HEADER    SIGNALING PROTEIN, HYDROLASE            11-AUG-10   3ODU              
TITLE     THE 2.5 A STRUCTURE OF THE CXCR4 CHEMOKINE RECEPTOR IN COMPLEX WITH   
TITLE    2 SMALL MOLECULE ANTAGONIST IT1T                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: C-X-C CHEMOKINE RECEPTOR TYPE 4, LYSOZYME CHIMERA;         
COMPND   3 CHAIN: A, B;                                                         
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, CHEMOKINE, CXCL12, SDF1, ISOTHIOUREA,     
KEYWDS   5 CHIMERA, T4L FUSION, MEMBRANE PROTEIN, TRANSMEMBRANE, SINGNALING     
KEYWDS   6 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   6   06-OCT-21 3ODU    1       REMARK SEQADV                            
REVDAT   5   26-JUL-17 3ODU    1       SOURCE REMARK                            
REVDAT   4   02-MAY-12 3ODU    1       REMARK VERSN                             
REVDAT   3   16-FEB-11 3ODU    1       HEADER                                   
REVDAT   2   05-JAN-11 3ODU    1       JRNL                                     
REVDAT   1   27-OCT-10 3ODU    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.    2.50 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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.98                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 41455                          
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)  : 0.240                          
REMARK   3   R VALUE            (WORKING SET)  : 0.237                          
REMARK   3   FREE R VALUE                      : 0.282                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.020                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2079                           
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               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.50                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.56                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2765                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2530                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2639                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2511                   
REMARK   3   BIN FREE R VALUE                        : 0.2902                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.56                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 126                      
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            : 7393                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 242                                     
REMARK   3   SOLVENT ATOMS            : 142                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 48.57                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.79                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.52430                                             
REMARK   3    B22 (A**2) : -0.49890                                             
REMARK   3    B33 (A**2) : 1.02330                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.04030                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.375               
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      : 0.896                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.856                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 7843   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 10596  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2598   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 144    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1126   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 7606   ; 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   : 1019   ; 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   : 9337   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.014                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.30                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 6.46                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 19.40                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 10                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|27 - A|229 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):   18.0031   -5.8007   56.0337           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0994 T22:   -0.0505                                    
REMARK   3     T33:   -0.0524 T12:    0.0004                                    
REMARK   3     T13:    0.0032 T23:    0.0185                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.8188 L22:    0.7696                                    
REMARK   3     L33:    1.2852 L12:   -0.1277                                    
REMARK   3     L13:    0.3250 L23:    0.1302                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0156 S12:    0.0511 S13:    0.0076                     
REMARK   3     S21:   -0.0153 S22:    0.0417 S23:   -0.0670                     
REMARK   3     S31:    0.0102 S32:    0.1170 S33:   -0.0261                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { A|900 - A|901 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):    1.1966   -8.5406   24.2529           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0290 T22:   -0.0153                                    
REMARK   3     T33:    0.0077 T12:   -0.0367                                    
REMARK   3     T13:    0.0298 T23:   -0.0198                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:   -0.0109 L22:    0.0000                                    
REMARK   3     L33:    0.0124 L12:    0.0562                                    
REMARK   3     L13:    0.0239 L23:   -0.0197                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0005 S12:   -0.0039 S13:    0.0019                     
REMARK   3     S21:    0.0033 S22:   -0.0002 S23:    0.0031                     
REMARK   3     S31:    0.0024 S32:    0.0015 S33:    0.0007                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { A|1002 - A|1161 }                                    
REMARK   3    ORIGIN FOR THE GROUP (A):   -5.6476   -2.7030   11.4639           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0020 T22:   -0.0307                                    
REMARK   3     T33:   -0.1619 T12:    0.0204                                    
REMARK   3     T13:   -0.0921 T23:   -0.0259                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.5805 L22:    2.7047                                    
REMARK   3     L33:    0.6937 L12:    1.7319                                    
REMARK   3     L13:   -0.2717 L23:   -0.1222                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0105 S12:   -0.0448 S13:    0.0669                     
REMARK   3     S21:   -0.0232 S22:   -0.0513 S23:    0.1089                     
REMARK   3     S31:   -0.0372 S32:   -0.2476 S33:    0.0408                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { A|1200 - A|1201 }                                    
REMARK   3    ORIGIN FOR THE GROUP (A):    6.0277  -13.9636   22.6564           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0140 T22:    0.0093                                    
REMARK   3     T33:   -0.0007 T12:    0.0108                                    
REMARK   3     T13:    0.0023 T23:    0.0039                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:   -0.0020 L22:    0.0000                                    
REMARK   3     L33:    0.0149 L12:   -0.0123                                    
REMARK   3     L13:    0.0031 L23:   -0.0083                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0006 S12:    0.0005 S13:    0.0011                     
REMARK   3     S21:    0.0009 S22:   -0.0008 S23:   -0.0005                     
REMARK   3     S31:    0.0007 S32:    0.0018 S33:    0.0014                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: { A|230 - A|328 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):   12.8482  -21.3175   53.1576           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0575 T22:   -0.0211                                    
REMARK   3     T33:   -0.0398 T12:    0.0093                                    
REMARK   3     T13:   -0.0208 T23:    0.0231                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.2882 L22:    0.8357                                    
REMARK   3     L33:    0.0144 L12:   -0.0842                                    
REMARK   3     L13:    0.0644 L23:    0.3698                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0081 S12:    0.0201 S13:    0.0189                     
REMARK   3     S21:    0.0104 S22:    0.0287 S23:    0.0314                     
REMARK   3     S31:    0.1131 S32:   -0.0465 S33:   -0.0368                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: { B|28 - B|229 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):  -10.9674   12.3628   56.0292           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1136 T22:   -0.0683                                    
REMARK   3     T33:   -0.0386 T12:    0.0205                                    
REMARK   3     T13:   -0.0261 T23:   -0.0111                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.3160 L22:    0.9931                                    
REMARK   3     L33:    0.9347 L12:   -0.1484                                    
REMARK   3     L13:   -0.2715 L23:   -0.1358                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0225 S12:    0.0227 S13:   -0.0936                     
REMARK   3     S21:   -0.0007 S22:    0.0155 S23:    0.0970                     
REMARK   3     S31:   -0.0253 S32:   -0.0743 S33:    0.0069                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: { B|900 - B|901 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):   14.0751   26.6463   27.0151           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0038 T22:   -0.0118                                    
REMARK   3     T33:   -0.0083 T12:    0.0480                                    
REMARK   3     T13:   -0.0665 T23:   -0.0098                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0142 L22:    0.0079                                    
REMARK   3     L33:    0.0012 L12:    0.0278                                    
REMARK   3     L13:    0.0044 L23:   -0.0129                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0009 S12:    0.0026 S13:   -0.0021                     
REMARK   3     S21:   -0.0004 S22:   -0.0005 S23:    0.0025                     
REMARK   3     S31:   -0.0008 S32:   -0.0015 S33:   -0.0004                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: { B|1002 - B|1161 }                                    
REMARK   3    ORIGIN FOR THE GROUP (A):   12.2733   32.6790   14.5479           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0354 T22:   -0.0964                                    
REMARK   3     T33:   -0.1919 T12:   -0.0094                                    
REMARK   3     T13:   -0.0576 T23:    0.0476                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.4466 L22:    1.4877                                    
REMARK   3     L33:    2.2365 L12:   -0.9193                                    
REMARK   3     L13:    1.0414 L23:   -0.4138                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0444 S12:    0.2863 S13:    0.0149                     
REMARK   3     S21:   -0.0285 S22:   -0.0553 S23:   -0.0263                     
REMARK   3     S31:   -0.1306 S32:    0.1717 S33:    0.0108                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: { B|1200 - B|1201 }                                    
REMARK   3    ORIGIN FOR THE GROUP (A):   -1.1693   20.3124   23.1779           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0199 T22:    0.0109                                    
REMARK   3     T33:    0.0269 T12:   -0.0003                                    
REMARK   3     T13:   -0.0118 T23:    0.0070                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0142 L22:    0.0174                                    
REMARK   3     L33:    0.0132 L12:   -0.0143                                    
REMARK   3     L13:    0.0059 L23:   -0.0132                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0003 S12:    0.0010 S13:   -0.0015                     
REMARK   3     S21:   -0.0007 S22:    0.0010 S23:    0.0011                     
REMARK   3     S31:    0.0031 S32:    0.0006 S33:   -0.0007                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: { B|230 - B|319 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):   -5.6312   25.4603   55.6226           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1113 T22:   -0.0250                                    
REMARK   3     T33:   -0.0279 T12:    0.0222                                    
REMARK   3     T13:    0.0135 T23:   -0.0148                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.1564 L22:    0.5618                                    
REMARK   3     L33:   -0.0606 L12:    0.1857                                    
REMARK   3     L13:   -0.1240 L23:    0.2114                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0020 S12:   -0.0431 S13:    0.0549                     
REMARK   3     S21:    0.0009 S22:    0.0196 S23:   -0.0202                     
REMARK   3     S31:   -0.0421 S32:    0.0747 S33:   -0.0177                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3ODU 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_1000060990.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-JUN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
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   : 41569                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
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     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY                : 2.300                              
REMARK 200  R MERGE                    (I) : 0.12000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49000                            
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, 20% PEG400, 0.3M SODIUM MALONATE, 5MM TAURINE,     
REMARK 280  0.1M SODIUM CITRATE, PH 5.5, LIPIDIC CUBIC PHASE, TEMPERATURE       
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-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   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       41.84600            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: 2530 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 49030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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     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     PRO B    27                                                      
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 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     MET B  63    CE                                                  
REMARK 470     LYS B  68    CG   CD   CE   NZ                                   
REMARK 470     SER B 319    O                                                   
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    GLY A1200   N   -  CA  -  C   ANGL. DEV. =  22.1 DEGREES          
REMARK 500    MET B  63   CB  -  CA  -  C   ANGL. DEV. =  22.4 DEGREES          
REMARK 500    TYR B  65   CB  -  CA  -  C   ANGL. DEV. =  26.8 DEGREES          
REMARK 500    TYR B  65   N   -  CA  -  CB  ANGL. DEV. = -14.1 DEGREES          
REMARK 500    ALA B 100   N   -  CA  -  CB  ANGL. DEV. =  -9.5 DEGREES          
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 A 1200     SER A 1201                 -148.66                    
REMARK 500 SER A 1201     LYS A  230                   99.07                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     OLC A 1600                                                       
REMARK 610     OLC A 1603                                                       
REMARK 610     OLC A 1604                                                       
REMARK 610     OLA A 1610                                                       
REMARK 610     OLC B 1601                                                       
REMARK 610     OLC B 1602                                                       
REMARK 610     OLA B 1608                                                       
REMARK 610     OLA B 1609                                                       
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 OLC A 1600                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC B 1601                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC B 1602                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 1603                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 1604                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA B 1605                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA B 1606                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA B 1607                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA B 1608                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA B 1609                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLA A 1610                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: ATCG3D_11   RELATED DB: TARGETDB                         
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: 3OE8   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN IN P1 SPACEGROUP WITH 3 MOLECULES PER ASYMMETRIC UNIT   
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  3ODU A    2   229  UNP    P61073   CXCR4_HUMAN      2    229             
DBREF  3ODU A 1002  1161  UNP    P00720   LYS_BPT4      1002   1161             
DBREF  3ODU A  230   319  UNP    P61073   CXCR4_HUMAN    230    319             
DBREF  3ODU B    2   229  UNP    P61073   CXCR4_HUMAN      2    229             
DBREF  3ODU B 1002  1161  UNP    P00720   LYS_BPT4      1002   1161             
DBREF  3ODU B  230   319  UNP    P61073   CXCR4_HUMAN    230    319             
SEQADV 3ODU ASP A   -9  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU TYR A   -8  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU LYS A   -7  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU ASP A   -6  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU ASP A   -5  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU ASP A   -4  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU ASP A   -3  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU ALA A   -2  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU GLY A   -1  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU ALA A    0  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU PRO A    1  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU TRP A  125  UNP  P61073    LEU   125 ENGINEERED MUTATION            
SEQADV 3ODU GLY A  900  UNP  P61073              LINKER                         
SEQADV 3ODU SER A  901  UNP  P61073              LINKER                         
SEQADV 3ODU GLY A 1200  UNP  P61073              LINKER                         
SEQADV 3ODU SER A 1201  UNP  P61073              LINKER                         
SEQADV 3ODU THR A 1054  UNP  P00720    CYS  1054 ENGINEERED MUTATION            
SEQADV 3ODU ALA A 1097  UNP  P00720    CYS  1097 ENGINEERED MUTATION            
SEQADV 3ODU GLY A  320  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU ARG A  321  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU PRO A  322  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU LEU A  323  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU GLU A  324  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU VAL A  325  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU LEU A  326  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU PHE A  327  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU GLN A  328  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU ASP B   -9  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU TYR B   -8  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU LYS B   -7  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU ASP B   -6  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU ASP B   -5  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU ASP B   -4  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU ASP B   -3  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU ALA B   -2  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU GLY B   -1  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU ALA B    0  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU PRO B    1  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU TRP B  125  UNP  P61073    LEU   125 ENGINEERED MUTATION            
SEQADV 3ODU GLY B  900  UNP  P61073              LINKER                         
SEQADV 3ODU SER B  901  UNP  P61073              LINKER                         
SEQADV 3ODU GLY B 1200  UNP  P61073              LINKER                         
SEQADV 3ODU SER B 1201  UNP  P61073              LINKER                         
SEQADV 3ODU THR B 1054  UNP  P00720    CYS  1054 ENGINEERED MUTATION            
SEQADV 3ODU ALA B 1097  UNP  P00720    CYS  1097 ENGINEERED MUTATION            
SEQADV 3ODU GLY B  320  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU ARG B  321  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU PRO B  322  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU LEU B  323  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU GLU B  324  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU VAL B  325  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU LEU B  326  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU PHE B  327  UNP  P61073              EXPRESSION TAG                 
SEQADV 3ODU GLN B  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                              
HET    ITD  A1500      27                                                       
HET    OLC  A1600      18                                                       
HET    OLC  A1603      22                                                       
HET    OLC  A1604      16                                                       
HET    OLA  A1610      10                                                       
HET    ITD  B1500      27                                                       
HET    OLC  B1601      15                                                       
HET    OLC  B1602      22                                                       
HET    OLA  B1605      20                                                       
HET    OLA  B1606      20                                                       
HET    OLA  B1607      20                                                       
HET    OLA  B1608      12                                                       
HET    OLA  B1609      13                                                       
HETNAM     ITD (6,6-DIMETHYL-5,6-DIHYDROIMIDAZO[2,1-B][1,3]THIAZOL-3-           
HETNAM   2 ITD  YL)METHYL N,N'-DICYCLOHEXYLIMIDOTHIOCARBAMATE                   
HETNAM     OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE                   
HETNAM     OLA OLEIC ACID                                                       
HETSYN     OLC 1-OLEOYL-R-GLYCEROL                                              
FORMUL   3  ITD    2(C21 H34 N4 S2)                                             
FORMUL   4  OLC    5(C21 H40 O4)                                                
FORMUL   7  OLA    6(C18 H34 O2)                                                
FORMUL  16  HOH   *142(H2 O)                                                    
HELIX    1   1 PHE A   36  MET A   63  1                                  28    
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 PHE A  104  HIS A  140  1                                  37    
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 SER A  227  SER A  229  5                                   3    
HELIX   12  12 ASN A 1002  GLU A 1011  1                                  10    
HELIX   13  13 SER A 1038  GLY A 1051  1                                  14    
HELIX   14  14 THR A 1059  LEU A 1079  1                                  21    
HELIX   15  15 LEU A 1084  SER A 1090  1                                   7    
HELIX   16  16 ASP A 1092  GLY A 1113  1                                  22    
HELIX   17  17 PHE A 1114  LYS A 1124  1                                  11    
HELIX   18  18 ARG A 1125  ALA A 1134  1                                  10    
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 TRP A 1158  SER A 1201  1                                   6    
HELIX   22  22 LYS A  230  LEU A  267  1                                  38    
HELIX   23  23 GLY A  273  PHE A  292  1                                  20    
HELIX   24  24 PHE A  293  TYR A  302  1                                  10    
HELIX   25  25 SER A  312  THR A  318  1                                   7    
HELIX   26  26 LEU A  323  PHE A  327  5                                   5    
HELIX   27  27 PHE B   36  TYR B   65  1                                  30    
HELIX   28  28 SER B   71  ILE B   89  1                                  19    
HELIX   29  29 THR B   90  ALA B  100  1                                  11    
HELIX   30  30 PHE B  104  HIS B  140  1                                  37    
HELIX   31  31 SER B  144  LYS B  154  1                                  11    
HELIX   32  32 LYS B  154  VAL B  160  1                                   7    
HELIX   33  33 VAL B  160  LEU B  167  1                                   8    
HELIX   34  34 THR B  168  PHE B  174  1                                   7    
HELIX   35  35 ASN B  192  LEU B  208  1                                  17    
HELIX   36  36 LEU B  208  LEU B  226  1                                  19    
HELIX   37  37 SER B  901  GLY B 1012  1                                  12    
HELIX   38  38 SER B 1038  GLY B 1051  1                                  14    
HELIX   39  39 THR B 1059  LEU B 1079  1                                  21    
HELIX   40  40 LEU B 1084  LEU B 1091  1                                   8    
HELIX   41  41 ASP B 1092  GLY B 1113  1                                  22    
HELIX   42  42 PHE B 1114  GLN B 1123  1                                  10    
HELIX   43  43 ARG B 1125  ALA B 1134  1                                  10    
HELIX   44  44 SER B 1136  THR B 1142  1                                   7    
HELIX   45  45 THR B 1142  GLY B 1156  1                                  15    
HELIX   46  46 LYS B  230  LEU B  267  1                                  38    
HELIX   47  47 GLY B  273  PHE B  292  1                                  20    
HELIX   48  48 PHE B  293  TYR B  302  1                                  10    
SHEET    1   A 2 ALA A 175  GLU A 179  0                                        
SHEET    2   A 2 TYR A 184  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  GLY A1028   N  ARG A1014           
SHEET    3   B 3 HIS A1031  THR A1034 -1  O  LEU A1033   N  TYR A1025           
SHEET    1   C 2 ALA B 175  ALA B 180  0                                        
SHEET    2   C 2 ARG B 183  ARG B 188 -1  O  ARG B 183   N  ALA B 180           
SHEET    1   D 3 ARG B1014  LYS B1019  0                                        
SHEET    2   D 3 TYR B1025  GLY B1028 -1  O  GLY B1028   N  ARG B1014           
SHEET    3   D 3 HIS B1031  LEU B1032 -1  O  HIS B1031   N  ILE B1027           
SSBOND   1 CYS A   28    CYS A  274                          1555   1555  2.03  
SSBOND   2 CYS A  109    CYS A  186                          1555   1555  2.05  
SSBOND   3 CYS B   28    CYS B  274                          1555   1555  2.04  
SSBOND   4 CYS B  109    CYS B  186                          1555   1555  2.07  
SITE     1 AC1 10 TRP A  94  ASP A  97  TYR A 116  ARG A 183                    
SITE     2 AC1 10 ILE A 185  CYS A 186  ASP A 187  GLU A 288                    
SITE     3 AC1 10 HOH A1629  HOH A1720                                          
SITE     1 AC2  9 TRP B  94  ASP B  97  TYR B 116  ARG B 183                    
SITE     2 AC2  9 CYS B 186  ASP B 187  GLU B 288  HOH B1642                    
SITE     3 AC2  9 HOH B1685                                                     
SITE     1 AC3  4 PHE A 104  PHE A 107  LEU A 108  PHE B 107                    
SITE     1 AC4  9 THR B  51  LEU B  58  VAL B  59  VAL B  62                    
SITE     2 AC4  9 PRO B 299  ILE B 300  TYR B 302  ALA B 303                    
SITE     3 AC4  9 HOH B1751                                                     
SITE     1 AC5  1 ILE B 270                                                     
SITE     1 AC6  9 GLN A 200  PHE A 201  ILE A 204  ILE A 209                    
SITE     2 AC6  9 ASP A 262  SER A 263  LEU A 266  HIS A 281                    
SITE     3 AC6  9 VAL B 198                                                     
SITE     1 AC7  9 LEU A 120  VAL A 124  HIS A 203  ILE A 204                    
SITE     2 AC7  9 GLY A 207  ILE A 209  PHE A 248  TYR A 256                    
SITE     3 AC7  9 SER A 260                                                     
SITE     1 AC8  4 ILE B  39  THR B  43  SER B  46  TYR B 103                    
SITE     1 AC9  9 VAL A 198  VAL B 196  GLN B 200  PHE B 201                    
SITE     2 AC9  9 ILE B 204  ILE B 209  ASP B 262  SER B 263                    
SITE     3 AC9  9 LEU B 266                                                     
SITE     1 BC1  6 ARG B  70  LEU B  78  HIS B  79  TYR B 157                    
SITE     2 BC1  6 TRP B 161  LEU B 165                                          
SITE     1 BC2  3 ALA B 250  CYS B 251  LEU B 290                               
SITE     1 BC3  6 LEU B 120  HIS B 203  ILE B 204  LEU B 208                    
SITE     2 BC3  6 TYR B 256  SER B 260                                          
SITE     1 BC4  2 ALA A 100  TYR A 103                                          
CRYST1   64.540   83.692  119.995  90.00 102.17  90.00 P 1 21 1      4          
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      0.015494  0.000000  0.003341        0.00000                         
SCALE2      0.000000  0.011949  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008525        0.00000                         
ATOM      1  N   PRO A  27       7.282  -8.921  90.749  1.00 48.96           N  
ANISOU    1  N   PRO A  27     6665   7516   4421    478    510    641       N  
ATOM      2  CA  PRO A  27       7.915  -8.281  89.588  1.00 47.20           C  
ANISOU    2  CA  PRO A  27     6398   7195   4340    495    438    562       C  
ATOM      3  C   PRO A  27       8.627  -9.284  88.676  1.00 49.65           C  
ANISOU    3  C   PRO A  27     6726   7384   4755    437    382    622       C  
ATOM      4  O   PRO A  27       9.356 -10.143  89.171  1.00 49.67           O  
ANISOU    4  O   PRO A  27     6807   7351   4715    432    337    683       O  
ATOM      5  CB  PRO A  27       8.924  -7.304  90.217  1.00 48.91           C  
ANISOU    5  CB  PRO A  27     6660   7409   4512    587    356    464       C  
ATOM      6  CG  PRO A  27       8.707  -7.370  91.715  1.00 54.81           C  
ANISOU    6  CG  PRO A  27     7473   8263   5088    627    390    483       C  
ATOM      7  CD  PRO A  27       7.990  -8.640  92.009  1.00 51.08           C  
ANISOU    7  CD  PRO A  27     7020   7828   4561    552    467    614       C  
ATOM      8  N   CYS A  28       8.406  -9.177  87.364  1.00 44.74           N  
ANISOU    8  N   CYS A  28     6032   6701   4265    400    381    603       N  
ATOM      9  CA  CYS A  28       9.126 -10.002  86.380  1.00 43.66           C  
ANISOU    9  CA  CYS A  28     5906   6449   4234    356    324    641       C  
ATOM     10  C   CYS A  28      10.475  -9.353  86.043  1.00 45.73           C  
ANISOU   10  C   CYS A  28     6179   6644   4552    414    224    560       C  
ATOM     11  O   CYS A  28      10.539  -8.164  85.759  1.00 44.90           O  
ANISOU   11  O   CYS A  28     6032   6549   4481    453    209    470       O  
ATOM     12  CB  CYS A  28       8.313 -10.166  85.091  1.00 43.48           C  
ANISOU   12  CB  CYS A  28     5804   6395   4321    292    366    653       C  
ATOM     13  SG  CYS A  28       6.550 -10.610  85.321  1.00 48.46           S  
ANISOU   13  SG  CYS A  28     6382   7124   4906    220    490    723       S  
ATOM     14  N   PHE A  29      11.542 -10.144  86.090  1.00 41.28           N  
ANISOU   14  N   PHE A  29     5673   6013   3997    417    154    595       N  
ATOM     15  CA  PHE A  29      12.875  -9.713  85.676  1.00 39.71           C  
ANISOU   15  CA  PHE A  29     5473   5753   3861    459     59    529       C  
ATOM     16  C   PHE A  29      13.295 -10.458  84.416  1.00 43.42           C  
ANISOU   16  C   PHE A  29     5921   6129   4449    418     31    556       C  
ATOM     17  O   PHE A  29      12.861 -11.587  84.178  1.00 43.05           O  
ANISOU   17  O   PHE A  29     5896   6051   4411    367     60    639       O  
ATOM     18  CB  PHE A  29      13.893  -9.989  86.798  1.00 41.75           C  
ANISOU   18  CB  PHE A  29     5811   6021   4031    513    -10    537       C  
ATOM     19  CG  PHE A  29      13.702  -9.131  88.021  1.00 43.62           C  
ANISOU   19  CG  PHE A  29     6076   6348   4151    566     -1    490       C  
ATOM     20  CD1 PHE A  29      13.985  -7.765  87.977  1.00 46.16           C  
ANISOU   20  CD1 PHE A  29     6361   6685   4492    609    -31    381       C  
ATOM     21  CD2 PHE A  29      13.240  -9.684  89.214  1.00 46.42           C  
ANISOU   21  CD2 PHE A  29     6497   6769   4372    572     37    555       C  
ATOM     22  CE1 PHE A  29      13.811  -6.954  89.110  1.00 47.93           C  
ANISOU   22  CE1 PHE A  29     6617   6989   4606    664    -27    327       C  
ATOM     23  CE2 PHE A  29      13.061  -8.892  90.353  1.00 49.98           C  
ANISOU   23  CE2 PHE A  29     6976   7310   4705    627     47    507       C  
ATOM     24  CZ  PHE A  29      13.350  -7.523  90.308  1.00 47.99           C  
ANISOU   24  CZ  PHE A  29     6689   7072   4475    677     13    388       C  
ATOM     25  N   ARG A  30      14.143  -9.828  83.607  1.00 40.21           N  
ANISOU   25  N   ARG A  30     5473   5678   4129    438    -25    486       N  
ATOM     26  CA  ARG A  30      14.779 -10.517  82.479  1.00 39.69           C  
ANISOU   26  CA  ARG A  30     5390   5528   4162    414    -62    501       C  
ATOM     27  C   ARG A  30      16.014 -11.285  82.948  1.00 46.79           C  
ANISOU   27  C   ARG A  30     6346   6393   5039    453   -141    522       C  
ATOM     28  O   ARG A  30      17.007 -10.691  83.389  1.00 45.89           O  
ANISOU   28  O   ARG A  30     6234   6294   4909    504   -205    466       O  
ATOM     29  CB  ARG A  30      15.180  -9.538  81.370  1.00 36.21           C  
ANISOU   29  CB  ARG A  30     4877   5060   3820    415    -84    423       C  
ATOM     30  CG  ARG A  30      15.807 -10.201  80.131  1.00 39.57           C  
ANISOU   30  CG  ARG A  30     5278   5412   4344    393   -114    433       C  
ATOM     31  CD  ARG A  30      14.786 -10.434  79.030  1.00 42.81           C  
ANISOU   31  CD  ARG A  30     5648   5800   4818    335    -54    457       C  
ATOM     32  NE  ARG A  30      13.600 -11.126  79.541  1.00 46.70           N  
ANISOU   32  NE  ARG A  30     6168   6318   5256    298      8    527       N  
ATOM     33  CZ  ARG A  30      12.394 -11.089  78.984  1.00 54.03           C  
ANISOU   33  CZ  ARG A  30     7056   7262   6211    249     72    544       C  
ATOM     34  NH1 ARG A  30      12.185 -10.396  77.871  1.00 38.63           N  
ANISOU   34  NH1 ARG A  30     5042   5298   4337    237     79    497       N  
ATOM     35  NH2 ARG A  30      11.387 -11.748  79.558  1.00 37.69           N  
ANISOU   35  NH2 ARG A  30     5009   5226   4088    210    128    610       N  
ATOM     36  N   GLU A  31      15.935 -12.611  82.845  1.00 46.67           N  
ANISOU   36  N   GLU A  31     6376   6330   5024    429   -139    603       N  
ATOM     37  CA  GLU A  31      17.098 -13.484  83.022  1.00 48.06           C  
ANISOU   37  CA  GLU A  31     6604   6457   5201    470   -218    625       C  
ATOM     38  C   GLU A  31      17.512 -14.045  81.673  1.00 53.93           C  
ANISOU   38  C   GLU A  31     7312   7122   6055    453   -238    619       C  
ATOM     39  O   GLU A  31      16.676 -14.542  80.926  1.00 53.74           O  
ANISOU   39  O   GLU A  31     7279   7065   6076    396   -188    656       O  
ATOM     40  CB  GLU A  31      16.783 -14.632  83.985  1.00 50.47           C  
ANISOU   40  CB  GLU A  31     7006   6754   5416    465   -211    723       C  
ATOM     41  CG  GLU A  31      16.890 -14.255  85.472  1.00 62.65           C  
ANISOU   41  CG  GLU A  31     8603   8371   6831    510   -224    726       C  
ATOM     42  CD  GLU A  31      15.591 -13.716  86.068  1.00 83.88           C  
ANISOU   42  CD  GLU A  31    11285  11140   9446    474   -132    741       C  
ATOM     43  OE1 GLU A  31      15.650 -13.053  87.131  1.00 79.74           O  
ANISOU   43  OE1 GLU A  31    10783  10689   8825    516   -137    713       O  
ATOM     44  OE2 GLU A  31      14.509 -13.965  85.492  1.00 77.59           O  
ANISOU   44  OE2 GLU A  31    10459  10338   8685    406    -57    778       O  
ATOM     45  N   GLU A  32      18.785 -13.972  81.326  1.00 51.80           N  
ANISOU   45  N   GLU A  32     7020   6830   5831    502   -311    571       N  
ATOM     46  CA  GLU A  32      19.233 -14.577  80.077  1.00 51.67           C  
ANISOU   46  CA  GLU A  32     6974   6747   5910    496   -330    564       C  
ATOM     47  C   GLU A  32      19.420 -16.070  80.226  1.00 57.12           C  
ANISOU   47  C   GLU A  32     7745   7371   6588    510   -360    636       C  
ATOM     48  O   GLU A  32      19.960 -16.523  81.178  1.00 57.17           O  
ANISOU   48  O   GLU A  32     7813   7378   6530    558   -409    664       O  
ATOM     49  CB  GLU A  32      20.492 -13.947  79.523  1.00 52.59           C  
ANISOU   49  CB  GLU A  32     7024   6872   6086    537   -387    484       C  
ATOM     50  CG  GLU A  32      20.771 -12.568  79.962  1.00 62.63           C  
ANISOU   50  CG  GLU A  32     8251   8207   7339    548   -398    417       C  
ATOM     51  CD  GLU A  32      19.934 -11.531  79.304  1.00 82.93           C  
ANISOU   51  CD  GLU A  32    10767  10796   9949    497   -336    383       C  
ATOM     52  OE1 GLU A  32      19.902 -10.438  79.858  1.00 80.55           O  
ANISOU   52  OE1 GLU A  32    10450  10541   9616    504   -338    338       O  
ATOM     53  OE2 GLU A  32      19.312 -11.761  78.258  1.00 76.67           O  
ANISOU   53  OE2 GLU A  32     9947   9970   9214    453   -290    398       O  
ATOM     54  N   ASN A  33      18.914 -16.823  79.278  1.00 54.92           N  
ANISOU   54  N   ASN A  33     7469   7029   6368    467   -332    666       N  
ATOM     55  CA  ASN A  33      18.973 -18.271  79.287  1.00 56.05           C  
ANISOU   55  CA  ASN A  33     7696   7091   6510    472   -359    734       C  
ATOM     56  C   ASN A  33      20.292 -18.811  78.847  1.00 61.75           C  
ANISOU   56  C   ASN A  33     8418   7766   7276    548   -439    700       C  
ATOM     57  O   ASN A  33      20.916 -18.255  78.006  1.00 60.88           O  
ANISOU   57  O   ASN A  33     8230   7673   7230    567   -452    629       O  
ATOM     58  CB  ASN A  33      17.898 -18.833  78.364  1.00 55.90           C  
ANISOU   58  CB  ASN A  33     7676   7020   6542    393   -302    769       C  
ATOM     59  CG  ASN A  33      18.004 -20.318  78.201  1.00 77.05           C  
ANISOU   59  CG  ASN A  33    10443   9597   9234    395   -337    829       C  
ATOM     60  OD1 ASN A  33      18.748 -20.959  78.894  1.00 74.55           O  
ANISOU   60  OD1 ASN A  33    10197   9249   8878    454   -398    857       O  
ATOM     61  ND2 ASN A  33      17.256 -20.867  77.290  1.00 66.27           N  
ANISOU   61  ND2 ASN A  33     9079   8177   7925    331   -305    847       N  
ATOM     62  N   ALA A  34      20.785 -19.852  79.428  1.00 60.22           N  
ANISOU   62  N   ALA A  34     8311   7522   7048    596   -496    749       N  
ATOM     63  CA  ALA A  34      22.046 -20.228  78.901  1.00 60.61           C  
ANISOU   63  CA  ALA A  34     8341   7541   7148    676   -569    701       C  
ATOM     64  C   ALA A  34      21.926 -21.505  78.211  1.00 66.03           C  
ANISOU   64  C   ALA A  34     9088   8124   7879    675   -583    737       C  
ATOM     65  O   ALA A  34      22.248 -21.643  77.057  1.00 65.40           O  
ANISOU   65  O   ALA A  34     8959   8016   7875    686   -586    688       O  
ATOM     66  CB  ALA A  34      23.029 -20.380  79.994  1.00 62.13           C  
ANISOU   66  CB  ALA A  34     8574   7755   7276    762   -647    706       C  
ATOM     67  N   ASN A  35      21.332 -22.437  78.915  1.00 63.83           N  
ANISOU   67  N   ASN A  35     8920   7786   7547    652   -584    828       N  
ATOM     68  CA  ASN A  35      21.554 -23.806  78.650  1.00 64.46           C  
ANISOU   68  CA  ASN A  35     9090   7752   7649    682   -632    869       C  
ATOM     69  C   ASN A  35      21.392 -23.950  77.202  1.00 66.20           C  
ANISOU   69  C   ASN A  35     9258   7932   7963    655   -609    820       C  
ATOM     70  O   ASN A  35      22.243 -24.475  76.531  1.00 66.57           O  
ANISOU   70  O   ASN A  35     9301   7933   8060    727   -662    777       O  
ATOM     71  CB  ASN A  35      20.540 -24.694  79.393  1.00 68.15           C  
ANISOU   71  CB  ASN A  35     9680   8156   8058    614   -609    983       C  
ATOM     72  CG  ASN A  35      19.076 -24.355  79.072  1.00 95.17           C  
ANISOU   72  CG  ASN A  35    13072  11599  11490    486   -509   1013       C  
ATOM     73  OD1 ASN A  35      18.173 -25.096  79.443  1.00 90.43           O  
ANISOU   73  OD1 ASN A  35    12553  10947  10858    413   -480   1102       O  
ATOM     74  ND2 ASN A  35      18.851 -23.236  78.396  1.00 87.01           N  
ANISOU   74  ND2 ASN A  35    11920  10643  10498    459   -459    940       N  
ATOM     75  N   PHE A  36      20.351 -23.419  76.663  1.00 59.98           N  
ANISOU   75  N   PHE A  36     8420   7171   7200    561   -531    817       N  
ATOM     76  CA  PHE A  36      20.283 -23.607  75.277  1.00 58.27           C  
ANISOU   76  CA  PHE A  36     8161   6915   7066    545   -519    769       C  
ATOM     77  C   PHE A  36      20.754 -22.362  74.563  1.00 57.88           C  
ANISOU   77  C   PHE A  36     7981   6955   7056    561   -498    678       C  
ATOM     78  O   PHE A  36      21.498 -22.442  73.653  1.00 57.26           O  
ANISOU   78  O   PHE A  36     7859   6867   7031    609   -523    617       O  
ATOM     79  CB  PHE A  36      18.877 -23.959  74.951  1.00 60.22           C  
ANISOU   79  CB  PHE A  36     8437   7121   7325    433   -458    822       C  
ATOM     80  CG  PHE A  36      18.736 -24.640  73.680  1.00 61.93           C  
ANISOU   80  CG  PHE A  36     8657   7258   7614    418   -465    795       C  
ATOM     81  CD1 PHE A  36      19.414 -25.798  73.451  1.00 65.88           C  
ANISOU   81  CD1 PHE A  36     9237   7658   8136    482   -534    798       C  
ATOM     82  CD2 PHE A  36      17.928 -24.111  72.683  1.00 63.27           C  
ANISOU   82  CD2 PHE A  36     8754   7457   7831    344   -406    763       C  
ATOM     83  CE1 PHE A  36      19.279 -26.444  72.268  1.00 66.81           C  
ANISOU   83  CE1 PHE A  36     9366   7701   8318    472   -543    766       C  
ATOM     84  CE2 PHE A  36      17.805 -24.742  71.513  1.00 66.14           C  
ANISOU   84  CE2 PHE A  36     9125   7751   8255    332   -417    734       C  
ATOM     85  CZ  PHE A  36      18.486 -25.923  71.304  1.00 65.07           C  
ANISOU   85  CZ  PHE A  36     9073   7512   8138    396   -485    734       C  
ATOM     86  N   ASN A  37      20.316 -21.210  75.009  1.00 51.21           N  
ANISOU   86  N   ASN A  37     7079   6197   6180    520   -450    670       N  
ATOM     87  CA  ASN A  37      20.581 -19.988  74.301  1.00 48.87           C  
ANISOU   87  CA  ASN A  37     6670   5975   5923    516   -424    593       C  
ATOM     88  C   ASN A  37      22.007 -19.441  74.156  1.00 50.59           C  
ANISOU   88  C   ASN A  37     6820   6241   6160    596   -474    520       C  
ATOM     89  O   ASN A  37      22.229 -18.777  73.209  1.00 49.40           O  
ANISOU   89  O   ASN A  37     6588   6124   6060    586   -453    463       O  
ATOM     90  CB  ASN A  37      19.531 -18.937  74.613  1.00 48.03           C  
ANISOU   90  CB  ASN A  37     6525   5934   5791    443   -356    602       C  
ATOM     91  CG  ASN A  37      18.201 -19.203  73.931  1.00 66.71           C  
ANISOU   91  CG  ASN A  37     8895   8269   8184    356   -295    634       C  
ATOM     92  OD1 ASN A  37      17.571 -20.222  74.103  1.00 64.07           O  
ANISOU   92  OD1 ASN A  37     8633   7872   7838    320   -291    697       O  
ATOM     93  ND2 ASN A  37      17.767 -18.259  73.180  1.00 54.91           N  
ANISOU   93  ND2 ASN A  37     7322   6818   6724    319   -252    591       N  
ATOM     94  N   LYS A  38      22.946 -19.698  75.088  1.00 45.95           N  
ANISOU   94  N   LYS A  38     6263   5664   5532    672   -539    524       N  
ATOM     95  CA  LYS A  38      24.358 -19.303  74.946  1.00 44.64           C  
ANISOU   95  CA  LYS A  38     6026   5547   5389    750   -594    454       C  
ATOM     96  C   LYS A  38      25.049 -20.346  74.087  1.00 45.34           C  
ANISOU   96  C   LYS A  38     6123   5577   5527    812   -633    432       C  
ATOM     97  O   LYS A  38      26.208 -20.294  73.869  1.00 44.57           O  
ANISOU   97  O   LYS A  38     5969   5513   5452    884   -679    379       O  
ATOM     98  CB  LYS A  38      25.116 -19.320  76.268  1.00 48.42           C  
ANISOU   98  CB  LYS A  38     6537   6057   5804    817   -661    465       C  
ATOM     99  CG  LYS A  38      24.304 -19.103  77.500  1.00 64.30           C  
ANISOU   99  CG  LYS A  38     8614   8083   7733    780   -641    524       C  
ATOM    100  CD  LYS A  38      24.893 -17.936  78.304  1.00 73.39           C  
ANISOU  100  CD  LYS A  38     9712   9327   8847    800   -666    479       C  
ATOM    101  CE  LYS A  38      23.949 -16.731  78.361  1.00 80.84           C  
ANISOU  101  CE  LYS A  38    10617  10320   9777    720   -594    466       C  
ATOM    102  NZ  LYS A  38      23.649 -16.294  79.750  1.00 88.81           N  
ANISOU  102  NZ  LYS A  38    11674  11376  10694    723   -599    491       N  
ATOM    103  N   ILE A  39      24.322 -21.361  73.691  1.00 39.97           N  
ANISOU  103  N   ILE A  39     5520   4808   4860    788   -620    477       N  
ATOM    104  CA  ILE A  39      24.845 -22.353  72.826  1.00 39.17           C  
ANISOU  104  CA  ILE A  39     5436   4641   4804    845   -654    452       C  
ATOM    105  C   ILE A  39      24.220 -22.345  71.470  1.00 40.98           C  
ANISOU  105  C   ILE A  39     5634   4848   5089    788   -600    426       C  
ATOM    106  O   ILE A  39      24.865 -22.516  70.501  1.00 39.37           O  
ANISOU  106  O   ILE A  39     5384   4647   4930    833   -610    368       O  
ATOM    107  CB  ILE A  39      24.603 -23.684  73.380  1.00 43.07           C  
ANISOU  107  CB  ILE A  39     6062   5031   5272    872   -697    520       C  
ATOM    108  CG1 ILE A  39      25.398 -23.849  74.661  1.00 44.39           C  
ANISOU  108  CG1 ILE A  39     6269   5215   5381    951   -767    543       C  
ATOM    109  CG2 ILE A  39      24.977 -24.706  72.367  1.00 43.28           C  
ANISOU  109  CG2 ILE A  39     6115   4978   5351    925   -728    488       C  
ATOM    110  CD1 ILE A  39      24.816 -24.841  75.560  1.00 52.60           C  
ANISOU  110  CD1 ILE A  39     7450   6167   6369    941   -791    638       C  
ATOM    111  N   PHE A  40      22.935 -22.106  71.436  1.00 37.84           N  
ANISOU  111  N   PHE A  40     5256   4436   4684    688   -540    469       N  
ATOM    112  CA  PHE A  40      22.168 -22.177  70.202  1.00 37.08           C  
ANISOU  112  CA  PHE A  40     5142   4313   4635    626   -493    452       C  
ATOM    113  C   PHE A  40      22.371 -20.979  69.264  1.00 37.53           C  
ANISOU  113  C   PHE A  40     5081   4454   4726    606   -451    386       C  
ATOM    114  O   PHE A  40      22.637 -21.169  68.080  1.00 36.99           O  
ANISOU  114  O   PHE A  40     4980   4376   4699    621   -446    338       O  
ATOM    115  CB  PHE A  40      20.685 -22.375  70.487  1.00 39.53           C  
ANISOU  115  CB  PHE A  40     5508   4584   4927    525   -448    522       C  
ATOM    116  CG  PHE A  40      19.978 -23.053  69.370  1.00 42.30           C  
ANISOU  116  CG  PHE A  40     5883   4867   5324    478   -431    519       C  
ATOM    117  CD1 PHE A  40      19.245 -22.329  68.440  1.00 45.55           C  
ANISOU  117  CD1 PHE A  40     6225   5318   5764    411   -375    491       C  
ATOM    118  CD2 PHE A  40      20.099 -24.433  69.202  1.00 46.09           C  
ANISOU  118  CD2 PHE A  40     6458   5236   5817    508   -479    538       C  
ATOM    119  CE1 PHE A  40      18.604 -22.983  67.373  1.00 46.73           C  
ANISOU  119  CE1 PHE A  40     6398   5405   5953    370   -367    483       C  
ATOM    120  CE2 PHE A  40      19.467 -25.084  68.156  1.00 49.28           C  
ANISOU  120  CE2 PHE A  40     6889   5571   6263    465   -471    527       C  
ATOM    121  CZ  PHE A  40      18.720 -24.359  67.235  1.00 46.66           C  
ANISOU  121  CZ  PHE A  40     6484   5288   5958    395   -415    498       C  
ATOM    122  N   LEU A  41      22.262 -19.763  69.791  1.00 31.54           N  
ANISOU  122  N   LEU A  41     4264   3774   3944    574   -422    382       N  
ATOM    123  CA  LEU A  41      22.395 -18.547  68.967  1.00 29.41           C  
ANISOU  123  CA  LEU A  41     3894   3577   3705    545   -383    328       C  
ATOM    124  C   LEU A  41      23.777 -18.385  68.296  1.00 32.48           C  
ANISOU  124  C   LEU A  41     4211   4008   4125    612   -411    261       C  
ATOM    125  O   LEU A  41      23.831 -18.235  67.081  1.00 31.43           O  
ANISOU  125  O   LEU A  41     4030   3884   4027    599   -384    223       O  
ATOM    126  CB  LEU A  41      21.998 -17.290  69.743  1.00 28.66           C  
ANISOU  126  CB  LEU A  41     3765   3545   3579    501   -355    337       C  
ATOM    127  CG  LEU A  41      20.529 -17.226  70.190  1.00 32.36           C  
ANISOU  127  CG  LEU A  41     4278   3998   4021    428   -309    393       C  
ATOM    128  CD1 LEU A  41      20.310 -16.213  71.320  1.00 31.47           C  
ANISOU  128  CD1 LEU A  41     4154   3944   3860    415   -297    402       C  
ATOM    129  CD2 LEU A  41      19.618 -16.947  69.004  1.00 33.92           C  
ANISOU  129  CD2 LEU A  41     4443   4189   4257    365   -259    383       C  
ATOM    130  N   PRO A  42      24.893 -18.431  69.060  1.00 29.13           N  
ANISOU  130  N   PRO A  42     3772   3613   3682    684   -464    244       N  
ATOM    131  CA  PRO A  42      26.228 -18.371  68.406  1.00 28.83           C  
ANISOU  131  CA  PRO A  42     3655   3624   3676    750   -489    178       C  
ATOM    132  C   PRO A  42      26.444 -19.406  67.301  1.00 31.76           C  
ANISOU  132  C   PRO A  42     4041   3949   4079    794   -494    152       C  
ATOM    133  O   PRO A  42      27.030 -19.068  66.259  1.00 31.78           O  
ANISOU  133  O   PRO A  42     3963   4000   4111    805   -473     98       O  
ATOM    134  CB  PRO A  42      27.202 -18.632  69.550  1.00 31.40           C  
ANISOU  134  CB  PRO A  42     3989   3969   3973    828   -559    178       C  
ATOM    135  CG  PRO A  42      26.357 -19.240  70.630  1.00 35.98           C  
ANISOU  135  CG  PRO A  42     4682   4483   4507    816   -574    250       C  
ATOM    136  CD  PRO A  42      25.028 -18.574  70.515  1.00 30.79           C  
ANISOU  136  CD  PRO A  42     4035   3822   3843    712   -506    282       C  
ATOM    137  N   THR A  43      25.945 -20.627  67.521  1.00 27.27           N  
ANISOU  137  N   THR A  43     3576   3284   3501    816   -520    191       N  
ATOM    138  CA  THR A  43      25.984 -21.716  66.521  1.00 26.82           C  
ANISOU  138  CA  THR A  43     3558   3161   3472    856   -531    168       C  
ATOM    139  C   THR A  43      25.288 -21.348  65.209  1.00 29.10           C  
ANISOU  139  C   THR A  43     3812   3457   3787    788   -470    145       C  
ATOM    140  O   THR A  43      25.851 -21.528  64.130  1.00 27.83           O  
ANISOU  140  O   THR A  43     3609   3317   3650    828   -464     88       O  
ATOM    141  CB  THR A  43      25.311 -23.012  67.052  1.00 33.37           C  
ANISOU  141  CB  THR A  43     4523   3870   4288    862   -567    227       C  
ATOM    142  OG1 THR A  43      25.837 -23.361  68.349  1.00 33.50           O  
ANISOU  142  OG1 THR A  43     4587   3873   4269    921   -625    261       O  
ATOM    143  CG2 THR A  43      25.536 -24.161  66.086  1.00 31.69           C  
ANISOU  143  CG2 THR A  43     4355   3582   4104    921   -594    190       C  
ATOM    144  N   ILE A  44      24.059 -20.838  65.328  1.00 25.38           N  
ANISOU  144  N   ILE A  44     3360   2976   3308    689   -426    189       N  
ATOM    145  CA  ILE A  44      23.267 -20.357  64.183  1.00 24.37           C  
ANISOU  145  CA  ILE A  44     3199   2859   3200    618   -371    175       C  
ATOM    146  C   ILE A  44      23.867 -19.101  63.565  1.00 26.26           C  
ANISOU  146  C   ILE A  44     3329   3199   3449    607   -336    129       C  
ATOM    147  O   ILE A  44      23.942 -18.989  62.360  1.00 25.06           O  
ANISOU  147  O   ILE A  44     3139   3067   3314    602   -309     91       O  
ATOM    148  CB  ILE A  44      21.794 -20.033  64.578  1.00 26.99           C  
ANISOU  148  CB  ILE A  44     3568   3168   3520    519   -335    234       C  
ATOM    149  CG1 ILE A  44      21.088 -21.293  65.095  1.00 28.16           C  
ANISOU  149  CG1 ILE A  44     3825   3215   3659    508   -362    287       C  
ATOM    150  CG2 ILE A  44      21.029 -19.410  63.376  1.00 26.50           C  
ANISOU  150  CG2 ILE A  44     3461   3129   3477    453   -284    214       C  
ATOM    151  CD1 ILE A  44      20.828 -22.379  64.002  1.00 38.37           C  
ANISOU  151  CD1 ILE A  44     5168   4430   4982    513   -376    264       C  
ATOM    152  N   TYR A  45      24.303 -18.163  64.382  1.00 22.94           N  
ANISOU  152  N   TYR A  45     2861   2840   3016    602   -337    133       N  
ATOM    153  CA  TYR A  45      24.996 -16.995  63.852  1.00 22.56           C  
ANISOU  153  CA  TYR A  45     2711   2880   2979    589   -311     92       C  
ATOM    154  C   TYR A  45      26.247 -17.384  63.039  1.00 27.50           C  
ANISOU  154  C   TYR A  45     3279   3546   3622    661   -324     33       C  
ATOM    155  O   TYR A  45      26.399 -16.954  61.929  1.00 27.59           O  
ANISOU  155  O   TYR A  45     3236   3599   3647    640   -286      3       O  
ATOM    156  CB  TYR A  45      25.385 -16.054  64.988  1.00 23.38           C  
ANISOU  156  CB  TYR A  45     2782   3034   3068    579   -325    101       C  
ATOM    157  CG  TYR A  45      24.218 -15.453  65.736  1.00 24.59           C  
ANISOU  157  CG  TYR A  45     2975   3169   3198    512   -304    148       C  
ATOM    158  CD1 TYR A  45      22.989 -15.184  65.094  1.00 26.25           C  
ANISOU  158  CD1 TYR A  45     3202   3356   3415    444   -256    169       C  
ATOM    159  CD2 TYR A  45      24.336 -15.128  67.071  1.00 25.17           C  
ANISOU  159  CD2 TYR A  45     3065   3256   3242    521   -331    168       C  
ATOM    160  CE1 TYR A  45      21.935 -14.640  65.790  1.00 26.89           C  
ANISOU  160  CE1 TYR A  45     3311   3431   3476    392   -235    206       C  
ATOM    161  CE2 TYR A  45      23.272 -14.569  67.775  1.00 25.50           C  
ANISOU  161  CE2 TYR A  45     3141   3291   3257    467   -307    205       C  
ATOM    162  CZ  TYR A  45      22.082 -14.331  67.143  1.00 32.49           C  
ANISOU  162  CZ  TYR A  45     4036   4157   4152    405   -258    224       C  
ATOM    163  OH  TYR A  45      21.038 -13.769  67.851  1.00 32.98           O  
ANISOU  163  OH  TYR A  45     4121   4221   4186    360   -233    256       O  
ATOM    164  N   SER A  46      27.103 -18.224  63.610  1.00 24.62           N  
ANISOU  164  N   SER A  46     2931   3170   3254    749   -378     20       N  
ATOM    165  CA  SER A  46      28.328 -18.713  62.960  1.00 25.10           C  
ANISOU  165  CA  SER A  46     2935   3272   3329    836   -396    -40       C  
ATOM    166  C   SER A  46      28.107 -19.423  61.629  1.00 29.17           C  
ANISOU  166  C   SER A  46     3469   3758   3855    854   -373    -72       C  
ATOM    167  O   SER A  46      28.937 -19.252  60.695  1.00 29.31           O  
ANISOU  167  O   SER A  46     3407   3848   3882    887   -351   -127       O  
ATOM    168  CB  SER A  46      29.086 -19.670  63.901  1.00 27.51           C  
ANISOU  168  CB  SER A  46     3277   3549   3626    938   -469    -43       C  
ATOM    169  OG  SER A  46      29.633 -18.956  64.999  1.00 31.11           O  
ANISOU  169  OG  SER A  46     3691   4060   4069    938   -497    -33       O  
ATOM    170  N   ILE A  47      27.022 -20.211  61.560  1.00 25.20           N  
ANISOU  170  N   ILE A  47     3070   3155   3351    831   -378    -39       N  
ATOM    171  CA  ILE A  47      26.625 -20.942  60.343  1.00 25.21           C  
ANISOU  171  CA  ILE A  47     3108   3112   3360    840   -364    -68       C  
ATOM    172  C   ILE A  47      26.170 -20.007  59.222  1.00 28.76           C  
ANISOU  172  C   ILE A  47     3501   3618   3810    764   -299    -81       C  
ATOM    173  O   ILE A  47      26.661 -20.088  58.078  1.00 28.46           O  
ANISOU  173  O   ILE A  47     3420   3622   3770    796   -276   -134       O  
ATOM    174  CB  ILE A  47      25.501 -21.966  60.611  1.00 28.40           C  
ANISOU  174  CB  ILE A  47     3637   3390   3764    816   -390    -25       C  
ATOM    175  CG1 ILE A  47      26.036 -23.107  61.498  1.00 30.37           C  
ANISOU  175  CG1 ILE A  47     3959   3568   4011    906   -460    -16       C  
ATOM    176  CG2 ILE A  47      25.002 -22.552  59.312  1.00 27.69           C  
ANISOU  176  CG2 ILE A  47     3579   3259   3683    809   -375    -59       C  
ATOM    177  CD1 ILE A  47      24.986 -24.153  61.942  1.00 38.03           C  
ANISOU  177  CD1 ILE A  47     5062   4407   4981    875   -491     39       C  
ATOM    178  N   ILE A  48      25.233 -19.125  59.559  1.00 24.69           N  
ANISOU  178  N   ILE A  48     2987   3103   3291    670   -270    -33       N  
ATOM    179  CA  ILE A  48      24.820 -18.056  58.655  1.00 23.88           C  
ANISOU  179  CA  ILE A  48     2831   3055   3187    598   -214    -36       C  
ATOM    180  C   ILE A  48      26.020 -17.193  58.325  1.00 28.06           C  
ANISOU  180  C   ILE A  48     3256   3690   3717    615   -192    -72       C  
ATOM    181  O   ILE A  48      26.200 -16.794  57.160  1.00 27.70           O  
ANISOU  181  O   ILE A  48     3163   3695   3665    599   -152   -100       O  
ATOM    182  CB  ILE A  48      23.697 -17.159  59.255  1.00 26.08           C  
ANISOU  182  CB  ILE A  48     3125   3323   3463    507   -194     19       C  
ATOM    183  CG1 ILE A  48      22.433 -17.969  59.522  1.00 26.51           C  
ANISOU  183  CG1 ILE A  48     3269   3286   3517    475   -207     58       C  
ATOM    184  CG2 ILE A  48      23.383 -16.002  58.322  1.00 25.98           C  
ANISOU  184  CG2 ILE A  48     3058   3365   3449    444   -144     15       C  
ATOM    185  CD1 ILE A  48      22.059 -18.879  58.343  1.00 39.15           C  
ANISOU  185  CD1 ILE A  48     4909   4841   5123    485   -209     30       C  
ATOM    186  N   PHE A  49      26.858 -16.912  59.322  1.00 24.47           N  
ANISOU  186  N   PHE A  49     2762   3270   3265    644   -219    -72       N  
ATOM    187  CA  PHE A  49      28.085 -16.169  59.025  1.00 24.62           C  
ANISOU  187  CA  PHE A  49     2673   3393   3289    658   -202   -109       C  
ATOM    188  C   PHE A  49      28.884 -16.887  57.920  1.00 30.47           C  
ANISOU  188  C   PHE A  49     3378   4173   4027    730   -191   -167       C  
ATOM    189  O   PHE A  49      29.105 -16.303  56.863  1.00 30.73           O  
ANISOU  189  O   PHE A  49     3352   4272   4053    698   -141   -187       O  
ATOM    190  CB  PHE A  49      28.980 -15.923  60.243  1.00 26.35           C  
ANISOU  190  CB  PHE A  49     2852   3648   3513    690   -244   -110       C  
ATOM    191  CG  PHE A  49      30.352 -15.437  59.866  1.00 28.26           C  
ANISOU  191  CG  PHE A  49     2976   3999   3764    715   -233   -157       C  
ATOM    192  CD1 PHE A  49      30.514 -14.207  59.267  1.00 30.74           C  
ANISOU  192  CD1 PHE A  49     3216   4381   4082    635   -184   -156       C  
ATOM    193  CD2 PHE A  49      31.474 -16.241  60.045  1.00 31.12           C  
ANISOU  193  CD2 PHE A  49     3298   4396   4130    818   -272   -201       C  
ATOM    194  CE1 PHE A  49      31.791 -13.752  58.890  1.00 32.14           C  
ANISOU  194  CE1 PHE A  49     3277   4667   4269    645   -169   -195       C  
ATOM    195  CE2 PHE A  49      32.744 -15.802  59.664  1.00 34.32           C  
ANISOU  195  CE2 PHE A  49     3579   4915   4544    838   -258   -246       C  
ATOM    196  CZ  PHE A  49      32.903 -14.557  59.089  1.00 32.01           C  
ANISOU  196  CZ  PHE A  49     3209   4696   4256    746   -204   -242       C  
ATOM    197  N   LEU A  50      29.280 -18.146  58.148  1.00 27.71           N  
ANISOU  197  N   LEU A  50     3069   3782   3679    828   -237   -194       N  
ATOM    198  CA  LEU A  50      30.125 -18.852  57.175  1.00 28.69           C  
ANISOU  198  CA  LEU A  50     3155   3947   3798    914   -231   -259       C  
ATOM    199  C   LEU A  50      29.441 -19.098  55.804  1.00 32.76           C  
ANISOU  199  C   LEU A  50     3705   4444   4298    891   -190   -278       C  
ATOM    200  O   LEU A  50      30.024 -18.790  54.777  1.00 32.62           O  
ANISOU  200  O   LEU A  50     3615   4512   4265    900   -145   -318       O  
ATOM    201  CB  LEU A  50      30.677 -20.171  57.757  1.00 29.76           C  
ANISOU  201  CB  LEU A  50     3338   4030   3939   1036   -299   -286       C  
ATOM    202  CG  LEU A  50      31.747 -20.021  58.850  1.00 34.78           C  
ANISOU  202  CG  LEU A  50     3914   4718   4585   1091   -343   -292       C  
ATOM    203  CD1 LEU A  50      31.891 -21.265  59.738  1.00 35.48           C  
ANISOU  203  CD1 LEU A  50     4089   4717   4675   1191   -423   -288       C  
ATOM    204  CD2 LEU A  50      33.090 -19.658  58.233  1.00 37.72           C  
ANISOU  204  CD2 LEU A  50     4147   5225   4958   1139   -318   -354       C  
ATOM    205  N   THR A  51      28.230 -19.648  55.776  1.00 29.14           N  
ANISOU  205  N   THR A  51     3353   3880   3840    859   -204   -249       N  
ATOM    206  CA  THR A  51      27.598 -19.978  54.490  1.00 28.74           C  
ANISOU  206  CA  THR A  51     3338   3808   3772    845   -177   -273       C  
ATOM    207  C   THR A  51      27.194 -18.711  53.744  1.00 32.21           C  
ANISOU  207  C   THR A  51     3725   4316   4197    749   -115   -252       C  
ATOM    208  O   THR A  51      27.105 -18.697  52.514  1.00 31.17           O  
ANISOU  208  O   THR A  51     3584   4217   4042    745    -80   -283       O  
ATOM    209  CB  THR A  51      26.325 -20.871  54.642  1.00 33.77           C  
ANISOU  209  CB  THR A  51     4100   4314   4417    821   -213   -245       C  
ATOM    210  OG1 THR A  51      25.396 -20.227  55.514  1.00 32.50           O  
ANISOU  210  OG1 THR A  51     3962   4120   4267    730   -211   -175       O  
ATOM    211  CG2 THR A  51      26.649 -22.275  55.172  1.00 31.91           C  
ANISOU  211  CG2 THR A  51     3940   3990   4193    916   -278   -266       C  
ATOM    212  N   GLY A  52      26.945 -17.648  54.502  1.00 28.87           N  
ANISOU  212  N   GLY A  52     3274   3910   3786    675   -104   -201       N  
ATOM    213  CA  GLY A  52      26.503 -16.383  53.932  1.00 28.00           C  
ANISOU  213  CA  GLY A  52     3126   3849   3665    583    -54   -173       C  
ATOM    214  C   GLY A  52      27.644 -15.606  53.314  1.00 32.23           C  
ANISOU  214  C   GLY A  52     3557   4500   4188    583    -10   -200       C  
ATOM    215  O   GLY A  52      27.470 -14.978  52.257  1.00 32.50           O  
ANISOU  215  O   GLY A  52     3569   4580   4199    536     37   -198       O  
ATOM    216  N   ILE A  53      28.800 -15.619  53.972  1.00 28.13           N  
ANISOU  216  N   ILE A  53     2972   4032   3682    631    -26   -221       N  
ATOM    217  CA  ILE A  53      29.989 -14.983  53.399  1.00 28.51           C  
ANISOU  217  CA  ILE A  53     2909   4203   3722    632     15   -249       C  
ATOM    218  C   ILE A  53      30.382 -15.682  52.078  1.00 32.69           C  
ANISOU  218  C   ILE A  53     3423   4779   4219    693     48   -305       C  
ATOM    219  O   ILE A  53      30.675 -15.027  51.089  1.00 32.92           O  
ANISOU  219  O   ILE A  53     3397   4891   4222    653    105   -309       O  
ATOM    220  CB AILE A  53      31.193 -14.961  54.400  0.65 32.12           C  
ANISOU  220  CB AILE A  53     3290   4712   4202    679    -17   -268       C  
ATOM    221  CB BILE A  53      31.174 -14.936  54.407  0.35 31.89           C  
ANISOU  221  CB BILE A  53     3262   4683   4174    676    -17   -267       C  
ATOM    222  CG1AILE A  53      30.893 -14.042  55.577  0.65 31.94           C  
ANISOU  222  CG1AILE A  53     3271   4662   4202    608    -40   -219       C  
ATOM    223  CG1BILE A  53      32.290 -14.038  53.873  0.35 32.80           C  
ANISOU  223  CG1BILE A  53     3250   4929   4284    644     32   -284       C  
ATOM    224  CG2AILE A  53      32.460 -14.434  53.754  0.65 33.71           C  
ANISOU  224  CG2AILE A  53     3363   5048   4395    680     28   -303       C  
ATOM    225  CG2BILE A  53      31.696 -16.331  54.713  0.35 32.84           C  
ANISOU  225  CG2BILE A  53     3403   4777   4297    802    -65   -314       C  
ATOM    226  CD1AILE A  53      30.676 -12.623  55.197  0.65 37.05           C  
ANISOU  226  CD1AILE A  53     3883   5347   4848    498      5   -184       C  
ATOM    227  CD1BILE A  53      33.397 -13.813  54.847  0.35 40.27           C  
ANISOU  227  CD1BILE A  53     4110   5934   5256    669     -1   -300       C  
ATOM    228  N   VAL A  54      30.315 -16.999  52.037  1.00 28.69           N  
ANISOU  228  N   VAL A  54     2975   4214   3710    786     10   -344       N  
ATOM    229  CA  VAL A  54      30.740 -17.714  50.855  1.00 28.86           C  
ANISOU  229  CA  VAL A  54     2987   4281   3699    858     35   -408       C  
ATOM    230  C   VAL A  54      29.735 -17.497  49.743  1.00 33.64           C  
ANISOU  230  C   VAL A  54     3646   4864   4271    797     70   -395       C  
ATOM    231  O   VAL A  54      30.110 -17.195  48.598  1.00 33.94           O  
ANISOU  231  O   VAL A  54     3637   4991   4268    794    125   -421       O  
ATOM    232  CB  VAL A  54      30.911 -19.202  51.139  1.00 33.02           C  
ANISOU  232  CB  VAL A  54     3576   4734   4234    978    -25   -457       C  
ATOM    233  CG1 VAL A  54      31.438 -19.922  49.895  1.00 33.78           C  
ANISOU  233  CG1 VAL A  54     3657   4884   4293   1066      1   -535       C  
ATOM    234  CG2 VAL A  54      31.884 -19.395  52.319  1.00 33.22           C  
ANISOU  234  CG2 VAL A  54     3551   4780   4291   1043    -69   -465       C  
ATOM    235  N   GLY A  55      28.452 -17.662  50.084  1.00 29.54           N  
ANISOU  235  N   GLY A  55     3225   4233   3766    750     37   -354       N  
ATOM    236  CA  GLY A  55      27.364 -17.552  49.122  1.00 28.28           C  
ANISOU  236  CA  GLY A  55     3125   4042   3579    696     56   -342       C  
ATOM    237  C   GLY A  55      27.208 -16.171  48.524  1.00 31.48           C  
ANISOU  237  C   GLY A  55     3480   4519   3961    603    113   -302       C  
ATOM    238  O   GLY A  55      27.233 -16.005  47.306  1.00 32.08           O  
ANISOU  238  O   GLY A  55     3546   4651   3992    596    154   -321       O  
ATOM    239  N   ASN A  56      27.050 -15.170  49.371  1.00 27.04           N  
ANISOU  239  N   ASN A  56     2894   3954   3428    532    113   -245       N  
ATOM    240  CA  ASN A  56      26.907 -13.798  48.884  1.00 26.23           C  
ANISOU  240  CA  ASN A  56     2753   3905   3308    442    160   -202       C  
ATOM    241  C   ASN A  56      28.158 -13.248  48.236  1.00 30.23           C  
ANISOU  241  C   ASN A  56     3162   4534   3789    442    215   -221       C  
ATOM    242  O   ASN A  56      28.058 -12.533  47.254  1.00 29.98           O  
ANISOU  242  O   ASN A  56     3117   4553   3719    390    261   -203       O  
ATOM    243  CB  ASN A  56      26.419 -12.875  50.002  1.00 25.37           C  
ANISOU  243  CB  ASN A  56     2650   3753   3237    373    141   -143       C  
ATOM    244  CG  ASN A  56      24.990 -13.190  50.405  1.00 41.90           C  
ANISOU  244  CG  ASN A  56     4833   5744   5345    351    104   -115       C  
ATOM    245  OD1 ASN A  56      24.051 -12.961  49.620  1.00 27.53           O  
ANISOU  245  OD1 ASN A  56     3052   3904   3503    313    115    -99       O  
ATOM    246  ND2 ASN A  56      24.818 -13.775  51.608  1.00 35.54           N  
ANISOU  246  ND2 ASN A  56     4058   4875   4572    378     60   -109       N  
ATOM    247  N   GLY A  57      29.327 -13.589  48.772  1.00 27.29           N  
ANISOU  247  N   GLY A  57     2720   4214   3434    500    209   -256       N  
ATOM    248  CA  GLY A  57      30.617 -13.134  48.205  1.00 27.29           C  
ANISOU  248  CA  GLY A  57     2610   4347   3413    502    263   -279       C  
ATOM    249  C   GLY A  57      30.807 -13.688  46.806  1.00 31.10           C  
ANISOU  249  C   GLY A  57     3090   4891   3836    549    307   -325       C  
ATOM    250  O   GLY A  57      31.285 -13.001  45.919  1.00 31.16           O  
ANISOU  250  O   GLY A  57     3039   4997   3804    507    370   -317       O  
ATOM    251  N   LEU A  58      30.421 -14.943  46.602  1.00 27.81           N  
ANISOU  251  N   LEU A  58     2744   4414   3410    637    272   -374       N  
ATOM    252  CA  LEU A  58      30.398 -15.509  45.265  1.00 27.76           C  
ANISOU  252  CA  LEU A  58     2757   4449   3343    684    304   -423       C  
ATOM    253  C   LEU A  58      29.475 -14.708  44.371  1.00 32.28           C  
ANISOU  253  C   LEU A  58     3374   5017   3873    593    337   -375       C  
ATOM    254  O   LEU A  58      29.865 -14.298  43.287  1.00 33.03           O  
ANISOU  254  O   LEU A  58     3430   5210   3910    576    398   -381       O  
ATOM    255  CB  LEU A  58      29.915 -16.946  45.281  1.00 27.54           C  
ANISOU  255  CB  LEU A  58     2821   4325   3319    778    247   -478       C  
ATOM    256  CG  LEU A  58      30.937 -18.017  45.549  1.00 32.16           C  
ANISOU  256  CG  LEU A  58     3373   4934   3914    906    224   -553       C  
ATOM    257  CD1 LEU A  58      30.184 -19.361  45.778  1.00 32.04           C  
ANISOU  257  CD1 LEU A  58     3479   4779   3917    976    151   -587       C  
ATOM    258  CD2 LEU A  58      31.953 -18.052  44.406  1.00 33.80           C  
ANISOU  258  CD2 LEU A  58     3497   5285   4060    961    291   -612       C  
ATOM    259  N   VAL A  59      28.237 -14.494  44.802  1.00 28.31           N  
ANISOU  259  N   VAL A  59     2953   4406   3398    536    296   -327       N  
ATOM    260  CA  VAL A  59      27.337 -13.712  43.970  1.00 28.21           C  
ANISOU  260  CA  VAL A  59     2981   4389   3347    457    319   -282       C  
ATOM    261  C   VAL A  59      28.031 -12.420  43.575  1.00 32.66           C  
ANISOU  261  C   VAL A  59     3467   5055   3887    385    383   -239       C  
ATOM    262  O   VAL A  59      28.160 -12.143  42.398  1.00 32.41           O  
ANISOU  262  O   VAL A  59     3429   5096   3791    371    432   -240       O  
ATOM    263  CB  VAL A  59      25.983 -13.394  44.645  1.00 31.33           C  
ANISOU  263  CB  VAL A  59     3451   4671   3783    397    271   -228       C  
ATOM    264  CG1 VAL A  59      25.161 -12.436  43.755  1.00 30.83           C  
ANISOU  264  CG1 VAL A  59     3418   4618   3680    320    294   -179       C  
ATOM    265  CG2 VAL A  59      25.211 -14.674  44.911  1.00 30.93           C  
ANISOU  265  CG2 VAL A  59     3480   4520   3752    451    211   -264       C  
ATOM    266  N   ILE A  60      28.517 -11.672  44.561  1.00 30.20           N  
ANISOU  266  N   ILE A  60     3100   4750   3625    340    381   -203       N  
ATOM    267  CA  ILE A  60      29.154 -10.368  44.317  1.00 30.85           C  
ANISOU  267  CA  ILE A  60     3112   4913   3694    254    435   -155       C  
ATOM    268  C   ILE A  60      30.319 -10.458  43.310  1.00 39.53           C  
ANISOU  268  C   ILE A  60     4129   6153   4737    278    505   -189       C  
ATOM    269  O   ILE A  60      30.415  -9.636  42.406  1.00 40.03           O  
ANISOU  269  O   ILE A  60     4179   6280   4751    212    560   -151       O  
ATOM    270  CB  ILE A  60      29.638  -9.716  45.626  1.00 33.13           C  
ANISOU  270  CB  ILE A  60     3350   5188   4050    214    412   -127       C  
ATOM    271  CG1 ILE A  60      28.443  -9.399  46.531  1.00 32.05           C  
ANISOU  271  CG1 ILE A  60     3293   4927   3957    178    356    -85       C  
ATOM    272  CG2 ILE A  60      30.416  -8.420  45.341  1.00 33.95           C  
ANISOU  272  CG2 ILE A  60     3378   5376   4144    120    466    -83       C  
ATOM    273  CD1 ILE A  60      28.796  -8.965  47.929  1.00 35.30           C  
ANISOU  273  CD1 ILE A  60     3672   5311   4429    157    321    -70       C  
ATOM    274  N   LEU A  61      31.167 -11.472  43.427  1.00 39.17           N  
ANISOU  274  N   LEU A  61     4032   6156   4693    376    504   -261       N  
ATOM    275  CA  LEU A  61      32.321 -11.600  42.543  1.00 41.52           C  
ANISOU  275  CA  LEU A  61     4237   6601   4937    410    573   -302       C  
ATOM    276  C   LEU A  61      31.945 -12.116  41.151  1.00 48.92           C  
ANISOU  276  C   LEU A  61     5227   7571   5789    451    607   -335       C  
ATOM    277  O   LEU A  61      32.465 -11.639  40.142  1.00 49.82           O  
ANISOU  277  O   LEU A  61     5293   7801   5837    420    681   -326       O  
ATOM    278  CB  LEU A  61      33.386 -12.504  43.169  1.00 42.38           C  
ANISOU  278  CB  LEU A  61     4267   6756   5077    515    556   -374       C  
ATOM    279  CG  LEU A  61      34.022 -11.989  44.474  1.00 47.37           C  
ANISOU  279  CG  LEU A  61     4826   7389   5784    481    528   -351       C  
ATOM    280  CD1 LEU A  61      34.684 -13.149  45.268  1.00 47.91           C  
ANISOU  280  CD1 LEU A  61     4861   7453   5889    608    477   -423       C  
ATOM    281  CD2 LEU A  61      35.010 -10.830  44.254  1.00 50.39           C  
ANISOU  281  CD2 LEU A  61     5089   7898   6159    387    594   -315       C  
ATOM    282  N   VAL A  62      31.046 -13.086  41.089  1.00 46.72           N  
ANISOU  282  N   VAL A  62     5048   7194   5510    516    552   -372       N  
ATOM    283  CA  VAL A  62      30.707 -13.734  39.816  1.00 47.77           C  
ANISOU  283  CA  VAL A  62     5236   7352   5562    569    572   -419       C  
ATOM    284  C   VAL A  62      29.836 -12.868  38.918  1.00 53.61           C  
ANISOU  284  C   VAL A  62     6034   8088   6246    479    596   -357       C  
ATOM    285  O   VAL A  62      29.975 -12.902  37.702  1.00 54.03           O  
ANISOU  285  O   VAL A  62     6092   8224   6212    493    645   -376       O  
ATOM    286  CB  VAL A  62      30.000 -15.069  40.067  1.00 51.23           C  
ANISOU  286  CB  VAL A  62     5767   7674   6023    660    496   -480       C  
ATOM    287  CG1 VAL A  62      29.256 -15.556  38.804  1.00 51.30           C  
ANISOU  287  CG1 VAL A  62     5862   7675   5955    686    497   -515       C  
ATOM    288  CG2 VAL A  62      31.019 -16.085  40.582  1.00 51.60           C  
ANISOU  288  CG2 VAL A  62     5761   7746   6097    777    480   -558       C  
ATOM    289  N   MET A  63      28.924 -12.114  39.515  1.00 50.74           N  
ANISOU  289  N   MET A  63     5720   7630   5930    395    558   -284       N  
ATOM    290  CA  MET A  63      28.104 -11.189  38.762  1.00 51.28           C  
ANISOU  290  CA  MET A  63     5842   7689   5952    312    573   -218       C  
ATOM    291  C   MET A  63      28.814  -9.876  38.731  1.00 58.04           C  
ANISOU  291  C   MET A  63     6628   8623   6803    218    633   -149       C  
ATOM    292  O   MET A  63      29.152  -9.357  37.665  1.00 58.76           O  
ANISOU  292  O   MET A  63     6703   8808   6816    183    696   -126       O  
ATOM    293  CB  MET A  63      26.754 -10.980  39.427  1.00 52.47           C  
ANISOU  293  CB  MET A  63     6077   7703   6158    272    503   -176       C  
ATOM    294  CG  MET A  63      25.835 -12.150  39.315  1.00 55.91           C  
ANISOU  294  CG  MET A  63     6594   8056   6595    337    443   -230       C  
ATOM    295  SD  MET A  63      24.185 -11.527  39.037  1.00 59.55           S  
ANISOU  295  SD  MET A  63     7147   8429   7050    268    399   -169       S  
ATOM    296  CE  MET A  63      23.406 -11.900  40.606  1.00 55.07           C  
ANISOU  296  CE  MET A  63     6606   7729   6588    266    324   -159       C  
ATOM    297  N   GLY A  64      29.057  -9.346  39.925  1.00 55.75           N  
ANISOU  297  N   GLY A  64     6298   8292   6593    175    610   -117       N  
ATOM    298  CA  GLY A  64      29.627  -8.022  40.071  1.00 56.55           C  
ANISOU  298  CA  GLY A  64     6342   8440   6705     72    652    -47       C  
ATOM    299  C   GLY A  64      30.611  -7.746  38.970  1.00 63.29           C  
ANISOU  299  C   GLY A  64     7127   9440   7480     53    739    -45       C  
ATOM    300  O   GLY A  64      30.556  -6.699  38.332  1.00 63.06           O  
ANISOU  300  O   GLY A  64     7109   9441   7409    -38    780     25       O  
ATOM    301  N   TYR A  65      31.481  -8.698  38.711  1.00 62.36           N  
ANISOU  301  N   TYR A  65     6944   9414   7338    141    769   -123       N  
ATOM    302  CA  TYR A  65      32.527  -8.453  37.752  1.00 64.44           C  
ANISOU  302  CA  TYR A  65     7122   9835   7526    125    861   -126       C  
ATOM    303  C   TYR A  65      32.512  -9.125  36.393  1.00 71.26           C  
ANISOU  303  C   TYR A  65     8012  10780   8282    192    907   -174       C  
ATOM    304  O   TYR A  65      32.497  -8.461  35.356  1.00 71.66           O  
ANISOU  304  O   TYR A  65     8076  10901   8251    130    966   -125       O  
ATOM    305  CB  TYR A  65      33.822  -8.726  38.450  1.00 66.26           C  
ANISOU  305  CB  TYR A  65     7223  10150   7804    158    880   -170       C  
ATOM    306  CG  TYR A  65      33.997  -7.761  39.572  1.00 67.86           C  
ANISOU  306  CG  TYR A  65     7389  10303   8092     64    852   -111       C  
ATOM    307  CD1 TYR A  65      33.107  -7.704  40.604  1.00 68.61           C  
ANISOU  307  CD1 TYR A  65     7559  10249   8260     57    769    -92       C  
ATOM    308  CD2 TYR A  65      35.024  -6.866  39.567  1.00 69.64           C  
ANISOU  308  CD2 TYR A  65     7508  10632   8322    -26    910    -72       C  
ATOM    309  CE1 TYR A  65      33.266  -6.811  41.587  1.00 69.16           C  
ANISOU  309  CE1 TYR A  65     7601  10277   8399    -24    744    -44       C  
ATOM    310  CE2 TYR A  65      35.175  -5.986  40.544  1.00 70.19           C  
ANISOU  310  CE2 TYR A  65     7551  10652   8466   -113    880    -23       C  
ATOM    311  CZ  TYR A  65      34.317  -5.955  41.543  1.00 76.65           C  
ANISOU  311  CZ  TYR A  65     8448  11326   9352   -108    797    -12       C  
ATOM    312  OH  TYR A  65      34.541  -5.038  42.505  1.00 77.97           O  
ANISOU  312  OH  TYR A  65     8586  11452   9587   -194    769     31       O  
ATOM    313  N   GLN A  66      32.521 -10.432  36.369  1.00 68.96           N  
ANISOU  313  N   GLN A  66     7735  10481   7987    319    878   -268       N  
ATOM    314  CA  GLN A  66      32.541 -11.075  35.100  1.00 70.09           C  
ANISOU  314  CA  GLN A  66     7904  10703   8025    388    918   -323       C  
ATOM    315  C   GLN A  66      31.338 -10.881  34.241  1.00 74.47           C  
ANISOU  315  C   GLN A  66     8582  11198   8517    358    899   -290       C  
ATOM    316  O   GLN A  66      31.483 -10.679  33.063  1.00 74.97           O  
ANISOU  316  O   GLN A  66     8652  11359   8476    349    960   -284       O  
ATOM    317  CB  GLN A  66      32.701 -12.554  35.297  1.00 71.72           C  
ANISOU  317  CB  GLN A  66     8117  10887   8245    535    877   -436       C  
ATOM    318  CG  GLN A  66      33.960 -12.926  35.983  1.00 90.38           C  
ANISOU  318  CG  GLN A  66    10357  13327  10656    594    895   -486       C  
ATOM    319  CD  GLN A  66      34.065 -14.412  36.229  1.00109.82           C  
ANISOU  319  CD  GLN A  66    12843  15747  13136    747    842   -597       C  
ATOM    320  OE1 GLN A  66      34.350 -15.202  35.327  1.00106.44           O  
ANISOU  320  OE1 GLN A  66    12420  15390  12633    845    870   -677       O  
ATOM    321  NE2 GLN A  66      33.836 -14.796  37.455  1.00 99.99           N  
ANISOU  321  NE2 GLN A  66    11618  14384  11988    771    763   -601       N  
ATOM    322  N   LYS A  67      30.145 -10.979  34.817  1.00 70.51           N  
ANISOU  322  N   LYS A  67     8175  10542   8073    347    813   -271       N  
ATOM    323  CA  LYS A  67      28.908 -10.981  34.035  1.00 70.43           C  
ANISOU  323  CA  LYS A  67     8282  10470   8009    337    778   -255       C  
ATOM    324  C   LYS A  67      28.759  -9.816  33.051  1.00 75.26           C  
ANISOU  324  C   LYS A  67     8914  11145   8536    243    832   -170       C  
ATOM    325  O   LYS A  67      28.999  -8.661  33.401  1.00 75.16           O  
ANISOU  325  O   LYS A  67     8866  11138   8552    144    858    -84       O  
ATOM    326  CB  LYS A  67      27.693 -11.030  34.967  1.00 71.81           C  
ANISOU  326  CB  LYS A  67     8532  10479   8272    317    683   -231       C  
ATOM    327  CG  LYS A  67      27.541 -12.341  35.720  1.00 86.76           C  
ANISOU  327  CG  LYS A  67    10444  12291  10229    411    618   -313       C  
ATOM    328  CD  LYS A  67      27.432 -13.518  34.764  1.00 98.14           C  
ANISOU  328  CD  LYS A  67    11934  13755  11599    510    610   -406       C  
ATOM    329  CE  LYS A  67      27.416 -14.839  35.515  1.00111.76           C  
ANISOU  329  CE  LYS A  67    13679  15395  13388    604    546   -487       C  
ATOM    330  NZ  LYS A  67      26.254 -15.685  35.124  1.00121.80           N  
ANISOU  330  NZ  LYS A  67    15062  16568  14647    637    475   -529       N  
ATOM    331  N   LYS A  68      28.348 -10.133  31.824  1.00 71.97           N  
ANISOU  331  N   LYS A  68     8561  10770   8014    277    845   -195       N  
ATOM    332  CA  LYS A  68      27.996  -9.119  30.838  1.00 71.79           C  
ANISOU  332  CA  LYS A  68     8584  10791   7903    198    881   -113       C  
ATOM    333  C   LYS A  68      26.555  -9.196  30.308  1.00 74.15           C  
ANISOU  333  C   LYS A  68     9007  10999   8168    202    808   -103       C  
ATOM    334  O   LYS A  68      25.959  -8.187  29.954  1.00 73.95           O  
ANISOU  334  O   LYS A  68     9032  10950   8114    125    803    -14       O  
ATOM    335  CB  LYS A  68      29.014  -9.075  29.701  1.00 75.56           C  
ANISOU  335  CB  LYS A  68     9009  11442   8258    209    984   -126       C  
ATOM    336  CG  LYS A  68      29.550  -7.690  29.383  1.00 87.85           C  
ANISOU  336  CG  LYS A  68    10526  13075   9776     86   1060    -14       C  
ATOM    337  CD  LYS A  68      30.584  -7.244  30.372  1.00 95.87           C  
ANISOU  337  CD  LYS A  68    11424  14120  10881     35   1096     10       C  
ATOM    338  CE  LYS A  68      31.072  -5.857  30.055  1.00104.27           C  
ANISOU  338  CE  LYS A  68    12458  15247  11912    -99   1165    124       C  
ATOM    339  NZ  LYS A  68      32.352  -5.549  30.756  1.00112.21           N  
ANISOU  339  NZ  LYS A  68    13326  16331  12979   -144   1220    130       N  
ATOM    340  N   LEU A  69      25.944 -10.356  30.263  1.00 68.72           N  
ANISOU  340  N   LEU A  69     8371  10252   7486    289    745   -190       N  
ATOM    341  CA  LEU A  69      24.556 -10.266  29.917  1.00 67.03           C  
ANISOU  341  CA  LEU A  69     8261   9950   7259    273    671   -168       C  
ATOM    342  C   LEU A  69      23.828 -10.565  31.227  1.00 66.57           C  
ANISOU  342  C   LEU A  69     8213   9748   7333    272    588   -173       C  
ATOM    343  O   LEU A  69      23.771 -11.697  31.690  1.00 65.71           O  
ANISOU  343  O   LEU A  69     8108   9589   7272    342    546   -254       O  
ATOM    344  CB  LEU A  69      24.188 -11.203  28.779  1.00 67.98           C  
ANISOU  344  CB  LEU A  69     8446  10105   7278    352    653   -250       C  
ATOM    345  CG  LEU A  69      23.031 -10.705  27.933  1.00 72.83           C  
ANISOU  345  CG  LEU A  69     9155  10694   7825    316    609   -204       C  
ATOM    346  CD1 LEU A  69      23.261 -10.925  26.459  1.00 74.27           C  
ANISOU  346  CD1 LEU A  69     9374  10992   7853    357    651   -239       C  
ATOM    347  CD2 LEU A  69      21.715 -11.267  28.401  1.00 74.34           C  
ANISOU  347  CD2 LEU A  69     9409  10748   8087    331    499   -234       C  
ATOM    348  N   ARG A  70      23.270  -9.519  31.819  1.00 59.78           N  
ANISOU  348  N   ARG A  70     7362   8821   6529    191    565    -84       N  
ATOM    349  CA  ARG A  70      22.591  -9.626  33.099  1.00 56.79           C  
ANISOU  349  CA  ARG A  70     6989   8319   6270    180    496    -77       C  
ATOM    350  C   ARG A  70      21.143  -9.194  33.033  1.00 55.16           C  
ANISOU  350  C   ARG A  70     6857   8026   6076    145    426    -33       C  
ATOM    351  O   ARG A  70      20.812  -8.191  32.466  1.00 54.80           O  
ANISOU  351  O   ARG A  70     6841   7997   5983     94    435     37       O  
ATOM    352  CB  ARG A  70      23.338  -8.798  34.130  1.00 57.34           C  
ANISOU  352  CB  ARG A  70     6987   8387   6414    124    530    -21       C  
ATOM    353  CG  ARG A  70      24.099  -9.582  35.184  1.00 65.70           C  
ANISOU  353  CG  ARG A  70     7980   9433   7550    171    529    -78       C  
ATOM    354  CD  ARG A  70      23.928  -8.896  36.556  1.00 73.95           C  
ANISOU  354  CD  ARG A  70     9002  10397   8699    117    500    -25       C  
ATOM    355  NE  ARG A  70      24.316  -7.480  36.589  1.00 80.05           N  
ANISOU  355  NE  ARG A  70     9746  11199   9469     28    541     61       N  
ATOM    356  CZ  ARG A  70      25.420  -6.998  37.152  1.00 91.34           C  
ANISOU  356  CZ  ARG A  70    11096  12677  10932     -7    585     79       C  
ATOM    357  NH1 ARG A  70      26.271  -7.803  37.723  1.00 80.07           N  
ANISOU  357  NH1 ARG A  70     9603  11281   9540     48    594     17       N  
ATOM    358  NH2 ARG A  70      25.676  -5.713  37.139  1.00 74.79           N  
ANISOU  358  NH2 ARG A  70     8987  10594   8836    -96    614    158       N  
ATOM    359  N   SER A  71      20.278  -9.993  33.614  1.00 47.20           N  
ANISOU  359  N   SER A  71     5877   6925   5130    175    354    -76       N  
ATOM    360  CA  SER A  71      18.882  -9.686  33.670  1.00 44.34           C  
ANISOU  360  CA  SER A  71     5570   6486   4791    148    284    -43       C  
ATOM    361  C   SER A  71      18.606  -8.646  34.726  1.00 44.54           C  
ANISOU  361  C   SER A  71     5573   6453   4897     89    275     33       C  
ATOM    362  O   SER A  71      19.472  -8.281  35.443  1.00 43.49           O  
ANISOU  362  O   SER A  71     5387   6332   4806     69    315     53       O  
ATOM    363  CB  SER A  71      18.093 -10.934  33.888  1.00 45.94           C  
ANISOU  363  CB  SER A  71     5806   6621   5030    192    216   -116       C  
ATOM    364  OG  SER A  71      18.214 -11.378  35.177  1.00 51.20           O  
ANISOU  364  OG  SER A  71     6439   7221   5795    197    200   -129       O  
ATOM    365  N   MET A  72      17.411  -8.108  34.739  1.00 39.33           N  
ANISOU  365  N   MET A  72     4954   5738   4252     62    222     73       N  
ATOM    366  CA  MET A  72      17.002  -7.157  35.776  1.00 37.94           C  
ANISOU  366  CA  MET A  72     4763   5498   4153     17    204    136       C  
ATOM    367  C   MET A  72      16.940  -7.805  37.143  1.00 37.98           C  
ANISOU  367  C   MET A  72     4734   5440   4257     30    181    104       C  
ATOM    368  O   MET A  72      17.462  -7.266  38.134  1.00 37.62           O  
ANISOU  368  O   MET A  72     4649   5376   4269      6    202    133       O  
ATOM    369  CB  MET A  72      15.662  -6.503  35.461  1.00 40.53           C  
ANISOU  369  CB  MET A  72     5140   5786   4473      0    146    178       C  
ATOM    370  CG  MET A  72      15.763  -5.010  35.308  1.00 44.97           C  
ANISOU  370  CG  MET A  72     5717   6352   5018    -47    166    265       C  
ATOM    371  SD  MET A  72      16.776  -4.627  33.893  1.00 51.22           S  
ANISOU  371  SD  MET A  72     6528   7246   5688    -62    234    291       S  
ATOM    372  CE  MET A  72      16.988  -2.863  34.078  1.00 48.16           C  
ANISOU  372  CE  MET A  72     6156   6834   5309   -133    254    401       C  
ATOM    373  N   THR A  73      16.310  -8.969  37.190  1.00 31.07           N  
ANISOU  373  N   THR A  73     3877   4530   3398     66    136     45       N  
ATOM    374  CA  THR A  73      16.215  -9.699  38.419  1.00 29.22           C  
ANISOU  374  CA  THR A  73     3620   4233   3248     78    113     17       C  
ATOM    375  C   THR A  73      17.621  -9.899  38.979  1.00 30.36           C  
ANISOU  375  C   THR A  73     3716   4408   3411     95    164      0       C  
ATOM    376  O   THR A  73      17.835  -9.697  40.163  1.00 29.01           O  
ANISOU  376  O   THR A  73     3514   4202   3308     82    165     19       O  
ATOM    377  CB  THR A  73      15.460 -11.008  38.191  1.00 37.00           C  
ANISOU  377  CB  THR A  73     4641   5180   4238    110     60    -47       C  
ATOM    378  OG1 THR A  73      14.133 -10.681  37.774  1.00 37.41           O  
ANISOU  378  OG1 THR A  73     4723   5210   4279     86     10    -26       O  
ATOM    379  CG2 THR A  73      15.392 -11.858  39.449  1.00 33.02           C  
ANISOU  379  CG2 THR A  73     4123   4608   3816    119     37    -71       C  
ATOM    380  N   ASP A  74      18.581 -10.244  38.123  1.00 25.82           N  
ANISOU  380  N   ASP A  74     3131   3907   2773    126    207    -35       N  
ATOM    381  CA  ASP A  74      19.982 -10.388  38.568  1.00 24.76           C  
ANISOU  381  CA  ASP A  74     2937   3819   2652    147    258    -53       C  
ATOM    382  C   ASP A  74      20.610  -9.114  39.088  1.00 27.23           C  
ANISOU  382  C   ASP A  74     3203   4156   2987     91    298     13       C  
ATOM    383  O   ASP A  74      21.261  -9.136  40.126  1.00 26.27           O  
ANISOU  383  O   ASP A  74     3034   4023   2923     92    306     11       O  
ATOM    384  CB  ASP A  74      20.850 -10.985  37.480  1.00 26.93           C  
ANISOU  384  CB  ASP A  74     3204   4180   2847    196    301   -108       C  
ATOM    385  CG  ASP A  74      20.498 -12.415  37.201  1.00 35.29           C  
ANISOU  385  CG  ASP A  74     4305   5205   3898    263    258   -190       C  
ATOM    386  OD1 ASP A  74      20.762 -12.864  36.077  1.00 39.05           O  
ANISOU  386  OD1 ASP A  74     4802   5742   4295    303    277   -237       O  
ATOM    387  OD2 ASP A  74      19.931 -13.100  38.076  1.00 35.32           O  
ANISOU  387  OD2 ASP A  74     4329   5121   3972    274    205   -208       O  
ATOM    388  N   LYS A  75      20.409  -8.001  38.392  1.00 23.43           N  
ANISOU  388  N   LYS A  75     2739   3703   2461     40    318     72       N  
ATOM    389  CA  LYS A  75      20.855  -6.715  38.914  1.00 22.38           C  
ANISOU  389  CA  LYS A  75     2576   3573   2356    -23    344    140       C  
ATOM    390  C   LYS A  75      20.375  -6.527  40.371  1.00 22.81           C  
ANISOU  390  C   LYS A  75     2623   3540   2504    -35    301    153       C  
ATOM    391  O   LYS A  75      21.118  -6.028  41.211  1.00 21.45           O  
ANISOU  391  O   LYS A  75     2405   3370   2377    -61    320    171       O  
ATOM    392  CB  LYS A  75      20.339  -5.555  38.035  1.00 25.55           C  
ANISOU  392  CB  LYS A  75     3023   3982   2703    -74    349    209       C  
ATOM    393  CG  LYS A  75      20.942  -5.458  36.615  1.00 38.27           C  
ANISOU  393  CG  LYS A  75     4641   5690   4209    -78    404    215       C  
ATOM    394  CD  LYS A  75      20.052  -4.606  35.692  1.00 44.37           C  
ANISOU  394  CD  LYS A  75     5485   6452   4922   -109    384    276       C  
ATOM    395  CE  LYS A  75      20.802  -4.054  34.492  1.00 51.41           C  
ANISOU  395  CE  LYS A  75     6382   7437   5712   -142    449    315       C  
ATOM    396  NZ  LYS A  75      20.916  -5.053  33.387  1.00 60.30           N  
ANISOU  396  NZ  LYS A  75     7523   8641   6749    -84    467    254       N  
ATOM    397  N   TYR A  76      19.144  -6.962  40.660  1.00 18.07           N  
ANISOU  397  N   TYR A  76     2064   2870   1931    -16    245    142       N  
ATOM    398  CA  TYR A  76      18.525  -6.727  41.964  1.00 16.90           C  
ANISOU  398  CA  TYR A  76     1914   2648   1860    -28    207    159       C  
ATOM    399  C   TYR A  76      19.124  -7.641  42.990  1.00 22.14           C  
ANISOU  399  C   TYR A  76     2542   3298   2573      6    205    116       C  
ATOM    400  O   TYR A  76      19.369  -7.238  44.115  1.00 21.55           O  
ANISOU  400  O   TYR A  76     2442   3196   2551    -10    201    133       O  
ATOM    401  CB  TYR A  76      16.992  -6.855  41.918  1.00 17.20           C  
ANISOU  401  CB  TYR A  76     1997   2630   1908    -23    152    164       C  
ATOM    402  CG  TYR A  76      16.324  -5.621  41.342  1.00 18.07           C  
ANISOU  402  CG  TYR A  76     2140   2736   1991    -57    142    221       C  
ATOM    403  CD1 TYR A  76      16.416  -4.408  41.988  1.00 18.93           C  
ANISOU  403  CD1 TYR A  76     2243   2819   2132    -93    147    272       C  
ATOM    404  CD2 TYR A  76      15.617  -5.665  40.137  1.00 18.84           C  
ANISOU  404  CD2 TYR A  76     2279   2852   2028    -49    123    223       C  
ATOM    405  CE1 TYR A  76      15.820  -3.281  41.471  1.00 19.03           C  
ANISOU  405  CE1 TYR A  76     2292   2816   2120   -116    132    324       C  
ATOM    406  CE2 TYR A  76      15.017  -4.540  39.624  1.00 19.42           C  
ANISOU  406  CE2 TYR A  76     2387   2918   2075    -72    108    279       C  
ATOM    407  CZ  TYR A  76      15.128  -3.345  40.302  1.00 25.03           C  
ANISOU  407  CZ  TYR A  76     3094   3595   2821   -105    113    330       C  
ATOM    408  OH  TYR A  76      14.550  -2.187  39.811  1.00 24.03           O  
ANISOU  408  OH  TYR A  76     3010   3450   2670   -122     92    387       O  
ATOM    409  N   ARG A  77      19.425  -8.863  42.568  1.00 20.34           N  
ANISOU  409  N   ARG A  77     2316   3089   2323     55    205     58       N  
ATOM    410  CA  ARG A  77      19.990  -9.870  43.443  1.00 19.97           C  
ANISOU  410  CA  ARG A  77     2246   3023   2318     99    196     14       C  
ATOM    411  C   ARG A  77      21.477  -9.640  43.736  1.00 26.33           C  
ANISOU  411  C   ARG A  77     2987   3891   3128    107    240      7       C  
ATOM    412  O   ARG A  77      22.045 -10.271  44.638  1.00 26.81           O  
ANISOU  412  O   ARG A  77     3020   3937   3228    142    229    -21       O  
ATOM    413  CB  ARG A  77      19.707 -11.245  42.850  1.00 17.95           C  
ANISOU  413  CB  ARG A  77     2028   2754   2040    153    172    -47       C  
ATOM    414  CG  ARG A  77      18.191 -11.569  42.843  1.00 16.97           C  
ANISOU  414  CG  ARG A  77     1958   2560   1930    137    119    -41       C  
ATOM    415  CD  ARG A  77      17.910 -12.857  42.080  1.00 19.54           C  
ANISOU  415  CD  ARG A  77     2327   2870   2227    180     91   -104       C  
ATOM    416  NE  ARG A  77      18.527 -14.017  42.728  1.00 21.10           N  
ANISOU  416  NE  ARG A  77     2525   3036   2458    231     79   -151       N  
ATOM    417  CZ  ARG A  77      18.614 -15.253  42.220  1.00 32.45           C  
ANISOU  417  CZ  ARG A  77     4000   4452   3877    283     56   -216       C  
ATOM    418  NH1 ARG A  77      18.125 -15.564  41.020  1.00 18.68           N  
ANISOU  418  NH1 ARG A  77     2295   2722   2078    290     42   -250       N  
ATOM    419  NH2 ARG A  77      19.209 -16.200  42.935  1.00 19.03           N  
ANISOU  419  NH2 ARG A  77     2303   2714   2212    332     41   -251       N  
ATOM    420  N   LEU A  78      22.108  -8.729  42.999  1.00 23.82           N  
ANISOU  420  N   LEU A  78     2640   3642   2767     71    287     35       N  
ATOM    421  CA  LEU A  78      23.449  -8.257  43.354  1.00 24.09           C  
ANISOU  421  CA  LEU A  78     2601   3739   2813     56    329     40       C  
ATOM    422  C   LEU A  78      23.335  -7.259  44.503  1.00 27.04           C  
ANISOU  422  C   LEU A  78     2963   4066   3246      3    311     87       C  
ATOM    423  O   LEU A  78      24.098  -7.335  45.469  1.00 26.66           O  
ANISOU  423  O   LEU A  78     2866   4023   3240     11    307     74       O  
ATOM    424  CB  LEU A  78      24.151  -7.631  42.147  1.00 24.98           C  
ANISOU  424  CB  LEU A  78     2687   3947   2858     24    390     58       C  
ATOM    425  CG  LEU A  78      25.586  -7.138  42.351  1.00 30.68           C  
ANISOU  425  CG  LEU A  78     3320   4750   3585     -2    440     63       C  
ATOM    426  CD1 LEU A  78      26.566  -8.246  42.796  1.00 30.88           C  
ANISOU  426  CD1 LEU A  78     3284   4819   3630     74    444     -7       C  
ATOM    427  CD2 LEU A  78      26.068  -6.518  41.053  1.00 34.64           C  
ANISOU  427  CD2 LEU A  78     3807   5343   4010    -44    504     92       C  
ATOM    428  N   HIS A  79      22.365  -6.342  44.404  1.00 23.42           N  
ANISOU  428  N   HIS A  79     2552   3560   2788    -45    294    138       N  
ATOM    429  CA  HIS A  79      22.080  -5.356  45.471  1.00 22.12           C  
ANISOU  429  CA  HIS A  79     2390   3341   2676    -89    270    178       C  
ATOM    430  C   HIS A  79      21.717  -6.109  46.748  1.00 24.90           C  
ANISOU  430  C   HIS A  79     2744   3636   3081    -49    229    150       C  
ATOM    431  O   HIS A  79      22.117  -5.739  47.839  1.00 24.94           O  
ANISOU  431  O   HIS A  79     2724   3625   3128    -60    218    156       O  
ATOM    432  CB  HIS A  79      20.898  -4.442  45.100  1.00 22.40           C  
ANISOU  432  CB  HIS A  79     2484   3326   2699   -124    250    227       C  
ATOM    433  CG  HIS A  79      21.216  -3.389  44.081  1.00 26.30           C  
ANISOU  433  CG  HIS A  79     2988   3857   3148   -177    283    275       C  
ATOM    434  ND1 HIS A  79      21.697  -2.144  44.420  1.00 28.16           N  
ANISOU  434  ND1 HIS A  79     3213   4082   3403   -239    293    320       N  
ATOM    435  CD2 HIS A  79      21.065  -3.372  42.735  1.00 28.81           C  
ANISOU  435  CD2 HIS A  79     3334   4217   3398   -181    305    288       C  
ATOM    436  CE1 HIS A  79      21.859  -1.419  43.328  1.00 28.24           C  
ANISOU  436  CE1 HIS A  79     3244   4124   3361   -283    323    364       C  
ATOM    437  NE2 HIS A  79      21.487  -2.141  42.290  1.00 28.94           N  
ANISOU  437  NE2 HIS A  79     3355   4248   3391   -247    332    346       N  
ATOM    438  N   LEU A  80      20.930  -7.166  46.582  1.00 19.88           N  
ANISOU  438  N   LEU A  80     2145   2970   2439     -5    204    122       N  
ATOM    439  CA  LEU A  80      20.501  -8.021  47.681  1.00 17.81           C  
ANISOU  439  CA  LEU A  80     1894   2653   2218     29    167    101       C  
ATOM    440  C   LEU A  80      21.701  -8.673  48.379  1.00 22.86           C  
ANISOU  440  C   LEU A  80     2490   3318   2879     68    171     66       C  
ATOM    441  O   LEU A  80      21.882  -8.484  49.568  1.00 23.03           O  
ANISOU  441  O   LEU A  80     2496   3315   2938     65    154     74       O  
ATOM    442  CB  LEU A  80      19.532  -9.072  47.145  1.00 16.99           C  
ANISOU  442  CB  LEU A  80     1838   2518   2100     59    142     76       C  
ATOM    443  CG  LEU A  80      18.752  -9.909  48.159  1.00 20.91           C  
ANISOU  443  CG  LEU A  80     2362   2947   2637     77    102     68       C  
ATOM    444  CD1 LEU A  80      18.012  -9.077  49.278  1.00 19.70           C  
ANISOU  444  CD1 LEU A  80     2210   2754   2519     43     86    109       C  
ATOM    445  CD2 LEU A  80      17.784 -10.791  47.367  1.00 22.36           C  
ANISOU  445  CD2 LEU A  80     2591   3105   2802     88     78     47       C  
ATOM    446  N   SER A  81      22.509  -9.424  47.631  1.00 19.77           N  
ANISOU  446  N   SER A  81     2076   2978   2458    109    193     25       N  
ATOM    447  CA  SER A  81      23.755 -10.006  48.136  1.00 20.26           C  
ANISOU  447  CA  SER A  81     2085   3078   2534    155    198    -12       C  
ATOM    448  C   SER A  81      24.766  -8.994  48.731  1.00 25.52           C  
ANISOU  448  C   SER A  81     2683   3791   3222    117    218      8       C  
ATOM    449  O   SER A  81      25.577  -9.368  49.578  1.00 25.07           O  
ANISOU  449  O   SER A  81     2586   3747   3192    151    203    -16       O  
ATOM    450  CB  SER A  81      24.445 -10.812  47.021  1.00 24.32           C  
ANISOU  450  CB  SER A  81     2581   3655   3004    208    226    -62       C  
ATOM    451  OG  SER A  81      23.805 -12.063  46.810  1.00 30.75           O  
ANISOU  451  OG  SER A  81     3454   4415   3813    261    193   -100       O  
ATOM    452  N   VAL A  82      24.748  -7.735  48.280  1.00 22.89           N  
ANISOU  452  N   VAL A  82     2340   3482   2876     47    245     50       N  
ATOM    453  CA  VAL A  82      25.556  -6.718  48.932  1.00 22.86           C  
ANISOU  453  CA  VAL A  82     2283   3505   2900     -3    253     72       C  
ATOM    454  C   VAL A  82      24.959  -6.381  50.292  1.00 26.18           C  
ANISOU  454  C   VAL A  82     2733   3850   3366    -13    207     89       C  
ATOM    455  O   VAL A  82      25.687  -6.242  51.271  1.00 26.46           O  
ANISOU  455  O   VAL A  82     2727   3895   3432    -11    191     79       O  
ATOM    456  CB  VAL A  82      25.714  -5.446  48.064  1.00 27.18           C  
ANISOU  456  CB  VAL A  82     2821   4087   3421    -82    292    118       C  
ATOM    457  CG1 VAL A  82      26.212  -4.206  48.928  1.00 26.59           C  
ANISOU  457  CG1 VAL A  82     2715   4001   3385   -151    284    149       C  
ATOM    458  CG2 VAL A  82      26.652  -5.754  46.870  1.00 27.82           C  
ANISOU  458  CG2 VAL A  82     2850   4268   3451    -74    348     98       C  
ATOM    459  N   ALA A  83      23.636  -6.279  50.356  1.00 23.08           N  
ANISOU  459  N   ALA A  83     2407   3388   2973    -20    185    112       N  
ATOM    460  CA  ALA A  83      22.911  -6.059  51.637  1.00 22.53           C  
ANISOU  460  CA  ALA A  83     2369   3253   2939    -21    146    125       C  
ATOM    461  C   ALA A  83      23.267  -7.142  52.616  1.00 25.83           C  
ANISOU  461  C   ALA A  83     2777   3661   3376     36    119     93       C  
ATOM    462  O   ALA A  83      23.760  -6.863  53.705  1.00 25.77           O  
ANISOU  462  O   ALA A  83     2747   3650   3393     36    100     90       O  
ATOM    463  CB  ALA A  83      21.409  -6.043  51.432  1.00 22.72           C  
ANISOU  463  CB  ALA A  83     2456   3220   2957    -24    130    146       C  
ATOM    464  N   ASP A  84      23.052  -8.378  52.183  1.00 21.74           N  
ANISOU  464  N   ASP A  84     2280   3136   2844     86    116     67       N  
ATOM    465  CA  ASP A  84      23.279  -9.526  53.011  1.00 21.50           C  
ANISOU  465  CA  ASP A  84     2258   3083   2829    145     86     41       C  
ATOM    466  C   ASP A  84      24.736  -9.750  53.481  1.00 25.34           C  
ANISOU  466  C   ASP A  84     2681   3621   3326    181     83     11       C  
ATOM    467  O   ASP A  84      24.940 -10.111  54.630  1.00 23.95           O  
ANISOU  467  O   ASP A  84     2508   3423   3169    210     49      6       O  
ATOM    468  CB  ASP A  84      22.664 -10.754  52.335  1.00 23.31           C  
ANISOU  468  CB  ASP A  84     2534   3281   3042    184     78     20       C  
ATOM    469  CG  ASP A  84      21.157 -10.779  52.491  1.00 34.44           C  
ANISOU  469  CG  ASP A  84     4003   4626   4457    155     61     49       C  
ATOM    470  OD1 ASP A  84      20.654 -10.312  53.546  1.00 34.80           O  
ANISOU  470  OD1 ASP A  84     4059   4641   4522    134     46     77       O  
ATOM    471  OD2 ASP A  84      20.454 -11.240  51.568  1.00 41.86           O  
ANISOU  471  OD2 ASP A  84     4975   5552   5379    155     62     42       O  
ATOM    472  N   LEU A  85      25.727  -9.501  52.626  1.00 23.18           N  
ANISOU  472  N   LEU A  85     2346   3424   3036    178    118     -8       N  
ATOM    473  CA  LEU A  85      27.133  -9.610  53.027  1.00 24.05           C  
ANISOU  473  CA  LEU A  85     2380   3600   3159    208    116    -38       C  
ATOM    474  C   LEU A  85      27.488  -8.592  54.099  1.00 29.23           C  
ANISOU  474  C   LEU A  85     3005   4258   3844    162     97    -18       C  
ATOM    475  O   LEU A  85      28.174  -8.929  55.070  1.00 28.50           O  
ANISOU  475  O   LEU A  85     2883   4177   3770    201     64    -38       O  
ATOM    476  CB  LEU A  85      28.073  -9.417  51.834  1.00 24.77           C  
ANISOU  476  CB  LEU A  85     2403   3786   3224    202    167    -59       C  
ATOM    477  CG  LEU A  85      29.569  -9.725  52.068  1.00 30.28           C  
ANISOU  477  CG  LEU A  85     3004   4569   3930    246    170   -101       C  
ATOM    478  CD1 LEU A  85      29.747 -11.177  52.505  1.00 30.84           C  
ANISOU  478  CD1 LEU A  85     3096   4615   4007    354    131   -146       C  
ATOM    479  CD2 LEU A  85      30.430  -9.460  50.838  1.00 32.29           C  
ANISOU  479  CD2 LEU A  85     3184   4931   4153    231    232   -116       C  
ATOM    480  N   LEU A  86      27.033  -7.351  53.934  1.00 27.26           N  
ANISOU  480  N   LEU A  86     2767   3995   3596     83    113     20       N  
ATOM    481  CA  LEU A  86      27.273  -6.311  54.954  1.00 27.45           C  
ANISOU  481  CA  LEU A  86     2775   4009   3647     36     90     36       C  
ATOM    482  C   LEU A  86      26.780  -6.723  56.322  1.00 28.24           C  
ANISOU  482  C   LEU A  86     2918   4051   3761     74     40     34       C  
ATOM    483  O   LEU A  86      27.373  -6.357  57.317  1.00 27.74           O  
ANISOU  483  O   LEU A  86     2826   3998   3715     70     11     25       O  
ATOM    484  CB  LEU A  86      26.593  -4.975  54.599  1.00 28.00           C  
ANISOU  484  CB  LEU A  86     2876   4046   3716    -45    105     78       C  
ATOM    485  CG  LEU A  86      27.040  -3.819  55.527  1.00 33.73           C  
ANISOU  485  CG  LEU A  86     3582   4765   4470    -98     80     86       C  
ATOM    486  CD1 LEU A  86      28.585  -3.608  55.505  1.00 34.67           C  
ANISOU  486  CD1 LEU A  86     3603   4968   4603   -121     88     64       C  
ATOM    487  CD2 LEU A  86      26.311  -2.514  55.176  1.00 36.53           C  
ANISOU  487  CD2 LEU A  86     3982   5072   4825   -169     88    127       C  
ATOM    488  N   PHE A  87      25.681  -7.462  56.373  1.00 23.22           N  
ANISOU  488  N   PHE A  87     2350   3356   3114    106     32     43       N  
ATOM    489  CA  PHE A  87      25.091  -7.819  57.643  1.00 22.25           C  
ANISOU  489  CA  PHE A  87     2274   3181   2998    132     -7     51       C  
ATOM    490  C   PHE A  87      25.753  -9.062  58.223  1.00 26.78           C  
ANISOU  490  C   PHE A  87     2841   3762   3572    207    -36     24       C  
ATOM    491  O   PHE A  87      26.008  -9.163  59.429  1.00 26.99           O  
ANISOU  491  O   PHE A  87     2872   3779   3603    230    -74     22       O  
ATOM    492  CB  PHE A  87      23.597  -8.065  57.476  1.00 22.98           C  
ANISOU  492  CB  PHE A  87     2438   3213   3081    125     -2     77       C  
ATOM    493  CG  PHE A  87      23.006  -8.807  58.606  1.00 23.71           C  
ANISOU  493  CG  PHE A  87     2578   3260   3172    159    -32     85       C  
ATOM    494  CD1 PHE A  87      22.932  -8.220  59.862  1.00 25.60           C  
ANISOU  494  CD1 PHE A  87     2826   3489   3414    151    -55     94       C  
ATOM    495  CD2 PHE A  87      22.584 -10.107  58.448  1.00 25.34           C  
ANISOU  495  CD2 PHE A  87     2823   3434   3372    198    -40     83       C  
ATOM    496  CE1 PHE A  87      22.409  -8.905  60.937  1.00 25.99           C  
ANISOU  496  CE1 PHE A  87     2919   3503   3452    181    -79    107       C  
ATOM    497  CE2 PHE A  87      22.048 -10.804  59.518  1.00 27.67           C  
ANISOU  497  CE2 PHE A  87     3166   3685   3663    221    -66     99       C  
ATOM    498  CZ  PHE A  87      21.965 -10.202  60.768  1.00 25.27           C  
ANISOU  498  CZ  PHE A  87     2868   3379   3355    212    -83    114       C  
ATOM    499  N   VAL A  88      26.001 -10.016  57.348  1.00 23.05           N  
ANISOU  499  N   VAL A  88     2364   3303   3091    249    -23      2       N  
ATOM    500  CA  VAL A  88      26.617 -11.285  57.699  1.00 23.57           C  
ANISOU  500  CA  VAL A  88     2431   3368   3157    331    -53    -27       C  
ATOM    501  C   VAL A  88      28.030 -11.120  58.294  1.00 29.00           C  
ANISOU  501  C   VAL A  88     3040   4121   3856    361    -75    -56       C  
ATOM    502  O   VAL A  88      28.357 -11.704  59.309  1.00 28.00           O  
ANISOU  502  O   VAL A  88     2927   3979   3734    414   -120    -62       O  
ATOM    503  CB  VAL A  88      26.563 -12.186  56.456  1.00 27.57           C  
ANISOU  503  CB  VAL A  88     2949   3877   3650    367    -31    -52       C  
ATOM    504  CG1 VAL A  88      27.719 -13.087  56.355  1.00 28.09           C  
ANISOU  504  CG1 VAL A  88     2974   3983   3716    450    -46    -98       C  
ATOM    505  CG2 VAL A  88      25.235 -12.934  56.452  1.00 27.19           C  
ANISOU  505  CG2 VAL A  88     2993   3743   3597    367    -44    -30       C  
ATOM    506  N   ILE A  89      28.833 -10.259  57.694  1.00 27.63           N  
ANISOU  506  N   ILE A  89     2788   4023   3689    321    -45    -68       N  
ATOM    507  CA  ILE A  89      30.164  -9.895  58.237  1.00 28.48           C  
ANISOU  507  CA  ILE A  89     2806   4203   3812    330    -64    -94       C  
ATOM    508  C   ILE A  89      30.177  -9.366  59.698  1.00 32.63           C  
ANISOU  508  C   ILE A  89     3343   4705   4349    315   -114    -82       C  
ATOM    509  O   ILE A  89      31.222  -9.379  60.368  1.00 32.75           O  
ANISOU  509  O   ILE A  89     3298   4771   4376    344   -150   -109       O  
ATOM    510  CB  ILE A  89      30.848  -8.872  57.276  1.00 32.15           C  
ANISOU  510  CB  ILE A  89     3186   4748   4280    260    -15    -97       C  
ATOM    511  CG1 ILE A  89      31.551  -9.645  56.155  1.00 32.80           C  
ANISOU  511  CG1 ILE A  89     3216   4900   4348    312     21   -134       C  
ATOM    512  CG2 ILE A  89      31.830  -7.934  58.012  1.00 34.19           C  
ANISOU  512  CG2 ILE A  89     3366   5061   4563    216    -37   -105       C  
ATOM    513  CD1 ILE A  89      32.307  -8.772  55.187  1.00 41.40           C  
ANISOU  513  CD1 ILE A  89     4217   6082   5432    246     76   -134       C  
ATOM    514  N   THR A  90      29.031  -8.904  60.188  1.00 28.34           N  
ANISOU  514  N   THR A  90     2875   4091   3800    275   -118    -46       N  
ATOM    515  CA  THR A  90      28.920  -8.405  61.559  1.00 27.48           C  
ANISOU  515  CA  THR A  90     2789   3959   3692    265   -162    -38       C  
ATOM    516  C   THR A  90      28.408  -9.464  62.538  1.00 30.59           C  
ANISOU  516  C   THR A  90     3256   4300   4068    331   -201    -27       C  
ATOM    517  O   THR A  90      28.374  -9.218  63.728  1.00 30.04           O  
ANISOU  517  O   THR A  90     3208   4218   3989    337   -239    -22       O  
ATOM    518  CB  THR A  90      27.982  -7.168  61.630  1.00 31.19           C  
ANISOU  518  CB  THR A  90     3298   4390   4163    186   -144     -8       C  
ATOM    519  OG1 THR A  90      26.626  -7.573  61.399  1.00 29.47           O  
ANISOU  519  OG1 THR A  90     3158   4110   3930    189   -125     21       O  
ATOM    520  CG2 THR A  90      28.393  -6.121  60.614  1.00 26.79           C  
ANISOU  520  CG2 THR A  90     2686   3870   3621    114   -107     -8       C  
ATOM    521  N   LEU A  91      28.020 -10.639  62.036  1.00 26.66           N  
ANISOU  521  N   LEU A  91     2799   3769   3562    380   -192    -23       N  
ATOM    522  CA  LEU A  91      27.527 -11.729  62.899  1.00 25.62           C  
ANISOU  522  CA  LEU A  91     2744   3578   3413    436   -228     -5       C  
ATOM    523  C   LEU A  91      28.534 -12.239  63.952  1.00 29.61           C  
ANISOU  523  C   LEU A  91     3233   4105   3912    506   -288    -24       C  
ATOM    524  O   LEU A  91      28.122 -12.686  65.030  1.00 29.22           O  
ANISOU  524  O   LEU A  91     3249   4012   3840    532   -323      2       O  
ATOM    525  CB  LEU A  91      26.972 -12.908  62.063  1.00 25.24           C  
ANISOU  525  CB  LEU A  91     2746   3482   3362    468   -213     -2       C  
ATOM    526  CG  LEU A  91      25.504 -12.757  61.621  1.00 28.40           C  
ANISOU  526  CG  LEU A  91     3206   3828   3756    410   -178     34       C  
ATOM    527  CD1 LEU A  91      25.167 -13.746  60.564  1.00 28.34           C  
ANISOU  527  CD1 LEU A  91     3228   3789   3750    432   -164     24       C  
ATOM    528  CD2 LEU A  91      24.532 -12.898  62.810  1.00 30.24           C  
ANISOU  528  CD2 LEU A  91     3510   4007   3971    398   -196     75       C  
ATOM    529  N   PRO A  92      29.846 -12.201  63.651  1.00 25.89           N  
ANISOU  529  N   PRO A  92     2673   3708   3458    539   -300    -66       N  
ATOM    530  CA  PRO A  92      30.768 -12.604  64.704  1.00 25.66           C  
ANISOU  530  CA  PRO A  92     2624   3704   3422    607   -365    -85       C  
ATOM    531  C   PRO A  92      30.538 -11.834  66.009  1.00 29.05           C  
ANISOU  531  C   PRO A  92     3078   4125   3834    574   -398    -66       C  
ATOM    532  O   PRO A  92      30.674 -12.412  67.088  1.00 28.62           O  
ANISOU  532  O   PRO A  92     3066   4051   3755    631   -452    -57       O  
ATOM    533  CB  PRO A  92      32.147 -12.282  64.103  1.00 27.73           C  
ANISOU  533  CB  PRO A  92     2762   4066   3709    620   -362   -135       C  
ATOM    534  CG  PRO A  92      31.973 -12.434  62.655  1.00 32.12           C  
ANISOU  534  CG  PRO A  92     3299   4632   4274    604   -300   -144       C  
ATOM    535  CD  PRO A  92      30.528 -12.102  62.343  1.00 27.40           C  
ANISOU  535  CD  PRO A  92     2784   3959   3666    535   -260   -100       C  
ATOM    536  N   PHE A  93      30.173 -10.553  65.904  1.00 25.18           N  
ANISOU  536  N   PHE A  93     2570   3646   3352    487   -368    -60       N  
ATOM    537  CA  PHE A  93      29.937  -9.733  67.084  1.00 25.08           C  
ANISOU  537  CA  PHE A  93     2582   3626   3320    457   -399    -52       C  
ATOM    538  C   PHE A  93      28.705 -10.242  67.839  1.00 28.39           C  
ANISOU  538  C   PHE A  93     3111   3974   3701    470   -400     -8       C  
ATOM    539  O   PHE A  93      28.664 -10.210  69.075  1.00 27.47           O  
ANISOU  539  O   PHE A  93     3033   3852   3552    492   -442      0       O  
ATOM    540  CB  PHE A  93      29.694  -8.278  66.716  1.00 26.67           C  
ANISOU  540  CB  PHE A  93     2755   3839   3540    363   -366    -55       C  
ATOM    541  CG  PHE A  93      30.857  -7.587  66.065  1.00 28.81           C  
ANISOU  541  CG  PHE A  93     2919   4181   3847    326   -362    -90       C  
ATOM    542  CD1 PHE A  93      31.867  -7.028  66.838  1.00 32.77           C  
ANISOU  542  CD1 PHE A  93     3361   4733   4356    320   -414   -123       C  
ATOM    543  CD2 PHE A  93      30.899  -7.413  64.685  1.00 31.06           C  
ANISOU  543  CD2 PHE A  93     3163   4485   4154    287   -305    -89       C  
ATOM    544  CE1 PHE A  93      32.923  -6.334  66.248  1.00 34.20           C  
ANISOU  544  CE1 PHE A  93     3437   4985   4573    270   -407   -152       C  
ATOM    545  CE2 PHE A  93      31.956  -6.725  64.076  1.00 34.54           C  
ANISOU  545  CE2 PHE A  93     3503   4998   4623    241   -293   -114       C  
ATOM    546  CZ  PHE A  93      32.972  -6.195  64.860  1.00 33.28           C  
ANISOU  546  CZ  PHE A  93     3278   4891   4478    229   -343   -145       C  
ATOM    547  N   TRP A  94      27.701 -10.689  67.082  1.00 24.41           N  
ANISOU  547  N   TRP A  94     2654   3421   3199    454   -353     21       N  
ATOM    548  CA  TRP A  94      26.458 -11.182  67.662  1.00 23.52           C  
ANISOU  548  CA  TRP A  94     2634   3247   3055    453   -344     66       C  
ATOM    549  C   TRP A  94      26.745 -12.454  68.486  1.00 28.15           C  
ANISOU  549  C   TRP A  94     3273   3808   3615    529   -392     82       C  
ATOM    550  O   TRP A  94      26.211 -12.649  69.589  1.00 27.68           O  
ANISOU  550  O   TRP A  94     3279   3723   3514    538   -411    115       O  
ATOM    551  CB  TRP A  94      25.461 -11.543  66.559  1.00 21.37           C  
ANISOU  551  CB  TRP A  94     2389   2933   2797    422   -292     87       C  
ATOM    552  CG  TRP A  94      24.780 -10.436  65.871  1.00 21.77           C  
ANISOU  552  CG  TRP A  94     2421   2989   2862    351   -246     89       C  
ATOM    553  CD1 TRP A  94      25.335  -9.508  65.048  1.00 24.52           C  
ANISOU  553  CD1 TRP A  94     2702   3376   3237    314   -227     63       C  
ATOM    554  CD2 TRP A  94      23.361 -10.172  65.875  1.00 20.99           C  
ANISOU  554  CD2 TRP A  94     2371   2853   2752    309   -212    122       C  
ATOM    555  NE1 TRP A  94      24.357  -8.657  64.563  1.00 23.13           N  
ANISOU  555  NE1 TRP A  94     2540   3182   3065    256   -189     79       N  
ATOM    556  CE2 TRP A  94      23.140  -9.052  65.053  1.00 24.29           C  
ANISOU  556  CE2 TRP A  94     2752   3286   3190    256   -180    111       C  
ATOM    557  CE3 TRP A  94      22.267 -10.763  66.517  1.00 21.92           C  
ANISOU  557  CE3 TRP A  94     2555   2931   2842    310   -206    161       C  
ATOM    558  CZ2 TRP A  94      21.863  -8.510  64.853  1.00 23.04           C  
ANISOU  558  CZ2 TRP A  94     2623   3104   3028    215   -148    134       C  
ATOM    559  CZ3 TRP A  94      21.003 -10.218  66.327  1.00 22.79           C  
ANISOU  559  CZ3 TRP A  94     2683   3028   2949    263   -168    181       C  
ATOM    560  CH2 TRP A  94      20.811  -9.111  65.496  1.00 22.99           C  
ANISOU  560  CH2 TRP A  94     2670   3067   2996    222   -142    165       C  
ATOM    561  N   ALA A  95      27.550 -13.333  67.895  1.00 25.01           N  
ANISOU  561  N   ALA A  95     2851   3416   3237    586   -410     61       N  
ATOM    562  CA  ALA A  95      27.899 -14.597  68.504  1.00 25.59           C  
ANISOU  562  CA  ALA A  95     2977   3456   3291    668   -461     74       C  
ATOM    563  C   ALA A  95      28.633 -14.387  69.830  1.00 28.37           C  
ANISOU  563  C   ALA A  95     3325   3843   3613    708   -524     68       C  
ATOM    564  O   ALA A  95      28.221 -14.932  70.839  1.00 27.78           O  
ANISOU  564  O   ALA A  95     3332   3729   3496    733   -552    108       O  
ATOM    565  CB  ALA A  95      28.745 -15.439  67.525  1.00 27.04           C  
ANISOU  565  CB  ALA A  95     3122   3647   3505    731   -471     37       C  
ATOM    566  N   VAL A  96      29.685 -13.561  69.826  1.00 25.26           N  
ANISOU  566  N   VAL A  96     2836   3525   3237    708   -544     20       N  
ATOM    567  CA  VAL A  96      30.458 -13.233  71.055  1.00 25.57           C  
ANISOU  567  CA  VAL A  96     2859   3608   3249    742   -611      4       C  
ATOM    568  C   VAL A  96      29.607 -12.510  72.072  1.00 28.64           C  
ANISOU  568  C   VAL A  96     3307   3981   3595    694   -607     32       C  
ATOM    569  O   VAL A  96      29.766 -12.700  73.284  1.00 28.66           O  
ANISOU  569  O   VAL A  96     3354   3987   3550    734   -660     44       O  
ATOM    570  CB  VAL A  96      31.690 -12.334  70.786  1.00 29.89           C  
ANISOU  570  CB  VAL A  96     3281   4244   3831    729   -629    -56       C  
ATOM    571  CG1 VAL A  96      32.275 -11.848  72.107  1.00 30.54           C  
ANISOU  571  CG1 VAL A  96     3354   4366   3882    747   -699    -72       C  
ATOM    572  CG2 VAL A  96      32.770 -13.072  69.945  1.00 30.01           C  
ANISOU  572  CG2 VAL A  96     3220   4301   3883    795   -642    -93       C  
ATOM    573  N   ASP A  97      28.709 -11.666  71.573  1.00 24.23           N  
ANISOU  573  N   ASP A  97     2750   3409   3049    614   -545     41       N  
ATOM    574  CA  ASP A  97      27.741 -10.992  72.425  1.00 23.39           C  
ANISOU  574  CA  ASP A  97     2701   3287   2901    573   -531     64       C  
ATOM    575  C   ASP A  97      26.836 -12.000  73.107  1.00 28.67           C  
ANISOU  575  C   ASP A  97     3472   3903   3520    600   -528    123       C  
ATOM    576  O   ASP A  97      26.542 -11.876  74.282  1.00 29.36           O  
ANISOU  576  O   ASP A  97     3611   3994   3550    610   -549    141       O  
ATOM    577  CB  ASP A  97      26.901 -10.026  71.613  1.00 24.06           C  
ANISOU  577  CB  ASP A  97     2768   3360   3013    493   -466     63       C  
ATOM    578  CG  ASP A  97      25.866  -9.357  72.433  1.00 33.58           C  
ANISOU  578  CG  ASP A  97     4029   4553   4177    462   -448     82       C  
ATOM    579  OD1 ASP A  97      24.660  -9.492  72.114  1.00 33.12           O  
ANISOU  579  OD1 ASP A  97     4013   4459   4113    432   -396    117       O  
ATOM    580  OD2 ASP A  97      26.268  -8.729  73.432  1.00 39.47           O  
ANISOU  580  OD2 ASP A  97     4775   5328   4892    472   -490     58       O  
ATOM    581  N   ALA A  98      26.375 -12.996  72.374  1.00 25.18           N  
ANISOU  581  N   ALA A  98     3062   3411   3095    607   -500    153       N  
ATOM    582  CA  ALA A  98      25.442 -13.947  72.934  1.00 25.11           C  
ANISOU  582  CA  ALA A  98     3151   3345   3044    614   -492    215       C  
ATOM    583  C   ALA A  98      26.151 -14.832  73.958  1.00 30.39           C  
ANISOU  583  C   ALA A  98     3869   4006   3670    693   -562    232       C  
ATOM    584  O   ALA A  98      25.596 -15.143  75.005  1.00 29.30           O  
ANISOU  584  O   ALA A  98     3810   3851   3473    697   -570    280       O  
ATOM    585  CB  ALA A  98      24.801 -14.786  71.815  1.00 25.60           C  
ANISOU  585  CB  ALA A  98     3235   3350   3142    596   -451    237       C  
ATOM    586  N   VAL A  99      27.373 -15.239  73.631  1.00 29.17           N  
ANISOU  586  N   VAL A  99     3669   3870   3546    757   -611    195       N  
ATOM    587  CA  VAL A  99      28.114 -16.189  74.450  1.00 30.59           C  
ANISOU  587  CA  VAL A  99     3894   4037   3692    846   -686    209       C  
ATOM    588  C   VAL A  99      28.831 -15.549  75.634  1.00 36.21           C  
ANISOU  588  C   VAL A  99     4587   4811   4360    876   -745    187       C  
ATOM    589  O   VAL A  99      28.817 -16.093  76.738  1.00 37.20           O  
ANISOU  589  O   VAL A  99     4791   4921   4423    921   -791    226       O  
ATOM    590  CB  VAL A  99      29.144 -16.970  73.608  1.00 34.73           C  
ANISOU  590  CB  VAL A  99     4373   4558   4265    918   -720    171       C  
ATOM    591  CG1 VAL A  99      28.443 -17.775  72.525  1.00 33.87           C  
ANISOU  591  CG1 VAL A  99     4302   4377   4190    900   -673    192       C  
ATOM    592  CG2 VAL A  99      30.162 -16.018  73.000  1.00 34.60           C  
ANISOU  592  CG2 VAL A  99     4223   4628   4294    912   -721     98       C  
ATOM    593  N   ALA A 100      29.428 -14.376  75.443  1.00 31.81           N  
ANISOU  593  N   ALA A 100     3932   4323   3830    847   -747    128       N  
ATOM    594  CA  ALA A 100      30.252 -13.805  76.512  1.00 32.12           C  
ANISOU  594  CA  ALA A 100     3946   4424   3833    878   -816     96       C  
ATOM    595  C   ALA A 100      30.022 -12.390  77.064  1.00 34.38           C  
ANISOU  595  C   ALA A 100     4209   4754   4100    815   -807     68       C  
ATOM    596  O   ALA A 100      30.020 -12.187  78.278  1.00 35.19           O  
ANISOU  596  O   ALA A 100     4358   4876   4137    836   -850     74       O  
ATOM    597  CB  ALA A 100      31.731 -13.894  76.130  1.00 33.58           C  
ANISOU  597  CB  ALA A 100     4030   4666   4064    935   -874     37       C  
ATOM    598  N   ASN A 101      29.856 -11.417  76.175  1.00 28.75           N  
ANISOU  598  N   ASN A 101     3428   4054   3440    742   -755     36       N  
ATOM    599  CA  ASN A 101      30.074 -10.056  76.485  1.00 28.25           C  
ANISOU  599  CA  ASN A 101     3319   4035   3380    692   -766    -10       C  
ATOM    600  C   ASN A 101      29.732  -9.087  75.338  1.00 32.13           C  
ANISOU  600  C   ASN A 101     3753   4522   3933    608   -700    -31       C  
ATOM    601  O   ASN A 101      29.327  -9.541  74.266  1.00 32.89           O  
ANISOU  601  O   ASN A 101     3843   4588   4066    592   -646     -9       O  
ATOM    602  CB  ASN A 101      31.355  -9.790  77.300  1.00 27.49           C  
ANISOU  602  CB  ASN A 101     3173   4001   3270    735   -858    -59       C  
ATOM    603  CG  ASN A 101      31.177  -8.747  78.384  1.00 47.18           C  
ANISOU  603  CG  ASN A 101     5695   6518   5715    709   -888    -84       C  
ATOM    604  OD1 ASN A 101      30.273  -7.911  78.334  1.00 39.07           O  
ANISOU  604  OD1 ASN A 101     4696   5467   4682    649   -838    -83       O  
ATOM    605  ND2 ASN A 101      32.066  -8.781  79.373  1.00 44.20           N  
ANISOU  605  ND2 ASN A 101     5308   6186   5300    760   -976   -113       N  
ATOM    606  N   TRP A 102      29.776  -7.804  75.547  1.00 27.24           N  
ANISOU  606  N   TRP A 102     3107   3924   3321    554   -705    -68       N  
ATOM    607  CA  TRP A 102      29.993  -6.832  74.523  1.00 26.48           C  
ANISOU  607  CA  TRP A 102     2937   3836   3288    482   -672    -98       C  
ATOM    608  C   TRP A 102      31.399  -6.265  74.856  1.00 30.59           C  
ANISOU  608  C   TRP A 102     3372   4420   3831    479   -743   -156       C  
ATOM    609  O   TRP A 102      31.557  -5.452  75.786  1.00 30.39           O  
ANISOU  609  O   TRP A 102     3360   4409   3779    465   -791   -188       O  
ATOM    610  CB  TRP A 102      28.911  -5.742  74.479  1.00 24.72           C  
ANISOU  610  CB  TRP A 102     2754   3578   3060    417   -626    -95       C  
ATOM    611  CG  TRP A 102      29.122  -4.838  73.331  1.00 25.39           C  
ANISOU  611  CG  TRP A 102     2774   3662   3211    344   -593   -116       C  
ATOM    612  CD1 TRP A 102      29.621  -3.567  73.359  1.00 28.44           C  
ANISOU  612  CD1 TRP A 102     3121   4062   3625    286   -617   -158       C  
ATOM    613  CD2 TRP A 102      28.905  -5.155  71.957  1.00 24.71           C  
ANISOU  613  CD2 TRP A 102     2658   3562   3169    320   -532    -93       C  
ATOM    614  NE1 TRP A 102      29.710  -3.063  72.084  1.00 27.57           N  
ANISOU  614  NE1 TRP A 102     2960   3945   3572    222   -572   -156       N  
ATOM    615  CE2 TRP A 102      29.275  -4.020  71.203  1.00 28.54           C  
ANISOU  615  CE2 TRP A 102     3087   4055   3703    245   -518   -117       C  
ATOM    616  CE3 TRP A 102      28.425  -6.294  71.284  1.00 25.54           C  
ANISOU  616  CE3 TRP A 102     2785   3645   3275    351   -491    -54       C  
ATOM    617  CZ2 TRP A 102      29.183  -3.990  69.811  1.00 27.58           C  
ANISOU  617  CZ2 TRP A 102     2929   3928   3623    205   -462   -101       C  
ATOM    618  CZ3 TRP A 102      28.323  -6.259  69.903  1.00 26.50           C  
ANISOU  618  CZ3 TRP A 102     2868   3760   3440    314   -439    -46       C  
ATOM    619  CH2 TRP A 102      28.706  -5.119  69.180  1.00 27.19           C  
ANISOU  619  CH2 TRP A 102     2898   3864   3568    244   -423    -68       C  
ATOM    620  N   TYR A 103      32.392  -6.716  74.073  1.00 26.83           N  
ANISOU  620  N   TYR A 103     2807   3984   3402    493   -750   -172       N  
ATOM    621  CA  TYR A 103      33.801  -6.345  74.227  1.00 27.31           C  
ANISOU  621  CA  TYR A 103     2765   4119   3492    492   -813   -225       C  
ATOM    622  C   TYR A 103      34.171  -5.223  73.266  1.00 31.78           C  
ANISOU  622  C   TYR A 103     3247   4706   4122    393   -779   -252       C  
ATOM    623  O   TYR A 103      35.327  -4.792  73.244  1.00 32.32           O  
ANISOU  623  O   TYR A 103     3216   4840   4224    369   -821   -295       O  
ATOM    624  CB  TYR A 103      34.757  -7.509  73.866  1.00 28.87           C  
ANISOU  624  CB  TYR A 103     2900   4363   3708    571   -838   -232       C  
ATOM    625  CG  TYR A 103      34.722  -8.738  74.750  1.00 30.38           C  
ANISOU  625  CG  TYR A 103     3162   4539   3844    679   -888   -208       C  
ATOM    626  CD1 TYR A 103      35.273  -8.713  76.019  1.00 33.15           C  
ANISOU  626  CD1 TYR A 103     3523   4922   4151    726   -976   -229       C  
ATOM    627  CD2 TYR A 103      34.195  -9.941  74.285  1.00 30.44           C  
ANISOU  627  CD2 TYR A 103     3225   4497   3843    734   -853   -164       C  
ATOM    628  CE1 TYR A 103      35.266  -9.830  76.828  1.00 34.94           C  
ANISOU  628  CE1 TYR A 103     3821   5132   4322    825  -1025   -200       C  
ATOM    629  CE2 TYR A 103      34.176 -11.077  75.087  1.00 31.84           C  
ANISOU  629  CE2 TYR A 103     3478   4650   3971    829   -902   -136       C  
ATOM    630  CZ  TYR A 103      34.718 -11.018  76.364  1.00 41.62           C  
ANISOU  630  CZ  TYR A 103     4730   5921   5162    875   -987   -151       C  
ATOM    631  OH  TYR A 103      34.721 -12.130  77.190  1.00 42.86           O  
ANISOU  631  OH  TYR A 103     4969   6052   5264    971  -1041   -116       O  
ATOM    632  N   PHE A 104      33.233  -4.760  72.445  1.00 27.91           N  
ANISOU  632  N   PHE A 104     2792   4165   3649    333   -705   -224       N  
ATOM    633  CA  PHE A 104      33.607  -3.978  71.256  1.00 27.99           C  
ANISOU  633  CA  PHE A 104     2723   4192   3718    247   -660   -234       C  
ATOM    634  C   PHE A 104      33.376  -2.484  71.339  1.00 33.17           C  
ANISOU  634  C   PHE A 104     3391   4820   4392    152   -662   -249       C  
ATOM    635  O   PHE A 104      33.647  -1.775  70.373  1.00 33.15           O  
ANISOU  635  O   PHE A 104     3335   4825   4435     73   -626   -249       O  
ATOM    636  CB  PHE A 104      32.924  -4.560  70.020  1.00 28.98           C  
ANISOU  636  CB  PHE A 104     2866   4289   3856    249   -579   -193       C  
ATOM    637  CG  PHE A 104      32.975  -6.068  69.972  1.00 30.70           C  
ANISOU  637  CG  PHE A 104     3098   4513   4054    346   -581   -178       C  
ATOM    638  CD1 PHE A 104      34.158  -6.730  69.616  1.00 34.69           C  
ANISOU  638  CD1 PHE A 104     3511   5088   4581    393   -602   -205       C  
ATOM    639  CD2 PHE A 104      31.865  -6.824  70.320  1.00 31.59           C  
ANISOU  639  CD2 PHE A 104     3314   4562   4126    391   -565   -138       C  
ATOM    640  CE1 PHE A 104      34.215  -8.124  69.587  1.00 35.49           C  
ANISOU  640  CE1 PHE A 104     3635   5184   4666    491   -610   -194       C  
ATOM    641  CE2 PHE A 104      31.915  -8.201  70.297  1.00 34.29           C  
ANISOU  641  CE2 PHE A 104     3680   4896   4452    475   -573   -121       C  
ATOM    642  CZ  PHE A 104      33.086  -8.859  69.939  1.00 33.28           C  
ANISOU  642  CZ  PHE A 104     3472   4826   4346    529   -599   -151       C  
ATOM    643  N   GLY A 105      32.912  -1.986  72.478  1.00 30.19           N  
ANISOU  643  N   GLY A 105     3086   4410   3976    159   -704   -263       N  
ATOM    644  CA  GLY A 105      32.854  -0.547  72.676  1.00 30.59           C  
ANISOU  644  CA  GLY A 105     3148   4431   4045     76   -723   -290       C  
ATOM    645  C   GLY A 105      31.613   0.085  72.069  1.00 34.93           C  
ANISOU  645  C   GLY A 105     3768   4905   4598     35   -659   -259       C  
ATOM    646  O   GLY A 105      30.880  -0.536  71.292  1.00 34.32           O  
ANISOU  646  O   GLY A 105     3714   4807   4519     55   -595   -216       O  
ATOM    647  N   ASN A 106      31.378   1.331  72.445  1.00 31.85           N  
ANISOU  647  N   ASN A 106     3417   4472   4214    -19   -684   -285       N  
ATOM    648  CA  ASN A 106      30.174   2.057  72.067  1.00 30.94           C  
ANISOU  648  CA  ASN A 106     3378   4281   4097    -47   -638   -264       C  
ATOM    649  C   ASN A 106      29.980   2.255  70.578  1.00 33.68           C  
ANISOU  649  C   ASN A 106     3697   4610   4491   -104   -571   -226       C  
ATOM    650  O   ASN A 106      28.837   2.224  70.085  1.00 32.50           O  
ANISOU  650  O   ASN A 106     3604   4414   4330    -92   -519   -191       O  
ATOM    651  CB  ASN A 106      30.153   3.438  72.743  1.00 31.38           C  
ANISOU  651  CB  ASN A 106     3476   4291   4156    -93   -690   -310       C  
ATOM    652  CG  ASN A 106      29.091   3.543  73.811  1.00 54.53           C  
ANISOU  652  CG  ASN A 106     6507   7188   7024    -29   -701   -324       C  
ATOM    653  OD1 ASN A 106      27.906   3.304  73.546  1.00 50.36           O  
ANISOU  653  OD1 ASN A 106     6033   6628   6474      4   -644   -289       O  
ATOM    654  ND2 ASN A 106      29.498   3.899  75.021  1.00 46.63           N  
ANISOU  654  ND2 ASN A 106     5527   6199   5991    -11   -774   -376       N  
ATOM    655  N   PHE A 107      31.078   2.506  69.868  1.00 29.60           N  
ANISOU  655  N   PHE A 107     3092   4132   4022   -169   -573   -231       N  
ATOM    656  CA  PHE A 107      30.980   2.878  68.465  1.00 28.48           C  
ANISOU  656  CA  PHE A 107     2927   3976   3919   -236   -513   -195       C  
ATOM    657  C   PHE A 107      30.506   1.701  67.648  1.00 30.52           C  
ANISOU  657  C   PHE A 107     3179   4254   4162   -182   -449   -154       C  
ATOM    658  O   PHE A 107      29.603   1.837  66.834  1.00 29.73           O  
ANISOU  658  O   PHE A 107     3123   4111   4062   -193   -398   -119       O  
ATOM    659  CB  PHE A 107      32.300   3.392  67.875  1.00 31.14           C  
ANISOU  659  CB  PHE A 107     3163   4362   4306   -325   -522   -206       C  
ATOM    660  CG  PHE A 107      32.198   3.694  66.424  1.00 32.58           C  
ANISOU  660  CG  PHE A 107     3326   4537   4516   -390   -454   -162       C  
ATOM    661  CD1 PHE A 107      31.519   4.820  65.999  1.00 36.11           C  
ANISOU  661  CD1 PHE A 107     3841   4901   4977   -454   -440   -140       C  
ATOM    662  CD2 PHE A 107      32.710   2.823  65.485  1.00 34.57           C  
ANISOU  662  CD2 PHE A 107     3501   4861   4773   -377   -404   -142       C  
ATOM    663  CE1 PHE A 107      31.371   5.100  64.655  1.00 37.38           C  
ANISOU  663  CE1 PHE A 107     3995   5052   5154   -511   -380    -93       C  
ATOM    664  CE2 PHE A 107      32.567   3.072  64.126  1.00 37.85           C  
ANISOU  664  CE2 PHE A 107     3904   5274   5202   -433   -338   -100       C  
ATOM    665  CZ  PHE A 107      31.898   4.218  63.700  1.00 36.37           C  
ANISOU  665  CZ  PHE A 107     3787   5005   5026   -503   -326    -72       C  
ATOM    666  N   LEU A 108      31.143   0.555  67.834  1.00 26.64           N  
ANISOU  666  N   LEU A 108     2635   3827   3660   -121   -459   -163       N  
ATOM    667  CA  LEU A 108      30.737  -0.634  67.101  1.00 25.72           C  
ANISOU  667  CA  LEU A 108     2520   3724   3530    -66   -407   -131       C  
ATOM    668  C   LEU A 108      29.296  -1.047  67.494  1.00 29.25           C  
ANISOU  668  C   LEU A 108     3068   4109   3936    -12   -389   -105       C  
ATOM    669  O   LEU A 108      28.567  -1.588  66.669  1.00 28.74           O  
ANISOU  669  O   LEU A 108     3027   4026   3868      2   -337    -72       O  
ATOM    670  CB  LEU A 108      31.761  -1.758  67.274  1.00 25.70           C  
ANISOU  670  CB  LEU A 108     2445   3795   3525     -4   -429   -150       C  
ATOM    671  CG  LEU A 108      33.063  -1.426  66.525  1.00 30.71           C  
ANISOU  671  CG  LEU A 108     2963   4504   4202    -61   -423   -169       C  
ATOM    672  CD1 LEU A 108      34.221  -2.380  66.869  1.00 31.26           C  
ANISOU  672  CD1 LEU A 108     2947   4658   4272      6   -461   -201       C  
ATOM    673  CD2 LEU A 108      32.849  -1.364  65.010  1.00 32.05           C  
ANISOU  673  CD2 LEU A 108     3113   4677   4388   -105   -346   -136       C  
ATOM    674  N   CYS A 109      28.876  -0.732  68.721  1.00 25.67           N  
ANISOU  674  N   CYS A 109     2672   3629   3453     12   -430   -122       N  
ATOM    675  CA  CYS A 109      27.524  -1.083  69.174  1.00 24.79           C  
ANISOU  675  CA  CYS A 109     2647   3472   3299     58   -409    -98       C  
ATOM    676  C   CYS A 109      26.506  -0.370  68.292  1.00 27.33           C  
ANISOU  676  C   CYS A 109     3005   3744   3637     16   -360    -73       C  
ATOM    677  O   CYS A 109      25.567  -0.975  67.793  1.00 26.54           O  
ANISOU  677  O   CYS A 109     2935   3625   3524     39   -316    -40       O  
ATOM    678  CB  CYS A 109      27.311  -0.755  70.655  1.00 25.29           C  
ANISOU  678  CB  CYS A 109     2762   3527   3320     90   -459   -124       C  
ATOM    679  SG  CYS A 109      25.638  -1.043  71.279  1.00 28.75           S  
ANISOU  679  SG  CYS A 109     3297   3925   3701    139   -426    -96       S  
ATOM    680  N   LYS A 110      26.730   0.909  68.060  1.00 23.70           N  
ANISOU  680  N   LYS A 110     2541   3259   3205    -49   -372    -89       N  
ATOM    681  CA  LYS A 110      25.919   1.657  67.117  1.00 22.36           C  
ANISOU  681  CA  LYS A 110     2402   3041   3054    -90   -332    -64       C  
ATOM    682  C   LYS A 110      26.013   1.042  65.706  1.00 26.25           C  
ANISOU  682  C   LYS A 110     2854   3554   3565   -107   -279    -28       C  
ATOM    683  O   LYS A 110      24.976   0.813  65.058  1.00 25.15           O  
ANISOU  683  O   LYS A 110     2750   3389   3416    -93   -238      3       O  
ATOM    684  CB  LYS A 110      26.360   3.109  67.102  1.00 24.13           C  
ANISOU  684  CB  LYS A 110     2630   3229   3309   -162   -363    -85       C  
ATOM    685  CG  LYS A 110      26.074   3.853  68.414  1.00 20.62           C  
ANISOU  685  CG  LYS A 110     2241   2750   2842   -142   -415   -127       C  
ATOM    686  CD  LYS A 110      26.732   5.213  68.429  1.00 17.18           C  
ANISOU  686  CD  LYS A 110     1806   2277   2444   -220   -458   -154       C  
ATOM    687  CE  LYS A 110      26.436   5.939  69.708  1.00 25.43           C  
ANISOU  687  CE  LYS A 110     2914   3284   3464   -194   -514   -204       C  
ATOM    688  NZ  LYS A 110      24.945   6.029  70.039  1.00 34.65           N  
ANISOU  688  NZ  LYS A 110     4163   4411   4593   -128   -490   -199       N  
ATOM    689  N   ALA A 111      27.242   0.714  65.279  1.00 22.77           N  
ANISOU  689  N   ALA A 111     2336   3169   3146   -129   -281    -36       N  
ATOM    690  CA  ALA A 111      27.499   0.299  63.900  1.00 22.13           C  
ANISOU  690  CA  ALA A 111     2211   3118   3079   -150   -231    -11       C  
ATOM    691  C   ALA A 111      26.838  -1.011  63.530  1.00 25.61           C  
ANISOU  691  C   ALA A 111     2670   3565   3496    -85   -198      9       C  
ATOM    692  O   ALA A 111      26.378  -1.167  62.392  1.00 25.80           O  
ANISOU  692  O   ALA A 111     2700   3582   3520    -98   -154     35       O  
ATOM    693  CB  ALA A 111      28.964   0.228  63.603  1.00 23.41           C  
ANISOU  693  CB  ALA A 111     2279   3350   3266   -182   -238    -29       C  
ATOM    694  N   VAL A 112      26.791  -1.944  64.467  1.00 21.07           N  
ANISOU  694  N   VAL A 112     2109   2998   2898    -18   -224     -3       N  
ATOM    695  CA  VAL A 112      26.171  -3.224  64.175  1.00 20.51           C  
ANISOU  695  CA  VAL A 112     2063   2923   2807     38   -199     17       C  
ATOM    696  C   VAL A 112      24.641  -3.086  64.105  1.00 23.83           C  
ANISOU  696  C   VAL A 112     2555   3288   3211     39   -174     45       C  
ATOM    697  O   VAL A 112      24.011  -3.767  63.307  1.00 24.16           O  
ANISOU  697  O   VAL A 112     2612   3320   3249     51   -141     66       O  
ATOM    698  CB  VAL A 112      26.645  -4.371  65.156  1.00 24.25           C  
ANISOU  698  CB  VAL A 112     2535   3419   3261    110   -236      3       C  
ATOM    699  CG1 VAL A 112      28.167  -4.520  65.085  1.00 24.12           C  
ANISOU  699  CG1 VAL A 112     2434   3466   3264    115   -261    -29       C  
ATOM    700  CG2 VAL A 112      26.212  -4.098  66.570  1.00 24.18           C  
ANISOU  700  CG2 VAL A 112     2576   3387   3223    130   -273     -2       C  
ATOM    701  N   HIS A 113      24.064  -2.213  64.931  1.00 19.18           N  
ANISOU  701  N   HIS A 113     2007   2669   2613     29   -192     40       N  
ATOM    702  CA  HIS A 113      22.642  -1.815  64.823  1.00 17.98           C  
ANISOU  702  CA  HIS A 113     1910   2473   2449     27   -169     61       C  
ATOM    703  C   HIS A 113      22.371  -1.176  63.452  1.00 22.39           C  
ANISOU  703  C   HIS A 113     2461   3015   3030    -19   -137     79       C  
ATOM    704  O   HIS A 113      21.563  -1.681  62.666  1.00 21.84           O  
ANISOU  704  O   HIS A 113     2406   2936   2955    -11   -105    103       O  
ATOM    705  CB  HIS A 113      22.226  -0.851  65.960  1.00 18.26           C  
ANISOU  705  CB  HIS A 113     1985   2485   2469     32   -197     41       C  
ATOM    706  CG  HIS A 113      21.923  -1.537  67.255  1.00 21.08           C  
ANISOU  706  CG  HIS A 113     2371   2854   2785     85   -214     36       C  
ATOM    707  ND1 HIS A 113      22.897  -1.893  68.157  1.00 23.07           N  
ANISOU  707  ND1 HIS A 113     2607   3134   3022    107   -255     14       N  
ATOM    708  CD2 HIS A 113      20.755  -1.956  67.790  1.00 21.88           C  
ANISOU  708  CD2 HIS A 113     2514   2946   2852    118   -195     53       C  
ATOM    709  CE1 HIS A 113      22.345  -2.516  69.182  1.00 22.03           C  
ANISOU  709  CE1 HIS A 113     2516   3008   2847    153   -260     22       C  
ATOM    710  NE2 HIS A 113      21.043  -2.558  68.989  1.00 21.70           N  
ANISOU  710  NE2 HIS A 113     2508   2946   2792    157   -221     47       N  
ATOM    711  N   VAL A 114      23.060  -0.084  63.146  1.00 19.17           N  
ANISOU  711  N   VAL A 114     2036   2603   2647    -71   -148     70       N  
ATOM    712  CA  VAL A 114      22.842   0.600  61.882  1.00 18.87           C  
ANISOU  712  CA  VAL A 114     1999   2545   2623   -119   -121     94       C  
ATOM    713  C   VAL A 114      22.781  -0.455  60.787  1.00 23.58           C  
ANISOU  713  C   VAL A 114     2573   3173   3213   -106    -82    114       C  
ATOM    714  O   VAL A 114      21.873  -0.442  59.960  1.00 23.06           O  
ANISOU  714  O   VAL A 114     2535   3087   3140   -107    -58    138       O  
ATOM    715  CB  VAL A 114      23.952   1.658  61.584  1.00 23.84           C  
ANISOU  715  CB  VAL A 114     2597   3179   3281   -190   -134     88       C  
ATOM    716  CG1 VAL A 114      23.913   2.129  60.118  1.00 23.75           C  
ANISOU  716  CG1 VAL A 114     2584   3162   3278   -242    -98    123       C  
ATOM    717  CG2 VAL A 114      23.814   2.858  62.516  1.00 23.94           C  
ANISOU  717  CG2 VAL A 114     2652   3142   3303   -208   -177     67       C  
ATOM    718  N   ILE A 115      23.730  -1.387  60.805  1.00 21.31           N  
ANISOU  718  N   ILE A 115     2237   2934   2926    -87    -82     99       N  
ATOM    719  CA  ILE A 115      23.938  -2.328  59.706  1.00 21.51           C  
ANISOU  719  CA  ILE A 115     2235   2992   2945    -74    -49    107       C  
ATOM    720  C   ILE A 115      22.789  -3.340  59.704  1.00 27.70           C  
ANISOU  720  C   ILE A 115     3063   3750   3709    -26    -40    119       C  
ATOM    721  O   ILE A 115      22.283  -3.745  58.631  1.00 27.74           O  
ANISOU  721  O   ILE A 115     3079   3755   3707    -26    -12    133       O  
ATOM    722  CB  ILE A 115      25.355  -3.017  59.813  1.00 24.71           C  
ANISOU  722  CB  ILE A 115     2572   3460   3357    -55    -56     80       C  
ATOM    723  CG1 ILE A 115      26.428  -2.042  59.301  1.00 25.42           C  
ANISOU  723  CG1 ILE A 115     2603   3588   3466   -122    -48     76       C  
ATOM    724  CG2 ILE A 115      25.426  -4.299  59.011  1.00 24.83           C  
ANISOU  724  CG2 ILE A 115     2573   3501   3359    -11    -32     76       C  
ATOM    725  CD1 ILE A 115      27.856  -2.506  59.443  1.00 27.32           C  
ANISOU  725  CD1 ILE A 115     2761   3903   3719   -110    -56     46       C  
ATOM    726  N   TYR A 116      22.360  -3.708  60.912  1.00 24.44           N  
ANISOU  726  N   TYR A 116     2680   3320   3288     10    -64    113       N  
ATOM    727  CA  TYR A 116      21.166  -4.509  61.094  1.00 24.10           C  
ANISOU  727  CA  TYR A 116     2679   3249   3227     41    -56    130       C  
ATOM    728  C   TYR A 116      19.955  -3.804  60.482  1.00 26.62           C  
ANISOU  728  C   TYR A 116     3028   3540   3547     16    -37    151       C  
ATOM    729  O   TYR A 116      19.273  -4.364  59.648  1.00 25.54           O  
ANISOU  729  O   TYR A 116     2902   3398   3405     18    -18    164       O  
ATOM    730  CB  TYR A 116      20.949  -4.808  62.588  1.00 26.25           C  
ANISOU  730  CB  TYR A 116     2978   3513   3484     74    -83    126       C  
ATOM    731  CG  TYR A 116      19.699  -5.597  62.873  1.00 29.28           C  
ANISOU  731  CG  TYR A 116     3403   3872   3848     94    -71    149       C  
ATOM    732  CD1 TYR A 116      19.667  -6.987  62.694  1.00 31.36           C  
ANISOU  732  CD1 TYR A 116     3678   4131   4107    119    -69    158       C  
ATOM    733  CD2 TYR A 116      18.535  -4.961  63.275  1.00 30.34           C  
ANISOU  733  CD2 TYR A 116     3565   3991   3973     87    -62    160       C  
ATOM    734  CE1 TYR A 116      18.496  -7.736  62.939  1.00 31.40           C  
ANISOU  734  CE1 TYR A 116     3721   4113   4099    124    -58    184       C  
ATOM    735  CE2 TYR A 116      17.369  -5.695  63.522  1.00 31.59           C  
ANISOU  735  CE2 TYR A 116     3749   4139   4115     97    -46    183       C  
ATOM    736  CZ  TYR A 116      17.363  -7.080  63.363  1.00 40.62           C  
ANISOU  736  CZ  TYR A 116     4903   5275   5255    109    -44    197       C  
ATOM    737  OH  TYR A 116      16.197  -7.788  63.599  1.00 45.44           O  
ANISOU  737  OH  TYR A 116     5539   5873   5853    105    -30    224       O  
ATOM    738  N   THR A 117      19.695  -2.569  60.870  1.00 23.67           N  
ANISOU  738  N   THR A 117     2668   3147   3177     -4    -48    149       N  
ATOM    739  CA  THR A 117      18.535  -1.882  60.334  1.00 23.45           C  
ANISOU  739  CA  THR A 117     2668   3092   3148    -15    -36    167       C  
ATOM    740  C   THR A 117      18.662  -1.696  58.834  1.00 27.02           C  
ANISOU  740  C   THR A 117     3111   3549   3607    -46    -16    183       C  
ATOM    741  O   THR A 117      17.716  -1.947  58.092  1.00 26.17           O  
ANISOU  741  O   THR A 117     3019   3434   3491    -41     -3    199       O  
ATOM    742  CB  THR A 117      18.304  -0.523  60.966  1.00 35.02           C  
ANISOU  742  CB  THR A 117     4158   4529   4620    -24    -56    158       C  
ATOM    743  OG1 THR A 117      18.190  -0.663  62.390  1.00 37.42           O  
ANISOU  743  OG1 THR A 117     4474   4836   4909      8    -74    139       O  
ATOM    744  CG2 THR A 117      17.007   0.079  60.414  1.00 33.42           C  
ANISOU  744  CG2 THR A 117     3984   4299   4415    -20    -47    175       C  
ATOM    745  N   VAL A 118      19.825  -1.263  58.370  1.00 24.38           N  
ANISOU  745  N   VAL A 118     2748   3232   3282    -80    -13    180       N  
ATOM    746  CA  VAL A 118      20.023  -1.133  56.926  1.00 24.51           C  
ANISOU  746  CA  VAL A 118     2756   3263   3294   -110     12    198       C  
ATOM    747  C   VAL A 118      19.570  -2.400  56.200  1.00 27.34           C  
ANISOU  747  C   VAL A 118     3113   3639   3635    -81     30    199       C  
ATOM    748  O   VAL A 118      18.840  -2.323  55.236  1.00 27.23           O  
ANISOU  748  O   VAL A 118     3119   3619   3609    -87     42    217       O  
ATOM    749  CB  VAL A 118      21.491  -0.803  56.568  1.00 29.49           C  
ANISOU  749  CB  VAL A 118     3340   3931   3933   -151     21    193       C  
ATOM    750  CG1 VAL A 118      21.709  -0.865  55.053  1.00 29.97           C  
ANISOU  750  CG1 VAL A 118     3389   4020   3976   -177     56    213       C  
ATOM    751  CG2 VAL A 118      21.867   0.551  57.082  1.00 29.50           C  
ANISOU  751  CG2 VAL A 118     3350   3904   3954   -196     -1    195       C  
ATOM    752  N   ASN A 119      19.989  -3.559  56.694  1.00 23.63           N  
ANISOU  752  N   ASN A 119     2625   3189   3164    -47     27    179       N  
ATOM    753  CA  ASN A 119      19.721  -4.847  56.059  1.00 23.01           C  
ANISOU  753  CA  ASN A 119     2550   3120   3073    -18     38    173       C  
ATOM    754  C   ASN A 119      18.251  -5.231  56.086  1.00 27.59           C  
ANISOU  754  C   ASN A 119     3168   3667   3647     -7     33    187       C  
ATOM    755  O   ASN A 119      17.712  -5.658  55.079  1.00 26.72           O  
ANISOU  755  O   ASN A 119     3068   3557   3525     -8     42    191       O  
ATOM    756  CB  ASN A 119      20.549  -5.932  56.745  1.00 21.78           C  
ANISOU  756  CB  ASN A 119     2374   2979   2920     21     26    149       C  
ATOM    757  CG  ASN A 119      20.421  -7.292  56.067  1.00 38.61           C  
ANISOU  757  CG  ASN A 119     4517   5112   5042     53     31    137       C  
ATOM    758  OD1 ASN A 119      19.695  -8.171  56.535  1.00 27.27           O  
ANISOU  758  OD1 ASN A 119     3114   3643   3605     76     18    141       O  
ATOM    759  ND2 ASN A 119      21.151  -7.479  54.973  1.00 33.43           N  
ANISOU  759  ND2 ASN A 119     3834   4494   4375     55     52    122       N  
ATOM    760  N   LEU A 120      17.598  -5.113  57.238  1.00 25.65           N  
ANISOU  760  N   LEU A 120     2939   3399   3407      4     18    192       N  
ATOM    761  CA  LEU A 120      16.173  -5.439  57.304  1.00 26.08           C  
ANISOU  761  CA  LEU A 120     3018   3435   3458      9     18    206       C  
ATOM    762  C   LEU A 120      15.364  -4.613  56.273  1.00 29.51           C  
ANISOU  762  C   LEU A 120     3459   3865   3888    -10     23    220       C  
ATOM    763  O   LEU A 120      14.480  -5.144  55.583  1.00 28.91           O  
ANISOU  763  O   LEU A 120     3391   3787   3806    -11     24    226       O  
ATOM    764  CB  LEU A 120      15.601  -5.202  58.706  1.00 26.42           C  
ANISOU  764  CB  LEU A 120     3072   3467   3499     22      9    210       C  
ATOM    765  CG  LEU A 120      15.772  -6.309  59.774  1.00 32.10           C  
ANISOU  765  CG  LEU A 120     3799   4184   4212     44      2    209       C  
ATOM    766  CD1 LEU A 120      14.549  -6.366  60.724  1.00 32.54           C  
ANISOU  766  CD1 LEU A 120     3871   4237   4257     48      6    225       C  
ATOM    767  CD2 LEU A 120      16.030  -7.684  59.175  1.00 35.03           C  
ANISOU  767  CD2 LEU A 120     4177   4549   4585     51      1    207       C  
ATOM    768  N   TYR A 121      15.659  -3.320  56.182  1.00 25.22           N  
ANISOU  768  N   TYR A 121     2917   3316   3348    -26     21    226       N  
ATOM    769  CA  TYR A 121      14.930  -2.471  55.265  1.00 25.03           C  
ANISOU  769  CA  TYR A 121     2909   3281   3319    -38     19    244       C  
ATOM    770  C   TYR A 121      15.314  -2.741  53.812  1.00 28.73           C  
ANISOU  770  C   TYR A 121     3377   3769   3771    -56     32    251       C  
ATOM    771  O   TYR A 121      14.429  -2.915  52.954  1.00 28.79           O  
ANISOU  771  O   TYR A 121     3397   3778   3765    -52     29    260       O  
ATOM    772  CB  TYR A 121      15.114  -1.001  55.629  1.00 26.17           C  
ANISOU  772  CB  TYR A 121     3070   3401   3474    -50      7    250       C  
ATOM    773  CG  TYR A 121      14.528  -0.646  56.973  1.00 27.66           C  
ANISOU  773  CG  TYR A 121     3266   3573   3670    -24     -7    237       C  
ATOM    774  CD1 TYR A 121      13.559  -1.457  57.576  1.00 29.52           C  
ANISOU  774  CD1 TYR A 121     3494   3820   3900      3     -3    233       C  
ATOM    775  CD2 TYR A 121      14.902   0.514  57.636  1.00 28.32           C  
ANISOU  775  CD2 TYR A 121     3366   3630   3763    -29    -23    229       C  
ATOM    776  CE1 TYR A 121      13.010  -1.133  58.806  1.00 29.99           C  
ANISOU  776  CE1 TYR A 121     3560   3878   3958     29     -9    222       C  
ATOM    777  CE2 TYR A 121      14.351   0.842  58.851  1.00 29.24           C  
ANISOU  777  CE2 TYR A 121     3493   3736   3879      3    -35    212       C  
ATOM    778  CZ  TYR A 121      13.401   0.011  59.433  1.00 36.47           C  
ANISOU  778  CZ  TYR A 121     4397   4675   4783     34    -24    209       C  
ATOM    779  OH  TYR A 121      12.834   0.308  60.655  1.00 39.05           O  
ANISOU  779  OH  TYR A 121     4732   5005   5100     67    -29    191       O  
ATOM    780  N   SER A 122      16.612  -2.820  53.527  1.00 24.45           N  
ANISOU  780  N   SER A 122     2816   3250   3226    -72     47    244       N  
ATOM    781  CA  SER A 122      17.039  -2.774  52.133  1.00 23.70           C  
ANISOU  781  CA  SER A 122     2719   3180   3105    -91     66    253       C  
ATOM    782  C   SER A 122      16.599  -4.026  51.398  1.00 25.97           C  
ANISOU  782  C   SER A 122     3010   3485   3374    -68     69    238       C  
ATOM    783  O   SER A 122      16.117  -3.950  50.271  1.00 26.22           O  
ANISOU  783  O   SER A 122     3059   3524   3379    -74     71    249       O  
ATOM    784  CB  SER A 122      18.541  -2.526  51.992  1.00 25.81           C  
ANISOU  784  CB  SER A 122     2953   3481   3372   -117     87    249       C  
ATOM    785  OG  SER A 122      19.287  -3.443  52.757  1.00 34.04           O  
ANISOU  785  OG  SER A 122     3964   4542   4427    -91     87    218       O  
ATOM    786  N   SER A 123      16.727  -5.168  52.042  1.00 20.83           N  
ANISOU  786  N   SER A 123     2348   2832   2734    -42     65    214       N  
ATOM    787  CA  SER A 123      16.477  -6.435  51.382  1.00 20.07           C  
ANISOU  787  CA  SER A 123     2261   2742   2623    -22     63    193       C  
ATOM    788  C   SER A 123      15.013  -6.632  51.075  1.00 23.91           C  
ANISOU  788  C   SER A 123     2771   3206   3107    -24     44    202       C  
ATOM    789  O   SER A 123      14.677  -6.999  49.949  1.00 24.51           O  
ANISOU  789  O   SER A 123     2860   3293   3158    -24     42    195       O  
ATOM    790  CB  SER A 123      17.004  -7.599  52.216  1.00 22.63           C  
ANISOU  790  CB  SER A 123     2577   3058   2962      8     56    169       C  
ATOM    791  OG  SER A 123      16.534  -7.524  53.523  1.00 29.18           O  
ANISOU  791  OG  SER A 123     3413   3860   3815     10     42    180       O  
ATOM    792  N   VAL A 124      14.130  -6.386  52.045  1.00 19.08           N  
ANISOU  792  N   VAL A 124     2162   2571   2517    -25     30    215       N  
ATOM    793  CA  VAL A 124      12.702  -6.530  51.798  1.00 17.93           C  
ANISOU  793  CA  VAL A 124     2025   2415   2372    -29     13    223       C  
ATOM    794  C   VAL A 124      12.271  -5.570  50.696  1.00 21.75           C  
ANISOU  794  C   VAL A 124     2518   2911   2835    -37      8    239       C  
ATOM    795  O   VAL A 124      11.493  -5.941  49.802  1.00 22.26           O  
ANISOU  795  O   VAL A 124     2591   2983   2883    -38     -8    235       O  
ATOM    796  CB  VAL A 124      11.832  -6.366  53.097  1.00 20.78           C  
ANISOU  796  CB  VAL A 124     2377   2763   2756    -26      7    234       C  
ATOM    797  CG1 VAL A 124      11.764  -4.911  53.538  1.00 20.18           C  
ANISOU  797  CG1 VAL A 124     2298   2684   2684    -22      7    249       C  
ATOM    798  CG2 VAL A 124      10.408  -7.016  52.913  1.00 20.25           C  
ANISOU  798  CG2 VAL A 124     2305   2696   2694    -35     -9    236       C  
ATOM    799  N   TRP A 125      12.821  -4.363  50.704  1.00 17.55           N  
ANISOU  799  N   TRP A 125     1990   2379   2300    -44     16    257       N  
ATOM    800  CA  TRP A 125      12.478  -3.387  49.651  1.00 17.34           C  
ANISOU  800  CA  TRP A 125     1984   2355   2250    -52      8    280       C  
ATOM    801  C   TRP A 125      13.091  -3.752  48.300  1.00 22.71           C  
ANISOU  801  C   TRP A 125     2674   3065   2891    -62     22    277       C  
