HEADER    SIGNALING PROTEIN                       30-JAN-17   5UNF              
TITLE     XFEL STRUCTURE OF HUMAN ANGIOTENSIN II TYPE 2 RECEPTOR (MONOCLINIC    
TITLE    2 FORM) IN COMPLEX WITH COMPOUND 1 (N-BENZYL-N-(2-ETHYL-4-OXO-3-{[2'-  
TITLE    3 (2H-TETRAZOL-5-YL)[1,1'-BIPHENYL]-4-YL])                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHIMERA PROTEIN OF TYPE-2 ANGIOTENSIN II RECEPTOR AND      
COMPND   3 SOLUBLE CYTOCHROME B562;                                             
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 FRAGMENT: UNP P0ABE7 RESIDUES 23-128 AND UNP P50052 35-335 LINKED VIA
COMPND   6 LINKER RESDIUES GSGS;                                                
COMPND   7 SYNONYM: CYTOCHROME B-562,ANGIOTENSIN II TYPE-2 RECEPTOR,AT2;        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI, HOMO SAPIENS;                 
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 562, 9606;                                           
SOURCE   5 GENE: CYBC, AGTR2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PFASTBAC                                  
KEYWDS    HUMAN ANGIOTENSIN II RECEPTOR COMPLEX, GPCR SIGNALING, GPCR, BRIL,    
KEYWDS   2 MEMBRANE PROTEIN, LCP, XFEL, BLOOD PRESSURE REGULATION, MONOCLINIC   
KEYWDS   3 CRYSTAL, COMPOUND 1 (CPD 1), SIGNALING PROTEIN                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.ZHANG,G.W.HAN,A.BATYUK,A.ISHCHENKO,K.L.WHITE,N.PATEL,A.SADYBEKOV,   
AUTHOR   2 B.ZAMLYNNY,M.T.RUDD,K.HOLLENSTEIN,A.TOLSTIKOVA,T.A.WHITE,M.S.HUNTER, 
AUTHOR   3 U.WEIERSTALL,W.LIU,K.BABAOGLU,E.L.MOORE,R.D.KATZ,J.M.SHIPMAN,        
AUTHOR   4 M.GARCIA-CALVO,S.SHARMA,P.SHETH,S.M.SOISSON,R.C.STEVENS,V.KATRITCH,  
AUTHOR   5 V.CHEREZOV                                                           
REVDAT   3   28-NOV-18 5UNF    1       REMARK                                   
REVDAT   2   10-MAY-17 5UNF    1       JRNL   REMARK                            
REVDAT   1   05-APR-17 5UNF    0                                                
JRNL        AUTH   H.ZHANG,G.W.HAN,A.BATYUK,A.ISHCHENKO,K.L.WHITE,N.PATEL,      
JRNL        AUTH 2 A.SADYBEKOV,B.ZAMLYNNY,M.T.RUDD,K.HOLLENSTEIN,A.TOLSTIKOVA,  
JRNL        AUTH 3 T.A.WHITE,M.S.HUNTER,U.WEIERSTALL,W.LIU,K.BABAOGLU,          
JRNL        AUTH 4 E.L.MOORE,R.D.KATZ,J.M.SHIPMAN,M.GARCIA-CALVO,S.SHARMA,      
JRNL        AUTH 5 P.SHETH,S.M.SOISSON,R.C.STEVENS,V.KATRITCH,V.CHEREZOV        
JRNL        TITL   STRUCTURAL BASIS FOR SELECTIVITY AND DIVERSITY IN            
JRNL        TITL 2 ANGIOTENSIN II RECEPTORS.                                    
JRNL        REF    NATURE                        V. 544   327 2017              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   28379944                                                     
JRNL        DOI    10.1038/NATURE22035                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.2                                        
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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.57                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 22906                          
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)  : 0.228                          
REMARK   3   R VALUE            (WORKING SET)  : 0.227                          
REMARK   3   FREE R VALUE                      : 0.256                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.880                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1118                           
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               : 12                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.80                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.92                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.78                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2762                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2250                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2613                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2240                   
REMARK   3   BIN FREE R VALUE                        : 0.2490                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.39                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 149                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6151                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 92                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 90.78                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 111.9                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 7.10360                                              
REMARK   3    B22 (A**2) : -10.18020                                            
REMARK   3    B33 (A**2) : 3.07660                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.58750                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.480               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.359               
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      : 0.926                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.900                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : NULL   ; NULL   ; NULL                
REMARK   3    BOND ANGLES               : 8739   ; 2.500  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2836   ; 15.000 ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 117    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 925    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 6414   ; 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   : 850    ; 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   : 7691   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : NULL                     
REMARK   3    BOND ANGLES                  (DEGREES) : 0.90                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.54                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 1.53                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A| 1001 - 1100 }                                     
REMARK   3    ORIGIN FOR THE GROUP (A):  102.5845   19.7753   41.6970           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1920 T22:    0.0445                                    
REMARK   3     T33:   -0.1112 T12:   -0.0324                                    
REMARK   3     T13:   -0.0325 T23:    0.0221                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.8239 L22:    4.0630                                    
REMARK   3     L33:    6.3458 L12:    0.4122                                    
REMARK   3     L13:   -3.7327 L23:   -2.0703                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1144 S12:   -0.2944 S13:   -0.2836                     
