47.172  40.005  1.00 84.91           O  
ANISOU 9812  O   ALA C 247    13479  10838   7945  -1111    -27   -614       O  
ATOM   9813  CB  ALA C 247     -53.854  48.193  43.089  1.00 83.35           C  
ANISOU 9813  CB  ALA C 247    13822  10377   7471  -1220    -70   -715       C  
ATOM   9814  N   PHE C 248     -53.653  45.479  41.372  1.00 82.45           N  
ANISOU 9814  N   PHE C 248    13238  10544   7544  -1097   -115   -640       N  
ATOM   9815  CA  PHE C 248     -53.014  44.637  40.355  1.00 81.85           C  
ANISOU 9815  CA  PHE C 248    12970  10577   7550  -1097   -145   -613       C  
ATOM   9816  C   PHE C 248     -53.981  44.256  39.238  1.00 85.22           C  
ANISOU 9816  C   PHE C 248    13292  11052   8038  -1064    -37   -615       C  
ATOM   9817  O   PHE C 248     -53.607  44.329  38.066  1.00 85.31           O  
ANISOU 9817  O   PHE C 248    13177  11136   8101  -1101    -46   -603       O  
ATOM   9818  CB  PHE C 248     -52.413  43.374  40.993  1.00 84.10           C  
ANISOU 9818  CB  PHE C 248    13231  10891   7831  -1075   -171   -584       C  
ATOM   9819  CG  PHE C 248     -51.756  42.396  40.039  1.00 85.67           C  
ANISOU 9819  CG  PHE C 248    13266  11159   8125  -1060   -138   -547       C  
ATOM   9820  CD1 PHE C 248     -50.402  42.494  39.740  1.00 89.50           C  
ANISOU 9820  CD1 PHE C 248    13657  11689   8660  -1100   -219   -465       C  
ATOM   9821  CD2 PHE C 248     -52.476  41.334  39.498  1.00 87.35           C  
ANISOU 9821  CD2 PHE C 248    13435  11380   8375  -1014    -10   -581       C  
ATOM   9822  CE1 PHE C 248     -49.790  41.570  38.887  1.00 90.44           C  
ANISOU 9822  CE1 PHE C 248    13648  11839   8877  -1069   -138   -416       C  
ATOM   9823  CE2 PHE C 248     -51.864  40.419  38.637  1.00 90.20           C  
ANISOU 9823  CE2 PHE C 248    13694  11769   8811  -1013     66   -562       C  
ATOM   9824  CZ  PHE C 248     -50.525  40.540  38.342  1.00 88.93           C  
ANISOU 9824  CZ  PHE C 248    13448  11632   8710  -1028     18   -478       C  
ATOM   9825  N   PHE C 249     -55.203  43.824  39.592  1.00 81.11           N  
ANISOU 9825  N   PHE C 249    12820  10498   7501  -1010     58   -616       N  
ATOM   9826  CA  PHE C 249     -56.182  43.428  38.586  1.00 80.24           C  
ANISOU 9826  CA  PHE C 249    12609  10452   7427  -1019    138   -588       C  
ATOM   9827  C   PHE C 249     -56.817  44.594  37.855  1.00 82.61           C  
ANISOU 9827  C   PHE C 249    12852  10777   7760  -1047    170   -520       C  
ATOM   9828  O   PHE C 249     -57.104  44.464  36.668  1.00 81.77           O  
ANISOU 9828  O   PHE C 249    12616  10778   7677  -1112    182   -483       O  
ATOM   9829  CB  PHE C 249     -57.192  42.404  39.122  1.00 82.21           C  
ANISOU 9829  CB  PHE C 249    12896  10678   7664   -965    215   -579       C  
ATOM   9830  CG  PHE C 249     -56.542  41.066  39.398  1.00 84.06           C  
ANISOU 9830  CG  PHE C 249    13123  10917   7900   -950    212   -629       C  
ATOM   9831  CD1 PHE C 249     -55.972  40.321  38.367  1.00 87.12           C  
ANISOU 9831  CD1 PHE C 249    13420  11365   8317  -1010    233   -658       C  
ATOM   9832  CD2 PHE C 249     -56.470  40.563  40.692  1.00 86.68           C  
ANISOU 9832  CD2 PHE C 249    13541  11185   8207   -874    213   -635       C  
ATOM   9833  CE1 PHE C 249     -55.350  39.096  38.625  1.00 88.18           C  
ANISOU 9833  CE1 PHE C 249    13547  11477   8479   -982    281   -681       C  
ATOM   9834  CE2 PHE C 249     -55.854  39.332  40.948  1.00 89.66           C  
ANISOU 9834  CE2 PHE C 249    13882  11571   8613   -850    233   -647       C  
ATOM   9835  CZ  PHE C 249     -55.299  38.608  39.912  1.00 87.57           C  
ANISOU 9835  CZ  PHE C 249    13524  11348   8402   -897    281   -664       C  
ATOM   9836  N   ALA C 250     -56.952  45.753  38.533  1.00 79.12           N  
ANISOU 9836  N   ALA C 250    12511  10236   7314  -1014    195   -498       N  
ATOM   9837  CA  ALA C 250     -57.479  46.989  37.951  1.00 79.12           C  
ANISOU 9837  CA  ALA C 250    12455  10233   7373  -1022    261   -408       C  
ATOM   9838  C   ALA C 250     -56.523  47.485  36.867  1.00 82.77           C  
ANISOU 9838  C   ALA C 250    12786  10789   7872  -1096    174   -420       C  
ATOM   9839  O   ALA C 250     -56.969  47.993  35.839  1.00 81.97           O  
ANISOU 9839  O   ALA C 250    12538  10776   7829  -1128    210   -328       O  
ATOM   9840  CB  ALA C 250     -57.637  48.048  39.031  1.00 80.74           C  
ANISOU 9840  CB  ALA C 250    12849  10266   7561   -974    340   -409       C  
ATOM   9841  N   CYS C 251     -55.209  47.296  37.098  1.00 80.16           N  
ANISOU 9841  N   CYS C 251    12491  10454   7514  -1123     58   -503       N  
ATOM   9842  CA  CYS C 251     -54.120  47.646  36.189  1.00 80.26           C  
ANISOU 9842  CA  CYS C 251    12387  10542   7567  -1177    -32   -505       C  
ATOM   9843  C   CYS C 251     -54.158  46.787  34.922  1.00 84.98           C  
ANISOU 9843  C   CYS C 251    12832  11274   8182  -1214    -21   -495       C  
ATOM   9844  O   CYS C 251     -53.897  47.303  33.834  1.00 85.34           O  
ANISOU 9844  O   CYS C 251    12751  11405   8269  -1257    -38   -457       O  
ATOM   9845  CB  CYS C 251     -52.771  47.535  36.898  1.00 80.95           C  
ANISOU 9845  CB  CYS C 251    12545  10588   7623  -1197   -152   -546       C  
ATOM   9846  SG  CYS C 251     -52.424  48.886  38.057  1.00 85.78           S  
ANISOU 9846  SG  CYS C 251    13346  11062   8183  -1238   -198   -566       S  
ATOM   9847  N   TRP C 252     -54.500  45.486  35.065  1.00 81.55           N  
ANISOU 9847  N   TRP C 252    12426  10852   7709  -1209     19   -530       N  
ATOM   9848  CA  TRP C 252     -54.594  44.521  33.964  1.00 81.23           C  
ANISOU 9848  CA  TRP C 252    12305  10908   7653  -1275     60   -546       C  
ATOM   9849  C   TRP C 252     -55.987  44.415  33.318  1.00 84.56           C  
ANISOU 9849  C   TRP C 252    12669  11416   8044  -1344    121   -485       C  
ATOM   9850  O   TRP C 252     -56.093  43.824  32.242  1.00 84.11           O  
ANISOU 9850  O   TRP C 252    12555  11458   7946  -1451    144   -495       O  
ATOM   9851  CB  TRP C 252     -54.115  43.135  34.412  1.00 80.12           C  
ANISOU 9851  CB  TRP C 252    12231  10718   7495  -1249     94   -609       C  
ATOM   9852  CG  TRP C 252     -52.628  42.977  34.468  1.00 81.37           C  
ANISOU 9852  CG  TRP C 252    12371  10847   7698  -1220     54   -610       C  
ATOM   9853  CD1 TRP C 252     -51.857  42.897  35.588  1.00 84.44           C  
ANISOU 9853  CD1 TRP C 252    12808  11171   8104  -1162     -4   -586       C  
ATOM   9854  CD2 TRP C 252     -51.733  42.861  33.353  1.00 81.35           C  
ANISOU 9854  CD2 TRP C 252    12288  10888   7731  -1254     74   -599       C  
ATOM   9855  NE1 TRP C 252     -50.534  42.740  35.244  1.00 84.37           N  
ANISOU 9855  NE1 TRP C 252    12730  11169   8156  -1156    -27   -532       N  
ATOM   9856  CE2 TRP C 252     -50.427  42.724  33.877  1.00 85.63           C  
ANISOU 9856  CE2 TRP C 252    12818  11383   8336  -1197     32   -544       C  
ATOM   9857  CE3 TRP C 252     -51.905  42.858  31.959  1.00 82.71           C  
ANISOU 9857  CE3 TRP C 252    12401  11143   7883  -1337    126   -612       C  
ATOM   9858  CZ2 TRP C 252     -49.302  42.580  33.055  1.00 85.20           C  
ANISOU 9858  CZ2 TRP C 252    12685  11338   8348  -1192     61   -489       C  
ATOM   9859  CZ3 TRP C 252     -50.785  42.740  31.146  1.00 84.41           C  
ANISOU 9859  CZ3 TRP C 252    12565  11364   8143  -1337    156   -592       C  
ATOM   9860  CH2 TRP C 252     -49.503  42.600  31.694  1.00 85.33           C  
ANISOU 9860  CH2 TRP C 252    12664  11411   8345  -1251    134   -525       C  
ATOM   9861  N   LEU C 253     -57.041  44.970  33.963  1.00 81.16           N  
ANISOU 9861  N   LEU C 253    12260  10948   7629  -1298    157   -404       N  
ATOM   9862  CA  LEU C 253     -58.426  44.955  33.466  1.00 81.40           C  
ANISOU 9862  CA  LEU C 253    12207  11070   7653  -1361    212   -276       C  
ATOM   9863  C   LEU C 253     -58.604  45.560  32.055  1.00 86.38           C  
ANISOU 9863  C   LEU C 253    12665  11866   8290  -1482    194   -173       C  
ATOM   9864  O   LEU C 253     -59.255  44.899  31.240  1.00 86.16           O  
ANISOU 9864  O   LEU C 253    12573  11968   8197  -1621    196   -124       O  
ATOM   9865  CB  LEU C 253     -59.414  45.568  34.485  1.00 81.65           C  
ANISOU 9865  CB  LEU C 253    12290  11001   7731  -1255    288   -166       C  
ATOM   9866  CG  LEU C 253     -60.889  45.723  34.073  1.00 86.79           C  
ANISOU 9866  CG  LEU C 253    12822  11741   8413  -1298    358     47       C  
ATOM   9867  CD1 LEU C 253     -61.596  44.379  33.985  1.00 86.96           C  
ANISOU 9867  CD1 LEU C 253    12849  11824   8367  -1374    349     52       C  
ATOM   9868  CD2 LEU C 253     -61.626  46.623  35.042  1.00 89.70           C  
ANISOU 9868  CD2 LEU C 253    13247  11972   8864  -1160    480    176       C  
ATOM   9869  N   PRO C 254     -58.040  46.759  31.708  1.00 83.54           N  
ANISOU 9869  N   PRO C 254    12228  11517   7997  -1456    173   -136       N  
ATOM   9870  CA  PRO C 254     -58.218  47.280  30.342  1.00 83.83           C  
ANISOU 9870  CA  PRO C 254    12079  11733   8041  -1573    157    -23       C  
ATOM   9871  C   PRO C 254     -57.526  46.414  29.285  1.00 88.94           C  
ANISOU 9871  C   PRO C 254    12717  12483   8593  -1701    109   -130       C  
ATOM   9872  O   PRO C 254     -58.034  46.309  28.171  1.00 89.47           O  
ANISOU 9872  O   PRO C 254    12673  12724   8598  -1860    101    -44       O  
ATOM   9873  CB  PRO C 254     -57.619  48.691  30.415  1.00 85.28           C  
ANISOU 9873  CB  PRO C 254    12207  11862   8332  -1487    157     15       C  
ATOM   9874  CG  PRO C 254     -57.560  49.013  31.859  1.00 89.74           C  
ANISOU 9874  CG  PRO C 254    12943  12223   8933  -1353    199    -38       C  
ATOM   9875  CD  PRO C 254     -57.246  47.709  32.509  1.00 84.93           C  
ANISOU 9875  CD  PRO C 254    12480  11553   8237  -1343    162   -184       C  
ATOM   9876  N   TYR C 255     -56.400  45.763  29.649  1.00 85.85           N  
ANISOU 9876  N   TYR C 255    12450  11983   8187  -1644     94   -295       N  
ATOM   9877  CA  TYR C 255     -55.655  44.860  28.766  1.00 86.34           C  
ANISOU 9877  CA  TYR C 255    12544  12085   8177  -1734    107   -397       C  
ATOM   9878  C   TYR C 255     -56.453  43.591  28.526  1.00 90.63           C  
ANISOU 9878  C   TYR C 255    13167  12664   8604  -1866    165   -437       C  
ATOM   9879  O   TYR C 255     -56.446  43.093  27.401  1.00 90.60           O  
ANISOU 9879  O   TYR C 255    13166  12760   8499  -2032    193   -465       O  
ATOM   9880  CB  TYR C 255     -54.273  44.521  29.354  1.00 87.78           C  
ANISOU 9880  CB  TYR C 255    12816  12125   8410  -1614    105   -501       C  
ATOM   9881  CG  TYR C 255     -53.481  43.506  28.553  1.00 90.57           C  
ANISOU 9881  CG  TYR C 255    13224  12473   8717  -1673    180   -585       C  
ATOM   9882  CD1 TYR C 255     -52.759  43.888  27.426  1.00 93.04           C  
ANISOU 9882  CD1 TYR C 255    13464  12854   9032  -1718    182   -570       C  
ATOM   9883  CD2 TYR C 255     -53.444  42.166  28.929  1.00 91.68           C  
ANISOU 9883  CD2 TYR C 255    13496  12520   8820  -1675    278   -670       C  
ATOM   9884  CE1 TYR C 255     -52.015  42.961  26.693  1.00 94.79           C  