ATOM    802  O   TRP A 125      12.473  -3.528  47.261  1.00 23.78           O  
ANISOU  802  O   TRP A 125     2830   3209   2995    -61      8    289       O  
ATOM    803  CB  TRP A 125      12.790  -1.949  50.092  1.00 15.64           C  
ANISOU  803  CB  TRP A 125     1779   2117   2045    -61      8    303       C  
ATOM    804  CG  TRP A 125      11.661  -1.445  50.894  1.00 16.38           C  
ANISOU  804  CG  TRP A 125     1875   2189   2162    -38    -14    305       C  
ATOM    805  CD1 TRP A 125      11.539  -1.480  52.253  1.00 18.90           C  
ANISOU  805  CD1 TRP A 125     2179   2497   2507    -25    -14    292       C  
ATOM    806  CD2 TRP A 125      10.425  -0.938  50.392  1.00 16.35           C  
ANISOU  806  CD2 TRP A 125     1882   2179   2150    -19    -41    318       C  
ATOM    807  NE1 TRP A 125      10.330  -0.991  52.621  1.00 18.25           N  
ANISOU  807  NE1 TRP A 125     2095   2407   2433      1    -32    294       N  
ATOM    808  CE2 TRP A 125       9.622  -0.646  51.496  1.00 19.77           C  
ANISOU  808  CE2 TRP A 125     2300   2602   2608      8    -52    309       C  
ATOM    809  CE3 TRP A 125       9.942  -0.649  49.110  1.00 17.92           C  
ANISOU  809  CE3 TRP A 125     2103   2386   2320    -17    -59    336       C  
ATOM    810  CZ2 TRP A 125       8.348  -0.087  51.369  1.00 19.24           C  
ANISOU  810  CZ2 TRP A 125     2232   2535   2544     40    -78    314       C  
ATOM    811  CZ3 TRP A 125       8.658  -0.107  48.980  1.00 19.37           C  
ANISOU  811  CZ3 TRP A 125     2289   2564   2506     15    -92    343       C  
ATOM    812  CH2 TRP A 125       7.882   0.164  50.104  1.00 19.74           C  
ANISOU  812  CH2 TRP A 125     2313   2604   2584     44   -101    330       C  
ATOM    813  N   ILE A 126      14.272  -4.357  48.293  1.00 18.92           N  
ANISOU  813  N   ILE A 126     2179   2606   2405    -65     47    258       N  
ATOM    814  CA  ILE A 126      14.799  -4.867  47.035  1.00 19.16           C  
ANISOU  814  CA  ILE A 126     2215   2673   2391    -64     64    246       C  
ATOM    815  C   ILE A 126      13.807  -5.881  46.451  1.00 22.22           C  
ANISOU  815  C   ILE A 126     2618   3058   2765    -46     38    222       C  
ATOM    816  O   ILE A 126      13.463  -5.800  45.273  1.00 21.22           O  
ANISOU  816  O   ILE A 126     2514   2953   2597    -47     31    226       O  
ATOM    817  CB  ILE A 126      16.235  -5.423  47.198  1.00 22.23           C  
ANISOU  817  CB  ILE A 126     2575   3093   2779    -59     95    221       C  
ATOM    818  CG1 ILE A 126      17.202  -4.280  47.438  1.00 21.83           C  
ANISOU  818  CG1 ILE A 126     2506   3055   2734    -91    119    248       C  
ATOM    819  CG2 ILE A 126      16.699  -6.183  45.956  1.00 23.57           C  
ANISOU  819  CG2 ILE A 126     2748   3306   2900    -44    113    195       C  
ATOM    820  CD1 ILE A 126      18.476  -4.764  48.016  1.00 27.22           C  
ANISOU  820  CD1 ILE A 126     3146   3765   3433    -83    140    222       C  
ATOM    821  N   LEU A 127      13.287  -6.763  47.306  1.00 19.83           N  
ANISOU  821  N   LEU A 127     2308   2730   2498    -35     21    202       N  
ATOM    822  CA  LEU A 127      12.224  -7.726  46.910  1.00 19.93           C  
ANISOU  822  CA  LEU A 127     2334   2732   2508    -31    -10    182       C  
ATOM    823  C   LEU A 127      10.994  -7.063  46.302  1.00 24.36           C  
ANISOU  823  C   LEU A 127     2903   3297   3056    -38    -38    202       C  
ATOM    824  O   LEU A 127      10.421  -7.557  45.331  1.00 24.03           O  
ANISOU  824  O   LEU A 127     2876   3266   2987    -37    -62    185       O  
ATOM    825  CB  LEU A 127      11.757  -8.573  48.107  1.00 19.38           C  
ANISOU  825  CB  LEU A 127     2254   2628   2482    -32    -23    172       C  
ATOM    826  CG  LEU A 127      12.765  -9.493  48.807  1.00 23.22           C  
ANISOU  826  CG  LEU A 127     2739   3099   2984    -16     -9    151       C  
ATOM    827  CD1 LEU A 127      12.005 -10.518  49.719  1.00 22.74           C  
ANISOU  827  CD1 LEU A 127     2685   2999   2956    -24    -30    147       C  
ATOM    828  CD2 LEU A 127      13.670 -10.196  47.813  1.00 24.11           C  
ANISOU  828  CD2 LEU A 127     2865   3230   3064      6     -1    115       C  
ATOM    829  N   ALA A 128      10.590  -5.951  46.912  1.00 21.02           N  
ANISOU  829  N   ALA A 128     2471   2864   2653    -41    -40    233       N  
ATOM    830  CA  ALA A 128       9.485  -5.149  46.422  1.00 20.17           C  
ANISOU  830  CA  ALA A 128     2368   2761   2535    -36    -70    254       C  
ATOM    831  C   ALA A 128       9.796  -4.565  45.043  1.00 23.99           C  
ANISOU  831  C   ALA A 128     2885   3266   2966    -36    -71    270       C  
ATOM    832  O   ALA A 128       8.913  -4.482  44.180  1.00 24.81           O  
ANISOU  832  O   ALA A 128     3000   3382   3042    -29   -105    272       O  
ATOM    833  CB  ALA A 128       9.174  -4.036  47.421  1.00 20.38           C  
ANISOU  833  CB  ALA A 128     2384   2767   2593    -29    -69    279       C  
ATOM    834  N   PHE A 129      11.032  -4.130  44.836  1.00 19.87           N  
ANISOU  834  N   PHE A 129     2374   2752   2423    -47    -36    283       N  
ATOM    835  CA  PHE A 129      11.452  -3.666  43.505  1.00 20.02           C  
ANISOU  835  CA  PHE A 129     2425   2799   2381    -54    -27    302       C  
ATOM    836  C   PHE A 129      11.537  -4.831  42.497  1.00 22.62           C  
ANISOU  836  C   PHE A 129     2763   3163   2667    -45    -29    264       C  
ATOM    837  O   PHE A 129      11.185  -4.660  41.329  1.00 22.98           O  
ANISOU  837  O   PHE A 129     2839   3234   2659    -41    -45    272       O  
ATOM    838  CB  PHE A 129      12.796  -2.937  43.581  1.00 22.39           C  
ANISOU  838  CB  PHE A 129     2726   3108   2674    -79     17    327       C  
ATOM    839  CG  PHE A 129      12.676  -1.471  43.812  1.00 24.63           C  
ANISOU  839  CG  PHE A 129     3031   3359   2967    -94      9    375       C  
ATOM    840  CD1 PHE A 129      12.202  -0.982  45.023  1.00 28.02           C  
ANISOU  840  CD1 PHE A 129     3449   3745   3452    -85     -9    378       C  
ATOM    841  CD2 PHE A 129      13.053  -0.568  42.820  1.00 27.53           C  
ANISOU  841  CD2 PHE A 129     3436   3737   3286   -117     19    419       C  
ATOM    842  CE1 PHE A 129      12.090   0.387  45.237  1.00 29.24           C  
ANISOU  842  CE1 PHE A 129     3633   3861   3617    -93    -22    416       C  
ATOM    843  CE2 PHE A 129      12.952   0.797  43.023  1.00 30.69           C  
ANISOU  843  CE2 PHE A 129     3869   4094   3699   -132      6    466       C  
ATOM    844  CZ  PHE A 129      12.470   1.282  44.225  1.00 28.54           C  
ANISOU  844  CZ  PHE A 129     3587   3771   3485   -118    -18    461       C  
ATOM    845  N   ILE A 130      12.020  -6.000  42.920  1.00 18.02           N  
ANISOU  845  N   ILE A 130     2162   2582   2104    -38    -16    221       N  
ATOM    846  CA  ILE A 130      11.904  -7.197  42.069  1.00 18.21           C  
ANISOU  846  CA  ILE A 130     2201   2624   2094    -22    -30    175       C  
ATOM    847  C   ILE A 130      10.440  -7.475  41.655  1.00 24.04           C  
ANISOU  847  C   ILE A 130     2952   3352   2832    -21    -85    166       C  
ATOM    848  O   ILE A 130      10.197  -7.902  40.531  1.00 24.14           O  
ANISOU  848  O   ILE A 130     2990   3389   2793    -12   -106    143       O  
ATOM    849  CB  ILE A 130      12.521  -8.450  42.712  1.00 20.72           C  
ANISOU  849  CB  ILE A 130     2504   2926   2442     -9    -18    130       C  
ATOM    850  CG1 ILE A 130      14.046  -8.345  42.701  1.00 21.27           C  
ANISOU  850  CG1 ILE A 130     2559   3028   2495      0     33    125       C  
ATOM    851  CG2 ILE A 130      12.090  -9.713  41.984  1.00 20.56           C  
ANISOU  851  CG2 ILE A 130     2509   2903   2400      7    -49     78       C  
ATOM    852  CD1 ILE A 130      14.726  -9.388  43.600  1.00 27.17           C  
ANISOU  852  CD1 ILE A 130     3288   3754   3281     22     41     89       C  
ATOM    853  N   SER A 131       9.477  -7.197  42.528  1.00 21.02           N  
ANISOU  853  N   SER A 131     2546   2941   2500    -29   -110    182       N  
ATOM    854  CA  SER A 131       8.063  -7.347  42.161  1.00 21.51           C  
ANISOU  854  CA  SER A 131     2604   3004   2563    -30   -163    176       C  
ATOM    855  C   SER A 131       7.459  -6.221  41.244  1.00 26.10           C  
ANISOU  855  C   SER A 131     3205   3610   3103    -18   -191    210       C  
ATOM    856  O   SER A 131       6.620  -6.488  40.367  1.00 25.23           O  
ANISOU  856  O   SER A 131     3105   3519   2963    -12   -236    194       O  
ATOM    857  CB ASER A 131       7.193  -7.567  43.408  0.50 24.41           C  
ANISOU  857  CB ASER A 131     2931   3345   2997    -42   -177    178       C  
ATOM    858  CB BSER A 131       7.233  -7.489  43.435  0.50 24.30           C  
ANISOU  858  CB BSER A 131     2917   3332   2984    -41   -175    180       C  
ATOM    859  OG ASER A 131       7.218  -6.453  44.264  0.50 32.34           O  
ANISOU  859  OG ASER A 131     3918   4340   4028    -35   -159    215       O  
ATOM    860  OG BSER A 131       7.838  -8.444  44.284  0.50 32.13           O  
ANISOU  860  OG BSER A 131     3902   4298   4009    -51   -151    159       O  
ATOM    861  N   LEU A 132       7.862  -4.976  41.469  1.00 23.31           N  
ANISOU  861  N   LEU A 132     2860   3249   2747    -14   -169    255       N  
ATOM    862  CA  LEU A 132       7.514  -3.876  40.547  1.00 23.85           C  
ANISOU  862  CA  LEU A 132     2963   3330   2768     -1   -193    294       C  
ATOM    863  C   LEU A 132       8.088  -4.144  39.151  1.00 28.07           C  
ANISOU  863  C   LEU A 132     3541   3904   3222     -2   -185    289       C  
ATOM    864  O   LEU A 132       7.449  -3.855  38.155  1.00 28.45           O  
ANISOU  864  O   LEU A 132     3618   3973   3220     12   -225    300       O  
ATOM    865  CB  LEU A 132       8.041  -2.536  41.059  1.00 23.91           C  
ANISOU  865  CB  LEU A 132     2985   3311   2789     -5   -168    344       C  
ATOM    866  CG  LEU A 132       7.380  -2.000  42.329  1.00 28.44           C  
ANISOU  866  CG  LEU A 132     3527   3850   3430      8   -181    351       C  
ATOM    867  CD1 LEU A 132       8.187  -0.856  42.947  1.00 27.98           C  
ANISOU  867  CD1 LEU A 132     3487   3757   3388     -2   -152    388       C  
ATOM    868  CD2 LEU A 132       5.948  -1.537  42.025  1.00 32.26           C  
ANISOU  868  CD2 LEU A 132     4006   4338   3913     41   -240    359       C  
ATOM    869  N   ASP A 133       9.300  -4.698  39.101  1.00 24.32           N  
ANISOU  869  N   ASP A 133     3067   3444   2731    -14   -135    270       N  
ATOM    870  CA  ASP A 133       9.973  -5.040  37.847  1.00 24.11           C  
ANISOU  870  CA  ASP A 133     3074   3464   2623    -11   -116    257       C  
ATOM    871  C   ASP A 133       9.228  -6.139  37.093  1.00 28.32           C  
ANISOU  871  C   ASP A 133     3619   4015   3127      6   -162    203       C  
ATOM    872  O   ASP A 133       8.964  -6.029  35.893  1.00 28.65           O  
ANISOU  872  O   ASP A 133     3699   4092   3093     18   -185    204       O  
ATOM    873  CB  ASP A 133      11.396  -5.501  38.135  1.00 25.50           C  
ANISOU  873  CB  ASP A 133     3233   3656   2799    -19    -52    238       C  
ATOM    874  CG  ASP A 133      12.182  -5.773  36.883  1.00 34.78           C  
ANISOU  874  CG  ASP A 133     4436   4893   3887    -11    -21    224       C  
ATOM    875  OD1 ASP A 133      12.447  -6.938  36.600  1.00 36.68           O  
ANISOU  875  OD1 ASP A 133     4675   5151   4111     10    -18    163       O  
ATOM    876  OD2 ASP A 133      12.528  -4.834  36.159  1.00 40.09           O  
ANISOU  876  OD2 ASP A 133     5136   5594   4501    -25      1    273       O  
ATOM    877  N   ARG A 134       8.887  -7.200  37.805  1.00 24.08           N  
ANISOU  877  N   ARG A 134     3053   3450   2647      5   -178    156       N  
ATOM    878  CA  ARG A 134       8.045  -8.244  37.250  1.00 23.82           C  
ANISOU  878  CA  ARG A 134     3029   3420   2603     10   -232    103       C  
ATOM    879  C   ARG A 134       6.726  -7.696  36.734  1.00 27.05           C  
ANISOU  879  C   ARG A 134     3440   3840   2997     14   -296    122       C  
ATOM    880  O   ARG A 134       6.243  -8.125  35.674  1.00 26.65           O  
ANISOU  880  O   ARG A 134     3417   3816   2892     23   -340     91       O  
ATOM    881  CB  ARG A 134       7.752  -9.327  38.287  1.00 23.40           C  
ANISOU  881  CB  ARG A 134     2944   3322   2625     -4   -243     66       C  
ATOM    882  CG  ARG A 134       7.298 -10.607  37.627  1.00 34.16           C  
ANISOU  882  CG  ARG A 134     4328   4681   3971     -5   -289      1       C  
ATOM    883  CD  ARG A 134       8.428 -11.583  37.380  1.00 39.87           C  
ANISOU  883  CD  ARG A 134     5078   5400   4669     15   -258    -49       C  
ATOM    884  NE  ARG A 134       9.677 -11.035  36.847  1.00 40.89           N  
ANISOU  884  NE  ARG A 134     5224   5575   4738     40   -199    -35       N  
ATOM    885  CZ  ARG A 134      10.007 -10.965  35.555  1.00 48.09           C  
ANISOU  885  CZ  ARG A 134     6173   6541   5559     62   -195    -51       C  
ATOM    886  NH1 ARG A 134       9.162 -11.346  34.619  1.00 30.25           N  
ANISOU  886  NH1 ARG A 134     3945   4294   3256     67   -253    -84       N  
ATOM    887  NH2 ARG A 134      11.188 -10.472  35.194  1.00 31.33           N  
ANISOU  887  NH2 ARG A 134     4054   4465   3386     76   -131    -33       N  
ATOM    888  N   TYR A 135       6.138  -6.772  37.491  1.00 23.57           N  
ANISOU  888  N   TYR A 135     2971   3380   2604     11   -304    166       N  
ATOM    889  CA  TYR A 135       4.853  -6.171  37.116  1.00 23.81           C  
ANISOU  889  CA  TYR A 135     2995   3424   2629     25   -367    184       C  
ATOM    890  C   TYR A 135       4.979  -5.404  35.801  1.00 26.97           C  
ANISOU  890  C   TYR A 135     3451   3858   2938     47   -383    215       C  
ATOM    891  O   TYR A 135       4.050  -5.370  35.026  1.00 27.05           O  
ANISOU  891  O   TYR A 135     3470   3892   2914     63   -445    207       O  
ATOM    892  CB  TYR A 135       4.305  -5.234  38.214  1.00 25.20           C  
ANISOU  892  CB  TYR A 135     3131   3574   2870     31   -367    224       C  
ATOM    893  CG  TYR A 135       3.408  -4.083  37.711  1.00 27.95           C  
ANISOU  893  CG  TYR A 135     3489   3935   3194     64   -417    262       C  
ATOM    894  CD1 TYR A 135       2.046  -4.265  37.465  1.00 30.61           C  
ANISOU  894  CD1 TYR A 135     3792   4296   3542     78   -487    243       C  
ATOM    895  CD2 TYR A 135       3.932  -2.819  37.508  1.00 28.83           C  
ANISOU  895  CD2 TYR A 135     3645   4033   3276     80   -399    319       C  
ATOM    896  CE1 TYR A 135       1.231  -3.186  37.006  1.00 32.44           C  
ANISOU  896  CE1 TYR A 135     4033   4541   3752    121   -539    277       C  
ATOM    897  CE2 TYR A 135       3.143  -1.752  37.059  1.00 30.26           C  
ANISOU  897  CE2 TYR A 135     3847   4215   3435    117   -450    357       C  
ATOM    898  CZ  TYR A 135       1.809  -1.937  36.813  1.00 38.44           C  
ANISOU  898  CZ  TYR A 135     4848   5277   4480    143   -520    335       C  
ATOM    899  OH  TYR A 135       1.097  -0.860  36.353  1.00 39.50           O  
ANISOU  899  OH  TYR A 135     5006   5412   4591    190   -574    372       O  
ATOM    900  N   LEU A 136       6.120  -4.782  35.566  1.00 23.17           N  
ANISOU  900  N   LEU A 136     3006   3382   2416     44   -327    251       N  
ATOM    901  CA  LEU A 136       6.311  -4.049  34.348  1.00 23.95           C  
ANISOU  901  CA  LEU A 136     3164   3513   2422     57   -334    289       C  
ATOM    902  C   LEU A 136       6.604  -5.012  33.207  1.00 29.37           C  
ANISOU  902  C   LEU A 136     3883   4248   3029     63   -338    240       C  
ATOM    903  O   LEU A 136       6.040  -4.878  32.150  1.00 29.70           O  
ANISOU  903  O   LEU A 136     3961   4322   3000     82   -386    243       O  
ATOM    904  CB  LEU A 136       7.418  -3.013  34.510  1.00 24.11           C  
ANISOU  904  CB  LEU A 136     3209   3523   2429     40   -270    351       C  
ATOM    905  CG  LEU A 136       7.165  -1.918  35.559  1.00 28.79           C  
ANISOU  905  CG  LEU A 136     3786   4062   3092     38   -272    399       C  
ATOM    906  CD1 LEU A 136       8.464  -1.131  35.807  1.00 28.73           C  
ANISOU  906  CD1 LEU A 136     3798   4041   3079      6   -204    447       C  
ATOM    907  CD2 LEU A 136       6.017  -0.964  35.137  1.00 32.09           C  
ANISOU  907  CD2 LEU A 136     4232   4469   3494     71   -341    438       C  
ATOM    908  N   ALA A 137       7.476  -5.987  33.430  1.00 26.67           N  
ANISOU  908  N   ALA A 137     3527   3910   2696     53   -291    193       N  
ATOM    909  CA  ALA A 137       7.783  -7.008  32.434  1.00 27.41           C  
ANISOU  909  CA  ALA A 137     3652   4045   2719     67   -295    132       C  
ATOM    910  C   ALA A 137       6.547  -7.733  31.851  1.00 34.25           C  
ANISOU  910  C   ALA A 137     4525   4916   3571     78   -382     81       C  
ATOM    911  O   ALA A 137       6.529  -8.043  30.675  1.00 34.73           O  
ANISOU  911  O   ALA A 137     4632   5022   3543     97   -406     53       O  
ATOM    912  CB  ALA A 137       8.771  -8.029  33.018  1.00 27.56           C  
ANISOU  912  CB  ALA A 137     3648   4052   2772     64   -243     81       C  
ATOM    913  N   ILE A 138       5.523  -7.989  32.663  1.00 32.55           N  
ANISOU  913  N   ILE A 138     4263   4661   3442     65   -430     68       N  
ATOM    914  CA  ILE A 138       4.350  -8.779  32.249  1.00 33.25           C  
ANISOU  914  CA  ILE A 138     4344   4754   3535     63   -514     15       C  
ATOM    915  C   ILE A 138       3.141  -7.928  31.888  1.00 40.12           C  
ANISOU  915  C   ILE A 138     5204   5644   4394     76   -583     50       C  
ATOM    916  O   ILE A 138       2.408  -8.248  30.955  1.00 40.65           O  
ANISOU  916  O   ILE A 138     5291   5743   4412     87   -653     17       O  
ATOM    917  CB  ILE A 138       3.902  -9.735  33.375  1.00 35.51           C  
ANISOU  917  CB  ILE A 138     4577   4991   3925     30   -525    -24       C  
ATOM    918  CG1 ILE A 138       4.976 -10.777  33.665  1.00 35.25           C  
ANISOU  918  CG1 ILE A 138     4560   4931   3903     26   -476    -70       C  
ATOM    919  CG2 ILE A 138       2.573 -10.420  33.030  1.00 36.33           C  
ANISOU  919  CG2 ILE A 138     4661   5099   4045     14   -615    -70       C  
ATOM    920  CD1 ILE A 138       4.644 -11.623  34.869  1.00 39.44           C  
ANISOU  920  CD1 ILE A 138     5048   5405   4534     -8   -481    -92       C  
ATOM    921  N   VAL A 139       2.852  -6.952  32.707  1.00 38.20           N  
ANISOU  921  N   VAL A 139     4927   5380   4206     78   -572    107       N  
ATOM    922  CA  VAL A 139       1.770  -6.040  32.483  1.00 39.30           C  
ANISOU  922  CA  VAL A 139     5055   5536   4343    103   -634    143       C  
ATOM    923  C   VAL A 139       1.916  -4.995  31.402  1.00 46.63           C  
ANISOU  923  C   VAL A 139     6050   6493   5174    137   -649    195       C  
ATOM    924  O   VAL A 139       0.995  -4.716  30.727  1.00 46.29           O  
ANISOU  924  O   VAL A 139     6014   6477   5096    164   -723    197       O  
ATOM    925  CB  VAL A 139       1.297  -5.427  33.751  1.00 42.46           C  
ANISOU  925  CB  VAL A 139     5395   5903   4835    101   -624    175       C  
ATOM    926  CG1 VAL A 139       0.144  -4.553  33.495  1.00 42.69           C  
ANISOU  926  CG1 VAL A 139     5407   5951   4862    138   -693    202       C  
ATOM    927  CG2 VAL A 139       0.925  -6.479  34.683  1.00 41.70           C  
ANISOU  927  CG2 VAL A 139     5234   5787   4821     65   -622    127       C  
ATOM    928  N   HIS A 140       3.078  -4.415  31.241  1.00 45.84           N  
ANISOU  928  N   HIS A 140     5999   6389   5031    134   -580    240       N  
ATOM    929  CA  HIS A 140       3.231  -3.369  30.272  1.00 47.71           C  
ANISOU  929  CA  HIS A 140     6304   6647   5175    158   -590    302       C  
ATOM    930  C   HIS A 140       4.361  -3.664  29.349  1.00 54.83           C  
ANISOU  930  C   HIS A 140     7266   7589   5980    149   -536    299       C  
ATOM    931  O   HIS A 140       5.291  -2.939  29.312  1.00 54.22           O  
ANISOU  931  O   HIS A 140     7221   7508   5872    135   -474    355       O  
ATOM    932  CB  HIS A 140       3.680  -2.103  30.970  1.00 48.34           C  
ANISOU  932  CB  HIS A 140     6394   6682   5291    155   -547    378       C  
ATOM    933  CG  HIS A 140       2.654  -1.476  31.843  1.00 51.69           C  
ANISOU  933  CG  HIS A 140     6772   7070   5800    178   -593    395       C  
ATOM    934  ND1 HIS A 140       2.041  -0.304  31.517  1.00 54.08           N  
ANISOU  934  ND1 HIS A 140     7109   7358   6079    218   -644    451       N  
ATOM    935  CD2 HIS A 140       2.155  -1.835  33.043  1.00 52.88           C  
ANISOU  935  CD2 HIS A 140     6845   7194   6052    171   -594    362       C  
ATOM    936  CE1 HIS A 140       1.194   0.028  32.467  1.00 53.23           C  
ANISOU  936  CE1 HIS A 140     6944   7224   6058    240   -675    446       C  
ATOM    937  NE2 HIS A 140       1.231  -0.893  33.398  1.00 52.78           N  
ANISOU  937  NE2 HIS A 140     6817   7164   6075    210   -643    393       N  
ATOM    938  N   ALA A 141       4.265  -4.683  28.539  1.00 54.43           N  
ANISOU  938  N   ALA A 141     7230   7579   5870    156   -562    234       N  
ATOM    939  CA  ALA A 141       5.373  -5.012  27.679  1.00 55.85           C  
ANISOU  939  CA  ALA A 141     7462   7807   5952    154   -505    222       C  
ATOM    940  C   ALA A 141       5.299  -4.257  26.343  1.00 63.57           C  
ANISOU  940  C   ALA A 141     8519   8836   6799    177   -529    273       C  
ATOM    941  O   ALA A 141       6.055  -4.472  25.436  1.00 64.23           O  
ANISOU  941  O   ALA A 141     8652   8975   6779    181   -489    266       O  
ATOM    942  CB  ALA A 141       5.495  -6.454  27.511  1.00 56.63           C  
ANISOU  942  CB  ALA A 141     7548   7920   6048    155   -510    126       C  
ATOM    943  N   THR A 142       4.362  -3.357  26.224  1.00 61.44           N  
ANISOU  943  N   THR A 142     8264   8551   6531    197   -596    324       N  
ATOM    944  CA  THR A 142       4.386  -2.517  25.088  1.00 62.57           C  
ANISOU  944  CA  THR A 142     8489   8731   6554    218   -614    388       C  
ATOM    945  C   THR A 142       5.700  -1.723  25.250  1.00 67.23           C  
ANISOU  945  C   THR A 142     9109   9313   7122    182   -509    464       C  
ATOM    946  O   THR A 142       6.510  -1.590  24.331  1.00 68.27           O  
ANISOU  946  O   THR A 142     9299   9499   7141    174   -460    491       O  
ATOM    947  CB  THR A 142       3.176  -1.640  25.172  1.00 71.22           C  
ANISOU  947  CB  THR A 142     9586   9796   7678    251   -704    432       C  
ATOM    948  OG1 THR A 142       3.101  -0.771  24.049  1.00 71.30           O  
ANISOU  948  OG1 THR A 142     9687   9836   7569    276   -735    502       O  
ATOM    949  CG2 THR A 142       3.226  -0.860  26.436  1.00 69.28           C  
ANISOU  949  CG2 THR A 142     9299   9479   7546    236   -674    479       C  
ATOM    950  N   ASN A 143       5.883  -1.189  26.455  1.00 62.40           N  
ANISOU  950  N   ASN A 143     8453   8636   6621    159   -477    496       N  
ATOM    951  CA  ASN A 143       7.063  -0.399  26.790  1.00 61.68           C  
ANISOU  951  CA  ASN A 143     8378   8527   6532    117   -387    565       C  
ATOM    952  C   ASN A 143       7.455  -0.550  28.258  1.00 62.79           C  
ANISOU  952  C   ASN A 143     8443   8613   6804     89   -342    544       C  
ATOM    953  O   ASN A 143       6.999   0.205  29.117  1.00 62.17           O  
ANISOU  953  O   ASN A 143     8347   8469   6807     91   -365    579       O  
ATOM    954  CB  ASN A 143       6.834   1.076  26.454  1.00 64.04           C  
ANISOU  954  CB  ASN A 143     8748   8792   6794    119   -412    671       C  
ATOM    955  CG  ASN A 143       5.696   1.684  27.251  1.00 92.78           C  
ANISOU  955  CG  ASN A 143    12363  12360  10528    152   -490    684       C  
ATOM    956  OD1 ASN A 143       4.650   1.062  27.436  1.00 85.49           O  
ANISOU  956  OD1 ASN A 143    11393  11442   9647    188   -559    621       O  
ATOM    957  ND2 ASN A 143       5.896   2.908  27.728  1.00 88.26           N  
ANISOU  957  ND2 ASN A 143    11822  11723   9991    138   -478    762       N  
ATOM    958  N   SER A 144       8.304  -1.535  28.533  1.00 57.06           N  
ANISOU  958  N   SER A 144     7674   7913   6092     71   -279    485       N  
ATOM    959  CA  SER A 144       8.755  -1.816  29.846  1.00 55.08           C  
ANISOU  959  CA  SER A 144     7355   7620   5952     48   -237    460       C  
ATOM    960  C   SER A 144      10.152  -1.253  29.989  1.00 57.26           C  
ANISOU  960  C   SER A 144     7636   7908   6214      4   -144    509       C  
ATOM    961  O   SER A 144      10.455  -0.742  31.016  1.00 56.51           O  
ANISOU  961  O   SER A 144     7510   7763   6200    -20   -121    534       O  
ATOM    962  CB  SER A 144       8.738  -3.330  30.154  1.00 57.72           C  
ANISOU  962  CB  SER A 144     7639   7968   6323     60   -238    360       C  
ATOM    963  OG  SER A 144       9.613  -4.109  29.356  1.00 65.28           O  
ANISOU  963  OG  SER A 144     8613   8989   7200     65   -191    318       O  
ATOM    964  N   GLN A 145      10.975  -1.336  28.938  1.00 52.63           N  
ANISOU  964  N   GLN A 145     7086   7393   5520     -6    -94    521       N  
ATOM    965  CA  GLN A 145      12.430  -1.231  28.982  1.00 51.80           C  
ANISOU  965  CA  GLN A 145     6961   7328   5393    -48      5    540       C  
ATOM    966  C   GLN A 145      12.939   0.029  29.572  1.00 54.04           C  
ANISOU  966  C   GLN A 145     7248   7565   5719   -100     39    625       C  
ATOM    967  O   GLN A 145      13.841  -0.009  30.339  1.00 53.25           O  
ANISOU  967  O   GLN A 145     7096   7462   5675   -132     96    619       O  
ATOM    968  CB  GLN A 145      13.081  -1.441  27.598  1.00 54.22           C  
ANISOU  968  CB  GLN A 145     7310   7734   5559    -47     52    544       C  
ATOM    969  CG  GLN A 145      14.501  -2.105  27.582  1.00 71.43           C  
ANISOU  969  CG  GLN A 145     9438   9986   7714    -61    150    503       C  
ATOM    970  CD  GLN A 145      15.624  -1.431  26.675  1.00 93.45           C  
ANISOU  970  CD  GLN A 145    12252  12862  10392   -106    240    571       C  
ATOM    971  OE1 GLN A 145      16.794  -1.460  27.028  1.00 90.66           O  
ANISOU  971  OE1 GLN A 145    11843  12548  10057   -139    322    571       O  
ATOM    972  NE2 GLN A 145      15.260  -0.890  25.523  1.00 84.24           N  
ANISOU  972  NE2 GLN A 145    11166  11730   9110   -106    223    626       N  
ATOM    973  N   ARG A 146      12.368   1.155  29.257  1.00 49.47           N  
ANISOU  973  N   ARG A 146     6733   6946   5118   -108     -2    703       N  
ATOM    974  CA  ARG A 146      12.853   2.362  29.859  1.00 48.35           C  
ANISOU  974  CA  ARG A 146     6603   6746   5022   -160     23    782       C  
ATOM    975  C   ARG A 146      12.592   2.447  31.334  1.00 49.01           C  
ANISOU  975  C   ARG A 146     6631   6750   5239   -157      2    755       C  
ATOM    976  O   ARG A 146      13.451   2.821  32.069  1.00 48.64           O  
ANISOU  976  O   ARG A 146     6554   6682   5245   -204     51    773       O  
ATOM    977  CB  ARG A 146      12.228   3.567  29.167  1.00 49.44           C  
ANISOU  977  CB  ARG A 146     6836   6845   5104   -161    -27    873       C  
ATOM    978  CG  ARG A 146      13.128   4.740  28.974  1.00 61.88           C  
ANISOU  978  CG  ARG A 146     8459   8404   6650   -234     26    972       C  
ATOM    979  CD  ARG A 146      12.991   5.260  27.539  1.00 76.71           C  
ANISOU  979  CD  ARG A 146    10434  10321   8391   -238     16   1046       C  
ATOM    980  NE  ARG A 146      13.995   6.260  27.157  1.00 88.24           N  
ANISOU  980  NE  ARG A 146    11943  11783   9801   -323     82   1147       N  
ATOM    981  CZ  ARG A 146      14.004   6.894  25.985  1.00104.38           C  
ANISOU  981  CZ  ARG A 146    14081  13853  11725   -343     83   1233       C  
ATOM    982  NH1 ARG A 146      13.079   6.627  25.081  1.00 91.20           N  
ANISOU  982  NH1 ARG A 146    12467  12212   9972   -276     18   1225       N  
ATOM    983  NH2 ARG A 146      14.935   7.794  25.710  1.00 92.43           N  
ANISOU  983  NH2 ARG A 146    12609  12338  10173   -432    146   1329       N  
ATOM    984  N   PRO A 147      11.397   2.141  31.778  1.00 43.09           N  
ANISOU  984  N   PRO A 147     5868   5960   4543   -105    -72    715       N  
ATOM    985  CA  PRO A 147      11.104   2.244  33.189  1.00 41.19           C  
ANISOU  985  CA  PRO A 147     5578   5651   4421   -100    -89    692       C  
ATOM    986  C   PRO A 147      11.774   1.197  34.033  1.00 42.25           C  
ANISOU  986  C   PRO A 147     5634   5806   4614   -109    -42    622       C  
ATOM    987  O   PRO A 147      12.052   1.485  35.143  1.00 41.75           O  
ANISOU  987  O   PRO A 147     5535   5697   4629   -126    -29    622       O  
ATOM    988  CB  PRO A 147       9.598   2.179  33.239  1.00 42.82           C  
ANISOU  988  CB  PRO A 147     5789   5829   4651    -41   -178    670       C  
ATOM    989  CG  PRO A 147       9.196   2.553  32.014  1.00 48.44           C  
ANISOU  989  CG  PRO A 147     6569   6566   5270    -24   -212    710       C  
ATOM    990  CD  PRO A 147      10.160   2.127  31.018  1.00 44.78           C  
ANISOU  990  CD  PRO A 147     6126   6177   4710    -53   -152    714       C  
ATOM    991  N   ARG A 148      11.944  -0.010  33.529  1.00 36.26           N  
ANISOU  991  N   ARG A 148     4852   5109   3816    -90    -27    561       N  
ATOM    992  CA  ARG A 148      12.605  -1.037  34.300  1.00 34.25           C  
ANISOU  992  CA  ARG A 148     4531   4868   3614    -91     13    496       C  
ATOM    993  C   ARG A 148      14.102  -0.724  34.423  1.00 38.37           C  
ANISOU  993  C   ARG A 148     5031   5422   4127   -138     95    520       C  
ATOM    994  O   ARG A 148      14.711  -0.976  35.465  1.00 37.50           O  
ANISOU  994  O   ARG A 148     4865   5295   4087   -150    123    495       O  
ATOM    995  CB  ARG A 148      12.410  -2.389  33.638  1.00 30.94           C  
ANISOU  995  CB  ARG A 148     4105   4500   3151    -55      2    422       C  
ATOM    996  CG  ARG A 148      10.987  -2.864  33.646  1.00 29.15           C  
ANISOU  996  CG  ARG A 148     3883   4245   2947    -19    -79    387       C  
ATOM    997  CD  ARG A 148      10.850  -4.046  32.759  1.00 28.23           C  
ANISOU  997  CD  ARG A 148     3777   4178   2770      8    -94    320       C  
ATOM    998  NE  ARG A 148      11.467  -5.207  33.375  1.00 32.65           N  
ANISOU  998  NE  ARG A 148     4293   4738   3375     14    -64    253       N  
ATOM    999  CZ  ARG A 148      11.849  -6.306  32.737  1.00 44.97           C  
ANISOU  999  CZ  ARG A 148     5861   6340   4886     38    -53    187       C  
ATOM   1000  NH1 ARG A 148      11.698  -6.427  31.437  1.00 36.26           N  
ANISOU 1000  NH1 ARG A 148     4805   5290   3681     57    -67    176       N  
ATOM   1001  NH2 ARG A 148      12.401  -7.290  33.420  1.00 32.91           N  
ANISOU 1001  NH2 ARG A 148     4296   4799   3409     48    -31    130       N  
ATOM   1002  N   LYS A 149      14.680  -0.173  33.358  1.00 35.99           N  
ANISOU 1002  N   LYS A 149     4770   5171   3735   -167    133    570       N  
ATOM   1003  CA  LYS A 149      16.071   0.264  33.357  1.00 36.46           C  
ANISOU 1003  CA  LYS A 149     4804   5270   3778   -223    213    605       C  
ATOM   1004  C   LYS A 149      16.278   1.386  34.370  1.00 40.76           C  
ANISOU 1004  C   LYS A 149     5345   5741   4403   -270    211    658       C  
ATOM   1005  O   LYS A 149      17.242   1.366  35.129  1.00 40.05           O  
ANISOU 1005  O   LYS A 149     5197   5657   4362   -303    255    647       O  
ATOM   1006  CB  LYS A 149      16.494   0.707  31.955  1.00 40.21           C  
ANISOU 1006  CB  LYS A 149     5332   5816   4132   -249    251    659       C  
ATOM   1007  CG  LYS A 149      17.988   1.027  31.819  1.00 57.50           C  
ANISOU 1007  CG  LYS A 149     7484   8071   6294   -312    345    690       C  
ATOM   1008  CD  LYS A 149      18.444   1.088  30.353  1.00 68.02           C  
ANISOU 1008  CD  LYS A 149     8854   9501   7488   -327    395    724       C  
ATOM   1009  CE  LYS A 149      19.957   1.321  30.243  1.00 77.49           C  
ANISOU 1009  CE  LYS A 149     9998  10784   8662   -393    497    749       C  
ATOM   1010  NZ  LYS A 149      20.485   0.980  28.886  1.00 87.43           N  
ANISOU 1010  NZ  LYS A 149    11270  12165   9783   -389    559    751       N  
ATOM   1011  N   LEU A 150      15.349   2.332  34.390  1.00 37.61           N  
ANISOU 1011  N   LEU A 150     5005   5269   4015   -268    152    710       N  
ATOM   1012  CA  LEU A 150      15.350   3.432  35.348  1.00 37.40           C  
ANISOU 1012  CA  LEU A 150     4988   5157   4064   -301    135    754       C  
ATOM   1013  C   LEU A 150      15.252   2.925  36.796  1.00 39.18           C  
ANISOU 1013  C   LEU A 150     5148   5344   4395   -278    122    692       C  
ATOM   1014  O   LEU A 150      15.986   3.381  37.666  1.00 38.36           O  
ANISOU 1014  O   LEU A 150     5015   5212   4347   -319    146    701       O  
ATOM   1015  CB  LEU A 150      14.166   4.367  35.053  1.00 38.30           C  
ANISOU 1015  CB  LEU A 150     5181   5201   4168   -275     62    805       C  
ATOM   1016  CG  LEU A 150      14.191   5.827  35.520  1.00 44.10           C  
ANISOU 1016  CG  LEU A 150     5969   5845   4943   -313     41    876       C  
ATOM   1017  CD1 LEU A 150      15.155   6.671  34.663  1.00 45.52           C  
ANISOU 1017  CD1 LEU A 150     6200   6042   5054   -392     90    961       C  
ATOM   1018  CD2 LEU A 150      12.765   6.425  35.491  1.00 46.91           C  
ANISOU 1018  CD2 LEU A 150     6383   6130   5309   -251    -48    893       C  
ATOM   1019  N   LEU A 151      14.330   2.008  37.068  1.00 34.84           N  
ANISOU 1019  N   LEU A 151     4576   4792   3869   -218     81    632       N  
ATOM   1020  CA  LEU A 151      14.183   1.481  38.428  1.00 33.56           C  
ANISOU 1020  CA  LEU A 151     4357   4596   3797   -198     69    579       C  
ATOM   1021  C   LEU A 151      15.459   0.782  38.893  1.00 38.11           C  
ANISOU 1021  C   LEU A 151     4871   5217   4393   -221    130    542       C  
ATOM   1022  O   LEU A 151      15.940   1.039  39.987  1.00 37.23           O  
ANISOU 1022  O   LEU A 151     4726   5075   4346   -240    140    537       O  
ATOM   1023  CB  LEU A 151      13.002   0.518  38.536  1.00 33.01           C  
ANISOU 1023  CB  LEU A 151     4274   4526   3744   -141     20    524       C  
ATOM   1024  CG  LEU A 151      11.627   1.127  38.833  1.00 37.32           C  
ANISOU 1024  CG  LEU A 151     4845   5016   4321   -107    -47    540       C  
ATOM   1025  CD1 LEU A 151      10.551   0.136  38.473  1.00 37.54           C  
ANISOU 1025  CD1 LEU A 151     4859   5067   4337    -64    -91    493       C  
ATOM   1026  CD2 LEU A 151      11.498   1.534  40.290  1.00 37.78           C  
ANISOU 1026  CD2 LEU A 151     4873   5016   4465   -105    -55    532       C  
ATOM   1027  N   ALA A 152      16.016  -0.082  38.049  1.00 35.95           N  
ANISOU 1027  N   ALA A 152     4582   5018   4059   -213    167    513       N  
ATOM   1028  CA  ALA A 152      17.164  -0.900  38.432  1.00 35.70           C  
ANISOU 1028  CA  ALA A 152     4486   5035   4042   -216    218    467       C  
ATOM   1029  C   ALA A 152      18.456  -0.109  38.639  1.00 41.31           C  
ANISOU 1029  C   ALA A 152     5169   5769   4760   -279    273    506       C  
ATOM   1030  O   ALA A 152      19.276  -0.505  39.469  1.00 41.15           O  
ANISOU 1030  O   ALA A 152     5087   5762   4786   -282    297    472       O  
ATOM   1031  CB  ALA A 152      17.383  -1.995  37.425  1.00 36.56           C  
ANISOU 1031  CB  ALA A 152     4592   5218   4081   -182    240    420       C  
ATOM   1032  N   GLU A 153      18.651   0.986  37.897  1.00 38.84           N  
ANISOU 1032  N   GLU A 153     4899   5460   4399   -330    290    578       N  
ATOM   1033  CA  GLU A 153      19.934   1.711  37.906  1.00 39.19           C  
ANISOU 1033  CA  GLU A 153     4914   5538   4439   -405    348    619       C  
ATOM   1034  C   GLU A 153      19.900   3.046  38.635  1.00 43.44           C  
ANISOU 1034  C   GLU A 153     5480   5990   5034   -460    323    676       C  
ATOM   1035  O   GLU A 153      20.953   3.567  38.998  1.00 43.90           O  
ANISOU 1035  O   GLU A 153     5501   6063   5117   -525    360    698       O  
ATOM   1036  CB  GLU A 153      20.409   1.978  36.487  1.00 41.69           C  
ANISOU 1036  CB  GLU A 153     5257   5931   4653   -440    398    665       C  
ATOM   1037  CG  GLU A 153      20.726   0.736  35.650  1.00 52.63           C  
ANISOU 1037  CG  GLU A 153     6612   7417   5967   -390    436    607       C  
ATOM   1038  CD  GLU A 153      20.802   1.057  34.154  1.00 73.06           C  
ANISOU 1038  CD  GLU A 153     9251  10071   8436   -411    471    656       C  
ATOM   1039  OE1 GLU A 153      20.667   2.249  33.801  1.00 66.97           O  
ANISOU 1039  OE1 GLU A 153     8538   9265   7642   -470    466    742       O  
ATOM   1040  OE2 GLU A 153      20.990   0.123  33.333  1.00 67.09           O  
ANISOU 1040  OE2 GLU A 153     8483   9400   7607   -367    500    608       O  
ATOM   1041  N   LYS A 154      18.717   3.617  38.846  1.00 39.28           N  
ANISOU 1041  N   LYS A 154     5017   5378   4529   -435    259    698       N  
ATOM   1042  CA  LYS A 154      18.625   4.908  39.537  1.00 38.73           C  
ANISOU 1042  CA  LYS A 154     4986   5217   4513   -477    228    746       C  
ATOM   1043  C   LYS A 154      17.722   4.990  40.756  1.00 41.01           C  
ANISOU 1043  C   LYS A 154     5278   5424   4880   -428    167    711       C  
ATOM   1044  O   LYS A 154      18.135   5.503  41.800  1.00 41.01           O  
ANISOU 1044  O   LYS A 154     5261   5379   4944   -456    160    706       O  
ATOM   1045  CB  LYS A 154      18.109   5.980  38.594  1.00 41.73           C  
ANISOU 1045  CB  LYS A 154     5460   5555   4839   -501    205    826       C  
ATOM   1046  CG  LYS A 154      19.187   6.567  37.680  1.00 55.89           C  
ANISOU 1046  CG  LYS A 154     7267   7397   6571   -589    266    894       C  
ATOM   1047  CD  LYS A 154      19.091   6.078  36.224  1.00 64.87           C  
ANISOU 1047  CD  LYS A 154     8430   8619   7598   -574    296    912       C  
ATOM   1048  CE  LYS A 154      19.778   7.064  35.273  1.00 74.94           C  
ANISOU 1048  CE  LYS A 154     9757   9912   8804   -664    338   1008       C  
ATOM   1049  NZ  LYS A 154      19.578   8.501  35.709  1.00 83.12           N  
ANISOU 1049  NZ  LYS A 154    10867  10827   9887   -716    294   1079       N  
ATOM   1050  N   VAL A 155      16.532   4.439  40.680  1.00 35.39           N  
ANISOU 1050  N   VAL A 155     4580   4701   4164   -357    125    681       N  
ATOM   1051  CA  VAL A 155      15.566   4.610  41.759  1.00 33.63           C  
ANISOU 1051  CA  VAL A 155     4362   4409   4008   -310     70    655       C  
ATOM   1052  C   VAL A 155      15.886   3.658  42.919  1.00 35.68           C  
ANISOU 1052  C   VAL A 155     4548   4687   4323   -290     84    589       C  
ATOM   1053  O   VAL A 155      15.537   3.943  44.064  1.00 34.42           O  
ANISOU 1053  O   VAL A 155     4381   4475   4221   -273     56    570       O  
ATOM   1054  CB  VAL A 155      14.113   4.449  41.277  1.00 36.91           C  
ANISOU 1054  CB  VAL A 155     4813   4810   4401   -246     17    651       C  
ATOM   1055  CG1 VAL A 155      13.129   4.407  42.449  1.00 35.91           C  
ANISOU 1055  CG1 VAL A 155     4668   4635   4341   -193    -28    613       C  
ATOM   1056  CG2 VAL A 155      13.764   5.591  40.316  1.00 37.32           C  
ANISOU 1056  CG2 VAL A 155     4949   4826   4405   -259     -9    723       C  
ATOM   1057  N   VAL A 156      16.572   2.552  42.638  1.00 31.95           N  
ANISOU 1057  N   VAL A 156     4024   4286   3827   -289    125    553       N  
ATOM   1058  CA  VAL A 156      16.945   1.621  43.696  1.00 31.02           C  
ANISOU 1058  CA  VAL A 156     3844   4183   3758   -268    134    495       C  
ATOM   1059  C   VAL A 156      17.854   2.281  44.732  1.00 35.55           C  
ANISOU 1059  C   VAL A 156     4393   4733   4383   -309    145    500       C  
ATOM   1060  O   VAL A 156      17.790   1.938  45.912  1.00 35.17           O  
ANISOU 1060  O   VAL A 156     4315   4664   4385   -286    129    463       O  
ATOM   1061  CB  VAL A 156      17.631   0.338  43.169  1.00 34.62           C  
ANISOU 1061  CB  VAL A 156     4256   4717   4180   -253    174    454       C  
ATOM   1062  CG1 VAL A 156      19.056   0.617  42.719  1.00 34.86           C  
ANISOU 1062  CG1 VAL A 156     4256   4806   4184   -306    230    472       C  
ATOM   1063  CG2 VAL A 156      17.633  -0.729  44.246  1.00 33.73           C  
ANISOU 1063  CG2 VAL A 156     4099   4602   4117   -214    165    396       C  
ATOM   1064  N   TYR A 157      18.694   3.224  44.302  1.00 32.35           N  
ANISOU 1064  N   TYR A 157     3999   4330   3961   -375    169    546       N  
ATOM   1065  CA  TYR A 157      19.558   3.956  45.225  1.00 31.82           C  
ANISOU 1065  CA  TYR A 157     3910   4235   3943   -425    173    551       C  
ATOM   1066  C   TYR A 157      18.740   4.945  46.029  1.00 36.36           C  
ANISOU 1066  C   TYR A 157     4539   4715   4563   -415    118    564       C  
ATOM   1067  O   TYR A 157      18.733   4.921  47.256  1.00 35.79           O  
ANISOU 1067  O   TYR A 157     4446   4613   4541   -398     97    528       O  
ATOM   1068  CB  TYR A 157      20.670   4.690  44.471  1.00 33.18           C  
ANISOU 1068  CB  TYR A 157     4080   4440   4087   -511    215    602       C  
ATOM   1069  CG  TYR A 157      21.632   3.734  43.829  1.00 34.23           C  
ANISOU 1069  CG  TYR A 157     4144   4680   4180   -516    275    580       C  
ATOM   1070  CD1 TYR A 157      21.572   3.459  42.479  1.00 36.39           C  
ANISOU 1070  CD1 TYR A 157     4437   5011   4378   -515    307    603       C  
ATOM   1071  CD2 TYR A 157      22.566   3.067  44.591  1.00 34.57           C  
ANISOU 1071  CD2 TYR A 157     4107   4772   4258   -512    294    530       C  
ATOM   1072  CE1 TYR A 157      22.429   2.547  41.905  1.00 37.47           C  
ANISOU 1072  CE1 TYR A 157     4512   5251   4475   -508    362    573       C  
ATOM   1073  CE2 TYR A 157      23.431   2.161  44.035  1.00 35.69           C  
ANISOU 1073  CE2 TYR A 157     4183   5013   4364   -502    346    502       C  
ATOM   1074  CZ  TYR A 157      23.364   1.897  42.696  1.00 43.60           C  
ANISOU 1074  CZ  TYR A 157     5204   6072   5292   -499    382    521       C  
ATOM   1075  OH  TYR A 157      24.227   0.983  42.150  1.00 45.14           O  
ANISOU 1075  OH  TYR A 157     5333   6369   5447   -480    434    485       O  
ATOM   1076  N   VAL A 158      18.033   5.811  45.333  1.00 34.02           N  
ANISOU 1076  N   VAL A 158     4314   4370   4241   -420     94    613       N  
ATOM   1077  CA  VAL A 158      17.479   6.986  45.984  1.00 34.81           C  
ANISOU 1077  CA  VAL A 158     4472   4374   4380   -418     45    630       C  
ATOM   1078  C   VAL A 158      16.238   6.634  46.800  1.00 39.06           C  
ANISOU 1078  C   VAL A 158     5011   4883   4946   -333      3    586       C  
ATOM   1079  O   VAL A 158      15.854   7.394  47.683  1.00 39.20           O  
ANISOU 1079  O   VAL A 158     5058   4833   5005   -316    -35    577       O  
ATOM   1080  CB  VAL A 158      17.172   8.113  44.948  1.00 40.00           C  
ANISOU 1080  CB  VAL A 158     5217   4982   5001   -448     27    703       C  
ATOM   1081  CG1 VAL A 158      15.943   7.763  44.111  1.00 39.77           C  
ANISOU 1081  CG1 VAL A 158     5220   4962   4927   -381      3    710       C  
ATOM   1082  CG2 VAL A 158      16.997   9.448  45.646  1.00 40.30           C  
ANISOU 1082  CG2 VAL A 158     5317   4912   5084   -463    -21    722       C  
ATOM   1083  N   GLY A 159      15.633   5.479  46.492  1.00 34.99           N  
ANISOU 1083  N   GLY A 159     4464   4422   4410   -283     10    557       N  
ATOM   1084  CA  GLY A 159      14.412   5.009  47.119  1.00 33.78           C  
ANISOU 1084  CA  GLY A 159     4301   4257   4277   -212    -22    520       C  
ATOM   1085  C   GLY A 159      14.566   3.761  47.968  1.00 37.26           C  
ANISOU 1085  C   GLY A 159     4676   4741   4740   -189     -4    466       C  
ATOM   1086  O   GLY A 159      13.664   3.448  48.752  1.00 37.14           O  
ANISOU 1086  O   GLY A 159     4648   4714   4749   -142    -26    437       O  
ATOM   1087  N   VAL A 160      15.674   3.027  47.836  1.00 32.83           N  
ANISOU 1087  N   VAL A 160     4072   4230   4169   -220     36    453       N  
ATOM   1088  CA  VAL A 160      15.911   1.886  48.734  1.00 31.71           C  
ANISOU 1088  CA  VAL A 160     3879   4119   4052   -195     47    404       C  
ATOM   1089  C   VAL A 160      17.072   2.171  49.672  1.00 34.47           C  
ANISOU 1089  C   VAL A 160     4199   4466   4433   -227     58    392       C  
ATOM   1090  O   VAL A 160      16.888   2.294  50.879  1.00 33.64           O  
ANISOU 1090  O   VAL A 160     4087   4331   4361   -208     38    370       O  
ATOM   1091  CB  VAL A 160      16.164   0.564  47.972  1.00 35.58           C  
ANISOU 1091  CB  VAL A 160     4339   4670   4510   -183     73    383       C  
ATOM   1092  CG1 VAL A 160      16.431  -0.582  48.942  1.00 34.81           C  
ANISOU 1092  CG1 VAL A 160     4198   4588   4439   -157     78    338       C  
ATOM   1093  CG2 VAL A 160      14.978   0.224  47.065  1.00 35.47           C  
ANISOU 1093  CG2 VAL A 160     4352   4660   4465   -154     54    389       C  
ATOM   1094  N   TRP A 161      18.265   2.303  49.113  1.00 30.77           N  
ANISOU 1094  N   TRP A 161     3709   4033   3950   -276     90    406       N  
ATOM   1095  CA  TRP A 161      19.447   2.403  49.932  1.00 30.33           C  
ANISOU 1095  CA  TRP A 161     3610   3991   3923   -307    100    388       C  
ATOM   1096  C   TRP A 161      19.447   3.650  50.796  1.00 34.49           C  
ANISOU 1096  C   TRP A 161     4167   4452   4486   -333     68    398       C  
ATOM   1097  O   TRP A 161      19.665   3.552  52.006  1.00 34.67           O  
ANISOU 1097  O   TRP A 161     4170   4464   4541   -319     51    365       O  
ATOM   1098  CB  TRP A 161      20.721   2.332  49.088  1.00 29.59           C  
ANISOU 1098  CB  TRP A 161     3476   3961   3805   -358    145    402       C  
ATOM   1099  CG  TRP A 161      21.060   0.965  48.632  1.00 30.34           C  
ANISOU 1099  CG  TRP A 161     3526   4127   3874   -321    174    369       C  
ATOM   1100  CD1 TRP A 161      20.938   0.473  47.366  1.00 33.40           C  
ANISOU 1100  CD1 TRP A 161     3921   4558   4211   -312    202    378       C  
ATOM   1101  CD2 TRP A 161      21.578  -0.100  49.427  1.00 29.88           C  
ANISOU 1101  CD2 TRP A 161     3416   4099   3837   -281    175    320       C  
ATOM   1102  NE1 TRP A 161      21.363  -0.834  47.319  1.00 32.64           N  
ANISOU 1102  NE1 TRP A 161     3780   4515   4105   -269    220    332       N  
ATOM   1103  CE2 TRP A 161      21.755  -1.213  48.574  1.00 33.89           C  
ANISOU 1103  CE2 TRP A 161     3903   4664   4308   -248    202    299       C  
ATOM   1104  CE3 TRP A 161      21.901  -0.230  50.775  1.00 30.87           C  
ANISOU 1104  CE3 TRP A 161     3516   4209   4003   -267    151    292       C  
ATOM   1105  CZ2 TRP A 161      22.251  -2.448  49.030  1.00 33.11           C  
ANISOU 1105  CZ2 TRP A 161     3763   4598   4218   -198    205    251       C  
ATOM   1106  CZ3 TRP A 161      22.414  -1.451  51.228  1.00 32.25           C  
ANISOU 1106  CZ3 TRP A 161     3647   4422   4184   -220    155    250       C  
ATOM   1107  CH2 TRP A 161      22.565  -2.548  50.356  1.00 32.98           C  
ANISOU 1107  CH2 TRP A 161     3723   4562   4245   -185    180    230       C  
ATOM   1108  N   ILE A 162      19.201   4.815  50.206  1.00 30.80           N  
ANISOU 1108  N   ILE A 162     3755   3937   4012   -369     57    442       N  
ATOM   1109  CA  ILE A 162      19.368   6.069  50.960  1.00 30.76           C  
ANISOU 1109  CA  ILE A 162     3785   3861   4042   -402     23    449       C  
ATOM   1110  C   ILE A 162      18.382   6.204  52.124  1.00 34.23           C  
ANISOU 1110  C   ILE A 162     4249   4249   4507   -338    -18    415       C  
ATOM   1111  O   ILE A 162      18.792   6.576  53.219  1.00 33.60           O  
ANISOU 1111  O   ILE A 162     4164   4144   4459   -346    -39    387       O  
ATOM   1112  CB  ILE A 162      19.356   7.326  50.065  1.00 34.39           C  
ANISOU 1112  CB  ILE A 162     4310   4267   4489   -458     15    509       C  
ATOM   1113  CG1 ILE A 162      20.733   7.514  49.400  1.00 35.30           C  
ANISOU 1113  CG1 ILE A 162     4392   4429   4593   -549     57    540       C  
ATOM   1114  CG2 ILE A 162      19.037   8.558  50.882  1.00 35.20           C  
ANISOU 1114  CG2 ILE A 162     4474   4273   4629   -462    -36    508       C  
ATOM   1115  CD1 ILE A 162      20.810   8.677  48.407  1.00 41.15           C  
ANISOU 1115  CD1 ILE A 162     5200   5123   5312   -617     57    612       C  
ATOM   1116  N   PRO A 163      17.090   5.900  51.897  1.00 30.86           N  
ANISOU 1116  N   PRO A 163     3846   3814   4065   -276    -30    414       N  
ATOM   1117  CA  PRO A 163      16.119   5.871  53.011  1.00 30.29           C  
ANISOU 1117  CA  PRO A 163     3782   3715   4012   -211    -60    378       C  
ATOM   1118  C   PRO A 163      16.482   4.881  54.112  1.00 33.15           C  
ANISOU 1118  C   PRO A 163     4090   4119   4386   -190    -48    334       C  
ATOM   1119  O   PRO A 163      16.259   5.150  55.299  1.00 32.58           O  
ANISOU 1119  O   PRO A 163     4024   4023   4331   -162    -70    304       O  
ATOM   1120  CB  PRO A 163      14.821   5.432  52.328  1.00 31.84           C  
ANISOU 1120  CB  PRO A 163     3988   3924   4184   -159    -63    387       C  
ATOM   1121  CG  PRO A 163      14.940   5.973  50.936  1.00 36.73           C  
ANISOU 1121  CG  PRO A 163     4646   4534   4778   -195    -60    437       C  
ATOM   1122  CD  PRO A 163      16.414   5.911  50.582  1.00 32.56           C  
ANISOU 1122  CD  PRO A 163     4093   4036   4245   -268    -26    452       C  
ATOM   1123  N   ALA A 164      17.025   3.734  53.708  1.00 28.98           N  
ANISOU 1123  N   ALA A 164     3515   3653   3844   -198    -16    329       N  
ATOM   1124  CA  ALA A 164      17.464   2.714  54.639  1.00 27.69           C  
ANISOU 1124  CA  ALA A 164     3305   3526   3688   -177     -8    294       C  
ATOM   1125  C   ALA A 164      18.523   3.312  55.514  1.00 31.74           C  
ANISOU 1125  C   ALA A 164     3807   4028   4224   -209    -22    277       C  
ATOM   1126  O   ALA A 164      18.474   3.170  56.729  1.00 31.49           O  
ANISOU 1126  O   ALA A 164     3770   3991   4203   -181    -40    247       O  
ATOM   1127  CB  ALA A 164      18.005   1.528  53.902  1.00 28.14           C  
ANISOU 1127  CB  ALA A 164     3323   3642   3727   -181     23    292       C  
ATOM   1128  N   LEU A 165      19.473   4.013  54.903  1.00 28.32           N  
ANISOU 1128  N   LEU A 165     3370   3594   3796   -273    -14    298       N  
ATOM   1129  CA  LEU A 165      20.518   4.668  55.683  1.00 28.51           C  
ANISOU 1129  CA  LEU A 165     3380   3607   3848   -316    -33    282       C  
ATOM   1130  C   LEU A 165      19.972   5.758  56.589  1.00 31.73           C  
ANISOU 1130  C   LEU A 165     3842   3940   4273   -305    -76    269       C  
ATOM   1131  O   LEU A 165      20.327   5.801  57.761  1.00 31.54           O  
ANISOU 1131  O   LEU A 165     3807   3913   4264   -294   -100    232       O  
ATOM   1132  CB  LEU A 165      21.636   5.195  54.792  1.00 29.56           C  
ANISOU 1132  CB  LEU A 165     3491   3759   3983   -397    -12    312       C  
ATOM   1133  CG  LEU A 165      22.735   4.160  54.494  1.00 35.33           C  
ANISOU 1133  CG  LEU A 165     4141   4579   4705   -408     24    299       C  
ATOM   1134  CD1 LEU A 165      23.200   4.215  53.029  1.00 36.22           C  
ANISOU 1134  CD1 LEU A 165     4238   4733   4791   -457     69    339       C  
ATOM   1135  CD2 LEU A 165      23.897   4.355  55.469  1.00 39.50           C  
ANISOU 1135  CD2 LEU A 165     4619   5126   5263   -440      5    268       C  
ATOM   1136  N   LEU A 166      19.091   6.615  56.080  1.00 27.72           N  
ANISOU 1136  N   LEU A 166     3396   3374   3763   -299    -90    294       N  
ATOM   1137  CA  LEU A 166      18.559   7.711  56.891  1.00 27.71           C  
ANISOU 1137  CA  LEU A 166     3454   3297   3779   -280   -135    276       C  
ATOM   1138  C   LEU A 166      17.768   7.202  58.090  1.00 32.95           C  
ANISOU 1138  C   LEU A 166     4111   3972   4436   -201   -147    231       C  
ATOM   1139  O   LEU A 166      17.869   7.778  59.192  1.00 32.45           O  
ANISOU 1139  O   LEU A 166     4069   3876   4384   -188   -179    195       O  
ATOM   1140  CB  LEU A 166      17.668   8.638  56.069  1.00 27.78           C  
ANISOU 1140  CB  LEU A 166     3530   3241   3783   -271   -151    311       C  
ATOM   1141  CG  LEU A 166      18.335   9.480  54.982  1.00 32.16           C  
ANISOU 1141  CG  LEU A 166     4117   3761   4340   -353   -149    364       C  
ATOM   1142  CD1 LEU A 166      17.275  10.148  54.141  1.00 31.70           C  
ANISOU 1142  CD1 LEU A 166     4128   3648   4268   -324   -166    401       C  
ATOM   1143  CD2 LEU A 166      19.314  10.478  55.608  1.00 34.26           C  
ANISOU 1143  CD2 LEU A 166     4403   3973   4640   -421   -180    353       C  
ATOM   1144  N   LEU A 167      16.997   6.123  57.890  1.00 30.47           N  
ANISOU 1144  N   LEU A 167     3771   3707   4101   -153   -120    234       N  
ATOM   1145  CA  LEU A 167      16.180   5.547  58.980  1.00 30.52           C  
ANISOU 1145  CA  LEU A 167     3767   3732   4095    -86   -123    201       C  
ATOM   1146  C   LEU A 167      16.988   4.880  60.071  1.00 35.25           C  
ANISOU 1146  C   LEU A 167     4332   4369   4693    -86   -123    170       C  
ATOM   1147  O   LEU A 167      16.403   4.477  61.067  1.00 35.07           O  
ANISOU 1147  O   LEU A 167     4307   4361   4655    -36   -125    146       O  
ATOM   1148  CB  LEU A 167      15.164   4.525  58.461  1.00 30.23           C  
ANISOU 1148  CB  LEU A 167     3709   3736   4040    -48    -96    215       C  
ATOM   1149  CG  LEU A 167      14.041   5.069  57.580  1.00 34.96           C  
ANISOU 1149  CG  LEU A 167     4338   4309   4634    -26   -103    238       C  
ATOM   1150  CD1 LEU A 167      13.190   3.924  57.166  1.00 34.39           C  
ANISOU 1150  CD1 LEU A 167     4234   4287   4547      1    -80    246       C  
ATOM   1151  CD2 LEU A 167      13.213   6.149  58.302  1.00 37.93           C  
ANISOU 1151  CD2 LEU A 167     4757   4639   5017     23   -135    216       C  
ATOM   1152  N   THR A 168      18.309   4.739  59.896  1.00 32.49           N  
ANISOU 1152  N   THR A 168     3950   4038   4355   -138   -120    171       N  
ATOM   1153  CA  THR A 168      19.153   4.202  60.967  1.00 32.26           C  
ANISOU 1153  CA  THR A 168     3889   4043   4326   -133   -131    140       C  
ATOM   1154  C   THR A 168      19.595   5.245  62.000  1.00 36.32           C  
ANISOU 1154  C   THR A 168     4429   4519   4852   -145   -175    105       C  
ATOM   1155  O   THR A 168      20.202   4.902  63.014  1.00 36.13           O  
ANISOU 1155  O   THR A 168     4385   4522   4822   -134   -193     74       O  
ATOM   1156  CB  THR A 168      20.403   3.515  60.420  1.00 41.53           C  
ANISOU 1156  CB  THR A 168     5005   5267   5507   -173   -113    148       C  
ATOM   1157  OG1 THR A 168      21.294   4.487  59.855  1.00 40.84           O  
ANISOU 1157  OG1 THR A 168     4914   5162   5443   -245   -121    159       O  
ATOM   1158  CG2 THR A 168      20.009   2.488  59.383  1.00 41.73           C  
ANISOU 1158  CG2 THR A 168     5011   5326   5517   -159    -75    174       C  
ATOM   1159  N   ILE A 169      19.296   6.513  61.748  1.00 32.86           N  
ANISOU 1159  N   ILE A 169     4042   4015   4429   -165   -197    109       N  
ATOM   1160  CA  ILE A 169      19.703   7.584  62.652  1.00 33.27           C  
ANISOU 1160  CA  ILE A 169     4129   4016   4494   -180   -245     71       C  
ATOM   1161  C   ILE A 169      19.278   7.321  64.107  1.00 37.76           C  
ANISOU 1161  C   ILE A 169     4709   4602   5037   -112   -264     24       C  
ATOM   1162  O   ILE A 169      20.068   7.550  65.005  1.00 37.84           O  
ANISOU 1162  O   ILE A 169     4716   4613   5049   -126   -298    -13       O  
ATOM   1163  CB  ILE A 169      19.235   8.972  62.104  1.00 36.77           C  
ANISOU 1163  CB  ILE A 169     4642   4372   4957   -200   -270     85       C  
ATOM   1164  CG1 ILE A 169      20.224   9.445  61.024  1.00 37.43           C  
ANISOU 1164  CG1 ILE A 169     4715   4438   5067   -296   -265    125       C  
ATOM   1165  CG2 ILE A 169      19.071  10.010  63.217  1.00 37.84           C  
ANISOU 1165  CG2 ILE A 169     4836   4443   5097   -176   -323     34       C  
ATOM   1166  CD1 ILE A 169      19.587  10.272  59.925  1.00 43.29           C  
ANISOU 1166  CD1 ILE A 169     5517   5117   5817   -312   -264    170       C  
ATOM   1167  N   PRO A 170      18.045   6.815  64.338  1.00 34.56           N  
ANISOU 1167  N   PRO A 170     4314   4215   4603    -42   -241     25       N  
ATOM   1168  CA  PRO A 170      17.629   6.351  65.664  1.00 34.25           C  
ANISOU 1168  CA  PRO A 170     4276   4209   4526     20   -244    -10       C  
ATOM   1169  C   PRO A 170      18.579   5.373  66.331  1.00 38.95           C  
ANISOU 1169  C   PRO A 170     4830   4862   5109     12   -246    -19       C  
ATOM   1170  O   PRO A 170      18.995   5.610  67.467  1.00 38.88           O  
ANISOU 1170  O   PRO A 170     4834   4856   5082     27   -280    -59       O  
ATOM   1171  CB  PRO A 170      16.295   5.675  65.389  1.00 35.48           C  
ANISOU 1171  CB  PRO A 170     4426   4395   4662     71   -203     13       C  
ATOM   1172  CG  PRO A 170      15.716   6.467  64.287  1.00 40.26           C  
ANISOU 1172  CG  PRO A 170     5056   4951   5289     61   -203     35       C  
ATOM   1173  CD  PRO A 170      16.883   6.964  63.443  1.00 35.98           C  
ANISOU 1173  CD  PRO A 170     4513   4375   4781    -17   -218     55       C  
ATOM   1174  N   ASP A 171      18.920   4.287  65.643  1.00 35.62           N  
ANISOU 1174  N   ASP A 171     4361   4482   4691     -5   -215     15       N  
ATOM   1175  CA  ASP A 171      19.861   3.291  66.178  1.00 35.44           C  
ANISOU 1175  CA  ASP A 171     4298   4510   4658     -4   -220      9       C  
ATOM   1176  C   ASP A 171      21.188   3.919  66.538  1.00 38.73           C  
ANISOU 1176  C   ASP A 171     4698   4922   5095    -48   -264    -21       C  
ATOM   1177  O   ASP A 171      21.738   3.676  67.618  1.00 38.80           O  
ANISOU 1177  O   ASP A 171     4701   4956   5084    -27   -295    -51       O  
ATOM   1178  CB  ASP A 171      20.111   2.165  65.171  1.00 37.46           C  
ANISOU 1178  CB  ASP A 171     4510   4800   4922    -17   -184     45       C  
ATOM   1179  CG  ASP A 171      18.967   1.160  65.118  1.00 54.73           C  
ANISOU 1179  CG  ASP A 171     6705   7004   7084     26   -149     69       C  
ATOM   1180  OD1 ASP A 171      19.160   0.016  65.619  1.00 56.88           O  
ANISOU 1180  OD1 ASP A 171     6964   7310   7337     52   -145     73       O  
ATOM   1181  OD2 ASP A 171      17.875   1.511  64.588  1.00 61.07           O  
ANISOU 1181  OD2 ASP A 171     7529   7786   7888     34   -130     84       O  
ATOM   1182  N   PHE A 172      21.710   4.724  65.628  1.00 34.90           N  
ANISOU 1182  N   PHE A 172     4206   4407   4648   -111   -268    -10       N  
ATOM   1183  CA  PHE A 172      22.942   5.458  65.896  1.00 35.24           C  
ANISOU 1183  CA  PHE A 172     4229   4442   4717   -169   -310    -37       C  
ATOM   1184  C   PHE A 172      22.804   6.289  67.166  1.00 37.75           C  
ANISOU 1184  C   PHE A 172     4597   4724   5021   -148   -362    -87       C  
ATOM   1185  O   PHE A 172      23.741   6.375  67.958  1.00 38.86           O  
ANISOU 1185  O   PHE A 172     4718   4885   5163   -162   -406   -123       O  
ATOM   1186  CB  PHE A 172      23.300   6.370  64.721  1.00 37.81           C  
ANISOU 1186  CB  PHE A 172     4555   4729   5083   -248   -303    -10       C  
ATOM   1187  CG  PHE A 172      24.357   7.370  65.041  1.00 40.94           C  
ANISOU 1187  CG  PHE A 172     4945   5099   5510   -319   -351    -36       C  
ATOM   1188  CD1 PHE A 172      25.702   7.020  64.949  1.00 45.57           C  
ANISOU 1188  CD1 PHE A 172     5453   5746   6116   -370   -357    -41       C  
ATOM   1189  CD2 PHE A 172      24.019   8.657  65.445  1.00 44.10           C  
ANISOU 1189  CD2 PHE A 172     5417   5417   5923   -335   -393    -59       C  
ATOM   1190  CE1 PHE A 172      26.708   7.955  65.252  1.00 47.84           C  
ANISOU 1190  CE1 PHE A 172     5726   6014   6437   -447   -404    -67       C  
ATOM   1191  CE2 PHE A 172      24.995   9.598  65.745  1.00 48.43           C  
ANISOU 1191  CE2 PHE A 172     5964   5933   6503   -411   -444    -86       C  
ATOM   1192  CZ  PHE A 172      26.352   9.252  65.652  1.00 47.39           C  
ANISOU 1192  CZ  PHE A 172     5747   5865   6393   -473   -449    -88       C  
ATOM   1193  N   ILE A 173      21.647   6.902  67.371  1.00 31.30           N  
ANISOU 1193  N   ILE A 173     3845   3858   4190   -108   -362    -95       N  
ATOM   1194  CA  ILE A 173      21.481   7.757  68.520  1.00 30.58           C  
ANISOU 1194  CA  ILE A 173     3808   3731   4082    -81   -411   -149       C  
ATOM   1195  C   ILE A 173      21.264   6.951  69.802  1.00 32.58           C  
ANISOU 1195  C   ILE A 173     4060   4039   4280    -10   -415   -177       C  
ATOM   1196  O   ILE A 173      21.885   7.241  70.825  1.00 32.12           O  
ANISOU 1196  O   ILE A 173     4012   3986   4205     -7   -464   -224       O  
ATOM   1197  CB  ILE A 173      20.334   8.762  68.316  1.00 33.57           C  
ANISOU 1197  CB  ILE A 173     4256   4037   4462    -52   -412   -155       C  
ATOM   1198  CG1 ILE A 173      20.763   9.834  67.318  1.00 34.25           C  
ANISOU 1198  CG1 ILE A 173     4363   4050   4600   -130   -430   -136       C  
ATOM   1199  CG2 ILE A 173      19.938   9.404  69.643  1.00 34.16           C  
ANISOU 1199  CG2 ILE A 173     4387   4089   4503      5   -453   -219       C  
ATOM   1200  CD1 ILE A 173      19.613  10.403  66.537  1.00 43.54           C  
ANISOU 1200  CD1 ILE A 173     5589   5171   5783   -103   -412   -110       C  
ATOM   1201  N   PHE A 174      20.407   5.938  69.744  1.00 27.82           N  
ANISOU 1201  N   PHE A 174     3447   3478   3645     41   -365   -146       N  
ATOM   1202  CA  PHE A 174      19.941   5.276  70.961  1.00 27.32           C  
ANISOU 1202  CA  PHE A 174     3398   3461   3521    108   -362   -163       C  
ATOM   1203  C   PHE A 174      20.706   3.995  71.315  1.00 29.51           C  
ANISOU 1203  C   PHE A 174     3632   3801   3780    113   -361   -146       C  
ATOM   1204  O   PHE A 174      20.561   3.489  72.409  1.00 29.57           O  
ANISOU 1204  O   PHE A 174     3656   3844   3734    161   -369   -159       O  
ATOM   1205  CB  PHE A 174      18.441   4.972  70.868  1.00 28.56           C  
ANISOU 1205  CB  PHE A 174     3574   3628   3651    161   -311   -140       C  
ATOM   1206  CG  PHE A 174      17.567   6.187  70.942  1.00 30.30           C  
ANISOU 1206  CG  PHE A 174     3844   3798   3871    189   -320   -171       C  
ATOM   1207  CD1 PHE A 174      17.411   6.868  72.149  1.00 33.94           C  
ANISOU 1207  CD1 PHE A 174     4351   4252   4291    234   -354   -229       C  
ATOM   1208  CD2 PHE A 174      16.881   6.640  69.819  1.00 31.78           C  
ANISOU 1208  CD2 PHE A 174     4036   3945   4093    178   -298   -145       C  
ATOM   1209  CE1 PHE A 174      16.601   7.968  72.240  1.00 34.93           C  
ANISOU 1209  CE1 PHE A 174     4525   4330   4415    272   -365   -265       C  
ATOM   1210  CE2 PHE A 174      16.081   7.735  69.890  1.00 35.03           C  
ANISOU 1210  CE2 PHE A 174     4496   4309   4505    214   -312   -175       C  
ATOM   1211  CZ  PHE A 174      15.933   8.413  71.110  1.00 33.93           C  
ANISOU 1211  CZ  PHE A 174     4401   4160   4329    264   -345   -237       C  
ATOM   1212  N   ALA A 175      21.491   3.458  70.394  1.00 24.56           N  
ANISOU 1212  N   ALA A 175     2952   3186   3192     70   -351   -117       N  
ATOM   1213  CA  ALA A 175      22.350   2.305  70.714  1.00 23.65           C  
ANISOU 1213  CA  ALA A 175     2796   3125   3064     82   -360   -108       C  
ATOM   1214  C   ALA A 175      23.513   2.718  71.618  1.00 25.83           C  
ANISOU 1214  C   ALA A 175     3061   3417   3336     72   -426   -155       C  
ATOM   1215  O   ALA A 175      24.318   3.555  71.248  1.00 24.18           O  
ANISOU 1215  O   ALA A 175     2829   3190   3171     14   -456   -176       O  
ATOM   1216  CB  ALA A 175      22.865   1.667  69.439  1.00 24.20           C  
ANISOU 1216  CB  ALA A 175     2810   3209   3174     47   -331    -72       C  
ATOM   1217  N   ASN A 176      23.586   2.126  72.801  1.00 23.54           N  
ANISOU 1217  N   ASN A 176     2788   3162   2992    125   -450   -169       N  
ATOM   1218  CA  ASN A 176      24.648   2.402  73.770  1.00 24.22           C  
ANISOU 1218  CA  ASN A 176     2865   3272   3064    125   -520   -216       C  
ATOM   1219  C   ASN A 176      24.982   1.149  74.646  1.00 28.17           C  
ANISOU 1219  C   ASN A 176     3363   3828   3513    185   -538   -205       C  
ATOM   1220  O   ASN A 176      24.193   0.195  74.733  1.00 26.44           O  
ANISOU 1220  O   ASN A 176     3169   3620   3257    227   -495   -163       O  
ATOM   1221  CB  ASN A 176      24.285   3.616  74.663  1.00 25.53           C  
ANISOU 1221  CB  ASN A 176     3091   3405   3204    133   -559   -270       C  
ATOM   1222  CG  ASN A 176      24.203   4.958  73.885  1.00 51.21           C  
ANISOU 1222  CG  ASN A 176     6354   6590   6514     71   -563   -287       C  
ATOM   1223  OD1 ASN A 176      23.139   5.603  73.828  1.00 48.08           O  
ANISOU 1223  OD1 ASN A 176     6010   6149   6107     89   -540   -292       O  
ATOM   1224  ND2 ASN A 176      25.315   5.366  73.278  1.00 42.14           N  
ANISOU 1224  ND2 ASN A 176     5154   5434   5423     -2   -591   -294       N  
ATOM   1225  N   VAL A 177      26.157   1.166  75.275  1.00 27.05           N  
ANISOU 1225  N   VAL A 177     3191   3719   3367    185   -604   -240       N  
ATOM   1226  CA  VAL A 177      26.644   0.040  76.074  1.00 28.52           C  
ANISOU 1226  CA  VAL A 177     3374   3955   3506    244   -634   -231       C  
ATOM   1227  C   VAL A 177      26.373   0.250  77.539  1.00 36.09           C  
ANISOU 1227  C   VAL A 177     4398   4929   4387    292   -675   -261       C  
ATOM   1228  O   VAL A 177      26.670   1.292  78.080  1.00 36.94           O  
ANISOU 1228  O   VAL A 177     4519   5027   4490    274   -724   -317       O  
ATOM   1229  CB  VAL A 177      28.139  -0.191  75.898  1.00 32.73           C  
ANISOU 1229  CB  VAL A 177     3828   4530   4079    227   -687   -252       C  
ATOM   1230  CG1 VAL A 177      28.610  -1.348  76.777  1.00 32.39           C  
ANISOU 1230  CG1 VAL A 177     3790   4534   3983    301   -727   -242       C  
ATOM   1231  CG2 VAL A 177      28.436  -0.475  74.419  1.00 32.11           C  
ANISOU 1231  CG2 VAL A 177     3682   4449   4070    185   -639   -222       C  
ATOM   1232  N   SER A 178      25.801  -0.753  78.178  1.00 34.33           N  
ANISOU 1232  N   SER A 178     4220   4727   4098    352   -655   -223       N  
ATOM   1233  CA  SER A 178      25.356  -0.644  79.568  1.00 35.20           C  
ANISOU 1233  CA  SER A 178     4400   4858   4116    403   -678   -241       C  
ATOM   1234  C   SER A 178      25.971  -1.796  80.373  1.00 40.05           C  
ANISOU 1234  C   SER A 178     5025   5517   4675    459   -720   -218       C  
ATOM   1235  O   SER A 178      26.209  -2.865  79.834  1.00 39.46           O  
ANISOU 1235  O   SER A 178     4924   5445   4623    469   -703   -170       O  
ATOM   1236  CB  SER A 178      23.826  -0.721  79.606  1.00 38.10           C  
ANISOU 1236  CB  SER A 178     4822   5210   4443    420   -601   -206       C  
ATOM   1237  OG  SER A 178      23.312  -0.497  80.908  1.00 47.08           O  
ANISOU 1237  OG  SER A 178     6025   6375   5487    467   -612   -227       O  
ATOM   1238  N   GLU A 179      26.244  -1.558  81.652  1.00 37.84           N  
ANISOU 1238  N   GLU A 179     4787   5270   4322    498   -779   -254       N  
ATOM   1239  CA  GLU A 179      26.692  -2.612  82.587  1.00 38.14           C  
ANISOU 1239  CA  GLU A 179     4854   5350   4287    561   -822   -228       C  
ATOM   1240  C   GLU A 179      25.478  -3.238  83.252  1.00 41.37           C  
ANISOU 1240  C   GLU A 179     5346   5766   4607    600   -764   -173       C  
ATOM   1241  O   GLU A 179      24.732  -2.545  83.953  1.00 40.71           O  
ANISOU 1241  O   GLU A 179     5312   5692   4462    610   -748   -199       O  
ATOM   1242  CB  GLU A 179      27.583  -2.012  83.684  1.00 40.58           C  
ANISOU 1242  CB  GLU A 179     5172   5697   4551    584   -920   -296       C  
ATOM   1243  CG  GLU A 179      29.018  -2.501  83.727  1.00 51.29           C  
ANISOU 1243  CG  GLU A 179     6466   7087   5934    600  -1003   -311       C  
ATOM   1244  CD  GLU A 179      29.729  -2.097  85.013  1.00 67.76           C  
ANISOU 1244  CD  GLU A 179     8576   9218   7951    637  -1103   -370       C  
ATOM   1245  OE1 GLU A 179      29.302  -1.129  85.687  1.00 55.64           O  
ANISOU 1245  OE1 GLU A 179     7090   7680   6369    630  -1116   -420       O  
ATOM   1246  OE2 GLU A 179      30.726  -2.750  85.359  1.00 65.27           O  
ANISOU 1246  OE2 GLU A 179     8231   8942   7625    677  -1174   -371       O  
ATOM   1247  N   ALA A 180      25.279  -4.535  83.059  1.00 37.99           N  
ANISOU 1247  N   ALA A 180     4932   5334   4168    621   -734    -99       N  
ATOM   1248  CA  ALA A 180      24.128  -5.233  83.664  1.00 37.99           C  
ANISOU 1248  CA  ALA A 180     5007   5341   4085    645   -675    -35       C  
ATOM   1249  C   ALA A 180      24.407  -6.716  83.796  1.00 43.21           C  
ANISOU 1249  C   ALA A 180     5698   5999   4723    680   -687     37       C  
ATOM   1250  O   ALA A 180      24.813  -7.371  82.835  1.00 42.98           O  
ANISOU 1250  O   ALA A 180     5626   5937   4768    668   -684     60       O  
ATOM   1251  CB  ALA A 180      22.853  -5.007  82.859  1.00 37.85           C  
ANISOU 1251  CB  ALA A 180     4983   5295   4102    602   -580    -10       C  
ATOM   1252  N   ASP A 181      24.180  -7.225  85.003  1.00 40.81           N  
ANISOU 1252  N   ASP A 181     5470   5725   4310    725   -702     70       N  
ATOM   1253  CA  ASP A 181      24.508  -8.606  85.412  1.00 40.85           C  
ANISOU 1253  CA  ASP A 181     5525   5723   4272    768   -730    141       C  
ATOM   1254  C   ASP A 181      25.871  -9.184  84.957  1.00 42.44           C  
ANISOU 1254  C   ASP A 181     5678   5910   4535    799   -809    128       C  
ATOM   1255  O   ASP A 181      25.947 -10.152  84.184  1.00 41.66           O  
ANISOU 1255  O   ASP A 181     5571   5769   4489    799   -793    174       O  
ATOM   1256  CB  ASP A 181      23.328  -9.538  85.127  1.00 42.69           C  
ANISOU 1256  CB  ASP A 181     5804   5925   4492    741   -643    230       C  
ATOM   1257  CG  ASP A 181      22.279  -9.480  86.249  1.00 53.14           C  
ANISOU 1257  CG  ASP A 181     7205   7289   5696    747   -596    266       C  
ATOM   1258  OD1 ASP A 181      21.184  -8.918  85.998  1.00 53.10           O  
ANISOU 1258  OD1 ASP A 181     7187   7294   5695    706   -516    262       O  
ATOM   1259  OD2 ASP A 181      22.575  -9.956  87.387  1.00 58.39           O  
ANISOU 1259  OD2 ASP A 181     7941   7985   6261    795   -640    295       O  
ATOM   1260  N   ASP A 182      26.923  -8.543  85.469  1.00 37.63           N  
ANISOU 1260  N   ASP A 182     5037   5341   3918    827   -895     60       N  
ATOM   1261  CA  ASP A 182      28.289  -9.061  85.499  1.00 37.31           C  
ANISOU 1261  CA  ASP A 182     4959   5315   3902    877   -988     42       C  
ATOM   1262  C   ASP A 182      28.945  -8.972  84.149  1.00 38.64           C  
ANISOU 1262  C   ASP A 182     5023   5464   4194    846   -983     11       C  
ATOM   1263  O   ASP A 182      29.862  -9.736  83.853  1.00 38.30           O  
ANISOU 1263  O   ASP A 182     4944   5422   4186    890  -1033     16       O  
ATOM   1264  CB  ASP A 182      28.330 -10.509  86.008  1.00 39.83           C  
ANISOU 1264  CB  ASP A 182     5357   5617   4161    941  -1011    122       C  
ATOM   1265  CG  ASP A 182      27.715 -10.671  87.403  1.00 48.86           C  
ANISOU 1265  CG  ASP A 182     6611   6787   5168    972  -1015    164       C  
ATOM   1266  OD1 ASP A 182      27.839  -9.738  88.230  1.00 48.27           O  
ANISOU 1266  OD1 ASP A 182     6543   6763   5034    979  -1049    107       O  
ATOM   1267  OD2 ASP A 182      27.111 -11.748  87.662  1.00 54.97           O  
ANISOU 1267  OD2 ASP A 182     7467   7529   5890    987   -983    253       O  
ATOM   1268  N   ARG A 183      28.347  -8.134  83.309  1.00 33.34           N  
ANISOU 1268  N   ARG A 183     4311   4774   3584    775   -915    -12       N  
ATOM   1269  CA  ARG A 183      28.711  -7.985  81.912  1.00 31.88           C  
ANISOU 1269  CA  ARG A 183     4036   4569   3510    732   -888    -31       C  
ATOM   1270  C   ARG A 183      28.301  -6.685  81.250  1.00 35.53           C  
ANISOU 1270  C   ARG A 183     4453   5020   4025    656   -841    -75       C  
ATOM   1271  O   ARG A 183      27.536  -5.953  81.762  1.00 34.62           O  
ANISOU 1271  O   ARG A 183     4381   4904   3867    638   -818    -86       O  
ATOM   1272  CB  ARG A 183      28.178  -9.154  81.097  1.00 29.29           C  
ANISOU 1272  CB  ARG A 183     3727   4191   3209    737   -830     37       C  
ATOM   1273  CG  ARG A 183      26.683  -9.207  80.941  1.00 35.11           C  
ANISOU 1273  CG  ARG A 183     4524   4891   3924    697   -739     87       C  
ATOM   1274  CD  ARG A 183      26.252 -10.086  79.827  1.00 38.25           C  
ANISOU 1274  CD  ARG A 183     4916   5239   4377    679   -685    134       C  
ATOM   1275  NE  ARG A 183      26.451  -9.431  78.567  1.00 39.77           N  
ANISOU 1275  NE  ARG A 183     5025   5427   4660    630   -655     94       N  
ATOM   1276  CZ  ARG A 183      26.300 -10.006  77.407  1.00 49.32           C  
ANISOU 1276  CZ  ARG A 183     6210   6602   5928    614   -616    114       C  
ATOM   1277  NH1 ARG A 183      26.500  -9.343  76.329  1.00 32.85           N  
ANISOU 1277  NH1 ARG A 183     4052   4518   3912    570   -590     80       N  
ATOM   1278  NH2 ARG A 183      25.949 -11.230  77.344  1.00 37.83           N  
ANISOU 1278  NH2 ARG A 183     4807   5108   4459    640   -604    169       N  
ATOM   1279  N   TYR A 184      28.823  -6.433  80.074  1.00 33.11           N  
ANISOU 1279  N   TYR A 184     4062   4707   3811    616   -828    -97       N  
ATOM   1280  CA  TYR A 184      28.389  -5.297  79.244  1.00 32.88           C  
ANISOU 1280  CA  TYR A 184     3997   4656   3839    540   -778   -125       C  
ATOM   1281  C   TYR A 184      27.242  -5.672  78.285  1.00 35.21           C  
ANISOU 1281  C   TYR A 184     4312   4905   4160    513   -686    -72       C  
ATOM   1282  O   TYR A 184      27.317  -6.681  77.574  1.00 35.20           O  
ANISOU 1282  O   TYR A 184     4298   4889   4188    527   -663    -35       O  
ATOM   1283  CB  TYR A 184      29.580  -4.718  78.450  1.00 34.90           C  
ANISOU 1283  CB  TYR A 184     4148   4935   4179    500   -811   -174       C  
ATOM   1284  CG  TYR A 184      30.576  -3.949  79.300  1.00 38.44           C  
ANISOU 1284  CG  TYR A 184     4565   5425   4614    499   -900   -239       C  
ATOM   1285  CD1 TYR A 184      30.169  -2.846  80.050  1.00 40.28           C  
ANISOU 1285  CD1 TYR A 184     4843   5649   4811    475   -918   -278       C  
ATOM   1286  CD2 TYR A 184      31.925  -4.317  79.348  1.00 40.56           C  
ANISOU 1286  CD2 TYR A 184     4757   5745   4907    525   -969   -266       C  
ATOM   1287  CE1 TYR A 184      31.062  -2.131  80.824  1.00 42.14           C  
ANISOU 1287  CE1 TYR A 184     5056   5920   5036    470  -1005   -343       C  
ATOM   1288  CE2 TYR A 184      32.835  -3.606  80.129  1.00 42.70           C  
ANISOU 1288  CE2 TYR A 184     4995   6061   5169    519  -1056   -329       C  
ATOM   1289  CZ  TYR A 184      32.392  -2.506  80.871  1.00 52.06           C  
ANISOU 1289  CZ  TYR A 184     6233   7229   6318    488  -1075   -367       C  
ATOM   1290  OH  TYR A 184      33.271  -1.771  81.662  1.00 56.52           O  
ANISOU 1290  OH  TYR A 184     6771   7832   6873    477  -1168   -435       O  
ATOM   1291  N   ILE A 185      26.198  -4.845  78.277  1.00 30.59           N  
ANISOU 1291  N   ILE A 185     3759   4298   3565    477   -638    -76       N  
ATOM   1292  CA  ILE A 185      25.031  -5.015  77.413  1.00 29.32           C  
ANISOU 1292  CA  ILE A 185     3613   4100   3427    447   -555    -34       C  
ATOM   1293  C   ILE A 185      24.954  -3.932  76.324  1.00 30.60           C  
ANISOU 1293  C   ILE A 185     3725   4239   3661    384   -527    -63       C  
ATOM   1294  O   ILE A 185      24.829  -2.769  76.635  1.00 29.91           O  
ANISOU 1294  O   ILE A 185     3646   4148   3571    362   -540   -104       O  
ATOM   1295  CB  ILE A 185      23.721  -4.943  78.265  1.00 32.73           C  
ANISOU 1295  CB  ILE A 185     4121   4531   3784    461   -515    -10       C  
ATOM   1296  CG1 ILE A 185      23.631  -6.120  79.240  1.00 33.80           C  
ANISOU 1296  CG1 ILE A 185     4316   4683   3844    513   -529     38       C  
ATOM   1297  CG2 ILE A 185      22.472  -4.935  77.377  1.00 32.28           C  
ANISOU 1297  CG2 ILE A 185     4066   4443   3755    426   -434     24       C  
ATOM   1298  CD1 ILE A 185      23.233  -7.450  78.561  1.00 40.88           C  
ANISOU 1298  CD1 ILE A 185     5224   5549   4760    513   -488    106       C  
ATOM   1299  N   CYS A 186      25.025  -4.334  75.056  1.00 26.13           N  
ANISOU 1299  N   CYS A 186     3117   3657   3156    358   -491    -41       N  
ATOM   1300  CA  CYS A 186      24.802  -3.436  73.893  1.00 25.19           C  
ANISOU 1300  CA  CYS A 186     2961   3513   3098    297   -454    -53       C  
ATOM   1301  C   CYS A 186      23.335  -3.537  73.445  1.00 28.41           C  
ANISOU 1301  C   CYS A 186     3408   3889   3499    288   -386    -15       C  
ATOM   1302  O   CYS A 186      22.860  -4.626  73.122  1.00 27.36           O  
ANISOU 1302  O   CYS A 186     3289   3749   3360    304   -354     29       O  
ATOM   1303  CB  CYS A 186      25.757  -3.769  72.735  1.00 25.23           C  
ANISOU 1303  CB  CYS A 186     2893   3528   3166    275   -453    -54       C  
ATOM   1304  SG  CYS A 186      25.359  -3.065  71.094  1.00 28.45           S  
ANISOU 1304  SG  CYS A 186     3266   3907   3638    206   -395    -45       S  
ATOM   1305  N   ASP A 187      22.635  -2.392  73.463  1.00 24.40           N  
ANISOU 1305  N   ASP A 187     2917   3361   2991    264   -371    -35       N  
ATOM   1306  CA  ASP A 187      21.185  -2.327  73.231  1.00 23.15           C  
ANISOU 1306  CA  ASP A 187     2793   3185   2820    263   -313     -8       C  
ATOM   1307  C   ASP A 187      20.755  -0.900  72.887  1.00 25.98           C  
ANISOU 1307  C   ASP A 187     3155   3515   3203    235   -308    -40       C  
ATOM   1308  O   ASP A 187      21.579   0.006  72.876  1.00 26.27           O  
ANISOU 1308  O   ASP A 187     3176   3540   3266    210   -349    -80       O  
ATOM   1309  CB  ASP A 187      20.450  -2.823  74.486  1.00 25.15           C  
ANISOU 1309  CB  ASP A 187     3099   3462   2995    308   -305      8       C  
ATOM   1310  CG  ASP A 187      19.060  -3.362  74.187  1.00 32.41           C  
ANISOU 1310  CG  ASP A 187     4035   4377   3901    307   -240     54       C  
ATOM   1311  OD1 ASP A 187      18.556  -3.109  73.080  1.00 32.64           O  
ANISOU 1311  OD1 ASP A 187     4041   4383   3978    277   -207     63       O  
ATOM   1312  OD2 ASP A 187      18.468  -4.022  75.064  1.00 35.72           O  
ANISOU 1312  OD2 ASP A 187     4492   4821   4260    333   -223     83       O  
ATOM   1313  N   ARG A 188      19.491  -0.694  72.567  1.00 21.75           N  
ANISOU 1313  N   ARG A 188     2638   2965   2663    238   -261    -22       N  
ATOM   1314  CA  ARG A 188      18.877   0.628  72.406  1.00 20.86           C  
ANISOU 1314  CA  ARG A 188     2542   2822   2563    230   -258    -53       C  
ATOM   1315  C   ARG A 188      18.152   1.060  73.636  1.00 24.12           C  
ANISOU 1315  C   ARG A 188     3000   3252   2913    277   -260    -80       C  
ATOM   1316  O   ARG A 188      17.233   0.452  74.039  1.00 23.53           O  
ANISOU 1316  O   ARG A 188     2938   3208   2796    306   -221    -54       O  
ATOM   1317  CB  ARG A 188      17.842   0.609  71.330  1.00 19.97           C  
ANISOU 1317  CB  ARG A 188     2420   2691   2477    217   -209    -21       C  
ATOM   1318  CG  ARG A 188      18.282   1.081  70.061  1.00 30.38           C  
ANISOU 1318  CG  ARG A 188     3713   3975   3856    170   -211    -16       C  
ATOM   1319  CD  ARG A 188      18.610  -0.036  69.199  1.00 38.56           C  
ANISOU 1319  CD  ARG A 188     4712   5024   4913    151   -189     23       C  
ATOM   1320  NE  ARG A 188      17.572  -0.383  68.253  1.00 43.69           N  
ANISOU 1320  NE  ARG A 188     5357   5666   5575    146   -145     57       N  
ATOM   1321  CZ  ARG A 188      16.904  -1.519  68.279  1.00 55.37           C  
ANISOU 1321  CZ  ARG A 188     6836   7166   7035    160   -115     89       C  
ATOM   1322  NH1 ARG A 188      17.140  -2.389  69.228  1.00 42.85           N  
ANISOU 1322  NH1 ARG A 188     5262   5605   5414    184   -122     97       N  
ATOM   1323  NH2 ARG A 188      16.003  -1.777  67.370  1.00 38.62           N  
ANISOU 1323  NH2 ARG A 188     4706   5038   4929    149    -82    115       N  
ATOM   1324  N   PHE A 189      18.582   2.142  74.228  1.00 20.99           N  
ANISOU 1324  N   PHE A 189     2627   2838   2510    283   -306   -135       N  
ATOM   1325  CA  PHE A 189      18.006   2.613  75.495  1.00 20.39           C  
ANISOU 1325  CA  PHE A 189     2598   2783   2365    336   -314   -174       C  
ATOM   1326  C   PHE A 189      17.340   3.961  75.313  1.00 24.65           C  
ANISOU 1326  C   PHE A 189     3164   3279   2921    347   -317   -217       C  
ATOM   1327  O   PHE A 189      17.962   4.928  74.875  1.00 24.57           O  
ANISOU 1327  O   PHE A 189     3160   3214   2960    313   -360   -248       O  
ATOM   1328  CB  PHE A 189      19.097   2.761  76.556  1.00 22.30           C  
ANISOU 1328  CB  PHE A 189     2857   3041   2573    346   -379   -217       C  
ATOM   1329  CG  PHE A 189      19.755   1.455  76.936  1.00 23.21           C  
ANISOU 1329  CG  PHE A 189     2956   3201   2662    353   -386   -180       C  
ATOM   1330  CD1 PHE A 189      19.234   0.678  77.970  1.00 25.90           C  
ANISOU 1330  CD1 PHE A 189     3329   3591   2920    401   -366   -159       C  
ATOM   1331  CD2 PHE A 189      20.877   0.996  76.234  1.00 23.98           C  
ANISOU 1331  CD2 PHE A 189     3006   3291   2815    314   -411   -164       C  
ATOM   1332  CE1 PHE A 189      19.814  -0.532  78.307  1.00 26.45           C  
ANISOU 1332  CE1 PHE A 189     3394   3690   2964    410   -378   -119       C  
ATOM   1333  CE2 PHE A 189      21.458  -0.200  76.564  1.00 26.34           C  
ANISOU 1333  CE2 PHE A 189     3293   3625   3090    331   -423   -133       C  
ATOM   1334  CZ  PHE A 189      20.938  -0.967  77.604  1.00 24.87           C  
ANISOU 1334  CZ  PHE A 189     3150   3476   2823    380   -410   -109       C  
ATOM   1335  N   TYR A 190      16.082   4.022  75.707  1.00 21.84           N  
ANISOU 1335  N   TYR A 190     2827   2950   2521    397   -275   -218       N  
ATOM   1336  CA  TYR A 190      15.236   5.173  75.468  1.00 21.70           C  
ANISOU 1336  CA  TYR A 190     2833   2896   2517    425   -271   -254       C  
ATOM   1337  C   TYR A 190      14.862   5.908  76.760  1.00 25.83           C  
ANISOU 1337  C   TYR A 190     3405   3437   2970    492   -289   -321       C  
ATOM   1338  O   TYR A 190      15.127   5.432  77.864  1.00 25.95           O  
ANISOU 1338  O   TYR A 190     3436   3504   2918    517   -296   -332       O  
ATOM   1339  CB  TYR A 190      13.956   4.709  74.793  1.00 22.38           C  
ANISOU 1339  CB  TYR A 190     2888   3006   2609    438   -204   -209       C  
ATOM   1340  CG  TYR A 190      14.209   3.985  73.502  1.00 23.39           C  
ANISOU 1340  CG  TYR A 190     2973   3118   2797    379   -185   -149       C  
ATOM   1341  CD1 TYR A 190      14.671   4.681  72.386  1.00 25.30           C  
ANISOU 1341  CD1 TYR A 190     3211   3294   3107    336   -210   -149       C  
ATOM   1342  CD2 TYR A 190      13.962   2.620  73.381  1.00 23.52           C  
ANISOU 1342  CD2 TYR A 190     2958   3181   2799    365   -142    -92       C  
ATOM   1343  CE1 TYR A 190      14.895   4.044  71.203  1.00 25.27           C  
ANISOU 1343  CE1 TYR A 190     3170   3282   3149    288   -191    -99       C  
ATOM   1344  CE2 TYR A 190      14.181   1.965  72.195  1.00 23.98           C  
ANISOU 1344  CE2 TYR A 190     2981   3221   2908    318   -128    -46       C  
ATOM   1345  CZ  TYR A 190      14.653   2.680  71.104  1.00 31.83           C  
ANISOU 1345  CZ  TYR A 190     3969   4161   3965    282   -151    -51       C  
ATOM   1346  OH  TYR A 190      14.877   2.052  69.907  1.00 32.56           O  
ANISOU 1346  OH  TYR A 190     4028   4242   4099    238   -136     -9       O  
ATOM   1347  N   PRO A 191      14.230   7.073  76.617  1.00 22.18           N  
ANISOU 1347  N   PRO A 191     2973   2931   2522    527   -299   -367       N  
ATOM   1348  CA  PRO A 191      13.613   7.752  77.765  1.00 22.99           C  
ANISOU 1348  CA  PRO A 191     3123   3059   2555    607   -305   -435       C  
ATOM   1349  C   PRO A 191      12.522   6.970  78.516  1.00 27.36           C  
ANISOU 1349  C   PRO A 191     3657   3714   3025    664   -234   -415       C  
ATOM   1350  O   PRO A 191      12.437   7.093  79.731  1.00 27.55           O  
ANISOU 1350  O   PRO A 191     3715   3785   2968    717   -239   -460       O  
ATOM   1351  CB  PRO A 191      13.039   9.017  77.139  1.00 24.68           C  
ANISOU 1351  CB  PRO A 191     3364   3198   2815    633   -323   -474       C  
ATOM   1352  CG  PRO A 191      14.040   9.330  76.052  1.00 28.54           C  
ANISOU 1352  CG  PRO A 191     3848   3602   3392    547   -367   -450       C  
ATOM   1353  CD  PRO A 191      14.426   7.988  75.485  1.00 23.10           C  
ANISOU 1353  CD  PRO A 191     3098   2960   2721    489   -329   -371       C  
ATOM   1354  N   ASN A 192      11.716   6.182  77.798  1.00 23.44           N  
ANISOU 1354  N   ASN A 192     3108   3252   2548    649   -170   -350       N  
ATOM   1355  CA  ASN A 192      10.602   5.439  78.390  1.00 23.82           C  
ANISOU 1355  CA  ASN A 192     3127   3397   2525    688    -96   -323       C  
ATOM   1356  C   ASN A 192      10.030   4.398  77.433  1.00 29.58           C  
ANISOU 1356  C   ASN A 192     3795   4149   3294    640    -41   -242       C  
ATOM   1357  O   ASN A 192      10.471   4.271  76.286  1.00 28.97           O  
ANISOU 1357  O   ASN A 192     3700   4014   3294    585    -59   -210       O  
ATOM   1358  CB  ASN A 192       9.480   6.384  78.888  1.00 22.70           C  
ANISOU 1358  CB  ASN A 192     2998   3285   2341    777    -75   -386       C  
ATOM   1359  CG  ASN A 192       8.835   7.232  77.756  1.00 28.16           C  
ANISOU 1359  CG  ASN A 192     3674   3917   3107    791    -81   -399       C  
ATOM   1360  OD1 ASN A 192       8.766   6.819  76.586  1.00 19.19           O  
ANISOU 1360  OD1 ASN A 192     2498   2754   2039    738    -69   -343       O  
ATOM   1361  ND2 ASN A 192       8.372   8.420  78.117  1.00 10.70           N  
ANISOU 1361  ND2 ASN A 192     1500   1685    880    870   -104   -476       N  
ATOM   1362  N   ASP A 193       9.041   3.655  77.909  1.00 28.15           N  
ANISOU 1362  N   ASP A 193     3583   4055   3057    659     27   -209       N  
ATOM   1363  CA  ASP A 193       8.523   2.497  77.184  1.00 28.09           C  
ANISOU 1363  CA  ASP A 193     3522   4075   3077    605     77   -130       C  
ATOM   1364  C   ASP A 193       7.751   2.880  75.917  1.00 29.43           C  
ANISOU 1364  C   ASP A 193     3648   4217   3318    600     89   -124       C  
ATOM   1365  O   ASP A 193       7.700   2.128  74.954  1.00 28.85           O  
ANISOU 1365  O   ASP A 193     3539   4127   3294    543    102    -69       O  
ATOM   1366  CB  ASP A 193       7.616   1.700  78.112  1.00 31.56           C  
ANISOU 1366  CB  ASP A 193     3940   4617   3433    621    147    -98       C  
ATOM   1367  CG  ASP A 193       6.277   2.376  78.309  1.00 50.59           C  
ANISOU 1367  CG  ASP A 193     6316   7089   5815    684    193   -135       C  
ATOM   1368  OD1 ASP A 193       6.244   3.468  78.951  1.00 52.35           O  
ANISOU 1368  OD1 ASP A 193     6573   7314   6002    757    171   -211       O  
ATOM   1369  OD2 ASP A 193       5.270   1.825  77.777  1.00 59.86           O  
ANISOU 1369  OD2 ASP A 193     7428   8310   7008    661    246    -91       O  
ATOM   1370  N   LEU A 194       7.162   4.058  75.903  1.00 24.93           N  
ANISOU 1370  N   LEU A 194     3083   3637   2751    663     79   -182       N  
ATOM   1371  CA  LEU A 194       6.529   4.582  74.669  1.00 23.84           C  
ANISOU 1371  CA  LEU A 194     2915   3462   2683    666     75   -181       C  
ATOM   1372  C   LEU A 194       7.459   4.628  73.455  1.00 24.92           C  
ANISOU 1372  C   LEU A 194     3064   3505   2899    602     28   -155       C  
ATOM   1373  O   LEU A 194       7.028   4.352  72.350  1.00 23.72           O  
ANISOU 1373  O   LEU A 194     2875   3342   2795    573     40   -118       O  
ATOM   1374  CB  LEU A 194       5.943   5.964  74.930  1.00 24.57           C  
ANISOU 1374  CB  LEU A 194     3030   3541   2765    755     55   -256       C  
ATOM   1375  CG  LEU A 194       4.872   5.967  76.034  1.00 29.96           C  
ANISOU 1375  CG  LEU A 194     3687   4331   3366    830    110   -287       C  
ATOM   1376  CD1 LEU A 194       4.378   7.399  76.372  1.00 30.67           C  
ANISOU 1376  CD1 LEU A 194     3808   4402   3441    934     83   -377       C  
ATOM   1377  CD2 LEU A 194       3.728   5.027  75.564  1.00 32.02           C  
ANISOU 1377  CD2 LEU A 194     3859   4675   3631    805    179   -228       C  
ATOM   1378  N   TRP A 195       8.732   4.981  73.665  1.00 20.89           N  
ANISOU 1378  N   TRP A 195     2604   2935   2399    579    -25   -176       N  
ATOM   1379  CA  TRP A 195       9.756   4.865  72.621  1.00 19.67           C  
ANISOU 1379  CA  TRP A 195     2454   2710   2310    510    -60   -146       C  
ATOM   1380  C   TRP A 195       9.961   3.407  72.081  1.00 22.04           C  
ANISOU 1380  C   TRP A 195     2713   3038   2624    447    -28    -76       C  
ATOM   1381  O   TRP A 195      10.225   3.196  70.904  1.00 19.19           O  
ANISOU 1381  O   TRP A 195     2334   2639   2317    402    -35    -44       O  
ATOM   1382  CB  TRP A 195      11.074   5.401  73.126  1.00 18.63           C  
ANISOU 1382  CB  TRP A 195     2370   2530   2180    494   -118   -183       C  
ATOM   1383  CG  TRP A 195      11.189   6.888  73.204  1.00 20.24           C  
ANISOU 1383  CG  TRP A 195     2624   2666   2400    527   -168   -246       C  
ATOM   1384  CD1 TRP A 195      10.943   7.670  74.284  1.00 23.80           C  
ANISOU 1384  CD1 TRP A 195     3118   3124   2803    593   -186   -313       C  
ATOM   1385  CD2 TRP A 195      11.651   7.772  72.174  1.00 20.11           C  
ANISOU 1385  CD2 TRP A 195     2631   2560   2451    492   -210   -248       C  
ATOM   1386  NE1 TRP A 195      11.214   8.983  73.995  1.00 23.68           N  
ANISOU 1386  NE1 TRP A 195     3154   3019   2826    603   -243   -359       N  
ATOM   1387  CE2 TRP A 195      11.646   9.071  72.703  1.00 24.71           C  
ANISOU 1387  CE2 TRP A 195     3273   3087   3027    537   -257   -316       C  
ATOM   1388  CE3 TRP A 195      12.072   7.585  70.862  1.00 20.99           C  
ANISOU 1388  CE3 TRP A 195     2722   2632   2623    426   -212   -199       C  
ATOM   1389  CZ2 TRP A 195      12.042  10.186  71.965  1.00 24.51           C  
ANISOU 1389  CZ2 TRP A 195     3292   2962   3060    513   -308   -330       C  
ATOM   1390  CZ3 TRP A 195      12.470   8.695  70.123  1.00 22.93           C  
ANISOU 1390  CZ3 TRP A 195     3006   2788   2919    402   -257   -210       C  
ATOM   1391  CH2 TRP A 195      12.444   9.981  70.677  1.00 24.35           C  
ANISOU 1391  CH2 TRP A 195     3250   2907   3097    442   -305   -272       C  
ATOM   1392  N   VAL A 196       9.838   2.415  72.952  1.00 20.12           N  
ANISOU 1392  N   VAL A 196     2460   2857   2328    448      4    -53       N  
ATOM   1393  CA  VAL A 196       9.853   1.032  72.515  1.00 20.02           C  
ANISOU 1393  CA  VAL A 196     2417   2864   2325    397     33     10       C  
ATOM   1394  C   VAL A 196       8.746   0.813  71.507  1.00 25.67           C  
ANISOU 1394  C   VAL A 196     3087   3593   3075    385     67     39       C  
ATOM   1395  O   VAL A 196       8.933   0.106  70.523  1.00 25.57           O  
ANISOU 1395  O   VAL A 196     3054   3557   3103    336     68     78       O  
ATOM   1396  CB  VAL A 196       9.703  -0.006  73.707  1.00 23.37           C  
ANISOU 1396  CB  VAL A 196     2847   3354   2679    401     66     38       C  
ATOM   1397  CG1 VAL A 196       9.493  -1.459  73.178  1.00 22.44           C  
ANISOU 1397  CG1 VAL A 196     2702   3247   2576    346     97    108       C  
ATOM   1398  CG2 VAL A 196      10.902   0.086  74.639  1.00 22.72           C  
ANISOU 1398  CG2 VAL A 196     2810   3260   2562    412     23     14       C  
ATOM   1399  N   VAL A 197       7.596   1.423  71.746  1.00 24.48           N  
ANISOU 1399  N   VAL A 197     2916   3480   2904    433     91     15       N  
ATOM   1400  CA  VAL A 197       6.406   1.166  70.931  1.00 24.73           C  
ANISOU 1400  CA  VAL A 197     2893   3542   2961    427    124     40       C  
ATOM   1401  C   VAL A 197       6.483   1.899  69.597  1.00 30.38           C  
ANISOU 1401  C   VAL A 197     3609   4193   3740    422     89     32       C  
ATOM   1402  O   VAL A 197       6.200   1.326  68.531  1.00 28.92           O  
ANISOU 1402  O   VAL A 197     3394   4003   3592    382     95     68       O  
ATOM   1403  CB  VAL A 197       5.130   1.585  71.667  1.00 28.72           C  
ANISOU 1403  CB  VAL A 197     3368   4124   3422    488    164     13       C  
ATOM   1404  CG1 VAL A 197       3.910   1.282  70.799  1.00 28.36           C  
ANISOU 1404  CG1 VAL A 197     3253   4116   3405    479    193     38       C  
ATOM   1405  CG2 VAL A 197       5.043   0.861  73.030  1.00 28.82           C  
ANISOU 1405  CG2 VAL A 197     3384   4208   3359    490    205     26       C  
ATOM   1406  N   VAL A 198       6.885   3.167  69.670  1.00 28.76           N  
ANISOU 1406  N   VAL A 198     3446   3937   3544    461     48    -15       N  
ATOM   1407  CA  VAL A 198       7.067   3.979  68.475  1.00 28.42           C  
ANISOU 1407  CA  VAL A 198     3419   3824   3556    455     10    -19       C  
ATOM   1408  C   VAL A 198       8.001   3.283  67.504  1.00 31.20           C  
ANISOU 1408  C   VAL A 198     3770   4138   3945    380     -1     24       C  
ATOM   1409  O   VAL A 198       7.669   3.163  66.332  1.00 31.00           O  
ANISOU 1409  O   VAL A 198     3726   4100   3954    359     -2     51       O  
ATOM   1410  CB  VAL A 198       7.561   5.414  68.803  1.00 32.54           C  
ANISOU 1410  CB  VAL A 198     4001   4281   4082    495    -39    -73       C  
ATOM   1411  CG1 VAL A 198       7.751   6.232  67.537  1.00 32.28           C  
ANISOU 1411  CG1 VAL A 198     3992   4169   4103    480    -77    -65       C  
ATOM   1412  CG2 VAL A 198       6.568   6.114  69.685  1.00 32.94           C  
ANISOU 1412  CG2 VAL A 198     4053   4369   4093    582    -28   -123       C  
ATOM   1413  N   PHE A 199       9.135   2.785  67.977  1.00 27.11           N  
ANISOU 1413  N   PHE A 199     3272   3611   3418    345    -10     30       N  
ATOM   1414  CA  PHE A 199      10.115   2.175  67.051  1.00 26.06           C  
ANISOU 1414  CA  PHE A 199     3135   3447   3320    283    -22     63       C  
ATOM   1415  C   PHE A 199       9.799   0.761  66.593  1.00 30.30           C  
ANISOU 1415  C   PHE A 199     3635   4019   3859    249     11    107       C  
ATOM   1416  O   PHE A 199      10.186   0.389  65.505  1.00 29.25           O  
ANISOU 1416  O   PHE A 199     3494   3863   3757    212      5    131       O  
ATOM   1417  CB  PHE A 199      11.557   2.290  67.564  1.00 27.31           C  
ANISOU 1417  CB  PHE A 199     3320   3578   3477    261    -53     46       C  
ATOM   1418  CG  PHE A 199      12.064   3.694  67.562  1.00 29.01           C  
ANISOU 1418  CG  PHE A 199     3574   3737   3711    269    -95      8       C  
ATOM   1419  CD1 PHE A 199      11.800   4.548  66.493  1.00 32.81           C  
ANISOU 1419  CD1 PHE A 199     4067   4171   4230    262   -109     13       C  
ATOM   1420  CD2 PHE A 199      12.769   4.189  68.636  1.00 31.18           C  
ANISOU 1420  CD2 PHE A 199     3879   4003   3965    282   -125    -32       C  
ATOM   1421  CE1 PHE A 199      12.238   5.880  66.516  1.00 34.38           C  
ANISOU 1421  CE1 PHE A 199     4311   4305   4446    264   -152    -18       C  
ATOM   1422  CE2 PHE A 199      13.217   5.492  68.658  1.00 34.30           C  
ANISOU 1422  CE2 PHE A 199     4315   4338   4381    282   -169    -69       C  
ATOM   1423  CZ  PHE A 199      12.945   6.343  67.609  1.00 32.93           C  
ANISOU 1423  CZ  PHE A 199     4157   4108   4245    271   -182    -61       C  
ATOM   1424  N   GLN A 200       9.094  -0.023  67.396  1.00 27.51           N  
ANISOU 1424  N   GLN A 200     3263   3719   3470    260     44    120       N  
ATOM   1425  CA  GLN A 200       8.729  -1.344  66.956  1.00 27.29           C  
ANISOU 1425  CA  GLN A 200     3208   3713   3447    222     70    163       C  
ATOM   1426  C   GLN A 200       7.709  -1.240  65.848  1.00 32.54           C  
ANISOU 1426  C   GLN A 200     3838   4384   4140    216     78    174       C  
ATOM   1427  O   GLN A 200       7.797  -1.985  64.869  1.00 32.50           O  
ANISOU 1427  O   GLN A 200     3822   4365   4161    177     77    199       O  
ATOM   1428  CB  GLN A 200       8.169  -2.189  68.091  1.00 28.89           C  
ANISOU 1428  CB  GLN A 200     3402   3970   3603    225    105    182       C  
ATOM   1429  CG  GLN A 200       7.851  -3.643  67.647  1.00 43.91           C  
ANISOU 1429  CG  GLN A 200     5286   5882   5516    174    126    230       C  
ATOM   1430  CD  GLN A 200       9.096  -4.472  67.286  1.00 55.58           C  
ANISOU 1430  CD  GLN A 200     6792   7314   7011    144    102    246       C  
ATOM   1431  OE1 GLN A 200       9.714  -5.087  68.147  1.00 52.34           O  
ANISOU 1431  OE1 GLN A 200     6409   6905   6572    145     99    258       O  
ATOM   1432  NE2 GLN A 200       9.433  -4.516  66.008  1.00 42.74           N  
ANISOU 1432  NE2 GLN A 200     5159   5654   5428    123     84    246       N  
ATOM   1433  N   PHE A 201       6.741  -0.327  65.995  1.00 29.79           N  
ANISOU 1433  N   PHE A 201     3475   4058   3786    261     83    150       N  
ATOM   1434  CA  PHE A 201       5.702  -0.137  64.990  1.00 29.98           C  
ANISOU 1434  CA  PHE A 201     3462   4094   3834    267     84    157       C  
ATOM   1435  C   PHE A 201       6.313   0.284  63.641  1.00 34.76           C  
ANISOU 1435  C   PHE A 201     4090   4640   4479    247     49    162       C  
ATOM   1436  O   PHE A 201       5.968  -0.289  62.605  1.00 34.36           O  
ANISOU 1436  O   PHE A 201     4017   4592   4447    217     48    185       O  
ATOM   1437  CB  PHE A 201       4.653   0.871  65.474  1.00 32.59           C  
ANISOU 1437  CB  PHE A 201     3773   4459   4149    334     90    123       C  
ATOM   1438  CG  PHE A 201       3.318   0.792  64.748  1.00 34.97           C  
ANISOU 1438  CG  PHE A 201     4016   4804   4466    345     99    131       C  
ATOM   1439  CD1 PHE A 201       2.317   1.695  65.053  1.00 39.19           C  
ANISOU 1439  CD1 PHE A 201     4525   5376   4991    416    101     98       C  
ATOM   1440  CD2 PHE A 201       3.054  -0.184  63.766  1.00 37.44           C  
ANISOU 1440  CD2 PHE A 201     4298   5123   4803    289    101    167       C  
ATOM   1441  CE1 PHE A 201       1.076   1.655  64.393  1.00 40.71           C  
ANISOU 1441  CE1 PHE A 201     4652   5616   5198    432    105    102       C  
ATOM   1442  CE2 PHE A 201       1.831  -0.230  63.108  1.00 40.91           C  
ANISOU 1442  CE2 PHE A 201     4680   5607   5257    298    103    170       C  
ATOM   1443  CZ  PHE A 201       0.840   0.695  63.414  1.00 39.59           C  
ANISOU 1443  CZ  PHE A 201     4478   5482   5081    370    104    139       C  
ATOM   1444  N   GLN A 202       7.242   1.248  63.666  1.00 32.09           N  
ANISOU 1444  N   GLN A 202     3796   4248   4147    258     19    142       N  
ATOM   1445  CA  GLN A 202       8.087   1.550  62.497  1.00 32.09           C  
ANISOU 1445  CA  GLN A 202     3822   4195   4177    224     -7    155       C  
ATOM   1446  C   GLN A 202       8.788   0.327  61.879  1.00 36.98           C  
ANISOU 1446  C   GLN A 202     4431   4818   4804    170      3    183       C  
ATOM   1447  O   GLN A 202       8.841   0.211  60.654  1.00 36.77           O  
ANISOU 1447  O   GLN A 202     4401   4776   4793    146     -5    200       O  
ATOM   1448  CB  GLN A 202       9.159   2.579  62.842  1.00 33.56           C  
ANISOU 1448  CB  GLN A 202     4055   4330   4369    226    -36    132       C  
ATOM   1449  CG  GLN A 202       9.811   3.208  61.615  1.00 50.37           C  
ANISOU 1449  CG  GLN A 202     6208   6405   6524    194    -61    148       C  
ATOM   1450  CD  GLN A 202      11.029   4.019  61.955  1.00 72.20           C  
ANISOU 1450  CD  GLN A 202     9012   9123   9299    173    -86    131       C  
ATOM   1451  OE1 GLN A 202      11.019   5.253  61.861  1.00 69.90           O  
ANISOU 1451  OE1 GLN A 202     8760   8779   9018    187   -116    118       O  
ATOM   1452  NE2 GLN A 202      12.100   3.337  62.343  1.00 62.38           N  
ANISOU 1452  NE2 GLN A 202     7756   7893   8052    139    -80    131       N  
ATOM   1453  N   HIS A 203       9.337  -0.569  62.693  1.00 34.39           N  
ANISOU 1453  N   HIS A 203     4100   4506   4461    155     17    186       N  
ATOM   1454  CA  HIS A 203      10.012  -1.752  62.132  1.00 34.83           C  
ANISOU 1454  CA  HIS A 203     4151   4559   4525    114     22    208       C  
ATOM   1455  C   HIS A 203       9.015  -2.656  61.369  1.00 36.96           C  
ANISOU 1455  C   HIS A 203     4393   4850   4801     97     36    229       C  
ATOM   1456  O   HIS A 203       9.296  -3.118  60.263  1.00 35.81           O  
ANISOU 1456  O   HIS A 203     4247   4690   4668     71     30    239       O  
ATOM   1457  CB  HIS A 203      10.811  -2.541  63.198  1.00 36.53           C  
ANISOU 1457  CB  HIS A 203     4375   4782   4722    111     27    208       C  
ATOM   1458  CG  HIS A 203      12.255  -2.137  63.282  1.00 41.21           C  
ANISOU 1458  CG  HIS A 203     4986   5350   5322    104      4    192       C  
ATOM   1459  ND1 HIS A 203      12.743  -1.281  64.257  1.00 43.99           N  
ANISOU 1459  ND1 HIS A 203     5356   5697   5663    124    -13    166       N  
ATOM   1460  CD2 HIS A 203      13.315  -2.448  62.496  1.00 43.56           C  
ANISOU 1460  CD2 HIS A 203     5279   5633   5637     79     -5    195       C  
ATOM   1461  CE1 HIS A 203      14.040  -1.094  64.073  1.00 43.61           C  
ANISOU 1461  CE1 HIS A 203     5310   5631   5629    104    -33    157       C  
ATOM   1462  NE2 HIS A 203      14.414  -1.796  63.015  1.00 43.74           N  
ANISOU 1462  NE2 HIS A 203     5311   5647   5663     79    -26    175       N  
ATOM   1463  N   ILE A 204       7.843  -2.864  61.959  1.00 32.58           N  
ANISOU 1463  N   ILE A 204     3813   4332   4234    109     55    233       N  
ATOM   1464  CA  ILE A 204       6.796  -3.658  61.347  1.00 31.91           C  
ANISOU 1464  CA  ILE A 204     3695   4272   4156     86     65    251       C  
ATOM   1465  C   ILE A 204       6.234  -2.984  60.105  1.00 35.96           C  
ANISOU 1465  C   ILE A 204     4196   4781   4688     95     45    246       C  
ATOM   1466  O   ILE A 204       5.942  -3.648  59.130  1.00 35.82           O  
ANISOU 1466  O   ILE A 204     4165   4763   4680     67     37    257       O  
ATOM   1467  CB  ILE A 204       5.628  -3.866  62.321  1.00 34.98           C  
ANISOU 1467  CB  ILE A 204     4049   4715   4527     96     93    256       C  
ATOM   1468  CG1 ILE A 204       6.071  -4.663  63.550  1.00 34.78           C  
ANISOU 1468  CG1 ILE A 204     4041   4698   4475     83    114    270       C  
ATOM   1469  CG2 ILE A 204       4.492  -4.567  61.630  1.00 36.23           C  
ANISOU 1469  CG2 ILE A 204     4163   4903   4700     65     99    272       C  
ATOM   1470  CD1 ILE A 204       5.093  -4.564  64.713  1.00 37.73           C  
ANISOU 1470  CD1 ILE A 204     4386   5132   4816    101    149    272       C  
ATOM   1471  N   MET A 205       6.066  -1.693  60.142  1.00 32.15           N  
ANISOU 1471  N   MET A 205     3720   4290   4204    136     32    229       N  
ATOM   1472  CA  MET A 205       5.581  -1.009  58.995  1.00 32.21           C  
ANISOU 1472  CA  MET A 205     3727   4288   4225    150      7    230       C  
ATOM   1473  C   MET A 205       6.495  -0.980  57.811  1.00 33.76           C  
ANISOU 1473  C   MET A 205     3955   4444   4428    122    -11    241       C  
ATOM   1474  O   MET A 205       6.191  -1.460  56.784  1.00 33.50           O  
ANISOU 1474  O   MET A 205     3912   4417   4399    103    -20    252       O  
ATOM   1475  CB  MET A 205       5.441   0.438  59.417  1.00 35.55           C  
ANISOU 1475  CB  MET A 205     4169   4692   4645    204     -8    208       C  
ATOM   1476  CG  MET A 205       4.486   1.254  58.717  1.00 40.57           C  
ANISOU 1476  CG  MET A 205     4795   5332   5289    243    -32    204       C  
ATOM   1477  SD  MET A 205       3.000   0.621  59.350  1.00 46.72           S  
ANISOU 1477  SD  MET A 205     5499   6193   6061    262     -6    197       S  
ATOM   1478  CE  MET A 205       1.768   1.578  58.553  1.00 44.02           C  
ANISOU 1478  CE  MET A 205     5131   5867   5727    323    -40    186       C  
ATOM   1479  N   VAL A 206       7.678  -0.482  58.011  1.00 28.88           N  
ANISOU 1479  N   VAL A 206     3373   3790   3811    116    -15    237       N  
ATOM   1480  CA  VAL A 206       8.668  -0.326  56.974  1.00 27.78           C  
ANISOU 1480  CA  VAL A 206     3260   3621   3675     87    -25    248       C  
ATOM   1481  C   VAL A 206       9.240  -1.638  56.536  1.00 30.26           C  
ANISOU 1481  C   VAL A 206     3564   3947   3986     52    -12    255       C  
ATOM   1482  O   VAL A 206       9.582  -1.827  55.408  1.00 29.54           O  
ANISOU 1482  O   VAL A 206     3481   3851   3890     33    -16    264       O  
ATOM   1483  CB  VAL A 206       9.699   0.724  57.367  1.00 31.40           C  
ANISOU 1483  CB  VAL A 206     3753   4041   4137     87    -35    241       C  
ATOM   1484  CG1 VAL A 206      10.900   0.698  56.520  1.00 31.22           C  
ANISOU 1484  CG1 VAL A 206     3744   4001   4115     46    -34    254       C  
ATOM   1485  CG2 VAL A 206       9.087   1.976  57.249  1.00 31.21           C  
ANISOU 1485  CG2 VAL A 206     3751   3991   4117    119    -58    239       C  
ATOM   1486  N   GLY A 207       9.385  -2.484  57.527  1.00 25.55           N  
ANISOU 1486  N   GLY A 207     2956   3363   3388     49      3    249       N  
ATOM   1487  CA  GLY A 207       9.813  -3.834  57.426  1.00 24.48           C  
ANISOU 1487  CA  GLY A 207     2817   3234   3252     25     13    253       C  
ATOM   1488  C   GLY A 207       8.910  -4.812  56.788  1.00 28.03           C  
ANISOU 1488  C   GLY A 207     3251   3697   3703      9     12    260       C  
ATOM   1489  O   GLY A 207       9.360  -5.700  56.177  1.00 27.80           O  
ANISOU 1489  O   GLY A 207     3230   3659   3673     -9     10    258       O  
ATOM   1490  N   LEU A 208       7.626  -4.698  57.013  1.00 24.37           N  
ANISOU 1490  N   LEU A 208     2762   3257   3242     15     12    264       N  
ATOM   1491  CA  LEU A 208       6.733  -5.679  56.497  1.00 23.94           C  
ANISOU 1491  CA  LEU A 208     2686   3217   3192    -10      8    269       C  
ATOM   1492  C   LEU A 208       5.527  -5.243  55.697  1.00 28.95           C  
ANISOU 1492  C   LEU A 208     3292   3877   3831     -4     -9    268       C  
ATOM   1493  O   LEU A 208       5.213  -5.784  54.702  1.00 28.81           O  
ANISOU 1493  O   LEU A 208     3271   3861   3814    -24    -27    267       O  
ATOM   1494  CB  LEU A 208       6.392  -6.578  57.649  1.00 23.85           C  
ANISOU 1494  CB  LEU A 208     2664   3217   3181    -27     28    279       C  
ATOM   1495  CG  LEU A 208       5.611  -7.774  57.358  1.00 28.30           C  
ANISOU 1495  CG  LEU A 208     3212   3787   3754    -69     25    289       C  
ATOM   1496  CD1 LEU A 208       6.364  -8.521  56.474  1.00 27.69           C  
ANISOU 1496  CD1 LEU A 208     3166   3675   3679    -84      8    280       C  
ATOM   1497  CD2 LEU A 208       5.443  -8.441  58.600  1.00 30.90           C  
ANISOU 1497  CD2 LEU A 208     3540   4124   4078    -85     48    306       C  
ATOM   1498  N   ILE A 209       4.806  -4.291  56.180  1.00 25.74           N  
ANISOU 1498  N   ILE A 209     2863   3493   3424     29     -8    266       N  
ATOM   1499  CA  ILE A 209       3.447  -3.974  55.821  1.00 25.82           C  
ANISOU 1499  CA  ILE A 209     2829   3543   3440     44    -22    263       C  
ATOM   1500  C   ILE A 209       3.417  -3.052  54.673  1.00 29.69           C  
ANISOU 1500  C   ILE A 209     3337   4019   3926     70    -55    261       C  
ATOM   1501  O   ILE A 209       2.570  -3.138  53.883  1.00 30.75           O  
ANISOU 1501  O   ILE A 209     3447   4176   4061     71    -78    260       O  
ATOM   1502  CB  ILE A 209       2.734  -3.204  56.847  1.00 29.05           C  
ANISOU 1502  CB  ILE A 209     3207   3984   3847     85     -8    256       C  
ATOM   1503  CG1 ILE A 209       2.801  -4.002  58.121  1.00 29.45           C  
ANISOU 1503  CG1 ILE A 209     3246   4053   3892     61     29    262       C  
ATOM   1504  CG2 ILE A 209       1.364  -2.921  56.393  1.00 29.45           C  
ANISOU 1504  CG2 ILE A 209     3203   4082   3904    106    -25    250       C  
ATOM   1505  CD1 ILE A 209       1.616  -4.071  58.826  1.00 36.31           C  
ANISOU 1505  CD1 ILE A 209     4056   4982   4757     68     50    262       C  
ATOM   1506  N   LEU A 210       4.394  -2.210  54.541  1.00 24.58           N  
ANISOU 1506  N   LEU A 210     2737   3331   3271     87    -58    264       N  
ATOM   1507  CA  LEU A 210       4.474  -1.381  53.348  1.00 24.20           C  
ANISOU 1507  CA  LEU A 210     2718   3263   3213    103    -88    272       C  
ATOM   1508  C   LEU A 210       5.103  -2.236  52.207  1.00 27.05           C  
ANISOU 1508  C   LEU A 210     3099   3617   3560     62    -93    278       C  
ATOM   1509  O   LEU A 210       4.548  -2.301  51.123  1.00 27.35           O  
ANISOU 1509  O   LEU A 210     3136   3669   3587     63   -119    281       O  
ATOM   1510  CB  LEU A 210       5.215  -0.060  53.601  1.00 24.23           C  
ANISOU 1510  CB  LEU A 210     2767   3223   3215    128    -93    276       C  
ATOM   1511  CG  LEU A 210       4.541   0.882  54.624  1.00 28.92           C  
ANISOU 1511  CG  LEU A 210     3350   3820   3818    181    -96    261       C  
ATOM   1512  CD1 LEU A 210       5.283   2.208  54.790  1.00 29.56           C  
ANISOU 1512  CD1 LEU A 210     3488   3844   3901    201   -110    262       C  
ATOM   1513  CD2 LEU A 210       3.122   1.168  54.201  1.00 31.26           C  
ANISOU 1513  CD2 LEU A 210     3610   4152   4117    223   -122    256       C  
ATOM   1514  N   PRO A 211       6.230  -2.918  52.446  1.00 22.16           N  
ANISOU 1514  N   PRO A 211     2498   2981   2939     33    -69    276       N  
ATOM   1515  CA  PRO A 211       6.723  -3.733  51.338  1.00 22.02           C  
ANISOU 1515  CA  PRO A 211     2497   2963   2905      6    -74    273       C  
ATOM   1516  C   PRO A 211       5.778  -4.879  50.980  1.00 25.90           C  
ANISOU 1516  C   PRO A 211     2962   3478   3402    -13    -88    262       C  
ATOM   1517  O   PRO A 211       5.620  -5.230  49.799  1.00 25.20           O  
ANISOU 1517  O   PRO A 211     2884   3396   3294    -22   -110    256       O  
ATOM   1518  CB  PRO A 211       8.071  -4.269  51.853  1.00 23.38           C  
ANISOU 1518  CB  PRO A 211     2685   3118   3079    -10    -46    267       C  
ATOM   1519  CG  PRO A 211       8.140  -3.902  53.296  1.00 26.96           C  
ANISOU 1519  CG  PRO A 211     3128   3565   3551      2    -31    268       C  
ATOM   1520  CD  PRO A 211       7.239  -2.752  53.499  1.00 22.90           C  
ANISOU 1520  CD  PRO A 211     2606   3055   3041     32    -45    273       C  
ATOM   1521  N   GLY A 212       5.138  -5.436  51.996  1.00 22.76           N  
ANISOU 1521  N   GLY A 212     2530   3091   3025    -23    -78    259       N  
ATOM   1522  CA  GLY A 212       4.132  -6.475  51.784  1.00 22.65           C  
ANISOU 1522  CA  GLY A 212     2486   3098   3022    -53    -93    252       C  
ATOM   1523  C   GLY A 212       3.016  -5.989  50.905  1.00 26.37           C  
ANISOU 1523  C   GLY A 212     2930   3602   3488    -39   -128    249       C  
ATOM   1524  O   GLY A 212       2.597  -6.691  50.016  1.00 26.56           O  
ANISOU 1524  O   GLY A 212     2951   3634   3508    -63   -155    237       O  
ATOM   1525  N   ILE A 213       2.528  -4.780  51.151  1.00 23.21           N  
ANISOU 1525  N   ILE A 213     2513   3217   3089      3   -133    256       N  
ATOM   1526  CA  ILE A 213       1.420  -4.241  50.358  1.00 23.43           C  
ANISOU 1526  CA  ILE A 213     2512   3279   3112     28   -173    253       C  
ATOM   1527  C   ILE A 213       1.816  -4.101  48.882  1.00 26.88           C  
ANISOU 1527  C   ILE A 213     2994   3700   3517     31   -205    255       C  
ATOM   1528  O   ILE A 213       1.022  -4.411  47.966  1.00 27.10           O  
ANISOU 1528  O   ILE A 213     3005   3756   3536     26   -245    246       O  
ATOM   1529  CB  ILE A 213       0.926  -2.899  50.934  1.00 26.59           C  
ANISOU 1529  CB  ILE A 213     2897   3690   3518     88   -175    258       C  
ATOM   1530  CG1 ILE A 213       0.166  -3.157  52.244  1.00 26.77           C  
ANISOU 1530  CG1 ILE A 213     2856   3752   3563     88   -147    250       C  
ATOM   1531  CG2 ILE A 213       0.025  -2.130  49.915  1.00 27.38           C  
ANISOU 1531  CG2 ILE A 213     2985   3812   3606    130   -227    258       C  
ATOM   1532  CD1 ILE A 213      -0.056  -1.892  53.104  1.00 31.34           C  
ANISOU 1532  CD1 ILE A 213     3428   4334   4143    152   -138    246       C  
ATOM   1533  N   VAL A 214       3.056  -3.672  48.667  1.00 22.06           N  
ANISOU 1533  N   VAL A 214     2441   3053   2888     34   -187    267       N  
ATOM   1534  CA  VAL A 214       3.527  -3.347  47.343  1.00 21.67           C  
ANISOU 1534  CA  VAL A 214     2438   2995   2800     39   -207    276       C  
ATOM   1535  C   VAL A 214       3.643  -4.613  46.553  1.00 25.00           C  
ANISOU 1535  C   VAL A 214     2867   3428   3206      4   -217    255       C  
ATOM   1536  O   VAL A 214       3.107  -4.699  45.453  1.00 25.32           O  
ANISOU 1536  O   VAL A 214     2913   3489   3219      8   -255    249       O  
ATOM   1537  CB  VAL A 214       4.868  -2.588  47.390  1.00 25.69           C  
ANISOU 1537  CB  VAL A 214     2998   3469   3294     41   -179    295       C  
ATOM   1538  CG1 VAL A 214       5.505  -2.489  46.013  1.00 25.72           C  
ANISOU 1538  CG1 VAL A 214     3049   3473   3250     32   -186    307       C  
ATOM   1539  CG2 VAL A 214       4.656  -1.173  47.951  1.00 25.77           C  
ANISOU 1539  CG2 VAL A 214     3017   3458   3316     78   -185    314       C  
ATOM   1540  N   ILE A 215       4.349  -5.583  47.131  1.00 20.39           N  
ANISOU 1540  N   ILE A 215     2285   2827   2636    -25   -186    241       N  
ATOM   1541  CA  ILE A 215       4.550  -6.892  46.541  1.00 19.58           C  
ANISOU 1541  CA  ILE A 215     2195   2721   2523    -54   -194    214       C  
ATOM   1542  C   ILE A 215       3.231  -7.538  46.216  1.00 25.16           C  
ANISOU 1542  C   ILE A 215     2866   3451   3242    -73   -236    197       C  
ATOM   1543  O   ILE A 215       3.031  -7.947  45.089  1.00 25.90           O  
ANISOU 1543  O   ILE A 215     2978   3555   3307    -79   -269    178       O  
ATOM   1544  CB  ILE A 215       5.411  -7.849  47.493  1.00 21.55           C  
ANISOU 1544  CB  ILE A 215     2451   2940   2796    -74   -159    204       C  
ATOM   1545  CG1 ILE A 215       6.893  -7.404  47.501  1.00 20.83           C  
ANISOU 1545  CG1 ILE A 215     2393   2836   2687    -58   -124    211       C  
ATOM   1546  CG2 ILE A 215       5.285  -9.360  47.081  1.00 20.54           C  
ANISOU 1546  CG2 ILE A 215     2335   2798   2671   -105   -178    173       C  
ATOM   1547  CD1 ILE A 215       7.676  -7.813  48.753  1.00 21.42           C  
ANISOU 1547  CD1 ILE A 215     2463   2886   2788    -62    -92    211       C  
ATOM   1548  N   LEU A 216       2.329  -7.645  47.188  1.00 22.78           N  
ANISOU 1548  N   LEU A 216     2512   3163   2979    -86   -233    202       N  
ATOM   1549  CA  LEU A 216       1.021  -8.284  46.943  1.00 23.45           C  
ANISOU 1549  CA  LEU A 216     2550   3279   3083   -116   -272    187       C  
ATOM   1550  C   LEU A 216       0.154  -7.520  45.929  1.00 28.00           C  
ANISOU 1550  C   LEU A 216     3107   3894   3636    -85   -321    185       C  
ATOM   1551  O   LEU A 216      -0.572  -8.155  45.169  1.00 28.32           O  
ANISOU 1551  O   LEU A 216     3131   3956   3673   -109   -366    162       O  
ATOM   1552  CB  LEU A 216       0.230  -8.495  48.227  1.00 23.91           C  
ANISOU 1552  CB  LEU A 216     2546   3356   3183   -138   -251    197       C  
ATOM   1553  CG  LEU A 216       0.855  -9.405  49.297  1.00 28.97           C  
ANISOU 1553  CG  LEU A 216     3203   3960   3845   -175   -211    204       C  
ATOM   1554  CD1 LEU A 216       0.138  -9.168  50.651  1.00 29.48           C  
ANISOU 1554  CD1 LEU A 216     3209   4057   3937   -181   -179    224       C  
ATOM   1555  CD2 LEU A 216       0.838 -10.900  48.884  1.00 30.54           C  
ANISOU 1555  CD2 LEU A 216     3424   4127   4053   -232   -233    183       C  
ATOM   1556  N   SER A 217       0.236  -6.185  45.897  1.00 24.25           N  
ANISOU 1556  N   SER A 217     2642   3427   3147    -32   -319    207       N  
ATOM   1557  CA  SER A 217      -0.509  -5.421  44.891  1.00 24.34           C  
ANISOU 1557  CA  SER A 217     2649   3470   3132      6   -372    210       C  
ATOM   1558  C   SER A 217       0.013  -5.730  43.503  1.00 28.87           C  
ANISOU 1558  C   SER A 217     3281   4035   3653      0   -398    200       C  
ATOM   1559  O   SER A 217      -0.774  -5.839  42.561  1.00 28.28           O  
ANISOU 1559  O   SER A 217     3196   3992   3556      6   -454    186       O  
ATOM   1560  CB  SER A 217      -0.451  -3.912  45.134  1.00 26.89           C  
ANISOU 1560  CB  SER A 217     2985   3785   3448     66   -368    238       C  
ATOM   1561  OG  SER A 217      -0.773  -3.610  46.479  1.00 34.11           O  
ANISOU 1561  OG  SER A 217     3852   4704   4402     78   -336    241       O  
ATOM   1562  N   CYS A 218       1.339  -5.866  43.384  1.00 26.37           N  
ANISOU 1562  N   CYS A 218     3024   3684   3313     -8   -359    205       N  
ATOM   1563  CA  CYS A 218       1.971  -6.124  42.090  1.00 26.62           C  
ANISOU 1563  CA  CYS A 218     3113   3715   3285     -9   -373    195       C  
ATOM   1564  C   CYS A 218       1.501  -7.480  41.633  1.00 31.84           C  
ANISOU 1564  C   CYS A 218     3763   4386   3949    -44   -405    151       C  
ATOM   1565  O   CYS A 218       1.008  -7.622  40.538  1.00 31.63           O  
ANISOU 1565  O   CYS A 218     3749   4385   3883    -39   -455    134       O  
ATOM   1566  CB  CYS A 218       3.488  -6.091  42.175  1.00 26.69           C  
ANISOU 1566  CB  CYS A 218     3171   3697   3275    -12   -317    205       C  
ATOM   1567  SG  CYS A 218       4.192  -4.432  42.346  1.00 30.65           S  
ANISOU 1567  SG  CYS A 218     3703   4181   3760     18   -288    258       S  
ATOM   1568  N   TYR A 219       1.604  -8.472  42.504  1.00 29.89           N  
ANISOU 1568  N   TYR A 219     3495   4115   3746    -82   -383    133       N  
ATOM   1569  CA  TYR A 219       1.180  -9.817  42.147  1.00 30.65           C  
ANISOU 1569  CA  TYR A 219     3589   4205   3851   -124   -417     91       C  
ATOM   1570  C   TYR A 219      -0.364  -9.939  42.014  1.00 37.90           C  
ANISOU 1570  C   TYR A 219     4443   5161   4794   -146   -474     81       C  
ATOM   1571  O   TYR A 219      -0.837 -10.805  41.301  1.00 39.10           O  
ANISOU 1571  O   TYR A 219     4599   5317   4938   -176   -522     44       O  
ATOM   1572  CB  TYR A 219       1.803 -10.848  43.104  1.00 30.91           C  
ANISOU 1572  CB  TYR A 219     3630   4190   3923   -158   -379     81       C  
ATOM   1573  CG  TYR A 219       3.291 -11.094  42.831  1.00 31.37           C  
ANISOU 1573  CG  TYR A 219     3751   4219   3948   -137   -342     71       C  
ATOM   1574  CD1 TYR A 219       4.270 -10.472  43.570  1.00 32.35           C  
ANISOU 1574  CD1 TYR A 219     3882   4332   4078   -115   -288     99       C  
ATOM   1575  CD2 TYR A 219       3.704 -11.941  41.813  1.00 32.31           C  
ANISOU 1575  CD2 TYR A 219     3918   4328   4029   -136   -365     27       C  
ATOM   1576  CE1 TYR A 219       5.624 -10.679  43.304  1.00 31.75           C  
ANISOU 1576  CE1 TYR A 219     3848   4241   3972    -95   -255     88       C  
ATOM   1577  CE2 TYR A 219       5.035 -12.149  41.548  1.00 32.66           C  
ANISOU 1577  CE2 TYR A 219     4009   4359   4041   -109   -329     13       C  
ATOM   1578  CZ  TYR A 219       6.000 -11.516  42.299  1.00 37.70           C  
ANISOU 1578  CZ  TYR A 219     4644   4993   4688    -90   -272     45       C  
ATOM   1579  OH  TYR A 219       7.354 -11.741  42.045  1.00 37.00           O  
ANISOU 1579  OH  TYR A 219     4589   4902   4570    -63   -235     29       O  
ATOM   1580  N   CYS A 220      -1.148  -9.068  42.646  1.00 35.77           N  
ANISOU 1580  N   CYS A 220     4115   4925   4553   -127   -473    108       N  
ATOM   1581  CA  CYS A 220      -2.596  -9.043  42.378  1.00 37.42           C  
ANISOU 1581  CA  CYS A 220     4254   5186   4779   -136   -530     96       C  
ATOM   1582  C   CYS A 220      -2.853  -8.642  40.928  1.00 41.28           C  
ANISOU 1582  C   CYS A 220     4773   5703   5210   -102   -592     83       C  
ATOM   1583  O   CYS A 220      -3.660  -9.251  40.243  1.00 41.81           O  
ANISOU 1583  O   CYS A 220     4816   5798   5273   -128   -653     50       O  
ATOM   1584  CB  CYS A 220      -3.342  -8.064  43.310  1.00 38.72           C  
ANISOU 1584  CB  CYS A 220     4346   5387   4977   -105   -515    124       C  
ATOM   1585  SG  CYS A 220      -5.058  -7.541  42.761  1.00 44.29           S  
ANISOU 1585  SG  CYS A 220     4962   6177   5690    -78   -592    112       S  
ATOM   1586  N   ILE A 221      -2.167  -7.604  40.471  1.00 36.74           N  
ANISOU 1586  N   ILE A 221     4252   5121   4587    -46   -579    111       N  
ATOM   1587  CA  ILE A 221      -2.297  -7.155  39.100  1.00 36.25           C  
ANISOU 1587  CA  ILE A 221     4231   5084   4458    -11   -633    108       C  
ATOM   1588  C   ILE A 221      -1.752  -8.212  38.119  1.00 40.88           C  
ANISOU 1588  C   ILE A 221     4875   5659   4998    -39   -649     68       C  
ATOM   1589  O   ILE A 221      -2.322  -8.406  37.042  1.00 41.79           O  
ANISOU 1589  O   ILE A 221     5001   5806   5071    -34   -715     42       O  
ATOM   1590  CB  ILE A 221      -1.621  -5.793  38.882  1.00 38.18           C  
ANISOU 1590  CB  ILE A 221     4530   5316   4662     46   -609    157       C  
ATOM   1591  CG1 ILE A 221      -2.314  -4.724  39.745  1.00 37.98           C  
ANISOU 1591  CG1 ILE A 221     4452   5300   4679     86   -609    186       C  
ATOM   1592  CG2 ILE A 221      -1.673  -5.415  37.403  1.00 38.63           C  
ANISOU 1592  CG2 ILE A 221     4643   5398   4638     78   -662    160       C  
ATOM   1593  CD1 ILE A 221      -1.374  -3.671  40.332  1.00 41.34           C  
ANISOU 1593  CD1 ILE A 221     4921   5682   5104    114   -554    229       C  
ATOM   1594  N   ILE A 222      -0.687  -8.917  38.489  1.00 35.95           N  
ANISOU 1594  N   ILE A 222     4289   4991   4380    -65   -595     57       N  
ATOM   1595  CA  ILE A 222      -0.098  -9.894  37.573  1.00 35.45           C  
ANISOU 1595  CA  ILE A 222     4284   4916   4269    -79   -608     12       C  
ATOM   1596  C   ILE A 222      -1.069 -11.055  37.329  1.00 42.42           C  
ANISOU 1596  C   ILE A 222     5137   5801   5178   -127   -672    -40       C  
ATOM   1597  O   ILE A 222      -1.612 -11.174  36.226  1.00 43.22           O  
ANISOU 1597  O   ILE A 222     5254   5936   5233   -120   -738    -69       O  
ATOM   1598  CB  ILE A 222       1.248 -10.426  38.060  1.00 37.00           C  
ANISOU 1598  CB  ILE A 222     4521   5066   4471    -87   -540      7       C  
ATOM   1599  CG1 ILE A 222       2.325  -9.342  37.959  1.00 35.79           C  
ANISOU 1599  CG1 ILE A 222     4404   4917   4275    -47   -485     50       C  
ATOM   1600  CG2 ILE A 222       1.657 -11.640  37.236  1.00 38.48           C  
ANISOU 1600  CG2 ILE A 222     4761   5239   4622    -99   -562    -53       C  
ATOM   1601  CD1 ILE A 222       3.625  -9.685  38.696  1.00 34.77           C  
ANISOU 1601  CD1 ILE A 222     4293   4752   4165    -52   -415     52       C  
ATOM   1602  N   ILE A 223      -1.323 -11.884  38.348  1.00 39.69           N  
ANISOU 1602  N   ILE A 223     4752   5423   4904   -179   -658    -50       N  
ATOM   1603  CA  ILE A 223      -2.179 -13.074  38.171  1.00 40.15           C  
ANISOU 1603  CA  ILE A 223     4788   5474   4994   -241   -717    -98       C  
ATOM   1604  C   ILE A 223      -3.573 -12.746  37.640  1.00 44.85           C  
ANISOU 1604  C   ILE A 223     5319   6131   5590   -247   -792   -106       C  
ATOM   1605  O   ILE A 223      -4.213 -13.611  37.024  1.00 45.40           O  
ANISOU 1605  O   ILE A 223     5385   6205   5661   -290   -859   -155       O  
ATOM   1606  CB  ILE A 223      -2.296 -13.984  39.448  1.00 43.00           C  
ANISOU 1606  CB  ILE A 223     5116   5787   5435   -306   -686    -94       C  
ATOM   1607  CG1 ILE A 223      -2.803 -13.231  40.668  1.00 42.78           C  
ANISOU 1607  CG1 ILE A 223     5010   5786   5459   -308   -645    -42       C  
ATOM   1608  CG2 ILE A 223      -0.964 -14.656  39.755  1.00 43.93           C  
ANISOU 1608  CG2 ILE A 223     5308   5837   5548   -301   -636   -104       C  
ATOM   1609  CD1 ILE A 223      -2.279 -13.799  41.995  1.00 46.68           C  
ANISOU 1609  CD1 ILE A 223     5506   6228   6004   -343   -583    -21       C  
ATOM   1610  N   SER A 224      -4.041 -11.514  37.851  1.00 40.61           N  
ANISOU 1610  N   SER A 224     4734   5641   5053   -203   -788    -64       N  
ATOM   1611  CA  SER A 224      -5.321 -11.109  37.279  1.00 40.88           C  
ANISOU 1611  CA  SER A 224     4707   5743   5084   -192   -864    -73       C  
ATOM   1612  C   SER A 224      -5.197 -10.838  35.791  1.00 46.17           C  
ANISOU 1612  C   SER A 224     5441   6437   5666   -148   -922    -93       C  
ATOM   1613  O   SER A 224      -6.194 -10.810  35.090  1.00 46.72           O  
ANISOU 1613  O   SER A 224     5473   6557   5720   -145  -1003   -117       O  
ATOM   1614  CB  SER A 224      -5.887  -9.871  37.975  1.00 43.45           C  
ANISOU 1614  CB  SER A 224     4963   6109   5437   -146   -846    -26       C  
ATOM   1615  OG  SER A 224      -5.305  -8.679  37.472  1.00 50.97           O  
ANISOU 1615  OG  SER A 224     5973   7063   6329    -68   -836      9       O  
ATOM   1616  N   LYS A 225      -3.979 -10.616  35.309  1.00 43.13           N  
ANISOU 1616  N   LYS A 225     5148   6022   5217   -112   -881    -83       N  
ATOM   1617  CA  LYS A 225      -3.765 -10.244  33.905  1.00 43.69           C  
ANISOU 1617  CA  LYS A 225     5287   6122   5190    -65   -925    -92       C  
ATOM   1618  C   LYS A 225      -2.766 -11.153  33.187  1.00 48.12           C  
ANISOU 1618  C   LYS A 225     5936   6654   5695    -75   -911   -137       C  
ATOM   1619  O   LYS A 225      -2.466 -10.940  32.020  1.00 48.10           O  
ANISOU 1619  O   LYS A 225     5997   6678   5600    -38   -937   -148       O  
ATOM   1620  CB  LYS A 225      -3.333  -8.763  33.814  1.00 45.83           C  
ANISOU 1620  CB  LYS A 225     5588   6407   5420      2   -892    -26       C  
ATOM   1621  CG  LYS A 225      -4.467  -7.768  34.167  1.00 56.94           C  
ANISOU 1621  CG  LYS A 225     6921   7852   6862     36   -931      7       C  
ATOM   1622  CD  LYS A 225      -3.974  -6.321  34.437  1.00 65.06           C  
ANISOU 1622  CD  LYS A 225     7980   8867   7873     96   -888     76       C  
ATOM   1623  CE  LYS A 225      -3.603  -5.575  33.130  1.00 76.20           C  
ANISOU 1623  CE  LYS A 225     9480  10294   9180    146   -918    103       C  
ATOM   1624  NZ  LYS A 225      -3.118  -4.160  33.328  1.00 82.33           N  
ANISOU 1624  NZ  LYS A 225    10297  11046   9938    196   -883    175       N  
ATOM   1625  N   LEU A 226      -2.272 -12.184  33.860  1.00 45.12           N  
ANISOU 1625  N   LEU A 226     5560   6220   5363   -120   -873   -165       N  
ATOM   1626  CA  LEU A 226      -1.232 -13.022  33.279  1.00 45.49           C  
ANISOU 1626  CA  LEU A 226     5689   6236   5360   -116   -854   -211       C  
ATOM   1627  C   LEU A 226      -1.695 -13.637  31.944  1.00 52.40           C  
ANISOU 1627  C   LEU A 226     6604   7136   6168   -115   -939   -276       C  
ATOM   1628  O   LEU A 226      -0.937 -13.672  30.982  1.00 52.88           O  
ANISOU 1628  O   LEU A 226     6741   7213   6139    -75   -932   -299       O  
ATOM   1629  CB  LEU A 226      -0.789 -14.106  34.277  1.00 45.01           C  
ANISOU 1629  CB  LEU A 226     5624   6104   5372   -163   -815   -233       C  
ATOM   1630  CG  LEU A 226       0.296 -15.105  33.818  1.00 49.84           C  
ANISOU 1630  CG  LEU A 226     6317   6674   5944   -152   -796   -289       C  
ATOM   1631  CD1 LEU A 226       1.550 -14.412  33.257  1.00 49.62           C  
ANISOU 1631  CD1 LEU A 226     6345   6675   5833    -87   -734   -269       C  
ATOM   1632  CD2 LEU A 226       0.672 -16.061  34.954  1.00 51.25           C  
ANISOU 1632  CD2 LEU A 226     6492   6778   6203   -192   -761   -298       C  
ATOM   1633  N   SER A 227      -2.949 -14.088  31.891  1.00 50.07           N  
ANISOU 1633  N   SER A 227     6256   6854   5914   -160  -1020   -307       N  
ATOM   1634  CA  SER A 227      -3.488 -14.797  30.724  1.00 50.75           C  
ANISOU 1634  CA  SER A 227     6375   6960   5948   -170  -1114   -379       C  
ATOM   1635  C   SER A 227      -3.754 -13.909  29.510  1.00 55.40           C  
ANISOU 1635  C   SER A 227     6991   7622   6435   -109  -1163   -369       C  
ATOM   1636  O   SER A 227      -3.727 -14.400  28.391  1.00 56.13           O  
ANISOU 1636  O   SER A 227     7145   7733   6450    -96  -1219   -427       O  
ATOM   1637  CB  SER A 227      -4.779 -15.526  31.101  1.00 54.21           C  
ANISOU 1637  CB  SER A 227     6735   7392   6468   -247  -1187   -411       C  
ATOM   1638  OG  SER A 227      -4.551 -16.421  32.175  1.00 61.52           O  
ANISOU 1638  OG  SER A 227     7647   8245   7481   -310  -1146   -417       O  
ATOM   1639  N   HIS A 228      -4.024 -12.624  29.717  1.00 51.52           N  
ANISOU 1639  N   HIS A 228     6462   7171   5941    -70  -1147   -297       N  
ATOM   1640  CA  HIS A 228      -4.249 -11.699  28.602  1.00 52.02           C  
ANISOU 1640  CA  HIS A 228     6562   7297   5905     -8  -1194   -275       C  
ATOM   1641  C   HIS A 228      -3.114 -10.682  28.450  1.00 55.12           C  
ANISOU 1641  C   HIS A 228     7019   7691   6231     47  -1112   -209       C  
ATOM   1642  O   HIS A 228      -3.342  -9.520  28.108  1.00 54.43           O  
ANISOU 1642  O   HIS A 228     6939   7639   6101     95  -1126   -152       O  
ATOM   1643  CB  HIS A 228      -5.595 -10.981  28.754  1.00 53.33           C  
ANISOU 1643  CB  HIS A 228     6640   7511   6110      1  -1264   -248       C  
ATOM   1644  CG  HIS A 228      -6.770 -11.907  28.782  1.00 57.65           C  
ANISOU 1644  CG  HIS A 228     7115   8073   6716    -58  -1352   -311       C  
ATOM   1645  ND1 HIS A 228      -7.936 -11.610  29.455  1.00 59.70           N  
ANISOU 1645  ND1 HIS A 228     7260   8365   7058    -78  -1388   -296       N  
ATOM   1646  CD2 HIS A 228      -6.950 -13.135  28.239  1.00 60.16           C  
ANISOU 1646  CD2 HIS A 228     7456   8377   7024   -107  -1410   -392       C  
ATOM   1647  CE1 HIS A 228      -8.788 -12.610  29.313  1.00 59.94           C  
ANISOU 1647  CE1 HIS A 228     7241   8407   7128   -144  -1463   -360       C  
ATOM   1648  NE2 HIS A 228      -8.213 -13.550  28.583  1.00 60.57           N  
ANISOU 1648  NE2 HIS A 228     7407   8451   7155   -165  -1481   -419       N  
ATOM   1649  N   SER A 229      -1.888 -11.139  28.672  1.00 51.52           N  
ANISOU 1649  N   SER A 229     6611   7197   5766     40  -1030   -219       N  
ATOM   1650  CA  SER A 229      -0.717 -10.295  28.522  1.00 51.20           C  
ANISOU 1650  CA  SER A 229     6626   7162   5665     79   -947   -162       C  
ATOM   1651  C   SER A 229       0.192 -10.811  27.414  1.00 56.01           C  
ANISOU 1651  C   SER A 229     7323   7794   6163    102   -931   -204       C  
ATOM   1652  O   SER A 229      -0.080 -11.854  26.816  1.00 56.15           O  
ANISOU 1652  O   SER A 229     7364   7816   6156     92   -987   -284       O  
ATOM   1653  CB  SER A 229       0.030 -10.221  29.843  1.00 53.91           C  
ANISOU 1653  CB  SER A 229     6936   7452   6093     58   -855   -128       C  
ATOM   1654  OG  SER A 229      -0.628  -9.302  30.696  1.00 64.08           O  
ANISOU 1654  OG  SER A 229     8162   8736   7451     59   -856    -70       O  
ATOM   1655  N   GLY A 900       1.252 -10.057  27.133  1.00 45.01           N  
ANISOU 1655  N   GLY A 900     5535   5672   5897   -368    299   -198       N  
ATOM   1656  CA  GLY A 900       2.208 -10.415  26.106  1.00 44.83           C  
ANISOU 1656  CA  GLY A 900     5512   5648   5874   -367    298   -197       C  
ATOM   1657  C   GLY A 900       2.241  -9.406  24.978  1.00 49.07           C  
ANISOU 1657  C   GLY A 900     6048   6185   6412   -366    298   -198       C  
ATOM   1658  O   GLY A 900       3.273  -9.261  24.314  1.00 49.24           O  
ANISOU 1658  O   GLY A 900     6069   6206   6433   -366    297   -197       O  
ATOM   1659  N   SER A 901       1.122  -8.709  24.755  1.00 44.89           N  
ANISOU 1659  N   SER A 901     5518   5655   5884   -367    299   -199       N  
ATOM   1660  CA  SER A 901       1.048  -7.730  23.680  1.00 44.60           C  
ANISOU 1660  CA  SER A 901     5479   5617   5849   -367    298   -199       C  
ATOM   1661  C   SER A 901      -0.143  -6.762  23.746  1.00 50.24           C  
ANISOU 1661  C   SER A 901     6193   6331   6566   -368    298   -200       C  
ATOM   1662  O   SER A 901      -1.227  -7.094  24.210  1.00 50.15           O  
ANISOU 1662  O   SER A 901     6181   6319   6554   -368    299   -200       O  
ATOM   1663  CB  SER A 901       1.030  -8.444  22.331  1.00 46.77           C  
ANISOU 1663  CB  SER A 901     5755   5891   6124   -368    297   -198       C  
ATOM   1664  OG  SER A 901       1.162  -7.528  21.276  1.00 52.21           O  
ANISOU 1664  OG  SER A 901     6443   6581   6816   -369    296   -198       O  
ATOM   1665  N   ASN A1002       0.121  -5.559  23.249  1.00 48.16           N  
ANISOU 1665  N   ASN A1002     7150   6397   4750   -779  -1383    265       N  
ATOM   1666  CA  ASN A1002      -0.826  -4.466  23.064  1.00 47.63           C  
ANISOU 1666  CA  ASN A1002     7108   6392   4598   -724  -1234    106       C  
ATOM   1667  C   ASN A1002      -1.437  -4.570  21.659  1.00 50.26           C  
ANISOU 1667  C   ASN A1002     7341   6715   5042   -546  -1148     36       C  
ATOM   1668  O   ASN A1002      -0.922  -5.309  20.815  1.00 48.99           O  
ANISOU 1668  O   ASN A1002     7110   6495   5011   -471  -1193     97       O  
ATOM   1669  CB  ASN A1002      -0.001  -3.163  23.157  1.00 48.87           C  
ANISOU 1669  CB  ASN A1002     7301   6521   4746   -714  -1244     87       C  
ATOM   1670  CG  ASN A1002      -0.795  -1.979  23.632  1.00 75.75           C  
ANISOU 1670  CG  ASN A1002    10773   9979   8029   -745  -1115    -54       C  
ATOM   1671  OD1 ASN A1002      -1.425  -1.265  22.832  1.00 68.56           O  
ANISOU 1671  OD1 ASN A1002     9811   9068   7171   -610  -1005   -159       O  
ATOM   1672  ND2 ASN A1002      -0.722  -1.711  24.945  1.00 70.35           N  
ANISOU 1672  ND2 ASN A1002    10210   9331   7188   -935  -1127    -54       N  
ATOM   1673  N   ILE A1003      -2.494  -3.799  21.393  1.00 46.79           N  
ANISOU 1673  N   ILE A1003     6892   6323   4561   -486  -1027    -91       N  
ATOM   1674  CA  ILE A1003      -2.992  -3.583  20.009  1.00 45.79           C  
ANISOU 1674  CA  ILE A1003     6682   6186   4532   -326   -968   -149       C  
ATOM   1675  C   ILE A1003      -2.005  -2.769  19.131  1.00 48.18           C  
ANISOU 1675  C   ILE A1003     6966   6420   4919   -225   -993   -134       C  
ATOM   1676  O   ILE A1003      -1.959  -2.918  17.911  1.00 46.70           O  
ANISOU 1676  O   ILE A1003     6725   6202   4816   -124   -985   -135       O  
ATOM   1677  CB  ILE A1003      -4.387  -2.873  20.012  1.00 49.33           C  
ANISOU 1677  CB  ILE A1003     7109   6690   4945   -291   -849   -272       C  
ATOM   1678  CG1 ILE A1003      -5.073  -2.996  18.642  1.00 48.92           C  
ANISOU 1678  CG1 ILE A1003     6966   6636   4983   -161   -825   -299       C  
ATOM   1679  CG2 ILE A1003      -4.257  -1.390  20.411  1.00 50.73           C  
ANISOU 1679  CG2 ILE A1003     7327   6853   5095   -285   -792   -343       C  
ATOM   1680  CD1 ILE A1003      -6.464  -2.367  18.595  1.00 53.97           C  
ANISOU 1680  CD1 ILE A1003     7553   7317   5635   -120   -730   -400       C  
ATOM   1681  N   PHE A1004      -1.246  -1.885  19.765  1.00 45.13           N  
ANISOU 1681  N   PHE A1004     6636   6014   4497   -269  -1016   -127       N  
ATOM   1682  CA  PHE A1004      -0.150  -1.168  19.106  1.00 44.57           C  
ANISOU 1682  CA  PHE A1004     6556   5875   4503   -199  -1047   -102       C  
ATOM   1683  C   PHE A1004       0.917  -2.150  18.612  1.00 47.92           C  
ANISOU 1683  C   PHE A1004     6933   6231   5043   -190  -1128      0       C  
ATOM   1684  O   PHE A1004       1.280  -2.144  17.439  1.00 47.23           O  
ANISOU 1684  O   PHE A1004     6800   6093   5051    -96  -1107     -5       O  
ATOM   1685  CB  PHE A1004       0.458  -0.174  20.095  1.00 47.09           C  
ANISOU 1685  CB  PHE A1004     6952   6191   4750   -283  -1065   -107       C  
ATOM   1686  CG  PHE A1004       1.622   0.596  19.558  1.00 48.49           C  
ANISOU 1686  CG  PHE A1004     7124   6300   5001   -228  -1099    -81       C  
ATOM   1687  CD1 PHE A1004       1.427   1.645  18.662  1.00 51.35           C  
ANISOU 1687  CD1 PHE A1004     7474   6639   5399   -115  -1029   -152       C  
ATOM   1688  CD2 PHE A1004       2.913   0.296  19.971  1.00 50.85           C  
ANISOU 1688  CD2 PHE A1004     7425   6551   5343   -298  -1208     23       C  
ATOM   1689  CE1 PHE A1004       2.517   2.375  18.166  1.00 52.14           C  
ANISOU 1689  CE1 PHE A1004     7576   6675   5561    -75  -1053   -130       C  
ATOM   1690  CE2 PHE A1004       4.008   1.014  19.489  1.00 53.60           C  
ANISOU 1690  CE2 PHE A1004     7760   6834   5773   -254  -1232     44       C  
ATOM   1691  CZ  PHE A1004       3.814   2.052  18.582  1.00 51.39           C  
ANISOU 1691  CZ  PHE A1004     7480   6536   5510   -144  -1147    -39       C  
ATOM   1692  N   GLU A1005       1.386  -3.014  19.505  1.00 44.30           N  
ANISOU 1692  N   GLU A1005     6485   5764   4582   -297  -1216     93       N  
ATOM   1693  CA  GLU A1005       2.403  -4.007  19.170  1.00 43.94           C  
ANISOU 1693  CA  GLU A1005     6375   5632   4687   -293  -1294    199       C  
ATOM   1694  C   GLU A1005       1.934  -5.001  18.114  1.00 46.61           C  
ANISOU 1694  C   GLU A1005     6649   5948   5112   -219  -1237    179       C  
ATOM   1695  O   GLU A1005       2.690  -5.305  17.193  1.00 46.04           O  
ANISOU 1695  O   GLU A1005     6518   5791   5183   -157  -1223    196       O  
ATOM   1696  CB  GLU A1005       2.840  -4.777  20.428  1.00 46.43           C  
ANISOU 1696  CB  GLU A1005     6714   5941   4988   -437  -1420    321       C  
ATOM   1697  CG  GLU A1005       3.491  -3.923  21.515  1.00 57.08           C  
ANISOU 1697  CG  GLU A1005     8137   7303   6247   -550  -1502    364       C  
ATOM   1698  CD  GLU A1005       4.727  -3.195  21.029  1.00 76.89           C  
ANISOU 1698  CD  GLU A1005    10604   9735   8875   -492  -1535    390       C  
ATOM   1699  OE1 GLU A1005       5.575  -3.838  20.361  1.00 79.24           O  
ANISOU 1699  OE1 GLU A1005    10802   9936   9368   -433  -1570    459       O  
ATOM   1700  OE2 GLU A1005       4.844  -1.982  21.312  1.00 65.89           O  
ANISOU 1700  OE2 GLU A1005     9275   8370   7389   -511  -1511    335       O  
ATOM   1701  N   MET A1006       0.698  -5.502  18.264  1.00 42.36           N  
ANISOU 1701  N   MET A1006     6125   5484   4486   -238  -1194    135       N  
ATOM   1702  CA  MET A1006       0.059  -6.403  17.284  1.00 41.20           C  
ANISOU 1702  CA  MET A1006     5931   5332   4390   -184  -1136    102       C  
ATOM   1703  C   MET A1006       0.199  -5.881  15.865  1.00 44.93           C  
ANISOU 1703  C   MET A1006     6381   5772   4919    -79  -1067     40       C  
ATOM   1704  O   MET A1006       0.660  -6.590  14.962  1.00 44.61           O  
ANISOU 1704  O   MET A1006     6302   5660   4989    -52  -1040     49       O  
ATOM   1705  CB  MET A1006      -1.435  -6.554  17.592  1.00 43.28           C  
ANISOU 1705  CB  MET A1006     6215   5697   4532   -210  -1086     37       C  
ATOM   1706  CG  MET A1006      -2.187  -7.623  16.771  1.00 46.20           C  
ANISOU 1706  CG  MET A1006     6543   6075   4937   -186  -1043     14       C  
ATOM   1707  SD  MET A1006      -3.975  -7.571  17.067  1.00 50.00           S  
ANISOU 1707  SD  MET A1006     7027   6675   5294   -207   -980    -71       S  
ATOM   1708  CE  MET A1006      -4.563  -9.094  16.321  1.00 46.72           C  
ANISOU 1708  CE  MET A1006     6570   6255   4926   -217   -961    -65       C  
ATOM   1709  N   LEU A1007      -0.214  -4.635  15.680  1.00 41.43           N  
ANISOU 1709  N   LEU A1007     5967   5373   4400    -33  -1033    -26       N  
ATOM   1710  CA  LEU A1007      -0.243  -4.005  14.366  1.00 40.90           C  
ANISOU 1710  CA  LEU A1007     5897   5287   4356     49   -982    -78       C  
ATOM   1711  C   LEU A1007       1.127  -3.496  13.974  1.00 43.87           C  
ANISOU 1711  C   LEU A1007     6275   5576   4818     72   -989    -52       C  
ATOM   1712  O   LEU A1007       1.445  -3.446  12.792  1.00 42.82           O  
ANISOU 1712  O   LEU A1007     6139   5396   4733    111   -943    -77       O  
ATOM   1713  CB  LEU A1007      -1.279  -2.867  14.339  1.00 41.03           C  
ANISOU 1713  CB  LEU A1007     5932   5371   4287     91   -953   -145       C  
ATOM   1714  CG  LEU A1007      -2.704  -3.381  14.146  1.00 45.96           C  
ANISOU 1714  CG  LEU A1007     6528   6066   4869     92   -928   -182       C  
ATOM   1715  CD1 LEU A1007      -3.734  -2.366  14.582  1.00 46.36           C  
ANISOU 1715  CD1 LEU A1007     6571   6172   4872    117   -899   -240       C  
ATOM   1716  CD2 LEU A1007      -2.906  -3.772  12.671  1.00 48.80           C  
ANISOU 1716  CD2 LEU A1007     6876   6409   5257    126   -913   -192       C  
ATOM   1717  N   ARG A1008       1.935  -3.130  14.969  1.00 40.52           N  
ANISOU 1717  N   ARG A1008     5860   5131   4406     32  -1047     -3       N  
ATOM   1718  CA  ARG A1008       3.347  -2.813  14.745  1.00 40.20           C  
ANISOU 1718  CA  ARG A1008     5800   4999   4474     40  -1066     37       C  
ATOM   1719  C   ARG A1008       4.083  -4.014  14.144  1.00 43.49           C  
ANISOU 1719  C   ARG A1008     6150   5321   5053     38  -1051     77       C  
ATOM   1720  O   ARG A1008       5.069  -3.850  13.433  1.00 42.95           O  
ANISOU 1720  O   ARG A1008     6053   5164   5100     63  -1014     74       O  
ATOM   1721  CB  ARG A1008       4.008  -2.381  16.059  1.00 41.83           C  
ANISOU 1721  CB  ARG A1008     6026   5206   4662    -30  -1155     99       C  
ATOM   1722  CG  ARG A1008       5.397  -1.734  15.917  1.00 52.35           C  
ANISOU 1722  CG  ARG A1008     7338   6456   6095    -23  -1182    134       C  
ATOM   1723  CD  ARG A1008       6.534  -2.705  16.161  1.00 62.48           C  
ANISOU 1723  CD  ARG A1008     8538   7643   7557    -63  -1254    239       C  
ATOM   1724  NE  ARG A1008       7.733  -2.075  16.727  1.00 70.16           N  
ANISOU 1724  NE  ARG A1008     9496   8567   8596   -105  -1335    305       N  
ATOM   1725  CZ  ARG A1008       7.880  -1.708  18.004  1.00 84.74           C  
ANISOU 1725  CZ  ARG A1008    11390  10456  10352   -204  -1446    367       C  
ATOM   1726  NH1 ARG A1008       9.024  -1.160  18.404  1.00 72.74           N  
ANISOU 1726  NH1 ARG A1008     9850   8885   8902   -248  -1526    431       N  
ATOM   1727  NH2 ARG A1008       6.894  -1.867  18.889  1.00 71.53           N  
ANISOU 1727  NH2 ARG A1008     9790   8876   8512   -274  -1471    361       N  
ATOM   1728  N   ILE A1009       3.597  -5.216  14.444  1.00 39.93           N  
ANISOU 1728  N   ILE A1009     5673   4878   4620      2  -1066    107       N  
ATOM   1729  CA  ILE A1009       4.146  -6.452  13.897  1.00 39.76           C  
ANISOU 1729  CA  ILE A1009     5584   4756   4768     -3  -1034    135       C  
ATOM   1730  C   ILE A1009       3.499  -6.830  12.564  1.00 44.67           C  
ANISOU 1730  C   ILE A1009     6223   5382   5370     28   -920     45       C  
ATOM   1731  O   ILE A1009       4.178  -7.351  11.656  1.00 45.33           O  
ANISOU 1731  O   ILE A1009     6271   5362   5589     34   -838     21       O  
ATOM   1732  CB  ILE A1009       3.973  -7.637  14.888  1.00 42.84           C  
ANISOU 1732  CB  ILE A1009     5940   5138   5198    -68  -1113    223       C  
ATOM   1733  CG1 ILE A1009       5.032  -7.562  16.005  1.00 43.64           C  
ANISOU 1733  CG1 ILE A1009     6007   5185   5387   -123  -1243    345       C  
ATOM   1734  CG2 ILE A1009       4.039  -8.982  14.147  1.00 43.12           C  
ANISOU 1734  CG2 ILE A1009     5918   5085   5383    -64  -1045    218       C  
ATOM   1735  CD1 ILE A1009       5.043  -8.778  16.918  1.00 49.35           C  
ANISOU 1735  CD1 ILE A1009     6696   5876   6179   -201  -1342    460       C  
ATOM   1736  N   ASP A1010       2.192  -6.609  12.450  1.00 40.62           N  
ANISOU 1736  N   ASP A1010     5759   4979   4696     34   -910     -6       N  
ATOM   1737  CA  ASP A1010       1.480  -6.986  11.239  1.00 40.15           C  
ANISOU 1737  CA  ASP A1010     5723   4936   4597     39   -829    -77       C  
ATOM   1738  C   ASP A1010       1.774  -5.997  10.094  1.00 44.87           C  
ANISOU 1738  C   ASP A1010     6368   5517   5165     70   -774   -133       C  
ATOM   1739  O   ASP A1010       1.843  -6.401   8.920  1.00 45.17           O  
ANISOU 1739  O   ASP A1010     6430   5512   5219     47   -691   -182       O  
ATOM   1740  CB  ASP A1010      -0.031  -7.110  11.500  1.00 41.34           C  
ANISOU 1740  CB  ASP A1010     5894   5205   4610     29   -851   -101       C  
ATOM   1741  CG  ASP A1010      -0.429  -8.455  12.158  1.00 48.12           C  
ANISOU 1741  CG  ASP A1010     6719   6067   5498    -23   -868    -65       C  
ATOM   1742  OD1 ASP A1010       0.378  -9.407  12.191  1.00 48.34           O  
ANISOU 1742  OD1 ASP A1010     6708   5996   5663    -47   -857    -25       O  
ATOM   1743  OD2 ASP A1010      -1.577  -8.571  12.632  1.00 52.52           O  
ANISOU 1743  OD2 ASP A1010     7283   6719   5954    -41   -889    -77       O  
ATOM   1744  N   GLU A1011       1.985  -4.724  10.442  1.00 40.91           N  
ANISOU 1744  N   GLU A1011     5889   5041   4615    107   -814   -125       N  
ATOM   1745  CA  GLU A1011       1.994  -3.635   9.467  1.00 40.25           C  
ANISOU 1745  CA  GLU A1011     5862   4961   4472    134   -784   -167       C  
ATOM   1746  C   GLU A1011       3.308  -2.847   9.414  1.00 45.28           C  
ANISOU 1746  C   GLU A1011     6502   5519   5185    149   -769   -157       C  
ATOM   1747  O   GLU A1011       3.579  -2.160   8.436  1.00 45.29           O  
ANISOU 1747  O   GLU A1011     6553   5493   5161    153   -724   -191       O  
ATOM   1748  CB  GLU A1011       0.817  -2.709   9.769  1.00 41.18           C  
ANISOU 1748  CB  GLU A1011     6002   5177   4466    169   -836   -177       C  
ATOM   1749  CG  GLU A1011       0.316  -1.892   8.589  1.00 53.52           C  
ANISOU 1749  CG  GLU A1011     7620   6757   5957    186   -828   -206       C  
ATOM   1750  CD  GLU A1011      -1.212  -1.921   8.450  1.00 78.62           C  
ANISOU 1750  CD  GLU A1011    10788  10025   9059    193   -867   -213       C  
ATOM   1751  OE1 GLU A1011      -1.774  -3.016   8.225  1.00 78.28           O  
ANISOU 1751  OE1 GLU A1011    10730  10009   9005    151   -856   -221       O  
ATOM   1752  OE2 GLU A1011      -1.857  -0.852   8.552  1.00 74.85           O  
ANISOU 1752  OE2 GLU A1011    10309   9581   8550    240   -908   -211       O  
ATOM   1753  N   GLY A1012       4.126  -2.940  10.459  1.00 42.89           N  
ANISOU 1753  N   GLY A1012     6148   5177   4971    144   -816   -104       N  
ATOM   1754  CA  GLY A1012       5.420  -2.252  10.491  1.00 43.31           C  
ANISOU 1754  CA  GLY A1012     6187   5153   5115    151   -812    -86       C  
ATOM   1755  C   GLY A1012       5.292  -0.842  11.020  1.00 47.97           C  
ANISOU 1755  C   GLY A1012     6825   5796   5607    177   -864    -86       C  
ATOM   1756  O   GLY A1012       4.210  -0.239  10.934  1.00 47.83           O  
ANISOU 1756  O   GLY A1012     6855   5856   5463    203   -872   -119       O  
ATOM   1757  N   LEU A1013       6.392  -0.312  11.566  1.00 44.75           N  
ANISOU 1757  N   LEU A1013     6396   5336   5271    167   -897    -50       N  
ATOM   1758  CA  LEU A1013       6.409   1.024  12.206  1.00 44.28           C  
ANISOU 1758  CA  LEU A1013     6384   5313   5127    175   -942    -52       C  
ATOM   1759  C   LEU A1013       7.354   1.953  11.464  1.00 47.69           C  
ANISOU 1759  C   LEU A1013     6837   5677   5605    193   -897    -74       C  
ATOM   1760  O   LEU A1013       8.531   1.659  11.340  1.00 47.73           O  
ANISOU 1760  O   LEU A1013     6788   5598   5750    172   -884    -47       O  
ATOM   1761  CB  LEU A1013       6.843   0.911  13.669  1.00 44.88           C  
ANISOU 1761  CB  LEU A1013     6435   5399   5216    118  -1038     15       C  
ATOM   1762  CG  LEU A1013       7.307   2.173  14.427  1.00 50.02           C  
ANISOU 1762  CG  LEU A1013     7133   6060   5814     93  -1082     20       C  
ATOM   1763  CD1 LEU A1013       6.122   3.134  14.660  1.00 50.14           C  
ANISOU 1763  CD1 LEU A1013     7223   6153   5675    117  -1052    -49       C  
ATOM   1764  CD2 LEU A1013       8.020   1.799  15.745  1.00 51.88           C  
ANISOU 1764  CD2 LEU A1013     7341   6287   6084     -1  -1194    110       C  
ATOM   1765  N   ARG A1014       6.835   3.086  10.995  1.00 43.48           N  
ANISOU 1765  N   ARG A1014     6375   5173   4971    229   -875   -118       N  
ATOM   1766  CA  ARG A1014       7.615   4.043  10.232  1.00 42.81           C  
ANISOU 1766  CA  ARG A1014     6329   5028   4909    239   -831   -139       C  
ATOM   1767  C   ARG A1014       7.790   5.384  10.962  1.00 46.92           C  
ANISOU 1767  C   ARG A1014     6889   5558   5379    247   -871   -139       C  
ATOM   1768  O   ARG A1014       6.875   6.202  11.000  1.00 46.48           O  
ANISOU 1768  O   ARG A1014     6885   5546   5230    281   -876   -167       O  
ATOM   1769  CB  ARG A1014       6.961   4.269   8.871  1.00 41.09           C  
ANISOU 1769  CB  ARG A1014     6175   4816   4621    257   -774   -180       C  
ATOM   1770  CG  ARG A1014       7.258   3.188   7.846  1.00 48.22           C  
ANISOU 1770  CG  ARG A1014     7067   5675   5582    219   -696   -200       C  
ATOM   1771  CD  ARG A1014       7.028   3.725   6.436  1.00 56.66           C  
ANISOU 1771  CD  ARG A1014     8231   6730   6568    199   -640   -235       C  
ATOM   1772  NE  ARG A1014       6.818   2.668   5.445  1.00 60.69           N  
ANISOU 1772  NE  ARG A1014     8761   7227   7073    142   -566   -268       N  
ATOM   1773  CZ  ARG A1014       7.775   2.061   4.747  1.00 68.91           C  
ANISOU 1773  CZ  ARG A1014     9796   8181   8206     82   -450   -309       C  
ATOM   1774  NH1 ARG A1014       9.053   2.391   4.903  1.00 51.17           N  
ANISOU 1774  NH1 ARG A1014     7510   5850   6083     78   -401   -315       N  
ATOM   1775  NH2 ARG A1014       7.443   1.112   3.876  1.00 53.62           N  
ANISOU 1775  NH2 ARG A1014     7892   6235   6246     17   -373   -352       N  
ATOM   1776  N   LEU A1015       8.982   5.610  11.514  1.00 43.70           N  
ANISOU 1776  N   LEU A1015     6452   5101   5051    210   -896   -108       N  
ATOM   1777  CA  LEU A1015       9.355   6.921  12.066  1.00 43.51           C  
ANISOU 1777  CA  LEU A1015     6475   5070   4986    201   -920   -116       C  
ATOM   1778  C   LEU A1015       9.593   7.981  10.972  1.00 47.51           C  
ANISOU 1778  C   LEU A1015     7043   5529   5479    234   -857   -154       C  
ATOM   1779  O   LEU A1015       9.491   9.172  11.238  1.00 47.81           O  
ANISOU 1779  O   LEU A1015     7139   5566   5460    245   -863   -174       O  
ATOM   1780  CB  LEU A1015      10.585   6.794  12.975  1.00 43.90           C  
ANISOU 1780  CB  LEU A1015     6472   5083   5126    134   -986    -59       C  
ATOM   1781  CG  LEU A1015      10.432   5.833  14.170  1.00 49.10           C  
ANISOU 1781  CG  LEU A1015     7084   5783   5787     75  -1077      2       C  
ATOM   1782  CD1 LEU A1015      11.708   5.722  14.998  1.00 49.99           C  
ANISOU 1782  CD1 LEU A1015     7139   5850   6003     -5  -1172     84       C  
ATOM   1783  CD2 LEU A1015       9.266   6.235  15.074  1.00 51.88           C  
ANISOU 1783  CD2 LEU A1015     7510   6225   5977     57  -1096    -30       C  
ATOM   1784  N   LYS A1016       9.894   7.554   9.751  1.00 43.64           N  
ANISOU 1784  N   LYS A1016     6552   4994   5036    237   -790   -167       N  
ATOM   1785  CA  LYS A1016      10.099   8.469   8.627  1.00 43.46           C  
ANISOU 1785  CA  LYS A1016     6604   4926   4981    244   -731   -196       C  
ATOM   1786  C   LYS A1016       9.007   8.297   7.549  1.00 46.20           C  
ANISOU 1786  C   LYS A1016     7010   5304   5239    262   -708   -212       C  
ATOM   1787  O   LYS A1016       8.541   7.169   7.294  1.00 45.51           O  
ANISOU 1787  O   LYS A1016     6892   5244   5155    252   -696   -214       O  
ATOM   1788  CB  LYS A1016      11.485   8.224   8.014  1.00 46.52           C  
ANISOU 1788  CB  LYS A1016     6960   5225   5491    197   -657   -205       C  
ATOM   1789  CG  LYS A1016      11.879   9.226   6.937  1.00 59.94           C  
ANISOU 1789  CG  LYS A1016     8749   6872   7153    179   -590   -235       C  
ATOM   1790  CD  LYS A1016      13.347   9.136   6.611  1.00 71.38           C  
ANISOU 1790  CD  LYS A1016    10151   8229   8741    127   -510   -251       C  
ATOM   1791  CE  LYS A1016      13.653   9.757   5.240  1.00 83.06           C  
ANISOU 1791  CE  LYS A1016    11734   9654  10170     81   -407   -294       C  
ATOM   1792  NZ  LYS A1016      13.017  11.090   5.061  1.00 91.59           N  
ANISOU 1792  NZ  LYS A1016    12930  10760  11109    105   -459   -281       N  