REMARK   3     S21:    0.2874 S22:   -0.1144 S23:    0.2193                     
REMARK   3     S31:   -0.0306 S32:   -0.0615 S33:    0.0000                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { A| 43 - 334 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   68.9021   -1.9496   34.3486           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3372 T22:    0.3040                                    
REMARK   3     T33:   -0.2707 T12:    0.1096                                    
REMARK   3     T13:    0.0609 T23:    0.1849                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.6346 L22:    2.2799                                    
REMARK   3     L33:    2.8729 L12:   -1.3278                                    
REMARK   3     L13:   -0.5126 L23:   -0.2802                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.2198 S12:   -0.6620 S13:   -0.2399                     
REMARK   3     S21:    0.4053 S22:    0.3253 S23:    0.4066                     
REMARK   3     S31:    0.2141 S32:    0.3926 S33:   -0.1055                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { B| 1001 - 1110 }                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   38.7976   30.9461    4.3458           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3009 T22:   -0.2209                                    
REMARK   3     T33:    0.0676 T12:   -0.0056                                    
REMARK   3     T13:   -0.0345 T23:   -0.0127                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    9.2243 L22:    5.7082                                    
REMARK   3     L33:    7.4066 L12:   -1.7595                                    
REMARK   3     L13:   -1.6628 L23:   -1.1169                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0113 S12:   -0.0034 S13:   -0.0337                     
REMARK   3     S21:   -0.2532 S22:    0.0186 S23:   -0.3855                     
REMARK   3     S31:    0.0050 S32:    0.0802 S33:   -0.0299                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { B| 35 - 334 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   75.0278   11.9359    6.0131           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2139 T22:   -0.2136                                    
REMARK   3     T33:    0.0190 T12:   -0.0067                                    
REMARK   3     T13:   -0.0348 T23:   -0.0139                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.2431 L22:    2.0458                                    
REMARK   3     L33:    1.3565 L12:   -0.8457                                    
REMARK   3     L13:   -0.3922 L23:   -0.2856                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0445 S12:   -0.2517 S13:    0.1585                     
REMARK   3     S21:    0.0737 S22:    0.1000 S23:   -0.1267                     
REMARK   3     S31:    0.0473 S32:    0.0532 S33:   -0.0555                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5UNF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000226050.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-DEC-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 294                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : FREE ELECTRON LASER                
REMARK 200  BEAMLINE                       : CXI                                
REMARK 200  X-RAY GENERATOR MODEL          : SLAC LCLS BEAMLINE CXI             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.3                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : K-B MIRRORS                        
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : CS-PAD CXI-1                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CRYSTFEL                           
REMARK 200  DATA SCALING SOFTWARE          : CRYSTFEL                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22934                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 61.60                              
REMARK 200  R MERGE                    (I) : 0.16400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 61.60                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.72000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.800                              
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: 4YAY, 4ZUD                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL, PH 8.0, 25 MM           
REMARK 280  POTASSIUM FORMATE, 25% (V/V) PEG400, AND 0.3% (V/V) (+/-)-2-        
REMARK 280  METHYL-2,4-PENTANEDIOL, LIPIDIC CUBIC PHASE, TEMPERATURE 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       34.55500            
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 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL UNIT IS UNKNOWN            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 37220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 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     TYR A  1101                                                      
REMARK 465     ILE A  1102                                                      
REMARK 465     GLN A  1103                                                      
REMARK 465     LYS A  1104                                                      
REMARK 465     TYR A  1105                                                      
REMARK 465     LEU A  1106                                                      
REMARK 465     GLY A  1107                                                      
REMARK 465     SER A  1108                                                      
REMARK 465     GLY A  1109                                                      
REMARK 465     SER A  1110                                                      
REMARK 465     CYS A    35                                                      
REMARK 465     SER A    36                                                      
REMARK 465     GLN A    37                                                      
REMARK 465     LYS A    38                                                      
REMARK 465     PRO A    39                                                      
REMARK 465     SER A    40                                                      
REMARK 465     ASP A    41                                                      
REMARK 465     LYS A    42                                                      
REMARK 465     LEU A   151                                                      
REMARK 465     SER A   152                                                      
REMARK 465     GLN A   153                                                      
REMARK 465     ARG A   154                                                      
REMARK 465     ARG A   155                                                      
REMARK 465     ASN A   156                                                      
REMARK 465     VAL A   335                                                      