ANISOU 9884  CE1 TYR C 255    13765  13038   9213  -1762    297   -640       C  
ATOM   9885  CE2 TYR C 255     -52.701  41.231  28.207  1.00 93.45           C  
ANISOU 9885  CE2 TYR C 255    13794  12698   9013  -1720    404   -739       C  
ATOM   9886  CZ  TYR C 255     -51.982  41.635  27.093  1.00101.07           C  
ANISOU 9886  CZ  TYR C 255    14708  13719   9976  -1762    421   -725       C  
ATOM   9887  OH  TYR C 255     -51.251  40.720  26.372  1.00101.67           O  
ANISOU 9887  OH  TYR C 255    14884  13721  10024  -1798    588   -786       O  
ATOM   9888  N   TYR C 256     -57.116  43.055  29.588  1.00 87.18           N  
ANISOU 9888  N   TYR C 256    12812  12139   8173  -1804    188   -443       N  
ATOM   9889  CA  TYR C 256     -57.951  41.853  29.511  1.00 87.45           C  
ANISOU 9889  CA  TYR C 256    12924  12193   8112  -1923    238   -471       C  
ATOM   9890  C   TYR C 256     -59.126  42.111  28.577  1.00 90.18           C  
ANISOU 9890  C   TYR C 256    13156  12732   8377  -2123    204   -321       C  
ATOM   9891  O   TYR C 256     -59.439  41.256  27.750  1.00 89.83           O  
ANISOU 9891  O   TYR C 256    13162  12771   8199  -2332    225   -359       O  
ATOM   9892  CB  TYR C 256     -58.461  41.412  30.901  1.00 88.80           C  
ANISOU 9892  CB  TYR C 256    13174  12238   8328  -1789    260   -474       C  
ATOM   9893  CG  TYR C 256     -57.419  40.937  31.899  1.00 91.00           C  
ANISOU 9893  CG  TYR C 256    13558  12353   8665  -1628    288   -592       C  
ATOM   9894  CD1 TYR C 256     -56.266  40.275  31.479  1.00 93.33           C  
ANISOU 9894  CD1 TYR C 256    13904  12601   8957  -1637    343   -697       C  
ATOM   9895  CD2 TYR C 256     -57.633  41.062  33.271  1.00 91.64           C  
ANISOU 9895  CD2 TYR C 256    13690  12330   8801  -1476    278   -574       C  
ATOM   9896  CE1 TYR C 256     -55.319  39.814  32.396  1.00 94.73           C  
ANISOU 9896  CE1 TYR C 256    14140  12650   9204  -1496    372   -745       C  
ATOM   9897  CE2 TYR C 256     -56.702  40.593  34.199  1.00 92.38           C  
ANISOU 9897  CE2 TYR C 256    13860  12307   8933  -1358    289   -649       C  
ATOM   9898  CZ  TYR C 256     -55.545  39.970  33.758  1.00100.50           C  
ANISOU 9898  CZ  TYR C 256    14900  13310   9977  -1369    330   -717       C  
ATOM   9899  OH  TYR C 256     -54.625  39.514  34.679  1.00100.02           O  
ANISOU 9899  OH  TYR C 256    14876  13155   9970  -1258    342   -732       O  
ATOM   9900  N   ILE C 257     -59.742  43.311  28.685  1.00 86.34           N  
ANISOU 9900  N   ILE C 257    12517  12317   7971  -2074    163   -135       N  
ATOM   9901  CA  ILE C 257     -60.856  43.751  27.841  1.00 87.15           C  
ANISOU 9901  CA  ILE C 257    12451  12629   8035  -2250    129     88       C  
ATOM   9902  C   ILE C 257     -60.390  43.835  26.380  1.00 92.03           C  
ANISOU 9902  C   ILE C 257    13005  13416   8547  -2448     92     71       C  
ATOM   9903  O   ILE C 257     -61.053  43.278  25.504  1.00 93.26           O  
ANISOU 9903  O   ILE C 257    13143  13738   8556  -2706     65    133       O  
ATOM   9904  CB  ILE C 257     -61.512  45.059  28.384  1.00 90.20           C  
ANISOU 9904  CB  ILE C 257    12687  13012   8574  -2108    148    316       C  
ATOM   9905  CG1 ILE C 257     -62.283  44.766  29.695  1.00 90.85           C  
ANISOU 9905  CG1 ILE C 257    12853  12950   8717  -1966    206    363       C  
ATOM   9906  CG2 ILE C 257     -62.448  45.709  27.345  1.00 91.80           C  
ANISOU 9906  CG2 ILE C 257    12652  13458   8770  -2282    122    603       C  
ATOM   9907  CD1 ILE C 257     -62.537  45.961  30.614  1.00100.32           C  
ANISOU 9907  CD1 ILE C 257    14022  14022  10074  -1755    288    491       C  
ATOM   9908  N   GLY C 258     -59.231  44.466  26.160  1.00 87.67           N  
ANISOU 9908  N   GLY C 258    12437  12814   8057  -2341     90    -16       N  
ATOM   9909  CA  GLY C 258     -58.596  44.628  24.853  1.00 87.72           C  
ANISOU 9909  CA  GLY C 258    12394  12952   7985  -2480     71    -45       C  
ATOM   9910  C   GLY C 258     -58.341  43.314  24.145  1.00 92.72           C  
ANISOU 9910  C   GLY C 258    13205  13591   8435  -2676    120   -211       C  
ATOM   9911  O   GLY C 258     -58.784  43.141  23.008  1.00 93.77           O  
ANISOU 9911  O   GLY C 258    13306  13912   8410  -2938     98   -155       O  
ATOM   9912  N   ILE C 259     -57.653  42.369  24.828  1.00 89.28           N  
ANISOU 9912  N   ILE C 259    12964  12946   8012  -2564    204   -403       N  
ATOM   9913  CA  ILE C 259     -57.348  41.021  24.320  1.00 90.33           C  
ANISOU 9913  CA  ILE C 259    13307  13015   7998  -2715    315   -576       C  
ATOM   9914  C   ILE C 259     -58.636  40.231  24.037  1.00 96.87           C  
ANISOU 9914  C   ILE C 259    14195  13951   8660  -2980    304   -538       C  
ATOM   9915  O   ILE C 259     -58.758  39.665  22.956  1.00 97.84           O  
ANISOU 9915  O   ILE C 259    14418  14166   8591  -3254    342   -593       O  
ATOM   9916  CB  ILE C 259     -56.342  40.254  25.238  1.00 92.62           C  
ANISOU 9916  CB  ILE C 259    13750  13053   8388  -2503    429   -732       C  
ATOM   9917  CG1 ILE C 259     -54.942  40.928  25.256  1.00 92.29           C  
ANISOU 9917  CG1 ILE C 259    13654  12932   8480  -2308    435   -745       C  
ATOM   9918  CG2 ILE C 259     -56.249  38.749  24.911  1.00 94.38           C  
ANISOU 9918  CG2 ILE C 259    14203  13170   8486  -2644    596   -892       C  
ATOM   9919  CD1 ILE C 259     -54.126  40.934  23.906  1.00101.96           C  
ANISOU 9919  CD1 ILE C 259    14907  14202   9630  -2412    509   -788       C  
ATOM   9920  N   SER C 260     -59.605  40.237  24.974  1.00 94.54           N  
ANISOU 9920  N   SER C 260    13842  13649   8430  -2916    251   -429       N  
ATOM   9921  CA  SER C 260     -60.890  39.551  24.814  1.00 96.20           C  
ANISOU 9921  CA  SER C 260    14076  13967   8509  -3155    218   -343       C  
ATOM   9922  C   SER C 260     -61.578  39.923  23.495  1.00103.05           C  
ANISOU 9922  C   SER C 260    14828  15116   9209  -3484    126   -181       C  
ATOM   9923  O   SER C 260     -62.021  39.025  22.782  1.00104.69           O  
ANISOU 9923  O   SER C 260    15168  15404   9206  -3797    136   -229       O  
ATOM   9924  CB  SER C 260     -61.806  39.832  25.998  1.00 99.18           C  
ANISOU 9924  CB  SER C 260    14351  14311   9022  -2990    171   -184       C  
ATOM   9925  OG  SER C 260     -61.202  39.383  27.200  1.00108.08           O  
ANISOU 9925  OG  SER C 260    15598  15200  10268  -2728    248   -335       O  
ATOM   9926  N   ILE C 261     -61.603  41.237  23.149  1.00 99.80           N  
ANISOU 9926  N   ILE C 261    14180  14853   8884  -3427     47     10       N  
ATOM   9927  CA  ILE C 261     -62.164  41.782  21.900  1.00101.32           C  
ANISOU 9927  CA  ILE C 261    14205  15344   8948  -3714    -48    214       C  
ATOM   9928  C   ILE C 261     -61.385  41.209  20.690  1.00108.25           C  
ANISOU 9928  C   ILE C 261    15261  16260   9609  -3948      2     13       C  
ATOM   9929  O   ILE C 261     -62.004  40.683  19.764  1.00109.81           O  
ANISOU 9929  O   ILE C 261    15515  16642   9567  -4323    -41     56       O  
ATOM   9930  CB  ILE C 261     -62.198  43.348  21.920  1.00103.16           C  
ANISOU 9930  CB  ILE C 261    14142  15682   9374  -3538   -100    454       C  
ATOM   9931  CG1 ILE C 261     -63.175  43.886  23.000  1.00102.57           C  
ANISOU 9931  CG1 ILE C 261    13913  15572   9486  -3358   -106    692       C  
ATOM   9932  CG2 ILE C 261     -62.532  43.934  20.532  1.00104.96           C  
ANISOU 9932  CG2 ILE C 261    14176  16226   9478  -3819   -184    659       C  
ATOM   9933  CD1 ILE C 261     -62.883  45.326  23.507  1.00104.01           C  
ANISOU 9933  CD1 ILE C 261    13914  15692   9914  -3063    -71    819       C  
ATOM   9934  N   ASP C 262     -60.034  41.271  20.736  1.00105.12           N  
ANISOU 9934  N   ASP C 262    14970  15679   9293  -3736    102   -196       N  
ATOM   9935  CA  ASP C 262     -59.152  40.753  19.684  1.00106.80           C  
ANISOU 9935  CA  ASP C 262    15372  15870   9337  -3891    203   -387       C  
ATOM   9936  C   ASP C 262     -59.132  39.221  19.617  1.00112.88           C  
ANISOU 9936  C   ASP C 262    16474  16485   9930  -4069    348   -614       C  
ATOM   9937  O   ASP C 262     -58.844  38.674  18.552  1.00114.43           O  
ANISOU 9937  O   ASP C 262    16861  16711   9907  -4329    438   -736       O  
ATOM   9938  CB  ASP C 262     -57.725  41.303  19.835  1.00107.73           C  
ANISOU 9938  CB  ASP C 262    15475  15826   9632  -3583    276   -487       C  
ATOM   9939  CG  ASP C 262     -56.985  41.572  18.527  1.00123.30           C  
ANISOU 9939  CG  ASP C 262    17465  17892  11489  -3708    317   -525       C  
ATOM   9940  OD1 ASP C 262     -55.756  41.343  18.483  1.00124.48           O  
ANISOU 9940  OD1 ASP C 262    17741  17852  11704  -3541    452   -674       O  
ATOM   9941  OD2 ASP C 262     -57.625  42.064  17.565  1.00130.31           O  
ANISOU 9941  OD2 ASP C 262    18221  19054  12237  -3963    214   -373       O  
ATOM   9942  N   SER C 263     -59.431  38.531  20.742  1.00109.38           N  
ANISOU 9942  N   SER C 263    16114  15868   9579  -3934    390   -671       N  
ATOM   9943  CA  SER C 263     -59.500  37.069  20.802  1.00110.69           C  
ANISOU 9943  CA  SER C 263    16578  15869   9609  -4084    543   -870       C  
ATOM   9944  C   SER C 263     -60.664  36.598  19.934  1.00117.94           C  
ANISOU 9944  C   SER C 263    17563  17003  10244  -4547    463   -801       C  
ATOM   9945  O   SER C 263     -60.521  35.615  19.206  1.00119.51           O  
ANISOU 9945  O   SER C 263    18050  17140  10217  -4824    601   -983       O  
ATOM   9946  CB  SER C 263     -59.677  36.586  22.238  1.00112.53           C  
ANISOU 9946  CB  SER C 263    16823  15910  10024  -3828    575   -895       C  
ATOM   9947  OG  SER C 263     -58.569  36.944  23.049  1.00118.44           O  
ANISOU 9947  OG  SER C 263    17526  16471  11004  -3449    640   -950       O  
ATOM   9948  N   PHE C 264     -61.788  37.353  19.960  1.00115.36           N  
ANISOU 9948  N   PHE C 264    16970  16936   9925  -4645    250   -515       N  
ATOM   9949  CA  PHE C 264     -62.976  37.086  19.151  1.00117.96           C  
ANISOU 9949  CA  PHE C 264    17288  17533   9997  -5104    121   -356       C  
ATOM   9950  C   PHE C 264     -62.757  37.467  17.689  1.00124.06           C  
ANISOU 9950  C   PHE C 264    18066  18532  10539  -5421     83   -331       C  
ATOM   9951  O   PHE C 264     -63.471  36.962  16.825  1.00126.37           O  
ANISOU 9951  O   PHE C 264    18463  19017  10537  -5883     17   -284       O  
ATOM   9952  CB  PHE C 264     -64.225  37.783  19.726  1.00119.50           C  
ANISOU 9952  CB  PHE C 264    17162  17923  10319  -5070    -69      4       C  
ATOM   9953  CG  PHE C 264     -64.683  37.273  21.074  1.00120.16           C  
ANISOU 9953  CG  PHE C 264    17265  17817  10573  -4839    -40      3       C  
ATOM   9954  CD1 PHE C 264     -65.078  35.950  21.240  1.00124.69           C  
ANISOU 9954  CD1 PHE C 264    18083  18284  11010  -5031     20   -139       C  
ATOM   9955  CD2 PHE C 264     -64.774  38.128  22.163  1.00120.21           C  
ANISOU 9955  CD2 PHE C 264    17053  17753  10866  -4449    -66    153       C  
ATOM   9956  CE1 PHE C 264     -65.503  35.481  22.487  1.00124.52           C  