ATOM   1793  N   ILE A1017       8.613   9.408   6.918  1.00 41.89           N  
ANISOU 1793  N   ILE A1017     6549   4747   4618    280   -713   -215       N  
ATOM   1794  CA  ILE A1017       7.615   9.383   5.838  1.00 41.58           C  
ANISOU 1794  CA  ILE A1017     6573   4731   4493    279   -720   -208       C  
ATOM   1795  C   ILE A1017       8.116   8.554   4.643  1.00 45.34           C  
ANISOU 1795  C   ILE A1017     7085   5176   4968    200   -638   -229       C  
ATOM   1796  O   ILE A1017       9.254   8.708   4.208  1.00 45.36           O  
ANISOU 1796  O   ILE A1017     7108   5109   5018    150   -560   -254       O  
ATOM   1797  CB  ILE A1017       7.246  10.809   5.344  1.00 45.01           C  
ANISOU 1797  CB  ILE A1017     7092   5138   4872    302   -756   -186       C  
ATOM   1798  CG1 ILE A1017       6.423  11.564   6.396  1.00 45.33           C  
ANISOU 1798  CG1 ILE A1017     7097   5203   4922    380   -817   -180       C  
ATOM   1799  CG2 ILE A1017       6.439  10.740   4.045  1.00 46.19           C  
ANISOU 1799  CG2 ILE A1017     7317   5299   4937    269   -782   -156       C  
ATOM   1800  CD1 ILE A1017       5.816  12.901   5.881  1.00 51.41           C  
ANISOU 1800  CD1 ILE A1017     7929   5931   5672    418   -860   -149       C  
ATOM   1801  N   TYR A1018       7.258   7.672   4.132  1.00 41.07           N  
ANISOU 1801  N   TYR A1018     6551   4680   4375    179   -645   -229       N  
ATOM   1802  CA  TYR A1018       7.596   6.790   3.015  1.00 40.71           C  
ANISOU 1802  CA  TYR A1018     6550   4605   4312     85   -551   -265       C  
ATOM   1803  C   TYR A1018       6.559   6.934   1.909  1.00 43.62           C  
ANISOU 1803  C   TYR A1018     7024   5011   4538     34   -596   -240       C  
ATOM   1804  O   TYR A1018       5.355   6.873   2.154  1.00 42.66           O  
ANISOU 1804  O   TYR A1018     6879   4957   4372     79   -693   -202       O  
ATOM   1805  CB  TYR A1018       7.666   5.333   3.487  1.00 41.87           C  
ANISOU 1805  CB  TYR A1018     6602   4763   4546     82   -510   -289       C  
ATOM   1806  CG  TYR A1018       7.873   4.302   2.386  1.00 44.22           C  
ANISOU 1806  CG  TYR A1018     6942   5024   4836    -20   -394   -342       C  
ATOM   1807  CD1 TYR A1018       6.786   3.624   1.833  1.00 46.41           C  
ANISOU 1807  CD1 TYR A1018     7262   5361   5012    -60   -418   -342       C  
ATOM   1808  CD2 TYR A1018       9.152   3.998   1.912  1.00 45.45           C  
ANISOU 1808  CD2 TYR A1018     7091   5080   5098    -85   -250   -400       C  
ATOM   1809  CE1 TYR A1018       6.964   2.681   0.827  1.00 48.49           C  
ANISOU 1809  CE1 TYR A1018     7580   5589   5255   -174   -298   -403       C  
ATOM   1810  CE2 TYR A1018       9.342   3.059   0.908  1.00 47.21           C  
ANISOU 1810  CE2 TYR A1018     7358   5257   5321   -192   -113   -470       C  
ATOM   1811  CZ  TYR A1018       8.243   2.400   0.371  1.00 55.76           C  
ANISOU 1811  CZ  TYR A1018     8503   6404   6280   -241   -136   -473       C  
ATOM   1812  OH  TYR A1018       8.409   1.461  -0.623  1.00 57.63           O  
ANISOU 1812  OH  TYR A1018     8800   6594   6504   -366     11   -553       O  
ATOM   1813  N   LYS A1019       7.063   7.149   0.699  1.00 40.11           N  
ANISOU 1813  N   LYS A1019     6696   4519   4026    -74   -524   -261       N  
ATOM   1814  CA  LYS A1019       6.270   7.233  -0.515  1.00 40.11           C  
ANISOU 1814  CA  LYS A1019     6823   4545   3871   -170   -567   -230       C  
ATOM   1815  C   LYS A1019       6.384   5.882  -1.198  1.00 44.20           C  
ANISOU 1815  C   LYS A1019     7371   5062   4363   -284   -454   -297       C  
ATOM   1816  O   LYS A1019       7.492   5.477  -1.551  1.00 44.39           O  
ANISOU 1816  O   LYS A1019     7410   5012   4444   -356   -295   -374       O  
ATOM   1817  CB  LYS A1019       6.857   8.331  -1.415  1.00 42.86           C  
ANISOU 1817  CB  LYS A1019     7307   4835   4144   -251   -547   -215       C  
ATOM   1818  CG  LYS A1019       6.088   8.639  -2.695  1.00 52.00           C  
ANISOU 1818  CG  LYS A1019     8620   6012   5124   -374   -623   -156       C  
ATOM   1819  CD  LYS A1019       6.955   9.437  -3.677  1.00 60.65           C  
ANISOU 1819  CD  LYS A1019     9871   7037   6137   -500   -554   -164       C  
ATOM   1820  CE  LYS A1019       6.293   9.579  -5.056  1.00 73.80           C  
ANISOU 1820  CE  LYS A1019    11720   8722   7599   -673   -626   -102       C  
ATOM   1821  NZ  LYS A1019       5.375  10.764  -5.199  1.00 84.50           N  
ANISOU 1821  NZ  LYS A1019    13113  10088   8904   -630   -840     41       N  
ATOM   1822  N   ASP A1020       5.257   5.186  -1.370  1.00 40.39           N  
ANISOU 1822  N   ASP A1020     6887   4650   3810   -302   -524   -273       N  
ATOM   1823  CA  ASP A1020       5.234   3.874  -2.066  1.00 40.50           C  
ANISOU 1823  CA  ASP A1020     6942   4662   3784   -425   -416   -341       C  
ATOM   1824  C   ASP A1020       5.182   3.997  -3.606  1.00 44.11           C  
ANISOU 1824  C   ASP A1020     7594   5107   4058   -621   -376   -353       C  
ATOM   1825  O   ASP A1020       5.321   5.095  -4.151  1.00 44.24           O  
ANISOU 1825  O   ASP A1020     7715   5106   3988   -664   -427   -305       O  
ATOM   1826  CB  ASP A1020       4.093   2.985  -1.533  1.00 42.00           C  
ANISOU 1826  CB  ASP A1020     7046   4934   3979   -373   -499   -318       C  
ATOM   1827  CG  ASP A1020       2.716   3.462  -1.953  1.00 51.35           C  
ANISOU 1827  CG  ASP A1020     8279   6198   5032   -388   -674   -226       C  
ATOM   1828  OD1 ASP A1020       2.604   4.453  -2.705  1.00 52.86           O  
ANISOU 1828  OD1 ASP A1020     8580   6380   5125   -444   -746   -169       O  
ATOM   1829  OD2 ASP A1020       1.729   2.846  -1.510  1.00 57.36           O  
ANISOU 1829  OD2 ASP A1020     8963   7027   5803   -343   -748   -204       O  
ATOM   1830  N   THR A1021       4.989   2.878  -4.304  1.00 40.46           N  
ANISOU 1830  N   THR A1021     7195   4651   3529   -756   -285   -416       N  
ATOM   1831  CA  THR A1021       5.065   2.870  -5.774  1.00 41.32           C  
ANISOU 1831  CA  THR A1021     7511   4742   3447   -984   -216   -447       C  
ATOM   1832  C   THR A1021       3.851   3.460  -6.484  1.00 45.96           C  
ANISOU 1832  C   THR A1021     8219   5412   3834  -1066   -425   -327       C  
ATOM   1833  O   THR A1021       3.925   3.721  -7.674  1.00 47.38           O  
ANISOU 1833  O   THR A1021     8590   5579   3831  -1266   -407   -323       O  
ATOM   1834  CB  THR A1021       5.295   1.461  -6.335  1.00 46.00           C  
ANISOU 1834  CB  THR A1021     8147   5302   4029  -1129    -25   -572       C  
ATOM   1835  OG1 THR A1021       4.298   0.579  -5.817  1.00 44.28           O  
ANISOU 1835  OG1 THR A1021     7835   5156   3834  -1066   -113   -547       O  
ATOM   1836  CG2 THR A1021       6.685   0.952  -5.976  1.00 43.45           C  
ANISOU 1836  CG2 THR A1021     7732   4861   3916  -1097    209   -694       C  
ATOM   1837  N   GLU A1022       2.748   3.662  -5.779  1.00 42.06           N  
ANISOU 1837  N   GLU A1022     7610   4993   3377   -926   -621   -226       N  
ATOM   1838  CA  GLU A1022       1.554   4.272  -6.378  1.00 43.41           C  
ANISOU 1838  CA  GLU A1022     7856   5229   3410   -984   -844    -90       C  
ATOM   1839  C   GLU A1022       1.297   5.726  -5.932  1.00 48.80           C  
ANISOU 1839  C   GLU A1022     8485   5900   4156   -843  -1009     28       C  
ATOM   1840  O   GLU A1022       0.184   6.246  -6.095  1.00 48.97           O  
ANISOU 1840  O   GLU A1022     8495   5965   4148   -826  -1217    156       O  
ATOM   1841  CB  GLU A1022       0.308   3.405  -6.108  1.00 44.59           C  
ANISOU 1841  CB  GLU A1022     7918   5465   3559   -959   -949    -58       C  
ATOM   1842  CG  GLU A1022       0.378   1.972  -6.664  1.00 52.49           C  
ANISOU 1842  CG  GLU A1022     8989   6477   4479  -1120   -805   -165       C  
ATOM   1843  CD  GLU A1022       0.563   1.901  -8.180  1.00 65.40           C  
ANISOU 1843  CD  GLU A1022    10867   8098   5883  -1401   -758   -183       C  
ATOM   1844  OE1 GLU A1022       0.922   0.814  -8.672  1.00 58.96           O  
ANISOU 1844  OE1 GLU A1022    10130   7261   5012  -1550   -577   -306       O  
ATOM   1845  OE2 GLU A1022       0.353   2.913  -8.880  1.00 55.84           O  
ANISOU 1845  OE2 GLU A1022     9778   6892   4546  -1488   -896    -77       O  
ATOM   1846  N   GLY A1023       2.331   6.380  -5.397  1.00 45.49           N  
ANISOU 1846  N   GLY A1023     8030   5413   3840   -750   -915    -13       N  
ATOM   1847  CA  GLY A1023       2.251   7.784  -5.009  1.00 45.59           C  
ANISOU 1847  CA  GLY A1023     8010   5396   3917   -632  -1036     78       C  
ATOM   1848  C   GLY A1023       1.657   8.110  -3.642  1.00 49.69           C  
ANISOU 1848  C   GLY A1023     8333   5938   4610   -408  -1121    109       C  
ATOM   1849  O   GLY A1023       1.456   9.288  -3.329  1.00 49.48           O  
ANISOU 1849  O   GLY A1023     8276   5879   4646   -313  -1219    182       O  
ATOM   1850  N   TYR A1024       1.375   7.118  -2.823  1.00 46.31           N  
ANISOU 1850  N   TYR A1024     7779   5558   4261   -332  -1075     52       N  
ATOM   1851  CA  TYR A1024       0.779   7.349  -1.530  1.00 45.56           C  
ANISOU 1851  CA  TYR A1024     7514   5487   4308   -151  -1136     68       C  
ATOM   1852  C   TYR A1024       1.798   7.612  -0.456  1.00 47.85           C  
ANISOU 1852  C   TYR A1024     7731   5734   4715    -47  -1030      0       C  
ATOM   1853  O   TYR A1024       2.719   6.880  -0.317  1.00 47.03           O  
ANISOU 1853  O   TYR A1024     7626   5611   4633    -81   -899    -79       O  
ATOM   1854  CB  TYR A1024      -0.008   6.122  -1.140  1.00 46.82           C  
ANISOU 1854  CB  TYR A1024     7586   5721   4484   -140  -1139     41       C  
ATOM   1855  CG  TYR A1024      -1.245   5.943  -1.937  1.00 50.23           C  
ANISOU 1855  CG  TYR A1024     8049   6207   4830   -216  -1281    123       C  
ATOM   1856  CD1 TYR A1024      -1.216   5.380  -3.178  1.00 53.08           C  
ANISOU 1856  CD1 TYR A1024     8554   6581   5034   -402  -1273    125       C  
ATOM   1857  CD2 TYR A1024      -2.453   6.347  -1.447  1.00 51.63           C  
ANISOU 1857  CD2 TYR A1024     8109   6418   5092   -115  -1421    197       C  
ATOM   1858  CE1 TYR A1024      -2.351   5.243  -3.901  1.00 55.21           C  
ANISOU 1858  CE1 TYR A1024     8856   6904   5219   -489  -1426    214       C  
ATOM   1859  CE2 TYR A1024      -3.589   6.195  -2.165  1.00 53.89           C  
ANISOU 1859  CE2 TYR A1024     8403   6749   5324   -186  -1568    286       C  
ATOM   1860  CZ  TYR A1024      -3.533   5.640  -3.393  1.00 61.54           C  
ANISOU 1860  CZ  TYR A1024     9522   7738   6122   -376  -1583    302       C  
ATOM   1861  OH  TYR A1024      -4.680   5.495  -4.102  1.00 62.53           O  
ANISOU 1861  OH  TYR A1024     9659   7913   6187   -464  -1752    403       O  
ATOM   1862  N   TYR A1025       1.608   8.644   0.331  1.00 43.69           N  
ANISOU 1862  N   TYR A1025     7138   5187   4277     74  -1088     33       N  
ATOM   1863  CA  TYR A1025       2.545   8.934   1.401  1.00 42.43           C  
ANISOU 1863  CA  TYR A1025     6917   4992   4213    154  -1002    -26       C  
ATOM   1864  C   TYR A1025       2.035   8.402   2.748  1.00 45.87           C  
ANISOU 1864  C   TYR A1025     7216   5479   4735    252  -1003    -56       C  
ATOM   1865  O   TYR A1025       0.916   8.589   3.126  1.00 44.79           O  
ANISOU 1865  O   TYR A1025     7012   5376   4629    314  -1080    -25       O  
ATOM   1866  CB  TYR A1025       2.853  10.428   1.435  1.00 43.51           C  
ANISOU 1866  CB  TYR A1025     7091   5062   4377    199  -1037     11       C  
ATOM   1867  CG  TYR A1025       3.577  10.973   0.223  1.00 44.72           C  
ANISOU 1867  CG  TYR A1025     7392   5158   4442     89  -1018     34       C  
ATOM   1868  CD1 TYR A1025       2.898  11.487  -0.833  1.00 47.42           C  
ANISOU 1868  CD1 TYR A1025     7826   5492   4701     24  -1128    124       C  
ATOM   1869  CD2 TYR A1025       4.945  11.000   0.169  1.00 44.88           C  
ANISOU 1869  CD2 TYR A1025     7456   5128   4470     42   -894    -28       C  
ATOM   1870  CE1 TYR A1025       3.555  11.979  -1.909  1.00 48.39           C  
ANISOU 1870  CE1 TYR A1025     8100   5563   4722    -98  -1109    146       C  
ATOM   1871  CE2 TYR A1025       5.605  11.505  -0.895  1.00 46.25           C  
ANISOU 1871  CE2 TYR A1025     7765   5246   4560    -68   -858    -18       C  
ATOM   1872  CZ  TYR A1025       4.910  11.985  -1.940  1.00 53.68           C  
ANISOU 1872  CZ  TYR A1025     8818   6186   5393   -145   -962     67       C  
ATOM   1873  OH  TYR A1025       5.573  12.477  -3.024  1.00 53.58           O  
ANISOU 1873  OH  TYR A1025     8963   6120   5275   -281   -924     79       O  
ATOM   1874  N   THR A1026       2.876   7.668   3.442  1.00 43.38           N  
ANISOU 1874  N   THR A1026     6857   5162   4465    251   -913   -116       N  
ATOM   1875  CA  THR A1026       2.488   6.983   4.678  1.00 43.03           C  
ANISOU 1875  CA  THR A1026     6703   5167   4478    308   -911   -140       C  
ATOM   1876  C   THR A1026       3.501   7.111   5.815  1.00 46.90           C  
ANISOU 1876  C   THR A1026     7149   5630   5040    337   -863   -171       C  
ATOM   1877  O   THR A1026       4.655   7.346   5.589  1.00 46.53           O  
ANISOU 1877  O   THR A1026     7136   5526   5018    305   -811   -185       O  
ATOM   1878  CB  THR A1026       2.170   5.522   4.387  1.00 50.29           C  
ANISOU 1878  CB  THR A1026     7603   6132   5374    254   -886   -157       C  
ATOM   1879  OG1 THR A1026       0.927   5.190   4.958  1.00 49.25           O  
ANISOU 1879  OG1 THR A1026     7399   6069   5246    298   -946   -144       O  
ATOM   1880  CG2 THR A1026       3.179   4.651   4.951  1.00 48.93           C  
ANISOU 1880  CG2 THR A1026     7389   5935   5268    235   -806   -196       C  
ATOM   1881  N   ILE A1027       3.048   6.998   7.045  1.00 43.36           N  
ANISOU 1881  N   ILE A1027     6629   5222   4623    383   -884   -181       N  
ATOM   1882  CA  ILE A1027       3.912   7.184   8.199  1.00 42.87           C  
ANISOU 1882  CA  ILE A1027     6538   5141   4608    387   -864   -198       C  
ATOM   1883  C   ILE A1027       3.521   6.298   9.373  1.00 47.18           C  
ANISOU 1883  C   ILE A1027     7016   5744   5165    381   -876   -205       C  
ATOM   1884  O   ILE A1027       2.459   5.750   9.406  1.00 46.69           O  
ANISOU 1884  O   ILE A1027     6924   5737   5078    392   -892   -207       O  
ATOM   1885  CB  ILE A1027       3.970   8.673   8.617  1.00 45.92           C  
ANISOU 1885  CB  ILE A1027     6955   5494   5000    427   -875   -205       C  
ATOM   1886  CG1 ILE A1027       4.876   8.891   9.803  1.00 45.96           C  
ANISOU 1886  CG1 ILE A1027     6945   5484   5033    405   -863   -220       C  
ATOM   1887  CG2 ILE A1027       2.664   9.164   9.006  1.00 46.80           C  
ANISOU 1887  CG2 ILE A1027     7038   5635   5108    481   -902   -213       C  
ATOM   1888  CD1 ILE A1027       6.236   9.129   9.484  1.00 49.55           C  
ANISOU 1888  CD1 ILE A1027     7424   5877   5524    370   -839   -212       C  
ATOM   1889  N   GLY A1028       4.408   6.125  10.328  1.00 43.98           N  
ANISOU 1889  N   GLY A1028     6590   5325   4796    351   -876   -201       N  
ATOM   1890  CA  GLY A1028       4.062   5.378  11.516  1.00 43.60           C  
ANISOU 1890  CA  GLY A1028     6498   5330   4740    323   -900   -196       C  
ATOM   1891  C   GLY A1028       3.542   4.005  11.242  1.00 46.54           C  
ANISOU 1891  C   GLY A1028     6829   5736   5117    308   -900   -184       C  
ATOM   1892  O   GLY A1028       4.160   3.256  10.560  1.00 46.11           O  
ANISOU 1892  O   GLY A1028     6762   5644   5115    288   -877   -171       O  
ATOM   1893  N   ILE A1029       2.415   3.680  11.825  1.00 42.74           N  
ANISOU 1893  N   ILE A1029     6326   5322   4591    311   -912   -198       N  
ATOM   1894  CA  ILE A1029       1.768   2.422  11.573  1.00 42.55           C  
ANISOU 1894  CA  ILE A1029     6267   5337   4564    295   -912   -190       C  
ATOM   1895  C   ILE A1029       0.684   2.531  10.507  1.00 46.29           C  
ANISOU 1895  C   ILE A1029     6745   5838   5004    331   -907   -207       C  
ATOM   1896  O   ILE A1029      -0.473   2.627  10.804  1.00 45.86           O  
ANISOU 1896  O   ILE A1029     6664   5837   4924    352   -918   -224       O  
ATOM   1897  CB  ILE A1029       1.267   1.788  12.878  1.00 45.82           C  
ANISOU 1897  CB  ILE A1029     6653   5806   4949    253   -932   -186       C  
ATOM   1898  CG1 ILE A1029       2.461   1.269  13.672  1.00 46.20           C  
ANISOU 1898  CG1 ILE A1029     6693   5818   5044    192   -967   -135       C  
ATOM   1899  CG2 ILE A1029       0.302   0.698  12.596  1.00 46.03           C  
ANISOU 1899  CG2 ILE A1029     6646   5881   4962    245   -926   -190       C  
ATOM   1900  CD1 ILE A1029       2.118   0.437  14.761  1.00 52.69           C  
ANISOU 1900  CD1 ILE A1029     7501   6684   5836    127  -1000   -110       C  
ATOM   1901  N   GLY A1030       1.095   2.513   9.259  1.00 42.75           N  
ANISOU 1901  N   GLY A1030     6333   5349   4560    325   -892   -201       N  
ATOM   1902  CA  GLY A1030       0.189   2.614   8.144  1.00 43.16           C  
ANISOU 1902  CA  GLY A1030     6407   5423   4567    330   -910   -198       C  
ATOM   1903  C   GLY A1030      -0.672   3.851   8.051  1.00 47.79           C  
ANISOU 1903  C   GLY A1030     6994   6021   5144    386   -955   -190       C  
ATOM   1904  O   GLY A1030      -1.757   3.807   7.529  1.00 47.63           O  
ANISOU 1904  O   GLY A1030     6955   6037   5108    394   -998   -174       O  
ATOM   1905  N   HIS A1031      -0.167   4.975   8.519  1.00 44.39           N  
ANISOU 1905  N   HIS A1031     6579   5548   4737    422   -948   -196       N  
ATOM   1906  CA  HIS A1031      -0.965   6.173   8.516  1.00 44.27           C  
ANISOU 1906  CA  HIS A1031     6552   5521   4746    482   -979   -192       C  
ATOM   1907  C   HIS A1031      -0.833   6.908   7.205  1.00 49.11           C  
ANISOU 1907  C   HIS A1031     7228   6087   5345    482  -1021   -148       C  
ATOM   1908  O   HIS A1031       0.186   7.440   6.868  1.00 48.14           O  
ANISOU 1908  O   HIS A1031     7169   5909   5211    466  -1000   -144       O  
ATOM   1909  CB  HIS A1031      -0.604   7.058   9.697  1.00 44.42           C  
ANISOU 1909  CB  HIS A1031     6566   5514   4797    509   -943   -229       C  
ATOM   1910  CG  HIS A1031      -1.514   8.220   9.833  1.00 48.18           C  
ANISOU 1910  CG  HIS A1031     7011   5963   5333    575   -949   -240       C  
ATOM   1911  ND1 HIS A1031      -2.764   8.118  10.385  1.00 50.27           N  
ANISOU 1911  ND1 HIS A1031     7195   6262   5645    603   -937   -267       N  
ATOM   1912  CD2 HIS A1031      -1.398   9.488   9.403  1.00 50.06           C  
ANISOU 1912  CD2 HIS A1031     7277   6129   5614    618   -964   -223       C  
ATOM   1913  CE1 HIS A1031      -3.373   9.276  10.301  1.00 50.35           C  
ANISOU 1913  CE1 HIS A1031     7172   6214   5744    667   -940   -270       C  
ATOM   1914  NE2 HIS A1031      -2.562  10.127   9.715  1.00 50.64           N  
ANISOU 1914  NE2 HIS A1031     7277   6185   5777    678   -962   -239       N  
ATOM   1915  N   LEU A1032      -1.901   6.914   6.447  1.00 47.59           N  
ANISOU 1915  N   LEU A1032     7018   5916   5150    487  -1088   -107       N  
ATOM   1916  CA  LEU A1032      -1.865   7.542   5.150  1.00 48.58           C  
ANISOU 1916  CA  LEU A1032     7217   6000   5242    461  -1152    -46       C  
ATOM   1917  C   LEU A1032      -1.960   9.033   5.287  1.00 54.48           C  
ANISOU 1917  C   LEU A1032     7961   6679   6061    530  -1182    -21       C  
ATOM   1918  O   LEU A1032      -2.831   9.521   5.953  1.00 54.25           O  
ANISOU 1918  O   LEU A1032     7843   6644   6125    602  -1195    -28       O  
ATOM   1919  CB  LEU A1032      -2.987   7.036   4.258  1.00 49.20           C  
ANISOU 1919  CB  LEU A1032     7281   6124   5290    422  -1242     10       C  
ATOM   1920  CG  LEU A1032      -2.588   6.521   2.890  1.00 54.32           C  
ANISOU 1920  CG  LEU A1032     8045   6774   5819    303  -1261     41       C  
ATOM   1921  CD1 LEU A1032      -3.761   6.181   2.104  1.00 55.54           C  
ANISOU 1921  CD1 LEU A1032     8188   6974   5940    254  -1372    106       C  
ATOM   1922  CD2 LEU A1032      -1.765   7.439   2.161  1.00 56.88           C  
ANISOU 1922  CD2 LEU A1032     8477   7030   6104    269  -1265     70       C  
ATOM   1923  N   LEU A1033      -1.077   9.765   4.615  1.00 52.47           N  
ANISOU 1923  N   LEU A1033     7802   6362   5772    501  -1183      4       N  
ATOM   1924  CA  LEU A1033      -1.052  11.222   4.742  1.00 53.36           C  
ANISOU 1924  CA  LEU A1033     7922   6396   5959    564  -1206     27       C  
ATOM   1925  C   LEU A1033      -1.671  11.987   3.565  1.00 60.24           C  
ANISOU 1925  C   LEU A1033     8831   7220   6839    553  -1329    133       C  
ATOM   1926  O   LEU A1033      -2.482  12.891   3.764  1.00 61.14           O  
ANISOU 1926  O   LEU A1033     8874   7281   7074    632  -1386    172       O  
ATOM   1927  CB  LEU A1033       0.381  11.709   4.978  1.00 52.68           C  
ANISOU 1927  CB  LEU A1033     7911   6260   5847    544  -1127    -13       C  
ATOM   1928  CG  LEU A1033       0.916  11.572   6.405  1.00 56.38           C  
ANISOU 1928  CG  LEU A1033     8330   6742   6349    572  -1039    -95       C  
ATOM   1929  CD1 LEU A1033       2.395  11.924   6.459  1.00 56.12           C  
ANISOU 1929  CD1 LEU A1033     8368   6664   6293    533   -982   -119       C  
ATOM   1930  CD2 LEU A1033       0.119  12.442   7.364  1.00 59.24           C  
ANISOU 1930  CD2 LEU A1033     8622   7078   6808    652  -1031   -122       C  
ATOM   1931  N   THR A1034      -1.276  11.629   2.348  1.00 57.91           N  
ANISOU 1931  N   THR A1034     8648   6933   6422    445  -1366    180       N  
ATOM   1932  CA  THR A1034      -1.644  12.379   1.161  1.00 59.38           C  
ANISOU 1932  CA  THR A1034     8909   7073   6582    397  -1494    294       C  
ATOM   1933  C   THR A1034      -1.303  11.506  -0.009  1.00 63.85           C  
ANISOU 1933  C   THR A1034     9601   7682   6978    242  -1501    312       C  
ATOM   1934  O   THR A1034      -0.525  10.603   0.117  1.00 62.45           O  
ANISOU 1934  O   THR A1034     9455   7540   6735    191  -1382    226       O  
ATOM   1935  CB  THR A1034      -1.086  13.825   0.960  1.00 68.38           C  
ANISOU 1935  CB  THR A1034    10114   8107   7762    422  -1512    336       C  
ATOM   1936  OG1 THR A1034       0.291  13.805   0.609  1.00 67.27           O  
ANISOU 1936  OG1 THR A1034    10099   7948   7513    339  -1415    289       O  
ATOM   1937  CG2 THR A1034      -1.213  14.595   2.196  1.00 66.69           C  
ANISOU 1937  CG2 THR A1034     9793   7844   7703    555  -1458    284       C  
ATOM   1938  N   LYS A1035      -1.934  11.728  -1.141  1.00 62.25           N  
ANISOU 1938  N   LYS A1035     9467   7475   6712    156  -1643    425       N  
ATOM   1939  CA  LYS A1035      -1.650  10.908  -2.301  1.00 62.74           C  
ANISOU 1939  CA  LYS A1035     9673   7579   6589    -24  -1640    432       C  
ATOM   1940  C   LYS A1035      -1.401  11.722  -3.539  1.00 68.81           C  
ANISOU 1940  C   LYS A1035    10607   8293   7246   -153  -1732    534       C  
ATOM   1941  O   LYS A1035      -1.811  11.345  -4.588  1.00 69.39           O  
ANISOU 1941  O   LYS A1035    10783   8398   7185   -304  -1823    602       O  
ATOM   1942  CB  LYS A1035      -2.726   9.840  -2.553  1.00 65.41           C  
ANISOU 1942  CB  LYS A1035     9962   8002   6889    -75  -1715    457       C  
ATOM   1943  CG  LYS A1035      -4.112  10.149  -2.042  1.00 78.44           C  
ANISOU 1943  CG  LYS A1035    11445   9664   8696     42  -1855    534       C  
ATOM   1944  CD  LYS A1035      -5.104   9.077  -2.439  1.00 88.16           C  
ANISOU 1944  CD  LYS A1035    12644  10981   9873    -35  -1934    564       C  
ATOM   1945  CE  LYS A1035      -6.138   9.533  -3.451  1.00 99.21           C  
ANISOU 1945  CE  LYS A1035    14061  12374  11260   -116  -2168    734       C  
ATOM   1946  NZ  LYS A1035      -7.162   8.512  -3.747  1.00107.16           N  
ANISOU 1946  NZ  LYS A1035    15019  13468  12230   -190  -2255    765       N  
ATOM   1947  N   SER A1036      -0.735  12.850  -3.397  1.00 66.13           N  
ANISOU 1947  N   SER A1036    10301   7869   6955   -104  -1712    545       N  
ATOM   1948  CA  SER A1036      -0.403  13.716  -4.522  1.00 67.46           C  
ANISOU 1948  CA  SER A1036    10638   7975   7017   -230  -1793    644       C  
ATOM   1949  C   SER A1036       1.064  13.974  -4.394  1.00 70.51           C  
ANISOU 1949  C   SER A1036    11109   8316   7367   -253  -1613    540       C  
ATOM   1950  O   SER A1036       1.582  13.890  -3.320  1.00 69.02           O  
ANISOU 1950  O   SER A1036    10816   8123   7285   -130  -1490    438       O  
ATOM   1951  CB  SER A1036      -1.134  15.038  -4.448  1.00 72.43           C  
ANISOU 1951  CB  SER A1036    11207   8524   7790   -132  -1965    782       C  
ATOM   1952  OG  SER A1036      -0.218  16.078  -4.688  1.00 81.45           O  
ANISOU 1952  OG  SER A1036    12458   9578   8913   -154  -1929    795       O  
ATOM   1953  N   PRO A1037       1.719  14.354  -5.475  1.00 67.66           N  
ANISOU 1953  N   PRO A1037    10937   7915   6856   -418  -1605    573       N  
ATOM   1954  CA  PRO A1037       3.169  14.388  -5.541  1.00 66.59           C  
ANISOU 1954  CA  PRO A1037    10891   7741   6670   -479  -1411    460       C  
ATOM   1955  C   PRO A1037       3.988  15.183  -4.566  1.00 68.15           C  
ANISOU 1955  C   PRO A1037    11011   7876   7008   -338  -1320    401       C  
ATOM   1956  O   PRO A1037       5.028  14.690  -4.221  1.00 67.54           O  
ANISOU 1956  O   PRO A1037    10921   7798   6943   -347  -1146    279       O  
ATOM   1957  CB  PRO A1037       3.416  14.834  -6.985  1.00 70.06           C  
ANISOU 1957  CB  PRO A1037    11560   8146   6916   -700  -1461    540       C  
ATOM   1958  CG  PRO A1037       2.418  14.074  -7.696  1.00 75.47           C  
ANISOU 1958  CG  PRO A1037    12289   8901   7486   -816  -1581    608       C  
ATOM   1959  CD  PRO A1037       1.198  13.964  -6.789  1.00 70.57           C  
ANISOU 1959  CD  PRO A1037    11457   8320   7038   -624  -1716    663       C  
ATOM   1960  N   SER A1038       3.612  16.341  -4.119  1.00 63.00           N  
ANISOU 1960  N   SER A1038    10304   7164   6470   -220  -1422    477       N  
ATOM   1961  CA  SER A1038       4.510  17.000  -3.225  1.00 60.92           C  
ANISOU 1961  CA  SER A1038     9988   6846   6314   -118  -1314    401       C  
ATOM   1962  C   SER A1038       4.742  16.160  -1.971  1.00 60.84           C  
ANISOU 1962  C   SER A1038     9824   6891   6401     -8  -1199    279       C  
ATOM   1963  O   SER A1038       3.831  15.663  -1.374  1.00 59.82           O  
ANISOU 1963  O   SER A1038     9577   6815   6337     78  -1250    282       O  
ATOM   1964  CB  SER A1038       3.881  18.328  -2.856  1.00 65.02           C  
ANISOU 1964  CB  SER A1038    10456   7286   6961      0  -1439    495       C  
ATOM   1965  OG  SER A1038       4.839  19.284  -2.532  1.00 73.58           O  
ANISOU 1965  OG  SER A1038    11577   8292   8089     26  -1360    459       O  
ATOM   1966  N   LEU A1039       6.003  15.966  -1.627  1.00 54.66           N  
ANISOU 1966  N   LEU A1039     9048   6093   5629    -28  -1046    178       N  
ATOM   1967  CA  LEU A1039       6.442  15.438  -0.364  1.00 52.03           C  
ANISOU 1967  CA  LEU A1039     8580   5789   5401     66   -955     83       C  
ATOM   1968  C   LEU A1039       6.244  16.448   0.733  1.00 53.68           C  
ANISOU 1968  C   LEU A1039     8708   5961   5726    199   -992     88       C  
ATOM   1969  O   LEU A1039       5.880  16.111   1.804  1.00 53.25           O  
ANISOU 1969  O   LEU A1039     8539   5946   5748    288   -986     50       O  
ATOM   1970  CB  LEU A1039       7.909  15.071  -0.418  1.00 51.60           C  
ANISOU 1970  CB  LEU A1039     8552   5709   5346     -7   -801     -5       C  
ATOM   1971  CG  LEU A1039       8.463  14.622   0.919  1.00 55.08           C  
ANISOU 1971  CG  LEU A1039     8855   6168   5906     78   -736    -78       C  
ATOM   1972  CD1 LEU A1039       7.783  13.396   1.431  1.00 54.42           C  
ANISOU 1972  CD1 LEU A1039     8671   6162   5844    117   -750    -97       C  
ATOM   1973  CD2 LEU A1039       9.928  14.458   0.891  1.00 57.21           C  
ANISOU 1973  CD2 LEU A1039     9128   6391   6218     15   -605   -145       C  
ATOM   1974  N   ASN A1040       6.535  17.702   0.452  1.00 48.85           N  
ANISOU 1974  N   ASN A1040     8170   5268   5124    196  -1017    130       N  
ATOM   1975  CA  ASN A1040       6.338  18.804   1.404  1.00 47.90           C  
ANISOU 1975  CA  ASN A1040     7990   5090   5118    309  -1038    129       C  
ATOM   1976  C   ASN A1040       4.876  18.970   1.838  1.00 51.85           C  
ANISOU 1976  C   ASN A1040     8393   5598   5708    416  -1138    176       C  
ATOM   1977  O   ASN A1040       4.605  19.314   2.993  1.00 51.35           O  
ANISOU 1977  O   ASN A1040     8238   5524   5750    511  -1108    125       O  
ATOM   1978  CB  ASN A1040       6.883  20.123   0.838  1.00 46.27           C  
ANISOU 1978  CB  ASN A1040     7895   4780   4904    274  -1050    175       C  
ATOM   1979  CG  ASN A1040       8.400  20.188   0.852  1.00 54.71           C  
ANISOU 1979  CG  ASN A1040     9020   5828   5940    199   -926    102       C  
ATOM   1980  OD1 ASN A1040       9.041  19.579   1.691  1.00 46.35           O  
ANISOU 1980  OD1 ASN A1040     7883   4809   4919    215   -842     18       O  
ATOM   1981  ND2 ASN A1040       8.975  20.945  -0.073  1.00 46.25           N  
ANISOU 1981  ND2 ASN A1040     8079   4686   4807    111   -921    143       N  
ATOM   1982  N   ALA A1041       3.946  18.710   0.915  1.00 48.62           N  
ANISOU 1982  N   ALA A1041     8006   5207   5261    384  -1250    269       N  
ATOM   1983  CA  ALA A1041       2.512  18.707   1.227  1.00 48.50           C  
ANISOU 1983  CA  ALA A1041     7877   5202   5351    477  -1349    319       C  
ATOM   1984  C   ALA A1041       2.185  17.557   2.170  1.00 50.76           C  
ANISOU 1984  C   ALA A1041     8047   5585   5654    521  -1286    231       C  
ATOM   1985  O   ALA A1041       1.314  17.681   3.026  1.00 50.58           O  
ANISOU 1985  O   ALA A1041     7905   5563   5751    619  -1293    211       O  
ATOM   1986  CB  ALA A1041       1.686  18.602  -0.046  1.00 50.36           C  
ANISOU 1986  CB  ALA A1041     8167   5440   5529    406  -1503    453       C  
ATOM   1987  N   ALA A1042       2.889  16.438   2.000  1.00 45.98           N  
ANISOU 1987  N   ALA A1042     7478   5054   4940    440  -1215    177       N  
ATOM   1988  CA  ALA A1042       2.821  15.307   2.938  1.00 44.25           C  
ANISOU 1988  CA  ALA A1042     7162   4918   4732    467  -1147     95       C  
ATOM   1989  C   ALA A1042       3.308  15.729   4.323  1.00 46.90           C  
ANISOU 1989  C   ALA A1042     7437   5236   5146    534  -1065     14       C  
ATOM   1990  O   ALA A1042       2.635  15.463   5.322  1.00 45.75           O  
ANISOU 1990  O   ALA A1042     7195   5127   5062    596  -1052    -26       O  
ATOM   1991  CB  ALA A1042       3.638  14.130   2.426  1.00 44.23           C  
ANISOU 1991  CB  ALA A1042     7211   4966   4628    365  -1079     57       C  
ATOM   1992  N   LYS A1043       4.467  16.395   4.367  1.00 43.16           N  
ANISOU 1992  N   LYS A1043     7029   4707   4663    505  -1009    -11       N  
ATOM   1993  CA  LYS A1043       5.009  16.947   5.618  1.00 42.44           C  
ANISOU 1993  CA  LYS A1043     6904   4591   4630    542   -944    -80       C  
ATOM   1994  C   LYS A1043       3.992  17.860   6.333  1.00 46.94           C  
ANISOU 1994  C   LYS A1043     7417   5117   5302    633   -961    -87       C  
ATOM   1995  O   LYS A1043       3.727  17.702   7.536  1.00 46.52           O  
ANISOU 1995  O   LYS A1043     7298   5094   5286    662   -911   -156       O  
ATOM   1996  CB  LYS A1043       6.310  17.714   5.370  1.00 44.65           C  
ANISOU 1996  CB  LYS A1043     7268   4804   4892    493   -898    -89       C  
ATOM   1997  CG  LYS A1043       7.488  16.836   4.986  1.00 54.37           C  
ANISOU 1997  CG  LYS A1043     8525   6063   6071    406   -840   -113       C  
ATOM   1998  CD  LYS A1043       8.728  17.675   4.670  1.00 62.69           C  
ANISOU 1998  CD  LYS A1043     9655   7042   7123    353   -790   -122       C  
ATOM   1999  CE  LYS A1043       9.902  16.823   4.188  1.00 69.40           C  
ANISOU 1999  CE  LYS A1043    10513   7898   7955    264   -714   -151       C  
ATOM   2000  NZ  LYS A1043      10.618  16.122   5.293  1.00 75.61           N  
ANISOU 2000  NZ  LYS A1043    11201   8718   8809    264   -678   -198       N  
ATOM   2001  N   SER A1044       3.407  18.788   5.586  1.00 43.85           N  
ANISOU 2001  N   SER A1044     7050   4647   4962    668  -1027    -16       N  
ATOM   2002  CA  SER A1044       2.422  19.719   6.146  1.00 44.29           C  
ANISOU 2002  CA  SER A1044     7036   4630   5161    761  -1034    -20       C  
ATOM   2003  C   SER A1044       1.199  19.036   6.796  1.00 48.18           C  
ANISOU 2003  C   SER A1044     7404   5180   5721    816  -1033    -50       C  
ATOM   2004  O   SER A1044       0.761  19.446   7.882  1.00 47.94           O  
ANISOU 2004  O   SER A1044     7308   5122   5786    865   -956   -128       O  
ATOM   2005  CB  SER A1044       2.002  20.706   5.069  1.00 48.62           C  
ANISOU 2005  CB  SER A1044     7624   5076   5773    783  -1135     92       C  
ATOM   2006  OG  SER A1044       3.163  21.298   4.488  1.00 56.99           O  
ANISOU 2006  OG  SER A1044     8809   6086   6757    717  -1123    112       O  
ATOM   2007  N   GLU A1045       0.679  17.989   6.154  1.00 44.46           N  
ANISOU 2007  N   GLU A1045     6909   4789   5196    792  -1103      1       N  
ATOM   2008  CA  GLU A1045      -0.370  17.145   6.751  1.00 44.39           C  
ANISOU 2008  CA  GLU A1045     6785   4851   5229    826  -1095    -31       C  
ATOM   2009  C   GLU A1045       0.106  16.433   8.035  1.00 48.22           C  
ANISOU 2009  C   GLU A1045     7252   5410   5658    798   -985   -143       C  
ATOM   2010  O   GLU A1045      -0.607  16.395   9.039  1.00 48.11           O  
ANISOU 2010  O   GLU A1045     7160   5408   5713    831   -925   -210       O  
ATOM   2011  CB  GLU A1045      -0.845  16.092   5.743  1.00 45.59           C  
ANISOU 2011  CB  GLU A1045     6937   5080   5307    783  -1191     45       C  
ATOM   2012  CG  GLU A1045      -2.060  15.281   6.181  1.00 55.89           C  
ANISOU 2012  CG  GLU A1045     8119   6450   6667    817  -1203     29       C  
ATOM   2013  CD  GLU A1045      -3.355  15.772   5.555  1.00 80.31           C  
ANISOU 2013  CD  GLU A1045    11126   9490   9897    873  -1319    124       C  
ATOM   2014  OE1 GLU A1045      -3.757  16.931   5.822  1.00 76.69           O  
ANISOU 2014  OE1 GLU A1045    10614   8923   9601    950  -1315    132       O  
ATOM   2015  OE2 GLU A1045      -3.974  14.986   4.794  1.00 75.69           O  
ANISOU 2015  OE2 GLU A1045    10524   8965   9268    834  -1417    193       O  
ATOM   2016  N   LEU A1046       1.299  15.850   7.986  1.00 44.30           N  
ANISOU 2016  N   LEU A1046     6829   4959   5046    724   -961   -157       N  
ATOM   2017  CA  LEU A1046       1.927  15.257   9.167  1.00 43.48           C  
ANISOU 2017  CA  LEU A1046     6716   4910   4893    681   -887   -235       C  
ATOM   2018  C   LEU A1046       2.095  16.307  10.277  1.00 48.60           C  
ANISOU 2018  C   LEU A1046     7374   5502   5591    692   -811   -308       C  
ATOM   2019  O   LEU A1046       1.822  16.026  11.437  1.00 48.66           O  
ANISOU 2019  O   LEU A1046     7349   5549   5592    670   -753   -379       O  
ATOM   2020  CB  LEU A1046       3.287  14.658   8.777  1.00 42.67           C  
ANISOU 2020  CB  LEU A1046     6676   4830   4707    607   -884   -220       C  
ATOM   2021  CG  LEU A1046       4.146  13.920   9.800  1.00 46.62           C  
ANISOU 2021  CG  LEU A1046     7164   5378   5169    547   -844   -264       C  
ATOM   2022  CD1 LEU A1046       3.382  12.828  10.504  1.00 46.38           C  
ANISOU 2022  CD1 LEU A1046     7067   5431   5125    541   -844   -284       C  
ATOM   2023  CD2 LEU A1046       5.365  13.351   9.082  1.00 48.57           C  
ANISOU 2023  CD2 LEU A1046     7446   5620   5388    490   -844   -235       C  
ATOM   2024  N   ASP A1047       2.531  17.515   9.909  1.00 45.73           N  
ANISOU 2024  N   ASP A1047     7065   5043   5267    710   -808   -295       N  
ATOM   2025  CA  ASP A1047       2.715  18.608  10.871  1.00 46.01           C  
ANISOU 2025  CA  ASP A1047     7122   5010   5351    711   -727   -371       C  
ATOM   2026  C   ASP A1047       1.367  19.054  11.477  1.00 50.41           C  
ANISOU 2026  C   ASP A1047     7597   5525   6031    776   -671   -425       C  
ATOM   2027  O   ASP A1047       1.229  19.136  12.698  1.00 50.28           O  
ANISOU 2027  O   ASP A1047     7574   5519   6012    739   -574   -525       O  
ATOM   2028  CB  ASP A1047       3.441  19.800  10.225  1.00 48.38           C  
ANISOU 2028  CB  ASP A1047     7499   5207   5678    718   -738   -338       C  
ATOM   2029  CG  ASP A1047       4.873  19.456   9.725  1.00 60.76           C  
ANISOU 2029  CG  ASP A1047     9143   6802   7143    642   -761   -305       C  
ATOM   2030  OD1 ASP A1047       5.337  18.294   9.875  1.00 61.43           O  
ANISOU 2030  OD1 ASP A1047     9211   6974   7155    591   -771   -305       O  
ATOM   2031  OD2 ASP A1047       5.540  20.359   9.158  1.00 66.44           O  
ANISOU 2031  OD2 ASP A1047     9932   7443   7870    633   -765   -279       O  
ATOM   2032  N   LYS A1048       0.366  19.327  10.644  1.00 47.38           N  
ANISOU 2032  N   LYS A1048     7149   5090   5763    859   -731   -360       N  
ATOM   2033  CA  LYS A1048      -0.977  19.659  11.165  1.00 48.04           C  
ANISOU 2033  CA  LYS A1048     7121   5124   6007    928   -675   -409       C  
ATOM   2034  C   LYS A1048      -1.436  18.676  12.252  1.00 51.21           C  
ANISOU 2034  C   LYS A1048     7474   5627   6357    883   -595   -499       C  
ATOM   2035  O   LYS A1048      -1.905  19.078  13.319  1.00 51.20           O  
ANISOU 2035  O   LYS A1048     7443   5590   6422    875   -467   -611       O  
ATOM   2036  CB  LYS A1048      -2.015  19.678  10.037  1.00 50.84           C  
ANISOU 2036  CB  LYS A1048     7390   5442   6485   1009   -793   -295       C  
ATOM   2037  CG  LYS A1048      -3.376  20.249  10.453  1.00 62.56           C  
ANISOU 2037  CG  LYS A1048     8733   6836   8203   1097   -739   -331       C  
ATOM   2038  CD  LYS A1048      -4.264  20.540   9.239  1.00 73.11           C  
ANISOU 2038  CD  LYS A1048     9985   8102   9690   1173   -893   -185       C  
ATOM   2039  CE  LYS A1048      -5.641  21.085   9.660  1.00 85.36           C  
ANISOU 2039  CE  LYS A1048    11360   9546  11526   1269   -839   -217       C  
ATOM   2040  NZ  LYS A1048      -6.418  21.673   8.521  1.00 94.90           N  
ANISOU 2040  NZ  LYS A1048    12480  10646  12930   1347  -1007    -54       N  
ATOM   2041  N   ALA A1049      -1.278  17.385  11.958  1.00 46.97           N  
ANISOU 2041  N   ALA A1049     6940   5209   5700    843   -664   -453       N  
ATOM   2042  CA  ALA A1049      -1.776  16.300  12.805  1.00 46.46           C  
ANISOU 2042  CA  ALA A1049     6829   5244   5580    798   -617   -511       C  
ATOM   2043  C   ALA A1049      -0.949  16.145  14.087  1.00 49.25           C  
ANISOU 2043  C   ALA A1049     7260   5640   5813    691   -531   -599       C  
ATOM   2044  O   ALA A1049      -1.502  16.101  15.186  1.00 49.16           O  
ANISOU 2044  O   ALA A1049     7230   5644   5807    648   -427   -696       O  
ATOM   2045  CB  ALA A1049      -1.783  14.991  12.015  1.00 46.31           C  
ANISOU 2045  CB  ALA A1049     6796   5324   5476    783   -721   -428       C  
ATOM   2046  N   ILE A1050       0.374  16.061  13.929  1.00 44.64           N  
ANISOU 2046  N   ILE A1050     6764   5073   5124    635   -578   -562       N  
ATOM   2047  CA  ILE A1050       1.286  15.907  15.060  1.00 43.87           C  
ANISOU 2047  CA  ILE A1050     6741   5015   4915    519   -536   -614       C  
ATOM   2048  C   ILE A1050       1.363  17.218  15.851  1.00 49.27           C  
ANISOU 2048  C   ILE A1050     7475   5612   5632    492   -430   -709       C  
ATOM   2049  O   ILE A1050       1.417  17.196  17.085  1.00 49.89           O  
ANISOU 2049  O   ILE A1050     7599   5719   5638    386   -352   -793       O  
ATOM   2050  CB  ILE A1050       2.698  15.425  14.607  1.00 45.32           C  
ANISOU 2050  CB  ILE A1050     6977   5228   5016    471   -623   -538       C  
ATOM   2051  CG1 ILE A1050       2.610  14.060  13.931  1.00 44.53           C  
ANISOU 2051  CG1 ILE A1050     6829   5201   4890    482   -698   -467       C  
ATOM   2052  CG2 ILE A1050       3.636  15.303  15.785  1.00 45.24           C  
ANISOU 2052  CG2 ILE A1050     7029   5250   4910    344   -610   -570       C  
ATOM   2053  CD1 ILE A1050       2.048  12.973  14.818  1.00 50.99           C  
ANISOU 2053  CD1 ILE A1050     7610   6105   5656    428   -686   -492       C  
ATOM   2054  N   GLY A1051       1.343  18.347  15.137  1.00 45.95           N  
ANISOU 2054  N   GLY A1051     7056   5084   5318    573   -426   -694       N  
ATOM   2055  CA  GLY A1051       1.322  19.683  15.750  1.00 46.81           C  
ANISOU 2055  CA  GLY A1051     7206   5086   5494    563   -313   -787       C  
ATOM   2056  C   GLY A1051       2.691  20.338  15.853  1.00 50.09           C  
ANISOU 2056  C   GLY A1051     7729   5470   5834    493   -326   -783       C  
ATOM   2057  O   GLY A1051       2.936  21.147  16.753  1.00 50.00           O  
ANISOU 2057  O   GLY A1051     7782   5408   5807    420   -226   -879       O  
ATOM   2058  N   ARG A1052       3.586  20.001  14.928  1.00 45.73           N  
ANISOU 2058  N   ARG A1052     7196   4943   5236    505   -438   -680       N  
ATOM   2059  CA  ARG A1052       4.936  20.532  14.966  1.00 45.33           C  
ANISOU 2059  CA  ARG A1052     7232   4866   5126    436   -455   -669       C  
ATOM   2060  C   ARG A1052       5.680  20.268  13.671  1.00 48.56           C  
ANISOU 2060  C   ARG A1052     7645   5276   5531    473   -553   -562       C  
ATOM   2061  O   ARG A1052       5.332  19.341  12.940  1.00 47.75           O  
ANISOU 2061  O   ARG A1052     7491   5226   5425    514   -615   -499       O  
ATOM   2062  CB  ARG A1052       5.704  19.908  16.121  1.00 45.18           C  
ANISOU 2062  CB  ARG A1052     7257   4932   4977    294   -458   -700       C  
ATOM   2063  CG  ARG A1052       5.929  18.393  16.011  1.00 50.47           C  
ANISOU 2063  CG  ARG A1052     7880   5714   5585    267   -549   -627       C  
ATOM   2064  CD  ARG A1052       6.925  17.929  17.077  1.00 51.31           C  
ANISOU 2064  CD  ARG A1052     8031   5879   5583    117   -587   -625       C  
ATOM   2065  NE  ARG A1052       7.449  16.597  16.806  1.00 52.19           N  
ANISOU 2065  NE  ARG A1052     8090   6064   5678     99   -686   -534       N  
ATOM   2066  CZ  ARG A1052       8.434  16.323  15.952  1.00 61.55           C  
ANISOU 2066  CZ  ARG A1052     9250   7232   6905    120   -749   -459       C  
ATOM   2067  NH1 ARG A1052       9.031  17.286  15.257  1.00 44.67           N  
ANISOU 2067  NH1 ARG A1052     7144   5017   4810    152   -732   -457       N  
ATOM   2068  NH2 ARG A1052       8.827  15.061  15.795  1.00 48.44           N  
ANISOU 2068  NH2 ARG A1052     7529   5621   5254    102   -819   -390       N  
ATOM   2069  N   ASN A1053       6.714  21.072  13.410  1.00 45.19           N  
ANISOU 2069  N   ASN A1053     7284   4787   5098    442   -555   -551       N  
ATOM   2070  CA  ASN A1053       7.515  20.975  12.185  1.00 44.49           C  
ANISOU 2070  CA  ASN A1053     7216   4683   5005    455   -619   -466       C  
ATOM   2071  C   ASN A1053       8.409  19.723  12.222  1.00 48.06           C  
ANISOU 2071  C   ASN A1053     7642   5225   5392    387   -667   -430       C  
ATOM   2072  O   ASN A1053       9.559  19.780  12.649  1.00 47.76           O  
ANISOU 2072  O   ASN A1053     7630   5190   5328    305   -672   -434       O  
ATOM   2073  CB  ASN A1053       8.340  22.265  11.983  1.00 44.10           C  
ANISOU 2073  CB  ASN A1053     7244   4534   4977    434   -592   -476       C  
ATOM   2074  CG  ASN A1053       9.067  22.321  10.617  1.00 60.72           C  
ANISOU 2074  CG  ASN A1053     9385   6608   7080    439   -637   -396       C  
ATOM   2075  OD1 ASN A1053       8.638  23.033   9.699  1.00 52.10           O  
ANISOU 2075  OD1 ASN A1053     8323   5439   6034    496   -653   -352       O  
ATOM   2076  ND2 ASN A1053      10.181  21.588  10.495  1.00 50.23           N  
ANISOU 2076  ND2 ASN A1053     8050   5328   5705    369   -656   -376       N  
ATOM   2077  N   THR A1054       7.860  18.601  11.760  1.00 44.31           N  
ANISOU 2077  N   THR A1054     7111   4815   4910    419   -704   -391       N  
ATOM   2078  CA  THR A1054       8.521  17.297  11.848  1.00 43.62           C  
ANISOU 2078  CA  THR A1054     6981   4801   4793    364   -740   -360       C  
ATOM   2079  C   THR A1054       9.704  17.120  10.896  1.00 47.49           C  
ANISOU 2079  C   THR A1054     7484   5260   5301    335   -750   -316       C  
ATOM   2080  O   THR A1054      10.648  16.398  11.210  1.00 46.96           O  
ANISOU 2080  O   THR A1054     7378   5215   5249    274   -766   -301       O  
ATOM   2081  CB  THR A1054       7.525  16.147  11.568  1.00 52.54           C  
ANISOU 2081  CB  THR A1054     8049   5998   5915    405   -764   -339       C  
ATOM   2082  OG1 THR A1054       6.908  16.340  10.283  1.00 53.93           O  
ANISOU 2082  OG1 THR A1054     8237   6144   6111    470   -778   -301       O  
ATOM   2083  CG2 THR A1054       6.457  16.096  12.636  1.00 51.07           C  
ANISOU 2083  CG2 THR A1054     7836   5852   5715    414   -742   -390       C  
ATOM   2084  N   ASN A1055       9.650  17.765   9.737  1.00 44.29           N  
ANISOU 2084  N   ASN A1055     7129   4795   4905    370   -738   -294       N  
ATOM   2085  CA  ASN A1055      10.569  17.459   8.642  1.00 43.96           C  
ANISOU 2085  CA  ASN A1055     7107   4726   4870    332   -724   -263       C  
ATOM   2086  C   ASN A1055      10.446  15.990   8.168  1.00 47.02           C  
ANISOU 2086  C   ASN A1055     7439   5170   5256    321   -728   -244       C  
ATOM   2087  O   ASN A1055      11.403  15.414   7.636  1.00 46.38           O  
ANISOU 2087  O   ASN A1055     7343   5070   5207    269   -692   -240       O  
ATOM   2088  CB  ASN A1055      12.024  17.804   9.015  1.00 44.65           C  
ANISOU 2088  CB  ASN A1055     7197   4775   4993    262   -699   -277       C  
ATOM   2089  CG  ASN A1055      12.263  19.307   9.150  1.00 62.88           C  
ANISOU 2089  CG  ASN A1055     9582   7011   7298    260   -681   -296       C  
ATOM   2090  OD1 ASN A1055      11.888  20.082   8.273  1.00 56.18           O  
ANISOU 2090  OD1 ASN A1055     8802   6107   6438    292   -672   -279       O  
ATOM   2091  ND2 ASN A1055      12.896  19.719  10.260  1.00 53.02           N  
ANISOU 2091  ND2 ASN A1055     8327   5760   6059    210   -684   -326       N  
ATOM   2092  N   GLY A1056       9.253  15.412   8.339  1.00 43.20           N  
ANISOU 2092  N   GLY A1056     6921   4744   4748    366   -759   -238       N  
ATOM   2093  CA  GLY A1056       8.990  14.022   7.950  1.00 42.50           C  
ANISOU 2093  CA  GLY A1056     6784   4709   4654    355   -762   -225       C  
ATOM   2094  C   GLY A1056       9.559  12.951   8.884  1.00 45.58           C  
ANISOU 2094  C   GLY A1056     7092   5140   5088    319   -766   -230       C  
ATOM   2095  O   GLY A1056       9.641  11.788   8.506  1.00 44.72           O  
ANISOU 2095  O   GLY A1056     6940   5051   5002    301   -754   -220       O  
ATOM   2096  N   VAL A1057       9.952  13.331  10.097  1.00 42.26           N  
ANISOU 2096  N   VAL A1057     6655   4724   4680    298   -789   -241       N  
ATOM   2097  CA  VAL A1057      10.388  12.358  11.104  1.00 41.93           C  
ANISOU 2097  CA  VAL A1057     6539   4720   4671    250   -825   -223       C  
ATOM   2098  C   VAL A1057       9.580  12.491  12.412  1.00 45.74           C  
ANISOU 2098  C   VAL A1057     7027   5261   5090    241   -859   -242       C  
ATOM   2099  O   VAL A1057       9.442  13.596  12.948  1.00 45.26           O  
ANISOU 2099  O   VAL A1057     7021   5184   4992    235   -846   -278       O  
ATOM   2100  CB  VAL A1057      11.892  12.504  11.397  1.00 45.87           C  
ANISOU 2100  CB  VAL A1057     7011   5169   5249    186   -835   -203       C  
ATOM   2101  CG1 VAL A1057      12.302  11.611  12.579  1.00 45.72           C  
ANISOU 2101  CG1 VAL A1057     6917   5184   5269    124   -909   -159       C  
ATOM   2102  CG2 VAL A1057      12.704  12.174  10.142  1.00 45.60           C  
ANISOU 2102  CG2 VAL A1057     6957   5072   5297    181   -772   -199       C  
ATOM   2103  N   ILE A1058       9.026  11.374  12.903  1.00 42.08           N  
ANISOU 2103  N   ILE A1058     6515   4860   4614    230   -888   -227       N  
ATOM   2104  CA  ILE A1058       8.329  11.360  14.200  1.00 42.20           C  
ANISOU 2104  CA  ILE A1058     6542   4933   4560    191   -908   -250       C  
ATOM   2105  C   ILE A1058       8.883  10.298  15.151  1.00 45.55           C  
ANISOU 2105  C   ILE A1058     6922   5393   4992    101   -979   -196       C  
ATOM   2106  O   ILE A1058       9.468   9.291  14.722  1.00 45.00           O  
ANISOU 2106  O   ILE A1058     6785   5308   5005     99  -1009   -141       O  
ATOM   2107  CB  ILE A1058       6.785  11.149  14.068  1.00 45.15           C  
ANISOU 2107  CB  ILE A1058     6908   5353   4894    252   -876   -286       C  
ATOM   2108  CG1 ILE A1058       6.458   9.801  13.418  1.00 44.69           C  
ANISOU 2108  CG1 ILE A1058     6791   5328   4861    276   -894   -248       C  
ATOM   2109  CG2 ILE A1058       6.142  12.292  13.291  1.00 46.16           C  
ANISOU 2109  CG2 ILE A1058     7070   5435   5033    334   -830   -321       C  
ATOM   2110  CD1 ILE A1058       4.997   9.450  13.496  1.00 49.89           C  
ANISOU 2110  CD1 ILE A1058     7429   6043   5484    315   -877   -276       C  
ATOM   2111  N   THR A1059       8.656  10.522  16.446  1.00 41.94           N  
ANISOU 2111  N   THR A1059     6507   4977   4451     17  -1003   -212       N  
ATOM   2112  CA  THR A1059       9.078   9.585  17.477  1.00 41.73           C  
ANISOU 2112  CA  THR A1059     6459   4989   4409    -93  -1094   -146       C  
ATOM   2113  C   THR A1059       8.112   8.405  17.505  1.00 44.55           C  
ANISOU 2113  C   THR A1059     6776   5401   4749    -72  -1095   -136       C  
ATOM   2114  O   THR A1059       6.986   8.497  17.003  1.00 42.88           O  
ANISOU 2114  O   THR A1059     6567   5211   4512      8  -1022   -195       O  
ATOM   2115  CB  THR A1059       9.143  10.240  18.889  1.00 48.84           C  
ANISOU 2115  CB  THR A1059     7447   5920   5190   -228  -1119   -169       C  
ATOM   2116  OG1 THR A1059       7.821  10.471  19.385  1.00 49.30           O  
ANISOU 2116  OG1 THR A1059     7560   6026   5147   -231  -1036   -257       O  
ATOM   2117  CG2 THR A1059       9.917  11.561  18.865  1.00 46.62           C  
ANISOU 2117  CG2 THR A1059     7219   5583   4910   -249  -1099   -201       C  
ATOM   2118  N   LYS A1060       8.575   7.300  18.090  1.00 41.64           N  
ANISOU 2118  N   LYS A1060     6365   5049   4409   -150  -1187    -50       N  
ATOM   2119  CA  LYS A1060       7.737   6.132  18.353  1.00 41.24           C  
ANISOU 2119  CA  LYS A1060     6287   5051   4331   -160  -1200    -31       C  
ATOM   2120  C   LYS A1060       6.493   6.521  19.153  1.00 46.30           C  
ANISOU 2120  C   LYS A1060     7005   5762   4826   -201  -1140   -112       C  
ATOM   2121  O   LYS A1060       5.441   5.896  19.008  1.00 45.28           O  
ANISOU 2121  O   LYS A1060     6855   5675   4675   -164  -1099   -140       O  
ATOM   2122  CB  LYS A1060       8.539   5.080  19.120  1.00 43.97           C  
ANISOU 2122  CB  LYS A1060     6591   5391   4726   -266  -1330     89       C  
ATOM   2123  CG  LYS A1060       7.822   3.725  19.295  1.00 55.13           C  
ANISOU 2123  CG  LYS A1060     7967   6842   6138   -277  -1353    126       C  
ATOM   2124  CD  LYS A1060       8.232   2.984  20.578  1.00 61.50           C  
ANISOU 2124  CD  LYS A1060     8786   7667   6912   -433  -1493    237       C  
ATOM   2125  CE  LYS A1060       9.742   2.722  20.650  1.00 69.27           C  
ANISOU 2125  CE  LYS A1060     9693   8570   8058   -476  -1621    364       C  
ATOM   2126  NZ  LYS A1060      10.475   3.865  21.273  1.00 77.90           N  
ANISOU 2126  NZ  LYS A1060    10851   9660   9088   -566  -1671    368       N  
ATOM   2127  N   ASP A1061       6.621   7.548  19.997  1.00 44.77           N  
ANISOU 2127  N   ASP A1061     6897   5574   4540   -286  -1124   -158       N  
ATOM   2128  CA  ASP A1061       5.505   8.041  20.812  1.00 45.79           C  
ANISOU 2128  CA  ASP A1061     7102   5751   4545   -341  -1033   -259       C  
ATOM   2129  C   ASP A1061       4.421   8.748  20.000  1.00 49.44           C  
ANISOU 2129  C   ASP A1061     7542   6196   5049   -199   -905   -361       C  
ATOM   2130  O   ASP A1061       3.227   8.565  20.275  1.00 49.91           O  
ANISOU 2130  O   ASP A1061     7598   6294   5073   -194   -830   -426       O  
ATOM   2131  CB  ASP A1061       6.005   8.987  21.916  1.00 49.05           C  
ANISOU 2131  CB  ASP A1061     7625   6162   4849   -490  -1033   -293       C  
ATOM   2132  CG  ASP A1061       6.488   8.247  23.156  1.00 64.27           C  
ANISOU 2132  CG  ASP A1061     9610   8138   6672   -688  -1151   -209       C  
ATOM   2133  OD1 ASP A1061       7.445   8.754  23.798  1.00 66.74           O  
ANISOU 2133  OD1 ASP A1061     9986   8437   6934   -815  -1226   -171       O  
ATOM   2134  OD2 ASP A1061       5.914   7.172  23.492  1.00 70.58           O  
ANISOU 2134  OD2 ASP A1061    10393   8987   7435   -728  -1178   -174       O  
ATOM   2135  N   GLU A1062       4.822   9.571  19.031  1.00 44.48           N  
ANISOU 2135  N   GLU A1062     6896   5504   4502    -95   -885   -370       N  
ATOM   2136  CA  GLU A1062       3.845  10.234  18.166  1.00 43.71           C  
ANISOU 2136  CA  GLU A1062     6769   5376   4462     37   -797   -436       C  
ATOM   2137  C   GLU A1062       3.135   9.245  17.226  1.00 47.16           C  
ANISOU 2137  C   GLU A1062     7125   5840   4953    129   -813   -401       C  
ATOM   2138  O   GLU A1062       1.953   9.415  16.909  1.00 47.04           O  
ANISOU 2138  O   GLU A1062     7075   5833   4966    199   -756   -449       O  
ATOM   2139  CB  GLU A1062       4.508  11.358  17.378  1.00 44.76           C  
ANISOU 2139  CB  GLU A1062     6920   5430   4656    105   -787   -438       C  
ATOM   2140  CG  GLU A1062       4.565  12.664  18.150  1.00 54.29           C  
ANISOU 2140  CG  GLU A1062     8203   6597   5827     52   -717   -518       C  
ATOM   2141  CD  GLU A1062       5.835  13.453  17.905  1.00 71.02           C  
ANISOU 2141  CD  GLU A1062    10363   8657   7963     34   -751   -491       C  
ATOM   2142  OE1 GLU A1062       6.762  12.919  17.247  1.00 53.10           O  
ANISOU 2142  OE1 GLU A1062     8059   6380   5738     49   -828   -409       O  
ATOM   2143  OE2 GLU A1062       5.904  14.613  18.394  1.00 68.66           O  
ANISOU 2143  OE2 GLU A1062    10132   8313   7644     -2   -687   -561       O  
ATOM   2144  N   ALA A1063       3.862   8.211  16.807  1.00 43.01           N  
ANISOU 2144  N   ALA A1063     6565   5323   4455    119   -889   -319       N  
ATOM   2145  CA  ALA A1063       3.320   7.133  15.985  1.00 42.23           C  
ANISOU 2145  CA  ALA A1063     6402   5249   4394    176   -903   -288       C  
ATOM   2146  C   ALA A1063       2.153   6.385  16.664  1.00 46.40           C  
ANISOU 2146  C   ALA A1063     6910   5848   4870    143   -881   -315       C  
ATOM   2147  O   ALA A1063       1.156   6.058  16.018  1.00 45.50           O  
ANISOU 2147  O   ALA A1063     6751   5756   4781    210   -856   -332       O  
ATOM   2148  CB  ALA A1063       4.438   6.163  15.613  1.00 42.50           C  
ANISOU 2148  CB  ALA A1063     6403   5259   4485    151   -967   -207       C  
ATOM   2149  N   GLU A1064       2.294   6.115  17.962  1.00 43.70           N  
ANISOU 2149  N   GLU A1064     6609   5543   4454     26   -896   -314       N  
ATOM   2150  CA  GLU A1064       1.217   5.524  18.768  1.00 43.75           C  
ANISOU 2150  CA  GLU A1064     6616   5614   4392    -33   -859   -352       C  
ATOM   2151  C   GLU A1064       0.001   6.461  18.931  1.00 46.92           C  
ANISOU 2151  C   GLU A1064     7017   6018   4793      7   -741   -465       C  
ATOM   2152  O   GLU A1064      -1.138   5.993  19.060  1.00 46.56           O  
ANISOU 2152  O   GLU A1064     6930   6014   4746     14   -690   -505       O  
ATOM   2153  CB  GLU A1064       1.751   5.094  20.149  1.00 45.89           C  
ANISOU 2153  CB  GLU A1064     6955   5919   4562   -200   -910   -317       C  
ATOM   2154  CG  GLU A1064       0.755   4.243  20.968  1.00 58.02           C  
ANISOU 2154  CG  GLU A1064     8504   7526   6017   -287   -881   -340       C  
ATOM   2155  CD  GLU A1064       1.434   3.398  22.046  1.00 79.75           C  
ANISOU 2155  CD  GLU A1064    11314  10306   8683   -456   -985   -249       C  
ATOM   2156  OE1 GLU A1064       1.103   2.193  22.163  1.00 78.10           O  
ANISOU 2156  OE1 GLU A1064    11076  10130   8468   -487  -1027   -195       O  
ATOM   2157  OE2 GLU A1064       2.305   3.934  22.767  1.00 71.98           O  
ANISOU 2157  OE2 GLU A1064    10403   9307   7638   -564  -1037   -222       O  
ATOM   2158  N   LYS A1065       0.230   7.773  18.923  1.00 43.22           N  
ANISOU 2158  N   LYS A1065     6583   5494   4345     34   -692   -516       N  
ATOM   2159  CA  LYS A1065      -0.879   8.729  18.973  1.00 43.60           C  
ANISOU 2159  CA  LYS A1065     6608   5512   4444     89   -573   -620       C  
ATOM   2160  C   LYS A1065      -1.660   8.776  17.664  1.00 46.77           C  
ANISOU 2160  C   LYS A1065     6913   5891   4967    240   -584   -601       C  
ATOM   2161  O   LYS A1065      -2.890   8.769  17.674  1.00 47.00           O  
ANISOU 2161  O   LYS A1065     6875   5929   5055    279   -520   -653       O  
ATOM   2162  CB  LYS A1065      -0.387  10.126  19.330  1.00 46.82           C  
ANISOU 2162  CB  LYS A1065     7082   5853   4856     72   -515   -680       C  
ATOM   2163  CG  LYS A1065      -1.491  11.177  19.370  1.00 59.42           C  
ANISOU 2163  CG  LYS A1065     8640   7389   6549    137   -381   -789       C  
ATOM   2164  CD  LYS A1065      -1.081  12.357  20.252  1.00 69.57           C  
ANISOU 2164  CD  LYS A1065    10018   8618   7798     53   -285   -880       C  
ATOM   2165  CE  LYS A1065      -2.160  13.449  20.284  1.00 81.59           C  
ANISOU 2165  CE  LYS A1065    11489  10053   9460    126   -131   -998       C  
ATOM   2166  NZ  LYS A1065      -1.964  14.410  21.417  1.00 92.15           N  
ANISOU 2166  NZ  LYS A1065    12928  11341  10743      2      8  -1123       N  
ATOM   2167  N   LEU A1066      -0.950   8.832  16.539  1.00 42.24           N  
ANISOU 2167  N   LEU A1066     6333   5284   4431    310   -664   -525       N  
ATOM   2168  CA  LEU A1066      -1.603   8.761  15.228  1.00 41.53           C  
ANISOU 2168  CA  LEU A1066     6176   5181   4425    419   -700   -487       C  
ATOM   2169  C   LEU A1066      -2.453   7.487  15.126  1.00 44.81           C  
ANISOU 2169  C   LEU A1066     6529   5669   4828    410   -718   -471       C  
ATOM   2170  O   LEU A1066      -3.570   7.494  14.586  1.00 45.28           O  
ANISOU 2170  O   LEU A1066     6515   5733   4957    473   -714   -477       O  
ATOM   2171  CB  LEU A1066      -0.566   8.796  14.101  1.00 40.77           C  
ANISOU 2171  CB  LEU A1066     6110   5048   4333    449   -774   -412       C  
ATOM   2172  CG  LEU A1066       0.044  10.160  13.790  1.00 45.74           C  
ANISOU 2172  CG  LEU A1066     6787   5596   4999    485   -763   -418       C  
ATOM   2173  CD1 LEU A1066       1.205  10.034  12.796  1.00 45.20           C  
ANISOU 2173  CD1 LEU A1066     6758   5497   4919    484   -819   -352       C  
ATOM   2174  CD2 LEU A1066      -1.031  11.125  13.274  1.00 48.61           C  
ANISOU 2174  CD2 LEU A1066     7103   5906   5461    576   -743   -435       C  
ATOM   2175  N   PHE A1067      -1.898   6.409  15.668  1.00 39.78           N  
ANISOU 2175  N   PHE A1067     5920   5082   4114    325   -746   -443       N  
ATOM   2176  CA  PHE A1067      -2.493   5.091  15.647  1.00 39.06           C  
ANISOU 2176  CA  PHE A1067     5786   5054   4000    299   -765   -422       C  
ATOM   2177  C   PHE A1067      -3.754   4.994  16.514  1.00 44.11           C  
ANISOU 2177  C   PHE A1067     6387   5738   4634    269   -688   -495       C  
ATOM   2178  O   PHE A1067      -4.754   4.385  16.112  1.00 43.38           O  
ANISOU 2178  O   PHE A1067     6224   5682   4576    298   -687   -496       O  
ATOM   2179  CB  PHE A1067      -1.443   4.083  16.124  1.00 40.23           C  
ANISOU 2179  CB  PHE A1067     5975   5221   4091    212   -818   -365       C  
ATOM   2180  CG  PHE A1067      -1.983   2.713  16.329  1.00 41.59           C  
ANISOU 2180  CG  PHE A1067     6114   5451   4238    167   -833   -343       C  
ATOM   2181  CD1 PHE A1067      -2.383   1.952  15.235  1.00 44.09           C  
ANISOU 2181  CD1 PHE A1067     6381   5776   4594    217   -857   -315       C  
ATOM   2182  CD2 PHE A1067      -2.098   2.182  17.609  1.00 43.94           C  
ANISOU 2182  CD2 PHE A1067     6442   5791   4461     57   -823   -351       C  
ATOM   2183  CE1 PHE A1067      -2.884   0.691  15.403  1.00 45.01           C  
ANISOU 2183  CE1 PHE A1067     6470   5940   4691    174   -866   -299       C  
ATOM   2184  CE2 PHE A1067      -2.603   0.920  17.794  1.00 46.93           C  
ANISOU 2184  CE2 PHE A1067     6795   6218   4819     12   -838   -327       C  
ATOM   2185  CZ  PHE A1067      -3.001   0.165  16.682  1.00 44.83           C  
ANISOU 2185  CZ  PHE A1067     6469   5956   4607     77   -857   -303       C  
ATOM   2186  N   ASN A1068      -3.688   5.579  17.709  1.00 41.93           N  
ANISOU 2186  N   ASN A1068     6162   5458   4312    195   -615   -561       N  
ATOM   2187  CA  ASN A1068      -4.825   5.577  18.628  1.00 43.02           C  
ANISOU 2187  CA  ASN A1068     6276   5627   4443    143   -507   -654       C  
ATOM   2188  C   ASN A1068      -6.021   6.379  18.108  1.00 48.30           C  
ANISOU 2188  C   ASN A1068     6842   6253   5257    253   -436   -714       C  
ATOM   2189  O   ASN A1068      -7.162   6.024  18.391  1.00 48.95           O  
ANISOU 2189  O   ASN A1068     6852   6364   5382    245   -368   -767       O  
ATOM   2190  CB  ASN A1068      -4.393   6.075  20.016  1.00 44.15           C  
ANISOU 2190  CB  ASN A1068     6523   5769   4484      8   -432   -720       C  
ATOM   2191  CG  ASN A1068      -3.684   4.991  20.845  1.00 57.60           C  
ANISOU 2191  CG  ASN A1068     8309   7533   6045   -140   -503   -658       C  
ATOM   2192  OD1 ASN A1068      -3.415   3.878  20.369  1.00 47.36           O  
ANISOU 2192  OD1 ASN A1068     6982   6265   4746   -127   -602   -566       O  
ATOM   2193  ND2 ASN A1068      -3.402   5.316  22.105  1.00 49.29           N  
ANISOU 2193  ND2 ASN A1068     7361   6492   4876   -293   -452   -707       N  
ATOM   2194  N   GLN A1069      -5.753   7.445  17.349  1.00 44.98           N  
ANISOU 2194  N   GLN A1069     6408   5756   4926    350   -457   -698       N  
ATOM   2195  CA  GLN A1069      -6.791   8.151  16.581  1.00 45.64           C  
ANISOU 2195  CA  GLN A1069     6377   5783   5179    470   -442   -709       C  
ATOM   2196  C   GLN A1069      -7.371   7.261  15.481  1.00 49.64           C  
ANISOU 2196  C   GLN A1069     6807   6334   5721    523   -547   -625       C  
ATOM   2197  O   GLN A1069      -8.594   7.104  15.380  1.00 50.05           O  
ANISOU 2197  O   GLN A1069     6747   6395   5875    558   -522   -647       O  
ATOM   2198  CB  GLN A1069      -6.232   9.421  15.938  1.00 46.96           C  
ANISOU 2198  CB  GLN A1069     6566   5855   5422    549   -470   -684       C  
ATOM   2199  CG  GLN A1069      -6.120  10.603  16.886  1.00 60.20           C  
ANISOU 2199  CG  GLN A1069     8281   7458   7133    523   -339   -789       C  
ATOM   2200  CD  GLN A1069      -5.036  11.578  16.477  1.00 74.06           C  
ANISOU 2200  CD  GLN A1069    10114   9143   8883    552   -381   -755       C  
ATOM   2201  OE1 GLN A1069      -4.452  11.453  15.392  1.00 67.48           O  
ANISOU 2201  OE1 GLN A1069     9296   8308   8037    601   -502   -652       O  
ATOM   2202  NE2 GLN A1069      -4.744  12.546  17.351  1.00 62.99           N  
ANISOU 2202  NE2 GLN A1069     8770   7681   7481    506   -269   -847       N  
ATOM   2203  N   ASP A1070      -6.490   6.697  14.653  1.00 45.50           N  
ANISOU 2203  N   ASP A1070     6339   5831   5118    521   -657   -535       N  
ATOM   2204  CA  ASP A1070      -6.909   5.777  13.580  1.00 45.06           C  
ANISOU 2204  CA  ASP A1070     6239   5819   5064    541   -750   -461       C  
ATOM   2205  C   ASP A1070      -7.766   4.635  14.127  1.00 48.75           C  
ANISOU 2205  C   ASP A1070     6652   6363   5505    488   -718   -491       C  
ATOM   2206  O   ASP A1070      -8.781   4.283  13.527  1.00 48.14           O  
ANISOU 2206  O   ASP A1070     6487   6310   5495    518   -753   -470       O  
ATOM   2207  CB  ASP A1070      -5.699   5.199  12.830  1.00 45.86           C  
ANISOU 2207  CB  ASP A1070     6426   5926   5072    513   -827   -389       C  
ATOM   2208  CG  ASP A1070      -5.036   6.211  11.906  1.00 56.67           C  
ANISOU 2208  CG  ASP A1070     7839   7223   6469    565   -875   -346       C  
ATOM   2209  OD1 ASP A1070      -5.737   7.087  11.348  1.00 58.26           O  
ANISOU 2209  OD1 ASP A1070     7990   7379   6765    632   -902   -329       O  
ATOM   2210  OD2 ASP A1070      -3.802   6.122  11.727  1.00 61.97           O  
ANISOU 2210  OD2 ASP A1070     8590   7877   7080    534   -888   -322       O  
ATOM   2211  N   VAL A1071      -7.345   4.075  15.263  1.00 45.45           N  
ANISOU 2211  N   VAL A1071     6293   5984   4991    396   -660   -531       N  
ATOM   2212  CA  VAL A1071      -8.089   3.015  15.941  1.00 45.81           C  
ANISOU 2212  CA  VAL A1071     6307   6101   4998    326   -618   -562       C  
ATOM   2213  C   VAL A1071      -9.463   3.509  16.409  1.00 51.89           C  
ANISOU 2213  C   VAL A1071     6974   6865   5875    347   -517   -649       C  
ATOM   2214  O   VAL A1071     -10.454   2.787  16.288  1.00 52.30           O  
ANISOU 2214  O   VAL A1071     6945   6964   5964    340   -512   -655       O  
ATOM   2215  CB  VAL A1071      -7.294   2.415  17.143  1.00 49.34           C  
ANISOU 2215  CB  VAL A1071     6854   6580   5312    202   -591   -573       C  
ATOM   2216  CG1 VAL A1071      -8.205   1.555  18.027  1.00 49.69           C  
ANISOU 2216  CG1 VAL A1071     6876   6690   5315    113   -524   -621       C  
ATOM   2217  CG2 VAL A1071      -6.100   1.609  16.649  1.00 47.95           C  
ANISOU 2217  CG2 VAL A1071     6737   6404   5077    182   -693   -479       C  
ATOM   2218  N   ASP A1072      -9.534   4.735  16.922  1.00 49.10           N  
ANISOU 2218  N   ASP A1072     6618   6447   5592    370   -427   -721       N  
ATOM   2219  CA  ASP A1072     -10.838   5.318  17.287  1.00 50.27           C  
ANISOU 2219  CA  ASP A1072     6645   6561   5896    403   -309   -813       C  
ATOM   2220  C   ASP A1072     -11.734   5.687  16.076  1.00 53.59           C  
ANISOU 2220  C   ASP A1072     6917   6938   6505    531   -390   -754       C  
ATOM   2221  O   ASP A1072     -12.952   5.761  16.232  1.00 54.59           O  
ANISOU 2221  O   ASP A1072     6908   7052   6782    556   -322   -805       O  
ATOM   2222  CB  ASP A1072     -10.651   6.517  18.221  1.00 53.34           C  
ANISOU 2222  CB  ASP A1072     7074   6875   6317    380   -167   -921       C  
ATOM   2223  CG  ASP A1072     -10.232   6.102  19.637  1.00 66.61           C  
ANISOU 2223  CG  ASP A1072     8881   8606   7819    214    -63  -1000       C  
ATOM   2224  OD1 ASP A1072      -9.898   7.002  20.444  1.00 68.66           O  
ANISOU 2224  OD1 ASP A1072     9213   8815   8059    158     49  -1088       O  
ATOM   2225  OD2 ASP A1072     -10.240   4.886  19.954  1.00 72.46           O  
ANISOU 2225  OD2 ASP A1072     9659   9436   8438    125    -96   -970       O  
ATOM   2226  N   ALA A1073     -11.151   5.885  14.887  1.00 48.39           N  
ANISOU 2226  N   ALA A1073     6285   6258   5842    595   -535   -645       N  
ATOM   2227  CA  ALA A1073     -11.941   6.062  13.645  1.00 48.39           C  
ANISOU 2227  CA  ALA A1073     6171   6234   5983    681   -653   -558       C  
ATOM   2228  C   ALA A1073     -12.540   4.760  13.114  1.00 51.84           C  
ANISOU 2228  C   ALA A1073     6565   6761   6372    642   -733   -506       C  
ATOM   2229  O   ALA A1073     -13.670   4.736  12.618  1.00 52.18           O  
ANISOU 2229  O   ALA A1073     6471   6800   6556    681   -781   -476       O  
ATOM   2230  CB  ALA A1073     -11.101   6.716  12.546  1.00 48.56           C  
ANISOU 2230  CB  ALA A1073     6261   6202   5986    731   -777   -459       C  
ATOM   2231  N   ALA A1074     -11.758   3.688  13.183  1.00 47.44           N  
ANISOU 2231  N   ALA A1074     6119   6275   5631    563   -754   -489       N  
ATOM   2232  CA  ALA A1074     -12.181   2.386  12.694  1.00 46.97           C  
ANISOU 2232  CA  ALA A1074     6042   6295   5510    513   -818   -447       C  
ATOM   2233  C   ALA A1074     -13.251   1.786  13.607  1.00 51.99           C  
ANISOU 2233  C   ALA A1074     6588   6980   6188    470   -720   -524       C  
ATOM   2234  O   ALA A1074     -14.188   1.138  13.134  1.00 52.52           O  
ANISOU 2234  O   ALA A1074     6564   7089   6302    462   -768   -497       O  
ATOM   2235  CB  ALA A1074     -10.986   1.453  12.580  1.00 46.31           C  
ANISOU 2235  CB  ALA A1074     6095   6248   5253    445   -847   -415       C  
ATOM   2236  N   VAL A1075     -13.121   2.003  14.912  1.00 48.63           N  
ANISOU 2236  N   VAL A1075     6193   6549   5737    427   -581   -620       N  
ATOM   2237  CA  VAL A1075     -14.153   1.564  15.853  1.00 49.21           C  
ANISOU 2237  CA  VAL A1075     6189   6659   5850    370   -459   -710       C  
ATOM   2238  C   VAL A1075     -15.448   2.335  15.609  1.00 54.39           C  
ANISOU 2238  C   VAL A1075     6660   7260   6744    452   -424   -742       C  
ATOM   2239  O   VAL A1075     -16.516   1.734  15.565  1.00 54.97           O  
ANISOU 2239  O   VAL A1075     6618   7373   6895    437   -413   -755       O  
ATOM   2240  CB  VAL A1075     -13.718   1.718  17.334  1.00 53.29           C  
ANISOU 2240  CB  VAL A1075     6804   7177   6269    274   -309   -813       C  
ATOM   2241  CG1 VAL A1075     -14.895   1.398  18.280  1.00 54.43           C  
ANISOU 2241  CG1 VAL A1075     6868   7349   6465    203   -156   -923       C  
ATOM   2242  CG2 VAL A1075     -12.514   0.820  17.641  1.00 51.70           C  
ANISOU 2242  CG2 VAL A1075     6761   7024   5857    182   -366   -760       C  
ATOM   2243  N   ARG A1076     -15.340   3.656  15.437  1.00 51.18           N  
ANISOU 2243  N   ARG A1076     6218   6756   6470    540   -411   -749       N  
ATOM   2244  CA  ARG A1076     -16.498   4.506  15.110  1.00 52.49           C  
ANISOU 2244  CA  ARG A1076     6189   6841   6914    635   -397   -759       C  
ATOM   2245  C   ARG A1076     -17.252   4.057  13.839  1.00 57.02           C  
ANISOU 2245  C   ARG A1076     6645   7440   7579    679   -580   -633       C  
ATOM   2246  O   ARG A1076     -18.482   4.093  13.805  1.00 57.90           O  
ANISOU 2246  O   ARG A1076     6572   7531   7896    709   -562   -647       O  
ATOM   2247  CB  ARG A1076     -16.084   5.991  14.998  1.00 52.30           C  
ANISOU 2247  CB  ARG A1076     6164   6694   7015    724   -380   -763       C  
ATOM   2248  CG  ARG A1076     -16.229   6.772  16.311  1.00 60.93           C  
ANISOU 2248  CG  ARG A1076     7249   7715   8185    699   -145   -926       C  
ATOM   2249  CD  ARG A1076     -15.972   8.266  16.157  1.00 67.39           C  
ANISOU 2249  CD  ARG A1076     8043   8394   9167    793   -119   -935       C  
ATOM   2250  NE  ARG A1076     -14.637   8.650  16.639  1.00 73.73           N  
ANISOU 2250  NE  ARG A1076     9044   9195   9774    740    -81   -966       N  
ATOM   2251  CZ  ARG A1076     -13.598   9.022  15.879  1.00 82.41           C  
ANISOU 2251  CZ  ARG A1076    10247  10280  10785    779   -220   -863       C  
ATOM   2252  NH1 ARG A1076     -13.682   9.084  14.552  1.00 66.09           N  
ANISOU 2252  NH1 ARG A1076     8128   8198   8783    861   -410   -720       N  
ATOM   2253  NH2 ARG A1076     -12.452   9.344  16.465  1.00 66.07           N  
ANISOU 2253  NH2 ARG A1076     8342   8209   8555    719   -168   -905       N  
ATOM   2254  N   GLY A1077     -16.514   3.638  12.811  1.00 52.84           N  
ANISOU 2254  N   GLY A1077     6222   6952   6901    669   -748   -516       N  
ATOM   2255  CA  GLY A1077     -17.110   3.137  11.570  1.00 53.35           C  
ANISOU 2255  CA  GLY A1077     6219   7052   6998    671   -930   -395       C  
ATOM   2256  C   GLY A1077     -17.728   1.748  11.698  1.00 58.15           C  
ANISOU 2256  C   GLY A1077     6799   7765   7530    586   -924   -411       C  
ATOM   2257  O   GLY A1077     -18.751   1.458  11.061  1.00 58.48           O  
ANISOU 2257  O   GLY A1077     6709   7826   7685    587  -1021   -352       O  
ATOM   2258  N   ILE A1078     -17.087   0.888  12.498  1.00 54.51           N  
ANISOU 2258  N   ILE A1078     6464   7366   6881    505   -824   -480       N  
ATOM   2259  CA  ILE A1078     -17.603  -0.451  12.816  1.00 54.52           C  
ANISOU 2259  CA  ILE A1078     6453   7458   6802    415   -792   -509       C  
ATOM   2260  C   ILE A1078     -18.939  -0.384  13.544  1.00 60.00           C  
ANISOU 2260  C   ILE A1078     6972   8151   7676    417   -678   -593       C  
ATOM   2261  O   ILE A1078     -19.831  -1.179  13.269  1.00 60.54           O  
ANISOU 2261  O   ILE A1078     6947   8273   7781    379   -717   -575       O  
ATOM   2262  CB  ILE A1078     -16.613  -1.254  13.699  1.00 56.56           C  
ANISOU 2262  CB  ILE A1078     6878   7762   6850    328   -704   -559       C  
ATOM   2263  CG1 ILE A1078     -15.437  -1.764  12.865  1.00 55.82           C  
ANISOU 2263  CG1 ILE A1078     6931   7681   6598    306   -815   -475       C  
ATOM   2264  CG2 ILE A1078     -17.300  -2.452  14.348  1.00 57.49           C  
ANISOU 2264  CG2 ILE A1078     6968   7955   6919    234   -633   -609       C  
ATOM   2265  CD1 ILE A1078     -14.329  -2.394  13.695  1.00 61.96           C  
ANISOU 2265  CD1 ILE A1078     7853   8475   7214    236   -751   -502       C  
ATOM   2266  N   LEU A1079     -19.065   0.557  14.477  1.00 56.91           N  
ANISOU 2266  N   LEU A1079     6536   7691   7398    451   -525   -692       N  
ATOM   2267  CA  LEU A1079     -20.308   0.752  15.234  1.00 58.26           C  
ANISOU 2267  CA  LEU A1079     6533   7836   7769    450   -374   -798       C  
ATOM   2268  C   LEU A1079     -21.440   1.395  14.419  1.00 63.48           C  
ANISOU 2268  C   LEU A1079     6960   8430   8731    550   -464   -737       C  
ATOM   2269  O   LEU A1079     -22.564   1.491  14.909  1.00 65.06           O  
ANISOU 2269  O   LEU A1079     6978   8600   9140    555   -349   -815       O  
ATOM   2270  CB  LEU A1079     -20.055   1.599  16.495  1.00 58.81           C  
ANISOU 2270  CB  LEU A1079     6641   7839   7865    436   -157   -941       C  
ATOM   2271  CG  LEU A1079     -19.209   0.970  17.602  1.00 62.27           C  
ANISOU 2271  CG  LEU A1079     7281   8341   8036    304    -44  -1015       C  
ATOM   2272  CD1 LEU A1079     -18.946   1.991  18.689  1.00 63.19           C  
ANISOU 2272  CD1 LEU A1079     7446   8383   8180    280    150  -1146       C  
ATOM   2273  CD2 LEU A1079     -19.872  -0.277  18.180  1.00 64.66           C  
ANISOU 2273  CD2 LEU A1079     7573   8734   8259    186     27  -1063       C  
ATOM   2274  N   ARG A1080     -21.142   1.869  13.211  1.00 59.28           N  
ANISOU 2274  N   ARG A1080     6428   7864   8231    621   -666   -597       N  
ATOM   2275  CA  ARG A1080     -22.169   2.391  12.304  1.00 60.65           C  
ANISOU 2275  CA  ARG A1080     6390   7978   8677    698   -809   -496       C  
ATOM   2276  C   ARG A1080     -22.421   1.433  11.140  1.00 63.45           C  
ANISOU 2276  C   ARG A1080     6755   8424   8930    641  -1029   -360       C  
ATOM   2277  O   ARG A1080     -23.407   1.570  10.417  1.00 64.60           O  
ANISOU 2277  O   ARG A1080     6722   8547   9277    667  -1169   -265       O  
ATOM   2278  CB  ARG A1080     -21.769   3.771  11.767  1.00 61.97           C  
ANISOU 2278  CB  ARG A1080     6543   8023   8981    806   -891   -424       C  
ATOM   2279  CG  ARG A1080     -21.716   4.866  12.834  1.00 74.46           C  
ANISOU 2279  CG  ARG A1080     8079   9489  10723    868   -671   -561       C  
ATOM   2280  CD  ARG A1080     -21.497   6.242  12.210  1.00 89.41           C  
ANISOU 2280  CD  ARG A1080     9926  11245  12801    981   -767   -476       C  
ATOM   2281  NE  ARG A1080     -22.654   6.687  11.426  1.00105.34           N  
ANISOU 2281  NE  ARG A1080    11696  13182  15147   1058   -915   -360       N  
ATOM   2282  CZ  ARG A1080     -22.734   7.842  10.763  1.00123.50           C  
ANISOU 2282  CZ  ARG A1080    13907  15348  17670   1158  -1038   -251       C  
ATOM   2283  NH1 ARG A1080     -21.721   8.710  10.768  1.00111.46           N  
ANISOU 2283  NH1 ARG A1080    12525  13756  16069   1197  -1018   -253       N  
ATOM   2284  NH2 ARG A1080     -23.838   8.135  10.083  1.00112.64           N  
ANISOU 2284  NH2 ARG A1080    12292  13900  16605   1215  -1193   -129       N  
ATOM   2285  N   ASN A1081     -21.520   0.473  10.946  1.00 57.46           N  
ANISOU 2285  N   ASN A1081     6203   7759   7870    554  -1061   -346       N  
ATOM   2286  CA  ASN A1081     -21.734  -0.579   9.965  1.00 56.54           C  
ANISOU 2286  CA  ASN A1081     6120   7731   7631    471  -1225   -249       C  
ATOM   2287  C   ASN A1081     -22.580  -1.658  10.614  1.00 59.94           C  
ANISOU 2287  C   ASN A1081     6471   8239   8066    397  -1127   -327       C  
ATOM   2288  O   ASN A1081     -22.152  -2.304  11.565  1.00 58.32           O  
ANISOU 2288  O   ASN A1081     6367   8076   7715    342   -971   -430       O  
ATOM   2289  CB  ASN A1081     -20.399  -1.146   9.485  1.00 54.91           C  
ANISOU 2289  CB  ASN A1081     6159   7571   7133    408  -1273   -216       C  
ATOM   2290  CG  ASN A1081     -20.535  -1.976   8.234  1.00 75.53           C  
ANISOU 2290  CG  ASN A1081     8822  10248   9628    319  -1450   -109       C  
ATOM   2291  OD1 ASN A1081     -21.368  -2.880   8.166  1.00 71.11           O  
ANISOU 2291  OD1 ASN A1081     8189   9754   9076    251  -1471   -111       O  
ATOM   2292  ND2 ASN A1081     -19.707  -1.682   7.236  1.00 64.92           N  
ANISOU 2292  ND2 ASN A1081     7615   8885   8166    303  -1570    -23       N  
ATOM   2293  N   ALA A1082     -23.793  -1.834  10.104  1.00 58.01           N  
ANISOU 2293  N   ALA A1082     6040   8007   7996    390  -1228   -270       N  
ATOM   2294  CA  ALA A1082     -24.735  -2.801  10.660  1.00 58.31           C  
ANISOU 2294  CA  ALA A1082     5974   8111   8070    320  -1140   -341       C  
ATOM   2295  C   ALA A1082     -24.248  -4.264  10.557  1.00 60.96           C  
ANISOU 2295  C   ALA A1082     6489   8558   8117    194  -1146   -348       C  
ATOM   2296  O   ALA A1082     -24.617  -5.119  11.385  1.00 60.42           O  
ANISOU 2296  O   ALA A1082     6410   8542   8004    126  -1010   -441       O  
ATOM   2297  CB  ALA A1082     -26.076  -2.634   9.991  1.00 61.03           C  
ANISOU 2297  CB  ALA A1082     6073   8440   8675    336  -1280   -255       C  
ATOM   2298  N   LYS A1083     -23.408  -4.552   9.564  1.00 56.44           N  
ANISOU 2298  N   LYS A1083     6082   8009   7353    156  -1288   -256       N  
ATOM   2299  CA  LYS A1083     -22.894  -5.908   9.392  1.00 55.04           C  
ANISOU 2299  CA  LYS A1083     6069   7911   6931     42  -1285   -265       C  
ATOM   2300  C   LYS A1083     -21.817  -6.264  10.438  1.00 57.40           C  
ANISOU 2300  C   LYS A1083     6530   8209   7070     30  -1115   -359       C  
ATOM   2301  O   LYS A1083     -21.775  -7.396  10.938  1.00 56.38           O  
ANISOU 2301  O   LYS A1083     6464   8134   6826    -55  -1038   -408       O  
ATOM   2302  CB  LYS A1083     -22.375  -6.116   7.966  1.00 57.18           C  
ANISOU 2302  CB  LYS A1083     6465   8198   7064    -14  -1468   -152       C  
ATOM   2303  CG  LYS A1083     -23.374  -5.722   6.857  1.00 72.18           C  
ANISOU 2303  CG  LYS A1083     8228  10100   9099    -28  -1676    -30       C  
ATOM   2304  CD  LYS A1083     -23.549  -6.832   5.810  1.00 82.17           C  
ANISOU 2304  CD  LYS A1083     9581  11442  10200   -179  -1803     32       C  
ATOM   2305  CE  LYS A1083     -24.022  -6.293   4.461  1.00 91.44           C  
ANISOU 2305  CE  LYS A1083    10715  12609  11419   -223  -2051    185       C  
ATOM   2306  NZ  LYS A1083     -22.862  -5.946   3.592  1.00 97.74           N  
ANISOU 2306  NZ  LYS A1083    11724  13377  12034   -256  -2117    238       N  
ATOM   2307  N   LEU A1084     -20.970  -5.292  10.779  1.00 53.30           N  
ANISOU 2307  N   LEU A1084     6074   7625   6554    108  -1069   -375       N  
ATOM   2308  CA  LEU A1084     -19.937  -5.468  11.809  1.00 51.70           C  
ANISOU 2308  CA  LEU A1084     6014   7413   6218     92   -930   -449       C  
ATOM   2309  C   LEU A1084     -20.389  -5.089  13.240  1.00 57.12           C  
ANISOU 2309  C   LEU A1084     6628   8084   6992    100   -749   -564       C  
ATOM   2310  O   LEU A1084     -19.782  -5.540  14.214  1.00 56.24           O  
ANISOU 2310  O   LEU A1084     6630   7988   6750     40   -640   -622       O  
ATOM   2311  CB  LEU A1084     -18.691  -4.665  11.432  1.00 50.56           C  
ANISOU 2311  CB  LEU A1084     5991   7208   6010    150   -973   -409       C  
ATOM   2312  CG  LEU A1084     -18.024  -5.040  10.102  1.00 54.30           C  
ANISOU 2312  CG  LEU A1084     6577   7688   6367    119  -1113   -317       C  
ATOM   2313  CD1 LEU A1084     -17.123  -3.921   9.621  1.00 54.09           C  
ANISOU 2313  CD1 LEU A1084     6619   7592   6341    189  -1162   -274       C  
ATOM   2314  CD2 LEU A1084     -17.235  -6.337  10.212  1.00 55.16           C  
ANISOU 2314  CD2 LEU A1084     6826   7829   6302     30  -1073   -332       C  
ATOM   2315  N   LYS A1085     -21.458  -4.299  13.369  1.00 55.65           N  
ANISOU 2315  N   LYS A1085     6254   7862   7028    159   -715   -595       N  
ATOM   2316  CA  LYS A1085     -21.841  -3.685  14.665  1.00 56.43           C  
ANISOU 2316  CA  LYS A1085     6286   7921   7232    167   -515   -723       C  
ATOM   2317  C   LYS A1085     -22.054  -4.663  15.834  1.00 61.45           C  
ANISOU 2317  C   LYS A1085     6976   8619   7754     44   -357   -821       C  
ATOM   2318  O   LYS A1085     -21.300  -4.630  16.813  1.00 60.85           O  
ANISOU 2318  O   LYS A1085     7040   8538   7542    -10   -245   -883       O  
ATOM   2319  CB  LYS A1085     -23.083  -2.780  14.504  1.00 60.18           C  
ANISOU 2319  CB  LYS A1085     6515   8331   8018    250   -498   -740       C  
ATOM   2320  CG  LYS A1085     -23.195  -1.662  15.523  1.00 68.01           C  
ANISOU 2320  CG  LYS A1085     7451   9234   9157    294   -304   -863       C  
ATOM   2321  CD  LYS A1085     -24.087  -2.011  16.700  1.00 75.66           C  
ANISOU 2321  CD  LYS A1085     8335  10218  10196    213    -80  -1011       C  
ATOM   2322  CE  LYS A1085     -24.206  -0.841  17.672  1.00 82.98           C  
ANISOU 2322  CE  LYS A1085     9212  11041  11275    241    138  -1151       C  
ATOM   2323  NZ  LYS A1085     -25.481  -0.881  18.435  1.00 94.18           N  
ANISOU 2323  NZ  LYS A1085    10448  12437  12901    198    344  -1287       N  
ATOM   2324  N   PRO A1086     -23.065  -5.548  15.739  1.00 59.09           N  
ANISOU 2324  N   PRO A1086     6575   8378   7500    -15   -358   -829       N  
ATOM   2325  CA  PRO A1086     -23.371  -6.369  16.916  1.00 59.28           C  
ANISOU 2325  CA  PRO A1086     6641   8451   7431   -139   -192   -929       C  
ATOM   2326  C   PRO A1086     -22.308  -7.440  17.261  1.00 61.41           C  
ANISOU 2326  C   PRO A1086     7135   8772   7427   -240   -213   -896       C  
ATOM   2327  O   PRO A1086     -22.261  -7.908  18.403  1.00 61.13           O  
ANISOU 2327  O   PRO A1086     7182   8761   7283   -351    -79   -969       O  
ATOM   2328  CB  PRO A1086     -24.719  -7.007  16.547  1.00 62.20           C  
ANISOU 2328  CB  PRO A1086     6831   8865   7938   -168   -211   -930       C  
ATOM   2329  CG  PRO A1086     -24.675  -7.134  15.073  1.00 66.13           C  
ANISOU 2329  CG  PRO A1086     7297   9374   8456   -111   -440   -792       C  
ATOM   2330  CD  PRO A1086     -23.870  -5.952  14.567  1.00 61.21           C  
ANISOU 2330  CD  PRO A1086     6714   8677   7867      2   -519   -738       C  
ATOM   2331  N   VAL A1087     -21.467  -7.809  16.297  1.00 56.63           N  
ANISOU 2331  N   VAL A1087     6625   8172   6720   -211   -375   -788       N  
ATOM   2332  CA  VAL A1087     -20.386  -8.768  16.547  1.00 55.32           C  
ANISOU 2332  CA  VAL A1087     6649   8027   6345   -289   -400   -747       C  
ATOM   2333  C   VAL A1087     -19.292  -8.132  17.399  1.00 58.49           C  
ANISOU 2333  C   VAL A1087     7180   8384   6658   -291   -341   -769       C  
ATOM   2334  O   VAL A1087     -18.837  -8.726  18.368  1.00 57.54           O  
ANISOU 2334  O   VAL A1087     7177   8280   6405   -396   -280   -785       O  
ATOM   2335  CB  VAL A1087     -19.783  -9.319  15.234  1.00 58.34           C  
ANISOU 2335  CB  VAL A1087     7088   8410   6668   -263   -563   -642       C  
ATOM   2336  CG1 VAL A1087     -18.485 -10.073  15.501  1.00 56.80           C  
ANISOU 2336  CG1 VAL A1087     7071   8199   6311   -316   -577   -602       C  
ATOM   2337  CG2 VAL A1087     -20.792 -10.232  14.534  1.00 58.86           C  
ANISOU 2337  CG2 VAL A1087     7066   8531   6769   -310   -618   -622       C  
ATOM   2338  N   TYR A1088     -18.880  -6.923  17.036  1.00 55.28           N  
ANISOU 2338  N   TYR A1088     6757   7922   6326   -187   -369   -760       N  
ATOM   2339  CA  TYR A1088     -17.926  -6.154  17.843  1.00 55.03           C  
ANISOU 2339  CA  TYR A1088     6835   7846   6228   -191   -308   -790       C  
ATOM   2340  C   TYR A1088     -18.372  -6.080  19.307  1.00 60.16           C  
ANISOU 2340  C   TYR A1088     7506   8510   6844   -300   -130   -903       C  
ATOM   2341  O   TYR A1088     -17.594  -6.407  20.205  1.00 59.52           O  
ANISOU 2341  O   TYR A1088     7575   8438   6604   -403    -99   -902       O  
ATOM   2342  CB  TYR A1088     -17.764  -4.739  17.272  1.00 56.41           C  
ANISOU 2342  CB  TYR A1088     6950   7953   6530    -62   -337   -785       C  
ATOM   2343  CG  TYR A1088     -16.717  -3.875  17.956  1.00 57.94           C  
ANISOU 2343  CG  TYR A1088     7260   8097   6657    -61   -288   -811       C  
ATOM   2344  CD1 TYR A1088     -15.383  -3.917  17.561  1.00 58.53           C  
ANISOU 2344  CD1 TYR A1088     7459   8151   6627    -44   -391   -729       C  
ATOM   2345  CD2 TYR A1088     -17.070  -2.987  18.969  1.00 59.99           C  
ANISOU 2345  CD2 TYR A1088     7498   8323   6971    -85   -129   -924       C  
ATOM   2346  CE1 TYR A1088     -14.430  -3.115  18.161  1.00 59.32           C  
ANISOU 2346  CE1 TYR A1088     7657   8207   6673    -49   -358   -746       C  
ATOM   2347  CE2 TYR A1088     -16.116  -2.177  19.584  1.00 60.77           C  
ANISOU 2347  CE2 TYR A1088     7713   8378   7000   -101    -87   -950       C  
ATOM   2348  CZ  TYR A1088     -14.795  -2.245  19.176  1.00 67.59           C  
ANISOU 2348  CZ  TYR A1088     8697   9230   7755    -81   -212   -854       C  
ATOM   2349  OH  TYR A1088     -13.834  -1.443  19.779  1.00 68.98           O  
ANISOU 2349  OH  TYR A1088     8982   9365   7864   -104   -181   -873       O  
ATOM   2350  N   ASP A1089     -19.629  -5.686  19.533  1.00 58.05           N  
ANISOU 2350  N   ASP A1089     7087   8241   6730   -290    -14   -995       N  
ATOM   2351  CA  ASP A1089     -20.173  -5.509  20.893  1.00 59.03           C  
ANISOU 2351  CA  ASP A1089     7221   8368   6839   -407    194  -1131       C  
ATOM   2352  C   ASP A1089     -20.043  -6.751  21.781  1.00 62.35           C  
ANISOU 2352  C   ASP A1089     7777   8855   7058   -583    233  -1132       C  
ATOM   2353  O   ASP A1089     -19.954  -6.635  23.002  1.00 62.93           O  
ANISOU 2353  O   ASP A1089     7954   8932   7024   -719    374  -1215       O  
ATOM   2354  CB  ASP A1089     -21.656  -5.116  20.848  1.00 62.58           C  
ANISOU 2354  CB  ASP A1089     7454   8800   7526   -369    314  -1227       C  
ATOM   2355  CG  ASP A1089     -21.903  -3.779  20.173  1.00 73.81           C  
ANISOU 2355  CG  ASP A1089     8727  10135   9184   -207    296  -1231       C  
ATOM   2356  OD1 ASP A1089     -23.011  -3.606  19.622  1.00 76.00           O  
ANISOU 2356  OD1 ASP A1089     8794  10391   9690   -135    292  -1238       O  
ATOM   2357  OD2 ASP A1089     -21.011  -2.902  20.192  1.00 78.92           O  
ANISOU 2357  OD2 ASP A1089     9459  10726   9799   -156    278  -1220       O  
ATOM   2358  N   SER A1090     -20.049  -7.932  21.170  1.00 57.62           N  
ANISOU 2358  N   SER A1090     7184   8304   6407   -595    111  -1041       N  
ATOM   2359  CA  SER A1090     -20.066  -9.190  21.909  1.00 57.22           C  
ANISOU 2359  CA  SER A1090     7238   8307   6196   -756    137  -1030       C  
ATOM   2360  C   SER A1090     -18.679  -9.679  22.269  1.00 59.81           C  
ANISOU 2360  C   SER A1090     7760   8625   6338   -822     37   -932       C  
ATOM   2361  O   SER A1090     -18.547 -10.713  22.918  1.00 60.04           O  
ANISOU 2361  O   SER A1090     7891   8685   6234   -961     35   -899       O  
ATOM   2362  CB  SER A1090     -20.760 -10.269  21.077  1.00 60.40           C  
ANISOU 2362  CB  SER A1090     7548   8753   6647   -743     59   -981       C  
ATOM   2363  OG  SER A1090     -20.001 -10.599  19.924  1.00 66.73           O  
ANISOU 2363  OG  SER A1090     8375   9539   7439   -651   -119   -863       O  
ATOM   2364  N   LEU A1091     -17.644  -8.948  21.851  1.00 54.73           N  
ANISOU 2364  N   LEU A1091     7162   7934   5700   -727    -50   -878       N  
ATOM   2365  CA  LEU A1091     -16.273  -9.460  21.909  1.00 52.93           C  
ANISOU 2365  CA  LEU A1091     7079   7683   5349   -759   -177   -762       C  
ATOM   2366  C   LEU A1091     -15.423  -8.817  23.006  1.00 55.53           C  
ANISOU 2366  C   LEU A1091     7546   7990   5562   -849   -143   -772       C  
ATOM   2367  O   LEU A1091     -15.602  -7.647  23.372  1.00 55.45           O  
ANISOU 2367  O   LEU A1091     7522   7961   5586   -832    -41   -865       O  
ATOM   2368  CB  LEU A1091     -15.584  -9.284  20.547  1.00 51.65           C  
ANISOU 2368  CB  LEU A1091     6877   7480   5268   -604   -314   -679       C  
ATOM   2369  CG  LEU A1091     -16.127 -10.103  19.375  1.00 55.94           C  
ANISOU 2369  CG  LEU A1091     7332   8043   5882   -547   -383   -641       C  
ATOM   2370  CD1 LEU A1091     -15.438  -9.682  18.098  1.00 55.24           C  
ANISOU 2370  CD1 LEU A1091     7226   7909   5854   -419   -492   -580       C  
ATOM   2371  CD2 LEU A1091     -15.965 -11.601  19.608  1.00 58.53           C  
ANISOU 2371  CD2 LEU A1091     7727   8386   6125   -654   -419   -581       C  
ATOM   2372  N   ASP A1092     -14.484  -9.610  23.512  1.00 50.89           N  
ANISOU 2372  N   ASP A1092     7091   7396   4849   -953   -236   -670       N  
ATOM   2373  CA  ASP A1092     -13.514  -9.149  24.501  1.00 50.53           C  
ANISOU 2373  CA  ASP A1092     7190   7329   4679  -1060   -254   -642       C  
ATOM   2374  C   ASP A1092     -12.546  -8.151  23.883  1.00 52.12           C  
ANISOU 2374  C   ASP A1092     7382   7475   4946   -925   -324   -612       C  
ATOM   2375  O   ASP A1092     -12.554  -7.935  22.671  1.00 51.20           O  
ANISOU 2375  O   ASP A1092     7162   7335   4958   -759   -371   -598       O  
ATOM   2376  CB  ASP A1092     -12.739 -10.339  25.089  1.00 52.43           C  
ANISOU 2376  CB  ASP A1092     7552   7566   4804  -1198   -375   -507       C  
ATOM   2377  CG  ASP A1092     -12.136 -11.252  24.010  1.00 60.55           C  
ANISOU 2377  CG  ASP A1092     8527   8550   5931  -1087   -519   -386       C  
ATOM   2378  OD1 ASP A1092     -12.880 -12.114  23.478  1.00 60.22           O  
ANISOU 2378  OD1 ASP A1092     8414   8529   5938  -1064   -505   -393       O  
ATOM   2379  OD2 ASP A1092     -10.921 -11.113  23.716  1.00 65.03           O  
ANISOU 2379  OD2 ASP A1092     9122   9056   6529  -1033   -634   -292       O  
ATOM   2380  N   ALA A1093     -11.713  -7.550  24.723  1.00 48.11           N  
ANISOU 2380  N   ALA A1093     6993   6949   4339  -1015   -336   -599       N  
ATOM   2381  CA  ALA A1093     -10.670  -6.630  24.273  1.00 46.86           C  
ANISOU 2381  CA  ALA A1093     6843   6735   4226   -913   -407   -563       C  
ATOM   2382  C   ALA A1093      -9.783  -7.240  23.179  1.00 49.32           C  
ANISOU 2382  C   ALA A1093     7112   7001   4626   -793   -562   -435       C  
ATOM   2383  O   ALA A1093      -9.621  -6.649  22.099  1.00 48.20           O  
ANISOU 2383  O   ALA A1093     6892   6827   4596   -634   -580   -444       O  
ATOM   2384  CB  ALA A1093      -9.813  -6.198  25.445  1.00 48.25           C  
ANISOU 2384  CB  ALA A1093     7172   6904   4258  -1070   -427   -539       C  
ATOM   2385  N   VAL A1094      -9.225  -8.415  23.455  1.00 45.34           N  
ANISOU 2385  N   VAL A1094     6659   6486   4080   -878   -666   -320       N  
ATOM   2386  CA  VAL A1094      -8.268  -9.029  22.535  1.00 44.10           C  
ANISOU 2386  CA  VAL A1094     6467   6266   4025   -784   -791   -208       C  
ATOM   2387  C   VAL A1094      -8.892  -9.351  21.162  1.00 46.94           C  
ANISOU 2387  C   VAL A1094     6712   6625   4499   -643   -767   -242       C  
ATOM   2388  O   VAL A1094      -8.299  -9.054  20.120  1.00 45.06           O  
ANISOU 2388  O   VAL A1094     6431   6337   4351   -523   -807   -221       O  
ATOM   2389  CB  VAL A1094      -7.612 -10.301  23.141  1.00 48.45           C  
ANISOU 2389  CB  VAL A1094     7079   6785   4545   -906   -904    -72       C  
ATOM   2390  CG1 VAL A1094      -6.667 -10.935  22.144  1.00 47.42           C  
ANISOU 2390  CG1 VAL A1094     6890   6568   4561   -803  -1000     24       C  
ATOM   2391  CG2 VAL A1094      -6.866  -9.964  24.440  1.00 49.15           C  
ANISOU 2391  CG2 VAL A1094     7291   6870   4513  -1065   -967    -10       C  
ATOM   2392  N   ARG A1095     -10.087  -9.941  21.175  1.00 44.22           N  
ANISOU 2392  N   ARG A1095     6326   6336   4140   -676   -700   -295       N  
ATOM   2393  CA  ARG A1095     -10.792 -10.314  19.947  1.00 43.42           C  
ANISOU 2393  CA  ARG A1095     6124   6245   4128   -575   -688   -323       C  
ATOM   2394  C   ARG A1095     -11.283  -9.098  19.152  1.00 47.77           C  
ANISOU 2394  C   ARG A1095     6596   6804   4749   -449   -646   -399       C  
ATOM   2395  O   ARG A1095     -11.425  -9.166  17.934  1.00 47.23           O  
ANISOU 2395  O   ARG A1095     6467   6725   4754   -358   -679   -391       O  
ATOM   2396  CB  ARG A1095     -11.976 -11.233  20.263  1.00 43.58           C  
ANISOU 2396  CB  ARG A1095     6117   6326   4117   -658   -631   -359       C  
ATOM   2397  CG  ARG A1095     -11.590 -12.618  20.770  1.00 49.75           C  
ANISOU 2397  CG  ARG A1095     6962   7086   4853   -770   -687   -269       C  
ATOM   2398  CD  ARG A1095     -12.821 -13.534  20.853  1.00 54.55           C  
ANISOU 2398  CD  ARG A1095     7532   7752   5441   -838   -628   -310       C  
ATOM   2399  NE  ARG A1095     -12.797 -14.437  22.005  1.00 62.61           N  
ANISOU 2399  NE  ARG A1095     8643   8780   6365  -1003   -636   -258       N  
ATOM   2400  CZ  ARG A1095     -12.025 -15.517  22.118  1.00 72.80           C  
ANISOU 2400  CZ  ARG A1095     9985  10008   7666  -1056   -731   -139       C  
ATOM   2401  NH1 ARG A1095     -11.176 -15.852  21.164  1.00 59.03           N  
ANISOU 2401  NH1 ARG A1095     8209   8184   6035   -957   -804    -76       N  
ATOM   2402  NH2 ARG A1095     -12.092 -16.269  23.201  1.00 58.68           N  
ANISOU 2402  NH2 ARG A1095     8283   8228   5785  -1218   -749    -83       N  
ATOM   2403  N   ARG A1096     -11.554  -7.994  19.837  1.00 45.03           N  
ANISOU 2403  N   ARG A1096     6254   6471   4383   -457   -572   -471       N  
ATOM   2404  CA  ARG A1096     -11.842  -6.741  19.148  1.00 44.86           C  
ANISOU 2404  CA  ARG A1096     6161   6433   4452   -334   -546   -525       C  
ATOM   2405  C   ARG A1096     -10.603  -6.208  18.447  1.00 48.39           C  
ANISOU 2405  C   ARG A1096     6645   6817   4924   -251   -630   -463       C  
ATOM   2406  O   ARG A1096     -10.692  -5.648  17.357  1.00 47.90           O  
ANISOU 2406  O   ARG A1096     6527   6734   4940   -143   -659   -462       O  
ATOM   2407  CB  ARG A1096     -12.343  -5.691  20.126  1.00 45.25           C  
ANISOU 2407  CB  ARG A1096     6212   6491   4492   -370   -426   -625       C  
ATOM   2408  CG  ARG A1096     -13.737  -5.930  20.590  1.00 51.45           C  
ANISOU 2408  CG  ARG A1096     6924   7325   5301   -424   -311   -715       C  
ATOM   2409  CD  ARG A1096     -14.059  -5.008  21.715  1.00 56.31           C  
ANISOU 2409  CD  ARG A1096     7568   7934   5893   -495   -165   -826       C  
ATOM   2410  NE  ARG A1096     -15.477  -5.053  22.030  1.00 61.63           N  
ANISOU 2410  NE  ARG A1096     8137   8638   6640   -526    -27   -933       N  
ATOM   2411  CZ  ARG A1096     -16.049  -4.338  22.986  1.00 75.74           C  
ANISOU 2411  CZ  ARG A1096     9925  10415   8438   -599    149  -1063       C  
ATOM   2412  NH1 ARG A1096     -15.316  -3.506  23.736  1.00 65.54           N  
ANISOU 2412  NH1 ARG A1096     8748   9089   7065   -658    201  -1101       N  
ATOM   2413  NH2 ARG A1096     -17.357  -4.454  23.186  1.00 61.74           N  
ANISOU 2413  NH2 ARG A1096     8035   8662   6763   -622    281  -1161       N  
ATOM   2414  N   ALA A1097      -9.448  -6.367  19.088  1.00 44.80           N  
ANISOU 2414  N   ALA A1097     6285   6331   4406   -314   -675   -405       N  
ATOM   2415  CA  ALA A1097      -8.174  -6.035  18.452  1.00 43.69           C  
ANISOU 2415  CA  ALA A1097     6174   6125   4303   -248   -752   -341       C  
ATOM   2416  C   ALA A1097      -8.018  -6.840  17.153  1.00 45.68           C  
ANISOU 2416  C   ALA A1097     6385   6352   4620   -187   -803   -295       C  
ATOM   2417  O   ALA A1097      -7.611  -6.298  16.129  1.00 45.03           O  
ANISOU 2417  O   ALA A1097     6288   6232   4591   -101   -826   -289       O  
ATOM   2418  CB  ALA A1097      -7.006  -6.299  19.414  1.00 44.57           C  
ANISOU 2418  CB  ALA A1097     6375   6204   4355   -344   -809   -268       C  
ATOM   2419  N   ALA A1098      -8.374  -8.122  17.208  1.00 41.13           N  
ANISOU 2419  N   ALA A1098     5800   5794   4032   -248   -810   -270       N  
ATOM   2420  CA  ALA A1098      -8.353  -9.003  16.042  1.00 39.88           C  
ANISOU 2420  CA  ALA A1098     5614   5612   3927   -218   -835   -244       C  
ATOM   2421  C   ALA A1098      -9.294  -8.545  14.914  1.00 43.09           C  
ANISOU 2421  C   ALA A1098     5958   6053   4360   -148   -821   -294       C  
ATOM   2422  O   ALA A1098      -8.990  -8.766  13.760  1.00 42.38           O  
ANISOU 2422  O   ALA A1098     5871   5932   4300   -117   -846   -278       O  
ATOM   2423  CB  ALA A1098      -8.674 -10.425  16.454  1.00 40.78           C  
ANISOU 2423  CB  ALA A1098     5732   5737   4023   -307   -836   -215       C  
ATOM   2424  N   LEU A1099     -10.424  -7.913  15.225  1.00 39.84           N  
ANISOU 2424  N   LEU A1099     5491   5701   3948   -135   -783   -351       N  
ATOM   2425  CA  LEU A1099     -11.303  -7.387  14.157  1.00 39.56           C  
ANISOU 2425  CA  LEU A1099     5380   5687   3963    -69   -801   -374       C  
ATOM   2426  C   LEU A1099     -10.768  -6.079  13.560  1.00 42.56           C  
ANISOU 2426  C   LEU A1099     5769   6022   4381     19   -830   -366       C  
ATOM   2427  O   LEU A1099     -10.824  -5.888  12.342  1.00 41.88           O  
ANISOU 2427  O   LEU A1099     5674   5924   4317     56   -883   -342       O  
ATOM   2428  CB  LEU A1099     -12.742  -7.169  14.646  1.00 40.46           C  
ANISOU 2428  CB  LEU A1099     5399   5861   4112    -77   -750   -433       C  
ATOM   2429  CG  LEU A1099     -13.771  -6.956  13.520  1.00 45.91           C  
ANISOU 2429  CG  LEU A1099     5992   6576   4875    -31   -799   -430       C  
ATOM   2430  CD1 LEU A1099     -13.945  -8.237  12.661  1.00 45.79           C  
ANISOU 2430  CD1 LEU A1099     5992   6587   4820    -89   -847   -396       C  
ATOM   2431  CD2 LEU A1099     -15.130  -6.470  14.060  1.00 49.09           C  
ANISOU 2431  CD2 LEU A1099     6269   7016   5367    -19   -740   -491       C  
ATOM   2432  N   ILE A1100     -10.266  -5.187  14.422  1.00 38.60           N  
ANISOU 2432  N   ILE A1100     5295   5494   3875     36   -796   -386       N  
ATOM   2433  CA  ILE A1100      -9.792  -3.859  14.002  1.00 37.73           C  
ANISOU 2433  CA  ILE A1100     5194   5336   3805    116   -813   -385       C  
ATOM   2434  C   ILE A1100      -8.558  -3.983  13.102  1.00 40.11           C  
ANISOU 2434  C   ILE A1100     5565   5584   4091    132   -866   -330       C  
ATOM   2435  O   ILE A1100      -8.359  -3.182  12.179  1.00 39.33           O  
ANISOU 2435  O   ILE A1100     5471   5452   4020    189   -902   -314       O  
ATOM   2436  CB  ILE A1100      -9.475  -2.955  15.233  1.00 40.82           C  
ANISOU 2436  CB  ILE A1100     5615   5710   4184    107   -750   -429       C  
ATOM   2437  CG1 ILE A1100     -10.750  -2.634  16.015  1.00 42.06           C  
ANISOU 2437  CG1 ILE A1100     5699   5905   4379     91   -662   -508       C  
ATOM   2438  CG2 ILE A1100      -8.829  -1.645  14.826  1.00 41.20           C  
ANISOU 2438  CG2 ILE A1100     5684   5698   4271    183   -766   -424       C  
ATOM   2439  CD1 ILE A1100     -10.484  -1.941  17.341  1.00 47.06           C  
ANISOU 2439  CD1 ILE A1100     6385   6525   4971     38   -573   -571       C  
ATOM   2440  N   ASN A1101      -7.744  -4.996  13.393  1.00 35.92           N  
ANISOU 2440  N   ASN A1101     5083   5035   3529     73   -868   -299       N  
ATOM   2441  CA  ASN A1101      -6.576  -5.362  12.592  1.00 35.10           C  
ANISOU 2441  CA  ASN A1101     5030   4867   3440     74   -891   -259       C  
ATOM   2442  C   ASN A1101      -6.982  -5.739  11.168  1.00 39.97           C  
ANISOU 2442  C   ASN A1101     5643   5487   4057     75   -908   -258       C  
ATOM   2443  O   ASN A1101      -6.364  -5.302  10.189  1.00 39.82           O  
ANISOU 2443  O   ASN A1101     5665   5423   4043     95   -919   -248       O  
ATOM   2444  CB  ASN A1101      -5.855  -6.527  13.288  1.00 34.76           C  
ANISOU 2444  CB  ASN A1101     5009   4795   3403      7   -889   -223       C  
ATOM   2445  CG  ASN A1101      -4.634  -7.019  12.536  1.00 53.65           C  
ANISOU 2445  CG  ASN A1101     7429   7100   5855      6   -890   -189       C  
ATOM   2446  OD1 ASN A1101      -4.637  -7.121  11.307  1.00 50.73           O  
ANISOU 2446  OD1 ASN A1101     7070   6710   5494     17   -873   -206       O  
ATOM   2447  ND2 ASN A1101      -3.584  -7.355  13.278  1.00 40.42           N  
ANISOU 2447  ND2 ASN A1101     5764   5366   4228    -21   -907   -141       N  
ATOM   2448  N   MET A1102      -8.031  -6.548  11.050  1.00 36.99           N  
ANISOU 2448  N   MET A1102     5226   5166   3663     36   -909   -270       N  
ATOM   2449  CA  MET A1102      -8.554  -6.919   9.737  1.00 36.91           C  
ANISOU 2449  CA  MET A1102     5221   5172   3634     10   -936   -268       C  
ATOM   2450  C   MET A1102      -9.071  -5.699   8.977  1.00 42.23           C  
ANISOU 2450  C   MET A1102     5876   5858   4313     60   -993   -256       C  
ATOM   2451  O   MET A1102      -8.839  -5.565   7.769  1.00 42.03           O  
ANISOU 2451  O   MET A1102     5903   5810   4256     37  -1027   -237       O  
ATOM   2452  CB  MET A1102      -9.665  -7.940   9.873  1.00 39.36           C  
ANISOU 2452  CB  MET A1102     5482   5544   3927    -46   -933   -282       C  
ATOM   2453  CG  MET A1102      -9.207  -9.279  10.375  1.00 42.47           C  
ANISOU 2453  CG  MET A1102     5902   5914   4321   -108   -888   -281       C  
ATOM   2454  SD  MET A1102     -10.620 -10.364  10.512  1.00 47.09           S  
ANISOU 2454  SD  MET A1102     6431   6578   4882   -177   -885   -300       S  
ATOM   2455  CE  MET A1102     -10.837 -10.850   8.793  1.00 43.98           C  
ANISOU 2455  CE  MET A1102     6078   6181   4451   -235   -910   -304       C  
ATOM   2456  N   VAL A1103      -9.771  -4.817   9.684  1.00 40.03           N  
ANISOU 2456  N   VAL A1103     5526   5605   4079    118  -1000   -268       N  
ATOM   2457  CA  VAL A1103     -10.312  -3.604   9.070  1.00 41.02           C  
ANISOU 2457  CA  VAL A1103     5611   5724   4250    176  -1062   -246       C  
ATOM   2458  C   VAL A1103      -9.204  -2.696   8.564  1.00 46.47           C  
ANISOU 2458  C   VAL A1103     6381   6347   4930    211  -1075   -223       C  
ATOM   2459  O   VAL A1103      -9.320  -2.097   7.498  1.00 46.71           O  
ANISOU 2459  O   VAL A1103     6432   6360   4955    215  -1146   -181       O  
ATOM   2460  CB  VAL A1103     -11.249  -2.857  10.036  1.00 45.38           C  
ANISOU 2460  CB  VAL A1103     6057   6294   4891    234  -1035   -279       C  
ATOM   2461  CG1 VAL A1103     -11.525  -1.429   9.558  1.00 45.84           C  
ANISOU 2461  CG1 VAL A1103     6073   6310   5036    312  -1089   -251       C  
ATOM   2462  CG2 VAL A1103     -12.553  -3.650  10.197  1.00 45.69           C  
ANISOU 2462  CG2 VAL A1103     6002   6401   4958    195  -1035   -295       C  
ATOM   2463  N   PHE A1104      -8.108  -2.606   9.304  1.00 43.94           N  
ANISOU 2463  N   PHE A1104     6108   5987   4601    222  -1017   -242       N  
ATOM   2464  CA  PHE A1104      -6.932  -1.877   8.818  1.00 43.81           C  
ANISOU 2464  CA  PHE A1104     6167   5903   4576    243  -1019   -225       C  
ATOM   2465  C   PHE A1104      -6.262  -2.504   7.593  1.00 47.12           C  
ANISOU 2465  C   PHE A1104     6667   6292   4944    179  -1021   -209       C  
ATOM   2466  O   PHE A1104      -5.713  -1.790   6.768  1.00 46.79           O  
ANISOU 2466  O   PHE A1104     6686   6207   4886    182  -1040   -190       O  
ATOM   2467  CB  PHE A1104      -5.898  -1.736   9.937  1.00 45.36           C  
ANISOU 2467  CB  PHE A1104     6386   6064   4783    253   -966   -243       C  
ATOM   2468  CG  PHE A1104      -6.220  -0.663  10.924  1.00 47.60           C  
ANISOU 2468  CG  PHE A1104     6636   6351   5101    304   -949   -270       C  
ATOM   2469  CD1 PHE A1104      -5.794  -0.780  12.237  1.00 50.50           C  
ANISOU 2469  CD1 PHE A1104     7013   6721   5454    276   -905   -293       C  
ATOM   2470  CD2 PHE A1104      -6.940   0.472  10.551  1.00 50.82           C  
ANISOU 2470  CD2 PHE A1104     7003   6748   5559    366   -975   -270       C  
ATOM   2471  CE1 PHE A1104      -6.073   0.200  13.169  1.00 51.80           C  
ANISOU 2471  CE1 PHE A1104     7163   6883   5635    297   -866   -335       C  
ATOM   2472  CE2 PHE A1104      -7.221   1.457  11.489  1.00 54.24           C  
ANISOU 2472  CE2 PHE A1104     7401   7165   6042    408   -931   -311       C  
ATOM   2473  CZ  PHE A1104      -6.777   1.312  12.805  1.00 51.73           C  
ANISOU 2473  CZ  PHE A1104     7109   6856   5690    367   -865   -354       C  
ATOM   2474  N   GLN A1105      -6.278  -3.833   7.503  1.00 43.24           N  
ANISOU 2474  N   GLN A1105     6182   5815   4431    113   -989   -223       N  
ATOM   2475  CA  GLN A1105      -5.663  -4.545   6.375  1.00 42.69           C  
ANISOU 2475  CA  GLN A1105     6191   5706   4322     35   -956   -230       C  
ATOM   2476  C   GLN A1105      -6.497  -4.407   5.113  1.00 48.74           C  
ANISOU 2476  C   GLN A1105     6993   6509   5016    -22  -1021   -210       C  
ATOM   2477  O   GLN A1105      -5.982  -3.980   4.081  1.00 48.58           O  
ANISOU 2477  O   GLN A1105     7061   6452   4947    -66  -1025   -201       O  
ATOM   2478  CB  GLN A1105      -5.472  -6.032   6.684  1.00 43.18           C  
ANISOU 2478  CB  GLN A1105     6245   5758   4403    -21   -893   -255       C  
ATOM   2479  CG  GLN A1105      -5.123  -6.878   5.462  1.00 45.22           C  
ANISOU 2479  CG  GLN A1105     6580   5976   4627   -120   -837   -283       C  
ATOM   2480  CD  GLN A1105      -4.680  -8.281   5.808  1.00 58.25           C  
ANISOU 2480  CD  GLN A1105     8216   7578   6339   -164   -756   -310       C  
ATOM   2481  OE1 GLN A1105      -4.762  -8.706   6.966  1.00 53.21           O  
ANISOU 2481  OE1 GLN A1105     7513   6950   5756   -129   -764   -292       O  
ATOM   2482  NE2 GLN A1105      -4.197  -9.013   4.807  1.00 47.49           N  
ANISOU 2482  NE2 GLN A1105     6920   6153   4972   -252   -670   -353       N  
ATOM   2483  N   MET A1106      -7.768  -4.802   5.199  1.00 46.60           N  
ANISOU 2483  N   MET A1106     6659   6311   4737    -38  -1075   -199       N  
ATOM   2484  CA  MET A1106      -8.634  -4.853   4.028  1.00 47.75           C  
ANISOU 2484  CA  MET A1106     6831   6498   4814   -116  -1160   -165       C  
ATOM   2485  C   MET A1106      -9.885  -3.948   4.118  1.00 52.62           C  
ANISOU 2485  C   MET A1106     7347   7162   5482    -58  -1280   -109       C  
ATOM   2486  O   MET A1106     -10.822  -4.097   3.339  1.00 53.72           O  
ANISOU 2486  O   MET A1106     7475   7348   5590   -123  -1376    -65       O  
ATOM   2487  CB  MET A1106      -8.987  -6.318   3.682  1.00 50.45           C  
ANISOU 2487  CB  MET A1106     7195   6869   5103   -224  -1122   -198       C  
ATOM   2488  CG  MET A1106      -9.806  -7.090   4.709  1.00 53.99           C  
ANISOU 2488  CG  MET A1106     7539   7372   5602   -200  -1109   -216       C  
ATOM   2489  SD  MET A1106      -9.422  -8.872   4.694  1.00 58.00           S  
ANISOU 2489  SD  MET A1106     8094   7856   6086   -300   -999   -272       S  
ATOM   2490  CE  MET A1106     -10.265  -9.391   3.189  1.00 55.99           C  
ANISOU 2490  CE  MET A1106     7909   7649   5715   -452  -1059   -267       C  
ATOM   2491  N   GLY A1107      -9.887  -2.985   5.031  1.00 48.51           N  
ANISOU 2491  N   GLY A1107     6754   6624   5055     56  -1274   -109       N  
ATOM   2492  CA  GLY A1107     -10.936  -1.968   5.038  1.00 49.25           C  
ANISOU 2492  CA  GLY A1107     6745   6729   5239    121  -1371    -59       C  
ATOM   2493  C   GLY A1107     -12.286  -2.491   5.489  1.00 54.33           C  
ANISOU 2493  C   GLY A1107     7257   7436   5950    122  -1395    -64       C  
ATOM   2494  O   GLY A1107     -12.548  -3.703   5.486  1.00 53.90           O  
ANISOU 2494  O   GLY A1107     7210   7430   5838     47  -1367    -91       O  
ATOM   2495  N   GLU A1108     -13.155  -1.556   5.857  1.00 52.00           N  
ANISOU 2495  N   GLU A1108     6835   7132   5793    205  -1440    -42       N  
ATOM   2496  CA  GLU A1108     -14.446  -1.870   6.472  1.00 52.64           C  
ANISOU 2496  CA  GLU A1108     6762   7258   5981    222  -1436    -62       C  
ATOM   2497  C   GLU A1108     -15.395  -2.633   5.545  1.00 58.31           C  
ANISOU 2497  C   GLU A1108     7447   8037   6673    130  -1550     -5       C  
ATOM   2498  O   GLU A1108     -16.068  -3.556   5.993  1.00 58.35           O  
ANISOU 2498  O   GLU A1108     7387   8098   6685     92  -1510    -44       O  
ATOM   2499  CB  GLU A1108     -15.094  -0.579   6.971  1.00 54.82           C  
ANISOU 2499  CB  GLU A1108     6900   7482   6446    334  -1445    -55       C  
ATOM   2500  CG  GLU A1108     -16.348  -0.750   7.797  1.00 66.09           C  
ANISOU 2500  CG  GLU A1108     8153   8936   8020    362  -1394   -102       C  
ATOM   2501  CD  GLU A1108     -16.836   0.582   8.314  1.00 87.49           C  
ANISOU 2501  CD  GLU A1108    10732  11568  10941    474  -1366   -115       C  
ATOM   2502  OE1 GLU A1108     -17.886   1.074   7.845  1.00 82.62           O  
ANISOU 2502  OE1 GLU A1108     9964  10924  10503    509  -1467    -49       O  
ATOM   2503  OE2 GLU A1108     -16.138   1.157   9.172  1.00 82.03           O  
ANISOU 2503  OE2 GLU A1108    10089  10833  10248    520  -1245   -187       O  
ATOM   2504  N   THR A1109     -15.452  -2.264   4.267  1.00 56.00           N  
ANISOU 2504  N   THR A1109     7204   7733   6339     77  -1696     91       N  
ATOM   2505  CA  THR A1109     -16.306  -2.990   3.308  1.00 56.92           C  
ANISOU 2505  CA  THR A1109     7312   7911   6404    -43  -1822    155       C  
ATOM   2506  C   THR A1109     -15.927  -4.467   3.309  1.00 60.07           C  
ANISOU 2506  C   THR A1109     7813   8360   6650   -150  -1727     82       C  
ATOM   2507  O   THR A1109     -16.796  -5.333   3.396  1.00 60.32           O  
ANISOU 2507  O   THR A1109     7775   8453   6689   -206  -1740     71       O  
ATOM   2508  CB  THR A1109     -16.205  -2.444   1.838  1.00 64.48           C  
ANISOU 2508  CB  THR A1109     8368   8850   7281   -131  -1997    274       C  
ATOM   2509  OG1 THR A1109     -16.427  -1.029   1.817  1.00 65.71           O  
ANISOU 2509  OG1 THR A1109     8439   8938   7590    -28  -2090    352       O  
ATOM   2510  CG2 THR A1109     -17.236  -3.121   0.929  1.00 62.25           C  
ANISOU 2510  CG2 THR A1109     8064   8636   6954   -270  -2150    350       C  
ATOM   2511  N   GLY A1110     -14.625  -4.739   3.220  1.00 55.55           N  
ANISOU 2511  N   GLY A1110     7394   7752   5959   -175  -1628     34       N  
ATOM   2512  CA  GLY A1110     -14.111  -6.108   3.172  1.00 54.92           C  
ANISOU 2512  CA  GLY A1110     7413   7691   5764   -272  -1525    -34       C  
ATOM   2513  C   GLY A1110     -14.502  -6.956   4.374  1.00 58.88           C  
ANISOU 2513  C   GLY A1110     7825   8226   6322   -239  -1426   -101       C  
ATOM   2514  O   GLY A1110     -15.033  -8.055   4.215  1.00 58.83           O  
ANISOU 2514  O   GLY A1110     7815   8266   6270   -329  -1419   -120       O  
ATOM   2515  N   VAL A1111     -14.263  -6.439   5.577  1.00 55.17           N  
ANISOU 2515  N   VAL A1111     7290   7733   5941   -126  -1350   -137       N  
ATOM   2516  CA  VAL A1111     -14.538  -7.197   6.812  1.00 54.87           C  
ANISOU 2516  CA  VAL A1111     7190   7722   5936   -113  -1250   -198       C  
ATOM   2517  C   VAL A1111     -16.038  -7.408   7.054  1.00 60.01           C  
ANISOU 2517  C   VAL A1111     7696   8438   6666   -124  -1290   -196       C  
ATOM   2518  O   VAL A1111     -16.440  -8.349   7.752  1.00 59.40           O  
ANISOU 2518  O   VAL A1111     7586   8400   6584   -163  -1221   -241       O  
ATOM   2519  CB  VAL A1111     -13.938  -6.521   8.061  1.00 58.12           C  
ANISOU 2519  CB  VAL A1111     7585   8095   6401    -19  -1162   -237       C  
ATOM   2520  CG1 VAL A1111     -13.887  -7.509   9.203  1.00 57.49           C  
ANISOU 2520  CG1 VAL A1111     7504   8037   6304    -52  -1064   -289       C  
ATOM   2521  CG2 VAL A1111     -12.541  -5.979   7.770  1.00 57.21           C  
ANISOU 2521  CG2 VAL A1111     7583   7911   6244      8  -1147   -226       C  
ATOM   2522  N   ALA A1112     -16.855  -6.527   6.477  1.00 57.67           N  
ANISOU 2522  N   ALA A1112     7308   8148   6458    -93  -1405   -136       N  
ATOM   2523  CA  ALA A1112     -18.306  -6.662   6.534  1.00 58.45           C  
ANISOU 2523  CA  ALA A1112     7245   8298   6666   -105  -1462   -120       C  
ATOM   2524  C   ALA A1112     -18.796  -7.838   5.679  1.00 62.79           C  
ANISOU 2524  C   ALA A1112     7831   8909   7118   -242  -1530    -96       C  
ATOM   2525  O   ALA A1112     -19.900  -8.338   5.898  1.00 63.37           O  
ANISOU 2525  O   ALA A1112     7785   9035   7259   -275  -1546   -102       O  
ATOM   2526  CB  ALA A1112     -18.971  -5.370   6.106  1.00 60.30           C  
ANISOU 2526  CB  ALA A1112     7357   8498   7054    -32  -1583    -45       C  
ATOM   2527  N   GLY A1113     -17.936  -8.297   4.788  1.00 58.59           N  
ANISOU 2527  N   GLY A1113     7466   8363   6431   -328  -1546    -82       N  
ATOM   2528  CA  GLY A1113     -18.208  -9.419   3.934  1.00 58.62           C  
ANISOU 2528  CA  GLY A1113     7543   8413   6318   -478  -1586    -76       C  
ATOM   2529  C   GLY A1113     -17.864 -10.824   4.381  1.00 61.26           C  
ANISOU 2529  C   GLY A1113     7945   8756   6575   -545  -1454   -156       C  
ATOM   2530  O   GLY A1113     -18.098 -11.734   3.651  1.00 61.52           O  
ANISOU 2530  O   GLY A1113     8042   8817   6515   -675  -1476   -159       O  
ATOM   2531  N   PHE A1114     -17.275 -11.022   5.540  1.00 56.05           N  
ANISOU 2531  N   PHE A1114     7283   8065   5947   -472  -1323   -215       N  
ATOM   2532  CA  PHE A1114     -17.025 -12.370   6.016  1.00 55.15           C  
ANISOU 2532  CA  PHE A1114     7220   7950   5784   -537  -1216   -272       C  
ATOM   2533  C   PHE A1114     -18.219 -12.818   6.800  1.00 60.05           C  
ANISOU 2533  C   PHE A1114     7710   8635   6470   -545  -1204   -292       C  
ATOM   2534  O   PHE A1114     -18.087 -13.145   7.956  1.00 59.06           O  
ANISOU 2534  O   PHE A1114     7564   8504   6372   -514  -1107   -332       O  
ATOM   2535  CB  PHE A1114     -15.840 -12.389   6.957  1.00 55.43           C  
ANISOU 2535  CB  PHE A1114     7311   7919   5832   -469  -1104   -305       C  
ATOM   2536  CG  PHE A1114     -14.517 -12.242   6.286  1.00 56.03           C  
ANISOU 2536  CG  PHE A1114     7515   7917   5856   -473  -1079   -303       C  
ATOM   2537  CD1 PHE A1114     -13.742 -13.328   6.033  1.00 58.48           C  
ANISOU 2537  CD1 PHE A1114     7921   8172   6128   -545   -997   -335       C  
ATOM   2538  CD2 PHE A1114     -14.038 -11.009   5.930  1.00 57.62           C  
ANISOU 2538  CD2 PHE A1114     7735   8090   6069   -405  -1125   -272       C  
ATOM   2539  CE1 PHE A1114     -12.529 -13.180   5.460  1.00 58.89           C  
ANISOU 2539  CE1 PHE A1114     8073   8141   6162   -549   -952   -344       C  
ATOM   2540  CE2 PHE A1114     -12.839 -10.875   5.362  1.00 59.78           C  
ANISOU 2540  CE2 PHE A1114     8120   8292   6303   -415  -1088   -277       C  
ATOM   2541  CZ  PHE A1114     -12.090 -11.958   5.117  1.00 57.65           C  
ANISOU 2541  CZ  PHE A1114     7935   7967   6003   -488   -997   -317       C  
ATOM   2542  N   THR A1115     -19.366 -12.903   6.157  1.00 58.03           N  
ANISOU 2542  N   THR A1115     7375   8442   6233   -606  -1304   -260       N  
ATOM   2543  CA  THR A1115     -20.627 -13.068   6.840  1.00 58.73           C  
ANISOU 2543  CA  THR A1115     7305   8591   6420   -603  -1301   -275       C  
ATOM   2544  C   THR A1115     -20.845 -14.261   7.714  1.00 63.41           C  
ANISOU 2544  C   THR A1115     7899   9206   6990   -658  -1188   -336       C  
ATOM   2545  O   THR A1115     -21.354 -14.119   8.785  1.00 63.44           O  
ANISOU 2545  O   THR A1115     7804   9227   7073   -616  -1119   -372       O  
ATOM   2546  CB  THR A1115     -21.754 -13.151   5.875  1.00 65.65           C  
ANISOU 2546  CB  THR A1115     8102   9526   7318   -685  -1443   -220       C  
ATOM   2547  OG1 THR A1115     -21.769 -11.995   5.047  1.00 65.95           O  
ANISOU 2547  OG1 THR A1115     8118   9545   7395   -645  -1581   -139       O  
ATOM   2548  CG2 THR A1115     -22.993 -13.200   6.645  1.00 64.11           C  
ANISOU 2548  CG2 THR A1115     7720   9378   7260   -665  -1426   -240       C  
ATOM   2549  N   ASN A1116     -20.501 -15.436   7.254  1.00 60.00           N  
ANISOU 2549  N   ASN A1116     7578   8766   6452   -765  -1162   -351       N  
ATOM   2550  CA  ASN A1116     -20.623 -16.597   8.071  1.00 59.62           C  
ANISOU 2550  CA  ASN A1116     7542   8725   6385   -821  -1060   -399       C  
ATOM   2551  C   ASN A1116     -19.647 -16.624   9.237  1.00 62.60           C  
ANISOU 2551  C   ASN A1116     7976   9043   6766   -758   -952   -422       C  
ATOM   2552  O   ASN A1116     -19.999 -16.991  10.337  1.00 62.00           O  
ANISOU 2552  O   ASN A1116     7860   8986   6712   -767   -881   -450       O  
ATOM   2553  CB  ASN A1116     -20.477 -17.838   7.211  1.00 60.20           C  
ANISOU 2553  CB  ASN A1116     7723   8788   6362   -954  -1056   -410       C  
ATOM   2554  CG  ASN A1116     -21.779 -18.267   6.602  1.00 80.98           C  
ANISOU 2554  CG  ASN A1116    10277  11501   8989  -1058  -1136   -401       C  
ATOM   2555  OD1 ASN A1116     -22.817 -17.731   6.932  1.00 74.46           O  
ANISOU 2555  OD1 ASN A1116     9298  10736   8257  -1024  -1188   -386       O  
ATOM   2556  ND2 ASN A1116     -21.731 -19.246   5.725  1.00 72.78           N  
ANISOU 2556  ND2 ASN A1116     9339  10458   7855  -1193  -1140   -415       N  
ATOM   2557  N   SER A1117     -18.410 -16.230   8.967  1.00 58.34           N  
ANISOU 2557  N   SER A1117     7535   8432   6200   -708   -946   -406       N  
ATOM   2558  CA  SER A1117     -17.346 -16.257   9.943  1.00 57.08           C  
ANISOU 2558  CA  SER A1117     7436   8207   6046   -660   -870   -409       C  
ATOM   2559  C   SER A1117     -17.610 -15.340  11.097  1.00 61.15           C  
ANISOU 2559  C   SER A1117     7877   8748   6611   -586   -845   -419       C  
ATOM   2560  O   SER A1117     -17.341 -15.678  12.230  1.00 60.66           O  
ANISOU 2560  O   SER A1117     7838   8672   6539   -601   -781   -428       O  
ATOM   2561  CB  SER A1117     -16.035 -15.922   9.302  1.00 59.39           C  
ANISOU 2561  CB  SER A1117     7828   8417   6322   -623   -875   -390       C  
ATOM   2562  OG  SER A1117     -15.436 -17.078   8.839  1.00 67.48           O  
ANISOU 2562  OG  SER A1117     8939   9379   7321   -699   -828   -400       O  
ATOM   2563  N   LEU A1118     -18.133 -14.171  10.798  1.00 57.95           N  
ANISOU 2563  N   LEU A1118     7387   8371   6259   -517   -896   -415       N  
ATOM   2564  CA  LEU A1118     -18.495 -13.194  11.831  1.00 57.91           C  
ANISOU 2564  CA  LEU A1118     7301   8380   6322   -450   -851   -444       C  
ATOM   2565  C   LEU A1118     -19.641 -13.700  12.735  1.00 62.58           C  
ANISOU 2565  C   LEU A1118     7802   9030   6945   -509   -780   -494       C  
ATOM   2566  O   LEU A1118     -19.540 -13.619  13.970  1.00 62.04           O  
ANISOU 2566  O   LEU A1118     7748   8960   6865   -522   -687   -532       O  
ATOM   2567  CB  LEU A1118     -18.827 -11.818  11.213  1.00 58.32           C  
ANISOU 2567  CB  LEU A1118     7269   8428   6461   -359   -922   -425       C  
ATOM   2568  CG  LEU A1118     -17.667 -11.051  10.541  1.00 61.95           C  
ANISOU 2568  CG  LEU A1118     7820   8826   6892   -295   -973   -384       C  
ATOM   2569  CD1 LEU A1118     -18.185  -9.814   9.820  1.00 62.76           C  
ANISOU 2569  CD1 LEU A1118     7834   8926   7086   -224  -1065   -348       C  
ATOM   2570  CD2 LEU A1118     -16.562 -10.668  11.517  1.00 62.42           C  
ANISOU 2570  CD2 LEU A1118     7956   8834   6927   -253   -899   -401       C  
ATOM   2571  N   ARG A1119     -20.707 -14.249  12.146  1.00 59.81           N  
ANISOU 2571  N   ARG A1119     7368   8733   6624   -564   -819   -494       N  
ATOM   2572  CA  ARG A1119     -21.777 -14.819  12.973  1.00 60.44           C  
ANISOU 2572  CA  ARG A1119     7362   8867   6736   -632   -741   -546       C  
ATOM   2573  C   ARG A1119     -21.190 -15.853  13.932  1.00 63.54           C  
ANISOU 2573  C   ARG A1119     7874   9244   7025   -712   -656   -560       C  
ATOM   2574  O   ARG A1119     -21.545 -15.885  15.104  1.00 63.45           O  
ANISOU 2574  O   ARG A1119     7845   9251   7011   -753   -557   -607       O  
ATOM   2575  CB  ARG A1119     -22.948 -15.401  12.146  1.00 61.84           C  
ANISOU 2575  CB  ARG A1119     7437   9104   6957   -694   -808   -536       C  
ATOM   2576  CG  ARG A1119     -22.844 -16.878  11.703  1.00 71.77           C  
ANISOU 2576  CG  ARG A1119     8788  10373   8108   -810   -819   -524       C  
ATOM   2577  CD  ARG A1119     -24.228 -17.541  11.601  1.00 80.76           C  
ANISOU 2577  CD  ARG A1119     9807  11583   9294   -898   -825   -546       C  
ATOM   2578  NE  ARG A1119     -25.164 -16.764  10.783  1.00 88.56           N  
ANISOU 2578  NE  ARG A1119    10641  12608  10400   -864   -936   -516       N  
ATOM   2579  CZ  ARG A1119     -25.164 -16.722   9.450  1.00101.25           C  
ANISOU 2579  CZ  ARG A1119    12269  14223  11979   -891  -1078   -453       C  
ATOM   2580  NH1 ARG A1119     -24.273 -17.416   8.745  1.00 86.16           N  
ANISOU 2580  NH1 ARG A1119    10530  12283   9926   -951  -1099   -434       N  
ATOM   2581  NH2 ARG A1119     -26.057 -15.969   8.815  1.00 88.67           N  
ANISOU 2581  NH2 ARG A1119    10524  12657  10509   -866  -1199   -405       N  
ATOM   2582  N   MET A1120     -20.271 -16.674  13.439  1.00 59.36           N  
ANISOU 2582  N   MET A1120     7466   8670   6417   -744   -691   -517       N  
ATOM   2583  CA  MET A1120     -19.608 -17.656  14.283  1.00 58.79           C  
ANISOU 2583  CA  MET A1120     7501   8560   6275   -815   -636   -504       C  
ATOM   2584  C   MET A1120     -18.884 -16.968  15.452  1.00 62.35           C  
ANISOU 2584  C   MET A1120     8003   8981   6705   -785   -590   -502       C  
ATOM   2585  O   MET A1120     -19.009 -17.395  16.599  1.00 62.37           O  
ANISOU 2585  O   MET A1120     8042   8995   6662   -865   -527   -513       O  
ATOM   2586  CB  MET A1120     -18.650 -18.528  13.456  1.00 60.46           C  
ANISOU 2586  CB  MET A1120     7817   8701   6454   -837   -674   -460       C  
ATOM   2587  CG  MET A1120     -19.349 -19.479  12.462  1.00 64.42           C  
ANISOU 2587  CG  MET A1120     8302   9229   6945   -914   -697   -471       C  
ATOM   2588  SD  MET A1120     -18.193 -20.347  11.362  1.00 68.05           S  
ANISOU 2588  SD  MET A1120     8886   9586   7382   -945   -706   -448       S  
ATOM   2589  CE  MET A1120     -19.280 -21.457  10.474  1.00 65.66           C  
ANISOU 2589  CE  MET A1120     8568   9334   7047  -1073   -713   -480       C  
ATOM   2590  N   LEU A1121     -18.163 -15.886  15.173  1.00 58.17           N  
ANISOU 2590  N   LEU A1121     7486   8416   6199   -688   -624   -488       N  
ATOM   2591  CA  LEU A1121     -17.499 -15.123  16.244  1.00 57.61           C  
ANISOU 2591  CA  LEU A1121     7465   8320   6105   -668   -586   -491       C  
ATOM   2592  C   LEU A1121     -18.524 -14.503  17.213  1.00 62.69           C  
ANISOU 2592  C   LEU A1121     8033   9020   6766   -696   -491   -569       C  
ATOM   2593  O   LEU A1121     -18.280 -14.421  18.414  1.00 62.55           O  
ANISOU 2593  O   LEU A1121     8081   9000   6684   -762   -426   -586       O  
ATOM   2594  CB  LEU A1121     -16.582 -14.035  15.663  1.00 56.80           C  
ANISOU 2594  CB  LEU A1121     7382   8167   6031   -558   -638   -466       C  
ATOM   2595  CG  LEU A1121     -15.417 -14.508  14.778  1.00 60.54           C  
ANISOU 2595  CG  LEU A1121     7935   8570   6498   -535   -702   -405       C  
ATOM   2596  CD1 LEU A1121     -14.718 -13.335  14.087  1.00 59.89           C  
ANISOU 2596  CD1 LEU A1121     7859   8449   6447   -433   -745   -393       C  
ATOM   2597  CD2 LEU A1121     -14.410 -15.364  15.560  1.00 62.44           C  
ANISOU 2597  CD2 LEU A1121     8271   8749   6704   -597   -698   -351       C  
ATOM   2598  N   GLN A1122     -19.674 -14.092  16.685  1.00 60.16           N  
ANISOU 2598  N   GLN A1122     7575   8744   6540   -658   -481   -615       N  
ATOM   2599  CA  GLN A1122     -20.748 -13.520  17.498  1.00 61.18           C  
ANISOU 2599  CA  GLN A1122     7602   8911   6734   -679   -368   -704       C  
ATOM   2600  C   GLN A1122     -21.406 -14.537  18.424  1.00 66.09           C  
ANISOU 2600  C   GLN A1122     8240   9577   7294   -820   -274   -745       C  
ATOM   2601  O   GLN A1122     -21.785 -14.205  19.545  1.00 66.68           O  
ANISOU 2601  O   GLN A1122     8317   9666   7354   -886   -147   -820       O  
ATOM   2602  CB  GLN A1122     -21.821 -12.921  16.594  1.00 63.20           C  
ANISOU 2602  CB  GLN A1122     7679   9188   7147   -601   -403   -723       C  
ATOM   2603  CG  GLN A1122     -22.835 -12.041  17.318  1.00 75.09           C  
ANISOU 2603  CG  GLN A1122     9045  10700   8785   -588   -277   -821       C  
ATOM   2604  CD  GLN A1122     -23.803 -11.400  16.362  1.00 90.68           C  
ANISOU 2604  CD  GLN A1122    10825  12675  10955   -498   -344   -812       C  
ATOM   2605  OE1 GLN A1122     -24.100 -11.943  15.290  1.00 84.36           O  
ANISOU 2605  OE1 GLN A1122     9986  11902  10167   -498   -472   -744       O  
ATOM   2606  NE2 GLN A1122     -24.308 -10.240  16.739  1.00 84.39           N  
ANISOU 2606  NE2 GLN A1122     9905  11840  10319   -431   -260   -876       N  
ATOM   2607  N   GLN A1123     -21.565 -15.763  17.935  1.00 62.56           N  
ANISOU 2607  N   GLN A1123     7813   9148   6809   -878   -327   -702       N  
ATOM   2608  CA  GLN A1123     -22.097 -16.862  18.735  1.00 62.93           C  
ANISOU 2608  CA  GLN A1123     7893   9230   6787  -1020   -253   -725       C  
ATOM   2609  C   GLN A1123     -21.117 -17.334  19.800  1.00 67.26           C  
ANISOU 2609  C   GLN A1123     8613   9744   7199  -1113   -236   -682       C  
ATOM   2610  O   GLN A1123     -21.520 -18.015  20.742  1.00 67.94           O  
ANISOU 2610  O   GLN A1123     8747   9855   7210  -1250   -160   -703       O  
ATOM   2611  CB  GLN A1123     -22.425 -18.060  17.852  1.00 63.85           C  
ANISOU 2611  CB  GLN A1123     7996   9362   6902  -1058   -321   -684       C  
ATOM   2612  CG  GLN A1123     -23.638 -17.900  16.976  1.00 73.75           C  
ANISOU 2612  CG  GLN A1123     9081  10667   8272  -1027   -344   -719       C  
ATOM   2613  CD  GLN A1123     -23.994 -19.195  16.281  1.00 87.23           C  
ANISOU 2613  CD  GLN A1123    10799  12396   9950  -1104   -395   -690       C  
ATOM   2614  OE1 GLN A1123     -24.136 -20.232  16.932  1.00 82.59           O  
ANISOU 2614  OE1 GLN A1123    10273  11816   9292  -1218   -338   -696       O  
ATOM   2615  NE2 GLN A1123     -24.125 -19.151  14.954  1.00 75.52           N  
ANISOU 2615  NE2 GLN A1123     9267  10918   8509  -1059   -503   -656       N  
ATOM   2616  N   LYS A1124     -19.838 -16.992  19.637  1.00 63.01           N  
ANISOU 2616  N   LYS A1124     8165   9144   6632  -1050   -315   -613       N  
ATOM   2617  CA  LYS A1124     -18.760 -17.429  20.539  1.00 62.64           C  
ANISOU 2617  CA  LYS A1124     8272   9051   6479  -1132   -341   -541       C  
ATOM   2618  C   LYS A1124     -18.519 -18.925  20.381  1.00 66.26           C  
ANISOU 2618  C   LYS A1124     8790   9477   6911  -1207   -395   -463       C  
ATOM   2619  O   LYS A1124     -18.567 -19.684  21.347  1.00 66.75           O  
ANISOU 2619  O   LYS A1124     8933   9540   6890  -1344   -372   -434       O  
ATOM   2620  CB  LYS A1124     -19.028 -17.047  22.012  1.00 66.02           C  
ANISOU 2620  CB  LYS A1124     8763   9511   6812  -1257   -235   -593       C  
ATOM   2621  CG  LYS A1124     -19.217 -15.537  22.260  1.00 78.80           C  
ANISOU 2621  CG  LYS A1124    10330  11141   8469  -1192   -155   -684       C  
ATOM   2622  CD  LYS A1124     -19.057 -15.183  23.754  1.00 89.23           C  
ANISOU 2622  CD  LYS A1124    11771  12472   9659  -1342    -60   -723       C  
ATOM   2623  CE  LYS A1124     -18.988 -13.670  24.005  1.00 97.90           C  
ANISOU 2623  CE  LYS A1124    12844  13558  10795  -1281     19   -809       C  
ATOM   2624  NZ  LYS A1124     -20.326 -12.998  24.031  1.00105.69           N  
ANISOU 2624  NZ  LYS A1124    13681  14576  11899  -1257    182   -956       N  
ATOM   2625  N   ARG A1125     -18.292 -19.327  19.131  1.00 61.82           N  
ANISOU 2625  N   ARG A1125     8190   8881   6419  -1127   -462   -434       N  
ATOM   2626  CA  ARG A1125     -17.804 -20.666  18.781  1.00 61.25           C  
ANISOU 2626  CA  ARG A1125     8175   8744   6355  -1174   -511   -361       C  
ATOM   2627  C   ARG A1125     -16.573 -20.433  17.938  1.00 63.55           C  
ANISOU 2627  C   ARG A1125     8492   8946   6707  -1070   -583   -308       C  
ATOM   2628  O   ARG A1125     -16.660 -20.200  16.730  1.00 62.92           O  
ANISOU 2628  O   ARG A1125     8363   8867   6678   -993   -599   -337       O  
ATOM   2629  CB  ARG A1125     -18.852 -21.518  18.041  1.00 61.57           C  
ANISOU 2629  CB  ARG A1125     8149   8825   6419  -1212   -487   -404       C  
ATOM   2630  CG  ARG A1125     -19.695 -20.796  16.997  1.00 69.81           C  
ANISOU 2630  CG  ARG A1125     9074   9934   7518  -1133   -488   -473       C  
ATOM   2631  CD  ARG A1125     -21.173 -21.160  17.126  1.00 82.05           C  
ANISOU 2631  CD  ARG A1125    10531  11572   9074  -1209   -430   -538       C  
ATOM   2632  NE  ARG A1125     -21.503 -22.477  16.567  1.00 91.98           N  
ANISOU 2632  NE  ARG A1125    11803  12821  10324  -1288   -442   -526       N  
ATOM   2633  CZ  ARG A1125     -22.593 -23.192  16.866  1.00106.30           C  
ANISOU 2633  CZ  ARG A1125    13570  14692  12126  -1391   -390   -565       C  
ATOM   2634  NH1 ARG A1125     -23.497 -22.751  17.742  1.00 92.85           N  
ANISOU 2634  NH1 ARG A1125    11796  13058  10423  -1432   -309   -625       N  
ATOM   2635  NH2 ARG A1125     -22.777 -24.372  16.280  1.00 93.78           N  
ANISOU 2635  NH2 ARG A1125    12010  13088  10533  -1462   -405   -552       N  
ATOM   2636  N   TRP A1126     -15.425 -20.480  18.603  1.00 59.11           N  
ANISOU 2636  N   TRP A1126     8011   8308   6140  -1082   -628   -226       N  
ATOM   2637  CA  TRP A1126     -14.208 -19.889  18.081  1.00 57.93           C  
ANISOU 2637  CA  TRP A1126     7876   8081   6053   -981   -682   -185       C  
ATOM   2638  C   TRP A1126     -13.514 -20.791  17.052  1.00 61.93           C  
ANISOU 2638  C   TRP A1126     8388   8484   6657   -952   -704   -149       C  
ATOM   2639  O   TRP A1126     -13.044 -20.315  16.021  1.00 60.67           O  
ANISOU 2639  O   TRP A1126     8210   8292   6551   -864   -709   -172       O  
ATOM   2640  CB  TRP A1126     -13.255 -19.539  19.237  1.00 56.70           C  
ANISOU 2640  CB  TRP A1126     7794   7884   5865  -1017   -731   -107       C  
ATOM   2641  CG  TRP A1126     -13.917 -18.825  20.413  1.00 58.15           C  
ANISOU 2641  CG  TRP A1126     8004   8159   5932  -1092   -685   -151       C  
ATOM   2642  CD1 TRP A1126     -14.083 -19.314  21.687  1.00 61.97           C  
ANISOU 2642  CD1 TRP A1126     8567   8660   6319  -1244   -682   -111       C  
ATOM   2643  CD2 TRP A1126     -14.504 -17.515  20.414  1.00 57.83           C  
ANISOU 2643  CD2 TRP A1126     7914   8193   5866  -1035   -622   -249       C  
ATOM   2644  NE1 TRP A1126     -14.723 -18.387  22.472  1.00 61.83           N  
ANISOU 2644  NE1 TRP A1126     8561   8726   6206  -1293   -603   -194       N  
ATOM   2645  CE2 TRP A1126     -14.998 -17.277  21.718  1.00 62.63           C  
ANISOU 2645  CE2 TRP A1126     8575   8857   6365  -1159   -560   -281       C  
ATOM   2646  CE3 TRP A1126     -14.656 -16.521  19.444  1.00 58.35           C  
ANISOU 2646  CE3 TRP A1126     7900   8274   5995   -901   -610   -310       C  
ATOM   2647  CZ2 TRP A1126     -15.635 -16.087  22.073  1.00 62.23           C  
ANISOU 2647  CZ2 TRP A1126     8488   8867   6291  -1143   -467   -387       C  
ATOM   2648  CZ3 TRP A1126     -15.293 -15.340  19.798  1.00 60.16           C  
ANISOU 2648  CZ3 TRP A1126     8087   8562   6210   -876   -541   -396       C  
ATOM   2649  CH2 TRP A1126     -15.771 -15.133  21.104  1.00 61.76           C  
ANISOU 2649  CH2 TRP A1126     8331   8809   6325   -992   -460   -441       C  
ATOM   2650  N   ASP A1127     -13.471 -22.090  17.322  1.00 59.67           N  
ANISOU 2650  N   ASP A1127     8133   8139   6400  -1036   -706    -99       N  
ATOM   2651  CA  ASP A1127     -12.715 -23.026  16.478  1.00 59.62           C  
ANISOU 2651  CA  ASP A1127     8134   8005   6515  -1021   -704    -69       C  
ATOM   2652  C   ASP A1127     -13.261 -23.184  15.059  1.00 62.64           C  
ANISOU 2652  C   ASP A1127     8485   8409   6907   -997   -649   -160       C  
ATOM   2653  O   ASP A1127     -12.477 -23.273  14.109  1.00 62.74           O  
ANISOU 2653  O   ASP A1127     8505   8330   7003   -951   -630   -171       O  
ATOM   2654  CB  ASP A1127     -12.607 -24.402  17.152  1.00 62.65           C  
ANISOU 2654  CB  ASP A1127     8553   8308   6944  -1122   -718     11       C  
ATOM   2655  CG  ASP A1127     -11.737 -24.369  18.401  1.00 76.04           C  
ANISOU 2655  CG  ASP A1127    10293   9942   8656  -1160   -805    137       C  
ATOM   2656  OD1 ASP A1127     -10.602 -23.829  18.325  1.00 76.70           O  
ANISOU 2656  OD1 ASP A1127    10372   9949   8822  -1087   -853    188       O  
ATOM   2657  OD2 ASP A1127     -12.192 -24.878  19.455  1.00 83.39           O  
ANISOU 2657  OD2 ASP A1127    11270  10904   9511  -1275   -829    189       O  
ATOM   2658  N   GLU A1128     -14.581 -23.238  14.902  1.00 58.04           N  
ANISOU 2658  N   GLU A1128     7869   7941   6242  -1042   -622   -226       N  
ATOM   2659  CA  GLU A1128     -15.166 -23.347  13.556  1.00 57.30           C  
ANISOU 2659  CA  GLU A1128     7752   7880   6139  -1044   -595   -301       C  
ATOM   2660  C   GLU A1128     -15.042 -22.033  12.776  1.00 58.87           C  
ANISOU 2660  C   GLU A1128     7926   8122   6320   -951   -622   -334       C  
ATOM   2661  O   GLU A1128     -14.773 -22.040  11.575  1.00 58.35           O  
ANISOU 2661  O   GLU A1128     7881   8022   6266   -944   -613   -366       O  
ATOM   2662  CB  GLU A1128     -16.618 -23.841  13.605  1.00 59.24           C  
ANISOU 2662  CB  GLU A1128     7956   8232   6321  -1129   -575   -348       C  
ATOM   2663  CG  GLU A1128     -17.595 -22.958  14.360  1.00 69.23           C  
ANISOU 2663  CG  GLU A1128     9153   9623   7528  -1119   -582   -374       C  
ATOM   2664  CD  GLU A1128     -18.930 -23.654  14.586  1.00 86.93           C  
ANISOU 2664  CD  GLU A1128    11348  11948   9735  -1218   -548   -413       C  
ATOM   2665  OE1 GLU A1128     -18.967 -24.632  15.368  1.00 77.05           O  
ANISOU 2665  OE1 GLU A1128    10140  10666   8470  -1306   -519   -385       O  
ATOM   2666  OE2 GLU A1128     -19.941 -23.226  13.980  1.00 79.65           O  
ANISOU 2666  OE2 GLU A1128    10342  11115   8807  -1214   -559   -465       O  
ATOM   2667  N   ALA A1129     -15.219 -20.915  13.478  1.00 53.78           N  
ANISOU 2667  N   ALA A1129     7245   7544   5644   -894   -650   -329       N  
ATOM   2668  CA  ALA A1129     -14.943 -19.584  12.932  1.00 52.38           C  
ANISOU 2668  CA  ALA A1129     7047   7387   5466   -798   -682   -344       C  
ATOM   2669  C   ALA A1129     -13.478 -19.447  12.511  1.00 53.54           C  
ANISOU 2669  C   ALA A1129     7253   7418   5671   -745   -686   -311       C  
ATOM   2670  O   ALA A1129     -13.175 -18.824  11.497  1.00 53.08           O  
ANISOU 2670  O   ALA A1129     7204   7348   5614   -700   -696   -332       O  
ATOM   2671  CB  ALA A1129     -15.301 -18.512  13.955  1.00 53.17           C  
ANISOU 2671  CB  ALA A1129     7106   7555   5542   -757   -689   -348       C  
ATOM   2672  N   ALA A1130     -12.581 -20.031  13.298  1.00 48.46           N  
ANISOU 2672  N   ALA A1130     6646   6685   5082   -760   -682   -252       N  
ATOM   2673  CA  ALA A1130     -11.159 -20.085  12.971  1.00 47.15           C  
ANISOU 2673  CA  ALA A1130     6514   6388   5014   -717   -678   -215       C  
ATOM   2674  C   ALA A1130     -10.865 -21.118  11.886  1.00 50.19           C  
ANISOU 2674  C   ALA A1130     6924   6679   5467   -759   -614   -247       C  
ATOM   2675  O   ALA A1130      -9.874 -20.988  11.173  1.00 50.05           O  
ANISOU 2675  O   ALA A1130     6926   6563   5527   -724   -581   -257       O  
ATOM   2676  CB  ALA A1130     -10.344 -20.380  14.218  1.00 47.93           C  
ANISOU 2676  CB  ALA A1130     6626   6415   5170   -729   -717   -123       C  
ATOM   2677  N   VAL A1131     -11.703 -22.149  11.773  1.00 46.13           N  
ANISOU 2677  N   VAL A1131     6411   6187   4929   -844   -584   -273       N  
ATOM   2678  CA  VAL A1131     -11.591 -23.112  10.674  1.00 46.04           C  
ANISOU 2678  CA  VAL A1131     6434   6095   4963   -905   -506   -326       C  
ATOM   2679  C   VAL A1131     -12.048 -22.442   9.384  1.00 50.26           C  
ANISOU 2679  C   VAL A1131     6989   6702   5404   -913   -500   -400       C  
ATOM   2680  O   VAL A1131     -11.415 -22.587   8.323  1.00 50.32           O  
ANISOU 2680  O   VAL A1131     7048   6628   5442   -936   -434   -447       O  
ATOM   2681  CB  VAL A1131     -12.449 -24.381  10.899  1.00 50.17           C  
ANISOU 2681  CB  VAL A1131     6959   6629   5473  -1007   -477   -336       C  
ATOM   2682  CG1 VAL A1131     -12.515 -25.226   9.629  1.00 50.24           C  
ANISOU 2682  CG1 VAL A1131     7014   6576   5497  -1088   -388   -415       C  
ATOM   2683  CG2 VAL A1131     -11.892 -25.217  12.048  1.00 50.37           C  
ANISOU 2683  CG2 VAL A1131     6980   6553   5605  -1021   -488   -248       C  
ATOM   2684  N   ASN A1132     -13.147 -21.701   9.494  1.00 46.14           N  
ANISOU 2684  N   ASN A1132     6427   6328   4776   -905   -567   -407       N  
ATOM   2685  CA  ASN A1132     -13.732 -21.014   8.353  1.00 45.64           C  
ANISOU 2685  CA  ASN A1132     6372   6343   4626   -921   -600   -449       C  
ATOM   2686  C   ASN A1132     -12.855 -19.861   7.832  1.00 47.96           C  
ANISOU 2686  C   ASN A1132     6692   6604   4924   -843   -618   -443       C  
ATOM   2687  O   ASN A1132     -12.623 -19.744   6.626  1.00 47.90           O  
ANISOU 2687  O   ASN A1132     6749   6575   4877   -890   -598   -480       O  
ATOM   2688  CB  ASN A1132     -15.126 -20.504   8.715  1.00 45.58           C  
ANISOU 2688  CB  ASN A1132     6283   6482   4555   -920   -674   -444       C  
ATOM   2689  CG  ASN A1132     -16.091 -20.595   7.560  1.00 64.89           C  
ANISOU 2689  CG  ASN A1132     8729   9001   6925  -1007   -715   -476       C  
ATOM   2690  OD1 ASN A1132     -16.334 -21.682   7.025  1.00 57.79           O  
ANISOU 2690  OD1 ASN A1132     7876   8082   6000  -1118   -672   -511       O  
ATOM   2691  ND2 ASN A1132     -16.663 -19.460   7.177  1.00 57.13           N  
ANISOU 2691  ND2 ASN A1132     7694   8100   5912   -966   -805   -459       N  
ATOM   2692  N   LEU A1133     -12.362 -19.023   8.737  1.00 43.19           N  
ANISOU 2692  N   LEU A1133     6053   5998   4359   -742   -650   -399       N  
ATOM   2693  CA  LEU A1133     -11.501 -17.890   8.350  1.00 42.28           C  
ANISOU 2693  CA  LEU A1133     5961   5850   4255   -665   -666   -390       C  
ATOM   2694  C   LEU A1133     -10.248 -18.318   7.567  1.00 45.49           C  
ANISOU 2694  C   LEU A1133     6438   6121   4726   -688   -583   -415       C  
ATOM   2695  O   LEU A1133      -9.806 -17.595   6.686  1.00 45.01           O  
ANISOU 2695  O   LEU A1133     6422   6044   4636   -678   -577   -436       O  
ATOM   2696  CB  LEU A1133     -11.120 -17.053   9.577  1.00 41.67           C  
ANISOU 2696  CB  LEU A1133     5841   5781   4211   -571   -704   -342       C  
ATOM   2697  CG  LEU A1133     -12.290 -16.243  10.155  1.00 46.43           C  
ANISOU 2697  CG  LEU A1133     6374   6507   4760   -541   -761   -342       C  
ATOM   2698  CD1 LEU A1133     -12.036 -15.848  11.611  1.00 46.03           C  
ANISOU 2698  CD1 LEU A1133     6300   6460   4728   -499   -765   -310       C  
ATOM   2699  CD2 LEU A1133     -12.604 -15.015   9.269  1.00 49.02           C  
ANISOU 2699  CD2 LEU A1133     6689   6882   5055   -493   -815   -351       C  
ATOM   2700  N   ALA A1134      -9.713 -19.500   7.872  1.00 41.99           N  
ANISOU 2700  N   ALA A1134     6001   5572   4381   -724   -511   -415       N  
ATOM   2701  CA  ALA A1134      -8.583 -20.084   7.140  1.00 42.22           C  
ANISOU 2701  CA  ALA A1134     6079   5449   4516   -755   -400   -454       C  
ATOM   2702  C   ALA A1134      -8.935 -20.640   5.736  1.00 46.98           C  
ANISOU 2702  C   ALA A1134     6762   6042   5046   -877   -317   -545       C  
ATOM   2703  O   ALA A1134      -8.042 -21.071   4.990  1.00 46.84           O  
ANISOU 2703  O   ALA A1134     6796   5893   5107   -922   -194   -603       O  
ATOM   2704  CB  ALA A1134      -7.909 -21.189   7.997  1.00 43.20           C  
ANISOU 2704  CB  ALA A1134     6163   5443   4809   -750   -357   -410       C  
ATOM   2705  N   LYS A1135     -10.222 -20.629   5.384  1.00 43.82           N  
ANISOU 2705  N   LYS A1135     6373   5773   4503   -944   -379   -559       N  
ATOM   2706  CA  LYS A1135     -10.680 -21.047   4.049  1.00 44.31           C  
ANISOU 2706  CA  LYS A1135     6526   5851   4458  -1087   -331   -635       C  
ATOM   2707  C   LYS A1135     -10.943 -19.881   3.081  1.00 48.99           C  
ANISOU 2707  C   LYS A1135     7173   6529   4912  -1112   -406   -636       C  
ATOM   2708  O   LYS A1135     -11.384 -20.105   1.960  1.00 49.72           O  
ANISOU 2708  O   LYS A1135     7355   6652   4886  -1253   -396   -683       O  
ATOM   2709  CB  LYS A1135     -11.944 -21.903   4.172  1.00 46.26           C  
ANISOU 2709  CB  LYS A1135     6753   6181   4641  -1175   -363   -642       C  
ATOM   2710  CG  LYS A1135     -11.694 -23.259   4.786  1.00 50.42           C  
ANISOU 2710  CG  LYS A1135     7264   6604   5290  -1199   -268   -655       C  
ATOM   2711  CD  LYS A1135     -12.988 -23.924   5.178  1.00 55.49           C  
ANISOU 2711  CD  LYS A1135     7868   7346   5870  -1262   -319   -645       C  
ATOM   2712  CE  LYS A1135     -12.790 -25.390   5.469  1.00 61.81           C  
ANISOU 2712  CE  LYS A1135     8680   8030   6774  -1326   -213   -670       C  
ATOM   2713  NZ  LYS A1135     -14.089 -26.029   5.782  1.00 71.84           N  
ANISOU 2713  NZ  LYS A1135     9921   9403   7971  -1402   -259   -667       N  
ATOM   2714  N   SER A1136     -10.650 -18.653   3.504  1.00 44.96           N  
ANISOU 2714  N   SER A1136     6618   6051   4415   -989   -485   -580       N  
ATOM   2715  CA  SER A1136     -10.905 -17.456   2.697  1.00 44.83           C  
ANISOU 2715  CA  SER A1136     6641   6107   4286   -998   -577   -559       C  
ATOM   2716  C   SER A1136      -9.700 -17.048   1.838  1.00 49.73           C  
ANISOU 2716  C   SER A1136     7362   6628   4903  -1026   -488   -600       C  
ATOM   2717  O   SER A1136      -8.555 -17.470   2.087  1.00 48.83           O  
ANISOU 2717  O   SER A1136     7253   6384   4914   -993   -362   -636       O  
ATOM   2718  CB  SER A1136     -11.263 -16.294   3.614  1.00 46.79           C  
ANISOU 2718  CB  SER A1136     6785   6432   4562   -853   -697   -484       C  
ATOM   2719  OG  SER A1136     -10.220 -16.052   4.542  1.00 52.32           O  
ANISOU 2719  OG  SER A1136     7449   7054   5377   -738   -649   -468       O  
ATOM   2720  N   ARG A1137      -9.979 -16.214   0.831  1.00 47.36           N  
ANISOU 2720  N   ARG A1137     7138   6385   4470  -1093   -561   -589       N  
ATOM   2721  CA  ARG A1137      -8.948 -15.687  -0.079  1.00 47.46           C  
ANISOU 2721  CA  ARG A1137     7265   6320   4448  -1143   -484   -628       C  
ATOM   2722  C   ARG A1137      -7.880 -14.923   0.693  1.00 50.19           C  
ANISOU 2722  C   ARG A1137     7548   6597   4924   -981   -460   -601       C  
ATOM   2723  O   ARG A1137      -6.684 -15.024   0.383  1.00 50.06           O  
ANISOU 2723  O   ARG A1137     7583   6460   4977   -994   -324   -657       O  
ATOM   2724  CB  ARG A1137      -9.563 -14.766  -1.160  1.00 47.82           C  
ANISOU 2724  CB  ARG A1137     7399   6455   4317  -1241   -614   -586       C  
ATOM   2725  CG  ARG A1137      -9.907 -15.458  -2.472  1.00 58.84           C  
ANISOU 2725  CG  ARG A1137     8948   7859   5550  -1478   -572   -646       C  
ATOM   2726  CD  ARG A1137     -11.410 -15.484  -2.750  1.00 72.80           C  
ANISOU 2726  CD  ARG A1137    10692   9765   7203  -1560   -755   -577       C  
ATOM   2727  NE  ARG A1137     -11.831 -16.698  -3.467  1.00 82.29           N  
ANISOU 2727  NE  ARG A1137    11994  10970   8304  -1766   -684   -651       N  
ATOM   2728  CZ  ARG A1137     -11.950 -17.914  -2.921  1.00 91.96           C  
ANISOU 2728  CZ  ARG A1137    13171  12158   9611  -1766   -576   -713       C  
ATOM   2729  NH1 ARG A1137     -11.665 -18.125  -1.637  1.00 74.18           N  
ANISOU 2729  NH1 ARG A1137    10778   9867   7540  -1580   -534   -702       N  
ATOM   2730  NH2 ARG A1137     -12.352 -18.934  -3.671  1.00 77.77           N  
ANISOU 2730  NH2 ARG A1137    11479  10362   7709  -1970   -512   -784       N  
ATOM   2731  N   TRP A1138      -8.341 -14.158   1.683  1.00 45.47           N  
ANISOU 2731  N   TRP A1138     6840   6073   4363   -840   -586   -522       N  
ATOM   2732  CA  TRP A1138      -7.488 -13.363   2.575  1.00 44.39           C  
ANISOU 2732  CA  TRP A1138     6639   5892   4335   -691   -589   -486       C  
ATOM   2733  C   TRP A1138      -6.387 -14.205   3.212  1.00 47.93           C  
ANISOU 2733  C   TRP A1138     7056   6214   4940   -657   -463   -516       C  
ATOM   2734  O   TRP A1138      -5.241 -13.772   3.297  1.00 46.85           O  
ANISOU 2734  O   TRP A1138     6921   5989   4890   -605   -408   -519       O  
ATOM   2735  CB  TRP A1138      -8.373 -12.705   3.646  1.00 42.62           C  
ANISOU 2735  CB  TRP A1138     6303   5767   4123   -579   -718   -417       C  
ATOM   2736  CG  TRP A1138      -7.691 -12.209   4.890  1.00 42.63           C  
ANISOU 2736  CG  TRP A1138     6232   5734   4230   -448   -717   -385       C  
ATOM   2737  CD1 TRP A1138      -6.805 -11.178   4.984  1.00 45.15           C  
ANISOU 2737  CD1 TRP A1138     6563   6011   4583   -375   -720   -368       C  
ATOM   2738  CD2 TRP A1138      -7.885 -12.693   6.222  1.00 42.00           C  
ANISOU 2738  CD2 TRP A1138     6070   5667   4220   -396   -723   -362       C  
ATOM   2739  NE1 TRP A1138      -6.420 -11.004   6.288  1.00 43.97           N  
ANISOU 2739  NE1 TRP A1138     6344   5847   4517   -286   -730   -337       N  
ATOM   2740  CE2 TRP A1138      -7.069 -11.919   7.070  1.00 45.36           C  
ANISOU 2740  CE2 TRP A1138     6467   6057   4710   -303   -734   -330       C  
ATOM   2741  CE3 TRP A1138      -8.661 -13.710   6.777  1.00 43.52           C  
ANISOU 2741  CE3 TRP A1138     6220   5898   4417   -435   -720   -364       C  
ATOM   2742  CZ2 TRP A1138      -7.006 -12.127   8.447  1.00 44.33           C  
ANISOU 2742  CZ2 TRP A1138     6279   5931   4634   -262   -749   -297       C  
ATOM   2743  CZ3 TRP A1138      -8.598 -13.925   8.145  1.00 44.76           C  
ANISOU 2743  CZ3 TRP A1138     6318   6056   4633   -388   -729   -332       C  
ATOM   2744  CH2 TRP A1138      -7.776 -13.131   8.968  1.00 44.92           C  
ANISOU 2744  CH2 TRP A1138     6322   6043   4703   -309   -746   -296       C  
ATOM   2745  N   TYR A1139      -6.743 -15.413   3.640  1.00 45.05           N  
ANISOU 2745  N   TYR A1139     6657   5835   4626   -691   -424   -530       N  
ATOM   2746  CA  TYR A1139      -5.796 -16.331   4.266  1.00 44.88           C  
ANISOU 2746  CA  TYR A1139     6591   5682   4780   -665   -324   -539       C  
ATOM   2747  C   TYR A1139      -4.781 -16.887   3.250  1.00 48.79           C  
ANISOU 2747  C   TYR A1139     7157   6031   5349   -750   -154   -626       C  
ATOM   2748  O   TYR A1139      -3.593 -16.992   3.560  1.00 48.26           O  
ANISOU 2748  O   TYR A1139     7047   5833   5456   -696    -78   -625       O  
ATOM   2749  CB  TYR A1139      -6.558 -17.456   4.987  1.00 46.49           C  
ANISOU 2749  CB  TYR A1139     6743   5910   5011   -689   -339   -522       C  
ATOM   2750  CG  TYR A1139      -5.681 -18.482   5.677  1.00 49.17           C  
ANISOU 2750  CG  TYR A1139     7030   6105   5546   -668   -261   -508       C  
ATOM   2751  CD1 TYR A1139      -5.452 -18.421   7.051  1.00 50.68           C  
ANISOU 2751  CD1 TYR A1139     7140   6293   5824   -582   -342   -417       C  
ATOM   2752  CD2 TYR A1139      -5.085 -19.524   4.957  1.00 51.08           C  
ANISOU 2752  CD2 TYR A1139     7307   6205   5897   -749   -108   -581       C  
ATOM   2753  CE1 TYR A1139      -4.655 -19.360   7.686  1.00 51.93           C  
ANISOU 2753  CE1 TYR A1139     7244   6312   6173   -572   -302   -377       C  
ATOM   2754  CE2 TYR A1139      -4.289 -20.464   5.585  1.00 52.48           C  
ANISOU 2754  CE2 TYR A1139     7416   6231   6294   -723    -46   -554       C  
ATOM   2755  CZ  TYR A1139      -4.075 -20.376   6.948  1.00 59.41           C  
ANISOU 2755  CZ  TYR A1139     8206   7109   7258   -633   -158   -441       C  
ATOM   2756  OH  TYR A1139      -3.279 -21.307   7.579  1.00 61.85           O  
ANISOU 2756  OH  TYR A1139     8442   7260   7798   -616   -127   -388       O  
ATOM   2757  N   ASN A1140      -5.238 -17.234   2.046  1.00 45.52           N  
ANISOU 2757  N   ASN A1140     6850   5635   4811   -892    -90   -703       N  
ATOM   2758  CA  ASN A1140      -4.340 -17.771   1.016  1.00 46.18           C  
ANISOU 2758  CA  ASN A1140     7019   5577   4949  -1002    104   -811       C  
ATOM   2759  C   ASN A1140      -3.326 -16.729   0.561  1.00 50.14           C  
ANISOU 2759  C   ASN A1140     7558   6027   5464   -975    146   -825       C  
ATOM   2760  O   ASN A1140      -2.189 -17.059   0.214  1.00 50.38           O  
ANISOU 2760  O   ASN A1140     7597   5902   5643   -999    317   -897       O  
ATOM   2761  CB  ASN A1140      -5.127 -18.291  -0.198  1.00 46.60           C  
ANISOU 2761  CB  ASN A1140     7207   5677   4822  -1196    155   -893       C  
ATOM   2762  CG  ASN A1140      -4.282 -19.175  -1.111  1.00 65.63           C  
ANISOU 2762  CG  ASN A1140     9705   7922   7311  -1333    400  -1030       C  
ATOM   2763  OD1 ASN A1140      -3.762 -20.213  -0.694  1.00 57.29           O  
ANISOU 2763  OD1 ASN A1140     8581   6727   6461  -1311    527  -1067       O  
ATOM   2764  ND2 ASN A1140      -4.140 -18.758  -2.364  1.00 59.98           N  
ANISOU 2764  ND2 ASN A1140     9142   7211   6438  -1484    473  -1106       N  
ATOM   2765  N   GLN A1141      -3.747 -15.467   0.573  1.00 45.91           N  
ANISOU 2765  N   GLN A1141     7039   5614   4793   -924     -5   -758       N  
ATOM   2766  CA  GLN A1141      -2.901 -14.366   0.126  1.00 45.53           C  
ANISOU 2766  CA  GLN A1141     7036   5532   4731   -904     15   -763       C  
ATOM   2767  C   GLN A1141      -1.925 -13.863   1.192  1.00 48.58           C  
ANISOU 2767  C   GLN A1141     7304   5853   5300   -741     -3   -706       C  
ATOM   2768  O   GLN A1141      -0.752 -13.647   0.891  1.00 48.62           O  
ANISOU 2768  O   GLN A1141     7318   5742   5414   -740    112   -748       O  
ATOM   2769  CB  GLN A1141      -3.770 -13.211  -0.354  1.00 46.67           C  
ANISOU 2769  CB  GLN A1141     7247   5821   4665   -924   -145   -706       C  
ATOM   2770  CG  GLN A1141      -4.450 -13.476  -1.668  1.00 57.26           C  
ANISOU 2770  CG  GLN A1141     8737   7210   5810  -1121   -132   -755       C  
ATOM   2771  CD  GLN A1141      -5.433 -12.402  -2.010  1.00 71.41           C  
ANISOU 2771  CD  GLN A1141    10563   9141   7430  -1132   -333   -665       C  
ATOM   2772  OE1 GLN A1141      -5.270 -11.245  -1.622  1.00 64.14           O  
ANISOU 2772  OE1 GLN A1141     9597   8246   6528  -1014   -431   -595       O  
ATOM   2773  NE2 GLN A1141      -6.476 -12.774  -2.739  1.00 65.29           N  
ANISOU 2773  NE2 GLN A1141     9861   8448   6498  -1277   -402   -661       N  
ATOM   2774  N   THR A1142      -2.416 -13.648   2.416  1.00 44.25           N  
ANISOU 2774  N   THR A1142     6652   5380   4779   -620   -146   -614       N  
ATOM   2775  CA  THR A1142      -1.576 -13.190   3.535  1.00 43.25           C  
ANISOU 2775  CA  THR A1142     6424   5205   4803   -488   -188   -548       C  
ATOM   2776  C   THR A1142      -1.647 -14.185   4.692  1.00 46.77           C  
ANISOU 2776  C   THR A1142     6769   5620   5382   -444   -213   -499       C  
ATOM   2777  O   THR A1142      -2.165 -13.854   5.761  1.00 45.73           O  
ANISOU 2777  O   THR A1142     6581   5574   5219   -374   -340   -423       O  
ATOM   2778  CB  THR A1142      -1.967 -11.760   4.033  1.00 48.43           C  
ANISOU 2778  CB  THR A1142     7069   5976   5356   -397   -338   -478       C  
ATOM   2779  OG1 THR A1142      -3.328 -11.738   4.499  1.00 46.72           O  
ANISOU 2779  OG1 THR A1142     6828   5892   5031   -384   -455   -439       O  
ATOM   2780  CG2 THR A1142      -1.763 -10.727   2.919  1.00 46.05           C  
ANISOU 2780  CG2 THR A1142     6867   5685   4943   -439   -325   -508       C  
ATOM   2781  N   PRO A1143      -1.124 -15.412   4.481  1.00 43.72           N  
ANISOU 2781  N   PRO A1143     6362   5100   5148   -497    -84   -544       N  
ATOM   2782  CA  PRO A1143      -1.314 -16.505   5.455  1.00 43.27           C  
ANISOU 2782  CA  PRO A1143     6223   5007   5210   -479   -112   -491       C  
ATOM   2783  C   PRO A1143      -0.661 -16.274   6.807  1.00 45.29           C  
ANISOU 2783  C   PRO A1143     6377   5228   5601   -379   -215   -380       C  