REMARK 465     LYS B    73                                                      
REMARK 465     GLY B    74                                                      
REMARK 465     PRO B    75                                                      
REMARK 465     LYS B    76                                                      
REMARK 465     LEU B   151                                                      
REMARK 465     SER B   152                                                      
REMARK 465     GLN B   153                                                      
REMARK 465     ARG B   154                                                      
REMARK 465     ARG B   155                                                      
REMARK 465     ASN B   156                                                      
REMARK 465     PRO B   157                                                      
REMARK 465     VAL B   335                                                      
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     LYS A1042    CE   NZ                                             
REMARK 470     ARG A 107    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 188    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 203    CG   CD   CE   NZ                                   
REMARK 470     THR A 241    OG1  CG2                                            
REMARK 470     SER A 243    OG                                                  
REMARK 470     SER A 289    OG                                                  
REMARK 470     LEU A 300    CG   CD1  CD2                                       
REMARK 470     ARG A 330    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE A 333    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG A 334    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B1042    CE   NZ                                             
REMARK 470     LEU B1048    CG   CD1  CD2                                       
REMARK 470     ASP B1050    CG   OD1  OD2                                       
REMARK 470     LEU B1106    CG   CD1  CD2                                       
REMARK 470     SER B  36    OG                                                  
REMARK 470     GLN B  37    CG   CD   OE1  NE2                                  
REMARK 470     LYS B  38    CG   CD   CE   NZ                                   
REMARK 470     PHE B 150    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU B 188    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 240    NZ                                                  
REMARK 470     LYS B 246    CG   CD   CE   NZ                                   
REMARK 470     ASN B 247    CG   OD1  ND2                                       
REMARK 470     GLN B 326    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 330    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE B 333    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG B 334    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    CYS A  70      -75.46    -86.47                                   
REMARK 500    LYS A  73      -85.62   -148.13                                   
REMARK 500    LYS A  77      156.45     71.13                                   
REMARK 500    ALA A 198       78.12    -65.15                                   
REMARK 500    PHE A 220      -59.83   -140.22                                   
REMARK 500    TYR A 244      -29.30   -151.02                                   
REMARK 500    TYR A 318      -46.66   -130.72                                   
REMARK 500    LYS B1104      -69.94   -125.27                                   
REMARK 500    SER B1108       24.52    -78.74                                   
REMARK 500    SER B1110       68.95   -102.35                                   
REMARK 500    CYS B  35      -83.14   -164.66                                   
REMARK 500    PHE B 220      -59.62   -139.91                                   
REMARK 500    THR B 241      -73.77   -114.79                                   
REMARK 500    VAL B 321      -34.42   -133.22                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8ES A 1501                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8ES B 1201                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5UNG   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UNH   RELATED DB: PDB                                   
DBREF  5UNF A 1001  1106  UNP    P0ABE7   C562_ECOLX      23    128             
DBREF  5UNF A   35   335  UNP    P50052   AGTR2_HUMAN     35    335             
DBREF  5UNF B 1001  1106  UNP    P0ABE7   C562_ECOLX      23    128             
DBREF  5UNF B   35   335  UNP    P50052   AGTR2_HUMAN     35    335             
SEQADV 5UNF TRP A 1007  UNP  P0ABE7    MET    29 ENGINEERED MUTATION            
SEQADV 5UNF ILE A 1102  UNP  P0ABE7    HIS   124 ENGINEERED MUTATION            
SEQADV 5UNF LEU A 1106  UNP  P0ABE7    ARG   128 ENGINEERED MUTATION            
SEQADV 5UNF GLY A 1107  UNP  P0ABE7              LINKER                         
SEQADV 5UNF SER A 1108  UNP  P0ABE7              LINKER                         
SEQADV 5UNF GLY A 1109  UNP  P0ABE7              LINKER                         
SEQADV 5UNF SER A 1110  UNP  P0ABE7              LINKER                         
SEQADV 5UNF TRP B 1007  UNP  P0ABE7    MET    29 ENGINEERED MUTATION            
SEQADV 5UNF ILE B 1102  UNP  P0ABE7    HIS   124 ENGINEERED MUTATION            
SEQADV 5UNF LEU B 1106  UNP  P0ABE7    ARG   128 ENGINEERED MUTATION            
SEQADV 5UNF GLY B 1107  UNP  P0ABE7              LINKER                         
SEQADV 5UNF SER B 1108  UNP  P0ABE7              LINKER                         
SEQADV 5UNF GLY B 1109  UNP  P0ABE7              LINKER                         
SEQADV 5UNF SER B 1110  UNP  P0ABE7              LINKER                         
SEQRES   1 A  411  ALA ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN          
SEQRES   2 A  411  LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL          
SEQRES   3 A  411  LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP          
SEQRES   4 A  411  ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER          
SEQRES   5 A  411  PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE          
SEQRES   6 A  411  ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU          
SEQRES   7 A  411  ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA          
SEQRES   8 A  411  GLU GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS          
SEQRES   9 A  411  TYR LEU GLY SER GLY SER CYS SER GLN LYS PRO SER ASP          
SEQRES  10 A  411  LYS HIS LEU ASP ALA ILE PRO ILE LEU TYR TYR ILE ILE          
SEQRES  11 A  411  PHE VAL ILE GLY PHE LEU VAL ASN ILE VAL VAL VAL THR          
SEQRES  12 A  411  LEU PHE CYS CYS GLN LYS GLY PRO LYS LYS VAL SER SER          