ANISOU 9956  CE1 PHE C 264    18064  18095  11152  -4807     46   -129       C  
ATOM   9957  CE2 PHE C 264     -65.190  37.657  23.411  1.00122.10           C  
ANISOU 9957  CE2 PHE C 264    17324  17820  11249  -4238    -32    151       C  
ATOM   9958  CZ  PHE C 264     -65.559  36.339  23.563  1.00121.32           C  
ANISOU 9958  CZ  PHE C 264    17441  17630  11026  -4410     16     19       C  
ATOM   9959  N   ILE C 265     -61.777  38.352  17.411  1.00119.90           N  
ANISOU 9959  N   ILE C 265    17431  17991  10134  -5192    116   -352       N  
ATOM   9960  CA  ILE C 265     -61.418  38.771  16.052  1.00121.50           C  
ANISOU 9960  CA  ILE C 265    17632  18390  10143  -5438     98   -338       C  
ATOM   9961  C   ILE C 265     -60.694  37.605  15.347  1.00128.88           C  
ANISOU 9961  C   ILE C 265    18998  19141  10830  -5650    318   -670       C  
ATOM   9962  O   ILE C 265     -60.949  37.350  14.166  1.00130.86           O  
ANISOU 9962  O   ILE C 265    19385  19573  10762  -6081    303   -682       O  
ATOM   9963  CB  ILE C 265     -60.652  40.136  16.070  1.00122.40           C  
ANISOU 9963  CB  ILE C 265    17467  18539  10502  -5097     63   -229       C  
ATOM   9964  CG1 ILE C 265     -61.577  41.289  15.638  1.00122.98           C  
ANISOU 9964  CG1 ILE C 265    17156  18976  10595  -5225   -147    152       C  
ATOM   9965  CG2 ILE C 265     -59.352  40.133  15.253  1.00123.29           C  
ANISOU 9965  CG2 ILE C 265    17742  18551  10551  -5059    211   -433       C  
ATOM   9966  CD1 ILE C 265     -61.721  42.372  16.638  1.00125.85           C  
ANISOU 9966  CD1 ILE C 265    17210  19305  11300  -4837   -204    353       C  
ATOM   9967  N   LEU C 266     -59.851  36.869  16.109  1.00125.99           N  
ANISOU 9967  N   LEU C 266    18850  18412  10607  -5364    535   -918       N  
ATOM   9968  CA  LEU C 266     -59.113  35.686  15.665  1.00128.38           C  
ANISOU 9968  CA  LEU C 266    19574  18459  10747  -5484    820  -1223       C  
ATOM   9969  C   LEU C 266     -60.091  34.531  15.392  1.00137.34           C  
ANISOU 9969  C   LEU C 266    20977  19617  11588  -5931    842  -1305       C  
ATOM   9970  O   LEU C 266     -59.881  33.762  14.452  1.00139.66           O  
ANISOU 9970  O   LEU C 266    21621  19852  11593  -6267   1016  -1496       O  
ATOM   9971  CB  LEU C 266     -58.108  35.261  16.752  1.00126.48           C  
ANISOU 9971  CB  LEU C 266    19411  17850  10795  -5031   1028  -1376       C  
ATOM   9972  CG  LEU C 266     -56.674  34.963  16.297  1.00131.63           C  
ANISOU 9972  CG  LEU C 266    20278  18255  11482  -4879   1315  -1561       C  
ATOM   9973  CD1 LEU C 266     -55.703  35.119  17.446  1.00129.39           C  
ANISOU 9973  CD1 LEU C 266    19876  17730  11556  -4376   1400  -1559       C  
ATOM   9974  CD2 LEU C 266     -56.545  33.563  15.717  1.00136.88           C  
ANISOU 9974  CD2 LEU C 266    21396  18709  11905  -5161   1620  -1809       C  
ATOM   9975  N   LEU C 267     -61.156  34.419  16.216  1.00134.83           N  
ANISOU 9975  N   LEU C 267    20510  19377  11342  -5940    676  -1154       N  
ATOM   9976  CA  LEU C 267     -62.194  33.387  16.103  1.00137.67           C  
ANISOU 9976  CA  LEU C 267    21072  19776  11458  -6350    653  -1183       C  
ATOM   9977  C   LEU C 267     -63.450  33.904  15.362  1.00145.38           C  
ANISOU 9977  C   LEU C 267    21849  21182  12206  -6793    354   -882       C  
ATOM   9978  O   LEU C 267     -64.481  33.224  15.353  1.00146.82           O  
ANISOU 9978  O   LEU C 267    22115  21459  12210  -7140    262   -816       O  
ATOM   9979  CB  LEU C 267     -62.557  32.812  17.493  1.00136.10           C  
ANISOU 9979  CB  LEU C 267    20845  19377  11489  -6082    680  -1192       C  
ATOM   9980  CG  LEU C 267     -61.424  32.180  18.326  1.00139.34           C  
ANISOU 9980  CG  LEU C 267    21429  19386  12130  -5672    968  -1440       C  
ATOM   9981  CD1 LEU C 267     -61.816  32.077  19.785  1.00137.25           C  
ANISOU 9981  CD1 LEU C 267    20995  19014  12139  -5340    910  -1355       C  
ATOM   9982  CD2 LEU C 267     -61.027  30.811  17.794  1.00144.73           C  
ANISOU 9982  CD2 LEU C 267    22571  19817  12602  -5920   1279  -1740       C  
ATOM   9983  N   GLU C 268     -63.388  35.094  14.777  1.00142.96           N  
ANISOU 9983  N   GLU C 268    21258  21141  11919  -6782    200   -670       N  
ATOM   9984  CA  GLU C 268     -64.478  35.592  13.927  1.00145.41           C  
ANISOU 9984  CA  GLU C 268    21363  21884  12002  -7230    -63   -350       C  
ATOM   9985  C   GLU C 268     -65.961  35.927  14.193  1.00151.07           C  
ANISOU 9985  C   GLU C 268    21756  22914  12730  -7424   -340     66       C  
ATOM   9986  O   GLU C 268     -66.837  35.621  13.384  1.00154.16           O  
ANISOU 9986  O   GLU C 268    22182  23589  12804  -7965   -491    223       O  
ATOM   9987  CB  GLU C 268     -64.548  34.771  12.635  1.00150.57           C  
ANISOU 9987  CB  GLU C 268    22392  22629  12189  -7828     -7   -516       C  
ATOM   9988  CG  GLU C 268     -64.343  33.278  12.835  1.00161.97           C  
ANISOU 9988  CG  GLU C 268    24324  23733  13483  -7966    239   -878       C  
ATOM   9989  CD  GLU C 268     -65.488  32.453  12.283  1.00185.41           C  
ANISOU 9989  CD  GLU C 268    27486  26892  16068  -8607    116   -820       C  
ATOM   9990  OE1 GLU C 268     -65.582  31.256  12.629  1.00180.85           O  
ANISOU 9990  OE1 GLU C 268    27254  26055  15407  -8719    283  -1057       O  
ATOM   9991  OE2 GLU C 268     -66.295  33.000  11.503  1.00181.04           O  
ANISOU 9991  OE2 GLU C 268    26732  26755  15300  -9011   -149   -518       O  
ATOM   9992  N   ILE C 269     -66.209  36.573  15.329  1.00145.06           N  
ANISOU 9992  N   ILE C 269    20686  22097  12333  -6984   -395    258       N  
ATOM   9993  CA  ILE C 269     -67.433  37.330  15.637  1.00145.00           C  
ANISOU 9993  CA  ILE C 269    20264  22376  12454  -7009   -620    733       C  
ATOM   9994  C   ILE C 269     -67.865  38.800  15.436  1.00148.58           C  
ANISOU 9994  C   ILE C 269    20237  23134  13083  -6907   -773   1175       C  
ATOM   9995  O   ILE C 269     -69.049  39.056  15.206  1.00149.93           O  
ANISOU 9995  O   ILE C 269    20148  23617  13203  -7178   -956   1593       O  
ATOM   9996  CB  ILE C 269     -67.548  36.955  17.156  1.00145.88           C  
ANISOU 9996  CB  ILE C 269    20391  22181  12857  -6589   -534    662       C  
ATOM   9997  CG1 ILE C 269     -67.401  35.437  17.402  1.00147.35           C  
ANISOU 9997  CG1 ILE C 269    21000  22104  12885  -6729   -393    311       C  
ATOM   9998  CG2 ILE C 269     -68.866  37.450  17.777  1.00146.44           C  
ANISOU 9998  CG2 ILE C 269    20107  22440  13096  -6554   -701   1121       C  
ATOM   9999  CD1 ILE C 269     -66.050  34.985  17.904  1.00153.16           C  
ANISOU 9999  CD1 ILE C 269    22002  22443  13747  -6363   -134   -107       C  
ATOM  10000  N   ILE C 270     -66.914  39.751  15.533  1.00143.10           N  
ANISOU10000  N   ILE C 270    19417  22344  12609  -6520   -688   1108       N  
ATOM  10001  CA  ILE C 270     -67.191  41.190  15.400  1.00142.39           C  
ANISOU10001  CA  ILE C 270    18885  22487  12728  -6367   -781   1497       C  
ATOM  10002  C   ILE C 270     -67.264  41.597  13.917  1.00149.54           C  
ANISOU10002  C   ILE C 270    19678  23767  13375  -6785   -896   1665       C  
ATOM  10003  O   ILE C 270     -66.325  41.354  13.156  1.00149.81           O  
ANISOU10003  O   ILE C 270    19949  23748  13225  -6886   -819   1366       O  
ATOM  10004  CB  ILE C 270     -66.239  42.090  16.249  1.00142.08           C  
ANISOU10004  CB  ILE C 270    18747  22184  13053  -5779   -649   1383       C  
ATOM  10005  CG1 ILE C 270     -66.412  41.828  17.756  1.00140.47           C  
ANISOU10005  CG1 ILE C 270    18593  21681  13098  -5407   -569   1319       C  
ATOM  10006  CG2 ILE C 270     -66.435  43.586  15.952  1.00142.28           C  
ANISOU10006  CG2 ILE C 270    18347  22437  13277  -5653   -708   1758       C  
ATOM  10007  CD1 ILE C 270     -65.229  41.214  18.400  1.00146.07           C  
ANISOU10007  CD1 ILE C 270    19618  22015  13866  -5122   -409    873       C  
ATOM  10008  N   LYS C 271     -68.390  42.229  13.531  1.00147.84           N  
ANISOU10008  N   LYS C 271    19084  23929  13158  -7020  -1069   2175       N  
ATOM  10009  CA  LYS C 271     -68.668  42.721  12.181  1.00149.95           C  
ANISOU10009  CA  LYS C 271    19154  24622  13198  -7440  -1212   2449       C  
ATOM  10010  C   LYS C 271     -68.102  44.149  12.033  1.00151.72           C  
ANISOU10010  C   LYS C 271    19038  24906  13702  -7091  -1164   2610       C  
ATOM  10011  O   LYS C 271     -68.823  45.133  12.224  1.00151.27           O  
ANISOU10011  O   LYS C 271    18547  25041  13887  -6976  -1216   3080       O  
ATOM  10012  CB  LYS C 271     -70.189  42.654  11.906  1.00155.20           C  
ANISOU10012  CB  LYS C 271    19549  25676  13746  -7870  -1422   2977       C  
ATOM  10013  CG  LYS C 271     -70.629  42.987  10.472  1.00173.41           C  
ANISOU10013  CG  LYS C 271    21657  28481  15750  -8418  -1608   3308       C  
ATOM  10014  CD  LYS C 271     -72.097  42.594  10.188  1.00185.85           C  
ANISOU10014  CD  LYS C 271    23053  30430  17132  -8943  -1835   3790       C  
ATOM  10015  CE  LYS C 271     -73.149  43.352  10.979  1.00192.24           C  
ANISOU10015  CE  LYS C 271    23379  31321  18342  -8665  -1864   4358       C  
ATOM  10016  NZ  LYS C 271     -73.243  44.781  10.574  1.00196.35           N  
ANISOU10016  NZ  LYS C 271    23478  31763  19364  -8115  -1746   4614       N  
ATOM  10017  N   GLN C 272     -66.788  44.247  11.744  1.00146.53           N  
ANISOU10017  N   GLN C 272    18585  24055  13036  -6899  -1040   2226       N  
ATOM  10018  CA  GLN C 272     -66.062  45.512  11.560  1.00144.44           C  
ANISOU10018  CA  GLN C 272    18056  23807  13017  -6571   -985   2304       C  
ATOM  10019  C   GLN C 272     -64.848  45.367  10.629  1.00147.25           C  
ANISOU10019  C   GLN C 272    18653  24118  13179  -6640   -917   1961       C  
ATOM  10020  O   GLN C 272     -64.267  44.282  10.524  1.00147.11           O  
ANISOU10020  O   GLN C 272    19071  23886  12939  -6751   -826   1556       O  
ATOM  10021  CB  GLN C 272     -65.647  46.130  12.912  1.00142.52           C  
ANISOU10021  CB  GLN C 272    17732  23217  13203  -5968   -851   2237       C  
ATOM  10022  CG  GLN C 272     -66.566  47.257  13.413  1.00156.82           C  
ANISOU10022  CG  GLN C 272    19087  25167  15331  -5782   -872   2736       C  
ATOM  10023  CD  GLN C 272     -66.602  48.517  12.563  1.00177.52           C  
ANISOU10023  CD  GLN C 272    21301  28092  18055  -5807   -907   3094       C  
ATOM  10024  OE1 GLN C 272     -67.650  49.154  12.417  1.00175.06           O  
ANISOU10024  OE1 GLN C 272    20604  28060  17852  -5912   -964   3608       O  
ATOM  10025  NE2 GLN C 272     -65.471  48.927  11.997  1.00168.00           N  
ANISOU10025  NE2 GLN C 272    20147  26842  16843  -5696   -861   2867       N  
ATOM  10026  N   GLY C 273     -64.477  46.471   9.977  1.00142.66           N  
ANISOU10026  N   GLY C 273    17778  23723  12701  -6555   -936   2144       N  
ATOM  10027  CA  GLY C 273     -63.356  46.528   9.044  1.00142.27           C  
ANISOU10027  CA  GLY C 273    17887  23664  12505  -6590   -872   1893       C  
ATOM  10028  C   GLY C 273     -61.988  46.614   9.686  1.00142.18           C  