ATOM   2784  O   PRO A1143      -1.268 -16.576   7.833  1.00 44.50           O  
ANISOU 2784  O   PRO A1143     6240   5193   5475   -362   -320   -307       O  
ATOM   2785  CB  PRO A1143      -0.688 -17.720   4.754  1.00 46.20           C  
ANISOU 2785  CB  PRO A1143     6596   5208   5751   -556     71   -573       C  
ATOM   2786  CG  PRO A1143       0.282 -17.147   3.782  1.00 51.11           C  
ANISOU 2786  CG  PRO A1143     7262   5741   6415   -581    199   -652       C  
ATOM   2787  CD  PRO A1143      -0.319 -15.849   3.323  1.00 45.99           C  
ANISOU 2787  CD  PRO A1143     6705   5251   5516   -585    107   -651       C  
ATOM   2788  N   ASN A1144       0.558 -15.740   6.807  1.00 41.21           N  
ANISOU 2788  N   ASN A1144     5823   4613   5222   -332   -186   -366       N  
ATOM   2789  CA  ASN A1144       1.274 -15.478   8.055  1.00 40.65           C  
ANISOU 2789  CA  ASN A1144     5661   4506   5280   -258   -298   -251       C  
ATOM   2790  C   ASN A1144       0.452 -14.588   8.976  1.00 43.31           C  
ANISOU 2790  C   ASN A1144     6018   5011   5425   -220   -456   -188       C  
ATOM   2791  O   ASN A1144       0.137 -14.988  10.101  1.00 43.39           O  
ANISOU 2791  O   ASN A1144     5992   5053   5441   -220   -554   -105       O  
ATOM   2792  CB  ASN A1144       2.621 -14.816   7.798  1.00 40.03           C  
ANISOU 2792  CB  ASN A1144     5544   4318   5349   -218   -250   -254       C  
ATOM   2793  CG  ASN A1144       3.547 -15.675   6.973  1.00 54.84           C  
ANISOU 2793  CG  ASN A1144     7378   6000   7459   -255    -69   -325       C  
ATOM   2794  OD1 ASN A1144       3.513 -16.903   7.051  1.00 44.15           O  
ANISOU 2794  OD1 ASN A1144     5977   4549   6250   -286    -13   -325       O  
ATOM   2795  ND2 ASN A1144       4.384 -15.026   6.163  1.00 47.60           N  
ANISOU 2795  ND2 ASN A1144     6478   5017   6591   -258     39   -395       N  
ATOM   2796  N   ARG A1145       0.091 -13.406   8.468  1.00 37.98           N  
ANISOU 2796  N   ARG A1145     5407   4437   4587   -201   -469   -230       N  
ATOM   2797  CA  ARG A1145      -0.663 -12.393   9.223  1.00 36.44           C  
ANISOU 2797  CA  ARG A1145     5227   4385   4232   -161   -590   -191       C  
ATOM   2798  C   ARG A1145      -2.042 -12.883   9.665  1.00 40.76           C  
ANISOU 2798  C   ARG A1145     5781   5045   4660   -192   -637   -188       C  
ATOM   2799  O   ARG A1145      -2.464 -12.657  10.805  1.00 40.21           O  
ANISOU 2799  O   ARG A1145     5692   5045   4541   -179   -722   -135       O  
ATOM   2800  CB  ARG A1145      -0.818 -11.109   8.389  1.00 33.38           C  
ANISOU 2800  CB  ARG A1145     4902   4057   3722   -137   -583   -240       C  
ATOM   2801  CG  ARG A1145      -1.754 -10.061   8.999  1.00 35.95           C  
ANISOU 2801  CG  ARG A1145     5237   4518   3905    -95   -683   -219       C  
ATOM   2802  CD  ARG A1145      -1.728  -8.718   8.255  1.00 37.36           C  
ANISOU 2802  CD  ARG A1145     5465   4727   4004    -62   -690   -245       C  
ATOM   2803  NE  ARG A1145      -2.505  -7.725   8.991  1.00 37.79           N  
ANISOU 2803  NE  ARG A1145     5506   4879   3973    -13   -772   -224       N  
ATOM   2804  CZ  ARG A1145      -2.584  -6.432   8.695  1.00 44.97           C  
ANISOU 2804  CZ  ARG A1145     6442   5815   4831     31   -801   -230       C  
ATOM   2805  NH1 ARG A1145      -1.951  -5.942   7.647  1.00 37.23           N  
ANISOU 2805  NH1 ARG A1145     5513   4783   3848     25   -767   -249       N  
ATOM   2806  NH2 ARG A1145      -3.322  -5.629   9.447  1.00 24.98           N  
ANISOU 2806  NH2 ARG A1145     3885   3354   2253     74   -855   -221       N  
ATOM   2807  N   ALA A1146      -2.739 -13.530   8.742  1.00 37.76           N  
ANISOU 2807  N   ALA A1146     5435   4683   4228   -247   -574   -250       N  
ATOM   2808  CA  ALA A1146      -4.060 -14.071   9.002  1.00 37.69           C  
ANISOU 2808  CA  ALA A1146     5425   4775   4119   -286   -607   -255       C  
ATOM   2809  C   ALA A1146      -3.973 -15.305   9.910  1.00 41.73           C  
ANISOU 2809  C   ALA A1146     5894   5232   4729   -318   -613   -205       C  
ATOM   2810  O   ALA A1146      -4.892 -15.575  10.693  1.00 41.31           O  
ANISOU 2810  O   ALA A1146     5828   5265   4604   -339   -666   -180       O  
ATOM   2811  CB  ALA A1146      -4.762 -14.409   7.673  1.00 38.81           C  
ANISOU 2811  CB  ALA A1146     5624   4947   4175   -356   -548   -331       C  
ATOM   2812  N   LYS A1147      -2.882 -16.061   9.818  1.00 38.75           N  
ANISOU 2812  N   LYS A1147     5489   4703   4530   -326   -555   -187       N  
ATOM   2813  CA  LYS A1147      -2.655 -17.128  10.795  1.00 39.39           C  
ANISOU 2813  CA  LYS A1147     5520   4713   4734   -350   -589   -108       C  
ATOM   2814  C   LYS A1147      -2.696 -16.526  12.228  1.00 43.03           C  
ANISOU 2814  C   LYS A1147     5965   5245   5140   -329   -722    -13       C  
ATOM   2815  O   LYS A1147      -3.474 -16.984  13.091  1.00 42.64           O  
ANISOU 2815  O   LYS A1147     5921   5263   5018   -375   -777     27       O  
ATOM   2816  CB  LYS A1147      -1.338 -17.862  10.502  1.00 42.83           C  
ANISOU 2816  CB  LYS A1147     5903   4951   5421   -346   -516    -91       C  
ATOM   2817  CG  LYS A1147      -0.836 -18.822  11.592  1.00 56.97           C  
ANISOU 2817  CG  LYS A1147     7623   6635   7389   -360   -586     29       C  
ATOM   2818  CD  LYS A1147      -1.916 -19.766  12.109  1.00 65.49           C  
ANISOU 2818  CD  LYS A1147     8721   7773   8387   -424   -616     50       C  
ATOM   2819  CE  LYS A1147      -1.300 -20.939  12.869  1.00 77.64           C  
ANISOU 2819  CE  LYS A1147    10193   9161  10146   -451   -661    165       C  
ATOM   2820  NZ  LYS A1147      -0.469 -21.840  11.994  1.00 87.48           N  
ANISOU 2820  NZ  LYS A1147    11381  10202  11654   -447   -525    123       N  
ATOM   2821  N   ARG A1148      -1.897 -15.474  12.443  1.00 38.72           N  
ANISOU 2821  N   ARG A1148     5413   4688   4611   -277   -763     14       N  
ATOM   2822  CA  ARG A1148      -1.845 -14.778  13.733  1.00 38.29           C  
ANISOU 2822  CA  ARG A1148     5362   4697   4489   -277   -876     91       C  
ATOM   2823  C   ARG A1148      -3.224 -14.274  14.204  1.00 43.01           C  
ANISOU 2823  C   ARG A1148     6001   5458   4881   -298   -898     52       C  
ATOM   2824  O   ARG A1148      -3.676 -14.621  15.305  1.00 43.23           O  
ANISOU 2824  O   ARG A1148     6041   5534   4852   -358   -954    102       O  
ATOM   2825  CB  ARG A1148      -0.842 -13.635  13.673  1.00 36.55           C  
ANISOU 2825  CB  ARG A1148     5137   4444   4306   -222   -898    102       C  
ATOM   2826  CG  ARG A1148       0.601 -14.110  13.425  1.00 45.33           C  
ANISOU 2826  CG  ARG A1148     6184   5383   5656   -206   -883    154       C  
ATOM   2827  CD  ARG A1148       1.670 -13.059  13.783  1.00 48.92           C  
ANISOU 2827  CD  ARG A1148     6621   5805   6160   -170   -942    200       C  
ATOM   2828  NE  ARG A1148       1.750 -11.996  12.785  1.00 50.45           N  
ANISOU 2828  NE  ARG A1148     6850   6029   6290   -117   -865    105       N  
ATOM   2829  CZ  ARG A1148       2.414 -12.070  11.631  1.00 62.50           C  
ANISOU 2829  CZ  ARG A1148     8360   7457   7930    -95   -754     43       C  
ATOM   2830  NH1 ARG A1148       3.080 -13.166  11.287  1.00 48.90           N  
ANISOU 2830  NH1 ARG A1148     6572   5588   6418   -111   -686     52       N  
ATOM   2831  NH2 ARG A1148       2.415 -11.026  10.805  1.00 49.08           N  
ANISOU 2831  NH2 ARG A1148     6712   5798   6139    -64   -702    -31       N  
ATOM   2832  N   VAL A1149      -3.891 -13.487  13.357  1.00 38.89           N  
ANISOU 2832  N   VAL A1149     5499   5015   4263   -257   -852    -36       N  
ATOM   2833  CA  VAL A1149      -5.226 -12.932  13.644  1.00 38.37           C  
ANISOU 2833  CA  VAL A1149     5444   5086   4049   -262   -861    -82       C  
ATOM   2834  C   VAL A1149      -6.248 -13.996  14.092  1.00 44.46           C  
ANISOU 2834  C   VAL A1149     6207   5908   4777   -334   -854    -82       C  
ATOM   2835  O   VAL A1149      -7.029 -13.780  15.017  1.00 44.80           O  
ANISOU 2835  O   VAL A1149     6253   6036   4733   -368   -872    -84       O  
ATOM   2836  CB  VAL A1149      -5.789 -12.201  12.392  1.00 41.62           C  
ANISOU 2836  CB  VAL A1149     5861   5545   4407   -215   -825   -157       C  
ATOM   2837  CG1 VAL A1149      -7.297 -11.924  12.532  1.00 41.49           C  
ANISOU 2837  CG1 VAL A1149     5824   5651   4291   -224   -831   -199       C  
ATOM   2838  CG2 VAL A1149      -5.029 -10.916  12.119  1.00 40.90           C  
ANISOU 2838  CG2 VAL A1149     5786   5430   4324   -149   -836   -160       C  
ATOM   2839  N   ILE A1150      -6.234 -15.138  13.420  1.00 42.28           N  
ANISOU 2839  N   ILE A1150     5925   5574   4567   -365   -814    -89       N  
ATOM   2840  CA  ILE A1150      -7.169 -16.232  13.676  1.00 42.99           C  
ANISOU 2840  CA  ILE A1150     6009   5700   4625   -438   -800    -93       C  
ATOM   2841  C   ILE A1150      -6.848 -16.895  15.019  1.00 48.70           C  
ANISOU 2841  C   ILE A1150     6738   6388   5377   -499   -854     -2       C  
ATOM   2842  O   ILE A1150      -7.754 -17.270  15.769  1.00 48.84           O  
ANISOU 2842  O   ILE A1150     6765   6481   5311   -565   -862      1       O  
ATOM   2843  CB  ILE A1150      -7.126 -17.273  12.486  1.00 46.36           C  
ANISOU 2843  CB  ILE A1150     6439   6055   5121   -465   -729   -134       C  
ATOM   2844  CG1 ILE A1150      -7.863 -16.701  11.259  1.00 46.11           C  
ANISOU 2844  CG1 ILE A1150     6422   6098   5001   -452   -698   -218       C  
ATOM   2845  CG2 ILE A1150      -7.709 -18.633  12.890  1.00 47.82           C  
ANISOU 2845  CG2 ILE A1150     6619   6229   5320   -546   -716   -116       C  
ATOM   2846  CD1 ILE A1150      -7.286 -17.116   9.917  1.00 48.66           C  
ANISOU 2846  CD1 ILE A1150     6778   6330   5379   -473   -621   -267       C  
ATOM   2847  N   THR A1151      -5.555 -17.025  15.319  1.00 46.20           N  
ANISOU 2847  N   THR A1151     6415   5955   5183   -487   -895     78       N  
ATOM   2848  CA  THR A1151      -5.092 -17.515  16.620  1.00 46.76           C  
ANISOU 2848  CA  THR A1151     6497   5984   5286   -556   -984    195       C  
ATOM   2849  C   THR A1151      -5.635 -16.649  17.750  1.00 50.41           C  
ANISOU 2849  C   THR A1151     7006   6567   5581   -602  -1030    200       C  
ATOM   2850  O   THR A1151      -5.932 -17.156  18.834  1.00 50.82           O  
ANISOU 2850  O   THR A1151     7094   6643   5571   -704  -1079    262       O  
ATOM   2851  CB  THR A1151      -3.538 -17.554  16.694  1.00 56.08           C  
ANISOU 2851  CB  THR A1151     7642   7016   6648   -525  -1041    290       C  
ATOM   2852  OG1 THR A1151      -3.062 -18.687  15.967  1.00 58.00           O  
ANISOU 2852  OG1 THR A1151     7837   7119   7080   -516   -989    300       O  
ATOM   2853  CG2 THR A1151      -3.046 -17.655  18.120  1.00 54.92           C  
ANISOU 2853  CG2 THR A1151     7518   6851   6499   -606  -1173    427       C  
ATOM   2854  N   THR A1152      -5.747 -15.348  17.502  1.00 46.02           N  
ANISOU 2854  N   THR A1152     6454   6077   4953   -538  -1006    131       N  
ATOM   2855  CA  THR A1152      -6.289 -14.423  18.492  1.00 45.96           C  
ANISOU 2855  CA  THR A1152     6489   6172   4800   -580  -1014    107       C  
ATOM   2856  C   THR A1152      -7.800 -14.590  18.638  1.00 50.21           C  
ANISOU 2856  C   THR A1152     7025   6821   5233   -622   -946     25       C  
ATOM   2857  O   THR A1152      -8.327 -14.574  19.749  1.00 50.06           O  
ANISOU 2857  O   THR A1152     7049   6863   5109   -720   -943     27       O  
ATOM   2858  CB  THR A1152      -6.008 -12.966  18.105  1.00 51.98           C  
ANISOU 2858  CB  THR A1152     7248   6957   5545   -492   -996     51       C  
ATOM   2859  OG1 THR A1152      -4.613 -12.805  17.799  1.00 50.59           O  
ANISOU 2859  OG1 THR A1152     7063   6676   5484   -446  -1046    114       O  
ATOM   2860  CG2 THR A1152      -6.416 -12.028  19.242  1.00 50.33           C  
ANISOU 2860  CG2 THR A1152     7089   6829   5206   -550   -991     23       C  
ATOM   2861  N   PHE A1153      -8.492 -14.726  17.506  1.00 46.76           N  
ANISOU 2861  N   PHE A1153     6538   6408   4822   -560   -889    -47       N  
ATOM   2862  CA  PHE A1153      -9.928 -14.988  17.509  1.00 46.82           C  
ANISOU 2862  CA  PHE A1153     6517   6510   4762   -597   -832   -118       C  
ATOM   2863  C   PHE A1153     -10.235 -16.319  18.177  1.00 52.15           C  
ANISOU 2863  C   PHE A1153     7218   7179   5419   -709   -838    -71       C  
ATOM   2864  O   PHE A1153     -11.292 -16.474  18.790  1.00 52.65           O  
ANISOU 2864  O   PHE A1153     7281   7324   5401   -782   -795   -112       O  
ATOM   2865  CB  PHE A1153     -10.491 -15.043  16.089  1.00 48.04           C  
ANISOU 2865  CB  PHE A1153     6618   6680   4954   -531   -800   -178       C  
ATOM   2866  CG  PHE A1153     -10.821 -13.703  15.494  1.00 49.18           C  
ANISOU 2866  CG  PHE A1153     6726   6869   5090   -442   -790   -237       C  
ATOM   2867  CD1 PHE A1153     -11.519 -12.740  16.217  1.00 52.82           C  
ANISOU 2867  CD1 PHE A1153     7163   7399   5506   -436   -762   -284       C  
ATOM   2868  CD2 PHE A1153     -10.496 -13.432  14.179  1.00 50.46           C  
ANISOU 2868  CD2 PHE A1153     6881   6998   5295   -377   -801   -248       C  
ATOM   2869  CE1 PHE A1153     -11.837 -11.509  15.635  1.00 53.44           C  
ANISOU 2869  CE1 PHE A1153     7196   7500   5610   -348   -757   -328       C  
ATOM   2870  CE2 PHE A1153     -10.817 -12.229  13.597  1.00 53.07           C  
ANISOU 2870  CE2 PHE A1153     7181   7361   5622   -304   -810   -283       C  
ATOM   2871  CZ  PHE A1153     -11.485 -11.259  14.320  1.00 51.63           C  
ANISOU 2871  CZ  PHE A1153     6960   7236   5420   -280   -794   -318       C  
ATOM   2872  N   ARG A1154      -9.327 -17.283  18.042  1.00 48.67           N  
ANISOU 2872  N   ARG A1154     6791   6630   5070   -726   -884     14       N  
ATOM   2873  CA  ARG A1154      -9.583 -18.644  18.518  1.00 48.82           C  
ANISOU 2873  CA  ARG A1154     6830   6620   5099   -827   -896     69       C  
ATOM   2874  C   ARG A1154      -9.425 -18.729  20.040  1.00 52.75           C  
ANISOU 2874  C   ARG A1154     7396   7132   5514   -946   -957    152       C  
ATOM   2875  O   ARG A1154     -10.327 -19.199  20.736  1.00 52.77           O  
ANISOU 2875  O   ARG A1154     7429   7200   5420  -1052   -929    138       O  
ATOM   2876  CB  ARG A1154      -8.665 -19.645  17.793  1.00 48.31           C  
ANISOU 2876  CB  ARG A1154     6745   6413   5199   -800   -913    128       C  
ATOM   2877  CG  ARG A1154      -8.902 -21.106  18.153  1.00 56.72           C  
ANISOU 2877  CG  ARG A1154     7822   7423   6305   -894   -922    187       C  
ATOM   2878  CD  ARG A1154      -8.169 -22.046  17.203  1.00 62.16           C  
ANISOU 2878  CD  ARG A1154     8476   7963   7180   -857   -895    205       C  
ATOM   2879  NE  ARG A1154      -6.755 -21.706  17.038  1.00 66.01           N  
ANISOU 2879  NE  ARG A1154     8938   8327   7816   -788   -936    267       N  
ATOM   2880  CZ  ARG A1154      -5.793 -21.980  17.918  1.00 78.22           C  
ANISOU 2880  CZ  ARG A1154    10481   9773   9465   -820  -1039    406       C  
ATOM   2881  NH1 ARG A1154      -6.070 -22.596  19.065  1.00 64.76           N  
ANISOU 2881  NH1 ARG A1154     8817   8079   7709   -931  -1120    505       N  
ATOM   2882  NH2 ARG A1154      -4.540 -21.619  17.658  1.00 63.66           N  
ANISOU 2882  NH2 ARG A1154     8593   7817   7776   -751  -1069    453       N  
ATOM   2883  N   THR A1155      -8.294 -18.227  20.540  1.00 48.89           N  
ANISOU 2883  N   THR A1155     6938   6585   5054   -943  -1038    234       N  
ATOM   2884  CA  THR A1155      -7.890 -18.389  21.941  1.00 49.17           C  
ANISOU 2884  CA  THR A1155     7054   6611   5016  -1081  -1131    345       C  
ATOM   2885  C   THR A1155      -8.123 -17.155  22.807  1.00 53.17           C  
ANISOU 2885  C   THR A1155     7625   7216   5363  -1135  -1113    296       C  
ATOM   2886  O   THR A1155      -8.170 -17.269  24.024  1.00 54.11           O  
ANISOU 2886  O   THR A1155     7837   7364   5360  -1291  -1158    353       O  
ATOM   2887  CB  THR A1155      -6.377 -18.744  22.040  1.00 54.17           C  
ANISOU 2887  CB  THR A1155     7676   7099   5806  -1070  -1261    498       C  
ATOM   2888  OG1 THR A1155      -5.583 -17.578  21.769  1.00 53.34           O  
ANISOU 2888  OG1 THR A1155     7554   6983   5730   -982  -1277    480       O  
ATOM   2889  CG2 THR A1155      -5.997 -19.860  21.061  1.00 50.48           C  
ANISOU 2889  CG2 THR A1155     7131   6505   5543   -999  -1249    528       C  
ATOM   2890  N   GLY A1156      -8.222 -15.980  22.191  1.00 48.92           N  
ANISOU 2890  N   GLY A1156     7047   6717   4824  -1019  -1048    192       N  
ATOM   2891  CA  GLY A1156      -8.382 -14.717  22.923  1.00 49.15           C  
ANISOU 2891  CA  GLY A1156     7128   6818   4728  -1057  -1011    130       C  
ATOM   2892  C   GLY A1156      -7.147 -14.184  23.648  1.00 54.48           C  
ANISOU 2892  C   GLY A1156     7872   7445   5385  -1110  -1119    228       C  
ATOM   2893  O   GLY A1156      -7.242 -13.213  24.386  1.00 54.44           O  
ANISOU 2893  O   GLY A1156     7932   7493   5258  -1175  -1088    179       O  
ATOM   2894  N   THR A1157      -5.992 -14.812  23.448  1.00 52.08           N  
ANISOU 2894  N   THR A1157     7546   7030   5211  -1091  -1242    364       N  
ATOM   2895  CA  THR A1157      -4.730 -14.381  24.074  1.00 52.56           C  
ANISOU 2895  CA  THR A1157     7650   7033   5286  -1141  -1371    479       C  
ATOM   2896  C   THR A1157      -3.788 -13.817  23.007  1.00 56.38           C  
ANISOU 2896  C   THR A1157     8048   7440   5936   -974  -1379    472       C  
ATOM   2897  O   THR A1157      -4.009 -14.044  21.814  1.00 55.57           O  
ANISOU 2897  O   THR A1157     7863   7310   5940   -843  -1303    406       O  
ATOM   2898  CB  THR A1157      -4.018 -15.566  24.744  1.00 60.39           C  
ANISOU 2898  CB  THR A1157     8666   7935   6344  -1258  -1529    668       C  
ATOM   2899  OG1 THR A1157      -3.714 -16.563  23.755  1.00 60.16           O  
ANISOU 2899  OG1 THR A1157     8530   7799   6530  -1148  -1532    706       O  
ATOM   2900  CG2 THR A1157      -4.894 -16.167  25.834  1.00 58.88           C  
ANISOU 2900  CG2 THR A1157     8580   7817   5975  -1449  -1530    688       C  
ATOM   2901  N   TRP A1158      -2.735 -13.116  23.427  1.00 53.40           N  
ANISOU 2901  N   TRP A1158     7695   7024   5572   -994  -1470    541       N  
ATOM   2902  CA  TRP A1158      -1.738 -12.578  22.485  1.00 52.60           C  
ANISOU 2902  CA  TRP A1158     7513   6841   5631   -852  -1477    541       C  
ATOM   2903  C   TRP A1158      -0.590 -13.562  22.184  1.00 59.14           C  
ANISOU 2903  C   TRP A1158     8260   7519   6692   -827  -1582    684       C  
ATOM   2904  O   TRP A1158       0.510 -13.133  21.829  1.00 59.00           O  
ANISOU 2904  O   TRP A1158     8188   7419   6811   -764  -1626    725       O  
ATOM   2905  CB  TRP A1158      -1.143 -11.253  23.000  1.00 50.93           C  
ANISOU 2905  CB  TRP A1158     7356   6657   5340   -877  -1512    534       C  
ATOM   2906  CG  TRP A1158      -2.158 -10.206  23.361  1.00 51.31           C  
ANISOU 2906  CG  TRP A1158     7476   6825   5193   -904  -1398    392       C  
ATOM   2907  CD1 TRP A1158      -2.662  -9.968  24.594  1.00 55.15           C  
ANISOU 2907  CD1 TRP A1158     8075   7389   5490  -1070  -1395    380       C  
ATOM   2908  CD2 TRP A1158      -2.783  -9.263  22.485  1.00 49.98           C  
ANISOU 2908  CD2 TRP A1158     7270   6699   5020   -770  -1264    243       C  
ATOM   2909  NE1 TRP A1158      -3.572  -8.945  24.553  1.00 54.25           N  
ANISOU 2909  NE1 TRP A1158     7984   7355   5275  -1039  -1248    219       N  
ATOM   2910  CE2 TRP A1158      -3.669  -8.493  23.266  1.00 54.44           C  
ANISOU 2910  CE2 TRP A1158     7909   7356   5419   -849  -1179    144       C  
ATOM   2911  CE3 TRP A1158      -2.698  -9.008  21.114  1.00 49.99           C  
ANISOU 2911  CE3 TRP A1158     7188   6665   5144   -604  -1208    187       C  
ATOM   2912  CZ2 TRP A1158      -4.463  -7.472  22.723  1.00 53.15           C  
ANISOU 2912  CZ2 TRP A1158     7715   7238   5242   -748  -1049      0       C  
ATOM   2913  CZ3 TRP A1158      -3.483  -7.995  20.575  1.00 50.83           C  
ANISOU 2913  CZ3 TRP A1158     7280   6826   5206   -518  -1100     58       C  
ATOM   2914  CH2 TRP A1158      -4.356  -7.241  21.379  1.00 51.99           C  
ANISOU 2914  CH2 TRP A1158     7479   7053   5220   -581  -1027    -29       C  
ATOM   2915  N   ASP A1159      -0.837 -14.870  22.299  1.00 57.34           N  
ANISOU 2915  N   ASP A1159     8012   7243   6532   -875  -1612    754       N  
ATOM   2916  CA  ASP A1159       0.223 -15.877  22.105  1.00 58.33           C  
ANISOU 2916  CA  ASP A1159     8046   7202   6915   -859  -1707    895       C  
ATOM   2917  C   ASP A1159       0.912 -15.803  20.727  1.00 61.93           C  
ANISOU 2917  C   ASP A1159     8389   7551   7590   -698  -1616    833       C  
ATOM   2918  O   ASP A1159       2.095 -16.152  20.590  1.00 61.90           O  
ANISOU 2918  O   ASP A1159     8296   7399   7825   -670  -1686    936       O  
ATOM   2919  CB  ASP A1159      -0.332 -17.293  22.334  1.00 61.16           C  
ANISOU 2919  CB  ASP A1159     8404   7524   7312   -928  -1723    957       C  
ATOM   2920  CG  ASP A1159      -0.559 -17.614  23.815  1.00 74.43           C  
ANISOU 2920  CG  ASP A1159    10189   9253   8838  -1122  -1864   1086       C  
ATOM   2921  OD1 ASP A1159       0.348 -17.351  24.644  1.00 76.04           O  
ANISOU 2921  OD1 ASP A1159    10416   9416   9060  -1210  -2028   1231       O  
ATOM   2922  OD2 ASP A1159      -1.647 -18.149  24.144  1.00 81.04           O  
ANISOU 2922  OD2 ASP A1159    11090  10168   9532  -1200  -1813   1046       O  
ATOM   2923  N   ALA A1160       0.179 -15.345  19.717  1.00 58.08           N  
ANISOU 2923  N   ALA A1160     7906   7134   7028   -604  -1460    667       N  
ATOM   2924  CA  ALA A1160       0.704 -15.280  18.350  1.00 57.76           C  
ANISOU 2924  CA  ALA A1160     7789   7006   7152   -481  -1354    590       C  
ATOM   2925  C   ALA A1160       1.584 -14.049  18.101  1.00 61.82           C  
ANISOU 2925  C   ALA A1160     8291   7507   7692   -419  -1361    572       C  
ATOM   2926  O   ALA A1160       2.324 -14.005  17.103  1.00 61.66           O  
ANISOU 2926  O   ALA A1160     8205   7387   7837   -338  -1289    534       O  
ATOM   2927  CB  ALA A1160      -0.446 -15.346  17.348  1.00 57.69           C  
ANISOU 2927  CB  ALA A1160     7801   7076   7041   -433  -1209    439       C  
ATOM   2928  N   TYR A1161       1.496 -13.101  19.006  1.00 58.11           N  
ANISOU 2928  N   TYR A1161     7889   7131   7059   -471  -1434    591       N  
ATOM   2929  CA  TYR A1161       2.175 -11.840  18.886  1.00 57.45           C  
ANISOU 2929  CA  TYR A1161     7811   7054   6962   -426  -1440    566       C  
ATOM   2930  C   TYR A1161       3.134 -11.623  20.036  1.00 63.87           C  
ANISOU 2930  C   TYR A1161     8632   7831   7806   -518  -1604    711       C  
ATOM   2931  O   TYR A1161       3.746 -10.602  20.151  1.00 63.57           O  
ANISOU 2931  O   TYR A1161     8606   7799   7748   -507  -1631    707       O  
ATOM   2932  CB  TYR A1161       1.148 -10.710  18.863  1.00 57.21           C  
ANISOU 2932  CB  TYR A1161     7862   7170   6704   -409  -1364    439       C  
ATOM   2933  CG  TYR A1161       0.307 -10.655  17.620  1.00 57.18           C  
ANISOU 2933  CG  TYR A1161     7847   7203   6677   -317  -1228    309       C  
ATOM   2934  CD1 TYR A1161       0.794 -10.118  16.457  1.00 58.27           C  
ANISOU 2934  CD1 TYR A1161     7955   7293   6892   -224  -1158    247       C  
ATOM   2935  CD2 TYR A1161      -0.968 -11.126  17.618  1.00 57.57           C  
ANISOU 2935  CD2 TYR A1161     7918   7335   6619   -341  -1178    253       C  
ATOM   2936  CE1 TYR A1161       0.052 -10.068  15.368  1.00 57.89           C  
ANISOU 2936  CE1 TYR A1161     7911   7280   6805   -169  -1059    147       C  
ATOM   2937  CE2 TYR A1161      -1.709 -11.070  16.523  1.00 57.72           C  
ANISOU 2937  CE2 TYR A1161     7925   7388   6617   -275  -1082    153       C  
ATOM   2938  CZ  TYR A1161      -1.194 -10.541  15.401  1.00 63.36           C  
ANISOU 2938  CZ  TYR A1161     8621   8055   7397   -195  -1030    105       C  
ATOM   2939  OH  TYR A1161      -1.945 -10.496  14.287  1.00 62.35           O  
ANISOU 2939  OH  TYR A1161     8495   7964   7231   -154   -952     19       O  
ATOM   2940  N   GLY A1200       3.313 -12.594  20.916  1.00 62.31           N  
ANISOU 2940  N   GLY A1200     7956   7909   7810    107     23     39       N  
ATOM   2941  CA  GLY A1200       4.094 -12.356  22.113  1.00 62.66           C  
ANISOU 2941  CA  GLY A1200     8000   7953   7854    107     23     39       C  
ATOM   2942  C   GLY A1200       5.480 -12.761  22.597  1.00 68.14           C  
ANISOU 2942  C   GLY A1200     8694   8647   8548    107     23     39       C  
ATOM   2943  O   GLY A1200       6.163 -11.984  23.228  1.00 68.19           O  
ANISOU 2943  O   GLY A1200     8701   8654   8555    107     22     39       O  
ATOM   2944  N   SER A1201       5.795 -14.033  22.411  1.00 65.42           N  
ANISOU 2944  N   SER A1201     8350   8303   8203    108     23     39       N  
ATOM   2945  CA  SER A1201       6.674 -14.798  23.290  1.00 65.56           C  
ANISOU 2945  CA  SER A1201     8368   8321   8220    108     23     39       C  
ATOM   2946  C   SER A1201       8.077 -14.270  23.162  1.00 70.38           C  
ANISOU 2946  C   SER A1201     8978   8932   8831    108     23     40       C  
ATOM   2947  O   SER A1201       8.419 -13.581  22.217  1.00 70.04           O  
ANISOU 2947  O   SER A1201     8934   8889   8788    108     22     40       O  
ATOM   2948  CB  SER A1201       6.706 -16.310  23.060  1.00 69.03           C  
ANISOU 2948  CB  SER A1201     8808   8761   8659    108     24     39       C  
ATOM   2949  OG  SER A1201       5.556 -16.949  23.570  1.00 78.01           O  
ANISOU 2949  OG  SER A1201     9946   9897   9797    108     24     39       O  
ATOM   2950  N   LYS A 230       8.812 -14.433  24.247  1.00 72.41           N  
ANISOU 2950  N   LYS A 230    10087   9207   8221    273   -591    518       N  
ATOM   2951  CA  LYS A 230       9.812 -15.445  24.586  1.00 71.88           C  
ANISOU 2951  CA  LYS A 230     9988   9164   8160    253   -517    492       C  
ATOM   2952  C   LYS A 230       9.415 -15.931  25.992  1.00 74.26           C  
ANISOU 2952  C   LYS A 230    10164   9488   8562    238   -535    466       C  
ATOM   2953  O   LYS A 230      10.211 -15.930  26.928  1.00 73.33           O  
ANISOU 2953  O   LYS A 230     9980   9386   8495    218   -466    462       O  
ATOM   2954  CB  LYS A 230      11.258 -14.933  24.492  1.00 74.67           C  
ANISOU 2954  CB  LYS A 230    10367   9512   8491    237   -400    510       C  
ATOM   2955  CG  LYS A 230      12.224 -15.959  23.828  1.00 89.14           C  
ANISOU 2955  CG  LYS A 230    12251  11352  10268    229   -341    486       C  
ATOM   2956  CD  LYS A 230      12.194 -17.363  24.477  1.00 99.02           C  
ANISOU 2956  CD  LYS A 230    13429  12631  11563    219   -357    441       C  
ATOM   2957  CE  LYS A 230      12.170 -18.478  23.416  1.00110.94           C  
ANISOU 2957  CE  LYS A 230    15011  14142  13000    229   -381    415       C  
ATOM   2958  NZ  LYS A 230      12.343 -19.861  23.978  1.00119.72           N  
ANISOU 2958  NZ  LYS A 230    16058  15278  14153    217   -383    371       N  
ATOM   2959  N   GLY A 231       8.157 -16.359  26.104  1.00 70.38           N  
ANISOU 2959  N   GLY A 231     9645   8997   8099    249   -628    447       N  
ATOM   2960  CA  GLY A 231       7.500 -16.614  27.382  1.00 69.41           C  
ANISOU 2960  CA  GLY A 231     9412   8888   8072    236   -655    428       C  
ATOM   2961  C   GLY A 231       7.893 -17.879  28.124  1.00 72.49           C  
ANISOU 2961  C   GLY A 231     9742   9302   8497    218   -624    395       C  
ATOM   2962  O   GLY A 231       7.241 -18.243  29.106  1.00 71.41           O  
ANISOU 2962  O   GLY A 231     9525   9175   8433    207   -651    377       O  
ATOM   2963  N   HIS A 232       8.942 -18.555  27.656  1.00 68.93           N  
ANISOU 2963  N   HIS A 232     9333   8859   7998    212   -568    387       N  
ATOM   2964  CA  HIS A 232       9.497 -19.715  28.352  1.00 67.95           C  
ANISOU 2964  CA  HIS A 232     9157   8755   7907    195   -533    357       C  
ATOM   2965  C   HIS A 232      10.545 -19.215  29.348  1.00 69.37           C  
ANISOU 2965  C   HIS A 232     9285   8944   8130    177   -451    366       C  
ATOM   2966  O   HIS A 232      10.652 -19.741  30.469  1.00 68.36           O  
ANISOU 2966  O   HIS A 232     9083   8829   8061    162   -438    349       O  
ATOM   2967  CB  HIS A 232      10.075 -20.733  27.348  1.00 69.33           C  
ANISOU 2967  CB  HIS A 232     9396   8931   8014    199   -520    336       C  
ATOM   2968  CG  HIS A 232       9.070 -21.226  26.342  1.00 73.51           C  
ANISOU 2968  CG  HIS A 232     9980   9451   8500    221   -605    323       C  
ATOM   2969  ND1 HIS A 232       8.602 -22.524  26.324  1.00 75.36           N  
ANISOU 2969  ND1 HIS A 232    10192   9692   8748    222   -649    287       N  
ATOM   2970  CD2 HIS A 232       8.433 -20.585  25.328  1.00 75.85           C  
ANISOU 2970  CD2 HIS A 232    10351   9728   8743    245   -658    340       C  
ATOM   2971  CE1 HIS A 232       7.727 -22.662  25.341  1.00 75.28           C  
ANISOU 2971  CE1 HIS A 232    10239   9668   8697    247   -726    279       C  
ATOM   2972  NE2 HIS A 232       7.603 -21.500  24.724  1.00 75.95           N  
ANISOU 2972  NE2 HIS A 232    10384   9735   8738    262   -735    311       N  
ATOM   2973  N   GLN A 233      11.297 -18.187  28.944  1.00 64.38           N  
ANISOU 2973  N   GLN A 233     8692   8300   7467    179   -397    393       N  
ATOM   2974  CA  GLN A 233      12.226 -17.501  29.850  1.00 62.84           C  
ANISOU 2974  CA  GLN A 233     8447   8108   7321    166   -324    402       C  
ATOM   2975  C   GLN A 233      11.477 -16.567  30.821  1.00 63.88           C  
ANISOU 2975  C   GLN A 233     8513   8241   7516    166   -353    419       C  
ATOM   2976  O   GLN A 233      11.816 -16.509  32.003  1.00 63.39           O  
ANISOU 2976  O   GLN A 233     8379   8190   7517    155   -324    411       O  
ATOM   2977  CB  GLN A 233      13.289 -16.720  29.068  1.00 64.64           C  
ANISOU 2977  CB  GLN A 233     8738   8319   7502    168   -251    422       C  
ATOM   2978  CG  GLN A 233      14.275 -17.601  28.290  1.00 85.20           C  
ANISOU 2978  CG  GLN A 233    11395  10921  10055    162   -200    399       C  
ATOM   2979  CD  GLN A 233      15.337 -18.259  29.180  1.00109.57           C  
ANISOU 2979  CD  GLN A 233    14418  14018  13195    146   -142    367       C  
ATOM   2980  OE1 GLN A 233      16.115 -17.575  29.852  1.00105.20           O  
ANISOU 2980  OE1 GLN A 233    13823  13458  12688    140    -85    370       O  
ATOM   2981  NE2 GLN A 233      15.380 -19.597  29.169  1.00104.01           N  
ANISOU 2981  NE2 GLN A 233    13707  13326  12487    142   -161    333       N  
ATOM   2982  N   LYS A 234      10.468 -15.849  30.328  1.00 58.11           N  
ANISOU 2982  N   LYS A 234     7808   7498   6771    179   -412    439       N  
ATOM   2983  CA  LYS A 234       9.642 -14.985  31.179  1.00 56.38           C  
ANISOU 2983  CA  LYS A 234     7526   7279   6616    179   -447    451       C  
ATOM   2984  C   LYS A 234       8.958 -15.736  32.323  1.00 57.99           C  
ANISOU 2984  C   LYS A 234     7648   7499   6887    167   -478    424       C  
ATOM   2985  O   LYS A 234       8.877 -15.228  33.436  1.00 56.98           O  
ANISOU 2985  O   LYS A 234     7450   7379   6821    159   -464    426       O  
ATOM   2986  CB  LYS A 234       8.586 -14.244  30.357  1.00 58.99           C  
ANISOU 2986  CB  LYS A 234     7902   7588   6921    197   -519    470       C  
ATOM   2987  CG  LYS A 234       9.035 -12.895  29.853  1.00 72.22           C  
ANISOU 2987  CG  LYS A 234     9624   9246   8571    205   -488    508       C  
ATOM   2988  CD  LYS A 234       8.045 -12.308  28.843  1.00 81.92           C  
ANISOU 2988  CD  LYS A 234    10920  10449   9759    226   -567    526       C  
ATOM   2989  CE  LYS A 234       8.347 -10.839  28.553  1.00 91.29           C  
ANISOU 2989  CE  LYS A 234    12138  11614  10934    232   -543    566       C  
ATOM   2990  NZ  LYS A 234       9.807 -10.579  28.328  1.00 99.74           N  
ANISOU 2990  NZ  LYS A 234    13243  12682  11971    223   -437    583       N  
ATOM   2991  N   ARG A 235       8.465 -16.936  32.050  1.00 53.54           N  
ANISOU 2991  N   ARG A 235     7094   6939   6310    167   -518    398       N  
ATOM   2992  CA  ARG A 235       7.833 -17.754  33.090  1.00 52.48           C  
ANISOU 2992  CA  ARG A 235     6888   6816   6236    154   -541    372       C  
ATOM   2993  C   ARG A 235       8.848 -18.325  34.101  1.00 53.49           C  
ANISOU 2993  C   ARG A 235     6973   6960   6391    138   -476    360       C  
ATOM   2994  O   ARG A 235       8.507 -18.538  35.263  1.00 52.91           O  
ANISOU 2994  O   ARG A 235     6835   6895   6374    126   -476    350       O  
ATOM   2995  CB  ARG A 235       6.972 -18.879  32.473  1.00 53.97           C  
ANISOU 2995  CB  ARG A 235     7097   7000   6409    160   -605    346       C  
ATOM   2996  CG  ARG A 235       5.591 -18.394  31.969  1.00 66.70           C  
ANISOU 2996  CG  ARG A 235     8717   8593   8033    175   -689    346       C  
ATOM   2997  CD  ARG A 235       4.549 -19.531  31.820  1.00 77.83           C  
ANISOU 2997  CD  ARG A 235    10111   9996   9465    176   -754    310       C  
ATOM   2998  NE  ARG A 235       4.691 -20.305  30.582  1.00 83.84           N  
ANISOU 2998  NE  ARG A 235    10946  10752  10158    193   -781    299       N  
ATOM   2999  CZ  ARG A 235       5.394 -21.431  30.450  1.00 97.47           C  
ANISOU 2999  CZ  ARG A 235    12687  12491  11858    187   -750    283       C  
ATOM   3000  NH1 ARG A 235       5.451 -22.040  29.266  1.00 85.59           N  
ANISOU 3000  NH1 ARG A 235    11250  10980  10290    204   -779    271       N  
ATOM   3001  NH2 ARG A 235       6.056 -21.955  31.478  1.00 83.11           N  
ANISOU 3001  NH2 ARG A 235    10816  10688  10072    165   -693    277       N  
ATOM   3002  N   LYS A 236      10.077 -18.569  33.652  1.00 47.56           N  
ANISOU 3002  N   LYS A 236     6261   6210   5599    139   -422    360       N  
ATOM   3003  CA  LYS A 236      11.166 -18.974  34.540  1.00 45.87           C  
ANISOU 3003  CA  LYS A 236     6011   6005   5411    128   -362    346       C  
ATOM   3004  C   LYS A 236      11.582 -17.788  35.432  1.00 47.62           C  
ANISOU 3004  C   LYS A 236     6189   6228   5678    127   -323    363       C  
ATOM   3005  O   LYS A 236      11.987 -17.971  36.591  1.00 46.36           O  
ANISOU 3005  O   LYS A 236     5977   6075   5564    119   -298    351       O  
ATOM   3006  CB  LYS A 236      12.364 -19.482  33.720  1.00 48.13           C  
ANISOU 3006  CB  LYS A 236     6350   6287   5648    129   -315    336       C  
ATOM   3007  CG  LYS A 236      13.489 -20.122  34.541  1.00 61.35           C  
ANISOU 3007  CG  LYS A 236     7990   7966   7353    120   -265    312       C  
ATOM   3008  CD  LYS A 236      13.616 -21.645  34.311  1.00 72.13           C  
ANISOU 3008  CD  LYS A 236     9369   9336   8702    114   -280    281       C  
ATOM   3009  CE  LYS A 236      14.805 -22.242  35.097  1.00 81.84           C  
ANISOU 3009  CE  LYS A 236    10567  10564   9963    106   -234    255       C  
ATOM   3010  NZ  LYS A 236      14.757 -23.745  35.223  1.00 89.33           N  
ANISOU 3010  NZ  LYS A 236    11513  11516  10913     99   -259    225       N  
ATOM   3011  N   ALA A 237      11.482 -16.577  34.875  1.00 42.54           N  
ANISOU 3011  N   ALA A 237     5568   5574   5020    136   -321    390       N  
ATOM   3012  CA  ALA A 237      11.747 -15.347  35.618  1.00 40.92           C  
ANISOU 3012  CA  ALA A 237     5321   5368   4859    137   -292    407       C  
ATOM   3013  C   ALA A 237      10.688 -15.116  36.710  1.00 42.18           C  
ANISOU 3013  C   ALA A 237     5413   5536   5078    132   -332    404       C  
ATOM   3014  O   ALA A 237      11.016 -14.688  37.812  1.00 41.10           O  
ANISOU 3014  O   ALA A 237     5221   5406   4990    128   -304    402       O  
ATOM   3015  CB  ALA A 237      11.802 -14.153  34.660  1.00 41.87           C  
ANISOU 3015  CB  ALA A 237     5489   5471   4947    148   -285    438       C  
ATOM   3016  N   LEU A 238       9.427 -15.403  36.386  1.00 37.40           N  
ANISOU 3016  N   LEU A 238     4813   4929   4470    131   -397    401       N  
ATOM   3017  CA  LEU A 238       8.323 -15.244  37.322  1.00 36.24           C  
ANISOU 3017  CA  LEU A 238     4603   4785   4381    123   -435    394       C  
ATOM   3018  C   LEU A 238       8.453 -16.254  38.441  1.00 38.32           C  
ANISOU 3018  C   LEU A 238     4823   5061   4675    109   -416    370       C  
ATOM   3019  O   LEU A 238       8.197 -15.939  39.604  1.00 38.19           O  
ANISOU 3019  O   LEU A 238     4750   5051   4710    101   -407    366       O  
ATOM   3020  CB  LEU A 238       6.947 -15.419  36.627  1.00 36.50           C  
ANISOU 3020  CB  LEU A 238     4651   4807   4410    127   -511    388       C  
ATOM   3021  CG  LEU A 238       5.707 -15.053  37.480  1.00 40.66           C  
ANISOU 3021  CG  LEU A 238     5112   5332   5006    118   -549    378       C  
ATOM   3022  CD1 LEU A 238       5.784 -13.608  37.972  1.00 40.59           C  
ANISOU 3022  CD1 LEU A 238     5069   5323   5032    121   -534    397       C  
ATOM   3023  CD2 LEU A 238       4.390 -15.260  36.760  1.00 42.71           C  
ANISOU 3023  CD2 LEU A 238     5383   5573   5270    124   -627    364       C  
ATOM   3024  N   LYS A 239       8.854 -17.468  38.087  1.00 33.18           N  
ANISOU 3024  N   LYS A 239     4203   4412   3993    107   -411    354       N  
ATOM   3025  CA  LYS A 239       8.916 -18.576  39.050  1.00 31.54           C  
ANISOU 3025  CA  LYS A 239     3964   4211   3809     93   -401    332       C  
ATOM   3026  C   LYS A 239      10.013 -18.321  40.071  1.00 32.36           C  
ANISOU 3026  C   LYS A 239     4040   4320   3934     93   -347    331       C  
ATOM   3027  O   LYS A 239       9.800 -18.493  41.264  1.00 31.19           O  
ANISOU 3027  O   LYS A 239     3850   4176   3824     84   -340    323       O  
ATOM   3028  CB  LYS A 239       9.126 -19.926  38.322  1.00 33.66           C  
ANISOU 3028  CB  LYS A 239     4274   4477   4037     92   -413    315       C  
ATOM   3029  CG  LYS A 239       8.888 -21.184  39.181  1.00 43.28           C  
ANISOU 3029  CG  LYS A 239     5466   5698   5282     78   -417    293       C  
ATOM   3030  CD  LYS A 239       9.176 -22.488  38.404  1.00 52.03           C  
ANISOU 3030  CD  LYS A 239     6613   6803   6353     78   -429    274       C  
ATOM   3031  CE  LYS A 239       9.532 -23.648  39.349  1.00 62.27           C  
ANISOU 3031  CE  LYS A 239     7890   8100   7670     66   -413    255       C  
ATOM   3032  NZ  LYS A 239       9.394 -25.008  38.745  1.00 69.44           N  
ANISOU 3032  NZ  LYS A 239     8821   9004   8558     62   -438    235       N  
ATOM   3033  N   THR A 240      11.178 -17.899  39.584  1.00 27.98           N  
ANISOU 3033  N   THR A 240     3513   3763   3356    103   -307    338       N  
ATOM   3034  CA  THR A 240      12.297 -17.514  40.456  1.00 26.89           C  
ANISOU 3034  CA  THR A 240     3347   3625   3244    107   -257    332       C  
ATOM   3035  C   THR A 240      11.895 -16.430  41.437  1.00 29.22           C  
ANISOU 3035  C   THR A 240     3590   3925   3587    109   -256    343       C  
ATOM   3036  O   THR A 240      12.104 -16.569  42.638  1.00 28.20           O  
ANISOU 3036  O   THR A 240     3424   3799   3490    107   -242    331       O  
ATOM   3037  CB  THR A 240      13.489 -16.956  39.680  1.00 34.57           C  
ANISOU 3037  CB  THR A 240     4351   4588   4195    118   -212    337       C  
ATOM   3038  OG1 THR A 240      13.913 -17.896  38.694  1.00 34.84           O  
ANISOU 3038  OG1 THR A 240     4437   4618   4183    116   -208    325       O  
ATOM   3039  CG2 THR A 240      14.633 -16.678  40.631  1.00 33.76           C  
ANISOU 3039  CG2 THR A 240     4214   4482   4131    124   -166    323       C  
ATOM   3040  N   THR A 241      11.307 -15.353  40.927  1.00 25.04           N  
ANISOU 3040  N   THR A 241     3061   3394   3060    113   -272    365       N  
ATOM   3041  CA  THR A 241      10.939 -14.277  41.801  1.00 24.03           C  
ANISOU 3041  CA  THR A 241     2881   3269   2980    114   -271    373       C  
ATOM   3042  C   THR A 241       9.919 -14.738  42.849  1.00 27.47           C  
ANISOU 3042  C   THR A 241     3274   3713   3449    100   -297    360       C  
ATOM   3043  O   THR A 241      10.064 -14.403  44.020  1.00 27.40           O  
ANISOU 3043  O   THR A 241     3223   3710   3478    100   -278    354       O  
ATOM   3044  CB  THR A 241      10.454 -13.005  41.060  1.00 30.03           C  
ANISOU 3044  CB  THR A 241     3647   4023   3741    121   -288    398       C  
ATOM   3045  OG1 THR A 241       9.085 -13.140  40.669  1.00 32.38           O  
ANISOU 3045  OG1 THR A 241     3948   4319   4038    114   -346    400       O  
ATOM   3046  CG2 THR A 241      11.340 -12.673  39.872  1.00 26.19           C  
ANISOU 3046  CG2 THR A 241     3216   3524   3210    132   -261    413       C  
ATOM   3047  N   VAL A 242       8.923 -15.533  42.467  1.00 23.78           N  
ANISOU 3047  N   VAL A 242     2820   3244   2971     90   -337    353       N  
ATOM   3048  CA  VAL A 242       7.937 -15.988  43.453  1.00 23.41           C  
ANISOU 3048  CA  VAL A 242     2734   3199   2961     73   -353    339       C  
ATOM   3049  C   VAL A 242       8.581 -16.871  44.565  1.00 27.62           C  
ANISOU 3049  C   VAL A 242     3259   3736   3498     68   -321    324       C  
ATOM   3050  O   VAL A 242       8.268 -16.712  45.765  1.00 27.41           O  
ANISOU 3050  O   VAL A 242     3195   3713   3506     60   -309    317       O  
ATOM   3051  CB  VAL A 242       6.682 -16.688  42.797  1.00 27.01           C  
ANISOU 3051  CB  VAL A 242     3201   3647   3415     63   -404    329       C  
ATOM   3052  CG1 VAL A 242       5.852 -17.338  43.840  1.00 26.74           C  
ANISOU 3052  CG1 VAL A 242     3129   3611   3419     43   -406    311       C  
ATOM   3053  CG2 VAL A 242       5.815 -15.693  42.033  1.00 26.57           C  
ANISOU 3053  CG2 VAL A 242     3141   3583   3371     69   -446    339       C  
ATOM   3054  N   ILE A 243       9.490 -17.763  44.173  1.00 24.07           N  
ANISOU 3054  N   ILE A 243     2847   3284   3014     72   -308    317       N  
ATOM   3055  CA  ILE A 243      10.203 -18.627  45.119  1.00 23.83           C  
ANISOU 3055  CA  ILE A 243     2817   3252   2984     70   -284    302       C  
ATOM   3056  C   ILE A 243      11.084 -17.831  46.082  1.00 28.09           C  
ANISOU 3056  C   ILE A 243     3331   3793   3546     83   -251    301       C  
ATOM   3057  O   ILE A 243      11.094 -18.074  47.286  1.00 27.46           O  
ANISOU 3057  O   ILE A 243     3235   3714   3485     81   -241    291       O  
ATOM   3058  CB  ILE A 243      11.045 -19.670  44.347  1.00 27.26           C  
ANISOU 3058  CB  ILE A 243     3296   3681   3380     74   -280    291       C  
ATOM   3059  CG1 ILE A 243      10.125 -20.793  43.858  1.00 28.35           C  
ANISOU 3059  CG1 ILE A 243     3452   3816   3504     60   -314    284       C  
ATOM   3060  CG2 ILE A 243      12.208 -20.230  45.177  1.00 26.88           C  
ANISOU 3060  CG2 ILE A 243     3252   3627   3335     81   -254    274       C  
ATOM   3061  CD1 ILE A 243      10.853 -21.970  43.233  1.00 37.21           C  
ANISOU 3061  CD1 ILE A 243     4613   4932   4593     61   -314    269       C  
ATOM   3062  N   LEU A 244      11.830 -16.878  45.540  1.00 25.51           N  
ANISOU 3062  N   LEU A 244     3006   3467   3220     99   -233    309       N  
ATOM   3063  CA  LEU A 244      12.737 -16.033  46.328  1.00 25.10           C  
ANISOU 3063  CA  LEU A 244     2927   3414   3197    115   -202    305       C  
ATOM   3064  C   LEU A 244      11.941 -15.333  47.423  1.00 26.56           C  
ANISOU 3064  C   LEU A 244     3067   3608   3419    111   -208    308       C  
ATOM   3065  O   LEU A 244      12.205 -15.504  48.607  1.00 25.68           O  
ANISOU 3065  O   LEU A 244     2940   3496   3323    115   -197    295       O  
ATOM   3066  CB  LEU A 244      13.414 -15.012  45.384  1.00 25.72           C  
ANISOU 3066  CB  LEU A 244     3012   3488   3273    128   -182    317       C  
ATOM   3067  CG  LEU A 244      14.215 -13.870  46.011  1.00 31.19           C  
ANISOU 3067  CG  LEU A 244     3668   4177   4005    146   -152    314       C  
ATOM   3068  CD1 LEU A 244      15.404 -14.420  46.821  1.00 31.82           C  
ANISOU 3068  CD1 LEU A 244     3744   4246   4099    159   -130    286       C  
ATOM   3069  CD2 LEU A 244      14.668 -12.924  44.924  1.00 33.63           C  
ANISOU 3069  CD2 LEU A 244     3989   4477   4310    154   -131    331       C  
ATOM   3070  N   ILE A 245      10.946 -14.569  46.993  1.00 22.27           N  
ANISOU 3070  N   ILE A 245     2506   3070   2888    103   -228    324       N  
ATOM   3071  CA  ILE A 245      10.022 -13.864  47.884  1.00 21.71           C  
ANISOU 3071  CA  ILE A 245     2388   3006   2855     96   -236    324       C  
ATOM   3072  C   ILE A 245       9.231 -14.757  48.882  1.00 26.28           C  
ANISOU 3072  C   ILE A 245     2959   3586   3441     77   -240    311       C  
ATOM   3073  O   ILE A 245       9.192 -14.448  50.073  1.00 25.62           O  
ANISOU 3073  O   ILE A 245     2848   3506   3381     78   -225    303       O  
ATOM   3074  CB  ILE A 245       9.022 -13.017  47.055  1.00 24.36           C  
ANISOU 3074  CB  ILE A 245     2710   3342   3204     90   -265    340       C  
ATOM   3075  CG1 ILE A 245       9.776 -11.882  46.362  1.00 24.46           C  
ANISOU 3075  CG1 ILE A 245     2725   3351   3217    109   -252    356       C  
ATOM   3076  CG2 ILE A 245       7.899 -12.472  47.939  1.00 24.08           C  
ANISOU 3076  CG2 ILE A 245     2624   3312   3214     77   -277    334       C  
ATOM   3077  CD1 ILE A 245       8.883 -10.981  45.488  1.00 30.85           C  
ANISOU 3077  CD1 ILE A 245     3530   4156   4035    107   -286    374       C  
ATOM   3078  N   LEU A 246       8.595 -15.837  48.429  1.00 23.31           N  
ANISOU 3078  N   LEU A 246     2608   3204   3045     61   -260    307       N  
ATOM   3079  CA  LEU A 246       7.842 -16.672  49.388  1.00 23.58           C  
ANISOU 3079  CA  LEU A 246     2636   3235   3090     41   -257    295       C  
ATOM   3080  C   LEU A 246       8.739 -17.231  50.508  1.00 27.80           C  
ANISOU 3080  C   LEU A 246     3185   3765   3611     48   -230    286       C  
ATOM   3081  O   LEU A 246       8.347 -17.225  51.682  1.00 27.25           O  
ANISOU 3081  O   LEU A 246     3100   3695   3557     40   -215    279       O  
ATOM   3082  CB  LEU A 246       7.117 -17.827  48.718  1.00 23.90           C  
ANISOU 3082  CB  LEU A 246     2700   3266   3115     24   -280    290       C  
ATOM   3083  CG  LEU A 246       5.664 -17.557  48.359  1.00 29.48           C  
ANISOU 3083  CG  LEU A 246     3378   3968   3855      7   -308    286       C  
ATOM   3084  CD1 LEU A 246       5.214 -18.691  47.437  1.00 30.09           C  
ANISOU 3084  CD1 LEU A 246     3485   4034   3914     -1   -336    279       C  
ATOM   3085  CD2 LEU A 246       4.780 -17.481  49.616  1.00 32.50           C  
ANISOU 3085  CD2 LEU A 246     3723   4347   4278    -14   -289    274       C  
ATOM   3086  N   ALA A 247       9.928 -17.712  50.121  1.00 23.85           N  
ANISOU 3086  N   ALA A 247     2718   3261   3083     64   -225    283       N  
ATOM   3087  CA  ALA A 247      10.895 -18.262  51.067  1.00 23.14           C  
ANISOU 3087  CA  ALA A 247     2647   3162   2983     76   -209    270       C  
ATOM   3088  C   ALA A 247      11.378 -17.187  52.031  1.00 26.46           C  
ANISOU 3088  C   ALA A 247     3037   3587   3428     95   -192    266       C  
ATOM   3089  O   ALA A 247      11.617 -17.457  53.201  1.00 26.37           O  
ANISOU 3089  O   ALA A 247     3034   3570   3416    100   -183    256       O  
ATOM   3090  CB  ALA A 247      12.073 -18.845  50.324  1.00 23.74           C  
ANISOU 3090  CB  ALA A 247     2755   3230   3035     91   -210    262       C  
ATOM   3091  N   PHE A 248      11.543 -15.971  51.528  1.00 22.02           N  
ANISOU 3091  N   PHE A 248     2446   3034   2888    106   -189    274       N  
ATOM   3092  CA  PHE A 248      12.012 -14.878  52.359  1.00 21.42           C  
ANISOU 3092  CA  PHE A 248     2335   2962   2842    126   -175    268       C  
ATOM   3093  C   PHE A 248      10.990 -14.715  53.459  1.00 25.01           C  
ANISOU 3093  C   PHE A 248     2768   3423   3312    111   -172    267       C  
ATOM   3094  O   PHE A 248      11.328 -14.741  54.638  1.00 25.39           O  
ANISOU 3094  O   PHE A 248     2818   3468   3363    122   -162    254       O  
ATOM   3095  CB  PHE A 248      12.179 -13.591  51.541  1.00 22.95           C  
ANISOU 3095  CB  PHE A 248     2499   3161   3059    136   -172    280       C  
ATOM   3096  CG  PHE A 248      12.567 -12.378  52.353  1.00 23.84           C  
ANISOU 3096  CG  PHE A 248     2568   3278   3211    156   -159    274       C  
ATOM   3097  CD1 PHE A 248      13.917 -12.041  52.530  1.00 25.81           C  
ANISOU 3097  CD1 PHE A 248     2814   3517   3475    185   -143    259       C  
ATOM   3098  CD2 PHE A 248      11.572 -11.543  52.912  1.00 24.91           C  
ANISOU 3098  CD2 PHE A 248     2662   3426   3377    147   -163    279       C  
ATOM   3099  CE1 PHE A 248      14.267 -10.896  53.271  1.00 26.25           C  
ANISOU 3099  CE1 PHE A 248     2825   3575   3573    206   -133    251       C  
ATOM   3100  CE2 PHE A 248      11.904 -10.392  53.666  1.00 26.64           C  
ANISOU 3100  CE2 PHE A 248     2837   3650   3635    166   -153    271       C  
ATOM   3101  CZ  PHE A 248      13.239 -10.057  53.838  1.00 24.74           C  
ANISOU 3101  CZ  PHE A 248     2593   3400   3407    196   -139    258       C  
ATOM   3102  N  APHE A 249       9.725 -14.578  53.094  0.50 20.34           N  
ANISOU 3102  N  APHE A 249     2159   2838   2732     87   -183    276       N  
ATOM   3103  N  BPHE A 249       9.730 -14.552  53.070  0.50 21.28           N  
ANISOU 3103  N  BPHE A 249     2277   2957   2851     87   -183    276       N  
ATOM   3104  CA APHE A 249       8.712 -14.418  54.117  0.50 19.36           C  
ANISOU 3104  CA APHE A 249     2010   2718   2628     69   -174    270       C  
ATOM   3105  CA BPHE A 249       8.650 -14.425  54.036  0.50 20.79           C  
ANISOU 3105  CA BPHE A 249     2191   2899   2810     68   -175    270       C  
ATOM   3106  C  APHE A 249       8.596 -15.646  55.003  0.50 24.62           C  
ANISOU 3106  C  APHE A 249     2715   3373   3269     57   -162    261       C  
ATOM   3107  C  BPHE A 249       8.591 -15.632  54.973  0.50 25.27           C  
ANISOU 3107  C  BPHE A 249     2796   3455   3351     57   -162    261       C  
ATOM   3108  O  APHE A 249       8.360 -15.508  56.204  0.50 24.44           O  
ANISOU 3108  O  APHE A 249     2686   3349   3251     54   -143    253       O  
ATOM   3109  O  BPHE A 249       8.377 -15.462  56.173  0.50 25.09           O  
ANISOU 3109  O  BPHE A 249     2767   3432   3335     55   -144    253       O  
ATOM   3110  CB APHE A 249       7.400 -13.957  53.505  0.50 20.38           C  
ANISOU 3110  CB APHE A 249     2106   2851   2786     47   -190    275       C  
ATOM   3111  CB BPHE A 249       7.327 -14.161  53.308  0.50 22.39           C  
ANISOU 3111  CB BPHE A 249     2367   3104   3037     44   -193    276       C  
ATOM   3112  CG APHE A 249       7.464 -12.534  53.046  0.50 20.91           C  
ANISOU 3112  CG APHE A 249     2133   2928   2886     60   -199    283       C  
ATOM   3113  CG BPHE A 249       6.183 -15.021  53.764  0.50 23.97           C  
ANISOU 3113  CG BPHE A 249     2571   3296   3242     13   -189    267       C  
ATOM   3114  CD1APHE A 249       7.500 -11.510  53.966  0.50 23.28           C  
ANISOU 3114  CD1APHE A 249     2391   3237   3219     69   -186    276       C  
ATOM   3115  CD1BPHE A 249       5.133 -14.487  54.472  0.50 26.57           C  
ANISOU 3115  CD1BPHE A 249     2859   3626   3610     -6   -178    256       C  
ATOM   3116  CD2APHE A 249       7.578 -12.220  51.711  0.50 22.06           C  
ANISOU 3116  CD2APHE A 249     2285   3071   3025     66   -221    297       C  
ATOM   3117  CD2BPHE A 249       6.142 -16.374  53.445  0.50 25.99           C  
ANISOU 3117  CD2BPHE A 249     2869   3539   3467      1   -193    266       C  
ATOM   3118  CE1APHE A 249       7.592 -10.203  53.542  0.50 23.71           C  
ANISOU 3118  CE1APHE A 249     2407   3297   3305     82   -195    283       C  
ATOM   3119  CE1BPHE A 249       4.088 -15.289  54.871  0.50 27.25           C  
ANISOU 3119  CE1BPHE A 249     2948   3700   3707    -37   -166    245       C  
ATOM   3120  CE2APHE A 249       7.685 -10.927  51.300  0.50 24.25           C  
ANISOU 3120  CE2APHE A 249     2531   3353   3329     79   -228    307       C  
ATOM   3121  CE2BPHE A 249       5.100 -17.168  53.837  0.50 28.34           C  
ANISOU 3121  CE2BPHE A 249     3168   3824   3775    -28   -184    257       C  
ATOM   3122  CZ APHE A 249       7.691  -9.923  52.209  0.50 22.17           C  
ANISOU 3122  CZ APHE A 249     2222   3098   3103     86   -216    300       C  
ATOM   3123  CZ BPHE A 249       4.079 -16.629  54.550  0.50 26.20           C  
ANISOU 3123  CZ BPHE A 249     2858   3553   3545    -47   -169    246       C  
ATOM   3124  N   ALA A 250       8.846 -16.830  54.443  1.00 22.05           N  
ANISOU 3124  N   ALA A 250     2431   3036   2911     52   -171    263       N  
ATOM   3125  CA  ALA A 250       8.772 -18.075  55.221  1.00 22.49           C  
ANISOU 3125  CA  ALA A 250     2528   3076   2941     40   -161    257       C  
ATOM   3126  C   ALA A 250       9.785 -18.137  56.384  1.00 27.57           C  
ANISOU 3126  C   ALA A 250     3197   3712   3566     64   -150    248       C  
ATOM   3127  O   ALA A 250       9.435 -18.500  57.533  1.00 26.57           O  
ANISOU 3127  O   ALA A 250     3090   3577   3429     55   -133    244       O  
ATOM   3128  CB  ALA A 250       8.934 -19.254  54.324  1.00 23.32           C  
ANISOU 3128  CB  ALA A 250     2669   3172   3021     33   -177    259       C  
ATOM   3129  N   CYS A 251      11.020 -17.752  56.066  1.00 25.06           N  
ANISOU 3129  N   CYS A 251     2880   3395   3248     95   -159    242       N  
ATOM   3130  CA  CYS A 251      12.077 -17.526  57.041  1.00 25.23           C  
ANISOU 3130  CA  CYS A 251     2914   3408   3267    126   -158    227       C  
ATOM   3131  C   CYS A 251      11.659 -16.584  58.165  1.00 28.55           C  
ANISOU 3131  C   CYS A 251     3306   3836   3705    131   -143    223       C  
ATOM   3132  O   CYS A 251      11.832 -16.874  59.353  1.00 28.13           O  
ANISOU 3132  O   CYS A 251     3283   3773   3634    140   -137    213       O  
ATOM   3133  CB  CYS A 251      13.285 -16.912  56.340  1.00 26.05           C  
ANISOU 3133  CB  CYS A 251     2999   3510   3387    156   -165    219       C  
ATOM   3134  SG  CYS A 251      14.147 -18.033  55.251  1.00 30.64           S  
ANISOU 3134  SG  CYS A 251     3619   4077   3946    158   -179    213       S  
ATOM   3135  N   TRP A 252      11.097 -15.453  57.783  1.00 24.55           N  
ANISOU 3135  N   TRP A 252     2745   3348   3233    125   -138    229       N  
ATOM   3136  CA  TRP A 252      10.744 -14.418  58.741  1.00 23.95           C  
ANISOU 3136  CA  TRP A 252     2634   3283   3183    130   -125    222       C  
ATOM   3137  C   TRP A 252       9.458 -14.691  59.505  1.00 27.25           C  
ANISOU 3137  C   TRP A 252     3054   3702   3597     98   -105    223       C  
ATOM   3138  O   TRP A 252       9.211 -14.041  60.517  1.00 28.33           O  
ANISOU 3138  O   TRP A 252     3173   3844   3746    102    -89    214       O  
ATOM   3139  CB  TRP A 252      10.653 -13.050  58.043  1.00 22.60           C  
ANISOU 3139  CB  TRP A 252     2401   3129   3056    137   -129    227       C  
ATOM   3140  CG  TRP A 252      11.985 -12.406  57.907  1.00 23.51           C  
ANISOU 3140  CG  TRP A 252     2505   3241   3187    175   -135    218       C  
ATOM   3141  CD1 TRP A 252      12.740 -12.294  56.774  1.00 26.33           C  
ANISOU 3141  CD1 TRP A 252     2861   3594   3550    186   -141    223       C  
ATOM   3142  CD2 TRP A 252      12.754 -11.825  58.959  1.00 23.36           C  
ANISOU 3142  CD2 TRP A 252     2475   3218   3183    208   -133    198       C  
ATOM   3143  NE1 TRP A 252      13.930 -11.660  57.051  1.00 25.77           N  
ANISOU 3143  NE1 TRP A 252     2774   3515   3503    222   -140    206       N  
ATOM   3144  CE2 TRP A 252      13.968 -11.365  58.387  1.00 27.26           C  
ANISOU 3144  CE2 TRP A 252     2955   3704   3699    238   -138    190       C  
ATOM   3145  CE3 TRP A 252      12.540 -11.647  60.329  1.00 24.60           C  
ANISOU 3145  CE3 TRP A 252     2634   3376   3336    216   -126    184       C  
ATOM   3146  CZ2 TRP A 252      14.958 -10.727  59.138  1.00 26.30           C  
ANISOU 3146  CZ2 TRP A 252     2815   3573   3604    277   -141    165       C  
ATOM   3147  CZ3 TRP A 252      13.545 -11.005  61.092  1.00 25.98           C  
ANISOU 3147  CZ3 TRP A 252     2796   3544   3530    257   -132    161       C  
ATOM   3148  CH2 TRP A 252      14.732 -10.554  60.489  1.00 26.47           C  
ANISOU 3148  CH2 TRP A 252     2838   3597   3621    288   -142    150       C  
ATOM   3149  N   LEU A 253       8.647 -15.644  59.066  1.00 21.99           N  
ANISOU 3149  N   LEU A 253     2408   3028   2918     66   -102    232       N  
ATOM   3150  CA  LEU A 253       7.307 -15.799  59.652  1.00 21.39           C  
ANISOU 3150  CA  LEU A 253     2323   2951   2854     30    -77    230       C  
ATOM   3151  C   LEU A 253       7.269 -16.211  61.160  1.00 25.38           C  
ANISOU 3151  C   LEU A 253     2870   3444   3330     28    -48    221       C  
ATOM   3152  O   LEU A 253       6.490 -15.627  61.932  1.00 24.83           O  
ANISOU 3152  O   LEU A 253     2775   3380   3280     13    -21    213       O  
ATOM   3153  CB  LEU A 253       6.445 -16.709  58.766  1.00 21.17           C  
ANISOU 3153  CB  LEU A 253     2303   2914   2827     -2    -82    236       C  
ATOM   3154  CG  LEU A 253       5.051 -17.132  59.211  1.00 25.31           C  
ANISOU 3154  CG  LEU A 253     2819   3428   3370    -43    -54    230       C  
ATOM   3155  CD1 LEU A 253       4.167 -15.891  59.490  1.00 25.52           C  
ANISOU 3155  CD1 LEU A 253     2781   3467   3448    -54    -42    218       C  
ATOM   3156  CD2 LEU A 253       4.449 -18.049  58.153  1.00 26.58           C  
ANISOU 3156  CD2 LEU A 253     2986   3577   3536    -65    -70    234       C  
ATOM   3157  N   PRO A 254       8.117 -17.179  61.592  1.00 22.06           N  
ANISOU 3157  N   PRO A 254     2514   3004   2862     45    -53    222       N  
ATOM   3158  CA  PRO A 254       8.065 -17.581  63.018  1.00 21.34           C  
ANISOU 3158  CA  PRO A 254     2474   2898   2736     44    -28    217       C  
ATOM   3159  C   PRO A 254       8.457 -16.444  63.921  1.00 24.26           C  
ANISOU 3159  C   PRO A 254     2822   3279   3115     72    -24    203       C  
ATOM   3160  O   PRO A 254       7.931 -16.305  65.015  1.00 22.64           O  
ANISOU 3160  O   PRO A 254     2633   3071   2898     62      6    196       O  
ATOM   3161  CB  PRO A 254       9.063 -18.734  63.126  1.00 23.09           C  
ANISOU 3161  CB  PRO A 254     2767   3096   2911     64    -49    220       C  
ATOM   3162  CG  PRO A 254       9.277 -19.218  61.731  1.00 27.89           C  
ANISOU 3162  CG  PRO A 254     3362   3706   3530     59    -74    227       C  
ATOM   3163  CD  PRO A 254       9.061 -18.011  60.818  1.00 23.67           C  
ANISOU 3163  CD  PRO A 254     2753   3199   3043     61    -82    227       C  
ATOM   3164  N   TYR A 255       9.359 -15.597  63.445  1.00 21.72           N  
ANISOU 3164  N   TYR A 255     2464   2971   2817    107    -53    197       N  
ATOM   3165  CA  TYR A 255       9.710 -14.392  64.184  1.00 21.60           C  
ANISOU 3165  CA  TYR A 255     2416   2968   2823    135    -53    181       C  
ATOM   3166  C   TYR A 255       8.566 -13.372  64.227  1.00 26.72           C  
ANISOU 3166  C   TYR A 255     2998   3639   3517    110    -30    179       C  
ATOM   3167  O   TYR A 255       8.376 -12.725  65.249  1.00 27.03           O  
ANISOU 3167  O   TYR A 255     3027   3684   3560    117    -13    165       O  
ATOM   3168  CB  TYR A 255      10.970 -13.757  63.589  1.00 22.09           C  
ANISOU 3168  CB  TYR A 255     2450   3034   2909    177    -85    174       C  
ATOM   3169  CG  TYR A 255      11.314 -12.406  64.155  1.00 22.83           C  
ANISOU 3169  CG  TYR A 255     2495   3141   3038    206    -88    157       C  
ATOM   3170  CD1 TYR A 255      11.946 -12.279  65.387  1.00 24.19           C  
ANISOU 3170  CD1 TYR A 255     2697   3303   3191    240    -94    136       C  
ATOM   3171  CD2 TYR A 255      11.002 -11.247  63.452  1.00 23.32           C  
ANISOU 3171  CD2 TYR A 255     2482   3225   3154    202    -88    160       C  
ATOM   3172  CE1 TYR A 255      12.261 -11.032  65.897  1.00 23.66           C  
ANISOU 3172  CE1 TYR A 255     2581   3248   3161    270    -98    117       C  
ATOM   3173  CE2 TYR A 255      11.306  -9.998  63.960  1.00 23.87           C  
ANISOU 3173  CE2 TYR A 255     2502   3306   3261    229    -91    144       C  
ATOM   3174  CZ  TYR A 255      11.935  -9.898  65.171  1.00 31.17           C  
ANISOU 3174  CZ  TYR A 255     3453   4222   4170    263    -95    121       C  
ATOM   3175  OH  TYR A 255      12.224  -8.639  65.654  1.00 35.10           O  
ANISOU 3175  OH  TYR A 255     3896   4731   4710    291   -100    102       O  
ATOM   3176  N   TYR A 256       7.798 -13.209  63.149  1.00 22.87           N  
ANISOU 3176  N   TYR A 256     2466   3160   3063     81    -32    189       N  
ATOM   3177  CA  TYR A 256       6.654 -12.298  63.235  1.00 22.43           C  
ANISOU 3177  CA  TYR A 256     2347   3119   3055     56    -14    182       C  
ATOM   3178  C   TYR A 256       5.634 -12.816  64.240  1.00 25.38           C  
ANISOU 3178  C   TYR A 256     2746   3483   3415     22     29    174       C  
ATOM   3179  O   TYR A 256       4.964 -12.013  64.887  1.00 25.86           O  
ANISOU 3179  O   TYR A 256     2766   3553   3505     11     52    159       O  
ATOM   3180  CB  TYR A 256       5.929 -12.080  61.901  1.00 24.01           C  
ANISOU 3180  CB  TYR A 256     2501   3326   3295     33    -30    192       C  
ATOM   3181  CG  TYR A 256       6.761 -11.634  60.727  1.00 26.46           C  
ANISOU 3181  CG  TYR A 256     2793   3643   3618     58    -66    204       C  
ATOM   3182  CD1 TYR A 256       7.893 -10.825  60.879  1.00 27.84           C  
ANISOU 3182  CD1 TYR A 256     2953   3825   3799     98    -78    200       C  
ATOM   3183  CD2 TYR A 256       6.386 -11.999  59.431  1.00 27.88           C  
ANISOU 3183  CD2 TYR A 256     2969   3820   3803     42    -85    217       C  
ATOM   3184  CE1 TYR A 256       8.631 -10.411  59.767  1.00 27.69           C  
ANISOU 3184  CE1 TYR A 256     2919   3808   3793    118   -101    211       C  
ATOM   3185  CE2 TYR A 256       7.125 -11.598  58.321  1.00 28.55           C  
ANISOU 3185  CE2 TYR A 256     3045   3909   3893     63   -112    229       C  
ATOM   3186  CZ  TYR A 256       8.232 -10.801  58.499  1.00 33.73           C  
ANISOU 3186  CZ  TYR A 256     3689   4571   4557     99   -116    227       C  
ATOM   3187  OH  TYR A 256       8.916 -10.400  57.384  1.00 32.71           O  
ANISOU 3187  OH  TYR A 256     3551   4442   4435    116   -133    238       O  
ATOM   3188  N   ILE A 257       5.486 -14.140  64.354  1.00 20.33           N  
ANISOU 3188  N   ILE A 257     2170   2822   2733      4     43    183       N  
ATOM   3189  CA  ILE A 257       4.543 -14.715  65.306  1.00 19.38           C  
ANISOU 3189  CA  ILE A 257     2080   2686   2598    -31     92    176       C  
ATOM   3190  C   ILE A 257       5.003 -14.407  66.744  1.00 23.96           C  
ANISOU 3190  C   ILE A 257     2698   3264   3141     -9    112    165       C  
ATOM   3191  O   ILE A 257       4.204 -14.019  67.580  1.00 24.59           O  
ANISOU 3191  O   ILE A 257     2766   3346   3232    -30    153    151       O  
ATOM   3192  CB  ILE A 257       4.352 -16.221  65.070  1.00 21.75           C  
ANISOU 3192  CB  ILE A 257     2442   2960   2863    -54    101    190       C  
ATOM   3193  CG1 ILE A 257       3.668 -16.443  63.720  1.00 21.06           C  
ANISOU 3193  CG1 ILE A 257     2309   2874   2817    -79     84    194       C  
ATOM   3194  CG2 ILE A 257       3.546 -16.914  66.232  1.00 21.85           C  
ANISOU 3194  CG2 ILE A 257     2505   2950   2849    -88    160    185       C  
ATOM   3195  CD1 ILE A 257       3.966 -17.791  63.136  1.00 25.10           C  
ANISOU 3195  CD1 ILE A 257     2875   3367   3297    -84     70    209       C  
ATOM   3196  N   GLY A 258       6.293 -14.528  67.013  1.00 20.62           N  
ANISOU 3196  N   GLY A 258     2319   2837   2679     36     81    168       N  
ATOM   3197  CA  GLY A 258       6.858 -14.163  68.313  1.00 20.49           C  
ANISOU 3197  CA  GLY A 258     2339   2818   2629     67     87    154       C  
ATOM   3198  C   GLY A 258       6.608 -12.720  68.725  1.00 24.46           C  
ANISOU 3198  C   GLY A 258     2773   3346   3176     77     94    134       C  
ATOM   3199  O   GLY A 258       6.243 -12.450  69.867  1.00 24.81           O  
ANISOU 3199  O   GLY A 258     2835   3389   3203     74    127    120       O  
ATOM   3200  N   ILE A 259       6.823 -11.795  67.796  1.00 20.49           N  
ANISOU 3200  N   ILE A 259     2193   2864   2729     89     64    133       N  
ATOM   3201  CA  ILE A 259       6.670 -10.359  68.031  1.00 19.77           C  
ANISOU 3201  CA  ILE A 259     2026   2796   2689    102     63    115       C  
ATOM   3202  C   ILE A 259       5.196 -10.001  68.298  1.00 23.36           C  
ANISOU 3202  C   ILE A 259     2437   3258   3179     54    106    105       C  
ATOM   3203  O   ILE A 259       4.868  -9.169  69.155  1.00 22.74           O  
ANISOU 3203  O   ILE A 259     2331   3192   3119     56    127     84       O  
ATOM   3204  CB  ILE A 259       7.171  -9.571  66.791  1.00 22.43           C  
ANISOU 3204  CB  ILE A 259     2296   3147   3078    120     23    122       C  
ATOM   3205  CG1 ILE A 259       8.684  -9.723  66.629  1.00 21.98           C  
ANISOU 3205  CG1 ILE A 259     2270   3082   3000    169    -13    123       C  
ATOM   3206  CG2 ILE A 259       6.837  -8.108  66.900  1.00 23.59           C  
ANISOU 3206  CG2 ILE A 259     2360   3317   3287    125     22    106       C  
ATOM   3207  CD1 ILE A 259       9.486  -9.161  67.811  1.00 26.67           C  
ANISOU 3207  CD1 ILE A 259     2875   3675   3582    214    -21     99       C  
ATOM   3208  N   SER A 260       4.320 -10.651  67.541  1.00 20.18           N  
ANISOU 3208  N   SER A 260     2029   2847   2792     12    118    116       N  
ATOM   3209  CA  SER A 260       2.870 -10.521  67.711  1.00 19.93           C  
ANISOU 3209  CA  SER A 260     1959   2814   2801    -38    160    101       C  
ATOM   3210  C   SER A 260       2.441 -10.996  69.090  1.00 23.80           C  
ANISOU 3210  C   SER A 260     2506   3289   3249    -56    217     89       C  
ATOM   3211  O   SER A 260       1.556 -10.412  69.682  1.00 23.97           O  
ANISOU 3211  O   SER A 260     2488   3315   3303    -81    256     66       O  
ATOM   3212  CB ASER A 260       2.140 -11.270  66.586  0.50 23.35           C  
ANISOU 3212  CB ASER A 260     2382   3234   3257    -73    155    113       C  
ATOM   3213  CB BSER A 260       2.121 -11.362  66.668  0.50 22.88           C  
ANISOU 3213  CB BSER A 260     2329   3173   3193    -75    159    113       C  
ATOM   3214  OG ASER A 260       2.503 -10.739  65.308  0.50 30.04           O  
ANISOU 3214  OG ASER A 260     3181   4094   4139    -55    102    124       O  
ATOM   3215  OG BSER A 260       2.107 -12.738  67.033  0.50 28.50           O  
ANISOU 3215  OG BSER A 260     3122   3859   3848    -91    186    124       O  
ATOM   3216  N   ILE A 261       3.073 -12.054  69.589  1.00 20.56           N  
ANISOU 3216  N   ILE A 261     2189   2859   2765    -44    224    103       N  
ATOM   3217  CA  ILE A 261       2.790 -12.553  70.937  1.00 20.94           C  
ANISOU 3217  CA  ILE A 261     2310   2889   2759    -56    278     96       C  
ATOM   3218  C   ILE A 261       3.246 -11.501  71.961  1.00 25.82           C  
ANISOU 3218  C   ILE A 261     2919   3523   3368    -22    277     75       C  
ATOM   3219  O   ILE A 261       2.481 -11.120  72.838  1.00 25.89           O  
ANISOU 3219  O   ILE A 261     2921   3533   3382    -45    327     55       O  
ATOM   3220  CB  ILE A 261       3.396 -13.987  71.185  1.00 23.90           C  
ANISOU 3220  CB  ILE A 261     2794   3233   3054    -49    277    119       C  
ATOM   3221  CG1 ILE A 261       2.618 -15.042  70.387  1.00 23.87           C  
ANISOU 3221  CG1 ILE A 261     2794   3210   3065    -94    295    133       C  
ATOM   3222  CG2 ILE A 261       3.333 -14.386  72.647  1.00 25.32           C  
ANISOU 3222  CG2 ILE A 261     3061   3392   3166    -51    324    114       C  
ATOM   3223  CD1 ILE A 261       3.257 -16.430  70.374  1.00 27.65           C  
ANISOU 3223  CD1 ILE A 261     3367   3660   3478    -86    284    157       C  
ATOM   3224  N   ASP A 262       4.469 -11.006  71.813  1.00 22.93           N  
ANISOU 3224  N   ASP A 262     2548   3170   2995     33    221     77       N  
ATOM   3225  CA  ASP A 262       4.983  -9.913  72.651  1.00 23.35           C  
ANISOU 3225  CA  ASP A 262     2580   3239   3052     73    210     54       C  
ATOM   3226  C   ASP A 262       4.097  -8.671  72.625  1.00 27.82           C  
ANISOU 3226  C   ASP A 262     3046   3831   3693     51    229     31       C  
ATOM   3227  O   ASP A 262       3.876  -8.033  73.668  1.00 27.67           O  
ANISOU 3227  O   ASP A 262     3024   3820   3671     57    255      7       O  
ATOM   3228  CB  ASP A 262       6.391  -9.510  72.200  1.00 25.22           C  
ANISOU 3228  CB  ASP A 262     2805   3483   3295    132    143     56       C  
ATOM   3229  CG  ASP A 262       7.480  -9.832  73.227  1.00 38.28           C  
ANISOU 3229  CG  ASP A 262     4543   5120   4881    182    122     47       C  
ATOM   3230  OD1 ASP A 262       8.654  -9.544  72.889  1.00 39.50           O  
ANISOU 3230  OD1 ASP A 262     4686   5275   5048    231     69     43       O  
ATOM   3231  OD2 ASP A 262       7.198 -10.345  74.345  1.00 43.25           O  
ANISOU 3231  OD2 ASP A 262     5251   5733   5450    175    156     43       O  
ATOM   3232  N   SER A 263       3.618  -8.304  71.431  1.00 24.11           N  
ANISOU 3232  N   SER A 263     2497   3372   3291     30    211     37       N  
ATOM   3233  CA  SER A 263       2.638  -7.214  71.283  1.00 23.20           C  
ANISOU 3233  CA  SER A 263     2285   3276   3256      3    225     15       C  
ATOM   3234  C   SER A 263       1.379  -7.460  72.112  1.00 26.85           C  
ANISOU 3234  C   SER A 263     2755   3726   3719    -47    295     -6       C  
ATOM   3235  O   SER A 263       0.878  -6.555  72.768  1.00 26.85           O  
ANISOU 3235  O   SER A 263     2707   3740   3754    -54    319    -35       O  
ATOM   3236  CB  SER A 263       2.255  -7.041  69.824  1.00 25.82           C  
ANISOU 3236  CB  SER A 263     2551   3612   3649    -15    193     28       C  
ATOM   3237  OG  SER A 263       3.415  -6.770  69.057  1.00 35.44           O  
ANISOU 3237  OG  SER A 263     3762   4837   4865     29    137     46       O  
ATOM   3238  N   PHE A 264       0.882  -8.689  72.101  1.00 22.69           N  
ANISOU 3238  N   PHE A 264     2290   3174   3157    -82    331      7       N  
ATOM   3239  CA  PHE A 264      -0.292  -9.016  72.908  1.00 23.12           C  
ANISOU 3239  CA  PHE A 264     2360   3212   3213   -133    407    -14       C  
ATOM   3240  C   PHE A 264      -0.077  -8.818  74.425  1.00 27.75           C  
ANISOU 3240  C   PHE A 264     3004   3798   3742   -119    449    -30       C  
ATOM   3241  O   PHE A 264      -1.018  -8.535  75.164  1.00 27.50           O  
ANISOU 3241  O   PHE A 264     2956   3762   3730   -154    511    -58       O  
ATOM   3242  CB  PHE A 264      -0.737 -10.452  72.644  1.00 25.10           C  
ANISOU 3242  CB  PHE A 264     2673   3430   3432   -170    439      5       C  
ATOM   3243  CG  PHE A 264      -1.183 -10.707  71.229  1.00 26.53           C  
ANISOU 3243  CG  PHE A 264     2800   3609   3674   -191    407     15       C  
ATOM   3244  CD1 PHE A 264      -1.318  -9.677  70.314  1.00 29.06           C  
ANISOU 3244  CD1 PHE A 264     3022   3950   4069   -182    358      6       C  
ATOM   3245  CD2 PHE A 264      -1.497 -11.996  70.829  1.00 29.03           C  
ANISOU 3245  CD2 PHE A 264     3164   3896   3968   -218    424     32       C  
ATOM   3246  CE1 PHE A 264      -1.733  -9.941  69.026  1.00 29.73           C  
ANISOU 3246  CE1 PHE A 264     3067   4029   4201   -199    325     14       C  
ATOM   3247  CE2 PHE A 264      -1.913 -12.273  69.543  1.00 31.55           C  
ANISOU 3247  CE2 PHE A 264     3437   4211   4338   -235    391     38       C  
ATOM   3248  CZ  PHE A 264      -2.040 -11.257  68.640  1.00 29.17           C  
ANISOU 3248  CZ  PHE A 264     3045   3931   4106   -225    341     29       C  
ATOM   3249  N   ILE A 265       1.164  -8.979  74.873  1.00 24.79           N  
ANISOU 3249  N   ILE A 265     2698   3424   3297    -65    414    -16       N  
ATOM   3250  CA  ILE A 265       1.496  -8.884  76.284  1.00 24.69           C  
ANISOU 3250  CA  ILE A 265     2756   3407   3217    -43    442    -30       C  
ATOM   3251  C   ILE A 265       1.410  -7.415  76.658  1.00 28.65           C  
ANISOU 3251  C   ILE A 265     3173   3939   3773    -26    434    -63       C  
ATOM   3252  O   ILE A 265       0.626  -7.043  77.510  1.00 29.00           O  
ANISOU 3252  O   ILE A 265     3209   3985   3824    -52    492    -91       O  
ATOM   3253  CB  ILE A 265       2.913  -9.501  76.580  1.00 27.07           C  
ANISOU 3253  CB  ILE A 265     3155   3696   3435     15    393     -9       C  
ATOM   3254  CG1 ILE A 265       2.892 -11.011  76.316  1.00 27.14           C  
ANISOU 3254  CG1 ILE A 265     3251   3671   3389     -8    407     23       C  
ATOM   3255  CG2 ILE A 265       3.367  -9.241  78.011  1.00 27.08           C  
ANISOU 3255  CG2 ILE A 265     3226   3692   3369     50    406    -27       C  
ATOM   3256  CD1 ILE A 265       4.272 -11.615  76.230  1.00 30.36           C  
ANISOU 3256  CD1 ILE A 265     3732   4066   3739     47    345     42       C  
ATOM   3257  N   LEU A 266       2.189  -6.588  75.983  1.00 24.94           N  
ANISOU 3257  N   LEU A 266     2637   3492   3348     17    366    -62       N  
ATOM   3258  CA  LEU A 266       2.198  -5.150  76.226  1.00 24.81           C  
ANISOU 3258  CA  LEU A 266     2532   3504   3391     37    349    -92       C  
ATOM   3259  C   LEU A 266       0.838  -4.455  76.073  1.00 30.11           C  
ANISOU 3259  C   LEU A 266     3108   4186   4145    -16    389   -119       C  
ATOM   3260  O   LEU A 266       0.505  -3.517  76.805  1.00 31.15           O  
ANISOU 3260  O   LEU A 266     3195   4333   4306    -14    409   -153       O  
ATOM   3261  CB  LEU A 266       3.180  -4.493  75.267  1.00 24.34           C  
ANISOU 3261  CB  LEU A 266     2412   3461   3375     83    273    -81       C  
ATOM   3262  CG  LEU A 266       4.654  -4.752  75.569  1.00 28.91           C  
ANISOU 3262  CG  LEU A 266     3057   4032   3894    147    225    -72       C  
ATOM   3263  CD1 LEU A 266       5.509  -4.076  74.490  1.00 28.50           C  
ANISOU 3263  CD1 LEU A 266     2935   3993   3900    183    161    -63       C  
ATOM   3264  CD2 LEU A 266       4.958  -4.237  76.982  1.00 30.03           C  
ANISOU 3264  CD2 LEU A 266     3231   4178   4000    181    236   -103       C  
ATOM   3265  N   LEU A 267       0.069  -4.889  75.096  1.00 25.64           N  
ANISOU 3265  N   LEU A 267     2509   3610   3624    -60    396   -107       N  
ATOM   3266  CA  LEU A 267      -1.214  -4.289  74.825  1.00 24.78           C  
ANISOU 3266  CA  LEU A 267     2307   3505   3603   -108    424   -135       C  
ATOM   3267  C   LEU A 267      -2.338  -4.882  75.667  1.00 27.87           C  
ANISOU 3267  C   LEU A 267     2734   3875   3981   -164    513   -158       C  
ATOM   3268  O   LEU A 267      -3.480  -4.465  75.526  1.00 27.69           O  
ANISOU 3268  O   LEU A 267     2635   3849   4036   -209    544   -188       O  
ATOM   3269  CB  LEU A 267      -1.535  -4.460  73.344  1.00 24.36           C  
ANISOU 3269  CB  LEU A 267     2201   3447   3608   -127    384   -117       C  
ATOM   3270  CG  LEU A 267      -0.628  -3.669  72.411  1.00 28.16           C  
ANISOU 3270  CG  LEU A 267     2631   3949   4121    -81    305    -99       C  
ATOM   3271  CD1 LEU A 267      -1.179  -3.747  70.990  1.00 28.36           C  
ANISOU 3271  CD1 LEU A 267     2603   3967   4207   -105    271    -87       C  
ATOM   3272  CD2 LEU A 267      -0.496  -2.238  72.855  1.00 30.31           C  
ANISOU 3272  CD2 LEU A 267     2827   4246   4443    -57    289   -127       C  
ATOM   3273  N   GLU A 268      -2.010  -5.861  76.507  1.00 24.09           N  
ANISOU 3273  N   GLU A 268     2370   3376   3406   -161    553   -143       N  
ATOM   3274  CA  GLU A 268      -2.977  -6.612  77.342  1.00 24.45           C  
ANISOU 3274  CA  GLU A 268     2472   3394   3424   -214    647   -158       C  
ATOM   3275  C   GLU A 268      -4.068  -7.359  76.566  1.00 28.31           C  
ANISOU 3275  C   GLU A 268     2934   3857   3966   -275    681   -158       C  
ATOM   3276  O   GLU A 268      -5.196  -7.499  77.036  1.00 28.32           O  
ANISOU 3276  O   GLU A 268     2922   3838   4000   -329    758   -188       O  
ATOM   3277  CB  GLU A 268      -3.562  -5.701  78.430  1.00 25.99           C  
ANISOU 3277  CB  GLU A 268     2635   3601   3641   -228    701   -204       C  
ATOM   3278  CG  GLU A 268      -2.463  -5.211  79.360  1.00 33.40           C  
ANISOU 3278  CG  GLU A 268     3626   4557   4508   -167    674   -204       C  
ATOM   3279  CD  GLU A 268      -2.919  -4.158  80.336  1.00 53.86           C  
ANISOU 3279  CD  GLU A 268     6172   7166   7125   -171    713   -251       C  
ATOM   3280  OE1 GLU A 268      -3.962  -4.373  81.011  1.00 41.91           O  
ANISOU 3280  OE1 GLU A 268     4673   5635   5615   -225    802   -278       O  
ATOM   3281  OE2 GLU A 268      -2.205  -3.123  80.446  1.00 50.57           O  
ANISOU 3281  OE2 GLU A 268     5709   6779   6726   -121    657   -262       O  
ATOM   3282  N   ILE A 269      -3.724  -7.864  75.391  1.00 24.33           N  
ANISOU 3282  N   ILE A 269     2423   3349   3472   -265    624   -127       N  
ATOM   3283  CA  ILE A 269      -4.615  -8.757  74.674  1.00 24.46           C  
ANISOU 3283  CA  ILE A 269     2431   3336   3526   -314    650   -124       C  
ATOM   3284  C   ILE A 269      -4.598 -10.135  75.321  1.00 30.25           C  
ANISOU 3284  C   ILE A 269     3284   4036   4174   -333    710   -103       C  
ATOM   3285  O   ILE A 269      -5.570 -10.868  75.182  1.00 30.69           O  
ANISOU 3285  O   ILE A 269     3340   4060   4261   -386    764   -112       O  
ATOM   3286  CB  ILE A 269      -4.238  -8.894  73.196  1.00 26.54           C  
ANISOU 3286  CB  ILE A 269     2656   3607   3822   -296    569    -97       C  
ATOM   3287  CG1 ILE A 269      -4.340  -7.525  72.501  1.00 26.52           C  
ANISOU 3287  CG1 ILE A 269     2538   3632   3907   -281    511   -116       C  
ATOM   3288  CG2 ILE A 269      -5.121  -9.927  72.530  1.00 25.74           C  
ANISOU 3288  CG2 ILE A 269     2557   3472   3753   -343    594    -96       C  
ATOM   3289  CD1 ILE A 269      -3.912  -7.528  71.059  1.00 32.17           C  
ANISOU 3289  CD1 ILE A 269     3221   4355   4648   -259    432    -89       C  
ATOM   3290  N   ILE A 270      -3.480 -10.478  75.977  1.00 27.29           N  
ANISOU 3290  N   ILE A 270     3008   3663   3698   -289    695    -76       N  
ATOM   3291  CA  ILE A 270      -3.363 -11.614  76.912  1.00 27.47           C  
ANISOU 3291  CA  ILE A 270     3159   3654   3625   -300    754    -58       C  
ATOM   3292  C   ILE A 270      -2.685 -11.195  78.231  1.00 31.74           C  
ANISOU 3292  C   ILE A 270     3772   4203   4085   -262    766    -64       C  
ATOM   3293  O   ILE A 270      -1.954 -10.220  78.284  1.00 30.58           O  
ANISOU 3293  O   ILE A 270     3587   4088   3944   -214    710    -72       O  
ATOM   3294  CB  ILE A 270      -2.569 -12.818  76.319  1.00 30.22           C  
ANISOU 3294  CB  ILE A 270     3584   3983   3914   -279    711    -14       C  
ATOM   3295  CG1 ILE A 270      -1.106 -12.461  76.094  1.00 29.51           C  
ANISOU 3295  CG1 ILE A 270     3511   3918   3783   -209    621      6       C  
ATOM   3296  CG2 ILE A 270      -3.219 -13.301  75.020  1.00 31.00           C  
ANISOU 3296  CG2 ILE A 270     3620   4073   4086   -314    696     -9       C  
ATOM   3297  CD1 ILE A 270      -0.319 -13.519  75.326  1.00 35.89           C  
ANISOU 3297  CD1 ILE A 270     4373   4712   4551   -188    570     44       C  
ATOM   3298  N   LYS A 271      -2.954 -11.945  79.291  1.00 29.64           N  
ANISOU 3298  N   LYS A 271     3611   3906   3745   -284    842    -61       N  
ATOM   3299  CA  LYS A 271      -2.410 -11.677  80.603  1.00 29.79           C  
ANISOU 3299  CA  LYS A 271     3715   3925   3677   -252    860    -67       C  
ATOM   3300  C   LYS A 271      -1.907 -12.958  81.221  1.00 34.88           C  
ANISOU 3300  C   LYS A 271     4513   4532   4209   -243    880    -33       C  
ATOM   3301  O   LYS A 271      -2.641 -13.681  81.858  1.00 35.36           O  
ANISOU 3301  O   LYS A 271     4644   4558   4234   -289    968    -32       O  
ATOM   3302  CB  LYS A 271      -3.453 -11.018  81.504  1.00 32.61           C  
ANISOU 3302  CB  LYS A 271     4044   4284   4063   -293    950   -110       C  
ATOM   3303  CG  LYS A 271      -3.790  -9.591  81.040  1.00 42.88           C  
ANISOU 3303  CG  LYS A 271     5196   5624   5471   -291    918   -148       C  
ATOM   3304  CD  LYS A 271      -4.455  -8.754  82.123  1.00 47.53           C  
ANISOU 3304  CD  LYS A 271     5766   6222   6073   -311    988   -193       C  
ATOM   3305  CE  LYS A 271      -4.002  -7.331  82.041  1.00 46.22           C  
ANISOU 3305  CE  LYS A 271     5504   6100   5957   -267    922   -218       C  
ATOM   3306  NZ  LYS A 271      -2.608  -7.264  82.532  1.00 54.61           N  
ANISOU 3306  NZ  LYS A 271     6646   7174   6929   -192    858   -197       N  
ATOM   3307  N   GLN A 272      -0.630 -13.221  81.004  1.00 31.81           N  
ANISOU 3307  N   GLN A 272     4174   4147   3766   -182    795     -6       N  
ATOM   3308  CA  GLN A 272       0.052 -14.337  81.583  1.00 32.07           C  
ANISOU 3308  CA  GLN A 272     4352   4144   3689   -160    791     25       C  
ATOM   3309  C   GLN A 272       1.125 -13.811  82.515  1.00 37.25           C  
ANISOU 3309  C   GLN A 272     5073   4809   4272    -92    743     17       C  
ATOM   3310  O   GLN A 272       1.359 -12.621  82.569  1.00 37.05           O  
ANISOU 3310  O   GLN A 272     4969   4819   4288    -62    710    -10       O  
ATOM   3311  CB  GLN A 272       0.660 -15.164  80.470  1.00 32.72           C  
ANISOU 3311  CB  GLN A 272     4434   4218   3780   -147    725     58       C  
ATOM   3312  CG  GLN A 272      -0.371 -15.747  79.531  1.00 40.23           C  
ANISOU 3312  CG  GLN A 272     5326   5158   4803   -210    765     64       C  
ATOM   3313  CD  GLN A 272      -1.253 -16.789  80.212  1.00 55.34           C  
ANISOU 3313  CD  GLN A 272     7328   7025   6674   -267    866     73       C  
ATOM   3314  OE1 GLN A 272      -2.444 -16.566  80.428  1.00 49.61           O  
ANISOU 3314  OE1 GLN A 272     6559   6293   5999   -323    949     48       O  
ATOM   3315  NE2 GLN A 272      -0.664 -17.927  80.556  1.00 47.55           N  
ANISOU 3315  NE2 GLN A 272     6466   6002   5597   -252    858    106       N  
ATOM   3316  N   GLY A 273       1.762 -14.702  83.262  1.00 35.12           N  
ANISOU 3316  N   GLY A 273     4947   4503   3895    -65    737     40       N  
ATOM   3317  CA  GLY A 273       2.780 -14.318  84.223  1.00 35.44           C  
ANISOU 3317  CA  GLY A 273     5065   4544   3859      4    687     30       C  
ATOM   3318  C   GLY A 273       4.154 -14.204  83.606  1.00 40.70           C  
ANISOU 3318  C   GLY A 273     5712   5221   4533     73    570     35       C  
ATOM   3319  O   GLY A 273       4.304 -14.184  82.379  1.00 39.91           O  
ANISOU 3319  O   GLY A 273     5520   5137   4506     69    527     44       O  
ATOM   3320  N   CYS A 274       5.163 -14.141  84.474  1.00 39.14           N  
ANISOU 3320  N   CYS A 274     5605   5009   4258    139    517     28       N  
ATOM   3321  CA  CYS A 274       6.546 -13.875  84.079  1.00 39.19           C  
ANISOU 3321  CA  CYS A 274     5592   5022   4276    213    405     21       C  
ATOM   3322  C   CYS A 274       7.163 -15.043  83.296  1.00 39.85           C  
ANISOU 3322  C   CYS A 274     5716   5078   4346    219    357     53       C  
ATOM   3323  O   CYS A 274       7.869 -14.852  82.315  1.00 38.59           O  
ANISOU 3323  O   CYS A 274     5482   4935   4248    245    289     52       O  
ATOM   3324  CB  CYS A 274       7.369 -13.575  85.329  1.00 41.43           C  
ANISOU 3324  CB  CYS A 274     5971   5290   4480    281    365     -1       C  
ATOM   3325  SG  CYS A 274       6.612 -12.293  86.448  1.00 46.74           S  
ANISOU 3325  SG  CYS A 274     6616   5991   5150    275    429    -41       S  
ATOM   3326  N   GLU A 275       6.874 -16.252  83.742  1.00 35.26           N  
ANISOU 3326  N   GLU A 275     5257   4454   3687    192    397     81       N  
ATOM   3327  CA  GLU A 275       7.331 -17.472  83.091  1.00 34.32           C  
ANISOU 3327  CA  GLU A 275     5186   4304   3550    190    361    112       C  
ATOM   3328  C   GLU A 275       6.960 -17.477  81.605  1.00 35.57           C  
ANISOU 3328  C   GLU A 275     5218   4489   3808    151    359    122       C  
ATOM   3329  O   GLU A 275       7.791 -17.753  80.753  1.00 35.10           O  
ANISOU 3329  O   GLU A 275     5130   4431   3777    179    288    127       O  
ATOM   3330  CB  GLU A 275       6.699 -18.671  83.802  1.00 36.65           C  
ANISOU 3330  CB  GLU A 275     5616   4550   3758    148    431    141       C  
ATOM   3331  CG  GLU A 275       7.569 -19.914  83.940  1.00 49.92           C  
ANISOU 3331  CG  GLU A 275     7421   6181   5364    180    376    166       C  
ATOM   3332  CD  GLU A 275       7.147 -20.793  85.139  1.00 73.26           C  
ANISOU 3332  CD  GLU A 275    10543   9085   8206    160    439    187       C  
ATOM   3333  OE1 GLU A 275       7.933 -21.703  85.522  1.00 73.77           O  
ANISOU 3333  OE1 GLU A 275    10731   9104   8195    196    386    204       O  
ATOM   3334  OE2 GLU A 275       6.042 -20.566  85.699  1.00 61.76           O  
ANISOU 3334  OE2 GLU A 275     9096   7632   6740    109    541    186       O  
ATOM   3335  N   PHE A 276       5.706 -17.148  81.310  1.00 30.44           N  
ANISOU 3335  N   PHE A 276     4492   3860   3213     88    437    120       N  
ATOM   3336  CA  PHE A 276       5.192 -17.143  79.945  1.00 28.52           C  
ANISOU 3336  CA  PHE A 276     4134   3639   3063     48    440    127       C  
ATOM   3337  C   PHE A 276       5.930 -16.101  79.139  1.00 31.02           C  
ANISOU 3337  C   PHE A 276     4339   3996   3451     91    365    109       C  
ATOM   3338  O   PHE A 276       6.387 -16.399  78.045  1.00 30.63           O  
ANISOU 3338  O   PHE A 276     4246   3951   3439     98    316    121       O  
ATOM   3339  CB  PHE A 276       3.670 -16.875  79.921  1.00 30.24           C  
ANISOU 3339  CB  PHE A 276     4292   3868   3332    -24    536    119       C  
ATOM   3340  CG  PHE A 276       3.092 -16.739  78.534  1.00 30.79           C  
ANISOU 3340  CG  PHE A 276     4239   3960   3501    -60    531    120       C  
ATOM   3341  CD1 PHE A 276       2.619 -17.850  77.850  1.00 32.84           C  
ANISOU 3341  CD1 PHE A 276     4512   4195   3770   -102    552    144       C  
ATOM   3342  CD2 PHE A 276       3.026 -15.506  77.914  1.00 32.32           C  
ANISOU 3342  CD2 PHE A 276     4306   4196   3777    -51    503     98       C  
ATOM   3343  CE1 PHE A 276       2.105 -17.739  76.587  1.00 33.11           C  
ANISOU 3343  CE1 PHE A 276     4440   4247   3891   -130    542    143       C  
ATOM   3344  CE2 PHE A 276       2.494 -15.384  76.622  1.00 34.35           C  
ANISOU 3344  CE2 PHE A 276     4460   4471   4122    -81    493    100       C  
ATOM   3345  CZ  PHE A 276       2.043 -16.498  75.959  1.00 32.07           C  
ANISOU 3345  CZ  PHE A 276     4189   4157   3838   -120    510    121       C  
ATOM   3346  N   GLU A 277       6.058 -14.886  79.679  1.00 27.25           N  
ANISOU 3346  N   GLU A 277     3817   3545   2992    119    358     80       N  
ATOM   3347  CA  GLU A 277       6.798 -13.822  79.001  1.00 26.42           C  
ANISOU 3347  CA  GLU A 277     3608   3474   2956    162    290     61       C  
ATOM   3348  C   GLU A 277       8.247 -14.248  78.739  1.00 30.10           C  
ANISOU 3348  C   GLU A 277     4117   3923   3398    224    203     65       C  
ATOM   3349  O   GLU A 277       8.753 -14.067  77.636  1.00 29.20           O  
ANISOU 3349  O   GLU A 277     3928   3823   3342    236    157     68       O  
ATOM   3350  CB  GLU A 277       6.746 -12.504  79.778  1.00 28.19           C  
ANISOU 3350  CB  GLU A 277     3788   3725   3199    187    296     27       C  
ATOM   3351  CG  GLU A 277       5.323 -11.861  79.959  1.00 41.46           C  
ANISOU 3351  CG  GLU A 277     5402   5427   4925    127    378     13       C  
ATOM   3352  CD  GLU A 277       5.356 -10.605  80.862  1.00 62.14           C  
ANISOU 3352  CD  GLU A 277     7988   8069   7552    156    381    -23       C  
ATOM   3353  OE1 GLU A 277       4.375 -10.340  81.611  1.00 54.29           O  
ANISOU 3353  OE1 GLU A 277     6999   7077   6550    118    455    -39       O  
ATOM   3354  OE2 GLU A 277       6.391  -9.902  80.835  1.00 54.37           O  
ANISOU 3354  OE2 GLU A 277     6973   7099   6586    218    311    -39       O  
ATOM   3355  N   ASN A 278       8.901 -14.847  79.729  1.00 27.52           N  
ANISOU 3355  N   ASN A 278     3910   3561   2984    261    182     65       N  
ATOM   3356  CA  ASN A 278      10.269 -15.376  79.544  1.00 27.20           C  
ANISOU 3356  CA  ASN A 278     3919   3496   2922    318     97     64       C  
ATOM   3357  C   ASN A 278      10.366 -16.402  78.425  1.00 31.09           C  
ANISOU 3357  C   ASN A 278     4408   3976   3431    293     83     91       C  
ATOM   3358  O   ASN A 278      11.340 -16.393  77.698  1.00 30.23           O  
ANISOU 3358  O   ASN A 278     4264   3867   3357    328     18     84       O  
ATOM   3359  CB  ASN A 278      10.820 -16.009  80.824  1.00 28.59           C  
ANISOU 3359  CB  ASN A 278     4240   3628   2995    358     77     60       C  
ATOM   3360  CG  ASN A 278      12.166 -16.718  80.597  1.00 55.03           C  
ANISOU 3360  CG  ASN A 278     7642   6942   6324    412    -12     57       C  
ATOM   3361  OD1 ASN A 278      12.328 -17.902  80.926  1.00 49.00           O  
ANISOU 3361  OD1 ASN A 278     6991   6136   5491    410    -20     77       O  
ATOM   3362  ND2 ASN A 278      13.133 -15.996  80.023  1.00 46.85           N  
ANISOU 3362  ND2 ASN A 278     6524   5922   5355    460    -79     31       N  
ATOM   3363  N   THR A 279       9.373 -17.285  78.296  1.00 28.53           N  
ANISOU 3363  N   THR A 279     4118   3639   3085    232    145    119       N  
ATOM   3364  CA  THR A 279       9.370 -18.290  77.220  1.00 28.51           C  
ANISOU 3364  CA  THR A 279     4109   3625   3100    204    135    144       C  
ATOM   3365  C   THR A 279       9.192 -17.625  75.831  1.00 32.37           C  
ANISOU 3365  C   THR A 279     4461   4153   3685    188    124    141       C  
ATOM   3366  O   THR A 279       9.798 -18.028  74.840  1.00 31.79           O  
ANISOU 3366  O   THR A 279     4363   4078   3638    198     79    148       O  
ATOM   3367  CB  THR A 279       8.296 -19.390  77.488  1.00 35.89           C  
ANISOU 3367  CB  THR A 279     5114   4532   3992    143    208    172       C  
ATOM   3368  OG1 THR A 279       8.637 -20.090  78.697  1.00 37.11           O  
ANISOU 3368  OG1 THR A 279     5408   4643   4049    164    209    178       O  
ATOM   3369  CG2 THR A 279       8.227 -20.394  76.367  1.00 32.23           C  
ANISOU 3369  CG2 THR A 279     4636   4058   3552    114    198    194       C  
ATOM   3370  N   VAL A 280       8.387 -16.579  75.770  1.00 28.53           N  
ANISOU 3370  N   VAL A 280     3889   3700   3250    164    163    129       N  
ATOM   3371  CA  VAL A 280       8.246 -15.852  74.541  1.00 27.33           C  
ANISOU 3371  CA  VAL A 280     3617   3583   3184    154    147    126       C  
ATOM   3372  C   VAL A 280       9.576 -15.135  74.220  1.00 31.72           C  
ANISOU 3372  C   VAL A 280     4134   4151   3769    217     74    108       C  
ATOM   3373  O   VAL A 280       9.988 -15.077  73.064  1.00 31.43           O  
ANISOU 3373  O   VAL A 280     4039   4125   3779    221     41    113       O  
ATOM   3374  CB  VAL A 280       7.124 -14.798  74.644  1.00 30.70           C  
ANISOU 3374  CB  VAL A 280     3961   4041   3664    119    198    113       C  
ATOM   3375  CG1 VAL A 280       6.990 -14.054  73.314  1.00 29.72           C  
ANISOU 3375  CG1 VAL A 280     3718   3947   3626    111    175    112       C  
ATOM   3376  CG2 VAL A 280       5.786 -15.433  75.072  1.00 30.87           C  
ANISOU 3376  CG2 VAL A 280     4017   4046   3666     56    279    122       C  
ATOM   3377  N   HIS A 281      10.241 -14.575  75.227  1.00 28.29           N  
ANISOU 3377  N   HIS A 281     3729   3711   3307    266     50     85       N  
ATOM   3378  CA  HIS A 281      11.455 -13.818  74.959  1.00 27.85           C  
ANISOU 3378  CA  HIS A 281     3627   3663   3291    325    -14     61       C  
ATOM   3379  C   HIS A 281      12.494 -14.703  74.284  1.00 30.80           C  
ANISOU 3379  C   HIS A 281     4034   4011   3657    349    -67     67       C  
ATOM   3380  O   HIS A 281      13.111 -14.291  73.299  1.00 29.69           O  
ANISOU 3380  O   HIS A 281     3822   3883   3576    365   -100     61       O  
ATOM   3381  CB  HIS A 281      12.033 -13.180  76.224  1.00 29.20           C  
ANISOU 3381  CB  HIS A 281     3834   3827   3434    378    -37     31       C  
ATOM   3382  CG  HIS A 281      13.451 -12.709  76.075  1.00 32.71           C  
ANISOU 3382  CG  HIS A 281     4254   4264   3911    446   -110      3       C  
ATOM   3383  ND1 HIS A 281      13.786 -11.555  75.398  1.00 34.36           N  
ANISOU 3383  ND1 HIS A 281     4351   4500   4203    463   -128    -14       N  
ATOM   3384  CD2 HIS A 281      14.620 -13.229  76.529  1.00 34.62           C  
ANISOU 3384  CD2 HIS A 281     4567   4469   4119    501   -170    -15       C  
ATOM   3385  CE1 HIS A 281      15.097 -11.378  75.454  1.00 33.60           C  
ANISOU 3385  CE1 HIS A 281     4255   4384   4125    525   -190    -42       C  
ATOM   3386  NE2 HIS A 281      15.628 -12.384  76.129  1.00 34.17           N  
ANISOU 3386  NE2 HIS A 281     4436   4418   4129    549   -220    -45       N  
ATOM   3387  N   LYS A 282      12.641 -15.924  74.783  1.00 27.78           N  
ANISOU 3387  N   LYS A 282     3758   3592   3204    348    -72     80       N  
ATOM   3388  CA  LYS A 282      13.654 -16.827  74.273  1.00 27.91           C  
ANISOU 3388  CA  LYS A 282     3814   3580   3211    373   -126     80       C  
ATOM   3389  C   LYS A 282      13.349 -17.380  72.859  1.00 32.73           C  
ANISOU 3389  C   LYS A 282     4376   4201   3859    331   -116    104       C  
ATOM   3390  O   LYS A 282      14.271 -17.645  72.076  1.00 31.74           O  
ANISOU 3390  O   LYS A 282     4234   4067   3761    354   -161     96       O  
ATOM   3391  CB  LYS A 282      13.991 -17.931  75.304  1.00 31.09           C  
ANISOU 3391  CB  LYS A 282     4351   3936   3527    391   -143     84       C  
ATOM   3392  CG  LYS A 282      12.830 -18.748  75.910  1.00 45.76           C  
ANISOU 3392  CG  LYS A 282     6288   5780   5320    339    -78    114       C  
ATOM   3393  CD  LYS A 282      13.387 -20.021  76.628  1.00 56.22           C  
ANISOU 3393  CD  LYS A 282     7749   7050   6564    360   -109    122       C  
ATOM   3394  CE  LYS A 282      12.377 -21.179  76.723  1.00 65.89           C  
ANISOU 3394  CE  LYS A 282     9042   8254   7739    300    -49    159       C  
ATOM   3395  NZ  LYS A 282      13.070 -22.501  76.587  1.00 72.18           N  
ANISOU 3395  NZ  LYS A 282     9921   9005   8497    313    -96    170       N  
ATOM   3396  N   TRP A 283      12.072 -17.503  72.508  1.00 30.24           N  
ANISOU 3396  N   TRP A 283     4035   3904   3552    272    -57    127       N  
ATOM   3397  CA  TRP A 283      11.728 -18.030  71.200  1.00 30.10           C  
ANISOU 3397  CA  TRP A 283     3976   3895   3567    235    -51    147       C  
ATOM   3398  C   TRP A 283      11.833 -16.959  70.114  1.00 31.89           C  
ANISOU 3398  C   TRP A 283     4091   4157   3870    238    -63    140       C  
ATOM   3399  O   TRP A 283      12.060 -17.291  68.939  1.00 30.58           O  
ANISOU 3399  O   TRP A 283     3895   3995   3731    229    -80    148       O  
ATOM   3400  CB  TRP A 283      10.364 -18.717  71.229  1.00 29.98           C  
ANISOU 3400  CB  TRP A 283     3982   3876   3533    173     10    171       C  
ATOM   3401  CG  TRP A 283      10.470 -20.101  71.794  1.00 32.43           C  
ANISOU 3401  CG  TRP A 283     4402   4144   3775    167     12    186       C  
ATOM   3402  CD1 TRP A 283      10.351 -20.472  73.112  1.00 35.99           C  
ANISOU 3402  CD1 TRP A 283     4949   4568   4160    172     33    187       C  
ATOM   3403  CD2 TRP A 283      10.783 -21.299  71.070  1.00 32.75           C  
ANISOU 3403  CD2 TRP A 283     4475   4163   3806    157    -12    200       C  
ATOM   3404  NE1 TRP A 283      10.547 -21.825  73.245  1.00 36.22           N  
ANISOU 3404  NE1 TRP A 283     5068   4558   4138    165     24    204       N  
ATOM   3405  CE2 TRP A 283      10.809 -22.359  72.008  1.00 37.55           C  
ANISOU 3405  CE2 TRP A 283     5196   4730   4343    156     -4    211       C  
ATOM   3406  CE3 TRP A 283      11.020 -21.584  69.716  1.00 33.95           C  
ANISOU 3406  CE3 TRP A 283     4574   4326   4000    150    -37    204       C  
ATOM   3407  CZ2 TRP A 283      11.060 -23.676  71.636  1.00 37.21           C  
ANISOU 3407  CZ2 TRP A 283     5207   4656   4276    147    -23    226       C  
ATOM   3408  CZ3 TRP A 283      11.281 -22.889  69.344  1.00 35.72           C  
ANISOU 3408  CZ3 TRP A 283     4851   4522   4200    141    -55    217       C  
ATOM   3409  CH2 TRP A 283      11.299 -23.921  70.300  1.00 36.98           C  
ANISOU 3409  CH2 TRP A 283     5117   4640   4294    139    -49    227       C  
ATOM   3410  N   ILE A 284      11.686 -15.688  70.511  1.00 27.28           N  
ANISOU 3410  N   ILE A 284     3451   3596   3318    252    -54    124       N  
ATOM   3411  CA  ILE A 284      11.973 -14.549  69.638  1.00 26.04           C  
ANISOU 3411  CA  ILE A 284     3195   3468   3231    265    -70    114       C  
ATOM   3412  C   ILE A 284      13.472 -14.489  69.280  1.00 28.78           C  
ANISOU 3412  C   ILE A 284     3540   3801   3595    318   -125     96       C  
ATOM   3413  O   ILE A 284      13.817 -14.222  68.136  1.00 26.98           O  
ANISOU 3413  O   ILE A 284     3257   3583   3412    318   -138     99       O  
ATOM   3414  CB  ILE A 284      11.539 -13.207  70.292  1.00 28.92           C  
ANISOU 3414  CB  ILE A 284     3504   3857   3627    272    -51     98       C  
ATOM   3415  CG1 ILE A 284      10.028 -13.065  70.199  1.00 29.25           C  
ANISOU 3415  CG1 ILE A 284     3514   3917   3683    214      2    111       C  
ATOM   3416  CG2 ILE A 284      12.205 -12.022  69.634  1.00 28.62           C  
ANISOU 3416  CG2 ILE A 284     3379   3838   3656    303    -79     83       C  
ATOM   3417  CD1 ILE A 284       9.506 -11.816  70.828  1.00 35.43           C  
ANISOU 3417  CD1 ILE A 284     4240   4723   4498    216     24     93       C  
ATOM   3418  N   SER A 285      14.350 -14.744  70.251  1.00 25.80           N  
ANISOU 3418  N   SER A 285     3224   3396   3182    363   -157     75       N  
ATOM   3419  CA  SER A 285      15.774 -14.879  69.957  1.00 25.69           C  
ANISOU 3419  CA  SER A 285     3215   3359   3187    412   -210     51       C  
ATOM   3420  C   SER A 285      16.040 -16.064  69.007  1.00 29.99           C  
ANISOU 3420  C   SER A 285     3788   3887   3721    393   -222     67       C  
ATOM   3421  O   SER A 285      16.813 -15.955  68.039  1.00 29.31           O  
ANISOU 3421  O   SER A 285     3660   3800   3677    406   -244     57       O  
ATOM   3422  CB  SER A 285      16.579 -15.037  71.244  1.00 30.24           C  
ANISOU 3422  CB  SER A 285     3861   3903   3725    464   -248     23       C  
ATOM   3423  OG  SER A 285      16.759 -13.779  71.879  1.00 41.73           O  
ANISOU 3423  OG  SER A 285     5270   5372   5211    497   -254     -3       O  
ATOM   3424  N   ILE A 286      15.371 -17.188  69.266  1.00 26.86           N  
ANISOU 3424  N   ILE A 286     3461   3477   3268    359   -204     90       N  
ATOM   3425  CA  ILE A 286      15.534 -18.377  68.431  1.00 26.67           C  
ANISOU 3425  CA  ILE A 286     3466   3437   3231    339   -215    104       C  
ATOM   3426  C   ILE A 286      15.172 -18.054  67.010  1.00 28.55           C  
ANISOU 3426  C   ILE A 286     3626   3704   3518    309   -197    118       C  
ATOM   3427  O   ILE A 286      15.958 -18.301  66.104  1.00 28.52           O  
ANISOU 3427  O   ILE A 286     3605   3693   3539    321   -222    110       O  
ATOM   3428  CB  ILE A 286      14.682 -19.545  68.930  1.00 30.77           C  
ANISOU 3428  CB  ILE A 286     4064   3938   3689    302   -188    129       C  
ATOM   3429  CG1 ILE A 286      15.528 -20.469  69.777  1.00 32.51           C  
ANISOU 3429  CG1 ILE A 286     4382   4113   3857    336   -229    117       C  
ATOM   3430  CG2 ILE A 286      14.166 -20.402  67.808  1.00 31.82           C  
ANISOU 3430  CG2 ILE A 286     4186   4074   3828    258   -174    152       C  
ATOM   3431  CD1 ILE A 286      16.325 -21.491  68.947  1.00 45.90           C  
ANISOU 3431  CD1 ILE A 286     6095   5785   5559    342   -269    113       C  
ATOM   3432  N   THR A 287      13.988 -17.477  66.826  1.00 23.10           N  
ANISOU 3432  N   THR A 287     2891   3043   2843    271   -156    136       N  
ATOM   3433  CA  THR A 287      13.376 -17.330  65.504  1.00 21.39           C  
ANISOU 3433  CA  THR A 287     2614   2849   2662    236   -140    154       C  
ATOM   3434  C   THR A 287      14.018 -16.225  64.665  1.00 24.30           C  
ANISOU 3434  C   THR A 287     2908   3237   3089    259   -154    142       C  
ATOM   3435  O   THR A 287      14.120 -16.325  63.439  1.00 24.80           O  
ANISOU 3435  O   THR A 287     2942   3307   3173    247   -159    151       O  
ATOM   3436  CB  THR A 287      11.896 -16.998  65.636  1.00 23.25           C  
ANISOU 3436  CB  THR A 287     2823   3107   2906    191    -96    170       C  
ATOM   3437  OG1 THR A 287      11.763 -15.878  66.525  1.00 22.22           O  
ANISOU 3437  OG1 THR A 287     2664   2988   2789    208    -84    156       O  
ATOM   3438  CG2 THR A 287      11.124 -18.208  66.190  1.00 19.70           C  
ANISOU 3438  CG2 THR A 287     2442   2635   2406    157    -70    185       C  
ATOM   3439  N   GLU A 288      14.433 -15.166  65.322  1.00 19.32           N  
ANISOU 3439  N   GLU A 288     2247   2612   2481    292   -160    123       N  
ATOM   3440  CA  GLU A 288      15.181 -14.136  64.661  1.00 18.96           C  
ANISOU 3440  CA  GLU A 288     2136   2576   2492    318   -173    109       C  
ATOM   3441  C   GLU A 288      16.490 -14.726  64.092  1.00 25.07           C  
ANISOU 3441  C   GLU A 288     2930   3325   3272    346   -204     93       C  
ATOM   3442  O   GLU A 288      16.847 -14.502  62.919  1.00 25.50           O  
ANISOU 3442  O   GLU A 288     2946   3385   3359    343   -203     96       O  
ATOM   3443  CB  GLU A 288      15.487 -13.041  65.650  1.00 20.07           C  
ANISOU 3443  CB  GLU A 288     2250   2722   2656    354   -178     86       C  
ATOM   3444  CG  GLU A 288      16.349 -11.975  65.061  1.00 28.92           C  
ANISOU 3444  CG  GLU A 288     3302   3847   3839    384   -190     69       C  
ATOM   3445  CD  GLU A 288      16.824 -10.997  66.085  1.00 38.27           C  
ANISOU 3445  CD  GLU A 288     4462   5030   5050    427   -203     39       C  
ATOM   3446  OE1 GLU A 288      16.813  -9.800  65.741  1.00 37.15           O  
ANISOU 3446  OE1 GLU A 288     4247   4905   4963    433   -194     36       O  
ATOM   3447  OE2 GLU A 288      17.198 -11.415  67.205  1.00 22.28           O  
ANISOU 3447  OE2 GLU A 288     2492   2984   2990    455   -223     19       O  
ATOM   3448  N   ALA A 289      17.188 -15.474  64.939  1.00 21.59           N  
ANISOU 3448  N   ALA A 289     2552   2854   2799    374   -231     73       N  
ATOM   3449  CA  ALA A 289      18.369 -16.200  64.542  1.00 21.57           C  
ANISOU 3449  CA  ALA A 289     2575   2821   2801    399   -263     52       C  
ATOM   3450  C   ALA A 289      18.126 -17.051  63.299  1.00 26.63           C  
ANISOU 3450  C   ALA A 289     3221   3466   3433    362   -254     74       C  
ATOM   3451  O   ALA A 289      18.864 -16.949  62.323  1.00 26.41           O  
ANISOU 3451  O   ALA A 289     3162   3433   3439    371   -259     63       O  
ATOM   3452  CB  ALA A 289      18.823 -17.068  65.668  1.00 22.69           C  
ANISOU 3452  CB  ALA A 289     2795   2927   2898    424   -296     35       C  
ATOM   3453  N   LEU A 290      17.094 -17.893  63.354  1.00 24.08           N  
ANISOU 3453  N   LEU A 290     2937   3148   3066    323   -238    102       N  
ATOM   3454  CA  LEU A 290      16.699 -18.737  62.220  1.00 24.05           C  
ANISOU 3454  CA  LEU A 290     2939   3148   3052    287   -230    122       C  
ATOM   3455  C   LEU A 290      16.288 -17.930  60.972  1.00 27.24           C  
ANISOU 3455  C   LEU A 290     3276   3582   3493    267   -209    137       C  
ATOM   3456  O   LEU A 290      16.480 -18.372  59.850  1.00 26.96           O  
ANISOU 3456  O   LEU A 290     3236   3547   3462    255   -211    142       O  
ATOM   3457  CB  LEU A 290      15.536 -19.667  62.647  1.00 24.41           C  
ANISOU 3457  CB  LEU A 290     3032   3192   3050    248   -212    147       C  
ATOM   3458  CG  LEU A 290      15.848 -20.813  63.648  1.00 28.74           C  
ANISOU 3458  CG  LEU A 290     3665   3706   3550    259   -231    141       C  
ATOM   3459  CD1 LEU A 290      14.568 -21.505  64.170  1.00 28.96           C  
ANISOU 3459  CD1 LEU A 290     3735   3732   3539    217   -200    168       C  
ATOM   3460  CD2 LEU A 290      16.762 -21.854  63.028  1.00 29.58           C  
ANISOU 3460  CD2 LEU A 290     3800   3786   3652    269   -264    129       C  
ATOM   3461  N   ALA A 291      15.690 -16.757  61.201  1.00 23.51           N  
ANISOU 3461  N   ALA A 291     2754   3132   3044    264   -190    143       N  
ATOM   3462  CA  ALA A 291      15.217 -15.860  60.169  1.00 22.59           C  
ANISOU 3462  CA  ALA A 291     2578   3042   2963    248   -174    158       C  
ATOM   3463  C   ALA A 291      16.377 -15.312  59.357  1.00 26.16           C  
ANISOU 3463  C   ALA A 291     3000   3489   3452    275   -181    143       C  
ATOM   3464  O   ALA A 291      16.189 -14.909  58.213  1.00 25.34           O  
ANISOU 3464  O   ALA A 291     2865   3397   3364    260   -171    158       O  
ATOM   3465  CB  ALA A 291      14.434 -14.717  60.810  1.00 23.33           C  
ANISOU 3465  CB  ALA A 291     2629   3157   3078    244   -157    163       C  
ATOM   3466  N   PHE A 292      17.578 -15.310  59.929  1.00 23.25           N  
ANISOU 3466  N   PHE A 292     2641   3096   3095    314   -199    112       N  
ATOM   3467  CA  PHE A 292      18.739 -14.791  59.220  1.00 22.99           C  
ANISOU 3467  CA  PHE A 292     2576   3052   3107    340   -200     91       C  
ATOM   3468  C   PHE A 292      19.208 -15.698  58.109  1.00 27.80           C  
ANISOU 3468  C   PHE A 292     3208   3649   3705    328   -201     91       C  
ATOM   3469  O   PHE A 292      20.043 -15.248  57.304  1.00 27.64           O  
ANISOU 3469  O   PHE A 292     3160   3620   3721    340   -191     77       O  
ATOM   3470  CB  PHE A 292      19.933 -14.521  60.146  1.00 24.67           C  
ANISOU 3470  CB  PHE A 292     2788   3238   3349    389   -222     49       C  
ATOM   3471  CG  PHE A 292      19.698 -13.460  61.194  1.00 25.31           C  
ANISOU 3471  CG  PHE A 292     2838   3328   3449    409   -222     42       C  
ATOM   3472  CD1 PHE A 292      18.715 -12.505  61.056  1.00 27.34           C  
ANISOU 3472  CD1 PHE A 292     3052   3618   3719    388   -199     67       C  
ATOM   3473  CD2 PHE A 292      20.492 -13.431  62.317  1.00 26.61           C  
ANISOU 3473  CD2 PHE A 292     3019   3469   3624    453   -251      6       C  
ATOM   3474  CE1 PHE A 292      18.528 -11.567  62.014  1.00 27.88           C  
ANISOU 3474  CE1 PHE A 292     3091   3695   3808    407   -200     57       C  
ATOM   3475  CE2 PHE A 292      20.306 -12.501  63.291  1.00 29.06           C  
ANISOU 3475  CE2 PHE A 292     3305   3788   3950    474   -253     -4       C  
ATOM   3476  CZ  PHE A 292      19.332 -11.558  63.140  1.00 27.24           C  
ANISOU 3476  CZ  PHE A 292     3028   3592   3732    451   -225     21       C  
ATOM   3477  N   PHE A 293      18.691 -16.934  58.031  1.00 24.83           N  
ANISOU 3477  N   PHE A 293     2882   3271   3283    303   -210    104       N  
ATOM   3478  CA  PHE A 293      18.871 -17.747  56.822  1.00 25.15           C  
ANISOU 3478  CA  PHE A 293     2938   3306   3310    284   -208    109       C  
ATOM   3479  C   PHE A 293      18.350 -17.018  55.570  1.00 27.81           C  
ANISOU 3479  C   PHE A 293     3240   3668   3659    263   -184    133       C  
ATOM   3480  O   PHE A 293      18.693 -17.403  54.461  1.00 27.62           O  
ANISOU 3480  O   PHE A 293     3223   3640   3631    254   -178    133       O  
ATOM   3481  CB  PHE A 293      18.203 -19.147  56.921  1.00 27.95           C  
ANISOU 3481  CB  PHE A 293     3346   3657   3616    257   -221    123       C  
ATOM   3482  CG  PHE A 293      19.008 -20.189  57.726  1.00 30.94           C  
ANISOU 3482  CG  PHE A 293     3775   4003   3980    278   -250     96       C  
ATOM   3483  CD1 PHE A 293      18.654 -20.522  59.041  1.00 34.34           C  
ANISOU 3483  CD1 PHE A 293     4242   4422   4382    283   -263     98       C  
ATOM   3484  CD2 PHE A 293      20.101 -20.855  57.152  1.00 33.86           C  
ANISOU 3484  CD2 PHE A 293     4156   4347   4360    291   -266     69       C  
ATOM   3485  CE1 PHE A 293      19.378 -21.493  59.773  1.00 35.80           C  
ANISOU 3485  CE1 PHE A 293     4482   4572   4549    304   -296     76       C  
ATOM   3486  CE2 PHE A 293      20.836 -21.809  57.887  1.00 37.06           C  
ANISOU 3486  CE2 PHE A 293     4607   4717   4755    312   -300     42       C  
ATOM   3487  CZ  PHE A 293      20.469 -22.127  59.202  1.00 35.26           C  
ANISOU 3487  CZ  PHE A 293     4422   4479   4498    319   -318     47       C  
ATOM   3488  N   HIS A 294      17.527 -15.980  55.718  1.00 23.67           N  
ANISOU 3488  N   HIS A 294     2679   3166   3148    255   -172    153       N  
ATOM   3489  CA  HIS A 294      17.102 -15.189  54.547  1.00 23.07           C  
ANISOU 3489  CA  HIS A 294     2572   3108   3085    239   -155    175       C  
ATOM   3490  C   HIS A 294      18.315 -14.775  53.718  1.00 29.26           C  
ANISOU 3490  C   HIS A 294     3344   3878   3898    259   -140    159       C  
ATOM   3491  O   HIS A 294      18.223 -14.677  52.487  1.00 30.03           O  
ANISOU 3491  O   HIS A 294     3443   3980   3987    244   -127    174       O  
ATOM   3492  CB  HIS A 294      16.221 -13.958  54.925  1.00 22.80           C  
ANISOU 3492  CB  HIS A 294     2493   3094   3074    235   -148    192       C  
ATOM   3493  CG  HIS A 294      16.984 -12.734  55.340  1.00 25.43           C  
ANISOU 3493  CG  HIS A 294     2782   3424   3455    266   -138    176       C  
ATOM   3494  ND1 HIS A 294      17.099 -12.335  56.657  1.00 26.85           N  
ANISOU 3494  ND1 HIS A 294     2947   3602   3651    287   -145    158       N  
ATOM   3495  CD2 HIS A 294      17.653 -11.809  54.611  1.00 26.39           C  
ANISOU 3495  CD2 HIS A 294     2872   3541   3613    279   -122    174       C  
ATOM   3496  CE1 HIS A 294      17.818 -11.229  56.725  1.00 25.78           C  
ANISOU 3496  CE1 HIS A 294     2769   3462   3565    314   -136    144       C  
ATOM   3497  NE2 HIS A 294      18.161 -10.885  55.494  1.00 26.05           N  
ANISOU 3497  NE2 HIS A 294     2791   3494   3615    309   -120    154       N  
ATOM   3498  N   CYS A 295      19.444 -14.566  54.391  1.00 26.16           N  
ANISOU 3498  N   CYS A 295     2939   3462   3537    292   -142    126       N  
ATOM   3499  CA  CYS A 295      20.681 -14.158  53.749  1.00 26.49           C  
ANISOU 3499  CA  CYS A 295     2962   3484   3618    312   -122    102       C  
ATOM   3500  C   CYS A 295      21.309 -15.193  52.804  1.00 30.71           C  
ANISOU 3500  C   CYS A 295     3531   4002   4134    302   -118     89       C  
ATOM   3501  O   CYS A 295      22.149 -14.842  51.970  1.00 30.89           O  
ANISOU 3501  O   CYS A 295     3541   4010   4185    309    -91     75       O  
ATOM   3502  CB  CYS A 295      21.699 -13.770  54.813  1.00 27.33           C  
ANISOU 3502  CB  CYS A 295     3046   3566   3770    352   -132     61       C  
ATOM   3503  SG  CYS A 295      21.163 -12.398  55.940  1.00 31.53           S  
ANISOU 3503  SG  CYS A 295     3530   4115   4333    369   -135     67       S  
ATOM   3504  N   CYS A 296      20.913 -16.455  52.915  1.00 26.80           N  
ANISOU 3504  N   CYS A 296     3079   3507   3596    287   -141     93       N  
ATOM   3505  CA  CYS A 296      21.519 -17.510  52.106  1.00 26.42           C  
ANISOU 3505  CA  CYS A 296     3063   3444   3533    279   -141     76       C  
ATOM   3506  C   CYS A 296      20.607 -17.997  51.012  1.00 29.20           C  
ANISOU 3506  C   CYS A 296     3439   3816   3840    245   -136    109       C  
ATOM   3507  O   CYS A 296      21.018 -18.804  50.203  1.00 28.37           O  
ANISOU 3507  O   CYS A 296     3359   3702   3720    237   -134     98       O  
ATOM   3508  CB  CYS A 296      21.907 -18.678  52.990  1.00 26.84           C  
ANISOU 3508  CB  CYS A 296     3149   3475   3575    290   -175     50       C  
ATOM   3509  SG  CYS A 296      22.717 -18.082  54.437  1.00 30.71           S  
ANISOU 3509  SG  CYS A 296     3617   3941   4109    333   -193     15       S  
ATOM   3510  N   LEU A 297      19.367 -17.519  50.995  1.00 25.93           N  
ANISOU 3510  N   LEU A 297     3016   3428   3407    227   -139    145       N  
ATOM   3511  CA  LEU A 297      18.423 -17.893  49.946  1.00 25.94           C  
ANISOU 3511  CA  LEU A 297     3038   3448   3371    199   -141    173       C  
ATOM   3512  C   LEU A 297      18.950 -17.473  48.589  1.00 28.31           C  
ANISOU 3512  C   LEU A 297     3340   3744   3671    198   -115    175       C  
ATOM   3513  O   LEU A 297      19.051 -18.288  47.693  1.00 27.30           O  
ANISOU 3513  O   LEU A 297     3245   3614   3516    186   -115    172       O  
ATOM   3514  CB  LEU A 297      17.049 -17.243  50.184  1.00 26.23           C  
ANISOU 3514  CB  LEU A 297     3056   3508   3404    183   -149    204       C  
ATOM   3515  CG  LEU A 297      16.448 -17.635  51.533  1.00 31.61           C  
ANISOU 3515  CG  LEU A 297     3738   4191   4083    180   -166    203       C  
ATOM   3516  CD1 LEU A 297      15.264 -16.723  51.929  1.00 31.72           C  
ANISOU 3516  CD1 LEU A 297     3719   4224   4108    169   -165    225       C  
ATOM   3517  CD2 LEU A 297      16.076 -19.145  51.536  1.00 34.43           C  
ANISOU 3517  CD2 LEU A 297     4136   4542   4404    162   -184    201       C  
ATOM   3518  N   ASN A 298      19.277 -16.199  48.449  1.00 24.77           N  
ANISOU 3518  N   ASN A 298     2861   3295   3254    210    -90    180       N  
ATOM   3519  CA  ASN A 298      19.678 -15.655  47.158  1.00 25.34           C  
ANISOU 3519  CA  ASN A 298     2942   3363   3324    207    -58    188       C  
ATOM   3520  C   ASN A 298      20.829 -16.506  46.572  1.00 29.74           C  
ANISOU 3520  C   ASN A 298     3524   3898   3879    210    -40    156       C  
ATOM   3521  O   ASN A 298      20.686 -17.098  45.504  1.00 29.54           O  
ANISOU 3521  O   ASN A 298     3534   3874   3814    194    -36    163       O  
ATOM   3522  CB  ASN A 298      19.990 -14.129  47.274  1.00 25.78           C  
ANISOU 3522  CB  ASN A 298     2956   3414   3423    222    -31    195       C  
ATOM   3523  CG  ASN A 298      20.548 -13.520  45.991  1.00 39.61           C  
ANISOU 3523  CG  ASN A 298     4721   5155   5175    220     11    202       C  
ATOM   3524  OD1 ASN A 298      20.248 -13.975  44.899  1.00 34.91           O  
ANISOU 3524  OD1 ASN A 298     4167   4563   4533    203     13    217       O  
ATOM   3525  ND2 ASN A 298      21.361 -12.476  46.127  1.00 29.09           N  
ANISOU 3525  ND2 ASN A 298     3354   3805   3894    237     45    191       N  
ATOM   3526  N   PRO A 299      21.945 -16.622  47.296  1.00 26.62           N  
ANISOU 3526  N   PRO A 299     3109   3478   3526    231    -33    116       N  
ATOM   3527  CA  PRO A 299      22.962 -17.559  46.785  1.00 26.67           C  
ANISOU 3527  CA  PRO A 299     3137   3461   3534    232    -21     79       C  
ATOM   3528  C   PRO A 299      22.471 -18.988  46.500  1.00 30.64           C  
ANISOU 3528  C   PRO A 299     3681   3973   3989    213    -52     81       C  
ATOM   3529  O   PRO A 299      22.805 -19.547  45.449  1.00 31.17           O  
ANISOU 3529  O   PRO A 299     3774   4034   4034    202    -36     72       O  
ATOM   3530  CB  PRO A 299      24.025 -17.556  47.885  1.00 28.05           C  
ANISOU 3530  CB  PRO A 299     3283   3608   3766    260    -28     34       C  
ATOM   3531  CG  PRO A 299      23.896 -16.203  48.511  1.00 32.21           C  
ANISOU 3531  CG  PRO A 299     3769   4140   4331    276    -18     46       C  
ATOM   3532  CD  PRO A 299      22.445 -15.818  48.426  1.00 27.56           C  
ANISOU 3532  CD  PRO A 299     3186   3587   3700    257    -32     97       C  
ATOM   3533  N   ILE A 300      21.698 -19.586  47.388  1.00 26.31           N  
ANISOU 3533  N   ILE A 300     3139   3435   3423    209    -93     92       N  
ATOM   3534  CA  ILE A 300      21.308 -20.965  47.167  1.00 26.49           C  
ANISOU 3534  CA  ILE A 300     3197   3460   3407    193   -120     90       C  
ATOM   3535  C   ILE A 300      20.540 -21.125  45.874  1.00 32.86           C  
ANISOU 3535  C   ILE A 300     4029   4287   4170    170   -115    117       C  
ATOM   3536  O   ILE A 300      20.755 -22.075  45.141  1.00 33.45           O  
ANISOU 3536  O   ILE A 300     4131   4357   4222    161   -119    104       O  
ATOM   3537  CB  ILE A 300      20.467 -21.528  48.318  1.00 29.41           C  
ANISOU 3537  CB  ILE A 300     3573   3837   3764    189   -158    102       C  
ATOM   3538  CG1 ILE A 300      21.342 -21.810  49.531  1.00 29.63           C  
ANISOU 3538  CG1 ILE A 300     3596   3839   3823    213   -174     68       C  
ATOM   3539  CG2 ILE A 300      19.807 -22.839  47.915  1.00 30.23           C  
ANISOU 3539  CG2 ILE A 300     3711   3947   3829    167   -183    109       C  
ATOM   3540  CD1 ILE A 300      20.505 -22.192  50.736  1.00 37.25           C  
ANISOU 3540  CD1 ILE A 300     4573   4809   4771    210   -203     84       C  
ATOM   3541  N   LEU A 301      19.642 -20.189  45.587  1.00 30.84           N  
ANISOU 3541  N   LEU A 301     3763   4050   3903    164   -111    153       N  
ATOM   3542  CA  LEU A 301      18.826 -20.248  44.378  1.00 30.83           C  
ANISOU 3542  CA  LEU A 301     3789   4065   3860    147   -115    178       C  
ATOM   3543  C   LEU A 301      19.649 -20.283  43.094  1.00 34.76           C  
ANISOU 3543  C   LEU A 301     4314   4552   4342    146    -82    166       C  
ATOM   3544  O   LEU A 301      19.183 -20.795  42.073  1.00 34.53           O  
ANISOU 3544  O   LEU A 301     4319   4531   4270    134    -92    176       O  
ATOM   3545  CB  LEU A 301      17.797 -19.112  44.348  1.00 30.90           C  
ANISOU 3545  CB  LEU A 301     3781   4091   3869    143   -120    214       C  
ATOM   3546  CG  LEU A 301      16.515 -19.495  45.105  1.00 35.24           C  
ANISOU 3546  CG  LEU A 301     4321   4654   4414    131   -158    229       C  
ATOM   3547  CD1 LEU A 301      15.656 -18.290  45.424  1.00 34.82           C  
ANISOU 3547  CD1 LEU A 301     4238   4614   4379    131   -162    254       C  
ATOM   3548  CD2 LEU A 301      15.712 -20.575  44.296  1.00 36.88           C  
ANISOU 3548  CD2 LEU A 301     4562   4869   4582    114   -187    234       C  
ATOM   3549  N   TYR A 302      20.872 -19.759  43.151  1.00 30.97           N  
ANISOU 3549  N   TYR A 302     3818   4053   3898    160    -43    142       N  
ATOM   3550  CA  TYR A 302      21.799 -19.842  42.014  1.00 30.45           C  
ANISOU 3550  CA  TYR A 302     3776   3970   3823    157     -1    123       C  
ATOM   3551  C   TYR A 302      22.619 -21.127  42.029  1.00 34.72           C  
ANISOU 3551  C   TYR A 302     4326   4494   4370    156     -5     79       C  
ATOM   3552  O   TYR A 302      23.407 -21.344  41.116  1.00 35.04           O  
ANISOU 3552  O   TYR A 302     4386   4520   4406    152     30     57       O  
ATOM   3553  CB  TYR A 302      22.783 -18.674  42.002  1.00 30.63           C  
ANISOU 3553  CB  TYR A 302     3774   3974   3892    171     52    112       C  
ATOM   3554  CG  TYR A 302      22.243 -17.363  41.506  1.00 30.48           C  
ANISOU 3554  CG  TYR A 302     3756   3964   3862    170     72    152       C  
ATOM   3555  CD1 TYR A 302      21.676 -17.252  40.231  1.00 32.21           C  
ANISOU 3555  CD1 TYR A 302     4022   4192   4024    156     78    182       C  
ATOM   3556  CD2 TYR A 302      22.375 -16.203  42.289  1.00 30.32           C  
ANISOU 3556  CD2 TYR A 302     3690   3939   3890    184     83    159       C  
ATOM   3557  CE1 TYR A 302      21.217 -16.023  39.766  1.00 31.93           C  
ANISOU 3557  CE1 TYR A 302     3992   4160   3979    157     93    219       C  
ATOM   3558  CE2 TYR A 302      21.931 -15.001  41.848  1.00 31.09           C  
ANISOU 3558  CE2 TYR A 302     3787   4042   3983    184    100    194       C  
ATOM   3559  CZ  TYR A 302      21.339 -14.902  40.590  1.00 38.99           C  
ANISOU 3559  CZ  TYR A 302     4838   5050   4926    170    104    226       C  
ATOM   3560  OH  TYR A 302      20.890 -13.661  40.172  1.00 40.57           O  
ANISOU 3560  OH  TYR A 302     5041   5252   5122    171    116    262       O  
ATOM   3561  N   ALA A 303      22.461 -21.964  43.051  1.00 30.82           N  
ANISOU 3561  N   ALA A 303     3822   4000   3888    160    -47     66       N  
ATOM   3562  CA  ALA A 303      23.244 -23.195  43.143  1.00 30.58           C  
ANISOU 3562  CA  ALA A 303     3800   3949   3868    160    -59     23       C  
ATOM   3563  C   ALA A 303      22.879 -24.156  42.003  1.00 35.01           C  
ANISOU 3563  C   ALA A 303     4400   4521   4380    141    -66     25       C  
ATOM   3564  O   ALA A 303      21.752 -24.172  41.531  1.00 34.88           O  
ANISOU 3564  O   ALA A 303     4403   4528   4320    130    -85     61       O  
ATOM   3565  CB  ALA A 303      23.044 -23.873  44.511  1.00 30.94           C  
ANISOU 3565  CB  ALA A 303     3836   3990   3931    168   -105     15       C  
ATOM   3566  N   PHE A 304      23.855 -24.931  41.543  1.00 31.51           N  
ANISOU 3566  N   PHE A 304     3966   4057   3948    140    -52    -17       N  
ATOM   3567  CA  PHE A 304      23.612 -26.034  40.595  1.00 31.04           C  
ANISOU 3567  CA  PHE A 304     3941   4006   3848    124    -66    -25       C  
ATOM   3568  C   PHE A 304      23.115 -25.662  39.199  1.00 34.44           C  
ANISOU 3568  C   PHE A 304     4408   4455   4225    113    -42      1       C  
ATOM   3569  O   PHE A 304      22.557 -26.513  38.520  1.00 34.72           O  
ANISOU 3569  O   PHE A 304     4472   4503   4219    102    -66      4       O  
ATOM   3570  CB  PHE A 304      22.622 -27.050  41.196  1.00 32.36           C  
ANISOU 3570  CB  PHE A 304     4114   4185   3995    117   -125    -10       C  
ATOM   3571  CG  PHE A 304      23.132 -27.749  42.408  1.00 33.21           C  
ANISOU 3571  CG  PHE A 304     4204   4272   4143    127   -155    -38       C  
ATOM   3572  CD1 PHE A 304      24.119 -28.710  42.298  1.00 35.99           C  
ANISOU 3572  CD1 PHE A 304     4559   4599   4518    128   -159    -86       C  
ATOM   3573  CD2 PHE A 304      22.620 -27.458  43.659  1.00 34.66           C  
ANISOU 3573  CD2 PHE A 304     4372   4457   4339    135   -179    -18       C  
ATOM   3574  CE1 PHE A 304      24.580 -29.378  43.422  1.00 36.53           C  
ANISOU 3574  CE1 PHE A 304     4616   4643   4621    139   -194   -112       C  
ATOM   3575  CE2 PHE A 304      23.083 -28.124  44.792  1.00 36.98           C  
ANISOU 3575  CE2 PHE A 304     4661   4727   4662    146   -210    -42       C  
ATOM   3576  CZ  PHE A 304      24.059 -29.076  44.675  1.00 35.04           C  
ANISOU 3576  CZ  PHE A 304     4421   4456   4439    149   -220    -88       C  
ATOM   3577  N   LEU A 305      23.345 -24.443  38.731  1.00 30.55           N  
ANISOU 3577  N   LEU A 305     3916   3959   3731    116      5     16       N  
ATOM   3578  CA  LEU A 305      22.872 -24.072  37.383  1.00 30.47           C  
ANISOU 3578  CA  LEU A 305     3952   3962   3662    107     25     43       C  
ATOM   3579  C   LEU A 305      23.663 -24.813  36.340  1.00 34.70           C  
ANISOU 3579  C   LEU A 305     4519   4486   4179     99     56      7       C  
ATOM   3580  O   LEU A 305      24.892 -24.765  36.332  1.00 35.00           O  
ANISOU 3580  O   LEU A 305     4542   4499   4258    100    103    -34       O  
ATOM   3581  CB  LEU A 305      22.939 -22.556  37.145  1.00 30.47           C  
ANISOU 3581  CB  LEU A 305     3952   3959   3666    113     68     71       C  
ATOM   3582  CG  LEU A 305      21.996 -21.754  38.061  1.00 34.71           C  
ANISOU 3582  CG  LEU A 305     4459   4512   4217    120     35    109       C  
ATOM   3583  CD1 LEU A 305      22.242 -20.252  37.977  1.00 35.07           C  
ANISOU 3583  CD1 LEU A 305     4495   4550   4281    127     79    131       C  
ATOM   3584  CD2 LEU A 305      20.522 -22.098  37.760  1.00 36.55           C  
ANISOU 3584  CD2 LEU A 305     4717   4771   4401    113    -21    144       C  
ATOM   3585  N   GLY A 306      22.956 -25.513  35.462  1.00 31.04           N  
ANISOU 3585  N   GLY A 306     4097   4039   3658     90     29     16       N  
ATOM   3586  CA  GLY A 306      23.588 -26.326  34.420  1.00 31.19           C  
ANISOU 3586  CA  GLY A 306     4149   4050   3650     81     54    -19       C  
ATOM   3587  C   GLY A 306      23.773 -27.780  34.821  1.00 35.07           C  
ANISOU 3587  C   GLY A 306     4624   4539   4163     77     13    -57       C  
ATOM   3588  O   GLY A 306      23.913 -28.649  33.967  1.00 35.02           O  
ANISOU 3588  O   GLY A 306     4645   4534   4127     69     12    -81       O  
ATOM   3589  N   ALA A 307      23.784 -28.056  36.122  1.00 31.05           N  
ANISOU 3589  N   ALA A 307     4070   4024   3704     83    -21    -64       N  
ATOM   3590  CA  ALA A 307      23.947 -29.418  36.608  1.00 30.42           C  
ANISOU 3590  CA  ALA A 307     3976   3937   3645     81    -63    -97       C  
ATOM   3591  C   ALA A 307      22.764 -30.282  36.211  1.00 34.40           C  
ANISOU 3591  C   ALA A 307     4503   4463   4103     73   -116    -76       C  
ATOM   3592  O   ALA A 307      21.638 -29.809  36.130  1.00 33.43           O  
ANISOU 3592  O   ALA A 307     4392   4361   3950     74   -138    -33       O  
ATOM   3593  CB  ALA A 307      24.093 -29.412  38.139  1.00 30.58           C  
ANISOU 3593  CB  ALA A 307     3955   3944   3720     91    -90   -100       C  
ATOM   3594  N   LYS A 308      23.031 -31.558  35.974  1.00 31.69           N  
ANISOU 3594  N   LYS A 308     4164   4115   3763     67   -138   -111       N  
ATOM   3595  CA  LYS A 308      21.977 -32.570  35.863  1.00 31.31           C  
ANISOU 3595  CA  LYS A 308     4126   4082   3690     61   -196   -100       C  
ATOM   3596  C   LYS A 308      22.180 -33.626  36.949  1.00 33.90           C  
ANISOU 3596  C   LYS A 308     4425   4393   4062     60   -235   -122       C  
ATOM   3597  O   LYS A 308      23.298 -34.080  37.183  1.00 33.19           O  
ANISOU 3597  O   LYS A 308     4321   4279   4009     62   -224   -166       O  
ATOM   3598  CB  LYS A 308      21.982 -33.205  34.472  1.00 34.28           C  
ANISOU 3598  CB  LYS A 308     4538   4467   4022     55   -192   -120       C  
ATOM   3599  CG  LYS A 308      21.475 -32.259  33.360  1.00 50.33           C  
ANISOU 3599  CG  LYS A 308     6613   6516   5994     58   -168    -89       C  
ATOM   3600  CD  LYS A 308      19.977 -31.881  33.545  1.00 59.28           C  
ANISOU 3600  CD  LYS A 308     7750   7668   7105     63   -215    -41       C  
ATOM   3601  CE  LYS A 308      19.535 -30.754  32.606  1.00 67.21           C  
ANISOU 3601  CE  LYS A 308     8796   8683   8058     69   -195     -8       C  
ATOM   3602  NZ  LYS A 308      18.299 -30.050  33.093  1.00 73.32           N  
ANISOU 3602  NZ  LYS A 308     9558   9468   8831     74   -231     36       N  
ATOM   3603  N   PHE A 309      21.097 -34.001  37.624  1.00 29.31           N  
ANISOU 3603  N   PHE A 309     3837   3820   3479     58   -281    -94       N  
ATOM   3604  CA  PHE A 309      21.186 -34.986  38.682  1.00 28.18           C  
ANISOU 3604  CA  PHE A 309     3676   3658   3371     56   -318   -108       C  
ATOM   3605  C   PHE A 309      20.856 -36.362  38.113  1.00 29.98           C  
ANISOU 3605  C   PHE A 309     3915   3888   3590     47   -354   -127       C  
ATOM   3606  O   PHE A 309      19.749 -36.857  38.267  1.00 29.68           O  
ANISOU 3606  O   PHE A 309     3878   3859   3542     41   -390   -105       O  
ATOM   3607  CB  PHE A 309      20.287 -34.606  39.857  1.00 29.71           C  
ANISOU 3607  CB  PHE A 309     3858   3856   3575     57   -338    -68       C  
ATOM   3608  CG  PHE A 309      20.569 -33.247  40.412  1.00 31.11           C  
ANISOU 3608  CG  PHE A 309     4023   4033   3764     68   -305    -50       C  
ATOM   3609  CD1 PHE A 309      21.329 -33.098  41.562  1.00 33.42           C  
ANISOU 3609  CD1 PHE A 309     4299   4303   4096     78   -303    -64       C  
ATOM   3610  CD2 PHE A 309      20.083 -32.098  39.773  1.00 33.50           C  
ANISOU 3610  CD2 PHE A 309     4331   4356   4040     69   -280    -21       C  
ATOM   3611  CE1 PHE A 309      21.612 -31.828  42.079  1.00 33.91           C  
ANISOU 3611  CE1 PHE A 309     4346   4365   4173     90   -275    -51       C  
ATOM   3612  CE2 PHE A 309      20.360 -30.827  40.291  1.00 35.92           C  
ANISOU 3612  CE2 PHE A 309     4623   4663   4363     79   -250     -6       C  
ATOM   3613  CZ  PHE A 309      21.128 -30.701  41.452  1.00 33.32           C  
ANISOU 3613  CZ  PHE A 309     4272   4313   4076     89   -247    -22       C  
ATOM   3614  N   LYS A 310      21.835 -36.971  37.457  1.00 25.41           N  
ANISOU 3614  N   LYS A 310     3339   3297   3017     46   -343   -173       N  
ATOM   3615  CA  LYS A 310      21.651 -38.262  36.791  1.00 25.15           C  
ANISOU 3615  CA  LYS A 310     3313   3266   2976     38   -375   -198       C  
ATOM   3616  C   LYS A 310      22.617 -39.365  37.224  1.00 29.55           C  
ANISOU 3616  C   LYS A 310     3855   3794   3578     36   -394   -246       C  
ATOM   3617  O   LYS A 310      22.498 -40.487  36.731  1.00 30.08           O  
ANISOU 3617  O   LYS A 310     3925   3861   3644     30   -423   -269       O  
ATOM   3618  CB  LYS A 310      21.750 -38.082  35.272  1.00 26.98           C  
ANISOU 3618  CB  LYS A 310     3572   3516   3165     37   -348   -211       C  
ATOM   3619  CG  LYS A 310      20.705 -37.128  34.713  1.00 37.57           C  
ANISOU 3619  CG  LYS A 310     4935   4883   4458     40   -342   -166       C  
ATOM   3620  CD  LYS A 310      20.472 -37.344  33.206  1.00 50.17           C  
ANISOU 3620  CD  LYS A 310     6566   6495   6001     41   -339   -178       C  
ATOM   3621  CE  LYS A 310      19.246 -38.240  32.941  1.00 62.74           C  
ANISOU 3621  CE  LYS A 310     8161   8098   7580     40   -399   -169       C  
ATOM   3622  NZ  LYS A 310      19.320 -38.991  31.651  1.00 71.92           N  
ANISOU 3622  NZ  LYS A 310     9350   9268   8707     42   -409   -202       N  
ATOM   3623  N   THR A 311      23.553 -39.074  38.131  1.00 25.79           N  
ANISOU 3623  N   THR A 311     3363   3292   3143     44   -384   -263       N  
ATOM   3624  CA  THR A 311      24.644 -40.023  38.457  1.00 25.58           C  
ANISOU 3624  CA  THR A 311     3323   3232   3165     45   -403   -318       C  
ATOM   3625  C   THR A 311      24.404 -40.742  39.786  1.00 30.10           C  
ANISOU 3625  C   THR A 311     3892   3781   3765     48   -454   -308       C  
ATOM   3626  O   THR A 311      24.559 -40.148  40.870  1.00 30.81           O  
ANISOU 3626  O   THR A 311     3978   3856   3873     59   -455   -292       O  
ATOM   3627  CB  THR A 311      26.052 -39.308  38.513  1.00 29.10           C  
ANISOU 3627  CB  THR A 311     3753   3654   3649     54   -359   -359       C  
ATOM   3628  OG1 THR A 311      26.304 -38.626  37.277  1.00 25.15           O  
ANISOU 3628  OG1 THR A 311     3263   3172   3121     49   -302   -367       O  
ATOM   3629  CG2 THR A 311      27.193 -40.318  38.783  1.00 26.88           C  
ANISOU 3629  CG2 THR A 311     3454   3334   3425     57   -384   -424       C  
ATOM   3630  N   SER A 312      24.031 -42.013  39.716  1.00 25.38           N  
ANISOU 3630  N   SER A 312     3296   3177   3170     39   -497   -317       N  
ATOM   3631  CA  SER A 312      23.996 -42.837  40.910  1.00 24.60           C  
ANISOU 3631  CA  SER A 312     3200   3046   3099     41   -545   -315       C  
ATOM   3632  C   SER A 312      25.316 -43.581  41.025  1.00 29.70           C  
ANISOU 3632  C   SER A 312     3835   3655   3794     47   -565   -377       C  
ATOM   3633  O   SER A 312      26.162 -43.518  40.128  1.00 29.83           O  
ANISOU 3633  O   SER A 312     3838   3671   3824     47   -539   -423       O  
ATOM   3634  CB  SER A 312      22.808 -43.805  40.897  1.00 27.07           C  
ANISOU 3634  CB  SER A 312     3522   3368   3396     28   -581   -288       C  
ATOM   3635  OG  SER A 312      22.848 -44.726  39.810  1.00 36.54           O  
ANISOU 3635  OG  SER A 312     4714   4574   4594     19   -594   -320       O  
ATOM   3636  N   ALA A 313      25.499 -44.266  42.148  1.00 26.54           N  
ANISOU 3636  N   ALA A 313     3442   3218   3422     54   -611   -381       N  
ATOM   3637  CA  ALA A 313      26.709 -45.046  42.386  1.00 26.48           C  
ANISOU 3637  CA  ALA A 313     3426   3168   3467     62   -644   -442       C  
ATOM   3638  C   ALA A 313      26.908 -45.996  41.236  1.00 30.58           C  
ANISOU 3638  C   ALA A 313     3931   3694   3995     48   -651   -483       C  
ATOM   3639  O   ALA A 313      28.030 -46.229  40.841  1.00 29.80           O  
ANISOU 3639  O   ALA A 313     3813   3573   3936     51   -648   -545       O  
ATOM   3640  CB  ALA A 313      26.655 -45.790  43.719  1.00 27.05           C  
ANISOU 3640  CB  ALA A 313     3520   3200   3558     69   -702   -432       C  
ATOM   3641  N   GLN A 314      25.817 -46.511  40.663  1.00 28.31           N  
ANISOU 3641  N   GLN A 314     3650   3434   3671     33   -658   -453       N  
ATOM   3642  CA  GLN A 314      25.930 -47.456  39.529  1.00 28.57           C  
ANISOU 3642  CA  GLN A 314     3671   3477   3710     22   -668   -492       C  
ATOM   3643  C   GLN A 314      26.504 -46.764  38.272  1.00 34.26           C  
ANISOU 3643  C   GLN A 314     4380   4221   4416     20   -612   -524       C  
ATOM   3644  O   GLN A 314      27.349 -47.348  37.559  1.00 34.58           O  
ANISOU 3644  O   GLN A 314     4405   4250   4483     16   -610   -584       O  
ATOM   3645  CB  GLN A 314      24.601 -48.126  39.202  1.00 29.70           C  
ANISOU 3645  CB  GLN A 314     3821   3642   3821     10   -690   -455       C  
ATOM   3646  CG  GLN A 314      23.683 -48.431  40.391  1.00 41.57           C  
ANISOU 3646  CG  GLN A 314     5342   5131   5323      8   -722   -404       C  
ATOM   3647  CD  GLN A 314      24.269 -49.404  41.386  1.00 54.49           C  
ANISOU 3647  CD  GLN A 314     6984   6717   7002     11   -772   -425       C  
ATOM   3648  OE1 GLN A 314      24.999 -50.332  41.022  1.00 46.53           O  
ANISOU 3648  OE1 GLN A 314     5962   5689   6029     10   -801   -476       O  
ATOM   3649  NE2 GLN A 314      23.920 -49.223  42.654  1.00 51.09           N  
ANISOU 3649  NE2 GLN A 314     6577   6266   6568     16   -784   -385       N  
ATOM   3650  N   HIS A 315      26.094 -45.511  38.027  1.00 30.59           N  
ANISOU 3650  N   HIS A 315     3926   3785   3911     23   -564   -486       N  
ATOM   3651  CA  HIS A 315      26.687 -44.712  36.942  1.00 30.44           C  
ANISOU 3651  CA  HIS A 315     3906   3784   3876     21   -503   -510       C  
ATOM   3652  C   HIS A 315      28.182 -44.408  37.141  1.00 35.68           C  
ANISOU 3652  C   HIS A 315     4549   4412   4594     28   -477   -568       C  
ATOM   3653  O   HIS A 315      28.872 -43.990  36.211  1.00 35.77           O  
ANISOU 3653  O   HIS A 315     4557   4429   4606     24   -425   -604       O  
ATOM   3654  CB  HIS A 315      25.906 -43.420  36.729  1.00 30.89           C  
ANISOU 3654  CB  HIS A 315     3981   3874   3881     24   -463   -454       C  
ATOM   3655  CG  HIS A 315      24.500 -43.644  36.265  1.00 34.31           C  
ANISOU 3655  CG  HIS A 315     4431   4340   4264     18   -483   -409       C  
ATOM   3656  ND1 HIS A 315      23.449 -43.838  37.139  1.00 35.79           N  
ANISOU 3656  ND1 HIS A 315     4621   4529   4449     18   -520   -363       N  
ATOM   3657  CD2 HIS A 315      23.977 -43.748  35.016  1.00 36.13           C  
ANISOU 3657  CD2 HIS A 315     4677   4600   4451     13   -473   -409       C  
ATOM   3658  CE1 HIS A 315      22.339 -44.043  36.449  1.00 35.22           C  
ANISOU 3658  CE1 HIS A 315     4558   4483   4339     13   -533   -339       C  
ATOM   3659  NE2 HIS A 315      22.631 -43.994  35.159  1.00 35.78           N  
ANISOU 3659  NE2 HIS A 315     4640   4572   4384     12   -509   -365       N  
ATOM   3660  N   ALA A 316      28.677 -44.580  38.357  1.00 32.96           N  
ANISOU 3660  N   ALA A 316     4194   4030   4298     40   -513   -579       N  
ATOM   3661  CA  ALA A 316      30.115 -44.442  38.619  1.00 33.14           C  
ANISOU 3661  CA  ALA A 316     4193   4012   4388     49   -502   -644       C  
ATOM   3662  C   ALA A 316      30.816 -45.798  38.488  1.00 37.73           C  
ANISOU 3662  C   ALA A 316     4756   4561   5019     44   -547   -710       C  
ATOM   3663  O   ALA A 316      31.996 -45.851  38.173  1.00 37.99           O  
ANISOU 3663  O   ALA A 316     4763   4564   5106     45   -528   -779       O  
ATOM   3664  CB  ALA A 316      30.362 -43.830  40.005  1.00 33.38           C  
ANISOU 3664  CB  ALA A 316     4222   4014   4446     69   -521   -629       C  
ATOM   3665  N   LEU A 317      30.081 -46.884  38.715  1.00 33.88           N  
ANISOU 3665  N   LEU A 317     4280   4075   4518     39   -604   -689       N  
ATOM   3666  CA  LEU A 317      30.631 -48.234  38.548  1.00 33.88           C  
ANISOU 3666  CA  LEU A 317     4262   4045   4564     33   -652   -747       C  
ATOM   3667  C   LEU A 317      30.562 -48.744  37.097  1.00 38.16           C  
ANISOU 3667  C   LEU A 317     4796   4617   5087     16   -626   -777       C  
ATOM   3668  O   LEU A 317      31.263 -49.682  36.746  1.00 37.20           O  
ANISOU 3668  O   LEU A 317     4653   4471   5010     10   -650   -840       O  
ATOM   3669  CB  LEU A 317      29.946 -49.216  39.509  1.00 33.49           C  
ANISOU 3669  CB  LEU A 317     4230   3978   4516     36   -726   -715       C  
ATOM   3670  CG  LEU A 317      30.419 -49.079  40.958  1.00 37.34           C  
ANISOU 3670  CG  LEU A 317     4728   4420   5040     55   -766   -713       C  
ATOM   3671  CD1 LEU A 317      29.511 -49.817  41.929  1.00 37.39           C  
ANISOU 3671  CD1 LEU A 317     4765   4414   5028     56   -823   -661       C  
ATOM   3672  CD2 LEU A 317      31.823 -49.591  41.068  1.00 39.97           C  
ANISOU 3672  CD2 LEU A 317     5034   4701   5451     64   -795   -797       C  
ATOM   3673  N   THR A 318      29.733 -48.107  36.273  1.00 35.75           N  
ANISOU 3673  N   THR A 318     4510   4360   4715      9   -581   -734       N  
ATOM   3674  CA  THR A 318      29.457 -48.546  34.890  1.00 36.09           C  
ANISOU 3674  CA  THR A 318     4556   4434   4723     -4   -561   -752       C  
ATOM   3675  C   THR A 318      29.095 -47.332  34.033  1.00 42.21           C  
ANISOU 3675  C   THR A 318     5355   5248   5435     -6   -491   -720       C  
ATOM   3676  O   THR A 318      29.159 -46.204  34.489  1.00 41.73           O  
ANISOU 3676  O   THR A 318     5302   5187   5366      1   -457   -690       O  
ATOM   3677  CB  THR A 318      28.283 -49.557  34.850  1.00 38.41           C  
ANISOU 3677  CB  THR A 318     4858   4744   4991     -9   -618   -719       C  
ATOM   3678  OG1 THR A 318      27.069 -48.899  35.225  1.00 38.28           O  
ANISOU 3678  OG1 THR A 318     4865   4755   4925     -5   -617   -643       O  
ATOM   3679  CG2 THR A 318      28.531 -50.741  35.789  1.00 33.75           C  
ANISOU 3679  CG2 THR A 318     4251   4113   4459     -7   -689   -741       C  
ATOM   3680  N   SER A 319      28.694 -47.546  32.792  1.00 40.95           N  
ANISOU 3680  N   SER A 319     5211   5119   5227    -14   -472   -726       N  
ATOM   3681  CA  SER A 319      28.281 -46.419  31.955  1.00 41.71           C  
ANISOU 3681  CA  SER A 319     5341   5251   5257    -14   -412   -691       C  
ATOM   3682  C   SER A 319      26.770 -46.237  31.946  1.00 47.06           C  
ANISOU 3682  C   SER A 319     6043   5961   5875     -9   -441   -620       C  
ATOM   3683  O   SER A 319      26.259 -45.537  31.077  1.00 47.36           O  
ANISOU 3683  O   SER A 319     6113   6029   5851     -7   -407   -594       O  
ATOM   3684  CB  SER A 319      28.801 -46.589  30.525  1.00 45.78           C  
ANISOU 3684  CB  SER A 319     5869   5778   5748    -24   -366   -741       C  
ATOM   3685  OG  SER A 319      28.080 -47.593  29.830  1.00 55.34           O  
ANISOU 3685  OG  SER A 319     7089   7010   6930    -26   -408   -745       O  
ATOM   3686  N   GLY A 320      26.068 -46.854  32.906  1.00 43.61           N  
ANISOU 3686  N   GLY A 320     5593   5516   5459     -6   -502   -591       N  
ATOM   3687  CA  GLY A 320      24.603 -46.746  33.030  1.00 43.26           C  
ANISOU 3687  CA  GLY A 320     5565   5497   5374     -3   -531   -529       C  
ATOM   3688  C   GLY A 320      23.840 -48.077  32.980  1.00 47.51           C  
ANISOU 3688  C   GLY A 320     6093   6036   5924     -6   -594   -533       C  
ATOM   3689  O   GLY A 320      24.378 -49.140  33.316  1.00 47.21           O  
ANISOU 3689  O   GLY A 320     6032   5971   5934    -11   -628   -572       O  
ATOM   3690  N   ARG A 321      22.564 -47.995  32.598  1.00 43.92           N  
ANISOU 3690  N   ARG A 321     5653   5607   5429     -3   -611   -493       N  
ATOM   3691  CA  ARG A 321      21.709 -49.162  32.327  1.00 43.53           C  
ANISOU 3691  CA  ARG A 321     5592   5560   5387     -5   -665   -498       C  
ATOM   3692  C   ARG A 321      21.380 -49.125  30.851  1.00 47.05           C  
ANISOU 3692  C   ARG A 321     6059   6037   5782      1   -657   -515       C  
ATOM   3693  O   ARG A 321      21.321 -48.037  30.279  1.00 46.80           O  
ANISOU 3693  O   ARG A 321     6057   6025   5701      7   -616   -496       O  
ATOM   3694  CB  ARG A 321      20.411 -49.079  33.122  1.00 42.95           C  
ANISOU 3694  CB  ARG A 321     5516   5487   5316     -4   -693   -442       C  
ATOM   3695  CG  ARG A 321      20.581 -49.235  34.611  1.00 50.94           C  
ANISOU 3695  CG  ARG A 321     6515   6467   6371    -10   -706   -422       C  
ATOM   3696  CD  ARG A 321      19.714 -48.243  35.369  1.00 59.88           C  
ANISOU 3696  CD  ARG A 321     7658   7607   7487     -8   -691   -362       C  
ATOM   3697  NE  ARG A 321      19.930 -48.341  36.808  1.00 67.46           N  
ANISOU 3697  NE  ARG A 321     8614   8537   8482    -12   -699   -343       N  
ATOM   3698  CZ  ARG A 321      19.194 -49.092  37.621  1.00 83.77           C  
ANISOU 3698  CZ  ARG A 321    10675  10581  10572    -20   -732   -321       C  
ATOM   3699  NH1 ARG A 321      18.176 -49.809  37.146  1.00 73.83           N  
ANISOU 3699  NH1 ARG A 321     9406   9330   9317    -25   -759   -317       N  
ATOM   3700  NH2 ARG A 321      19.466 -49.124  38.919  1.00 69.97           N  
ANISOU 3700  NH2 ARG A 321     8934   8804   8847    -21   -736   -304       N  
ATOM   3701  N   PRO A 322      21.143 -50.297  30.222  1.00 43.06           N  
ANISOU 3701  N   PRO A 322     5541   5533   5286      1   -697   -549       N  
ATOM   3702  CA  PRO A 322      21.014 -50.282  28.754  1.00 42.92           C  
ANISOU 3702  CA  PRO A 322     5549   5541   5216      9   -688   -574       C  
ATOM   3703  C   PRO A 322      19.886 -49.372  28.279  1.00 46.35           C  
ANISOU 3703  C   PRO A 322     6016   6001   5592     22   -687   -528       C  
ATOM   3704  O   PRO A 322      18.864 -49.270  28.949  1.00 45.33           O  
ANISOU 3704  O   PRO A 322     5877   5870   5478     24   -716   -486       O  
ATOM   3705  CB  PRO A 322      20.720 -51.748  28.404  1.00 44.74           C  
ANISOU 3705  CB  PRO A 322     5755   5768   5478      9   -745   -612       C  
ATOM   3706  CG  PRO A 322      21.194 -52.536  29.567  1.00 49.02           C  
ANISOU 3706  CG  PRO A 322     6259   6275   6091     -3   -769   -622       C  
ATOM   3707  CD  PRO A 322      20.988 -51.657  30.771  1.00 44.33           C  
ANISOU 3707  CD  PRO A 322     5668   5670   5504     -5   -752   -567       C  
ATOM   3708  N   LEU A 323      20.093 -48.693  27.155  1.00 43.62           N  
ANISOU 3708  N   LEU A 323     5714   5676   5184     30   -651   -537       N  
ATOM   3709  CA  LEU A 323      19.054 -47.856  26.517  1.00 43.85           C  
ANISOU 3709  CA  LEU A 323     5782   5726   5152     46   -657   -499       C  
ATOM   3710  C   LEU A 323      18.461 -46.784  27.435  1.00 49.02           C  
ANISOU 3710  C   LEU A 323     6436   6380   5811     47   -647   -439       C  
ATOM   3711  O   LEU A 323      17.244 -46.745  27.635  1.00 48.74           O  
ANISOU 3711  O   LEU A 323     6393   6346   5778     55   -688   -409       O  
ATOM   3712  CB  LEU A 323      17.916 -48.732  25.959  1.00 43.88           C  
ANISOU 3712  CB  LEU A 323     5779   5737   5154     60   -725   -509       C  
ATOM   3713  CG  LEU A 323      18.299 -49.745  24.888  1.00 48.90           C  
ANISOU 3713  CG  LEU A 323     6421   6380   5778     64   -742   -568       C  
ATOM   3714  CD1 LEU A 323      17.059 -50.436  24.355  1.00 49.33           C  
ANISOU 3714  CD1 LEU A 323     6471   6441   5832     83   -812   -573       C  
ATOM   3715  CD2 LEU A 323      19.070 -49.070  23.736  1.00 51.55           C  
ANISOU 3715  CD2 LEU A 323     6814   6731   6040     69   -687   -588       C  
ATOM   3716  N   GLU A 324      19.314 -45.923  27.990  1.00 46.22           N  
ANISOU 3716  N   GLU A 324     6084   6018   5460     38   -593   -426       N  
ATOM   3717  CA  GLU A 324      18.842 -44.787  28.790  1.00 46.02           C  
ANISOU 3717  CA  GLU A 324     6059   5992   5433     40   -577   -372       C  
ATOM   3718  C   GLU A 324      18.085 -43.791  27.906  1.00 49.74           C  
ANISOU 3718  C   GLU A 324     6577   6484   5839     54   -572   -343       C  
ATOM   3719  O   GLU A 324      17.171 -43.108  28.364  1.00 49.17           O  
ANISOU 3719  O   GLU A 324     6502   6415   5766     60   -587   -299       O  
ATOM   3720  CB  GLU A 324      20.007 -44.089  29.528  1.00 47.35           C  
ANISOU 3720  CB  GLU A 324     6219   6147   5624     30   -521   -371       C  
ATOM   3721  CG  GLU A 324      20.727 -45.015  30.531  1.00 58.98           C  
ANISOU 3721  CG  GLU A 324     7650   7594   7166     19   -536   -399       C  
ATOM   3722  CD  GLU A 324      21.580 -44.297  31.593  1.00 73.41           C  
ANISOU 3722  CD  GLU A 324     9462   9402   9027     15   -499   -390       C  
ATOM   3723  OE1 GLU A 324      22.489 -43.503  31.237  1.00 66.09           O  
ANISOU 3723  OE1 GLU A 324     8549   8475   8088     15   -443   -404       O  
ATOM   3724  OE2 GLU A 324      21.359 -44.582  32.793  1.00 61.84           O  
ANISOU 3724  OE2 GLU A 324     7972   7920   7604     12   -527   -373       O  
ATOM   3725  N   VAL A 325      18.456 -43.736  26.633  1.00 46.61           N  
ANISOU 3725  N   VAL A 325     6224   6099   5387     62   -553   -368       N  
ATOM   3726  CA  VAL A 325      17.853 -42.786  25.701  1.00 46.73           C  
ANISOU 3726  CA  VAL A 325     6295   6129   5330     78   -548   -342       C  
ATOM   3727  C   VAL A 325      16.352 -43.047  25.455  1.00 50.89           C  
ANISOU 3727  C   VAL A 325     6823   6662   5850     95   -622   -326       C  
ATOM   3728  O   VAL A 325      15.601 -42.127  25.103  1.00 50.79           O  
ANISOU 3728  O   VAL A 325     6845   6656   5798    110   -632   -293       O  
ATOM   3729  CB  VAL A 325      18.617 -42.755  24.361  1.00 51.12           C  
ANISOU 3729  CB  VAL A 325     6907   6693   5823     82   -509   -376       C  
ATOM   3730  CG1 VAL A 325      18.087 -43.836  23.416  1.00 51.25           C  
ANISOU 3730  CG1 VAL A 325     6937   6718   5817     95   -564   -412       C  
ATOM   3731  CG2 VAL A 325      18.529 -41.357  23.737  1.00 51.21           C  
ANISOU 3731  CG2 VAL A 325     6983   6711   5765     91   -469   -341       C  
ATOM   3732  N   LEU A 326      15.925 -44.293  25.655  1.00 47.03           N  
ANISOU 3732  N   LEU A 326     6295   6168   5406     94   -674   -352       N  
ATOM   3733  CA  LEU A 326      14.505 -44.667  25.595  1.00 46.43           C  
ANISOU 3733  CA  LEU A 326     6204   6091   5345    109   -744   -343       C  
ATOM   3734  C   LEU A 326      13.695 -44.048  26.756  1.00 48.69           C  
ANISOU 3734  C   LEU A 326     6457   6368   5674    103   -752   -297       C  
ATOM   3735  O   LEU A 326      12.504 -43.763  26.616  1.00 47.66           O  
ANISOU 3735  O   LEU A 326     6328   6236   5545    116   -795   -280       O  
ATOM   3736  CB  LEU A 326      14.378 -46.196  25.605  1.00 46.38           C  
ANISOU 3736  CB  LEU A 326     6158   6077   5387    106   -789   -384       C  
ATOM   3737  CG  LEU A 326      12.994 -46.828  25.423  1.00 51.04           C  
ANISOU 3737  CG  LEU A 326     6727   6661   6004    121   -863   -390       C  
ATOM   3738  CD1 LEU A 326      12.355 -46.340  24.138  1.00 51.61           C  
ANISOU 3738  CD1 LEU A 326     6854   6746   6010    150   -894   -394       C  
ATOM   3739  CD2 LEU A 326      13.080 -48.352  25.436  1.00 52.79           C  
ANISOU 3739  CD2 LEU A 326     6908   6874   6276    116   -898   -433       C  
ATOM   3740  N   PHE A 327      14.355 -43.823  27.889  1.00 44.49           N  
ANISOU 3740  N   PHE A 327     5898   5828   5180     83   -712   -280       N  
ATOM   3741  CA  PHE A 327      13.674 -43.400  29.112  1.00 43.64           C  
ANISOU 3741  CA  PHE A 327     5755   5709   5117     75   -716   -242       C  
ATOM   3742  C   PHE A 327      13.990 -41.951  29.544  1.00 47.38           C  
ANISOU 3742  C   PHE A 327     6245   6188   5570     73   -667   -203       C  
ATOM   3743  O   PHE A 327      13.487 -41.495  30.572  1.00 46.91           O  
ANISOU 3743  O   PHE A 327     6159   6121   5544     65   -665   -172       O  
ATOM   3744  CB  PHE A 327      14.011 -44.387  30.237  1.00 44.76           C  
ANISOU 3744  CB  PHE A 327     5851   5833   5324     56   -719   -252       C  
ATOM   3745  CG  PHE A 327      13.760 -45.829  29.874  1.00 46.17           C  
ANISOU 3745  CG  PHE A 327     6010   6004   5530     57   -764   -290       C  
ATOM   3746  CD1 PHE A 327      12.485 -46.375  29.952  1.00 49.45           C  
ANISOU 3746  CD1 PHE A 327     6401   6410   5980     61   -814   -287       C  
ATOM   3747  CD2 PHE A 327      14.795 -46.640  29.452  1.00 48.11           C  
ANISOU 3747  CD2 PHE A 327     6258   6249   5774     53   -757   -331       C  
ATOM   3748  CE1 PHE A 327      12.254 -47.717  29.608  1.00 50.48           C  
ANISOU 3748  CE1 PHE A 327     6508   6531   6140     62   -857   -324       C  
ATOM   3749  CE2 PHE A 327      14.572 -47.975  29.104  1.00 51.09           C  
ANISOU 3749  CE2 PHE A 327     6614   6619   6180     54   -802   -368       C  
ATOM   3750  CZ  PHE A 327      13.305 -48.511  29.186  1.00 49.28           C  
ANISOU 3750  CZ  PHE A 327     6360   6381   5983     59   -851   -363       C  
ATOM   3751  N   GLN A 328      14.805 -41.242  28.755  1.00 43.76           N  
ANISOU 3751  N   GLN A 328     5830   5740   5057     78   -626   -207       N  
ATOM   3752  CA  GLN A 328      15.160 -39.836  29.006  1.00 64.84           C  
ANISOU 3752  CA  GLN A 328     8518   8414   7705     78   -577   -173       C  
ATOM   3753  C   GLN A 328      14.076 -39.039  29.754  1.00100.89           C  
ANISOU 3753  C   GLN A 328    13064  12977  12291     80   -596   -131       C  
ATOM   3754  O   GLN A 328      13.147 -38.482  29.149  1.00 63.45           O  
ANISOU 3754  O   GLN A 328     8346   8241   7521     94   -625   -114       O  
ATOM   3755  CB  GLN A 328      15.476 -39.128  27.680  1.00 66.51           C  
ANISOU 3755  CB  GLN A 328     8793   8635   7841     91   -553   -176       C  
ATOM   3756  CG  GLN A 328      16.865 -39.415  27.130  1.00 76.37           C  
ANISOU 3756  CG  GLN A 328    10063   9884   9071     84   -500   -212       C  
ATOM   3757  CD  GLN A 328      17.170 -38.675  25.836  1.00 88.11           C  
ANISOU 3757  CD  GLN A 328    11621  11378  10478     94   -466   -211       C  
ATOM   3758  OE1 GLN A 328      16.271 -38.244  25.120  1.00 81.60           O  
ANISOU 3758  OE1 GLN A 328    10838  10561   9606    112   -499   -192       O  
ATOM   3759  NE2 GLN A 328      18.452 -38.536  25.529  1.00 80.33           N  
ANISOU 3759  NE2 GLN A 328    10653  10389   9482     84   -399   -235       N  
TER    3760      GLN A 328                                                      
ATOM   3761  N   CYS B  28      -2.250  15.783  88.280  1.00 66.45           N  
ANISOU 3761  N   CYS B  28     8788  10317   6142    603   -634   -146       N  
ATOM   3762  CA  CYS B  28      -2.422  16.200  86.859  1.00 64.85           C  
ANISOU 3762  CA  CYS B  28     8545   9945   6149    552   -609   -195       C  
ATOM   3763  C   CYS B  28      -3.714  15.646  86.249  1.00 70.82           C  
ANISOU 3763  C   CYS B  28     9294  10596   7018    589   -474   -110       C  
ATOM   3764  O   CYS B  28      -3.813  14.450  85.967  1.00 70.27           O  
ANISOU 3764  O   CYS B  28     9175  10512   7014    622   -443     37       O  
ATOM   3765  CB  CYS B  28      -1.226  15.736  86.025  1.00 63.70           C  
ANISOU 3765  CB  CYS B  28     8309   9772   6121    514   -703   -148       C  
ATOM   3766  SG  CYS B  28      -0.860  16.863  84.663  1.00 65.77           S  
ANISOU 3766  SG  CYS B  28     8544   9887   6559    424   -734   -283       S  
ATOM   3767  N   PHE B  29      -4.696  16.520  86.045  1.00 69.08           N  
ANISOU 3767  N   PHE B  29     9120  10300   6826    583   -396   -204       N  
ATOM   3768  CA  PHE B  29      -6.000  16.121  85.511  1.00 68.88           C  
ANISOU 3768  CA  PHE B  29     9084  10184   6904    616   -270   -138       C  
ATOM   3769  C   PHE B  29      -6.319  16.943  84.272  1.00 73.58           C  
ANISOU 3769  C   PHE B  29     9662  10634   7660    571   -253   -225       C  
ATOM   3770  O   PHE B  29      -5.707  17.991  84.035  1.00 73.25           O  
ANISOU 3770  O   PHE B  29     9640  10565   7629    520   -318   -351       O  
ATOM   3771  CB  PHE B  29      -7.103  16.315  86.567  1.00 71.81           C  
ANISOU 3771  CB  PHE B  29     9523  10617   7142    672   -169   -146       C  
ATOM   3772  CG  PHE B  29      -6.716  15.845  87.945  1.00 74.96           C  
ANISOU 3772  CG  PHE B  29     9962  11180   7340    714   -195    -94       C  
ATOM   3773  CD1 PHE B  29      -6.329  16.755  88.925  1.00 79.46           C  
ANISOU 3773  CD1 PHE B  29    10606  11850   7737    709   -245   -219       C  
ATOM   3774  CD2 PHE B  29      -6.715  14.491  88.256  1.00 77.43           C  
ANISOU 3774  CD2 PHE B  29    10240  11546   7635    759   -171     81       C  
ATOM   3775  CE1 PHE B  29      -5.958  16.319  90.200  1.00 81.92           C  
ANISOU 3775  CE1 PHE B  29    10954  12327   7847    750   -276   -170       C  