SEQRES  13 A  411  ILE TYR ILE PHE ASN LEU ALA VAL ALA ASP LEU LEU LEU          
SEQRES  14 A  411  LEU ALA THR LEU PRO LEU TRP ALA THR TYR TYR SER TYR          
SEQRES  15 A  411  ARG TYR ASP TRP LEU PHE GLY PRO VAL MET CYS LYS VAL          
SEQRES  16 A  411  PHE GLY SER PHE LEU THR LEU ASN MET PHE ALA SER ILE          
SEQRES  17 A  411  PHE PHE ILE THR CYS MET SER VAL ASP ARG TYR GLN SER          
SEQRES  18 A  411  VAL ILE TYR PRO PHE LEU SER GLN ARG ARG ASN PRO TRP          
SEQRES  19 A  411  GLN ALA SER TYR ILE VAL PRO LEU VAL TRP CYS MET ALA          
SEQRES  20 A  411  CYS LEU SER SER LEU PRO THR PHE TYR PHE ARG ASP VAL          
SEQRES  21 A  411  ARG THR ILE GLU TYR LEU GLY VAL ASN ALA CYS ILE MET          
SEQRES  22 A  411  ALA PHE PRO PRO GLU LYS TYR ALA GLN TRP SER ALA GLY          
SEQRES  23 A  411  ILE ALA LEU MET LYS ASN ILE LEU GLY PHE ILE ILE PRO          
SEQRES  24 A  411  LEU ILE PHE ILE ALA THR CYS TYR PHE GLY ILE ARG LYS          
SEQRES  25 A  411  HIS LEU LEU LYS THR ASN SER TYR GLY LYS ASN ARG ILE          
SEQRES  26 A  411  THR ARG ASP GLN VAL LEU LYS MET ALA ALA ALA VAL VAL          
SEQRES  27 A  411  LEU ALA PHE ILE ILE CYS TRP LEU PRO PHE HIS VAL LEU          
SEQRES  28 A  411  THR PHE LEU ASP ALA LEU ALA TRP MET GLY VAL ILE ASN          
SEQRES  29 A  411  SER CYS GLU VAL ILE ALA VAL ILE ASP LEU ALA LEU PRO          
SEQRES  30 A  411  PHE ALA ILE LEU LEU GLY PHE THR ASN SER CYS VAL ASN          
SEQRES  31 A  411  PRO PHE LEU TYR CYS PHE VAL GLY ASN ARG PHE GLN GLN          
SEQRES  32 A  411  LYS LEU ARG SER VAL PHE ARG VAL                              
SEQRES   1 B  411  ALA ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN          
SEQRES   2 B  411  LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL          
SEQRES   3 B  411  LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP          
SEQRES   4 B  411  ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER          
SEQRES   5 B  411  PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE          
SEQRES   6 B  411  ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU          
SEQRES   7 B  411  ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA          
SEQRES   8 B  411  GLU GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS          
SEQRES   9 B  411  TYR LEU GLY SER GLY SER CYS SER GLN LYS PRO SER ASP          
SEQRES  10 B  411  LYS HIS LEU ASP ALA ILE PRO ILE LEU TYR TYR ILE ILE          
SEQRES  11 B  411  PHE VAL ILE GLY PHE LEU VAL ASN ILE VAL VAL VAL THR          
SEQRES  12 B  411  LEU PHE CYS CYS GLN LYS GLY PRO LYS LYS VAL SER SER          
SEQRES  13 B  411  ILE TYR ILE PHE ASN LEU ALA VAL ALA ASP LEU LEU LEU          
SEQRES  14 B  411  LEU ALA THR LEU PRO LEU TRP ALA THR TYR TYR SER TYR          
SEQRES  15 B  411  ARG TYR ASP TRP LEU PHE GLY PRO VAL MET CYS LYS VAL          
SEQRES  16 B  411  PHE GLY SER PHE LEU THR LEU ASN MET PHE ALA SER ILE          
SEQRES  17 B  411  PHE PHE ILE THR CYS MET SER VAL ASP ARG TYR GLN SER          
SEQRES  18 B  411  VAL ILE TYR PRO PHE LEU SER GLN ARG ARG ASN PRO TRP          
SEQRES  19 B  411  GLN ALA SER TYR ILE VAL PRO LEU VAL TRP CYS MET ALA          
SEQRES  20 B  411  CYS LEU SER SER LEU PRO THR PHE TYR PHE ARG ASP VAL          
SEQRES  21 B  411  ARG THR ILE GLU TYR LEU GLY VAL ASN ALA CYS ILE MET          
SEQRES  22 B  411  ALA PHE PRO PRO GLU LYS TYR ALA GLN TRP SER ALA GLY          
SEQRES  23 B  411  ILE ALA LEU MET LYS ASN ILE LEU GLY PHE ILE ILE PRO          
SEQRES  24 B  411  LEU ILE PHE ILE ALA THR CYS TYR PHE GLY ILE ARG LYS          
SEQRES  25 B  411  HIS LEU LEU LYS THR ASN SER TYR GLY LYS ASN ARG ILE          
SEQRES  26 B  411  THR ARG ASP GLN VAL LEU LYS MET ALA ALA ALA VAL VAL          
SEQRES  27 B  411  LEU ALA PHE ILE ILE CYS TRP LEU PRO PHE HIS VAL LEU          
SEQRES  28 B  411  THR PHE LEU ASP ALA LEU ALA TRP MET GLY VAL ILE ASN          
SEQRES  29 B  411  SER CYS GLU VAL ILE ALA VAL ILE ASP LEU ALA LEU PRO          
SEQRES  30 B  411  PHE ALA ILE LEU LEU GLY PHE THR ASN SER CYS VAL ASN          
SEQRES  31 B  411  PRO PHE LEU TYR CYS PHE VAL GLY ASN ARG PHE GLN GLN          
SEQRES  32 B  411  LYS LEU ARG SER VAL PHE ARG VAL                              
HET    8ES  A1501      46                                                       
HET    8ES  B1201      46                                                       
HETNAM     8ES N-BENZYL-N-(2-ETHYL-4-OXO-3-{[2'-(2H-TETRAZOL-5-YL)[1,           
HETNAM   2 8ES  1'-BIPHENYL]-4-YL]METHYL}-3,4-DIHYDROQUINAZOLIN-6-YL)           
HETNAM   3 8ES  THIOPHENE-2-CARBOXAMIDE                                         
FORMUL   3  8ES    2(C36 H29 N7 O2 S)                                           
HELIX    1 AA1 ASP A 1002  LYS A 1019  1                                  18    
HELIX    2 AA2 ASN A 1022  ALA A 1043  1                                  22    
HELIX    3 AA3 SER A 1055  GLY A 1082  1                                  28    
HELIX    4 AA4 LYS A 1083  GLU A 1092  1                                  10    
HELIX    5 AA5 GLU A 1092  ALA A 1100  1                                   9    
HELIX    6 AA6 ASP A   45  GLN A   72  1                                  28    
HELIX    7 AA7 VAL A   78  ALA A   95  1                                  18    
HELIX    8 AA8 THR A   96  TYR A  106  1                                  11    
HELIX    9 AA9 PHE A  112  TYR A  148  1                                  37    
HELIX   10 AB1 TRP A  158  SER A  175  1                                  18    
HELIX   11 AB2 SER A  175  PHE A  181  1                                   7    
HELIX   12 AB3 PRO A  200  LYS A  203  5                                   4    
HELIX   13 AB4 TYR A  204  PHE A  220  1                                  17    
HELIX   14 AB5 PHE A  220  THR A  241  1                                  22    
HELIX   15 AB6 GLY A  245  MET A  284  1                                  40    
HELIX   16 AB7 SER A  289  CYS A  319  1                                  31    
HELIX   17 AB8 VAL A  321  ARG A  334  1                                  14    
HELIX   18 AB9 ASP B 1002  LYS B 1019  1                                  18    
HELIX   19 AC1 ASN B 1022  ALA B 1043  1                                  22    
HELIX   20 AC2 SER B 1055  GLY B 1082  1                                  28    
HELIX   21 AC3 LYS B 1083  ALA B 1091  1                                   9    
HELIX   22 AC4 GLU B 1092  GLN B 1103  1                                  12    
HELIX   23 AC5 GLY B 1107  CYS B   35  5                                   5    
HELIX   24 AC6 ASP B   45  GLN B   72  1                                  28    
HELIX   25 AC7 VAL B   78  ALA B   95  1                                  18    
HELIX   26 AC8 THR B   96  TYR B  106  1                                  11    
HELIX   27 AC9 PHE B  112  TYR B  148  1                                  37    