ANISOU10028  C   GLY C 273    18066  23231  12726  -6096   -693   1519       C  
ATOM  10029  O   GLY C 273     -61.854  46.433  10.900  1.00139.81           O  
ANISOU10029  O   GLY C 273    17849  22620  12654  -5760   -617   1387       O  
ATOM  10030  N   CYS C 274     -60.958  46.895   8.864  1.00137.85           N  
ANISOU10030  N   CYS C 274    17577  22682  12117  -6059   -630   1371       N  
ATOM  10031  CA  CYS C 274     -59.566  47.011   9.312  1.00134.98           C  
ANISOU10031  CA  CYS C 274    17369  21953  11963  -5621   -470   1062       C  
ATOM  10032  C   CYS C 274     -59.282  48.266  10.131  1.00133.47           C  
ANISOU10032  C   CYS C 274    16841  21667  12206  -5149   -472   1221       C  
ATOM  10033  O   CYS C 274     -58.343  48.264  10.924  1.00130.59           O  
ANISOU10033  O   CYS C 274    16607  20963  12048  -4775   -366    992       O  
ATOM  10034  CB  CYS C 274     -58.594  46.858   8.148  1.00136.98           C  
ANISOU10034  CB  CYS C 274    17804  22232  12009  -5745   -388    880       C  
ATOM  10035  SG  CYS C 274     -58.480  45.169   7.506  1.00143.99           S  
ANISOU10035  SG  CYS C 274    19276  23006  12427  -6177   -258    522       S  
ATOM  10036  N   GLU C 275     -60.108  49.322   9.958  1.00128.65           N  
ANISOU10036  N   GLU C 275    15802  21349  11731  -5182   -579   1630       N  
ATOM  10037  CA  GLU C 275     -60.039  50.588  10.695  1.00125.57           C  
ANISOU10037  CA  GLU C 275    15083  20883  11745  -4781   -557   1827       C  
ATOM  10038  C   GLU C 275     -60.187  50.307  12.200  1.00125.94           C  
ANISOU10038  C   GLU C 275    15264  20598  11989  -4497   -492   1706       C  
ATOM  10039  O   GLU C 275     -59.421  50.843  12.998  1.00124.11           O  
ANISOU10039  O   GLU C 275    15039  20097  12022  -4113   -416   1584       O  
ATOM  10040  CB  GLU C 275     -61.139  51.549  10.184  1.00128.32           C  
ANISOU10040  CB  GLU C 275    14967  21624  12164  -4944   -649   2335       C  
ATOM  10041  CG  GLU C 275     -61.558  52.677  11.124  1.00136.31           C  
ANISOU10041  CG  GLU C 275    15661  22550  13579  -4598   -587   2608       C  
ATOM  10042  CD  GLU C 275     -60.650  53.885  11.267  1.00149.40           C  
ANISOU10042  CD  GLU C 275    17141  24074  15550  -4221   -501   2603       C  
ATOM  10043  OE1 GLU C 275     -59.642  53.983  10.530  1.00145.43           O  
ANISOU10043  OE1 GLU C 275    16695  23583  14979  -4207   -507   2432       O  
ATOM  10044  OE2 GLU C 275     -60.969  54.754  12.110  1.00139.28           O  
ANISOU10044  OE2 GLU C 275    15667  22670  14584  -3946   -415   2786       O  
ATOM  10045  N   PHE C 276     -61.138  49.434  12.566  1.00121.12           N  
ANISOU10045  N   PHE C 276    14777  20011  11231  -4707   -530   1734       N  
ATOM  10046  CA  PHE C 276     -61.396  49.045  13.946  1.00118.43           C  
ANISOU10046  CA  PHE C 276    14574  19385  11041  -4480   -474   1632       C  
ATOM  10047  C   PHE C 276     -60.460  47.923  14.408  1.00118.68           C  
ANISOU10047  C   PHE C 276    15032  19087  10975  -4386   -389   1183       C  
ATOM  10048  O   PHE C 276     -60.147  47.857  15.596  1.00116.85           O  
ANISOU10048  O   PHE C 276    14904  18563  10933  -4078   -322   1044       O  
ATOM  10049  CB  PHE C 276     -62.867  48.633  14.108  1.00121.94           C  
ANISOU10049  CB  PHE C 276    14926  20014  11391  -4740   -552   1908       C  
ATOM  10050  CG  PHE C 276     -63.378  48.696  15.526  1.00122.31           C  
ANISOU10050  CG  PHE C 276    14967  19830  11674  -4460   -490   1960       C  
ATOM  10051  CD1 PHE C 276     -63.832  49.894  16.067  1.00124.94           C  
ANISOU10051  CD1 PHE C 276    14987  20168  12316  -4211   -437   2274       C  
ATOM  10052  CD2 PHE C 276     -63.418  47.556  16.319  1.00124.13           C  
ANISOU10052  CD2 PHE C 276    15514  19828  11821  -4444   -461   1702       C  
ATOM  10053  CE1 PHE C 276     -64.298  49.953  17.383  1.00125.13           C  
ANISOU10053  CE1 PHE C 276    15042  19958  12542  -3955   -352   2313       C  
ATOM  10054  CE2 PHE C 276     -63.888  47.616  17.633  1.00126.14           C  
ANISOU10054  CE2 PHE C 276    15768  19875  12284  -4184   -401   1752       C  
ATOM  10055  CZ  PHE C 276     -64.325  48.813  18.156  1.00123.86           C  
ANISOU10055  CZ  PHE C 276    15193  19586  12281  -3945   -346   2052       C  
ATOM  10056  N   GLU C 277     -60.029  47.041  13.479  1.00114.35           N  
ANISOU10056  N   GLU C 277    14735  18582  10130  -4659   -373    976       N  
ATOM  10057  CA  GLU C 277     -59.130  45.915  13.765  1.00112.87           C  
ANISOU10057  CA  GLU C 277    14953  18086   9848  -4594   -244    582       C  
ATOM  10058  C   GLU C 277     -57.717  46.386  14.107  1.00112.75           C  
ANISOU10058  C   GLU C 277    14966  17818  10056  -4204   -149    410       C  
ATOM  10059  O   GLU C 277     -57.014  45.702  14.852  1.00110.95           O  
ANISOU10059  O   GLU C 277    14981  17287   9890  -4011    -41    166       O  
ATOM  10060  CB  GLU C 277     -59.115  44.905  12.607  1.00116.85           C  
ANISOU10060  CB  GLU C 277    15731  18697   9969  -5015   -211    433       C  
ATOM  10061  CG  GLU C 277     -60.275  43.917  12.644  1.00130.76           C  
ANISOU10061  CG  GLU C 277    17637  20554  11491  -5380   -265    463       C  
ATOM  10062  CD  GLU C 277     -60.574  43.117  11.385  1.00156.57           C  
ANISOU10062  CD  GLU C 277    21134  24020  14337  -5907   -275    399       C  
ATOM  10063  OE1 GLU C 277     -59.658  42.919  10.553  1.00154.32           O  
ANISOU10063  OE1 GLU C 277    21050  23679  13905  -5971   -159    200       O  
ATOM  10064  OE2 GLU C 277     -61.732  42.658  11.249  1.00152.34           O  
ANISOU10064  OE2 GLU C 277    20593  23681  13606  -6271   -390    552       O  
ATOM  10065  N   ASN C 278     -57.306  47.552  13.562  1.00107.87           N  
ANISOU10065  N   ASN C 278    14084  17335   9565  -4098   -191    564       N  
ATOM  10066  CA  ASN C 278     -56.006  48.176  13.814  1.00105.30           C  
ANISOU10066  CA  ASN C 278    13731  16812   9466  -3748   -131    462       C  
ATOM  10067  C   ASN C 278     -56.084  49.035  15.074  1.00106.39           C  
ANISOU10067  C   ASN C 278    13697  16807   9919  -3419   -158    558       C  
ATOM  10068  O   ASN C 278     -55.097  49.119  15.808  1.00104.71           O  
ANISOU10068  O   ASN C 278    13576  16334   9873  -3135   -108    408       O  
ATOM  10069  CB  ASN C 278     -55.545  49.012  12.613  1.00106.03           C  
ANISOU10069  CB  ASN C 278    13625  17116   9543  -3801   -160    583       C  
ATOM  10070  CG  ASN C 278     -55.114  48.199  11.415  1.00131.68           C  
ANISOU10070  CG  ASN C 278    17109  20431  12491  -4069    -89    431       C  
ATOM  10071  OD1 ASN C 278     -54.268  47.301  11.503  1.00125.96           O  
ANISOU10071  OD1 ASN C 278    16703  19455  11702  -4007     52    169       O  
ATOM  10072  ND2 ASN C 278     -55.658  48.521  10.254  1.00126.04           N  
ANISOU10072  ND2 ASN C 278    16244  20056  11589  -4373   -166    610       N  
ATOM  10073  N   THR C 279     -57.266  49.656  15.329  1.00102.43           N  
ANISOU10073  N   THR C 279    12955  16473   9493  -3472   -225    828       N  
ATOM  10074  CA  THR C 279     -57.539  50.487  16.509  1.00100.60           C  
ANISOU10074  CA  THR C 279    12584  16101   9537  -3195   -213    941       C  
ATOM  10075  C   THR C 279     -57.428  49.654  17.797  1.00103.22           C  
ANISOU10075  C   THR C 279    13186  16140   9895  -3050   -166    725       C  
ATOM  10076  O   THR C 279     -56.891  50.151  18.789  1.00101.56           O  
ANISOU10076  O   THR C 279    12996  15707   9885  -2770   -135    661       O  
ATOM  10077  CB  THR C 279     -58.869  51.252  16.354  1.00107.86           C  
ANISOU10077  CB  THR C 279    13189  17268  10525  -3303   -249   1318       C  
ATOM  10078  OG1 THR C 279     -58.796  52.061  15.179  1.00107.15           O  
ANISOU10078  OG1 THR C 279    12831  17446  10433  -3411   -287   1520       O  
ATOM  10079  CG2 THR C 279     -59.186  52.147  17.555  1.00104.89           C  
ANISOU10079  CG2 THR C 279    12700  16716  10436  -3015   -180   1443       C  
ATOM  10080  N   VAL C 280     -57.888  48.381  17.765  1.00100.30           N  
ANISOU10080  N   VAL C 280    13031  15769   9310  -3256   -159    610       N  
ATOM  10081  CA  VAL C 280     -57.774  47.486  18.919  1.00 99.42           C  
ANISOU10081  CA  VAL C 280    13167  15393   9215  -3130   -105    411       C  
ATOM  10082  C   VAL C 280     -56.318  47.128  19.195  1.00101.85           C  
ANISOU10082  C   VAL C 280    13670  15455   9574  -2935    -36    152       C  
ATOM  10083  O   VAL C 280     -55.886  47.284  20.333  1.00100.63           O  
ANISOU10083  O   VAL C 280    13565  15086   9583  -2687    -18     83       O  
ATOM  10084  CB  VAL C 280     -58.729  46.258  18.961  1.00104.92           C  
ANISOU10084  CB  VAL C 280    14026  16131   9708  -3378   -106    378       C  
ATOM  10085  CG1 VAL C 280     -60.183  46.686  19.130  1.00105.53           C  
ANISOU10085  CG1 VAL C 280    13886  16396   9815  -3485   -174    688       C  
ATOM  10086  CG2 VAL C 280     -58.559  45.351  17.747  1.00106.59           C  
ANISOU10086  CG2 VAL C 280    14407  16457   9635  -3698    -86    255       C  
ATOM  10087  N   HIS C 281     -55.542  46.741  18.150  1.00 97.96           N  
ANISOU10087  N   HIS C 281    13271  14999   8951  -3045      9     42       N  
ATOM  10088  CA  HIS C 281     -54.117  46.402  18.277  1.00 96.64           C  
ANISOU10088  CA  HIS C 281    13261  14609   8849  -2861    100   -146       C  
ATOM  10089  C   HIS C 281     -53.316  47.581  18.813  1.00 96.94           C  
ANISOU10089  C   HIS C 281    13128  14562   9141  -2574     48    -76       C  
ATOM  10090  O   HIS C 281     -52.333  47.377  19.533  1.00 95.73           O  
ANISOU10090  O   HIS C 281    13078  14191   9103  -2372     86   -180       O  
ATOM  10091  CB  HIS C 281     -53.531  45.938  16.942  1.00 99.08           C  
ANISOU10091  CB  HIS C 281    13681  14987   8979  -3034    183   -227       C  
ATOM  10092  CG  HIS C 281     -53.438  44.449  16.805  1.00104.05           C  
ANISOU10092  CG  HIS C 281    14636  15478   9418  -3182    335   -430       C  
ATOM  10093  ND1 HIS C 281     -54.270  43.749  15.944  1.00107.87           N  
ANISOU10093  ND1 HIS C 281    15250  16119   9619  -3544    356   -457       N  
ATOM  10094  CD2 HIS C 281     -52.598  43.574  17.409  1.00105.74           C  
ANISOU10094  CD2 HIS C 281    15066  15416   9693  -3024    484   -593       C  
ATOM  10095  CE1 HIS C 281     -53.911  42.481  16.055  1.00108.24           C  
ANISOU10095  CE1 HIS C 281    15609  15952   9564  -3589    535   -663       C  
ATOM  10096  NE2 HIS C 281     -52.913  42.326  16.926  1.00107.30           N  
ANISOU10096  NE2 HIS C 281    15539  15571   9660  -3269    627   -738       N  
ATOM  10097  N   LYS C 282     -53.751  48.816  18.466  1.00 91.93           N  
ANISOU10097  N   LYS C 282    12227  14105   8596  -2573    -36    122       N  
ATOM  10098  CA  LYS C 282     -53.156  50.070  18.926  1.00 89.96           C  
ANISOU10098  CA  LYS C 282    11808  13788   8584  -2337    -80    205       C  
ATOM  10099  C   LYS C 282     -53.448  50.194  20.416  1.00 90.12           C  
ANISOU10099  C   LYS C 282    11891  13623   8727  -2178    -86    184       C  
ATOM  10100  O   LYS C 282     -52.520  50.376  21.204  1.00 87.95           O  