ATOM   3776  CE2 PHE B  29      -6.341  14.050  89.525  1.00 81.80           C  
ANISOU 3776  CE2 PHE B  29    10829  12256   7995    803   -197    142       C  
ATOM   3777  CZ  PHE B  29      -5.964  14.968  90.497  1.00 81.14           C  
ANISOU 3777  CZ  PHE B  29    10818  12285   7726    800   -252     16       C  
ATOM   3778  N   ARG B  30      -7.274  16.456  83.483  1.00 70.77           N  
ANISOU 3778  N   ARG B  30     9269  10187   7432    587   -167   -155       N  
ATOM   3779  CA  ARG B  30      -7.782  17.202  82.330  1.00 70.05           C  
ANISOU 3779  CA  ARG B  30     9164   9965   7486    558   -138   -224       C  
ATOM   3780  C   ARG B  30      -8.680  18.338  82.829  1.00 75.25           C  
ANISOU 3780  C   ARG B  30     9890  10614   8086    579    -72   -332       C  
ATOM   3781  O   ARG B  30      -9.360  18.205  83.851  1.00 75.94           O  
ANISOU 3781  O   ARG B  30    10019  10776   8059    629     -4   -314       O  
ATOM   3782  CB  ARG B  30      -8.520  16.275  81.337  1.00 69.83           C  
ANISOU 3782  CB  ARG B  30     9071   9855   7607    568    -76   -116       C  
ATOM   3783  CG  ARG B  30     -10.064  16.144  81.488  1.00 82.15           C  
ANISOU 3783  CG  ARG B  30    10635  11394   9186    614     48    -80       C  
ATOM   3784  CD  ARG B  30     -10.526  15.561  82.837  1.00 94.80           C  
ANISOU 3784  CD  ARG B  30    12269  13104  10647    668    110    -11       C  
ATOM   3785  NE  ARG B  30     -11.579  14.551  82.679  1.00103.25           N  
ANISOU 3785  NE  ARG B  30    13293  14149  11789    697    206    109       N  
ATOM   3786  CZ  ARG B  30     -12.829  14.797  82.285  1.00116.08           C  
ANISOU 3786  CZ  ARG B  30    14899  15714  13492    711    297    101       C  
ATOM   3787  NH1 ARG B  30     -13.224  16.035  81.992  1.00104.69           N  
ANISOU 3787  NH1 ARG B  30    13483  14226  12069    709    308    -16       N  
ATOM   3788  NH2 ARG B  30     -13.695  13.793  82.179  1.00100.37           N  
ANISOU 3788  NH2 ARG B  30    12858  13707  11569    728    376    215       N  
ATOM   3789  N   GLU B  31      -8.631  19.465  82.153  1.00 71.85           N  
ANISOU 3789  N   GLU B  31     9475  10095   7730    543    -88   -443       N  
ATOM   3790  CA  GLU B  31      -9.419  20.607  82.537  1.00 72.67           C  
ANISOU 3790  CA  GLU B  31     9644  10172   7797    565    -26   -552       C  
ATOM   3791  C   GLU B  31     -10.077  21.310  81.358  1.00 76.32           C  
ANISOU 3791  C   GLU B  31    10086  10498   8415    556     14   -588       C  
ATOM   3792  O   GLU B  31      -9.449  22.204  80.806  1.00 75.85           O  
ANISOU 3792  O   GLU B  31    10039  10371   8409    509    -42   -676       O  
ATOM   3793  CB  GLU B  31      -8.482  21.629  83.166  1.00 75.06           C  
ANISOU 3793  CB  GLU B  31    10009  10508   8001    526   -105   -690       C  
ATOM   3794  CG  GLU B  31      -8.770  22.015  84.578  1.00 87.69           C  
ANISOU 3794  CG  GLU B  31    11690  12208   9420    565    -73   -758       C  
ATOM   3795  CD  GLU B  31      -8.090  23.305  84.950  1.00111.23           C  
ANISOU 3795  CD  GLU B  31    14739  15180  12345    519   -136   -928       C  
ATOM   3796  OE1 GLU B  31      -8.258  24.281  84.194  1.00107.79           O  
ANISOU 3796  OE1 GLU B  31    14313  14619  12022    493   -123  -1012       O  
ATOM   3797  OE2 GLU B  31      -7.389  23.338  85.988  1.00105.44           O  
ANISOU 3797  OE2 GLU B  31    14046  14561  11454    509   -199   -977       O  
ATOM   3798  N   GLU B  32     -11.307  20.963  80.971  1.00 72.54           N  
ANISOU 3798  N   GLU B  32     9574   9979   8009    600    108   -523       N  
ATOM   3799  CA  GLU B  32     -11.972  21.698  79.884  1.00 71.56           C  
ANISOU 3799  CA  GLU B  32     9431   9735   8024    599    143   -557       C  
ATOM   3800  C   GLU B  32     -12.301  23.118  80.338  1.00 75.87           C  
ANISOU 3800  C   GLU B  32    10051  10245   8529    617    177   -690       C  
ATOM   3801  O   GLU B  32     -12.737  23.323  81.458  1.00 76.59           O  
ANISOU 3801  O   GLU B  32    10197  10402   8503    660    231   -729       O  
ATOM   3802  CB  GLU B  32     -13.227  21.003  79.378  1.00 72.42           C  
ANISOU 3802  CB  GLU B  32     9478   9818   8220    640    228   -459       C  
ATOM   3803  CG  GLU B  32     -13.131  19.521  79.281  1.00 83.66           C  
ANISOU 3803  CG  GLU B  32    10841  11287   9659    634    221   -329       C  
ATOM   3804  CD  GLU B  32     -12.214  19.036  78.190  1.00103.89           C  
ANISOU 3804  CD  GLU B  32    13355  13804  12317    579    137   -294       C  
ATOM   3805  OE1 GLU B  32     -11.696  19.844  77.426  1.00 96.02           O  
ANISOU 3805  OE1 GLU B  32    12365  12740  11378    544     86   -361       O  
ATOM   3806  OE2 GLU B  32     -11.992  17.824  78.096  1.00 99.71           O  
ANISOU 3806  OE2 GLU B  32    12780  13302  11803    573    125   -195       O  
ATOM   3807  N   ASN B  33     -12.093  24.081  79.447  1.00 71.62           N  
ANISOU 3807  N   ASN B  33     9519   9599   8092    587    150   -757       N  
ATOM   3808  CA  ASN B  33     -12.218  25.507  79.723  1.00 72.07           C  
ANISOU 3808  CA  ASN B  33     9650   9596   8138    594    171   -891       C  
ATOM   3809  C   ASN B  33     -13.513  25.976  79.226  1.00 74.94           C  
ANISOU 3809  C   ASN B  33    10000   9882   8592    652    265   -882       C  
ATOM   3810  O   ASN B  33     -13.854  25.653  78.129  1.00 73.36           O  
ANISOU 3810  O   ASN B  33     9734   9628   8511    651    267   -806       O  
ATOM   3811  CB  ASN B  33     -11.158  26.264  78.947  1.00 72.86           C  
ANISOU 3811  CB  ASN B  33     9758   9613   8313    522     86   -954       C  
ATOM   3812  CG  ASN B  33     -10.713  27.515  79.645  1.00 97.87           C  
ANISOU 3812  CG  ASN B  33    13013  12753  11418    500     69  -1106       C  
ATOM   3813  OD1 ASN B  33     -11.160  27.814  80.744  1.00 94.40           O  
ANISOU 3813  OD1 ASN B  33    12635  12365  10868    542    119  -1172       O  
ATOM   3814  ND2 ASN B  33      -9.827  28.257  79.013  1.00 88.54           N  
ANISOU 3814  ND2 ASN B  33    11840  11492  10311    433      4  -1165       N  
ATOM   3815  N   ALA B  34     -14.287  26.649  80.058  1.00 71.89           N  
ANISOU 3815  N   ALA B  34     9670   9501   8142    710    347   -953       N  
ATOM   3816  CA  ALA B  34     -15.548  27.140  79.560  1.00 71.28           C  
ANISOU 3816  CA  ALA B  34     9572   9349   8163    774    439   -942       C  
ATOM   3817  C   ALA B  34     -15.442  28.342  78.655  1.00 74.24           C  
ANISOU 3817  C   ALA B  34     9966   9587   8655    761    423  -1008       C  
ATOM   3818  O   ALA B  34     -15.891  28.326  77.528  1.00 72.69           O  
ANISOU 3818  O   ALA B  34     9710   9324   8586    770    429   -942       O  
ATOM   3819  CB  ALA B  34     -16.501  27.431  80.698  1.00 73.20           C  
ANISOU 3819  CB  ALA B  34     9860   9641   8311    851    546   -987       C  
ATOM   3820  N   ASN B  35     -14.743  29.366  79.115  1.00 71.07           N  
ANISOU 3820  N   ASN B  35     9648   9145   8210    731    394  -1136       N  
ATOM   3821  CA  ASN B  35     -14.801  30.616  78.387  1.00 70.38           C  
ANISOU 3821  CA  ASN B  35     9590   8915   8236    731    403  -1201       C  
ATOM   3822  C   ASN B  35     -14.329  30.416  76.980  1.00 70.71           C  
ANISOU 3822  C   ASN B  35     9568   8895   8405    681    337  -1122       C  
ATOM   3823  O   ASN B  35     -14.844  31.025  76.067  1.00 70.39           O  
ANISOU 3823  O   ASN B  35     9509   8753   8482    708    366  -1102       O  
ATOM   3824  CB  ASN B  35     -14.131  31.809  79.077  1.00 72.57           C  
ANISOU 3824  CB  ASN B  35     9971   9140   8463    700    385  -1362       C  
ATOM   3825  CG  ASN B  35     -12.864  31.438  79.792  1.00 97.72           C  
ANISOU 3825  CG  ASN B  35    13183  12415  11530    621    291  -1410       C  
ATOM   3826  OD1 ASN B  35     -12.789  30.384  80.404  1.00 92.92           O  
ANISOU 3826  OD1 ASN B  35    12550  11937  10817    626    277  -1351       O  
ATOM   3827  ND2 ASN B  35     -11.857  32.296  79.718  1.00 90.34           N  
ANISOU 3827  ND2 ASN B  35    12297  11413  10616    548    224  -1512       N  
ATOM   3828  N   PHE B  36     -13.345  29.587  76.755  1.00 64.14           N  
ANISOU 3828  N   PHE B  36     8699   8120   7550    613    251  -1073       N  
ATOM   3829  CA  PHE B  36     -13.015  29.548  75.388  1.00 61.68           C  
ANISOU 3829  CA  PHE B  36     8334   7739   7360    577    207  -1009       C  
ATOM   3830  C   PHE B  36     -13.325  28.398  74.500  1.00 60.45           C  
ANISOU 3830  C   PHE B  36     8088   7621   7261    581    195   -876       C  
ATOM   3831  O   PHE B  36     -13.760  28.596  73.415  1.00 59.34           O  
ANISOU 3831  O   PHE B  36     7908   7413   7225    596    206   -827       O  
ATOM   3832  CB  PHE B  36     -11.564  29.858  75.163  1.00 63.62           C  
ANISOU 3832  CB  PHE B  36     8599   7960   7611    485    114  -1056       C  
ATOM   3833  CG  PHE B  36     -11.350  30.544  73.907  1.00 64.94           C  
ANISOU 3833  CG  PHE B  36     8753   8012   7909    460     98  -1041       C  
ATOM   3834  CD1 PHE B  36     -11.953  31.757  73.695  1.00 68.82           C  
ANISOU 3834  CD1 PHE B  36     9291   8389   8469    498    155  -1094       C  
ATOM   3835  CD2 PHE B  36     -10.654  29.952  72.892  1.00 66.06           C  
ANISOU 3835  CD2 PHE B  36     8834   8157   8107    410     38   -962       C  
ATOM   3836  CE1 PHE B  36     -11.810  32.395  72.521  1.00 69.41           C  
ANISOU 3836  CE1 PHE B  36     9354   8357   8663    482    147  -1065       C  
ATOM   3837  CE2 PHE B  36     -10.508  30.594  71.720  1.00 68.53           C  
ANISOU 3837  CE2 PHE B  36     9138   8369   8533    392     31   -940       C  
ATOM   3838  CZ  PHE B  36     -11.088  31.820  71.533  1.00 67.37           C  
ANISOU 3838  CZ  PHE B  36     9038   8109   8449    428     85   -987       C  
ATOM   3839  N   ASN B  37     -13.148  27.192  74.967  1.00 53.93           N  
ANISOU 3839  N   ASN B  37     7228   6901   6364    572    176   -818       N  
ATOM   3840  CA  ASN B  37     -13.352  26.062  74.103  1.00 51.18           C  
ANISOU 3840  CA  ASN B  37     6795   6577   6074    567    162   -702       C  
ATOM   3841  C   ASN B  37     -14.816  25.707  74.024  1.00 51.72           C  
ANISOU 3841  C   ASN B  37     6818   6656   6176    638    244   -641       C  
ATOM   3842  O   ASN B  37     -15.284  25.443  72.991  1.00 50.66           O  
ANISOU 3842  O   ASN B  37     6625   6489   6133    644    245   -578       O  
ATOM   3843  CB  ASN B  37     -12.482  24.880  74.480  1.00 51.22           C  
ANISOU 3843  CB  ASN B  37     6775   6673   6012    525    105   -654       C  
ATOM   3844  CG  ASN B  37     -11.068  24.978  73.905  1.00 66.18           C  
ANISOU 3844  CG  ASN B  37     8667   8546   7932    451     13   -671       C  
ATOM   3845  OD1 ASN B  37     -10.351  24.007  73.875  1.00 59.75           O  
ANISOU 3845  OD1 ASN B  37     7817   7789   7097    419    -37   -618       O  
ATOM   3846  ND2 ASN B  37     -10.680  26.145  73.463  1.00 54.11           N  
ANISOU 3846  ND2 ASN B  37     7174   6932   6453    424     -5   -741       N  
ATOM   3847  N   LYS B  38     -15.538  25.793  75.114  1.00 47.05           N  
ANISOU 3847  N   LYS B  38     6256   6110   5511    690    315   -668       N  
ATOM   3848  CA  LYS B  38     -16.964  25.551  75.211  1.00 46.03           C  
ANISOU 3848  CA  LYS B  38     6083   5997   5410    760    406   -618       C  
ATOM   3849  C   LYS B  38     -17.773  26.502  74.348  1.00 47.56           C  
ANISOU 3849  C   LYS B  38     6260   6097   5715    804    441   -629       C  
ATOM   3850  O   LYS B  38     -18.881  26.213  74.028  1.00 47.29           O  
ANISOU 3850  O   LYS B  38     6162   6069   5737    851    494   -569       O  
ATOM   3851  CB  LYS B  38     -17.377  25.753  76.657  1.00 49.72           C  
ANISOU 3851  CB  LYS B  38     6605   6526   5761    807    478   -671       C  
ATOM   3852  CG  LYS B  38     -18.653  25.060  77.092  1.00 63.01           C  
ANISOU 3852  CG  LYS B  38     8235   8270   7438    868    572   -599       C  
ATOM   3853  CD  LYS B  38     -18.752  24.950  78.608  1.00 70.72           C  
ANISOU 3853  CD  LYS B  38     9268   9336   8267    900    631   -634       C  
ATOM   3854  CE  LYS B  38     -20.189  24.844  79.078  1.00 77.20           C  
ANISOU 3854  CE  LYS B  38    10053  10189   9092    979    754   -598       C  
ATOM   3855  NZ  LYS B  38     -20.443  25.655  80.281  1.00 86.00           N  
ANISOU 3855  NZ  LYS B  38    11252  11331  10094   1034    828   -695       N  
ATOM   3856  N   ILE B  39     -17.246  27.678  74.063  1.00 42.00           N  
ANISOU 3856  N   ILE B  39     5614   5305   5038    791    416   -707       N  
ATOM   3857  CA  ILE B  39     -17.843  28.605  73.150  1.00 40.62           C  
ANISOU 3857  CA  ILE B  39     5428   5032   4973    829    439   -706       C  
ATOM   3858  C   ILE B  39     -17.189  28.704  71.764  1.00 41.47           C  
ANISOU 3858  C   ILE B  39     5509   5078   5170    779    364   -666       C  
ATOM   3859  O   ILE B  39     -17.844  28.779  70.783  1.00 40.28           O  
ANISOU 3859  O   ILE B  39     5305   4892   5106    808    371   -607       O  
ATOM   3860  CB  ILE B  39     -17.857  29.976  73.728  1.00 44.88           C  
ANISOU 3860  CB  ILE B  39     6056   5497   5501    862    482   -816       C  
ATOM   3861  CG1 ILE B  39     -18.786  30.033  74.916  1.00 46.14           C  
ANISOU 3861  CG1 ILE B  39     6235   5706   5589    934    578   -852       C  
ATOM   3862  CG2 ILE B  39     -18.333  30.937  72.691  1.00 46.02           C  
ANISOU 3862  CG2 ILE B  39     6189   5528   5767    899    498   -804       C  
ATOM   3863  CD1 ILE B  39     -18.560  31.158  75.768  1.00 53.41           C  
ANISOU 3863  CD1 ILE B  39     7258   6577   6460    951    613   -980       C  
ATOM   3864  N   PHE B  40     -15.883  28.718  71.688  1.00 36.60           N  
ANISOU 3864  N   PHE B  40     4927   4452   4526    703    291   -699       N  
ATOM   3865  CA  PHE B  40     -15.158  28.885  70.429  1.00 34.64           C  
ANISOU 3865  CA  PHE B  40     4661   4147   4355    653    227   -666       C  
ATOM   3866  C   PHE B  40     -15.368  27.710  69.458  1.00 33.81           C  
ANISOU 3866  C   PHE B  40     4468   4090   4288    641    195   -560       C  
ATOM   3867  O   PHE B  40     -15.693  27.922  68.301  1.00 32.49           O  
ANISOU 3867  O   PHE B  40     4265   3878   4202    653    186   -511       O  
ATOM   3868  CB  PHE B  40     -13.672  29.124  70.686  1.00 36.70           C  
ANISOU 3868  CB  PHE B  40     4971   4397   4575    572    161   -728       C  
ATOM   3869  CG  PHE B  40     -12.869  29.246  69.432  1.00 38.05           C  
ANISOU 3869  CG  PHE B  40     5120   4517   4820    518    103   -690       C  
ATOM   3870  CD1 PHE B  40     -12.894  30.420  68.698  1.00 41.51           C  
ANISOU 3870  CD1 PHE B  40     5587   4844   5340    525    115   -705       C  
ATOM   3871  CD2 PHE B  40     -12.115  28.168  68.963  1.00 40.05           C  
ANISOU 3871  CD2 PHE B  40     5324   4832   5063    466     43   -633       C  
ATOM   3872  CE1 PHE B  40     -12.171  30.538  67.535  1.00 42.36           C  
ANISOU 3872  CE1 PHE B  40     5675   4909   5510    478     70   -663       C  
ATOM   3873  CE2 PHE B  40     -11.379  28.271  67.792  1.00 42.56           C  
ANISOU 3873  CE2 PHE B  40     5621   5107   5443    420     -2   -598       C  
ATOM   3874  CZ  PHE B  40     -11.405  29.460  67.073  1.00 40.99           C  
ANISOU 3874  CZ  PHE B  40     5452   4805   5319    425     12   -611       C  
ATOM   3875  N   LEU B  41     -15.202  26.484  69.943  1.00 28.38           N  
ANISOU 3875  N   LEU B  41     3747   3493   3542    619    181   -526       N  
ATOM   3876  CA  LEU B  41     -15.276  25.277  69.097  1.00 26.13           C  
ANISOU 3876  CA  LEU B  41     3385   3249   3292    598    148   -437       C  
ATOM   3877  C   LEU B  41     -16.643  24.996  68.445  1.00 30.11           C  
ANISOU 3877  C   LEU B  41     3820   3756   3863    650    188   -374       C  
ATOM   3878  O   LEU B  41     -16.709  24.675  67.266  1.00 28.99           O  
ANISOU 3878  O   LEU B  41     3631   3603   3783    636    153   -324       O  
ATOM   3879  CB  LEU B  41     -14.824  24.037  69.877  1.00 25.28           C  
ANISOU 3879  CB  LEU B  41     3264   3229   3113    569    133   -413       C  
ATOM   3880  CG  LEU B  41     -13.396  24.003  70.399  1.00 29.02           C  
ANISOU 3880  CG  LEU B  41     3782   3723   3522    513     76   -456       C  
ATOM   3881  CD1 LEU B  41     -13.233  22.820  71.329  1.00 28.46           C  
ANISOU 3881  CD1 LEU B  41     3697   3743   3374    508     77   -420       C  
ATOM   3882  CD2 LEU B  41     -12.383  23.938  69.260  1.00 30.54           C  
ANISOU 3882  CD2 LEU B  41     3956   3881   3768    457      8   -438       C  
ATOM   3883  N   PRO B  42     -17.734  25.080  69.202  1.00 27.82           N  
ANISOU 3883  N   PRO B  42     3520   3490   3560    710    259   -377       N  
ATOM   3884  CA  PRO B  42     -19.022  24.793  68.580  1.00 27.94           C  
ANISOU 3884  CA  PRO B  42     3456   3515   3646    755    291   -315       C  
ATOM   3885  C   PRO B  42     -19.396  25.779  67.458  1.00 32.62           C  
ANISOU 3885  C   PRO B  42     4039   4037   4320    787    280   -307       C  
ATOM   3886  O   PRO B  42     -20.033  25.359  66.454  1.00 33.29           O  
ANISOU 3886  O   PRO B  42     4049   4134   4467    795    261   -245       O  
ATOM   3887  CB  PRO B  42     -20.001  24.886  69.735  1.00 30.65           C  
ANISOU 3887  CB  PRO B  42     3797   3893   3954    815    379   -329       C  
ATOM   3888  CG  PRO B  42     -19.282  25.589  70.818  1.00 35.39           C  
ANISOU 3888  CG  PRO B  42     4495   4482   4471    813    394   -414       C  
ATOM   3889  CD  PRO B  42     -17.853  25.336  70.640  1.00 30.30           C  
ANISOU 3889  CD  PRO B  42     3887   3835   3792    737    314   -432       C  
ATOM   3890  N   THR B  43     -18.978  27.040  67.629  1.00 27.75           N  
ANISOU 3890  N   THR B  43     3496   3346   3702    801    290   -368       N  
ATOM   3891  CA  THR B  43     -19.042  28.080  66.604  1.00 27.28           C  
ANISOU 3891  CA  THR B  43     3446   3203   3714    825    276   -360       C  
ATOM   3892  C   THR B  43     -18.255  27.746  65.327  1.00 29.81           C  
ANISOU 3892  C   THR B  43     3748   3515   4063    767    199   -315       C  
ATOM   3893  O   THR B  43     -18.759  27.934  64.201  1.00 28.32           O  
ANISOU 3893  O   THR B  43     3517   3309   3935    793    182   -260       O  
ATOM   3894  CB  THR B  43     -18.456  29.458  67.133  1.00 35.98           C  
ANISOU 3894  CB  THR B  43     4648   4214   4809    832    299   -445       C  
ATOM   3895  OG1 THR B  43     -18.866  29.722  68.499  1.00 35.41           O  
ANISOU 3895  OG1 THR B  43     4616   4156   4682    871    366   -511       O  
ATOM   3896  CG2 THR B  43     -18.870  30.599  66.209  1.00 34.41           C  
ANISOU 3896  CG2 THR B  43     4456   3921   4697    881    311   -424       C  
ATOM   3897  N   ILE B  44     -16.999  27.326  65.503  1.00 26.36           N  
ANISOU 3897  N   ILE B  44     3344   3091   3579    693    153   -341       N  
ATOM   3898  CA  ILE B  44     -16.176  26.877  64.375  1.00 25.37           C  
ANISOU 3898  CA  ILE B  44     3199   2969   3473    637     87   -302       C  
ATOM   3899  C   ILE B  44     -16.868  25.675  63.764  1.00 27.08           C  
ANISOU 3899  C   ILE B  44     3331   3254   3705    640     71   -236       C  
ATOM   3900  O   ILE B  44     -17.099  25.644  62.572  1.00 26.66           O  
ANISOU 3900  O   ILE B  44     3242   3195   3694    644     42   -190       O  
ATOM   3901  CB  ILE B  44     -14.703  26.465  64.764  1.00 28.39           C  
ANISOU 3901  CB  ILE B  44     3616   3367   3802    559     43   -337       C  
ATOM   3902  CG1 ILE B  44     -13.894  27.651  65.311  1.00 29.65           C  
ANISOU 3902  CG1 ILE B  44     3855   3459   3951    539     47   -411       C  
ATOM   3903  CG2 ILE B  44     -13.968  25.926  63.554  1.00 27.96           C  
ANISOU 3903  CG2 ILE B  44     3531   3321   3771    511    -12   -292       C  
ATOM   3904  CD1 ILE B  44     -13.787  28.884  64.314  1.00 38.74           C  
ANISOU 3904  CD1 ILE B  44     5034   4512   5174    547     48   -402       C  
ATOM   3905  N   TYR B  45     -17.265  24.719  64.593  1.00 22.91           N  
ANISOU 3905  N   TYR B  45     2772   2788   3143    640     94   -232       N  
ATOM   3906  CA  TYR B  45     -17.983  23.545  64.085  1.00 21.79           C  
ANISOU 3906  CA  TYR B  45     2548   2703   3027    637     83   -175       C  
ATOM   3907  C   TYR B  45     -19.229  23.903  63.247  1.00 25.80           C  
ANISOU 3907  C   TYR B  45     2997   3206   3599    690     93   -135       C  
ATOM   3908  O   TYR B  45     -19.411  23.351  62.168  1.00 25.02           O  
ANISOU 3908  O   TYR B  45     2846   3129   3530    673     50    -95       O  
ATOM   3909  CB  TYR B  45     -18.367  22.591  65.220  1.00 22.47           C  
ANISOU 3909  CB  TYR B  45     2613   2848   3077    636    122   -170       C  
ATOM   3910  CG  TYR B  45     -17.199  21.971  65.951  1.00 23.53           C  
ANISOU 3910  CG  TYR B  45     2788   3005   3147    585    102   -190       C  
ATOM   3911  CD1 TYR B  45     -17.316  21.654  67.287  1.00 25.77           C  
ANISOU 3911  CD1 TYR B  45     3091   3329   3372    597    146   -202       C  
ATOM   3912  CD2 TYR B  45     -15.962  21.697  65.304  1.00 23.53           C  
ANISOU 3912  CD2 TYR B  45     2805   2994   3142    529     40   -192       C  
ATOM   3913  CE1 TYR B  45     -16.259  21.093  68.000  1.00 25.76           C  
ANISOU 3913  CE1 TYR B  45     3124   3358   3305    558    123   -214       C  
ATOM   3914  CE2 TYR B  45     -14.903  21.136  66.008  1.00 24.05           C  
ANISOU 3914  CE2 TYR B  45     2899   3086   3153    490     20   -206       C  
ATOM   3915  CZ  TYR B  45     -15.066  20.847  67.371  1.00 31.18           C  
ANISOU 3915  CZ  TYR B  45     3821   4031   3995    506     58   -215       C  
ATOM   3916  OH  TYR B  45     -14.066  20.304  68.125  1.00 30.77           O  
ANISOU 3916  OH  TYR B  45     3794   4015   3881    475     35   -221       O  
ATOM   3917  N   SER B  46     -20.042  24.836  63.741  1.00 23.49           N  
ANISOU 3917  N   SER B  46     2714   2888   3324    757    148   -148       N  
ATOM   3918  CA  SER B  46     -21.298  25.250  63.088  1.00 23.93           C  
ANISOU 3918  CA  SER B  46     2706   2944   3443    822    163   -107       C  
ATOM   3919  C   SER B  46     -21.108  25.965  61.752  1.00 28.53           C  
ANISOU 3919  C   SER B  46     3294   3484   4062    832    115    -78       C  
ATOM   3920  O   SER B  46     -21.914  25.781  60.834  1.00 29.54           O  
ANISOU 3920  O   SER B  46     3350   3643   4231    857     90    -27       O  
ATOM   3921  CB  SER B  46     -22.123  26.164  64.030  1.00 26.70           C  
ANISOU 3921  CB  SER B  46     3072   3268   3803    900    244   -133       C  
ATOM   3922  OG  SER B  46     -22.700  25.424  65.118  1.00 31.81           O  
ANISOU 3922  OG  SER B  46     3689   3974   4424    907    298   -137       O  
ATOM   3923  N   ILE B  47     -20.065  26.781  61.651  1.00 24.13           N  
ANISOU 3923  N   ILE B  47     2819   2861   3491    812    103   -108       N  
ATOM   3924  CA  ILE B  47     -19.758  27.530  60.434  1.00 24.01           C  
ANISOU 3924  CA  ILE B  47     2820   2798   3506    819     67    -74       C  
ATOM   3925  C   ILE B  47     -19.336  26.610  59.284  1.00 26.69           C  
ANISOU 3925  C   ILE B  47     3120   3188   3833    766     -1    -35       C  
ATOM   3926  O   ILE B  47     -19.673  26.843  58.109  1.00 26.01           O  
ANISOU 3926  O   ILE B  47     3005   3108   3770    789    -35     16       O  
ATOM   3927  CB  ILE B  47     -18.602  28.564  60.683  1.00 27.19           C  
ANISOU 3927  CB  ILE B  47     3320   3112   3899    795     75   -119       C  
ATOM   3928  CG1 ILE B  47     -19.053  29.685  61.623  1.00 28.50           C  
ANISOU 3928  CG1 ILE B  47     3534   3209   4086    855    143   -164       C  
ATOM   3929  CG2 ILE B  47     -18.116  29.184  59.377  1.00 27.51           C  
ANISOU 3929  CG2 ILE B  47     3378   3108   3968    788     39    -73       C  
ATOM   3930  CD1 ILE B  47     -17.888  30.600  62.093  1.00 35.46           C  
ANISOU 3930  CD1 ILE B  47     4513   4003   4957    815    151   -230       C  
ATOM   3931  N   ILE B  48     -18.569  25.586  59.639  1.00 23.13           N  
ANISOU 3931  N   ILE B  48     2674   2774   3342    698    -21    -60       N  
ATOM   3932  CA  ILE B  48     -18.090  24.583  58.685  1.00 22.57           C  
ANISOU 3932  CA  ILE B  48     2571   2748   3256    645    -78    -37       C  
ATOM   3933  C   ILE B  48     -19.234  23.736  58.265  1.00 27.01           C  
ANISOU 3933  C   ILE B  48     3046   3376   3841    661    -92     -5       C  
ATOM   3934  O   ILE B  48     -19.466  23.544  57.061  1.00 27.06           O  
ANISOU 3934  O   ILE B  48     3016   3410   3856    660   -138     29       O  
ATOM   3935  CB  ILE B  48     -17.007  23.692  59.289  1.00 24.99           C  
ANISOU 3935  CB  ILE B  48     2901   3072   3521    578    -87    -71       C  
ATOM   3936  CG1 ILE B  48     -15.726  24.495  59.416  1.00 25.11           C  
ANISOU 3936  CG1 ILE B  48     2991   3031   3519    549    -91   -101       C  
ATOM   3937  CG2 ILE B  48     -16.769  22.467  58.415  1.00 25.17           C  
ANISOU 3937  CG2 ILE B  48     2881   3145   3539    533   -134    -51       C  
ATOM   3938  CD1 ILE B  48     -15.488  25.334  58.177  1.00 35.35           C  
ANISOU 3938  CD1 ILE B  48     4305   4289   4837    558   -112    -68       C  
ATOM   3939  N   PHE B  49     -19.976  23.266  59.262  1.00 24.07           N  
ANISOU 3939  N   PHE B  49     2639   3030   3477    675    -52    -15       N  
ATOM   3940  CA  PHE B  49     -21.266  22.644  59.003  1.00 24.22           C  
ANISOU 3940  CA  PHE B  49     2564   3105   3533    697    -55     16       C  
ATOM   3941  C   PHE B  49     -22.044  23.456  57.950  1.00 29.21           C  
ANISOU 3941  C   PHE B  49     3161   3739   4201    754    -79     57       C  
ATOM   3942  O   PHE B  49     -22.387  22.932  56.893  1.00 28.78           O  
ANISOU 3942  O   PHE B  49     3050   3730   4154    739   -134     84       O  
ATOM   3943  CB  PHE B  49     -22.106  22.515  60.279  1.00 26.14           C  
ANISOU 3943  CB  PHE B  49     2780   3363   3790    729     13      9       C  
ATOM   3944  CG  PHE B  49     -23.513  22.080  60.003  1.00 28.39           C  
ANISOU 3944  CG  PHE B  49     2958   3701   4127    756     17     45       C  
ATOM   3945  CD1 PHE B  49     -23.769  20.807  59.523  1.00 31.31           C  
ANISOU 3945  CD1 PHE B  49     3261   4122   4515    702    -21     58       C  
ATOM   3946  CD2 PHE B  49     -24.572  22.962  60.137  1.00 31.13           C  
ANISOU 3946  CD2 PHE B  49     3269   4045   4514    836     54     65       C  
ATOM   3947  CE1 PHE B  49     -25.074  20.408  59.237  1.00 32.75           C  
ANISOU 3947  CE1 PHE B  49     3335   4355   4752    719    -24     88       C  
ATOM   3948  CE2 PHE B  49     -25.883  22.562  59.844  1.00 34.33           C  
ANISOU 3948  CE2 PHE B  49     3561   4507   4975    860     53    102       C  
ATOM   3949  CZ  PHE B  49     -26.132  21.300  59.400  1.00 32.20           C  
ANISOU 3949  CZ  PHE B  49     3221   4292   4721    798     11    112       C  
ATOM   3950  N   LEU B  50     -22.299  24.731  58.245  1.00 26.59           N  
ANISOU 3950  N   LEU B  50     2863   3355   3886    820    -40     62       N  
ATOM   3951  CA  LEU B  50     -23.153  25.543  57.389  1.00 27.66           C  
ANISOU 3951  CA  LEU B  50     2959   3490   4061    889    -55    111       C  
ATOM   3952  C   LEU B  50     -22.574  25.738  55.978  1.00 31.25           C  
ANISOU 3952  C   LEU B  50     3432   3945   4496    872   -121    145       C  
ATOM   3953  O   LEU B  50     -23.236  25.481  54.985  1.00 30.83           O  
ANISOU 3953  O   LEU B  50     3313   3949   4452    888   -171    187       O  
ATOM   3954  CB  LEU B  50     -23.454  26.907  58.055  1.00 28.59           C  
ANISOU 3954  CB  LEU B  50     3121   3534   4208    968     10    106       C  
ATOM   3955  CG  LEU B  50     -24.706  26.912  58.939  1.00 33.80           C  
ANISOU 3955  CG  LEU B  50     3718   4218   4906   1029     71    106       C  
ATOM   3956  CD1 LEU B  50     -24.829  28.164  59.820  1.00 34.40           C  
ANISOU 3956  CD1 LEU B  50     3855   4213   5000   1099    149     78       C  
ATOM   3957  CD2 LEU B  50     -25.933  26.744  58.052  1.00 36.87           C  
ANISOU 3957  CD2 LEU B  50     3995   4672   5342   1075     36    169       C  
ATOM   3958  N   THR B  51     -21.337  26.207  55.911  1.00 27.38           N  
ANISOU 3958  N   THR B  51     3031   3396   3978    840   -120    127       N  
ATOM   3959  CA  THR B  51     -20.709  26.512  54.647  1.00 26.34           C  
ANISOU 3959  CA  THR B  51     2926   3258   3824    827   -168    162       C  
ATOM   3960  C   THR B  51     -20.353  25.217  53.945  1.00 27.30           C  
ANISOU 3960  C   THR B  51     3014   3453   3907    759   -224    155       C  
ATOM   3961  O   THR B  51     -20.212  25.202  52.729  1.00 25.72           O  
ANISOU 3961  O   THR B  51     2807   3282   3682    756   -272    189       O  
ATOM   3962  CB  THR B  51     -19.421  27.386  54.852  1.00 33.83           C  
ANISOU 3962  CB  THR B  51     3975   4118   4762    803   -142    143       C  
ATOM   3963  OG1 THR B  51     -18.456  26.656  55.606  1.00 32.75           O  
ANISOU 3963  OG1 THR B  51     3868   3981   4594    730   -136     84       O  
ATOM   3964  CG2 THR B  51     -19.725  28.684  55.601  1.00 32.75           C  
ANISOU 3964  CG2 THR B  51     3882   3893   4669    864    -82    136       C  
ATOM   3965  N   GLY B  52     -20.212  24.140  54.729  1.00 23.25           N  
ANISOU 3965  N   GLY B  52     2483   2965   3386    709   -214    109       N  
ATOM   3966  CA  GLY B  52     -19.806  22.834  54.222  1.00 22.69           C  
ANISOU 3966  CA  GLY B  52     2387   2947   3288    642   -257     92       C  
ATOM   3967  C   GLY B  52     -20.897  22.022  53.545  1.00 28.82           C  
ANISOU 3967  C   GLY B  52     3072   3798   4078    644   -301    107       C  
ATOM   3968  O   GLY B  52     -20.656  21.421  52.487  1.00 29.78           O  
ANISOU 3968  O   GLY B  52     3182   3963   4172    610   -354    106       O  
ATOM   3969  N   ILE B  53     -22.089  21.970  54.138  1.00 24.42           N  
ANISOU 3969  N   ILE B  53     2449   3264   3566    679   -279    116       N  
ATOM   3970  CA  ILE B  53     -23.226  21.375  53.436  1.00 24.63           C  
ANISOU 3970  CA  ILE B  53     2377   3364   3617    683   -325    133       C  
ATOM   3971  C   ILE B  53     -23.525  22.113  52.108  1.00 29.99           C  
ANISOU 3971  C   ILE B  53     3044   4073   4276    728   -381    180       C  
ATOM   3972  O   ILE B  53     -23.682  21.473  51.062  1.00 29.73           O  
ANISOU 3972  O   ILE B  53     2974   4104   4219    699   -448    178       O  
ATOM   3973  CB  ILE B  53     -24.522  21.231  54.326  1.00 27.69           C  
ANISOU 3973  CB  ILE B  53     2682   3775   4066    716   -285    142       C  
ATOM   3974  CG1 ILE B  53     -24.951  22.565  54.930  1.00 27.88           C  
ANISOU 3974  CG1 ILE B  53     2724   3755   4113    802   -230    169       C  
ATOM   3975  CG2 ILE B  53     -24.295  20.222  55.441  1.00 28.18           C  
ANISOU 3975  CG2 ILE B  53     2744   3825   4137    661   -240    105       C  
ATOM   3976  CD1 ILE B  53     -25.902  23.310  54.104  1.00 36.70           C  
ANISOU 3976  CD1 ILE B  53     3783   4905   5257    873   -262    222       C  
ATOM   3977  N   VAL B  54     -23.560  23.442  52.142  1.00 26.64           N  
ANISOU 3977  N   VAL B  54     2658   3604   3861    798   -355    220       N  
ATOM   3978  CA  VAL B  54     -23.957  24.213  50.974  1.00 26.87           C  
ANISOU 3978  CA  VAL B  54     2672   3661   3876    855   -401    280       C  
ATOM   3979  C   VAL B  54     -22.930  24.050  49.847  1.00 30.50           C  
ANISOU 3979  C   VAL B  54     3188   4134   4266    813   -447    283       C  
ATOM   3980  O   VAL B  54     -23.290  23.859  48.686  1.00 29.96           O  
ANISOU 3980  O   VAL B  54     3082   4139   4163    820   -514    310       O  
ATOM   3981  CB  VAL B  54     -24.111  25.734  51.301  1.00 30.83           C  
ANISOU 3981  CB  VAL B  54     3215   4088   4411    943   -350    326       C  
ATOM   3982  CG1 VAL B  54     -24.414  26.502  50.076  1.00 31.18           C  
ANISOU 3982  CG1 VAL B  54     3251   4157   4439   1003   -396    401       C  
ATOM   3983  CG2 VAL B  54     -25.225  25.991  52.379  1.00 31.11           C  
ANISOU 3983  CG2 VAL B  54     3193   4114   4515   1000   -296    325       C  
ATOM   3984  N   GLY B  55     -21.646  24.154  50.194  1.00 26.67           N  
ANISOU 3984  N   GLY B  55     2791   3584   3759    772   -412    255       N  
ATOM   3985  CA  GLY B  55     -20.573  24.220  49.201  1.00 25.94           C  
ANISOU 3985  CA  GLY B  55     2758   3492   3605    742   -437    266       C  
ATOM   3986  C   GLY B  55     -20.356  22.876  48.540  1.00 29.38           C  
ANISOU 3986  C   GLY B  55     3166   4000   3998    676   -488    224       C  
ATOM   3987  O   GLY B  55     -20.390  22.758  47.307  1.00 29.78           O  
ANISOU 3987  O   GLY B  55     3209   4112   3995    678   -541    246       O  
ATOM   3988  N   ASN B  56     -20.153  21.867  49.375  1.00 24.57           N  
ANISOU 3988  N   ASN B  56     2544   3383   3409    621   -469    165       N  
ATOM   3989  CA  ASN B  56     -19.992  20.499  48.926  1.00 24.27           C  
ANISOU 3989  CA  ASN B  56     2479   3396   3347    557   -507    116       C  
ATOM   3990  C   ASN B  56     -21.248  19.923  48.274  1.00 29.50           C  
ANISOU 3990  C   ASN B  56     3051   4141   4016    561   -568    115       C  
ATOM   3991  O   ASN B  56     -21.171  19.316  47.198  1.00 30.05           O  
ANISOU 3991  O   ASN B  56     3111   4270   4038    533   -623     95       O  
ATOM   3992  CB  ASN B  56     -19.552  19.623  50.099  1.00 23.82           C  
ANISOU 3992  CB  ASN B  56     2428   3299   3323    506   -465     65       C  
ATOM   3993  CG  ASN B  56     -18.165  19.948  50.545  1.00 39.71           C  
ANISOU 3993  CG  ASN B  56     4521   5249   5317    486   -424     56       C  
ATOM   3994  OD1 ASN B  56     -17.228  19.853  49.742  1.00 32.12           O  
ANISOU 3994  OD1 ASN B  56     3600   4293   4311    463   -439     51       O  
ATOM   3995  ND2 ASN B  56     -18.010  20.374  51.815  1.00 31.64           N  
ANISOU 3995  ND2 ASN B  56     3523   4173   4326    497   -373     51       N  
ATOM   3996  N   GLY B  57     -22.393  20.126  48.921  1.00 26.45           N  
ANISOU 3996  N   GLY B  57     2598   3763   3689    597   -557    132       N  
ATOM   3997  CA  GLY B  57     -23.694  19.769  48.343  1.00 26.97           C  
ANISOU 3997  CA  GLY B  57     2563   3912   3772    608   -617    141       C  
ATOM   3998  C   GLY B  57     -23.888  20.365  46.960  1.00 31.41           C  
ANISOU 3998  C   GLY B  57     3122   4538   4273    649   -683    184       C  
ATOM   3999  O   GLY B  57     -24.462  19.729  46.083  1.00 31.95           O  
ANISOU 3999  O   GLY B  57     3132   4691   4317    627   -756    166       O  
ATOM   4000  N   LEU B  58     -23.381  21.571  46.741  1.00 27.67           N  
ANISOU 4000  N   LEU B  58     2716   4025   3773    706   -660    241       N  
ATOM   4001  CA  LEU B  58     -23.447  22.158  45.406  1.00 28.05           C  
ANISOU 4001  CA  LEU B  58     2773   4132   3754    747   -717    296       C  
ATOM   4002  C   LEU B  58     -22.516  21.453  44.446  1.00 31.28           C  
ANISOU 4002  C   LEU B  58     3230   4577   4078    689   -751    257       C  
ATOM   4003  O   LEU B  58     -22.897  21.216  43.314  1.00 30.82           O  
ANISOU 4003  O   LEU B  58     3143   4610   3957    693   -823    263       O  
ATOM   4004  CB  LEU B  58     -23.102  23.643  45.412  1.00 28.12           C  
ANISOU 4004  CB  LEU B  58     2845   4075   3763    821   -674    374       C  
ATOM   4005  CG  LEU B  58     -24.252  24.592  45.612  1.00 33.12           C  
ANISOU 4005  CG  LEU B  58     3422   4710   4451    913   -672    443       C  
ATOM   4006  CD1 LEU B  58     -23.677  26.006  45.683  1.00 33.67           C  
ANISOU 4006  CD1 LEU B  58     3576   4688   4530    974   -616    510       C  
ATOM   4007  CD2 LEU B  58     -25.234  24.418  44.487  1.00 35.29           C  
ANISOU 4007  CD2 LEU B  58     3615   5105   4687    945   -764    479       C  
ATOM   4008  N   VAL B  59     -21.297  21.129  44.879  1.00 27.43           N  
ANISOU 4008  N   VAL B  59     2816   4024   3584    638   -699    216       N  
ATOM   4009  CA  VAL B  59     -20.368  20.451  43.973  1.00 27.32           C  
ANISOU 4009  CA  VAL B  59     2847   4041   3492    588   -721    177       C  
ATOM   4010  C   VAL B  59     -20.987  19.118  43.572  1.00 32.62           C  
ANISOU 4010  C   VAL B  59     3452   4786   4155    536   -782    106       C  
ATOM   4011  O   VAL B  59     -20.961  18.744  42.415  1.00 32.44           O  
ANISOU 4011  O   VAL B  59     3431   4839   4055    523   -838     88       O  
ATOM   4012  CB  VAL B  59     -18.965  20.228  44.589  1.00 30.00           C  
ANISOU 4012  CB  VAL B  59     3260   4300   3839    542   -655    143       C  
ATOM   4013  CG1 VAL B  59     -18.048  19.576  43.591  1.00 29.55           C  
ANISOU 4013  CG1 VAL B  59     3244   4280   3704    501   -671    108       C  
ATOM   4014  CG2 VAL B  59     -18.361  21.532  45.059  1.00 29.55           C  
ANISOU 4014  CG2 VAL B  59     3263   4164   3802    581   -597    202       C  
ATOM   4015  N   ILE B  60     -21.607  18.438  44.528  1.00 30.40           N  
ANISOU 4015  N   ILE B  60     3114   4485   3954    506   -770     66       N  
ATOM   4016  CA  ILE B  60     -22.194  17.123  44.265  1.00 31.05           C  
ANISOU 4016  CA  ILE B  60     3130   4618   4048    445   -819     -7       C  
ATOM   4017  C   ILE B  60     -23.328  17.190  43.236  1.00 37.72           C  
ANISOU 4017  C   ILE B  60     3901   5573   4858    467   -911      6       C  
ATOM   4018  O   ILE B  60     -23.325  16.434  42.264  1.00 37.75           O  
ANISOU 4018  O   ILE B  60     3898   5643   4804    426   -971    -49       O  
ATOM   4019  CB  ILE B  60     -22.684  16.458  45.570  1.00 33.51           C  
ANISOU 4019  CB  ILE B  60     3391   4881   4462    412   -778    -35       C  
ATOM   4020  CG1 ILE B  60     -21.482  16.178  46.476  1.00 32.52           C  
ANISOU 4020  CG1 ILE B  60     3339   4664   4354    382   -702    -57       C  
ATOM   4021  CG2 ILE B  60     -23.429  15.168  45.273  1.00 34.24           C  
ANISOU 4021  CG2 ILE B  60     3406   5021   4582    347   -830   -104       C  
ATOM   4022  CD1 ILE B  60     -21.816  15.525  47.796  1.00 39.87           C  
ANISOU 4022  CD1 ILE B  60     4232   5545   5370    353   -654    -76       C  
ATOM   4023  N   LEU B  61     -24.273  18.104  43.436  1.00 36.64           N  
ANISOU 4023  N   LEU B  61     3710   5458   4755    535   -921     76       N  
ATOM   4024  CA  LEU B  61     -25.448  18.200  42.569  1.00 38.74           C  
ANISOU 4024  CA  LEU B  61     3888   5834   4997    563  -1012     97       C  
ATOM   4025  C   LEU B  61     -25.081  18.836  41.226  1.00 47.18           C  
ANISOU 4025  C   LEU B  61     5007   6971   5948    606  -1063    141       C  
ATOM   4026  O   LEU B  61     -25.464  18.348  40.158  1.00 48.38           O  
ANISOU 4026  O   LEU B  61     5126   7227   6031    586  -1150    110       O  
ATOM   4027  CB  LEU B  61     -26.574  18.982  43.268  1.00 39.19           C  
ANISOU 4027  CB  LEU B  61     3864   5889   5136    631   -998    165       C  
ATOM   4028  CG  LEU B  61     -27.076  18.413  44.621  1.00 43.32           C  
ANISOU 4028  CG  LEU B  61     4329   6357   5774    597   -941    132       C  
ATOM   4029  CD1 LEU B  61     -27.580  19.528  45.564  1.00 43.44           C  
ANISOU 4029  CD1 LEU B  61     4326   6324   5857    681   -877    206       C  
ATOM   4030  CD2 LEU B  61     -28.138  17.304  44.445  1.00 45.24           C  
ANISOU 4030  CD2 LEU B  61     4453   6675   6062    536  -1005     77       C  
ATOM   4031  N   VAL B  62     -24.309  19.910  41.262  1.00 45.47           N  
ANISOU 4031  N   VAL B  62     4873   6697   5705    660  -1008    212       N  
ATOM   4032  CA  VAL B  62     -23.916  20.568  40.021  1.00 47.05           C  
ANISOU 4032  CA  VAL B  62     5127   6956   5794    704  -1044    269       C  
ATOM   4033  C   VAL B  62     -23.161  19.672  39.045  1.00 55.37           C  
ANISOU 4033  C   VAL B  62     6228   8064   6745    643  -1077    198       C  
ATOM   4034  O   VAL B  62     -23.466  19.696  37.863  1.00 56.30           O  
ANISOU 4034  O   VAL B  62     6336   8290   6765    662  -1152    212       O  
ATOM   4035  CB  VAL B  62     -23.099  21.814  40.274  1.00 50.03           C  
ANISOU 4035  CB  VAL B  62     5591   7245   6174    760   -967    353       C  
ATOM   4036  CG1 VAL B  62     -22.396  22.270  38.979  1.00 50.30           C  
ANISOU 4036  CG1 VAL B  62     5696   7330   6086    784   -987    403       C  
ATOM   4037  CG2 VAL B  62     -24.010  22.893  40.848  1.00 50.10           C  
ANISOU 4037  CG2 VAL B  62     5553   7223   6258    844   -952    437       C  
ATOM   4038  N   MET B  63     -22.188  18.890  39.502  1.00 54.37           N  
ANISOU 4038  N   MET B  63     6153   7868   6636    575  -1023    123       N  
ATOM   4039  CA  MET B  63     -21.505  17.989  38.578  1.00 56.41           C  
ANISOU 4039  CA  MET B  63     6454   8176   6803    521  -1048     47       C  
ATOM   4040  C   MET B  63     -22.242  16.674  38.513  1.00 64.53           C  
ANISOU 4040  C   MET B  63     7410   9252   7856    453  -1109    -57       C  
ATOM   4041  O   MET B  63     -22.703  16.269  37.449  1.00 65.26           O  
ANISOU 4041  O   MET B  63     7476   9451   7866    441  -1192    -94       O  
ATOM   4042  CB  MET B  63     -20.024  18.364  38.429  1.00 58.45           C  
ANISOU 4042  CB  MET B  63     6819   8376   7014    523   -973     69       C  
ATOM   4043  CG  MET B  63     -19.074  17.974  39.547  1.00 61.19           C  
ANISOU 4043  CG  MET B  63     7203   8605   7440    478   -888     29       C  
ATOM   4044  SD  MET B  63     -17.485  18.769  39.211  1.00 65.47           S  
ANISOU 4044  SD  MET B  63     7852   9100   7925    496   -811     84       S  
ATOM   4045  N   GLY B  64     -22.360  16.008  39.658  1.00 63.09           N  
ANISOU 4045  N   GLY B  64     7195   8990   7785    406  -1068   -104       N  
ATOM   4046  CA  GLY B  64     -23.189  14.802  39.773  1.00 64.33           C  
ANISOU 4046  CA  GLY B  64     7271   9175   7996    338  -1116   -193       C  
ATOM   4047  C   GLY B  64     -24.480  14.606  39.004  1.00 71.83           C  
ANISOU 4047  C   GLY B  64     8126  10243   8922    335  -1225   -210       C  
ATOM   4048  O   GLY B  64     -24.546  13.748  38.124  1.00 72.49           O  
ANISOU 4048  O   GLY B  64     8205  10393   8947    283  -1288   -296       O  
ATOM   4049  N   TYR B  65     -25.510  15.377  39.352  1.00 70.12           N  
ANISOU 4049  N   TYR B  65     7831  10055   8756    390  -1246   -134       N  
ATOM   4050  CA  TYR B  65     -26.796  15.354  38.651  1.00 71.85           C  
ANISOU 4050  CA  TYR B  65     7944  10398   8957    399  -1354   -133       C  
ATOM   4051  C   TYR B  65     -26.808  15.856  37.206  1.00 77.20           C  
ANISOU 4051  C   TYR B  65     8646  11199   9489    445  -1439   -103       C  
ATOM   4052  O   TYR B  65     -27.091  15.093  36.269  1.00 78.13           O  
ANISOU 4052  O   TYR B  65     8738  11412   9535    396  -1527   -183       O  
ATOM   4053  CB  TYR B  65     -27.677  15.493  39.898  1.00 73.18           C  
ANISOU 4053  CB  TYR B  65     8022  10516   9268    410  -1315    -98       C  
ATOM   4054  CG  TYR B  65     -27.624  14.293  40.832  1.00 74.97           C  
ANISOU 4054  CG  TYR B  65     8226  10661   9597    319  -1267   -182       C  
ATOM   4055  CD1 TYR B  65     -28.002  13.017  40.383  1.00 77.46           C  
ANISOU 4055  CD1 TYR B  65     8491  11016   9924    226  -1328   -289       C  
ATOM   4056  CD2 TYR B  65     -27.204  14.431  42.167  1.00 74.95           C  
ANISOU 4056  CD2 TYR B  65     8255  10541   9681    325  -1159   -155       C  
ATOM   4057  CE1 TYR B  65     -27.958  11.917  41.226  1.00 77.60           C  
ANISOU 4057  CE1 TYR B  65     8491  10950  10043    144  -1278   -356       C  
ATOM   4058  CE2 TYR B  65     -27.163  13.327  43.025  1.00 75.59           C  
ANISOU 4058  CE2 TYR B  65     8317  10551   9852    247  -1112   -219       C  
ATOM   4059  CZ  TYR B  65     -27.543  12.076  42.542  1.00 84.07           C  
ANISOU 4059  CZ  TYR B  65     9341  11658  10944    158  -1170   -315       C  
ATOM   4060  OH  TYR B  65     -27.511  10.983  43.381  1.00 85.41           O  
ANISOU 4060  OH  TYR B  65     9493  11748  11210     83  -1119   -369       O  
ATOM   4061  N   GLN B  66     -26.601  17.150  37.116  1.00 73.33           N  
ANISOU 4061  N   GLN B  66     8196  10704   8963    539  -1412     15       N  
ATOM   4062  CA  GLN B  66     -26.635  17.871  35.880  1.00 73.92           C  
ANISOU 4062  CA  GLN B  66     8294  10886   8905    603  -1477     80       C  
ATOM   4063  C   GLN B  66     -25.564  17.815  34.788  1.00 77.18           C  
ANISOU 4063  C   GLN B  66     8817  11339   9169    598  -1479     63       C  
ATOM   4064  O   GLN B  66     -25.867  17.564  33.639  1.00 77.98           O  
ANISOU 4064  O   GLN B  66     8906  11568   9153    596  -1571     38       O  
ATOM   4065  CB  GLN B  66     -26.923  19.308  36.266  1.00 75.19           C  
ANISOU 4065  CB  GLN B  66     8449  11014   9105    710  -1440    222       C  
ATOM   4066  CG  GLN B  66     -26.139  20.324  35.554  1.00 86.01           C  
ANISOU 4066  CG  GLN B  66     9918  12387  10374    780  -1414    317       C  
ATOM   4067  CD  GLN B  66     -26.839  21.625  35.599  1.00 98.29           C  
ANISOU 4067  CD  GLN B  66    11436  13953  11958    890  -1420    453       C  
ATOM   4068  OE1 GLN B  66     -26.312  22.606  36.097  1.00 91.03           O  
ANISOU 4068  OE1 GLN B  66    10578  12930  11078    943  -1334    534       O  
ATOM   4069  NE2 GLN B  66     -28.059  21.638  35.105  1.00 89.25           N  
ANISOU 4069  NE2 GLN B  66    10184  12928  10799    924  -1523    478       N  
ATOM   4070  N   LYS B  67     -24.314  17.984  35.144  1.00 72.09           N  
ANISOU 4070  N   LYS B  67     8275  10590   8525    591  -1378     70       N  
ATOM   4071  CA  LYS B  67     -23.280  18.139  34.140  1.00 71.87           C  
ANISOU 4071  CA  LYS B  67     8350  10598   8361    602  -1364     79       C  
ATOM   4072  C   LYS B  67     -22.514  16.886  33.808  1.00 75.25           C  
ANISOU 4072  C   LYS B  67     8825  11023   8743    517  -1354    -54       C  
ATOM   4073  O   LYS B  67     -21.842  16.337  34.641  1.00 73.53           O  
ANISOU 4073  O   LYS B  67     8635  10696   8607    467  -1279   -108       O  
ATOM   4074  CB  LYS B  67     -22.336  19.276  34.550  1.00 73.25           C  
ANISOU 4074  CB  LYS B  67     8607  10671   8553    657  -1261    186       C  
ATOM   4075  CG  LYS B  67     -20.947  19.206  33.997  1.00 84.81           C  
ANISOU 4075  CG  LYS B  67    10180  12116   9929    640  -1201    174       C  
ATOM   4076  CD  LYS B  67     -19.873  19.398  35.051  1.00 92.30           C  
ANISOU 4076  CD  LYS B  67    11183  12915  10970    619  -1085    179       C  
ATOM   4077  CE  LYS B  67     -19.164  20.742  34.916  1.00103.28           C  
ANISOU 4077  CE  LYS B  67    12643  14260  12339    682  -1020    305       C  
ATOM   4078  NZ  LYS B  67     -17.689  20.753  35.106  1.00111.55           N  
ANISOU 4078  NZ  LYS B  67    13773  15224  13386    651   -924    296       N  
ATOM   4079  N   LYS B  68     -22.690  16.405  32.580  1.00 72.79           N  
ANISOU 4079  N   LYS B  68     8518  10839   8299    502  -1436   -109       N  
ATOM   4080  CA  LYS B  68     -22.024  15.201  32.056  1.00 72.38           C  
ANISOU 4080  CA  LYS B  68     8515  10799   8185    428  -1434   -246       C  
ATOM   4081  C   LYS B  68     -20.534  15.085  31.699  1.00 74.66           C  
ANISOU 4081  C   LYS B  68     8920  11046   8402    422  -1346   -264       C  
ATOM   4082  O   LYS B  68     -19.889  14.086  32.042  1.00 73.68           O  
ANISOU 4082  O   LYS B  68     8823  10849   8323    358  -1297   -368       O  
ATOM   4083  CB  LYS B  68     -22.820  14.639  30.878  1.00 76.51           C  
ANISOU 4083  CB  LYS B  68     8999  11481   8591    407  -1561   -320       C  
ATOM   4084  N   LEU B  69     -19.957  16.047  31.003  1.00 70.41           N  
ANISOU 4084  N   LEU B  69     8448  10550   7756    488  -1319   -163       N  
ATOM   4085  CA  LEU B  69     -18.620  15.734  30.547  1.00 69.41           C  
ANISOU 4085  CA  LEU B  69     8417  10401   7554    471  -1242   -201       C  
ATOM   4086  C   LEU B  69     -17.601  16.104  31.543  1.00 69.86           C  
ANISOU 4086  C   LEU B  69     8514  10314   7717    471  -1124   -154       C  
ATOM   4087  O   LEU B  69     -17.361  17.275  31.789  1.00 69.57           O  
ANISOU 4087  O   LEU B  69     8497  10239   7698    526  -1080    -28       O  
ATOM   4088  CB  LEU B  69     -18.304  16.308  29.178  1.00 70.76           C  
ANISOU 4088  CB  LEU B  69     8650  10696   7540    525  -1260   -141       C  
ATOM   4089  CG  LEU B  69     -17.560  15.262  28.350  1.00 75.99           C  
ANISOU 4089  CG  LEU B  69     9374  11406   8093    480  -1246   -269       C  
ATOM   4090  CD1 LEU B  69     -17.618  13.935  29.012  1.00 75.54           C  
ANISOU 4090  CD1 LEU B  69     9285  11274   8143    397  -1246   -420       C  
ATOM   4091  CD2 LEU B  69     -18.064  15.170  26.941  1.00 79.89           C  
ANISOU 4091  CD2 LEU B  69     9879  12077   8398    502  -1342   -293       C  
ATOM   4092  N   ARG B  70     -16.982  15.072  32.096  1.00 63.15           N  
ANISOU 4092  N   ARG B  70     7676   9382   6936    408  -1074   -259       N  
ATOM   4093  CA  ARG B  70     -16.110  15.269  33.208  1.00 60.30           C  
ANISOU 4093  CA  ARG B  70     7336   8884   6690    399   -975   -229       C  
ATOM   4094  C   ARG B  70     -14.630  15.093  33.038  1.00 59.57           C  
ANISOU 4094  C   ARG B  70     7319   8747   6567    389   -881   -243       C  
ATOM   4095  O   ARG B  70     -14.167  14.138  32.469  1.00 59.39           O  
ANISOU 4095  O   ARG B  70     7324   8751   6489    357   -874   -342       O  
ATOM   4096  CB  ARG B  70     -16.630  14.464  34.374  1.00 60.61           C  
ANISOU 4096  CB  ARG B  70     7314   8842   6874    347   -981   -298       C  
ATOM   4097  CG  ARG B  70     -17.568  15.248  35.228  1.00 71.54           C  
ANISOU 4097  CG  ARG B  70     8635  10196   8349    377  -1002   -217       C  
ATOM   4098  CD  ARG B  70     -17.661  14.621  36.576  1.00 80.76           C  
ANISOU 4098  CD  ARG B  70     9765  11258   9663    332   -967   -262       C  
ATOM   4099  NE  ARG B  70     -18.952  13.996  36.753  1.00 88.12           N  
ANISOU 4099  NE  ARG B  70    10611  12225  10645    302  -1041   -314       N  
ATOM   4100  CZ  ARG B  70     -19.136  12.746  37.120  1.00102.25           C  
ANISOU 4100  CZ  ARG B  70    12371  13980  12501    234  -1047   -417       C  
ATOM   4101  NH1 ARG B  70     -18.116  11.946  37.353  1.00 87.56           N  
ANISOU 4101  NH1 ARG B  70    10560  12048  10661    195   -985   -480       N  
ATOM   4102  NH2 ARG B  70     -20.362  12.298  37.254  1.00 92.51           N  
ANISOU 4102  NH2 ARG B  70    11051  12782  11318    205  -1114   -453       N  
ATOM   4103  N   SER B  71     -13.949  16.111  33.544  1.00 52.06           N  
ANISOU 4103  N   SER B  71     6395   7728   5659    421   -810   -139       N  
ATOM   4104  CA  SER B  71     -12.514  16.289  33.665  1.00 49.54           C  
ANISOU 4104  CA  SER B  71     6131   7346   5345    417   -710   -116       C  
ATOM   4105  C   SER B  71     -11.998  15.433  34.773  1.00 49.52           C  
ANISOU 4105  C   SER B  71     6113   7240   5464    367   -665   -190       C  
ATOM   4106  O   SER B  71     -12.681  15.208  35.717  1.00 47.77           O  
ANISOU 4106  O   SER B  71     5842   6967   5341    349   -690   -208       O  
ATOM   4107  CB  SER B  71     -12.266  17.723  34.005  1.00 51.23           C  
ANISOU 4107  CB  SER B  71     6361   7514   5590    460   -668     19       C  
ATOM   4108  OG  SER B  71     -10.952  17.944  34.242  1.00 56.20           O  
ANISOU 4108  OG  SER B  71     7030   8079   6244    448   -577     43       O  
ATOM   4109  N   MET B  72     -10.792  14.936  34.640  1.00 44.50           N  
ANISOU 4109  N   MET B  72     5515   6576   4817    349   -595   -229       N  
ATOM   4110  CA  MET B  72     -10.275  14.008  35.607  1.00 42.79           C  
ANISOU 4110  CA  MET B  72     5282   6268   4708    307   -556   -299       C  
ATOM   4111  C   MET B  72     -10.123  14.573  36.987  1.00 42.60           C  
ANISOU 4111  C   MET B  72     5234   6145   4807    304   -524   -240       C  
ATOM   4112  O   MET B  72     -10.545  13.980  37.934  1.00 40.97           O  
ANISOU 4112  O   MET B  72     4990   5883   4693    278   -538   -281       O  
ATOM   4113  CB  MET B  72      -8.982  13.400  35.107  1.00 45.37           C  
ANISOU 4113  CB  MET B  72     5651   6592   4995    299   -485   -346       C  
ATOM   4114  CG  MET B  72      -8.943  11.957  35.265  1.00 49.11           C  
ANISOU 4114  CG  MET B  72     6114   7036   5508    261   -487   -467       C  
ATOM   4115  SD  MET B  72      -9.430  11.083  33.857  1.00 54.68           S  
ANISOU 4115  SD  MET B  72     6845   7845   6087    254   -537   -576       S  
ATOM   4116  CE  MET B  72     -10.442   9.865  34.522  1.00 51.17           C  
ANISOU 4116  CE  MET B  72     6349   7351   5743    201   -597   -682       C  
ATOM   4117  N   THR B  73      -9.575  15.760  37.076  1.00 37.33           N  
ANISOU 4117  N   THR B  73     4589   5457   4137    331   -483   -142       N  
ATOM   4118  CA  THR B  73      -9.479  16.428  38.353  1.00 35.35           C  
ANISOU 4118  CA  THR B  73     4321   5118   3994    329   -458    -90       C  
ATOM   4119  C   THR B  73     -10.883  16.621  38.916  1.00 37.32           C  
ANISOU 4119  C   THR B  73     4527   5366   4289    339   -521    -81       C  
ATOM   4120  O   THR B  73     -11.100  16.365  40.097  1.00 36.94           O  
ANISOU 4120  O   THR B  73     4448   5251   4336    320   -516   -100       O  
ATOM   4121  CB  THR B  73      -8.692  17.756  38.238  1.00 41.69           C  
ANISOU 4121  CB  THR B  73     5158   5896   4785    352   -405     11       C  
ATOM   4122  OG1 THR B  73      -7.411  17.467  37.696  1.00 43.92           O  
ANISOU 4122  OG1 THR B  73     5469   6188   5029    339   -344     -1       O  
ATOM   4123  CG2 THR B  73      -8.487  18.415  39.585  1.00 37.50           C  
ANISOU 4123  CG2 THR B  73     4614   5270   4365    343   -378     48       C  
ATOM   4124  N   ASP B  74     -11.835  17.039  38.087  1.00 32.48           N  
ANISOU 4124  N   ASP B  74     3905   4829   3606    371   -578    -51       N  
ATOM   4125  CA  ASP B  74     -13.230  17.151  38.555  1.00 31.48           C  
ANISOU 4125  CA  ASP B  74     3724   4712   3526    383   -640    -46       C  
ATOM   4126  C   ASP B  74     -13.815  15.857  39.080  1.00 33.57           C  
ANISOU 4126  C   ASP B  74     3941   4967   3848    338   -671   -143       C  
ATOM   4127  O   ASP B  74     -14.593  15.887  40.029  1.00 33.34           O  
ANISOU 4127  O   ASP B  74     3865   4900   3903    336   -685   -137       O  
ATOM   4128  CB  ASP B  74     -14.155  17.672  37.473  1.00 34.09           C  
ANISOU 4128  CB  ASP B  74     4044   5142   3766    426   -707     -2       C  
ATOM   4129  CG  ASP B  74     -13.822  19.055  37.070  1.00 42.87           C  
ANISOU 4129  CG  ASP B  74     5197   6254   4838    479   -678    113       C  
ATOM   4130  OD1 ASP B  74     -13.918  19.336  35.878  1.00 45.95           O  
ANISOU 4130  OD1 ASP B  74     5609   6732   5117    509   -706    149       O  
ATOM   4131  OD2 ASP B  74     -13.442  19.864  37.928  1.00 45.64           O  
ANISOU 4131  OD2 ASP B  74     5559   6515   5266    488   -626    169       O  
ATOM   4132  N   LYS B  75     -13.453  14.735  38.471  1.00 28.42           N  
ANISOU 4132  N   LYS B  75     3300   4343   3154    303   -677   -230       N  
ATOM   4133  CA  LYS B  75     -13.895  13.422  38.951  1.00 27.11           C  
ANISOU 4133  CA  LYS B  75     3096   4152   3054    254   -697   -326       C  
ATOM   4134  C   LYS B  75     -13.457  13.186  40.383  1.00 27.27           C  
ANISOU 4134  C   LYS B  75     3105   4067   3189    234   -641   -321       C  
ATOM   4135  O   LYS B  75     -14.227  12.697  41.196  1.00 25.76           O  
ANISOU 4135  O   LYS B  75     2865   3844   3078    213   -658   -344       O  
ATOM   4136  CB  LYS B  75     -13.361  12.300  38.053  1.00 30.16           C  
ANISOU 4136  CB  LYS B  75     3511   4569   3380    223   -696   -423       C  
ATOM   4137  CG  LYS B  75     -14.066  12.202  36.698  1.00 46.78           C  
ANISOU 4137  CG  LYS B  75     5615   6789   5369    229   -771   -459       C  
ATOM   4138  CD  LYS B  75     -13.164  11.554  35.618  1.00 55.34           C  
ANISOU 4138  CD  LYS B  75     6759   7914   6355    220   -746   -530       C  
ATOM   4139  CE  LYS B  75     -13.986  10.845  34.523  1.00 56.81           C  
ANISOU 4139  CE  LYS B  75     6934   8199   6453    199   -829   -624       C  
ATOM   4140  NZ  LYS B  75     -14.449   9.506  34.997  1.00 61.66           N  
ANISOU 4140  NZ  LYS B  75     7511   8759   7160    136   -849   -738       N  
ATOM   4141  N   TYR B  76     -12.214  13.550  40.681  1.00 23.07           N  
ANISOU 4141  N   TYR B  76     2616   3487   2663    242   -575   -289       N  
ATOM   4142  CA  TYR B  76     -11.643  13.360  42.013  1.00 21.72           C  
ANISOU 4142  CA  TYR B  76     2438   3227   2586    227   -525   -283       C  
ATOM   4143  C   TYR B  76     -12.217  14.360  42.984  1.00 25.33           C  
ANISOU 4143  C   TYR B  76     2876   3653   3097    249   -526   -215       C  
ATOM   4144  O   TYR B  76     -12.492  14.038  44.124  1.00 24.78           O  
ANISOU 4144  O   TYR B  76     2779   3533   3104    235   -514   -222       O  
ATOM   4145  CB  TYR B  76     -10.131  13.492  41.984  1.00 22.65           C  
ANISOU 4145  CB  TYR B  76     2600   3315   2692    228   -461   -269       C  
ATOM   4146  CG  TYR B  76      -9.449  12.325  41.334  1.00 25.15           C  
ANISOU 4146  CG  TYR B  76     2933   3641   2983    207   -442   -345       C  
ATOM   4147  CD1 TYR B  76      -9.550  11.051  41.880  1.00 27.04           C  
ANISOU 4147  CD1 TYR B  76     3150   3836   3289    177   -439   -413       C  
ATOM   4148  CD2 TYR B  76      -8.713  12.476  40.174  1.00 26.22           C  
ANISOU 4148  CD2 TYR B  76     3106   3826   3029    221   -421   -348       C  
ATOM   4149  CE1 TYR B  76      -8.930   9.975  41.296  1.00 27.94           C  
ANISOU 4149  CE1 TYR B  76     3281   3946   3387    163   -417   -486       C  
ATOM   4150  CE2 TYR B  76      -8.097  11.390  39.580  1.00 27.27           C  
ANISOU 4150  CE2 TYR B  76     3257   3966   3138    208   -397   -425       C  
ATOM   4151  CZ  TYR B  76      -8.202  10.148  40.156  1.00 33.06           C  
ANISOU 4151  CZ  TYR B  76     3970   4646   3946    180   -395   -496       C  
ATOM   4152  OH  TYR B  76      -7.591   9.059  39.584  1.00 33.88           O  
ANISOU 4152  OH  TYR B  76     4093   4745   4037    171   -365   -577       O  
ATOM   4153  N   ARG B  77     -12.425  15.582  42.528  1.00 22.13           N  
ANISOU 4153  N   ARG B  77     2486   3276   2647    288   -536   -147       N  
ATOM   4154  CA  ARG B  77     -13.025  16.574  43.385  1.00 21.35           C  
ANISOU 4154  CA  ARG B  77     2370   3142   2598    316   -533    -87       C  
ATOM   4155  C   ARG B  77     -14.487  16.257  43.732  1.00 25.59           C  
ANISOU 4155  C   ARG B  77     2846   3702   3176    319   -581   -102       C  
ATOM   4156  O   ARG B  77     -15.003  16.779  44.721  1.00 25.10           O  
ANISOU 4156  O   ARG B  77     2763   3602   3174    337   -568    -71       O  
ATOM   4157  CB  ARG B  77     -12.821  17.962  42.788  1.00 20.22           C  
ANISOU 4157  CB  ARG B  77     2263   3011   2409    358   -525     -6       C  
ATOM   4158  CG  ARG B  77     -11.343  18.355  42.870  1.00 24.99           C  
ANISOU 4158  CG  ARG B  77     2916   3569   3009    346   -463     14       C  
ATOM   4159  CD  ARG B  77     -11.054  19.610  42.075  1.00 29.22           C  
ANISOU 4159  CD  ARG B  77     3491   4117   3495    380   -449     95       C  
ATOM   4160  NE  ARG B  77     -11.591  20.793  42.744  1.00 31.05           N  
ANISOU 4160  NE  ARG B  77     3722   4297   3778    413   -443    156       N  
ATOM   4161  CZ  ARG B  77     -11.679  21.999  42.195  1.00 41.13           C  
ANISOU 4161  CZ  ARG B  77     5025   5570   5031    454   -435    238       C  
ATOM   4162  NH1 ARG B  77     -11.255  22.192  40.958  1.00 30.41           N  
ANISOU 4162  NH1 ARG B  77     3697   4265   3591    466   -432    276       N  
ATOM   4163  NH2 ARG B  77     -12.207  23.014  42.880  1.00 25.97           N  
ANISOU 4163  NH2 ARG B  77     3106   3593   3171    487   -425    284       N  
ATOM   4164  N   LEU B  78     -15.131  15.380  42.956  1.00 22.57           N  
ANISOU 4164  N   LEU B  78     2433   3382   2763    299   -633   -155       N  
ATOM   4165  CA  LEU B  78     -16.465  14.891  43.292  1.00 22.85           C  
ANISOU 4165  CA  LEU B  78     2397   3438   2848    289   -677   -180       C  
ATOM   4166  C   LEU B  78     -16.363  13.970  44.500  1.00 28.11           C  
ANISOU 4166  C   LEU B  78     3043   4035   3604    248   -639   -220       C  
ATOM   4167  O   LEU B  78     -17.139  14.090  45.470  1.00 27.74           O  
ANISOU 4167  O   LEU B  78     2952   3963   3624    254   -632   -199       O  
ATOM   4168  CB  LEU B  78     -17.106  14.153  42.111  1.00 23.39           C  
ANISOU 4168  CB  LEU B  78     2437   3591   2860    268   -747   -236       C  
ATOM   4169  CG  LEU B  78     -18.550  13.653  42.301  1.00 28.12           C  
ANISOU 4169  CG  LEU B  78     2949   4224   3511    249   -803   -263       C  
ATOM   4170  CD1 LEU B  78     -19.455  14.732  42.913  1.00 28.21           C  
ANISOU 4170  CD1 LEU B  78     2917   4238   3565    301   -806   -183       C  
ATOM   4171  CD2 LEU B  78     -19.138  13.187  40.970  1.00 30.76           C  
ANISOU 4171  CD2 LEU B  78     3259   4658   3770    233   -885   -314       C  
ATOM   4172  N   HIS B  79     -15.400  13.049  44.419  1.00 25.43           N  
ANISOU 4172  N   HIS B  79     2736   3666   3261    212   -612   -272       N  
ATOM   4173  CA  HIS B  79     -15.049  12.169  45.524  1.00 25.19           C  
ANISOU 4173  CA  HIS B  79     2698   3565   3308    180   -569   -299       C  
ATOM   4174  C   HIS B  79     -14.723  12.987  46.805  1.00 28.15           C  
ANISOU 4174  C   HIS B  79     3086   3886   3723    205   -522   -238       C  
ATOM   4175  O   HIS B  79     -15.222  12.695  47.893  1.00 27.69           O  
ANISOU 4175  O   HIS B  79     2995   3794   3730    196   -504   -232       O  
ATOM   4176  CB  HIS B  79     -13.858  11.270  45.120  1.00 26.06           C  
ANISOU 4176  CB  HIS B  79     2850   3651   3400    154   -542   -351       C  
ATOM   4177  CG  HIS B  79     -14.212  10.139  44.182  1.00 30.48           C  
ANISOU 4177  CG  HIS B  79     3396   4240   3944    118   -578   -433       C  
ATOM   4178  ND1 HIS B  79     -14.265   8.820  44.589  1.00 32.50           N  
ANISOU 4178  ND1 HIS B  79     3634   4444   4269     75   -564   -492       N  
ATOM   4179  CD2 HIS B  79     -14.500  10.125  42.855  1.00 33.17           C  
ANISOU 4179  CD2 HIS B  79     3744   4654   4205    117   -626   -470       C  
ATOM   4180  CE1 HIS B  79     -14.575   8.048  43.561  1.00 32.55           C  
ANISOU 4180  CE1 HIS B  79     3637   4484   4246     46   -602   -570       C  
ATOM   4181  NE2 HIS B  79     -14.725   8.813  42.495  1.00 33.34           N  
ANISOU 4181  NE2 HIS B  79     3752   4666   4249     70   -643   -561       N  
ATOM   4182  N   LEU B  80     -13.901  14.021  46.672  1.00 23.70           N  
ANISOU 4182  N   LEU B  80     2569   3316   3120    233   -500   -196       N  
ATOM   4183  CA  LEU B  80     -13.486  14.824  47.824  1.00 22.04           C  
ANISOU 4183  CA  LEU B  80     2377   3054   2942    250   -459   -152       C  
ATOM   4184  C   LEU B  80     -14.725  15.396  48.482  1.00 26.67           C  
ANISOU 4184  C   LEU B  80     2926   3644   3566    277   -468   -123       C  
ATOM   4185  O   LEU B  80     -14.942  15.208  49.665  1.00 26.88           O  
ANISOU 4185  O   LEU B  80     2936   3635   3641    273   -441   -121       O  
ATOM   4186  CB  LEU B  80     -12.520  15.941  47.411  1.00 21.51           C  
ANISOU 4186  CB  LEU B  80     2361   2980   2831    271   -439   -112       C  
ATOM   4187  CG  LEU B  80     -11.789  16.723  48.516  1.00 25.38           C  
ANISOU 4187  CG  LEU B  80     2879   3414   3352    276   -397    -84       C  
ATOM   4188  CD1 LEU B  80     -10.942  15.844  49.442  1.00 24.68           C  
ANISOU 4188  CD1 LEU B  80     2791   3290   3296    245   -370   -113       C  
ATOM   4189  CD2 LEU B  80     -10.920  17.786  47.904  1.00 27.04           C  
ANISOU 4189  CD2 LEU B  80     3132   3616   3525    287   -381    -46       C  
ATOM   4190  N   SER B  81     -15.563  16.053  47.696  1.00 23.49           N  
ANISOU 4190  N   SER B  81     2504   3286   3135    308   -505    -97       N  
ATOM   4191  CA  SER B  81     -16.799  16.656  48.212  1.00 23.02           C  
ANISOU 4191  CA  SER B  81     2399   3234   3112    343   -513    -64       C  
ATOM   4192  C   SER B  81     -17.798  15.679  48.820  1.00 26.27           C  
ANISOU 4192  C   SER B  81     2744   3654   3582    318   -521    -94       C  
ATOM   4193  O   SER B  81     -18.543  16.052  49.710  1.00 25.16           O  
ANISOU 4193  O   SER B  81     2573   3501   3488    342   -499    -70       O  
ATOM   4194  CB  SER B  81     -17.474  17.499  47.125  1.00 26.39           C  
ANISOU 4194  CB  SER B  81     2814   3716   3496    387   -558    -24       C  
ATOM   4195  OG  SER B  81     -16.858  18.765  47.034  1.00 30.29           O  
ANISOU 4195  OG  SER B  81     3363   4178   3966    425   -532     29       O  
ATOM   4196  N   VAL B  82     -17.817  14.437  48.354  1.00 24.06           N  
ANISOU 4196  N   VAL B  82     2443   3394   3306    270   -545   -147       N  
ATOM   4197  CA  VAL B  82     -18.605  13.397  49.023  1.00 24.25           C  
ANISOU 4197  CA  VAL B  82     2406   3408   3399    235   -540   -174       C  
ATOM   4198  C   VAL B  82     -18.029  13.057  50.394  1.00 28.17           C  
ANISOU 4198  C   VAL B  82     2926   3840   3939    223   -477   -167       C  
ATOM   4199  O   VAL B  82     -18.766  12.933  51.374  1.00 27.93           O  
ANISOU 4199  O   VAL B  82     2855   3797   3961    226   -450   -150       O  
ATOM   4200  CB  VAL B  82     -18.717  12.117  48.178  1.00 28.65           C  
ANISOU 4200  CB  VAL B  82     2941   3988   3957    180   -579   -241       C  
ATOM   4201  CG1 VAL B  82     -19.170  10.913  49.071  1.00 28.59           C  
ANISOU 4201  CG1 VAL B  82     2888   3939   4036    133   -553   -266       C  
ATOM   4202  CG2 VAL B  82     -19.699  12.338  47.016  1.00 29.13           C  
ANISOU 4202  CG2 VAL B  82     2954   4130   3984    187   -653   -250       C  
ATOM   4203  N   ALA B  83     -16.708  12.933  50.463  1.00 25.41           N  
ANISOU 4203  N   ALA B  83     2637   3456   3563    214   -453   -177       N  
ATOM   4204  CA  ALA B  83     -16.020  12.691  51.735  1.00 25.30           C  
ANISOU 4204  CA  ALA B  83     2648   3390   3576    209   -400   -165       C  
ATOM   4205  C   ALA B  83     -16.229  13.853  52.700  1.00 30.15           C  
ANISOU 4205  C   ALA B  83     3274   3992   4190    250   -371   -122       C  
ATOM   4206  O   ALA B  83     -16.406  13.644  53.903  1.00 30.88           O  
ANISOU 4206  O   ALA B  83     3357   4062   4312    251   -334   -109       O  
ATOM   4207  CB  ALA B  83     -14.526  12.430  51.525  1.00 25.58           C  
ANISOU 4207  CB  ALA B  83     2738   3400   3582    196   -386   -180       C  
ATOM   4208  N   ASP B  84     -16.242  15.070  52.188  1.00 25.57           N  
ANISOU 4208  N   ASP B  84     2715   3425   3574    286   -385    -99       N  
ATOM   4209  CA  ASP B  84     -16.431  16.218  53.057  1.00 25.14           C  
ANISOU 4209  CA  ASP B  84     2679   3350   3525    327   -355    -68       C  
ATOM   4210  C   ASP B  84     -17.883  16.493  53.495  1.00 28.99           C  
ANISOU 4210  C   ASP B  84     3109   3856   4049    358   -348    -48       C  
ATOM   4211  O   ASP B  84     -18.107  16.970  54.581  1.00 27.99           O  
ANISOU 4211  O   ASP B  84     2989   3707   3938    383   -307    -35       O  
ATOM   4212  CB  ASP B  84     -15.795  17.458  52.415  1.00 26.86           C  
ANISOU 4212  CB  ASP B  84     2947   3557   3703    353   -362    -47       C  
ATOM   4213  CG  ASP B  84     -14.279  17.349  52.358  1.00 36.16           C  
ANISOU 4213  CG  ASP B  84     4176   4708   4853    324   -350    -60       C  
ATOM   4214  OD1 ASP B  84     -13.660  16.903  53.350  1.00 34.81           O  
ANISOU 4214  OD1 ASP B  84     4018   4513   4694    304   -324    -74       O  
ATOM   4215  OD2 ASP B  84     -13.711  17.693  51.312  1.00 44.05           O  
ANISOU 4215  OD2 ASP B  84     5200   5718   5817    323   -367    -53       O  
ATOM   4216  N   LEU B  85     -18.865  16.218  52.657  1.00 26.87           N  
ANISOU 4216  N   LEU B  85     2782   3633   3794    360   -389    -48       N  
ATOM   4217  CA  LEU B  85     -20.246  16.399  53.072  1.00 27.58           C  
ANISOU 4217  CA  LEU B  85     2804   3747   3929    388   -382    -27       C  
ATOM   4218  C   LEU B  85     -20.603  15.357  54.135  1.00 32.69           C  
ANISOU 4218  C   LEU B  85     3414   4382   4625    355   -343    -39       C  
ATOM   4219  O   LEU B  85     -21.319  15.644  55.091  1.00 32.75           O  
ANISOU 4219  O   LEU B  85     3393   4387   4664    383   -300    -18       O  
ATOM   4220  CB  LEU B  85     -21.176  16.268  51.869  1.00 28.33           C  
ANISOU 4220  CB  LEU B  85     2835   3905   4026    391   -445    -26       C  
ATOM   4221  CG  LEU B  85     -22.683  16.293  52.146  1.00 33.61           C  
ANISOU 4221  CG  LEU B  85     3409   4611   4751    414   -447     -6       C  
ATOM   4222  CD1 LEU B  85     -23.086  17.621  52.776  1.00 33.69           C  
ANISOU 4222  CD1 LEU B  85     3428   4603   4770    490   -407     39       C  
ATOM   4223  CD2 LEU B  85     -23.447  16.019  50.858  1.00 35.91           C  
ANISOU 4223  CD2 LEU B  85     3635   4974   5035    405   -526    -14       C  
ATOM   4224  N   LEU B  86     -20.098  14.141  53.968  1.00 29.93           N  
ANISOU 4224  N   LEU B  86     3066   4023   4283    299   -352    -70       N  
ATOM   4225  CA  LEU B  86     -20.350  13.075  54.938  1.00 30.04           C  
ANISOU 4225  CA  LEU B  86     3050   4017   4346    265   -312    -72       C  
ATOM   4226  C   LEU B  86     -19.812  13.457  56.312  1.00 31.03           C  
ANISOU 4226  C   LEU B  86     3224   4110   4457    289   -251    -49       C  
ATOM   4227  O   LEU B  86     -20.492  13.310  57.312  1.00 31.77           O  
ANISOU 4227  O   LEU B  86     3286   4204   4581    299   -204    -26       O  
ATOM   4228  CB  LEU B  86     -19.686  11.798  54.455  1.00 30.72           C  
ANISOU 4228  CB  LEU B  86     3147   4083   4442    207   -330   -108       C  
ATOM   4229  CG  LEU B  86     -19.957  10.503  55.203  1.00 36.38           C  
ANISOU 4229  CG  LEU B  86     3829   4770   5221    164   -294   -108       C  
ATOM   4230  CD1 LEU B  86     -21.383  10.022  54.935  1.00 37.51           C  
ANISOU 4230  CD1 LEU B  86     3880   4943   5431    138   -310   -113       C  
ATOM   4231  CD2 LEU B  86     -18.924   9.472  54.725  1.00 38.77           C  
ANISOU 4231  CD2 LEU B  86     4171   5038   5524    122   -305   -145       C  
ATOM   4232  N   PHE B  87     -18.593  13.969  56.363  1.00 24.78           N  
ANISOU 4232  N   PHE B  87     2506   3294   3616    298   -250    -55       N  
ATOM   4233  CA  PHE B  87     -18.004  14.341  57.634  1.00 22.98           C  
ANISOU 4233  CA  PHE B  87     2326   3043   3364    316   -203    -42       C  
ATOM   4234  C   PHE B  87     -18.751  15.517  58.231  1.00 26.63           C  
ANISOU 4234  C   PHE B  87     2786   3511   3822    369   -174    -26       C  
ATOM   4235  O   PHE B  87     -19.069  15.534  59.413  1.00 27.19           O  
ANISOU 4235  O   PHE B  87     2857   3581   3894    386   -124    -13       O  
ATOM   4236  CB  PHE B  87     -16.541  14.712  57.464  1.00 23.44           C  
ANISOU 4236  CB  PHE B  87     2454   3079   3375    309   -217    -56       C  
ATOM   4237  CG  PHE B  87     -15.986  15.489  58.621  1.00 24.05           C  
ANISOU 4237  CG  PHE B  87     2580   3138   3418    332   -184    -52       C  
ATOM   4238  CD1 PHE B  87     -15.974  14.942  59.892  1.00 26.22           C  
ANISOU 4238  CD1 PHE B  87     2858   3415   3690    330   -145    -40       C  
ATOM   4239  CD2 PHE B  87     -15.512  16.776  58.444  1.00 25.46           C  
ANISOU 4239  CD2 PHE B  87     2806   3301   3568    354   -191    -60       C  
ATOM   4240  CE1 PHE B  87     -15.471  15.648  60.963  1.00 26.85           C  
ANISOU 4240  CE1 PHE B  87     2986   3490   3727    350   -120    -45       C  
ATOM   4241  CE2 PHE B  87     -14.998  17.498  59.510  1.00 27.93           C  
ANISOU 4241  CE2 PHE B  87     3165   3596   3849    368   -164    -69       C  
ATOM   4242  CZ  PHE B  87     -14.976  16.938  60.768  1.00 25.93           C  
ANISOU 4242  CZ  PHE B  87     2915   3355   3583    366   -132    -66       C  
ATOM   4243  N   VAL B  88     -19.018  16.487  57.375  1.00 22.13           N  
ANISOU 4243  N   VAL B  88     2216   2947   3244    399   -202    -24       N  
ATOM   4244  CA  VAL B  88     -19.632  17.749  57.740  1.00 22.12           C  
ANISOU 4244  CA  VAL B  88     2221   2940   3244    458   -177     -9       C  
ATOM   4245  C   VAL B  88     -21.056  17.621  58.273  1.00 27.86           C  
ANISOU 4245  C   VAL B  88     2874   3695   4016    486   -143     10       C  
ATOM   4246  O   VAL B  88     -21.434  18.374  59.153  1.00 29.01           O  
ANISOU 4246  O   VAL B  88     3033   3830   4161    532    -94     16       O  
ATOM   4247  CB  VAL B  88     -19.569  18.689  56.536  1.00 25.95           C  
ANISOU 4247  CB  VAL B  88     2720   3424   3717    483   -219      0       C  
ATOM   4248  CG1 VAL B  88     -20.775  19.518  56.418  1.00 26.63           C  
ANISOU 4248  CG1 VAL B  88     2763   3524   3833    543   -211     27       C  
ATOM   4249  CG2 VAL B  88     -18.294  19.515  56.596  1.00 25.51           C  
ANISOU 4249  CG2 VAL B  88     2749   3322   3621    482   -214    -11       C  
ATOM   4250  N   ILE B  89     -21.844  16.673  57.774  1.00 24.52           N  
ANISOU 4250  N   ILE B  89     2374   3308   3636    457   -166     17       N  
ATOM   4251  CA  ILE B  89     -23.177  16.441  58.341  1.00 25.08           C  
ANISOU 4251  CA  ILE B  89     2363   3407   3760    476   -129     39       C  
ATOM   4252  C   ILE B  89     -23.140  15.915  59.800  1.00 28.77           C  
ANISOU 4252  C   ILE B  89     2841   3863   4227    468    -56     47       C  
ATOM   4253  O   ILE B  89     -24.145  16.008  60.524  1.00 29.03           O  
ANISOU 4253  O   ILE B  89     2823   3916   4292    498     -3     69       O  
ATOM   4254  CB  ILE B  89     -24.089  15.538  57.431  1.00 28.80           C  
ANISOU 4254  CB  ILE B  89     2737   3921   4286    437   -176     40       C  
ATOM   4255  CG1 ILE B  89     -23.544  14.141  57.246  1.00 29.08           C  
ANISOU 4255  CG1 ILE B  89     2774   3944   4333    361   -194     17       C  
ATOM   4256  CG2 ILE B  89     -24.304  16.154  56.044  1.00 30.09           C  
ANISOU 4256  CG2 ILE B  89     2883   4114   4437    458   -249     39       C  
ATOM   4257  CD1 ILE B  89     -24.459  13.285  56.358  1.00 38.74           C  
ANISOU 4257  CD1 ILE B  89     3903   5204   5612    316   -243      5       C  
ATOM   4258  N   THR B  90     -21.991  15.401  60.245  1.00 24.32           N  
ANISOU 4258  N   THR B  90     2343   3273   3625    434    -50     34       N  
ATOM   4259  CA  THR B  90     -21.851  14.933  61.621  1.00 23.95           C  
ANISOU 4259  CA  THR B  90     2316   3222   3563    431     14     49       C  
ATOM   4260  C   THR B  90     -21.351  16.009  62.586  1.00 29.23           C  
ANISOU 4260  C   THR B  90     3059   3878   4169    478     52     37       C  
ATOM   4261  O   THR B  90     -21.284  15.762  63.795  1.00 29.22           O  
ANISOU 4261  O   THR B  90     3078   3885   4138    485    106     48       O  
ATOM   4262  CB  THR B  90     -20.877  13.761  61.736  1.00 25.72           C  
ANISOU 4262  CB  THR B  90     2567   3427   3778    376      2     48       C  
ATOM   4263  OG1 THR B  90     -19.526  14.236  61.571  1.00 21.98           O  
ANISOU 4263  OG1 THR B  90     2173   2931   3246    375    -30     23       O  
ATOM   4264  CG2 THR B  90     -21.215  12.672  60.724  1.00 22.06           C  
ANISOU 4264  CG2 THR B  90     2043   2963   3376    324    -38     44       C  
ATOM   4265  N   LEU B  91     -21.011  17.196  62.080  1.00 25.54           N  
ANISOU 4265  N   LEU B  91     2635   3391   3680    508     25     14       N  
ATOM   4266  CA  LEU B  91     -20.505  18.259  62.941  1.00 24.90           C  
ANISOU 4266  CA  LEU B  91     2628   3288   3545    545     58    -10       C  
ATOM   4267  C   LEU B  91     -21.481  18.788  64.049  1.00 29.70           C  
ANISOU 4267  C   LEU B  91     3225   3911   4150    602    134     -6       C  
ATOM   4268  O   LEU B  91     -21.024  19.167  65.144  1.00 29.35           O  
ANISOU 4268  O   LEU B  91     3242   3861   4048    618    173    -29       O  
ATOM   4269  CB  LEU B  91     -19.895  19.399  62.092  1.00 24.39           C  
ANISOU 4269  CB  LEU B  91     2612   3186   3470    559     16    -32       C  
ATOM   4270  CG  LEU B  91     -18.426  19.180  61.640  1.00 27.66           C  
ANISOU 4270  CG  LEU B  91     3080   3580   3851    509    -33    -51       C  
ATOM   4271  CD1 LEU B  91     -17.951  20.203  60.642  1.00 27.42           C  
ANISOU 4271  CD1 LEU B  91     3083   3514   3821    518    -69    -59       C  
ATOM   4272  CD2 LEU B  91     -17.485  19.174  62.849  1.00 29.11           C  
ANISOU 4272  CD2 LEU B  91     3325   3758   3979    495    -11    -75       C  
ATOM   4273  N   PRO B  92     -22.812  18.812  63.793  1.00 26.54           N  
ANISOU 4273  N   PRO B  92     2743   3533   3808    634    157     21       N  
ATOM   4274  CA  PRO B  92     -23.685  19.239  64.884  1.00 26.49           C  
ANISOU 4274  CA  PRO B  92     2723   3544   3798    690    241     26       C  
ATOM   4275  C   PRO B  92     -23.497  18.408  66.156  1.00 29.42           C  
ANISOU 4275  C   PRO B  92     3111   3941   4125    670    296     37       C  
ATOM   4276  O   PRO B  92     -23.649  18.948  67.245  1.00 29.16           O  
ANISOU 4276  O   PRO B  92     3117   3917   4046    714    361     21       O  
ATOM   4277  CB  PRO B  92     -25.103  19.062  64.317  1.00 28.80           C  
ANISOU 4277  CB  PRO B  92     2902   3868   4172    713    249     63       C  
ATOM   4278  CG  PRO B  92     -24.970  19.051  62.875  1.00 33.06           C  
ANISOU 4278  CG  PRO B  92     3415   4401   4745    689    164     67       C  
ATOM   4279  CD  PRO B  92     -23.566  18.583  62.550  1.00 28.21           C  
ANISOU 4279  CD  PRO B  92     2872   3761   4084    628    111     44       C  
ATOM   4280  N   PHE B  93     -23.139  17.131  66.021  1.00 25.72           N  
ANISOU 4280  N   PHE B  93     2620   3485   3668    609    271     63       N  
ATOM   4281  CA  PHE B  93     -22.858  16.277  67.207  1.00 26.52           C  
ANISOU 4281  CA  PHE B  93     2743   3610   3725    591    321     87       C  
ATOM   4282  C   PHE B  93     -21.641  16.783  68.009  1.00 29.45           C  
ANISOU 4282  C   PHE B  93     3219   3973   3997    598    316     50       C  
ATOM   4283  O   PHE B  93     -21.688  16.927  69.237  1.00 28.85           O  
ANISOU 4283  O   PHE B  93     3179   3924   3856    626    376     49       O  
ATOM   4284  CB  PHE B  93     -22.617  14.811  66.812  1.00 28.50           C  
ANISOU 4284  CB  PHE B  93     2953   3858   4017    524    292    123       C  
ATOM   4285  CG  PHE B  93     -23.789  14.154  66.148  1.00 30.90           C  
ANISOU 4285  CG  PHE B  93     3151   4173   4419    503    296    154       C  
ATOM   4286  CD1 PHE B  93     -24.829  13.639  66.908  1.00 34.84           C  
ANISOU 4286  CD1 PHE B  93     3585   4701   4952    510    374    199       C  
ATOM   4287  CD2 PHE B  93     -23.847  14.035  64.763  1.00 33.05           C  
ANISOU 4287  CD2 PHE B  93     3384   4430   4746    472    222    136       C  
ATOM   4288  CE1 PHE B  93     -25.927  13.010  66.303  1.00 36.20           C  
ANISOU 4288  CE1 PHE B  93     3646   4883   5223    481    374    225       C  
ATOM   4289  CE2 PHE B  93     -24.941  13.417  64.135  1.00 36.41           C  
ANISOU 4289  CE2 PHE B  93     3704   4872   5259    446    215    156       C  
ATOM   4290  CZ  PHE B  93     -25.985  12.905  64.910  1.00 35.27           C  
ANISOU 4290  CZ  PHE B  93     3488   4752   5160    448    290    200       C  
ATOM   4291  N   TRP B  94     -20.563  17.048  67.274  1.00 25.33           N  
ANISOU 4291  N   TRP B  94     2743   3419   3464    569    244     18       N  
ATOM   4292  CA  TRP B  94     -19.356  17.658  67.805  1.00 24.75           C  
ANISOU 4292  CA  TRP B  94     2759   3334   3310    568    222    -25       C  
ATOM   4293  C   TRP B  94     -19.645  18.949  68.581  1.00 28.76           C  
ANISOU 4293  C   TRP B  94     3316   3838   3772    623    268    -71       C  
ATOM   4294  O   TRP B  94     -19.065  19.203  69.655  1.00 28.27           O  
ANISOU 4294  O   TRP B  94     3319   3794   3627    631    287   -100       O  
ATOM   4295  CB  TRP B  94     -18.439  18.024  66.649  1.00 22.76           C  
ANISOU 4295  CB  TRP B  94     2528   3041   3076    537    146    -51       C  
ATOM   4296  CG  TRP B  94     -17.753  16.902  65.979  1.00 22.99           C  
ANISOU 4296  CG  TRP B  94     2536   3069   3129    483     97    -26       C  
ATOM   4297  CD1 TRP B  94     -18.304  15.962  65.152  1.00 25.74           C  
ANISOU 4297  CD1 TRP B  94     2817   3419   3544    458     83      6       C  
ATOM   4298  CD2 TRP B  94     -16.345  16.635  66.014  1.00 22.21           C  
ANISOU 4298  CD2 TRP B  94     2482   2965   2991    448     53    -39       C  
ATOM   4299  NE1 TRP B  94     -17.323  15.105  64.698  1.00 24.64           N  
ANISOU 4299  NE1 TRP B  94     2686   3270   3408    413     40     12       N  
ATOM   4300  CE2 TRP B  94     -16.110  15.505  65.204  1.00 25.79           C  
ANISOU 4300  CE2 TRP B  94     2895   3412   3490    410     22    -11       C  
ATOM   4301  CE3 TRP B  94     -15.268  17.236  66.657  1.00 23.16           C  
ANISOU 4301  CE3 TRP B  94     2669   3087   3045    445     37    -74       C  
ATOM   4302  CZ2 TRP B  94     -14.828  14.965  65.015  1.00 24.44           C  
ANISOU 4302  CZ2 TRP B  94     2748   3235   3303    376    -19    -12       C  
ATOM   4303  CZ3 TRP B  94     -13.985  16.683  66.483  1.00 24.15           C  
ANISOU 4303  CZ3 TRP B  94     2809   3213   3154    406    -11    -71       C  
ATOM   4304  CH2 TRP B  94     -13.787  15.567  65.658  1.00 24.32           C  
ANISOU 4304  CH2 TRP B  94     2788   3226   3225    377    -34    -38       C  
ATOM   4305  N   ALA B  95     -20.503  19.775  67.984  1.00 25.58           N  
ANISOU 4305  N   ALA B  95     2886   3410   3424    663    282    -80       N  
ATOM   4306  CA  ALA B  95     -20.894  21.051  68.547  1.00 26.42           C  
ANISOU 4306  CA  ALA B  95     3034   3496   3507    723    330   -125       C  
ATOM   4307  C   ALA B  95     -21.668  20.877  69.844  1.00 31.07           C  
ANISOU 4307  C   ALA B  95     3618   4133   4054    764    420   -118       C  
ATOM   4308  O   ALA B  95     -21.373  21.534  70.820  1.00 31.25           O  
ANISOU 4308  O   ALA B  95     3712   4158   4002    791    454   -168       O  
ATOM   4309  CB  ALA B  95     -21.741  21.822  67.538  1.00 27.69           C  
ANISOU 4309  CB  ALA B  95     3151   3623   3748    763    326   -118       C  
ATOM   4310  N   VAL B  96     -22.655  19.986  69.851  1.00 28.36           N  
ANISOU 4310  N   VAL B  96     3189   3830   3758    767    458    -57       N  
ATOM   4311  CA  VAL B  96     -23.421  19.672  71.086  1.00 29.01           C  
ANISOU 4311  CA  VAL B  96     3256   3964   3801    803    554    -34       C  
ATOM   4312  C   VAL B  96     -22.551  19.012  72.131  1.00 31.58           C  
ANISOU 4312  C   VAL B  96     3643   4329   4029    775    560    -30       C  
ATOM   4313  O   VAL B  96     -22.609  19.355  73.318  1.00 31.66           O  
ANISOU 4313  O   VAL B  96     3705   4374   3953    812    623    -54       O  
ATOM   4314  CB  VAL B  96     -24.591  18.671  70.841  1.00 33.15           C  
ANISOU 4314  CB  VAL B  96     3666   4523   4408    796    592     41       C  
ATOM   4315  CG1 VAL B  96     -25.123  18.159  72.170  1.00 34.01           C  
ANISOU 4315  CG1 VAL B  96     3767   4688   4466    819    691     76       C  
ATOM   4316  CG2 VAL B  96     -25.704  19.317  70.022  1.00 32.98           C  
ANISOU 4316  CG2 VAL B  96     3566   4485   4478    839    601     45       C  
ATOM   4317  N   ASP B  97     -21.769  18.038  71.683  1.00 27.12           N  
ANISOU 4317  N   ASP B  97     3070   3761   3474    712    497      3       N  
ATOM   4318  CA  ASP B  97     -20.808  17.371  72.551  1.00 26.88           C  
ANISOU 4318  CA  ASP B  97     3093   3766   3356    686    487     16       C  
ATOM   4319  C   ASP B  97     -19.911  18.395  73.227  1.00 30.94           C  
ANISOU 4319  C   ASP B  97     3707   4281   3768    702    469    -61       C  
ATOM   4320  O   ASP B  97     -19.658  18.295  74.420  1.00 31.39           O  
ANISOU 4320  O   ASP B  97     3812   4390   3724    718    504    -65       O  
ATOM   4321  CB  ASP B  97     -19.961  16.402  71.754  1.00 27.85           C  
ANISOU 4321  CB  ASP B  97     3197   3867   3518    623    411     48       C  
ATOM   4322  CG  ASP B  97     -18.807  15.848  72.554  1.00 38.75           C  
ANISOU 4322  CG  ASP B  97     4633   5279   4810    602    387     60       C  
ATOM   4323  OD1 ASP B  97     -17.649  16.061  72.131  1.00 39.69           O  
ANISOU 4323  OD1 ASP B  97     4791   5377   4913    573    312     25       O  
ATOM   4324  OD2 ASP B  97     -19.059  15.246  73.623  1.00 43.72           O  
ANISOU 4324  OD2 ASP B  97     5267   5960   5385    619    445    107       O  
ATOM   4325  N   ALA B  98     -19.445  19.391  72.486  1.00 26.77           N  
ANISOU 4325  N   ALA B  98     3209   3697   3264    697    416   -123       N  
ATOM   4326  CA  ALA B  98     -18.552  20.367  73.072  1.00 27.10           C  
ANISOU 4326  CA  ALA B  98     3342   3731   3223    701    393   -204       C  
ATOM   4327  C   ALA B  98     -19.232  21.317  74.045  1.00 32.56           C  
ANISOU 4327  C   ALA B  98     4078   4434   3859    763    472   -259       C  
ATOM   4328  O   ALA B  98     -18.650  21.650  75.061  1.00 32.41           O  
ANISOU 4328  O   ALA B  98     4132   4447   3734    767    476   -311       O  
ATOM   4329  CB  ALA B  98     -17.825  21.143  71.998  1.00 27.34           C  
ANISOU 4329  CB  ALA B  98     3393   3692   3305    672    320   -248       C  
ATOM   4330  N   VAL B  99     -20.456  21.745  73.761  1.00 30.67           N  
ANISOU 4330  N   VAL B  99     3795   4174   3686    814    533   -250       N  
ATOM   4331  CA  VAL B  99     -21.076  22.793  74.581  1.00 32.38           C  
ANISOU 4331  CA  VAL B  99     4056   4386   3859    882    612   -313       C  
ATOM   4332  C   VAL B  99     -21.582  22.106  75.858  1.00 39.32           C  
ANISOU 4332  C   VAL B  99     4934   5354   4653    910    694   -280       C  
ATOM   4333  O   VAL B  99     -21.454  22.684  76.961  1.00 40.95           O  
ANISOU 4333  O   VAL B  99     5217   5589   4753    943    738   -344       O  
ATOM   4334  CB  VAL B  99     -22.079  23.666  73.781  1.00 36.26           C  
ANISOU 4334  CB  VAL B  99     4505   4816   4456    935    644   -320       C  
ATOM   4335  CG1 VAL B  99     -21.470  24.180  72.509  1.00 35.03           C  
ANISOU 4335  CG1 VAL B  99     4352   4583   4373    901    559   -333       C  
ATOM   4336  CG2 VAL B  99     -23.315  22.884  73.456  1.00 36.31           C  
ANISOU 4336  CG2 VAL B  99     4400   4857   4538    957    692   -233       C  
ATOM   4337  N   ALA B 100     -22.370  21.020  75.690  1.00 35.02           N  
ANISOU 4337  N   ALA B 100     4298   4845   4161    906    730   -184       N  
ATOM   4338  CA  ALA B 100     -23.004  20.364  76.846  1.00 35.05           C  
ANISOU 4338  CA  ALA B 100     4290   4930   4098    937    824   -136       C  
ATOM   4339  C   ALA B 100     -22.694  18.922  77.170  1.00 36.66           C  
ANISOU 4339  C   ALA B 100     4466   5187   4276    891    817    -45       C  
ATOM   4340  O   ALA B 100     -22.183  18.604  78.245  1.00 36.54           O  
ANISOU 4340  O   ALA B 100     4510   5234   4141    894    834    -40       O  
ATOM   4341  CB  ALA B 100     -24.503  20.475  76.452  1.00 36.32           C  
ANISOU 4341  CB  ALA B 100     4355   5081   4364    984    903    -98       C  
ATOM   4342  N   ASN B 101     -23.030  18.037  76.242  1.00 31.95           N  
ANISOU 4342  N   ASN B 101     3780   4567   3793    852    791     27       N  
ATOM   4343  CA  ASN B 101     -23.110  16.625  76.574  1.00 31.33           C  
ANISOU 4343  CA  ASN B 101     3658   4529   3718    820    815    125       C  
ATOM   4344  C   ASN B 101     -23.154  15.736  75.366  1.00 33.89           C  
ANISOU 4344  C   ASN B 101     3901   4806   4169    761    757    177       C  
ATOM   4345  O   ASN B 101     -23.444  16.198  74.259  1.00 32.81           O  
ANISOU 4345  O   ASN B 101     3723   4620   4123    754    715    147       O  
ATOM   4346  CB  ASN B 101     -24.381  16.370  77.371  1.00 30.50           C  
ANISOU 4346  CB  ASN B 101     3502   4474   3611    865    941    179       C  
ATOM   4347  CG  ASN B 101     -24.183  15.359  78.470  1.00 43.12           C  
ANISOU 4347  CG  ASN B 101     5120   6139   5123    859    993    257       C  
ATOM   4348  OD1 ASN B 101     -23.429  14.375  78.325  1.00 30.42           O  
ANISOU 4348  OD1 ASN B 101     3514   4524   3519    808    939    311       O  
ATOM   4349  ND2 ASN B 101     -24.872  15.590  79.596  1.00 34.83           N  
ANISOU 4349  ND2 ASN B 101     4087   5153   3993    917   1104    268       N  
ATOM   4350  N   TRP B 102     -22.889  14.452  75.592  1.00 30.34           N  
ANISOU 4350  N   TRP B 102     3430   4373   3723    722    759    256       N  
ATOM   4351  CA  TRP B 102     -23.107  13.460  74.575  1.00 29.53           C  
ANISOU 4351  CA  TRP B 102     3246   4228   3745    666    724    307       C  
ATOM   4352  C   TRP B 102     -24.456  12.806  74.858  1.00 34.35           C  
ANISOU 4352  C   TRP B 102     3766   4859   4425    671    821    380       C  
ATOM   4353  O   TRP B 102     -24.525  11.776  75.539  1.00 34.26           O  
ANISOU 4353  O   TRP B 102     3742   4871   4402    655    873    461       O  
ATOM   4354  CB  TRP B 102     -21.960  12.423  74.527  1.00 27.76           C  
ANISOU 4354  CB  TRP B 102     3052   3991   3505    617    666    346       C  
ATOM   4355  CG  TRP B 102     -22.127  11.533  73.356  1.00 28.04           C  
ANISOU 4355  CG  TRP B 102     3014   3971   3670    560    624    374       C  
ATOM   4356  CD1 TRP B 102     -22.720  10.303  73.331  1.00 31.24           C  
ANISOU 4356  CD1 TRP B 102     3350   4362   4157    525    666    453       C  
ATOM   4357  CD2 TRP B 102     -21.803  11.857  72.000  1.00 26.86           C  
ANISOU 4357  CD2 TRP B 102     2849   3770   3587    531    536    319       C  
ATOM   4358  NE1 TRP B 102     -22.751   9.824  72.035  1.00 30.13           N  
ANISOU 4358  NE1 TRP B 102     3156   4165   4128    473    604    439       N  
ATOM   4359  CE2 TRP B 102     -22.200  10.763  71.200  1.00 30.60           C  
ANISOU 4359  CE2 TRP B 102     3247   4206   4172    478    524    359       C  
ATOM   4360  CE3 TRP B 102     -21.203  12.962  71.385  1.00 27.30           C  
ANISOU 4360  CE3 TRP B 102     2950   3807   3617    542    469    240       C  
ATOM   4361  CZ2 TRP B 102     -22.006  10.743  69.824  1.00 29.03           C  
ANISOU 4361  CZ2 TRP B 102     3021   3962   4047    441    445    318       C  
ATOM   4362  CZ3 TRP B 102     -21.008  12.943  70.016  1.00 27.86           C  
ANISOU 4362  CZ3 TRP B 102     2991   3831   3762    506    395    212       C  
ATOM   4363  CH2 TRP B 102     -21.415  11.848  69.248  1.00 28.42           C  
ANISOU 4363  CH2 TRP B 102     2990   3876   3931    459    383    249       C  
ATOM   4364  N   TYR B 103     -25.527  13.422  74.339  1.00 31.18           N  
ANISOU 4364  N   TYR B 103     3297   4451   4099    695    847    357       N  
ATOM   4365  CA  TYR B 103     -26.893  12.887  74.472  1.00 31.83           C  
ANISOU 4365  CA  TYR B 103     3272   4555   4268    696    935    422       C  
ATOM   4366  C   TYR B 103     -27.203  11.739  73.513  1.00 35.29           C  
ANISOU 4366  C   TYR B 103     3617   4952   4838    621    896    469       C  
ATOM   4367  O   TYR B 103     -28.266  11.134  73.631  1.00 35.94           O  
ANISOU 4367  O   TYR B 103     3604   5048   5002    606    965    528       O  
ATOM   4368  CB  TYR B 103     -27.966  13.957  74.175  1.00 33.63           C  
ANISOU 4368  CB  TYR B 103     3445   4791   4541    751    969    383       C  
ATOM   4369  CG  TYR B 103     -27.849  15.211  74.948  1.00 35.56           C  
ANISOU 4369  CG  TYR B 103     3772   5060   4681    829   1011    321       C  
ATOM   4370  CD1 TYR B 103     -27.413  16.375  74.345  1.00 36.80           C  
ANISOU 4370  CD1 TYR B 103     3979   5178   4826    855    945    237       C  
ATOM   4371  CD2 TYR B 103     -28.181  15.238  76.286  1.00 37.55           C  
ANISOU 4371  CD2 TYR B 103     4053   5370   4843    876   1121    345       C  
ATOM   4372  CE1 TYR B 103     -27.287  17.534  75.073  1.00 38.48           C  
ANISOU 4372  CE1 TYR B 103     4273   5401   4947    922    986    171       C  
ATOM   4373  CE2 TYR B 103     -28.065  16.377  77.021  1.00 39.20           C  
ANISOU 4373  CE2 TYR B 103     4343   5600   4949    946   1161    276       C  
ATOM   4374  CZ  TYR B 103     -27.622  17.528  76.415  1.00 47.24           C  
ANISOU 4374  CZ  TYR B 103     5413   6570   5966    967   1093    185       C  
ATOM   4375  OH  TYR B 103     -27.516  18.666  77.174  1.00 50.80           O  
ANISOU 4375  OH  TYR B 103     5949   7031   6321   1034   1137    108       O  
ATOM   4376  N   PHE B 104     -26.321  11.455  72.557  1.00 30.73           N  
ANISOU 4376  N   PHE B 104     3063   4326   4288    572    791    439       N  
ATOM   4377  CA  PHE B 104     -26.719  10.656  71.381  1.00 30.35           C  
ANISOU 4377  CA  PHE B 104     2926   4236   4371    506    740    451       C  
ATOM   4378  C   PHE B 104     -26.451   9.155  71.419  1.00 35.20           C  
ANISOU 4378  C   PHE B 104     3520   4818   5038    439    745    515       C  
ATOM   4379  O   PHE B 104     -26.622   8.505  70.390  1.00 35.40           O  
ANISOU 4379  O   PHE B 104     3485   4800   5164    380    693    507       O  
ATOM   4380  CB  PHE B 104     -26.084  11.239  70.118  1.00 30.76           C  
ANISOU 4380  CB  PHE B 104     3001   4252   4435    494    627    378       C  
ATOM   4381  CG  PHE B 104     -26.133  12.730  70.072  1.00 31.73           C  
ANISOU 4381  CG  PHE B 104     3162   4390   4505    559    617    318       C  
ATOM   4382  CD1 PHE B 104     -27.294  13.380  69.701  1.00 34.78           C  
ANISOU 4382  CD1 PHE B 104     3471   4793   4951    594    640    310       C  
ATOM   4383  CD2 PHE B 104     -25.011  13.492  70.435  1.00 32.57           C  
ANISOU 4383  CD2 PHE B 104     3379   4490   4504    587    588    271       C  
ATOM   4384  CE1 PHE B 104     -27.335  14.775  69.679  1.00 35.35           C  
ANISOU 4384  CE1 PHE B 104     3582   4867   4981    661    638    259       C  
ATOM   4385  CE2 PHE B 104     -25.047  14.869  70.405  1.00 34.76           C  
ANISOU 4385  CE2 PHE B 104     3697   4768   4744    643    584    213       C  
ATOM   4386  CZ  PHE B 104     -26.202  15.514  70.037  1.00 33.42           C  
ANISOU 4386  CZ  PHE B 104     3456   4606   4635    684    612    208       C  
ATOM   4387  N   GLY B 105     -26.036   8.604  72.561  1.00 31.72           N  
ANISOU 4387  N   GLY B 105     3130   4394   4530    450    806    576       N  
ATOM   4388  CA  GLY B 105     -25.910   7.158  72.716  1.00 31.88           C  
ANISOU 4388  CA  GLY B 105     3127   4377   4610    394    830    652       C  
ATOM   4389  C   GLY B 105     -24.621   6.569  72.162  1.00 36.37           C  
ANISOU 4389  C   GLY B 105     3752   4891   5174    358    744    636       C  
ATOM   4390  O   GLY B 105     -23.832   7.245  71.494  1.00 35.05           O  
ANISOU 4390  O   GLY B 105     3633   4715   4968    367    658    562       O  
ATOM   4391  N   ASN B 106     -24.420   5.285  72.440  1.00 33.49           N  
ANISOU 4391  N   ASN B 106     3381   4488   4857    320    774    711       N  
ATOM   4392  CA  ASN B 106     -23.189   4.584  72.080  1.00 32.63           C  
ANISOU 4392  CA  ASN B 106     3325   4326   4748    295    710    711       C  
ATOM   4393  C   ASN B 106     -22.972   4.437  70.579  1.00 35.92           C  
ANISOU 4393  C   ASN B 106     3713   4682   5253    245    618    635       C  
ATOM   4394  O   ASN B 106     -21.821   4.521  70.092  1.00 35.44           O  
ANISOU 4394  O   ASN B 106     3710   4599   5154    246    543    593       O  
ATOM   4395  CB  ASN B 106     -23.155   3.188  72.718  1.00 34.18           C  
ANISOU 4395  CB  ASN B 106     3513   4482   4993    269    775    818       C  
ATOM   4396  CG  ASN B 106     -21.792   2.841  73.293  1.00 57.72           C  
ANISOU 4396  CG  ASN B 106     6583   7464   7886    299    751    856       C  
ATOM   4397  OD1 ASN B 106     -21.417   3.306  74.383  1.00 54.07           O  
ANISOU 4397  OD1 ASN B 106     6179   7071   7293    355    779    889       O  
ATOM   4398  ND2 ASN B 106     -21.045   2.019  72.573  1.00 48.89           N  
ANISOU 4398  ND2 ASN B 106     5471   6269   6835    263    698    851       N  
ATOM   4399  N   PHE B 107     -24.058   4.201  69.842  1.00 31.59           N  
ANISOU 4399  N   PHE B 107     3074   4112   4818    199    622    618       N  
ATOM   4400  CA  PHE B 107     -23.919   3.784  68.451  1.00 30.09           C  
ANISOU 4400  CA  PHE B 107     2853   3864   4716    142    542    555       C  
ATOM   4401  C   PHE B 107     -23.500   4.950  67.580  1.00 33.02           C  
ANISOU 4401  C   PHE B 107     3254   4263   5030    168    455    464       C  
ATOM   4402  O   PHE B 107     -22.725   4.764  66.635  1.00 32.14           O  
ANISOU 4402  O   PHE B 107     3170   4114   4928    144    381    413       O  
ATOM   4403  CB  PHE B 107     -25.193   3.143  67.886  1.00 32.37           C  
ANISOU 4403  CB  PHE B 107     3031   4127   5143     78    561    557       C  
ATOM   4404  CG  PHE B 107     -25.117   2.909  66.408  1.00 33.35           C  
ANISOU 4404  CG  PHE B 107     3125   4209   5335     24    469    474       C  
ATOM   4405  CD1 PHE B 107     -25.631   3.838  65.524  1.00 35.78           C  
ANISOU 4405  CD1 PHE B 107     3394   4561   5639     32    408    405       C  
ATOM   4406  CD2 PHE B 107     -24.460   1.800  65.907  1.00 35.71           C  
ANISOU 4406  CD2 PHE B 107     3446   4429   5694    -27    442    465       C  
ATOM   4407  CE1 PHE B 107     -25.513   3.665  64.164  1.00 36.53           C  
ANISOU 4407  CE1 PHE B 107     3471   4630   5777    -12    320    329       C  
ATOM   4408  CE2 PHE B 107     -24.343   1.607  64.547  1.00 38.55           C  
ANISOU 4408  CE2 PHE B 107     3788   4756   6102    -73    359    379       C  
ATOM   4409  CZ  PHE B 107     -24.871   2.552  63.665  1.00 36.15           C  
ANISOU 4409  CZ  PHE B 107     3446   4508   5782    -66    295    311       C  
ATOM   4410  N   LEU B 108     -24.036   6.141  67.864  1.00 29.09           N  
ANISOU 4410  N   LEU B 108     2750   3825   4477    218    469    446       N  
ATOM   4411  CA  LEU B 108     -23.662   7.336  67.106  1.00 27.85           C  
ANISOU 4411  CA  LEU B 108     2626   3689   4267    248    396    370       C  
ATOM   4412  C   LEU B 108     -22.237   7.723  67.477  1.00 31.95           C  
ANISOU 4412  C   LEU B 108     3250   4208   4681    279    366    355       C  
ATOM   4413  O   LEU B 108     -21.461   8.180  66.614  1.00 30.71           O  
ANISOU 4413  O   LEU B 108     3129   4037   4502    276    291    298       O  
ATOM   4414  CB  LEU B 108     -24.661   8.484  67.312  1.00 27.89           C  
ANISOU 4414  CB  LEU B 108     2594   3746   4255    297    426    357       C  
ATOM   4415  CG  LEU B 108     -25.964   8.274  66.501  1.00 32.72           C  
ANISOU 4415  CG  LEU B 108     3090   4364   4979    263    418    351       C  
ATOM   4416  CD1 LEU B 108     -27.167   9.188  66.953  1.00 33.11           C  
ANISOU 4416  CD1 LEU B 108     3079   4469   5033    318    476    364       C  
ATOM   4417  CD2 LEU B 108     -25.692   8.435  65.036  1.00 33.19           C  
ANISOU 4417  CD2 LEU B 108     3141   4405   5065    235    316    286       C  
ATOM   4418  N   CYS B 109     -21.900   7.487  68.747  1.00 29.18           N  
ANISOU 4418  N   CYS B 109     2942   3877   4267    305    424    411       N  
ATOM   4419  CA  CYS B 109     -20.527   7.615  69.245  1.00 28.66           C  
ANISOU 4419  CA  CYS B 109     2965   3818   4107    328    396    409       C  
ATOM   4420  C   CYS B 109     -19.522   6.936  68.336  1.00 30.15           C  
ANISOU 4420  C   CYS B 109     3170   3953   4333    290    328    389       C  
ATOM   4421  O   CYS B 109     -18.564   7.564  67.918  1.00 29.21           O  
ANISOU 4421  O   CYS B 109     3100   3836   4163    300    267    339       O  
ATOM   4422  CB  CYS B 109     -20.372   7.045  70.648  1.00 29.88           C  
ANISOU 4422  CB  CYS B 109     3149   3999   4206    350    466    490       C  
ATOM   4423  SG  CYS B 109     -18.726   7.319  71.324  1.00 33.57           S  
ANISOU 4423  SG  CYS B 109     3716   4494   4545    383    422    486       S  
ATOM   4424  N   LYS B 110     -19.763   5.673  68.003  1.00 26.11           N  
ANISOU 4424  N   LYS B 110     2616   3390   3916    244    342    423       N  
ATOM   4425  CA  LYS B 110     -18.868   4.941  67.076  1.00 24.70           C  
ANISOU 4425  CA  LYS B 110     2450   3153   3783    209    286    397       C  
ATOM   4426  C   LYS B 110     -19.030   5.514  65.656  1.00 28.40           C  
ANISOU 4426  C   LYS B 110     2896   3613   4281    187    217    312       C  
ATOM   4427  O   LYS B 110     -18.040   5.807  64.968  1.00 27.65           O  
ANISOU 4427  O   LYS B 110     2842   3510   4156    190    157    265       O  
ATOM   4428  CB  LYS B 110     -19.125   3.444  67.100  1.00 26.23           C  
ANISOU 4428  CB  LYS B 110     2607   3281   4077    166    325    451       C  
ATOM   4429  CG  LYS B 110     -19.059   2.837  68.499  1.00 23.22           C  
ANISOU 4429  CG  LYS B 110     2246   2909   3669    191    400    552       C  
ATOM   4430  CD  LYS B 110     -19.553   1.405  68.548  1.00 21.32           C  
ANISOU 4430  CD  LYS B 110     1960   2594   3546    145    454    614       C  
ATOM   4431  CE  LYS B 110     -19.167   0.752  69.896  1.00 28.89           C  
ANISOU 4431  CE  LYS B 110     2954   3557   4464    179    521    728       C  
ATOM   4432  NZ  LYS B 110     -17.660   0.490  70.113  1.00 31.07           N  
ANISOU 4432  NZ  LYS B 110     3299   3826   4681    215    482    748       N  
ATOM   4433  N   ALA B 111     -20.278   5.750  65.272  1.00 25.19           N  
ANISOU 4433  N   ALA B 111     2423   3220   3926    172    227    297       N  
ATOM   4434  CA  ALA B 111     -20.596   6.278  63.964  1.00 24.78           C  
ANISOU 4434  CA  ALA B 111     2343   3172   3899    155    163    227       C  
ATOM   4435  C   ALA B 111     -19.875   7.575  63.644  1.00 28.82           C  
ANISOU 4435  C   ALA B 111     2911   3715   4324    196    114    182       C  
ATOM   4436  O   ALA B 111     -19.410   7.745  62.543  1.00 28.49           O  
ANISOU 4436  O   ALA B 111     2881   3662   4283    182     53    132       O  
ATOM   4437  CB  ALA B 111     -22.097   6.460  63.802  1.00 26.05           C  
ANISOU 4437  CB  ALA B 111     2417   3359   4121    144    184    229       C  
ATOM   4438  N   VAL B 112     -19.812   8.515  64.573  1.00 26.23           N  
ANISOU 4438  N   VAL B 112     2619   3424   3921    246    144    197       N  
ATOM   4439  CA  VAL B 112     -19.208   9.820  64.237  1.00 25.32           C  
ANISOU 4439  CA  VAL B 112     2555   3328   3737    279    101    150       C  
ATOM   4440  C   VAL B 112     -17.699   9.677  64.184  1.00 28.82           C  
ANISOU 4440  C   VAL B 112     3063   3753   4134    274     64    138       C  
ATOM   4441  O   VAL B 112     -17.045  10.328  63.374  1.00 28.00           O  
ANISOU 4441  O   VAL B 112     2988   3645   4007    275     13     95       O  
ATOM   4442  CB  VAL B 112     -19.613  10.945  65.198  1.00 29.04           C  
ANISOU 4442  CB  VAL B 112     3048   3837   4148    333    143    155       C  
ATOM   4443  CG1 VAL B 112     -21.108  11.059  65.235  1.00 29.32           C  
ANISOU 4443  CG1 VAL B 112     3010   3894   4238    344    184    171       C  
ATOM   4444  CG2 VAL B 112     -19.039  10.699  66.584  1.00 29.11           C  
ANISOU 4444  CG2 VAL B 112     3106   3863   4092    351    188    192       C  
ATOM   4445  N   HIS B 113     -17.171   8.798  65.038  1.00 25.62           N  
ANISOU 4445  N   HIS B 113     2676   3340   3719    270     94    183       N  
ATOM   4446  CA  HIS B 113     -15.755   8.430  65.026  1.00 24.58           C  
ANISOU 4446  CA  HIS B 113     2591   3192   3557    265     62    183       C  
ATOM   4447  C   HIS B 113     -15.361   7.779  63.725  1.00 28.20           C  
ANISOU 4447  C   HIS B 113     3033   3608   4075    229     20    151       C  
ATOM   4448  O   HIS B 113     -14.345   8.131  63.139  1.00 27.88           O  
ANISOU 4448  O   HIS B 113     3023   3563   4005    230    -24    118       O  
ATOM   4449  CB  HIS B 113     -15.431   7.481  66.179  1.00 25.61           C  
ANISOU 4449  CB  HIS B 113     2733   3323   3676    273    105    251       C  
ATOM   4450  CG  HIS B 113     -14.932   8.168  67.406  1.00 28.66           C  
ANISOU 4450  CG  HIS B 113     3169   3761   3961    313    118    269       C  
ATOM   4451  ND1 HIS B 113     -15.720   8.365  68.517  1.00 30.94           N  
ANISOU 4451  ND1 HIS B 113     3456   4087   4210    340    178    305       N  
ATOM   4452  CD2 HIS B 113     -13.725   8.693  67.703  1.00 29.75           C  
ANISOU 4452  CD2 HIS B 113     3355   3922   4025    329     79    250       C  
ATOM   4453  CE1 HIS B 113     -15.019   8.988  69.448  1.00 30.26           C  
ANISOU 4453  CE1 HIS B 113     3425   4049   4024    371    172    302       C  
ATOM   4454  NE2 HIS B 113     -13.799   9.186  68.983  1.00 29.98           N  
ANISOU 4454  NE2 HIS B 113     3417   4004   3968    362    108    270       N  
ATOM   4455  N   VAL B 114     -16.159   6.825  63.272  1.00 25.25           N  
ANISOU 4455  N   VAL B 114     2608   3201   3784    195     35    158       N  
ATOM   4456  CA  VAL B 114     -15.879   6.151  62.018  1.00 25.03           C  
ANISOU 4456  CA  VAL B 114     2567   3133   3811    159     -3    117       C  
ATOM   4457  C   VAL B 114     -15.855   7.205  60.958  1.00 28.00           C  
ANISOU 4457  C   VAL B 114     2950   3535   4154    163    -56     58       C  
ATOM   4458  O   VAL B 114     -14.883   7.316  60.223  1.00 27.51           O  
ANISOU 4458  O   VAL B 114     2919   3465   4070    161    -93     26       O  
ATOM   4459  CB  VAL B 114     -16.926   5.063  61.655  1.00 30.06           C  
ANISOU 4459  CB  VAL B 114     3143   3731   4546    113     17    119       C  
ATOM   4460  CG1 VAL B 114     -16.720   4.591  60.231  1.00 30.21           C  
ANISOU 4460  CG1 VAL B 114     3153   3718   4606     76    -31     54       C  
ATOM   4461  CG2 VAL B 114     -16.823   3.878  62.589  1.00 30.21           C  
ANISOU 4461  CG2 VAL B 114     3161   3708   4611    105     73    185       C  
ATOM   4462  N   ILE B 115     -16.903   8.013  60.912  1.00 24.62           N  
ANISOU 4462  N   ILE B 115     2493   3140   3723    174    -55     52       N  
ATOM   4463  CA  ILE B 115     -17.039   9.035  59.885  1.00 24.86           C  
ANISOU 4463  CA  ILE B 115     2524   3194   3727    184   -102      8       C  
ATOM   4464  C   ILE B 115     -15.848  10.026  59.889  1.00 30.57           C  
ANISOU 4464  C   ILE B 115     3313   3927   4377    212   -123     -5       C  
ATOM   4465  O   ILE B 115     -15.433  10.517  58.836  1.00 30.23           O  
ANISOU 4465  O   ILE B 115     3284   3886   4315    209   -165    -38       O  
ATOM   4466  CB  ILE B 115     -18.403   9.777  60.010  1.00 28.00           C  
ANISOU 4466  CB  ILE B 115     2874   3626   4137    204    -90     16       C  
ATOM   4467  CG1 ILE B 115     -19.537   8.837  59.593  1.00 28.33           C  
ANISOU 4467  CG1 ILE B 115     2839   3664   4262    164    -88     16       C  
ATOM   4468  CG2 ILE B 115     -18.406  11.064  59.166  1.00 28.09           C  
ANISOU 4468  CG2 ILE B 115     2901   3661   4109    232   -132    -12       C  
ATOM   4469  CD1 ILE B 115     -20.901   9.453  59.672  1.00 35.33           C  
ANISOU 4469  CD1 ILE B 115     3661   4589   5173    183    -76     28       C  
ATOM   4470  N   TYR B 116     -15.287  10.283  61.063  1.00 28.15           N  
ANISOU 4470  N   TYR B 116     3042   3626   4028    234    -95     21       N  
ATOM   4471  CA  TYR B 116     -14.077  11.095  61.179  1.00 27.93           C  
ANISOU 4471  CA  TYR B 116     3069   3603   3939    250   -117      7       C  
ATOM   4472  C   TYR B 116     -12.870  10.437  60.457  1.00 30.68           C  
ANISOU 4472  C   TYR B 116     3432   3930   4294    227   -146     -7       C  
ATOM   4473  O   TYR B 116     -12.311  10.994  59.536  1.00 28.80           O  
ANISOU 4473  O   TYR B 116     3210   3691   4040    223   -178    -37       O  
ATOM   4474  CB  TYR B 116     -13.768  11.296  62.662  1.00 29.89           C  
ANISOU 4474  CB  TYR B 116     3348   3870   4139    273    -85     35       C  
ATOM   4475  CG  TYR B 116     -12.615  12.201  62.912  1.00 32.71           C  
ANISOU 4475  CG  TYR B 116     3756   4237   4437    283   -109     14       C  
ATOM   4476  CD1 TYR B 116     -12.636  13.510  62.450  1.00 34.97           C  
ANISOU 4476  CD1 TYR B 116     4064   4521   4702    293   -127    -21       C  
ATOM   4477  CD2 TYR B 116     -11.497  11.766  63.599  1.00 33.77           C  
ANISOU 4477  CD2 TYR B 116     3913   4380   4540    281   -116     31       C  
ATOM   4478  CE1 TYR B 116     -11.565  14.368  62.667  1.00 36.07           C  
ANISOU 4478  CE1 TYR B 116     4246   4661   4795    292   -149    -44       C  
ATOM   4479  CE2 TYR B 116     -10.418  12.625  63.814  1.00 34.97           C  
ANISOU 4479  CE2 TYR B 116     4102   4545   4641    282   -144      6       C  
ATOM   4480  CZ  TYR B 116     -10.475  13.926  63.347  1.00 43.92           C  
ANISOU 4480  CZ  TYR B 116     5258   5671   5761    283   -159    -34       C  
ATOM   4481  OH  TYR B 116      -9.434  14.803  63.545  1.00 48.57           O  
ANISOU 4481  OH  TYR B 116     5880   6263   6310    275   -186    -62       O  
ATOM   4482  N   THR B 117     -12.521   9.227  60.875  1.00 27.89           N  
ANISOU 4482  N   THR B 117     3070   3556   3969    216   -127     19       N  
ATOM   4483  CA  THR B 117     -11.451   8.466  60.267  1.00 27.80           C  
ANISOU 4483  CA  THR B 117     3068   3520   3976    202   -144      9       C  
ATOM   4484  C   THR B 117     -11.592   8.369  58.747  1.00 31.61           C  
ANISOU 4484  C   THR B 117     3537   3990   4483    180   -172    -39       C  
ATOM   4485  O   THR B 117     -10.649   8.665  57.999  1.00 31.71           O  
ANISOU 4485  O   THR B 117     3571   4005   4474    180   -196    -64       O  
ATOM   4486  CB  THR B 117     -11.440   7.045  60.845  1.00 38.13           C  
ANISOU 4486  CB  THR B 117     4359   4794   5334    196   -111     49       C  
ATOM   4487  OG1 THR B 117     -11.360   7.126  62.276  1.00 38.33           O  
ANISOU 4487  OG1 THR B 117     4397   4842   5323    221    -84    101       O  
ATOM   4488  CG2 THR B 117     -10.260   6.196  60.269  1.00 36.83           C  
ANISOU 4488  CG2 THR B 117     4203   4597   5195    191   -122     40       C  
ATOM   4489  N   VAL B 118     -12.758   7.935  58.289  1.00 27.43           N  
ANISOU 4489  N   VAL B 118     2971   3452   3999    161   -171    -52       N  
ATOM   4490  CA  VAL B 118     -13.048   7.883  56.852  1.00 26.94           C  
ANISOU 4490  CA  VAL B 118     2895   3392   3948    140   -205   -103       C  
ATOM   4491  C   VAL B 118     -12.665   9.193  56.151  1.00 30.22           C  
ANISOU 4491  C   VAL B 118     3338   3842   4303    158   -236   -121       C  
ATOM   4492  O   VAL B 118     -12.048   9.173  55.092  1.00 30.06           O  
ANISOU 4492  O   VAL B 118     3333   3824   4266    150   -258   -152       O  
ATOM   4493  CB  VAL B 118     -14.524   7.540  56.615  1.00 31.20           C  
ANISOU 4493  CB  VAL B 118     3383   3935   4536    117   -207   -112       C  
ATOM   4494  CG1 VAL B 118     -14.959   7.860  55.200  1.00 31.33           C  
ANISOU 4494  CG1 VAL B 118     3385   3979   4540    104   -255   -161       C  
ATOM   4495  CG2 VAL B 118     -14.755   6.090  56.928  1.00 31.42           C  
ANISOU 4495  CG2 VAL B 118     3386   3914   4637     86   -179   -105       C  
ATOM   4496  N   ASN B 119     -12.999  10.323  56.763  1.00 26.14           N  
ANISOU 4496  N   ASN B 119     2830   3347   3754    183   -232    -99       N  
ATOM   4497  CA  ASN B 119     -12.711  11.628  56.181  1.00 25.52           C  
ANISOU 4497  CA  ASN B 119     2778   3289   3629    201   -254   -108       C  
ATOM   4498  C   ASN B 119     -11.214  11.941  56.138  1.00 30.49           C  
ANISOU 4498  C   ASN B 119     3449   3911   4225    202   -257   -110       C  
ATOM   4499  O   ASN B 119     -10.703  12.331  55.098  1.00 30.68           O  
ANISOU 4499  O   ASN B 119     3487   3942   4227    198   -276   -127       O  
ATOM   4500  CB  ASN B 119     -13.465  12.731  56.937  1.00 23.89           C  
ANISOU 4500  CB  ASN B 119     2574   3096   3409    231   -241    -88       C  
ATOM   4501  CG  ASN B 119     -13.300  14.110  56.290  1.00 39.63           C  
ANISOU 4501  CG  ASN B 119     4594   5096   5367    252   -260    -92       C  
ATOM   4502  OD1 ASN B 119     -12.540  14.944  56.775  1.00 29.57           O  
ANISOU 4502  OD1 ASN B 119     3360   3811   4065    262   -252    -89       O  
ATOM   4503  ND2 ASN B 119     -14.013  14.347  55.186  1.00 31.08           N  
ANISOU 4503  ND2 ASN B 119     3489   4032   4287    257   -287    -98       N  
ATOM   4504  N   LEU B 120     -10.512  11.789  57.252  1.00 27.93           N  
ANISOU 4504  N   LEU B 120     3139   3579   3895    206   -238    -91       N  
ATOM   4505  CA  LEU B 120      -9.073  12.111  57.289  1.00 28.38           C  
ANISOU 4505  CA  LEU B 120     3223   3635   3926    204   -245    -92       C  
ATOM   4506  C   LEU B 120      -8.274  11.310  56.243  1.00 32.63           C  
ANISOU 4506  C   LEU B 120     3755   4164   4478    189   -251   -110       C  
ATOM   4507  O   LEU B 120      -7.376  11.841  55.573  1.00 32.43           O  
ANISOU 4507  O   LEU B 120     3745   4146   4432    186   -260   -119       O  
ATOM   4508  CB  LEU B 120      -8.471  11.850  58.679  1.00 28.72           C  
ANISOU 4508  CB  LEU B 120     3273   3682   3959    211   -232    -67       C  
ATOM   4509  CG  LEU B 120      -8.786  12.821  59.838  1.00 34.56           C  
ANISOU 4509  CG  LEU B 120     4033   4436   4662    226   -225    -60       C  
ATOM   4510  CD1 LEU B 120      -7.983  12.430  61.091  1.00 35.34           C  
ANISOU 4510  CD1 LEU B 120     4140   4552   4737    231   -221    -37       C  
ATOM   4511  CD2 LEU B 120      -8.533  14.308  59.521  1.00 38.08           C  
ANISOU 4511  CD2 LEU B 120     4508   4881   5080    226   -239    -83       C  
ATOM   4512  N   TYR B 121      -8.604  10.030  56.118  1.00 28.52           N  
ANISOU 4512  N   TYR B 121     3213   3626   3998    181   -241   -115       N  
ATOM   4513  CA  TYR B 121      -7.874   9.148  55.236  1.00 27.94           C  
ANISOU 4513  CA  TYR B 121     3136   3536   3943    172   -239   -138       C  
ATOM   4514  C   TYR B 121      -8.280   9.325  53.770  1.00 30.79           C  
ANISOU 4514  C   TYR B 121     3500   3911   4288    162   -257   -179       C  
ATOM   4515  O   TYR B 121      -7.415   9.394  52.907  1.00 30.35           O  
ANISOU 4515  O   TYR B 121     3457   3863   4212    162   -257   -197       O  
ATOM   4516  CB  TYR B 121      -8.044   7.698  55.693  1.00 29.05           C  
ANISOU 4516  CB  TYR B 121     3258   3639   4140    168   -217   -130       C  
ATOM   4517  CG  TYR B 121      -7.451   7.391  57.052  1.00 30.35           C  
ANISOU 4517  CG  TYR B 121     3422   3796   4312    185   -199    -81       C  
ATOM   4518  CD1 TYR B 121      -7.731   6.194  57.686  1.00 32.33           C  
ANISOU 4518  CD1 TYR B 121     3658   4011   4613    186   -173    -54       C  
ATOM   4519  CD2 TYR B 121      -6.597   8.291  57.707  1.00 31.01           C  
ANISOU 4519  CD2 TYR B 121     3521   3912   4351    199   -209    -60       C  
ATOM   4520  CE1 TYR B 121      -7.193   5.891  58.915  1.00 33.11           C  
ANISOU 4520  CE1 TYR B 121     3758   4111   4710    208   -158      1       C  
ATOM   4521  CE2 TYR B 121      -6.054   7.994  58.951  1.00 31.92           C  
ANISOU 4521  CE2 TYR B 121     3634   4033   4460    216   -202    -16       C  
ATOM   4522  CZ  TYR B 121      -6.354   6.793  59.548  1.00 40.48           C  
ANISOU 4522  CZ  TYR B 121     4705   5088   5587    224   -176     19       C  
ATOM   4523  OH  TYR B 121      -5.818   6.484  60.793  1.00 43.48           O  
ANISOU 4523  OH  TYR B 121     5084   5482   5953    248   -170     73       O  
ATOM   4524  N   SER B 122      -9.579   9.421  53.480  1.00 26.82           N  
ANISOU 4524  N   SER B 122     2981   3419   3792    154   -273   -191       N  
ATOM   4525  CA  SER B 122     -10.022   9.517  52.077  1.00 26.31           C  
ANISOU 4525  CA  SER B 122     2915   3379   3704    145   -299   -229       C  
ATOM   4526  C   SER B 122      -9.646  10.877  51.488  1.00 28.09           C  
ANISOU 4526  C   SER B 122     3167   3637   3871    162   -313   -215       C  
ATOM   4527  O   SER B 122      -9.143  10.957  50.373  1.00 28.81           O  
ANISOU 4527  O   SER B 122     3273   3747   3926    161   -319   -236       O  
ATOM   4528  CB  SER B 122     -11.521   9.255  51.926  1.00 29.89           C  
ANISOU 4528  CB  SER B 122     3333   3842   4182    132   -320   -243       C  
ATOM   4529  OG  SER B 122     -12.295  10.210  52.647  1.00 38.52           O  
ANISOU 4529  OG  SER B 122     4414   4951   5270    150   -322   -206       O  
ATOM   4530  N   SER B 123      -9.855  11.943  52.236  1.00 22.23           N  
ANISOU 4530  N   SER B 123     2431   2897   3119    178   -311   -180       N  
ATOM   4531  CA  SER B 123      -9.557  13.257  51.717  1.00 21.31           C  
ANISOU 4531  CA  SER B 123     2340   2797   2960    193   -318   -162       C  
ATOM   4532  C   SER B 123      -8.130  13.332  51.235  1.00 25.57           C  
ANISOU 4532  C   SER B 123     2903   3335   3478    186   -304   -164       C  
ATOM   4533  O   SER B 123      -7.904  13.574  50.057  1.00 26.44           O  
ANISOU 4533  O   SER B 123     3025   3467   3552    187   -310   -170       O  
ATOM   4534  CB  SER B 123      -9.836  14.338  52.756  1.00 23.46           C  
ANISOU 4534  CB  SER B 123     2623   3056   3235    210   -310   -132       C  
ATOM   4535  OG  SER B 123      -9.125  14.070  53.951  1.00 31.95           O  
ANISOU 4535  OG  SER B 123     3703   4112   4326    203   -291   -126       O  
ATOM   4536  N   VAL B 124      -7.161  13.130  52.117  1.00 21.42           N  
ANISOU 4536  N   VAL B 124     2379   2789   2971    180   -285   -155       N  
ATOM   4537  CA  VAL B 124      -5.755  13.234  51.739  1.00 21.16           C  
ANISOU 4537  CA  VAL B 124     2355   2758   2926    173   -270   -153       C  
ATOM   4538  C   VAL B 124      -5.342  12.234  50.648  1.00 26.23           C  
ANISOU 4538  C   VAL B 124     2993   3410   3563    170   -259   -183       C  
ATOM   4539  O   VAL B 124      -4.613  12.590  49.704  1.00 27.04           O  
ANISOU 4539  O   VAL B 124     3107   3531   3635    170   -247   -184       O  
ATOM   4540  CB  VAL B 124      -4.827  13.120  52.958  1.00 24.73           C  
ANISOU 4540  CB  VAL B 124     2799   3195   3402    169   -260   -138       C  
ATOM   4541  CG1 VAL B 124      -4.837  11.676  53.533  1.00 24.13           C  
ANISOU 4541  CG1 VAL B 124     2701   3105   3362    173   -251   -145       C  
ATOM   4542  CG2 VAL B 124      -3.399  13.638  52.609  1.00 24.66           C  
ANISOU 4542  CG2 VAL B 124     2791   3194   3384    158   -247   -128       C  
ATOM   4543  N   TRP B 125      -5.823  10.997  50.707  1.00 21.93           N  
ANISOU 4543  N   TRP B 125     2433   2852   3048    168   -260   -211       N  
ATOM   4544  CA  TRP B 125      -5.450  10.058  49.626  1.00 21.42           C  
ANISOU 4544  CA  TRP B 125     2371   2791   2979    166   -247   -253       C  
ATOM   4545  C   TRP B 125      -6.085  10.426  48.271  1.00 26.04           C  
ANISOU 4545  C   TRP B 125     2971   3415   3507    165   -267   -278       C  
ATOM   4546  O   TRP B 125      -5.477  10.201  47.218  1.00 26.67           O  
ANISOU 4546  O   TRP B 125     3065   3516   3552    168   -252   -304       O  
ATOM   4547  CB  TRP B 125      -5.743   8.618  50.016  1.00 19.51           C  
ANISOU 4547  CB  TRP B 125     2111   2511   2792    160   -239   -281       C  
ATOM   4548  CG  TRP B 125      -4.659   8.091  50.848  1.00 20.08           C  
ANISOU 4548  CG  TRP B 125     2172   2554   2902    172   -211   -257       C  
ATOM   4549  CD1 TRP B 125      -4.618   8.060  52.196  1.00 22.50           C  
ANISOU 4549  CD1 TRP B 125     2466   2844   3240    177   -210   -216       C  
ATOM   4550  CD2 TRP B 125      -3.398   7.568  50.394  1.00 20.12           C  
ANISOU 4550  CD2 TRP B 125     2176   2554   2916    186   -180   -269       C  
ATOM   4551  NE1 TRP B 125      -3.429   7.533  52.622  1.00 21.85           N  
ANISOU 4551  NE1 TRP B 125     2371   2748   3183    193   -189   -198       N  
ATOM   4552  CE2 TRP B 125      -2.661   7.219  51.535  1.00 23.80           C  
ANISOU 4552  CE2 TRP B 125     2621   2998   3423    199   -168   -229       C  
ATOM   4553  CE3 TRP B 125      -2.839   7.339  49.137  1.00 21.57           C  
ANISOU 4553  CE3 TRP B 125     2371   2752   3073    191   -160   -308       C  
ATOM   4554  CZ2 TRP B 125      -1.395   6.645  51.464  1.00 23.54           C  
ANISOU 4554  CZ2 TRP B 125     2573   2957   3416    221   -138   -224       C  
ATOM   4555  CZ3 TRP B 125      -1.572   6.785  49.058  1.00 23.26           C  
ANISOU 4555  CZ3 TRP B 125     2572   2954   3311    212   -121   -308       C  
ATOM   4556  CH2 TRP B 125      -0.867   6.435  50.216  1.00 23.90           C  
ANISOU 4556  CH2 TRP B 125     2626   3011   3443    227   -112   -265       C  
ATOM   4557  N   ILE B 126      -7.291  10.979  48.281  1.00 21.48           N  
ANISOU 4557  N   ILE B 126     2389   2854   2918    164   -300   -269       N  
ATOM   4558  CA  ILE B 126      -7.856  11.462  47.034  1.00 21.65           C  
ANISOU 4558  CA  ILE B 126     2422   2923   2879    170   -326   -280       C  
ATOM   4559  C   ILE B 126      -6.901  12.507  46.480  1.00 24.88           C  
ANISOU 4559  C   ILE B 126     2859   3353   3240    183   -305   -243       C  
ATOM   4560  O   ILE B 126      -6.583  12.468  45.296  1.00 23.76           O  
ANISOU 4560  O   ILE B 126     2737   3249   3043    188   -300   -259       O  
ATOM   4561  CB  ILE B 126      -9.333  11.970  47.193  1.00 24.64           C  
ANISOU 4561  CB  ILE B 126     2781   3320   3259    175   -366   -265       C  
ATOM   4562  CG1 ILE B 126     -10.266  10.798  47.498  1.00 24.48           C  
ANISOU 4562  CG1 ILE B 126     2726   3286   3288    153   -383   -307       C  
ATOM   4563  CG2 ILE B 126      -9.839  12.639  45.920  1.00 25.46           C  
ANISOU 4563  CG2 ILE B 126     2897   3483   3292    189   -398   -260       C  
ATOM   4564  CD1 ILE B 126     -11.600  11.250  48.054  1.00 27.77           C  
ANISOU 4564  CD1 ILE B 126     3109   3711   3729    158   -409   -283       C  
ATOM   4565  N   LEU B 127      -6.379  13.380  47.357  1.00 22.48           N  
ANISOU 4565  N   LEU B 127     2560   3024   2959    185   -289   -197       N  
ATOM   4566  CA  LEU B 127      -5.337  14.362  46.961  1.00 22.54           C  
ANISOU 4566  CA  LEU B 127     2587   3037   2939    188   -263   -160       C  
ATOM   4567  C   LEU B 127      -4.096  13.688  46.405  1.00 27.20           C  
ANISOU 4567  C   LEU B 127     3177   3636   3521    182   -227   -180       C  
ATOM   4568  O   LEU B 127      -3.499  14.177  45.450  1.00 26.69           O  
ANISOU 4568  O   LEU B 127     3130   3600   3412    187   -204   -163       O  
ATOM   4569  CB  LEU B 127      -4.888  15.249  48.125  1.00 22.03           C  
ANISOU 4569  CB  LEU B 127     2522   2935   2912    181   -254   -124       C  
ATOM   4570  CG  LEU B 127      -5.919  16.117  48.856  1.00 26.04           C  
ANISOU 4570  CG  LEU B 127     3035   3425   3434    191   -276   -102       C  
ATOM   4571  CD1 LEU B 127      -5.137  17.112  49.730  1.00 25.52           C  
ANISOU 4571  CD1 LEU B 127     2979   3323   3392    179   -260    -76       C  
ATOM   4572  CD2 LEU B 127      -6.882  16.830  47.915  1.00 27.72           C  
ANISOU 4572  CD2 LEU B 127     3262   3663   3608    213   -295    -80       C  
ATOM   4573  N   ALA B 128      -3.691  12.588  47.039  1.00 24.23           N  
ANISOU 4573  N   ALA B 128     2779   3234   3191    177   -215   -210       N  
ATOM   4574  CA  ALA B 128      -2.578  11.785  46.540  1.00 23.97           C  
ANISOU 4574  CA  ALA B 128     2741   3206   3161    181   -177   -234       C  
ATOM   4575  C   ALA B 128      -2.892  11.287  45.139  1.00 27.93           C  
ANISOU 4575  C   ALA B 128     3263   3744   3604    189   -174   -278       C  
ATOM   4576  O   ALA B 128      -2.020  11.297  44.267  1.00 28.83           O  
ANISOU 4576  O   ALA B 128     3388   3885   3683    197   -136   -283       O  
ATOM   4577  CB  ALA B 128      -2.318  10.601  47.455  1.00 24.48           C  
ANISOU 4577  CB  ALA B 128     2780   3231   3290    182   -170   -255       C  
ATOM   4578  N   PHE B 129      -4.130  10.838  44.926  1.00 23.27           N  
ANISOU 4578  N   PHE B 129     2677   3159   3004    185   -212   -314       N  
ATOM   4579  CA  PHE B 129      -4.562  10.391  43.598  1.00 23.20           C  
ANISOU 4579  CA  PHE B 129     2690   3195   2931    188   -223   -366       C  
ATOM   4580  C   PHE B 129      -4.646  11.554  42.568  1.00 27.25           C  
ANISOU 4580  C   PHE B 129     3230   3770   3356    201   -229   -328       C  
ATOM   4581  O   PHE B 129      -4.363  11.363  41.378  1.00 28.29           O  
ANISOU 4581  O   PHE B 129     3385   3948   3415    210   -214   -356       O  
ATOM   4582  CB  PHE B 129      -5.917   9.686  43.690  1.00 24.73           C  
ANISOU 4582  CB  PHE B 129     2871   3383   3144    172   -271   -413       C  
ATOM   4583  CG  PHE B 129      -5.837   8.190  43.754  1.00 26.35           C  
ANISOU 4583  CG  PHE B 129     3068   3546   3397    160   -256   -484       C  
ATOM   4584  CD1 PHE B 129      -5.298   7.552  44.860  1.00 29.44           C  
ANISOU 4584  CD1 PHE B 129     3440   3873   3873    160   -227   -472       C  
ATOM   4585  CD2 PHE B 129      -6.362   7.413  42.736  1.00 28.93           C  
ANISOU 4585  CD2 PHE B 129     3409   3897   3688    149   -275   -563       C  
ATOM   4586  CE1 PHE B 129      -5.245   6.168  44.930  1.00 30.53           C  
ANISOU 4586  CE1 PHE B 129     3573   3960   4066    152   -209   -530       C  
ATOM   4587  CE2 PHE B 129      -6.300   6.025  42.802  1.00 32.24           C  
ANISOU 4587  CE2 PHE B 129     3825   4263   4164    135   -258   -634       C  
ATOM   4588  CZ  PHE B 129      -5.734   5.409  43.896  1.00 30.04           C  
ANISOU 4588  CZ  PHE B 129     3527   3909   3977    138   -221   -613       C  
ATOM   4589  N   ILE B 130      -5.070  12.741  42.990  1.00 21.88           N  
ANISOU 4589  N   ILE B 130     2548   3087   2677    204   -249   -264       N  
ATOM   4590  CA  ILE B 130      -4.972  13.896  42.093  1.00 21.29           C  
ANISOU 4590  CA  ILE B 130     2501   3058   2531    220   -244   -211       C  
ATOM   4591  C   ILE B 130      -3.528  14.142  41.647  1.00 25.54           C  
ANISOU 4591  C   ILE B 130     3051   3602   3051    222   -181   -187       C  
ATOM   4592  O   ILE B 130      -3.291  14.551  40.506  1.00 26.08           O  
ANISOU 4592  O   ILE B 130     3147   3723   3041    236   -161   -167       O  
ATOM   4593  CB  ILE B 130      -5.558  15.191  42.712  1.00 23.46           C  
ANISOU 4593  CB  ILE B 130     2774   3311   2827    228   -265   -143       C  
ATOM   4594  CG1 ILE B 130      -7.091  15.111  42.711  1.00 24.05           C  
ANISOU 4594  CG1 ILE B 130     2835   3406   2895    237   -326   -156       C  
ATOM   4595  CG2 ILE B 130      -5.125  16.395  41.937  1.00 23.30           C  
ANISOU 4595  CG2 ILE B 130     2784   3315   2755    242   -241    -74       C  
ATOM   4596  CD1 ILE B 130      -7.757  16.060  43.693  1.00 28.78           C  
ANISOU 4596  CD1 ILE B 130     3424   3968   3544    247   -342   -108       C  
ATOM   4597  N   SER B 131      -2.563  13.904  42.523  1.00 21.19           N  
ANISOU 4597  N   SER B 131     2477   3005   2569    209   -147   -185       N  
ATOM   4598  CA  SER B 131      -1.172  14.136  42.130  1.00 21.17           C  
ANISOU 4598  CA  SER B 131     2472   3012   2559    208    -86   -160       C  
ATOM   4599  C   SER B 131      -0.610  13.016  41.193  1.00 26.19           C  
ANISOU 4599  C   SER B 131     3114   3681   3156    222    -48   -219       C  
ATOM   4600  O   SER B 131       0.175  13.296  40.294  1.00 25.99           O  
ANISOU 4600  O   SER B 131     3101   3694   3080    231      2   -200       O  
ATOM   4601  CB ASER B 131      -0.268  14.343  43.353  0.50 22.60           C  
ANISOU 4601  CB ASER B 131     2618   3143   2826    189    -69   -135       C  
ATOM   4602  CB BSER B 131      -0.306  14.324  43.376  0.50 23.29           C  
ANISOU 4602  CB BSER B 131     2705   3229   2913    189    -70   -136       C  
ATOM   4603  OG ASER B 131       0.016  13.129  44.010  0.50 26.97           O  
ANISOU 4603  OG ASER B 131     3145   3672   3432    191    -67   -181       O  
ATOM   4604  OG BSER B 131      -0.822  15.394  44.160  0.50 30.11           O  
ANISOU 4604  OG BSER B 131     3573   4063   3804    177   -101    -92       O  
ATOM   4605  N   LEU B 132      -1.027  11.771  41.410  1.00 23.31           N  
ANISOU 4605  N   LEU B 132     2742   3298   2817    223    -66   -290       N  
ATOM   4606  CA  LEU B 132      -0.707  10.670  40.495  1.00 24.40           C  
ANISOU 4606  CA  LEU B 132     2894   3459   2918    238    -34   -362       C  
ATOM   4607  C   LEU B 132      -1.182  10.954  39.082  1.00 29.39           C  
ANISOU 4607  C   LEU B 132     3568   4165   3433    250    -42   -378       C  
ATOM   4608  O   LEU B 132      -0.504  10.661  38.088  1.00 29.48           O  
ANISOU 4608  O   LEU B 132     3600   4219   3382    267      9   -404       O  
ATOM   4609  CB  LEU B 132      -1.347   9.360  40.966  1.00 24.50           C  
ANISOU 4609  CB  LEU B 132     2898   3427   2984    232    -62   -437       C  
ATOM   4610  CG  LEU B 132      -0.615   8.657  42.113  1.00 29.00           C  
ANISOU 4610  CG  LEU B 132     3430   3930   3657    233    -37   -434       C  
ATOM   4611  CD1 LEU B 132      -1.291   7.342  42.429  1.00 29.20           C  
ANISOU 4611  CD1 LEU B 132     3453   3906   3733    227    -56   -503       C  
ATOM   4612  CD2 LEU B 132       0.856   8.424  41.763  1.00 31.70           C  
ANISOU 4612  CD2 LEU B 132     3760   4279   4006    256     36   -430       C  
ATOM   4613  N   ASP B 133      -2.374  11.531  39.027  1.00 26.21           N  
ANISOU 4613  N   ASP B 133     3177   3784   2998    244   -105   -359       N  
ATOM   4614  CA  ASP B 133      -3.040  11.822  37.789  1.00 26.38           C  
ANISOU 4614  CA  ASP B 133     3234   3884   2906    257   -131   -368       C  
ATOM   4615  C   ASP B 133      -2.301  12.902  37.021  1.00 30.62           C  
ANISOU 4615  C   ASP B 133     3794   4468   3371    275    -84   -290       C  
ATOM   4616  O   ASP B 133      -2.253  12.866  35.781  1.00 31.68           O  
ANISOU 4616  O   ASP B 133     3965   4678   3396    294    -69   -305       O  
ATOM   4617  CB  ASP B 133      -4.471  12.254  38.082  1.00 27.80           C  
ANISOU 4617  CB  ASP B 133     3405   4070   3086    251   -212   -352       C  
ATOM   4618  CG  ASP B 133      -5.216  12.570  36.839  1.00 37.57           C  
ANISOU 4618  CG  ASP B 133     4672   5399   4205    268   -251   -354       C  
ATOM   4619  OD1 ASP B 133      -5.332  13.769  36.523  1.00 38.34           O  
ANISOU 4619  OD1 ASP B 133     4784   5528   4257    287   -255   -266       O  
ATOM   4620  OD2 ASP B 133      -5.627  11.622  36.143  1.00 43.54           O  
ANISOU 4620  OD2 ASP B 133     5439   6193   4909    262   -277   -443       O  
ATOM   4621  N   ARG B 134      -1.741  13.860  37.757  1.00 25.95           N  
ANISOU 4621  N   ARG B 134     3185   3834   2842    267    -59   -208       N  
ATOM   4622  CA  ARG B 134      -0.988  14.963  37.176  1.00 26.01           C  
ANISOU 4622  CA  ARG B 134     3209   3868   2807    275     -6   -122       C  
ATOM   4623  C   ARG B 134       0.343  14.456  36.651  1.00 30.85           C  
ANISOU 4623  C   ARG B 134     3817   4499   3404    281     77   -141       C  
ATOM   4624  O   ARG B 134       0.818  14.871  35.607  1.00 31.00           O  
ANISOU 4624  O   ARG B 134     3863   4577   3340    297    126   -105       O  
ATOM   4625  CB  ARG B 134      -0.735  16.053  38.231  1.00 25.12           C  
ANISOU 4625  CB  ARG B 134     3073   3689   2782    256     -4    -45       C  
ATOM   4626  CG  ARG B 134      -0.536  17.432  37.637  1.00 35.40           C  
ANISOU 4626  CG  ARG B 134     4400   5008   4043    262     25     55       C  
ATOM   4627  CD  ARG B 134      -1.841  18.210  37.543  1.00 40.62           C  
ANISOU 4627  CD  ARG B 134     5083   5676   4673    280    -38     96       C  
ATOM   4628  NE  ARG B 134      -2.917  17.463  36.909  1.00 42.75           N  
ANISOU 4628  NE  ARG B 134     5367   6009   4867    302    -96     38       N  
ATOM   4629  CZ  ARG B 134      -3.167  17.447  35.603  1.00 61.31           C  
ANISOU 4629  CZ  ARG B 134     7752   8447   7096    329    -98     44       C  
ATOM   4630  NH1 ARG B 134      -2.406  18.124  34.745  1.00 49.81           N  
ANISOU 4630  NH1 ARG B 134     6323   7026   5575    343    -36    115       N  
ATOM   4631  NH2 ARG B 134      -4.181  16.720  35.141  1.00 51.65           N  
ANISOU 4631  NH2 ARG B 134     6534   7280   5812    341   -163    -22       N  
ATOM   4632  N   TYR B 135       0.953  13.581  37.432  1.00 28.47           N  
ANISOU 4632  N   TYR B 135     3480   4149   3189    271     95   -190       N  
ATOM   4633  CA  TYR B 135       2.139  12.873  37.027  1.00 29.84           C  
ANISOU 4633  CA  TYR B 135     3641   4335   3363    284    171   -222       C  
ATOM   4634  C   TYR B 135       1.902  12.128  35.694  1.00 34.52           C  
ANISOU 4634  C   TYR B 135     4279   4997   3842    311    188   -293       C  
ATOM   4635  O   TYR B 135       2.709  12.237  34.782  1.00 35.03           O  
ANISOU 4635  O   TYR B 135     4357   5113   3841    330    260   -280       O  
ATOM   4636  CB  TYR B 135       2.577  11.907  38.145  1.00 31.35           C  
ANISOU 4636  CB  TYR B 135     3786   4458   3667    277    172   -268       C  
ATOM   4637  CG  TYR B 135       3.349  10.693  37.670  1.00 34.94           C  
ANISOU 4637  CG  TYR B 135     4235   4919   4122    303    232   -339       C  
ATOM   4638  CD1 TYR B 135       4.687  10.790  37.297  1.00 38.04           C  
ANISOU 4638  CD1 TYR B 135     4602   5332   4518    318    318   -311       C  
ATOM   4639  CD2 TYR B 135       2.738   9.453  37.584  1.00 36.06           C  
ANISOU 4639  CD2 TYR B 135     4394   5041   4265    313    207   -435       C  
ATOM   4640  CE1 TYR B 135       5.412   9.652  36.860  1.00 40.00           C  
ANISOU 4640  CE1 TYR B 135     4842   5583   4771    350    381   -378       C  
ATOM   4641  CE2 TYR B 135       3.438   8.328  37.154  1.00 37.86           C  
ANISOU 4641  CE2 TYR B 135     4622   5264   4500    341    267   -505       C  
ATOM   4642  CZ  TYR B 135       4.773   8.432  36.791  1.00 46.82           C  
ANISOU 4642  CZ  TYR B 135     5731   6420   5636    364    355   -477       C  
ATOM   4643  OH  TYR B 135       5.447   7.310  36.355  1.00 49.34           O  
ANISOU 4643  OH  TYR B 135     6050   6731   5965    400    421   -550       O  
ATOM   4644  N   LEU B 136       0.795  11.395  35.583  1.00 30.74           N  
ANISOU 4644  N   LEU B 136     3821   4522   3336    310    123   -371       N  
ATOM   4645  CA  LEU B 136       0.489  10.654  34.364  1.00 31.41           C  
ANISOU 4645  CA  LEU B 136     3950   4673   3310    329    127   -455       C  
ATOM   4646  C   LEU B 136       0.242  11.590  33.201  1.00 36.76           C  
ANISOU 4646  C   LEU B 136     4671   5446   3850    346    128   -400       C  
ATOM   4647  O   LEU B 136       0.837  11.432  32.139  1.00 37.54           O  
ANISOU 4647  O   LEU B 136     4801   5610   3852    371    189   -418       O  
ATOM   4648  CB  LEU B 136      -0.736   9.767  34.554  1.00 31.35           C  
ANISOU 4648  CB  LEU B 136     3949   4648   3315    313     46   -546       C  
ATOM   4649  CG  LEU B 136      -0.570   8.470  35.355  1.00 35.39           C  
ANISOU 4649  CG  LEU B 136     4435   5074   3938    303     53   -627       C  
ATOM   4650  CD1 LEU B 136      -1.914   7.755  35.405  1.00 35.33           C  
ANISOU 4650  CD1 LEU B 136     4434   5055   3934    279    -29   -708       C  
ATOM   4651  CD2 LEU B 136       0.531   7.571  34.753  1.00 37.63           C  
ANISOU 4651  CD2 LEU B 136     4731   5358   4208    330    140   -693       C  
ATOM   4652  N   ALA B 137      -0.645  12.559  33.411  1.00 33.01           N  
ANISOU 4652  N   ALA B 137     4198   4979   3366    338     64   -330       N  
ATOM   4653  CA  ALA B 137      -0.903  13.615  32.445  1.00 33.39           C  
ANISOU 4653  CA  ALA B 137     4283   5107   3296    359     62   -249       C  
ATOM   4654  C   ALA B 137       0.377  14.256  31.882  1.00 38.77           C  
ANISOU 4654  C   ALA B 137     4974   5816   3943    374    165   -173       C  
ATOM   4655  O   ALA B 137       0.529  14.387  30.674  1.00 39.56           O  
ANISOU 4655  O   ALA B 137     5116   6005   3910    400    199   -162       O  
ATOM   4656  CB  ALA B 137      -1.773  14.680  33.078  1.00 33.43           C  
ANISOU 4656  CB  ALA B 137     4275   5083   3343    352     -3   -165       C  
ATOM   4657  N   ILE B 138       1.294  14.654  32.752  1.00 35.56           N  
ANISOU 4657  N   ILE B 138     4525   5336   3650    354    215   -119       N  
ATOM   4658  CA  ILE B 138       2.464  15.404  32.318  1.00 36.29           C  
ANISOU 4658  CA  ILE B 138     4614   5446   3729    358    310    -33       C  
ATOM   4659  C   ILE B 138       3.624  14.505  31.876  1.00 41.64           C  
ANISOU 4659  C   ILE B 138     5278   6146   4395    372    401    -90       C  
ATOM   4660  O   ILE B 138       4.204  14.737  30.820  1.00 42.64           O  
ANISOU 4660  O   ILE B 138     5431   6345   4426    395    475    -58       O  
ATOM   4661  CB  ILE B 138       2.954  16.373  33.435  1.00 38.49           C  
ANISOU 4661  CB  ILE B 138     4846   5639   4139    323    320     54       C  
ATOM   4662  CG1 ILE B 138       1.834  17.319  33.860  1.00 38.22           C  
ANISOU 4662  CG1 ILE B 138     4827   5576   4119    316    242    111       C  
ATOM   4663  CG2 ILE B 138       4.146  17.196  32.962  1.00 39.41           C  
ANISOU 4663  CG2 ILE B 138     4952   5770   4251    318    419    147       C  
ATOM   4664  CD1 ILE B 138       2.193  18.169  35.050  1.00 43.90           C  
ANISOU 4664  CD1 ILE B 138     5508   6204   4969    280    242    171       C  
ATOM   4665  N   VAL B 139       3.955  13.495  32.680  1.00 38.35           N  
ANISOU 4665  N   VAL B 139     4822   5670   4078    364    399   -169       N  
ATOM   4666  CA  VAL B 139       5.164  12.682  32.476  1.00 39.12           C  
ANISOU 4666  CA  VAL B 139     4894   5770   4199    382    491   -214       C  
ATOM   4667  C   VAL B 139       4.975  11.650  31.373  1.00 46.69           C  
ANISOU 4667  C   VAL B 139     5904   6794   5043    418    513   -319       C  
ATOM   4668  O   VAL B 139       5.855  11.468  30.547  1.00 46.77           O  
ANISOU 4668  O   VAL B 139     5921   6855   4993    446    607   -324       O  
ATOM   4669  CB  VAL B 139       5.627  11.952  33.779  1.00 41.74           C  
ANISOU 4669  CB  VAL B 139     5163   6012   4684    368    482   -251       C  
ATOM   4670  CG1 VAL B 139       6.991  11.248  33.573  1.00 41.91           C  
ANISOU 4670  CG1 VAL B 139     5145   6037   4741    394    584   -277       C  
ATOM   4671  CG2 VAL B 139       5.723  12.924  34.959  1.00 40.47           C  
ANISOU 4671  CG2 VAL B 139     4956   5790   4631    329    447   -164       C  
ATOM   4672  N   HIS B 140       3.802  11.054  31.278  1.00 45.86           N  
ANISOU 4672  N   HIS B 140     5834   6693   4897    416    429   -401       N  
ATOM   4673  CA  HIS B 140       3.499  10.082  30.253  1.00 47.78           C  
ANISOU 4673  CA  HIS B 140     6131   6995   5030    441    435   -516       C  
ATOM   4674  C   HIS B 140       2.264  10.427  29.480  1.00 54.54           C  
ANISOU 4674  C   HIS B 140     7040   7928   5752    440    354   -526       C  
ATOM   4675  O   HIS B 140       1.395   9.598  29.385  1.00 54.27           O  
ANISOU 4675  O   HIS B 140     7027   7894   5698    432    287   -631       O  
ATOM   4676  CB  HIS B 140       3.116   8.796  30.911  1.00 48.26           C  
ANISOU 4676  CB  HIS B 140     6178   6979   5180    431    394   -632       C  
ATOM   4677  CG  HIS B 140       4.187   8.199  31.736  1.00 51.38           C  
ANISOU 4677  CG  HIS B 140     6518   7293   5711    439    459   -639       C  
ATOM   4678  ND1 HIS B 140       5.301   7.618  31.195  1.00 54.07           N  
ANISOU 4678  ND1 HIS B 140     6856   7649   6040    476    564   -676       N  
ATOM   4679  CD2 HIS B 140       4.313   8.078  33.067  1.00 52.17           C  
ANISOU 4679  CD2 HIS B 140     6562   7302   5959    419    433   -611       C  
ATOM   4680  CE1 HIS B 140       6.079   7.180  32.158  1.00 53.05           C  
ANISOU 4680  CE1 HIS B 140     6665   7441   6052    480    597   -666       C  
ATOM   4681  NE2 HIS B 140       5.500   7.438  33.306  1.00 52.26           N  
ANISOU 4681  NE2 HIS B 140     6533   7276   6045    445    516   -627       N  
ATOM   4682  N   ALA B 141       2.235  11.594  28.859  1.00 53.46           N  
ANISOU 4682  N   ALA B 141     6926   7862   5523    451    365   -419       N  
ATOM   4683  CA  ALA B 141       1.107  12.118  28.106  1.00 55.05           C  
ANISOU 4683  CA  ALA B 141     7174   8149   5593    459    287   -399       C  
ATOM   4684  C   ALA B 141       0.753  11.414  26.801  1.00 63.96           C  
ANISOU 4684  C   ALA B 141     8365   9386   6550    484    279   -500       C  
ATOM   4685  O   ALA B 141      -0.268  11.687  26.207  1.00 64.47           O  
ANISOU 4685  O   ALA B 141     8463   9528   6505    490    198   -500       O  
ATOM   4686  CB  ALA B 141       1.341  13.530  27.825  1.00 55.96           C  
ANISOU 4686  CB  ALA B 141     7296   8299   5668    469    317   -246       C  
ATOM   4687  N   THR B 142       1.642  10.562  26.326  1.00 63.15           N  
ANISOU 4687  N   THR B 142     8278   9295   6420    504    367   -583       N  
ATOM   4688  CA  THR B 142       1.472   9.789  25.119  1.00 65.00           C  
ANISOU 4688  CA  THR B 142     8576   9626   6495    529    376   -700       C  
ATOM   4689  C   THR B 142       0.313   8.786  25.102  1.00 69.99           C  
ANISOU 4689  C   THR B 142     9226  10253   7113    504    267   -847       C  
ATOM   4690  O   THR B 142      -0.417   8.656  24.127  1.00 70.90           O  
ANISOU 4690  O   THR B 142     9393  10474   7073    512    211   -906       O  
ATOM   4691  CB  THR B 142       2.749   9.014  24.982  1.00 73.94           C  
ANISOU 4691  CB  THR B 142     9704  10730   7660    553    501   -761       C  
ATOM   4692  OG1 THR B 142       3.828   9.888  25.302  1.00 73.71           O  
ANISOU 4692  OG1 THR B 142     9633  10679   7694    561    594   -624       O  
ATOM   4693  CG2 THR B 142       2.919   8.484  23.609  1.00 73.89           C  
ANISOU 4693  CG2 THR B 142     9769  10836   7470    590    551   -853       C  
ATOM   4694  N   ASN B 143       0.172   8.054  26.199  1.00 65.72           N  
ANISOU 4694  N   ASN B 143     8640   9591   6740    473    239   -906       N  
ATOM   4695  CA  ASN B 143      -0.910   7.092  26.344  1.00 65.69           C  
ANISOU 4695  CA  ASN B 143     8641   9560   6758    439    142  -1039       C  
ATOM   4696  C   ASN B 143      -1.444   7.183  27.760  1.00 67.59           C  
ANISOU 4696  C   ASN B 143     8818   9687   7176    401     79   -995       C  
ATOM   4697  O   ASN B 143      -1.550   6.181  28.467  1.00 66.90           O  
ANISOU 4697  O   ASN B 143     8707   9502   7209    377     69  -1081       O  
ATOM   4698  CB  ASN B 143      -0.418   5.675  26.052  1.00 68.50           C  
ANISOU 4698  CB  ASN B 143     9024   9876   7127    446    199  -1199       C  
ATOM   4699  CG  ASN B 143       1.059   5.499  26.347  1.00 98.91           C  
ANISOU 4699  CG  ASN B 143    12854  13668  11058    479    334  -1168       C  
ATOM   4700  OD1 ASN B 143       1.436   4.974  27.395  1.00 93.19           O  
ANISOU 4700  OD1 ASN B 143    12081  12824  10502    469    355  -1175       O  
ATOM   4701  ND2 ASN B 143       1.904   5.938  25.422  1.00 94.48           N  
ANISOU 4701  ND2 ASN B 143    12326  13197  10377    522    426  -1129       N  
ATOM   4702  N   SER B 144      -1.768   8.404  28.170  1.00 62.62           N  
ANISOU 4702  N   SER B 144     8162   9070   6560    398     42   -857       N  
ATOM   4703  CA  SER B 144      -2.109   8.669  29.547  1.00 60.38           C  
ANISOU 4703  CA  SER B 144     7819   8684   6438    369      1   -798       C  
ATOM   4704  C   SER B 144      -3.584   8.361  29.798  1.00 63.18           C  
ANISOU 4704  C   SER B 144     8160   9037   6809    336   -120   -853       C  
ATOM   4705  O   SER B 144      -4.003   8.173  30.899  1.00 61.65           O  
ANISOU 4705  O   SER B 144     7921   8756   6746    308   -156   -847       O  
ATOM   4706  CB  SER B 144      -1.794  10.085  30.037  1.00 62.05           C  
ANISOU 4706  CB  SER B 144     8006   8887   6683    378     19   -636       C  
ATOM   4707  OG  SER B 144      -2.564  11.074  29.410  1.00 69.06           O  
ANISOU 4707  OG  SER B 144     8916   9861   7462    391    -37   -562       O  
ATOM   4708  N   GLN B 145      -4.357   8.272  28.740  1.00 60.39           N  
ANISOU 4708  N   GLN B 145     7843   8788   6314    338   -181   -909       N  
ATOM   4709  CA  GLN B 145      -5.791   8.197  28.865  1.00 59.92           C  
ANISOU 4709  CA  GLN B 145     7760   8750   6257    308   -302   -940       C  
ATOM   4710  C   GLN B 145      -6.171   6.844  29.335  1.00 62.74           C  
ANISOU 4710  C   GLN B 145     8098   9027   6712    264   -327  -1077       C  
ATOM   4711  O   GLN B 145      -6.991   6.715  30.195  1.00 61.63           O  
ANISOU 4711  O   GLN B 145     7910   8828   6679    231   -389  -1075       O  
ATOM   4712  CB  GLN B 145      -6.522   8.513  27.553  1.00 62.57           C  
ANISOU 4712  CB  GLN B 145     8134   9236   6405    324   -370   -958       C  
ATOM   4713  CG  GLN B 145      -8.056   8.749  27.689  1.00 80.38           C  
ANISOU 4713  CG  GLN B 145    10349  11532   8661    300   -504   -954       C  
ATOM   4714  CD  GLN B 145      -8.930   7.658  27.025  1.00102.90           C  
ANISOU 4714  CD  GLN B 145    13209  14438  11450    262   -589  -1117       C  
ATOM   4715  OE1 GLN B 145      -8.583   6.470  26.980  1.00 98.88           O  
ANISOU 4715  OE1 GLN B 145    12719  13876  10976    235   -556  -1253       O  
ATOM   4716  NE2 GLN B 145     -10.063   8.070  26.517  1.00 97.31           N  
ANISOU 4716  NE2 GLN B 145    12484  13836  10656    261   -699  -1104       N  
ATOM   4717  N   ARG B 146      -5.577   5.811  28.831  1.00 59.23           N  
ANISOU 4717  N   ARG B 146     7691   8569   6245    265   -274  -1196       N  
ATOM   4718  CA  ARG B 146      -6.094   4.570  29.264  1.00 58.67           C  
ANISOU 4718  CA  ARG B 146     7604   8415   6274    219   -308  -1322       C  
ATOM   4719  C   ARG B 146      -5.942   4.424  30.746  1.00 59.63           C  
ANISOU 4719  C   ARG B 146     7670   8401   6587    202   -286  -1267       C  
ATOM   4720  O   ARG B 146      -6.863   4.017  31.383  1.00 59.81           O  
ANISOU 4720  O   ARG B 146     7654   8372   6698    160   -350  -1296       O  
ATOM   4721  CB  ARG B 146      -5.452   3.408  28.506  1.00 60.75           C  
ANISOU 4721  CB  ARG B 146     7920   8668   6493    225   -246  -1470       C  
ATOM   4722  CG  ARG B 146      -5.246   2.206  29.345  1.00 72.89           C  
ANISOU 4722  CG  ARG B 146     9437  10059   8197    198   -212  -1552       C  
ATOM   4723  CD  ARG B 146      -6.368   1.216  29.220  1.00 85.61           C  
ANISOU 4723  CD  ARG B 146    11045  11645   9836    138   -296  -1691       C  
ATOM   4724  NE  ARG B 146      -5.815  -0.124  29.083  1.00 95.50           N  
ANISOU 4724  NE  ARG B 146    12332  12806  11147    133   -229  -1830       N  
ATOM   4725  CZ  ARG B 146      -5.514  -0.677  27.920  1.00110.47           C  
ANISOU 4725  CZ  ARG B 146    14293  14756  12923    146   -202  -1959       C  
ATOM   4726  NH1 ARG B 146      -5.754  -0.021  26.806  1.00 98.71           N  
ANISOU 4726  NH1 ARG B 146    12842  13423  11242    162   -241  -1963       N  
ATOM   4727  NH2 ARG B 146      -4.988  -1.885  27.872  1.00 96.81           N  
ANISOU 4727  NH2 ARG B 146    12593  12926  11262    146   -133  -2083       N  
ATOM   4728  N   PRO B 147      -4.801   4.775  31.298  1.00 53.31           N  
ANISOU 4728  N   PRO B 147     6861   7549   5845    234   -197  -1183       N  
ATOM   4729  CA  PRO B 147      -4.528   4.640  32.720  1.00 50.92           C  
ANISOU 4729  CA  PRO B 147     6508   7127   5713    223   -173  -1128       C  
ATOM   4730  C   PRO B 147      -5.158   5.656  33.668  1.00 50.72           C  
ANISOU 4730  C   PRO B 147     6436   7090   5745    211   -226  -1008       C  
ATOM   4731  O   PRO B 147      -5.532   5.304  34.755  1.00 49.67           O  
ANISOU 4731  O   PRO B 147     6264   6873   5737    186   -246  -1000       O  
ATOM   4732  CB  PRO B 147      -3.010   4.679  32.762  1.00 52.65           C  
ANISOU 4732  CB  PRO B 147     6736   7320   5950    264    -61  -1090       C  
ATOM   4733  CG  PRO B 147      -2.586   5.167  31.482  1.00 58.29           C  
ANISOU 4733  CG  PRO B 147     7497   8144   6506    296    -29  -1089       C  
ATOM   4734  CD  PRO B 147      -3.733   5.550  30.678  1.00 54.86           C  
ANISOU 4734  CD  PRO B 147     7086   7809   5948    281   -119  -1110       C  
ATOM   4735  N   ARG B 148      -5.223   6.905  33.257  1.00 44.70           N  
ANISOU 4735  N   ARG B 148     5682   6409   4893    233   -241   -913       N  
ATOM   4736  CA  ARG B 148      -5.772   7.956  34.066  1.00 42.55           C  
ANISOU 4736  CA  ARG B 148     5373   6125   4669    230   -283   -801       C  
ATOM   4737  C   ARG B 148      -7.228   7.666  34.263  1.00 46.40           C  
ANISOU 4737  C   ARG B 148     5831   6620   5179    197   -380   -844       C  
ATOM   4738  O   ARG B 148      -7.753   7.832  35.315  1.00 44.90           O  
ANISOU 4738  O   ARG B 148     5599   6373   5089    181   -406   -802       O  
ATOM   4739  CB  ARG B 148      -5.642   9.296  33.372  1.00 39.81           C  
ANISOU 4739  CB  ARG B 148     5048   5866   4212    263   -280   -700       C  
ATOM   4740  CG  ARG B 148      -4.292   9.919  33.376  1.00 38.76           C  
ANISOU 4740  CG  ARG B 148     4929   5722   4078    289   -187   -622       C  
ATOM   4741  CD  ARG B 148      -4.321  11.155  32.545  1.00 38.16           C  
ANISOU 4741  CD  ARG B 148     4880   5734   3886    318   -188   -528       C  
ATOM   4742  NE  ARG B 148      -4.853  12.278  33.277  1.00 38.96           N  
ANISOU 4742  NE  ARG B 148     4954   5808   4041    318   -225   -421       N  
ATOM   4743  CZ  ARG B 148      -5.227  13.417  32.744  1.00 50.07           C  
ANISOU 4743  CZ  ARG B 148     6378   7275   5371    343   -246   -328       C  
ATOM   4744  NH1 ARG B 148      -5.139  13.608  31.468  1.00 41.57           N  
ANISOU 4744  NH1 ARG B 148     5345   6299   4152    370   -238   -321       N  
ATOM   4745  NH2 ARG B 148      -5.659  14.375  33.499  1.00 31.16           N  
ANISOU 4745  NH2 ARG B 148     3959   4837   3042    345   -271   -241       N  
ATOM   4746  N   LYS B 149      -7.869   7.211  33.221  1.00 44.20           N  
ANISOU 4746  N   LYS B 149     5575   6417   4803    186   -431   -931       N  
ATOM   4747  CA  LYS B 149      -9.232   6.809  33.303  1.00 44.66           C  
ANISOU 4747  CA  LYS B 149     5598   6488   4883    148   -526   -986       C  
ATOM   4748  C   LYS B 149      -9.403   5.618  34.230  1.00 48.50           C  
ANISOU 4748  C   LYS B 149     6053   6859   5516    104   -517  -1061       C  
ATOM   4749  O   LYS B 149     -10.325   5.542  34.996  1.00 46.82           O  
ANISOU 4749  O   LYS B 149     5789   6610   5390     74   -566  -1048       O  
ATOM   4750  CB  LYS B 149      -9.713   6.449  31.924  1.00 48.79           C  
ANISOU 4750  CB  LYS B 149     6153   7119   5264    142   -580  -1081       C  
ATOM   4751  CG  LYS B 149     -10.849   7.262  31.485  1.00 63.53           C  
ANISOU 4751  CG  LYS B 149     7996   9090   7052    148   -677  -1032       C  
ATOM   4752  CD  LYS B 149     -11.804   6.459  30.688  1.00 74.60           C  
ANISOU 4752  CD  LYS B 149     9394  10561   8392    108   -765  -1160       C  
ATOM   4753  CE  LYS B 149     -12.843   7.348  30.033  1.00 85.03           C  
ANISOU 4753  CE  LYS B 149    10691  12013   9603    127   -865  -1104       C  
ATOM   4754  NZ  LYS B 149     -12.231   8.478  29.308  1.00 92.80           N  
ANISOU 4754  NZ  LYS B 149    11724  13082  10452    193   -833   -996       N  
ATOM   4755  N   LEU B 150      -8.493   4.674  34.147  1.00 46.04           N  
ANISOU 4755  N   LEU B 150     5772   6488   5234    104   -448  -1134       N  
ATOM   4756  CA  LEU B 150      -8.559   3.535  35.007  1.00 45.84           C  
ANISOU 4756  CA  LEU B 150     5722   6344   5350     69   -429  -1194       C  
ATOM   4757  C   LEU B 150      -8.388   3.871  36.464  1.00 47.82           C  
ANISOU 4757  C   LEU B 150     5930   6511   5729     73   -402  -1091       C  
ATOM   4758  O   LEU B 150      -9.105   3.384  37.284  1.00 47.39           O  
ANISOU 4758  O   LEU B 150     5836   6393   5778     38   -429  -1099       O  
ATOM   4759  CB  LEU B 150      -7.498   2.572  34.582  1.00 46.77           C  
ANISOU 4759  CB  LEU B 150     5885   6415   5470     83   -350  -1280       C  
ATOM   4760  CG  LEU B 150      -7.494   1.260  35.314  1.00 51.90           C  
ANISOU 4760  CG  LEU B 150     6519   6935   6264     52   -323  -1351       C  
ATOM   4761  CD1 LEU B 150      -8.416   0.347  34.658  1.00 53.28           C  
ANISOU 4761  CD1 LEU B 150     6703   7114   6426      1   -380  -1488       C  
ATOM   4762  CD2 LEU B 150      -6.118   0.730  35.295  1.00 55.01           C  
ANISOU 4762  CD2 LEU B 150     6944   7272   6685     93   -222  -1368       C  
ATOM   4763  N   LEU B 151      -7.429   4.722  36.768  1.00 42.86           N  
ANISOU 4763  N   LEU B 151     5309   5886   5090    114   -349   -993       N  
ATOM   4764  CA  LEU B 151      -7.221   5.236  38.133  1.00 41.32           C  
ANISOU 4764  CA  LEU B 151     5077   5627   4995    121   -329   -890       C  
ATOM   4765  C   LEU B 151      -8.482   5.858  38.735  1.00 44.50           C  
ANISOU 4765  C   LEU B 151     5438   6044   5426    101   -400   -839       C  
ATOM   4766  O   LEU B 151      -8.826   5.612  39.894  1.00 43.16           O  
ANISOU 4766  O   LEU B 151     5232   5805   5363     85   -401   -812       O  