HELIX   28 AD1 GLN B  159  SER B  175  1                                  17    
HELIX   29 AD2 SER B  175  PHE B  181  1                                   7    
HELIX   30 AD3 PRO B  200  GLU B  202  5                                   3    
HELIX   31 AD4 LYS B  203  PHE B  220  1                                  18    
HELIX   32 AD5 PHE B  220  LEU B  239  1                                  20    
HELIX   33 AD6 GLY B  245  MET B  284  1                                  40    
HELIX   34 AD7 SER B  289  TYR B  318  1                                  30    
HELIX   35 AD8 TYR B  318  ARG B  334  1                                  17    
SHEET    1 AA1 2 ARG A 182  THR A 186  0                                        
SHEET    2 AA1 2 ASN A 193  MET A 197 -1  O  ALA A 194   N  ARG A 185           
SHEET    1 AA2 2 ARG B 182  THR B 186  0                                        
SHEET    2 AA2 2 ASN B 193  MET B 197 -1  O  ILE B 196   N  ASP B 183           
SSBOND   1 CYS A  117    CYS A  195                          1555   1555  2.03  
SSBOND   2 CYS B   35    CYS B  290                          1555   1555  2.03  
SSBOND   3 CYS B  117    CYS B  195                          1555   1555  2.03  
SITE     1 AC1 16 TYR A  51  TRP A 100  TYR A 103  TYR A 108                    
SITE     2 AC1 16 LEU A 124  THR A 125  MET A 128  PHE A 129                    
SITE     3 AC1 16 THR A 178  ARG A 182  MET A 214  LYS A 215                    
SITE     4 AC1 16 TRP A 269  PHE A 272  ILE A 304  PHE A 308                    
SITE     1 AC2 15 TYR B  51  TRP B 100  TYR B 103  TYR B 108                    
SITE     2 AC2 15 LEU B 124  THR B 125  MET B 128  PHE B 129                    
SITE     3 AC2 15 THR B 178  ARG B 182  LYS B 215  TRP B 269                    
SITE     4 AC2 15 PHE B 272  ILE B 304  PHE B 308                               
CRYST1   77.390   69.110   90.070  90.00 104.33  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      0.012922  0.000000  0.003301        0.00000                         
SCALE2      0.000000  0.014470  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011459        0.00000                         
ATOM      1  N   ALA A1001     102.539  28.809  52.879  1.00174.71           N  
ANISOU    1  N   ALA A1001    23731  23423  19228  -1955   1373  -1174       N  
ATOM      2  CA  ALA A1001     103.410  27.737  53.358  1.00174.36           C  
ANISOU    2  CA  ALA A1001    23442  23842  18963  -2121    941  -1028       C  
ATOM      3  C   ALA A1001     102.592  26.524  53.849  1.00177.28           C  
ANISOU    3  C   ALA A1001    23643  24351  19363  -1866    922   -747       C  
ATOM      4  O   ALA A1001     103.155  25.439  54.018  1.00176.54           O  
ANISOU    4  O   ALA A1001    23315  24602  19161  -1893    610   -535       O  
ATOM      5  CB  ALA A1001     104.303  28.251  54.476  1.00179.42           C  
ANISOU    5  CB  ALA A1001    24355  24744  19074  -2613    867  -1281       C  
ATOM      6  N   ASP A1002     101.268  26.711  54.062  1.00173.72           N  
ANISOU    6  N   ASP A1002    23296  23629  19081  -1604   1284   -714       N  
ATOM      7  CA  ASP A1002     100.330  25.667  54.500  1.00173.04           C  
ANISOU    7  CA  ASP A1002    23055  23613  19079  -1370   1344   -457       C  
ATOM      8  C   ASP A1002     100.087  24.653  53.366  1.00173.10           C  
ANISOU    8  C   ASP A1002    22630  23605  19536  -1110   1140   -197       C  
ATOM      9  O   ASP A1002     100.116  25.037  52.197  1.00170.82           O  
ANISOU    9  O   ASP A1002    22224  23146  19534  -1005   1115   -234       O  
ATOM     10  CB  ASP A1002      99.002  26.313  54.949  1.00176.73           C  
ANISOU   10  CB  ASP A1002    23768  23807  19575  -1203   1842   -518       C  
ATOM     11  CG  ASP A1002      97.935  25.362  55.469  1.00186.56           C  
ANISOU   11  CG  ASP A1002    24863  25103  20919   -982   1978   -261       C  
ATOM     12  OD1 ASP A1002      98.296  24.266  55.956  1.00187.22           O  
ANISOU   12  OD1 ASP A1002    24806  25453  20875  -1037   1744    -82       O  
ATOM     13  OD2 ASP A1002      96.749  25.753  55.476  1.00192.62           O  
ANISOU   13  OD2 ASP A1002    25670  25649  21869   -754   2362   -223       O  
ATOM     14  N   LEU A1003      99.834  23.366  53.715  1.00168.76           N  
ANISOU   14  N   LEU A1003    21874  23217  19028  -1019   1022     58       N  
ATOM     15  CA  LEU A1003      99.610  22.273  52.754  1.00165.45           C  
ANISOU   15  CA  LEU A1003    21102  22765  18997   -836    861    273       C  
ATOM     16  C   LEU A1003      98.328  22.508  51.917  1.00167.06           C  
ANISOU   16  C   LEU A1003    21173  22733  19567   -626   1066    283       C  
ATOM     17  O   LEU A1003      98.354  22.295  50.705  1.00164.46           O  
ANISOU   17  O   LEU A1003    20632  22341  19517   -547    919    304       O  
ATOM     18  CB  LEU A1003      99.516  20.918  53.494  1.00166.43           C  
ANISOU   18  CB  LEU A1003    21117  23043  19076   -796    814    538       C  
ATOM     19  CG  LEU A1003      99.374  19.644  52.631  1.00169.16           C  
ANISOU   19  CG  LEU A1003    21163  23313  19796   -663    694    742       C  
ATOM     20  CD1 LEU A1003     100.618  19.391  51.795  1.00167.59           C  
ANISOU   20  CD1 LEU A1003    20838  23173  19665   -690    402    752       C  
ATOM     21  CD2 LEU A1003      99.140  18.432  53.497  1.00173.54           C  
ANISOU   21  CD2 LEU A1003    21681  23946  20308   -618    762   1008       C  
ATOM     22  N   GLU A1004      97.229  22.946  52.560  1.00164.69           N  
ANISOU   22  N   GLU A1004    20986  22342  19245   -534   1407    288       N  
ATOM     23  CA  GLU A1004      95.942  23.221  51.905  1.00163.95           C  
ANISOU   23  CA  GLU A1004    20719  22102  19471   -314   1629    356       C  
ATOM     24  C   GLU A1004      96.070  24.390  50.901  1.00165.64           C  
ANISOU   24  C   GLU A1004    20979  22168  19788   -232   1674    222       C  
ATOM     25  O   GLU A1004      95.520  24.318  49.799  1.00164.00           O  
ANISOU   25  O   GLU A1004    20501  21938  19874    -71   1633    317       O  
ATOM     26  CB  GLU A1004      94.875  23.543  52.969  1.00168.40           C  
ANISOU   26  CB  GLU A1004    21427  22615  19945   -219   2040    409       C  
ATOM     27  CG  GLU A1004      93.481  23.805  52.416  1.00180.85           C  
ANISOU   27  CG  GLU A1004    22761  24106  21849     36   2299    549       C  
ATOM     28  CD  GLU A1004      92.417  24.189  53.430  1.00209.10           C  
ANISOU   28  CD  GLU A1004    26469  27616  25365    177   2770    626       C  
ATOM     29  OE1 GLU A1004      91.281  24.492  52.999  1.00206.40           O  
ANISOU   29  OE1 GLU A1004    25902  27232  25289    419   3013    775       O  
ATOM     30  OE2 GLU A1004      92.718  24.212  54.646  1.00207.41           O  