ANISOU10100  O   LYS C 282    11689  13155   8574  -1991    -94    101       O  
ATOM  10101  CB  LYS C 282     -53.742  51.272  18.148  1.00 93.41           C  
ANISOU10101  CB  LYS C 282    11942  14466   9082  -2401   -129    443       C  
ATOM  10102  CG  LYS C 282     -52.953  52.572  18.328  1.00109.41           C  
ANISOU10102  CG  LYS C 282    13800  16428  11344  -2183   -153    515       C  
ATOM  10103  CD  LYS C 282     -53.761  53.824  17.992  1.00118.93           C  
ANISOU10103  CD  LYS C 282    14702  17813  12672  -2197   -161    778       C  
ATOM  10104  CE  LYS C 282     -54.162  54.592  19.230  1.00124.16           C  
ANISOU10104  CE  LYS C 282    15343  18308  13525  -2028   -121    841       C  
ATOM  10105  NZ  LYS C 282     -54.591  55.981  18.918  1.00130.37           N  
ANISOU10105  NZ  LYS C 282    15834  19203  14496  -1977    -79   1094       N  
ATOM  10106  N   TRP C 283     -54.734  50.026  20.797  1.00 86.52           N  
ANISOU10106  N   TRP C 283    11419  13230   8224  -2271    -82    272       N  
ATOM  10107  CA  TRP C 283     -55.202  50.098  22.181  1.00 85.59           C  
ANISOU10107  CA  TRP C 283    11375  12945   8199  -2138    -65    266       C  
ATOM  10108  C   TRP C 283     -54.745  48.958  23.081  1.00 85.84           C  
ANISOU10108  C   TRP C 283    11664  12772   8178  -2074    -40     60       C  
ATOM  10109  O   TRP C 283     -54.526  49.195  24.264  1.00 84.72           O  
ANISOU10109  O   TRP C 283    11596  12454   8139  -1913    -41     18       O  
ATOM  10110  CB  TRP C 283     -56.704  50.364  22.259  1.00 85.70           C  
ANISOU10110  CB  TRP C 283    11260  13090   8211  -2233    -49    476       C  
ATOM  10111  CG  TRP C 283     -57.019  51.815  22.078  1.00 87.45           C  
ANISOU10111  CG  TRP C 283    11230  13391   8604  -2160    -29    706       C  
ATOM  10112  CD1 TRP C 283     -57.311  52.453  20.907  1.00 91.35           C  
ANISOU10112  CD1 TRP C 283    11473  14132   9103  -2280    -46    908       C  
ATOM  10113  CD2 TRP C 283     -56.937  52.833  23.081  1.00 86.97           C  
ANISOU10113  CD2 TRP C 283    11157  13148   8740  -1951     32    747       C  
ATOM  10114  NE1 TRP C 283     -57.477  53.801  21.130  1.00 91.02           N  
ANISOU10114  NE1 TRP C 283    11239  14070   9276  -2139     15   1094       N  
ATOM  10115  CE2 TRP C 283     -57.252  54.062  22.458  1.00 91.86           C  
ANISOU10115  CE2 TRP C 283    11507  13899   9497  -1941     74    987       C  
ATOM  10116  CE3 TRP C 283     -56.658  52.824  24.458  1.00 87.64           C  
ANISOU10116  CE3 TRP C 283    11443  12970   8887  -1787     66    612       C  
ATOM  10117  CZ2 TRP C 283     -57.297  55.270  23.166  1.00 91.29           C  
ANISOU10117  CZ2 TRP C 283    11382  13673   9630  -1768    176   1080       C  
ATOM  10118  CZ3 TRP C 283     -56.704  54.019  25.158  1.00 89.18           C  
ANISOU10118  CZ3 TRP C 283    11608  13024   9254  -1641    148    692       C  
ATOM  10119  CH2 TRP C 283     -57.017  55.224  24.515  1.00 90.56           C  
ANISOU10119  CH2 TRP C 283    11534  13303   9572  -1628    216    916       C  
ATOM  10120  N   ILE C 284     -54.540  47.747  22.519  1.00 80.67           N  
ANISOU10120  N   ILE C 284    11152  12134   7365  -2206     -3    -65       N  
ATOM  10121  CA  ILE C 284     -54.006  46.581  23.234  1.00 79.43           C  
ANISOU10121  CA  ILE C 284    11222  11785   7173  -2145     56   -243       C  
ATOM  10122  C   ILE C 284     -52.567  46.902  23.686  1.00 81.93           C  
ANISOU10122  C   ILE C 284    11561  11942   7626  -1944     48   -300       C  
ATOM  10123  O   ILE C 284     -52.188  46.553  24.802  1.00 81.35           O  
ANISOU10123  O   ILE C 284    11593  11704   7614  -1819     52   -362       O  
ATOM  10124  CB  ILE C 284     -54.107  45.293  22.358  1.00 83.48           C  
ANISOU10124  CB  ILE C 284    11889  12342   7488  -2351    143   -351       C  
ATOM  10125  CG1 ILE C 284     -55.519  44.697  22.432  1.00 84.54           C  
ANISOU10125  CG1 ILE C 284    12059  12571   7493  -2538    136   -311       C  
ATOM  10126  CG2 ILE C 284     -53.052  44.226  22.713  1.00 84.03           C  
ANISOU10126  CG2 ILE C 284    12162  12200   7565  -2256    258   -516       C  
ATOM  10127  CD1 ILE C 284     -55.956  44.032  21.173  1.00 92.67           C  
ANISOU10127  CD1 ILE C 284    13151  13761   8297  -2840    167   -330       C  
ATOM  10128  N   SER C 285     -51.793  47.597  22.825  1.00 77.71           N  
ANISOU10128  N   SER C 285    10910  11475   7142  -1925     25   -251       N  
ATOM  10129  CA  SER C 285     -50.420  48.010  23.104  1.00 76.58           C  
ANISOU10129  CA  SER C 285    10749  11211   7137  -1756     -2   -254       C  
ATOM  10130  C   SER C 285     -50.354  49.119  24.151  1.00 78.79           C  
ANISOU10130  C   SER C 285    10957  11418   7561  -1625    -98   -192       C  
ATOM  10131  O   SER C 285     -49.431  49.117  24.976  1.00 78.49           O  
ANISOU10131  O   SER C 285    10980  11238   7604  -1509   -135   -215       O  
ATOM  10132  CB  SER C 285     -49.713  48.433  21.824  1.00 80.17           C  
ANISOU10132  CB  SER C 285    11094  11766   7601  -1779      7   -204       C  
ATOM  10133  OG  SER C 285     -49.538  47.305  20.983  1.00 89.93           O  
ANISOU10133  OG  SER C 285    12467  13009   8695  -1892    133   -289       O  
ATOM  10134  N   ILE C 286     -51.336  50.057  24.128  1.00 73.79           N  
ANISOU10134  N   ILE C 286    10201  10879   6956  -1658   -124    -95       N  
ATOM  10135  CA  ILE C 286     -51.432  51.160  25.097  1.00 72.52           C  
ANISOU10135  CA  ILE C 286    10011  10624   6920  -1553   -164    -42       C  
ATOM  10136  C   ILE C 286     -51.769  50.585  26.477  1.00 74.60           C  
ANISOU10136  C   ILE C 286    10459  10734   7151  -1508   -150   -123       C  
ATOM  10137  O   ILE C 286     -51.127  50.952  27.461  1.00 73.73           O  
ANISOU10137  O   ILE C 286    10432  10481   7100  -1422   -197   -157       O  
ATOM  10138  CB  ILE C 286     -52.426  52.269  24.645  1.00 75.76           C  
ANISOU10138  CB  ILE C 286    10235  11159   7392  -1587   -135    116       C  
ATOM  10139  CG1 ILE C 286     -51.945  52.950  23.354  1.00 76.39           C  
ANISOU10139  CG1 ILE C 286    10111  11392   7521  -1615   -160    209       C  
ATOM  10140  CG2 ILE C 286     -52.658  53.317  25.753  1.00 76.26           C  
ANISOU10140  CG2 ILE C 286    10328  11073   7575  -1483   -112    156       C  
ATOM  10141  CD1 ILE C 286     -53.045  53.546  22.528  1.00 86.00           C  
ANISOU10141  CD1 ILE C 286    11116  12814   8748  -1710   -119    394       C  
ATOM  10142  N   THR C 287     -52.749  49.666  26.527  1.00 70.64           N  
ANISOU10142  N   THR C 287    10024  10271   6544  -1584    -94   -147       N  
ATOM  10143  CA  THR C 287     -53.197  49.007  27.753  1.00 70.38           C  
ANISOU10143  CA  THR C 287    10154  10111   6475  -1543    -70   -214       C  
ATOM  10144  C   THR C 287     -52.136  48.066  28.339  1.00 75.74           C  
ANISOU10144  C   THR C 287    10973  10669   7136  -1488    -87   -330       C  
ATOM  10145  O   THR C 287     -52.086  47.924  29.565  1.00 75.75           O  
ANISOU10145  O   THR C 287    11090  10547   7146  -1420   -102   -368       O  
ATOM  10146  CB  THR C 287     -54.543  48.299  27.557  1.00 73.22           C  
ANISOU10146  CB  THR C 287    10521  10558   6740  -1647    -11   -179       C  
ATOM  10147  OG1 THR C 287     -54.415  47.299  26.548  1.00 69.39           O  
ANISOU10147  OG1 THR C 287    10051  10171   6143  -1777     10   -235       O  
ATOM  10148  CG2 THR C 287     -55.686  49.266  27.246  1.00 70.38           C  
ANISOU10148  CG2 THR C 287    10005  10308   6429  -1684     17      4       C  
ATOM  10149  N   GLU C 288     -51.297  47.429  27.476  1.00 72.43           N  
ANISOU10149  N   GLU C 288    10540  10283   6695  -1517    -65   -363       N  
ATOM  10150  CA  GLU C 288     -50.209  46.536  27.891  1.00 72.46           C  
ANISOU10150  CA  GLU C 288    10639  10176   6718  -1453    -42   -415       C  
ATOM  10151  C   GLU C 288     -49.129  47.365  28.587  1.00 77.06           C  
ANISOU10151  C   GLU C 288    11188  10682   7409  -1357   -150   -358       C  
ATOM  10152  O   GLU C 288     -48.706  47.022  29.693  1.00 76.78           O  
ANISOU10152  O   GLU C 288    11237  10547   7388  -1305   -183   -363       O  
ATOM  10153  CB  GLU C 288     -49.615  45.783  26.685  1.00 74.39           C  
ANISOU10153  CB  GLU C 288    10881  10455   6927  -1503     56   -437       C  
ATOM  10154  CG  GLU C 288     -48.606  44.709  27.073  1.00 85.32           C  
ANISOU10154  CG  GLU C 288    12359  11709   8352  -1427    144   -453       C  
ATOM  10155  CD  GLU C 288     -48.028  43.837  25.973  1.00107.33           C  
ANISOU10155  CD  GLU C 288    15195  14475  11108  -1462    311   -477       C  
ATOM  10156  OE1 GLU C 288     -47.043  43.121  26.264  1.00 94.66           O  
ANISOU10156  OE1 GLU C 288    13633  12749   9584  -1368    408   -436       O  
ATOM  10157  OE2 GLU C 288     -48.558  43.848  24.837  1.00105.94           O  
ANISOU10157  OE2 GLU C 288    15023  14402  10828  -1590    361   -520       O  
ATOM  10158  N   ALA C 289     -48.709  48.468  27.938  1.00 73.96           N  
ANISOU10158  N   ALA C 289    10668  10348   7085  -1351   -213   -290       N  
ATOM  10159  CA  ALA C 289     -47.726  49.410  28.459  1.00 73.70           C  
ANISOU10159  CA  ALA C 289    10595  10257   7150  -1295   -330   -224       C  
ATOM  10160  C   ALA C 289     -48.233  50.003  29.770  1.00 77.19           C  
ANISOU10160  C   ALA C 289    11142  10612   7576  -1294   -383   -251       C  
ATOM  10161  O   ALA C 289     -47.464  50.061  30.726  1.00 77.76           O  
ANISOU10161  O   ALA C 289    11286  10600   7660  -1282   -470   -234       O  
ATOM  10162  CB  ALA C 289     -47.480  50.514  27.446  1.00 74.35           C  
ANISOU10162  CB  ALA C 289    10515  10426   7307  -1297   -365   -153       C  
ATOM  10163  N   LEU C 290     -49.536  50.394  29.828  1.00 72.59           N  
ANISOU10163  N   LEU C 290    10574  10048   6959  -1318   -319   -272       N  
ATOM  10164  CA  LEU C 290     -50.165  50.961  31.026  1.00 72.13           C  
ANISOU10164  CA  LEU C 290    10642   9881   6881  -1309   -312   -295       C  
ATOM  10165  C   LEU C 290     -50.334  49.940  32.140  1.00 75.60           C  
ANISOU10165  C   LEU C 290    11245  10242   7239  -1297   -304   -362       C  
ATOM  10166  O   LEU C 290     -50.359  50.331  33.308  1.00 74.97           O  
ANISOU10166  O   LEU C 290    11306  10051   7128  -1295   -330   -388       O  
ATOM  10167  CB  LEU C 290     -51.508  51.639  30.716  1.00 71.99           C  
ANISOU10167  CB  LEU C 290    10571   9900   6883  -1315   -206   -244       C  
ATOM  10168  CG  LEU C 290     -51.457  53.030  30.085  1.00 76.61           C  
ANISOU10168  CG  LEU C 290    11019  10515   7574  -1311   -194   -155       C  
ATOM  10169  CD1 LEU C 290     -52.818  53.437  29.599  1.00 76.78           C  
ANISOU10169  CD1 LEU C 290    10931  10612   7628  -1319    -66    -46       C  
ATOM  10170  CD2 LEU C 290     -50.938  54.076  31.062  1.00 79.81           C  
ANISOU10170  CD2 LEU C 290    11548  10758   8019  -1297   -223   -179       C  
ATOM  10171  N   ALA C 291     -50.439  48.638  31.787  1.00 72.33           N  
ANISOU10171  N   ALA C 291    10825   9875   6782  -1298   -255   -392       N  
ATOM  10172  CA  ALA C 291     -50.579  47.556  32.764  1.00 72.56           C  