ATOM   4767  CB  LEU B 151      -6.118   6.313  38.177  1.00 40.78           C  
ANISOU 4767  CB  LEU B 151     5023   5584   4889    161   -276   -794       C  
ATOM   4768  CG  LEU B 151      -4.670   5.916  38.444  1.00 45.21           C  
ANISOU 4768  CG  LEU B 151     5590   6094   5493    185   -190   -788       C  
ATOM   4769  CD1 LEU B 151      -3.853   7.182  38.656  1.00 44.46           C  
ANISOU 4769  CD1 LEU B 151     5492   6025   5376    210   -157   -680       C  
ATOM   4770  CD2 LEU B 151      -4.539   4.967  39.655  1.00 47.47           C  
ANISOU 4770  CD2 LEU B 151     5846   6274   5915    173   -171   -799       C  
ATOM   4771  N   ALA B 152      -9.148   6.688  37.944  1.00 41.57           N  
ANISOU 4771  N   ALA B 152     5072   5767   4955    110   -454   -818       N  
ATOM   4772  CA  ALA B 152     -10.175   7.557  38.473  1.00 40.97           C  
ANISOU 4772  CA  ALA B 152     4957   5713   4898    109   -509   -747       C  
ATOM   4773  C   ALA B 152     -11.546   6.891  38.558  1.00 45.55           C  
ANISOU 4773  C   ALA B 152     5492   6296   5521     67   -579   -808       C  
ATOM   4774  O   ALA B 152     -12.468   7.461  39.123  1.00 45.28           O  
ANISOU 4774  O   ALA B 152     5413   6270   5522     66   -620   -753       O  
ATOM   4775  CB  ALA B 152     -10.239   8.826  37.650  1.00 41.89           C  
ANISOU 4775  CB  ALA B 152     5094   5922   4900    146   -532   -679       C  
ATOM   4776  N   GLU B 153     -11.679   5.689  38.016  1.00 42.90           N  
ANISOU 4776  N   GLU B 153     5165   5949   5188     31   -590   -922       N  
ATOM   4777  CA  GLU B 153     -12.977   5.006  37.945  1.00 43.20           C  
ANISOU 4777  CA  GLU B 153     5156   5994   5265    -20   -661   -993       C  
ATOM   4778  C   GLU B 153     -12.965   3.617  38.597  1.00 46.88           C  
ANISOU 4778  C   GLU B 153     5608   6348   5856    -68   -630  -1067       C  
ATOM   4779  O   GLU B 153     -14.003   3.099  38.981  1.00 46.59           O  
ANISOU 4779  O   GLU B 153     5520   6287   5896   -115   -671  -1098       O  
ATOM   4780  CB  GLU B 153     -13.427   4.931  36.485  1.00 45.72           C  
ANISOU 4780  CB  GLU B 153     5495   6422   5455    -29   -727  -1073       C  
ATOM   4781  CG  GLU B 153     -13.593   6.319  35.869  1.00 56.35           C  
ANISOU 4781  CG  GLU B 153     6849   7880   6681     21   -763   -983       C  
ATOM   4782  CD  GLU B 153     -14.044   6.312  34.413  1.00 81.10           C  
ANISOU 4782  CD  GLU B 153    10004  11140   9671     20   -834  -1049       C  
ATOM   4783  OE1 GLU B 153     -13.848   7.345  33.726  1.00 75.35           O  
ANISOU 4783  OE1 GLU B 153     9303  10501   8824     70   -844   -977       O  
ATOM   4784  OE2 GLU B 153     -14.586   5.284  33.949  1.00 78.54           O  
ANISOU 4784  OE2 GLU B 153     9669  10825   9347    -32   -881  -1173       O  
ATOM   4785  N   LYS B 154     -11.781   3.039  38.758  1.00 43.14           N  
ANISOU 4785  N   LYS B 154     5176   5803   5411    -52   -552  -1087       N  
ATOM   4786  CA  LYS B 154     -11.641   1.696  39.295  1.00 42.95           C  
ANISOU 4786  CA  LYS B 154     5149   5665   5506    -87   -514  -1152       C  
ATOM   4787  C   LYS B 154     -10.742   1.623  40.511  1.00 44.74           C  
ANISOU 4787  C   LYS B 154     5375   5801   5825    -58   -437  -1072       C  
ATOM   4788  O   LYS B 154     -11.071   0.968  41.506  1.00 44.59           O  
ANISOU 4788  O   LYS B 154     5324   5695   5924    -84   -421  -1058       O  
ATOM   4789  CB  LYS B 154     -10.990   0.782  38.250  1.00 46.38           C  
ANISOU 4789  CB  LYS B 154     5638   6089   5895    -91   -486  -1273       C  
ATOM   4790  CG  LYS B 154     -11.668   0.788  36.873  1.00 61.39           C  
ANISOU 4790  CG  LYS B 154     7555   8095   7675   -115   -560  -1370       C  
ATOM   4791  CD  LYS B 154     -12.892  -0.151  36.796  1.00 70.41           C  
ANISOU 4791  CD  LYS B 154     8658   9209   8884   -192   -624  -1472       C  
ATOM   4792  CE  LYS B 154     -12.560  -1.494  36.144  1.00 78.51           C  
ANISOU 4792  CE  LYS B 154     9729  10172   9930   -224   -598  -1624       C  
ATOM   4793  NZ  LYS B 154     -12.025  -2.512  37.105  1.00 85.64           N  
ANISOU 4793  NZ  LYS B 154    10634  10916  10991   -232   -517  -1628       N  
ATOM   4794  N   VAL B 155      -9.628   2.322  40.468  1.00 39.33           N  
ANISOU 4794  N   VAL B 155     4720   5139   5086     -7   -392  -1012       N  
ATOM   4795  CA  VAL B 155      -8.605   2.169  41.492  1.00 37.60           C  
ANISOU 4795  CA  VAL B 155     4501   4842   4944     22   -322   -949       C  
ATOM   4796  C   VAL B 155      -8.906   3.063  42.691  1.00 39.72           C  
ANISOU 4796  C   VAL B 155     4732   5109   5251     31   -333   -836       C  
ATOM   4797  O   VAL B 155      -8.514   2.730  43.798  1.00 39.03           O  
ANISOU 4797  O   VAL B 155     4630   4951   5249     38   -295   -789       O  
ATOM   4798  CB  VAL B 155      -7.184   2.418  40.978  1.00 40.88           C  
ANISOU 4798  CB  VAL B 155     4954   5276   5301     69   -263   -939       C  
ATOM   4799  CG1 VAL B 155      -6.180   2.141  42.071  1.00 39.88           C  
ANISOU 4799  CG1 VAL B 155     4817   5073   5264     96   -200   -879       C  
ATOM   4800  CG2 VAL B 155      -6.904   1.526  39.785  1.00 41.62           C  
ANISOU 4800  CG2 VAL B 155     5089   5374   5350     66   -245  -1058       C  
ATOM   4801  N   VAL B 156      -9.610   4.174  42.488  1.00 35.26           N  
ANISOU 4801  N   VAL B 156     4154   4621   4622     34   -383   -793       N  
ATOM   4802  CA  VAL B 156      -9.957   5.056  43.607  1.00 34.16           C  
ANISOU 4802  CA  VAL B 156     3984   4478   4517     45   -390   -696       C  
ATOM   4803  C   VAL B 156     -10.787   4.356  44.697  1.00 38.41           C  
ANISOU 4803  C   VAL B 156     4480   4952   5164     14   -393   -690       C  
ATOM   4804  O   VAL B 156     -10.646   4.669  45.881  1.00 37.22           O  
ANISOU 4804  O   VAL B 156     4314   4767   5061     27   -369   -617       O  
ATOM   4805  CB  VAL B 156     -10.744   6.307  43.164  1.00 37.48           C  
ANISOU 4805  CB  VAL B 156     4395   4984   4863     56   -444   -655       C  
ATOM   4806  CG1 VAL B 156     -12.144   5.917  42.709  1.00 37.73           C  
ANISOU 4806  CG1 VAL B 156     4390   5048   4896     20   -509   -709       C  
ATOM   4807  CG2 VAL B 156     -10.810   7.314  44.310  1.00 36.26           C  
ANISOU 4807  CG2 VAL B 156     4222   4816   4738     78   -433   -558       C  
ATOM   4808  N   TYR B 157     -11.655   3.428  44.300  1.00 35.79           N  
ANISOU 4808  N   TYR B 157     4128   4604   4867    -30   -422   -766       N  
ATOM   4809  CA  TYR B 157     -12.500   2.698  45.265  1.00 35.33           C  
ANISOU 4809  CA  TYR B 157     4025   4482   4918    -67   -420   -759       C  
ATOM   4810  C   TYR B 157     -11.662   1.668  46.022  1.00 40.32           C  
ANISOU 4810  C   TYR B 157     4672   5011   5636    -64   -354   -754       C  
ATOM   4811  O   TYR B 157     -11.794   1.516  47.230  1.00 40.03           O  
ANISOU 4811  O   TYR B 157     4612   4926   5672    -62   -326   -690       O  
ATOM   4812  CB  TYR B 157     -13.683   2.026  44.555  1.00 36.43           C  
ANISOU 4812  CB  TYR B 157     4132   4634   5076   -124   -474   -845       C  
ATOM   4813  CG  TYR B 157     -14.583   3.012  43.841  1.00 37.13           C  
ANISOU 4813  CG  TYR B 157     4195   4831   5081   -122   -547   -841       C  
ATOM   4814  CD1 TYR B 157     -15.660   3.593  44.490  1.00 38.77           C  
ANISOU 4814  CD1 TYR B 157     4344   5065   5321   -127   -575   -782       C  
ATOM   4815  CD2 TYR B 157     -14.348   3.375  42.528  1.00 37.85           C  
ANISOU 4815  CD2 TYR B 157     4321   5001   5059   -109   -583   -890       C  
ATOM   4816  CE1 TYR B 157     -16.486   4.502  43.845  1.00 39.22           C  
ANISOU 4816  CE1 TYR B 157     4373   5221   5308   -116   -641   -771       C  
ATOM   4817  CE2 TYR B 157     -15.167   4.293  41.873  1.00 38.78           C  
ANISOU 4817  CE2 TYR B 157     4415   5222   5098   -100   -652   -874       C  
ATOM   4818  CZ  TYR B 157     -16.240   4.851  42.541  1.00 44.00           C  
ANISOU 4818  CZ  TYR B 157     5013   5904   5802   -102   -682   -813       C  
ATOM   4819  OH  TYR B 157     -17.065   5.764  41.914  1.00 42.53           O  
ANISOU 4819  OH  TYR B 157     4797   5818   5544    -84   -750   -789       O  
ATOM   4820  N   VAL B 158     -10.777   0.987  45.307  1.00 37.62           N  
ANISOU 4820  N   VAL B 158     4370   4641   5283    -56   -325   -818       N  
ATOM   4821  CA  VAL B 158      -9.944  -0.061  45.900  1.00 37.76           C  
ANISOU 4821  CA  VAL B 158     4401   4558   5386    -45   -261   -816       C  
ATOM   4822  C   VAL B 158      -8.698   0.513  46.588  1.00 41.06           C  
ANISOU 4822  C   VAL B 158     4834   4980   5789     12   -218   -730       C  
ATOM   4823  O   VAL B 158      -8.196  -0.080  47.526  1.00 41.85           O  
ANISOU 4823  O   VAL B 158     4928   5009   5964     29   -175   -685       O  
ATOM   4824  CB  VAL B 158      -9.567  -1.147  44.835  1.00 42.76           C  
ANISOU 4824  CB  VAL B 158     5069   5149   6027    -58   -243   -932       C  
ATOM   4825  CG1 VAL B 158      -8.167  -1.736  45.082  1.00 42.75           C  
ANISOU 4825  CG1 VAL B 158     5097   5082   6064    -11   -170   -919       C  
ATOM   4826  CG2 VAL B 158     -10.644  -2.238  44.786  1.00 43.30           C  
ANISOU 4826  CG2 VAL B 158     5117   5152   6184   -124   -262  -1006       C  
ATOM   4827  N   GLY B 159      -8.209   1.662  46.146  1.00 35.63           N  
ANISOU 4827  N   GLY B 159     4161   4372   5006     41   -232   -703       N  
ATOM   4828  CA  GLY B 159      -7.050   2.284  46.780  1.00 34.30           C  
ANISOU 4828  CA  GLY B 159     3998   4211   4825     85   -198   -626       C  
ATOM   4829  C   GLY B 159      -7.368   3.278  47.886  1.00 37.58           C  
ANISOU 4829  C   GLY B 159     4391   4651   5238     92   -215   -536       C  
ATOM   4830  O   GLY B 159      -6.551   3.514  48.783  1.00 36.83           O  
ANISOU 4830  O   GLY B 159     4292   4542   5161    118   -189   -473       O  
ATOM   4831  N   VAL B 160      -8.551   3.885  47.821  1.00 33.93           N  
ANISOU 4831  N   VAL B 160     3912   4228   4752     70   -260   -533       N  
ATOM   4832  CA  VAL B 160      -8.921   4.941  48.752  1.00 32.67           C  
ANISOU 4832  CA  VAL B 160     3736   4095   4581     81   -274   -458       C  
ATOM   4833  C   VAL B 160     -10.085   4.499  49.596  1.00 35.63           C  
ANISOU 4833  C   VAL B 160     4076   4440   5022     56   -281   -443       C  
ATOM   4834  O   VAL B 160      -9.914   4.275  50.791  1.00 34.77           O  
ANISOU 4834  O   VAL B 160     3957   4294   4959     65   -253   -390       O  
ATOM   4835  CB  VAL B 160      -9.259   6.257  48.026  1.00 36.59           C  
ANISOU 4835  CB  VAL B 160     4242   4668   4994     90   -311   -448       C  
ATOM   4836  CG1 VAL B 160      -9.739   7.289  48.988  1.00 35.88           C  
ANISOU 4836  CG1 VAL B 160     4137   4592   4903    102   -320   -382       C  
ATOM   4837  CG2 VAL B 160      -8.034   6.781  47.272  1.00 36.52           C  
ANISOU 4837  CG2 VAL B 160     4267   4688   4922    114   -292   -448       C  
ATOM   4838  N   TRP B 161     -11.268   4.348  49.000  1.00 32.07           N  
ANISOU 4838  N   TRP B 161     3602   4010   4574     24   -319   -486       N  
ATOM   4839  CA  TRP B 161     -12.479   4.205  49.828  1.00 31.48           C  
ANISOU 4839  CA  TRP B 161     3482   3922   4557      2   -326   -459       C  
ATOM   4840  C   TRP B 161     -12.506   2.949  50.689  1.00 34.39           C  
ANISOU 4840  C   TRP B 161     3836   4207   5023    -19   -284   -450       C  
ATOM   4841  O   TRP B 161     -12.776   3.035  51.881  1.00 33.60           O  
ANISOU 4841  O   TRP B 161     3718   4091   4958    -10   -259   -384       O  
ATOM   4842  CB  TRP B 161     -13.754   4.293  49.003  1.00 30.81           C  
ANISOU 4842  CB  TRP B 161     3362   3883   4463    -30   -379   -505       C  
ATOM   4843  CG  TRP B 161     -14.093   5.686  48.575  1.00 31.60           C  
ANISOU 4843  CG  TRP B 161     3461   4064   4483     -2   -418   -478       C  
ATOM   4844  CD1 TRP B 161     -14.003   6.189  47.319  1.00 34.72           C  
ANISOU 4844  CD1 TRP B 161     3875   4519   4797      7   -458   -512       C  
ATOM   4845  CD2 TRP B 161     -14.582   6.750  49.400  1.00 31.03           C  
ANISOU 4845  CD2 TRP B 161     3369   4016   4404     26   -417   -408       C  
ATOM   4846  NE1 TRP B 161     -14.387   7.497  47.307  1.00 33.91           N  
ANISOU 4846  NE1 TRP B 161     3766   4473   4645     39   -481   -460       N  
ATOM   4847  CE2 TRP B 161     -14.756   7.866  48.572  1.00 34.94           C  
ANISOU 4847  CE2 TRP B 161     3873   4579   4823     52   -456   -400       C  
ATOM   4848  CE3 TRP B 161     -14.877   6.868  50.756  1.00 31.92           C  
ANISOU 4848  CE3 TRP B 161     3462   4101   4564     35   -382   -350       C  
ATOM   4849  CZ2 TRP B 161     -15.225   9.090  49.052  1.00 33.97           C  
ANISOU 4849  CZ2 TRP B 161     3740   4485   4682     87   -460   -341       C  
ATOM   4850  CZ3 TRP B 161     -15.346   8.069  51.230  1.00 33.20           C  
ANISOU 4850  CZ3 TRP B 161     3615   4299   4700     68   -386   -300       C  
ATOM   4851  CH2 TRP B 161     -15.512   9.171  50.381  1.00 33.87           C  
ANISOU 4851  CH2 TRP B 161     3708   4440   4720     94   -424   -297       C  
ATOM   4852  N   ILE B 162     -12.228   1.791  50.106  1.00 30.94           N  
ANISOU 4852  N   ILE B 162     3410   3716   4629    -42   -271   -513       N  
ATOM   4853  CA  ILE B 162     -12.358   0.539  50.860  1.00 31.10           C  
ANISOU 4853  CA  ILE B 162     3416   3644   4755    -64   -229   -501       C  
ATOM   4854  C   ILE B 162     -11.368   0.419  52.022  1.00 34.34           C  
ANISOU 4854  C   ILE B 162     3845   4018   5186    -21   -178   -420       C  
ATOM   4855  O   ILE B 162     -11.778   0.117  53.132  1.00 33.07           O  
ANISOU 4855  O   ILE B 162     3662   3824   5078    -24   -151   -357       O  
ATOM   4856  CB  ILE B 162     -12.303  -0.697  49.958  1.00 35.00           C  
ANISOU 4856  CB  ILE B 162     3923   4076   5301   -100   -224   -595       C  
ATOM   4857  CG1 ILE B 162     -13.659  -0.877  49.290  1.00 35.82           C  
ANISOU 4857  CG1 ILE B 162     3987   4201   5423   -161   -273   -662       C  
ATOM   4858  CG2 ILE B 162     -11.946  -1.953  50.778  1.00 36.31           C  
ANISOU 4858  CG2 ILE B 162     4092   4130   5576   -102   -163   -567       C  
ATOM   4859  CD1 ILE B 162     -13.636  -1.750  48.090  1.00 45.91           C  
ANISOU 4859  CD1 ILE B 162     5283   5448   6711   -199   -289   -780       C  
ATOM   4860  N   PRO B 163     -10.074   0.703  51.776  1.00 31.69           N  
ANISOU 4860  N   PRO B 163     3544   3695   4802     20   -167   -416       N  
ATOM   4861  CA  PRO B 163      -9.109   0.733  52.881  1.00 31.39           C  
ANISOU 4861  CA  PRO B 163     3514   3640   4771     64   -133   -336       C  
ATOM   4862  C   PRO B 163      -9.481   1.741  53.957  1.00 35.84           C  
ANISOU 4862  C   PRO B 163     4066   4256   5298     77   -142   -262       C  
ATOM   4863  O   PRO B 163      -9.413   1.422  55.147  1.00 36.07           O  
ANISOU 4863  O   PRO B 163     4087   4260   5359     92   -114   -194       O  
ATOM   4864  CB  PRO B 163      -7.799   1.132  52.208  1.00 32.64           C  
ANISOU 4864  CB  PRO B 163     3701   3828   4874     98   -132   -356       C  
ATOM   4865  CG  PRO B 163      -7.965   0.829  50.778  1.00 37.16           C  
ANISOU 4865  CG  PRO B 163     4286   4401   5429     75   -146   -450       C  
ATOM   4866  CD  PRO B 163      -9.429   0.893  50.465  1.00 33.12           C  
ANISOU 4866  CD  PRO B 163     3754   3907   4924     28   -183   -486       C  
ATOM   4867  N   ALA B 164      -9.885   2.943  53.541  1.00 32.20           N  
ANISOU 4867  N   ALA B 164     3604   3864   4767     76   -180   -274       N  
ATOM   4868  CA  ALA B 164     -10.349   3.988  54.474  1.00 31.40           C  
ANISOU 4868  CA  ALA B 164     3494   3808   4630     89   -187   -218       C  
ATOM   4869  C   ALA B 164     -11.406   3.453  55.424  1.00 35.43           C  
ANISOU 4869  C   ALA B 164     3973   4292   5199     72   -165   -180       C  
ATOM   4870  O   ALA B 164     -11.366   3.748  56.617  1.00 34.85           O  
ANISOU 4870  O   ALA B 164     3900   4228   5114     94   -144   -117       O  
ATOM   4871  CB  ALA B 164     -10.901   5.187  53.718  1.00 31.85           C  
ANISOU 4871  CB  ALA B 164     3549   3926   4624     87   -228   -243       C  
ATOM   4872  N   LEU B 165     -12.348   2.667  54.897  1.00 32.58           N  
ANISOU 4872  N   LEU B 165     3583   3899   4896     31   -168   -221       N  
ATOM   4873  CA  LEU B 165     -13.378   2.033  55.747  1.00 32.55           C  
ANISOU 4873  CA  LEU B 165     3542   3863   4964      7   -139   -183       C  
ATOM   4874  C   LEU B 165     -12.840   0.896  56.599  1.00 37.09           C  
ANISOU 4874  C   LEU B 165     4126   4364   5603     14    -87   -134       C  
ATOM   4875  O   LEU B 165     -13.195   0.800  57.768  1.00 36.92           O  
ANISOU 4875  O   LEU B 165     4091   4337   5598     23    -52    -62       O  
ATOM   4876  CB  LEU B 165     -14.555   1.546  54.924  1.00 33.01           C  
ANISOU 4876  CB  LEU B 165     3558   3909   5075    -48   -161   -243       C  
ATOM   4877  CG  LEU B 165     -15.654   2.603  54.830  1.00 37.89           C  
ANISOU 4877  CG  LEU B 165     4138   4601   5656    -50   -194   -240       C  
ATOM   4878  CD1 LEU B 165     -16.518   2.384  53.571  1.00 38.83           C  
ANISOU 4878  CD1 LEU B 165     4222   4739   5794    -97   -245   -320       C  
ATOM   4879  CD2 LEU B 165     -16.483   2.570  56.108  1.00 40.90           C  
ANISOU 4879  CD2 LEU B 165     4483   4978   6079    -50   -152   -169       C  
ATOM   4880  N   LEU B 166     -11.976   0.047  56.035  1.00 33.62           N  
ANISOU 4880  N   LEU B 166     3710   3869   5196     15    -78   -168       N  
ATOM   4881  CA  LEU B 166     -11.404  -1.074  56.805  1.00 33.82           C  
ANISOU 4881  CA  LEU B 166     3744   3816   5289     31    -26   -114       C  
ATOM   4882  C   LEU B 166     -10.644  -0.567  58.020  1.00 36.88           C  
ANISOU 4882  C   LEU B 166     4147   4241   5623     84    -11    -24       C  
ATOM   4883  O   LEU B 166     -10.749  -1.147  59.112  1.00 36.62           O  
ANISOU 4883  O   LEU B 166     4108   4176   5628     97     29     55       O  
ATOM   4884  CB  LEU B 166     -10.490  -1.962  55.941  1.00 34.32           C  
ANISOU 4884  CB  LEU B 166     3832   3815   5392     35    -17   -169       C  
ATOM   4885  CG  LEU B 166     -11.221  -2.970  55.029  1.00 39.74           C  
ANISOU 4885  CG  LEU B 166     4507   4429   6163    -22    -14   -253       C  
ATOM   4886  CD1 LEU B 166     -10.244  -3.823  54.228  1.00 39.97           C  
ANISOU 4886  CD1 LEU B 166     4569   4392   6227     -8      4   -312       C  
ATOM   4887  CD2 LEU B 166     -12.172  -3.847  55.850  1.00 42.62           C  
ANISOU 4887  CD2 LEU B 166     4840   4723   6629    -59     26   -204       C  
ATOM   4888  N   LEU B 167      -9.908   0.533  57.819  1.00 32.87           N  
ANISOU 4888  N   LEU B 167     3658   3803   5026    113    -45    -35       N  
ATOM   4889  CA  LEU B 167      -9.083   1.143  58.859  1.00 32.15           C  
ANISOU 4889  CA  LEU B 167     3582   3758   4875    158    -44     32       C  
ATOM   4890  C   LEU B 167      -9.912   1.743  59.978  1.00 35.84           C  
ANISOU 4890  C   LEU B 167     4041   4269   5308    161    -35     86       C  
ATOM   4891  O   LEU B 167      -9.359   2.064  61.004  1.00 35.62           O  
ANISOU 4891  O   LEU B 167     4026   4275   5234    195    -30    144       O  
ATOM   4892  CB  LEU B 167      -8.179   2.245  58.285  1.00 31.63           C  
ANISOU 4892  CB  LEU B 167     3535   3752   4731    176    -83     -3       C  
ATOM   4893  CG  LEU B 167      -7.013   1.914  57.344  1.00 36.25           C  
ANISOU 4893  CG  LEU B 167     4131   4319   5324    189    -87    -44       C  
ATOM   4894  CD1 LEU B 167      -6.349   3.181  56.883  1.00 35.35           C  
ANISOU 4894  CD1 LEU B 167     4028   4270   5132    198   -120    -67       C  
ATOM   4895  CD2 LEU B 167      -5.961   0.981  57.986  1.00 40.19           C  
ANISOU 4895  CD2 LEU B 167     4629   4778   5864    227    -58     11       C  
ATOM   4896  N   THR B 168     -11.220   1.913  59.799  1.00 32.67           N  
ANISOU 4896  N   THR B 168     3615   3872   4927    128    -34     66       N  
ATOM   4897  CA  THR B 168     -12.070   2.428  60.895  1.00 32.67           C  
ANISOU 4897  CA  THR B 168     3603   3911   4900    135    -13    118       C  
ATOM   4898  C   THR B 168     -12.538   1.380  61.912  1.00 38.22           C  
ANISOU 4898  C   THR B 168     4289   4571   5662    133     44    194       C  
ATOM   4899  O   THR B 168     -13.117   1.718  62.945  1.00 38.00           O  
ANISOU 4899  O   THR B 168     4255   4578   5604    146     73    248       O  
ATOM   4900  CB  THR B 168     -13.338   3.110  60.366  1.00 37.96           C  
ANISOU 4900  CB  THR B 168     4242   4612   5570    108    -29     76       C  
ATOM   4901  OG1 THR B 168     -14.241   2.126  59.837  1.00 33.78           O  
ANISOU 4901  OG1 THR B 168     3673   4030   5133     61    -16     54       O  
ATOM   4902  CG2 THR B 168     -12.981   4.126  59.306  1.00 37.19           C  
ANISOU 4902  CG2 THR B 168     4160   4553   5417    112    -82     12       C  
ATOM   4903  N   ILE B 169     -12.330   0.107  61.623  1.00 35.61           N  
ANISOU 4903  N   ILE B 169     3953   4159   5417    116     68    199       N  
ATOM   4904  CA  ILE B 169     -12.748  -0.931  62.562  1.00 36.38           C  
ANISOU 4904  CA  ILE B 169     4038   4205   5581    113    128    281       C  
ATOM   4905  C   ILE B 169     -12.280  -0.626  64.000  1.00 40.65           C  
ANISOU 4905  C   ILE B 169     4601   4797   6046    166    151    376       C  
ATOM   4906  O   ILE B 169     -13.044  -0.817  64.939  1.00 41.09           O  
ANISOU 4906  O   ILE B 169     4643   4860   6110    165    199    444       O  
ATOM   4907  CB  ILE B 169     -12.316  -2.359  62.068  1.00 39.90           C  
ANISOU 4907  CB  ILE B 169     4485   4541   6132     97    152    276       C  
ATOM   4908  CG1 ILE B 169     -13.330  -2.871  61.036  1.00 40.72           C  
ANISOU 4908  CG1 ILE B 169     4556   4589   6325     28    149    198       C  
ATOM   4909  CG2 ILE B 169     -12.187  -3.331  63.236  1.00 40.68           C  
ANISOU 4909  CG2 ILE B 169     4589   4590   6278    121    215    389       C  
ATOM   4910  CD1 ILE B 169     -12.699  -3.556  59.804  1.00 50.56           C  
ANISOU 4910  CD1 ILE B 169     5819   5768   7624     12    129    112       C  
ATOM   4911  N   PRO B 170     -11.030  -0.151  64.171  1.00 36.37           N  
ANISOU 4911  N   PRO B 170     4091   4296   5431    210    118    381       N  
ATOM   4912  CA  PRO B 170     -10.528   0.301  65.478  1.00 36.02           C  
ANISOU 4912  CA  PRO B 170     4069   4320   5296    258    122    454       C  
ATOM   4913  C   PRO B 170     -11.340   1.389  66.151  1.00 39.67           C  
ANISOU 4913  C   PRO B 170     4534   4860   5681    260    126    455       C  
ATOM   4914  O   PRO B 170     -11.560   1.323  67.359  1.00 39.24           O  
ANISOU 4914  O   PRO B 170     4488   4839   5583    286    162    530       O  
ATOM   4915  CB  PRO B 170      -9.159   0.835  65.142  1.00 37.25           C  
ANISOU 4915  CB  PRO B 170     4246   4511   5397    285     69    422       C  
ATOM   4916  CG  PRO B 170      -8.708  -0.043  64.021  1.00 42.02           C  
ANISOU 4916  CG  PRO B 170     4841   5035   6089    271     67    382       C  
ATOM   4917  CD  PRO B 170      -9.924  -0.421  63.241  1.00 37.68           C  
ANISOU 4917  CD  PRO B 170     4270   4431   5617    217     86    332       C  
ATOM   4918  N   ASP B 171     -11.774   2.391  65.398  1.00 36.18           N  
ANISOU 4918  N   ASP B 171     4086   4446   5216    239     93    375       N  
ATOM   4919  CA  ASP B 171     -12.640   3.411  65.966  1.00 36.35           C  
ANISOU 4919  CA  ASP B 171     4106   4528   5176    245    104    371       C  
ATOM   4920  C   ASP B 171     -13.936   2.766  66.371  1.00 40.72           C  
ANISOU 4920  C   ASP B 171     4623   5058   5793    225    165    416       C  
ATOM   4921  O   ASP B 171     -14.480   3.016  67.448  1.00 40.40           O  
ANISOU 4921  O   ASP B 171     4584   5060   5706    246    208    468       O  
ATOM   4922  CB  ASP B 171     -12.892   4.549  64.974  1.00 38.11           C  
ANISOU 4922  CB  ASP B 171     4326   4774   5379    230     58    284       C  
ATOM   4923  CG  ASP B 171     -11.802   5.596  65.020  1.00 54.52           C  
ANISOU 4923  CG  ASP B 171     6445   6899   7372    255     12    253       C  
ATOM   4924  OD1 ASP B 171     -12.106   6.730  65.498  1.00 56.36           O  
ANISOU 4924  OD1 ASP B 171     6694   7181   7538    271      8    237       O  
ATOM   4925  OD2 ASP B 171     -10.636   5.269  64.620  1.00 60.46           O  
ANISOU 4925  OD2 ASP B 171     7209   7634   8128    258    -18    246       O  
ATOM   4926  N   PHE B 172     -14.410   1.900  65.499  1.00 37.94           N  
ANISOU 4926  N   PHE B 172     4235   4636   5545    181    172    394       N  
ATOM   4927  CA  PHE B 172     -15.617   1.150  65.748  1.00 38.37           C  
ANISOU 4927  CA  PHE B 172     4244   4654   5682    148    229    433       C  
ATOM   4928  C   PHE B 172     -15.540   0.312  67.028  1.00 40.81           C  
ANISOU 4928  C   PHE B 172     4563   4948   5996    170    296    545       C  
ATOM   4929  O   PHE B 172     -16.535   0.214  67.745  1.00 41.86           O  
ANISOU 4929  O   PHE B 172     4668   5095   6142    164    355    598       O  
ATOM   4930  CB  PHE B 172     -15.916   0.257  64.546  1.00 40.92           C  
ANISOU 4930  CB  PHE B 172     4532   4895   6119     92    215    381       C  
ATOM   4931  CG  PHE B 172     -17.326  -0.189  64.483  1.00 43.94           C  
ANISOU 4931  CG  PHE B 172     4853   5252   6590     42    254    387       C  
ATOM   4932  CD1 PHE B 172     -17.712  -1.390  65.075  1.00 48.59           C  
ANISOU 4932  CD1 PHE B 172     5420   5774   7268     18    321    461       C  
ATOM   4933  CD2 PHE B 172     -18.283   0.609  63.860  1.00 46.42           C  
ANISOU 4933  CD2 PHE B 172     5124   5611   6903     20    225    327       C  
ATOM   4934  CE1 PHE B 172     -19.043  -1.801  65.026  1.00 50.72           C  
ANISOU 4934  CE1 PHE B 172     5622   6019   7630    -37    359    468       C  
ATOM   4935  CE2 PHE B 172     -19.609   0.220  63.804  1.00 50.24           C  
ANISOU 4935  CE2 PHE B 172     5536   6080   7472    -28    256    334       C  
ATOM   4936  CZ  PHE B 172     -20.002  -0.985  64.390  1.00 49.59           C  
ANISOU 4936  CZ  PHE B 172     5428   5930   7484    -61    324    402       C  
ATOM   4937  N   ILE B 173     -14.379  -0.276  67.327  1.00 34.48           N  
ANISOU 4937  N   ILE B 173     3797   4122   5182    200    290    588       N  
ATOM   4938  CA  ILE B 173     -14.265  -1.162  68.488  1.00 33.91           C  
ANISOU 4938  CA  ILE B 173     3735   4032   5117    227    352    706       C  
ATOM   4939  C   ILE B 173     -14.098  -0.398  69.800  1.00 35.51           C  
ANISOU 4939  C   ILE B 173     3970   4336   5186    280    365    763       C  
ATOM   4940  O   ILE B 173     -14.773  -0.704  70.777  1.00 36.30           O  
ANISOU 4940  O   ILE B 173     4063   4453   5277    290    433    847       O  
ATOM   4941  CB  ILE B 173     -13.086  -2.184  68.354  1.00 37.19           C  
ANISOU 4941  CB  ILE B 173     4173   4379   5577    248    344    743       C  
ATOM   4942  CG1 ILE B 173     -13.391  -3.261  67.299  1.00 37.78           C  
ANISOU 4942  CG1 ILE B 173     4220   4334   5800    195    358    704       C  
ATOM   4943  CG2 ILE B 173     -12.814  -2.861  69.679  1.00 38.55           C  
ANISOU 4943  CG2 ILE B 173     4364   4557   5725    293    398    877       C  
ATOM   4944  CD1 ILE B 173     -12.189  -4.197  66.991  1.00 42.25           C  
ANISOU 4944  CD1 ILE B 173     4810   4826   6419    221    350    722       C  
ATOM   4945  N   PHE B 174     -13.206   0.582  69.836  1.00 29.53           N  
ANISOU 4945  N   PHE B 174     3248   3647   4324    312    304    717       N  
ATOM   4946  CA  PHE B 174     -12.855   1.250  71.092  1.00 28.96           C  
ANISOU 4946  CA  PHE B 174     3215   3672   4119    363    306    762       C  
ATOM   4947  C   PHE B 174     -13.605   2.553  71.375  1.00 33.09           C  
ANISOU 4947  C   PHE B 174     3743   4268   4561    366    308    708       C  
ATOM   4948  O   PHE B 174     -13.486   3.100  72.459  1.00 32.93           O  
ANISOU 4948  O   PHE B 174     3756   4327   4429    404    320    737       O  
ATOM   4949  CB  PHE B 174     -11.359   1.543  71.133  1.00 29.93           C  
ANISOU 4949  CB  PHE B 174     3370   3829   4171    396    237    748       C  
ATOM   4950  CG  PHE B 174     -10.499   0.332  71.093  1.00 31.55           C  
ANISOU 4950  CG  PHE B 174     3573   3977   4437    413    238    815       C  
ATOM   4951  CD1 PHE B 174      -9.797   0.006  69.942  1.00 34.09           C  
ANISOU 4951  CD1 PHE B 174     3883   4237   4835    396    199    760       C  
ATOM   4952  CD2 PHE B 174     -10.357  -0.470  72.216  1.00 34.59           C  
ANISOU 4952  CD2 PHE B 174     3969   4373   4799    452    282    937       C  
ATOM   4953  CE1 PHE B 174      -8.964  -1.114  69.893  1.00 35.55           C  
ANISOU 4953  CE1 PHE B 174     4064   4361   5081    421    205    819       C  
ATOM   4954  CE2 PHE B 174      -9.538  -1.600  72.184  1.00 37.90           C  
ANISOU 4954  CE2 PHE B 174     4386   4733   5283    477    286   1007       C  
ATOM   4955  CZ  PHE B 174      -8.836  -1.926  71.016  1.00 35.56           C  
ANISOU 4955  CZ  PHE B 174     4075   4366   5070    462    248    945       C  
ATOM   4956  N   ALA B 175     -14.334   3.083  70.398  1.00 29.77           N  
ANISOU 4956  N   ALA B 175     3292   3825   4193    330    294    627       N  
ATOM   4957  CA  ALA B 175     -15.173   4.263  70.646  1.00 29.25           C  
ANISOU 4957  CA  ALA B 175     3226   3817   4070    339    307    584       C  
ATOM   4958  C   ALA B 175     -16.374   3.812  71.484  1.00 33.20           C  
ANISOU 4958  C   ALA B 175     3697   4328   4591    341    398    657       C  
ATOM   4959  O   ALA B 175     -17.091   2.908  71.094  1.00 31.94           O  
ANISOU 4959  O   ALA B 175     3487   4108   4542    303    435    687       O  
ATOM   4960  CB  ALA B 175     -15.619   4.924  69.313  1.00 29.27           C  
ANISOU 4960  CB  ALA B 175     3199   3794   4128    306    265    488       C  
ATOM   4961  N   ASN B 176     -16.546   4.427  72.650  1.00 31.31           N  
ANISOU 4961  N   ASN B 176     3488   4165   4242    384    434    684       N  
ATOM   4962  CA  ASN B 176     -17.629   4.116  73.584  1.00 32.23           C  
ANISOU 4962  CA  ASN B 176     3583   4309   4355    395    531    759       C  
ATOM   4963  C   ASN B 176     -17.973   5.357  74.415  1.00 37.76           C  
ANISOU 4963  C   ASN B 176     4317   5098   4933    440    554    726       C  
ATOM   4964  O   ASN B 176     -17.186   6.308  74.482  1.00 37.47           O  
ANISOU 4964  O   ASN B 176     4332   5102   4805    463    494    660       O  
ATOM   4965  CB  ASN B 176     -17.237   2.967  74.535  1.00 31.47           C  
ANISOU 4965  CB  ASN B 176     3504   4210   4244    413    578    881       C  
ATOM   4966  CG  ASN B 176     -17.159   1.621  73.837  1.00 51.27           C  
ANISOU 4966  CG  ASN B 176     5974   6614   6893    369    583    924       C  
ATOM   4967  OD1 ASN B 176     -18.184   1.041  73.477  1.00 41.72           O  
ANISOU 4967  OD1 ASN B 176     4705   5349   5797    327    634    943       O  
ATOM   4968  ND2 ASN B 176     -15.936   1.119  73.634  1.00 44.91           N  
ANISOU 4968  ND2 ASN B 176     5199   5779   6086    379    530    937       N  
ATOM   4969  N   VAL B 177     -19.136   5.325  75.062  1.00 35.67           N  
ANISOU 4969  N   VAL B 177     4021   4861   4671    452    644    772       N  
ATOM   4970  CA  VAL B 177     -19.557   6.397  75.939  1.00 36.54           C  
ANISOU 4970  CA  VAL B 177     4163   5053   4667    500    685    745       C  
ATOM   4971  C   VAL B 177     -19.352   5.999  77.390  1.00 43.52           C  
ANISOU 4971  C   VAL B 177     5093   6005   5436    542    747    836       C  
ATOM   4972  O   VAL B 177     -19.698   4.894  77.800  1.00 44.03           O  
ANISOU 4972  O   VAL B 177     5130   6052   5546    533    813    944       O  
ATOM   4973  CB  VAL B 177     -21.040   6.752  75.739  1.00 40.75           C  
ANISOU 4973  CB  VAL B 177     4628   5585   5268    496    754    732       C  
ATOM   4974  CG1 VAL B 177     -21.406   7.951  76.585  1.00 40.92           C  
ANISOU 4974  CG1 VAL B 177     4689   5685   5172    554    796    691       C  
ATOM   4975  CG2 VAL B 177     -21.329   7.032  74.267  1.00 39.68           C  
ANISOU 4975  CG2 VAL B 177     4440   5388   5248    455    690    655       C  
ATOM   4976  N   SER B 178     -18.793   6.910  78.168  1.00 41.57           N  
ANISOU 4976  N   SER B 178     4918   5837   5040    588    727    793       N  
ATOM   4977  CA  SER B 178     -18.628   6.696  79.587  1.00 43.16           C  
ANISOU 4977  CA  SER B 178     5169   6124   5105    634    781    868       C  
ATOM   4978  C   SER B 178     -19.300   7.840  80.330  1.00 48.49           C  
ANISOU 4978  C   SER B 178     5875   6874   5674    679    836    810       C  
ATOM   4979  O   SER B 178     -19.556   8.895  79.743  1.00 46.61           O  
ANISOU 4979  O   SER B 178     5634   6619   5456    677    808    703       O  
ATOM   4980  CB  SER B 178     -17.139   6.621  79.932  1.00 46.63           C  
ANISOU 4980  CB  SER B 178     5673   6599   5447    649    693    869       C  
ATOM   4981  OG  SER B 178     -16.957   6.639  81.335  1.00 58.26           O  
ANISOU 4981  OG  SER B 178     7202   8175   6759    700    733    924       O  
ATOM   4982  N   GLU B 179     -19.568   7.638  81.611  1.00 48.09           N  
ANISOU 4982  N   GLU B 179     5857   6905   5508    723    917    882       N  
ATOM   4983  CA  GLU B 179     -20.127   8.669  82.473  1.00 49.39           C  
ANISOU 4983  CA  GLU B 179     6064   7152   5550    774    979    828       C  
ATOM   4984  C   GLU B 179     -18.967   9.374  83.077  1.00 55.27           C  
ANISOU 4984  C   GLU B 179     6902   7967   6133    800    900    760       C  
ATOM   4985  O   GLU B 179     -18.063   8.741  83.519  1.00 55.09           O  
ANISOU 4985  O   GLU B 179     6910   7977   6045    804    858    821       O  
ATOM   4986  CB  GLU B 179     -20.907   8.046  83.608  1.00 52.08           C  
ANISOU 4986  CB  GLU B 179     6400   7559   5830    810   1108    944       C  
ATOM   4987  CG  GLU B 179     -22.078   7.239  83.206  1.00 61.85           C  
ANISOU 4987  CG  GLU B 179     7541   8738   7223    780   1199   1028       C  
ATOM   4988  CD  GLU B 179     -23.210   7.397  84.179  1.00 80.55           C  
ANISOU 4988  CD  GLU B 179     9897  11177   9531    825   1341   1075       C  
ATOM   4989  OE1 GLU B 179     -22.987   8.023  85.217  1.00 71.26           O  
ANISOU 4989  OE1 GLU B 179     8800  10099   8178    882   1367   1050       O  
ATOM   4990  OE2 GLU B 179     -24.319   6.907  83.915  1.00 72.05           O  
ANISOU 4990  OE2 GLU B 179     8732  10063   8580    803   1427   1135       O  
ATOM   4991  N   ALA B 180     -18.941  10.684  83.112  1.00 53.25           N  
ANISOU 4991  N   ALA B 180     6689   7731   5812    819    876    632       N  
ATOM   4992  CA  ALA B 180     -17.799  11.220  83.795  1.00 54.01           C  
ANISOU 4992  CA  ALA B 180     6872   7899   5751    836    800    574       C  
ATOM   4993  C   ALA B 180     -17.975  12.619  84.299  1.00 59.97           C  
ANISOU 4993  C   ALA B 180     7691   8698   6398    870    812    445       C  
ATOM   4994  O   ALA B 180     -18.152  13.536  83.517  1.00 59.63           O  
ANISOU 4994  O   ALA B 180     7639   8590   6429    855    785    342       O  
ATOM   4995  CB  ALA B 180     -16.611  11.003  82.980  1.00 53.66           C  
ANISOU 4995  CB  ALA B 180     6821   7804   5764    791    677    555       C  
ATOM   4996  N   ASP B 181     -17.766  12.840  85.572  1.00 57.77           N  
ANISOU 4996  N   ASP B 181     7484   8528   5937    913    839    440       N  
ATOM   4997  CA  ASP B 181     -17.884  14.205  86.048  1.00 58.17           C  
ANISOU 4997  CA  ASP B 181     7604   8613   5885    943    848    300       C  
ATOM   4998  C   ASP B 181     -19.041  15.047  85.528  1.00 60.24           C  
ANISOU 4998  C   ASP B 181     7835   8809   6243    960    923    229       C  
ATOM   4999  O   ASP B 181     -18.934  16.153  85.032  1.00 58.97           O  
ANISOU 4999  O   ASP B 181     7698   8596   6113    953    883    105       O  
ATOM   5000  CB  ASP B 181     -16.506  14.799  85.823  1.00 59.92           C  
ANISOU 5000  CB  ASP B 181     7875   8832   6060    907    707    201       C  
ATOM   5001  CG  ASP B 181     -15.403  14.027  86.624  1.00 73.29           C  
ANISOU 5001  CG  ASP B 181     9602  10622   7623    908    641    273       C  
ATOM   5002  OD1 ASP B 181     -15.431  14.023  87.883  1.00 75.73           O  
ANISOU 5002  OD1 ASP B 181     9971  11049   7755    953    681    289       O  
ATOM   5003  OD2 ASP B 181     -14.521  13.398  85.996  1.00 78.46           O  
ANISOU 5003  OD2 ASP B 181    10221  11241   8350    868    551    320       O  
ATOM   5004  N   ASP B 182     -20.174  14.397  85.671  1.00 56.03           N  
ANISOU 5004  N   ASP B 182     7243   8282   5764    983   1039    327       N  
ATOM   5005  CA  ASP B 182     -21.457  14.962  85.480  1.00 55.31           C  
ANISOU 5005  CA  ASP B 182     7111   8160   5744   1015   1140    297       C  
ATOM   5006  C   ASP B 182     -21.823  15.126  84.043  1.00 55.06           C  
ANISOU 5006  C   ASP B 182     6999   8012   5909    977   1102    275       C  
ATOM   5007  O   ASP B 182     -22.628  15.941  83.730  1.00 54.97           O  
ANISOU 5007  O   ASP B 182     6966   7966   5954   1004   1149    213       O  
ATOM   5008  CB  ASP B 182     -21.537  16.296  86.214  1.00 58.30           C  
ANISOU 5008  CB  ASP B 182     7577   8582   5993   1067   1170    162       C  
ATOM   5009  CG  ASP B 182     -21.324  16.150  87.731  1.00 71.48           C  
ANISOU 5009  CG  ASP B 182     9329  10384   7446   1113   1222    181       C  
ATOM   5010  OD1 ASP B 182     -21.786  15.154  88.296  1.00 73.31           O  
ANISOU 5010  OD1 ASP B 182     9529  10674   7650   1130   1304    314       O  
ATOM   5011  OD2 ASP B 182     -20.691  17.023  88.354  1.00 77.29           O  
ANISOU 5011  OD2 ASP B 182    10161  11167   8039   1130   1181     65       O  
ATOM   5012  N   ARG B 183     -21.263  14.325  83.164  1.00 47.86           N  
ANISOU 5012  N   ARG B 183     6041   7044   5100    918   1020    329       N  
ATOM   5013  CA  ARG B 183     -21.642  14.399  81.774  1.00 45.21           C  
ANISOU 5013  CA  ARG B 183     5628   6609   4943    882    983    313       C  
ATOM   5014  C   ARG B 183     -21.219  13.118  81.140  1.00 46.79           C  
ANISOU 5014  C   ARG B 183     5774   6770   5235    825    933    408       C  
ATOM   5015  O   ARG B 183     -20.511  12.372  81.729  1.00 45.88           O  
ANISOU 5015  O   ARG B 183     5690   6696   5046    818    915    471       O  
ATOM   5016  CB  ARG B 183     -21.071  15.579  81.024  1.00 42.27           C  
ANISOU 5016  CB  ARG B 183     5291   6178   4591    871    894    186       C  
ATOM   5017  CG  ARG B 183     -19.588  15.584  80.870  1.00 44.45           C  
ANISOU 5017  CG  ARG B 183     5623   6449   4816    831    774    150       C  
ATOM   5018  CD  ARG B 183     -19.188  16.493  79.772  1.00 42.92           C  
ANISOU 5018  CD  ARG B 183     5432   6174   4702    804    693     57       C  
ATOM   5019  NE  ARG B 183     -19.388  15.803  78.542  1.00 40.90           N  
ANISOU 5019  NE  ARG B 183     5093   5851   4596    763    662    112       N  
ATOM   5020  CZ  ARG B 183     -19.532  16.365  77.379  1.00 50.45           C  
ANISOU 5020  CZ  ARG B 183     6272   6986   5911    745    621     65       C  
ATOM   5021  NH1 ARG B 183     -19.479  17.652  77.253  1.00 34.47           N  
ANISOU 5021  NH1 ARG B 183     4292   4934   3872    766    608    -32       N  
ATOM   5022  NH2 ARG B 183     -19.704  15.612  76.349  1.00 36.19           N  
ANISOU 5022  NH2 ARG B 183     4393   5133   4223    707    593    118       N  
ATOM   5023  N   TYR B 184     -21.675  12.839  79.941  1.00 41.86           N  
ANISOU 5023  N   TYR B 184     5068   6067   4771    787    912    419       N  
ATOM   5024  CA  TYR B 184     -21.214  11.649  79.257  1.00 40.30           C  
ANISOU 5024  CA  TYR B 184     4826   5822   4665    731    860    492       C  
ATOM   5025  C   TYR B 184     -20.174  11.985  78.221  1.00 40.62           C  
ANISOU 5025  C   TYR B 184     4885   5804   4745    693    736    422       C  
ATOM   5026  O   TYR B 184     -20.421  12.719  77.338  1.00 39.80           O  
ANISOU 5026  O   TYR B 184     4760   5653   4708    685    704    353       O  
ATOM   5027  CB  TYR B 184     -22.346  10.942  78.535  1.00 41.41           C  
ANISOU 5027  CB  TYR B 184     4860   5912   4963    702    910    552       C  
ATOM   5028  CG  TYR B 184     -23.473  10.444  79.362  1.00 44.66           C  
ANISOU 5028  CG  TYR B 184     5226   6366   5374    726   1039    638       C  
ATOM   5029  CD1 TYR B 184     -23.559   9.141  79.747  1.00 47.22           C  
ANISOU 5029  CD1 TYR B 184     5521   6692   5727    702   1085    756       C  
ATOM   5030  CD2 TYR B 184     -24.484  11.275  79.708  1.00 46.26           C  
ANISOU 5030  CD2 TYR B 184     5411   6603   5563    773   1119    603       C  
ATOM   5031  CE1 TYR B 184     -24.588   8.704  80.462  1.00 49.49           C  
ANISOU 5031  CE1 TYR B 184     5764   7016   6023    720   1208    838       C  
ATOM   5032  CE2 TYR B 184     -25.504  10.848  80.400  1.00 48.29           C  
ANISOU 5032  CE2 TYR B 184     5620   6901   5827    795   1239    680       C  
ATOM   5033  CZ  TYR B 184     -25.567   9.567  80.790  1.00 57.44           C  
ANISOU 5033  CZ  TYR B 184     6750   8064   7010    766   1285    800       C  
ATOM   5034  OH  TYR B 184     -26.660   9.192  81.519  1.00 61.48           O  
ANISOU 5034  OH  TYR B 184     7209   8618   7532    787   1419    882       O  
ATOM   5035  N   ILE B 185     -19.012  11.396  78.324  1.00 35.23           N  
ANISOU 5035  N   ILE B 185     4236   5127   4022    671    670    449       N  
ATOM   5036  CA  ILE B 185     -17.963  11.514  77.311  1.00 33.18           C  
ANISOU 5036  CA  ILE B 185     3983   4813   3810    631    560    399       C  
ATOM   5037  C   ILE B 185     -18.043  10.402  76.261  1.00 36.32           C  
ANISOU 5037  C   ILE B 185     4311   5140   4350    583    539    455       C  
ATOM   5038  O   ILE B 185     -18.039   9.225  76.591  1.00 36.80           O  
ANISOU 5038  O   ILE B 185     4351   5200   4433    574    570    550       O  
ATOM   5039  CB  ILE B 185     -16.565  11.399  77.950  1.00 36.02           C  
ANISOU 5039  CB  ILE B 185     4408   5220   4057    633    494    400       C  
ATOM   5040  CG1 ILE B 185     -16.398  12.400  79.110  1.00 36.91           C  
ANISOU 5040  CG1 ILE B 185     4597   5414   4012    676    508    340       C  
ATOM   5041  CG2 ILE B 185     -15.466  11.558  76.883  1.00 35.28           C  
ANISOU 5041  CG2 ILE B 185     4313   5072   4018    592    386    348       C  
ATOM   5042  CD1 ILE B 185     -16.835  13.834  78.794  1.00 39.33           C  
ANISOU 5042  CD1 ILE B 185     4926   5696   4322    688    511    223       C  
ATOM   5043  N   CYS B 186     -18.104  10.772  74.991  1.00 31.54           N  
ANISOU 5043  N   CYS B 186     3673   4472   3840    553    488    397       N  
ATOM   5044  CA  CYS B 186     -17.865   9.832  73.899  1.00 30.31           C  
ANISOU 5044  CA  CYS B 186     3467   4249   3799    505    445    423       C  
ATOM   5045  C   CYS B 186     -16.385  10.009  73.482  1.00 33.23           C  
ANISOU 5045  C   CYS B 186     3882   4607   4137    489    350    382       C  
ATOM   5046  O   CYS B 186     -15.946  11.131  73.187  1.00 32.32           O  
ANISOU 5046  O   CYS B 186     3801   4494   3984    494    302    300       O  
ATOM   5047  CB  CYS B 186     -18.844  10.091  72.756  1.00 29.97           C  
ANISOU 5047  CB  CYS B 186     3359   4158   3869    483    446    388       C  
ATOM   5048  SG  CYS B 186     -18.497   9.368  71.146  1.00 32.97           S  
ANISOU 5048  SG  CYS B 186     3692   4460   4373    424    372    373       S  
ATOM   5049  N   ASP B 187     -15.620   8.905  73.527  1.00 28.72           N  
ANISOU 5049  N   ASP B 187     3308   4022   3581    474    329    443       N  
ATOM   5050  CA  ASP B 187     -14.171   8.915  73.253  1.00 27.53           C  
ANISOU 5050  CA  ASP B 187     3189   3869   3402    464    247    420       C  
ATOM   5051  C   ASP B 187     -13.668   7.497  72.921  1.00 30.67           C  
ANISOU 5051  C   ASP B 187     3558   4221   3872    445    239    492       C  
ATOM   5052  O   ASP B 187     -14.435   6.538  73.077  1.00 30.98           O  
ANISOU 5052  O   ASP B 187     3563   4235   3974    439    301    563       O  
ATOM   5053  CB  ASP B 187     -13.416   9.503  74.454  1.00 29.47           C  
ANISOU 5053  CB  ASP B 187     3498   4195   3505    497    230    411       C  
ATOM   5054  CG  ASP B 187     -12.013   9.927  74.107  1.00 36.08           C  
ANISOU 5054  CG  ASP B 187     4360   5036   4312    483    138    360       C  
ATOM   5055  OD1 ASP B 187     -11.391  10.725  74.858  1.00 36.88           O  
ANISOU 5055  OD1 ASP B 187     4510   5197   4304    498    106    317       O  
ATOM   5056  OD2 ASP B 187     -11.534   9.449  73.071  1.00 39.73           O  
ANISOU 5056  OD2 ASP B 187     4792   5442   4861    455    100    359       O  
ATOM   5057  N   ARG B 188     -12.425   7.367  72.422  1.00 25.96           N  
ANISOU 5057  N   ARG B 188     2974   3610   3281    434    169    473       N  
ATOM   5058  CA  ARG B 188     -11.755   6.036  72.303  1.00 25.68           C  
ANISOU 5058  CA  ARG B 188     2920   3536   3300    431    163    546       C  
ATOM   5059  C   ARG B 188     -11.157   5.609  73.630  1.00 29.94           C  
ANISOU 5059  C   ARG B 188     3490   4140   3746    472    173    627       C  
ATOM   5060  O   ARG B 188     -10.330   6.338  74.169  1.00 30.61           O  
ANISOU 5060  O   ARG B 188     3610   4292   3728    490    123    597       O  
ATOM   5061  CB  ARG B 188     -10.622   6.025  71.270  1.00 24.49           C  
ANISOU 5061  CB  ARG B 188     2764   3350   3192    412     91    499       C  
ATOM   5062  CG  ARG B 188     -11.035   5.452  69.913  1.00 33.78           C  
ANISOU 5062  CG  ARG B 188     3900   4441   4495    374     95    473       C  
ATOM   5063  CD  ARG B 188     -11.506   6.517  68.921  1.00 36.24           C  
ANISOU 5063  CD  ARG B 188     4204   4742   4822    349     69    380       C  
ATOM   5064  NE  ARG B 188     -10.391   7.006  68.096  1.00 44.67           N  
ANISOU 5064  NE  ARG B 188     5284   5804   5885    339      4    323       N  
ATOM   5065  CZ  ARG B 188      -9.717   8.149  68.283  1.00 61.53           C  
ANISOU 5065  CZ  ARG B 188     7450   7983   7944    346    -38    276       C  
ATOM   5066  NH1 ARG B 188     -10.019   9.006  69.271  1.00 49.40           N  
ANISOU 5066  NH1 ARG B 188     5945   6502   6325    366    -27    266       N  
ATOM   5067  NH2 ARG B 188      -8.717   8.451  67.460  1.00 48.49           N  
ANISOU 5067  NH2 ARG B 188     5800   6320   6306    331    -88    234       N  
ATOM   5068  N   PHE B 189     -11.562   4.443  74.149  1.00 25.54           N  
ANISOU 5068  N   PHE B 189     2917   3562   3224    484    234    731       N  
ATOM   5069  CA  PHE B 189     -11.084   3.932  75.457  1.00 25.27           C  
ANISOU 5069  CA  PHE B 189     2911   3593   3097    530    250    830       C  
ATOM   5070  C   PHE B 189     -10.345   2.597  75.311  1.00 28.63           C  
ANISOU 5070  C   PHE B 189     3319   3964   3595    540    246    919       C  
ATOM   5071  O   PHE B 189     -10.895   1.647  74.789  1.00 27.95           O  
ANISOU 5071  O   PHE B 189     3200   3789   3631    518    294    959       O  
ATOM   5072  CB  PHE B 189     -12.256   3.761  76.442  1.00 27.33           C  
ANISOU 5072  CB  PHE B 189     3177   3888   3318    548    344    898       C  
ATOM   5073  CG  PHE B 189     -12.838   5.059  76.917  1.00 28.26           C  
ANISOU 5073  CG  PHE B 189     3323   4078   3336    558    356    823       C  
ATOM   5074  CD1 PHE B 189     -12.247   5.761  77.954  1.00 31.28           C  
ANISOU 5074  CD1 PHE B 189     3760   4563   3562    596    327    810       C  
ATOM   5075  CD2 PHE B 189     -13.960   5.592  76.311  1.00 29.47           C  
ANISOU 5075  CD2 PHE B 189     3448   4196   3553    532    392    763       C  
ATOM   5076  CE1 PHE B 189     -12.766   6.983  78.385  1.00 32.16           C  
ANISOU 5076  CE1 PHE B 189     3905   4731   3584    606    341    729       C  
ATOM   5077  CE2 PHE B 189     -14.490   6.806  76.744  1.00 32.21           C  
ANISOU 5077  CE2 PHE B 189     3822   4600   3815    550    408    694       C  
ATOM   5078  CZ  PHE B 189     -13.893   7.496  77.783  1.00 30.89           C  
ANISOU 5078  CZ  PHE B 189     3716   4526   3495    587    386    674       C  
ATOM   5079  N   TYR B 190      -9.114   2.530  75.807  1.00 25.50           N  
ANISOU 5079  N   TYR B 190     2942   3622   3126    575    189    950       N  
ATOM   5080  CA  TYR B 190      -8.236   1.392  75.549  1.00 25.16           C  
ANISOU 5080  CA  TYR B 190     2878   3525   3155    593    174   1023       C  
ATOM   5081  C   TYR B 190      -7.814   0.714  76.856  1.00 30.11           C  
ANISOU 5081  C   TYR B 190     3524   4216   3699    653    190   1156       C  
ATOM   5082  O   TYR B 190      -7.894   1.330  77.927  1.00 30.58           O  
ANISOU 5082  O   TYR B 190     3618   4384   3616    679    187   1168       O  
ATOM   5083  CB  TYR B 190      -6.966   1.856  74.822  1.00 24.99           C  
ANISOU 5083  CB  TYR B 190     2847   3511   3136    588     82    947       C  
ATOM   5084  CG  TYR B 190      -7.196   2.611  73.545  1.00 24.68           C  
ANISOU 5084  CG  TYR B 190     2795   3423   3159    536     57    822       C  
ATOM   5085  CD1 TYR B 190      -7.647   1.961  72.417  1.00 25.97           C  
ANISOU 5085  CD1 TYR B 190     2929   3481   3459    503     86    802       C  
ATOM   5086  CD2 TYR B 190      -6.927   3.983  73.454  1.00 24.73           C  
ANISOU 5086  CD2 TYR B 190     2819   3490   3087    520      3    723       C  
ATOM   5087  CE1 TYR B 190      -7.858   2.639  71.250  1.00 25.35           C  
ANISOU 5087  CE1 TYR B 190     2839   3367   3424    460     61    695       C  
ATOM   5088  CE2 TYR B 190      -7.133   4.673  72.275  1.00 24.25           C  
ANISOU 5088  CE2 TYR B 190     2747   3383   3082    477    -17    621       C  
ATOM   5089  CZ  TYR B 190      -7.598   3.983  71.175  1.00 31.79           C  
ANISOU 5089  CZ  TYR B 190     3673   4243   4161    450     12    612       C  
ATOM   5090  OH  TYR B 190      -7.808   4.614  69.973  1.00 34.15           O  
ANISOU 5090  OH  TYR B 190     3962   4505   4509    412     -9    519       O  
ATOM   5091  N   PRO B 191      -7.340  -0.543  76.764  1.00 26.92           N  
ANISOU 5091  N   PRO B 191     3102   3747   3381    677    207   1254       N  
ATOM   5092  CA  PRO B 191      -6.715  -1.274  77.879  1.00 27.99           C  
ANISOU 5092  CA  PRO B 191     3251   3938   3448    744    211   1393       C  
ATOM   5093  C   PRO B 191      -5.561  -0.538  78.574  1.00 32.32           C  
ANISOU 5093  C   PRO B 191     3815   4620   3844    782    117   1379       C  
ATOM   5094  O   PRO B 191      -5.422  -0.667  79.771  1.00 32.93           O  
ANISOU 5094  O   PRO B 191     3917   4791   3802    831    120   1470       O  
ATOM   5095  CB  PRO B 191      -6.178  -2.551  77.216  1.00 29.68           C  
ANISOU 5095  CB  PRO B 191     3433   4034   3812    757    224   1458       C  
ATOM   5096  CG  PRO B 191      -7.040  -2.761  76.046  1.00 33.28           C  
ANISOU 5096  CG  PRO B 191     3866   4364   4413    693    269   1384       C  
ATOM   5097  CD  PRO B 191      -7.420  -1.376  75.554  1.00 27.80           C  
ANISOU 5097  CD  PRO B 191     3178   3720   3665    645    229   1238       C  
ATOM   5098  N   ASN B 192      -4.739   0.207  77.838  1.00 28.37           N  
ANISOU 5098  N   ASN B 192     3299   4131   3349    759     34   1268       N  
ATOM   5099  CA  ASN B 192      -3.635   0.965  78.453  1.00 28.57           C  
ANISOU 5099  CA  ASN B 192     3332   4284   3240    783    -62   1241       C  
ATOM   5100  C   ASN B 192      -3.080   2.107  77.586  1.00 33.16           C  
ANISOU 5100  C   ASN B 192     3900   4872   3828    734   -136   1091       C  
ATOM   5101  O   ASN B 192      -3.487   2.301  76.443  1.00 31.81           O  
ANISOU 5101  O   ASN B 192     3715   4609   3762    687   -117   1011       O  
ATOM   5102  CB  ASN B 192      -2.502   0.017  78.890  1.00 27.42           C  
ANISOU 5102  CB  ASN B 192     3160   4165   3093    847    -98   1361       C  
ATOM   5103  CG  ASN B 192      -1.885  -0.761  77.732  1.00 33.36           C  
ANISOU 5103  CG  ASN B 192     3865   4801   4010    845   -101   1363       C  
ATOM   5104  OD1 ASN B 192      -1.620  -0.214  76.670  1.00 24.32           O  
ANISOU 5104  OD1 ASN B 192     2700   3614   2928    800   -133   1249       O  
ATOM   5105  ND2 ASN B 192      -1.639  -2.044  77.951  1.00 24.55           N  
ANISOU 5105  ND2 ASN B 192     2734   3632   2961    899    -63   1497       N  
ATOM   5106  N   ASP B 193      -2.151   2.862  78.147  1.00 31.80           N  
ANISOU 5106  N   ASP B 193     3731   4811   3541    743   -222   1055       N  
ATOM   5107  CA  ASP B 193      -1.587   4.034  77.464  1.00 31.46           C  
ANISOU 5107  CA  ASP B 193     3677   4781   3494    693   -292    918       C  
ATOM   5108  C   ASP B 193      -0.789   3.696  76.177  1.00 32.45           C  
ANISOU 5108  C   ASP B 193     3750   4824   3757    676   -317    892       C  
ATOM   5109  O   ASP B 193      -0.704   4.512  75.284  1.00 31.28           O  
ANISOU 5109  O   ASP B 193     3594   4643   3648    626   -339    784       O  
ATOM   5110  CB  ASP B 193      -0.788   4.894  78.483  1.00 34.99           C  
ANISOU 5110  CB  ASP B 193     4140   5371   3784    701   -379    886       C  
ATOM   5111  CG  ASP B 193       0.538   5.430  77.934  1.00 50.99           C  
ANISOU 5111  CG  ASP B 193     6120   7422   5832    676   -474    818       C  
ATOM   5112  OD1 ASP B 193       0.530   6.307  77.019  1.00 51.97           O  
ANISOU 5112  OD1 ASP B 193     6240   7497   6009    618   -487    703       O  
ATOM   5113  OD2 ASP B 193       1.600   4.998  78.462  1.00 58.35           O  
ANISOU 5113  OD2 ASP B 193     7017   8430   6724    714   -537    884       O  
ATOM   5114  N   LEU B 194      -0.249   2.487  76.056  1.00 27.96           N  
ANISOU 5114  N   LEU B 194     3145   4216   3262    720   -305    992       N  
ATOM   5115  CA  LEU B 194       0.436   2.078  74.812  1.00 26.03           C  
ANISOU 5115  CA  LEU B 194     2853   3887   3151    711   -313    966       C  
ATOM   5116  C   LEU B 194      -0.459   2.106  73.545  1.00 28.87           C  
ANISOU 5116  C   LEU B 194     3220   4126   3623    660   -255    890       C  
ATOM   5117  O   LEU B 194       0.002   2.462  72.456  1.00 27.32           O  
ANISOU 5117  O   LEU B 194     2999   3890   3490    629   -276    812       O  
ATOM   5118  CB  LEU B 194       1.073   0.716  74.983  1.00 26.12           C  
ANISOU 5118  CB  LEU B 194     2831   3868   3226    777   -299   1092       C  
ATOM   5119  CG  LEU B 194       2.131   0.653  76.086  1.00 30.84           C  
ANISOU 5119  CG  LEU B 194     3407   4592   3721    833   -371   1171       C  
ATOM   5120  CD1 LEU B 194       2.605  -0.833  76.347  1.00 30.99           C  
ANISOU 5120  CD1 LEU B 194     3396   4570   3809    913   -343   1323       C  
ATOM   5121  CD2 LEU B 194       3.310   1.617  75.725  1.00 32.13           C  
ANISOU 5121  CD2 LEU B 194     3526   4826   3857    805   -467   1079       C  
ATOM   5122  N   TRP B 195      -1.729   1.731  73.703  1.00 25.68           N  
ANISOU 5122  N   TRP B 195     2846   3671   3240    653   -181    918       N  
ATOM   5123  CA  TRP B 195      -2.711   1.814  72.620  1.00 24.39           C  
ANISOU 5123  CA  TRP B 195     2687   3411   3168    603   -132    846       C  
ATOM   5124  C   TRP B 195      -2.859   3.217  72.028  1.00 26.65           C  
ANISOU 5124  C   TRP B 195     2984   3721   3419    551   -169    718       C  
ATOM   5125  O   TRP B 195      -3.009   3.358  70.830  1.00 23.95           O  
ANISOU 5125  O   TRP B 195     2630   3312   3156    516   -163    650       O  
ATOM   5126  CB  TRP B 195      -4.064   1.323  73.109  1.00 23.57           C  
ANISOU 5126  CB  TRP B 195     2607   3274   3076    601    -53    899       C  
ATOM   5127  CG  TRP B 195      -4.163  -0.150  73.170  1.00 25.32           C  
ANISOU 5127  CG  TRP B 195     2814   3415   3391    631      3   1006       C  
ATOM   5128  CD1 TRP B 195      -3.888  -0.939  74.227  1.00 29.26           C  
ANISOU 5128  CD1 TRP B 195     3318   3943   3855    687     21   1134       C  
ATOM   5129  CD2 TRP B 195      -4.568  -1.017  72.115  1.00 25.13           C  
ANISOU 5129  CD2 TRP B 195     2772   3263   3514    607     50    993       C  
ATOM   5130  NE1 TRP B 195      -4.095  -2.253  73.910  1.00 29.29           N  
ANISOU 5130  NE1 TRP B 195     3309   3835   3986    700     82   1208       N  
ATOM   5131  CE2 TRP B 195      -4.510  -2.330  72.610  1.00 30.03           C  
ANISOU 5131  CE2 TRP B 195     3388   3829   4194    648    100   1116       C  
ATOM   5132  CE3 TRP B 195      -4.962  -0.812  70.793  1.00 25.64           C  
ANISOU 5132  CE3 TRP B 195     2825   3255   3662    554     53    889       C  
ATOM   5133  CZ2 TRP B 195      -4.843  -3.446  71.833  1.00 29.66           C  
ANISOU 5133  CZ2 TRP B 195     3327   3647   4296    633    155   1129       C  
ATOM   5134  CZ3 TRP B 195      -5.294  -1.934  70.008  1.00 27.35           C  
ANISOU 5134  CZ3 TRP B 195     3026   3349   4016    539    103    898       C  
ATOM   5135  CH2 TRP B 195      -5.237  -3.229  70.541  1.00 28.93           C  
ANISOU 5135  CH2 TRP B 195     3224   3488   4282    577    154   1013       C  
ATOM   5136  N   VAL B 196      -2.820   4.239  72.886  1.00 24.49           N  
ANISOU 5136  N   VAL B 196     2738   3543   3024    549   -205    689       N  
ATOM   5137  CA  VAL B 196      -2.778   5.639  72.459  1.00 23.43           C  
ANISOU 5137  CA  VAL B 196     2617   3433   2854    506   -244    574       C  
ATOM   5138  C   VAL B 196      -1.585   5.898  71.554  1.00 28.02           C  
ANISOU 5138  C   VAL B 196     3163   4003   3481    488   -299    526       C  
ATOM   5139  O   VAL B 196      -1.702   6.603  70.563  1.00 26.63           O  
ANISOU 5139  O   VAL B 196     2986   3788   3345    447   -304    444       O  
ATOM   5140  CB  VAL B 196      -2.737   6.633  73.645  1.00 26.72           C  
ANISOU 5140  CB  VAL B 196     3071   3953   3129    510   -279    548       C  
ATOM   5141  CG1 VAL B 196      -2.581   8.077  73.130  1.00 25.97           C  
ANISOU 5141  CG1 VAL B 196     2988   3864   3014    462   -319    427       C  
ATOM   5142  CG2 VAL B 196      -3.979   6.497  74.503  1.00 26.35           C  
ANISOU 5142  CG2 VAL B 196     3060   3922   3030    528   -213    587       C  
ATOM   5143  N   VAL B 197      -0.436   5.315  71.847  1.00 26.94           N  
ANISOU 5143  N   VAL B 197     2993   3901   3344    520   -338    582       N  
ATOM   5144  CA  VAL B 197       0.702   5.568  70.969  1.00 26.96           C  
ANISOU 5144  CA  VAL B 197     2953   3896   3396    503   -382    539       C  
ATOM   5145  C   VAL B 197       0.605   4.807  69.636  1.00 30.87           C  
ANISOU 5145  C   VAL B 197     3425   4287   4018    499   -337    533       C  
ATOM   5146  O   VAL B 197       0.990   5.350  68.580  1.00 29.81           O  
ANISOU 5146  O   VAL B 197     3275   4126   3924    466   -350    462       O  
ATOM   5147  CB  VAL B 197       2.026   5.334  71.655  1.00 31.78           C  
ANISOU 5147  CB  VAL B 197     3522   4586   3965    538   -445    591       C  
ATOM   5148  CG1 VAL B 197       3.172   5.655  70.691  1.00 31.30           C  
ANISOU 5148  CG1 VAL B 197     3409   4519   3965    516   -483    542       C  
ATOM   5149  CG2 VAL B 197       2.122   6.234  72.883  1.00 32.30           C  
ANISOU 5149  CG2 VAL B 197     3614   4763   3895    531   -499    572       C  
ATOM   5150  N   VAL B 198       0.049   3.592  69.681  1.00 27.28           N  
ANISOU 5150  N   VAL B 198     2973   3770   3621    530   -281    603       N  
ATOM   5151  CA  VAL B 198      -0.102   2.779  68.476  1.00 26.44           C  
ANISOU 5151  CA  VAL B 198     2852   3561   3634    525   -236    590       C  
ATOM   5152  C   VAL B 198      -0.991   3.446  67.415  1.00 30.01           C  
ANISOU 5152  C   VAL B 198     3324   3966   4114    470   -216    495       C  
ATOM   5153  O   VAL B 198      -0.593   3.548  66.259  1.00 28.77           O  
ANISOU 5153  O   VAL B 198     3151   3772   4009    452   -220    439       O  
ATOM   5154  CB  VAL B 198      -0.544   1.346  68.816  1.00 30.30           C  
ANISOU 5154  CB  VAL B 198     3342   3985   4187    564   -178    683       C  
ATOM   5155  CG1 VAL B 198      -1.216   0.661  67.631  1.00 29.52           C  
ANISOU 5155  CG1 VAL B 198     3244   3771   4201    539   -124    644       C  
ATOM   5156  CG2 VAL B 198       0.661   0.555  69.292  1.00 30.70           C  
ANISOU 5156  CG2 VAL B 198     3357   4056   4250    625   -198    769       C  
ATOM   5157  N   PHE B 199      -2.151   3.944  67.825  1.00 27.97           N  
ANISOU 5157  N   PHE B 199     3098   3717   3814    449   -197    480       N  
ATOM   5158  CA  PHE B 199      -3.071   4.623  66.905  1.00 27.98           C  
ANISOU 5158  CA  PHE B 199     3114   3682   3835    404   -183    399       C  
ATOM   5159  C   PHE B 199      -2.670   6.048  66.519  1.00 32.67           C  
ANISOU 5159  C   PHE B 199     3716   4319   4379    374   -229    321       C  
ATOM   5160  O   PHE B 199      -2.976   6.505  65.423  1.00 32.59           O  
ANISOU 5160  O   PHE B 199     3708   4274   4402    344   -225    259       O  
ATOM   5161  CB  PHE B 199      -4.512   4.591  67.447  1.00 29.92           C  
ANISOU 5161  CB  PHE B 199     3382   3918   4068    397   -139    416       C  
ATOM   5162  CG  PHE B 199      -5.091   3.226  67.456  1.00 31.90           C  
ANISOU 5162  CG  PHE B 199     3621   4101   4398    407    -85    477       C  
ATOM   5163  CD1 PHE B 199      -5.069   2.453  66.305  1.00 35.30           C  
ANISOU 5163  CD1 PHE B 199     4034   4450   4929    392    -67    452       C  
ATOM   5164  CD2 PHE B 199      -5.634   2.695  68.602  1.00 34.57           C  
ANISOU 5164  CD2 PHE B 199     3969   4454   4713    431    -47    559       C  
ATOM   5165  CE1 PHE B 199      -5.582   1.172  66.309  1.00 36.84           C  
ANISOU 5165  CE1 PHE B 199     4219   4569   5208    396    -16    502       C  
ATOM   5166  CE2 PHE B 199      -6.158   1.429  68.607  1.00 37.77           C  
ANISOU 5166  CE2 PHE B 199     4363   4786   5203    436      8    621       C  
ATOM   5167  CZ  PHE B 199      -6.124   0.662  67.466  1.00 35.97           C  
ANISOU 5167  CZ  PHE B 199     4116   4467   5084    416     23    590       C  
ATOM   5168  N   GLN B 200      -1.998   6.762  67.400  1.00 29.50           N  
ANISOU 5168  N   GLN B 200     3320   3991   3897    381   -272    323       N  
ATOM   5169  CA  GLN B 200      -1.449   8.017  66.988  1.00 29.07           C  
ANISOU 5169  CA  GLN B 200     3269   3963   3814    348   -313    252       C  
ATOM   5170  C   GLN B 200      -0.440   7.748  65.890  1.00 34.09           C  
ANISOU 5170  C   GLN B 200     3868   4572   4515    342   -325    237       C  
ATOM   5171  O   GLN B 200      -0.499   8.411  64.849  1.00 33.80           O  
ANISOU 5171  O   GLN B 200     3834   4508   4501    310   -324    179       O  
ATOM   5172  CB  GLN B 200      -0.786   8.782  68.131  1.00 30.78           C  
ANISOU 5172  CB  GLN B 200     3493   4263   3938    349   -364    248       C  
ATOM   5173  CG  GLN B 200      -0.252  10.152  67.666  1.00 42.77           C  
ANISOU 5173  CG  GLN B 200     5016   5795   5441    305   -403    168       C  
ATOM   5174  CD  GLN B 200      -1.368  11.060  67.156  1.00 55.45           C  
ANISOU 5174  CD  GLN B 200     6661   7359   7050    279   -375    109       C  
ATOM   5175  OE1 GLN B 200      -2.281  11.443  67.904  1.00 50.06           O  
ANISOU 5175  OE1 GLN B 200     6014   6689   6316    287   -357    101       O  
ATOM   5176  NE2 GLN B 200      -1.309  11.389  65.878  1.00 46.38           N  
ANISOU 5176  NE2 GLN B 200     5503   6162   5958    255   -367     73       N  
ATOM   5177  N   PHE B 201       0.467   6.781  66.079  1.00 31.51           N  
ANISOU 5177  N   PHE B 201     3504   4252   4216    376   -331    294       N  
ATOM   5178  CA  PHE B 201       1.466   6.542  65.042  1.00 32.08           C  
ANISOU 5178  CA  PHE B 201     3538   4303   4350    375   -334    278       C  
ATOM   5179  C   PHE B 201       0.833   6.180  63.682  1.00 36.77           C  
ANISOU 5179  C   PHE B 201     4141   4817   5012    360   -288    239       C  
ATOM   5180  O   PHE B 201       1.263   6.690  62.645  1.00 36.35           O  
ANISOU 5180  O   PHE B 201     4079   4756   4978    337   -291    189       O  
ATOM   5181  CB  PHE B 201       2.533   5.520  65.456  1.00 34.77           C  
ANISOU 5181  CB  PHE B 201     3832   4660   4718    424   -344    348       C  
ATOM   5182  CG  PHE B 201       3.840   5.631  64.674  1.00 36.96           C  
ANISOU 5182  CG  PHE B 201     4059   4949   5037    423   -361    330       C  
ATOM   5183  CD1 PHE B 201       4.792   4.640  64.771  1.00 41.26           C  
ANISOU 5183  CD1 PHE B 201     4554   5495   5628    474   -358    389       C  
ATOM   5184  CD2 PHE B 201       4.119   6.713  63.836  1.00 39.51           C  
ANISOU 5184  CD2 PHE B 201     4379   5279   5355    375   -373    260       C  
ATOM   5185  CE1 PHE B 201       6.012   4.715  64.058  1.00 42.44           C  
ANISOU 5185  CE1 PHE B 201     4647   5659   5820    478   -366    375       C  
ATOM   5186  CE2 PHE B 201       5.324   6.787  63.118  1.00 42.69           C  
ANISOU 5186  CE2 PHE B 201     4729   5694   5798    375   -379    249       C  
ATOM   5187  CZ  PHE B 201       6.264   5.777  63.233  1.00 41.28           C  
ANISOU 5187  CZ  PHE B 201     4496   5522   5666    426   -375    305       C  
ATOM   5188  N   GLN B 202      -0.194   5.329  63.701  1.00 33.93           N  
ANISOU 5188  N   GLN B 202     3800   4406   4686    370   -247    260       N  
ATOM   5189  CA  GLN B 202      -0.928   4.950  62.486  1.00 33.84           C  
ANISOU 5189  CA  GLN B 202     3799   4326   4733    351   -211    216       C  
ATOM   5190  C   GLN B 202      -1.652   6.154  61.835  1.00 37.38           C  
ANISOU 5190  C   GLN B 202     4271   4782   5148    310   -221    149       C  
ATOM   5191  O   GLN B 202      -1.611   6.337  60.619  1.00 36.37           O  
ANISOU 5191  O   GLN B 202     4143   4632   5043    292   -215    100       O  
ATOM   5192  CB  GLN B 202      -1.934   3.856  62.829  1.00 35.54           C  
ANISOU 5192  CB  GLN B 202     4025   4487   4993    363   -169    254       C  
ATOM   5193  CG  GLN B 202      -2.697   3.281  61.663  1.00 49.71           C  
ANISOU 5193  CG  GLN B 202     5824   6209   6853    340   -137    207       C  
ATOM   5194  CD  GLN B 202      -3.878   2.456  62.122  1.00 71.57           C  
ANISOU 5194  CD  GLN B 202     8600   8931   9663    335    -99    240       C  
ATOM   5195  OE1 GLN B 202      -3.992   1.268  61.812  1.00 69.35           O  
ANISOU 5195  OE1 GLN B 202     8312   8578   9460    341    -65    252       O  
ATOM   5196  NE2 GLN B 202      -4.762   3.080  62.875  1.00 64.67           N  
ANISOU 5196  NE2 GLN B 202     7738   8093   8741    323   -101    254       N  
ATOM   5197  N   HIS B 203      -2.295   6.980  62.644  1.00 33.98           N  
ANISOU 5197  N   HIS B 203     3863   4387   4660    300   -235    149       N  
ATOM   5198  CA  HIS B 203      -2.941   8.168  62.114  1.00 33.88           C  
ANISOU 5198  CA  HIS B 203     3872   4379   4620    270   -243     94       C  
ATOM   5199  C   HIS B 203      -1.907   9.091  61.409  1.00 37.70           C  
ANISOU 5199  C   HIS B 203     4351   4883   5092    251   -271     57       C  
ATOM   5200  O   HIS B 203      -2.132   9.552  60.280  1.00 36.68           O  
ANISOU 5200  O   HIS B 203     4228   4733   4975    231   -265     18       O  
ATOM   5201  CB AHIS B 203      -3.694   8.931  63.218  0.50 34.84           C  
ANISOU 5201  CB AHIS B 203     4020   4534   4683    270   -248    100       C  
ATOM   5202  CB BHIS B 203      -3.669   8.886  63.256  0.50 34.73           C  
ANISOU 5202  CB BHIS B 203     4006   4521   4670    271   -248    102       C  
ATOM   5203  CG AHIS B 203      -5.083   8.422  63.472  0.50 38.43           C  
ANISOU 5203  CG AHIS B 203     4482   4965   5156    275   -211    117       C  
ATOM   5204  CG BHIS B 203      -4.188  10.240  62.897  0.50 37.85           C  
ANISOU 5204  CG BHIS B 203     4424   4921   5035    249   -258     51       C  
ATOM   5205  ND1AHIS B 203      -5.358   7.098  63.748  0.50 40.59           N  
ANISOU 5205  ND1AHIS B 203     4740   5209   5474    290   -180    167       N  
ATOM   5206  ND1BHIS B 203      -4.051  11.327  63.734  0.50 39.88           N  
ANISOU 5206  ND1BHIS B 203     4705   5215   5232    244   -278     34       N  
ATOM   5207  CD2AHIS B 203      -6.274   9.066  63.506  0.50 40.01           C  
ANISOU 5207  CD2AHIS B 203     4696   5164   5342    267   -197     96       C  
ATOM   5208  CD2BHIS B 203      -4.840  10.688  61.800  0.50 39.34           C  
ANISOU 5208  CD2BHIS B 203     4618   5081   5247    233   -250     14       C  
ATOM   5209  CE1AHIS B 203      -6.658   6.946  63.928  0.50 39.90           C  
ANISOU 5209  CE1AHIS B 203     4654   5105   5401    285   -149    173       C  
ATOM   5210  CE1BHIS B 203      -4.600  12.386  63.168  0.50 39.11           C  
ANISOU 5210  CE1BHIS B 203     4627   5101   5131    229   -277     -9       C  
ATOM   5211  NE2AHIS B 203      -7.235   8.126  63.792  0.50 39.96           N  
ANISOU 5211  NE2AHIS B 203     4677   5134   5372    273   -159    131       N  
ATOM   5212  NE2BHIS B 203      -5.080  12.027  61.990  0.50 39.13           N  
ANISOU 5212  NE2BHIS B 203     4617   5068   5181    224   -262    -16       N  
ATOM   5213  N   ILE B 204      -0.770   9.333  62.061  1.00 34.35           N  
ANISOU 5213  N   ILE B 204     3909   4500   4643    255   -300     74       N  
ATOM   5214  CA  ILE B 204       0.298  10.140  61.459  1.00 34.27           C  
ANISOU 5214  CA  ILE B 204     3881   4507   4631    232   -322     46       C  
ATOM   5215  C   ILE B 204       0.854   9.500  60.177  1.00 38.53           C  
ANISOU 5215  C   ILE B 204     4396   5018   5225    237   -297     39       C  
ATOM   5216  O   ILE B 204       1.308  10.195  59.277  1.00 38.05           O  
ANISOU 5216  O   ILE B 204     4332   4958   5168    215   -296      9       O  
ATOM   5217  CB  ILE B 204       1.466  10.341  62.435  1.00 37.60           C  
ANISOU 5217  CB  ILE B 204     4275   4986   5026    235   -362     68       C  
ATOM   5218  CG1 ILE B 204       1.011  11.122  63.667  1.00 37.69           C  
ANISOU 5218  CG1 ILE B 204     4317   5033   4969    226   -389     59       C  
ATOM   5219  CG2 ILE B 204       2.618  11.048  61.765  1.00 38.18           C  
ANISOU 5219  CG2 ILE B 204     4318   5074   5115    206   -379     43       C  
ATOM   5220  CD1 ILE B 204       2.016  11.068  64.800  1.00 42.03           C  
ANISOU 5220  CD1 ILE B 204     4840   5649   5480    235   -435     85       C  
ATOM   5221  N   MET B 205       0.795   8.177  60.092  1.00 35.07           N  
ANISOU 5221  N   MET B 205     3944   4551   4829    268   -271     66       N  
ATOM   5222  CA  MET B 205       1.390   7.453  58.980  1.00 34.90           C  
ANISOU 5222  CA  MET B 205     3901   4501   4858    280   -243     54       C  
ATOM   5223  C   MET B 205       0.422   7.467  57.781  1.00 35.55           C  
ANISOU 5223  C   MET B 205     4014   4545   4949    262   -219      6       C  
ATOM   5224  O   MET B 205       0.746   8.009  56.720  1.00 35.15           O  
ANISOU 5224  O   MET B 205     3965   4500   4891    246   -212    -27       O  
ATOM   5225  CB  MET B 205       1.765   6.023  59.440  1.00 38.27           C  
ANISOU 5225  CB  MET B 205     4303   4904   5333    325   -224    101       C  
ATOM   5226  CG  MET B 205       2.924   5.376  58.723  1.00 42.96           C  
ANISOU 5226  CG  MET B 205     4859   5488   5976    351   -202    103       C  
ATOM   5227  SD  MET B 205       4.488   6.178  59.153  1.00 48.44           S  
ANISOU 5227  SD  MET B 205     5499   6258   6650    350   -241    126       S  
ATOM   5228  CE  MET B 205       5.622   5.459  57.960  1.00 45.60           C  
ANISOU 5228  CE  MET B 205     5095   5879   6354    381   -195    116       C  
ATOM   5229  N   VAL B 206      -0.776   6.914  57.962  1.00 30.09           N  
ANISOU 5229  N   VAL B 206     3343   3821   4270    263   -207      6       N  
ATOM   5230  CA  VAL B 206      -1.793   6.866  56.897  1.00 28.99           C  
ANISOU 5230  CA  VAL B 206     3224   3652   4138    244   -193    -40       C  
ATOM   5231  C   VAL B 206      -2.328   8.258  56.511  1.00 31.87           C  
ANISOU 5231  C   VAL B 206     3611   4046   4453    218   -214    -66       C  
ATOM   5232  O   VAL B 206      -2.754   8.491  55.386  1.00 30.95           O  
ANISOU 5232  O   VAL B 206     3507   3925   4329    206   -211   -103       O  
ATOM   5233  CB  VAL B 206      -3.010   5.999  57.325  1.00 32.74           C  
ANISOU 5233  CB  VAL B 206     3705   4088   4645    244   -179    -31       C  
ATOM   5234  CG1 VAL B 206      -4.023   5.882  56.184  1.00 32.52           C  
ANISOU 5234  CG1 VAL B 206     3689   4038   4628    220   -174    -84       C  
ATOM   5235  CG2 VAL B 206      -2.555   4.615  57.775  1.00 32.89           C  
ANISOU 5235  CG2 VAL B 206     3708   4067   4722    272   -152      5       C  
ATOM   5236  N   GLY B 207      -2.320   9.176  57.463  1.00 28.60           N  
ANISOU 5236  N   GLY B 207     3204   3660   4004    214   -235    -47       N  
ATOM   5237  CA  GLY B 207      -2.931  10.467  57.280  1.00 28.39           C  
ANISOU 5237  CA  GLY B 207     3201   3646   3941    196   -249    -66       C  
ATOM   5238  C   GLY B 207      -1.979  11.346  56.506  1.00 33.91           C  
ANISOU 5238  C   GLY B 207     3899   4359   4625    181   -255    -80       C  
ATOM   5239  O   GLY B 207      -2.366  11.860  55.451  1.00 35.74           O  
ANISOU 5239  O   GLY B 207     4147   4587   4845    171   -250   -100       O  
ATOM   5240  N   LEU B 208      -0.756  11.530  57.007  1.00 29.36           N  
ANISOU 5240  N   LEU B 208     3303   3804   4049    177   -265    -65       N  
ATOM   5241  CA  LEU B 208       0.165  12.512  56.439  1.00 28.57           C  
ANISOU 5241  CA  LEU B 208     3197   3717   3940    154   -268    -73       C  
ATOM   5242  C   LEU B 208       1.506  12.126  55.821  1.00 32.85           C  
ANISOU 5242  C   LEU B 208     3702   4273   4507    156   -253    -66       C  
ATOM   5243  O   LEU B 208       1.977  12.792  54.889  1.00 32.72           O  
ANISOU 5243  O   LEU B 208     3685   4261   4487    138   -238    -74       O  
ATOM   5244  CB  LEU B 208       0.510  13.334  57.684  1.00 28.40           C  
ANISOU 5244  CB  LEU B 208     3177   3716   3899    139   -299    -67       C  
ATOM   5245  CG  LEU B 208       1.460  14.517  57.457  1.00 32.68           C  
ANISOU 5245  CG  LEU B 208     3711   4267   4440    103   -309    -77       C  
ATOM   5246  CD1 LEU B 208       0.846  15.498  56.467  1.00 32.19           C  
ANISOU 5246  CD1 LEU B 208     3684   4177   4370     88   -292    -90       C  
ATOM   5247  CD2 LEU B 208       1.831  15.228  58.785  1.00 34.18           C  
ANISOU 5247  CD2 LEU B 208     3900   4477   4608     82   -346    -84       C  
ATOM   5248  N   ILE B 209       2.124  11.071  56.342  1.00 29.15           N  
ANISOU 5248  N   ILE B 209     3199   3812   4065    180   -251    -46       N  
ATOM   5249  CA  ILE B 209       3.491  10.728  55.950  1.00 29.13           C  
ANISOU 5249  CA  ILE B 209     3148   3827   4091    188   -237    -35       C  
ATOM   5250  C   ILE B 209       3.484   9.927  54.656  1.00 31.78           C  
ANISOU 5250  C   ILE B 209     3487   4141   4447    208   -192    -54       C  
ATOM   5251  O   ILE B 209       4.235  10.234  53.748  1.00 31.77           O  
ANISOU 5251  O   ILE B 209     3469   4153   4448    201   -167    -61       O  
ATOM   5252  CB  ILE B 209       4.264   9.952  57.031  1.00 32.83           C  
ANISOU 5252  CB  ILE B 209     3574   4317   4583    214   -255      2       C  
ATOM   5253  CG1 ILE B 209       4.757  10.930  58.109  1.00 33.59           C  
ANISOU 5253  CG1 ILE B 209     3654   4455   4651    186   -303     12       C  
ATOM   5254  CG2 ILE B 209       5.458   9.217  56.413  1.00 34.08           C  
ANISOU 5254  CG2 ILE B 209     3680   4483   4786    240   -225     14       C  
ATOM   5255  CD1 ILE B 209       5.269  10.240  59.368  1.00 43.67           C  
ANISOU 5255  CD1 ILE B 209     4897   5766   5930    215   -335     52       C  
ATOM   5256  N   LEU B 210       2.647   8.897  54.577  1.00 27.18           N  
ANISOU 5256  N   LEU B 210     2925   3525   3879    230   -179    -65       N  
ATOM   5257  CA  LEU B 210       2.555   8.085  53.359  1.00 27.12           C  
ANISOU 5257  CA  LEU B 210     2926   3493   3886    246   -140    -98       C  
ATOM   5258  C   LEU B 210       1.931   8.829  52.178  1.00 30.15           C  
ANISOU 5258  C   LEU B 210     3346   3885   4226    223   -133   -133       C  
ATOM   5259  O   LEU B 210       2.469   8.796  51.104  1.00 30.74           O  
ANISOU 5259  O   LEU B 210     3419   3970   4290    228   -102   -152       O  
ATOM   5260  CB  LEU B 210       1.836   6.741  53.623  1.00 27.34           C  
ANISOU 5260  CB  LEU B 210     2963   3472   3951    269   -129   -105       C  
ATOM   5261  CG  LEU B 210       2.630   5.736  54.473  1.00 32.58           C  
ANISOU 5261  CG  LEU B 210     3590   4121   4667    307   -119    -64       C  
ATOM   5262  CD1 LEU B 210       1.794   4.539  54.850  1.00 33.23           C  
ANISOU 5262  CD1 LEU B 210     3688   4146   4792    323   -106    -61       C  
ATOM   5263  CD2 LEU B 210       3.870   5.281  53.753  1.00 35.81           C  
ANISOU 5263  CD2 LEU B 210     3966   4534   5107    335    -82    -70       C  
ATOM   5264  N   PRO B 211       0.795   9.506  52.365  1.00 25.65           N  
ANISOU 5264  N   PRO B 211     2808   3313   3626    203   -161   -137       N  
ATOM   5265  CA  PRO B 211       0.286  10.301  51.240  1.00 25.39           C  
ANISOU 5265  CA  PRO B 211     2804   3294   3547    188   -159   -158       C  
ATOM   5266  C   PRO B 211       1.195  11.459  50.862  1.00 30.38           C  
ANISOU 5266  C   PRO B 211     3430   3953   4159    171   -149   -137       C  
ATOM   5267  O   PRO B 211       1.283  11.804  49.672  1.00 30.47           O  
ANISOU 5267  O   PRO B 211     3459   3982   4138    169   -127   -147       O  
ATOM   5268  CB  PRO B 211      -1.056  10.827  51.749  1.00 26.61           C  
ANISOU 5268  CB  PRO B 211     2983   3441   3685    177   -191   -156       C  
ATOM   5269  CG  PRO B 211      -1.047  10.586  53.221  1.00 30.41           C  
ANISOU 5269  CG  PRO B 211     3449   3911   4194    181   -206   -131       C  
ATOM   5270  CD  PRO B 211      -0.178   9.424  53.466  1.00 26.62           C  
ANISOU 5270  CD  PRO B 211     2941   3421   3754    201   -188   -124       C  
ATOM   5271  N   GLY B 212       1.846  12.056  51.868  1.00 26.67           N  
ANISOU 5271  N   GLY B 212     2938   3489   3706    157   -166   -109       N  
ATOM   5272  CA  GLY B 212       2.853  13.103  51.657  1.00 25.96           C  
ANISOU 5272  CA  GLY B 212     2831   3417   3614    132   -157    -89       C  
ATOM   5273  C   GLY B 212       4.038  12.621  50.834  1.00 28.56           C  
ANISOU 5273  C   GLY B 212     3126   3767   3960    143   -114    -87       C  
ATOM   5274  O   GLY B 212       4.537  13.331  49.932  1.00 28.42           O  
ANISOU 5274  O   GLY B 212     3109   3765   3926    127    -84    -77       O  
ATOM   5275  N   ILE B 213       4.486  11.402  51.116  1.00 24.33           N  
ANISOU 5275  N   ILE B 213     2558   3228   3457    173   -103    -92       N  
ATOM   5276  CA  ILE B 213       5.550  10.806  50.306  1.00 24.44           C  
ANISOU 5276  CA  ILE B 213     2537   3258   3490    194    -54    -94       C  
ATOM   5277  C   ILE B 213       5.134  10.691  48.825  1.00 27.17           C  
ANISOU 5277  C   ILE B 213     2923   3607   3791    203    -14   -126       C  
ATOM   5278  O   ILE B 213       5.941  10.939  47.916  1.00 27.60           O  
ANISOU 5278  O   ILE B 213     2963   3689   3835    204     32   -121       O  
ATOM   5279  CB  ILE B 213       6.026   9.423  50.888  1.00 27.57           C  
ANISOU 5279  CB  ILE B 213     2897   3641   3938    236    -46    -93       C  
ATOM   5280  CG1 ILE B 213       6.884   9.665  52.143  1.00 27.71           C  
ANISOU 5280  CG1 ILE B 213     2859   3680   3990    230    -80    -51       C  
ATOM   5281  CG2 ILE B 213       6.858   8.609  49.863  1.00 27.97           C  
ANISOU 5281  CG2 ILE B 213     2925   3696   4008    271     17   -110       C  
ATOM   5282  CD1 ILE B 213       6.955   8.478  53.049  1.00 33.25           C  
ANISOU 5282  CD1 ILE B 213     3538   4365   4731    271    -92    -34       C  
ATOM   5283  N   VAL B 214       3.879  10.334  48.589  1.00 21.74           N  
ANISOU 5283  N   VAL B 214     2282   2900   3076    208    -32   -157       N  
ATOM   5284  CA  VAL B 214       3.434  10.056  47.249  1.00 21.41           C  
ANISOU 5284  CA  VAL B 214     2277   2869   2987    219     -5   -196       C  
ATOM   5285  C   VAL B 214       3.211  11.367  46.521  1.00 24.92           C  
ANISOU 5285  C   VAL B 214     2750   3344   3374    196     -5   -174       C  
ATOM   5286  O   VAL B 214       3.588  11.509  45.360  1.00 25.17           O  
ANISOU 5286  O   VAL B 214     2794   3407   3363    203     36   -179       O  
ATOM   5287  CB  VAL B 214       2.144   9.170  47.251  1.00 24.94           C  
ANISOU 5287  CB  VAL B 214     2757   3288   3431    227    -31   -241       C  
ATOM   5288  CG1 VAL B 214       1.446   9.201  45.896  1.00 24.89           C  
ANISOU 5288  CG1 VAL B 214     2793   3306   3357    226    -24   -283       C  
ATOM   5289  CG2 VAL B 214       2.473   7.719  47.687  1.00 24.80           C  
ANISOU 5289  CG2 VAL B 214     2717   3231   3476    254    -12   -264       C  
ATOM   5290  N   ILE B 215       2.600  12.329  47.199  1.00 20.44           N  
ANISOU 5290  N   ILE B 215     2195   2767   2805    173    -46   -146       N  
ATOM   5291  CA  ILE B 215       2.385  13.628  46.592  1.00 20.31           C  
ANISOU 5291  CA  ILE B 215     2205   2765   2745    155    -45   -116       C  
ATOM   5292  C   ILE B 215       3.737  14.210  46.200  1.00 26.86           C  
ANISOU 5292  C   ILE B 215     3007   3614   3585    141      2    -81       C  
ATOM   5293  O   ILE B 215       3.962  14.523  45.031  1.00 27.77           O  
ANISOU 5293  O   ILE B 215     3138   3758   3653    145     41    -70       O  
ATOM   5294  CB  ILE B 215       1.569  14.589  47.512  1.00 22.07           C  
ANISOU 5294  CB  ILE B 215     2445   2962   2979    136    -91    -94       C  
ATOM   5295  CG1 ILE B 215       0.099  14.133  47.600  1.00 21.48           C  
ANISOU 5295  CG1 ILE B 215     2396   2879   2886    151   -128   -122       C  
ATOM   5296  CG2 ILE B 215       1.644  16.005  47.018  1.00 22.18           C  
ANISOU 5296  CG2 ILE B 215     2480   2977   2970    117    -80    -52       C  
ATOM   5297  CD1 ILE B 215      -0.715  14.780  48.783  1.00 23.01           C  
ANISOU 5297  CD1 ILE B 215     2598   3045   3102    142   -168   -109       C  
ATOM   5298  N   LEU B 216       4.649  14.325  47.156  1.00 24.53           N  
ANISOU 5298  N   LEU B 216     2664   3309   3348    123     -2    -64       N  
ATOM   5299  CA  LEU B 216       5.963  14.905  46.868  1.00 25.37           C  
ANISOU 5299  CA  LEU B 216     2729   3434   3477    102     40    -30       C  
ATOM   5300  C   LEU B 216       6.745  14.110  45.830  1.00 29.63           C  
ANISOU 5300  C   LEU B 216     3248   4007   4004    131    104    -40       C  
ATOM   5301  O   LEU B 216       7.365  14.716  44.965  1.00 29.91           O  
ANISOU 5301  O   LEU B 216     3278   4067   4020    120    154    -11       O  
ATOM   5302  CB  LEU B 216       6.806  15.088  48.139  1.00 25.53           C  
ANISOU 5302  CB  LEU B 216     2692   3446   3563     76     13    -16       C  
ATOM   5303  CG  LEU B 216       6.155  16.097  49.107  1.00 29.65           C  
ANISOU 5303  CG  LEU B 216     3240   3936   4091     43    -40    -10       C  
ATOM   5304  CD1 LEU B 216       6.757  15.947  50.522  1.00 29.90           C  
ANISOU 5304  CD1 LEU B 216     3223   3969   4170     27    -82    -13       C  
ATOM   5305  CD2 LEU B 216       6.234  17.537  48.572  1.00 30.63           C  
ANISOU 5305  CD2 LEU B 216     3386   4045   4207      4    -21     23       C  
ATOM   5306  N   SER B 217       6.710  12.780  45.891  1.00 26.19           N  
ANISOU 5306  N   SER B 217     2803   3569   3579    169    108    -80       N  
ATOM   5307  CA  SER B 217       7.399  11.979  44.872  1.00 26.82           C  
ANISOU 5307  CA  SER B 217     2870   3676   3646    203    175   -102       C  
ATOM   5308  C   SER B 217       6.904  12.304  43.454  1.00 31.70           C  
ANISOU 5308  C   SER B 217     3544   4323   4175    209    208   -112       C  
ATOM   5309  O   SER B 217       7.724  12.539  42.550  1.00 31.50           O  
ANISOU 5309  O   SER B 217     3508   4336   4127    215    274    -93       O  
ATOM   5310  CB  SER B 217       7.275  10.478  45.153  1.00 29.88           C  
ANISOU 5310  CB  SER B 217     3250   4039   4063    245    175   -150       C  
ATOM   5311  OG  SER B 217       7.823  10.192  46.427  1.00 37.33           O  
ANISOU 5311  OG  SER B 217     4139   4964   5081    246    147   -127       O  
ATOM   5312  N   CYS B 218       5.580  12.334  43.268  1.00 28.41           N  
ANISOU 5312  N   CYS B 218     3187   3899   3710    210    164   -137       N  
ATOM   5313  CA  CYS B 218       4.976  12.675  41.960  1.00 28.86           C  
ANISOU 5313  CA  CYS B 218     3299   3994   3671    218    179   -144       C  
ATOM   5314  C   CYS B 218       5.440  14.050  41.477  1.00 35.80           C  
ANISOU 5314  C   CYS B 218     4180   4896   4524    195    210    -72       C  
ATOM   5315  O   CYS B 218       5.795  14.217  40.326  1.00 35.65           O  
ANISOU 5315  O   CYS B 218     4180   4924   4442    207    265    -59       O  
ATOM   5316  CB  CYS B 218       3.441  12.652  42.022  1.00 28.26           C  
ANISOU 5316  CB  CYS B 218     3270   3908   3559    217    113   -170       C  
ATOM   5317  SG  CYS B 218       2.697  11.016  42.198  1.00 31.82           S  
ANISOU 5317  SG  CYS B 218     3731   4334   4027    238     86   -260       S  
ATOM   5318  N   TYR B 219       5.436  15.028  42.371  1.00 34.95           N  
ANISOU 5318  N   TYR B 219     4057   4755   4466    160    178    -26       N  
ATOM   5319  CA  TYR B 219       5.878  16.374  42.024  1.00 36.57           C  
ANISOU 5319  CA  TYR B 219     4265   4964   4666    131    208     44       C  
ATOM   5320  C   TYR B 219       7.398  16.445  41.842  1.00 42.71           C  
ANISOU 5320  C   TYR B 219     4983   5760   5485    117    277     73       C  
ATOM   5321  O   TYR B 219       7.881  17.234  41.042  1.00 43.25           O  
ANISOU 5321  O   TYR B 219     5056   5850   5528    104    332    126       O  
ATOM   5322  CB  TYR B 219       5.367  17.393  43.049  1.00 37.96           C  
ANISOU 5322  CB  TYR B 219     4447   5088   4887     97    153     72       C  
ATOM   5323  CG  TYR B 219       3.853  17.664  42.956  1.00 40.66           C  
ANISOU 5323  CG  TYR B 219     4848   5420   5181    113    100     65       C  
ATOM   5324  CD1 TYR B 219       3.147  17.429  41.778  1.00 43.31           C  
ANISOU 5324  CD1 TYR B 219     5227   5800   5428    146    106     59       C  
ATOM   5325  CD2 TYR B 219       3.138  18.197  44.029  1.00 40.94           C  
ANISOU 5325  CD2 TYR B 219     4891   5408   5257     98     45     66       C  
ATOM   5326  CE1 TYR B 219       1.792  17.693  41.678  1.00 43.48           C  
ANISOU 5326  CE1 TYR B 219     5290   5821   5411    162     54     57       C  
ATOM   5327  CE2 TYR B 219       1.769  18.465  43.918  1.00 41.41           C  
ANISOU 5327  CE2 TYR B 219     4994   5462   5278    118      3     65       C  
ATOM   5328  CZ  TYR B 219       1.119  18.202  42.737  1.00 47.73           C  
ANISOU 5328  CZ  TYR B 219     5828   6309   5999    149      5     63       C  
ATOM   5329  OH  TYR B 219      -0.218  18.447  42.574  1.00 48.00           O  
ANISOU 5329  OH  TYR B 219     5894   6348   5997    171    -41     64       O  
ATOM   5330  N   CYS B 220       8.138  15.597  42.545  1.00 40.30           N  
ANISOU 5330  N   CYS B 220     4619   5450   5243    123    278     44       N  
ATOM   5331  CA  CYS B 220       9.558  15.420  42.259  1.00 41.93           C  
ANISOU 5331  CA  CYS B 220     4759   5685   5487    122    348     64       C  
ATOM   5332  C   CYS B 220       9.814  14.862  40.854  1.00 45.78           C  
ANISOU 5332  C   CYS B 220     5268   6224   5902    164    426     50       C  
ATOM   5333  O   CYS B 220      10.744  15.280  40.198  1.00 46.26           O  
ANISOU 5333  O   CYS B 220     5298   6318   5962    156    500     92       O  
ATOM   5334  CB  CYS B 220      10.224  14.508  43.298  1.00 43.08           C  
ANISOU 5334  CB  CYS B 220     4835   5819   5713    134    328     37       C  
ATOM   5335  SG  CYS B 220      11.829  13.863  42.776  1.00 48.61           S  
ANISOU 5335  SG  CYS B 220     5451   6563   6454    160    420     47       S  
ATOM   5336  N   ILE B 221       8.993  13.917  40.398  1.00 41.37           N  
ANISOU 5336  N   ILE B 221     4761   5674   5284    205    413    -13       N  
ATOM   5337  CA  ILE B 221       9.116  13.382  39.031  1.00 41.03           C  
ANISOU 5337  CA  ILE B 221     4751   5684   5155    245    481    -41       C  
ATOM   5338  C   ILE B 221       8.628  14.400  37.987  1.00 44.33           C  
ANISOU 5338  C   ILE B 221     5228   6140   5474    236    498      6       C  
ATOM   5339  O   ILE B 221       9.173  14.461  36.885  1.00 45.14           O  
ANISOU 5339  O   ILE B 221     5340   6298   5512    255    577     22       O  
ATOM   5340  CB  ILE B 221       8.317  12.078  38.840  1.00 43.62           C  
ANISOU 5340  CB  ILE B 221     5121   6005   5449    285    454   -133       C  
ATOM   5341  CG1 ILE B 221       8.723  11.026  39.870  1.00 43.48           C  
ANISOU 5341  CG1 ILE B 221     5051   5940   5529    301    440   -171       C  
ATOM   5342  CG2 ILE B 221       8.520  11.524  37.434  1.00 45.17           C  
ANISOU 5342  CG2 ILE B 221     5354   6259   5551    325    527   -176       C  
ATOM   5343  CD1 ILE B 221       7.545  10.271  40.431  1.00 48.39           C  
ANISOU 5343  CD1 ILE B 221     5710   6518   6160    306    366   -228       C  
ATOM   5344  N   ILE B 222       7.602  15.189  38.314  1.00 38.82           N  
ANISOU 5344  N   ILE B 222     4571   5418   4762    213    429     31       N  
ATOM   5345  CA  ILE B 222       7.115  16.183  37.362  1.00 38.35           C  
ANISOU 5345  CA  ILE B 222     4565   5391   4613    211    442     89       C  
ATOM   5346  C   ILE B 222       8.233  17.176  37.073  1.00 43.86           C  
ANISOU 5346  C   ILE B 222     5229   6098   5339    183    519    176       C  
ATOM   5347  O   ILE B 222       8.704  17.255  35.960  1.00 43.88           O  
ANISOU 5347  O   ILE B 222     5245   6156   5269    202    595    203       O  
ATOM   5348  CB  ILE B 222       5.827  16.903  37.836  1.00 39.83           C  
ANISOU 5348  CB  ILE B 222     4794   5544   4796    197    357    107       C  
ATOM   5349  CG1 ILE B 222       4.615  15.963  37.711  1.00 38.69           C  
ANISOU 5349  CG1 ILE B 222     4689   5413   4597    227    293     28       C  
ATOM   5350  CG2 ILE B 222       5.581  18.159  37.008  1.00 41.03           C  
ANISOU 5350  CG2 ILE B 222     4988   5717   4884    193    379    194       C  
ATOM   5351  CD1 ILE B 222       3.363  16.447  38.418  1.00 35.39           C  
ANISOU 5351  CD1 ILE B 222     4292   4957   4198    216    207     35       C  
ATOM   5352  N   ILE B 223       8.686  17.887  38.099  1.00 41.78           N  
ANISOU 5352  N   ILE B 223     4917   5777   5180    136    500    215       N  
ATOM   5353  CA  ILE B 223       9.692  18.941  37.940  1.00 42.63           C  
ANISOU 5353  CA  ILE B 223     4987   5879   5333     94    565    299       C  
ATOM   5354  C   ILE B 223      10.948  18.449  37.196  1.00 47.88           C  
ANISOU 5354  C   ILE B 223     5601   6600   5991    109    667    307       C  
ATOM   5355  O   ILE B 223      11.553  19.207  36.456  1.00 48.73           O  
ANISOU 5355  O   ILE B 223     5703   6731   6082     93    744    381       O  
ATOM   5356  CB  ILE B 223      10.078  19.609  39.311  1.00 45.41           C  
ANISOU 5356  CB  ILE B 223     5284   6160   5810     34    521    315       C  
ATOM   5357  CG1 ILE B 223      10.828  18.628  40.205  1.00 45.50           C  
ANISOU 5357  CG1 ILE B 223     5219   6171   5898     35    505    259       C  
ATOM   5358  CG2 ILE B 223       8.856  20.132  40.053  1.00 45.01           C  
ANISOU 5358  CG2 ILE B 223     5284   6054   5765     24    431    305       C  
ATOM   5359  CD1 ILE B 223      12.314  18.590  39.921  1.00 53.82           C  
ANISOU 5359  CD1 ILE B 223     6189   7258   7003     19    589    291       C  
ATOM   5360  N   SER B 224      11.323  17.190  37.377  1.00 44.72           N  
ANISOU 5360  N   SER B 224     5167   6219   5607    144    674    235       N  
ATOM   5361  CA  SER B 224      12.486  16.612  36.685  1.00 45.66           C  
ANISOU 5361  CA  SER B 224     5235   6391   5721    170    776    234       C  
ATOM   5362  C   SER B 224      12.252  16.359  35.191  1.00 51.52           C  
ANISOU 5362  C   SER B 224     6044   7205   6326    218    844    228       C  
ATOM   5363  O   SER B 224      13.188  16.434  34.400  1.00 52.70           O  
ANISOU 5363  O   SER B 224     6165   7404   6454    229    948    265       O  
ATOM   5364  CB  SER B 224      12.898  15.286  37.342  1.00 48.57           C  
ANISOU 5364  CB  SER B 224     5551   6751   6152    203    762    158       C  
ATOM   5365  OG  SER B 224      13.855  14.595  36.542  1.00 58.45           O  
ANISOU 5365  OG  SER B 224     6767   8055   7386    246    865    144       O  
ATOM   5366  N   LYS B 225      11.027  15.990  34.824  1.00 48.00           N  
ANISOU 5366  N   LYS B 225     5683   6770   5787    248    787    177       N  
ATOM   5367  CA  LYS B 225      10.624  15.831  33.418  1.00 48.82           C  
ANISOU 5367  CA  LYS B 225     5860   6949   5740    290    832    167       C  
ATOM   5368  C   LYS B 225      10.675  17.190  32.707  1.00 54.23           C  
ANISOU 5368  C   LYS B 225     6572   7661   6370    268    876    281       C  
ATOM   5369  O   LYS B 225      11.070  17.282  31.534  1.00 55.11           O  
ANISOU 5369  O   LYS B 225     6709   7846   6383    295    964    313       O  
ATOM   5370  CB  LYS B 225       9.202  15.244  33.338  1.00 50.37           C  
ANISOU 5370  CB  LYS B 225     6130   7147   5861    314    739     89       C  
ATOM   5371  CG  LYS B 225       8.577  15.172  31.936  1.00 61.45           C  
ANISOU 5371  CG  LYS B 225     7617   8636   7097    353    758     74       C  
ATOM   5372  CD  LYS B 225       9.331  14.229  31.016  1.00 71.17           C  
ANISOU 5372  CD  LYS B 225     8851   9930   8261    398    852     13       C  
ATOM   5373  CE  LYS B 225       8.500  13.845  29.805  1.00 81.82           C  
ANISOU 5373  CE  LYS B 225    10289  11362   9439    437    841    -43       C  
ATOM   5374  NZ  LYS B 225       9.212  12.879  28.922  1.00 93.21           N  
ANISOU 5374  NZ  LYS B 225    11742  12863  10811    484    937   -119       N  
ATOM   5375  N   LEU B 226      10.291  18.236  33.440  1.00 50.52           N  
ANISOU 5375  N   LEU B 226     6099   7128   5967    222    818    344       N  
ATOM   5376  CA  LEU B 226      10.307  19.608  32.941  1.00 51.10           C  
ANISOU 5376  CA  LEU B 226     6198   7202   6017    196    854    461       C  
ATOM   5377  C   LEU B 226      11.701  20.243  32.912  1.00 56.56           C  
ANISOU 5377  C   LEU B 226     6817   7885   6789    155    955    540       C  
ATOM   5378  O   LEU B 226      11.822  21.408  32.557  1.00 57.48           O  
ANISOU 5378  O   LEU B 226     6947   7988   6906    126    994    644       O  
ATOM   5379  CB  LEU B 226       9.379  20.485  33.786  1.00 50.31           C  
ANISOU 5379  CB  LEU B 226     6121   7024   5971    163    760    491       C  
ATOM   5380  CG  LEU B 226       7.901  20.091  33.882  1.00 54.27           C  
ANISOU 5380  CG  LEU B 226     6686   7527   6407    197    657    431       C  
ATOM   5381  CD1 LEU B 226       7.157  21.073  34.793  1.00 53.59           C  
ANISOU 5381  CD1 LEU B 226     6610   7358   6393    164    582    470       C  
ATOM   5382  CD2 LEU B 226       7.235  20.007  32.492  1.00 57.49           C  
ANISOU 5382  CD2 LEU B 226     7169   8025   6649    249    671    444       C  
ATOM   5383  N   SER B 227      12.746  19.495  33.262  1.00 53.08           N  
ANISOU 5383  N   SER B 227     6296   7453   6421    153    998    497       N  
ATOM   5384  CA  SER B 227      14.101  20.039  33.322  1.00 53.41           C  
ANISOU 5384  CA  SER B 227     6249   7490   6554    109   1088    568       C  
ATOM   5385  C   SER B 227      14.949  19.672  32.108  1.00 58.84           C  
ANISOU 5385  C   SER B 227     6924   8266   7166    148   1220    591       C  
ATOM   5386  O   SER B 227      16.033  20.238  31.915  1.00 59.57           O  
ANISOU 5386  O   SER B 227     6948   8368   7319    113   1312    667       O  
ATOM   5387  CB  SER B 227      14.816  19.564  34.595  1.00 55.92           C  
ANISOU 5387  CB  SER B 227     6467   7762   7017     78   1050    519       C  
ATOM   5388  OG  SER B 227      15.235  18.212  34.491  1.00 63.45           O  
ANISOU 5388  OG  SER B 227     7388   8760   7959    134   1076    438       O  
ATOM   5389  N   HIS B 228      14.495  18.710  31.307  1.00 55.43           N  
ANISOU 5389  N   HIS B 228     6553   7901   6607    218   1232    520       N  
ATOM   5390  CA  HIS B 228      15.232  18.362  30.080  1.00 56.55           C  
ANISOU 5390  CA  HIS B 228     6696   8134   6656    263   1364    535       C  
ATOM   5391  C   HIS B 228      14.976  19.425  28.999  1.00 59.82           C  
ANISOU 5391  C   HIS B 228     7178   8594   6958    260   1421    646       C  
ATOM   5392  O   HIS B 228      15.877  19.776  28.235  1.00 60.64           O  
ANISOU 5392  O   HIS B 228     7254   8750   7038    261   1547    721       O  
ATOM   5393  CB  HIS B 228      14.895  16.941  29.603  1.00 57.64           C  
ANISOU 5393  CB  HIS B 228     6878   8323   6698    337   1362    409       C  
ATOM   5394  CG  HIS B 228      15.484  15.861  30.468  1.00 60.77           C  
ANISOU 5394  CG  HIS B 228     7196   8684   7211    350   1349    323       C  
ATOM   5395  ND1 HIS B 228      16.791  15.435  30.347  1.00 63.44           N  
ANISOU 5395  ND1 HIS B 228     7444   9049   7610    368   1456    327       N  
ATOM   5396  CD2 HIS B 228      14.945  15.129  31.476  1.00 61.47           C  
ANISOU 5396  CD2 HIS B 228     7279   8710   7368    352   1244    238       C  
ATOM   5397  CE1 HIS B 228      17.031  14.489  31.241  1.00 62.25           C  
ANISOU 5397  CE1 HIS B 228     7237   8854   7560    384   1414    250       C  
ATOM   5398  NE2 HIS B 228      15.930  14.288  31.942  1.00 61.39           N  
ANISOU 5398  NE2 HIS B 228     7180   8690   7457    373   1287    198       N  
ATOM   5399  N   SER B 229      13.759  19.967  28.974  1.00 54.51           N  
ANISOU 5399  N   SER B 229     6589   7901   6222    258   1331    665       N  
ATOM   5400  CA  SER B 229      13.431  21.074  28.082  1.00 54.59           C  
ANISOU 5400  CA  SER B 229     6662   7940   6138    257   1371    785       C  
ATOM   5401  C   SER B 229      14.273  22.295  28.412  1.00 57.46           C  
ANISOU 5401  C   SER B 229     6963   8243   6628    186   1434    910       C  
ATOM   5402  O   SER B 229      14.700  22.473  29.553  1.00 55.96           O  
ANISOU 5402  O   SER B 229     6696   7969   6598    129   1396    896       O  
ATOM   5403  CB  SER B 229      11.946  21.438  28.167  1.00 57.45           C  
ANISOU 5403  CB  SER B 229     7112   8281   6435    270   1251    783       C  
ATOM   5404  OG  SER B 229      11.573  21.816  29.481  1.00 65.25           O  
ANISOU 5404  OG  SER B 229     8067   9159   7565    220   1153    769       O  
ATOM   5405  N   GLY B 900      14.516  23.110  27.383  1.00 40.18           N  
ANISOU 5405  N   GLY B 900     5180   5025   5063    479   -666   -100       N  
ATOM   5406  CA  GLY B 900      15.239  24.370  27.498  1.00 39.42           C  
ANISOU 5406  CA  GLY B 900     5084   4928   4965    479   -666    -99       C  
ATOM   5407  C   GLY B 900      14.296  25.558  27.649  1.00 42.17           C  
ANISOU 5407  C   GLY B 900     5433   5277   5314    479   -665    -99       C  
ATOM   5408  O   GLY B 900      13.180  25.418  28.142  1.00 41.70           O  
ANISOU 5408  O   GLY B 900     5373   5217   5254    479   -665    -99       O  
ATOM   5409  N   SER B 901      14.751  26.732  27.230  1.00 37.68           N  
ANISOU 5409  N   SER B 901     4864   4708   4743    480   -665    -98       N  
ATOM   5410  CA  SER B 901      13.976  27.949  27.409  1.00 37.11           C  
ANISOU 5410  CA  SER B 901     4793   4637   4671    480   -665    -98       C  
ATOM   5411  C   SER B 901      12.649  27.869  26.667  1.00 41.46           C  
ANISOU 5411  C   SER B 901     5342   5187   5222    480   -665    -98       C  
ATOM   5412  O   SER B 901      12.476  27.070  25.710  1.00 41.38           O  
ANISOU 5412  O   SER B 901     5332   5178   5212    480   -666    -98       O  
ATOM   5413  CB  SER B 901      14.758  29.181  26.939  1.00 39.65           C  
ANISOU 5413  CB  SER B 901     5116   4959   4992    480   -665    -97       C  
ATOM   5414  OG  SER B 901      14.910  29.206  25.524  1.00 45.88           O  
ANISOU 5414  OG  SER B 901     5903   5748   5779    481   -666    -98       O  
ATOM   5415  N   ASN B1002      11.715  28.698  27.121  1.00 30.66           N  
ANISOU 5415  N   ASN B1002     4855   3789   3005     97   -541    638       N  
ATOM   5416  CA  ASN B1002      10.411  28.779  26.481  1.00 30.37           C  
ANISOU 5416  CA  ASN B1002     4776   3753   3008     87   -489    665       C  
ATOM   5417  C   ASN B1002      10.541  29.139  24.987  1.00 34.02           C  
ANISOU 5417  C   ASN B1002     5212   4182   3533     39   -515    602       C  
ATOM   5418  O   ASN B1002       9.999  28.436  24.140  1.00 33.63           O  
ANISOU 5418  O   ASN B1002     5105   4112   3560      8   -512    615       O  
ATOM   5419  CB  ASN B1002       9.506  29.764  27.214  1.00 30.49           C  
ANISOU 5419  CB  ASN B1002     4828   3824   2933    157   -440    674       C  
ATOM   5420  CG  ASN B1002       8.957  29.197  28.515  1.00 47.13           C  
ANISOU 5420  CG  ASN B1002     6930   6003   4975    215   -384    770       C  
ATOM   5421  OD1 ASN B1002       8.793  28.002  28.638  1.00 42.03           O  
ANISOU 5421  OD1 ASN B1002     6231   5349   4390    178   -368    861       O  
ATOM   5422  ND2 ASN B1002       8.639  30.056  29.467  1.00 40.10           N  
ANISOU 5422  ND2 ASN B1002     6095   5181   3959    310   -356    755       N  
ATOM   5423  N   ILE B1003      11.297  30.187  24.660  1.00 30.21           N  
ANISOU 5423  N   ILE B1003     4768   3692   3017     29   -549    539       N  
ATOM   5424  CA  ILE B1003      11.552  30.522  23.260  1.00 29.83           C  
ANISOU 5424  CA  ILE B1003     4691   3634   3011    -14   -568    501       C  
ATOM   5425  C   ILE B1003      12.217  29.370  22.447  1.00 35.85           C  
ANISOU 5425  C   ILE B1003     5393   4397   3831    -40   -592    486       C  
ATOM   5426  O   ILE B1003      11.951  29.228  21.259  1.00 35.64           O  
ANISOU 5426  O   ILE B1003     5329   4377   3836    -52   -593    465       O  
ATOM   5427  CB  ILE B1003      12.345  31.844  23.131  1.00 32.48           C  
ANISOU 5427  CB  ILE B1003     5072   3957   3311    -37   -605    465       C  
ATOM   5428  CG1 ILE B1003      12.208  32.417  21.701  1.00 32.16           C  
ANISOU 5428  CG1 ILE B1003     5006   3917   3295    -71   -603    459       C  
ATOM   5429  CG2 ILE B1003      13.787  31.645  23.532  1.00 32.69           C  
ANISOU 5429  CG2 ILE B1003     5093   3994   3333    -64   -653    448       C  
ATOM   5430  CD1 ILE B1003      12.858  33.787  21.518  1.00 34.82           C  
ANISOU 5430  CD1 ILE B1003     5386   4225   3618   -111   -643    454       C  
ATOM   5431  N   PHE B1004      13.046  28.537  23.077  1.00 34.05           N  
ANISOU 5431  N   PHE B1004     5161   4166   3610    -31   -617    492       N  
ATOM   5432  CA  PHE B1004      13.685  27.419  22.360  1.00 34.43           C  
ANISOU 5432  CA  PHE B1004     5161   4209   3711    -27   -649    464       C  
ATOM   5433  C   PHE B1004      12.690  26.323  22.006  1.00 39.78           C  
ANISOU 5433  C   PHE B1004     5815   4837   4464    -23   -651    481       C  
ATOM   5434  O   PHE B1004      12.719  25.824  20.896  1.00 40.03           O  
ANISOU 5434  O   PHE B1004     5814   4863   4534    -17   -679    429       O  
ATOM   5435  CB  PHE B1004      14.824  26.811  23.185  1.00 36.57           C  
ANISOU 5435  CB  PHE B1004     5436   4485   3975     -4   -685    467       C  
ATOM   5436  CG  PHE B1004      15.395  25.532  22.609  1.00 38.31           C  
ANISOU 5436  CG  PHE B1004     5616   4688   4251     28   -726    435       C  
ATOM   5437  CD1 PHE B1004      16.447  25.575  21.700  1.00 41.28           C  
ANISOU 5437  CD1 PHE B1004     5943   5127   4616     46   -745    374       C  
ATOM   5438  CD2 PHE B1004      14.903  24.296  23.006  1.00 40.69           C  
ANISOU 5438  CD2 PHE B1004     5929   4913   4619     48   -748    471       C  
ATOM   5439  CE1 PHE B1004      16.992  24.415  21.179  1.00 42.51           C  
ANISOU 5439  CE1 PHE B1004     6067   5275   4810    106   -787    326       C  
ATOM   5440  CE2 PHE B1004      15.432  23.130  22.501  1.00 44.00           C  
ANISOU 5440  CE2 PHE B1004     6329   5292   5097     92   -805    428       C  
ATOM   5441  CZ  PHE B1004      16.483  23.185  21.581  1.00 42.22           C  
ANISOU 5441  CZ  PHE B1004     6061   5135   4847    134   -826    343       C  
ATOM   5442  N   GLU B1005      11.843  25.919  22.953  1.00 37.13           N  
ANISOU 5442  N   GLU B1005     5490   4469   4147    -25   -629    555       N  
ATOM   5443  CA  GLU B1005      10.842  24.870  22.676  1.00 37.36           C  
ANISOU 5443  CA  GLU B1005     5484   4438   4274    -47   -643    592       C  
ATOM   5444  C   GLU B1005       9.776  25.359  21.689  1.00 40.14           C  
ANISOU 5444  C   GLU B1005     5802   4805   4646    -67   -630    569       C  
ATOM   5445  O   GLU B1005       9.260  24.561  20.899  1.00 40.59           O  
ANISOU 5445  O   GLU B1005     5822   4812   4788    -86   -676    546       O  
ATOM   5446  CB  GLU B1005      10.189  24.331  23.967  1.00 39.44           C  
ANISOU 5446  CB  GLU B1005     5748   4684   4553    -55   -612    712       C  
ATOM   5447  CG  GLU B1005      10.750  22.961  24.446  1.00 51.17           C  
ANISOU 5447  CG  GLU B1005     7243   6091   6107    -53   -666    756       C  
ATOM   5448  CD  GLU B1005       9.925  21.747  23.956  1.00 78.08           C  
ANISOU 5448  CD  GLU B1005    10611   9394   9663   -102   -718    795       C  
ATOM   5449  OE1 GLU B1005       9.392  21.779  22.820  1.00 70.76           O  
ANISOU 5449  OE1 GLU B1005     9651   8446   8789   -124   -748    726       O  
ATOM   5450  OE2 GLU B1005       9.804  20.750  24.716  1.00 75.82           O  
ANISOU 5450  OE2 GLU B1005    10327   9037   9443   -121   -740    901       O  
ATOM   5451  N   MET B1006       9.468  26.660  21.731  1.00 34.62           N  
ANISOU 5451  N   MET B1006     5119   4163   3871    -57   -582    567       N  
ATOM   5452  CA  MET B1006       8.565  27.295  20.760  1.00 33.41           C  
ANISOU 5452  CA  MET B1006     4940   4034   3722    -61   -573    543       C  
ATOM   5453  C   MET B1006       9.044  27.128  19.314  1.00 36.80           C  
ANISOU 5453  C   MET B1006     5354   4467   4162    -60   -623    460       C  
ATOM   5454  O   MET B1006       8.303  26.649  18.469  1.00 36.45           O  
ANISOU 5454  O   MET B1006     5271   4408   4171    -66   -658    435       O  
ATOM   5455  CB  MET B1006       8.438  28.791  21.066  1.00 34.97           C  
ANISOU 5455  CB  MET B1006     5180   4275   3833    -35   -530    546       C  
ATOM   5456  CG  MET B1006       7.379  29.527  20.248  1.00 37.59           C  
ANISOU 5456  CG  MET B1006     5489   4630   4163    -23   -519    539       C  
ATOM   5457  SD  MET B1006       7.649  31.315  20.172  1.00 40.37           S  
ANISOU 5457  SD  MET B1006     5916   4995   4429      8   -507    517       S  
ATOM   5458  CE  MET B1006       5.974  31.820  19.744  1.00 37.24           C  
ANISOU 5458  CE  MET B1006     5480   4628   4043     51   -484    539       C  
ATOM   5459  N   LEU B1007      10.290  27.518  19.054  1.00 32.92           N  
ANISOU 5459  N   LEU B1007     4886   4007   3615    -48   -628    420       N  
ATOM   5460  CA  LEU B1007      10.847  27.523  17.702  1.00 32.65           C  
ANISOU 5460  CA  LEU B1007     4831   4018   3556    -30   -655    354       C  
ATOM   5461  C   LEU B1007      11.278  26.144  17.244  1.00 38.21           C  
ANISOU 5461  C   LEU B1007     5512   4696   4308      1   -714    292       C  
ATOM   5462  O   LEU B1007      11.362  25.890  16.034  1.00 38.13           O  
ANISOU 5462  O   LEU B1007     5482   4726   4281     38   -747    222       O  
ATOM   5463  CB  LEU B1007      12.024  28.504  17.600  1.00 32.18           C  
ANISOU 5463  CB  LEU B1007     4783   4020   3422    -37   -633    357       C  
ATOM   5464  CG  LEU B1007      11.586  29.960  17.343  1.00 35.84           C  
ANISOU 5464  CG  LEU B1007     5274   4503   3841    -58   -604    394       C  
ATOM   5465  CD1 LEU B1007      12.484  30.937  18.072  1.00 35.79           C  
ANISOU 5465  CD1 LEU B1007     5301   4493   3803    -91   -596    425       C  
ATOM   5466  CD2 LEU B1007      11.532  30.257  15.842  1.00 36.46           C  
ANISOU 5466  CD2 LEU B1007     5324   4647   3880    -43   -607    376       C  
ATOM   5467  N   ARG B1008      11.556  25.256  18.200  1.00 35.71           N  
ANISOU 5467  N   ARG B1008     5206   4315   4046      0   -733    315       N  
ATOM   5468  CA  ARG B1008      11.831  23.861  17.878  1.00 36.54           C  
ANISOU 5468  CA  ARG B1008     5304   4358   4221     36   -808    258       C  
ATOM   5469  C   ARG B1008      10.568  23.277  17.241  1.00 42.32           C  
ANISOU 5469  C   ARG B1008     6019   5025   5035     16   -861    236       C  
ATOM   5470  O   ARG B1008      10.630  22.601  16.219  1.00 42.97           O  
ANISOU 5470  O   ARG B1008     6096   5092   5140     61   -934    139       O  
ATOM   5471  CB  ARG B1008      12.227  23.097  19.143  1.00 36.64           C  
ANISOU 5471  CB  ARG B1008     5339   4298   4283     31   -821    315       C  
ATOM   5472  CG  ARG B1008      12.330  21.561  19.003  1.00 46.78           C  
ANISOU 5472  CG  ARG B1008     6632   5471   5672     63   -915    276       C  
ATOM   5473  CD  ARG B1008      12.797  20.937  20.328  1.00 54.78           C  
ANISOU 5473  CD  ARG B1008     7673   6422   6719     62   -922    359       C  
ATOM   5474  NE  ARG B1008      13.026  19.498  20.258  1.00 63.27           N  
ANISOU 5474  NE  ARG B1008     8769   7369   7900     99  -1023    330       N  
ATOM   5475  CZ  ARG B1008      13.293  18.725  21.313  1.00 78.36           C  
ANISOU 5475  CZ  ARG B1008    10711   9198   9866    100  -1050    414       C  
ATOM   5476  NH1 ARG B1008      13.373  19.244  22.541  1.00 67.67           N  
ANISOU 5476  NH1 ARG B1008     9366   7895   8452     72   -979    527       N  
ATOM   5477  NH2 ARG B1008      13.483  17.421  21.149  1.00 64.76           N  
ANISOU 5477  NH2 ARG B1008     9016   7335   8253    139  -1159    382       N  
ATOM   5478  N   ILE B1009       9.420  23.587  17.831  1.00 38.87           N  
ANISOU 5478  N   ILE B1009     5567   4564   4637    -43   -827    322       N  
ATOM   5479  CA  ILE B1009       8.145  23.132  17.309  1.00 39.34           C  
ANISOU 5479  CA  ILE B1009     5587   4573   4786    -78   -878    319       C  
ATOM   5480  C   ILE B1009       7.826  23.796  15.957  1.00 43.53           C  
ANISOU 5480  C   ILE B1009     6104   5180   5255    -46   -893    239       C  
ATOM   5481  O   ILE B1009       7.417  23.123  15.009  1.00 43.88           O  
ANISOU 5481  O   ILE B1009     6133   5191   5349    -32   -984    158       O  
ATOM   5482  CB  ILE B1009       7.011  23.341  18.345  1.00 42.40           C  
ANISOU 5482  CB  ILE B1009     5939   4950   5221   -142   -823    450       C  
ATOM   5483  CG1 ILE B1009       7.205  22.373  19.528  1.00 43.27           C  
ANISOU 5483  CG1 ILE B1009     6057   4979   5405   -174   -829    541       C  
ATOM   5484  CG2 ILE B1009       5.646  23.114  17.715  1.00 43.59           C  
ANISOU 5484  CG2 ILE B1009     6023   5082   5458   -185   -870    455       C  
ATOM   5485  CD1 ILE B1009       6.253  22.613  20.721  1.00 49.79           C  
ANISOU 5485  CD1 ILE B1009     6841   5835   6241   -219   -748    693       C  
ATOM   5486  N   ASP B1010       8.053  25.098  15.850  1.00 39.61           N  
ANISOU 5486  N   ASP B1010     5620   4780   4649    -31   -817    258       N  
ATOM   5487  CA  ASP B1010       7.599  25.840  14.674  1.00 39.42           C  
ANISOU 5487  CA  ASP B1010     5584   4831   4564     -4   -823    217       C  
ATOM   5488  C   ASP B1010       8.555  25.699  13.496  1.00 45.12           C  
ANISOU 5488  C   ASP B1010     6317   5620   5205     63   -856    121       C  
ATOM   5489  O   ASP B1010       8.114  25.533  12.347  1.00 45.48           O  
ANISOU 5489  O   ASP B1010     6350   5701   5229    103   -913     50       O  
ATOM   5490  CB  ASP B1010       7.398  27.323  15.015  1.00 40.07           C  
ANISOU 5490  CB  ASP B1010     5682   4970   4571    -13   -740    289       C  
ATOM   5491  CG  ASP B1010       6.045  27.610  15.635  1.00 45.95           C  
ANISOU 5491  CG  ASP B1010     6396   5696   5367    -40   -717    357       C  
ATOM   5492  OD1 ASP B1010       5.182  26.719  15.666  1.00 47.29           O  
ANISOU 5492  OD1 ASP B1010     6513   5821   5633    -69   -762    363       O  
ATOM   5493  OD2 ASP B1010       5.832  28.750  16.081  1.00 49.50           O  
ANISOU 5493  OD2 ASP B1010     6869   6177   5763    -29   -657    407       O  
ATOM   5494  N   GLU B1011       9.857  25.772  13.774  1.00 41.96           N  
ANISOU 5494  N   GLU B1011     5934   5256   4753     84   -821    121       N  
ATOM   5495  CA  GLU B1011      10.868  25.693  12.716  1.00 42.17           C  
ANISOU 5495  CA  GLU B1011     5953   5384   4686    159   -830     47       C  
ATOM   5496  C   GLU B1011      11.473  24.299  12.527  1.00 46.48           C  
ANISOU 5496  C   GLU B1011     6500   5891   5271    228   -906    -55       C  
ATOM   5497  O   GLU B1011      11.982  24.003  11.450  1.00 47.73           O  
ANISOU 5497  O   GLU B1011     6648   6137   5351    320   -935   -147       O  
ATOM   5498  CB  GLU B1011      11.984  26.712  12.970  1.00 43.17           C  
ANISOU 5498  CB  GLU B1011     6074   5599   4729    143   -748    113       C  
ATOM   5499  CG  GLU B1011      12.676  27.179  11.673  1.00 55.48           C  
ANISOU 5499  CG  GLU B1011     7602   7313   6165    202   -725     92       C  
ATOM   5500  CD  GLU B1011      13.022  28.651  11.689  1.00 76.48           C  
ANISOU 5500  CD  GLU B1011    10258  10036   8764    142   -653    202       C  
ATOM   5501  OE1 GLU B1011      12.123  29.469  12.011  1.00 69.33           O  
ANISOU 5501  OE1 GLU B1011     9387   9069   7885     90   -641    261       O  
ATOM   5502  OE2 GLU B1011      14.188  28.995  11.374  1.00 70.96           O  
ANISOU 5502  OE2 GLU B1011     9517   9446   7997    149   -613    235       O  
ATOM   5503  N   GLY B1012      11.439  23.457  13.562  1.00 41.70           N  
ANISOU 5503  N   GLY B1012     5910   5160   4774    197   -938    -36       N  
ATOM   5504  CA  GLY B1012      12.042  22.118  13.504  1.00 41.77           C  
ANISOU 5504  CA  GLY B1012     5935   5101   4836    267  -1023   -126       C  
ATOM   5505  C   GLY B1012      13.443  22.066  14.082  1.00 44.25           C  
ANISOU 5505  C   GLY B1012     6243   5463   5108    307   -983   -112       C  
ATOM   5506  O   GLY B1012      14.150  23.072  14.097  1.00 42.86           O  
ANISOU 5506  O   GLY B1012     6039   5410   4837    297   -899    -64       O  
ATOM   5507  N   LEU B1013      13.843  20.892  14.572  1.00 41.18           N  
ANISOU 5507  N   LEU B1013     5878   4968   4801    348  -1054   -148       N  
ATOM   5508  CA  LEU B1013      15.171  20.728  15.175  1.00 40.88           C  
ANISOU 5508  CA  LEU B1013     5828   4973   4731    398  -1031   -138       C  
ATOM   5509  C   LEU B1013      15.965  19.582  14.546  1.00 46.25           C  
ANISOU 5509  C   LEU B1013     6514   5647   5413    544  -1117   -272       C  
ATOM   5510  O   LEU B1013      15.645  18.411  14.729  1.00 46.56           O  
ANISOU 5510  O   LEU B1013     6603   5522   5565    572  -1224   -319       O  
ATOM   5511  CB  LEU B1013      15.065  20.524  16.691  1.00 40.38           C  
ANISOU 5511  CB  LEU B1013     5793   4800   4751    323  -1023    -25       C  
ATOM   5512  CG  LEU B1013      16.404  20.303  17.406  1.00 44.86           C  
ANISOU 5512  CG  LEU B1013     6349   5404   5291    377  -1017    -12       C  
ATOM   5513  CD1 LEU B1013      17.130  21.632  17.604  1.00 44.14           C  
ANISOU 5513  CD1 LEU B1013     6209   5467   5093    339   -923     42       C  
ATOM   5514  CD2 LEU B1013      16.222  19.536  18.737  1.00 46.84           C  
ANISOU 5514  CD2 LEU B1013     6647   5510   5640    344  -1056     73       C  
ATOM   5515  N   ARG B1014      17.024  19.953  13.836  1.00 43.22           N  
ANISOU 5515  N   ARG B1014     6074   5444   4902    638  -1071   -324       N  
ATOM   5516  CA  ARG B1014      17.930  19.021  13.189  1.00 44.21           C  
ANISOU 5516  CA  ARG B1014     6189   5617   4990    810  -1133   -459       C  
ATOM   5517  C   ARG B1014      19.236  18.902  13.987  1.00 48.37           C  
ANISOU 5517  C   ARG B1014     6672   6202   5505    854  -1104   -420       C  
ATOM   5518  O   ARG B1014      19.920  19.903  14.218  1.00 46.74           O  
ANISOU 5518  O   ARG B1014     6392   6145   5221    803  -1006   -334       O  
ATOM   5519  CB  ARG B1014      18.240  19.520  11.769  1.00 44.48           C  
ANISOU 5519  CB  ARG B1014     6169   5865   4868    906  -1088   -535       C  
ATOM   5520  CG  ARG B1014      17.017  19.654  10.837  1.00 49.80           C  
ANISOU 5520  CG  ARG B1014     6882   6512   5530    888  -1127   -589       C  
ATOM   5521  CD  ARG B1014      17.423  20.240   9.480  1.00 53.85           C  
ANISOU 5521  CD  ARG B1014     7337   7267   5857    991  -1068   -639       C  
ATOM   5522  NE  ARG B1014      16.328  20.227   8.503  1.00 54.57           N  
ANISOU 5522  NE  ARG B1014     7471   7344   5921   1008  -1129   -715       N  
ATOM   5523  CZ  ARG B1014      16.040  19.217   7.680  1.00 64.64           C  
ANISOU 5523  CZ  ARG B1014     8796   8575   7191   1146  -1257   -895       C  
ATOM   5524  NH1 ARG B1014      16.756  18.095   7.686  1.00 52.77           N  
ANISOU 5524  NH1 ARG B1014     7317   7026   5709   1294  -1341  -1025       N  
ATOM   5525  NH2 ARG B1014      15.017  19.322   6.839  1.00 47.61           N  
ANISOU 5525  NH2 ARG B1014     6670   6411   5007   1147  -1317   -954       N  
ATOM   5526  N   LEU B1015      19.580  17.678  14.394  1.00 46.67           N  
ANISOU 5526  N   LEU B1015     6501   5859   5374    947  -1204   -483       N  
ATOM   5527  CA  LEU B1015      20.856  17.399  15.100  1.00 46.81           C  
ANISOU 5527  CA  LEU B1015     6476   5931   5381   1020  -1198   -463       C  
ATOM   5528  C   LEU B1015      22.037  17.117  14.143  1.00 52.13           C  
ANISOU 5528  C   LEU B1015     7070   6800   5938   1217  -1193   -585       C  
ATOM   5529  O   LEU B1015      23.185  17.085  14.591  1.00 52.57           O  
ANISOU 5529  O   LEU B1015     7054   6958   5963   1280  -1170   -563       O  
ATOM   5530  CB  LEU B1015      20.685  16.244  16.113  1.00 47.25           C  
ANISOU 5530  CB  LEU B1015     6618   5751   5583   1030  -1308   -446       C  
ATOM   5531  CG  LEU B1015      19.912  16.583  17.409  1.00 50.72           C  
ANISOU 5531  CG  LEU B1015     7103   6061   6107    851  -1282   -282       C  
ATOM   5532  CD1 LEU B1015      18.885  15.530  17.812  1.00 51.42           C  
ANISOU 5532  CD1 LEU B1015     7290   5894   6355    810  -1389   -261       C  
ATOM   5533  CD2 LEU B1015      20.853  16.831  18.571  1.00 53.43           C  
ANISOU 5533  CD2 LEU B1015     7414   6459   6428    841  -1248   -187       C  
ATOM   5534  N   LYS B1016      21.762  16.935  12.844  1.00 48.98           N  
ANISOU 5534  N   LYS B1016     6673   6471   5464   1323  -1213   -711       N  
ATOM   5535  CA  LYS B1016      22.809  16.702  11.823  1.00 50.18           C  
ANISOU 5535  CA  LYS B1016     6743   6850   5474   1534  -1194   -831       C  
ATOM   5536  C   LYS B1016      22.670  17.641  10.609  1.00 54.36           C  
ANISOU 5536  C   LYS B1016     7203   7608   5841   1536  -1095   -831       C  
ATOM   5537  O   LYS B1016      21.567  17.843  10.113  1.00 53.61           O  
ANISOU 5537  O   LYS B1016     7175   7439   5755   1471  -1118   -850       O  
ATOM   5538  CB  LYS B1016      22.768  15.243  11.344  1.00 54.16           C  
ANISOU 5538  CB  LYS B1016     7336   7220   6022   1740  -1349  -1029       C  
ATOM   5539  CG  LYS B1016      23.834  14.880  10.291  1.00 67.68           C  
ANISOU 5539  CG  LYS B1016     8970   9174   7571   2005  -1338  -1180       C  
ATOM   5540  CD  LYS B1016      24.075  13.360  10.182  1.00 78.46           C  
ANISOU 5540  CD  LYS B1016    10430  10377   9005   2231  -1509  -1373       C  
ATOM   5541  CE  LYS B1016      23.086  12.673   9.239  1.00 89.44           C  
ANISOU 5541  CE  LYS B1016    11946  11623  10415   2313  -1649  -1554       C  
ATOM   5542  NZ  LYS B1016      23.307  13.044   7.806  1.00 99.91           N  
ANISOU 5542  NZ  LYS B1016    13209  13236  11517   2477  -1588  -1672       N  
ATOM   5543  N   ILE B1017      23.792  18.188  10.129  1.00 51.58           N  
ANISOU 5543  N   ILE B1017     6711   7542   5344   1614   -987   -800       N  
ATOM   5544  CA  ILE B1017      23.819  19.073   8.949  1.00 51.68           C  
ANISOU 5544  CA  ILE B1017     6644   7807   5187   1629   -882   -773       C  
ATOM   5545  C   ILE B1017      23.000  18.549   7.755  1.00 55.93           C  
ANISOU 5545  C   ILE B1017     7266   8333   5652   1761   -955   -935       C  
ATOM   5546  O   ILE B1017      22.967  17.347   7.486  1.00 56.92           O  
ANISOU 5546  O   ILE B1017     7467   8361   5800   1940  -1080  -1119       O  
ATOM   5547  CB  ILE B1017      25.269  19.327   8.455  1.00 56.30           C  
ANISOU 5547  CB  ILE B1017     7052   8720   5619   1760   -777   -747       C  
ATOM   5548  CG1 ILE B1017      25.929  20.463   9.236  1.00 55.60           C  
ANISOU 5548  CG1 ILE B1017     6845   8721   5561   1566   -671   -537       C  
ATOM   5549  CG2 ILE B1017      25.296  19.670   6.954  1.00 58.72           C  
ANISOU 5549  CG2 ILE B1017     7298   9294   5720   1885   -704   -787       C  
ATOM   5550  CD1 ILE B1017      27.298  20.878   8.671  1.00 63.17           C  
ANISOU 5550  CD1 ILE B1017     7596  10029   6375   1655   -555   -472       C  
ATOM   5551  N   TYR B1018      22.372  19.473   7.036  1.00 51.37           N  
ANISOU 5551  N   TYR B1018     6678   7855   4986   1679   -888   -869       N  
ATOM   5552  CA  TYR B1018      21.491  19.132   5.924  1.00 51.99           C  
ANISOU 5552  CA  TYR B1018     6837   7929   4990   1782   -961  -1009       C  
ATOM   5553  C   TYR B1018      21.635  20.093   4.739  1.00 56.59           C  
ANISOU 5553  C   TYR B1018     7334   8812   5357   1820   -841   -945       C  
ATOM   5554  O   TYR B1018      21.340  21.280   4.865  1.00 54.51           O  
ANISOU 5554  O   TYR B1018     7034   8586   5090   1637   -746   -764       O  
ATOM   5555  CB  TYR B1018      20.032  19.136   6.400  1.00 51.47           C  
ANISOU 5555  CB  TYR B1018     6892   7575   5087   1608  -1051   -992       C  
ATOM   5556  CG  TYR B1018      19.020  18.976   5.288  1.00 53.77           C  
ANISOU 5556  CG  TYR B1018     7253   7864   5312   1675  -1131  -1113       C  
ATOM   5557  CD1 TYR B1018      18.715  17.721   4.772  1.00 57.11           C  
ANISOU 5557  CD1 TYR B1018     7767   8173   5758   1845  -1299  -1338       C  
ATOM   5558  CD2 TYR B1018      18.371  20.083   4.748  1.00 54.05           C  
ANISOU 5558  CD2 TYR B1018     7269   8002   5265   1574  -1056  -1007       C  
ATOM   5559  CE1 TYR B1018      17.794  17.571   3.755  1.00 58.52           C  
ANISOU 5559  CE1 TYR B1018     8009   8349   5875   1907  -1393  -1461       C  
ATOM   5560  CE2 TYR B1018      17.447  19.944   3.732  1.00 55.73           C  
ANISOU 5560  CE2 TYR B1018     7541   8222   5409   1642  -1138  -1117       C  
ATOM   5561  CZ  TYR B1018      17.163  18.685   3.238  1.00 64.67           C  
ANISOU 5561  CZ  TYR B1018     8759   9252   6563   1807  -1309  -1349       C  
ATOM   5562  OH  TYR B1018      16.239  18.547   2.229  1.00 67.51           O  
ANISOU 5562  OH  TYR B1018     9177   9618   6855   1874  -1411  -1471       O  
ATOM   5563  N   LYS B1019      22.075  19.561   3.596  1.00 55.44           N  
ANISOU 5563  N   LYS B1019     7162   8874   5028   2069   -853  -1094       N  
ATOM   5564  CA  LYS B1019      22.013  20.269   2.316  1.00 56.41           C  
ANISOU 5564  CA  LYS B1019     7230   9277   4925   2143   -765  -1061       C  
ATOM   5565  C   LYS B1019      20.586  20.203   1.815  1.00 60.87           C  
ANISOU 5565  C   LYS B1019     7928   9686   5513   2110   -877  -1147       C  
ATOM   5566  O   LYS B1019      20.028  19.108   1.675  1.00 61.55           O  
ANISOU 5566  O   LYS B1019     8129   9593   5665   2221  -1046  -1359       O  
ATOM   5567  CB  LYS B1019      22.925  19.595   1.293  1.00 61.21           C  
ANISOU 5567  CB  LYS B1019     7774  10170   5313   2456   -752  -1216       C  
ATOM   5568  CG  LYS B1019      23.045  20.302  -0.047  1.00 72.99           C  
ANISOU 5568  CG  LYS B1019     9188  12013   6534   2561   -639  -1163       C  
ATOM   5569  CD  LYS B1019      24.203  19.701  -0.844  1.00 86.16           C  
ANISOU 5569  CD  LYS B1019    10752  14009   7976   2874   -588  -1281       C  
ATOM   5570  CE  LYS B1019      24.312  20.272  -2.258  1.00100.63           C  
ANISOU 5570  CE  LYS B1019    12510  16221   9503   3021   -478  -1240       C  
ATOM   5571  NZ  LYS B1019      25.274  19.502  -3.125  1.00112.20           N  
ANISOU 5571  NZ  LYS B1019    13898  18010  10724   3382   -453  -1409       N  
ATOM   5572  N   ASP B1020      19.987  21.364   1.558  1.00 56.56           N  
ANISOU 5572  N   ASP B1020     7367   9195   4928   1955   -798   -983       N  
ATOM   5573  CA  ASP B1020      18.655  21.420   0.955  1.00 56.12           C  
ANISOU 5573  CA  ASP B1020     7415   9042   4868   1936   -895  -1052       C  
ATOM   5574  C   ASP B1020      18.774  21.462  -0.572  1.00 62.29           C  
ANISOU 5574  C   ASP B1020     8175  10121   5372   2156   -876  -1137       C  
ATOM   5575  O   ASP B1020      19.861  21.301  -1.122  1.00 63.90           O  
ANISOU 5575  O   ASP B1020     8290  10595   5396   2338   -795  -1161       O  
ATOM   5576  CB  ASP B1020      17.862  22.617   1.493  1.00 55.91           C  
ANISOU 5576  CB  ASP B1020     7394   8905   4944   1676   -834   -842       C  
ATOM   5577  CG  ASP B1020      18.294  23.920   0.881  1.00 66.24           C  
ANISOU 5577  CG  ASP B1020     8606  10476   6084   1635   -674   -640       C  
ATOM   5578  OD1 ASP B1020      19.319  23.928   0.168  1.00 68.71           O  
ANISOU 5578  OD1 ASP B1020     8823  11074   6208   1784   -584   -629       O  
ATOM   5579  OD2 ASP B1020      17.611  24.936   1.113  1.00 70.50           O  
ANISOU 5579  OD2 ASP B1020     9164  10941   6683   1458   -637   -484       O  
ATOM   5580  N   THR B1021      17.655  21.699  -1.248  1.00 58.69           N  
ANISOU 5580  N   THR B1021     7792   9634   4873   2146   -949  -1175       N  
ATOM   5581  CA  THR B1021      17.574  21.558  -2.695  1.00 60.41           C  
ANISOU 5581  CA  THR B1021     8023  10103   4830   2376   -976  -1298       C  
ATOM   5582  C   THR B1021      18.179  22.711  -3.492  1.00 64.21           C  
ANISOU 5582  C   THR B1021     8389  10944   5065   2401   -784  -1091       C  
ATOM   5583  O   THR B1021      18.425  22.562  -4.685  1.00 65.69           O  
ANISOU 5583  O   THR B1021     8559  11410   4989   2630   -771  -1177       O  
ATOM   5584  CB  THR B1021      16.117  21.409  -3.114  1.00 70.39           C  
ANISOU 5584  CB  THR B1021     9402  11201   6142   2349  -1140  -1409       C  
ATOM   5585  OG1 THR B1021      15.373  22.511  -2.587  1.00 71.14           O  
ANISOU 5585  OG1 THR B1021     9489  11187   6356   2095  -1077  -1189       O  
ATOM   5586  CG2 THR B1021      15.528  20.099  -2.582  1.00 68.78           C  
ANISOU 5586  CG2 THR B1021     9307  10669   6157   2361  -1356  -1637       C  
ATOM   5587  N   GLU B1022      18.408  23.856  -2.855  1.00 59.17           N  
ANISOU 5587  N   GLU B1022     7674  10301   4507   2172   -642   -818       N  
ATOM   5588  CA  GLU B1022      18.999  25.009  -3.546  1.00 60.00           C  
ANISOU 5588  CA  GLU B1022     7664  10721   4411   2159   -463   -583       C  
ATOM   5589  C   GLU B1022      20.450  25.297  -3.132  1.00 65.31           C  
ANISOU 5589  C   GLU B1022     8178  11571   5065   2131   -304   -427       C  
ATOM   5590  O   GLU B1022      21.027  26.306  -3.550  1.00 65.65           O  
ANISOU 5590  O   GLU B1022     8105  11855   4984   2075   -150   -190       O  
ATOM   5591  CB  GLU B1022      18.119  26.251  -3.363  1.00 59.68           C  
ANISOU 5591  CB  GLU B1022     7657  10564   4454   1929   -434   -372       C  
ATOM   5592  CG  GLU B1022      16.726  26.136  -4.008  1.00 68.20           C  
ANISOU 5592  CG  GLU B1022     8859  11552   5503   1975   -571   -492       C  
ATOM   5593  CD  GLU B1022      16.755  26.049  -5.539  1.00 85.44           C  
ANISOU 5593  CD  GLU B1022    11038  14057   7370   2220   -567   -560       C  
ATOM   5594  OE1 GLU B1022      17.791  26.392  -6.142  1.00 82.27           O  
ANISOU 5594  OE1 GLU B1022    10523  13977   6758   2320   -419   -442       O  
ATOM   5595  OE2 GLU B1022      15.740  25.635  -6.141  1.00 73.94           O  
ANISOU 5595  OE2 GLU B1022     9681  12544   5869   2316   -714   -730       O  
ATOM   5596  N   GLY B1023      21.033  24.419  -2.313  1.00 62.22           N  
ANISOU 5596  N   GLY B1023     7776  11059   4804   2164   -349   -549       N  
ATOM   5597  CA  GLY B1023      22.483  24.416  -2.062  1.00 63.29           C  
ANISOU 5597  CA  GLY B1023     7750  11404   4894   2206   -223   -460       C  
ATOM   5598  C   GLY B1023      22.980  25.032  -0.761  1.00 66.26           C  
ANISOU 5598  C   GLY B1023     8058  11628   5489   1950   -164   -271       C  
ATOM   5599  O   GLY B1023      24.197  25.082  -0.537  1.00 66.94           O  
ANISOU 5599  O   GLY B1023     7992  11893   5547   1969    -66   -185       O  
ATOM   5600  N   TYR B1024      22.061  25.494   0.091  1.00 60.55           N  
ANISOU 5600  N   TYR B1024     7440  10592   4975   1722   -227   -212       N  
ATOM   5601  CA  TYR B1024      22.412  26.081   1.392  1.00 58.82           C  
ANISOU 5601  CA  TYR B1024     7184  10203   4963   1485   -196    -58       C  
ATOM   5602  C   TYR B1024      22.462  25.019   2.489  1.00 59.93           C  
ANISOU 5602  C   TYR B1024     7386  10100   5283   1500   -304   -219       C  
ATOM   5603  O   TYR B1024      21.741  24.019   2.424  1.00 58.93           O  
ANISOU 5603  O   TYR B1024     7380   9816   5196   1609   -432   -424       O  
ATOM   5604  CB  TYR B1024      21.378  27.126   1.820  1.00 58.83           C  
ANISOU 5604  CB  TYR B1024     7273   9992   5089   1255   -211     79       C  
ATOM   5605  CG  TYR B1024      21.126  28.255   0.847  1.00 61.66           C  
ANISOU 5605  CG  TYR B1024     7602  10522   5305   1213   -127    255       C  
ATOM   5606  CD1 TYR B1024      21.782  29.476   0.991  1.00 64.07           C  
ANISOU 5606  CD1 TYR B1024     7802  10920   5623   1044    -16    516       C  
ATOM   5607  CD2 TYR B1024      20.200  28.118  -0.188  1.00 62.97           C  
ANISOU 5607  CD2 TYR B1024     7849  10740   5337   1333   -175    169       C  
ATOM   5608  CE1 TYR B1024      21.539  30.529   0.120  1.00 66.11           C  
ANISOU 5608  CE1 TYR B1024     8041  11314   5763    996     53    701       C  
ATOM   5609  CE2 TYR B1024      19.953  29.162  -1.066  1.00 64.83           C  
ANISOU 5609  CE2 TYR B1024     8064  11132   5437   1300   -102    345       C  
ATOM   5610  CZ  TYR B1024      20.624  30.366  -0.903  1.00 73.20           C  
ANISOU 5610  CZ  TYR B1024     9024  12275   6515   1130     15    619       C  
ATOM   5611  OH  TYR B1024      20.391  31.416  -1.757  1.00 75.69           O  
ANISOU 5611  OH  TYR B1024     9324  12728   6708   1089     82    817       O  
ATOM   5612  N   TYR B1025      23.274  25.287   3.517  1.00 54.91           N  
ANISOU 5612  N   TYR B1025     6672   9423   4768   1375   -263   -111       N  
ATOM   5613  CA  TYR B1025      23.486  24.355   4.644  1.00 53.31           C  
ANISOU 5613  CA  TYR B1025     6513   9014   4728   1384   -353   -226       C  
ATOM   5614  C   TYR B1025      22.908  24.862   5.987  1.00 53.55           C  
ANISOU 5614  C   TYR B1025     6622   8753   4971   1145   -393   -134       C  
ATOM   5615  O   TYR B1025      23.167  25.997   6.415  1.00 52.09           O  
ANISOU 5615  O   TYR B1025     6382   8584   4828    965   -324     51       O  
ATOM   5616  CB  TYR B1025      24.986  24.043   4.787  1.00 55.58           C  
ANISOU 5616  CB  TYR B1025     6641   9511   4966   1483   -290   -209       C  
ATOM   5617  CG  TYR B1025      25.565  23.310   3.597  1.00 59.20           C  
ANISOU 5617  CG  TYR B1025     7030  10250   5214   1768   -263   -339       C  
ATOM   5618  CD1 TYR B1025      25.511  21.919   3.518  1.00 61.76           C  
ANISOU 5618  CD1 TYR B1025     7437  10491   5539   1990   -381   -587       C  
ATOM   5619  CD2 TYR B1025      26.154  24.003   2.551  1.00 61.55           C  
ANISOU 5619  CD2 TYR B1025     7183  10894   5309   1822   -126   -214       C  
ATOM   5620  CE1 TYR B1025      26.035  21.235   2.429  1.00 64.38           C  
ANISOU 5620  CE1 TYR B1025     7717  11079   5665   2281   -368   -733       C  
ATOM   5621  CE2 TYR B1025      26.679  23.336   1.460  1.00 64.79           C  
ANISOU 5621  CE2 TYR B1025     7527  11591   5499   2108    -94   -339       C  
ATOM   5622  CZ  TYR B1025      26.619  21.948   1.398  1.00 72.52           C  
ANISOU 5622  CZ  TYR B1025     8597  12484   6472   2348   -218   -613       C  
ATOM   5623  OH  TYR B1025      27.144  21.282   0.302  1.00 75.46           O  
ANISOU 5623  OH  TYR B1025     8914  13146   6611   2662   -196   -760       O  
ATOM   5624  N   THR B1026      22.146  23.996   6.651  1.00 48.69           N  
ANISOU 5624  N   THR B1026     6135   7878   4487   1153   -511   -265       N  
ATOM   5625  CA  THR B1026      21.385  24.366   7.843  1.00 46.72           C  
ANISOU 5625  CA  THR B1026     5973   7365   4413    960   -551   -196       C  
ATOM   5626  C   THR B1026      21.629  23.371   8.982  1.00 50.20           C  
ANISOU 5626  C   THR B1026     6456   7628   4991    979   -632   -273       C  
ATOM   5627  O   THR B1026      21.920  22.207   8.739  1.00 50.77           O  
ANISOU 5627  O   THR B1026     6541   7697   5050   1147   -699   -420       O  
ATOM   5628  CB  THR B1026      19.853  24.522   7.491  1.00 54.20           C  
ANISOU 5628  CB  THR B1026     7038   8167   5388    911   -605   -228       C  
ATOM   5629  OG1 THR B1026      19.599  25.874   7.090  1.00 53.49           O  
ANISOU 5629  OG1 THR B1026     6922   8164   5238    798   -523    -76       O  
ATOM   5630  CG2 THR B1026      18.924  24.181   8.658  1.00 52.18           C  
ANISOU 5630  CG2 THR B1026     6887   7626   5314    802   -686   -243       C  
ATOM   5631  N   ILE B1027      21.531  23.843  10.222  1.00 45.66           N  
ANISOU 5631  N   ILE B1027     5905   6906   4538    817   -632   -171       N  
ATOM   5632  CA  ILE B1027      21.634  22.969  11.393  1.00 45.37           C  
ANISOU 5632  CA  ILE B1027     5920   6692   4628    820   -708   -216       C  
ATOM   5633  C   ILE B1027      20.969  23.602  12.631  1.00 48.87           C  
ANISOU 5633  C   ILE B1027     6430   6954   5185    637   -712   -110       C  
ATOM   5634  O   ILE B1027      20.599  24.791  12.631  1.00 47.95           O  
ANISOU 5634  O   ILE B1027     6311   6854   5053    512   -656     -6       O  
ATOM   5635  CB  ILE B1027      23.118  22.569  11.685  1.00 49.34           C  
ANISOU 5635  CB  ILE B1027     6315   7327   5104    913   -694   -225       C  
ATOM   5636  CG1 ILE B1027      23.184  21.290  12.535  1.00 50.01           C  
ANISOU 5636  CG1 ILE B1027     6471   7236   5296    992   -798   -315       C  
ATOM   5637  CG2 ILE B1027      23.861  23.706  12.351  1.00 49.11           C  
ANISOU 5637  CG2 ILE B1027     6196   7380   5084    766   -625    -69       C  
ATOM   5638  CD1 ILE B1027      24.443  20.469  12.353  1.00 58.75           C  
ANISOU 5638  CD1 ILE B1027     7492   8475   6355   1177   -816   -397       C  
ATOM   5639  N   GLY B1028      20.788  22.786  13.667  1.00 45.59           N  
ANISOU 5639  N   GLY B1028     6079   6365   4877    637   -782   -137       N  
ATOM   5640  CA  GLY B1028      20.149  23.219  14.897  1.00 44.30           C  
ANISOU 5640  CA  GLY B1028     5982   6048   4804    498   -787    -48       C  
ATOM   5641  C   GLY B1028      18.741  23.665  14.570  1.00 47.96           C  
ANISOU 5641  C   GLY B1028     6510   6428   5285    425   -781    -31       C  
ATOM   5642  O   GLY B1028      18.041  22.991  13.822  1.00 47.24           O  
ANISOU 5642  O   GLY B1028     6453   6294   5203    487   -829   -115       O  
ATOM   5643  N   ILE B1029      18.355  24.811  15.130  1.00 45.16           N  
ANISOU 5643  N   ILE B1029     6171   6052   4935    301   -734     71       N  
ATOM   5644  CA  ILE B1029      17.090  25.474  14.843  1.00 44.71           C  
ANISOU 5644  CA  ILE B1029     6161   5943   4883    235   -717    102       C  
ATOM   5645  C   ILE B1029      17.346  26.550  13.798  1.00 50.30           C  
ANISOU 5645  C   ILE B1029     6821   6796   5495    220   -659    141       C  
ATOM   5646  O   ILE B1029      17.723  27.662  14.133  1.00 49.50           O  
ANISOU 5646  O   ILE B1029     6703   6726   5378    136   -617    231       O  
ATOM   5647  CB  ILE B1029      16.479  26.106  16.122  1.00 46.75           C  
ANISOU 5647  CB  ILE B1029     6474   6092   5196    134   -704    185       C  
ATOM   5648  CG1 ILE B1029      15.934  25.026  17.055  1.00 46.64           C  
ANISOU 5648  CG1 ILE B1029     6507   5941   5271    144   -752    175       C  
ATOM   5649  CG2 ILE B1029      15.340  27.040  15.786  1.00 47.55           C  
ANISOU 5649  CG2 ILE B1029     6607   6173   5287     79   -676    225       C  
ATOM   5650  CD1 ILE B1029      15.082  25.578  18.176  1.00 50.86           C  
ANISOU 5650  CD1 ILE B1029     7092   6396   5837     70   -729    255       C  
ATOM   5651  N   GLY B1030      17.173  26.185  12.528  1.00 49.31           N  
ANISOU 5651  N   GLY B1030     6675   6755   5304    306   -666     73       N  
ATOM   5652  CA  GLY B1030      17.212  27.125  11.403  1.00 50.23           C  
ANISOU 5652  CA  GLY B1030     6754   7016   5315    304   -611    121       C  
ATOM   5653  C   GLY B1030      18.476  27.952  11.265  1.00 56.45           C  
ANISOU 5653  C   GLY B1030     7452   7956   6039    268   -543    217       C  
ATOM   5654  O   GLY B1030      18.430  29.097  10.807  1.00 55.90           O  
ANISOU 5654  O   GLY B1030     7366   7950   5925    199   -495    320       O  
ATOM   5655  N   HIS B1031      19.596  27.336  11.561  1.00 55.14           N  
ANISOU 5655  N   HIS B1031     7221   7858   5871    321   -544    187       N  
ATOM   5656  CA  HIS B1031      20.840  28.032  11.494  1.00 56.40           C  
ANISOU 5656  CA  HIS B1031     7270   8171   5987    278   -486    285       C  
ATOM   5657  C   HIS B1031      21.568  27.769  10.210  1.00 63.83           C  
ANISOU 5657  C   HIS B1031     8107   9350   6795    399   -434    268       C  
ATOM   5658  O   HIS B1031      21.822  26.657   9.854  1.00 63.64           O  
ANISOU 5658  O   HIS B1031     8069   9380   6731    550   -461    145       O  
ATOM   5659  CB  HIS B1031      21.701  27.634  12.641  1.00 57.01           C  
ANISOU 5659  CB  HIS B1031     7318   8207   6136    263   -516    278       C  
ATOM   5660  CG  HIS B1031      23.019  28.307  12.633  1.00 61.27           C  
ANISOU 5660  CG  HIS B1031     7724   8907   6650    208   -471    379       C  
ATOM   5661  ND1 HIS B1031      23.193  29.587  13.079  1.00 62.84           N  
ANISOU 5661  ND1 HIS B1031     7911   9073   6893     46   -461    506       N  
ATOM   5662  CD2 HIS B1031      24.227  27.883  12.221  1.00 64.22           C  
ANISOU 5662  CD2 HIS B1031     7961   9476   6965    294   -440    374       C  
ATOM   5663  CE1 HIS B1031      24.454  29.928  12.946  1.00 63.42           C  
ANISOU 5663  CE1 HIS B1031     7839   9309   6948     13   -430    586       C  
ATOM   5664  NE2 HIS B1031      25.101  28.914  12.420  1.00 64.61           N  
ANISOU 5664  NE2 HIS B1031     7903   9616   7031    165   -407    513       N  
ATOM   5665  N   LEU B1032      21.877  28.839   9.523  1.00 63.26           N  
ANISOU 5665  N   LEU B1032     7966   9419   6653    334   -363    399       N  
ATOM   5666  CA  LEU B1032      22.437  28.751   8.222  1.00 65.50           C  
ANISOU 5666  CA  LEU B1032     8148   9956   6782    446   -296    412       C  
ATOM   5667  C   LEU B1032      23.901  28.927   8.370  1.00 73.25           C  
ANISOU 5667  C   LEU B1032     8969  11117   7747    429   -241    499       C  
ATOM   5668  O   LEU B1032      24.344  29.873   8.978  1.00 73.01           O  
ANISOU 5668  O   LEU B1032     8894  11053   7793    264   -228    638       O  
ATOM   5669  CB  LEU B1032      21.882  29.869   7.371  1.00 65.70           C  
ANISOU 5669  CB  LEU B1032     8185  10038   6739    375   -246    539       C  
ATOM   5670  CG  LEU B1032      22.093  29.685   5.889  1.00 71.89           C  
ANISOU 5670  CG  LEU B1032     8899  11082   7332    522   -183    536       C  
ATOM   5671  CD1 LEU B1032      21.549  28.383   5.441  1.00 72.00           C  
ANISOU 5671  CD1 LEU B1032     8983  11085   7290    716   -248    319       C  
ATOM   5672  CD2 LEU B1032      21.371  30.770   5.241  1.00 74.66           C  
ANISOU 5672  CD2 LEU B1032     9292  11436   7638    442   -155    664       C  
ATOM   5673  N   LEU B1033      24.647  27.991   7.823  1.00 72.96           N  
ANISOU 5673  N   LEU B1033     8843  11267   7613    608   -219    409       N  
ATOM   5674  CA  LEU B1033      26.075  28.037   7.791  1.00 75.25           C  
ANISOU 5674  CA  LEU B1033     8947  11781   7862    630   -156    485       C  
ATOM   5675  C   LEU B1033      26.271  28.908   6.601  1.00 83.54           C  
ANISOU 5675  C   LEU B1033     9898  13067   8775    610    -50    638       C  
ATOM   5676  O   LEU B1033      25.347  29.565   6.195  1.00 82.78           O  
ANISOU 5676  O   LEU B1033     9896  12893   8665    540    -48    691       O  
ATOM   5677  CB  LEU B1033      26.626  26.672   7.447  1.00 76.28           C  
ANISOU 5677  CB  LEU B1033     9034  12041   7910    875   -170    314       C  
ATOM   5678  CG  LEU B1033      26.266  25.688   8.558  1.00 79.54           C  
ANISOU 5678  CG  LEU B1033     9571  12190   8460    906   -289    163       C  
ATOM   5679  CD1 LEU B1033      27.181  24.532   8.598  1.00 80.94           C  
ANISOU 5679  CD1 LEU B1033     9676  12472   8605   1106   -313     39       C  
ATOM   5680  CD2 LEU B1033      26.294  26.353   9.881  1.00 80.37           C  
ANISOU 5680  CD2 LEU B1033     9703  12113   8723    699   -323    264       C  
ATOM   5681  N   THR B1034      27.503  28.982   6.109  1.00 84.17           N  
ANISOU 5681  N   THR B1034     9779  13441   8762    661     40    730       N  
ATOM   5682  CA  THR B1034      27.908  30.041   5.191  1.00 86.60           C  
ANISOU 5682  CA  THR B1034     9954  13983   8968    580    153    952       C  
ATOM   5683  C   THR B1034      27.847  29.682   3.713  1.00 94.26           C  
ANISOU 5683  C   THR B1034    10878  15236   9699    792    238    922       C  
ATOM   5684  O   THR B1034      27.286  28.657   3.326  1.00 94.20           O  
ANISOU 5684  O   THR B1034    10976  15207   9609    999    189    706       O  
ATOM   5685  CB  THR B1034      29.331  30.544   5.515  1.00 98.05           C  
ANISOU 5685  CB  THR B1034    11176  15617  10463    470    214   1129       C  
ATOM   5686  OG1 THR B1034      30.265  29.466   5.378  1.00 98.82           O  
ANISOU 5686  OG1 THR B1034    11140  15934  10474    683    242   1014       O  
ATOM   5687  CG2 THR B1034      29.394  31.087   6.934  1.00 96.38           C  
ANISOU 5687  CG2 THR B1034    11012  15131  10477    247    118   1172       C  
ATOM   5688  N   LYS B1035      28.433  30.551   2.894  1.00 93.29           N  
ANISOU 5688  N   LYS B1035    10599  15380   9468    735    359   1149       N  
ATOM   5689  CA  LYS B1035      28.419  30.383   1.451  1.00 95.13           C  
ANISOU 5689  CA  LYS B1035    10776  15924   9446    930    455   1161       C  
ATOM   5690  C   LYS B1035      28.990  29.160   0.745  1.00100.76           C  
ANISOU 5690  C   LYS B1035    11407  16919   9959   1250    495    979       C  
ATOM   5691  O   LYS B1035      28.718  28.955  -0.438  1.00101.94           O  
ANISOU 5691  O   LYS B1035    11564  17284   9884   1437    547    940       O  
ATOM   5692  CB  LYS B1035      29.054  31.655   0.883  1.00 99.62           C  
ANISOU 5692  CB  LYS B1035    11169  16718   9963    765    583   1492       C  
ATOM   5693  CG  LYS B1035      30.131  32.261   1.768  1.00115.31           C  
ANISOU 5693  CG  LYS B1035    12987  18699  12126    547    598   1672       C  
ATOM   5694  CD  LYS B1035      29.910  33.752   1.965  1.00125.29           C  
ANISOU 5694  CD  LYS B1035    14265  19812  13527    242    592   1940       C  
ATOM   5695  CE  LYS B1035      28.937  34.021   3.101  1.00131.93           C  
ANISOU 5695  CE  LYS B1035    15336  20205  14586     91    441   1835       C  
ATOM   5696  NZ  LYS B1035      28.581  35.463   3.198  1.00140.59           N  
ANISOU 5696  NZ  LYS B1035    16482  21133  15802   -167    419   2066       N  
ATOM   5697  N   SER B1036      29.779  28.345   1.442  1.00 96.93           N  
ANISOU 5697  N   SER B1036    10848  16438   9542   1332    463    860       N  
ATOM   5698  CA  SER B1036      30.355  27.203   0.757  1.00 98.35           C  
ANISOU 5698  CA  SER B1036    10951  16886   9530   1659    494    681       C  
ATOM   5699  C   SER B1036      29.348  26.207   0.202  1.00100.99           C  
ANISOU 5699  C   SER B1036    11493  17114   9766   1893    394    398       C  
ATOM   5700  O   SER B1036      28.281  26.024   0.767  1.00 98.41           O  
ANISOU 5700  O   SER B1036    11372  16432   9587   1807    265    284       O  
ATOM   5701  CB  SER B1036      31.244  26.491   1.747  1.00101.96           C  
ANISOU 5701  CB  SER B1036    11327  17299  10115   1698    446    590       C  
ATOM   5702  OG  SER B1036      30.914  26.936   3.049  1.00108.76           O  
ANISOU 5702  OG  SER B1036    12281  17807  11236   1433    353    641       O  
ATOM   5703  N   PRO B1037      29.724  25.563  -0.903  1.00 99.13           N  
ANISOU 5703  N   PRO B1037    11189  17201   9276   2194    450    288       N  
ATOM   5704  CA  PRO B1037      28.986  24.465  -1.535  1.00 98.89           C  
ANISOU 5704  CA  PRO B1037    11331  17115   9126   2469    340    -15       C  
ATOM   5705  C   PRO B1037      29.610  23.109  -1.222  1.00102.21           C  
ANISOU 5705  C   PRO B1037    11746  17534   9554   2722    262   -268       C  
ATOM   5706  O   PRO B1037      29.378  22.142  -1.947  1.00103.22           O  
ANISOU 5706  O   PRO B1037    11961  17725   9531   3016    190   -518       O  
ATOM   5707  CB  PRO B1037      29.120  24.773  -3.027  1.00103.30           C  
ANISOU 5707  CB  PRO B1037    11802  18082   9366   2651    465     50       C  
ATOM   5708  CG  PRO B1037      30.398  25.527  -3.136  1.00109.72           C  
ANISOU 5708  CG  PRO B1037    12335  19246  10109   2579    653    332       C  
ATOM   5709  CD  PRO B1037      30.500  26.346  -1.881  1.00103.20           C  
ANISOU 5709  CD  PRO B1037    11484  18149   9578   2216    637    528       C  
ATOM   5710  N   SER B1038      30.395  23.046  -0.151  1.00 96.83           N  
ANISOU 5710  N   SER B1038    10969  16776   9047   2617    262   -207       N  
ATOM   5711  CA  SER B1038      31.045  21.807   0.248  1.00 96.81           C  
ANISOU 5711  CA  SER B1038    10956  16757   9071   2847    183   -423       C  
ATOM   5712  C   SER B1038      30.630  21.388   1.654  1.00 96.71           C  
ANISOU 5712  C   SER B1038    11091  16304   9350   2688     30   -498       C  
ATOM   5713  O   SER B1038      30.781  22.154   2.604  1.00 94.54           O  
ANISOU 5713  O   SER B1038    10768  15903   9248   2411     53   -309       O  
ATOM   5714  CB  SER B1038      32.565  21.986   0.183  1.00102.26           C  
ANISOU 5714  CB  SER B1038    11355  17832   9667   2925    330   -284       C  
ATOM   5715  OG  SER B1038      33.234  20.743   0.289  1.00111.93           O  
ANISOU 5715  OG  SER B1038    12557  19114  10856   3225    265   -513       O  
ATOM   5716  N   LEU B1039      30.109  20.168   1.769  1.00 92.27           N  
ANISOU 5716  N   LEU B1039    10711  15511   8837   2869   -132   -770       N  
ATOM   5717  CA  LEU B1039      29.836  19.531   3.063  1.00 89.96           C  
ANISOU 5717  CA  LEU B1039    10549  14832   8799   2775   -279   -852       C  
ATOM   5718  C   LEU B1039      31.003  19.754   4.031  1.00 93.00           C  
ANISOU 5718  C   LEU B1039    10762  15292   9283   2688   -223   -713       C  
ATOM   5719  O   LEU B1039      30.798  20.098   5.187  1.00 90.50           O  
ANISOU 5719  O   LEU B1039    10491  14726   9168   2449   -267   -613       O  
ATOM   5720  CB  LEU B1039      29.589  18.025   2.863  1.00 91.11           C  
ANISOU 5720  CB  LEU B1039    10849  14827   8943   3063   -446  -1162       C  
ATOM   5721  CG  LEU B1039      28.744  17.230   3.871  1.00 94.17           C  
ANISOU 5721  CG  LEU B1039    11452  14749   9581   2977   -637  -1280       C  
ATOM   5722  CD1 LEU B1039      28.261  15.926   3.236  1.00 95.95           C  
ANISOU 5722  CD1 LEU B1039    11843  14846   9769   3253   -806  -1580       C  
ATOM   5723  CD2 LEU B1039      29.498  16.933   5.155  1.00 96.17           C  
ANISOU 5723  CD2 LEU B1039    11655  14884  10002   2917   -665  -1223       C  
ATOM   5724  N   ASN B1040      32.225  19.573   3.534  1.00 91.66           N  
ANISOU 5724  N   ASN B1040    10385  15485   8958   2892   -126   -708       N  
ATOM   5725  CA  ASN B1040      33.438  19.721   4.344  1.00 91.77           C  
ANISOU 5725  CA  ASN B1040    10202  15618   9049   2841    -78   -586       C  
ATOM   5726  C   ASN B1040      33.630  21.135   4.877  1.00 93.62           C  
ANISOU 5726  C   ASN B1040    10311  15880   9379   2490     19   -290       C  
ATOM   5727  O   ASN B1040      33.944  21.320   6.047  1.00 91.93           O  
ANISOU 5727  O   ASN B1040    10077  15505   9346   2318    -30   -212       O  
ATOM   5728  CB  ASN B1040      34.681  19.326   3.537  1.00 96.00           C  
ANISOU 5728  CB  ASN B1040    10508  16596   9373   3142     26   -625       C  
ATOM   5729  CG  ASN B1040      34.628  17.896   3.043  1.00121.13           C  
ANISOU 5729  CG  ASN B1040    13811  19755  12459   3525    -86   -940       C  
ATOM   5730  OD1 ASN B1040      33.714  17.516   2.310  1.00114.84           O  
ANISOU 5730  OD1 ASN B1040    13194  18861  11580   3638   -152  -1102       O  
ATOM   5731  ND2 ASN B1040      35.614  17.095   3.433  1.00115.25           N  
ANISOU 5731  ND2 ASN B1040    12968  19094  11727   3735   -121  -1036       N  
ATOM   5732  N   ALA B1041      33.452  22.123   4.006  1.00 90.12           N  
ANISOU 5732  N   ALA B1041     9792  15638   8811   2392    145   -127       N  
ATOM   5733  CA  ALA B1041      33.636  23.528   4.371  1.00 88.84           C  
ANISOU 5733  CA  ALA B1041     9515  15504   8737   2062    229    162       C  
ATOM   5734  C   ALA B1041      32.486  24.047   5.240  1.00 88.57           C  
ANISOU 5734  C   ALA B1041     9698  15051   8902   1789    128    192       C  
ATOM   5735  O   ALA B1041      32.657  25.013   5.990  1.00 87.01           O  
ANISOU 5735  O   ALA B1041     9449  14766   8844   1518    137    378       O  
ATOM   5736  CB  ALA B1041      33.793  24.390   3.115  1.00 91.31           C  
ANISOU 5736  CB  ALA B1041     9684  16161   8850   2055    392    341       C  
ATOM   5737  N   ALA B1042      31.316  23.417   5.122  1.00 83.06           N  
ANISOU 5737  N   ALA B1042     9238  14105   8217   1867     27      7       N  
ATOM   5738  CA  ALA B1042      30.193  23.688   6.022  1.00 79.78           C  
ANISOU 5738  CA  ALA B1042     9029  13295   7989   1652    -76      6       C  
ATOM   5739  C   ALA B1042      30.489  23.091   7.395  1.00 81.54           C  
ANISOU 5739  C   ALA B1042     9294  13295   8393   1618   -181    -56       C  
ATOM   5740  O   ALA B1042      30.293  23.749   8.419  1.00 79.53           O  
ANISOU 5740  O   ALA B1042     9078  12848   8291   1384   -213     54       O  
ATOM   5741  CB  ALA B1042      28.902  23.113   5.460  1.00 79.76           C  
ANISOU 5741  CB  ALA B1042     9238  13120   7949   1753   -156   -167       C  
ATOM   5742  N   LYS B1043      30.968  21.846   7.403  1.00 78.27           N  
ANISOU 5742  N   LYS B1043     8879  12909   7950   1865   -242   -235       N  
ATOM   5743  CA  LYS B1043      31.440  21.193   8.623  1.00 77.32           C  
ANISOU 5743  CA  LYS B1043     8776  12627   7977   1874   -337   -286       C  
ATOM   5744  C   LYS B1043      32.563  21.992   9.280  1.00 80.90           C  
ANISOU 5744  C   LYS B1043     9024  13235   8481   1724   -275    -99       C  
ATOM   5745  O   LYS B1043      32.702  21.986  10.503  1.00 79.37           O  
ANISOU 5745  O   LYS B1043     8864  12857   8436   1607   -352    -70       O  
ATOM   5746  CB  LYS B1043      31.918  19.764   8.339  1.00 81.38           C  
ANISOU 5746  CB  LYS B1043     9298  13191   8432   2198   -406   -501       C  
ATOM   5747  CG  LYS B1043      30.795  18.757   8.136  1.00 92.35           C  
ANISOU 5747  CG  LYS B1043    10928  14305   9855   2317   -537   -707       C  
ATOM   5748  CD  LYS B1043      31.312  17.321   8.063  1.00103.24           C  
ANISOU 5748  CD  LYS B1043    12338  15671  11218   2627   -640   -922       C  
ATOM   5749  CE  LYS B1043      32.304  17.115   6.929  1.00115.85           C  
ANISOU 5749  CE  LYS B1043    13758  17666  12595   2904   -548   -990       C  
ATOM   5750  NZ  LYS B1043      32.461  15.676   6.577  1.00126.35           N  
ANISOU 5750  NZ  LYS B1043    15178  18942  13886   3243   -673  -1254       N  
ATOM   5751  N   SER B1044      33.363  22.674   8.466  1.00 78.58           N  
ANISOU 5751  N   SER B1044     8511  13286   8061   1727   -142     32       N  
ATOM   5752  CA  SER B1044      34.391  23.578   8.976  1.00 78.58           C  
ANISOU 5752  CA  SER B1044     8296  13441   8121   1546    -86    236       C  
ATOM   5753  C   SER B1044      33.748  24.748   9.729  1.00 79.49           C  
ANISOU 5753  C   SER B1044     8504  13317   8383   1215   -116    386       C  
ATOM   5754  O   SER B1044      34.223  25.141  10.787  1.00 78.34           O  
ANISOU 5754  O   SER B1044     8310  13086   8371   1058   -170    465       O  
ATOM   5755  CB  SER B1044      35.266  24.087   7.826  1.00 84.20           C  
ANISOU 5755  CB  SER B1044     8750  14580   8663   1607     73    372       C  
ATOM   5756  OG  SER B1044      36.361  24.836   8.305  1.00 93.85           O  
ANISOU 5756  OG  SER B1044     9736  15967   9957   1442    114    567       O  
ATOM   5757  N   GLU B1045      32.659  25.287   9.182  1.00 74.45           N  
ANISOU 5757  N   GLU B1045     8002  12571   7714   1127    -92    413       N  