ANISOU   30  OE2 GLU A1004    26575  27414  24817     58   2909    553       O  
ATOM     31  N   ASP A1005      96.803  25.448  51.293  1.00162.29           N  
ANISOU   31  N   ASP A1005    20904  21656  19103   -366   1764      5       N  
ATOM     32  CA  ASP A1005      97.023  26.659  50.498  1.00161.55           C  
ANISOU   32  CA  ASP A1005    20940  21364  19077   -313   1879   -130       C  
ATOM     33  C   ASP A1005      97.980  26.393  49.328  1.00160.55           C  
ANISOU   33  C   ASP A1005    20620  21305  19079   -370   1509   -137       C  
ATOM     34  O   ASP A1005      97.850  27.037  48.284  1.00159.23           O  
ANISOU   34  O   ASP A1005    20382  21014  19103   -215   1560   -121       O  
ATOM     35  CB  ASP A1005      97.579  27.774  51.393  1.00166.35           C  
ANISOU   35  CB  ASP A1005    22027  21836  19343   -528   2116   -398       C  
ATOM     36  CG  ASP A1005      96.653  28.149  52.541  1.00180.74           C  
ANISOU   36  CG  ASP A1005    24122  23542  21010   -458   2562   -424       C  
ATOM     37  OD1 ASP A1005      95.418  27.971  52.398  1.00181.77           O  
ANISOU   37  OD1 ASP A1005    24060  23616  21387   -152   2795   -215       O  
ATOM     38  OD2 ASP A1005      97.153  28.671  53.556  1.00189.58           O  
ANISOU   38  OD2 ASP A1005    25646  24634  21752   -717   2700   -659       O  
ATOM     39  N   ASN A1006      98.931  25.450  49.498  1.00154.49           N  
ANISOU   39  N   ASN A1006    19764  20736  18200   -559   1167   -127       N  
ATOM     40  CA  ASN A1006      99.863  25.066  48.438  1.00151.26           C  
ANISOU   40  CA  ASN A1006    19169  20394  17911   -596    848   -111       C  
ATOM     41  C   ASN A1006      99.133  24.227  47.385  1.00152.31           C  
ANISOU   41  C   ASN A1006    18974  20537  18359   -397    742     55       C  
ATOM     42  O   ASN A1006      99.420  24.388  46.197  1.00150.71           O  
ANISOU   42  O   ASN A1006    18663  20299  18301   -330    629     47       O  
ATOM     43  CB  ASN A1006     101.078  24.319  48.993  1.00150.76           C  
ANISOU   43  CB  ASN A1006    19083  20553  17645   -805    570    -91       C  
ATOM     44  CG  ASN A1006     102.024  25.178  49.808  1.00169.82           C  
ANISOU   44  CG  ASN A1006    21767  23048  19711  -1086    580   -279       C  
ATOM     45  OD1 ASN A1006     102.018  26.416  49.744  1.00161.89           O  
ANISOU   45  OD1 ASN A1006    21007  21862  18641  -1166    791   -481       O  
ATOM     46  ND2 ASN A1006     102.905  24.530  50.551  1.00162.85           N  
ANISOU   46  ND2 ASN A1006    20837  22450  18590  -1256    357   -209       N  
ATOM     47  N   TRP A1007      98.157  23.369  47.803  1.00148.13           N  
ANISOU   47  N   TRP A1007    18299  20061  17920   -329    799    195       N  
ATOM     48  CA  TRP A1007      97.338  22.608  46.852  1.00146.45           C  
ANISOU   48  CA  TRP A1007    17781  19879  17985   -218    718    317       C  
ATOM     49  C   TRP A1007      96.401  23.549  46.102  1.00148.33           C  
ANISOU   49  C   TRP A1007    17924  20072  18362    -23    886    347       C  
ATOM     50  O   TRP A1007      96.074  23.283  44.946  1.00147.11           O  
ANISOU   50  O   TRP A1007    17534  19987  18375     45    746    401       O  
ATOM     51  CB  TRP A1007      96.539  21.475  47.513  1.00146.46           C  
ANISOU   51  CB  TRP A1007    17651  19940  18059   -247    768    455       C  
ATOM     52  CG  TRP A1007      97.339  20.225  47.713  1.00147.07           C  
ANISOU   52  CG  TRP A1007    17711  20053  18115   -368    577    509       C  
ATOM     53  CD1 TRP A1007      97.884  19.774  48.877  1.00150.99           C  
ANISOU   53  CD1 TRP A1007    18352  20609  18409   -443    586    574       C  
ATOM     54  CD2 TRP A1007      97.780  19.323  46.688  1.00145.77           C  
ANISOU   54  CD2 TRP A1007    17401  19866  18119   -402    374    521       C  
ATOM     55  NE1 TRP A1007      98.591  18.614  48.652  1.00149.99           N  
ANISOU   55  NE1 TRP A1007    18148  20491  18352   -479    423    675       N  
ATOM     56  CE2 TRP A1007      98.547  18.317  47.315  1.00150.07           C  
ANISOU   56  CE2 TRP A1007    18006  20418  18598   -461    313    624       C  
ATOM     57  CE3 TRP A1007      97.574  19.248  45.300  1.00146.24           C  
ANISOU   57  CE3 TRP A1007    17298  19909  18357   -384    260    465       C  
ATOM     58  CZ2 TRP A1007      99.118  17.254  46.602  1.00148.88           C  
ANISOU   58  CZ2 TRP A1007    17783  20193  18592   -480    195    666       C  
ATOM     59  CZ3 TRP A1007      98.168  18.214  44.591  1.00147.12           C  
ANISOU   59  CZ3 TRP A1007    17365  19964  18569   -450    116    458       C  
ATOM     60  CH2 TRP A1007      98.908  17.218  45.242  1.00148.12           C  
ANISOU   60  CH2 TRP A1007    17577  20034  18668   -488    112    557       C  
ATOM     61  N   GLU A1008      96.015  24.673  46.736  1.00144.58           N  
ANISOU   61  N   GLU A1008    17649  19486  17797     76   1203    322       N  
ATOM     62  CA  GLU A1008      95.188  25.690  46.096  1.00144.50           C  
ANISOU   62  CA  GLU A1008    17572  19411  17918    329   1435    407       C  
ATOM     63  C   GLU A1008      96.033  26.401  45.024  1.00143.70           C  
ANISOU   63  C   GLU A1008    17547  19230  17823    362   1334    330       C  
ATOM     64  O   GLU A1008      95.535  26.640  43.927  1.00143.12           O  
ANISOU   64  O   GLU A1008    17258  19223  17898    555   1311    461       O  
ATOM     65  CB  GLU A1008      94.620  26.668  47.139  1.00148.76           C  
ANISOU   65  CB  GLU A1008    18376  19785  18362    440   1882    398       C  
ATOM     66  CG  GLU A1008      93.614  27.663  46.579  1.00161.71           C  
ANISOU   66  CG  GLU A1008    19925  21347  20171    782   2207    569       C  
ATOM     67  CD  GLU A1008      92.929  28.562  47.594  1.00187.43           C  
ANISOU   67  CD  GLU A1008    23457  24393  23366    943   2737    584       C  
ATOM     68  OE1 GLU A1008      92.953  28.232  48.803  1.00185.36           O  
ANISOU   68  OE1 GLU A1008    23408  24099  22920    779   2843    475       O  
ATOM     69  OE2 GLU A1008      92.303  29.559  47.168  1.00183.40           O  
ANISOU   69  OE2 GLU A1008    22939  23757  22988   1263   3073    737       O  
ATOM     70  N   THR A1009      97.332  26.648  45.318  1.00137.00           N  
ANISOU   70  N   THR A1009    16967  18287  16800    154   1248    140       N  
ATOM     71  CA  THR A1009      98.282  27.275  44.391  1.00134.69           C  
ANISOU   71  CA  THR A1009    16757  17910  16510    136   1163     59       C  
ATOM     72  C   THR A1009      98.543  26.314  43.208  1.00133.76           C  
ANISOU   72  C   THR A1009    16344  17961  16516    151    816    134       C  
ATOM     73  O   THR A1009      98.640  26.774  42.068  1.00132.89           O  