ANISOU10172  CA  ALA C 291    10981   9838   6752  -1277   -232   -443       C  
ATOM  10173  C   ALA C 291     -49.294  47.340  33.543  1.00 78.76           C  
ANISOU10173  C   ALA C 291    11805  10565   7556  -1259   -325   -414       C  
ATOM  10174  O   ALA C 291     -49.366  46.998  34.720  1.00 79.40           O  
ANISOU10174  O   ALA C 291    12001  10580   7587  -1251   -347   -432       O  
ATOM  10175  CB  ALA C 291     -50.984  46.271  32.080  1.00 73.05           C  
ANISOU10175  CB  ALA C 291    11027   9954   6777  -1296   -132   -478       C  
ATOM  10176  N   PHE C 292     -48.125  47.591  32.911  1.00 76.34           N  
ANISOU10176  N   PHE C 292    11393  10293   7322  -1259   -386   -341       N  
ATOM  10177  CA  PHE C 292     -46.792  47.447  33.511  1.00 77.29           C  
ANISOU10177  CA  PHE C 292    11500  10384   7481  -1256   -489   -244       C  
ATOM  10178  C   PHE C 292     -46.668  48.178  34.852  1.00 83.24           C  
ANISOU10178  C   PHE C 292    12375  11077   8176  -1315   -615   -241       C  
ATOM  10179  O   PHE C 292     -45.843  47.792  35.683  1.00 83.77           O  
ANISOU10179  O   PHE C 292    12462  11135   8231  -1343   -703   -155       O  
ATOM  10180  CB  PHE C 292     -45.681  47.749  32.484  1.00 79.34           C  
ANISOU10180  CB  PHE C 292    11608  10691   7845  -1239   -521   -137       C  
ATOM  10181  CG  PHE C 292     -45.619  46.844  31.270  1.00 80.77           C  
ANISOU10181  CG  PHE C 292    11718  10909   8062  -1194   -370   -138       C  
ATOM  10182  CD1 PHE C 292     -46.150  45.557  31.307  1.00 83.72           C  
ANISOU10182  CD1 PHE C 292    12165  11256   8389  -1178   -224   -203       C  
ATOM  10183  CD2 PHE C 292     -44.982  47.260  30.105  1.00 82.85           C  
ANISOU10183  CD2 PHE C 292    11859  11219   8400  -1176   -361    -73       C  
ATOM  10184  CE1 PHE C 292     -46.086  44.724  30.187  1.00 84.68           C  
ANISOU10184  CE1 PHE C 292    12270  11387   8519  -1169    -60   -223       C  
ATOM  10185  CE2 PHE C 292     -44.908  46.420  28.990  1.00 85.63           C  
ANISOU10185  CE2 PHE C 292    12190  11589   8758  -1154   -198    -85       C  
ATOM  10186  CZ  PHE C 292     -45.459  45.159  29.039  1.00 83.84           C  
ANISOU10186  CZ  PHE C 292    12067  11322   8467  -1162    -42   -168       C  
ATOM  10187  N   PHE C 293     -47.528  49.197  35.077  1.00 80.84           N  
ANISOU10187  N   PHE C 293    12159  10729   7827  -1345   -604   -319       N  
ATOM  10188  CA  PHE C 293     -47.620  49.971  36.314  1.00 82.18           C  
ANISOU10188  CA  PHE C 293    12506  10806   7912  -1418   -672   -353       C  
ATOM  10189  C   PHE C 293     -47.789  49.076  37.559  1.00 86.32           C  
ANISOU10189  C   PHE C 293    13166  11295   8336  -1429   -678   -374       C  
ATOM  10190  O   PHE C 293     -47.531  49.526  38.680  1.00 86.84           O  
ANISOU10190  O   PHE C 293    13389  11301   8304  -1523   -764   -381       O  
ATOM  10191  CB  PHE C 293     -48.703  51.061  36.182  1.00 84.29           C  
ANISOU10191  CB  PHE C 293    12843  11006   8177  -1413   -568   -422       C  
ATOM  10192  CG  PHE C 293     -48.601  52.207  37.163  1.00 87.55           C  
ANISOU10192  CG  PHE C 293    13452  11292   8521  -1506   -605   -458       C  
ATOM  10193  CD1 PHE C 293     -47.733  53.270  36.931  1.00 91.49           C  
ANISOU10193  CD1 PHE C 293    13926  11775   9060  -1586   -704   -420       C  
ATOM  10194  CD2 PHE C 293     -49.404  52.246  38.299  1.00 90.66           C  
ANISOU10194  CD2 PHE C 293    14074  11569   8805  -1522   -522   -534       C  
ATOM  10195  CE1 PHE C 293     -47.647  54.334  37.836  1.00 93.84           C  
ANISOU10195  CE1 PHE C 293    14446  11935   9275  -1705   -720   -471       C  
ATOM  10196  CE2 PHE C 293     -49.313  53.309  39.206  1.00 94.86           C  
ANISOU10196  CE2 PHE C 293    14839  11957   9248  -1631   -523   -585       C  
ATOM  10197  CZ  PHE C 293     -48.438  54.347  38.966  1.00 93.64           C  
ANISOU10197  CZ  PHE C 293    14677  11781   9122  -1734   -620   -561       C  
ATOM  10198  N   HIS C 294     -48.157  47.790  37.351  1.00 82.14           N  
ANISOU10198  N   HIS C 294    12581  10806   7825  -1349   -586   -380       N  
ATOM  10199  CA  HIS C 294     -48.287  46.795  38.416  1.00 82.55           C  
ANISOU10199  CA  HIS C 294    12717  10839   7810  -1337   -576   -380       C  
ATOM  10200  C   HIS C 294     -46.952  46.546  39.154  1.00 87.26           C  
ANISOU10200  C   HIS C 294    13287  11473   8397  -1408   -724   -244       C  
ATOM  10201  O   HIS C 294     -46.964  46.080  40.294  1.00 87.82           O  
ANISOU10201  O   HIS C 294    13448  11534   8384  -1440   -759   -225       O  
ATOM  10202  CB  HIS C 294     -48.951  45.497  37.903  1.00 82.70           C  
ANISOU10202  CB  HIS C 294    12671  10882   7868  -1243   -429   -412       C  
ATOM  10203  CG  HIS C 294     -48.060  44.610  37.088  1.00 86.28           C  
ANISOU10203  CG  HIS C 294    12975  11389   8420  -1208   -391   -328       C  
ATOM  10204  ND1 HIS C 294     -47.327  43.593  37.673  1.00 88.93           N  
ANISOU10204  ND1 HIS C 294    13272  11729   8788  -1182   -384   -226       N  
ATOM  10205  CD2 HIS C 294     -47.848  44.584  35.751  1.00 87.73           C  
ANISOU10205  CD2 HIS C 294    13048  11610   8675  -1190   -327   -322       C  
ATOM  10206  CE1 HIS C 294     -46.684  42.998  36.680  1.00 88.39           C  
ANISOU10206  CE1 HIS C 294    13083  11678   8824  -1138   -292   -159       C  
ATOM  10207  NE2 HIS C 294     -46.965  43.560  35.507  1.00 88.06           N  
ANISOU10207  NE2 HIS C 294    13009  11655   8796  -1147   -259   -226       N  
ATOM  10208  N   CYS C 295     -45.821  46.927  38.512  1.00 83.62           N  
ANISOU10208  N   CYS C 295    12690  11062   8020  -1440   -816   -125       N  
ATOM  10209  CA  CYS C 295     -44.457  46.868  39.044  1.00 84.71           C  
ANISOU10209  CA  CYS C 295    12757  11257   8173  -1526   -977     69       C  
ATOM  10210  C   CYS C 295     -44.241  48.003  40.061  1.00 89.45           C  
ANISOU10210  C   CYS C 295    13525  11829   8632  -1705  -1150     55       C  
ATOM  10211  O   CYS C 295     -43.321  47.930  40.881  1.00 90.41           O  
ANISOU10211  O   CYS C 295    13641  12009   8700  -1833  -1311    213       O  
ATOM  10212  CB  CYS C 295     -43.434  46.958  37.914  1.00 85.07           C  
ANISOU10212  CB  CYS C 295    12600  11353   8370  -1487   -995    214       C  
ATOM  10213  SG  CYS C 295     -43.602  45.680  36.644  1.00 88.13           S  
ANISOU10213  SG  CYS C 295    12847  11743   8895  -1312   -756    215       S  
ATOM  10214  N   CYS C 296     -45.091  49.048  39.997  1.00 85.39           N  
ANISOU10214  N   CYS C 296    13165  11224   8055  -1729  -1104   -116       N  
ATOM  10215  CA  CYS C 296     -45.028  50.249  40.828  1.00 86.28           C  
ANISOU10215  CA  CYS C 296    13491  11261   8030  -1902  -1205   -173       C  
ATOM  10216  C   CYS C 296     -45.987  50.273  42.019  1.00 90.52           C  
ANISOU10216  C   CYS C 296    14298  11698   8396  -1945  -1132   -309       C  
ATOM  10217  O   CYS C 296     -45.803  51.105  42.905  1.00 91.70           O  
ANISOU10217  O   CYS C 296    14670  11778   8394  -2125  -1213   -349       O  
ATOM  10218  CB  CYS C 296     -45.193  51.496  39.962  1.00 86.25           C  
ANISOU10218  CB  CYS C 296    13479  11195   8095  -1898  -1167   -239       C  
ATOM  10219  SG  CYS C 296     -44.030  51.601  38.577  1.00 89.58           S  
ANISOU10219  SG  CYS C 296    13598  11727   8709  -1849  -1255    -74       S  
ATOM  10220  N   LEU C 297     -46.988  49.375  42.059  1.00 86.18           N  
ANISOU10220  N   LEU C 297    13746  11134   7863  -1796   -976   -376       N  
ATOM  10221  CA  LEU C 297     -47.991  49.332  43.136  1.00 86.48           C  
ANISOU10221  CA  LEU C 297    14027  11070   7760  -1800   -878   -489       C  
ATOM  10222  C   LEU C 297     -47.434  48.980  44.506  1.00 91.97           C  
ANISOU10222  C   LEU C 297    14858  11800   8287  -1950  -1014   -435       C  
ATOM  10223  O   LEU C 297     -47.688  49.714  45.462  1.00 92.83           O  
ANISOU10223  O   LEU C 297    15247  11804   8221  -2085  -1016   -522       O  
ATOM  10224  CB  LEU C 297     -49.156  48.402  42.788  1.00 85.06           C  
ANISOU10224  CB  LEU C 297    13779  10883   7655  -1606   -696   -540       C  
ATOM  10225  CG  LEU C 297     -49.949  48.715  41.532  1.00 88.62           C  
ANISOU10225  CG  LEU C 297    14115  11318   8237  -1487   -555   -581       C  
ATOM  10226  CD1 LEU C 297     -50.800  47.545  41.158  1.00 87.60           C  
ANISOU10226  CD1 LEU C 297    13884  11229   8169  -1350   -434   -588       C  
ATOM  10227  CD2 LEU C 297     -50.806  49.966  41.700  1.00 92.01           C  
ANISOU10227  CD2 LEU C 297    14723  11604   8633  -1498   -432   -658       C  
ATOM  10228  N   ASN C 298     -46.707  47.849  44.603  1.00 88.52           N  
ANISOU10228  N   ASN C 298    14229  11502   7901  -1931  -1104   -281       N  
ATOM  10229  CA  ASN C 298     -46.074  47.367  45.834  1.00 89.81           C  
ANISOU10229  CA  ASN C 298    14447  11749   7927  -2077  -1249   -163       C  
ATOM  10230  C   ASN C 298     -45.177  48.449  46.491  1.00 95.26           C  
ANISOU10230  C   ASN C 298    15296  12451   8447  -2365  -1459   -113       C  
ATOM  10231  O   ASN C 298     -45.427  48.745  47.665  1.00 95.92           O  
ANISOU10231  O   ASN C 298    15647  12488   8311  -2523  -1494   -182       O  
ATOM  10232  CB  ASN C 298     -45.343  46.042  45.587  1.00 90.79           C  
ANISOU10232  CB  ASN C 298    14279  12020   8197  -1988  -1276     48       C  
ATOM  10233  CG  ASN C 298     -44.260  45.693  46.575  1.00115.49           C  
ANISOU10233  CG  ASN C 298    17353  15290  11238  -2169  -1473    281       C  
ATOM  10234  OD1 ASN C 298     -44.518  45.375  47.738  1.00112.31           O  
ANISOU10234  OD1 ASN C 298    17082  14912  10679  -2250  -1506    282       O  
ATOM  10235  ND2 ASN C 298     -43.021  45.704  46.114  1.00107.92           N  
ANISOU10235  ND2 ASN C 298    16179  14441  10386  -2234  -1605    515       N  
ATOM  10236  N   PRO C 299     -44.210  49.106  45.770  1.00 92.20           N  
ANISOU10236  N   PRO C 299    14781  12109   8141  -2450  -1589    -10       N  
ATOM  10237  CA  PRO C 299     -43.393  50.155  46.413  1.00 94.52           C  
ANISOU10237  CA  PRO C 299    15244  12409   8259  -2757  -1799     36       C  
ATOM  10238  C   PRO C 299     -44.162  51.416  46.835  1.00 99.34           C  
ANISOU10238  C   PRO C 299    16228  12817   8700  -2870  -1704   -213       C  
ATOM  10239  O   PRO C 299     -43.861  51.976  47.894  1.00100.77           O  
ANISOU10239  O   PRO C 299    16679  12972   8638  -3149  -1823   -235       O  
ATOM  10240  CB  PRO C 299     -42.328  50.468  45.354  1.00 95.89           C  
ANISOU10240  CB  PRO C 299    15156  12666   8613  -2757  -1917    208       C  
ATOM  10241  CG  PRO C 299     -42.312  49.287  44.461  1.00 98.11           C  
ANISOU10241  CG  PRO C 299    15125  13024   9128  -2490  -1802    317       C  
ATOM  10242  CD  PRO C 299     -43.745  48.888  44.386  1.00 92.01           C  
ANISOU10242  CD  PRO C 299    14461  12140   8358  -2294  -1560     88       C  
ATOM  10243  N   ILE C 300     -45.156  51.859  46.024  1.00 94.60           N  
ANISOU10243  N   ILE C 300    15651  12071   8223  -2668  -1475   -383       N  
ATOM  10244  CA  ILE C 300     -45.993  53.033  46.327  1.00 95.39           C  
ANISOU10244  CA  ILE C 300    16083  11948   8215  -2723  -1307   -590       C  