ATOM   5758  CA  GLU B1045      31.947  26.415   9.799  1.00 72.18           C  
ANISOU 5758  CA  GLU B1045     7818  12054   7552    843   -122    539       C  
ATOM   5759  C   GLU B1045      31.271  26.049  11.128  1.00 72.16           C  
ANISOU 5759  C   GLU B1045     8012  11700   7704    776   -254    441       C  
ATOM   5760  O   GLU B1045      31.345  26.811  12.094  1.00 70.52           O  
ANISOU 5760  O   GLU B1045     7816  11359   7618    574   -300    537       O  
ATOM   5761  CB  GLU B1045      30.913  27.009   8.825  1.00 73.24           C  
ANISOU 5761  CB  GLU B1045     8052  12171   7603    800    -66    582       C  
ATOM   5762  CG  GLU B1045      31.437  28.177   7.981  1.00 86.47           C  
ANISOU 5762  CG  GLU B1045     9552  14100   9204    679     55    811       C  
ATOM   5763  CD  GLU B1045      31.533  29.504   8.752  1.00110.15           C  
ANISOU 5763  CD  GLU B1045    12532  16961  12361    373     28   1004       C  
ATOM   5764  OE1 GLU B1045      31.263  29.533   9.975  1.00106.03           O  
ANISOU 5764  OE1 GLU B1045    12124  16172  11990    268    -82    951       O  
ATOM   5765  OE2 GLU B1045      31.886  30.524   8.122  1.00105.88           O  
ANISOU 5765  OE2 GLU B1045    11863  16579  11788    242    110   1212       O  
ATOM   5766  N   LEU B1046      30.608  24.896  11.174  1.00 67.19           N  
ANISOU 5766  N   LEU B1046     7539  10923   7068    945   -320    256       N  
ATOM   5767  CA  LEU B1046      29.968  24.443  12.408  1.00 64.89           C  
ANISOU 5767  CA  LEU B1046     7422  10321   6912    896   -435    182       C  
ATOM   5768  C   LEU B1046      31.031  24.343  13.502  1.00 68.08           C  
ANISOU 5768  C   LEU B1046     7726  10744   7396    867   -485    216       C  
ATOM   5769  O   LEU B1046      30.951  25.055  14.507  1.00 66.52           O  
ANISOU 5769  O   LEU B1046     7565  10411   7299    682   -530    299       O  
ATOM   5770  CB  LEU B1046      29.243  23.106  12.202  1.00 64.61           C  
ANISOU 5770  CB  LEU B1046     7539  10144   6866   1091   -505     -8       C  
ATOM   5771  CG  LEU B1046      28.510  22.481  13.402  1.00 67.74           C  
ANISOU 5771  CG  LEU B1046     8114  10225   7397   1054   -619    -71       C  
ATOM   5772  CD1 LEU B1046      27.483  23.421  14.035  1.00 65.96           C  
ANISOU 5772  CD1 LEU B1046     8005   9806   7250    831   -624     22       C  
ATOM   5773  CD2 LEU B1046      27.842  21.182  12.965  1.00 70.45           C  
ANISOU 5773  CD2 LEU B1046     8587  10445   7737   1239   -691   -243       C  
ATOM   5774  N   ASP B1047      32.039  23.498  13.264  1.00 65.50           N  
ANISOU 5774  N   ASP B1047     7270  10603   7016   1063   -482    149       N  
ATOM   5775  CA  ASP B1047      33.208  23.343  14.154  1.00 65.78           C  
ANISOU 5775  CA  ASP B1047     7171  10712   7109   1070   -528    180       C  
ATOM   5776  C   ASP B1047      33.684  24.645  14.786  1.00 69.25           C  
ANISOU 5776  C   ASP B1047     7506  11181   7625    814   -523    353       C  
ATOM   5777  O   ASP B1047      33.983  24.679  15.974  1.00 68.54           O  
ANISOU 5777  O   ASP B1047     7435  10976   7631    740   -614    365       O  
ATOM   5778  CB  ASP B1047      34.398  22.733  13.401  1.00 69.82           C  
ANISOU 5778  CB  ASP B1047     7472  11542   7515   1291   -472    143       C  
ATOM   5779  CG  ASP B1047      34.149  21.306  12.942  1.00 81.26           C  
ANISOU 5779  CG  ASP B1047     9022  12950   8902   1581   -515    -59       C  
ATOM   5780  OD1 ASP B1047      33.239  20.634  13.479  1.00 80.46           O  
ANISOU 5780  OD1 ASP B1047     9142  12553   8878   1601   -614   -161       O  
ATOM   5781  OD2 ASP B1047      34.873  20.857  12.024  1.00 89.37           O  
ANISOU 5781  OD2 ASP B1047     9904  14248   9803   1794   -453   -114       O  
ATOM   5782  N   LYS B1048      33.771  25.706  13.988  1.00 66.25           N  
ANISOU 5782  N   LYS B1048     7019  10951   7203    685   -429    489       N  
ATOM   5783  CA  LYS B1048      34.148  27.029  14.493  1.00 66.11           C  
ANISOU 5783  CA  LYS B1048     6916  10929   7275    422   -441    659       C  
ATOM   5784  C   LYS B1048      33.122  27.590  15.481  1.00 68.09           C  
ANISOU 5784  C   LYS B1048     7388  10852   7630    253   -529    652       C  
ATOM   5785  O   LYS B1048      33.502  28.106  16.527  1.00 67.26           O  
ANISOU 5785  O   LYS B1048     7272  10660   7623    116   -615    697       O  
ATOM   5786  CB  LYS B1048      34.341  28.028  13.343  1.00 69.55           C  
ANISOU 5786  CB  LYS B1048     7208  11570   7647    318   -322    823       C  
ATOM   5787  CG  LYS B1048      35.570  27.771  12.472  1.00 84.73           C  
ANISOU 5787  CG  LYS B1048     8851  13876   9468    443   -221    886       C  
ATOM   5788  CD  LYS B1048      35.649  28.763  11.303  1.00 94.91           C  
ANISOU 5788  CD  LYS B1048    10011  15371  10680    336    -93   1075       C  
ATOM   5789  CE  LYS B1048      36.564  28.270  10.182  1.00106.12           C  
ANISOU 5789  CE  LYS B1048    11189  17196  11934    538     39   1105       C  
ATOM   5790  NZ  LYS B1048      35.917  27.242   9.316  1.00112.77           N  
ANISOU 5790  NZ  LYS B1048    12155  18081  12611    820     83    922       N  
ATOM   5791  N   ALA B1049      31.832  27.501  15.151  1.00 63.60           N  
ANISOU 5791  N   ALA B1049     7015  10117   7035    271   -514    593       N  
ATOM   5792  CA  ALA B1049      30.778  28.085  16.005  1.00 61.75           C  
ANISOU 5792  CA  ALA B1049     6980   9599   6882    127   -581    593       C  
ATOM   5793  C   ALA B1049      30.485  27.236  17.237  1.00 64.82           C  
ANISOU 5793  C   ALA B1049     7505   9798   7325    195   -679    483       C  
ATOM   5794  O   ALA B1049      29.980  27.742  18.231  1.00 63.50           O  
ANISOU 5794  O   ALA B1049     7459   9446   7224     80   -745    495       O  
ATOM   5795  CB  ALA B1049      29.507  28.312  15.216  1.00 61.42           C  
ANISOU 5795  CB  ALA B1049     7076   9467   6795    123   -528    580       C  
ATOM   5796  N   ILE B1050      30.802  25.947  17.168  1.00 61.90           N  
ANISOU 5796  N   ILE B1050     7119   9477   6922    392   -692    379       N  
ATOM   5797  CA  ILE B1050      30.649  25.049  18.311  1.00 61.17           C  
ANISOU 5797  CA  ILE B1050     7141   9221   6881    467   -787    298       C  
ATOM   5798  C   ILE B1050      31.921  24.979  19.174  1.00 66.47           C  
ANISOU 5798  C   ILE B1050     7682   9986   7587    472   -854    324       C  
ATOM   5799  O   ILE B1050      31.831  24.834  20.398  1.00 65.53           O  
ANISOU 5799  O   ILE B1050     7655   9725   7519    445   -943    312       O  
ATOM   5800  CB  ILE B1050      30.213  23.631  17.851  1.00 64.14           C  
ANISOU 5800  CB  ILE B1050     7599   9546   7225    678   -795    170       C  
ATOM   5801  CG1 ILE B1050      28.801  23.681  17.254  1.00 63.29           C  
ANISOU 5801  CG1 ILE B1050     7642   9298   7105    652   -763    139       C  
ATOM   5802  CG2 ILE B1050      30.245  22.634  19.015  1.00 64.78           C  
ANISOU 5802  CG2 ILE B1050     7775   9473   7365    762   -896    114       C  
ATOM   5803  CD1 ILE B1050      27.706  24.059  18.250  1.00 68.03           C  
ANISOU 5803  CD1 ILE B1050     8412   9661   7774    520   -804    170       C  
ATOM   5804  N   GLY B1051      33.086  25.100  18.534  1.00 64.82           N  
ANISOU 5804  N   GLY B1051     7252  10032   7344    508   -810    366       N  
ATOM   5805  CA  GLY B1051      34.389  25.023  19.210  1.00 66.07           C  
ANISOU 5805  CA  GLY B1051     7245  10323   7537    522   -872    393       C  
ATOM   5806  C   GLY B1051      34.902  23.597  19.357  1.00 71.33           C  
ANISOU 5806  C   GLY B1051     7892  11033   8177    768   -912    285       C  
ATOM   5807  O   GLY B1051      35.631  23.286  20.306  1.00 71.67           O  
ANISOU 5807  O   GLY B1051     7888  11084   8261    802  -1002    280       O  
ATOM   5808  N   ARG B1052      34.536  22.733  18.410  1.00 68.24           N  
ANISOU 5808  N   ARG B1052     7541  10669   7719    950   -858    194       N  
ATOM   5809  CA  ARG B1052      34.783  21.295  18.523  1.00 68.74           C  
ANISOU 5809  CA  ARG B1052     7643  10705   7771   1199   -916     69       C  
ATOM   5810  C   ARG B1052      34.640  20.623  17.151  1.00 73.09           C  
ANISOU 5810  C   ARG B1052     8175  11369   8227   1395   -844    -29       C  
ATOM   5811  O   ARG B1052      33.841  21.062  16.330  1.00 71.98           O  
ANISOU 5811  O   ARG B1052     8094  11213   8043   1333   -773    -22       O  
ATOM   5812  CB  ARG B1052      33.779  20.696  19.511  1.00 67.65           C  
ANISOU 5812  CB  ARG B1052     7753  10249   7702   1190  -1010     23       C  
ATOM   5813  CG  ARG B1052      34.037  19.248  19.911  1.00 80.78           C  
ANISOU 5813  CG  ARG B1052     9480  11827   9387   1416  -1102    -78       C  
ATOM   5814  CD  ARG B1052      32.785  18.620  20.534  1.00 90.90           C  
ANISOU 5814  CD  ARG B1052    11013  12792  10732   1399  -1168   -106       C  
ATOM   5815  NE  ARG B1052      31.690  18.527  19.563  1.00 98.69           N  
ANISOU 5815  NE  ARG B1052    12105  13691  11703   1395  -1117   -160       N  
ATOM   5816  CZ  ARG B1052      30.423  18.238  19.858  1.00111.12           C  
ANISOU 5816  CZ  ARG B1052    13871  15017  13333   1333  -1148   -164       C  
ATOM   5817  NH1 ARG B1052      30.060  17.994  21.118  1.00 99.75           N  
ANISOU 5817  NH1 ARG B1052    12546  13394  11959   1273  -1218   -107       N  
ATOM   5818  NH2 ARG B1052      29.513  18.190  18.886  1.00 94.18           N  
ANISOU 5818  NH2 ARG B1052    11793  12820  11170   1333  -1109   -219       N  
ATOM   5819  N   ASN B1053      35.418  19.566  16.911  1.00 71.09           N  
ANISOU 5819  N   ASN B1053     7844  11232   7935   1647   -872   -128       N  
ATOM   5820  CA  ASN B1053      35.350  18.789  15.659  1.00 71.80           C  
ANISOU 5820  CA  ASN B1053     7929  11429   7923   1883   -828   -257       C  
ATOM   5821  C   ASN B1053      34.074  17.928  15.619  1.00 74.14           C  
ANISOU 5821  C   ASN B1053     8492  11416   8261   1947   -905   -381       C  
ATOM   5822  O   ASN B1053      34.063  16.787  16.096  1.00 74.22           O  
ANISOU 5822  O   ASN B1053     8611  11262   8329   2104  -1016   -482       O  
ATOM   5823  CB  ASN B1053      36.613  17.916  15.525  1.00 74.86           C  
ANISOU 5823  CB  ASN B1053     8154  12027   8262   2152   -851   -335       C  
ATOM   5824  CG  ASN B1053      36.751  17.247  14.149  1.00100.90           C  
ANISOU 5824  CG  ASN B1053    11406  15509  11421   2423   -795   -473       C  
ATOM   5825  OD1 ASN B1053      35.761  16.972  13.456  1.00 96.05           O  
ANISOU 5825  OD1 ASN B1053    10954  14767  10772   2464   -795   -566       O  
ATOM   5826  ND2 ASN B1053      37.995  16.970  13.759  1.00 94.55           N  
ANISOU 5826  ND2 ASN B1053    10374  15019  10532   2624   -752   -493       N  
ATOM   5827  N   THR B1054      33.007  18.486  15.044  1.00 68.96           N  
ANISOU 5827  N   THR B1054     7936  10681   7586   1820   -853   -363       N  
ATOM   5828  CA  THR B1054      31.674  17.856  15.057  1.00 67.41           C  
ANISOU 5828  CA  THR B1054     7979  10186   7449   1823   -927   -451       C  
ATOM   5829  C   THR B1054      31.536  16.672  14.094  1.00 72.98           C  
ANISOU 5829  C   THR B1054     8746  10882   8100   2090   -976   -640       C  
ATOM   5830  O   THR B1054      30.915  15.657  14.417  1.00 72.65           O  
ANISOU 5830  O   THR B1054     8879  10578   8149   2166  -1096   -737       O  
ATOM   5831  CB  THR B1054      30.557  18.882  14.694  1.00 71.70           C  
ANISOU 5831  CB  THR B1054     8594  10665   7985   1609   -859   -374       C  
ATOM   5832  OG1 THR B1054      30.888  19.563  13.477  1.00 70.94           O  
ANISOU 5832  OG1 THR B1054     8358  10841   7755   1630   -742   -348       O  
ATOM   5833  CG2 THR B1054      30.372  19.904  15.800  1.00 68.90           C  
ANISOU 5833  CG2 THR B1054     8252  10218   7709   1355   -850   -221       C  
ATOM   5834  N   ASN B1055      32.109  16.820  12.904  1.00 70.88           N  
ANISOU 5834  N   ASN B1055     8340  10906   7686   2232   -889   -688       N  
ATOM   5835  CA  ASN B1055      31.825  15.936  11.769  1.00 71.74           C  
ANISOU 5835  CA  ASN B1055     8517  11036   7706   2478   -925   -879       C  
ATOM   5836  C   ASN B1055      30.331  15.915  11.374  1.00 73.69           C  
ANISOU 5836  C   ASN B1055     8960  11049   7989   2384   -969   -930       C  
ATOM   5837  O   ASN B1055      29.809  14.892  10.923  1.00 74.04           O  
ANISOU 5837  O   ASN B1055     9143  10940   8048   2549  -1079  -1105       O  
ATOM   5838  CB  ASN B1055      32.357  14.526  12.035  1.00 73.40           C  
ANISOU 5838  CB  ASN B1055     8778  11152   7959   2746  -1055  -1039       C  
ATOM   5839  CG  ASN B1055      33.009  13.927  10.818  1.00 93.09           C  
ANISOU 5839  CG  ASN B1055    11186  13898  10288   3068  -1036  -1208       C  
ATOM   5840  OD1 ASN B1055      32.334  13.503   9.883  1.00 87.22           O  
ANISOU 5840  OD1 ASN B1055    10553  13108   9481   3188  -1075  -1356       O  
ATOM   5841  ND2 ASN B1055      34.337  13.907  10.813  1.00 86.39           N  
ANISOU 5841  ND2 ASN B1055    10129  13336   9360   3218   -977  -1189       N  
ATOM   5842  N   GLY B1056      29.657  17.054  11.550  1.00 67.91           N  
ANISOU 5842  N   GLY B1056     8238  10286   7279   2120   -894   -780       N  
ATOM   5843  CA  GLY B1056      28.271  17.221  11.107  1.00 66.32           C  
ANISOU 5843  CA  GLY B1056     8185   9914   7097   2021   -917   -807       C  
ATOM   5844  C   GLY B1056      27.160  16.926  12.104  1.00 67.50           C  
ANISOU 5844  C   GLY B1056     8516   9707   7425   1864  -1017   -782       C  
ATOM   5845  O   GLY B1056      26.009  17.244  11.820  1.00 65.98           O  
ANISOU 5845  O   GLY B1056     8418   9396   7255   1749  -1022   -773       O  
ATOM   5846  N   VAL B1057      27.487  16.318  13.251  1.00 62.87           N  
ANISOU 5846  N   VAL B1057     7969   8963   6957   1865  -1095   -763       N  
ATOM   5847  CA  VAL B1057      26.498  16.009  14.302  1.00 60.76           C  
ANISOU 5847  CA  VAL B1057     7857   8379   6849   1719  -1180   -710       C  
ATOM   5848  C   VAL B1057      26.743  16.872  15.536  1.00 62.36           C  
ANISOU 5848  C   VAL B1057     8017   8582   7096   1526  -1126   -534       C  
ATOM   5849  O   VAL B1057      27.892  17.109  15.906  1.00 62.24           O  
ANISOU 5849  O   VAL B1057     7878   8726   7042   1561  -1095   -491       O  
ATOM   5850  CB  VAL B1057      26.532  14.518  14.732  1.00 65.78           C  
ANISOU 5850  CB  VAL B1057     8606   8792   7597   1872  -1334   -815       C  
ATOM   5851  CG1 VAL B1057      27.934  14.100  15.191  1.00 67.04           C  
ANISOU 5851  CG1 VAL B1057     8667   9072   7734   2028  -1350   -826       C  
ATOM   5852  CG2 VAL B1057      25.514  14.253  15.844  1.00 64.38           C  
ANISOU 5852  CG2 VAL B1057     8568   8313   7580   1703  -1404   -718       C  
ATOM   5853  N   ILE B1058      25.659  17.341  16.163  1.00 56.72           N  
ANISOU 5853  N   ILE B1058     7399   7697   6456   1333  -1123   -441       N  
ATOM   5854  CA  ILE B1058      25.733  18.135  17.403  1.00 54.68           C  
ANISOU 5854  CA  ILE B1058     7131   7412   6233   1162  -1089   -293       C  
ATOM   5855  C   ILE B1058      24.648  17.684  18.378  1.00 56.87           C  
ANISOU 5855  C   ILE B1058     7556   7425   6625   1070  -1153   -240       C  
ATOM   5856  O   ILE B1058      23.780  16.890  18.022  1.00 56.54           O  
ANISOU 5856  O   ILE B1058     7611   7221   6649   1104  -1216   -301       O  
ATOM   5857  CB  ILE B1058      25.605  19.681  17.150  1.00 56.38           C  
ANISOU 5857  CB  ILE B1058     7275   7767   6381    995   -978   -197       C  
ATOM   5858  CG1 ILE B1058      24.254  20.039  16.522  1.00 55.58           C  
ANISOU 5858  CG1 ILE B1058     7258   7578   6283    911   -953   -202       C  
ATOM   5859  CG2 ILE B1058      26.748  20.198  16.282  1.00 57.61           C  
ANISOU 5859  CG2 ILE B1058     7261   8202   6428   1059   -904   -203       C  
ATOM   5860  CD1 ILE B1058      23.992  21.525  16.469  1.00 59.25           C  
ANISOU 5860  CD1 ILE B1058     7685   8123   6704    744   -864    -96       C  
ATOM   5861  N   THR B1059      24.710  18.198  19.602  1.00 52.53           N  
ANISOU 5861  N   THR B1059     7017   6844   6097    956  -1140   -124       N  
ATOM   5862  CA  THR B1059      23.746  17.862  20.638  1.00 51.88           C  
ANISOU 5862  CA  THR B1059     7057   6556   6101    870  -1180    -44       C  
ATOM   5863  C   THR B1059      22.663  18.930  20.746  1.00 55.09           C  
ANISOU 5863  C   THR B1059     7495   6943   6493    703  -1106     31       C  
ATOM   5864  O   THR B1059      22.803  20.036  20.222  1.00 54.38           O  
ANISOU 5864  O   THR B1059     7340   6990   6333    640  -1033     36       O  
ATOM   5865  CB  THR B1059      24.420  17.717  22.018  1.00 58.99           C  
ANISOU 5865  CB  THR B1059     7962   7439   7010    873  -1217     38       C  
ATOM   5866  OG1 THR B1059      25.032  18.957  22.381  1.00 57.82           O  
ANISOU 5866  OG1 THR B1059     7732   7450   6787    788  -1157     89       O  
ATOM   5867  CG2 THR B1059      25.477  16.608  22.008  1.00 58.42           C  
ANISOU 5867  CG2 THR B1059     7863   7374   6960   1054  -1301    -29       C  
ATOM   5868  N   LYS B1060      21.584  18.577  21.431  1.00 51.51           N  
ANISOU 5868  N   LYS B1060     7138   6322   6111    635  -1128     98       N  
ATOM   5869  CA  LYS B1060      20.475  19.483  21.687  1.00 50.40           C  
ANISOU 5869  CA  LYS B1060     7031   6158   5962    498  -1063    173       C  
ATOM   5870  C   LYS B1060      20.986  20.714  22.435  1.00 54.30           C  
ANISOU 5870  C   LYS B1060     7491   6765   6375    427  -1009    234       C  
ATOM   5871  O   LYS B1060      20.740  21.851  22.018  1.00 53.65           O  
ANISOU 5871  O   LYS B1060     7383   6757   6245    352   -948    239       O  
ATOM   5872  CB  LYS B1060      19.401  18.755  22.505  1.00 53.09           C  
ANISOU 5872  CB  LYS B1060     7458   6324   6390    453  -1095    258       C  
ATOM   5873  CG  LYS B1060      18.097  19.488  22.678  1.00 64.48           C  
ANISOU 5873  CG  LYS B1060     8924   7742   7832    336  -1031    329       C  
ATOM   5874  CD  LYS B1060      17.156  18.754  23.654  1.00 74.73           C  
ANISOU 5874  CD  LYS B1060    10282   8902   9210    291  -1051    448       C  
ATOM   5875  CE  LYS B1060      16.420  17.569  23.021  1.00 86.76           C  
ANISOU 5875  CE  LYS B1060    11830  10266  10868    294  -1129    426       C  
ATOM   5876  NZ  LYS B1060      17.103  16.262  23.266  1.00 98.56           N  
ANISOU 5876  NZ  LYS B1060    13362  11644  12442    382  -1233    416       N  
ATOM   5877  N   ASP B1061      21.720  20.480  23.523  1.00 51.19           N  
ANISOU 5877  N   ASP B1061     7102   6375   5971    457  -1046    278       N  
ATOM   5878  CA  ASP B1061      22.293  21.563  24.339  1.00 50.62           C  
ANISOU 5878  CA  ASP B1061     7007   6398   5830    399  -1027    321       C  
ATOM   5879  C   ASP B1061      23.113  22.561  23.534  1.00 53.06           C  
ANISOU 5879  C   ASP B1061     7212   6855   6092    368   -996    277       C  
ATOM   5880  O   ASP B1061      23.041  23.763  23.774  1.00 52.43           O  
ANISOU 5880  O   ASP B1061     7130   6816   5976    274   -968    308       O  
ATOM   5881  CB  ASP B1061      23.170  20.992  25.454  1.00 53.58           C  
ANISOU 5881  CB  ASP B1061     7387   6775   6197    465  -1095    353       C  
ATOM   5882  CG  ASP B1061      22.373  20.589  26.674  1.00 68.10           C  
ANISOU 5882  CG  ASP B1061     9329   8506   8041    451  -1106    448       C  
ATOM   5883  OD1 ASP B1061      22.583  19.467  27.189  1.00 70.28           O  
ANISOU 5883  OD1 ASP B1061     9639   8708   8356    529  -1165    484       O  
ATOM   5884  OD2 ASP B1061      21.544  21.411  27.127  1.00 75.14           O  
ANISOU 5884  OD2 ASP B1061    10266   9394   8892    372  -1056    494       O  
ATOM   5885  N   GLU B1062      23.895  22.050  22.593  1.00 48.81           N  
ANISOU 5885  N   GLU B1062     6590   6399   5556    453  -1004    212       N  
ATOM   5886  CA  GLU B1062      24.724  22.884  21.733  1.00 48.24           C  
ANISOU 5886  CA  GLU B1062     6396   6496   5437    430   -963    194       C  
ATOM   5887  C   GLU B1062      23.896  23.605  20.670  1.00 49.81           C  
ANISOU 5887  C   GLU B1062     6602   6709   5615    364   -894    192       C  
ATOM   5888  O   GLU B1062      24.293  24.670  20.167  1.00 49.00           O  
ANISOU 5888  O   GLU B1062     6424   6718   5475    291   -851    223       O  
ATOM   5889  CB  GLU B1062      25.791  22.019  21.066  1.00 50.85           C  
ANISOU 5889  CB  GLU B1062     6626   6937   5757    573   -984    127       C  
ATOM   5890  CG  GLU B1062      26.794  21.456  22.053  1.00 62.89           C  
ANISOU 5890  CG  GLU B1062     8119   8480   7296    644  -1056    135       C  
ATOM   5891  CD  GLU B1062      27.726  20.443  21.426  1.00 82.99           C  
ANISOU 5891  CD  GLU B1062    10579  11117   9836    821  -1085     56       C  
ATOM   5892  OE1 GLU B1062      27.221  19.538  20.723  1.00 71.39           O  
ANISOU 5892  OE1 GLU B1062     9166   9572   8385    923  -1098    -19       O  
ATOM   5893  OE2 GLU B1062      28.959  20.564  21.646  1.00 77.66           O  
ANISOU 5893  OE2 GLU B1062     9778  10591   9138    862  -1103     64       O  
ATOM   5894  N   ALA B1063      22.767  22.996  20.312  1.00 45.15           N  
ANISOU 5894  N   ALA B1063     6096   6004   5056    389   -894    162       N  
ATOM   5895  CA  ALA B1063      21.814  23.593  19.383  1.00 43.96           C  
ANISOU 5895  CA  ALA B1063     5965   5851   4888    335   -842    158       C  
ATOM   5896  C   ALA B1063      21.092  24.760  20.059  1.00 45.88           C  
ANISOU 5896  C   ALA B1063     6264   6041   5129    208   -813    234       C  
ATOM   5897  O   ALA B1063      20.782  25.758  19.405  1.00 44.79           O  
ANISOU 5897  O   ALA B1063     6112   5949   4960    144   -767    255       O  
ATOM   5898  CB  ALA B1063      20.818  22.553  18.908  1.00 44.74           C  
ANISOU 5898  CB  ALA B1063     6132   5833   5035    395   -874    100       C  
ATOM   5899  N   GLU B1064      20.846  24.628  21.369  1.00 41.73           N  
ANISOU 5899  N   GLU B1064     5804   5424   4626    186   -841    274       N  
ATOM   5900  CA  GLU B1064      20.213  25.697  22.155  1.00 40.52           C  
ANISOU 5900  CA  GLU B1064     5712   5229   4455     97   -822    330       C  
ATOM   5901  C   GLU B1064      21.140  26.896  22.336  1.00 43.94           C  
ANISOU 5901  C   GLU B1064     6098   5743   4855     31   -830    348       C  
ATOM   5902  O   GLU B1064      20.680  28.043  22.380  1.00 43.11           O  
ANISOU 5902  O   GLU B1064     6028   5617   4735    -44   -813    373       O  
ATOM   5903  CB  GLU B1064      19.735  25.202  23.534  1.00 41.59           C  
ANISOU 5903  CB  GLU B1064     5927   5275   4601    112   -846    372       C  
ATOM   5904  CG  GLU B1064      18.888  26.249  24.278  1.00 48.52           C  
ANISOU 5904  CG  GLU B1064     6873   6120   5441     54   -819    412       C  
ATOM   5905  CD  GLU B1064      18.202  25.736  25.538  1.00 65.85           C  
ANISOU 5905  CD  GLU B1064     9140   8256   7624     82   -820    469       C  
ATOM   5906  OE1 GLU B1064      18.540  24.636  26.018  1.00 63.91           O  
ANISOU 5906  OE1 GLU B1064     8897   7985   7402    133   -854    493       O  
ATOM   5907  OE2 GLU B1064      17.325  26.453  26.063  1.00 55.81           O  
ANISOU 5907  OE2 GLU B1064     7921   6971   6313     62   -786    497       O  
ATOM   5908  N   LYS B1065      22.437  26.616  22.454  1.00 40.62           N  
ANISOU 5908  N   LYS B1065     5595   5407   4432     60   -866    337       N  
ATOM   5909  CA  LYS B1065      23.449  27.663  22.584  1.00 40.53           C  
ANISOU 5909  CA  LYS B1065     5512   5478   4410    -16   -890    362       C  
ATOM   5910  C   LYS B1065      23.614  28.383  21.254  1.00 43.82           C  
ANISOU 5910  C   LYS B1065     5848   5983   4819    -70   -836    384       C  
ATOM   5911  O   LYS B1065      23.671  29.606  21.209  1.00 43.81           O  
ANISOU 5911  O   LYS B1065     5844   5978   4823   -175   -840    430       O  
ATOM   5912  CB  LYS B1065      24.781  27.085  23.082  1.00 43.49           C  
ANISOU 5912  CB  LYS B1065     5801   5936   4789     35   -947    351       C  
ATOM   5913  CG  LYS B1065      24.714  26.644  24.545  1.00 56.65           C  
ANISOU 5913  CG  LYS B1065     7552   7525   6448     73  -1011    351       C  
ATOM   5914  CD  LYS B1065      26.094  26.366  25.137  1.00 68.45           C  
ANISOU 5914  CD  LYS B1065     8958   9109   7943    108  -1085    345       C  
ATOM   5915  CE  LYS B1065      26.020  26.118  26.648  1.00 78.76           C  
ANISOU 5915  CE  LYS B1065    10357  10348   9219    142  -1156    354       C  
ATOM   5916  NZ  LYS B1065      27.350  25.734  27.216  1.00 86.90           N  
ANISOU 5916  NZ  LYS B1065    11300  11470  10249    193  -1240    346       N  
ATOM   5917  N   LEU B1066      23.652  27.616  20.174  1.00 40.02           N  
ANISOU 5917  N   LEU B1066     5312   5574   4321     11   -794    353       N  
ATOM   5918  CA  LEU B1066      23.752  28.175  18.837  1.00 40.12           C  
ANISOU 5918  CA  LEU B1066     5249   5696   4300    -15   -733    381       C  
ATOM   5919  C   LEU B1066      22.486  28.995  18.480  1.00 43.54           C  
ANISOU 5919  C   LEU B1066     5775   6037   4729    -82   -702    407       C  
ATOM   5920  O   LEU B1066      22.554  30.038  17.817  1.00 43.39           O  
ANISOU 5920  O   LEU B1066     5722   6067   4696   -161   -671    472       O  
ATOM   5921  CB  LEU B1066      23.973  27.035  17.847  1.00 40.68           C  
ANISOU 5921  CB  LEU B1066     5261   5862   4333    124   -706    314       C  
ATOM   5922  CG  LEU B1066      24.524  27.404  16.481  1.00 46.51           C  
ANISOU 5922  CG  LEU B1066     5879   6789   5003    140   -640    343       C  
ATOM   5923  CD1 LEU B1066      25.567  28.523  16.589  1.00 47.43           C  
ANISOU 5923  CD1 LEU B1066     5876   7017   5127     19   -628    451       C  
ATOM   5924  CD2 LEU B1066      25.105  26.159  15.828  1.00 50.16           C  
ANISOU 5924  CD2 LEU B1066     6272   7367   5420    314   -636    254       C  
ATOM   5925  N   PHE B1067      21.341  28.502  18.937  1.00 38.62           N  
ANISOU 5925  N   PHE B1067     5264   5285   4126    -48   -712    369       N  
ATOM   5926  CA  PHE B1067      20.072  29.200  18.821  1.00 37.11           C  
ANISOU 5926  CA  PHE B1067     5161   5004   3936    -95   -691    389       C  
ATOM   5927  C   PHE B1067      20.033  30.501  19.645  1.00 39.58           C  
ANISOU 5927  C   PHE B1067     5525   5252   4262   -191   -715    438       C  
ATOM   5928  O   PHE B1067      19.460  31.507  19.209  1.00 39.05           O  
ANISOU 5928  O   PHE B1067     5492   5154   4190   -245   -699    474       O  
ATOM   5929  CB  PHE B1067      18.953  28.257  19.271  1.00 38.26           C  
ANISOU 5929  CB  PHE B1067     5386   5042   4109    -38   -699    350       C  
ATOM   5930  CG  PHE B1067      17.633  28.927  19.456  1.00 39.03           C  
ANISOU 5930  CG  PHE B1067     5563   5054   4212    -76   -681    374       C  
ATOM   5931  CD1 PHE B1067      16.910  29.369  18.355  1.00 42.00           C  
ANISOU 5931  CD1 PHE B1067     5938   5449   4572    -84   -650    377       C  
ATOM   5932  CD2 PHE B1067      17.114  29.113  20.733  1.00 40.43           C  
ANISOU 5932  CD2 PHE B1067     5813   5150   4398    -88   -694    393       C  
ATOM   5933  CE1 PHE B1067      15.680  29.994  18.528  1.00 42.73           C  
ANISOU 5933  CE1 PHE B1067     6094   5470   4670   -105   -636    398       C  
ATOM   5934  CE2 PHE B1067      15.898  29.732  20.924  1.00 42.90           C  
ANISOU 5934  CE2 PHE B1067     6188   5406   4707   -101   -671    412       C  
ATOM   5935  CZ  PHE B1067      15.168  30.171  19.832  1.00 41.31           C  
ANISOU 5935  CZ  PHE B1067     5979   5214   4502   -110   -643    414       C  
ATOM   5936  N   ASN B1068      20.625  30.472  20.835  1.00 35.15           N  
ANISOU 5936  N   ASN B1068     4978   4663   3713   -201   -767    432       N  
ATOM   5937  CA  ASN B1068      20.640  31.649  21.706  1.00 34.62           C  
ANISOU 5937  CA  ASN B1068     4974   4526   3654   -275   -816    451       C  
ATOM   5938  C   ASN B1068      21.405  32.785  21.029  1.00 38.99           C  
ANISOU 5938  C   ASN B1068     5461   5124   4231   -379   -831    507       C  
ATOM   5939  O   ASN B1068      21.031  33.950  21.162  1.00 39.33           O  
ANISOU 5939  O   ASN B1068     5570   5083   4292   -446   -860    531       O  
ATOM   5940  CB  ASN B1068      21.264  31.338  23.091  1.00 33.03           C  
ANISOU 5940  CB  ASN B1068     4794   4309   3449   -254   -885    425       C  
ATOM   5941  CG  ASN B1068      20.318  30.579  24.022  1.00 47.52           C  
ANISOU 5941  CG  ASN B1068     6722   6078   5255   -172   -874    402       C  
ATOM   5942  OD1 ASN B1068      19.110  30.539  23.814  1.00 41.58           O  
ANISOU 5942  OD1 ASN B1068     6026   5276   4497   -149   -825    407       O  
ATOM   5943  ND2 ASN B1068      20.875  29.979  25.059  1.00 39.28           N  
ANISOU 5943  ND2 ASN B1068     5686   5044   4195   -128   -921    391       N  
ATOM   5944  N   GLN B1069      22.470  32.439  20.308  1.00 35.26           N  
ANISOU 5944  N   GLN B1069     4853   4783   3759   -388   -812    536       N  
ATOM   5945  CA  GLN B1069      23.281  33.434  19.615  1.00 36.01           C  
ANISOU 5945  CA  GLN B1069     4855   4948   3881   -498   -816    622       C  
ATOM   5946  C   GLN B1069      22.471  34.064  18.483  1.00 41.57           C  
ANISOU 5946  C   GLN B1069     5586   5643   4566   -522   -756    676       C  
ATOM   5947  O   GLN B1069      22.533  35.277  18.277  1.00 42.11           O  
ANISOU 5947  O   GLN B1069     5666   5662   4671   -631   -782    753       O  
ATOM   5948  CB  GLN B1069      24.577  32.809  19.076  1.00 37.90           C  
ANISOU 5948  CB  GLN B1069     4920   5371   4109   -479   -791    648       C  
ATOM   5949  CG  GLN B1069      25.559  32.399  20.167  1.00 47.41           C  
ANISOU 5949  CG  GLN B1069     6076   6595   5341   -471   -867    614       C  
ATOM   5950  CD  GLN B1069      26.680  31.488  19.687  1.00 62.82           C  
ANISOU 5950  CD  GLN B1069     7863   8736   7270   -398   -836    615       C  
ATOM   5951  OE1 GLN B1069      26.543  30.751  18.716  1.00 57.44           O  
ANISOU 5951  OE1 GLN B1069     7137   8151   6535   -298   -759    596       O  
ATOM   5952  NE2 GLN B1069      27.797  31.529  20.388  1.00 57.82           N  
ANISOU 5952  NE2 GLN B1069     7137   8159   6674   -433   -906    626       N  
ATOM   5953  N   ASP B1070      21.712  33.233  17.766  1.00 38.29           N  
ANISOU 5953  N   ASP B1070     5186   5265   4099   -421   -691    635       N  
ATOM   5954  CA  ASP B1070      20.827  33.703  16.705  1.00 38.44           C  
ANISOU 5954  CA  ASP B1070     5237   5282   4086   -420   -641    672       C  
ATOM   5955  C   ASP B1070      19.731  34.628  17.242  1.00 42.77           C  
ANISOU 5955  C   ASP B1070     5923   5662   4664   -457   -676    673       C  
ATOM   5956  O   ASP B1070      19.508  35.723  16.696  1.00 42.64           O  
ANISOU 5956  O   ASP B1070     5929   5613   4659   -523   -678    750       O  
ATOM   5957  CB  ASP B1070      20.171  32.522  15.982  1.00 39.63           C  
ANISOU 5957  CB  ASP B1070     5387   5488   4182   -295   -593    600       C  
ATOM   5958  CG  ASP B1070      21.175  31.640  15.270  1.00 49.18           C  
ANISOU 5958  CG  ASP B1070     6471   6872   5344   -224   -560    583       C  
ATOM   5959  OD1 ASP B1070      22.116  32.179  14.643  1.00 49.34           O  
ANISOU 5959  OD1 ASP B1070     6380   7027   5338   -273   -529    669       O  
ATOM   5960  OD2 ASP B1070      21.012  30.396  15.345  1.00 56.16           O  
ANISOU 5960  OD2 ASP B1070     7364   7757   6218   -115   -567    488       O  
ATOM   5961  N   VAL B1071      19.045  34.162  18.293  1.00 38.72           N  
ANISOU 5961  N   VAL B1071     5498   5053   4160   -401   -701    596       N  
ATOM   5962  CA  VAL B1071      18.016  34.940  18.979  1.00 38.03           C  
ANISOU 5962  CA  VAL B1071     5535   4829   4087   -403   -730    581       C  
ATOM   5963  C   VAL B1071      18.585  36.291  19.353  1.00 42.94           C  
ANISOU 5963  C   VAL B1071     6189   5374   4752   -503   -801    625       C  
ATOM   5964  O   VAL B1071      17.914  37.306  19.244  1.00 43.25           O  
ANISOU 5964  O   VAL B1071     6309   5317   4805   -523   -824    647       O  
ATOM   5965  CB  VAL B1071      17.534  34.253  20.297  1.00 40.99           C  
ANISOU 5965  CB  VAL B1071     5976   5146   4454   -334   -748    510       C  
ATOM   5966  CG1 VAL B1071      16.723  35.236  21.159  1.00 40.85           C  
ANISOU 5966  CG1 VAL B1071     6077   5011   4432   -326   -785    491       C  
ATOM   5967  CG2 VAL B1071      16.747  32.985  20.008  1.00 39.72           C  
ANISOU 5967  CG2 VAL B1071     5799   5016   4276   -251   -694    478       C  
ATOM   5968  N   ASP B1072      19.830  36.292  19.805  1.00 39.75           N  
ANISOU 5968  N   ASP B1072     5720   5007   4378   -564   -850    636       N  
ATOM   5969  CA  ASP B1072      20.516  37.530  20.157  1.00 40.61           C  
ANISOU 5969  CA  ASP B1072     5844   5035   4550   -681   -943    679       C  
ATOM   5970  C   ASP B1072      20.714  38.417  18.905  1.00 44.34           C  
ANISOU 5970  C   ASP B1072     6265   5528   5055   -778   -922    803       C  
ATOM   5971  O   ASP B1072      20.301  39.573  18.891  1.00 44.50           O  
ANISOU 5971  O   ASP B1072     6374   5415   5120   -832   -978    838       O  
ATOM   5972  CB  ASP B1072      21.864  37.218  20.847  1.00 43.30           C  
ANISOU 5972  CB  ASP B1072     6096   5434   4921   -729  -1004    669       C  
ATOM   5973  CG  ASP B1072      22.252  38.254  21.895  1.00 57.13           C  
ANISOU 5973  CG  ASP B1072     7923   7052   6733   -807  -1143    642       C  
ATOM   5974  OD1 ASP B1072      21.502  39.236  22.104  1.00 59.06           O  
ANISOU 5974  OD1 ASP B1072     8297   7148   6996   -815  -1194    625       O  
ATOM   5975  OD2 ASP B1072      23.318  38.083  22.520  1.00 63.25           O  
ANISOU 5975  OD2 ASP B1072     8629   7868   7536   -849  -1213    628       O  
ATOM   5976  N   ALA B1073      21.320  37.865  17.856  1.00 40.62           N  
ANISOU 5976  N   ALA B1073     5654   5226   4554   -785   -844    871       N  
ATOM   5977  CA  ALA B1073      21.598  38.627  16.630  1.00 41.32           C  
ANISOU 5977  CA  ALA B1073     5674   5375   4652   -872   -809   1014       C  
ATOM   5978  C   ALA B1073      20.294  39.148  16.013  1.00 45.09           C  
ANISOU 5978  C   ALA B1073     6263   5768   5100   -828   -783   1030       C  
ATOM   5979  O   ALA B1073      20.226  40.282  15.535  1.00 44.86           O  
ANISOU 5979  O   ALA B1073     6264   5667   5114   -916   -812   1139       O  
ATOM   5980  CB  ALA B1073      22.365  37.769  15.638  1.00 42.29           C  
ANISOU 5980  CB  ALA B1073     5629   5731   4709   -838   -713   1063       C  
ATOM   5981  N   ALA B1074      19.258  38.306  16.065  1.00 41.08           N  
ANISOU 5981  N   ALA B1074     5814   5265   4531   -696   -737    927       N  
ATOM   5982  CA  ALA B1074      17.896  38.676  15.671  1.00 40.46           C  
ANISOU 5982  CA  ALA B1074     5839   5109   4427   -634   -722    917       C  
ATOM   5983  C   ALA B1074      17.360  39.863  16.462  1.00 45.53           C  
ANISOU 5983  C   ALA B1074     6616   5551   5131   -666   -810    908       C  
ATOM   5984  O   ALA B1074      16.803  40.796  15.890  1.00 45.83           O  
ANISOU 5984  O   ALA B1074     6715   5517   5183   -682   -825    975       O  
ATOM   5985  CB  ALA B1074      16.961  37.485  15.836  1.00 39.77           C  
ANISOU 5985  CB  ALA B1074     5773   5052   4287   -504   -677    803       C  
ATOM   5986  N   VAL B1075      17.517  39.828  17.778  1.00 42.71           N  
ANISOU 5986  N   VAL B1075     6316   5108   4804   -658   -873    820       N  
ATOM   5987  CA  VAL B1075      16.931  40.871  18.623  1.00 43.38           C  
ANISOU 5987  CA  VAL B1075     6545   5010   4929   -648   -964    775       C  
ATOM   5988  C   VAL B1075      17.652  42.211  18.427  1.00 50.30           C  
ANISOU 5988  C   VAL B1075     7444   5770   5897   -786  -1062    870       C  
ATOM   5989  O   VAL B1075      17.008  43.273  18.464  1.00 51.20           O  
ANISOU 5989  O   VAL B1075     7678   5728   6048   -778  -1128    876       O  
ATOM   5990  CB  VAL B1075      16.867  40.440  20.109  1.00 46.61           C  
ANISOU 5990  CB  VAL B1075     7014   5378   5318   -580  -1006    649       C  
ATOM   5991  CG1 VAL B1075      16.595  41.640  21.026  1.00 47.45           C  
ANISOU 5991  CG1 VAL B1075     7266   5303   5460   -571  -1125    592       C  
ATOM   5992  CG2 VAL B1075      15.795  39.366  20.291  1.00 44.94           C  
ANISOU 5992  CG2 VAL B1075     6806   5237   5031   -446   -916    584       C  
ATOM   5993  N   ARG B1076      18.967  42.140  18.183  1.00 47.86           N  
ANISOU 5993  N   ARG B1076     7013   5540   5632   -909  -1074    950       N  
ATOM   5994  CA  ARG B1076      19.808  43.314  17.857  1.00 49.41           C  
ANISOU 5994  CA  ARG B1076     7188   5649   5936  -1077  -1163   1080       C  
ATOM   5995  C   ARG B1076      19.304  44.114  16.649  1.00 54.01           C  
ANISOU 5995  C   ARG B1076     7793   6199   6529  -1111  -1134   1220       C  
ATOM   5996  O   ARG B1076      19.218  45.337  16.710  1.00 55.47           O  
ANISOU 5996  O   ARG B1076     8074   6195   6806  -1187  -1241   1277       O  
ATOM   5997  CB  ARG B1076      21.256  42.878  17.587  1.00 50.33           C  
ANISOU 5997  CB  ARG B1076     7118   5926   6080  -1192  -1141   1166       C  
ATOM   5998  CG  ARG B1076      22.289  43.324  18.617  1.00 61.26           C  
ANISOU 5998  CG  ARG B1076     8489   7220   7567  -1306  -1282   1141       C  
ATOM   5999  CD  ARG B1076      22.139  42.662  19.985  1.00 68.20           C  
ANISOU 5999  CD  ARG B1076     9440   8071   8403  -1196  -1329    955       C  
ATOM   6000  NE  ARG B1076      23.441  42.241  20.531  1.00 79.05           N  
ANISOU 6000  NE  ARG B1076    10686   9535   9813  -1269  -1379    950       N  
ATOM   6001  CZ  ARG B1076      24.413  43.060  20.955  1.00 94.67           C  
ANISOU 6001  CZ  ARG B1076    12630  11428  11911  -1424  -1523    990       C  
ATOM   6002  NH1 ARG B1076      24.270  44.388  20.905  1.00 84.00           N  
ANISOU 6002  NH1 ARG B1076    11376   9873  10667  -1533  -1643   1042       N  
ATOM   6003  NH2 ARG B1076      25.553  42.544  21.424  1.00 79.29           N  
ANISOU 6003  NH2 ARG B1076    10548   9593   9986  -1472  -1561    981       N  
ATOM   6004  N   GLY B1077      18.984  43.417  15.556  1.00 49.15           N  
ANISOU 6004  N   GLY B1077     7095   5762   5818  -1049  -1002   1273       N  
ATOM   6005  CA  GLY B1077      18.517  44.058  14.323  1.00 49.35           C  
ANISOU 6005  CA  GLY B1077     7131   5796   5825  -1064   -964   1415       C  
ATOM   6006  C   GLY B1077      17.145  44.693  14.453  1.00 52.62           C  
ANISOU 6006  C   GLY B1077     7713   6041   6238   -965  -1007   1358       C  
ATOM   6007  O   GLY B1077      16.830  45.677  13.759  1.00 53.52           O  
ANISOU 6007  O   GLY B1077     7883   6066   6384  -1003  -1039   1481       O  
ATOM   6008  N   ILE B1078      16.326  44.110  15.327  1.00 47.33           N  
ANISOU 6008  N   ILE B1078     7116   5339   5527   -832  -1004   1185       N  
ATOM   6009  CA  ILE B1078      15.008  44.650  15.671  1.00 46.69           C  
ANISOU 6009  CA  ILE B1078     7184   5116   5441   -715  -1045   1107       C  
ATOM   6010  C   ILE B1078      15.167  46.011  16.342  1.00 52.03           C  
ANISOU 6010  C   ILE B1078     7993   5550   6227   -775  -1194   1111       C  
ATOM   6011  O   ILE B1078      14.463  46.969  16.009  1.00 52.40           O  
ANISOU 6011  O   ILE B1078     8146   5459   6304   -743  -1248   1152       O  
ATOM   6012  CB  ILE B1078      14.247  43.695  16.638  1.00 48.07           C  
ANISOU 6012  CB  ILE B1078     7383   5330   5552   -574  -1007    935       C  
ATOM   6013  CG1 ILE B1078      13.868  42.395  15.914  1.00 46.63           C  
ANISOU 6013  CG1 ILE B1078     7092   5344   5280   -506   -883    924       C  
ATOM   6014  CG2 ILE B1078      13.016  44.399  17.255  1.00 48.76           C  
ANISOU 6014  CG2 ILE B1078     7618   5271   5639   -450  -1061    850       C  
ATOM   6015  CD1 ILE B1078      13.798  41.189  16.818  1.00 48.95           C  
ANISOU 6015  CD1 ILE B1078     7353   5709   5538   -440   -845    804       C  
ATOM   6016  N   LEU B1079      16.109  46.083  17.280  1.00 49.24           N  
ANISOU 6016  N   LEU B1079     7636   5138   5935   -857  -1276   1062       N  
ATOM   6017  CA  LEU B1079      16.416  47.331  17.991  1.00 50.64           C  
ANISOU 6017  CA  LEU B1079     7940   5073   6230   -926  -1449   1045       C  
ATOM   6018  C   LEU B1079      17.192  48.328  17.108  1.00 56.20           C  
ANISOU 6018  C   LEU B1079     8612   5688   7053  -1114  -1515   1249       C  
ATOM   6019  O   LEU B1079      17.450  49.452  17.528  1.00 57.92           O  
ANISOU 6019  O   LEU B1079     8938   5674   7394  -1194  -1677   1260       O  
ATOM   6020  CB  LEU B1079      17.179  47.037  19.294  1.00 50.64           C  
ANISOU 6020  CB  LEU B1079     7941   5050   6250   -949  -1528    919       C  
ATOM   6021  CG  LEU B1079      16.488  46.059  20.269  1.00 53.56           C  
ANISOU 6021  CG  LEU B1079     8340   5510   6501   -771  -1465    742       C  
ATOM   6022  CD1 LEU B1079      17.342  45.805  21.507  1.00 54.05           C  
ANISOU 6022  CD1 LEU B1079     8403   5561   6573   -796  -1552    636       C  
ATOM   6023  CD2 LEU B1079      15.108  46.544  20.677  1.00 55.29           C  
ANISOU 6023  CD2 LEU B1079     8714   5621   6671   -596  -1485    639       C  
ATOM   6024  N   ARG B1080      17.570  47.906  15.902  1.00 52.23           N  
ANISOU 6024  N   ARG B1080     7962   5373   6511  -1183  -1394   1412       N  
ATOM   6025  CA  ARG B1080      18.100  48.807  14.873  1.00 53.89           C  
ANISOU 6025  CA  ARG B1080     8131   5541   6805  -1341  -1421   1645       C  
ATOM   6026  C   ARG B1080      17.030  49.228  13.841  1.00 58.47           C  
ANISOU 6026  C   ARG B1080     8780   6105   7329  -1254  -1372   1735       C  
ATOM   6027  O   ARG B1080      17.185  50.227  13.148  1.00 59.69           O  
ANISOU 6027  O   ARG B1080     8964   6153   7564  -1358  -1428   1919       O  
ATOM   6028  CB  ARG B1080      19.295  48.153  14.166  1.00 53.82           C  
ANISOU 6028  CB  ARG B1080     7901   5778   6771  -1466  -1316   1790       C  
ATOM   6029  CG  ARG B1080      20.572  48.121  15.011  1.00 63.59           C  
ANISOU 6029  CG  ARG B1080     9054   6999   8110  -1609  -1402   1772       C  
ATOM   6030  CD  ARG B1080      21.835  47.997  14.164  1.00 74.29           C  
ANISOU 6030  CD  ARG B1080    10188   8551   9487  -1776  -1333   1987       C  
ATOM   6031  NE  ARG B1080      22.399  46.644  14.170  1.00 84.84           N  
ANISOU 6031  NE  ARG B1080    11360  10163  10714  -1712  -1207   1920       N  
ATOM   6032  CZ  ARG B1080      23.358  46.208  14.997  1.00101.40           C  
ANISOU 6032  CZ  ARG B1080    13365  12306  12858  -1768  -1253   1850       C  
ATOM   6033  NH1 ARG B1080      23.888  47.006  15.931  1.00 90.79           N  
ANISOU 6033  NH1 ARG B1080    12074  10757  11667  -1898  -1430   1828       N  
ATOM   6034  NH2 ARG B1080      23.794  44.953  14.896  1.00 86.47           N  
ANISOU 6034  NH2 ARG B1080    11331  10664  10859  -1685  -1134   1794       N  
ATOM   6035  N   ASN B1081      15.953  48.455  13.746  1.00 54.09           N  
ANISOU 6035  N   ASN B1081     8247   5660   6645  -1067  -1275   1613       N  
ATOM   6036  CA  ASN B1081      14.828  48.761  12.861  1.00 54.10           C  
ANISOU 6036  CA  ASN B1081     8311   5660   6584   -957  -1238   1666       C  
ATOM   6037  C   ASN B1081      13.849  49.672  13.586  1.00 58.25           C  
ANISOU 6037  C   ASN B1081     9032   5932   7168   -852  -1361   1560       C  
ATOM   6038  O   ASN B1081      13.409  49.350  14.692  1.00 57.19           O  
ANISOU 6038  O   ASN B1081     8960   5754   7017   -743  -1386   1365       O  
ATOM   6039  CB  ASN B1081      14.134  47.458  12.438  1.00 52.48           C  
ANISOU 6039  CB  ASN B1081     8023   5693   6225   -811  -1093   1577       C  
ATOM   6040  CG  ASN B1081      13.210  47.639  11.251  1.00 69.15           C  
ANISOU 6040  CG  ASN B1081    10149   7868   8257   -724  -1044   1665       C  
ATOM   6041  OD1 ASN B1081      12.232  48.371  11.330  1.00 66.91           O  
ANISOU 6041  OD1 ASN B1081     9993   7434   7996   -634  -1109   1642       O  
ATOM   6042  ND2 ASN B1081      13.505  46.955  10.154  1.00 56.01           N  
ANISOU 6042  ND2 ASN B1081     8356   6436   6489   -731   -934   1755       N  
ATOM   6043  N   ALA B1082      13.507  50.800  12.964  1.00 56.00           N  
ANISOU 6043  N   ALA B1082     8843   5489   6945   -871  -1437   1692       N  
ATOM   6044  CA  ALA B1082      12.687  51.830  13.616  1.00 56.82           C  
ANISOU 6044  CA  ALA B1082     9145   5323   7122   -769  -1579   1600       C  
ATOM   6045  C   ALA B1082      11.216  51.452  13.662  1.00 59.08           C  
ANISOU 6045  C   ALA B1082     9478   5674   7294   -534  -1518   1464       C  
ATOM   6046  O   ALA B1082      10.498  51.881  14.554  1.00 58.95           O  
ANISOU 6046  O   ALA B1082     9593   5510   7295   -396  -1599   1310       O  
ATOM   6047  CB  ALA B1082      12.858  53.182  12.928  1.00 60.05           C  
ANISOU 6047  CB  ALA B1082     9645   5518   7651   -872  -1697   1800       C  
ATOM   6048  N   LYS B1083      10.769  50.667  12.689  1.00 54.17           N  
ANISOU 6048  N   LYS B1083     8746   5281   6557   -482  -1381   1521       N  
ATOM   6049  CA  LYS B1083       9.396  50.164  12.675  1.00 52.55           C  
ANISOU 6049  CA  LYS B1083     8548   5170   6250   -278  -1318   1401       C  
ATOM   6050  C   LYS B1083       9.158  49.095  13.758  1.00 54.53           C  
ANISOU 6050  C   LYS B1083     8749   5525   6445   -195  -1257   1202       C  
ATOM   6051  O   LYS B1083       8.115  49.109  14.419  1.00 53.99           O  
ANISOU 6051  O   LYS B1083     8741   5425   6346    -31  -1266   1069       O  
ATOM   6052  CB  LYS B1083       9.059  49.579  11.302  1.00 54.40           C  
ANISOU 6052  CB  LYS B1083     8672   5619   6379   -258  -1209   1512       C  
ATOM   6053  CG  LYS B1083       8.907  50.595  10.190  1.00 66.08           C  
ANISOU 6053  CG  LYS B1083    10209   7023   7876   -280  -1258   1708       C  
ATOM   6054  CD  LYS B1083       9.117  49.941   8.823  1.00 74.00           C  
ANISOU 6054  CD  LYS B1083    11079   8277   8762   -313  -1146   1843       C  
ATOM   6055  CE  LYS B1083      10.553  50.071   8.314  1.00 83.80           C  
ANISOU 6055  CE  LYS B1083    12238   9572  10030   -512  -1121   2028       C  
ATOM   6056  NZ  LYS B1083      11.602  49.863   9.362  1.00 90.19           N  
ANISOU 6056  NZ  LYS B1083    13016  10322  10929   -637  -1143   1959       N  
ATOM   6057  N   LEU B1084      10.126  48.186  13.934  1.00 49.45           N  
ANISOU 6057  N   LEU B1084     7991   5011   5785   -303  -1193   1195       N  
ATOM   6058  CA  LEU B1084       9.977  47.028  14.832  1.00 47.32           C  
ANISOU 6058  CA  LEU B1084     7660   4861   5458   -238  -1125   1039       C  
ATOM   6059  C   LEU B1084      10.344  47.294  16.299  1.00 50.29           C  
ANISOU 6059  C   LEU B1084     8119   5107   5881   -232  -1206    914       C  
ATOM   6060  O   LEU B1084       9.703  46.745  17.187  1.00 49.03           O  
ANISOU 6060  O   LEU B1084     7968   4993   5667   -111  -1174    778       O  
ATOM   6061  CB  LEU B1084      10.796  45.831  14.316  1.00 46.32           C  
ANISOU 6061  CB  LEU B1084     7375   4941   5283   -328  -1022   1080       C  
ATOM   6062  CG  LEU B1084      10.373  45.216  12.974  1.00 50.38           C  
ANISOU 6062  CG  LEU B1084     7795   5634   5713   -296   -931   1152       C  
ATOM   6063  CD1 LEU B1084      11.435  44.256  12.414  1.00 49.70           C  
ANISOU 6063  CD1 LEU B1084     7569   5729   5584   -386   -854   1200       C  
ATOM   6064  CD2 LEU B1084       9.022  44.521  13.120  1.00 51.38           C  
ANISOU 6064  CD2 LEU B1084     7912   5832   5780   -141   -886   1038       C  
ATOM   6065  N   LYS B1085      11.365  48.119  16.547  1.00 47.34           N  
ANISOU 6065  N   LYS B1085     7801   4580   5606   -364  -1316    964       N  
ATOM   6066  CA  LYS B1085      11.870  48.365  17.910  1.00 47.32           C  
ANISOU 6066  CA  LYS B1085     7876   4458   5646   -370  -1415    837       C  
ATOM   6067  C   LYS B1085      10.831  48.876  18.917  1.00 51.60           C  
ANISOU 6067  C   LYS B1085     8565   4882   6158   -177  -1481    676       C  
ATOM   6068  O   LYS B1085      10.794  48.380  20.038  1.00 51.14           O  
ANISOU 6068  O   LYS B1085     8518   4868   6044   -100  -1474    539       O  
ATOM   6069  CB  LYS B1085      13.081  49.317  17.904  1.00 51.24           C  
ANISOU 6069  CB  LYS B1085     8410   4782   6277   -556  -1553    928       C  
ATOM   6070  CG  LYS B1085      13.431  49.882  19.297  1.00 61.02           C  
ANISOU 6070  CG  LYS B1085     9774   5840   7571   -539  -1709    777       C  
ATOM   6071  CD  LYS B1085      14.806  50.529  19.326  1.00 70.74           C  
ANISOU 6071  CD  LYS B1085    10993   6939   8945   -759  -1842    867       C  
ATOM   6072  CE  LYS B1085      15.087  51.181  20.680  1.00 81.32           C  
ANISOU 6072  CE  LYS B1085    12477   8078  10342   -730  -2029    698       C  
ATOM   6073  NZ  LYS B1085      15.109  50.194  21.816  1.00 87.22           N  
ANISOU 6073  NZ  LYS B1085    13196   8972  10973   -623  -1978    526       N  
ATOM   6074  N   PRO B1086      10.019  49.887  18.540  1.00 48.48           N  
ANISOU 6074  N   PRO B1086     8283   4343   5792    -90  -1547    696       N  
ATOM   6075  CA  PRO B1086       8.964  50.397  19.415  1.00 48.58           C  
ANISOU 6075  CA  PRO B1086     8429   4265   5764    125  -1601    541       C  
ATOM   6076  C   PRO B1086       7.940  49.357  19.877  1.00 49.95           C  
ANISOU 6076  C   PRO B1086     8524   4653   5804    295  -1460    442       C  
ATOM   6077  O   PRO B1086       7.464  49.426  21.009  1.00 50.16           O  
ANISOU 6077  O   PRO B1086     8619   4670   5769    449  -1482    295       O  
ATOM   6078  CB  PRO B1086       8.271  51.457  18.543  1.00 51.51           C  
ANISOU 6078  CB  PRO B1086     8892   4493   6188    180  -1666    625       C  
ATOM   6079  CG  PRO B1086       9.282  51.902  17.615  1.00 56.70           C  
ANISOU 6079  CG  PRO B1086     9526   5066   6952    -39  -1715    809       C  
ATOM   6080  CD  PRO B1086      10.117  50.701  17.313  1.00 50.88           C  
ANISOU 6080  CD  PRO B1086     8607   4552   6173   -181  -1587    872       C  
ATOM   6081  N   VAL B1087       7.591  48.425  19.000  1.00 44.25           N  
ANISOU 6081  N   VAL B1087     7657   4122   5036    270  -1323    527       N  
ATOM   6082  CA  VAL B1087       6.672  47.344  19.348  1.00 42.50           C  
ANISOU 6082  CA  VAL B1087     7336   4099   4713    392  -1194    461       C  
ATOM   6083  C   VAL B1087       7.343  46.375  20.331  1.00 44.46           C  
ANISOU 6083  C   VAL B1087     7527   4444   4922    348  -1149    395       C  
ATOM   6084  O   VAL B1087       6.759  45.997  21.345  1.00 43.91           O  
ANISOU 6084  O   VAL B1087     7460   4445   4777    478  -1110    296       O  
ATOM   6085  CB  VAL B1087       6.240  46.537  18.113  1.00 45.41           C  
ANISOU 6085  CB  VAL B1087     7565   4631   5058    355  -1086    562       C  
ATOM   6086  CG1 VAL B1087       4.963  45.807  18.409  1.00 44.59           C  
ANISOU 6086  CG1 VAL B1087     7385   4677   4881    504   -993    502       C  
ATOM   6087  CG2 VAL B1087       6.076  47.443  16.909  1.00 46.29           C  
ANISOU 6087  CG2 VAL B1087     7721   4653   5214    332  -1138    676       C  
ATOM   6088  N   TYR B1088       8.573  45.983  20.013  1.00 39.76           N  
ANISOU 6088  N   TYR B1088     6872   3862   4371    172  -1153    460       N  
ATOM   6089  CA  TYR B1088       9.337  45.065  20.849  1.00 38.54           C  
ANISOU 6089  CA  TYR B1088     6661   3794   4188    122  -1122    410       C  
ATOM   6090  C   TYR B1088       9.504  45.634  22.256  1.00 43.87           C  
ANISOU 6090  C   TYR B1088     7459   4366   4843    201  -1219    283       C  
ATOM   6091  O   TYR B1088       9.521  44.885  23.234  1.00 43.16           O  
ANISOU 6091  O   TYR B1088     7344   4373   4680    258  -1177    212       O  
ATOM   6092  CB  TYR B1088      10.707  44.806  20.228  1.00 39.05           C  
ANISOU 6092  CB  TYR B1088     6648   3873   4315    -71  -1134    504       C  
ATOM   6093  CG  TYR B1088      11.563  43.825  20.984  1.00 39.72           C  
ANISOU 6093  CG  TYR B1088     6665   4052   4376   -121  -1108    462       C  
ATOM   6094  CD1 TYR B1088      11.583  42.487  20.644  1.00 40.24           C  
ANISOU 6094  CD1 TYR B1088     6601   4287   4401   -133   -995    488       C  
ATOM   6095  CD2 TYR B1088      12.377  44.240  22.019  1.00 41.37           C  
ANISOU 6095  CD2 TYR B1088     6942   4170   4607   -152  -1213    394       C  
ATOM   6096  CE1 TYR B1088      12.370  41.587  21.330  1.00 39.84           C  
ANISOU 6096  CE1 TYR B1088     6494   4311   4333   -167   -979    455       C  
ATOM   6097  CE2 TYR B1088      13.178  43.344  22.704  1.00 41.74           C  
ANISOU 6097  CE2 TYR B1088     6924   4308   4628   -189  -1196    361       C  
ATOM   6098  CZ  TYR B1088      13.167  42.023  22.359  1.00 47.15           C  
ANISOU 6098  CZ  TYR B1088     7483   5159   5273   -194  -1076    397       C  
ATOM   6099  OH  TYR B1088      13.959  41.134  23.047  1.00 48.50           O  
ANISOU 6099  OH  TYR B1088     7597   5410   5421   -219  -1068    369       O  
ATOM   6100  N   ASP B1089       9.613  46.959  22.356  1.00 41.65           N  
ANISOU 6100  N   ASP B1089     7318   3883   4622    212  -1358    254       N  
ATOM   6101  CA  ASP B1089       9.775  47.612  23.650  1.00 42.22           C  
ANISOU 6101  CA  ASP B1089     7529   3838   4673    303  -1481    110       C  
ATOM   6102  C   ASP B1089       8.516  47.536  24.504  1.00 45.56           C  
ANISOU 6102  C   ASP B1089     8000   4339   4970    547  -1428     -8       C  
ATOM   6103  O   ASP B1089       8.613  47.445  25.732  1.00 45.40           O  
ANISOU 6103  O   ASP B1089     8037   4344   4868    646  -1459   -128       O  
ATOM   6104  CB  ASP B1089      10.238  49.053  23.458  1.00 45.49           C  
ANISOU 6104  CB  ASP B1089     8088   3989   5208    242  -1666    111       C  
ATOM   6105  CG  ASP B1089      11.668  49.128  22.949  1.00 54.36           C  
ANISOU 6105  CG  ASP B1089     9152   5050   6452     -9  -1731    223       C  
ATOM   6106  OD1 ASP B1089      12.319  48.067  22.813  1.00 53.33           O  
ANISOU 6106  OD1 ASP B1089     8876   5088   6298   -110  -1633    277       O  
ATOM   6107  OD2 ASP B1089      12.147  50.242  22.675  1.00 62.45           O  
ANISOU 6107  OD2 ASP B1089    10269   5859   7601   -105  -1882    263       O  
ATOM   6108  N   SER B1090       7.353  47.535  23.854  1.00 41.49           N  
ANISOU 6108  N   SER B1090     7447   3885   4431    648  -1344     34       N  
ATOM   6109  CA  SER B1090       6.067  47.453  24.552  1.00 41.93           C  
ANISOU 6109  CA  SER B1090     7514   4048   4369    883  -1275    -53       C  
ATOM   6110  C   SER B1090       5.573  46.017  24.865  1.00 44.73           C  
ANISOU 6110  C   SER B1090     7707   4656   4632    910  -1102    -20       C  
ATOM   6111  O   SER B1090       4.521  45.837  25.495  1.00 44.88           O  
ANISOU 6111  O   SER B1090     7703   4799   4550   1092  -1027    -68       O  
ATOM   6112  CB  SER B1090       4.987  48.179  23.730  1.00 45.69           C  
ANISOU 6112  CB  SER B1090     8016   4474   4870    989  -1279    -22       C  
ATOM   6113  OG  SER B1090       4.545  47.392  22.629  1.00 49.46           O  
ANISOU 6113  OG  SER B1090     8339   5088   5366    914  -1159    105       O  
ATOM   6114  N   LEU B1091       6.287  44.995  24.408  1.00 39.06           N  
ANISOU 6114  N   LEU B1091     6871   4017   3951    736  -1040     68       N  
ATOM   6115  CA  LEU B1091       5.778  43.635  24.577  1.00 37.19           C  
ANISOU 6115  CA  LEU B1091     6487   3986   3657    748   -894    114       C  
ATOM   6116  C   LEU B1091       6.411  42.942  25.787  1.00 41.14           C  
ANISOU 6116  C   LEU B1091     6986   4559   4088    749   -879     70       C  
ATOM   6117  O   LEU B1091       7.583  43.183  26.123  1.00 41.14           O  
ANISOU 6117  O   LEU B1091     7050   4467   4114    662   -973     34       O  
ATOM   6118  CB  LEU B1091       5.994  42.787  23.307  1.00 35.41           C  
ANISOU 6118  CB  LEU B1091     6131   3819   3505    591   -831    229       C  
ATOM   6119  CG  LEU B1091       5.254  43.159  22.016  1.00 39.53           C  
ANISOU 6119  CG  LEU B1091     6620   4326   4074    594   -821    292       C  
ATOM   6120  CD1 LEU B1091       5.590  42.143  20.920  1.00 37.87           C  
ANISOU 6120  CD1 LEU B1091     6283   4200   3908    453   -763    381       C  
ATOM   6121  CD2 LEU B1091       3.730  43.299  22.227  1.00 42.18           C  
ANISOU 6121  CD2 LEU B1091     6929   4744   4355    773   -766    268       C  
ATOM   6122  N   ASP B1092       5.609  42.090  26.426  1.00 36.91           N  
ANISOU 6122  N   ASP B1092     6367   4192   3464    846   -765     84       N  
ATOM   6123  CA  ASP B1092       6.088  41.130  27.412  1.00 36.31           C  
ANISOU 6123  CA  ASP B1092     6255   4220   3322    835   -721     89       C  
ATOM   6124  C   ASP B1092       6.923  40.091  26.703  1.00 38.12           C  
ANISOU 6124  C   ASP B1092     6385   4461   3638    646   -697    174       C  
ATOM   6125  O   ASP B1092       6.791  39.917  25.490  1.00 36.99           O  
ANISOU 6125  O   ASP B1092     6174   4300   3581    556   -677    236       O  
ATOM   6126  CB  ASP B1092       4.907  40.433  28.113  1.00 38.70           C  
ANISOU 6126  CB  ASP B1092     6470   4711   3524    970   -590    127       C  
ATOM   6127  CG  ASP B1092       3.965  39.726  27.129  1.00 49.57           C  
ANISOU 6127  CG  ASP B1092     7695   6168   4970    920   -492    233       C  
ATOM   6128  OD1 ASP B1092       3.726  38.506  27.285  1.00 50.35           O  
ANISOU 6128  OD1 ASP B1092     7674   6384   5073    871   -402    322       O  
ATOM   6129  OD2 ASP B1092       3.474  40.384  26.185  1.00 54.81           O  
ANISOU 6129  OD2 ASP B1092     8363   6770   5691    928   -518    231       O  
ATOM   6130  N   ALA B1093       7.752  39.386  27.471  1.00 33.97           N  
ANISOU 6130  N   ALA B1093     5852   3976   3080    606   -701    173       N  
ATOM   6131  CA  ALA B1093       8.641  38.335  26.959  1.00 32.60           C  
ANISOU 6131  CA  ALA B1093     5590   3819   2977    454   -686    239       C  
ATOM   6132  C   ALA B1093       7.938  37.316  26.048  1.00 35.99           C  
ANISOU 6132  C   ALA B1093     5888   4322   3463    405   -589    330       C  
ATOM   6133  O   ALA B1093       8.413  37.045  24.947  1.00 35.39           O  
ANISOU 6133  O   ALA B1093     5762   4214   3469    295   -602    362       O  
ATOM   6134  CB  ALA B1093       9.327  37.617  28.123  1.00 33.57           C  
ANISOU 6134  CB  ALA B1093     5720   4003   3033    467   -689    231       C  
ATOM   6135  N   VAL B1094       6.809  36.766  26.491  1.00 32.52           N  
ANISOU 6135  N   VAL B1094     5388   3988   2978    489   -500    372       N  
ATOM   6136  CA  VAL B1094       6.092  35.764  25.701  1.00 31.36           C  
ANISOU 6136  CA  VAL B1094     5115   3900   2901    435   -430    454       C  
ATOM   6137  C   VAL B1094       5.768  36.291  24.306  1.00 35.29           C  
ANISOU 6137  C   VAL B1094     5595   4344   3470    395   -455    450       C  
ATOM   6138  O   VAL B1094       5.962  35.593  23.308  1.00 34.45           O  
ANISOU 6138  O   VAL B1094     5419   4234   3437    301   -455    483       O  
ATOM   6139  CB  VAL B1094       4.770  35.305  26.376  1.00 35.79           C  
ANISOU 6139  CB  VAL B1094     5599   4586   3414    529   -334    516       C  
ATOM   6140  CG1 VAL B1094       4.003  34.290  25.480  1.00 34.94           C  
ANISOU 6140  CG1 VAL B1094     5353   4517   3407    451   -289    599       C  
ATOM   6141  CG2 VAL B1094       5.038  34.691  27.755  1.00 36.19           C  
ANISOU 6141  CG2 VAL B1094     5659   4713   3378    573   -297    548       C  
ATOM   6142  N   ARG B1095       5.265  37.519  24.228  1.00 32.37           N  
ANISOU 6142  N   ARG B1095     5294   3934   3071    480   -482    407       N  
ATOM   6143  CA  ARG B1095       4.874  38.092  22.934  1.00 31.83           C  
ANISOU 6143  CA  ARG B1095     5217   3820   3058    459   -508    417       C  
ATOM   6144  C   ARG B1095       6.088  38.521  22.095  1.00 36.32           C  
ANISOU 6144  C   ARG B1095     5835   4288   3675    345   -582    413       C  
ATOM   6145  O   ARG B1095       5.985  38.630  20.874  1.00 34.93           O  
ANISOU 6145  O   ARG B1095     5627   4102   3543    297   -592    447       O  
ATOM   6146  CB  ARG B1095       3.907  39.260  23.116  1.00 30.68           C  
ANISOU 6146  CB  ARG B1095     5130   3657   2869    600   -519    380       C  
ATOM   6147  CG  ARG B1095       2.518  38.834  23.576  1.00 36.40           C  
ANISOU 6147  CG  ARG B1095     5758   4518   3555    711   -431    410       C  
ATOM   6148  CD  ARG B1095       1.581  40.008  23.606  1.00 41.36           C  
ANISOU 6148  CD  ARG B1095     6437   5137   4142    869   -446    368       C  
ATOM   6149  NE  ARG B1095       0.208  39.641  23.956  1.00 46.06           N  
ANISOU 6149  NE  ARG B1095     6911   5889   4701    980   -355    407       N  
ATOM   6150  CZ  ARG B1095      -0.310  39.654  25.188  1.00 58.01           C  
ANISOU 6150  CZ  ARG B1095     8413   7515   6114   1118   -291    395       C  
ATOM   6151  NH1 ARG B1095       0.412  39.989  26.259  1.00 39.18           N  
ANISOU 6151  NH1 ARG B1095     6146   5099   3642   1175   -316    328       N  
ATOM   6152  NH2 ARG B1095      -1.577  39.306  25.353  1.00 49.13           N  
ANISOU 6152  NH2 ARG B1095     7147   6551   4969   1203   -201    456       N  
ATOM   6153  N   ARG B1096       7.221  38.755  22.756  1.00 33.93           N  
ANISOU 6153  N   ARG B1096     5600   3929   3361    305   -633    379       N  
ATOM   6154  CA  ARG B1096       8.459  39.096  22.076  1.00 33.92           C  
ANISOU 6154  CA  ARG B1096     5620   3856   3412    185   -697    394       C  
ATOM   6155  C   ARG B1096       8.996  37.839  21.429  1.00 38.73           C  
ANISOU 6155  C   ARG B1096     6120   4544   4052     95   -654    437       C  
ATOM   6156  O   ARG B1096       9.567  37.891  20.341  1.00 39.57           O  
ANISOU 6156  O   ARG B1096     6193   4648   4193     16   -667    474       O  
ATOM   6157  CB  ARG B1096       9.503  39.658  23.055  1.00 33.80           C  
ANISOU 6157  CB  ARG B1096     5693   3766   3385    164   -777    343       C  
ATOM   6158  CG  ARG B1096       9.219  41.052  23.612  1.00 37.53           C  
ANISOU 6158  CG  ARG B1096     6299   4120   3839    247   -861    278       C  
ATOM   6159  CD  ARG B1096      10.305  41.468  24.608  1.00 38.80           C  
ANISOU 6159  CD  ARG B1096     6543   4208   3993    219   -961    213       C  
ATOM   6160  NE  ARG B1096      10.303  42.908  24.859  1.00 43.16           N  
ANISOU 6160  NE  ARG B1096     7234   4599   4564    260  -1083    150       N  
ATOM   6161  CZ  ARG B1096      11.148  43.553  25.659  1.00 54.97           C  
ANISOU 6161  CZ  ARG B1096     8826   5992   6071    241  -1210     75       C  
ATOM   6162  NH1 ARG B1096      12.082  42.899  26.324  1.00 49.27           N  
ANISOU 6162  NH1 ARG B1096     8066   5325   5328    186  -1227     57       N  
ATOM   6163  NH2 ARG B1096      11.047  44.865  25.806  1.00 38.79           N  
ANISOU 6163  NH2 ARG B1096     6912   3771   4054    282  -1336     12       N  
ATOM   6164  N   ALA B1097       8.828  36.705  22.097  1.00 34.78           N  
ANISOU 6164  N   ALA B1097     5567   4113   3534    116   -605    435       N  
ATOM   6165  CA  ALA B1097       9.121  35.417  21.469  1.00 34.20           C  
ANISOU 6165  CA  ALA B1097     5397   4099   3499     56   -574    464       C  
ATOM   6166  C   ALA B1097       8.307  35.261  20.179  1.00 38.33           C  
ANISOU 6166  C   ALA B1097     5863   4651   4051     54   -554    486       C  
ATOM   6167  O   ALA B1097       8.821  34.777  19.161  1.00 38.31           O  
ANISOU 6167  O   ALA B1097     5812   4674   4071      1   -562    494       O  
ATOM   6168  CB  ALA B1097       8.822  34.271  22.419  1.00 34.89           C  
ANISOU 6168  CB  ALA B1097     5447   4235   3576     85   -533    476       C  
ATOM   6169  N   ALA B1098       7.045  35.683  20.227  1.00 34.43           N  
ANISOU 6169  N   ALA B1098     5372   4165   3546    125   -532    492       N  
ATOM   6170  CA  ALA B1098       6.172  35.627  19.059  1.00 33.94           C  
ANISOU 6170  CA  ALA B1098     5255   4134   3508    135   -527    509       C  
ATOM   6171  C   ALA B1098       6.780  36.368  17.861  1.00 37.32           C  
ANISOU 6171  C   ALA B1098     5712   4537   3932     93   -566    522       C  
ATOM   6172  O   ALA B1098       6.809  35.830  16.752  1.00 36.33           O  
ANISOU 6172  O   ALA B1098     5530   4460   3815     66   -569    530       O  
ATOM   6173  CB  ALA B1098       4.788  36.179  19.393  1.00 35.14           C  
ANISOU 6173  CB  ALA B1098     5404   4305   3643    231   -504    515       C  
ATOM   6174  N   LEU B1099       7.276  37.581  18.102  1.00 34.45           N  
ANISOU 6174  N   LEU B1099     5438   4097   3554     91   -602    528       N  
ATOM   6175  CA  LEU B1099       7.798  38.444  17.041  1.00 34.83           C  
ANISOU 6175  CA  LEU B1099     5515   4113   3604     45   -638    574       C  
ATOM   6176  C   LEU B1099       9.140  37.942  16.520  1.00 38.73           C  
ANISOU 6176  C   LEU B1099     5962   4650   4102    -51   -638    598       C  
ATOM   6177  O   LEU B1099       9.380  37.987  15.318  1.00 38.26           O  
ANISOU 6177  O   LEU B1099     5868   4644   4026    -78   -634    644       O  
ATOM   6178  CB  LEU B1099       7.926  39.894  17.529  1.00 35.72           C  
ANISOU 6178  CB  LEU B1099     5743   4104   3725     60   -696    579       C  
ATOM   6179  CG  LEU B1099       8.098  40.982  16.454  1.00 41.07           C  
ANISOU 6179  CG  LEU B1099     6464   4725   4417     26   -740    654       C  
ATOM   6180  CD1 LEU B1099       6.768  41.267  15.767  1.00 41.64           C  
ANISOU 6180  CD1 LEU B1099     6534   4818   4470    121   -732    668       C  
ATOM   6181  CD2 LEU B1099       8.670  42.265  17.035  1.00 43.60           C  
ANISOU 6181  CD2 LEU B1099     6899   4891   4775     -3   -823    661       C  
ATOM   6182  N   ILE B1100      10.004  37.468  17.423  1.00 35.79           N  
ANISOU 6182  N   ILE B1100     5586   4273   3740    -87   -640    570       N  
ATOM   6183  CA  ILE B1100      11.267  36.784  17.052  1.00 35.40           C  
ANISOU 6183  CA  ILE B1100     5470   4289   3693   -156   -634    582       C  
ATOM   6184  C   ILE B1100      11.014  35.574  16.136  1.00 38.68           C  
ANISOU 6184  C   ILE B1100     5800   4803   4092   -131   -598    564       C  
ATOM   6185  O   ILE B1100      11.703  35.387  15.132  1.00 38.37           O  
ANISOU 6185  O   ILE B1100     5710   4841   4028   -155   -590    588       O  
ATOM   6186  CB  ILE B1100      12.061  36.344  18.316  1.00 38.39           C  
ANISOU 6186  CB  ILE B1100     5855   4647   4083   -175   -649    544       C  
ATOM   6187  CG1 ILE B1100      12.674  37.574  18.999  1.00 39.38           C  
ANISOU 6187  CG1 ILE B1100     6059   4679   4227   -218   -713    553       C  
ATOM   6188  CG2 ILE B1100      13.184  35.348  17.963  1.00 39.15           C  
ANISOU 6188  CG2 ILE B1100     5865   4830   4181   -213   -637    543       C  
ATOM   6189  CD1 ILE B1100      13.088  37.346  20.449  1.00 46.35           C  
ANISOU 6189  CD1 ILE B1100     6978   5531   5102   -202   -744    498       C  
ATOM   6190  N   ASN B1101      10.035  34.753  16.505  1.00 34.79           N  
ANISOU 6190  N   ASN B1101     5292   4312   3614    -78   -583    523       N  
ATOM   6191  CA  ASN B1101       9.564  33.662  15.657  1.00 34.49           C  
ANISOU 6191  CA  ASN B1101     5188   4335   3580    -52   -578    492       C  
ATOM   6192  C   ASN B1101       9.324  34.154  14.211  1.00 39.47           C  
ANISOU 6192  C   ASN B1101     5807   5023   4169    -38   -585    515       C  
ATOM   6193  O   ASN B1101       9.848  33.573  13.250  1.00 39.61           O  
ANISOU 6193  O   ASN B1101     5777   5121   4151    -31   -587    497       O  
ATOM   6194  CB  ASN B1101       8.286  33.063  16.274  1.00 33.61           C  
ANISOU 6194  CB  ASN B1101     5062   4198   3510    -15   -571    474       C  
ATOM   6195  CG  ASN B1101       7.821  31.793  15.583  1.00 44.64           C  
ANISOU 6195  CG  ASN B1101     6392   5627   4942     -5   -592    435       C  
ATOM   6196  OD1 ASN B1101       7.600  31.772  14.378  1.00 43.20           O  
ANISOU 6196  OD1 ASN B1101     6186   5491   4736     13   -616    415       O  
ATOM   6197  ND2 ASN B1101       7.647  30.734  16.355  1.00 30.48           N  
ANISOU 6197  ND2 ASN B1101     4572   3803   3205    -14   -594    426       N  
ATOM   6198  N   MET B1102       8.565  35.239  14.066  1.00 36.16           N  
ANISOU 6198  N   MET B1102     5431   4568   3740    -19   -590    554       N  
ATOM   6199  CA  MET B1102       8.244  35.784  12.743  1.00 36.51           C  
ANISOU 6199  CA  MET B1102     5472   4664   3736      4   -601    592       C  
ATOM   6200  C   MET B1102       9.479  36.279  12.004  1.00 42.01           C  
ANISOU 6200  C   MET B1102     6164   5413   4383    -45   -592    657       C  
ATOM   6201  O   MET B1102       9.569  36.143  10.785  1.00 42.48           O  
ANISOU 6201  O   MET B1102     6188   5574   4378    -21   -588    676       O  
ATOM   6202  CB  MET B1102       7.221  36.927  12.842  1.00 39.00           C  
ANISOU 6202  CB  MET B1102     5845   4916   4057     44   -617    629       C  
ATOM   6203  CG  MET B1102       5.840  36.471  13.257  1.00 42.16           C  
ANISOU 6203  CG  MET B1102     6216   5313   4491    106   -618    583       C  
ATOM   6204  SD  MET B1102       4.624  37.788  13.284  1.00 46.84           S  
ANISOU 6204  SD  MET B1102     6861   5855   5079    187   -637    617       S  
ATOM   6205  CE  MET B1102       4.538  38.267  11.558  1.00 43.98           C  
ANISOU 6205  CE  MET B1102     6498   5555   4657    204   -670    672       C  
ATOM   6206  N   VAL B1103      10.413  36.878  12.734  1.00 38.89           N  
ANISOU 6206  N   VAL B1103     5799   4960   4016   -112   -592    696       N  
ATOM   6207  CA  VAL B1103      11.695  37.252  12.155  1.00 38.98           C  
ANISOU 6207  CA  VAL B1103     5777   5035   4000   -179   -579    774       C  
ATOM   6208  C   VAL B1103      12.447  35.993  11.713  1.00 42.09           C  
ANISOU 6208  C   VAL B1103     6080   5561   4353   -159   -549    724       C  
ATOM   6209  O   VAL B1103      13.017  35.972  10.619  1.00 42.23           O  
ANISOU 6209  O   VAL B1103     6042   5706   4297   -152   -523    773       O  
ATOM   6210  CB  VAL B1103      12.546  38.124  13.132  1.00 42.92           C  
ANISOU 6210  CB  VAL B1103     6317   5430   4559   -267   -609    818       C  
ATOM   6211  CG1 VAL B1103      13.994  38.184  12.693  1.00 43.39           C  
ANISOU 6211  CG1 VAL B1103     6301   5580   4607   -349   -591    895       C  
ATOM   6212  CG2 VAL B1103      11.969  39.534  13.216  1.00 43.19           C  
ANISOU 6212  CG2 VAL B1103     6449   5335   4625   -280   -654    879       C  
ATOM   6213  N   PHE B1104      12.425  34.945  12.543  1.00 38.00           N  
ANISOU 6213  N   PHE B1104     5549   5016   3872   -136   -555    632       N  
ATOM   6214  CA  PHE B1104      13.087  33.666  12.212  1.00 37.66           C  
ANISOU 6214  CA  PHE B1104     5435   5071   3804    -97   -544    567       C  
ATOM   6215  C   PHE B1104      12.545  33.075  10.910  1.00 41.93           C  
ANISOU 6215  C   PHE B1104     5946   5710   4276    -16   -547    523       C  
ATOM   6216  O   PHE B1104      13.294  32.438  10.158  1.00 41.80           O  
ANISOU 6216  O   PHE B1104     5870   5816   4194     31   -534    493       O  
ATOM   6217  CB  PHE B1104      12.934  32.632  13.344  1.00 38.69           C  
ANISOU 6217  CB  PHE B1104     5574   5127   4001    -81   -564    487       C  
ATOM   6218  CG  PHE B1104      14.138  32.513  14.233  1.00 40.28           C  
ANISOU 6218  CG  PHE B1104     5757   5322   4226   -123   -563    495       C  
ATOM   6219  CD1 PHE B1104      14.577  33.599  14.994  1.00 43.54           C  
ANISOU 6219  CD1 PHE B1104     6206   5675   4664   -196   -572    555       C  
ATOM   6220  CD2 PHE B1104      14.837  31.312  14.321  1.00 42.30           C  
ANISOU 6220  CD2 PHE B1104     5963   5625   4485    -82   -570    435       C  
ATOM   6221  CE1 PHE B1104      15.711  33.494  15.814  1.00 44.42           C  
ANISOU 6221  CE1 PHE B1104     6291   5787   4797   -236   -588    557       C  
ATOM   6222  CE2 PHE B1104      15.961  31.200  15.144  1.00 45.20           C  
ANISOU 6222  CE2 PHE B1104     6305   5997   4873   -111   -576    444       C  
ATOM   6223  CZ  PHE B1104      16.398  32.301  15.889  1.00 43.31           C  
ANISOU 6223  CZ  PHE B1104     6091   5712   4654   -193   -586    506       C  
ATOM   6224  N   GLN B1105      11.249  33.288  10.657  1.00 38.15           N  
ANISOU 6224  N   GLN B1105     5504   5185   3805     13   -571    511       N  
ATOM   6225  CA  GLN B1105      10.589  32.749   9.473  1.00 38.29           C  
ANISOU 6225  CA  GLN B1105     5501   5285   3764     92   -598    455       C  
ATOM   6226  C   GLN B1105      10.712  33.660   8.257  1.00 44.92           C  
ANISOU 6226  C   GLN B1105     6338   6235   4496    111   -577    540       C  
ATOM   6227  O   GLN B1105      11.085  33.208   7.185  1.00 45.26           O  
ANISOU 6227  O   GLN B1105     6341   6419   4438    178   -574    512       O  
ATOM   6228  CB  GLN B1105       9.114  32.482   9.761  1.00 38.81           C  
ANISOU 6228  CB  GLN B1105     5587   5264   3896    111   -643    408       C  
ATOM   6229  CG  GLN B1105       8.444  31.616   8.712  1.00 40.53           C  
ANISOU 6229  CG  GLN B1105     5775   5543   4080    186   -702    317       C  
ATOM   6230  CD  GLN B1105       6.949  31.525   8.887  1.00 48.95           C  
ANISOU 6230  CD  GLN B1105     6839   6542   5217    191   -750    294       C  
ATOM   6231  OE1 GLN B1105       6.401  31.969   9.884  1.00 41.01           O  
ANISOU 6231  OE1 GLN B1105     5848   5451   4284    151   -728    340       O  
ATOM   6232  NE2 GLN B1105       6.281  30.935   7.917  1.00 43.60           N  
ANISOU 6232  NE2 GLN B1105     6136   5915   4515    249   -821    218       N  
ATOM   6233  N   MET B1106      10.407  34.941   8.432  1.00 42.90           N  
ANISOU 6233  N   MET B1106     6129   5915   4255     62   -568    646       N  
ATOM   6234  CA  MET B1106      10.181  35.861   7.303  1.00 44.04           C  
ANISOU 6234  CA  MET B1106     6287   6134   4311     84   -562    744       C  
ATOM   6235  C   MET B1106      11.278  36.879   7.047  1.00 49.12           C  
ANISOU 6235  C   MET B1106     6922   6819   4921     10   -518    896       C  
ATOM   6236  O   MET B1106      11.145  37.720   6.160  1.00 49.46           O  
ANISOU 6236  O   MET B1106     6980   6916   4896     16   -511   1009       O  
ATOM   6237  CB  MET B1106       8.879  36.621   7.539  1.00 46.27           C  
ANISOU 6237  CB  MET B1106     6633   6305   4642     98   -600    764       C  
ATOM   6238  CG  MET B1106       7.663  35.761   7.351  1.00 49.74           C  
ANISOU 6238  CG  MET B1106     7054   6751   5094    174   -648    650       C  
ATOM   6239  SD  MET B1106       6.235  36.629   7.963  1.00 53.92           S  
ANISOU 6239  SD  MET B1106     7633   7156   5699    191   -679    674       S  
ATOM   6240  CE  MET B1106       6.000  35.745   9.508  1.00 49.50           C  
ANISOU 6240  CE  MET B1106     7053   6498   5257    158   -671    585       C  
ATOM   6241  N   GLY B1107      12.356  36.813   7.820  1.00 46.01           N  
ANISOU 6241  N   GLY B1107     6500   6402   4580    -66   -494    911       N  
ATOM   6242  CA  GLY B1107      13.401  37.827   7.771  1.00 46.62           C  
ANISOU 6242  CA  GLY B1107     6559   6491   4664   -168   -468   1065       C  
ATOM   6243  C   GLY B1107      12.886  39.092   8.420  1.00 50.52           C  
ANISOU 6243  C   GLY B1107     7152   6793   5252   -235   -515   1136       C  
ATOM   6244  O   GLY B1107      11.675  39.331   8.457  1.00 49.66           O  
ANISOU 6244  O   GLY B1107     7113   6601   5155   -176   -550   1097       O  
ATOM   6245  N   GLU B1108      13.805  39.898   8.942  1.00 47.85           N  
ANISOU 6245  N   GLU B1108     6816   6383   4983   -353   -527   1233       N  
ATOM   6246  CA  GLU B1108      13.455  41.155   9.596  1.00 48.01           C  
ANISOU 6246  CA  GLU B1108     6942   6198   5100   -414   -594   1289       C  
ATOM   6247  C   GLU B1108      12.625  42.089   8.693  1.00 52.42           C  
ANISOU 6247  C   GLU B1108     7566   6725   5625   -381   -613   1393       C  
ATOM   6248  O   GLU B1108      11.700  42.743   9.173  1.00 52.38           O  
ANISOU 6248  O   GLU B1108     7666   6561   5675   -344   -671   1363       O  
ATOM   6249  CB  GLU B1108      14.736  41.856  10.065  1.00 50.37           C  
ANISOU 6249  CB  GLU B1108     7217   6440   5480   -561   -620   1392       C  
ATOM   6250  CG  GLU B1108      14.541  43.189  10.810  1.00 61.16           C  
ANISOU 6250  CG  GLU B1108     8707   7567   6964   -633   -718   1436       C  
ATOM   6251  CD  GLU B1108      15.830  44.002  10.876  1.00 84.03           C  
ANISOU 6251  CD  GLU B1108    11563  10420   9945   -803   -757   1583       C  
ATOM   6252  OE1 GLU B1108      16.868  43.445  11.291  1.00 80.43           O  
ANISOU 6252  OE1 GLU B1108    11009  10046   9506   -864   -739   1562       O  
ATOM   6253  OE2 GLU B1108      15.812  45.196  10.502  1.00 80.61           O  
ANISOU 6253  OE2 GLU B1108    11190   9870   9570   -878   -812   1727       O  
ATOM   6254  N   THR B1109      12.940  42.147   7.399  1.00 49.17           N  
ANISOU 6254  N   THR B1109     7092   6476   5113   -377   -565   1514       N  
ATOM   6255  CA  THR B1109      12.271  43.098   6.487  1.00 49.76           C  
ANISOU 6255  CA  THR B1109     7228   6531   5149   -350   -587   1643       C  
ATOM   6256  C   THR B1109      10.780  42.798   6.301  1.00 51.76           C  
ANISOU 6256  C   THR B1109     7538   6768   5361   -207   -614   1528       C  
ATOM   6257  O   THR B1109       9.929  43.671   6.510  1.00 51.61           O  
ANISOU 6257  O   THR B1109     7617   6596   5395   -178   -675   1550       O  
ATOM   6258  CB  THR B1109      12.984  43.172   5.104  1.00 59.43           C  
ANISOU 6258  CB  THR B1109     8362   7973   6246   -367   -518   1815       C  
ATOM   6259  OG1 THR B1109      14.061  44.118   5.177  1.00 61.44           O  
ANISOU 6259  OG1 THR B1109     8593   8176   6574   -527   -522   2007       O  
ATOM   6260  CG2 THR B1109      12.025  43.608   4.003  1.00 58.18           C  
ANISOU 6260  CG2 THR B1109     8253   7864   5987   -271   -529   1890       C  
ATOM   6261  N   GLY B1110      10.485  41.563   5.904  1.00 46.67           N  
ANISOU 6261  N   GLY B1110     6825   6278   4629   -115   -578   1405       N  
ATOM   6262  CA  GLY B1110       9.125  41.079   5.788  1.00 45.22           C  
ANISOU 6262  CA  GLY B1110     6665   6093   4424      5   -611   1282       C  
ATOM   6263  C   GLY B1110       8.311  41.425   7.013  1.00 47.14           C  
ANISOU 6263  C   GLY B1110     6982   6143   4787     14   -659   1204       C  
ATOM   6264  O   GLY B1110       7.252  42.037   6.886  1.00 47.16           O  
ANISOU 6264  O   GLY B1110     7042   6078   4799     82   -703   1215       O  
ATOM   6265  N   VAL B1111       8.809  41.066   8.201  1.00 41.98           N  
ANISOU 6265  N   VAL B1111     6325   5412   4215    -42   -652   1130       N  
ATOM   6266  CA  VAL B1111       8.062  41.298   9.450  1.00 40.88           C  
ANISOU 6266  CA  VAL B1111     6249   5118   4164    -14   -687   1046       C  
ATOM   6267  C   VAL B1111       7.759  42.779   9.627  1.00 46.16           C  
ANISOU 6267  C   VAL B1111     7028   5629   4883    -15   -744   1131       C  
ATOM   6268  O   VAL B1111       6.668  43.157  10.075  1.00 45.52           O  
ANISOU 6268  O   VAL B1111     7002   5465   4829     73   -778   1079       O  
ATOM   6269  CB  VAL B1111       8.811  40.806  10.711  1.00 43.27           C  
ANISOU 6269  CB  VAL B1111     6542   5369   4530    -75   -675    973       C  
ATOM   6270  CG1 VAL B1111       8.002  41.144  11.963  1.00 42.48           C  
ANISOU 6270  CG1 VAL B1111     6513   5135   4492    -24   -706    897       C  
ATOM   6271  CG2 VAL B1111       9.088  39.302  10.640  1.00 42.10           C  
ANISOU 6271  CG2 VAL B1111     6298   5348   4349    -63   -631    884       C  
ATOM   6272  N   ALA B1112       8.747  43.598   9.255  1.00 44.19           N  
ANISOU 6272  N   ALA B1112     6802   5341   4646   -115   -757   1267       N  
ATOM   6273  CA  ALA B1112       8.668  45.067   9.297  1.00 45.36           C  
ANISOU 6273  CA  ALA B1112     7064   5313   4859   -140   -831   1374       C  
ATOM   6274  C   ALA B1112       7.612  45.676   8.356  1.00 50.28           C  
ANISOU 6274  C   ALA B1112     7732   5937   5435    -41   -859   1442       C  
ATOM   6275  O   ALA B1112       7.272  46.854   8.492  1.00 51.07           O  
ANISOU 6275  O   ALA B1112     7944   5866   5595    -24   -935   1504       O  
ATOM   6276  CB  ALA B1112      10.049  45.661   8.996  1.00 47.25           C  
ANISOU 6276  CB  ALA B1112     7288   5532   5134   -297   -838   1531       C  
ATOM   6277  N   GLY B1113       7.110  44.887   7.401  1.00 46.44           N  
ANISOU 6277  N   GLY B1113     7168   5636   4843     31   -813   1426       N  
ATOM   6278  CA  GLY B1113       6.014  45.318   6.531  1.00 46.95           C  
ANISOU 6278  CA  GLY B1113     7262   5726   4850    144   -847   1469       C  
ATOM   6279  C   GLY B1113       4.604  45.147   7.091  1.00 49.96           C  
ANISOU 6279  C   GLY B1113     7658   6067   5258    277   -878   1334       C  
ATOM   6280  O   GLY B1113       3.641  45.637   6.494  1.00 50.30           O  
ANISOU 6280  O   GLY B1113     7730   6113   5270    379   -920   1367       O  
ATOM   6281  N   PHE B1114       4.456  44.454   8.220  1.00 44.98           N  
ANISOU 6281  N   PHE B1114     6997   5415   4679    282   -856   1193       N  
ATOM   6282  CA  PHE B1114       3.134  44.249   8.826  1.00 44.31           C  
ANISOU 6282  CA  PHE B1114     6901   5319   4618    403   -870   1080       C  
ATOM   6283  C   PHE B1114       2.727  45.504   9.592  1.00 48.57           C  
ANISOU 6283  C   PHE B1114     7561   5673   5222    467   -929   1087       C  
ATOM   6284  O   PHE B1114       2.445  45.428  10.791  1.00 48.00           O  
ANISOU 6284  O   PHE B1114     7504   5541   5193    508   -924    987       O  
ATOM   6285  CB  PHE B1114       3.145  43.059   9.810  1.00 44.82           C  
ANISOU 6285  CB  PHE B1114     6888   5433   4710    383   -819    952       C  
ATOM   6286  CG  PHE B1114       3.156  41.689   9.162  1.00 45.48           C  
ANISOU 6286  CG  PHE B1114     6853   5680   4746    362   -784    904       C  
ATOM   6287  CD1 PHE B1114       1.978  40.961   9.036  1.00 48.32           C  
ANISOU 6287  CD1 PHE B1114     7131   6121   5106    438   -793    830       C  
ATOM   6288  CD2 PHE B1114       4.349  41.106   8.747  1.00 46.85           C  
ANISOU 6288  CD2 PHE B1114     6994   5921   4885    271   -752    924       C  
ATOM   6289  CE1 PHE B1114       1.982  39.675   8.478  1.00 48.70           C  
ANISOU 6289  CE1 PHE B1114     7084   6291   5130    417   -787    769       C  
ATOM   6290  CE2 PHE B1114       4.371  39.833   8.187  1.00 49.08           C  
ANISOU 6290  CE2 PHE B1114     7185   6338   5125    273   -735    857       C  
ATOM   6291  CZ  PHE B1114       3.184  39.114   8.054  1.00 47.24           C  
ANISOU 6291  CZ  PHE B1114     6888   6160   4903    343   -762    774       C  
ATOM   6292  N   THR B1115       2.681  46.647   8.907  1.00 45.90           N  
ANISOU 6292  N   THR B1115     7312   5244   4884    488   -990   1205       N  
ATOM   6293  CA  THR B1115       2.509  47.954   9.561  1.00 46.62           C  
ANISOU 6293  CA  THR B1115     7545   5119   5049    540  -1071   1218       C  
ATOM   6294  C   THR B1115       1.270  48.080  10.454  1.00 50.37           C  
ANISOU 6294  C   THR B1115     8035   5563   5540    711  -1088   1088       C  
ATOM   6295  O   THR B1115       1.370  48.639  11.541  1.00 50.49           O  
ANISOU 6295  O   THR B1115     8141   5435   5608    746  -1126   1019       O  
ATOM   6296  CB  THR B1115       2.485  49.116   8.533  1.00 56.13           C  
ANISOU 6296  CB  THR B1115     8841   6231   6254    551  -1145   1382       C  
ATOM   6297  OG1 THR B1115       3.639  49.045   7.695  1.00 56.18           O  
ANISOU 6297  OG1 THR B1115     8820   6291   6234    395  -1117   1528       O  
ATOM   6298  CG2 THR B1115       2.495  50.453   9.227  1.00 56.23           C  
ANISOU 6298  CG2 THR B1115     9018   5981   6364    586  -1250   1394       C  
ATOM   6299  N   ASN B1116       0.112  47.581  10.022  1.00 46.65           N  
ANISOU 6299  N   ASN B1116     7469   5234   5020    824  -1065   1052       N  
ATOM   6300  CA  ASN B1116      -1.112  47.782  10.816  1.00 46.90           C  
ANISOU 6300  CA  ASN B1116     7495   5263   5064    998  -1074    951       C  
ATOM   6301  C   ASN B1116      -1.316  46.751  11.933  1.00 49.52           C  
ANISOU 6301  C   ASN B1116     7727   5693   5397   1000   -994    830       C  
ATOM   6302  O   ASN B1116      -1.820  47.096  13.002  1.00 49.21           O  
ANISOU 6302  O   ASN B1116     7719   5609   5368   1115   -994    749       O  
ATOM   6303  CB  ASN B1116      -2.357  47.896   9.925  1.00 48.89           C  
ANISOU 6303  CB  ASN B1116     7686   5613   5278   1132  -1102    978       C  
ATOM   6304  CG  ASN B1116      -2.377  49.189   9.114  1.00 75.72           C  
ANISOU 6304  CG  ASN B1116    11215   8876   8679   1185  -1196   1095       C  
ATOM   6305  OD1 ASN B1116      -1.362  49.858   8.976  1.00 73.13           O  
ANISOU 6305  OD1 ASN B1116    11003   8400   8383   1082  -1235   1184       O  
ATOM   6306  ND2 ASN B1116      -3.530  49.538   8.575  1.00 68.58           N  
ANISOU 6306  ND2 ASN B1116    10286   8022   7749   1341  -1240   1107       N  
ATOM   6307  N   SER B1117      -0.924  45.499  11.700  1.00 44.64           N  
ANISOU 6307  N   SER B1117     6992   5208   4762    884   -929    822       N  
ATOM   6308  CA  SER B1117      -0.952  44.480  12.759  1.00 43.20           C  
ANISOU 6308  CA  SER B1117     6725   5101   4590    860   -857    734       C  
ATOM   6309  C   SER B1117       0.027  44.836  13.901  1.00 47.49           C  
ANISOU 6309  C   SER B1117     7372   5518   5155    812   -858    697       C  
ATOM   6310  O   SER B1117      -0.333  44.779  15.089  1.00 47.45           O  
ANISOU 6310  O   SER B1117     7368   5515   5145    891   -830    621       O  
ATOM   6311  CB  SER B1117      -0.626  43.092  12.190  1.00 44.94           C  
ANISOU 6311  CB  SER B1117     6820   5455   4800    743   -812    735       C  
ATOM   6312  OG  SER B1117      -1.561  42.708  11.190  1.00 51.68           O  
ANISOU 6312  OG  SER B1117     7577   6425   5634    791   -831    748       O  
ATOM   6313  N   LEU B1118       1.254  45.217  13.536  1.00 43.53           N  
ANISOU 6313  N   LEU B1118     6949   4919   4671    689   -892    756       N  
ATOM   6314  CA  LEU B1118       2.250  45.637  14.517  1.00 43.04           C  
ANISOU 6314  CA  LEU B1118     6985   4727   4641    630   -919    725       C  
ATOM   6315  C   LEU B1118       1.742  46.797  15.365  1.00 48.00           C  
ANISOU 6315  C   LEU B1118     7743   5210   5284    771   -987    664       C  
ATOM   6316  O   LEU B1118       2.009  46.853  16.567  1.00 48.35           O  
ANISOU 6316  O   LEU B1118     7838   5206   5327    799   -993    577       O  
ATOM   6317  CB  LEU B1118       3.565  46.022  13.836  1.00 43.19           C  
ANISOU 6317  CB  LEU B1118     7053   4667   4691    472   -957    825       C  
ATOM   6318  CG  LEU B1118       4.414  44.856  13.310  1.00 46.80           C  
ANISOU 6318  CG  LEU B1118     7396   5263   5124    338   -889    857       C  
ATOM   6319  CD1 LEU B1118       5.537  45.368  12.425  1.00 47.79           C  
ANISOU 6319  CD1 LEU B1118     7546   5348   5263    208   -918    985       C  
ATOM   6320  CD2 LEU B1118       4.976  43.995  14.438  1.00 47.23           C  
ANISOU 6320  CD2 LEU B1118     7412   5347   5185    293   -848    770       C  
ATOM   6321  N   ARG B1119       1.000  47.708  14.740  1.00 45.06           N  
ANISOU 6321  N   ARG B1119     7427   4774   4918    875  -1046    704       N  
ATOM   6322  CA  ARG B1119       0.516  48.906  15.413  1.00 46.15           C  
ANISOU 6322  CA  ARG B1119     7706   4753   5074   1032  -1131    642       C  
ATOM   6323  C   ARG B1119      -0.550  48.582  16.449  1.00 50.27           C  
ANISOU 6323  C   ARG B1119     8174   5386   5540   1215  -1075    521       C  
ATOM   6324  O   ARG B1119      -0.617  49.217  17.492  1.00 51.74           O  
ANISOU 6324  O   ARG B1119     8466   5477   5716   1332  -1120    423       O  
ATOM   6325  CB  ARG B1119      -0.047  49.905  14.394  1.00 47.08           C  
ANISOU 6325  CB  ARG B1119     7893   4782   5214   1108  -1210    728       C  
ATOM   6326  CG  ARG B1119      -0.293  51.299  14.971  1.00 58.90           C  
ANISOU 6326  CG  ARG B1119     9574   6053   6752   1253  -1334    673       C  
ATOM   6327  CD  ARG B1119      -1.315  52.093  14.179  1.00 69.68           C  
ANISOU 6327  CD  ARG B1119    10978   7379   8119   1409  -1394    726       C  
ATOM   6328  NE  ARG B1119      -2.677  51.580  14.369  1.00 77.97           N  
ANISOU 6328  NE  ARG B1119    11898   8628   9098   1594  -1318    652       N  
ATOM   6329  CZ  ARG B1119      -3.358  50.829  13.496  1.00 92.42           C  
ANISOU 6329  CZ  ARG B1119    13570  10658  10890   1591  -1251    710       C  
ATOM   6330  NH1 ARG B1119      -4.597  50.437  13.799  1.00 80.20           N  
ANISOU 6330  NH1 ARG B1119    11897   9280   9297   1756  -1195    643       N  
ATOM   6331  NH2 ARG B1119      -2.830  50.468  12.322  1.00 78.82           N  
ANISOU 6331  NH2 ARG B1119    11804   8978   9168   1432  -1243    833       N  
ATOM   6332  N   MET B1120      -1.403  47.619  16.150  1.00 45.16           N  
ANISOU 6332  N   MET B1120     7359   4945   4855   1245   -982    531       N  
ATOM   6333  CA  MET B1120      -2.386  47.152  17.115  1.00 44.87           C  
ANISOU 6333  CA  MET B1120     7229   5051   4766   1391   -906    450       C  
ATOM   6334  C   MET B1120      -1.686  46.417  18.286  1.00 46.81           C  
ANISOU 6334  C   MET B1120     7461   5337   4987   1322   -846    393       C  
ATOM   6335  O   MET B1120      -2.131  46.492  19.429  1.00 46.51           O  
ANISOU 6335  O   MET B1120     7431   5349   4894   1460   -814    312       O  
ATOM   6336  CB  MET B1120      -3.399  46.213  16.438  1.00 46.74           C  
ANISOU 6336  CB  MET B1120     7270   5494   4995   1398   -834    496       C  
ATOM   6337  CG  MET B1120      -4.204  46.807  15.260  1.00 51.24           C  
ANISOU 6337  CG  MET B1120     7829   6064   5576   1480   -893    552       C  
ATOM   6338  SD  MET B1120      -5.010  45.496  14.271  1.00 54.58           S  
ANISOU 6338  SD  MET B1120     8022   6712   6005   1413   -839    605       S  
ATOM   6339  CE  MET B1120      -5.416  46.340  12.735  1.00 51.99           C  
ANISOU 6339  CE  MET B1120     7740   6340   5675   1468   -939    682       C  
ATOM   6340  N   LEU B1121      -0.596  45.704  17.990  1.00 41.91           N  
ANISOU 6340  N   LEU B1121     6818   4709   4397   1122   -831    437       N  
ATOM   6341  CA  LEU B1121       0.166  44.987  19.021  1.00 40.80           C  
ANISOU 6341  CA  LEU B1121     6667   4598   4235   1049   -786    393       C  
ATOM   6342  C   LEU B1121       0.833  45.947  19.994  1.00 45.86           C  
ANISOU 6342  C   LEU B1121     7479   5081   4866   1099   -867    312       C  
ATOM   6343  O   LEU B1121       0.808  45.715  21.193  1.00 46.45           O  
ANISOU 6343  O   LEU B1121     7563   5206   4881   1174   -835    237       O  
ATOM   6344  CB  LEU B1121       1.218  44.055  18.401  1.00 39.13           C  
ANISOU 6344  CB  LEU B1121     6394   4411   4061    841   -764    455       C  
ATOM   6345  CG  LEU B1121       0.624  42.827  17.716  1.00 42.44           C  
ANISOU 6345  CG  LEU B1121     6644   4994   4486    794   -689    500       C  
ATOM   6346  CD1 LEU B1121       1.633  42.182  16.795  1.00 41.29           C  
ANISOU 6346  CD1 LEU B1121     6466   4852   4370    625   -694    552       C  
ATOM   6347  CD2 LEU B1121       0.111  41.836  18.749  1.00 44.35           C  
ANISOU 6347  CD2 LEU B1121     6784   5365   4702    830   -604    472       C  
ATOM   6348  N   GLN B1122       1.423  47.020  19.470  1.00 42.47           N  
ANISOU 6348  N   GLN B1122     7184   4460   4495   1057   -980    333       N  
ATOM   6349  CA  GLN B1122       2.045  48.069  20.295  1.00 43.02           C  
ANISOU 6349  CA  GLN B1122     7431   4336   4579   1097  -1097    250       C  
ATOM   6350  C   GLN B1122       1.015  48.765  21.178  1.00 47.99           C  
ANISOU 6350  C   GLN B1122     8136   4956   5142   1354  -1121    132       C  
ATOM   6351  O   GLN B1122       1.343  49.254  22.257  1.00 49.20           O  
ANISOU 6351  O   GLN B1122     8409   5024   5262   1436  -1188     18       O  
ATOM   6352  CB  GLN B1122       2.748  49.111  19.407  1.00 44.80           C  
ANISOU 6352  CB  GLN B1122     7773   4346   4904    990  -1222    327       C  
ATOM   6353  CG  GLN B1122       3.462  50.231  20.169  1.00 49.88           C  
ANISOU 6353  CG  GLN B1122     8605   4749   5597   1001  -1377    248       C  
ATOM   6354  CD  GLN B1122       4.034  51.285  19.246  1.00 65.25           C  
ANISOU 6354  CD  GLN B1122    10656   6475   7661    887  -1504    355       C  
ATOM   6355  OE1 GLN B1122       3.344  51.781  18.356  1.00 64.91           O  
ANISOU 6355  OE1 GLN B1122    10626   6400   7636    947  -1518    430       O  
ATOM   6356  NE2 GLN B1122       5.292  51.645  19.457  1.00 54.26           N  
ANISOU 6356  NE2 GLN B1122     9332   4932   6351    719  -1602    374       N  
ATOM   6357  N   GLN B1123      -0.226  48.805  20.712  1.00 44.16           N  
ANISOU 6357  N   GLN B1123     7578   4571   4631   1492  -1072    154       N  
ATOM   6358  CA  GLN B1123      -1.318  49.428  21.448  1.00 45.37           C  
ANISOU 6358  CA  GLN B1123     7774   4755   4711   1763  -1079     50       C  
ATOM   6359  C   GLN B1123      -1.986  48.444  22.391  1.00 48.87           C  
ANISOU 6359  C   GLN B1123     8071   5452   5047   1859   -935     14       C  
ATOM   6360  O   GLN B1123      -2.931  48.806  23.089  1.00 50.54           O  
ANISOU 6360  O   GLN B1123     8280   5749   5172   2096   -909    -65       O  
ATOM   6361  CB  GLN B1123      -2.334  50.050  20.463  1.00 47.36           C  
ANISOU 6361  CB  GLN B1123     8012   4992   4991   1877  -1107    100       C  
ATOM   6362  CG  GLN B1123      -1.956  51.486  20.047  1.00 59.89           C  
ANISOU 6362  CG  GLN B1123     9810   6289   6656   1906  -1281     92       C  
ATOM   6363  CD  GLN B1123      -2.565  51.927  18.733  1.00 79.02           C  
ANISOU 6363  CD  GLN B1123    12214   8679   9130   1923  -1316    201       C  
ATOM   6364  OE1 GLN B1123      -3.711  51.588  18.408  1.00 73.79           O  
ANISOU 6364  OE1 GLN B1123    11417   8196   8423   2047  -1240    219       O  
ATOM   6365  NE2 GLN B1123      -1.797  52.701  17.964  1.00 71.59           N  
ANISOU 6365  NE2 GLN B1123    11402   7514   8284   1797  -1435    286       N  
ATOM   6366  N   LYS B1124      -1.477  47.213  22.424  1.00 43.45           N  
ANISOU 6366  N   LYS B1124     7260   4884   4363   1682   -843     78       N  
ATOM   6367  CA  LYS B1124      -2.029  46.116  23.233  1.00 42.95           C  
ANISOU 6367  CA  LYS B1124     7042   5059   4219   1725   -703     86       C  
ATOM   6368  C   LYS B1124      -3.457  45.711  22.821  1.00 48.04           C  
ANISOU 6368  C   LYS B1124     7505   5897   4851   1824   -608    147       C  
ATOM   6369  O   LYS B1124      -4.232  45.187  23.621  1.00 48.22           O  
ANISOU 6369  O   LYS B1124     7408   6117   4796   1935   -502    149       O  
ATOM   6370  CB  LYS B1124      -1.932  46.444  24.727  1.00 46.35           C  
ANISOU 6370  CB  LYS B1124     7566   5512   4533   1889   -704    -32       C  
ATOM   6371  CG  LYS B1124      -0.524  46.841  25.129  1.00 58.92           C  
ANISOU 6371  CG  LYS B1124     9327   6911   6148   1783   -819    -97       C  
ATOM   6372  CD  LYS B1124      -0.308  46.890  26.630  1.00 68.29           C  
ANISOU 6372  CD  LYS B1124    10589   8152   7206   1920   -818   -212       C  
ATOM   6373  CE  LYS B1124       1.063  47.483  26.952  1.00 79.55           C  
ANISOU 6373  CE  LYS B1124    12196   9355   8673   1821   -972   -293       C  
ATOM   6374  NZ  LYS B1124       2.186  46.750  26.274  1.00 87.01           N  
ANISOU 6374  NZ  LYS B1124    13082  10252   9726   1535   -973   -188       N  
ATOM   6375  N   ARG B1125      -3.778  45.935  21.553  1.00 44.98           N  
ANISOU 6375  N   ARG B1125     7088   5462   4541   1776   -650    208       N  
ATOM   6376  CA  ARG B1125      -5.065  45.560  21.000  1.00 45.29           C  
ANISOU 6376  CA  ARG B1125     6949   5672   4588   1846   -587    267       C  
ATOM   6377  C   ARG B1125      -4.939  44.125  20.472  1.00 48.19           C  
ANISOU 6377  C   ARG B1125     7145   6153   5012   1636   -517    363       C  
ATOM   6378  O   ARG B1125      -4.836  43.884  19.261  1.00 46.41           O  
ANISOU 6378  O   ARG B1125     6883   5896   4855   1516   -556    420       O  
ATOM   6379  CB  ARG B1125      -5.463  46.543  19.894  1.00 45.64           C  
ANISOU 6379  CB  ARG B1125     7058   5604   4678   1912   -685    280       C  
ATOM   6380  CG  ARG B1125      -5.438  48.010  20.324  1.00 54.74           C  
ANISOU 6380  CG  ARG B1125     8414   6583   5801   2103   -788    183       C  
ATOM   6381  CD  ARG B1125      -5.852  48.934  19.181  1.00 65.30           C  
ANISOU 6381  CD  ARG B1125     9814   7805   7193   2163   -889    221       C  
ATOM   6382  NE  ARG B1125      -7.222  49.449  19.324  1.00 77.84           N  
ANISOU 6382  NE  ARG B1125    11343   9500   8735   2427   -879    183       N  
ATOM   6383  CZ  ARG B1125      -7.548  50.680  19.739  1.00 91.37           C  
ANISOU 6383  CZ  ARG B1125    13209  11089  10418   2660   -966     89       C  
ATOM   6384  NH1 ARG B1125      -8.833  51.026  19.822  1.00 76.70           N  
ANISOU 6384  NH1 ARG B1125    11265   9365   8513   2909   -944     59       N  
ATOM   6385  NH2 ARG B1125      -6.612  51.574  20.072  1.00 77.67           N  
ANISOU 6385  NH2 ARG B1125    11709   9095   8707   2653  -1087     20       N  
ATOM   6386  N   TRP B1126      -4.955  43.172  21.400  1.00 45.54           N  
ANISOU 6386  N   TRP B1126     6711   5951   4641   1605   -419    379       N  
ATOM   6387  CA  TRP B1126      -4.562  41.806  21.082  1.00 44.70           C  
ANISOU 6387  CA  TRP B1126     6487   5900   4597   1397   -375    454       C  
ATOM   6388  C   TRP B1126      -5.527  41.137  20.091  1.00 50.40           C  
ANISOU 6388  C   TRP B1126     7026   6734   5392   1347   -362    528       C  
ATOM   6389  O   TRP B1126      -5.089  40.542  19.101  1.00 48.85           O  
ANISOU 6389  O   TRP B1126     6804   6491   5265   1188   -403    558       O  
ATOM   6390  CB  TRP B1126      -4.397  40.961  22.360  1.00 43.36           C  
ANISOU 6390  CB  TRP B1126     6260   5839   4376   1383   -281    472       C  
ATOM   6391  CG  TRP B1126      -3.552  41.608  23.436  1.00 44.48           C  
ANISOU 6391  CG  TRP B1126     6575   5896   4429   1457   -303    387       C  
ATOM   6392  CD1 TRP B1126      -3.927  41.856  24.716  1.00 48.59           C  
ANISOU 6392  CD1 TRP B1126     7109   6521   4832   1629   -244    347       C  
ATOM   6393  CD2 TRP B1126      -2.210  42.097  23.313  1.00 43.62           C  
ANISOU 6393  CD2 TRP B1126     6642   5593   4338   1368   -398    329       C  
ATOM   6394  NE1 TRP B1126      -2.909  42.468  25.404  1.00 47.98           N  
ANISOU 6394  NE1 TRP B1126     7218   6315   4698   1657   -311    251       N  
ATOM   6395  CE2 TRP B1126      -1.842  42.628  24.567  1.00 48.13           C  
ANISOU 6395  CE2 TRP B1126     7333   6145   4810   1488   -409    243       C  
ATOM   6396  CE3 TRP B1126      -1.281  42.137  22.263  1.00 43.81           C  
ANISOU 6396  CE3 TRP B1126     6724   5473   4448   1201   -476    346       C  
ATOM   6397  CZ2 TRP B1126      -0.589  43.190  24.811  1.00 47.16           C  
ANISOU 6397  CZ2 TRP B1126     7382   5847   4691   1430   -509    172       C  
ATOM   6398  CZ3 TRP B1126      -0.027  42.705  22.505  1.00 45.04           C  
ANISOU 6398  CZ3 TRP B1126     7038   5469   4606   1141   -558    294       C  
ATOM   6399  CH2 TRP B1126       0.304  43.221  23.776  1.00 46.49           C  
ANISOU 6399  CH2 TRP B1126     7335   5621   4709   1248   -581    206       C  
ATOM   6400  N   ASP B1127      -6.829  41.256  20.349  1.00 49.63           N  
ANISOU 6400  N   ASP B1127     6796   6789   5272   1491   -311    549       N  
ATOM   6401  CA  ASP B1127      -7.848  40.587  19.527  1.00 50.09           C  
ANISOU 6401  CA  ASP B1127     6654   6971   5406   1446   -307    619       C  
ATOM   6402  C   ASP B1127      -7.910  41.127  18.103  1.00 53.70           C  
ANISOU 6402  C   ASP B1127     7158   7339   5905   1434   -413    606       C  
ATOM   6403  O   ASP B1127      -7.899  40.352  17.145  1.00 52.71           O  
ANISOU 6403  O   ASP B1127     6952   7223   5852   1293   -453    640       O  
ATOM   6404  CB  ASP B1127      -9.223  40.684  20.193  1.00 54.06           C  
ANISOU 6404  CB  ASP B1127     6989   7679   5872   1616   -225    653       C  
ATOM   6405  CG  ASP B1127      -9.376  39.696  21.337  1.00 68.60           C  
ANISOU 6405  CG  ASP B1127     8701   9668   7697   1571   -106    725       C  
ATOM   6406  OD1 ASP B1127      -9.576  38.491  21.065  1.00 68.72           O  
ANISOU 6406  OD1 ASP B1127     8559   9743   7809   1400    -88    813       O  
ATOM   6407  OD2 ASP B1127      -9.291  40.125  22.513  1.00 78.04           O  
ANISOU 6407  OD2 ASP B1127     9957  10915   8779   1712    -37    695       O  
ATOM   6408  N   GLU B1128      -7.990  42.453  17.973  1.00 50.82           N  
ANISOU 6408  N   GLU B1128     6928   6887   5492   1591   -468    556       N  
ATOM   6409  CA  GLU B1128      -7.882  43.118  16.674  1.00 50.02           C  
ANISOU 6409  CA  GLU B1128     6911   6680   5416   1586   -573    559       C  
ATOM   6410  C   GLU B1128      -6.661  42.609  15.916  1.00 51.92           C  
ANISOU 6410  C   GLU B1128     7225   6811   5691   1378   -615    577       C  
ATOM   6411  O   GLU B1128      -6.768  42.176  14.767  1.00 51.57           O  
ANISOU 6411  O   GLU B1128     7120   6794   5681   1295   -661    610       O  
ATOM   6412  CB  GLU B1128      -7.723  44.631  16.848  1.00 52.19           C  
ANISOU 6412  CB  GLU B1128     7379   6808   5642   1752   -636    506       C  
ATOM   6413  CG  GLU B1128      -8.966  45.396  17.268  1.00 62.10           C  
ANISOU 6413  CG  GLU B1128     8587   8153   6855   2005   -627    475       C  
ATOM   6414  CD  GLU B1128      -8.660  46.874  17.472  1.00 78.71           C  
ANISOU 6414  CD  GLU B1128    10918  10065   8923   2164   -714    408       C  
ATOM   6415  OE1 GLU B1128      -8.800  47.364  18.608  1.00 73.14           O  
ANISOU 6415  OE1 GLU B1128    10273   9363   8154   2327   -687    330       O  
ATOM   6416  OE2 GLU B1128      -8.241  47.541  16.505  1.00 70.13           O  
ANISOU 6416  OE2 GLU B1128     9956   8818   7872   2125   -816    436       O  
ATOM   6417  N   ALA B1129      -5.503  42.685  16.570  1.00 46.93           N  
ANISOU 6417  N   ALA B1129     6722   6069   5040   1309   -602    550       N  
ATOM   6418  CA  ALA B1129      -4.238  42.302  15.959  1.00 45.41           C  
ANISOU 6418  CA  ALA B1129     6601   5782   4871   1130   -634    567       C  
ATOM   6419  C   ALA B1129      -4.235  40.830  15.562  1.00 48.52           C  
ANISOU 6419  C   ALA B1129     6847   6278   5310    987   -603    592       C  
ATOM   6420  O   ALA B1129      -3.737  40.484  14.484  1.00 48.17           O  
ANISOU 6420  O   ALA B1129     6807   6213   5281    886   -648    609       O  
ATOM   6421  CB  ALA B1129      -3.094  42.601  16.890  1.00 45.73           C  
ANISOU 6421  CB  ALA B1129     6778   5708   4890   1091   -627    530       C  
ATOM   6422  N   ALA B1130      -4.787  39.970  16.422  1.00 44.21           N  
ANISOU 6422  N   ALA B1130     6175   5841   4783    985   -532    599       N  
ATOM   6423  CA  ALA B1130      -4.954  38.541  16.103  1.00 42.99           C  
ANISOU 6423  CA  ALA B1130     5873   5766   4696    853   -520    627       C  
ATOM   6424  C   ALA B1130      -5.824  38.372  14.866  1.00 46.73           C  
ANISOU 6424  C   ALA B1130     6244   6304   5208    857   -586    640       C  
ATOM   6425  O   ALA B1130      -5.483  37.603  13.950  1.00 45.77           O  
ANISOU 6425  O   ALA B1130     6095   6174   5122    747   -639    631       O  
ATOM   6426  CB  ALA B1130      -5.566  37.779  17.285  1.00 44.06           C  
ANISOU 6426  CB  ALA B1130     5879   6009   4852    859   -433    663       C  
ATOM   6427  N   VAL B1131      -6.949  39.096  14.853  1.00 43.63           N  
ANISOU 6427  N   VAL B1131     5795   5982   4802   1001   -589    651       N  
ATOM   6428  CA  VAL B1131      -7.890  39.090  13.726  1.00 43.58           C  
ANISOU 6428  CA  VAL B1131     5686   6050   4824   1033   -663    661       C  
ATOM   6429  C   VAL B1131      -7.215  39.540  12.421  1.00 46.28           C  
ANISOU 6429  C   VAL B1131     6151   6306   5127   1007   -751    647       C  
ATOM   6430  O   VAL B1131      -7.306  38.844  11.407  1.00 46.24           O  
ANISOU 6430  O   VAL B1131     6082   6340   5146    933   -816    639       O  
ATOM   6431  CB  VAL B1131      -9.153  39.948  14.047  1.00 48.79           C  
ANISOU 6431  CB  VAL B1131     6274   6803   5463   1222   -647    675       C  
ATOM   6432  CG1 VAL B1131      -9.968  40.247  12.802  1.00 49.33           C  
ANISOU 6432  CG1 VAL B1131     6279   6924   5541   1281   -743    682       C  
ATOM   6433  CG2 VAL B1131     -10.015  39.233  15.085  1.00 49.35           C  
ANISOU 6433  CG2 VAL B1131     6154   7021   5576   1230   -559    715       C  
ATOM   6434  N   ASN B1132      -6.512  40.671  12.456  1.00 41.68           N  
ANISOU 6434  N   ASN B1132     5745   5608   4485   1063   -757    647       N  
ATOM   6435  CA  ASN B1132      -5.873  41.215  11.254  1.00 40.80           C  
ANISOU 6435  CA  ASN B1132     5746   5427   4330   1042   -829    668       C  
ATOM   6436  C   ASN B1132      -4.814  40.296  10.664  1.00 43.30           C  
ANISOU 6436  C   ASN B1132     6074   5734   4644    886   -836    660       C  
ATOM   6437  O   ASN B1132      -4.695  40.170   9.436  1.00 42.86           O  
ANISOU 6437  O   ASN B1132     6019   5713   4552    865   -896    670       O  
ATOM   6438  CB  ASN B1132      -5.243  42.578  11.534  1.00 40.62           C  
ANISOU 6438  CB  ASN B1132     5908   5258   4268   1106   -839    688       C  
ATOM   6439  CG  ASN B1132      -5.238  43.478  10.305  1.00 56.57           C  
ANISOU 6439  CG  ASN B1132     8013   7234   6247   1155   -920    745       C  
ATOM   6440  OD1 ASN B1132      -6.293  43.757   9.741  1.00 47.55           O  
ANISOU 6440  OD1 ASN B1132     6808   6161   5096   1265   -967    757       O  
ATOM   6441  ND2 ASN B1132      -4.050  43.926   9.881  1.00 46.90           N  
ANISOU 6441  ND2 ASN B1132     6919   5904   4997   1071   -938    793       N  
ATOM   6442  N   LEU B1133      -4.049  39.650  11.539  1.00 39.31           N  
ANISOU 6442  N   LEU B1133     5578   5194   4164    793   -777    638       N  
ATOM   6443  CA  LEU B1133      -2.924  38.810  11.111  1.00 38.36           C  
ANISOU 6443  CA  LEU B1133     5477   5060   4039    664   -779    622       C  
ATOM   6444  C   LEU B1133      -3.404  37.547  10.390  1.00 42.32           C  
ANISOU 6444  C   LEU B1133     5850   5654   4577    612   -824    585       C  
ATOM   6445  O   LEU B1133      -2.714  37.047   9.497  1.00 41.66           O  
ANISOU 6445  O   LEU B1133     5786   5584   4460    556   -861    563       O  
ATOM   6446  CB  LEU B1133      -2.031  38.444  12.301  1.00 37.50           C  
ANISOU 6446  CB  LEU B1133     5407   4891   3952    593   -714    608       C  
ATOM   6447  CG  LEU B1133      -1.111  39.545  12.835  1.00 41.83           C  
ANISOU 6447  CG  LEU B1133     6104   5325   4465    603   -699    627       C  
ATOM   6448  CD1 LEU B1133      -0.533  39.133  14.202  1.00 41.07           C  
ANISOU 6448  CD1 LEU B1133     6023   5194   4388    561   -642    601       C  
ATOM   6449  CD2 LEU B1133       0.009  39.866  11.842  1.00 43.94           C  
ANISOU 6449  CD2 LEU B1133     6450   5554   4692    535   -731    663       C  
ATOM   6450  N   ALA B1134      -4.584  37.056  10.768  1.00 39.13           N  
ANISOU 6450  N   ALA B1134     5311   5316   4241    635   -827    579       N  
ATOM   6451  CA  ALA B1134      -5.228  35.931  10.078  1.00 39.43           C  
ANISOU 6451  CA  ALA B1134     5217   5426   4338    584   -899    543       C  
ATOM   6452  C   ALA B1134      -5.723  36.233   8.646  1.00 43.87           C  
ANISOU 6452  C   ALA B1134     5769   6051   4849    645   -999    526       C  
ATOM   6453  O   ALA B1134      -6.168  35.327   7.955  1.00 44.36           O  
ANISOU 6453  O   ALA B1134     5739   6165   4951    607  -1085    476       O  
ATOM   6454  CB  ALA B1134      -6.391  35.381  10.919  1.00 40.81           C  
ANISOU 6454  CB  ALA B1134     5230   5662   4614    577   -875    568       C  
ATOM   6455  N   LYS B1135      -5.652  37.486   8.204  1.00 40.30           N  
ANISOU 6455  N   LYS B1135     5414   5586   4310    740  -1002    567       N  
ATOM   6456  CA  LYS B1135      -6.058  37.851   6.841  1.00 40.76           C  
ANISOU 6456  CA  LYS B1135     5478   5712   4299    811  -1095    567       C  
ATOM   6457  C   LYS B1135      -4.879  37.980   5.843  1.00 43.75           C  
ANISOU 6457  C   LYS B1135     5975   6082   4567    786  -1112    574       C  
ATOM   6458  O   LYS B1135      -5.089  38.086   4.636  1.00 44.26           O  
ANISOU 6458  O   LYS B1135     6043   6223   4550    840  -1189    571       O  
ATOM   6459  CB  LYS B1135      -6.886  39.139   6.888  1.00 43.79           C  
ANISOU 6459  CB  LYS B1135     5881   6100   4659    948  -1101    626       C  
ATOM   6460  CG  LYS B1135      -8.221  38.994   7.645  1.00 47.95           C  
ANISOU 6460  CG  LYS B1135     6254   6691   5275   1002  -1091    621       C  
ATOM   6461  CD  LYS B1135      -8.751  40.347   8.108  1.00 52.13           C  
ANISOU 6461  CD  LYS B1135     6836   7194   5779   1154  -1064    668       C  
ATOM   6462  CE  LYS B1135     -10.185  40.266   8.628  1.00 56.99           C  
ANISOU 6462  CE  LYS B1135     7273   7920   6459   1242  -1060    669       C  
ATOM   6463  NZ  LYS B1135     -10.798  41.630   8.778  1.00 63.33           N  
ANISOU 6463  NZ  LYS B1135     8130   8712   7220   1432  -1064    700       N  
ATOM   6464  N   SER B1136      -3.651  37.922   6.353  1.00 38.93           N  
ANISOU 6464  N   SER B1136     5447   5398   3945    710  -1040    585       N  
ATOM   6465  CA  SER B1136      -2.441  38.140   5.551  1.00 38.15           C  
ANISOU 6465  CA  SER B1136     5445   5307   3742    686  -1031    616       C  
ATOM   6466  C   SER B1136      -2.065  36.938   4.707  1.00 42.56           C  
ANISOU 6466  C   SER B1136     5959   5952   4261    653  -1080    532       C  
ATOM   6467  O   SER B1136      -2.572  35.834   4.923  1.00 42.39           O  
ANISOU 6467  O   SER B1136     5845   5942   4320    619  -1122    443       O  
ATOM   6468  CB  SER B1136      -1.265  38.432   6.474  1.00 38.89           C  
ANISOU 6468  CB  SER B1136     5621   5301   3856    611   -944    652       C  
ATOM   6469  OG  SER B1136      -1.066  37.339   7.334  1.00 40.12           O  
ANISOU 6469  OG  SER B1136     5718   5436   4091    537   -914    582       O  
ATOM   6470  N   ARG B1137      -1.150  37.164   3.762  1.00 39.61           N  
ANISOU 6470  N   ARG B1137     5652   5638   3762    665  -1075    565       N  
ATOM   6471  CA  ARG B1137      -0.583  36.091   2.927  1.00 39.75           C  
ANISOU 6471  CA  ARG B1137     5647   5750   3709    662  -1114    475       C  
ATOM   6472  C   ARG B1137       0.248  35.106   3.746  1.00 43.14           C  
ANISOU 6472  C   ARG B1137     6060   6119   4212    574  -1069    408       C  
ATOM   6473  O   ARG B1137       0.402  33.933   3.366  1.00 43.04           O  
ANISOU 6473  O   ARG B1137     6009   6145   4198    573  -1125    294       O  
ATOM   6474  CB  ARG B1137       0.267  36.672   1.797  1.00 40.65           C  
ANISOU 6474  CB  ARG B1137     5827   5969   3650    709  -1095    551       C  
ATOM   6475  CG  ARG B1137      -0.561  37.136   0.596  1.00 50.15           C  
ANISOU 6475  CG  ARG B1137     7031   7280   4742    819  -1178    575       C  
ATOM   6476  CD  ARG B1137      -0.170  38.534   0.111  1.00 57.31           C  
ANISOU 6476  CD  ARG B1137     8023   8203   5548    851  -1131    754       C  
ATOM   6477  NE  ARG B1137       0.898  38.543  -0.886  1.00 64.35           N  
ANISOU 6477  NE  ARG B1137     8947   9234   6271    871  -1094    812       N  
ATOM   6478  CZ  ARG B1137       0.717  38.438  -2.205  1.00 80.76           C  
ANISOU 6478  CZ  ARG B1137    11023  11484   8178    977  -1151    808       C  
ATOM   6479  NH1 ARG B1137      -0.503  38.276  -2.718  1.00 68.11           N  
ANISOU 6479  NH1 ARG B1137     9390   9927   6562   1067  -1265    735       N  
ATOM   6480  NH2 ARG B1137       1.767  38.486  -3.025  1.00 68.87           N  
ANISOU 6480  NH2 ARG B1137     9538  10125   6505   1001  -1094    880       N  
ATOM   6481  N   TRP B1138       0.774  35.582   4.871  1.00 38.81           N  
ANISOU 6481  N   TRP B1138     5548   5469   3728    510   -982    472       N  
ATOM   6482  CA  TRP B1138       1.487  34.725   5.804  1.00 37.69           C  
ANISOU 6482  CA  TRP B1138     5393   5264   3664    431   -940    423       C  
ATOM   6483  C   TRP B1138       0.555  33.640   6.322  1.00 41.74           C  
ANISOU 6483  C   TRP B1138     5820   5740   4300    407   -994    337       C  
ATOM   6484  O   TRP B1138       0.883  32.452   6.277  1.00 41.73           O  
ANISOU 6484  O   TRP B1138     5789   5732   4334    377  -1031    249       O  
ATOM   6485  CB  TRP B1138       2.052  35.554   6.955  1.00 35.58           C  
ANISOU 6485  CB  TRP B1138     5182   4898   3439    379   -855    505       C  
ATOM   6486  CG  TRP B1138       2.577  34.763   8.115  1.00 35.61           C  
ANISOU 6486  CG  TRP B1138     5169   4832   3529    309   -816    465       C  
ATOM   6487  CD1 TRP B1138       3.415  33.697   8.065  1.00 38.20           C  
ANISOU 6487  CD1 TRP B1138     5479   5178   3859    276   -818    400       C  
ATOM   6488  CD2 TRP B1138       2.314  35.006   9.506  1.00 34.93           C  
ANISOU 6488  CD2 TRP B1138     5090   4655   3526    279   -771    489       C  
ATOM   6489  NE1 TRP B1138       3.683  33.241   9.334  1.00 37.08           N  
ANISOU 6489  NE1 TRP B1138     5331   4954   3805    219   -781    393       N  
ATOM   6490  CE2 TRP B1138       3.024  34.030  10.241  1.00 38.43           C  
ANISOU 6490  CE2 TRP B1138     5517   5065   4019    220   -748    448       C  
ATOM   6491  CE3 TRP B1138       1.555  35.958  10.202  1.00 36.25           C  
ANISOU 6491  CE3 TRP B1138     5279   4773   3721    316   -751    537       C  
ATOM   6492  CZ2 TRP B1138       2.996  33.974  11.645  1.00 37.21           C  
ANISOU 6492  CZ2 TRP B1138     5366   4841   3930    189   -703    464       C  
ATOM   6493  CZ3 TRP B1138       1.532  35.905  11.600  1.00 37.29           C  
ANISOU 6493  CZ3 TRP B1138     5415   4843   3912    296   -703    539       C  
ATOM   6494  CH2 TRP B1138       2.245  34.917  12.302  1.00 37.35           C  
ANISOU 6494  CH2 TRP B1138     5405   4830   3958    229   -678    508       C  
ATOM   6495  N   TYR B1139      -0.610  34.056   6.799  1.00 37.90           N  
ANISOU 6495  N   TYR B1139     5290   5229   3883    422  -1002    369       N  
ATOM   6496  CA  TYR B1139      -1.565  33.138   7.375  1.00 37.74           C  
ANISOU 6496  CA  TYR B1139     5166   5183   3991    384  -1042    326       C  
ATOM   6497  C   TYR B1139      -2.037  32.136   6.319  1.00 43.04           C  
ANISOU 6497  C   TYR B1139     5775   5905   4672    394  -1169    225       C  
ATOM   6498  O   TYR B1139      -1.974  30.920   6.530  1.00 41.88           O  
ANISOU 6498  O   TYR B1139     5585   5712   4616    333  -1219    155       O  
ATOM   6499  CB  TYR B1139      -2.750  33.904   7.973  1.00 39.08           C  
ANISOU 6499  CB  TYR B1139     5282   5355   4209    422  -1020    391       C  
ATOM   6500  CG  TYR B1139      -3.721  32.996   8.668  1.00 41.34           C  
ANISOU 6500  CG  TYR B1139     5439   5636   4634    370  -1041    380       C  
ATOM   6501  CD1 TYR B1139      -3.498  32.590   9.986  1.00 42.61           C  
ANISOU 6501  CD1 TYR B1139     5581   5739   4869    307   -963    415       C  
ATOM   6502  CD2 TYR B1139      -4.846  32.498   8.000  1.00 43.21           C  
ANISOU 6502  CD2 TYR B1139     5561   5930   4929    377  -1147    343       C  
ATOM   6503  CE1 TYR B1139      -4.372  31.731  10.622  1.00 44.15           C  
ANISOU 6503  CE1 TYR B1139     5645   5937   5192    247   -975    436       C  
ATOM   6504  CE2 TYR B1139      -5.747  31.642   8.639  1.00 44.81           C  
ANISOU 6504  CE2 TYR B1139     5621   6126   5277    306  -1171    357       C  
ATOM   6505  CZ  TYR B1139      -5.503  31.260   9.949  1.00 52.55           C  
ANISOU 6505  CZ  TYR B1139     6584   7053   6330    239  -1078    413       C  
ATOM   6506  OH  TYR B1139      -6.383  30.408  10.593  1.00 54.88           O  
ANISOU 6506  OH  TYR B1139     6730   7352   6770    159  -1093    457       O  
ATOM   6507  N   ASN B1140      -2.471  32.668   5.171  1.00 41.64           N  
ANISOU 6507  N   ASN B1140     5605   5817   4399    477  -1233    217       N  
ATOM   6508  CA  ASN B1140      -3.016  31.855   4.087  1.00 42.74           C  
ANISOU 6508  CA  ASN B1140     5693   6016   4529    507  -1376    108       C  
ATOM   6509  C   ASN B1140      -2.012  30.844   3.543  1.00 46.92           C  
ANISOU 6509  C   ASN B1140     6268   6548   5010    504  -1420     -2       C  
ATOM   6510  O   ASN B1140      -2.407  29.790   3.047  1.00 47.33           O  
ANISOU 6510  O   ASN B1140     6274   6594   5113    501  -1551   -122       O  
ATOM   6511  CB  ASN B1140      -3.550  32.740   2.954  1.00 45.16           C  
ANISOU 6511  CB  ASN B1140     6015   6434   4709    616  -1429    131       C  
ATOM   6512  CG  ASN B1140      -4.847  33.449   3.332  1.00 71.45           C  
ANISOU 6512  CG  ASN B1140     9268   9770   8109    641  -1436    201       C  
ATOM   6513  OD1 ASN B1140      -5.930  33.084   2.863  1.00 66.95           O  
ANISOU 6513  OD1 ASN B1140     8600   9250   7589    661  -1552    151       O  
ATOM   6514  ND2 ASN B1140      -4.745  34.447   4.207  1.00 63.09           N  
ANISOU 6514  ND2 ASN B1140     8248   8662   7060    645  -1321    308       N  
ATOM   6515  N   GLN B1141      -0.720  31.156   3.646  1.00 43.22           N  
ANISOU 6515  N   GLN B1141     5884   6087   4450    509  -1320     34       N  
ATOM   6516  CA  GLN B1141       0.322  30.244   3.164  1.00 43.39           C  
ANISOU 6516  CA  GLN B1141     5944   6131   4411    530  -1347    -69       C  
ATOM   6517  C   GLN B1141       0.800  29.251   4.239  1.00 47.32           C  
ANISOU 6517  C   GLN B1141     6429   6503   5048    442  -1327   -105       C  
ATOM   6518  O   GLN B1141       0.884  28.054   3.965  1.00 48.45           O  
ANISOU 6518  O   GLN B1141     6561   6609   5238    446  -1428   -230       O  
ATOM   6519  CB  GLN B1141       1.482  31.027   2.520  1.00 44.51           C  
ANISOU 6519  CB  GLN B1141     6161   6385   4367    594  -1259     -8       C  
ATOM   6520  CG  GLN B1141       1.099  31.578   1.124  1.00 58.71           C  
ANISOU 6520  CG  GLN B1141     7975   8333   6000    706  -1317     -7       C  
ATOM   6521  CD  GLN B1141       2.090  32.591   0.534  1.00 72.06           C  
ANISOU 6521  CD  GLN B1141     9725  10142   7513    752  -1214    115       C  
ATOM   6522  OE1 GLN B1141       1.702  33.449  -0.267  1.00 66.19           O  
ANISOU 6522  OE1 GLN B1141     9002   9490   6657    818  -1225    193       O  
ATOM   6523  NE2 GLN B1141       3.364  32.488   0.919  1.00 61.31           N  
ANISOU 6523  NE2 GLN B1141     8383   8781   6130    716  -1118    145       N  
ATOM   6524  N   THR B1142       1.088  29.725   5.451  1.00 42.38           N  
ANISOU 6524  N   THR B1142     5811   5805   4487    371  -1213      1       N  
ATOM   6525  CA  THR B1142       1.537  28.836   6.537  1.00 41.48           C  
ANISOU 6525  CA  THR B1142     5687   5579   4493    293  -1190    -13       C  
ATOM   6526  C   THR B1142       0.624  28.940   7.772  1.00 44.77           C  
ANISOU 6526  C   THR B1142     6045   5916   5052    214  -1152     72       C  
ATOM   6527  O   THR B1142       1.001  29.518   8.789  1.00 43.46           O  
ANISOU 6527  O   THR B1142     5904   5718   4892    184  -1046    159       O  
ATOM   6528  CB  THR B1142       3.051  29.058   6.892  1.00 48.12           C  
ANISOU 6528  CB  THR B1142     6594   6429   5260    293  -1089     18       C  
ATOM   6529  OG1 THR B1142       3.307  30.433   7.209  1.00 45.83           O  
ANISOU 6529  OG1 THR B1142     6341   6168   4906    288   -986    138       O  
ATOM   6530  CG2 THR B1142       3.928  28.664   5.704  1.00 48.09           C  
ANISOU 6530  CG2 THR B1142     6622   6526   5124    381  -1127    -75       C  
ATOM   6531  N   PRO B1143      -0.587  28.359   7.686  1.00 42.07           N  
ANISOU 6531  N   PRO B1143     5614   5550   4822    184  -1246     47       N  
ATOM   6532  CA  PRO B1143      -1.546  28.484   8.781  1.00 41.56           C  
ANISOU 6532  CA  PRO B1143     5466   5450   4876    121  -1200    143       C  
ATOM   6533  C   PRO B1143      -1.165  27.722  10.059  1.00 44.36           C  
ANISOU 6533  C   PRO B1143     5810   5708   5337     36  -1149    189       C  
ATOM   6534  O   PRO B1143      -1.438  28.205  11.150  1.00 43.37           O  
ANISOU 6534  O   PRO B1143     5660   5583   5234     16  -1049    291       O  
ATOM   6535  CB  PRO B1143      -2.836  27.903   8.179  1.00 44.61           C  
ANISOU 6535  CB  PRO B1143     5742   5848   5360    101  -1334    100       C  
ATOM   6536  CG  PRO B1143      -2.366  26.910   7.189  1.00 49.71           C  
ANISOU 6536  CG  PRO B1143     6426   6464   5999    116  -1468    -42       C  
ATOM   6537  CD  PRO B1143      -1.120  27.522   6.591  1.00 44.72           C  
ANISOU 6537  CD  PRO B1143     5914   5898   5181    207  -1405    -74       C  
ATOM   6538  N   ASN B1144      -0.562  26.541   9.943  1.00 40.70           N  
ANISOU 6538  N   ASN B1144     5368   5164   4932      0  -1220    115       N  
ATOM   6539  CA  ASN B1144      -0.287  25.752  11.138  1.00 40.05           C  
ANISOU 6539  CA  ASN B1144     5273   4984   4959    -80  -1185    173       C  
ATOM   6540  C   ASN B1144       0.541  26.581  12.087  1.00 43.07           C  
ANISOU 6540  C   ASN B1144     5722   5390   5254    -60  -1040    250       C  
ATOM   6541  O   ASN B1144       0.161  26.793  13.241  1.00 43.20           O  
ANISOU 6541  O   ASN B1144     5703   5402   5310    -95   -958    355       O  
ATOM   6542  CB  ASN B1144       0.453  24.450  10.812  1.00 40.00           C  
ANISOU 6542  CB  ASN B1144     5310   4876   5012    -95  -1289     70       C  
ATOM   6543  CG  ASN B1144      -0.448  23.398  10.185  1.00 58.64           C  
ANISOU 6543  CG  ASN B1144     7603   7164   7514   -143  -1460     -2       C  
ATOM   6544  OD1 ASN B1144      -1.666  23.370  10.405  1.00 52.47           O  
ANISOU 6544  OD1 ASN B1144     6712   6383   6841   -212  -1489     69       O  
ATOM   6545  ND2 ASN B1144       0.155  22.522   9.395  1.00 50.34           N  
ANISOU 6545  ND2 ASN B1144     6612   6050   6464   -101  -1584   -147       N  
ATOM   6546  N   ARG B1145       1.676  27.046  11.572  1.00 38.18           N  
ANISOU 6546  N   ARG B1145     5193   4805   4510      0  -1014    198       N  
ATOM   6547  CA  ARG B1145       2.580  27.918  12.299  1.00 36.38           C  
ANISOU 6547  CA  ARG B1145     5032   4596   4196     15   -900    256       C  
ATOM   6548  C   ARG B1145       1.833  29.195  12.709  1.00 40.30           C  
ANISOU 6548  C   ARG B1145     5518   5139   4654     38   -829    338       C  
ATOM   6549  O   ARG B1145       1.675  29.477  13.918  1.00 39.68           O  
ANISOU 6549  O   ARG B1145     5437   5044   4596     22   -756    411       O  
ATOM   6550  CB  ARG B1145       3.808  28.231  11.425  1.00 33.52           C  
ANISOU 6550  CB  ARG B1145     4738   4284   3713     68   -899    197       C  
ATOM   6551  CG  ARG B1145       4.864  29.089  12.075  1.00 35.65           C  
ANISOU 6551  CG  ARG B1145     5068   4566   3912     66   -805    254       C  
ATOM   6552  CD  ARG B1145       6.246  28.899  11.426  1.00 37.41           C  
ANISOU 6552  CD  ARG B1145     5325   4836   4053     97   -806    203       C  
ATOM   6553  NE  ARG B1145       7.333  29.387  12.278  1.00 37.47           N  
ANISOU 6553  NE  ARG B1145     5369   4835   4035     70   -736    256       N  
ATOM   6554  CZ  ARG B1145       8.623  29.382  11.949  1.00 48.30           C  
ANISOU 6554  CZ  ARG B1145     6750   6260   5341     85   -718    241       C  
ATOM   6555  NH1 ARG B1145       9.018  28.933  10.771  1.00 39.05           N  
ANISOU 6555  NH1 ARG B1145     5561   5172   4105    144   -752    174       N  
ATOM   6556  NH2 ARG B1145       9.528  29.850  12.799  1.00 33.15           N  
ANISOU 6556  NH2 ARG B1145     4852   4327   3416     49   -669    292       N  
ATOM   6557  N   ALA B1146       1.343  29.937  11.709  1.00 36.61           N  
ANISOU 6557  N   ALA B1146     5049   4735   4124     91   -857    321       N  
ATOM   6558  CA  ALA B1146       0.753  31.254  11.967  1.00 36.03           C  
ANISOU 6558  CA  ALA B1146     4988   4697   4004    137   -802    388       C  
ATOM   6559  C   ALA B1146      -0.362  31.178  13.011  1.00 39.44           C  
ANISOU 6559  C   ALA B1146     5338   5128   4517    126   -766    449       C  
ATOM   6560  O   ALA B1146      -0.525  32.101  13.807  1.00 38.80           O  
ANISOU 6560  O   ALA B1146     5287   5057   4400    168   -694    502       O  
ATOM   6561  CB  ALA B1146       0.255  31.911  10.670  1.00 37.29           C  
ANISOU 6561  CB  ALA B1146     5148   4923   4096    200   -855    368       C  
ATOM   6562  N   LYS B1147      -1.096  30.071  13.039  1.00 36.52           N  
ANISOU 6562  N   LYS B1147     4866   4750   4258     71   -819    446       N  
ATOM   6563  CA  LYS B1147      -2.154  29.901  14.040  1.00 37.18           C  
ANISOU 6563  CA  LYS B1147     4845   4859   4422     50   -774    531       C  
ATOM   6564  C   LYS B1147      -1.598  29.909  15.465  1.00 40.59           C  
ANISOU 6564  C   LYS B1147     5316   5266   4839     38   -673    594       C  
ATOM   6565  O   LYS B1147      -2.159  30.568  16.339  1.00 41.11           O  
ANISOU 6565  O   LYS B1147     5357   5389   4874     89   -593    659       O  
ATOM   6566  CB  LYS B1147      -3.003  28.629  13.789  1.00 40.60           C  
ANISOU 6566  CB  LYS B1147     5149   5275   5003    -36   -863    535       C  
ATOM   6567  CG  LYS B1147      -4.295  28.892  13.018  1.00 51.79           C  
ANISOU 6567  CG  LYS B1147     6455   6767   6455    -11   -929    531       C  
ATOM   6568  CD  LYS B1147      -4.632  27.788  11.991  1.00 62.51           C  
ANISOU 6568  CD  LYS B1147     7753   8080   7917    -78  -1088    452       C  
ATOM   6569  CE  LYS B1147      -5.100  26.479  12.623  1.00 70.47           C  
ANISOU 6569  CE  LYS B1147     8651   9019   9106   -207  -1132    511       C  
ATOM   6570  NZ  LYS B1147      -5.023  25.367  11.633  1.00 77.72           N  
ANISOU 6570  NZ  LYS B1147     9570   9844  10118   -264  -1308    397       N  
ATOM   6571  N   ARG B1148      -0.506  29.188  15.701  1.00 35.83           N  
ANISOU 6571  N   ARG B1148     4775   4591   4247    -13   -682    570       N  
ATOM   6572  CA  ARG B1148       0.101  29.172  17.040  1.00 34.96           C  
ANISOU 6572  CA  ARG B1148     4709   4463   4110    -18   -599    626       C  
ATOM   6573  C   ARG B1148       0.646  30.562  17.431  1.00 38.03           C  
ANISOU 6573  C   ARG B1148     5201   4874   4374     63   -536    617       C  
ATOM   6574  O   ARG B1148       0.335  31.090  18.505  1.00 38.05           O  
ANISOU 6574  O   ARG B1148     5208   4914   4335    111   -463    668       O  
ATOM   6575  CB  ARG B1148       1.199  28.099  17.133  1.00 33.16           C  
ANISOU 6575  CB  ARG B1148     4526   4152   3923    -78   -637    597       C  
ATOM   6576  CG  ARG B1148       0.641  26.679  17.057  1.00 37.61           C  
ANISOU 6576  CG  ARG B1148     5000   4659   4632   -162   -708    622       C  
ATOM   6577  CD  ARG B1148       1.642  25.647  17.524  1.00 37.06           C  
ANISOU 6577  CD  ARG B1148     4979   4498   4606   -204   -733    619       C  
ATOM   6578  NE  ARG B1148       2.708  25.449  16.549  1.00 37.62           N  
ANISOU 6578  NE  ARG B1148     5127   4530   4639   -176   -801    496       N  
ATOM   6579  CZ  ARG B1148       2.601  24.723  15.433  1.00 46.76           C  
ANISOU 6579  CZ  ARG B1148     6268   5642   5854   -184   -914    403       C  
ATOM   6580  NH1 ARG B1148       1.458  24.110  15.119  1.00 33.84           N  
ANISOU 6580  NH1 ARG B1148     4545   3975   4339   -239   -990    417       N  
ATOM   6581  NH2 ARG B1148       3.653  24.598  14.622  1.00 24.81           N  
ANISOU 6581  NH2 ARG B1148     3557   2859   3010   -132   -957    294       N  
ATOM   6582  N   VAL B1149       1.434  31.152  16.538  1.00 33.40           N  
ANISOU 6582  N   VAL B1149     4695   4267   3728     80   -570    553       N  
ATOM   6583  CA  VAL B1149       2.005  32.481  16.768  1.00 32.49           C  
ANISOU 6583  CA  VAL B1149     4681   4144   3520    135   -536    549       C  
ATOM   6584  C   VAL B1149       0.920  33.530  17.081  1.00 37.81           C  
ANISOU 6584  C   VAL B1149     5346   4858   4163    222   -505    578       C  
ATOM   6585  O   VAL B1149       1.092  34.356  17.992  1.00 37.36           O  
ANISOU 6585  O   VAL B1149     5357   4788   4051    278   -464    585       O  
ATOM   6586  CB  VAL B1149       2.858  32.948  15.566  1.00 35.02           C  
ANISOU 6586  CB  VAL B1149     5062   4451   3792    128   -580    507       C  
ATOM   6587  CG1 VAL B1149       3.377  34.374  15.781  1.00 34.51           C  
ANISOU 6587  CG1 VAL B1149     5098   4355   3659    164   -562    522       C  
ATOM   6588  CG2 VAL B1149       3.990  32.011  15.364  1.00 34.23           C  
ANISOU 6588  CG2 VAL B1149     4969   4331   3704     72   -601    472       C  
ATOM   6589  N   ILE B1150      -0.186  33.503  16.335  1.00 35.14           N  
ANISOU 6589  N   ILE B1150     4925   4570   3858    246   -534    584       N  
ATOM   6590  CA  ILE B1150      -1.259  34.484  16.569  1.00 35.61           C  
ANISOU 6590  CA  ILE B1150     4963   4679   3888    349   -508    608       C  
ATOM   6591  C   ILE B1150      -1.913  34.252  17.932  1.00 39.47           C  
ANISOU 6591  C   ILE B1150     5386   5228   4384    385   -430    660       C  
ATOM   6592  O   ILE B1150      -2.293  35.211  18.599  1.00 39.50           O  
ANISOU 6592  O   ILE B1150     5425   5261   4323    496   -387    663       O  
ATOM   6593  CB  ILE B1150      -2.342  34.477  15.448  1.00 39.27           C  
ANISOU 6593  CB  ILE B1150     5333   5200   4386    373   -564    606       C  
ATOM   6594  CG1 ILE B1150      -1.743  34.988  14.128  1.00 39.31           C  
ANISOU 6594  CG1 ILE B1150     5420   5171   4343    374   -630    567       C  
ATOM   6595  CG2 ILE B1150      -3.564  35.319  15.869  1.00 40.35           C  
ANISOU 6595  CG2 ILE B1150     5418   5410   4504    492   -530    638       C  
ATOM   6596  CD1 ILE B1150      -2.408  34.402  12.870  1.00 45.31           C  
ANISOU 6596  CD1 ILE B1150     6094   5984   5139    358   -712    541       C  
ATOM   6597  N   THR B1151      -2.039  32.985  18.338  1.00 36.17           N  
ANISOU 6597  N   THR B1151     4875   4831   4039    299   -415    704       N  
ATOM   6598  CA  THR B1151      -2.618  32.647  19.652  1.00 36.81           C  
ANISOU 6598  CA  THR B1151     4879   4988   4119    322   -329    785       C  
ATOM   6599  C   THR B1151      -1.710  33.146  20.788  1.00 39.65           C  
ANISOU 6599  C   THR B1151     5363   5323   4379    375   -276    770       C  
ATOM   6600  O   THR B1151      -2.210  33.548  21.839  1.00 40.28           O  
ANISOU 6600  O   THR B1151     5428   5488   4391    471   -202    807       O  
ATOM   6601  CB  THR B1151      -2.919  31.117  19.798  1.00 45.77           C  
ANISOU 6601  CB  THR B1151     5887   6129   5374    198   -338    860       C  
ATOM   6602  OG1 THR B1151      -3.986  30.742  18.914  1.00 46.98           O  
ANISOU 6602  OG1 THR B1151     5905   6319   5624    160   -394    876       O  
ATOM   6603  CG2 THR B1151      -3.336  30.767  21.217  1.00 44.37           C  
ANISOU 6603  CG2 THR B1151     5639   6039   5179    215   -237    972       C  
ATOM   6604  N   THR B1152      -0.392  33.133  20.554  1.00 34.26           N  
ANISOU 6604  N   THR B1152     4796   4539   3681    321   -320    714       N  
ATOM   6605  CA  THR B1152       0.577  33.688  21.482  1.00 33.66           C  
ANISOU 6605  CA  THR B1152     4844   4426   3519    361   -300    684       C  
ATOM   6606  C   THR B1152       0.378  35.195  21.622  1.00 37.66           C  
ANISOU 6606  C   THR B1152     5442   4925   3943    485   -304    633       C  
ATOM   6607  O   THR B1152       0.268  35.692  22.728  1.00 37.81           O  
ANISOU 6607  O   THR B1152     5505   4979   3881    583   -263    625       O  
ATOM   6608  CB  THR B1152       2.051  33.382  21.055  1.00 41.32           C  
ANISOU 6608  CB  THR B1152     5897   5300   4504    271   -356    638       C  
ATOM   6609  OG1 THR B1152       2.241  31.970  20.904  1.00 41.74           O  
ANISOU 6609  OG1 THR B1152     5878   5343   4637    176   -368    670       O  
ATOM   6610  CG2 THR B1152       3.043  33.901  22.086  1.00 38.80           C  
ANISOU 6610  CG2 THR B1152     5688   4946   4107    301   -350    609       C  
ATOM   6611  N   PHE B1153       0.337  35.916  20.507  1.00 34.60           N  
ANISOU 6611  N   PHE B1153     5089   4486   3570    491   -360    597       N  
ATOM   6612  CA  PHE B1153       0.040  37.357  20.515  1.00 35.34           C  
ANISOU 6612  CA  PHE B1153     5273   4547   3606    611   -381    557       C  
ATOM   6613  C   PHE B1153      -1.295  37.644  21.192  1.00 42.11           C  
ANISOU 6613  C   PHE B1153     6059   5516   4424    752   -322    575       C  
ATOM   6614  O   PHE B1153      -1.411  38.567  21.994  1.00 42.52           O  
ANISOU 6614  O   PHE B1153     6194   5563   4397    884   -313    532       O  
ATOM   6615  CB  PHE B1153      -0.025  37.924  19.083  1.00 36.75           C  
ANISOU 6615  CB  PHE B1153     5472   4675   3816    593   -447    550       C  
ATOM   6616  CG  PHE B1153       1.324  38.109  18.426  1.00 37.24           C  
ANISOU 6616  CG  PHE B1153     5624   4638   3886    493   -501    536       C  
ATOM   6617  CD1 PHE B1153       2.300  38.902  19.020  1.00 40.06           C  
ANISOU 6617  CD1 PHE B1153     6108   4900   4212    492   -530    506       C  
ATOM   6618  CD2 PHE B1153       1.607  37.502  17.203  1.00 38.36           C  
ANISOU 6618  CD2 PHE B1153     5717   4794   4064    405   -529    551       C  
ATOM   6619  CE1 PHE B1153       3.539  39.081  18.414  1.00 40.56           C  
ANISOU 6619  CE1 PHE B1153     6228   4892   4292    390   -575    514       C  
ATOM   6620  CE2 PHE B1153       2.848  37.681  16.585  1.00 40.63           C  
ANISOU 6620  CE2 PHE B1153     6068   5025   4344    325   -564    552       C  
ATOM   6621  CZ  PHE B1153       3.816  38.477  17.184  1.00 38.84           C  
ANISOU 6621  CZ  PHE B1153     5947   4711   4098    309   -583    545       C  
ATOM   6622  N   ARG B1154      -2.304  36.837  20.872  1.00 40.25           N  
ANISOU 6622  N   ARG B1154     5663   5386   4246    728   -287    637       N  
ATOM   6623  CA  ARG B1154      -3.647  37.077  21.389  1.00 41.54           C  
ANISOU 6623  CA  ARG B1154     5719   5686   4379    859   -224    673       C  
ATOM   6624  C   ARG B1154      -3.675  37.013  22.907  1.00 47.09           C  
ANISOU 6624  C   ARG B1154     6425   6474   4991    944   -138    692       C  
ATOM   6625  O   ARG B1154      -4.097  37.972  23.554  1.00 48.33           O  
ANISOU 6625  O   ARG B1154     6633   6678   5053   1118   -113    649       O  
ATOM   6626  CB  ARG B1154      -4.658  36.087  20.808  1.00 41.16           C  
ANISOU 6626  CB  ARG B1154     5472   5736   4428    785   -212    751       C  
ATOM   6627  CG  ARG B1154      -6.058  36.637  20.810  1.00 50.21           C  
ANISOU 6627  CG  ARG B1154     6503   7014   5559    924   -180    776       C  
ATOM   6628  CD  ARG B1154      -7.056  35.653  20.286  1.00 56.51           C  
ANISOU 6628  CD  ARG B1154     7089   7911   6468    835   -182    859       C  
ATOM   6629  NE  ARG B1154      -7.415  34.711  21.338  1.00 65.90           N  
ANISOU 6629  NE  ARG B1154     8147   9215   7678    790    -89    966       N  
ATOM   6630  CZ  ARG B1154      -7.170  33.402  21.328  1.00 79.28           C  
ANISOU 6630  CZ  ARG B1154     9767  10879   9476    616   -100   1035       C  
ATOM   6631  NH1 ARG B1154      -6.570  32.816  20.296  1.00 66.39           N  
ANISOU 6631  NH1 ARG B1154     8177   9116   7934    480   -203    988       N  
ATOM   6632  NH2 ARG B1154      -7.548  32.662  22.366  1.00 65.22           N  
ANISOU 6632  NH2 ARG B1154     7868   9206   7705    586     -8   1158       N  
ATOM   6633  N   THR B1155      -3.212  35.891  23.463  1.00 43.28           N  
ANISOU 6633  N   THR B1155     5899   6012   4533    834   -100    753       N  
ATOM   6634  CA  THR B1155      -3.313  35.626  24.912  1.00 43.87           C  
ANISOU 6634  CA  THR B1155     5954   6201   4515    907     -7    802       C  
ATOM   6635  C   THR B1155      -2.117  36.129  25.717  1.00 47.11           C  
ANISOU 6635  C   THR B1155     6545   6528   4825    949    -33    720       C  
ATOM   6636  O   THR B1155      -2.284  36.593  26.830  1.00 48.02           O  
ANISOU 6636  O   THR B1155     6702   6730   4814   1095     17    701       O  
ATOM   6637  CB  THR B1155      -3.477  34.107  25.212  1.00 50.45           C  
ANISOU 6637  CB  THR B1155     6643   7100   5427    768     46    936       C  
ATOM   6638  OG1 THR B1155      -2.340  33.388  24.720  1.00 48.01           O  
ANISOU 6638  OG1 THR B1155     6401   6646   5197    611    -26    916       O  
ATOM   6639  CG2 THR B1155      -4.726  33.562  24.564  1.00 48.94           C  
ANISOU 6639  CG2 THR B1155     6253   6997   5344    719     62   1026       C  
ATOM   6640  N   GLY B1156      -0.915  36.025  25.165  1.00 42.18           N  
ANISOU 6640  N   GLY B1156     6022   5751   4254    827   -115    670       N  
ATOM   6641  CA  GLY B1156       0.306  36.242  25.951  1.00 41.76           C  
ANISOU 6641  CA  GLY B1156     6110   5627   4131    829   -149    611       C  
ATOM   6642  C   GLY B1156       0.634  35.046  26.842  1.00 46.02           C  
ANISOU 6642  C   GLY B1156     6595   6235   4655    770    -92    696       C  
ATOM   6643  O   GLY B1156       1.233  35.204  27.901  1.00 45.59           O  
ANISOU 6643  O   GLY B1156     6627   6197   4499    832    -89    667       O  
ATOM   6644  N   THR B1157       0.221  33.856  26.401  1.00 43.10           N  
ANISOU 6644  N   THR B1157     6088   5898   4390    654    -62    799       N  
ATOM   6645  CA  THR B1157       0.501  32.570  27.063  1.00 43.09           C  
ANISOU 6645  CA  THR B1157     6028   5931   4413    571    -23    904       C  
ATOM   6646  C   THR B1157       1.203  31.627  26.072  1.00 45.42           C  
ANISOU 6646  C   THR B1157     6308   6101   4848    404    -96    905       C  
ATOM   6647  O   THR B1157       1.404  31.988  24.917  1.00 44.89           O  
ANISOU 6647  O   THR B1157     6265   5951   4840    363   -162    831       O  
ATOM   6648  CB  THR B1157      -0.817  31.873  27.515  1.00 52.66           C  
ANISOU 6648  CB  THR B1157     7066   7299   5643    583     78   1054       C  
ATOM   6649  OG1 THR B1157      -1.558  31.446  26.363  1.00 51.84           O  
ANISOU 6649  OG1 THR B1157     6841   7170   5684    487     49   1086       O  
ATOM   6650  CG2 THR B1157      -1.685  32.807  28.345  1.00 52.58           C  
ANISOU 6650  CG2 THR B1157     7042   7449   5487    774    162   1052       C  
ATOM   6651  N   TRP B1158       1.541  30.416  26.504  1.00 41.35           N  
ANISOU 6651  N   TRP B1158     5753   5578   4382    321    -87    992       N  
ATOM   6652  CA  TRP B1158       2.125  29.417  25.608  1.00 40.37           C  
ANISOU 6652  CA  TRP B1158     5611   5337   4391    187   -162    986       C  
ATOM   6653  C   TRP B1158       1.121  28.309  25.224  1.00 43.83           C  
ANISOU 6653  C   TRP B1158     5902   5786   4967     95   -158   1094       C  
ATOM   6654  O   TRP B1158       1.514  27.272  24.688  1.00 42.48           O  
ANISOU 6654  O   TRP B1158     5715   5514   4911     -8   -226   1100       O  
ATOM   6655  CB  TRP B1158       3.379  28.803  26.241  1.00 39.10           C  
ANISOU 6655  CB  TRP B1158     5527   5119   4209    157   -189    988       C  
ATOM   6656  CG  TRP B1158       4.419  29.813  26.601  1.00 39.67           C  
ANISOU 6656  CG  TRP B1158     5731   5174   4170    224   -216    883       C  
ATOM   6657  CD1 TRP B1158       4.612  30.393  27.819  1.00 43.17           C  
ANISOU 6657  CD1 TRP B1158     6242   5684   4477    324   -181    880       C  
ATOM   6658  CD2 TRP B1158       5.412  30.365  25.733  1.00 38.69           C  
ANISOU 6658  CD2 TRP B1158     5680   4960   4061    194   -292    770       C  
ATOM   6659  NE1 TRP B1158       5.661  31.275  27.766  1.00 42.12           N  
ANISOU 6659  NE1 TRP B1158     6223   5488   4292    346   -248    763       N  
ATOM   6660  CE2 TRP B1158       6.167  31.283  26.495  1.00 42.69           C  
ANISOU 6660  CE2 TRP B1158     6293   5469   4460    260   -309    708       C  
ATOM   6661  CE3 TRP B1158       5.731  30.181  24.380  1.00 39.17           C  
ANISOU 6661  CE3 TRP B1158     5722   4951   4209    121   -348    719       C  
ATOM   6662  CZ2 TRP B1158       7.225  32.010  25.957  1.00 41.47           C  
ANISOU 6662  CZ2 TRP B1158     6212   5239   4305    233   -381    616       C  
ATOM   6663  CZ3 TRP B1158       6.777  30.898  23.846  1.00 39.99           C  
ANISOU 6663  CZ3 TRP B1158     5897   5006   4290    110   -401    635       C  
ATOM   6664  CH2 TRP B1158       7.518  31.807  24.633  1.00 40.78           C  
ANISOU 6664  CH2 TRP B1158     6090   5100   4304    154   -417    593       C  
ATOM   6665  N   ASP B1159      -0.166  28.560  25.460  1.00 41.50           N  
ANISOU 6665  N   ASP B1159     5497   5608   4665    136    -89   1171       N  
ATOM   6666  CA  ASP B1159      -1.225  27.548  25.313  1.00 42.68           C  
ANISOU 6666  CA  ASP B1159     5480   5788   4950     41    -80   1304       C  
ATOM   6667  C   ASP B1159      -1.300  26.889  23.942  1.00 47.93           C  
ANISOU 6667  C   ASP B1159     6104   6330   5775    -75   -196   1250       C  
ATOM   6668  O   ASP B1159      -1.727  25.747  23.839  1.00 49.07           O  
ANISOU 6668  O   ASP B1159     6151   6430   6064   -189   -234   1343       O  
ATOM   6669  CB  ASP B1159      -2.607  28.168  25.561  1.00 45.50           C  
ANISOU 6669  CB  ASP B1159     5709   6311   5267    120      6   1372       C  
ATOM   6670  CG  ASP B1159      -2.808  28.652  26.982  1.00 54.70           C  
ANISOU 6670  CG  ASP B1159     6879   7636   6268    251    130   1446       C  
ATOM   6671  OD1 ASP B1159      -2.063  28.212  27.890  1.00 56.02           O  
ANISOU 6671  OD1 ASP B1159     7114   7796   6377    249    155   1495       O  
ATOM   6672  OD2 ASP B1159      -3.736  29.474  27.180  1.00 58.32           O  
ANISOU 6672  OD2 ASP B1159     7271   8239   6649    371    200   1453       O  
ATOM   6673  N   ALA B1160      -0.936  27.613  22.885  1.00 43.99           N  
ANISOU 6673  N   ALA B1160     5679   5780   5254    -43   -258   1105       N  
ATOM   6674  CA  ALA B1160      -1.096  27.110  21.518  1.00 43.41           C  
ANISOU 6674  CA  ALA B1160     5570   5623   5301   -121   -368   1037       C  
ATOM   6675  C   ALA B1160      -0.171  25.944  21.223  1.00 47.45           C  
ANISOU 6675  C   ALA B1160     6131   5998   5901   -209   -455   1008       C  
ATOM   6676  O   ALA B1160      -0.427  25.172  20.297  1.00 47.90           O  
ANISOU 6676  O   ALA B1160     6141   5978   6079   -281   -557    972       O  
ATOM   6677  CB  ALA B1160      -0.849  28.226  20.514  1.00 43.13           C  
ANISOU 6677  CB  ALA B1160     5610   5586   5190    -49   -402    907       C  
ATOM   6678  N   TYR B1161       0.915  25.849  21.964  1.00 43.59           N  
ANISOU 6678  N   TYR B1161     5739   5476   5346   -189   -429   1007       N  
ATOM   6679  CA  TYR B1161       1.903  24.818  21.778  1.00 43.24           C  
ANISOU 6679  CA  TYR B1161     5750   5310   5369   -243   -506    973       C  
ATOM   6680  C   TYR B1161       1.482  23.787  22.775  1.00 49.21           C  
ANISOU 6680  C   TYR B1161     6439   6048   6209   -309   -484   1131       C  
ATOM   6681  O   TYR B1161       0.818  24.106  23.685  1.00 49.58           O  
ANISOU 6681  O   TYR B1161     6430   6201   6208   -287   -388   1246       O  
ATOM   6682  CB  TYR B1161       3.315  25.403  22.000  1.00 42.90           C  
ANISOU 6682  CB  TYR B1161     5836   5259   5204   -178   -493    889       C  
ATOM   6683  CG  TYR B1161       3.660  26.501  21.007  1.00 43.06           C  
ANISOU 6683  CG  TYR B1161     5909   5304   5148   -127   -509    767       C  
ATOM   6684  CD1 TYR B1161       4.366  26.231  19.862  1.00 44.40           C  
ANISOU 6684  CD1 TYR B1161     6110   5421   5340   -137   -587    663       C  
ATOM   6685  CD2 TYR B1161       3.248  27.799  21.198  1.00 43.29           C  
ANISOU 6685  CD2 TYR B1161     5954   5412   5082    -61   -448    763       C  
ATOM   6686  CE1 TYR B1161       4.642  27.195  18.955  1.00 43.95           C  
ANISOU 6686  CE1 TYR B1161     6090   5399   5211    -97   -594    583       C  
ATOM   6687  CE2 TYR B1161       3.510  28.757  20.277  1.00 43.35           C  
ANISOU 6687  CE2 TYR B1161     6009   5426   5037    -27   -470    678       C  
ATOM   6688  CZ  TYR B1161       4.199  28.451  19.151  1.00 49.21           C  
ANISOU 6688  CZ  TYR B1161     6771   6125   5800    -52   -539    600       C  
ATOM   6689  OH  TYR B1161       4.470  29.407  18.226  1.00 47.06           O  
ANISOU 6689  OH  TYR B1161     6540   5874   5466    -20   -553    541       O  
ATOM   6690  N   GLY B1200       1.782  22.532  22.615  1.00 51.19           N  
ANISOU 6690  N   GLY B1200     6488   6402   6560     -2   -118     70       N  
ATOM   6691  CA  GLY B1200       1.299  21.622  23.631  1.00 51.59           C  
ANISOU 6691  CA  GLY B1200     6539   6451   6610     -2   -118     70       C  
ATOM   6692  C   GLY B1200       0.002  21.013  23.214  1.00 56.45           C  
ANISOU 6692  C   GLY B1200     7156   7067   7227     -3   -118     70       C  
ATOM   6693  O   GLY B1200      -0.440  21.311  22.138  1.00 56.33           O  
ANISOU 6693  O   GLY B1200     7140   7052   7211     -3   -118     70       O  
ATOM   6694  N   SER B1201      -0.649  20.180  24.013  1.00 53.58           N  
ANISOU 6694  N   SER B1201     6793   6703   6863     -3   -118     70       N  
ATOM   6695  CA  SER B1201      -1.824  19.651  23.335  1.00 53.69           C  
ANISOU 6695  CA  SER B1201     6807   6717   6878     -4   -118     70       C  
ATOM   6696  C   SER B1201      -3.104  20.471  23.501  1.00 57.23           C  
ANISOU 6696  C   SER B1201     7254   7165   7326     -4   -118     71       C  
ATOM   6697  O   SER B1201      -3.874  20.640  22.569  1.00 56.68           O  
ANISOU 6697  O   SER B1201     7184   7095   7256     -5   -118     71       O  
ATOM   6698  CB  SER B1201      -2.062  18.234  23.834  1.00 58.06           C  
ANISOU 6698  CB  SER B1201     7361   7269   7431     -4   -118     71       C  
ATOM   6699  OG  SER B1201      -2.823  17.470  22.929  1.00 67.24           O  
ANISOU 6699  OG  SER B1201     8523   8430   8594     -4   -119     70       O  
ATOM   6700  N   LYS B 230      -3.446  20.655  24.770  1.00 51.14           N  
ANISOU 6700  N   LYS B 230     6830   6335   6265   -488    431     62       N  
ATOM   6701  CA  LYS B 230      -4.709  21.068  25.299  1.00 50.94           C  
ANISOU 6701  CA  LYS B 230     6794   6318   6242   -432    358     91       C  
ATOM   6702  C   LYS B 230      -4.119  22.055  26.344  1.00 54.92           C  
ANISOU 6702  C   LYS B 230     7263   6823   6781   -408    362     76       C  
ATOM   6703  O   LYS B 230      -4.611  22.148  27.476  1.00 53.98           O  
ANISOU 6703  O   LYS B 230     7084   6731   6697   -351    329     80       O  
ATOM   6704  CB  LYS B 230      -5.566  19.991  25.985  1.00 53.02           C  
ANISOU 6704  CB  LYS B 230     6987   6624   6532   -379    331     99       C  
ATOM   6705  CG  LYS B 230      -6.404  19.190  25.018  1.00 65.61           C  
ANISOU 6705  CG  LYS B 230     8617   8218   8093   -393    312    117       C  
ATOM   6706  CD  LYS B 230      -7.597  18.534  25.673  1.00 75.09           C  
ANISOU 6706  CD  LYS B 230     9764   9449   9318   -332    265    131       C  
ATOM   6707  CE  LYS B 230      -7.197  17.336  26.534  1.00 83.70           C  
ANISOU 6707  CE  LYS B 230    10765  10585  10451   -307    304    109       C  
ATOM   6708  NZ  LYS B 230      -8.386  16.483  26.844  1.00 90.43           N  
ANISOU 6708  NZ  LYS B 230    11579  11462  11316   -260    269    121       N  
ATOM   6709  N   GLY B 231      -3.111  22.830  25.933  1.00 52.11           N  
ANISOU 6709  N   GLY B 231     6949   6435   6414   -452    403     59       N  
ATOM   6710  CA  GLY B 231      -2.261  23.619  26.836  1.00 51.76           C  
ANISOU 6710  CA  GLY B 231     6868   6393   6406   -440    424     35       C  
ATOM   6711  C   GLY B 231      -2.983  24.547  27.791  1.00 54.99           C  
ANISOU 6711  C   GLY B 231     7252   6808   6832   -387    369     51       C  
ATOM   6712  O   GLY B 231      -2.618  24.650  28.953  1.00 53.83           O  
ANISOU 6712  O   GLY B 231     7038   6687   6728   -353    375     33       O  
ATOM   6713  N   HIS B 232      -4.009  25.229  27.292  1.00 52.27           N  
ANISOU 6713  N   HIS B 232     6964   6438   6457   -380    316     84       N  
ATOM   6714  CA  HIS B 232      -4.834  26.078  28.134  1.00 52.23           C  
ANISOU 6714  CA  HIS B 232     6936   6435   6473   -331    262    101       C  
ATOM   6715  C   HIS B 232      -5.428  25.292  29.295  1.00 55.02           C  
ANISOU 6715  C   HIS B 232     7204   6833   6867   -274    239     99       C  
ATOM   6716  O   HIS B 232      -5.334  25.723  30.439  1.00 54.68           O  
ANISOU 6716  O   HIS B 232     7108   6807   6860   -240    234     88       O  
ATOM   6717  CB  HIS B 232      -5.976  26.716  27.346  1.00 53.58           C  
ANISOU 6717  CB  HIS B 232     7176   6571   6610   -332    202    138       C  
ATOM   6718  CG  HIS B 232      -6.944  27.446  28.217  1.00 57.15           C  
ANISOU 6718  CG  HIS B 232     7598   7025   7094   -280    145    154       C  
ATOM   6719  ND1 HIS B 232      -8.147  26.900  28.611  1.00 58.98           N  
ANISOU 6719  ND1 HIS B 232     7794   7272   7343   -236     95    171       N  
ATOM   6720  CD2 HIS B 232      -6.857  28.649  28.830  1.00 59.19           C  
ANISOU 6720  CD2 HIS B 232     7849   7269   7372   -265    135    153       C  
ATOM   6721  CE1 HIS B 232      -8.774  27.752  29.404  1.00 58.40           C  
ANISOU 6721  CE1 HIS B 232     7696   7193   7301   -199     57    178       C  
ATOM   6722  NE2 HIS B 232      -8.014  28.823  29.553  1.00 58.87           N  
ANISOU 6722  NE2 HIS B 232     7771   7235   7362   -216     80    168       N  
ATOM   6723  N   GLN B 233      -6.044  24.153  28.983  1.00 50.46           N  
ANISOU 6723  N   GLN B 233     6617   6274   6282   -266    227    109       N  
ATOM   6724  CA  GLN B 233      -6.662  23.282  29.985  1.00 49.40           C  
ANISOU 6724  CA  GLN B 233     6408   6180   6183   -215    209    108       C  
ATOM   6725  C   GLN B 233      -5.591  22.694  30.933  1.00 51.89           C  
ANISOU 6725  C   GLN B 233     6652   6530   6532   -207    258     76       C  
ATOM   6726  O   GLN B 233      -5.788  22.678  32.144  1.00 51.15           O  
ANISOU 6726  O   GLN B 233     6499   6462   6473   -164    244     70       O  
ATOM   6727  CB  GLN B 233      -7.471  22.163  29.291  1.00 50.70           C  
ANISOU 6727  CB  GLN B 233     6582   6352   6328   -214    193    123       C  
ATOM   6728  CG  GLN B 233      -8.706  21.659  30.049  1.00 65.94           C  
ANISOU 6728  CG  GLN B 233     8463   8304   8285   -157    149    133       C  
ATOM   6729  CD  GLN B 233      -9.150  20.241  29.611  1.00 89.29           C  
ANISOU 6729  CD  GLN B 233    11407  11284  11237   -154    155    136       C  
ATOM   6730  OE1 GLN B 233      -8.835  19.792  28.505  1.00 85.09           O  
ANISOU 6730  OE1 GLN B 233    10918  10742  10671   -198    178    138       O  
ATOM   6731  NE2 GLN B 233      -9.872  19.534  30.496  1.00 82.44           N  
ANISOU 6731  NE2 GLN B 233    10479  10445  10402   -105    139    133       N  
ATOM   6732  N   LYS B 234      -4.462  22.231  30.384  1.00 47.40           N  
ANISOU 6732  N   LYS B 234     6092   5960   5957   -251    313     56       N  
ATOM   6733  CA  LYS B 234      -3.367  21.659  31.200  1.00 46.32           C  
ANISOU 6733  CA  LYS B 234     5890   5852   5858   -247    357     24       C  
ATOM   6734  C   LYS B 234      -2.725  22.669  32.165  1.00 49.30           C  
ANISOU 6734  C   LYS B 234     6241   6229   6262   -233    361      7       C  
ATOM   6735  O   LYS B 234      -2.286  22.304  33.262  1.00 48.43           O  
ANISOU 6735  O   LYS B 234     6064   6148   6187   -206    370    -11       O  
ATOM   6736  CB  LYS B 234      -2.265  21.080  30.317  1.00 48.52           C  
ANISOU 6736  CB  LYS B 234     6187   6119   6129   -303    418      3       C  
ATOM   6737  CG  LYS B 234      -2.552  19.728  29.715  1.00 60.48           C  
ANISOU 6737  CG  LYS B 234     7695   7648   7634   -314    432      8       C  
ATOM   6738  CD  LYS B 234      -1.257  19.102  29.189  1.00 69.10           C  
ANISOU 6738  CD  LYS B 234     8783   8735   8739   -366    500    -23       C  
ATOM   6739  CE  LYS B 234      -1.520  17.998  28.187  1.00 79.69           C  
ANISOU 6739  CE  LYS B 234    10143  10076  10058   -396    521    -16       C  
ATOM   6740  NZ  LYS B 234      -2.095  18.541  26.923  1.00 89.90           N  
ANISOU 6740  NZ  LYS B 234    11531  11334  11295   -433    505      5       N  
ATOM   6741  N   ARG B 235      -2.665  23.931  31.739  1.00 45.25           N  
ANISOU 6741  N   ARG B 235     5781   5681   5730   -253    354     12       N  
ATOM   6742  CA  ARG B 235      -2.079  25.014  32.538  1.00 44.38           C  
ANISOU 6742  CA  ARG B 235     5653   5567   5642   -244    360     -5       C  
ATOM   6743  C   ARG B 235      -2.918  25.268  33.793  1.00 46.68           C  
ANISOU 6743  C   ARG B 235     5896   5882   5958   -188    314      5       C  
ATOM   6744  O   ARG B 235      -2.405  25.276  34.903  1.00 46.06           O  
ANISOU 6744  O   ARG B 235     5761   5829   5912   -165    323    -15       O  
ATOM   6745  CB  ARG B 235      -1.986  26.281  31.682  1.00 43.51           C  
ANISOU 6745  CB  ARG B 235     5618   5411   5503   -279    361      2       C  
ATOM   6746  CG  ARG B 235      -1.040  27.370  32.201  1.00 49.66           C  
ANISOU 6746  CG  ARG B 235     6388   6179   6302   -286    388    -24       C  
ATOM   6747  CD  ARG B 235      -1.760  28.687  32.485  1.00 54.71           C  
ANISOU 6747  CD  ARG B 235     7049   6799   6938   -266    348     -5       C  
ATOM   6748  NE  ARG B 235      -2.550  29.152  31.342  1.00 59.20           N  
ANISOU 6748  NE  ARG B 235     7698   7330   7466   -286    320     27       N  
ATOM   6749  CZ  ARG B 235      -3.157  30.333  31.275  1.00 72.71           C  