ANISOU   73  O   THR A1009    16165  17840  16487    289    794    185       O  
ATOM     74  CB  THR A1009      99.581  27.653  45.130  1.00142.75           C  
ANISOU   74  CB  THR A1009    18077  18855  17306   -154   1137   -155       C  
ATOM     75  OG1 THR A1009      99.257  28.430  46.286  1.00144.77           O  
ANISOU   75  OG1 THR A1009    18645  18961  17401   -215   1470   -267       O  
ATOM     76  CG2 THR A1009     100.569  28.423  44.246  1.00140.77           C  
ANISOU   76  CG2 THR A1009    17918  18496  17073   -203   1101   -239       C  
ATOM     77  N   LEU A1010      98.619  24.988  43.481  1.00127.39           N  
ANISOU   77  N   LEU A1010    15393  17295  15715     19    587    150       N  
ATOM     78  CA  LEU A1010      98.818  23.957  42.454  1.00124.84           C  
ANISOU   78  CA  LEU A1010    14851  17084  15498      0    316    187       C  
ATOM     79  C   LEU A1010      97.597  23.838  41.536  1.00128.76           C  
ANISOU   79  C   LEU A1010    15088  17700  16135    153    310    304       C  
ATOM     80  O   LEU A1010      97.770  23.725  40.325  1.00127.80           O  
ANISOU   80  O   LEU A1010    14865  17648  16046    199    165    308       O  
ATOM     81  CB  LEU A1010      99.119  22.581  43.082  1.00124.09           C  
ANISOU   81  CB  LEU A1010    14706  17045  15397   -156    175    199       C  
ATOM     82  CG  LEU A1010     100.508  22.376  43.681  1.00127.89           C  
ANISOU   82  CG  LEU A1010    15333  17522  15737   -296     79    152       C  
ATOM     83  CD1 LEU A1010     100.566  21.116  44.519  1.00128.31           C  
ANISOU   83  CD1 LEU A1010    15344  17629  15777   -374     32    245       C  
ATOM     84  CD2 LEU A1010     101.569  22.322  42.604  1.00128.92           C  
ANISOU   84  CD2 LEU A1010    15438  17645  15900   -300    -83    116       C  
ATOM     85  N   ASN A1011      96.373  23.879  42.104  1.00126.37           N  
ANISOU   85  N   ASN A1011    14663  17459  15894    227    470    412       N  
ATOM     86  CA  ASN A1011      95.123  23.743  41.348  1.00127.23           C  
ANISOU   86  CA  ASN A1011    14444  17771  16127    348    454    564       C  
ATOM     87  C   ASN A1011      94.794  25.024  40.546  1.00130.11           C  
ANISOU   87  C   ASN A1011    14773  18163  16499    624    585    688       C  
ATOM     88  O   ASN A1011      94.319  24.901  39.416  1.00130.09           O  
ANISOU   88  O   ASN A1011    14510  18388  16529    696    429    790       O  
ATOM     89  CB  ASN A1011      93.957  23.404  42.285  1.00131.28           C  
ANISOU   89  CB  ASN A1011    14812  18350  16718    358    630    681       C  
ATOM     90  CG  ASN A1011      94.078  22.052  42.974  1.00158.84           C  
ANISOU   90  CG  ASN A1011    18296  21828  20229    113    532    622       C  
ATOM     91  OD1 ASN A1011      94.673  21.094  42.455  1.00152.39           O  
ANISOU   91  OD1 ASN A1011    17461  21013  19427    -62    303    531       O  
ATOM     92  ND2 ASN A1011      93.460  21.929  44.140  1.00153.27           N  
ANISOU   92  ND2 ASN A1011    17611  21091  19531    117    749    695       N  
ATOM     93  N   ASP A1012      95.042  26.235  41.113  1.00126.07           N  
ANISOU   93  N   ASP A1012    14535  17423  15940    767    886    682       N  
ATOM     94  CA  ASP A1012      94.768  27.512  40.430  1.00126.99           C  
ANISOU   94  CA  ASP A1012    14676  17488  16087   1068   1103    832       C  
ATOM     95  C   ASP A1012      95.649  27.701  39.192  1.00127.90           C  
ANISOU   95  C   ASP A1012    14833  17610  16154   1066    910    788       C  
ATOM     96  O   ASP A1012      95.169  28.236  38.190  1.00129.03           O  
ANISOU   96  O   ASP A1012    14818  17882  16324   1315    939    986       O  
ATOM     97  CB  ASP A1012      94.968  28.721  41.365  1.00130.36           C  
ANISOU   97  CB  ASP A1012    15480  17576  16475   1163   1532    781       C  
ATOM     98  CG  ASP A1012      93.952  28.871  42.482  1.00143.81           C  
ANISOU   98  CG  ASP A1012    17179  19243  18219   1273   1850    875       C  
ATOM     99  OD1 ASP A1012      93.141  27.935  42.684  1.00144.84           O  
ANISOU   99  OD1 ASP A1012    16991  19621  18420   1238   1715    979       O  
ATOM    100  OD2 ASP A1012      93.975  29.916  43.164  1.00152.08           O  
ANISOU  100  OD2 ASP A1012    18561  19994  19226   1374   2264    833       O  
ATOM    101  N   ASN A1013      96.933  27.287  39.267  1.00120.65           N  
ANISOU  101  N   ASN A1013    14108  16578  15156    813    733    566       N  
ATOM    102  CA  ASN A1013      97.880  27.418  38.157  1.00118.39           C  
ANISOU  102  CA  ASN A1013    13872  16284  14828    800    578    521       C  
ATOM    103  C   ASN A1013      97.611  26.357  37.076  1.00119.89           C  
ANISOU  103  C   ASN A1013    13779  16758  15013    764    259    558       C  
ATOM    104  O   ASN A1013      97.939  26.602  35.915  1.00119.71           O  
ANISOU  104  O   ASN A1013    13727  16813  14943    864    178    609       O  
ATOM    105  CB  ASN A1013      99.318  27.323  38.645  1.00116.58           C  
ANISOU  105  CB  ASN A1013    13888  15879  14527    552    517    311       C  
ATOM    106  CG  ASN A1013      99.763  28.464  39.533  1.00137.25           C  
ANISOU  106  CG  ASN A1013    16822  18234  17094    497    807    215       C  
ATOM    107  OD1 ASN A1013     100.639  28.301  40.380  1.00133.04           O  
ANISOU  107  OD1 ASN A1013    16439  17642  16467    244    756     54       O  
ATOM    108  ND2 ASN A1013      99.153  29.637  39.392  1.00129.11           N  
ANISOU  108  ND2 ASN A1013    15901  17047  16108    724   1138    319       N  
ATOM    109  N   LEU A1014      96.990  25.205  37.438  1.00114.72           N  
ANISOU  109  N   LEU A1014    12941  16252  14394    607    106    527       N  
ATOM    110  CA  LEU A1014      96.590  24.177  36.465  1.00114.28           C  
ANISOU  110  CA  LEU A1014    12646  16453  14324    500   -164    517       C  
ATOM    111  C   LEU A1014      95.531  24.725  35.510  1.00119.66           C  
ANISOU  111  C   LEU A1014    13046  17442  14977    707   -185    732       C  
ATOM    112  O   LEU A1014      95.544  24.394  34.324  1.00119.99           O  
ANISOU  112  O   LEU A1014    12960  17713  14918    658   -404    721       O  
ATOM    113  CB  LEU A1014      96.062  22.909  37.157  1.00114.38           C  
ANISOU  113  CB  LEU A1014    12541  16510  14407    266   -248    447       C  
ATOM    114  CG  LEU A1014      97.085  21.952  37.750  1.00116.98           C  
ANISOU  114  CG  LEU A1014    13071  16632  14743     56   -308    279       C  
ATOM    115  CD1 LEU A1014      96.422  20.966  38.692  1.00117.80           C  
ANISOU  115  CD1 LEU A1014    13092  16729  14936   -108   -280    279       C  
ATOM    116  CD2 LEU A1014      97.882  21.232  36.656  1.00118.39           C  