ATOM  10245  C   ILE C 300     -46.847  52.783  47.574  1.00100.70           C  
ANISOU10245  C   ILE C 300    17062  12515   8684  -2756  -1189   -708       C  
ATOM  10246  O   ILE C 300     -47.067  53.714  48.352  1.00102.38           O  
ANISOU10246  O   ILE C 300    17639  12561   8702  -2938  -1127   -835       O  
ATOM  10247  CB  ILE C 300     -46.786  53.548  45.073  1.00 96.78           C  
ANISOU10247  CB  ILE C 300    16140  12026   8607  -2494  -1092   -670       C  
ATOM  10248  CG1 ILE C 300     -46.017  54.670  44.340  1.00 97.86           C  
ANISOU10248  CG1 ILE C 300    16217  12146   8820  -2597  -1178   -639       C  
ATOM  10249  CG2 ILE C 300     -48.220  54.015  45.393  1.00 97.43           C  
ANISOU10249  CG2 ILE C 300    16472  11894   8653  -2388   -796   -833       C  
ATOM  10250  CD1 ILE C 300     -44.897  54.224  43.386  1.00104.38           C  
ANISOU10250  CD1 ILE C 300    16679  13169   9813  -2561  -1372   -449       C  
ATOM  10251  N   LEU C 301     -47.265  51.513  47.789  1.00 96.34           N  
ANISOU10251  N   LEU C 301    16376  12056   8172  -2594  -1153   -659       N  
ATOM  10252  CA  LEU C 301     -48.047  51.085  48.952  1.00 96.89           C  
ANISOU10252  CA  LEU C 301    16687  12056   8072  -2594  -1050   -739       C  
ATOM  10253  C   LEU C 301     -47.267  51.177  50.270  1.00102.65           C  
ANISOU10253  C   LEU C 301    17641  12847   8516  -2914  -1252   -695       C  
ATOM  10254  O   LEU C 301     -47.874  51.409  51.310  1.00103.44           O  
ANISOU10254  O   LEU C 301    18080  12818   8404  -3000  -1149   -815       O  
ATOM  10255  CB  LEU C 301     -48.632  49.673  48.744  1.00 95.06           C  
ANISOU10255  CB  LEU C 301    16218  11919   7983  -2336   -970   -680       C  
ATOM  10256  CG  LEU C 301     -50.147  49.558  48.459  1.00 98.48           C  
ANISOU10256  CG  LEU C 301    16701  12205   8513  -2083   -685   -795       C  
ATOM  10257  CD1 LEU C 301     -50.990  49.995  49.647  1.00100.29           C  
ANISOU10257  CD1 LEU C 301    17312  12250   8542  -2131   -531   -916       C  
ATOM  10258  CD2 LEU C 301     -50.557  50.300  47.179  1.00 99.79           C  
ANISOU10258  CD2 LEU C 301    16756  12296   8862  -1964   -557   -832       C  
ATOM  10259  N   TYR C 302     -45.932  51.029  50.225  1.00 99.93           N  
ANISOU10259  N   TYR C 302    17113  12697   8159  -3103  -1533   -504       N  
ATOM  10260  CA  TYR C 302     -45.077  51.164  51.402  1.00102.64           C  
ANISOU10260  CA  TYR C 302    17632  13142   8223  -3462  -1770   -410       C  
ATOM  10261  C   TYR C 302     -44.996  52.640  51.830  1.00110.17           C  
ANISOU10261  C   TYR C 302    18998  13915   8948  -3755  -1771   -573       C  
ATOM  10262  O   TYR C 302     -44.975  52.934  53.027  1.00112.54           O  
ANISOU10262  O   TYR C 302    19649  14175   8937  -4034  -1822   -636       O  
ATOM  10263  CB  TYR C 302     -43.674  50.607  51.123  1.00103.92           C  
ANISOU10263  CB  TYR C 302    17434  13572   8478  -3570  -2058    -98       C  
ATOM  10264  CG  TYR C 302     -43.550  49.113  51.331  1.00104.52           C  
ANISOU10264  CG  TYR C 302    17216  13837   8661  -3417  -2082    102       C  
ATOM  10265  CD1 TYR C 302     -43.593  48.562  52.608  1.00108.18           C  
ANISOU10265  CD1 TYR C 302    17803  14391   8909  -3563  -2153    163       C  
ATOM  10266  CD2 TYR C 302     -43.325  48.256  50.258  1.00103.03           C  
ANISOU10266  CD2 TYR C 302    16630  13735   8783  -3143  -2027    245       C  
ATOM  10267  CE1 TYR C 302     -43.453  47.190  52.809  1.00108.17           C  
ANISOU10267  CE1 TYR C 302    17510  14562   9026  -3418  -2160    369       C  
ATOM  10268  CE2 TYR C 302     -43.172  46.882  50.449  1.00103.35           C  
ANISOU10268  CE2 TYR C 302    16410  13923   8936  -3007  -2013    437       C  
ATOM  10269  CZ  TYR C 302     -43.242  46.353  51.727  1.00111.09           C  
ANISOU10269  CZ  TYR C 302    17492  14993   9725  -3136  -2079    505       C  
ATOM  10270  OH  TYR C 302     -43.101  45.003  51.934  1.00109.51           O  
ANISOU10270  OH  TYR C 302    17020  14934   9653  -2993  -2045    709       O  
ATOM  10271  N   ALA C 303     -44.986  53.559  50.843  1.00106.84           N  
ANISOU10271  N   ALA C 303    18544  13372   8677  -3694  -1695   -647       N  
ATOM  10272  CA  ALA C 303     -44.930  55.005  51.057  1.00109.19           C  
ANISOU10272  CA  ALA C 303    19207  13465   8814  -3937  -1649   -805       C  
ATOM  10273  C   ALA C 303     -46.233  55.552  51.654  1.00115.19           C  
ANISOU10273  C   ALA C 303    20392  13927   9447  -3876  -1305  -1060       C  
ATOM  10274  O   ALA C 303     -46.184  56.226  52.684  1.00117.46           O  
ANISOU10274  O   ALA C 303    21119  14081   9429  -4181  -1293  -1179       O  
ATOM  10275  CB  ALA C 303     -44.603  55.717  49.751  1.00108.53           C  
ANISOU10275  CB  ALA C 303    18908  13350   8978  -3834  -1638   -783       C  
ATOM  10276  N   PHE C 304     -47.390  55.254  51.021  1.00110.62           N  
ANISOU10276  N   PHE C 304    19692  13243   9095  -3499  -1020  -1125       N  
ATOM  10277  CA  PHE C 304     -48.699  55.729  51.476  1.00111.41           C  
ANISOU10277  CA  PHE C 304    20139  13055   9136  -3384   -655  -1309       C  
ATOM  10278  C   PHE C 304     -49.225  55.026  52.722  1.00116.00           C  
ANISOU10278  C   PHE C 304    20953  13621   9499  -3411   -601  -1351       C  
ATOM  10279  O   PHE C 304     -49.580  55.698  53.693  1.00117.73           O  
ANISOU10279  O   PHE C 304    21643  13623   9465  -3590   -444  -1498       O  
ATOM  10280  CB  PHE C 304     -49.733  55.712  50.339  1.00110.82           C  
ANISOU10280  CB  PHE C 304    19825  12897   9385  -2999   -387  -1308       C  
ATOM  10281  CG  PHE C 304     -49.679  56.928  49.446  1.00112.87           C  
ANISOU10281  CG  PHE C 304    20077  13018   9790  -2994   -269  -1344       C  
ATOM  10282  CD1 PHE C 304     -49.281  56.819  48.119  1.00113.99           C  
ANISOU10282  CD1 PHE C 304    19798  13318  10195  -2851   -377  -1230       C  
ATOM  10283  CD2 PHE C 304     -50.026  58.186  49.932  1.00117.83           C  
ANISOU10283  CD2 PHE C 304    21129  13346  10294  -3131    -27  -1489       C  
ATOM  10284  CE1 PHE C 304     -49.232  57.949  47.292  1.00115.14           C  
ANISOU10284  CE1 PHE C 304    19915  13348  10483  -2841   -268  -1248       C  
ATOM  10285  CE2 PHE C 304     -49.970  59.314  49.107  1.00120.94           C  
ANISOU10285  CE2 PHE C 304    21499  13607  10845  -3118    101  -1506       C  
ATOM  10286  CZ  PHE C 304     -49.575  59.188  47.793  1.00116.66           C  
ANISOU10286  CZ  PHE C 304    20505  13250  10570  -2970    -32  -1381       C  
ATOM  10287  N   LEU C 305     -49.283  53.681  52.691  1.00110.87           N  
ANISOU10287  N   LEU C 305    19990  13187   8947  -3234   -709  -1223       N  
ATOM  10288  CA  LEU C 305     -49.765  52.854  53.797  1.00136.06           C  
ANISOU10288  CA  LEU C 305    23323  16402  11971  -3222   -674  -1230       C  
ATOM  10289  C   LEU C 305     -48.609  52.567  54.750  1.00159.58           C  
ANISOU10289  C   LEU C 305    26370  19587  14677  -3583  -1003  -1131       C  
ATOM  10290  O   LEU C 305     -48.629  53.016  55.891  1.00122.59           O  
ANISOU10290  O   LEU C 305    22106  14804   9669  -3851   -988  -1230       O  
ATOM  10291  CB  LEU C 305     -50.346  51.541  53.245  1.00133.13           C  
ANISOU10291  CB  LEU C 305    22560  16166  11857  -2866   -629  -1125       C  
ATOM  10292  CG  LEU C 305     -51.425  50.859  54.068  1.00137.91           C  
ANISOU10292  CG  LEU C 305    23306  16693  12400  -2702   -440  -1167       C  
ATOM  10293  CD1 LEU C 305     -52.414  50.165  53.170  1.00135.13           C  
ANISOU10293  CD1 LEU C 305    22659  16335  12351  -2323   -262  -1127       C  
ATOM  10294  CD2 LEU C 305     -50.828  49.865  55.063  1.00141.66           C  
ANISOU10294  CD2 LEU C 305    23738  17385  12703  -2843   -662  -1060       C  
TER   10295      LEU C 305                                                      
HETATM10296  C1  ITD A1500     -28.403  -0.080  23.035  1.00 72.83           C  
HETATM10297  N1  ITD A1500     -30.641   0.818  22.781  1.00188.81           N  
HETATM10298  S1  ITD A1500     -32.903   0.534  21.160  1.00106.59           S  
HETATM10299  C2  ITD A1500     -29.229   1.100  22.545  1.00101.24           C  
HETATM10300  N2  ITD A1500     -30.455   1.010  20.609  1.00 94.22           N  
HETATM10301  S2  ITD A1500     -30.272   2.983  17.927  1.00 95.23           S  
HETATM10302  C3  ITD A1500     -28.859   2.396  23.265  1.00 54.88           C  
HETATM10303  N3  ITD A1500     -32.532   2.822  16.783  1.00 81.09           N  
HETATM10304  C4  ITD A1500     -31.268   0.778  21.601  1.00129.54           C  
HETATM10305  N4  ITD A1500     -32.135   4.833  17.980  1.00124.06           N  
HETATM10306  C5  ITD A1500     -32.470   0.723  19.486  1.00113.39           C  
HETATM10307  C6  ITD A1500     -29.079   1.241  21.020  1.00131.96           C  
HETATM10308  C7  ITD A1500     -31.081   0.971  19.404  1.00191.69           C  
HETATM10309  C8  ITD A1500     -30.368   1.233  18.104  1.00168.40           C  
HETATM10310  C9  ITD A1500     -31.773   3.609  17.558  1.00117.72           C  
HETATM10311  C10 ITD A1500     -33.854   3.008  16.205  1.00133.38           C  
HETATM10312  C11 ITD A1500     -33.818   3.750  14.876  1.00107.43           C  
HETATM10313  C12 ITD A1500     -35.148   3.572  14.149  1.00 90.75           C  
HETATM10314  C13 ITD A1500     -36.310   4.064  15.009  1.00117.50           C  
HETATM10315  C14 ITD A1500     -36.330   3.380  16.376  1.00 45.18           C  
HETATM10316  C15 ITD A1500     -34.986   3.489  17.106  1.00187.01           C  
HETATM10317  C16 ITD A1500     -32.216   5.324  19.363  1.00 75.22           C  
HETATM10318  C17 ITD A1500     -31.260   4.683  20.371  1.00 99.53           C  
HETATM10319  C18 ITD A1500     -31.481   5.214  21.790  1.00164.68           C  
HETATM10320  C19 ITD A1500     -31.377   6.738  21.877  1.00 37.69           C  
HETATM10321  C20 ITD A1500     -32.245   7.409  20.812  1.00 95.34           C  
HETATM10322  C21 ITD A1500     -32.010   6.838  19.411  1.00105.79           C  
HETATM10323  C1  ITD B1500     -63.280  11.408  21.786  1.00 89.06           C  
HETATM10324  N1  ITD B1500     -64.261   9.210  21.342  1.00223.18           N  
HETATM10325  S1  ITD B1500     -64.889   7.100  19.618  1.00 81.57           S  
HETATM10326  C2  ITD B1500     -64.514  10.649  21.312  1.00 51.76           C  
HETATM10327  N2  ITD B1500     -65.019   9.636  19.342  1.00128.98           N  
HETATM10328  S2  ITD B1500     -67.709  10.061  17.102  1.00103.04           S  
HETATM10329  C3  ITD B1500     -65.733  10.950  22.176  1.00 50.92           C  
HETATM10330  N3  ITD B1500     -67.688   8.317  15.295  1.00117.93           N  
HETATM10331  C4  ITD B1500     -64.594   8.702  20.151  1.00203.21           C  
HETATM10332  N4  ITD B1500     -68.956   7.732  17.203  1.00152.33           N  
HETATM10333  C5  ITD B1500     -65.464   7.735  18.099  1.00147.79           C  
HETATM10334  C6  ITD B1500     -64.851  10.985  19.852  1.00 89.57           C  
HETATM10335  C7  ITD B1500     -65.460   9.151  18.159  1.00158.56           C  
HETATM10336  C8  ITD B1500     -65.947  10.057  17.055  1.00224.09           C  
HETATM10337  C9  ITD B1500     -68.188   8.584  16.505  1.00 39.29           C  
HETATM10338  C10 ITD B1500     -67.833   7.148  14.448  1.00 45.87           C  