ANISOU 6749  CZ  ARG B 235     9443   9014   9169   -279    286     47       C  
ATOM   6750  NH1 ARG B 235      -3.065  31.208  32.274  1.00 59.55           N  
ANISOU 6750  NH1 ARG B 235     7738   7354   7534   -254    281     36       N  
ATOM   6751  NH2 ARG B 235      -3.859  30.648  30.190  1.00 59.32           N  
ANISOU 6751  NH2 ARG B 235     7822   7283   7436   -298    257     77       N  
ATOM   6752  N   LYS B 236      -4.214  25.463  33.592  1.00 42.49           N  
ANISOU 6752  N   LYS B 236     5389   5341   5413   -167    266     35       N  
ATOM   6753  CA  LYS B 236      -5.152  25.677  34.686  1.00 41.93           C  
ANISOU 6753  CA  LYS B 236     5278   5288   5367   -116    224     44       C  
ATOM   6754  C   LYS B 236      -5.281  24.442  35.602  1.00 44.95           C  
ANISOU 6754  C   LYS B 236     5593   5712   5773    -82    226     36       C  
ATOM   6755  O   LYS B 236      -5.505  24.575  36.808  1.00 44.10           O  
ANISOU 6755  O   LYS B 236     5438   5624   5692    -47    213     29       O  
ATOM   6756  CB  LYS B 236      -6.529  26.089  34.129  1.00 44.65           C  
ANISOU 6756  CB  LYS B 236     5664   5605   5696   -105    172     76       C  
ATOM   6757  CG  LYS B 236      -6.506  27.441  33.402  1.00 61.25           C  
ANISOU 6757  CG  LYS B 236     7830   7664   7778   -132    161     88       C  
ATOM   6758  CD  LYS B 236      -7.890  27.958  32.991  1.00 71.09           C  
ANISOU 6758  CD  LYS B 236     9112   8880   9018   -116    101    120       C  
ATOM   6759  CE  LYS B 236      -8.809  28.205  34.193  1.00 80.81           C  
ANISOU 6759  CE  LYS B 236    10290  10123  10291    -67     66    121       C  
ATOM   6760  NZ  LYS B 236      -8.148  28.961  35.294  1.00 88.96           N  
ANISOU 6760  NZ  LYS B 236    11282  11167  11351    -58     88     99       N  
ATOM   6761  N   ALA B 237      -5.130  23.251  35.027  1.00 40.76           N  
ANISOU 6761  N   ALA B 237     5060   5194   5232    -95    246     35       N  
ATOM   6762  CA  ALA B 237      -5.213  22.017  35.792  1.00 39.70           C  
ANISOU 6762  CA  ALA B 237     4867   5098   5120    -65    252     28       C  
ATOM   6763  C   ALA B 237      -4.033  21.888  36.776  1.00 42.70           C  
ANISOU 6763  C   ALA B 237     5195   5502   5528    -62    282      0       C  
ATOM   6764  O   ALA B 237      -4.215  21.508  37.936  1.00 41.87           O  
ANISOU 6764  O   ALA B 237     5038   5424   5445    -25    271     -5       O  
ATOM   6765  CB  ALA B 237      -5.289  20.814  34.856  1.00 40.30           C  
ANISOU 6765  CB  ALA B 237     4954   5179   5179    -84    269     34       C  
ATOM   6766  N   LEU B 238      -2.830  22.222  36.323  1.00 38.98           N  
ANISOU 6766  N   LEU B 238     4737   5017   5056   -100    320    -19       N  
ATOM   6767  CA  LEU B 238      -1.661  22.140  37.179  1.00 38.32           C  
ANISOU 6767  CA  LEU B 238     4604   4951   5004    -99    346    -48       C  
ATOM   6768  C   LEU B 238      -1.800  23.130  38.344  1.00 41.07           C  
ANISOU 6768  C   LEU B 238     4932   5307   5368    -70    321    -53       C  
ATOM   6769  O   LEU B 238      -1.477  22.799  39.500  1.00 40.89           O  
ANISOU 6769  O   LEU B 238     4856   5311   5370    -44    318    -66       O  
ATOM   6770  CB  LEU B 238      -0.379  22.403  36.382  1.00 38.68           C  
ANISOU 6770  CB  LEU B 238     4672   4973   5050   -149    393    -72       C  
ATOM   6771  CG  LEU B 238       0.943  22.369  37.170  1.00 43.73           C  
ANISOU 6771  CG  LEU B 238     5262   5626   5729   -152    421   -107       C  
ATOM   6772  CD1 LEU B 238       1.087  21.099  38.031  1.00 43.96           C  
ANISOU 6772  CD1 LEU B 238     5226   5692   5786   -123    418   -112       C  
ATOM   6773  CD2 LEU B 238       2.131  22.502  36.238  1.00 46.05           C  
ANISOU 6773  CD2 LEU B 238     5580   5891   6028   -205    472   -133       C  
ATOM   6774  N   LYS B 239      -2.306  24.325  38.043  1.00 36.02           N  
ANISOU 6774  N   LYS B 239     4334   4640   4713    -75    303    -41       N  
ATOM   6775  CA  LYS B 239      -2.408  25.390  39.048  1.00 34.94           C  
ANISOU 6775  CA  LYS B 239     4180   4505   4592    -54    285    -47       C  
ATOM   6776  C   LYS B 239      -3.486  25.085  40.105  1.00 37.67           C  
ANISOU 6776  C   LYS B 239     4491   4872   4948     -8    248    -35       C  
ATOM   6777  O   LYS B 239      -3.303  25.365  41.286  1.00 36.93           O  
ANISOU 6777  O   LYS B 239     4361   4797   4875     13    243    -48       O  
ATOM   6778  CB  LYS B 239      -2.685  26.735  38.361  1.00 36.86           C  
ANISOU 6778  CB  LYS B 239     4478   4709   4817    -74    276    -37       C  
ATOM   6779  CG  LYS B 239      -2.458  27.958  39.247  1.00 48.25           C  
ANISOU 6779  CG  LYS B 239     5905   6150   6279    -64    272    -50       C  
ATOM   6780  CD  LYS B 239      -2.449  29.265  38.428  1.00 56.51           C  
ANISOU 6780  CD  LYS B 239     7007   7154   7309    -92    275    -43       C  
ATOM   6781  CE  LYS B 239      -3.030  30.460  39.197  1.00 61.45           C  
ANISOU 6781  CE  LYS B 239     7625   7773   7951    -71    251    -39       C  
ATOM   6782  NZ  LYS B 239      -4.453  30.212  39.590  1.00 67.06           N  
ANISOU 6782  NZ  LYS B 239     8325   8487   8667    -37    206    -15       N  
ATOM   6783  N   THR B 240      -4.603  24.515  39.666  1.00 33.85           N  
ANISOU 6783  N   THR B 240     4023   4385   4452      6    225    -11       N  
ATOM   6784  CA  THR B 240      -5.697  24.141  40.560  1.00 33.31           C  
ANISOU 6784  CA  THR B 240     3926   4332   4397     47    195     -2       C  
ATOM   6785  C   THR B 240      -5.230  23.091  41.574  1.00 35.75           C  
ANISOU 6785  C   THR B 240     4181   4679   4722     68    208    -17       C  
ATOM   6786  O   THR B 240      -5.445  23.245  42.777  1.00 34.58           O  
ANISOU 6786  O   THR B 240     4003   4547   4590     95    196    -24       O  
ATOM   6787  CB  THR B 240      -6.871  23.527  39.777  1.00 41.78           C  
ANISOU 6787  CB  THR B 240     5023   5394   5457     56    172     21       C  
ATOM   6788  OG1 THR B 240      -7.267  24.400  38.721  1.00 42.16           O  
ANISOU 6788  OG1 THR B 240     5126   5405   5487     33    156     37       O  
ATOM   6789  CG2 THR B 240      -8.049  23.273  40.687  1.00 40.11           C  
ANISOU 6789  CG2 THR B 240     4784   5191   5264     97    144     26       C  
ATOM   6790  N   THR B 241      -4.586  22.042  41.054  1.00 31.80           N  
ANISOU 6790  N   THR B 241     3673   4192   4218     54    233    -21       N  
ATOM   6791  CA  THR B 241      -4.091  20.949  41.856  1.00 31.40           C  
ANISOU 6791  CA  THR B 241     3573   4173   4183     71    246    -33       C  
ATOM   6792  C   THR B 241      -3.129  21.422  42.961  1.00 33.69           C  
ANISOU 6792  C   THR B 241     3831   4478   4493     76    251    -55       C  
ATOM   6793  O   THR B 241      -3.346  21.124  44.140  1.00 33.27           O  
ANISOU 6793  O   THR B 241     3744   4446   4450    106    237    -58       O  
ATOM   6794  CB  THR B 241      -3.386  19.869  40.973  1.00 44.08           C  
ANISOU 6794  CB  THR B 241     5176   5785   5787     47    277    -36       C  
ATOM   6795  OG1 THR B 241      -2.286  20.456  40.252  1.00 47.22           O  
ANISOU 6795  OG1 THR B 241     5594   6163   6184      5    305    -51       O  
ATOM   6796  CG2 THR B 241      -4.369  19.229  39.987  1.00 43.12           C  
ANISOU 6796  CG2 THR B 241     5082   5656   5647     45    271    -15       C  
ATOM   6797  N   VAL B 242      -2.077  22.146  42.591  1.00 28.98           N  
ANISOU 6797  N   VAL B 242     3243   3867   3899     45    272    -72       N  
ATOM   6798  CA  VAL B 242      -1.119  22.671  43.574  1.00 28.45           C  
ANISOU 6798  CA  VAL B 242     3146   3811   3852     47    276    -96       C  
ATOM   6799  C   VAL B 242      -1.774  23.596  44.633  1.00 32.52           C  
ANISOU 6799  C   VAL B 242     3658   4330   4370     71    249    -94       C  
ATOM   6800  O   VAL B 242      -1.436  23.518  45.834  1.00 32.11           O  
ANISOU 6800  O   VAL B 242     3570   4300   4331     90    241   -107       O  
ATOM   6801  CB  VAL B 242       0.049  23.412  42.874  1.00 32.12           C  
ANISOU 6801  CB  VAL B 242     3628   4255   4323      8    306   -117       C  
ATOM   6802  CG1 VAL B 242       0.879  24.183  43.874  1.00 31.98           C  
ANISOU 6802  CG1 VAL B 242     3582   4244   4326     12    307   -143       C  
ATOM   6803  CG2 VAL B 242       0.934  22.428  42.121  1.00 31.75           C  
ANISOU 6803  CG2 VAL B 242     3571   4206   4286    -17    339   -128       C  
ATOM   6804  N   ILE B 243      -2.682  24.473  44.201  1.00 28.61           N  
ANISOU 6804  N   ILE B 243     3198   3811   3862     69    235    -79       N  
ATOM   6805  CA  ILE B 243      -3.397  25.360  45.134  1.00 28.43           C  
ANISOU 6805  CA  ILE B 243     3170   3786   3845     89    212    -78       C  
ATOM   6806  C   ILE B 243      -4.184  24.538  46.184  1.00 31.58           C  
ANISOU 6806  C   ILE B 243     3541   4208   4249    125    193    -73       C  
ATOM   6807  O   ILE B 243      -4.138  24.811  47.402  1.00 30.15           O  
ANISOU 6807  O   ILE B 243     3336   4041   4077    140    186    -85       O  
ATOM   6808  CB  ILE B 243      -4.374  26.326  44.374  1.00 31.86           C  
ANISOU 6808  CB  ILE B 243     3647   4186   4271     82    196    -60       C  
ATOM   6809  CG1 ILE B 243      -3.594  27.483  43.739  1.00 32.68           C  
ANISOU 6809  CG1 ILE B 243     3778   4267   4372     50    214    -69       C  
ATOM   6810  CG2 ILE B 243      -5.438  26.907  45.313  1.00 32.21           C  
ANISOU 6810  CG2 ILE B 243     3683   4227   4328    107    171    -55       C  
ATOM   6811  CD1 ILE B 243      -4.459  28.683  43.341  1.00 40.50           C  
ANISOU 6811  CD1 ILE B 243     4804   5224   5361     46    196    -54       C  
ATOM   6812  N   LEU B 244      -4.895  23.526  45.689  1.00 28.22           N  
ANISOU 6812  N   LEU B 244     3121   3784   3816    136    188    -56       N  
ATOM   6813  CA  LEU B 244      -5.724  22.674  46.519  1.00 28.02           C  
ANISOU 6813  CA  LEU B 244     3076   3776   3795    168    175    -51       C  
ATOM   6814  C   LEU B 244      -4.894  21.997  47.621  1.00 31.85           C  
ANISOU 6814  C   LEU B 244     3522   4293   4287    180    182    -66       C  
ATOM   6815  O   LEU B 244      -5.147  22.180  48.810  1.00 32.02           O  
ANISOU 6815  O   LEU B 244     3529   4324   4312    198    171    -73       O  
ATOM   6816  CB  LEU B 244      -6.392  21.628  45.627  1.00 28.13           C  
ANISOU 6816  CB  LEU B 244     3100   3787   3801    174    176    -34       C  
ATOM   6817  CG  LEU B 244      -7.522  20.831  46.249  1.00 32.90           C  
ANISOU 6817  CG  LEU B 244     3691   4400   4410    207    164    -27       C  
ATOM   6818  CD1 LEU B 244      -8.688  21.764  46.648  1.00 33.25           C  
ANISOU 6818  CD1 LEU B 244     3749   4420   4465    220    141    -25       C  
ATOM   6819  CD2 LEU B 244      -7.951  19.765  45.259  1.00 34.80           C  
ANISOU 6819  CD2 LEU B 244     3940   4641   4643    209    169    -14       C  
ATOM   6820  N   ILE B 245      -3.888  21.249  47.192  1.00 27.70           N  
ANISOU 6820  N   ILE B 245     2983   3780   3763    167    200    -71       N  
ATOM   6821  CA  ILE B 245      -2.986  20.501  48.062  1.00 27.00           C  
ANISOU 6821  CA  ILE B 245     2857   3717   3683    176    204    -84       C  
ATOM   6822  C   ILE B 245      -2.184  21.389  49.007  1.00 29.98           C  
ANISOU 6822  C   ILE B 245     3221   4101   4070    172    198   -104       C  
ATOM   6823  O   ILE B 245      -2.191  21.162  50.184  1.00 28.78           O  
ANISOU 6823  O   ILE B 245     3049   3966   3919    191    185   -110       O  
ATOM   6824  CB  ILE B 245      -2.025  19.628  47.211  1.00 29.92           C  
ANISOU 6824  CB  ILE B 245     3215   4091   4062    157    227    -88       C  
ATOM   6825  CG1 ILE B 245      -2.832  18.500  46.569  1.00 29.85           C  
ANISOU 6825  CG1 ILE B 245     3211   4085   4045    167    232    -69       C  
ATOM   6826  CG2 ILE B 245      -0.834  19.077  48.065  1.00 30.26           C  
ANISOU 6826  CG2 ILE B 245     3217   4155   4124    161    228   -105       C  
ATOM   6827  CD1 ILE B 245      -2.166  17.903  45.316  1.00 37.90           C  
ANISOU 6827  CD1 ILE B 245     4234   5098   5069    138    260    -70       C  
ATOM   6828  N   LEU B 246      -1.498  22.406  48.520  1.00 27.00           N  
ANISOU 6828  N   LEU B 246     2853   3707   3697    146    209   -117       N  
ATOM   6829  CA  LEU B 246      -0.839  23.325  49.461  1.00 26.66           C  
ANISOU 6829  CA  LEU B 246     2797   3670   3663    144    203   -138       C  
ATOM   6830  C   LEU B 246      -1.776  23.867  50.558  1.00 30.98           C  
ANISOU 6830  C   LEU B 246     3347   4222   4204    164    183   -135       C  
ATOM   6831  O   LEU B 246      -1.440  23.848  51.755  1.00 30.76           O  
ANISOU 6831  O   LEU B 246     3298   4213   4178    175    171   -147       O  
ATOM   6832  CB  LEU B 246      -0.212  24.492  48.717  1.00 26.63           C  
ANISOU 6832  CB  LEU B 246     2811   3644   3665    114    221   -151       C  
ATOM   6833  CG  LEU B 246       1.192  24.226  48.200  1.00 31.02           C  
ANISOU 6833  CG  LEU B 246     3351   4198   4238     91    244   -172       C  
ATOM   6834  CD1 LEU B 246       1.663  25.486  47.514  1.00 31.51           C  
ANISOU 6834  CD1 LEU B 246     3436   4234   4302     62    264   -186       C  
ATOM   6835  CD2 LEU B 246       2.132  23.858  49.341  1.00 32.92           C  
ANISOU 6835  CD2 LEU B 246     3549   4463   4497    102    234   -193       C  
ATOM   6836  N   ALA B 247      -2.955  24.327  50.145  1.00 27.21           N  
ANISOU 6836  N   ALA B 247     2896   3725   3719    167    178   -119       N  
ATOM   6837  CA  ALA B 247      -3.939  24.858  51.080  1.00 26.88           C  
ANISOU 6837  CA  ALA B 247     2858   3679   3677    182    163   -118       C  
ATOM   6838  C   ALA B 247      -4.448  23.768  52.021  1.00 31.16           C  
ANISOU 6838  C   ALA B 247     3385   4240   4213    209    153   -114       C  
ATOM   6839  O   ALA B 247      -4.781  24.033  53.189  1.00 31.51           O  
ANISOU 6839  O   ALA B 247     3424   4291   4257    218    145   -122       O  
ATOM   6840  CB  ALA B 247      -5.092  25.515  50.341  1.00 27.50           C  
ANISOU 6840  CB  ALA B 247     2965   3727   3757    179    158   -103       C  
ATOM   6841  N   PHE B 248      -4.513  22.542  51.517  1.00 26.63           N  
ANISOU 6841  N   PHE B 248     2808   3675   3636    218    157   -102       N  
ATOM   6842  CA  PHE B 248      -4.923  21.418  52.353  1.00 25.42           C  
ANISOU 6842  CA  PHE B 248     2641   3539   3477    244    151    -98       C  
ATOM   6843  C   PHE B 248      -3.920  21.302  53.494  1.00 28.55           C  
ANISOU 6843  C   PHE B 248     3016   3960   3872    246    144   -113       C  
ATOM   6844  O   PHE B 248      -4.277  21.363  54.663  1.00 28.15           O  
ANISOU 6844  O   PHE B 248     2966   3916   3815    257    134   -118       O  
ATOM   6845  CB  PHE B 248      -4.993  20.115  51.552  1.00 26.33           C  
ANISOU 6845  CB  PHE B 248     2752   3662   3591    251    160    -84       C  
ATOM   6846  CG  PHE B 248      -5.386  18.918  52.375  1.00 27.09           C  
ANISOU 6846  CG  PHE B 248     2836   3776   3683    278    157    -79       C  
ATOM   6847  CD1 PHE B 248      -4.433  18.156  53.001  1.00 29.26           C  
ANISOU 6847  CD1 PHE B 248     3087   4074   3958    283    155    -84       C  
ATOM   6848  CD2 PHE B 248      -6.708  18.556  52.519  1.00 28.35           C  
ANISOU 6848  CD2 PHE B 248     3006   3924   3839    298    156    -71       C  
ATOM   6849  CE1 PHE B 248      -4.776  17.058  53.751  1.00 29.33           C  
ANISOU 6849  CE1 PHE B 248     3087   4097   3961    307    152    -79       C  
ATOM   6850  CE2 PHE B 248      -7.047  17.452  53.269  1.00 30.39           C  
ANISOU 6850  CE2 PHE B 248     3256   4197   4093    321    158    -69       C  
ATOM   6851  CZ  PHE B 248      -6.075  16.711  53.881  1.00 28.15           C  
ANISOU 6851  CZ  PHE B 248     2952   3937   3805    326    156    -71       C  
ATOM   6852  N   PHE B 249      -2.654  21.181  53.148  1.00 24.69           N  
ANISOU 6852  N   PHE B 249     2510   3480   3392    232    149   -122       N  
ATOM   6853  CA  PHE B 249      -1.632  21.058  54.170  1.00 24.51           C  
ANISOU 6853  CA  PHE B 249     2464   3477   3372    233    137   -137       C  
ATOM   6854  C   PHE B 249      -1.500  22.290  55.043  1.00 27.68           C  
ANISOU 6854  C   PHE B 249     2868   3877   3770    225    128   -154       C  
ATOM   6855  O   PHE B 249      -1.271  22.155  56.249  1.00 27.23           O  
ANISOU 6855  O   PHE B 249     2804   3836   3706    235    112   -162       O  
ATOM   6856  CB  PHE B 249      -0.323  20.583  53.552  1.00 26.62           C  
ANISOU 6856  CB  PHE B 249     2707   3749   3657    220    145   -145       C  
ATOM   6857  CG  PHE B 249      -0.412  19.156  53.093  1.00 28.58           C  
ANISOU 6857  CG  PHE B 249     2946   4006   3909    232    151   -130       C  
ATOM   6858  CD1 PHE B 249      -0.417  18.120  54.023  1.00 31.47           C  
ANISOU 6858  CD1 PHE B 249     3295   4390   4270    255    136   -125       C  
ATOM   6859  CD2 PHE B 249      -0.597  18.843  51.757  1.00 30.76           C  
ANISOU 6859  CD2 PHE B 249     3230   4268   4189    219    173   -121       C  
ATOM   6860  CE1 PHE B 249      -0.525  16.799  53.607  1.00 32.08           C  
ANISOU 6860  CE1 PHE B 249     3361   4474   4353    266    145   -111       C  
ATOM   6861  CE2 PHE B 249      -0.736  17.528  51.350  1.00 33.45           C  
ANISOU 6861  CE2 PHE B 249     3560   4617   4533    229    181   -108       C  
ATOM   6862  CZ  PHE B 249      -0.694  16.505  52.287  1.00 31.28           C  
ANISOU 6862  CZ  PHE B 249     3265   4362   4259    253    168   -103       C  
ATOM   6863  N   ALA B 250      -1.701  23.470  54.451  1.00 23.72           N  
ANISOU 6863  N   ALA B 250     2382   3356   3274    208    139   -158       N  
ATOM   6864  CA  ALA B 250      -1.738  24.738  55.198  1.00 23.24           C  
ANISOU 6864  CA  ALA B 250     2326   3291   3214    199    135   -174       C  
ATOM   6865  C   ALA B 250      -2.833  24.798  56.316  1.00 26.91           C  
ANISOU 6865  C   ALA B 250     2802   3757   3667    213    126   -171       C  
ATOM   6866  O   ALA B 250      -2.560  25.218  57.461  1.00 26.12           O  
ANISOU 6866  O   ALA B 250     2695   3668   3560    211    117   -186       O  
ATOM   6867  CB  ALA B 250      -1.890  25.883  54.235  1.00 23.81           C  
ANISOU 6867  CB  ALA B 250     2413   3338   3294    179    150   -174       C  
ATOM   6868  N   CYS B 251      -4.048  24.352  55.997  1.00 24.10           N  
ANISOU 6868  N   CYS B 251     2461   3388   3308    226    128   -154       N  
ATOM   6869  CA  CYS B 251      -5.099  24.167  57.017  1.00 23.95           C  
ANISOU 6869  CA  CYS B 251     2452   3365   3281    240    124   -154       C  
ATOM   6870  C   CYS B 251      -4.643  23.238  58.141  1.00 26.41           C  
ANISOU 6870  C   CYS B 251     2756   3702   3575    252    113   -157       C  
ATOM   6871  O   CYS B 251      -4.845  23.511  59.337  1.00 25.68           O  
ANISOU 6871  O   CYS B 251     2671   3614   3473    252    108   -169       O  
ATOM   6872  CB  CYS B 251      -6.379  23.597  56.410  1.00 24.63           C  
ANISOU 6872  CB  CYS B 251     2553   3433   3372    254    130   -137       C  
ATOM   6873  SG  CYS B 251      -7.210  24.688  55.234  1.00 29.24           S  
ANISOU 6873  SG  CYS B 251     3153   3982   3976    242    135   -130       S  
ATOM   6874  N   TRP B 252      -4.023  22.134  57.767  1.00 22.15           N  
ANISOU 6874  N   TRP B 252     2204   3179   3034    262    109   -148       N  
ATOM   6875  CA  TRP B 252      -3.674  21.129  58.771  1.00 21.80           C  
ANISOU 6875  CA  TRP B 252     2154   3156   2975    277     95   -148       C  
ATOM   6876  C   TRP B 252      -2.431  21.478  59.554  1.00 25.38           C  
ANISOU 6876  C   TRP B 252     2591   3626   3425    268     77   -164       C  
ATOM   6877  O   TRP B 252      -2.285  21.016  60.659  1.00 26.24           O  
ANISOU 6877  O   TRP B 252     2704   3748   3517    276     61   -166       O  
ATOM   6878  CB  TRP B 252      -3.544  19.737  58.152  1.00 20.57           C  
ANISOU 6878  CB  TRP B 252     1986   3008   2822    293     97   -131       C  
ATOM   6879  CG  TRP B 252      -4.863  19.106  57.940  1.00 21.54           C  
ANISOU 6879  CG  TRP B 252     2124   3118   2940    310    110   -118       C  
ATOM   6880  CD1 TRP B 252      -5.553  19.008  56.771  1.00 24.19           C  
ANISOU 6880  CD1 TRP B 252     2466   3440   3288    311    124   -107       C  
ATOM   6881  CD2 TRP B 252      -5.684  18.513  58.944  1.00 21.45           C  
ANISOU 6881  CD2 TRP B 252     2129   3108   2914    327    110   -116       C  
ATOM   6882  NE1 TRP B 252      -6.751  18.368  56.981  1.00 23.58           N  
ANISOU 6882  NE1 TRP B 252     2401   3353   3206    330    132   -100       N  
ATOM   6883  CE2 TRP B 252      -6.856  18.055  58.308  1.00 25.10           C  
ANISOU 6883  CE2 TRP B 252     2601   3554   3383    340    126   -107       C  
ATOM   6884  CE3 TRP B 252      -5.541  18.326  60.318  1.00 22.97           C  
ANISOU 6884  CE3 TRP B 252     2331   3310   3085    332     98   -123       C  
ATOM   6885  CZ2 TRP B 252      -7.870  17.423  58.989  1.00 24.40           C  
ANISOU 6885  CZ2 TRP B 252     2528   3458   3286    358    135   -107       C  
ATOM   6886  CZ3 TRP B 252      -6.562  17.701  61.007  1.00 24.50           C  
ANISOU 6886  CZ3 TRP B 252     2547   3497   3267    347    107   -121       C  
ATOM   6887  CH2 TRP B 252      -7.715  17.259  60.342  1.00 24.96           C  
ANISOU 6887  CH2 TRP B 252     2611   3537   3337    360    128   -114       C  
ATOM   6888  N   LEU B 253      -1.575  22.342  59.031  1.00 20.79           N  
ANISOU 6888  N   LEU B 253     1997   3043   2860    249     80   -176       N  
ATOM   6889  CA  LEU B 253      -0.243  22.526  59.615  1.00 20.78           C  
ANISOU 6889  CA  LEU B 253     1975   3059   2864    242     62   -194       C  
ATOM   6890  C   LEU B 253      -0.220  22.893  61.118  1.00 25.47           C  
ANISOU 6890  C   LEU B 253     2577   3663   3436    241     42   -207       C  
ATOM   6891  O   LEU B 253       0.511  22.248  61.872  1.00 25.51           O  
ANISOU 6891  O   LEU B 253     2572   3685   3434    248     17   -209       O  
ATOM   6892  CB  LEU B 253       0.604  23.482  58.746  1.00 20.62           C  
ANISOU 6892  CB  LEU B 253     1939   3029   2866    220     74   -210       C  
ATOM   6893  CG  LEU B 253       2.011  23.859  59.210  1.00 24.68           C  
ANISOU 6893  CG  LEU B 253     2428   3554   3394    210     60   -235       C  
ATOM   6894  CD1 LEU B 253       2.830  22.602  59.540  1.00 24.94           C  
ANISOU 6894  CD1 LEU B 253     2440   3603   3434    224     36   -232       C  
ATOM   6895  CD2 LEU B 253       2.701  24.772  58.152  1.00 25.35           C  
ANISOU 6895  CD2 LEU B 253     2503   3624   3504    188     82   -251       C  
ATOM   6896  N   PRO B 254      -1.030  23.880  61.567  1.00 22.31           N  
ANISOU 6896  N   PRO B 254     2196   3252   3028    231     53   -214       N  
ATOM   6897  CA  PRO B 254      -1.062  24.188  63.013  1.00 22.11           C  
ANISOU 6897  CA  PRO B 254     2184   3237   2980    226     38   -227       C  
ATOM   6898  C   PRO B 254      -1.539  23.032  63.901  1.00 26.11           C  
ANISOU 6898  C   PRO B 254     2709   3750   3459    243     25   -214       C  
ATOM   6899  O   PRO B 254      -1.210  22.989  65.078  1.00 25.31           O  
ANISOU 6899  O   PRO B 254     2618   3661   3336    240      5   -222       O  
ATOM   6900  CB  PRO B 254      -2.032  25.389  63.125  1.00 23.58           C  
ANISOU 6900  CB  PRO B 254     2387   3404   3169    210     61   -235       C  
ATOM   6901  CG  PRO B 254      -2.128  25.968  61.771  1.00 28.10           C  
ANISOU 6901  CG  PRO B 254     2950   3959   3768    204     80   -231       C  
ATOM   6902  CD  PRO B 254      -1.791  24.872  60.773  1.00 24.11           C  
ANISOU 6902  CD  PRO B 254     2433   3457   3269    219     78   -214       C  
ATOM   6903  N   TYR B 255      -2.301  22.091  63.356  1.00 23.01           N  
ANISOU 6903  N   TYR B 255     2324   3350   3067    261     36   -194       N  
ATOM   6904  CA  TYR B 255      -2.709  20.950  64.162  1.00 23.40           C  
ANISOU 6904  CA  TYR B 255     2393   3406   3093    278     27   -183       C  
ATOM   6905  C   TYR B 255      -1.501  20.036  64.333  1.00 28.59           C  
ANISOU 6905  C   TYR B 255     3030   4084   3750    289     -3   -177       C  
ATOM   6906  O   TYR B 255      -1.196  19.564  65.444  1.00 28.45           O  
ANISOU 6906  O   TYR B 255     3024   4077   3707    293    -28   -177       O  
ATOM   6907  CB  TYR B 255      -3.889  20.240  63.506  1.00 24.36           C  
ANISOU 6907  CB  TYR B 255     2525   3512   3220    294     50   -167       C  
ATOM   6908  CG  TYR B 255      -4.256  18.908  64.097  1.00 25.38           C  
ANISOU 6908  CG  TYR B 255     2669   3645   3328    315     46   -154       C  
ATOM   6909  CD1 TYR B 255      -3.943  17.737  63.432  1.00 27.16           C  
ANISOU 6909  CD1 TYR B 255     2877   3881   3563    334     43   -136       C  
ATOM   6910  CD2 TYR B 255      -4.919  18.815  65.316  1.00 25.92           C  
ANISOU 6910  CD2 TYR B 255     2771   3708   3369    314     48   -159       C  
ATOM   6911  CE1 TYR B 255      -4.277  16.497  63.967  1.00 27.72           C  
ANISOU 6911  CE1 TYR B 255     2961   3956   3617    354     42   -124       C  
ATOM   6912  CE2 TYR B 255      -5.256  17.573  65.863  1.00 26.58           C  
ANISOU 6912  CE2 TYR B 255     2873   3794   3433    333     46   -147       C  
ATOM   6913  CZ  TYR B 255      -4.924  16.423  65.171  1.00 34.28           C  
ANISOU 6913  CZ  TYR B 255     3827   4779   4418    354     43   -129       C  
ATOM   6914  OH  TYR B 255      -5.240  15.184  65.665  1.00 35.89           O  
ANISOU 6914  OH  TYR B 255     4048   4985   4604    374     44   -117       O  
ATOM   6915  N   TYR B 256      -0.787  19.835  63.227  1.00 25.36           N  
ANISOU 6915  N   TYR B 256     2590   3677   3369    290     -1   -174       N  
ATOM   6916  CA  TYR B 256       0.421  19.029  63.217  1.00 25.47           C  
ANISOU 6916  CA  TYR B 256     2576   3705   3394    298    -26   -171       C  
ATOM   6917  C   TYR B 256       1.433  19.511  64.254  1.00 28.60           C  
ANISOU 6917  C   TYR B 256     2967   4114   3784    288    -60   -189       C  
ATOM   6918  O   TYR B 256       2.051  18.696  64.917  1.00 28.74           O  
ANISOU 6918  O   TYR B 256     2979   4143   3796    299    -92   -184       O  
ATOM   6919  CB  TYR B 256       1.082  19.054  61.837  1.00 27.16           C  
ANISOU 6919  CB  TYR B 256     2759   3914   3645    291    -12   -173       C  
ATOM   6920  CG  TYR B 256       0.261  18.517  60.666  1.00 29.29           C  
ANISOU 6920  CG  TYR B 256     3031   4173   3923    298     18   -156       C  
ATOM   6921  CD1 TYR B 256       0.609  18.869  59.356  1.00 31.71           C  
ANISOU 6921  CD1 TYR B 256     3322   4469   4256    284     39   -159       C  
ATOM   6922  CD2 TYR B 256      -0.829  17.645  60.846  1.00 29.26           C  
ANISOU 6922  CD2 TYR B 256     3048   4168   3902    317     27   -137       C  
ATOM   6923  CE1 TYR B 256      -0.094  18.397  58.269  1.00 32.60           C  
ANISOU 6923  CE1 TYR B 256     3439   4572   4374    288     63   -144       C  
ATOM   6924  CE2 TYR B 256      -1.535  17.148  59.742  1.00 29.52           C  
ANISOU 6924  CE2 TYR B 256     3080   4191   3945    323     53   -124       C  
ATOM   6925  CZ  TYR B 256      -1.163  17.537  58.463  1.00 38.13           C  
ANISOU 6925  CZ  TYR B 256     4156   5273   5058    308     69   -126       C  
ATOM   6926  OH  TYR B 256      -1.837  17.064  57.353  1.00 39.00           O  
ANISOU 6926  OH  TYR B 256     4270   5374   5176    312     92   -113       O  
ATOM   6927  N   ILE B 257       1.607  20.829  64.375  1.00 23.82           N  
ANISOU 6927  N   ILE B 257     2362   3507   3182    268    -55   -210       N  
ATOM   6928  CA  ILE B 257       2.544  21.419  65.323  1.00 22.77           C  
ANISOU 6928  CA  ILE B 257     2222   3385   3044    257    -85   -231       C  
ATOM   6929  C   ILE B 257       2.091  21.141  66.772  1.00 27.02           C  
ANISOU 6929  C   ILE B 257     2796   3931   3540    260   -106   -227       C  
ATOM   6930  O   ILE B 257       2.905  20.844  67.664  1.00 26.64           O  
ANISOU 6930  O   ILE B 257     2747   3896   3481    262   -146   -232       O  
ATOM   6931  CB  ILE B 257       2.687  22.928  65.043  1.00 25.27           C  
ANISOU 6931  CB  ILE B 257     2532   3696   3375    234    -65   -254       C  
ATOM   6932  CG1 ILE B 257       3.312  23.140  63.666  1.00 24.51           C  
ANISOU 6932  CG1 ILE B 257     2404   3590   3317    229    -46   -260       C  
ATOM   6933  CG2 ILE B 257       3.562  23.674  66.114  1.00 26.21           C  
ANISOU 6933  CG2 ILE B 257     2645   3827   3486    221    -93   -280       C  
ATOM   6934  CD1 ILE B 257       3.174  24.533  63.176  1.00 24.82           C  
ANISOU 6934  CD1 ILE B 257     2444   3618   3369    209    -18   -277       C  
ATOM   6935  N   GLY B 258       0.782  21.215  66.992  1.00 24.16           N  
ANISOU 6935  N   GLY B 258     2469   3558   3155    260    -81   -219       N  
ATOM   6936  CA  GLY B 258       0.181  20.953  68.294  1.00 24.22           C  
ANISOU 6936  CA  GLY B 258     2517   3566   3120    259    -91   -216       C  
ATOM   6937  C   GLY B 258       0.438  19.534  68.745  1.00 28.70           C  
ANISOU 6937  C   GLY B 258     3092   4141   3671    280   -119   -197       C  
ATOM   6938  O   GLY B 258       0.873  19.305  69.875  1.00 28.30           O  
ANISOU 6938  O   GLY B 258     3061   4100   3591    278   -153   -198       O  
ATOM   6939  N   ILE B 259       0.145  18.592  67.844  1.00 25.35           N  
ANISOU 6939  N   ILE B 259     2654   3713   3264    300   -104   -178       N  
ATOM   6940  CA  ILE B 259       0.294  17.145  68.073  1.00 24.96           C  
ANISOU 6940  CA  ILE B 259     2609   3669   3206    323   -123   -156       C  
ATOM   6941  C   ILE B 259       1.757  16.765  68.312  1.00 27.23           C  
ANISOU 6941  C   ILE B 259     2867   3971   3509    327   -170   -157       C  
ATOM   6942  O   ILE B 259       2.063  15.893  69.150  1.00 26.14           O  
ANISOU 6942  O   ILE B 259     2744   3839   3350    339   -204   -145       O  
ATOM   6943  CB  ILE B 259      -0.267  16.360  66.851  1.00 27.98           C  
ANISOU 6943  CB  ILE B 259     2974   4044   3613    340    -91   -139       C  
ATOM   6944  CG1 ILE B 259      -1.808  16.359  66.893  1.00 28.31           C  
ANISOU 6944  CG1 ILE B 259     3050   4069   3636    343    -53   -135       C  
ATOM   6945  CG2 ILE B 259       0.273  14.924  66.790  1.00 28.93           C  
ANISOU 6945  CG2 ILE B 259     3078   4173   3742    362   -112   -120       C  
ATOM   6946  CD1 ILE B 259      -2.389  15.643  68.091  1.00 35.69           C  
ANISOU 6946  CD1 ILE B 259     4028   5001   4531    351    -59   -128       C  
ATOM   6947  N   SER B 260       2.638  17.435  67.560  1.00 22.72           N  
ANISOU 6947  N   SER B 260     2256   3403   2976    317   -172   -173       N  
ATOM   6948  CA  SER B 260       4.083  17.299  67.710  1.00 22.29           C  
ANISOU 6948  CA  SER B 260     2166   3357   2947    318   -214   -183       C  
ATOM   6949  C   SER B 260       4.538  17.681  69.112  1.00 24.99           C  
ANISOU 6949  C   SER B 260     2531   3708   3257    309   -258   -194       C  
ATOM   6950  O   SER B 260       5.420  17.043  69.674  1.00 24.32           O  
ANISOU 6950  O   SER B 260     2435   3629   3176    319   -305   -190       O  
ATOM   6951  CB  SER B 260       4.818  18.176  66.678  1.00 25.01           C  
ANISOU 6951  CB  SER B 260     2470   3698   3337    303   -198   -205       C  
ATOM   6952  OG  SER B 260       4.819  17.524  65.429  1.00 33.73           O  
ANISOU 6952  OG  SER B 260     3547   4794   4474    311   -172   -194       O  
ATOM   6953  N   ILE B 261       3.952  18.743  69.651  1.00 21.41           N  
ANISOU 6953  N   ILE B 261     2106   3253   2775    290   -242   -208       N  
ATOM   6954  CA  ILE B 261       4.345  19.247  70.962  1.00 21.53           C  
ANISOU 6954  CA  ILE B 261     2145   3277   2758    277   -279   -222       C  
ATOM   6955  C   ILE B 261       3.889  18.286  72.039  1.00 26.49           C  
ANISOU 6955  C   ILE B 261     2821   3906   3339    287   -303   -201       C  
ATOM   6956  O   ILE B 261       4.663  17.931  72.901  1.00 26.96           O  
ANISOU 6956  O   ILE B 261     2887   3973   3383    290   -355   -200       O  
ATOM   6957  CB  ILE B 261       3.837  20.667  71.207  1.00 24.14           C  
ANISOU 6957  CB  ILE B 261     2492   3605   3074    251   -250   -244       C  
ATOM   6958  CG1 ILE B 261       4.557  21.618  70.261  1.00 24.04           C  
ANISOU 6958  CG1 ILE B 261     2433   3593   3109    241   -235   -266       C  
ATOM   6959  CG2 ILE B 261       4.137  21.065  72.607  1.00 25.63           C  
ANISOU 6959  CG2 ILE B 261     2711   3803   3224    235   -285   -257       C  
ATOM   6960  CD1 ILE B 261       3.734  22.765  69.730  1.00 26.95           C  
ANISOU 6960  CD1 ILE B 261     2806   3951   3484    223   -185   -278       C  
ATOM   6961  N   ASP B 262       2.657  17.815  71.939  1.00 23.84           N  
ANISOU 6961  N   ASP B 262     2517   3560   2982    294   -266   -185       N  
ATOM   6962  CA  ASP B 262       2.149  16.712  72.774  1.00 24.85           C  
ANISOU 6962  CA  ASP B 262     2690   3685   3069    307   -279   -163       C  
ATOM   6963  C   ASP B 262       3.006  15.443  72.713  1.00 28.98           C  
ANISOU 6963  C   ASP B 262     3191   4214   3607    331   -321   -143       C  
ATOM   6964  O   ASP B 262       3.396  14.914  73.745  1.00 29.43           O  
ANISOU 6964  O   ASP B 262     3276   4274   3633    335   -367   -134       O  
ATOM   6965  CB  ASP B 262       0.708  16.354  72.365  1.00 27.01           C  
ANISOU 6965  CB  ASP B 262     2988   3942   3333    313   -224   -152       C  
ATOM   6966  CG  ASP B 262      -0.187  16.081  73.550  1.00 41.79           C  
ANISOU 6966  CG  ASP B 262     4926   5804   5151    306   -217   -149       C  
ATOM   6967  OD1 ASP B 262      -1.160  15.304  73.377  1.00 44.35           O  
ANISOU 6967  OD1 ASP B 262     5270   6114   5466    320   -184   -136       O  
ATOM   6968  OD2 ASP B 262       0.065  16.661  74.634  1.00 46.02           O  
ANISOU 6968  OD2 ASP B 262     5492   6342   5650    285   -240   -162       O  
ATOM   6969  N   SER B 263       3.286  14.946  71.518  1.00 25.20           N  
ANISOU 6969  N   SER B 263     2665   3735   3177    347   -307   -135       N  
ATOM   6970  CA  SER B 263       4.334  13.922  71.347  1.00 25.07           C  
ANISOU 6970  CA  SER B 263     2612   3722   3191    366   -348   -122       C  
ATOM   6971  C   SER B 263       5.625  14.215  72.135  1.00 29.60           C  
ANISOU 6971  C   SER B 263     3174   4303   3770    360   -413   -135       C  
ATOM   6972  O   SER B 263       6.172  13.307  72.771  1.00 30.26           O  
ANISOU 6972  O   SER B 263     3262   4387   3847    374   -462   -119       O  
ATOM   6973  CB  SER B 263       4.685  13.737  69.879  1.00 27.93           C  
ANISOU 6973  CB  SER B 263     2917   4082   3614    373   -321   -124       C  
ATOM   6974  OG  SER B 263       3.516  13.371  69.171  1.00 37.96           O  
ANISOU 6974  OG  SER B 263     4198   5345   4878    380   -268   -110       O  
ATOM   6975  N   PHE B 264       6.107  15.458  72.099  1.00 24.76           N  
ANISOU 6975  N   PHE B 264     2544   3694   3168    339   -414   -163       N  
ATOM   6976  CA  PHE B 264       7.317  15.813  72.849  1.00 24.74           C  
ANISOU 6976  CA  PHE B 264     2528   3698   3173    332   -475   -180       C  
ATOM   6977  C   PHE B 264       7.120  15.637  74.364  1.00 29.06           C  
ANISOU 6977  C   PHE B 264     3136   4250   3656    328   -517   -171       C  
ATOM   6978  O   PHE B 264       8.030  15.277  75.085  1.00 29.23           O  
ANISOU 6978  O   PHE B 264     3156   4274   3676    333   -581   -170       O  
ATOM   6979  CB  PHE B 264       7.760  17.256  72.551  1.00 26.15           C  
ANISOU 6979  CB  PHE B 264     2681   3881   3374    310   -461   -215       C  
ATOM   6980  CG  PHE B 264       8.243  17.482  71.138  1.00 26.83           C  
ANISOU 6980  CG  PHE B 264     2709   3961   3525    311   -430   -228       C  
ATOM   6981  CD1 PHE B 264       8.471  18.766  70.691  1.00 29.52           C  
ANISOU 6981  CD1 PHE B 264     3029   4302   3886    291   -403   -258       C  
ATOM   6982  CD2 PHE B 264       8.469  16.426  70.263  1.00 28.23           C  
ANISOU 6982  CD2 PHE B 264     2853   4131   3742    329   -423   -212       C  
ATOM   6983  CE1 PHE B 264       8.926  19.010  69.409  1.00 30.13           C  
ANISOU 6983  CE1 PHE B 264     3059   4370   4019    289   -372   -271       C  
ATOM   6984  CE2 PHE B 264       8.908  16.657  68.966  1.00 30.61           C  
ANISOU 6984  CE2 PHE B 264     3105   4424   4100    325   -390   -226       C  
ATOM   6985  CZ  PHE B 264       9.143  17.955  68.540  1.00 28.65           C  
ANISOU 6985  CZ  PHE B 264     2843   4175   3869    304   -365   -256       C  
ATOM   6986  N   ILE B 265       5.918  15.903  74.843  1.00 25.53           N  
ANISOU 6986  N   ILE B 265     2745   3800   3156    317   -481   -166       N  
ATOM   6987  CA  ILE B 265       5.615  15.710  76.248  1.00 25.20           C  
ANISOU 6987  CA  ILE B 265     2769   3757   3048    308   -512   -158       C  
ATOM   6988  C   ILE B 265       5.734  14.236  76.576  1.00 28.59           C  
ANISOU 6988  C   ILE B 265     3214   4181   3466    333   -547   -126       C  
ATOM   6989  O   ILE B 265       6.505  13.862  77.447  1.00 29.20           O  
ANISOU 6989  O   ILE B 265     3307   4262   3527    336   -612   -120       O  
ATOM   6990  CB  ILE B 265       4.214  16.287  76.611  1.00 27.64           C  
ANISOU 6990  CB  ILE B 265     3133   4059   3311    288   -455   -164       C  
ATOM   6991  CG1 ILE B 265       4.277  17.839  76.549  1.00 27.97           C  
ANISOU 6991  CG1 ILE B 265     3161   4106   3362    259   -433   -197       C  
ATOM   6992  CG2 ILE B 265       3.787  15.806  77.955  1.00 27.72           C  
ANISOU 6992  CG2 ILE B 265     3218   4063   3253    280   -477   -152       C  
ATOM   6993  CD1 ILE B 265       2.913  18.573  76.447  1.00 31.87           C  
ANISOU 6993  CD1 ILE B 265     3684   4588   3837    239   -364   -207       C  
ATOM   6994  N   LEU B 266       4.991  13.404  75.855  1.00 23.99           N  
ANISOU 6994  N   LEU B 266     2628   3592   2896    352   -505   -107       N  
ATOM   6995  CA  LEU B 266       4.945  11.962  76.118  1.00 23.29           C  
ANISOU 6995  CA  LEU B 266     2556   3497   2796    377   -527    -75       C  
ATOM   6996  C   LEU B 266       6.312  11.256  76.042  1.00 28.03           C  
ANISOU 6996  C   LEU B 266     3110   4100   3440    395   -592    -66       C  
ATOM   6997  O   LEU B 266       6.678  10.489  76.946  1.00 28.47           O  
ANISOU 6997  O   LEU B 266     3196   4153   3470    405   -647    -47       O  
ATOM   6998  CB  LEU B 266       3.959  11.293  75.163  1.00 22.42           C  
ANISOU 6998  CB  LEU B 266     2437   3380   2703    393   -463    -61       C  
ATOM   6999  CG  LEU B 266       2.466  11.612  75.370  1.00 26.74           C  
ANISOU 6999  CG  LEU B 266     3037   3916   3206    382   -402    -65       C  
ATOM   7000  CD1 LEU B 266       1.628  10.726  74.430  1.00 26.00           C  
ANISOU 7000  CD1 LEU B 266     2929   3814   3134    404   -350    -49       C  
ATOM   7001  CD2 LEU B 266       2.034  11.437  76.854  1.00 29.09           C  
ANISOU 7001  CD2 LEU B 266     3416   4206   3432    370   -421    -59       C  
ATOM   7002  N   LEU B 267       7.053  11.537  74.975  1.00 23.75           N  
ANISOU 7002  N   LEU B 267     2496   3562   2967    398   -587    -81       N  
ATOM   7003  CA  LEU B 267       8.382  10.981  74.744  1.00 23.06           C  
ANISOU 7003  CA  LEU B 267     2353   3473   2937    412   -641    -80       C  
ATOM   7004  C   LEU B 267       9.491  11.639  75.583  1.00 27.01           C  
ANISOU 7004  C   LEU B 267     2849   3977   3438    400   -711   -100       C  
ATOM   7005  O   LEU B 267      10.683  11.353  75.376  1.00 26.42           O  
ANISOU 7005  O   LEU B 267     2720   3897   3421    409   -758   -107       O  
ATOM   7006  CB  LEU B 267       8.735  11.145  73.266  1.00 22.33           C  
ANISOU 7006  CB  LEU B 267     2189   3378   2918    413   -601    -94       C  
ATOM   7007  CG  LEU B 267       7.801  10.446  72.278  1.00 26.13           C  
ANISOU 7007  CG  LEU B 267     2663   3855   3409    426   -536    -76       C  
ATOM   7008  CD1 LEU B 267       8.268  10.685  70.815  1.00 25.53           C  
ANISOU 7008  CD1 LEU B 267     2519   3776   3404    421   -500    -93       C  
ATOM   7009  CD2 LEU B 267       7.663   8.962  72.598  1.00 27.58           C  
ANISOU 7009  CD2 LEU B 267     2861   4034   3586    450   -555    -43       C  
ATOM   7010  N   GLU B 268       9.111  12.540  76.488  1.00 23.66           N  
ANISOU 7010  N   GLU B 268     2476   3559   2955    379   -715   -112       N  
ATOM   7011  CA  GLU B 268      10.055  13.266  77.360  1.00 23.97           C  
ANISOU 7011  CA  GLU B 268     2517   3603   2986    364   -778   -134       C  
ATOM   7012  C   GLU B 268      11.112  14.090  76.615  1.00 27.61           C  
ANISOU 7012  C   GLU B 268     2905   4067   3519    358   -783   -169       C  
ATOM   7013  O   GLU B 268      12.218  14.311  77.108  1.00 27.39           O  
ANISOU 7013  O   GLU B 268     2855   4039   3512    356   -847   -185       O  
ATOM   7014  CB  GLU B 268      10.678  12.298  78.377  1.00 25.71           C  
ANISOU 7014  CB  GLU B 268     2763   3818   3187    378   -861   -111       C  
ATOM   7015  CG  GLU B 268       9.617  11.720  79.317  1.00 34.70           C  
ANISOU 7015  CG  GLU B 268     3990   4953   4242    377   -855    -82       C  
ATOM   7016  CD  GLU B 268      10.171  10.658  80.250  1.00 55.55           C  
ANISOU 7016  CD  GLU B 268     6661   7586   6862    393   -935    -54       C  
ATOM   7017  OE1 GLU B 268      11.249  10.904  80.839  1.00 48.11           O  
ANISOU 7017  OE1 GLU B 268     5705   6644   5930    390  -1011    -65       O  
ATOM   7018  OE2 GLU B 268       9.526   9.579  80.393  1.00 46.53           O  
ANISOU 7018  OE2 GLU B 268     5554   6434   5692    409   -923    -22       O  
ATOM   7019  N   ILE B 269      10.745  14.568  75.434  1.00 24.08           N  
ANISOU 7019  N   ILE B 269     2423   3620   3107    353   -715   -181       N  
ATOM   7020  CA  ILE B 269      11.577  15.476  74.666  1.00 24.34           C  
ANISOU 7020  CA  ILE B 269     2394   3652   3200    343   -704   -217       C  
ATOM   7021  C   ILE B 269      11.566  16.841  75.357  1.00 30.44           C  
ANISOU 7021  C   ILE B 269     3191   4435   3939    317   -705   -246       C  
ATOM   7022  O   ILE B 269      12.565  17.550  75.341  1.00 30.61           O  
ANISOU 7022  O   ILE B 269     3174   4458   3999    309   -731   -277       O  
ATOM   7023  CB  ILE B 269      11.122  15.551  73.178  1.00 26.31           C  
ANISOU 7023  CB  ILE B 269     2608   3896   3492    344   -628   -219       C  
ATOM   7024  CG1 ILE B 269      11.300  14.163  72.527  1.00 26.26           C  
ANISOU 7024  CG1 ILE B 269     2572   3880   3526    367   -631   -195       C  
ATOM   7025  CG2 ILE B 269      11.899  16.625  72.409  1.00 25.89           C  
ANISOU 7025  CG2 ILE B 269     2502   3840   3495    329   -609   -259       C  
ATOM   7026  CD1 ILE B 269      10.815  14.024  71.102  1.00 28.36           C  
ANISOU 7026  CD1 ILE B 269     2809   4139   3827    369   -561   -192       C  
ATOM   7027  N   ILE B 270      10.438  17.189  75.964  1.00 28.10           N  
ANISOU 7027  N   ILE B 270     2957   4144   3574    303   -676   -236       N  
ATOM   7028  CA  ILE B 270      10.349  18.304  76.896  1.00 28.39           C  
ANISOU 7028  CA  ILE B 270     3029   4191   3567    277   -684   -258       C  
ATOM   7029  C   ILE B 270       9.663  17.849  78.187  1.00 33.05           C  
ANISOU 7029  C   ILE B 270     3698   4783   4077    271   -709   -236       C  
ATOM   7030  O   ILE B 270       8.897  16.895  78.171  1.00 31.85           O  
ANISOU 7030  O   ILE B 270     3578   4623   3901    285   -693   -206       O  
ATOM   7031  CB  ILE B 270       9.553  19.516  76.307  1.00 30.94           C  
ANISOU 7031  CB  ILE B 270     3351   4516   3888    255   -609   -278       C  
ATOM   7032  CG1 ILE B 270       8.072  19.175  76.123  1.00 30.97           C  
ANISOU 7032  CG1 ILE B 270     3399   4514   3855    256   -551   -254       C  
ATOM   7033  CG2 ILE B 270      10.173  19.995  74.992  1.00 31.37           C  
ANISOU 7033  CG2 ILE B 270     3335   4567   4017    259   -579   -300       C  
ATOM   7034  CD1 ILE B 270       7.282  20.279  75.365  1.00 40.71           C  
ANISOU 7034  CD1 ILE B 270     4624   5744   5099    238   -478   -271       C  
ATOM   7035  N   LYS B 271       9.950  18.544  79.283  1.00 31.43           N  
ANISOU 7035  N   LYS B 271     3526   4586   3832    249   -745   -253       N  
ATOM   7036  CA  LYS B 271       9.290  18.334  80.555  1.00 32.30           C  
ANISOU 7036  CA  LYS B 271     3718   4695   3860    234   -761   -238       C  
ATOM   7037  C   LYS B 271       8.779  19.660  81.099  1.00 38.90           C  
ANISOU 7037  C   LYS B 271     4585   5538   4658    197   -726   -266       C  
ATOM   7038  O   LYS B 271       9.553  20.552  81.436  1.00 38.91           O  
ANISOU 7038  O   LYS B 271     4566   5550   4669    181   -753   -295       O  
ATOM   7039  CB  LYS B 271      10.250  17.687  81.555  1.00 35.30           C  
ANISOU 7039  CB  LYS B 271     4117   5076   4221    242   -856   -228       C  
ATOM   7040  CG  LYS B 271      10.701  16.303  81.091  1.00 50.41           C  
ANISOU 7040  CG  LYS B 271     6002   6979   6173    278   -891   -198       C  
ATOM   7041  CD  LYS B 271      11.639  15.581  82.068  1.00 58.06           C  
ANISOU 7041  CD  LYS B 271     6988   7944   7126    289   -991   -184       C  
ATOM   7042  CE  LYS B 271      11.887  14.128  81.617  1.00 57.33           C  
ANISOU 7042  CE  LYS B 271     6873   7839   7070    324  -1016   -150       C  
ATOM   7043  NZ  LYS B 271      10.736  13.255  81.957  1.00 59.64           N  
ANISOU 7043  NZ  LYS B 271     7234   8124   7302    329   -986   -115       N  
ATOM   7044  N   GLN B 272       7.466  19.803  81.145  1.00 37.04           N  
ANISOU 7044  N   GLN B 272     4394   5294   4385    183   -662   -260       N  
ATOM   7045  CA  GLN B 272       6.856  20.967  81.752  1.00 37.57           C  
ANISOU 7045  CA  GLN B 272     4497   5364   4415    145   -625   -284       C  
ATOM   7046  C   GLN B 272       5.703  20.499  82.637  1.00 44.01           C  
ANISOU 7046  C   GLN B 272     5397   6165   5159    129   -602   -268       C  
ATOM   7047  O   GLN B 272       5.321  19.323  82.625  1.00 43.36           O  
ANISOU 7047  O   GLN B 272     5341   6072   5061    151   -608   -237       O  
ATOM   7048  CB  GLN B 272       6.339  21.933  80.685  1.00 38.01           C  
ANISOU 7048  CB  GLN B 272     4508   5417   4515    137   -551   -304       C  
ATOM   7049  CG  GLN B 272       7.304  22.241  79.544  1.00 41.73           C  
ANISOU 7049  CG  GLN B 272     4897   5896   5063    155   -556   -317       C  
ATOM   7050  CD  GLN B 272       8.420  23.192  79.945  1.00 58.29           C  
ANISOU 7050  CD  GLN B 272     6966   8008   7175    140   -594   -351       C  
ATOM   7051  OE1 GLN B 272       9.600  22.972  79.620  1.00 54.33           O  
ANISOU 7051  OE1 GLN B 272     6414   7511   6719    158   -640   -358       O  
ATOM   7052  NE2 GLN B 272       8.056  24.261  80.641  1.00 47.00           N  
ANISOU 7052  NE2 GLN B 272     5564   6583   5712    106   -572   -374       N  
ATOM   7053  N   GLY B 273       5.146  21.430  83.399  1.00 42.82           N  
ANISOU 7053  N   GLY B 273     5289   6012   4966     90   -573   -290       N  
ATOM   7054  CA  GLY B 273       4.082  21.107  84.315  1.00 43.78           C  
ANISOU 7054  CA  GLY B 273     5496   6118   5022     68   -547   -281       C  
ATOM   7055  C   GLY B 273       2.803  20.773  83.584  1.00 49.34           C  
ANISOU 7055  C   GLY B 273     6203   6801   5741     78   -473   -270       C  
ATOM   7056  O   GLY B 273       2.804  20.566  82.379  1.00 48.01           O  
ANISOU 7056  O   GLY B 273     5977   6635   5630    106   -452   -262       O  
ATOM   7057  N   CYS B 274       1.712  20.739  84.339  1.00 48.72           N  
ANISOU 7057  N   CYS B 274     6197   6704   5613     51   -432   -273       N  
ATOM   7058  CA  CYS B 274       0.395  20.369  83.831  1.00 49.47           C  
ANISOU 7058  CA  CYS B 274     6306   6775   5718     58   -362   -266       C  
ATOM   7059  C   CYS B 274      -0.305  21.544  83.195  1.00 47.83           C  
ANISOU 7059  C   CYS B 274     6063   6559   5551     39   -294   -293       C  
ATOM   7060  O   CYS B 274      -1.143  21.372  82.323  1.00 46.51           O  
ANISOU 7060  O   CYS B 274     5874   6377   5419     54   -243   -288       O  
ATOM   7061  CB  CYS B 274      -0.457  19.829  84.972  1.00 52.30           C  
ANISOU 7061  CB  CYS B 274     6757   7109   6005     35   -345   -262       C  
ATOM   7062  SG  CYS B 274       0.229  18.308  85.613  1.00 58.11           S  
ANISOU 7062  SG  CYS B 274     7537   7848   6695     62   -421   -224       S  
ATOM   7063  N   GLU B 275       0.041  22.734  83.658  1.00 41.40           N  
ANISOU 7063  N   GLU B 275     5244   5755   4731      5   -295   -321       N  
ATOM   7064  CA  GLU B 275      -0.479  23.964  83.109  1.00 39.82           C  
ANISOU 7064  CA  GLU B 275     5008   5549   4572    -15   -237   -348       C  
ATOM   7065  C   GLU B 275      -0.001  24.139  81.669  1.00 40.11           C  
ANISOU 7065  C   GLU B 275     4961   5598   4679     18   -236   -342       C  
ATOM   7066  O   GLU B 275      -0.690  24.730  80.842  1.00 38.89           O  
ANISOU 7066  O   GLU B 275     4776   5431   4568     16   -183   -351       O  
ATOM   7067  CB  GLU B 275       0.006  25.105  83.981  1.00 41.76           C  
ANISOU 7067  CB  GLU B 275     5265   5807   4795    -57   -247   -378       C  
ATOM   7068  CG  GLU B 275      -0.543  26.478  83.689  1.00 53.37           C  
ANISOU 7068  CG  GLU B 275     6707   7269   6301    -87   -187   -409       C  
ATOM   7069  CD  GLU B 275       0.204  27.539  84.490  1.00 77.80           C  
ANISOU 7069  CD  GLU B 275     9803  10383   9376   -123   -207   -438       C  
ATOM   7070  OE1 GLU B 275       0.099  28.738  84.123  1.00 77.21           O  
ANISOU 7070  OE1 GLU B 275     9688  10309   9340   -142   -168   -463       O  
ATOM   7071  OE2 GLU B 275       0.914  27.164  85.469  1.00 69.57           O  
ANISOU 7071  OE2 GLU B 275     8799   9353   8281   -132   -264   -435       O  
ATOM   7072  N   PHE B 276       1.184  23.609  81.380  1.00 34.49           N  
ANISOU 7072  N   PHE B 276     4216   4907   3980     46   -296   -328       N  
ATOM   7073  CA  PHE B 276       1.748  23.662  80.045  1.00 32.48           C  
ANISOU 7073  CA  PHE B 276     3887   4662   3790     75   -298   -324       C  
ATOM   7074  C   PHE B 276       1.053  22.623  79.201  1.00 35.88           C  
ANISOU 7074  C   PHE B 276     4314   5080   4240    107   -274   -297       C  
ATOM   7075  O   PHE B 276       0.716  22.896  78.060  1.00 35.35           O  
ANISOU 7075  O   PHE B 276     4205   5007   4221    118   -236   -297       O  
ATOM   7076  CB  PHE B 276       3.266  23.400  80.072  1.00 33.75           C  
ANISOU 7076  CB  PHE B 276     4014   4847   3965     93   -369   -322       C  
ATOM   7077  CG  PHE B 276       3.893  23.354  78.714  1.00 33.85           C  
ANISOU 7077  CG  PHE B 276     3953   4864   4043    121   -369   -319       C  
ATOM   7078  CD1 PHE B 276       4.391  24.494  78.133  1.00 35.55           C  
ANISOU 7078  CD1 PHE B 276     4118   5087   4300    110   -353   -345       C  
ATOM   7079  CD2 PHE B 276       3.952  22.164  78.000  1.00 35.20           C  
ANISOU 7079  CD2 PHE B 276     4107   5032   4235    155   -379   -291       C  
ATOM   7080  CE1 PHE B 276       4.953  24.456  76.873  1.00 35.98           C  
ANISOU 7080  CE1 PHE B 276     4112   5143   4414    132   -348   -344       C  
ATOM   7081  CE2 PHE B 276       4.524  22.114  76.727  1.00 37.14           C  
ANISOU 7081  CE2 PHE B 276     4288   5280   4541    176   -375   -290       C  
ATOM   7082  CZ  PHE B 276       5.021  23.253  76.162  1.00 34.86           C  
ANISOU 7082  CZ  PHE B 276     3956   4998   4293    164   -359   -316       C  
ATOM   7083  N   GLU B 277       0.859  21.435  79.773  1.00 32.39           N  
ANISOU 7083  N   GLU B 277     3916   4632   3759    120   -296   -274       N  
ATOM   7084  CA  GLU B 277       0.224  20.317  79.085  1.00 31.69           C  
ANISOU 7084  CA  GLU B 277     3826   4530   3684    151   -276   -248       C  
ATOM   7085  C   GLU B 277      -1.226  20.612  78.772  1.00 35.59           C  
ANISOU 7085  C   GLU B 277     4338   5000   4185    140   -204   -255       C  
ATOM   7086  O   GLU B 277      -1.729  20.203  77.734  1.00 35.43           O  
ANISOU 7086  O   GLU B 277     4290   4972   4202    164   -174   -243       O  
ATOM   7087  CB  GLU B 277       0.298  19.039  79.926  1.00 33.48           C  
ANISOU 7087  CB  GLU B 277     4104   4754   3862    164   -313   -223       C  
ATOM   7088  CG  GLU B 277       1.686  18.380  79.974  1.00 45.64           C  
ANISOU 7088  CG  GLU B 277     5618   6314   5411    187   -388   -208       C  
ATOM   7089  CD  GLU B 277       1.744  17.159  80.902  1.00 66.26           C  
ANISOU 7089  CD  GLU B 277     8286   8920   7971    197   -429   -182       C  
ATOM   7090  OE1 GLU B 277       2.856  16.818  81.374  1.00 56.12           O  
ANISOU 7090  OE1 GLU B 277     6997   7648   6679    205   -500   -174       O  
ATOM   7091  OE2 GLU B 277       0.679  16.546  81.162  1.00 59.07           O  
ANISOU 7091  OE2 GLU B 277     7424   7990   7030    198   -391   -171       O  
ATOM   7092  N   ASN B 278      -1.910  21.310  79.667  1.00 32.21           N  
ANISOU 7092  N   ASN B 278     3956   4557   3724    104   -175   -276       N  
ATOM   7093  CA  ASN B 278      -3.321  21.611  79.455  1.00 31.82           C  
ANISOU 7093  CA  ASN B 278     3924   4479   3688     92   -106   -288       C  
ATOM   7094  C   ASN B 278      -3.542  22.744  78.456  1.00 35.38           C  
ANISOU 7094  C   ASN B 278     4321   4927   4197     86    -71   -304       C  
ATOM   7095  O   ASN B 278      -4.585  22.791  77.840  1.00 35.02           O  
ANISOU 7095  O   ASN B 278     4269   4859   4180     90    -23   -306       O  
ATOM   7096  CB  ASN B 278      -4.063  21.888  80.781  1.00 33.94           C  
ANISOU 7096  CB  ASN B 278     4264   4726   3906     52    -81   -307       C  
ATOM   7097  CG  ASN B 278      -4.831  20.656  81.302  1.00 58.37           C  
ANISOU 7097  CG  ASN B 278     7419   7798   6962     61    -68   -292       C  
ATOM   7098  OD1 ASN B 278      -6.061  20.544  81.137  1.00 52.46           O  
ANISOU 7098  OD1 ASN B 278     6687   7018   6226     57    -10   -300       O  
ATOM   7099  ND2 ASN B 278      -4.110  19.726  81.912  1.00 51.46           N  
ANISOU 7099  ND2 ASN B 278     6574   6937   6043     74   -121   -270       N  
ATOM   7100  N   THR B 279      -2.572  23.647  78.296  1.00 31.86           N  
ANISOU 7100  N   THR B 279     3836   4503   3768     76    -95   -317       N  
ATOM   7101  CA  THR B 279      -2.626  24.681  77.252  1.00 31.06           C  
ANISOU 7101  CA  THR B 279     3681   4400   3722     74    -66   -329       C  
ATOM   7102  C   THR B 279      -2.346  24.030  75.849  1.00 33.99           C  
ANISOU 7102  C   THR B 279     4002   4776   4135    114    -73   -306       C  
ATOM   7103  O   THR B 279      -2.975  24.386  74.851  1.00 33.17           O  
ANISOU 7103  O   THR B 279     3873   4658   4071    119    -37   -306       O  
ATOM   7104  CB  THR B 279      -1.659  25.878  77.586  1.00 37.70           C  
ANISOU 7104  CB  THR B 279     4497   5260   4565     50    -85   -353       C  
ATOM   7105  OG1 THR B 279      -1.968  26.408  78.874  1.00 39.31           O  
ANISOU 7105  OG1 THR B 279     4749   5459   4729     11    -76   -374       O  
ATOM   7106  CG2 THR B 279      -1.773  27.038  76.588  1.00 34.36           C  
ANISOU 7106  CG2 THR B 279     4024   4833   4197     44    -50   -368       C  
ATOM   7107  N   VAL B 280      -1.436  23.056  75.794  1.00 29.53           N  
ANISOU 7107  N   VAL B 280     3429   4231   3562    139   -120   -287       N  
ATOM   7108  CA  VAL B 280      -1.214  22.293  74.574  1.00 28.71           C  
ANISOU 7108  CA  VAL B 280     3285   4130   3494    173   -124   -266       C  
ATOM   7109  C   VAL B 280      -2.527  21.641  74.112  1.00 33.13           C  
ANISOU 7109  C   VAL B 280     3862   4666   4059    186    -81   -252       C  
ATOM   7110  O   VAL B 280      -2.937  21.767  72.958  1.00 31.82           O  
ANISOU 7110  O   VAL B 280     3666   4492   3933    198    -54   -248       O  
ATOM   7111  CB  VAL B 280      -0.109  21.218  74.758  1.00 32.21           C  
ANISOU 7111  CB  VAL B 280     3720   4592   3927    196   -180   -248       C  
ATOM   7112  CG1 VAL B 280       0.052  20.378  73.502  1.00 31.34           C  
ANISOU 7112  CG1 VAL B 280     3569   4482   3855    227   -177   -227       C  
ATOM   7113  CG2 VAL B 280       1.229  21.876  75.100  1.00 32.24           C  
ANISOU 7113  CG2 VAL B 280     3697   4615   3935    184   -224   -264       C  
ATOM   7114  N   HIS B 281      -3.223  20.993  75.028  1.00 31.41           N  
ANISOU 7114  N   HIS B 281     3698   4437   3802    183    -74   -248       N  
ATOM   7115  CA  HIS B 281      -4.448  20.301  74.663  1.00 31.34           C  
ANISOU 7115  CA  HIS B 281     3706   4404   3799    197    -35   -238       C  
ATOM   7116  C   HIS B 281      -5.610  21.198  74.229  1.00 34.12           C  
ANISOU 7116  C   HIS B 281     4054   4729   4181    181     19   -256       C  
ATOM   7117  O   HIS B 281      -6.381  20.801  73.361  1.00 33.25           O  
ANISOU 7117  O   HIS B 281     3931   4603   4099    200     46   -248       O  
ATOM   7118  CB  HIS B 281      -4.825  19.331  75.764  1.00 32.86           C  
ANISOU 7118  CB  HIS B 281     3957   4588   3942    198    -40   -231       C  
ATOM   7119  CG  HIS B 281      -3.714  18.376  76.080  1.00 36.92           C  
ANISOU 7119  CG  HIS B 281     4471   5125   4433    218    -96   -209       C  
ATOM   7120  ND1 HIS B 281      -3.497  17.862  77.343  1.00 39.23           N  
ANISOU 7120  ND1 HIS B 281     4818   5418   4670    209   -124   -205       N  
ATOM   7121  CD2 HIS B 281      -2.716  17.896  75.299  1.00 38.42           C  
ANISOU 7121  CD2 HIS B 281     4612   5335   4650    243   -131   -192       C  
ATOM   7122  CE1 HIS B 281      -2.423  17.090  77.318  1.00 38.76           C  
ANISOU 7122  CE1 HIS B 281     4740   5378   4608    231   -178   -184       C  
ATOM   7123  NE2 HIS B 281      -1.936  17.090  76.089  1.00 38.69           N  
ANISOU 7123  NE2 HIS B 281     4667   5381   4651    251   -181   -178       N  
ATOM   7124  N   LYS B 282      -5.713  22.405  74.767  1.00 31.14           N  
ANISOU 7124  N   LYS B 282     3684   4345   3801    148     32   -281       N  
ATOM   7125  CA  LYS B 282      -6.753  23.340  74.302  1.00 31.08           C  
ANISOU 7125  CA  LYS B 282     3667   4311   3832    132     80   -298       C  
ATOM   7126  C   LYS B 282      -6.446  23.881  72.896  1.00 34.56           C  
ANISOU 7126  C   LYS B 282     4052   4758   4323    146     80   -292       C  
ATOM   7127  O   LYS B 282      -7.350  24.073  72.089  1.00 34.25           O  
ANISOU 7127  O   LYS B 282     3999   4695   4320    152    111   -292       O  
ATOM   7128  CB  LYS B 282      -7.030  24.467  75.328  1.00 34.24           C  
ANISOU 7128  CB  LYS B 282     4092   4698   4218     89    100   -328       C  
ATOM   7129  CG  LYS B 282      -6.143  25.719  75.252  1.00 50.56           C  
ANISOU 7129  CG  LYS B 282     6127   6785   6300     69     87   -343       C  
ATOM   7130  CD  LYS B 282      -6.680  26.861  76.153  1.00 58.87           C  
ANISOU 7130  CD  LYS B 282     7200   7819   7347     25    120   -374       C  
ATOM   7131  CE  LYS B 282      -6.157  28.246  75.714  1.00 67.37           C  
ANISOU 7131  CE  LYS B 282     8233   8905   8458      8    124   -390       C  
ATOM   7132  NZ  LYS B 282      -6.877  29.413  76.358  1.00 72.72           N  
ANISOU 7132  NZ  LYS B 282     8924   9560   9148    -34    166   -421       N  
ATOM   7133  N   TRP B 283      -5.173  24.098  72.593  1.00 31.17           N  
ANISOU 7133  N   TRP B 283     3590   4356   3896    151     45   -288       N  
ATOM   7134  CA  TRP B 283      -4.773  24.571  71.265  1.00 31.06           C  
ANISOU 7134  CA  TRP B 283     3529   4348   3926    161     46   -283       C  
ATOM   7135  C   TRP B 283      -4.843  23.468  70.201  1.00 31.19           C  
ANISOU 7135  C   TRP B 283     3527   4365   3958    194     42   -257       C  
ATOM   7136  O   TRP B 283      -5.096  23.776  69.041  1.00 30.03           O  
ANISOU 7136  O   TRP B 283     3354   4209   3847    201     58   -252       O  
ATOM   7137  CB  TRP B 283      -3.392  25.248  71.312  1.00 31.12           C  
ANISOU 7137  CB  TRP B 283     3508   4381   3936    151     16   -293       C  
ATOM   7138  CG  TRP B 283      -3.472  26.641  71.919  1.00 33.31           C  
ANISOU 7138  CG  TRP B 283     3788   4653   4214    117     33   -320       C  
ATOM   7139  CD1 TRP B 283      -3.222  27.002  73.217  1.00 36.67           C  
ANISOU 7139  CD1 TRP B 283     4241   5088   4606     93     23   -338       C  
ATOM   7140  CD2 TRP B 283      -3.863  27.840  71.244  1.00 33.51           C  
ANISOU 7140  CD2 TRP B 283     3791   4664   4278    103     65   -333       C  
ATOM   7141  NE1 TRP B 283      -3.421  28.352  73.383  1.00 36.47           N  
ANISOU 7141  NE1 TRP B 283     4206   5053   4596     63     49   -362       N  
ATOM   7142  CE2 TRP B 283      -3.807  28.889  72.184  1.00 37.98           C  
ANISOU 7142  CE2 TRP B 283     4367   5230   4834     70     75   -359       C  
ATOM   7143  CE3 TRP B 283      -4.241  28.129  69.927  1.00 34.82           C  
ANISOU 7143  CE3 TRP B 283     3930   4814   4484    114     84   -324       C  
ATOM   7144  CZ2 TRP B 283      -4.127  30.199  71.855  1.00 37.60           C  
ANISOU 7144  CZ2 TRP B 283     4300   5168   4820     49    105   -376       C  
ATOM   7145  CZ3 TRP B 283      -4.554  29.430  69.595  1.00 36.56           C  
ANISOU 7145  CZ3 TRP B 283     4136   5020   4736     94    111   -339       C  
ATOM   7146  CH2 TRP B 283      -4.499  30.452  70.555  1.00 37.60           C  
ANISOU 7146  CH2 TRP B 283     4275   5152   4861     62    122   -365       C  
ATOM   7147  N   ILE B 284      -4.632  22.204  70.597  1.00 25.75           N  
ANISOU 7147  N   ILE B 284     2855   3687   3243    214     22   -241       N  
ATOM   7148  CA  ILE B 284      -4.960  21.053  69.727  1.00 24.74           C  
ANISOU 7148  CA  ILE B 284     2716   3555   3127    244     27   -218       C  
ATOM   7149  C   ILE B 284      -6.469  20.969  69.394  1.00 27.21           C  
ANISOU 7149  C   ILE B 284     3045   3837   3455    247     69   -220       C  
ATOM   7150  O   ILE B 284      -6.848  20.732  68.246  1.00 25.78           O  
ANISOU 7150  O   ILE B 284     2842   3648   3304    263     82   -209       O  
ATOM   7151  CB  ILE B 284      -4.493  19.699  70.328  1.00 27.54           C  
ANISOU 7151  CB  ILE B 284     3088   3925   3452    263     -1   -201       C  
ATOM   7152  CG1 ILE B 284      -2.974  19.543  70.160  1.00 27.74           C  
ANISOU 7152  CG1 ILE B 284     3081   3977   3483    269    -45   -196       C  
ATOM   7153  CG2 ILE B 284      -5.217  18.535  69.669  1.00 26.50           C  
ANISOU 7153  CG2 ILE B 284     2956   3784   3330    290     18   -182       C  
ATOM   7154  CD1 ILE B 284      -2.415  18.322  70.825  1.00 31.34           C  
ANISOU 7154  CD1 ILE B 284     3550   4445   3912    286    -79   -179       C  
ATOM   7155  N   SER B 285      -7.322  21.172  70.390  1.00 23.66           N  
ANISOU 7155  N   SER B 285     2634   3367   2987    231     90   -235       N  
ATOM   7156  CA  SER B 285      -8.741  21.328  70.115  1.00 23.44           C  
ANISOU 7156  CA  SER B 285     2617   3305   2983    230    131   -243       C  
ATOM   7157  C   SER B 285      -9.012  22.526  69.194  1.00 27.92           C  
ANISOU 7157  C   SER B 285     3154   3858   3594    219    145   -252       C  
ATOM   7158  O   SER B 285      -9.828  22.427  68.291  1.00 27.34           O  
ANISOU 7158  O   SER B 285     3069   3764   3553    231    164   -247       O  
ATOM   7159  CB  SER B 285      -9.529  21.482  71.403  1.00 27.74           C  
ANISOU 7159  CB  SER B 285     3209   3827   3505    207    155   -264       C  
ATOM   7160  OG  SER B 285      -9.339  20.351  72.245  1.00 40.80           O  
ANISOU 7160  OG  SER B 285     4898   5490   5115    217    142   -255       O  
ATOM   7161  N   ILE B 286      -8.322  23.650  69.391  1.00 25.21           N  
ANISOU 7161  N   ILE B 286     2798   3526   3253    196    136   -264       N  
ATOM   7162  CA  ILE B 286      -8.562  24.811  68.512  1.00 25.31           C  
ANISOU 7162  CA  ILE B 286     2784   3524   3308    185    150   -271       C  
ATOM   7163  C   ILE B 286      -8.070  24.597  67.074  1.00 28.88           C  
ANISOU 7163  C   ILE B 286     3202   3987   3783    206    136   -251       C  
ATOM   7164  O   ILE B 286      -8.809  24.889  66.122  1.00 28.64           O  
ANISOU 7164  O   ILE B 286     3162   3935   3787    211    152   -247       O  
ATOM   7165  CB  ILE B 286      -7.935  26.105  69.041  1.00 28.90           C  
ANISOU 7165  CB  ILE B 286     3231   3987   3762    155    147   -291       C  
ATOM   7166  CG1 ILE B 286      -8.697  26.602  70.267  1.00 30.03           C  
ANISOU 7166  CG1 ILE B 286     3406   4110   3894    127    172   -315       C  
ATOM   7167  CG2 ILE B 286      -7.979  27.193  67.974  1.00 29.23           C  
ANISOU 7167  CG2 ILE B 286     3242   4018   3846    149    157   -293       C  
ATOM   7168  CD1 ILE B 286      -8.031  27.827  70.942  1.00 38.48           C  
ANISOU 7168  CD1 ILE B 286     4471   5192   4959     95    170   -336       C  
ATOM   7169  N   THR B 287      -6.831  24.119  66.920  1.00 24.33           N  
ANISOU 7169  N   THR B 287     2611   3442   3191    215    108   -240       N  
ATOM   7170  CA  THR B 287      -6.205  24.026  65.607  1.00 23.36           C  
ANISOU 7170  CA  THR B 287     2458   3329   3090    227     99   -226       C  
ATOM   7171  C   THR B 287      -6.816  22.936  64.750  1.00 26.66           C  
ANISOU 7171  C   THR B 287     2875   3739   3517    253    106   -206       C  
ATOM   7172  O   THR B 287      -6.861  23.047  63.522  1.00 27.96           O  
ANISOU 7172  O   THR B 287     3021   3896   3705    258    111   -196       O  
ATOM   7173  CB  THR B 287      -4.717  23.749  65.702  1.00 28.94           C  
ANISOU 7173  CB  THR B 287     3145   4065   3784    230     69   -224       C  
ATOM   7174  OG1 THR B 287      -4.524  22.537  66.445  1.00 28.83           O  
ANISOU 7174  OG1 THR B 287     3147   4066   3742    245     51   -215       O  
ATOM   7175  CG2 THR B 287      -3.991  24.926  66.382  1.00 25.59           C  
ANISOU 7175  CG2 THR B 287     2716   3652   3357    205     61   -246       C  
ATOM   7176  N   GLU B 288      -7.286  21.883  65.390  1.00 20.84           N  
ANISOU 7176  N   GLU B 288     2158   3001   2759    267    108   -200       N  
ATOM   7177  CA  GLU B 288      -8.040  20.852  64.711  1.00 19.62           C  
ANISOU 7177  CA  GLU B 288     2004   2837   2614    291    120   -185       C  
ATOM   7178  C   GLU B 288      -9.361  21.412  64.155  1.00 23.85           C  
ANISOU 7178  C   GLU B 288     2544   3337   3179    288    145   -191       C  
ATOM   7179  O   GLU B 288      -9.748  21.120  63.020  1.00 23.95           O  
ANISOU 7179  O   GLU B 288     2545   3342   3214    301    150   -179       O  
ATOM   7180  CB  GLU B 288      -8.332  19.719  65.686  1.00 20.65           C  
ANISOU 7180  CB  GLU B 288     2160   2971   2715    304    120   -182       C  
ATOM   7181  CG  GLU B 288      -9.032  18.566  65.052  1.00 26.21           C  
ANISOU 7181  CG  GLU B 288     2863   3667   3428    330    135   -168       C  
ATOM   7182  CD  GLU B 288      -9.605  17.597  66.053  1.00 36.44           C  
ANISOU 7182  CD  GLU B 288     4190   4957   4699    341    145   -169       C  
ATOM   7183  OE1 GLU B 288      -9.561  16.386  65.734  1.00 28.09           O  
ANISOU 7183  OE1 GLU B 288     3127   3909   3637    364    145   -153       O  
ATOM   7184  OE2 GLU B 288     -10.110  18.027  67.130  1.00 26.70           O  
ANISOU 7184  OE2 GLU B 288     2988   3708   3450    325    157   -187       O  
ATOM   7185  N   ALA B 289     -10.069  22.197  64.961  1.00 19.39           N  
ANISOU 7185  N   ALA B 289     1997   2751   2618    270    161   -211       N  
ATOM   7186  CA  ALA B 289     -11.324  22.794  64.515  1.00 18.79           C  
ANISOU 7186  CA  ALA B 289     1923   2637   2580    266    183   -220       C  
ATOM   7187  C   ALA B 289     -11.086  23.697  63.324  1.00 24.05           C  
ANISOU 7187  C   ALA B 289     2565   3298   3273    260    175   -213       C  
ATOM   7188  O   ALA B 289     -11.864  23.731  62.379  1.00 24.13           O  
ANISOU 7188  O   ALA B 289     2570   3286   3313    269    181   -206       O  
ATOM   7189  CB  ALA B 289     -11.919  23.597  65.627  1.00 19.73           C  
ANISOU 7189  CB  ALA B 289     2062   2734   2701    242    202   -245       C  
ATOM   7190  N   LEU B 290      -9.998  24.455  63.397  1.00 21.82           N  
ANISOU 7190  N   LEU B 290     2272   3037   2983    244    162   -216       N  
ATOM   7191  CA  LEU B 290      -9.631  25.378  62.351  1.00 21.72           C  
ANISOU 7191  CA  LEU B 290     2241   3020   2993    235    158   -211       C  
ATOM   7192  C   LEU B 290      -9.197  24.597  61.109  1.00 25.56           C  
ANISOU 7192  C   LEU B 290     2714   3518   3479    252    147   -189       C  
ATOM   7193  O   LEU B 290      -9.370  25.052  59.982  1.00 25.12           O  
ANISOU 7193  O   LEU B 290     2653   3448   3445    250    147   -180       O  
ATOM   7194  CB  LEU B 290      -8.531  26.303  62.869  1.00 21.94           C  
ANISOU 7194  CB  LEU B 290     2259   3067   3010    213    150   -224       C  
ATOM   7195  CG  LEU B 290      -8.995  27.440  63.815  1.00 26.02           C  
ANISOU 7195  CG  LEU B 290     2784   3568   3536    188    166   -247       C  
ATOM   7196  CD1 LEU B 290      -7.805  28.277  64.284  1.00 26.32           C  
ANISOU 7196  CD1 LEU B 290     2810   3628   3562    168    158   -261       C  
ATOM   7197  CD2 LEU B 290     -10.025  28.359  63.158  1.00 26.33           C  
ANISOU 7197  CD2 LEU B 290     2819   3568   3617    180    181   -250       C  
ATOM   7198  N   ALA B 291      -8.676  23.393  61.338  1.00 22.09           N  
ANISOU 7198  N   ALA B 291     2274   3103   3016    268    138   -180       N  
ATOM   7199  CA  ALA B 291      -8.275  22.507  60.273  1.00 21.67           C  
ANISOU 7199  CA  ALA B 291     2208   3061   2963    283    133   -161       C  
ATOM   7200  C   ALA B 291      -9.447  22.065  59.409  1.00 25.68           C  
ANISOU 7200  C   ALA B 291     2721   3545   3489    298    143   -150       C  
ATOM   7201  O   ALA B 291      -9.265  21.895  58.199  1.00 25.49           O  
ANISOU 7201  O   ALA B 291     2689   3521   3474    300    141   -136       O  
ATOM   7202  CB  ALA B 291      -7.569  21.313  60.847  1.00 22.53           C  
ANISOU 7202  CB  ALA B 291     2314   3198   3049    297    122   -155       C  
ATOM   7203  N   PHE B 292     -10.643  21.913  59.987  1.00 21.51           N  
ANISOU 7203  N   PHE B 292     2209   2996   2969    305    156   -158       N  
ATOM   7204  CA  PHE B 292     -11.784  21.367  59.235  1.00 20.43           C  
ANISOU 7204  CA  PHE B 292     2075   2836   2852    322    164   -151       C  
ATOM   7205  C   PHE B 292     -12.226  22.278  58.111  1.00 27.19           C  
ANISOU 7205  C   PHE B 292     2927   3666   3736    314    159   -146       C  
ATOM   7206  O   PHE B 292     -13.025  21.872  57.265  1.00 27.17           O  
ANISOU 7206  O   PHE B 292     2926   3646   3751    327    160   -138       O  
ATOM   7207  CB  PHE B 292     -13.000  21.062  60.112  1.00 21.14           C  
ANISOU 7207  CB  PHE B 292     2180   2901   2950    331    182   -166       C  
ATOM   7208  CG  PHE B 292     -12.747  20.069  61.207  1.00 21.35           C  
ANISOU 7208  CG  PHE B 292     2218   2946   2947    340    188   -170       C  
ATOM   7209  CD1 PHE B 292     -11.769  19.096  61.092  1.00 23.64           C  
ANISOU 7209  CD1 PHE B 292     2500   3271   3211    352    177   -154       C  
ATOM   7210  CD2 PHE B 292     -13.512  20.106  62.353  1.00 21.79           C  
ANISOU 7210  CD2 PHE B 292     2295   2982   3001    336    206   -190       C  
ATOM   7211  CE1 PHE B 292     -11.545  18.227  62.111  1.00 24.11           C  
ANISOU 7211  CE1 PHE B 292     2573   3346   3244    361    180   -155       C  
ATOM   7212  CE2 PHE B 292     -13.294  19.244  63.381  1.00 23.96           C  
ANISOU 7212  CE2 PHE B 292     2587   3272   3244    343    212   -192       C  
ATOM   7213  CZ  PHE B 292     -12.321  18.308  63.275  1.00 22.50           C  
ANISOU 7213  CZ  PHE B 292     2394   3121   3032    356    196   -174       C  
ATOM   7214  N   PHE B 293     -11.717  23.500  58.090  1.00 26.03           N  
ANISOU 7214  N   PHE B 293     2778   3517   3595    292    154   -152       N  
ATOM   7215  CA  PHE B 293     -11.856  24.378  56.929  1.00 27.37           C  
ANISOU 7215  CA  PHE B 293     2947   3666   3787    282    146   -143       C  
ATOM   7216  C   PHE B 293     -11.346  23.732  55.615  1.00 31.71           C  
ANISOU 7216  C   PHE B 293     3494   4229   4327    288    139   -122       C  
ATOM   7217  O   PHE B 293     -11.709  24.159  54.525  1.00 31.09           O  
ANISOU 7217  O   PHE B 293     3421   4128   4262    283    131   -112       O  
ATOM   7218  CB  PHE B 293     -11.110  25.688  57.215  1.00 30.21           C  
ANISOU 7218  CB  PHE B 293     3303   4029   4148    257    145   -153       C  
ATOM   7219  CG  PHE B 293     -11.405  26.806  56.247  1.00 32.86           C  
ANISOU 7219  CG  PHE B 293     3641   4336   4508    244    140   -147       C  
ATOM   7220  CD1 PHE B 293     -10.361  27.527  55.670  1.00 36.45           C  
ANISOU 7220  CD1 PHE B 293     4093   4801   4955    227    137   -144       C  
ATOM   7221  CD2 PHE B 293     -12.719  27.163  55.931  1.00 35.53           C  
ANISOU 7221  CD2 PHE B 293     3986   4635   4880    249    137   -147       C  
ATOM   7222  CE1 PHE B 293     -10.615  28.574  54.790  1.00 37.66           C  
ANISOU 7222  CE1 PHE B 293     4254   4926   5129    215    132   -137       C  
ATOM   7223  CE2 PHE B 293     -12.986  28.206  55.041  1.00 38.47           C  
ANISOU 7223  CE2 PHE B 293     4363   4979   5276    237    127   -139       C  
ATOM   7224  CZ  PHE B 293     -11.934  28.917  54.479  1.00 36.94           C  
ANISOU 7224  CZ  PHE B 293     4170   4796   5069    220    125   -133       C  
ATOM   7225  N   HIS B 294     -10.511  22.704  55.704  1.00 29.12           N  
ANISOU 7225  N   HIS B 294     3157   3932   3975    296    140   -117       N  
ATOM   7226  CA  HIS B 294     -10.136  21.950  54.509  1.00 29.39           C  
ANISOU 7226  CA  HIS B 294     3188   3975   4003    300    138   -100       C  
ATOM   7227  C   HIS B 294     -11.382  21.525  53.726  1.00 34.46           C  
ANISOU 7227  C   HIS B 294     3840   4594   4661    314    138    -90       C  
ATOM   7228  O   HIS B 294     -11.367  21.518  52.490  1.00 35.09           O  
ANISOU 7228  O   HIS B 294     3925   4665   4742    309    133    -76       O  
ATOM   7229  CB  HIS B 294      -9.227  20.735  54.843  1.00 29.94           C  
ANISOU 7229  CB  HIS B 294     3244   4080   4053    310    142    -96       C  
ATOM   7230  CG  HIS B 294      -9.954  19.537  55.385  1.00 33.07           C  
ANISOU 7230  CG  HIS B 294     3640   4480   4445    334    149    -95       C  
ATOM   7231  ND1 HIS B 294     -10.516  18.576  54.568  1.00 34.64           N  
ANISOU 7231  ND1 HIS B 294     3837   4675   4648    349    155    -83       N  
ATOM   7232  CD2 HIS B 294     -10.171  19.119  56.659  1.00 34.63           C  
ANISOU 7232  CD2 HIS B 294     3840   4684   4632    346    153   -104       C  
ATOM   7233  CE1 HIS B 294     -11.078  17.637  55.315  1.00 33.77           C  
ANISOU 7233  CE1 HIS B 294     3728   4570   4535    370    165    -86       C  
ATOM   7234  NE2 HIS B 294     -10.877  17.937  56.588  1.00 34.20           N  
ANISOU 7234  NE2 HIS B 294     3787   4629   4579    368    163    -98       N  
ATOM   7235  N   CYS B 295     -12.457  21.190  54.430  1.00 30.90           N  
ANISOU 7235  N   CYS B 295     3391   4127   4221    331    143    -99       N  
ATOM   7236  CA  CYS B 295     -13.722  20.791  53.773  1.00 30.67           C  
ANISOU 7236  CA  CYS B 295     3367   4072   4213    346    142    -94       C  
ATOM   7237  C   CYS B 295     -14.375  21.869  52.905  1.00 35.33           C  
ANISOU 7237  C   CYS B 295     3969   4627   4830    336    126    -90       C  
ATOM   7238  O   CYS B 295     -15.260  21.564  52.114  1.00 35.17           O  
ANISOU 7238  O   CYS B 295     3953   4584   4825    346    118    -84       O  
ATOM   7239  CB  CYS B 295     -14.748  20.367  54.809  1.00 30.99           C  
ANISOU 7239  CB  CYS B 295     3409   4097   4267    363    155   -111       C  
ATOM   7240  SG  CYS B 295     -14.209  19.055  55.927  1.00 34.95           S  
ANISOU 7240  SG  CYS B 295     3907   4635   4740    378    172   -115       S  
ATOM   7241  N   CYS B 296     -13.948  23.120  53.046  1.00 32.19           N  
ANISOU 7241  N   CYS B 296     3573   4221   4436    315    120    -94       N  
ATOM   7242  CA  CYS B 296     -14.530  24.219  52.290  1.00 32.05           C  
ANISOU 7242  CA  CYS B 296     3567   4167   4444    304    104    -89       C  
ATOM   7243  C   CYS B 296     -13.692  24.623  51.098  1.00 34.81           C  
ANISOU 7243  C   CYS B 296     3928   4522   4777    286     94    -71       C  
ATOM   7244  O   CYS B 296     -14.200  25.290  50.206  1.00 33.94           O  
ANISOU 7244  O   CYS B 296     3832   4381   4681    279     77    -61       O  
ATOM   7245  CB  CYS B 296     -14.716  25.417  53.202  1.00 32.92           C  
ANISOU 7245  CB  CYS B 296     3673   4259   4575    291    108   -106       C  
ATOM   7246  SG  CYS B 296     -15.718  25.006  54.608  1.00 37.07           S  
ANISOU 7246  SG  CYS B 296     4192   4773   5121    304    125   -131       S  
ATOM   7247  N   LEU B 297     -12.421  24.210  51.065  1.00 30.81           N  
ANISOU 7247  N   LEU B 297     3416   4051   4241    278    105    -69       N  
ATOM   7248  CA  LEU B 297     -11.507  24.698  50.033  1.00 30.77           C  
ANISOU 7248  CA  LEU B 297     3423   4048   4221    256    103    -58       C  
ATOM   7249  C   LEU B 297     -11.944  24.277  48.642  1.00 33.32           C  
ANISOU 7249  C   LEU B 297     3765   4355   4539    256     92    -39       C  
ATOM   7250  O   LEU B 297     -11.959  25.101  47.723  1.00 33.45           O  
ANISOU 7250  O   LEU B 297     3804   4349   4557    239     80    -28       O  
ATOM   7251  CB  LEU B 297     -10.076  24.215  50.256  1.00 31.13           C  
ANISOU 7251  CB  LEU B 297     3456   4130   4243    248    118    -63       C  
ATOM   7252  CG  LEU B 297      -9.469  24.450  51.624  1.00 36.30           C  
ANISOU 7252  CG  LEU B 297     4092   4806   4895    248    126    -81       C  
ATOM   7253  CD1 LEU B 297      -8.247  23.561  51.751  1.00 37.03           C  
ANISOU 7253  CD1 LEU B 297     4169   4933   4969    247    135    -84       C  
ATOM   7254  CD2 LEU B 297      -9.118  25.898  51.801  1.00 38.72           C  
ANISOU 7254  CD2 LEU B 297     4402   5099   5210    228    126    -91       C  
ATOM   7255  N   ASN B 298     -12.273  22.999  48.488  1.00 28.38           N  
ANISOU 7255  N   ASN B 298     3133   3743   3908    274     96    -34       N  
ATOM   7256  CA  ASN B 298     -12.691  22.457  47.196  1.00 27.89           C  
ANISOU 7256  CA  ASN B 298     3088   3669   3839    273     87    -17       C  
ATOM   7257  C   ASN B 298     -13.876  23.260  46.653  1.00 31.43           C  
ANISOU 7257  C   ASN B 298     3555   4075   4311    275     60    -10       C  
ATOM   7258  O   ASN B 298     -13.805  23.765  45.552  1.00 31.28           O  
ANISOU 7258  O   ASN B 298     3563   4037   4284    257     46      5       O  
ATOM   7259  CB  ASN B 298     -12.945  20.931  47.313  1.00 27.94           C  
ANISOU 7259  CB  ASN B 298     3077   3697   3840    295     99    -17       C  
ATOM   7260  CG  ASN B 298     -13.540  20.291  46.047  1.00 41.33           C  
ANISOU 7260  CG  ASN B 298     4789   5383   5533    297     91     -2       C  
ATOM   7261  OD1 ASN B 298     -13.352  20.759  44.926  1.00 38.07           O  
ANISOU 7261  OD1 ASN B 298     4402   4955   5109    275     80     11       O  
ATOM   7262  ND2 ASN B 298     -14.238  19.182  46.239  1.00 30.05           N  
ANISOU 7262  ND2 ASN B 298     3346   3961   4111    321     97     -5       N  
ATOM   7263  N   PRO B 299     -14.952  23.420  47.434  1.00 28.33           N  
ANISOU 7263  N   PRO B 299     3151   3662   3950    294     52    -21       N  
ATOM   7264  CA  PRO B 299     -15.989  24.348  46.940  1.00 28.14           C  
ANISOU 7264  CA  PRO B 299     3143   3593   3956    293     24    -16       C  
ATOM   7265  C   PRO B 299     -15.549  25.795  46.656  1.00 32.50           C  
ANISOU 7265  C   PRO B 299     3712   4126   4511    268     13    -10       C  
ATOM   7266  O   PRO B 299     -15.957  26.369  45.630  1.00 32.91           O  
ANISOU 7266  O   PRO B 299     3790   4147   4569    259    -13      6       O  
ATOM   7267  CB  PRO B 299     -17.042  24.312  48.041  1.00 29.53           C  
ANISOU 7267  CB  PRO B 299     3298   3751   4171    314     26    -36       C  
ATOM   7268  CG  PRO B 299     -16.899  22.931  48.632  1.00 33.92           C  
ANISOU 7268  CG  PRO B 299     3837   4341   4711    333     50    -45       C  
ATOM   7269  CD  PRO B 299     -15.474  22.505  48.471  1.00 29.37           C  
ANISOU 7269  CD  PRO B 299     3260   3806   4092    319     67    -37       C  
ATOM   7270  N   ILE B 300     -14.733  26.383  47.524  1.00 28.92           N  
ANISOU 7270  N   ILE B 300     3246   3690   4053    257     32    -23       N  
ATOM   7271  CA  ILE B 300     -14.314  27.774  47.338  1.00 29.14           C  
ANISOU 7271  CA  ILE B 300     3286   3700   4085    235     27    -21       C  
ATOM   7272  C   ILE B 300     -13.494  27.938  46.063  1.00 33.48           C  
ANISOU 7272  C   ILE B 300     3867   4251   4605    213     24     -2       C  
ATOM   7273  O   ILE B 300     -13.693  28.886  45.312  1.00 34.04           O  
ANISOU 7273  O   ILE B 300     3962   4290   4681    199      6     10       O  
ATOM   7274  CB  ILE B 300     -13.508  28.318  48.532  1.00 32.60           C  
ANISOU 7274  CB  ILE B 300     3703   4159   4522    226     51    -40       C  
ATOM   7275  CG1 ILE B 300     -14.373  28.365  49.794  1.00 32.93           C  
ANISOU 7275  CG1 ILE B 300     3723   4193   4596    241     55    -60       C  
ATOM   7276  CG2 ILE B 300     -13.026  29.738  48.246  1.00 34.32           C  
ANISOU 7276  CG2 ILE B 300     3934   4360   4745    203     49    -39       C  
ATOM   7277  CD1 ILE B 300     -13.627  28.913  51.022  1.00 39.28           C  
ANISOU 7277  CD1 ILE B 300     4510   5018   5397    231     77    -80       C  
ATOM   7278  N   LEU B 301     -12.586  27.011  45.798  1.00 29.63           N  
ANISOU 7278  N   LEU B 301     3377   3796   4084    209     43     -1       N  
ATOM   7279  CA  LEU B 301     -11.844  27.021  44.537  1.00 29.40           C  
ANISOU 7279  CA  LEU B 301     3379   3766   4026    185     46     13       C  
ATOM   7280  C   LEU B 301     -12.750  26.900  43.304  1.00 33.05           C  
ANISOU 7280  C   LEU B 301     3874   4197   4486    184     18     35       C  
ATOM   7281  O   LEU B 301     -12.330  27.215  42.189  1.00 33.06           O  
ANISOU 7281  O   LEU B 301     3912   4185   4464    160     14     49       O  
ATOM   7282  CB  LEU B 301     -10.785  25.907  44.515  1.00 29.30           C  
ANISOU 7282  CB  LEU B 301     3353   3792   3987    180     74      7       C  
ATOM   7283  CG  LEU B 301      -9.623  25.999  45.518  1.00 33.80           C  
ANISOU 7283  CG  LEU B 301     3896   4393   4555    176     99    -13       C  
ATOM   7284  CD1 LEU B 301      -8.612  24.879  45.249  1.00 33.65           C  
ANISOU 7284  CD1 LEU B 301     3866   4404   4517    169    122    -17       C  
ATOM   7285  CD2 LEU B 301      -8.955  27.375  45.438  1.00 36.38           C  
ANISOU 7285  CD2 LEU B 301     4235   4705   4883    152    105    -19       C  
ATOM   7286  N   TYR B 302     -13.982  26.442  43.479  1.00 28.63           N  
ANISOU 7286  N   TYR B 302     3305   3624   3950    209     -3     37       N  
ATOM   7287  CA  TYR B 302     -14.923  26.445  42.363  1.00 28.41           C  
ANISOU 7287  CA  TYR B 302     3307   3562   3925    210    -38     56       C  
ATOM   7288  C   TYR B 302     -15.736  27.757  42.259  1.00 33.23           C  
ANISOU 7288  C   TYR B 302     3931   4125   4568    209    -71     63       C  
ATOM   7289  O   TYR B 302     -16.513  27.927  41.317  1.00 32.79           O  
ANISOU 7289  O   TYR B 302     3905   4036   4519    208   -107     80       O  
ATOM   7290  CB  TYR B 302     -15.890  25.261  42.477  1.00 28.79           C  
ANISOU 7290  CB  TYR B 302     3336   3614   3987    238    -46     53       C  
ATOM   7291  CG  TYR B 302     -15.405  23.954  41.880  1.00 28.72           C  
ANISOU 7291  CG  TYR B 302     3331   3637   3945    236    -27     58       C  
ATOM   7292  CD1 TYR B 302     -14.961  23.897  40.552  1.00 30.55           C  
ANISOU 7292  CD1 TYR B 302     3601   3863   4143    209    -32     76       C  
ATOM   7293  CD2 TYR B 302     -15.448  22.767  42.617  1.00 28.36           C  
ANISOU 7293  CD2 TYR B 302     3250   3622   3903    258     -4     44       C  
ATOM   7294  CE1 TYR B 302     -14.552  22.702  39.982  1.00 29.71           C  
ANISOU 7294  CE1 TYR B 302     3496   3783   4010    204    -12     79       C  
ATOM   7295  CE2 TYR B 302     -15.041  21.582  42.060  1.00 28.91           C  
ANISOU 7295  CE2 TYR B 302     3319   3718   3947    255     14     49       C  
ATOM   7296  CZ  TYR B 302     -14.596  21.551  40.733  1.00 35.03           C  
ANISOU 7296  CZ  TYR B 302     4130   4488   4692    227     11     65       C  
ATOM   7297  OH  TYR B 302     -14.180  20.370  40.160  1.00 33.55           O  
ANISOU 7297  OH  TYR B 302     3941   4326   4482    221     33     68       O  
ATOM   7298  N   ALA B 303     -15.582  28.670  43.219  1.00 30.36           N  
ANISOU 7298  N   ALA B 303     3548   3758   4228    208    -61     49       N  
ATOM   7299  CA  ALA B 303     -16.392  29.903  43.236  1.00 30.50           C  
ANISOU 7299  CA  ALA B 303     3573   3731   4287    207    -90     53       C  
ATOM   7300  C   ALA B 303     -16.020  30.820  42.064  1.00 34.96           C  
ANISOU 7300  C   ALA B 303     4183   4269   4831    181   -108     75       C  
ATOM   7301  O   ALA B 303     -14.926  30.728  41.512  1.00 34.04           O  
ANISOU 7301  O   ALA B 303     4090   4173   4672    159    -87     81       O  
ATOM   7302  CB  ALA B 303     -16.243  30.643  44.575  1.00 31.10           C  
ANISOU 7302  CB  ALA B 303     3615   3812   4391    208    -68     30       C  
ATOM   7303  N   PHE B 304     -16.957  31.674  41.668  1.00 32.14           N  
ANISOU 7303  N   PHE B 304     3841   3864   4508    182   -147     87       N  
ATOM   7304  CA  PHE B 304     -16.693  32.740  40.692  1.00 32.49           C  
ANISOU 7304  CA  PHE B 304     3931   3876   4538    158   -167    109       C  
ATOM   7305  C   PHE B 304     -16.124  32.272  39.343  1.00 37.36           C  
ANISOU 7305  C   PHE B 304     4600   4498   5099    137   -171    131       C  
ATOM   7306  O   PHE B 304     -15.518  33.055  38.642  1.00 36.61           O  
ANISOU 7306  O   PHE B 304     4544   4386   4979    111   -170    144       O  
ATOM   7307  CB  PHE B 304     -15.723  33.769  41.281  1.00 34.25           C  
ANISOU 7307  CB  PHE B 304     4145   4108   4759    140   -133     97       C  
ATOM   7308  CG  PHE B 304     -16.192  34.411  42.553  1.00 35.39           C  
ANISOU 7308  CG  PHE B 304     4245   4246   4956    152   -126     76       C  
ATOM   7309  CD1 PHE B 304     -15.606  34.078  43.768  1.00 37.90           C  
ANISOU 7309  CD1 PHE B 304     4522   4604   5273    157    -85     50       C  
ATOM   7310  CD2 PHE B 304     -17.198  35.373  42.535  1.00 37.30           C  
ANISOU 7310  CD2 PHE B 304     4485   4438   5249    156   -159     83       C  
ATOM   7311  CE1 PHE B 304     -16.023  34.681  44.948  1.00 38.39           C  
ANISOU 7311  CE1 PHE B 304     4547   4660   5381    164    -76     29       C  
ATOM   7312  CE2 PHE B 304     -17.627  35.981  43.717  1.00 39.70           C  
ANISOU 7312  CE2 PHE B 304     4746   4732   5605    163   -147     61       C  
ATOM   7313  CZ  PHE B 304     -17.042  35.632  44.920  1.00 37.43           C  
ANISOU 7313  CZ  PHE B 304     4423   4488   5312    166   -104     33       C  
ATOM   7314  N   LEU B 305     -16.330  31.013  38.971  1.00 35.22           N  
ANISOU 7314  N   LEU B 305     4330   4245   4809    147   -173    133       N  
ATOM   7315  CA  LEU B 305     -15.921  30.521  37.648  1.00 35.27           C  
ANISOU 7315  CA  LEU B 305     4386   4252   4763    124   -178    153       C  
ATOM   7316  C   LEU B 305     -16.598  31.314  36.551  1.00 39.52           C  
ANISOU 7316  C   LEU B 305     4977   4737   5301    113   -229    180       C  
ATOM   7317  O   LEU B 305     -17.822  31.379  36.509  1.00 39.50           O  
ANISOU 7317  O   LEU B 305     4968   4704   5337    135   -275    187       O  
ATOM   7318  CB  LEU B 305     -16.291  29.052  37.478  1.00 35.18           C  
ANISOU 7318  CB  LEU B 305     4361   4264   4741    140   -177    150       C  
ATOM   7319  CG  LEU B 305     -15.296  28.025  38.019  1.00 39.71           C  
ANISOU 7319  CG  LEU B 305     4904   4891   5291    139   -125    131       C  
ATOM   7320  CD1 LEU B 305     -15.924  26.612  38.031  1.00 39.47           C  
ANISOU 7320  CD1 LEU B 305     4853   4881   5265    163   -127    127       C  
ATOM   7321  CD2 LEU B 305     -14.047  28.069  37.170  1.00 42.67           C  
ANISOU 7321  CD2 LEU B 305     5320   5277   5618    101    -96    138       C  
ATOM   7322  N   GLY B 306     -15.804  31.909  35.665  1.00 36.10           N  
ANISOU 7322  N   GLY B 306     4597   4291   4826     79   -222    195       N  
ATOM   7323  CA  GLY B 306     -16.334  32.750  34.589  1.00 36.44           C  
ANISOU 7323  CA  GLY B 306     4700   4283   4863     64   -271    225       C  
ATOM   7324  C   GLY B 306     -16.786  34.149  35.006  1.00 40.94           C  
ANISOU 7324  C   GLY B 306     5264   4814   5479     70   -296    229       C  
ATOM   7325  O   GLY B 306     -17.307  34.893  34.193  1.00 40.39           O  
ANISOU 7325  O   GLY B 306     5239   4697   5410     61   -342    254       O  
ATOM   7326  N   ALA B 307     -16.611  34.507  36.279  1.00 38.28           N  
ANISOU 7326  N   ALA B 307     4870   4495   5180     84   -266    204       N  
ATOM   7327  CA  ALA B 307     -16.890  35.871  36.738  1.00 38.37           C  
ANISOU 7327  CA  ALA B 307     4871   4474   5236     85   -278    205       C  
ATOM   7328  C   ALA B 307     -15.831  36.842  36.208  1.00 42.04           C  
ANISOU 7328  C   ALA B 307     5379   4928   5664     51   -253    213       C  
ATOM   7329  O   ALA B 307     -14.666  36.469  36.045  1.00 41.40           O  
ANISOU 7329  O   ALA B 307     5313   4881   5537     31   -207    203       O  
ATOM   7330  CB  ALA B 307     -16.922  35.920  38.261  1.00 38.73           C  
ANISOU 7330  CB  ALA B 307     4846   4544   5327    105   -246    173       C  
ATOM   7331  N   LYS B 308     -16.242  38.077  35.937  1.00 38.51           N  
ANISOU 7331  N   LYS B 308     4954   4434   5243     45   -283    229       N  
ATOM   7332  CA  LYS B 308     -15.299  39.159  35.665  1.00 38.49           C  
ANISOU 7332  CA  LYS B 308     4985   4421   5219     16   -255    232       C  
ATOM   7333  C   LYS B 308     -15.416  40.237  36.739  1.00 41.81           C  
ANISOU 7333  C   LYS B 308     5357   4833   5696     26   -241    216       C  
ATOM   7334  O   LYS B 308     -16.501  40.768  36.945  1.00 41.52           O  
ANISOU 7334  O   LYS B 308     5303   4759   5715     42   -283    224       O  
ATOM   7335  CB  LYS B 308     -15.551  39.758  34.277  1.00 41.54           C  
ANISOU 7335  CB  LYS B 308     5451   4755   5577     -5   -298    269       C  
ATOM   7336  CG  LYS B 308     -15.103  38.883  33.106  1.00 58.33           C  
ANISOU 7336  CG  LYS B 308     7639   6889   7633    -28   -297    283       C  
ATOM   7337  CD  LYS B 308     -13.594  38.524  33.164  1.00 69.28           C  
ANISOU 7337  CD  LYS B 308     9032   8319   8973    -54   -223    260       C  
ATOM   7338  CE  LYS B 308     -13.182  37.666  31.965  1.00 82.90           C  
ANISOU 7338  CE  LYS B 308    10819  10047  10633    -81   -219    273       C  
ATOM   7339  NZ  LYS B 308     -13.454  38.334  30.643  1.00 92.75           N  
ANISOU 7339  NZ  LYS B 308    12155  11240  11845   -107   -259    308       N  
ATOM   7340  N   PHE B 309     -14.314  40.559  37.422  1.00 37.78           N  
ANISOU 7340  N   PHE B 309     4823   4355   5176     14   -182    191       N  
ATOM   7341  CA  PHE B 309     -14.346  41.573  38.481  1.00 37.48           C  
ANISOU 7341  CA  PHE B 309     4738   4313   5190     19   -163    172       C  
ATOM   7342  C   PHE B 309     -14.068  42.976  37.932  1.00 42.11           C  
ANISOU 7342  C   PHE B 309     5363   4860   5779     -3   -163    187       C  
ATOM   7343  O   PHE B 309     -13.005  43.540  38.171  1.00 41.62           O  
ANISOU 7343  O   PHE B 309     5300   4814   5701    -21   -114    170       O  
ATOM   7344  CB  PHE B 309     -13.367  41.225  39.616  1.00 38.96           C  
ANISOU 7344  CB  PHE B 309     4875   4557   5372     20   -103    135       C  
ATOM   7345  CG  PHE B 309     -13.662  39.913  40.290  1.00 40.25           C  
ANISOU 7345  CG  PHE B 309     4998   4758   5537     43   -102    120       C  
ATOM   7346  CD1 PHE B 309     -14.429  39.864  41.444  1.00 43.04           C  
ANISOU 7346  CD1 PHE B 309     5295   5116   5942     65   -106    103       C  
ATOM   7347  CD2 PHE B 309     -13.182  38.716  39.757  1.00 42.53           C  
ANISOU 7347  CD2 PHE B 309     5307   5076   5777     40    -94    123       C  
ATOM   7348  CE1 PHE B 309     -14.725  38.634  42.061  1.00 43.64           C  
ANISOU 7348  CE1 PHE B 309     5339   5225   6019     86   -103     89       C  
ATOM   7349  CE2 PHE B 309     -13.465  37.491  40.369  1.00 45.12           C  
ANISOU 7349  CE2 PHE B 309     5598   5438   6108     62    -91    110       C  
ATOM   7350  CZ  PHE B 309     -14.238  37.449  41.518  1.00 42.97           C  
ANISOU 7350  CZ  PHE B 309     5273   5169   5885     86    -97     94       C  
ATOM   7351  N   LYS B 310     -15.040  43.547  37.223  1.00 39.83           N  
ANISOU 7351  N   LYS B 310     5106   4516   5512      0   -220    217       N  
ATOM   7352  CA  LYS B 310     -14.867  44.859  36.581  1.00 40.36           C  
ANISOU 7352  CA  LYS B 310     5217   4538   5580    -21   -226    237       C  
ATOM   7353  C   LYS B 310     -15.934  45.908  36.940  1.00 45.73           C  
ANISOU 7353  C   LYS B 310     5870   5169   6336     -8   -265    246       C  
ATOM   7354  O   LYS B 310     -16.061  46.910  36.246  1.00 45.89           O  
ANISOU 7354  O   LYS B 310     5932   5142   6360    -21   -288    271       O  
ATOM   7355  CB  LYS B 310     -14.812  44.687  35.056  1.00 43.12           C  
ANISOU 7355  CB  LYS B 310     5654   4857   5872    -40   -259    272       C  
ATOM   7356  CG  LYS B 310     -13.704  43.732  34.578  1.00 58.99           C  
ANISOU 7356  CG  LYS B 310     7697   6908   7809    -60   -217    262       C  
ATOM   7357  CD  LYS B 310     -13.373  43.910  33.081  1.00 70.34           C  
ANISOU 7357  CD  LYS B 310     9231   8311   9185    -91   -231    292       C  
ATOM   7358  CE  LYS B 310     -14.546  43.497  32.163  1.00 82.24           C  
ANISOU 7358  CE  LYS B 310    10781   9781  10687    -83   -309    329       C  
ATOM   7359  NZ  LYS B 310     -14.389  43.982  30.746  1.00 93.31           N  
ANISOU 7359  NZ  LYS B 310    12283  11136  12035   -115   -334    363       N  
ATOM   7360  N   THR B 311     -16.680  45.704  38.021  1.00 43.05           N  
ANISOU 7360  N   THR B 311     5461   4838   6057     16   -269    226       N  
ATOM   7361  CA  THR B 311     -17.773  46.613  38.364  1.00 43.58           C  
ANISOU 7361  CA  THR B 311     5498   4856   6205     27   -306    232       C  
ATOM   7362  C   THR B 311     -17.556  47.332  39.702  1.00 49.63           C  
ANISOU 7362  C   THR B 311     6197   5638   7023     26   -256    198       C  
ATOM   7363  O   THR B 311     -17.475  46.699  40.768  1.00 48.79           O  
ANISOU 7363  O   THR B 311     6037   5573   6927     37   -224    166       O  
ATOM   7364  CB  THR B 311     -19.117  45.871  38.391  1.00 47.99           C  
ANISOU 7364  CB  THR B 311     6035   5392   6807     53   -363    237       C  
ATOM   7365  OG1 THR B 311     -19.341  45.264  37.111  1.00 46.35           O  
ANISOU 7365  OG1 THR B 311     5891   5168   6553     52   -412    269       O  
ATOM   7366  CG2 THR B 311     -20.272  46.839  38.718  1.00 46.32           C  
ANISOU 7366  CG2 THR B 311     5789   5122   6690     63   -401    241       C  
ATOM   7367  N   SER B 312     -17.456  48.658  39.635  1.00 48.09           N  
ANISOU 7367  N   SER B 312     6006   5409   6856     12   -250    205       N  
ATOM   7368  CA  SER B 312     -17.324  49.486  40.826  1.00 48.44           C  
ANISOU 7368  CA  SER B 312     5989   5461   6954      8   -205    175       C  
ATOM   7369  C   SER B 312     -18.598  50.306  41.021  1.00 54.64           C  
ANISOU 7369  C   SER B 312     6744   6186   7831     17   -247    183       C  
ATOM   7370  O   SER B 312     -19.486  50.306  40.156  1.00 54.43           O  
ANISOU 7370  O   SER B 312     6749   6109   7823     25   -313    214       O  
ATOM   7371  CB  SER B 312     -16.092  50.392  40.720  1.00 51.15           C  
ANISOU 7371  CB  SER B 312     6352   5817   7264    -16   -153    169       C  
ATOM   7372  OG  SER B 312     -16.237  51.349  39.692  1.00 59.62           O  
ANISOU 7372  OG  SER B 312     7478   6837   8339    -28   -182    202       O  
ATOM   7373  N   ALA B 313     -18.687  50.987  42.163  1.00 52.58           N  
ANISOU 7373  N   ALA B 313     6422   5927   7629     13   -209    153       N  
ATOM   7374  CA  ALA B 313     -19.858  51.799  42.514  1.00 53.53           C  
ANISOU 7374  CA  ALA B 313     6501   5989   7847     17   -238    153       C  
ATOM   7375  C   ALA B 313     -20.192  52.810  41.423  1.00 59.94           C  
ANISOU 7375  C   ALA B 313     7358   6738   8680     11   -285    193       C  
ATOM   7376  O   ALA B 313     -21.352  53.152  41.223  1.00 59.31           O  
ANISOU 7376  O   ALA B 313     7265   6598   8671     20   -340    207       O  
ATOM   7377  CB  ALA B 313     -19.637  52.514  43.852  1.00 54.07           C  
ANISOU 7377  CB  ALA B 313     6504   6074   7965      6   -177    114       C  
ATOM   7378  N   GLN B 314     -19.160  53.272  40.723  1.00 59.17           N  
ANISOU 7378  N   GLN B 314     7313   6650   8518     -7   -264    209       N  
ATOM   7379  CA  GLN B 314     -19.320  54.207  39.604  1.00 60.70           C  
ANISOU 7379  CA  GLN B 314     7563   6785   8714    -16   -305    250       C  
ATOM   7380  C   GLN B 314     -19.891  53.484  38.369  1.00 67.71           C  
ANISOU 7380  C   GLN B 314     8516   7645   9567     -5   -380    289       C  
ATOM   7381  O   GLN B 314     -20.689  54.053  37.621  1.00 67.82           O  
ANISOU 7381  O   GLN B 314     8558   7594   9617     -2   -444    323       O  
ATOM   7382  CB  GLN B 314     -17.979  54.875  39.257  1.00 62.04           C  
ANISOU 7382  CB  GLN B 314     7774   6976   8823    -39   -250    251       C  
ATOM   7383  CG  GLN B 314     -17.136  55.381  40.457  1.00 75.69           C  
ANISOU 7383  CG  GLN B 314     9444   8749  10566    -51   -167    207       C  
ATOM   7384  CD  GLN B 314     -17.682  56.636  41.119  1.00 94.81           C  
ANISOU 7384  CD  GLN B 314    11811  11132  13078    -56   -156    198       C  
ATOM   7385  OE1 GLN B 314     -18.842  57.011  40.925  1.00 91.11           O  
ANISOU 7385  OE1 GLN B 314    11331  10605  12680    -47   -212    217       O  
ATOM   7386  NE2 GLN B 314     -16.835  57.299  41.903  1.00 85.91           N  
ANISOU 7386  NE2 GLN B 314    10649  10036  11955    -71    -85    166       N  
ATOM   7387  N   HIS B 315     -19.498  52.224  38.178  1.00 66.05           N  
ANISOU 7387  N   HIS B 315     8326   7481   9288      0   -375    284       N  
ATOM   7388  CA  HIS B 315     -19.988  51.406  37.053  1.00 67.00           C  
ANISOU 7388  CA  HIS B 315     8506   7583   9370      9   -441    317       C  
ATOM   7389  C   HIS B 315     -21.421  50.864  37.257  1.00 72.54           C  
ANISOU 7389  C   HIS B 315     9168   8252  10140     35   -503    317       C  
ATOM   7390  O   HIS B 315     -21.977  50.223  36.361  1.00 72.17           O  
ANISOU 7390  O   HIS B 315     9165   8185  10072     44   -564    343       O  
ATOM   7391  CB  HIS B 315     -19.022  50.240  36.766  1.00 67.59           C  
ANISOU 7391  CB  HIS B 315     8615   7718   9349      2   -407    309       C  
ATOM   7392  CG  HIS B 315     -18.659  50.096  35.319  1.00 71.59           C  
ANISOU 7392  CG  HIS B 315     9216   8206   9780    -14   -437    346       C  
ATOM   7393  ND1 HIS B 315     -17.369  49.847  34.898  1.00 73.39           N  
ANISOU 7393  ND1 HIS B 315     9490   8471   9924    -37   -385    341       N  
ATOM   7394  CD2 HIS B 315     -19.410  50.190  34.195  1.00 73.92           C  
ANISOU 7394  CD2 HIS B 315     9570   8447  10071    -13   -513    387       C  
ATOM   7395  CE1 HIS B 315     -17.344  49.777  33.578  1.00 73.23           C  
ANISOU 7395  CE1 HIS B 315     9555   8420   9848    -51   -424    377       C  
ATOM   7396  NE2 HIS B 315     -18.569  49.986  33.127  1.00 73.91           N  
ANISOU 7396  NE2 HIS B 315     9652   8452   9979    -37   -504    407       N  
ATOM   7397  N   ALA B 316     -21.998  51.085  38.439  1.00 70.29           N  
ANISOU 7397  N   ALA B 316     8804   7964   9937     46   -484    285       N  
ATOM   7398  CA  ALA B 316     -23.440  50.883  38.647  1.00 70.76           C  
ANISOU 7398  CA  ALA B 316     8824   7977  10085     68   -542    283       C  
ATOM   7399  C   ALA B 316     -24.202  52.167  38.293  1.00 76.52           C  
ANISOU 7399  C   ALA B 316     9552   8629  10893     65   -590    306       C  
ATOM   7400  O   ALA B 316     -25.425  52.150  38.127  1.00 76.33           O  
ANISOU 7400  O   ALA B 316     9510   8549  10943     82   -655    313       O  
ATOM   7401  CB  ALA B 316     -23.730  50.467  40.087  1.00 70.98           C  
ANISOU 7401  CB  ALA B 316     8769   8034  10165     78   -495    235       C  
ATOM   7402  N   LEU B 317     -23.463  53.271  38.179  1.00 74.24           N  
ANISOU 7402  N   LEU B 317     9282   8334  10591     44   -558    316       N  
ATOM   7403  CA  LEU B 317     -24.026  54.580  37.858  1.00 75.08           C  
ANISOU 7403  CA  LEU B 317     9389   8369  10769     38   -596    339       C  
ATOM   7404  C   LEU B 317     -23.662  55.075  36.443  1.00 79.67           C  
ANISOU 7404  C   LEU B 317    10064   8918  11289     26   -639    389       C  
ATOM   7405  O   LEU B 317     -24.318  55.982  35.925  1.00 79.96           O  
ANISOU 7405  O   LEU B 317    10115   8885  11380     26   -694    418       O  
ATOM   7406  CB  LEU B 317     -23.565  55.602  38.910  1.00 75.15           C  
ANISOU 7406  CB  LEU B 317     9340   8389  10824     23   -524    309       C  
ATOM   7407  CG  LEU B 317     -24.073  55.387  40.349  1.00 79.56           C  
ANISOU 7407  CG  LEU B 317     9806   8963  11460     29   -484    260       C  
ATOM   7408  CD1 LEU B 317     -23.057  55.860  41.376  1.00 79.35           C  
ANISOU 7408  CD1 LEU B 317     9742   8989  11419     10   -391    225       C  
ATOM   7409  CD2 LEU B 317     -25.427  56.070  40.571  1.00 82.55           C  
ANISOU 7409  CD2 LEU B 317    10135   9264  11966     37   -532    259       C  
ATOM   7410  N   THR B 318     -22.636  54.481  35.825  1.00 75.96           N  
ANISOU 7410  N   THR B 318     9659   8494  10708     14   -614    398       N  
ATOM   7411  CA  THR B 318     -22.128  54.933  34.516  1.00 76.16           C  
ANISOU 7411  CA  THR B 318     9781   8492  10663     -4   -640    442       C  
ATOM   7412  C   THR B 318     -21.586  53.771  33.669  1.00 79.22           C  
ANISOU 7412  C   THR B 318    10238   8917  10945     -9   -647    454       C  
ATOM   7413  O   THR B 318     -21.556  52.628  34.119  1.00 78.18           O  
ANISOU 7413  O   THR B 318    10077   8834  10795      3   -629    430       O  
ATOM   7414  CB  THR B 318     -21.000  55.992  34.697  1.00 85.03           C  
ANISOU 7414  CB  THR B 318    10916   9630  11764    -28   -567    434       C  
ATOM   7415  OG1 THR B 318     -19.974  55.471  35.552  1.00 84.33           O  
ANISOU 7415  OG1 THR B 318    10791   9617  11634    -34   -480    392       O  
ATOM   7416  CG2 THR B 318     -21.548  57.282  35.304  1.00 84.09           C  
ANISOU 7416  CG2 THR B 318    10740   9464  11748    -28   -567    430       C  
ATOM   7417  N   SER B 319     -21.169  54.067  32.440  1.00 75.96           N  
ANISOU 7417  N   SER B 319     9920   8478  10463    -28   -671    492       N  
ATOM   7418  CA  SER B 319     -20.487  53.079  31.590  1.00103.33           C  
ANISOU 7418  CA  SER B 319    13460  11979  13824    -42   -665    502       C  
ATOM   7419  C   SER B 319     -19.020  52.963  31.997  1.00129.61           C  
ANISOU 7419  C   SER B 319    16787  15369  17089    -62   -565    471       C  
ATOM   7420  CB  SER B 319     -20.577  53.464  30.110  1.00107.28           C  
ANISOU 7420  CB  SER B 319    14068  12423  14270    -60   -726    553       C  
ATOM   7421  OG  SER B 319     -21.922  53.516  29.673  1.00115.99           O  
ANISOU 7421  OG  SER B 319    15175  13467  15430    -40   -826    583       O  
TER    7422      SER B 319                                                      
HETATM 7423  C1  ITD A1500      16.263  -6.280  67.102  1.00 44.81           C  
HETATM 7424  N1  ITD A1500      17.926  -7.984  67.615  1.00 58.38           N  
HETATM 7425  S1  ITD A1500      18.853  -9.843  69.494  1.00 45.52           S  
HETATM 7426  C2  ITD A1500      17.661  -6.546  67.643  1.00 44.41           C  
HETATM 7427  N2  ITD A1500      18.209  -7.382  69.701  1.00 40.65           N  
HETATM 7428  S2  ITD A1500      20.266  -6.133  72.241  1.00 53.27           S  
HETATM 7429  C3  ITD A1500      18.729  -5.812  66.836  1.00 26.95           C  
HETATM 7430  N3  ITD A1500      20.721  -8.189  73.690  1.00115.79           N  
HETATM 7431  C4  ITD A1500      18.229  -8.379  68.859  1.00 88.49           C  
HETATM 7432  N4  ITD A1500      22.509  -7.497  72.324  1.00137.15           N  
HETATM 7433  C5  ITD A1500      18.981  -9.093  71.061  1.00 50.93           C  
HETATM 7434  C6  ITD A1500      17.752  -6.132  69.120  1.00 58.02           C  
HETATM 7435  C7  ITD A1500      18.588  -7.737  70.955  1.00153.64           C  
HETATM 7436  C8  ITD A1500      18.621  -6.760  72.105  1.00112.42           C  
HETATM 7437  C9  ITD A1500      21.255  -7.369  72.779  1.00 22.70           C  
HETATM 7438  C10 ITD A1500      21.301  -9.340  74.366  1.00 15.76           C  
HETATM 7439  C11 ITD A1500      22.147  -9.006  75.586  1.00 32.96           C  
HETATM 7440  C12 ITD A1500      22.268 -10.246  76.470  1.00 26.94           C  
HETATM 7441  C13 ITD A1500      22.821 -11.453  75.710  1.00 15.46           C  
HETATM 7442  C14 ITD A1500      22.144 -11.682  74.350  1.00 27.46           C  
HETATM 7443  C15 ITD A1500      21.967 -10.410  73.516  1.00 37.27           C  
HETATM 7444  C16 ITD A1500      22.954  -7.432  70.931  1.00 31.99           C  
HETATM 7445  C17 ITD A1500      21.895  -7.605  69.845  1.00 39.16           C  
HETATM 7446  C18 ITD A1500      22.552  -7.752  68.473  1.00 99.65           C  
HETATM 7447  C19 ITD A1500      23.512  -6.603  68.157  1.00 26.16           C  
HETATM 7448  C20 ITD A1500      24.516  -6.362  69.280  1.00 24.74           C  
HETATM 7449  C21 ITD A1500      23.828  -6.218  70.637  1.00 40.40           C  
HETATM 7450  C10 OLC A1600      37.080  -4.797  63.675  1.00 50.57           C  
HETATM 7451  C9  OLC A1600      36.845  -4.793  62.362  1.00 72.19           C  
HETATM 7452  C11 OLC A1600      36.882  -3.558  64.521  1.00 49.14           C  
HETATM 7453  C8  OLC A1600      36.372  -3.551  61.640  1.00 89.87           C  
HETATM 7454  C24 OLC A1600      37.479  -2.016  70.028  1.00 80.89           C  
HETATM 7455  C7  OLC A1600      37.568  -2.656  61.331  1.00115.37           C  
HETATM 7456  C6  OLC A1600      37.136  -1.214  61.083  1.00 60.17           C  
HETATM 7457  C5  OLC A1600      37.544  -0.310  62.242  1.00 79.40           C  
HETATM 7458  C4  OLC A1600      36.345   0.043  63.116  1.00 43.92           C  
HETATM 7459  C3  OLC A1600      36.787   0.738  64.400  1.00 62.15           C  
HETATM 7460  C2  OLC A1600      36.819  -0.220  65.590  1.00 58.12           C  
HETATM 7461  C21 OLC A1600      36.515   0.229  69.287  1.00 46.84           C  
HETATM 7462  C1  OLC A1600      36.456   0.504  66.871  1.00 49.09           C  
HETATM 7463  C22 OLC A1600      37.165  -0.574  70.415  1.00112.06           C  
HETATM 7464  O19 OLC A1600      35.900   1.594  66.896  1.00 51.99           O  
HETATM 7465  O25 OLC A1600      38.086  -2.680  71.145  1.00 48.27           O  
HETATM 7466  O23 OLC A1600      38.341   0.092  70.890  1.00 49.29           O  
HETATM 7467  O20 OLC A1600      36.842  -0.231  67.970  1.00 79.01           O  
HETATM 7468  C10 OLC A1603       1.525  -3.140  67.522  1.00 36.35           C  
HETATM 7469  C9  OLC A1603       2.203  -2.658  68.565  1.00 48.36           C  
HETATM 7470  C11 OLC A1603       2.106  -3.214  66.130  1.00 47.17           C  
HETATM 7471  C8  OLC A1603       3.623  -2.152  68.452  1.00 23.47           C  
HETATM 7472  C24 OLC A1603      13.486  -7.605  72.004  1.00 79.20           C  
HETATM 7473  C12 OLC A1603       1.038  -2.787  65.128  1.00 61.55           C  
HETATM 7474  C7  OLC A1603       4.325  -2.295  69.802  1.00 77.77           C  
HETATM 7475  C15 OLC A1603       0.064  -2.915  61.854  1.00 24.04           C  
HETATM 7476  C13 OLC A1603       0.767  -3.866  64.087  1.00 41.19           C  
HETATM 7477  C6  OLC A1603       4.473  -3.756  70.227  1.00 39.34           C  
HETATM 7478  C14 OLC A1603       1.226  -3.435  62.695  1.00 37.98           C  
HETATM 7479  C5  OLC A1603       5.830  -4.019  70.876  1.00 60.18           C  
HETATM 7480  C4  OLC A1603       6.327  -5.434  70.594  1.00 45.16           C  
HETATM 7481  C3  OLC A1603       7.461  -5.825  71.540  1.00 39.41           C  
HETATM 7482  C2  OLC A1603       8.405  -6.851  70.913  1.00 46.70           C  
HETATM 7483  C21 OLC A1603      11.366  -8.440  70.944  1.00 64.72           C  
HETATM 7484  C1  OLC A1603       9.827  -6.603  71.373  1.00 42.89           C  
HETATM 7485  C22 OLC A1603      12.641  -8.835  71.693  1.00 51.30           C  
HETATM 7486  O19 OLC A1603      10.350  -5.500  71.370  1.00134.91           O  
HETATM 7487  O25 OLC A1603      14.876  -7.919  71.850  1.00 87.15           O  
HETATM 7488  O23 OLC A1603      12.353  -9.562  72.895  1.00 44.09           O  
HETATM 7489  O20 OLC A1603      10.423  -7.772  71.785  1.00 64.39           O  
HETATM 7490  C9  OLC A1604       1.633  -7.060  60.903  1.00 27.90           C  
HETATM 7491  C8  OLC A1604       2.342  -8.220  61.565  1.00 57.24           C  
HETATM 7492  C24 OLC A1604      12.883  -7.465  57.614  1.00 44.84           C  
HETATM 7493  C7  OLC A1604       2.889  -7.793  62.922  1.00 43.13           C  
HETATM 7494  C6  OLC A1604       4.170  -8.550  63.260  1.00 29.72           C  
HETATM 7495  C5  OLC A1604       5.347  -8.025  62.445  1.00 45.72           C  
HETATM 7496  C4  OLC A1604       6.668  -8.589  62.953  1.00 37.10           C  
HETATM 7497  C3  OLC A1604       7.828  -7.618  62.747  1.00 32.59           C  
HETATM 7498  C2  OLC A1604       8.116  -7.349  61.276  1.00 57.48           C  
HETATM 7499  C21 OLC A1604      11.448  -7.637  59.635  1.00 40.07           C  
HETATM 7500  C1  OLC A1604       9.570  -6.975  61.084  1.00150.54           C  
HETATM 7501  C22 OLC A1604      11.447  -7.476  58.117  1.00 74.41           C  
HETATM 7502  O19 OLC A1604      10.135  -6.094  61.715  1.00 60.78           O  
HETATM 7503  O25 OLC A1604      12.909  -7.406  56.184  1.00 28.80           O  
HETATM 7504  O23 OLC A1604      10.741  -8.553  57.492  1.00 26.78           O  
HETATM 7505  O20 OLC A1604      10.109  -7.773  60.106  1.00 97.44           O  
HETATM 7506  C1  OLA A1610      35.077 -15.714  77.072  1.00117.15           C  
HETATM 7507  O1  OLA A1610      34.349 -15.738  78.090  1.00 70.60           O  
HETATM 7508  O2  OLA A1610      36.262 -15.326  77.185  1.00 52.35           O  
HETATM 7509  C2  OLA A1610      34.528 -16.159  75.735  1.00 41.49           C  
HETATM 7510  C3  OLA A1610      35.299 -15.527  74.579  1.00 73.86           C  
HETATM 7511  C4  OLA A1610      34.385 -15.233  73.394  1.00 39.95           C  
HETATM 7512  C5  OLA A1610      33.839 -16.514  72.774  1.00 36.04           C  
HETATM 7513  C6  OLA A1610      34.164 -16.581  71.286  1.00 36.89           C  
HETATM 7514  C7  OLA A1610      33.071 -17.314  70.516  1.00 23.20           C  
HETATM 7515  C8  OLA A1610      33.002 -16.827  69.069  1.00 23.86           C  
HETATM 7516  C1  ITD B1500      -9.112  13.063  67.333  1.00 25.11           C  
HETATM 7517  N1  ITD B1500     -10.811  14.738  67.816  1.00 59.87           N  
HETATM 7518  S1  ITD B1500     -11.888  16.499  69.696  1.00 52.45           S  
HETATM 7519  C2  ITD B1500     -10.533  13.305  67.814  1.00 46.03           C  
HETATM 7520  N2  ITD B1500     -11.196  14.050  69.862  1.00 52.82           N  
HETATM 7521  S2  ITD B1500     -13.354  12.663  72.337  1.00 51.31           S  
HETATM 7522  C3  ITD B1500     -11.571  12.598  66.954  1.00 16.42           C  
HETATM 7523  N3  ITD B1500     -13.831  14.662  73.847  1.00 42.68           N  
HETATM 7524  C4  ITD B1500     -11.174  15.082  69.058  1.00 53.60           C  
HETATM 7525  N4  ITD B1500     -15.530  14.155  72.312  1.00 35.84           N  
HETATM 7526  C5  ITD B1500     -12.075  15.690  71.231  1.00 59.03           C  
HETATM 7527  C6  ITD B1500     -10.680  12.833  69.267  1.00 54.96           C  
HETATM 7528  C7  ITD B1500     -11.650  14.345  71.105  1.00 57.01           C  
HETATM 7529  C8  ITD B1500     -11.714  13.312  72.210  1.00 55.54           C  
HETATM 7530  C9  ITD B1500     -14.328  13.919  72.851  1.00114.42           C  
HETATM 7531  C10 ITD B1500     -14.375  15.836  74.514  1.00 30.42           C  
HETATM 7532  C11 ITD B1500     -15.253  15.526  75.723  1.00 26.42           C  
HETATM 7533  C12 ITD B1500     -15.495  16.816  76.507  1.00 25.63           C  
HETATM 7534  C13 ITD B1500     -16.166  17.874  75.631  1.00 34.54           C  
HETATM 7535  C14 ITD B1500     -15.383  18.155  74.349  1.00 27.07           C  
HETATM 7536  C15 ITD B1500     -14.993  16.886  73.592  1.00 34.27           C  
HETATM 7537  C16 ITD B1500     -15.938  13.980  70.920  1.00 38.43           C  
HETATM 7538  C17 ITD B1500     -14.854  14.186  69.863  1.00 24.29           C  
HETATM 7539  C18 ITD B1500     -15.428  14.078  68.450  1.00 50.92           C  
HETATM 7540  C19 ITD B1500     -16.189  12.769  68.236  1.00 35.19           C  
HETATM 7541  C20 ITD B1500     -17.294  12.596  69.275  1.00 28.81           C  
HETATM 7542  C21 ITD B1500     -16.749  12.703  70.700  1.00 15.67           C  
HETATM 7543  C8  OLC B1601     -17.285  28.123  52.010  1.00 55.05           C  
HETATM 7544  C24 OLC B1601     -19.701  24.378  40.466  1.00 26.24           C  
HETATM 7545  C7  OLC B1601     -17.858  27.231  50.913  1.00103.04           C  
HETATM 7546  C6  OLC B1601     -18.987  27.924  50.157  1.00 33.50           C  
HETATM 7547  C5  OLC B1601     -18.461  28.621  48.907  1.00 29.13           C  
HETATM 7548  C4  OLC B1601     -18.477  27.673  47.713  1.00 48.51           C  
HETATM 7549  C3  OLC B1601     -19.422  28.163  46.622  1.00 34.74           C  
HETATM 7550  C2  OLC B1601     -20.120  26.993  45.931  1.00 32.83           C  
HETATM 7551  C21 OLC B1601     -20.211  25.609  42.566  1.00 17.89           C  
HETATM 7552  C1  OLC B1601     -19.460  26.677  44.610  1.00 38.09           C  
HETATM 7553  C22 OLC B1601     -20.046  24.225  41.947  1.00 31.12           C  
HETATM 7554  O19 OLC B1601     -18.503  27.300  44.173  1.00 71.36           O  
HETATM 7555  O25 OLC B1601     -19.065  23.187  39.976  1.00 41.99           O  
HETATM 7556  O23 OLC B1601     -18.995  23.520  42.611  1.00 55.87           O  
HETATM 7557  O20 OLC B1601     -20.081  25.611  43.995  1.00 47.24           O  
HETATM 7558  C10 OLC B1602      13.229  20.360  66.762  1.00 62.98           C  
HETATM 7559  C9  OLC B1602      12.764  20.134  67.993  1.00 55.69           C  
HETATM 7560  C11 OLC B1602      14.653  20.807  66.515  1.00 52.15           C  
HETATM 7561  C8  OLC B1602      13.627  20.308  69.222  1.00 36.82           C  
HETATM 7562  C24 OLC B1602      14.354  26.189  79.223  1.00 68.21           C  
HETATM 7563  C12 OLC B1602      15.172  20.232  65.198  1.00 74.31           C  
HETATM 7564  C7  OLC B1602      12.741  20.497  70.449  1.00 39.93           C  
HETATM 7565  C15 OLC B1602      16.357  18.372  62.956  1.00 38.63           C  
HETATM 7566  C13 OLC B1602      15.490  18.742  65.296  1.00 29.98           C  
HETATM 7567  C6  OLC B1602      13.323  21.551  71.386  1.00 34.23           C  
HETATM 7568  C14 OLC B1602      15.266  18.031  63.967  1.00 53.06           C  
HETATM 7569  C5  OLC B1602      12.684  21.496  72.770  1.00 35.17           C  
HETATM 7570  C4  OLC B1602      12.572  22.891  73.379  1.00 36.61           C  
HETATM 7571  C3  OLC B1602      12.468  22.818  74.899  1.00 30.87           C  
HETATM 7572  C2  OLC B1602      11.926  24.123  75.470  1.00 50.89           C  
HETATM 7573  C21 OLC B1602      14.298  23.927  78.129  1.00104.54           C  
HETATM 7574  C1  OLC B1602      12.984  24.816  76.301  1.00134.73           C  
HETATM 7575  C22 OLC B1602      14.530  24.688  79.432  1.00125.38           C  
HETATM 7576  O19 OLC B1602      13.676  25.736  75.892  1.00 54.80           O  
HETATM 7577  O25 OLC B1602      15.136  26.906  80.186  1.00 56.63           O  
HETATM 7578  O23 OLC B1602      13.621  24.223  80.436  1.00 53.36           O  
HETATM 7579  O20 OLC B1602      13.035  24.269  77.556  1.00 48.54           O  
HETATM 7580  C1  OLA B1605     -29.448  21.832  76.893  1.00 83.13           C  
HETATM 7581  O1  OLA B1605     -29.422  22.218  78.082  1.00 59.03           O  
HETATM 7582  O2  OLA B1605     -30.295  20.973  76.559  1.00 69.93           O  
HETATM 7583  C2  OLA B1605     -28.479  22.412  75.885  1.00 49.29           C  
HETATM 7584  C3  OLA B1605     -28.035  21.359  74.874  1.00 62.00           C  
HETATM 7585  C4  OLA B1605     -28.250  21.844  73.445  1.00 39.29           C  
HETATM 7586  C5  OLA B1605     -26.925  22.189  72.774  1.00 38.73           C  
HETATM 7587  C6  OLA B1605     -27.108  23.282  71.726  1.00 32.88           C  
HETATM 7588  C7  OLA B1605     -26.253  23.022  70.492  1.00 54.14           C  
HETATM 7589  C8  OLA B1605     -25.766  24.324  69.867  1.00 59.39           C  
HETATM 7590  C9  OLA B1605     -24.685  24.018  68.855  1.00 38.48           C  
HETATM 7591  C10 OLA B1605     -23.961  24.977  68.270  1.00150.46           C  
HETATM 7592  C11 OLA B1605     -24.163  26.449  68.560  1.00 34.81           C  
HETATM 7593  C12 OLA B1605     -23.308  26.868  69.755  1.00 37.87           C  
HETATM 7594  C13 OLA B1605     -22.790  28.295  69.597  1.00 38.93           C  
HETATM 7595  C14 OLA B1605     -22.039  28.739  70.848  1.00 48.07           C  
HETATM 7596  C15 OLA B1605     -22.273  30.217  71.140  1.00 49.45           C  
HETATM 7597  C16 OLA B1605     -21.209  31.078  70.468  1.00 61.15           C  
HETATM 7598  C17 OLA B1605     -21.597  32.555  70.455  1.00 41.76           C  
HETATM 7599  C18 OLA B1605     -20.510  33.397  69.790  1.00 36.05           C  
HETATM 7600  C1  OLA B1606      -0.845  11.556  71.777  1.00154.24           C  
HETATM 7601  O1  OLA B1606      -0.592  12.756  71.524  1.00 63.48           O  
HETATM 7602  O2  OLA B1606      -1.827  11.291  72.507  1.00 54.23           O  
HETATM 7603  C2  OLA B1606       0.003  10.435  71.215  1.00125.80           C  
HETATM 7604  C3  OLA B1606       1.371  10.938  70.761  1.00 49.52           C  
HETATM 7605  C4  OLA B1606       2.404   9.818  70.816  1.00 32.98           C  
HETATM 7606  C5  OLA B1606       3.501  10.026  69.779  1.00 30.70           C  
HETATM 7607  C6  OLA B1606       3.170   9.321  68.471  1.00 38.06           C  
HETATM 7608  C7  OLA B1606       4.430   8.757  67.826  1.00 41.48           C  
HETATM 7609  C8  OLA B1606       4.827   9.543  66.584  1.00 50.26           C  
HETATM 7610  C9  OLA B1606       6.302   9.340  66.329  1.00 38.72           C  
HETATM 7611  C10 OLA B1606       6.849   9.568  65.135  1.00 86.74           C  
HETATM 7612  C11 OLA B1606       6.027  10.053  63.964  1.00 30.75           C  
HETATM 7613  C12 OLA B1606       6.821   9.908  62.668  1.00 60.46           C  
HETATM 7614  C13 OLA B1606       7.319  11.262  62.171  1.00 94.41           C  
HETATM 7615  C14 OLA B1606       8.682  11.143  61.496  1.00 55.14           C  
HETATM 7616  C15 OLA B1606       9.131  12.482  60.919  1.00 60.25           C  
HETATM 7617  C16 OLA B1606      10.101  12.296  59.755  1.00 50.66           C  
HETATM 7618  C17 OLA B1606       9.520  12.828  58.448  1.00 80.03           C  
HETATM 7619  C18 OLA B1606       9.930  11.959  57.263  1.00 55.38           C  
HETATM 7620  C1  OLA B1607     -18.229   9.617  40.878  1.00124.05           C  
HETATM 7621  O1  OLA B1607     -19.078   8.793  40.464  1.00 36.07           O  
HETATM 7622  O2  OLA B1607     -17.460  10.148  40.045  1.00 54.01           O  
HETATM 7623  C2  OLA B1607     -18.107   9.977  42.346  1.00 35.04           C  
HETATM 7624  C3  OLA B1607     -19.260   9.426  43.177  1.00 34.02           C  
HETATM 7625  C4  OLA B1607     -18.854   8.163  43.928  1.00 36.68           C  
HETATM 7626  C5  OLA B1607     -18.571   8.450  45.400  1.00 57.58           C  
HETATM 7627  C6  OLA B1607     -18.361   7.153  46.176  1.00 37.42           C  
HETATM 7628  C7  OLA B1607     -18.760   7.299  47.641  1.00 68.09           C  
HETATM 7629  C8  OLA B1607     -17.998   6.321  48.531  1.00 41.44           C  
HETATM 7630  C9  OLA B1607     -18.854   5.106  48.803  1.00 53.88           C  
HETATM 7631  C10 OLA B1607     -18.935   4.534  50.007  1.00155.36           C  
HETATM 7632  C11 OLA B1607     -18.175   5.050  51.208  1.00 52.54           C  
HETATM 7633  C12 OLA B1607     -19.160   5.578  52.245  1.00 60.14           C  
HETATM 7634  C13 OLA B1607     -18.724   5.202  53.655  1.00 75.43           C  
HETATM 7635  C14 OLA B1607     -19.680   5.763  54.702  1.00 65.21           C  
HETATM 7636  C15 OLA B1607     -19.173   5.483  56.112  1.00 54.69           C  
HETATM 7637  C16 OLA B1607     -20.260   5.752  57.146  1.00 58.13           C  
HETATM 7638  C17 OLA B1607     -20.453   4.546  58.057  1.00 65.21           C  
HETATM 7639  C18 OLA B1607     -21.409   4.875  59.197  1.00 36.93           C  
HETATM 7640  C1  OLA B1608      -5.935  27.586  59.339  1.00 72.46           C  
HETATM 7641  O1  OLA B1608      -5.748  27.298  60.542  1.00 41.32           O  
HETATM 7642  O2  OLA B1608      -7.020  27.268  58.802  1.00 61.58           O  
HETATM 7643  C2  OLA B1608      -4.870  28.314  58.551  1.00 76.03           C  
HETATM 7644  C3  OLA B1608      -4.758  27.717  57.152  1.00 52.82           C  
HETATM 7645  C4  OLA B1608      -4.481  28.790  56.107  1.00 49.20           C  
HETATM 7646  C5  OLA B1608      -5.139  28.441  54.778  1.00 31.96           C  
HETATM 7647  C6  OLA B1608      -5.564  29.701  54.036  1.00 54.55           C  
HETATM 7648  C7  OLA B1608      -6.186  29.348  52.692  1.00 37.84           C  
HETATM 7649  C8  OLA B1608      -5.097  29.111  51.653  1.00 40.21           C  
HETATM 7650  C9  OLA B1608      -5.526  29.705  50.330  1.00 27.59           C  
HETATM 7651  C10 OLA B1608      -4.969  29.283  49.197  1.00 61.00           C  
HETATM 7652  C1  OLA B1609      -4.726  14.719  57.615  1.00 51.02           C  
HETATM 7653  O1  OLA B1609      -5.624  14.162  56.929  1.00 22.80           O  
HETATM 7654  O2  OLA B1609      -3.810  15.337  57.035  1.00 30.49           O  
HETATM 7655  C2  OLA B1609      -4.727  14.659  59.126  1.00 36.94           C  
HETATM 7656  C3  OLA B1609      -3.598  13.755  59.614  1.00 62.93           C  
HETATM 7657  C4  OLA B1609      -2.961  14.269  60.903  1.00 54.20           C  
HETATM 7658  C5  OLA B1609      -1.462  13.976  60.927  1.00105.41           C  
HETATM 7659  C6  OLA B1609      -0.925  13.834  62.347  1.00 70.97           C  
HETATM 7660  C7  OLA B1609       0.031  14.966  62.719  1.00 36.69           C  
HETATM 7661  C8  OLA B1609       1.468  14.687  62.285  1.00 34.72           C  
HETATM 7662  C9  OLA B1609       2.431  15.035  63.401  1.00 36.91           C  
HETATM 7663  C10 OLA B1609       3.746  15.165  63.206  1.00 35.57           C  
HETATM 7664  C11 OLA B1609       4.386  14.972  61.849  1.00 36.08           C  
HETATM 7665  O   HOH A1612       9.293 -11.201  75.691  1.00 30.81           O  
HETATM 7666  O   HOH A1613      12.244  -8.814  38.379  1.00 27.84           O  
HETATM 7667  O   HOH A1614      10.690  11.349   3.304  1.00 40.61           O  
HETATM 7668  O   HOH A1615      15.420 -10.882  69.355  1.00 16.10           O  
HETATM 7669  O   HOH A1622     -13.288  -9.789   1.656  1.00 44.35           O  
HETATM 7670  O   HOH A1625       1.758 -16.648  11.428  1.00 27.75           O  
HETATM 7671  O   HOH A1626      13.528  -2.624  37.236  1.00 27.22           O  
HETATM 7672  O   HOH A1628      23.125 -11.474  70.508  1.00 28.33           O  
HETATM 7673  O   HOH A1629      24.772  -6.889  74.296  1.00 19.87           O  
HETATM 7674  O   HOH A1630      18.637  -4.143  77.676  1.00 26.56           O  
HETATM 7675  O   HOH A1631      -1.991 -13.485  26.242  1.00 39.12           O  
HETATM 7676  O   HOH A1632      11.880 -16.562  62.003  1.00 12.15           O  
HETATM 7677  O   HOH A1633      23.569 -43.788  44.227  1.00 22.21           O  
HETATM 7678  O   HOH A1638      -4.643 -14.260  78.910  1.00 31.08           O  
HETATM 7679  O   HOH A1639      21.958  -0.827  39.899  1.00 25.42           O  
HETATM 7680  O   HOH A1640       2.172  -0.726   5.979  1.00 34.17           O  
HETATM 7681  O   HOH A1644      -7.251 -19.854   2.014  1.00 50.68           O  
HETATM 7682  O   HOH A1645       5.870 -12.570  15.763  1.00 34.51           O  
HETATM 7683  O   HOH A1650      17.436  -9.171  74.545  1.00 31.61           O  
HETATM 7684  O   HOH A1651      18.577 -13.741  67.621  1.00 14.55           O  
HETATM 7685  O   HOH A1653       1.455  -7.460  28.347  1.00 31.74           O  
HETATM 7686  O   HOH A1654       3.357  23.238   7.314  1.00 39.03           O  
HETATM 7687  O   HOH A1655       1.648 -12.506   0.531  1.00 47.42           O  
HETATM 7688  O   HOH A1656      26.244 -40.467  34.828  1.00 32.49           O  
HETATM 7689  O   HOH A1664       0.546  21.979  13.142  1.00 41.50           O  
HETATM 7690  O   HOH A1668      21.401 -12.434  49.523  1.00 24.29           O  
HETATM 7691  O   HOH A1669      11.888  -1.305  70.803  1.00 35.00           O  
HETATM 7692  O   HOH A1670      14.290  -4.590  65.220  1.00 35.96           O  
HETATM 7693  O   HOH A1671       4.207  -7.794  21.468  1.00 42.66           O  
HETATM 7694  O   HOH A1672       3.359   0.953   8.727  1.00 43.29           O  
HETATM 7695  O   HOH A1674       4.969   4.334  22.460  1.00 51.15           O  
HETATM 7696  O   HOH A1675     -14.401   5.529  18.878  1.00 41.30           O  
HETATM 7697  O   HOH A1676      -8.929  -3.881  21.974  1.00 43.71           O  
HETATM 7698  O   HOH A1677      -8.380 -10.710   0.601  1.00 42.36           O  
HETATM 7699  O   HOH A1679       3.876 -15.406  12.637  1.00 32.09           O  
HETATM 7700  O   HOH A1680      -5.011 -21.036  10.459  1.00 34.38           O  
HETATM 7701  O   HOH A1681      33.906 -48.581  36.672  1.00 54.40           O  
HETATM 7702  O   HOH A1682       0.299  -3.234  27.435  1.00 30.17           O  
HETATM 7703  O   HOH A1693      25.993 -14.028  78.129  1.00 57.98           O  
HETATM 7704  O   HOH A1694      24.640 -36.507  36.474  1.00 29.28           O  
HETATM 7705  O   HOH A1695      19.340 -14.018  50.263  1.00 24.88           O  
HETATM 7706  O   HOH A1701      24.233  -6.274  62.562  1.00 17.36           O  
HETATM 7707  O   HOH A1704      33.428   0.631  69.417  1.00 32.52           O  
HETATM 7708  O   HOH A1705       0.087  18.755  19.426  1.00 39.36           O  
HETATM 7709  O   HOH A1710      21.061  -1.717  81.759  1.00 25.11           O  
HETATM 7710  O   HOH A1712     -12.831   2.433   8.744  1.00 43.81           O  
HETATM 7711  O   HOH A1713      17.639 -14.247  38.748  1.00 32.41           O  
HETATM 7712  O   HOH A1715      27.279   1.056  81.896  1.00 48.78           O  
HETATM 7713  O   HOH A1716      16.445   2.106  66.936  1.00 48.00           O  
HETATM 7714  O   HOH A1717       2.396 -16.835  26.901  1.00 50.32           O  
HETATM 7715  O   HOH A1718       3.670   4.572   1.482  1.00 57.97           O  
HETATM 7716  O   HOH A1719       8.449  23.895   6.777  1.00 38.25           O  
HETATM 7717  O   HOH A1720      19.004  -3.715  70.543  1.00 22.81           O  
HETATM 7718  O   HOH A1723     -14.931 -12.275   1.641  1.00 51.10           O  
HETATM 7719  O   HOH A1725      16.510 -38.440  39.455  1.00 43.51           O  
HETATM 7720  O   HOH A1727       5.209  -0.433   3.550  1.00 56.85           O  
HETATM 7721  O   HOH A1729       0.604 -14.670  25.539  1.00 41.85           O  
HETATM 7722  O   HOH A1734      26.391   3.317  80.419  1.00 55.31           O  
HETATM 7723  O   HOH A1735      30.293   1.078  80.542  1.00 49.04           O  
HETATM 7724  O   HOH A1736      20.559   5.587  74.554  1.00 41.16           O  
HETATM 7725  O   HOH A1739      17.697 -10.463  76.882  1.00 28.23           O  
HETATM 7726  O   HOH A1742       9.194 -11.770  82.152  1.00 42.16           O  
HETATM 7727  O   HOH A1743      13.171 -13.628  81.451  1.00 48.43           O  
HETATM 7728  O   HOH A1744      15.170  -4.115  70.661  1.00 40.40           O  
HETATM 7729  O   HOH A1747      14.643  -9.857  33.342  1.00 49.82           O  
HETATM 7730  O   HOH A1748       2.165 -12.747   4.887  1.00 52.32           O  
HETATM 7731  O   HOH A1749       9.547 -25.259  35.949  1.00 46.67           O  
HETATM 7732  O   HOH A1752      11.121 -13.470  86.722  1.00 47.16           O  
HETATM 7733  O   HOH A1753      33.262 -49.010  33.893  1.00 39.52           O  
HETATM 7734  O   HOH A1754      25.514  -6.375  32.681  1.00 48.05           O  
HETATM 7735  O   HOH A1755     -25.646 -20.434  12.488  1.00 51.56           O  
HETATM 7736  O   HOH A1756     -23.364 -26.006  19.170  1.00 47.22           O  
HETATM 7737  O   HOH A1758       4.123   4.380  79.892  1.00 32.86           O  
HETATM 7738  O   HOH B1611      -6.718   9.432  37.075  1.00 18.60           O  
HETATM 7739  O   HOH B1616     -12.691  21.993  36.060  1.00 38.78           O  
HETATM 7740  O   HOH B1617      15.612  15.999   5.609  1.00 40.70           O  
HETATM 7741  O   HOH B1618      19.979  28.077  15.658  1.00 25.75           O  
HETATM 7742  O   HOH B1619       1.755  25.697   7.897  1.00 37.10           O  
HETATM 7743  O   HOH B1620     -17.530  42.871  35.920  1.00 29.57           O  
HETATM 7744  O   HOH B1621     -16.291  17.872  70.449  1.00 29.49           O  
HETATM 7745  O   HOH B1623      -3.493  15.921  30.057  1.00 49.58           O  
HETATM 7746  O   HOH B1624     -11.478  31.259  44.954  1.00 30.29           O  
HETATM 7747  O   HOH B1627       7.088  51.693  14.609  1.00 42.44           O  
HETATM 7748  O   HOH B1634     -17.447  12.789  62.492  1.00 20.98           O  
HETATM 7749  O   HOH B1635      -4.818  23.202  62.089  1.00 11.17           O  
HETATM 7750  O   HOH B1636       9.749  20.240  15.519  1.00 31.94           O  
HETATM 7751  O   HOH B1637      -5.424  31.367  16.307  1.00 33.09           O  
HETATM 7752  O   HOH B1641     -11.540  20.433  67.523  1.00 23.02           O  
HETATM 7753  O   HOH B1642     -17.457  13.280  74.239  1.00 21.69           O  
HETATM 7754  O   HOH B1643      14.072  33.558   6.322  1.00 45.55           O  
HETATM 7755  O   HOH B1646      -8.334  17.238  69.411  1.00 17.00           O  
HETATM 7756  O   HOH B1648     -13.483   0.876  74.724  1.00 33.69           O  
HETATM 7757  O   HOH B1649      -5.639  15.768  38.244  1.00 23.89           O  
HETATM 7758  O   HOH B1652       1.663  20.733  32.215  1.00 43.10           O  
HETATM 7759  O   HOH B1657     -27.110   3.089  71.993  1.00 42.63           O  
HETATM 7760  O   HOH B1658     -25.372   9.296  75.254  1.00 33.55           O  
HETATM 7761  O  AHOH B1659     -17.772  -1.354  72.212  0.40 25.75           O  
HETATM 7762  O  BHOH B1659     -17.650  -3.214  72.253  0.60 20.76           O  
HETATM 7763  O   HOH B1660      -7.633  10.765  65.736  1.00 46.62           O  
HETATM 7764  O   HOH B1661      18.795  32.086  12.259  1.00 45.11           O  
HETATM 7765  O   HOH B1662       5.973  32.850  12.474  1.00 21.35           O  
HETATM 7766  O   HOH B1663       2.931  51.631  23.362  1.00 52.57           O  
HETATM 7767  O   HOH B1665       1.331  29.948  29.477  1.00 40.55           O  
HETATM 7768  O   HOH B1666     -11.992  16.491  59.064  1.00 25.32           O  
HETATM 7769  O   HOH B1667     -12.188  20.865  50.228  1.00 27.29           O  
HETATM 7770  O   HOH B1673      -3.116  23.692  12.853  1.00 41.50           O  
HETATM 7771  O   HOH B1683     -14.918   8.010  39.665  1.00 37.28           O  
HETATM 7772  O   HOH B1684     -14.534  18.915  49.172  1.00 27.72           O  
HETATM 7773  O   HOH B1685     -12.007  10.362  70.576  1.00 29.86           O  
HETATM 7774  O   HOH B1686      -8.392  15.919  55.952  1.00 25.44           O  
HETATM 7775  O   HOH B1687      11.966  32.123  26.521  1.00 41.52           O  
HETATM 7776  O   HOH B1688       9.759  34.100  26.048  1.00 32.30           O  
HETATM 7777  O   HOH B1689       8.022  19.495  21.466  1.00 34.66           O  
HETATM 7778  O   HOH B1690      25.036  31.080  23.773  1.00 32.61           O  
HETATM 7779  O   HOH B1691      -2.947  41.088   7.761  1.00 41.78           O  
HETATM 7780  O   HOH B1692      -2.479  25.718  15.993  1.00 51.10           O  
HETATM 7781  O   HOH B1696     -18.807  39.146  35.840  1.00 35.26           O  
HETATM 7782  O   HOH B1697      11.703  20.871  78.887  1.00 30.87           O  
HETATM 7783  O   HOH B1698      -2.358   3.013  80.854  1.00 35.21           O  
HETATM 7784  O   HOH B1699     -17.897   3.615  82.051  1.00 42.25           O  
HETATM 7785  O   HOH B1700     -26.202   4.136  74.307  1.00 44.62           O  
HETATM 7786  O   HOH B1702      13.099  22.177  82.904  1.00 35.70           O  
HETATM 7787  O   HOH B1703      -8.495   8.050  73.119  1.00 38.86           O  
HETATM 7788  O   HOH B1706      -1.309  23.740  18.129  1.00 46.11           O  
HETATM 7789  O   HOH B1707       6.423  26.684  26.775  1.00 44.51           O  
HETATM 7790  O   HOH B1708       6.501  24.478  24.854  1.00 51.03           O  
HETATM 7791  O   HOH B1711      12.930  39.769   5.076  1.00 47.99           O  
HETATM 7792  O   HOH B1721      -8.917  22.163  76.952  1.00 54.03           O  
HETATM 7793  O   HOH B1722     -30.271   3.341  71.214  1.00 32.14           O  
HETATM 7794  O   HOH B1724      -0.729  20.132  33.490  1.00 31.90           O  
HETATM 7795  O   HOH B1726      -9.396  18.856  76.461  1.00 60.59           O  
HETATM 7796  O   HOH B1728      -9.273   4.648  67.076  1.00 34.05           O  
HETATM 7797  O   HOH B1730      13.841  30.951   5.651  1.00 54.85           O  
HETATM 7798  O   HOH B1731      14.210  35.481   4.402  1.00 54.51           O  
HETATM 7799  O   HOH B1737      -5.656   7.904  70.976  1.00 54.32           O  
HETATM 7800  O   HOH B1738     -22.088   5.134  80.449  1.00 42.38           O  
HETATM 7801  O   HOH B1740      -9.436  14.708  31.548  1.00 49.13           O  
HETATM 7802  O   HOH B1741     -26.599   5.897  69.510  1.00 35.26           O  
HETATM 7803  O   HOH B1745      -4.400  -1.255  62.720  1.00 59.04           O  
HETATM 7804  O   HOH B1746     -27.922   8.306  43.688  1.00 43.68           O  
HETATM 7805  O   HOH B1750      -7.882  10.658  70.059  1.00 55.55           O  
HETATM 7806  O   HOH B1751     -17.945  21.574  38.042  1.00 45.32           O  
HETATM 7807  O   HOH B1757      -5.245   4.565  51.908  1.00 31.53           O  
CONECT   13 3325                                                                
CONECT  679 1304                                                                
CONECT 1304  679                                                                
CONECT 3325   13                                                                
CONECT 3766 7062                                                                
CONECT 4423 5048                                                                
CONECT 5048 4423                                                                
CONECT 7062 3766                                                                
CONECT 7423 7426                                                                
CONECT 7424 7426 7431                                                           
CONECT 7425 7431 7433                                                           
CONECT 7426 7423 7424 7429 7434                                                 
CONECT 7427 7431 7434 7435                                                      
CONECT 7428 7436 7437                                                           
CONECT 7429 7426                                                                
CONECT 7430 7437 7438                                                           
CONECT 7431 7424 7425 7427                                                      
CONECT 7432 7437 7444                                                           
CONECT 7433 7425 7435                                                           
CONECT 7434 7426 7427                                                           
CONECT 7435 7427 7433 7436                                                      
CONECT 7436 7428 7435                                                           
CONECT 7437 7428 7430 7432                                                      
CONECT 7438 7430 7439 7443                                                      
CONECT 7439 7438 7440                                                           
CONECT 7440 7439 7441                                                           
CONECT 7441 7440 7442                                                           
CONECT 7442 7441 7443                                                           
CONECT 7443 7438 7442                                                           
CONECT 7444 7432 7445 7449                                                      
CONECT 7445 7444 7446                                                           
CONECT 7446 7445 7447                                                           
CONECT 7447 7446 7448                                                           
CONECT 7448 7447 7449                                                           
CONECT 7449 7444 7448                                                           
CONECT 7450 7451 7452                                                           
CONECT 7451 7450 7453                                                           
CONECT 7452 7450                                                                
CONECT 7453 7451 7455                                                           
CONECT 7454 7463 7465                                                           
CONECT 7455 7453 7456                                                           
CONECT 7456 7455 7457                                                           
CONECT 7457 7456 7458                                                           
CONECT 7458 7457 7459                                                           
CONECT 7459 7458 7460                                                           
CONECT 7460 7459 7462                                                           
CONECT 7461 7463 7467                                                           
CONECT 7462 7460 7464 7467                                                      
CONECT 7463 7454 7461 7466                                                      
CONECT 7464 7462                                                                
CONECT 7465 7454                                                                
CONECT 7466 7463                                                                
CONECT 7467 7461 7462                                                           
CONECT 7468 7469 7470                                                           
CONECT 7469 7468 7471                                                           
CONECT 7470 7468 7473                                                           
CONECT 7471 7469 7474                                                           
CONECT 7472 7485 7487                                                           
CONECT 7473 7470 7476                                                           
CONECT 7474 7471 7477                                                           
CONECT 7475 7478                                                                
CONECT 7476 7473 7478                                                           
CONECT 7477 7474 7479                                                           
CONECT 7478 7475 7476                                                           
CONECT 7479 7477 7480                                                           
CONECT 7480 7479 7481                                                           
CONECT 7481 7480 7482                                                           
CONECT 7482 7481 7484                                                           
CONECT 7483 7485 7489                                                           
CONECT 7484 7482 7486 7489                                                      
CONECT 7485 7472 7483 7488                                                      
CONECT 7486 7484                                                                
CONECT 7487 7472                                                                
CONECT 7488 7485                                                                
CONECT 7489 7483 7484                                                           
CONECT 7490 7491                                                                
CONECT 7491 7490 7493                                                           
CONECT 7492 7501 7503                                                           
CONECT 7493 7491 7494                                                           
CONECT 7494 7493 7495                                                           
CONECT 7495 7494 7496                                                           
CONECT 7496 7495 7497                                                           
CONECT 7497 7496 7498                                                           
CONECT 7498 7497 7500                                                           
CONECT 7499 7501 7505                                                           
CONECT 7500 7498 7502 7505                                                      
CONECT 7501 7492 7499 7504                                                      
CONECT 7502 7500                                                                
CONECT 7503 7492                                                                
CONECT 7504 7501                                                                
CONECT 7505 7499 7500                                                           
CONECT 7506 7507 7508 7509                                                      
CONECT 7507 7506                                                                
CONECT 7508 7506                                                                
CONECT 7509 7506 7510                                                           
CONECT 7510 7509 7511                                                           
CONECT 7511 7510 7512                                                           
CONECT 7512 7511 7513                                                           
CONECT 7513 7512 7514                                                           
CONECT 7514 7513 7515                                                           
CONECT 7515 7514                                                                
CONECT 7516 7519                                                                
CONECT 7517 7519 7524                                                           
CONECT 7518 7524 7526                                                           
CONECT 7519 7516 7517 7522 7527                                                 
CONECT 7520 7524 7527 7528                                                      
CONECT 7521 7529 7530                                                           
CONECT 7522 7519                                                                
CONECT 7523 7530 7531                                                           
CONECT 7524 7517 7518 7520                                                      
CONECT 7525 7530 7537                                                           
CONECT 7526 7518 7528                                                           
CONECT 7527 7519 7520                                                           
CONECT 7528 7520 7526 7529                                                      
CONECT 7529 7521 7528                                                           
CONECT 7530 7521 7523 7525                                                      
CONECT 7531 7523 7532 7536                                                      
CONECT 7532 7531 7533                                                           
CONECT 7533 7532 7534                                                           
CONECT 7534 7533 7535                                                           
CONECT 7535 7534 7536                                                           
CONECT 7536 7531 7535                                                           
CONECT 7537 7525 7538 7542                                                      
CONECT 7538 7537 7539                                                           
CONECT 7539 7538 7540                                                           
CONECT 7540 7539 7541                                                           
CONECT 7541 7540 7542                                                           
CONECT 7542 7537 7541                                                           
CONECT 7543 7545                                                                
CONECT 7544 7553 7555                                                           
CONECT 7545 7543 7546                                                           
CONECT 7546 7545 7547                                                           
CONECT 7547 7546 7548                                                           
CONECT 7548 7547 7549                                                           
CONECT 7549 7548 7550                                                           
CONECT 7550 7549 7552                                                           
CONECT 7551 7553 7557                                                           
CONECT 7552 7550 7554 7557                                                      
CONECT 7553 7544 7551 7556                                                      
CONECT 7554 7552                                                                
CONECT 7555 7544                                                                
CONECT 7556 7553                                                                
CONECT 7557 7551 7552                                                           
CONECT 7558 7559 7560                                                           
CONECT 7559 7558 7561                                                           
CONECT 7560 7558 7563                                                           
CONECT 7561 7559 7564                                                           
CONECT 7562 7575 7577                                                           
CONECT 7563 7560 7566                                                           
CONECT 7564 7561 7567                                                           
CONECT 7565 7568                                                                
CONECT 7566 7563 7568                                                           
CONECT 7567 7564 7569                                                           
CONECT 7568 7565 7566                                                           
CONECT 7569 7567 7570                                                           
CONECT 7570 7569 7571                                                           
CONECT 7571 7570 7572                                                           
CONECT 7572 7571 7574                                                           
CONECT 7573 7575 7579                                                           
CONECT 7574 7572 7576 7579                                                      
CONECT 7575 7562 7573 7578                                                      
CONECT 7576 7574                                                                
CONECT 7577 7562                                                                
CONECT 7578 7575                                                                
CONECT 7579 7573 7574                                                           
CONECT 7580 7581 7582 7583                                                      
CONECT 7581 7580                                                                
CONECT 7582 7580                                                                
CONECT 7583 7580 7584                                                           
CONECT 7584 7583 7585                                                           
CONECT 7585 7584 7586                                                           
CONECT 7586 7585 7587                                                           
CONECT 7587 7586 7588                                                           
CONECT 7588 7587 7589                                                           
CONECT 7589 7588 7590                                                           
CONECT 7590 7589 7591                                                           
CONECT 7591 7590 7592                                                           
CONECT 7592 7591 7593                                                           
CONECT 7593 7592 7594                                                           
CONECT 7594 7593 7595                                                           
CONECT 7595 7594 7596                                                           
CONECT 7596 7595 7597                                                           
CONECT 7597 7596 7598                                                           
CONECT 7598 7597 7599                                                           
CONECT 7599 7598                                                                
CONECT 7600 7601 7602 7603                                                      
CONECT 7601 7600                                                                
CONECT 7602 7600                                                                
CONECT 7603 7600 7604                                                           
CONECT 7604 7603 7605                                                           
CONECT 7605 7604 7606                                                           
CONECT 7606 7605 7607                                                           
CONECT 7607 7606 7608                                                           
CONECT 7608 7607 7609                                                           
CONECT 7609 7608 7610                                                           
CONECT 7610 7609 7611                                                           
CONECT 7611 7610 7612                                                           
CONECT 7612 7611 7613                                                           
CONECT 7613 7612 7614                                                           
CONECT 7614 7613 7615                                                           
CONECT 7615 7614 7616                                                           
CONECT 7616 7615 7617                                                           
CONECT 7617 7616 7618                                                           
CONECT 7618 7617 7619                                                           
CONECT 7619 7618                                                                
CONECT 7620 7621 7622 7623                                                      
CONECT 7621 7620                                                                
CONECT 7622 7620                                                                
CONECT 7623 7620 7624                                                           
CONECT 7624 7623 7625                                                           
CONECT 7625 7624 7626                                                           
CONECT 7626 7625 7627                                                           
CONECT 7627 7626 7628                                                           
CONECT 7628 7627 7629                                                           
CONECT 7629 7628 7630                                                           
CONECT 7630 7629 7631                                                           
CONECT 7631 7630 7632                                                           
CONECT 7632 7631 7633                                                           
CONECT 7633 7632 7634                                                           
CONECT 7634 7633 7635                                                           
CONECT 7635 7634 7636                                                           
CONECT 7636 7635 7637                                                           
CONECT 7637 7636 7638                                                           
CONECT 7638 7637 7639                                                           
CONECT 7639 7638                                                                
CONECT 7640 7641 7642 7643                                                      
CONECT 7641 7640                                                                
CONECT 7642 7640                                                                
CONECT 7643 7640 7644                                                           
CONECT 7644 7643 7645                                                           
CONECT 7645 7644 7646                                                           
CONECT 7646 7645 7647                                                           
CONECT 7647 7646 7648                                                           
CONECT 7648 7647 7649                                                           
CONECT 7649 7648 7650                                                           
CONECT 7650 7649 7651                                                           
CONECT 7651 7650                                                                
CONECT 7652 7653 7654 7655                                                      
CONECT 7653 7652                                                                
CONECT 7654 7652                                                                
CONECT 7655 7652 7656                                                           
CONECT 7656 7655 7657                                                           
CONECT 7657 7656 7658                                                           
CONECT 7658 7657 7659                                                           
CONECT 7659 7658 7660                                                           
CONECT 7660 7659 7661                                                           
CONECT 7661 7660 7662                                                           
CONECT 7662 7661 7663                                                           
CONECT 7663 7662 7664                                                           
CONECT 7664 7663                                                                
MASTER      588    0   13   48   10    0   27    6 7777    2  250   78          
END