HETATM10339  C11 ITD B1500     -68.678   7.369  13.203  1.00153.16           C  
HETATM10340  C12 ITD B1500     -68.315   6.287  12.191  1.00 27.38           C  
HETATM10341  C13 ITD B1500     -68.563   4.892  12.764  1.00169.28           C  
HETATM10342  C14 ITD B1500     -67.864   4.669  14.106  1.00 24.82           C  
HETATM10343  C15 ITD B1500     -68.105   5.800  15.104  1.00132.97           C  
HETATM10344  C16 ITD B1500     -69.470   7.896  18.564  1.00 24.30           C  
HETATM10345  C17 ITD B1500     -68.437   8.413  19.576  1.00 42.86           C  
HETATM10346  C18 ITD B1500     -69.012   8.631  20.974  1.00 41.54           C  
HETATM10347  C19 ITD B1500     -70.336   9.397  20.956  1.00151.67           C  
HETATM10348  C20 ITD B1500     -71.340   8.807  19.967  1.00 37.98           C  
HETATM10349  C21 ITD B1500     -70.735   8.749  18.569  1.00 95.10           C  
HETATM10350  C1  ITD C1500     -47.001  40.592  24.035  1.00 35.05           C  
HETATM10351  N1  ITD C1500     -45.748  42.688  23.901  1.00120.84           N  
HETATM10352  S1  ITD C1500     -45.707  44.971  22.263  1.00128.08           S  
HETATM10353  C2  ITD C1500     -45.673  41.245  23.657  1.00108.22           C  
HETATM10354  N2  ITD C1500     -45.457  42.479  21.746  1.00124.34           N  
HETATM10355  S2  ITD C1500     -43.379  42.051  19.161  1.00106.76           S  
HETATM10356  C3  ITD C1500     -44.502  40.650  24.433  1.00 43.52           C  
HETATM10357  N3  ITD C1500     -43.368  44.257  17.936  1.00203.44           N  
HETATM10358  C4  ITD C1500     -45.610  43.323  22.730  1.00125.35           C  
HETATM10359  N4  ITD C1500     -41.627  43.975  19.512  1.00110.32           N  
HETATM10360  C5  ITD C1500     -45.465  44.496  20.602  1.00133.81           C  
HETATM10361  C6  ITD C1500     -45.419  41.084  22.150  1.00105.08           C  
HETATM10362  C7  ITD C1500     -45.364  43.084  20.540  1.00218.80           C  
HETATM10363  C8  ITD C1500     -45.121  42.289  19.281  1.00168.89           C  
HETATM10364  C9  ITD C1500     -42.720  43.548  18.865  1.00 62.31           C  
HETATM10365  C10 ITD C1500     -43.091  45.589  17.439  1.00 70.33           C  
HETATM10366  C11 ITD C1500     -41.802  45.713  16.638  1.00107.30           C  
HETATM10367  C12 ITD C1500     -41.800  47.061  15.917  1.00 81.48           C  
HETATM10368  C13 ITD C1500     -41.991  48.230  16.889  1.00 49.33           C  
HETATM10369  C14 ITD C1500     -43.184  48.050  17.832  1.00117.61           C  
HETATM10370  C15 ITD C1500     -43.194  46.677  18.501  1.00 44.72           C  
HETATM10371  C16 ITD C1500     -41.511  44.187  20.956  1.00 94.58           C  
HETATM10372  C17 ITD C1500     -42.116  43.050  21.780  1.00 91.23           C  
HETATM10373  C18 ITD C1500     -41.924  43.256  23.278  1.00 51.65           C  
HETATM10374  C19 ITD C1500     -40.444  43.384  23.625  1.00 80.53           C  
HETATM10375  C20 ITD C1500     -39.816  44.519  22.826  1.00108.40           C  
HETATM10376  C21 ITD C1500     -40.035  44.314  21.332  1.00 48.48           C  
CONECT   13 3200                                                                
CONECT  617 1232                                                                
CONECT 1232  617                                                                
CONECT 1579 1583                                                                
CONECT 1583 1579                                                                
CONECT 1589 1593                                                                
CONECT 1593 1589                                                                
CONECT 3200   13                                                                
CONECT 3473 6617                                                                
CONECT 4103 4705                                                                
CONECT 4705 4103                                                                
CONECT 6286 6296                                                                
CONECT 6296 6286                                                                
CONECT 6302 6306                                                                
CONECT 6306 6302                                                                
CONECT 6617 3473                                                                
CONECT 687810035                                                                
CONECT 7480 8062                                                                
CONECT 8062 7480                                                                
CONECT 9662 9672                                                                
CONECT 9672 9662                                                                
CONECT 9678 9681                                                                
CONECT 9681 9678                                                                
CONECT10035 6878                                                                
CONECT1029610299                                                                
CONECT102971029910304                                                           
CONECT102981030410306                                                           
CONECT1029910296102971030210307                                                 
CONECT10300103041030710308                                                      
CONECT103011030910310                                                           
CONECT1030210299                                                                
CONECT103031031010311                                                           
CONECT10304102971029810300                                                      
CONECT103051031010317                                                           
CONECT103061029810308                                                           
CONECT103071029910300                                                           
CONECT10308103001030610309                                                      
CONECT103091030110308                                                           
CONECT10310103011030310305                                                      
CONECT10311103031031210316                                                      
CONECT103121031110313                                                           
CONECT103131031210314                                                           
CONECT103141031310315                                                           
CONECT103151031410316                                                           
CONECT103161031110315                                                           
CONECT10317103051031810322                                                      
CONECT103181031710319                                                           
CONECT103191031810320                                                           
CONECT103201031910321                                                           
CONECT103211032010322                                                           
CONECT103221031710321                                                           
CONECT1032310326                                                                
CONECT103241032610331                                                           
CONECT103251033110333                                                           
CONECT1032610323103241032910334                                                 
CONECT10327103311033410335                                                      
CONECT103281033610337                                                           
CONECT1032910326                                                                
CONECT103301033710338                                                           
CONECT10331103241032510327                                                      
CONECT103321033710344                                                           
CONECT103331032510335                                                           
CONECT103341032610327                                                           
CONECT10335103271033310336                                                      
CONECT103361032810335                                                           
CONECT10337103281033010332                                                      
CONECT10338103301033910343                                                      
CONECT103391033810340                                                           
CONECT103401033910341                                                           
CONECT103411034010342                                                           
CONECT103421034110343                                                           
CONECT103431033810342                                                           
CONECT10344103321034510349                                                      
CONECT103451034410346                                                           
CONECT103461034510347                                                           
CONECT103471034610348                                                           
CONECT103481034710349                                                           
CONECT103491034410348                                                           
CONECT1035010353                                                                
CONECT103511035310358                                                           
CONECT103521035810360                                                           
CONECT1035310350103511035610361                                                 
CONECT10354103581036110362                                                      
CONECT103551036310364                                                           
CONECT1035610353                                                                
CONECT103571036410365                                                           
CONECT10358103511035210354                                                      
CONECT103591036410371                                                           
CONECT103601035210362                                                           
CONECT103611035310354                                                           
CONECT10362103541036010363                                                      
CONECT103631035510362                                                           
CONECT10364103551035710359                                                      
CONECT10365103571036610370                                                      
CONECT103661036510367                                                           
CONECT103671036610368                                                           
CONECT103681036710369                                                           
CONECT103691036810370                                                           
CONECT103701036510369                                                           
CONECT10371103591037210376                                                      
CONECT103721037110373                                                           
CONECT103731037210374                                                           
CONECT103741037310375                                                           
CONECT103751037410376                                                           
CONECT103761037110375                                                           
MASTER      835    0    3   71   15    0    7    610373    3  105  117          
END