ANISOU  116  CD2 LEU A1014    13299  16814  14870    -48   -491    156       C  
ATOM    117  N   LYS A1015      94.631  25.590  36.039  1.00116.99           N  
ANISOU  117  N   LYS A1015    12616  17123  14709    952     62    943       N  
ATOM    118  CA  LYS A1015      93.556  26.258  35.298  1.00119.24           C  
ANISOU  118  CA  LYS A1015    12590  17729  14986   1233     99   1245       C  
ATOM    119  C   LYS A1015      94.136  27.262  34.308  1.00121.79           C  
ANISOU  119  C   LYS A1015    13041  18020  15215   1478    156   1355       C  
ATOM    120  O   LYS A1015      93.516  27.536  33.279  1.00124.19           O  
ANISOU  120  O   LYS A1015    13076  18683  15426   1649     41   1577       O  
ATOM    121  CB  LYS A1015      92.585  26.970  36.267  1.00123.94           C  
ANISOU  121  CB  LYS A1015    13098  18279  15716   1479    443   1467       C  
ATOM    122  CG  LYS A1015      91.995  26.098  37.388  1.00140.38           C  
ANISOU  122  CG  LYS A1015    15081  20360  17897   1270    463   1390       C  
ATOM    123  CD  LYS A1015      91.125  24.929  36.899  1.00152.48           C  
ANISOU  123  CD  LYS A1015    16187  22309  19441   1035    153   1414       C  
ATOM    124  CE  LYS A1015      90.591  24.078  38.034  1.00161.87           C  
ANISOU  124  CE  LYS A1015    17313  23442  20748    819    218   1345       C  
ATOM    125  NZ  LYS A1015      89.687  24.838  38.944  1.00171.63           N  
ANISOU  125  NZ  LYS A1015    18465  24644  22103   1095    592   1583       N  
ATOM    126  N   VAL A1016      95.328  27.816  34.628  1.00114.53           N  
ANISOU  126  N   VAL A1016    12518  16694  14304   1478    334   1212       N  
ATOM    127  CA  VAL A1016      96.031  28.787  33.790  1.00113.92           C  
ANISOU  127  CA  VAL A1016    12623  16494  14167   1679    454   1297       C  
ATOM    128  C   VAL A1016      96.616  28.053  32.567  1.00116.50           C  
ANISOU  128  C   VAL A1016    12903  17021  14340   1533    120   1192       C  
ATOM    129  O   VAL A1016      96.425  28.520  31.446  1.00117.71           O  
ANISOU  129  O   VAL A1016    12980  17361  14384   1749    101   1385       O  
ATOM    130  CB  VAL A1016      97.123  29.557  34.589  1.00115.93           C  
ANISOU  130  CB  VAL A1016    13304  16263  14483   1624    744   1134       C  
ATOM    131  CG1 VAL A1016      97.923  30.495  33.688  1.00116.27           C  
ANISOU  131  CG1 VAL A1016    13541  16145  14491   1792    898   1217       C  
ATOM    132  CG2 VAL A1016      96.513  30.329  35.755  1.00117.23           C  
ANISOU  132  CG2 VAL A1016    13580  16208  14754   1746   1116   1198       C  
ATOM    133  N   ILE A1017      97.285  26.890  32.786  1.00110.63           N  
ANISOU  133  N   ILE A1017    12217  16237  13579   1193   -108    912       N  
ATOM    134  CA  ILE A1017      97.917  26.057  31.747  1.00109.54           C  
ANISOU  134  CA  ILE A1017    12099  16217  13305   1030   -365    765       C  
ATOM    135  C   ILE A1017      96.868  25.636  30.690  1.00116.89           C  
ANISOU  135  C   ILE A1017    12717  17621  14076   1043   -600    879       C  
ATOM    136  O   ILE A1017      97.149  25.735  29.495  1.00117.75           O  
ANISOU  136  O   ILE A1017    12843  17897  14001   1102   -707    909       O  
ATOM    137  CB  ILE A1017      98.608  24.806  32.376  1.00110.06           C  
ANISOU  137  CB  ILE A1017    12279  16111  13426    704   -483    489       C  
ATOM    138  CG1 ILE A1017      99.666  25.222  33.425  1.00108.14           C  
ANISOU  138  CG1 ILE A1017    12291  15509  13286    668   -300    405       C  
ATOM    139  CG2 ILE A1017      99.236  23.914  31.291  1.00110.69           C  
ANISOU  139  CG2 ILE A1017    12416  16265  13376    555   -676    334       C  
ATOM    140  CD1 ILE A1017     100.296  24.066  34.249  1.00113.89           C  
ANISOU  140  CD1 ILE A1017    13094  16106  14074    415   -383    227       C  
ATOM    141  N   GLU A1018      95.670  25.189  31.131  1.00115.21           N  
ANISOU  141  N   GLU A1018    12209  17654  13912    972   -679    949       N  
ATOM    142  CA  GLU A1018      94.576  24.749  30.247  1.00118.39           C  
ANISOU  142  CA  GLU A1018    12245  18586  14153    909   -936   1056       C  
ATOM    143  C   GLU A1018      94.115  25.871  29.306  1.00124.95           C  
ANISOU  143  C   GLU A1018    12898  19733  14843   1293   -894   1419       C  
ATOM    144  O   GLU A1018      93.858  25.618  28.128  1.00127.02           O  
ANISOU  144  O   GLU A1018    12987  20424  14850   1249  -1143   1470       O  
ATOM    145  CB  GLU A1018      93.362  24.257  31.068  1.00121.41           C  
ANISOU  145  CB  GLU A1018    12306  19157  14666    774   -969   1109       C  
ATOM    146  CG  GLU A1018      93.621  23.064  31.976  1.00130.26           C  
ANISOU  146  CG  GLU A1018    13566  20008  15919    406   -998    806       C  
ATOM    147  CD  GLU A1018      92.442  22.597  32.815  1.00153.66           C  
ANISOU  147  CD  GLU A1018    16231  23122  19029    268   -984    871       C  
ATOM    148  OE1 GLU A1018      92.684  21.957  33.864  1.00150.51           O  
ANISOU  148  OE1 GLU A1018    15994  22407  18785    110   -872    725       O  
ATOM    149  OE2 GLU A1018      91.285  22.921  32.463  1.00149.39           O  
ANISOU  149  OE2 GLU A1018    15277  23034  18452    345  -1065   1111       O  
ATOM    150  N   LYS A1019      94.001  27.103  29.837  1.00121.55           N  
ANISOU  150  N   LYS A1019    12533  19087  14562   1668   -555   1675       N  
ATOM    151  CA  LYS A1019      93.515  28.276  29.105  1.00124.59           C  
ANISOU  151  CA  LYS A1019    12776  19693  14871   2118   -406   2096       C  
ATOM    152  C   LYS A1019      94.681  29.173  28.622  1.00126.91           C  
ANISOU  152  C   LYS A1019    13461  19626  15132   2310   -191   2103       C  
ATOM    153  O   LYS A1019      94.442  30.310  28.202  1.00128.78           O  
ANISOU  153  O   LYS A1019    13694  19863  15373   2726     69   2459       O  
ATOM    154  CB  LYS A1019      92.560  29.095  30.002  1.00129.20           C  
ANISOU  154  CB  LYS A1019    13199  20219  15672   2443    -72   2408       C  
ATOM    155  CG  LYS A1019      91.322  28.330  30.471  1.00143.72           C  
ANISOU  155  CG  LYS A1019    14598  22438  17570   2296   -232   2471       C  
ATOM    156  CD  LYS A1019      90.451  29.170  31.397  1.00154.14           C  
ANISOU  156  CD  LYS A1019    15796  23652  19118   2662    173   2793       C  
ATOM    157  CE  LYS A1019      89.244  28.402  31.879  1.00164.29           C  
ANISOU  157  CE  LYS A1019    16617  25321  20484   2515     41   2877       C  
ATOM    158  NZ  LYS A1019      88.388  29.224  32.772  1.00173.74           N  
ANISOU  158  NZ  LYS A1019    17699  26410  21906   2914    489   3216       N  
ATOM    159  N   ALA A1020      95.930  28.656  28.655  1.00120.04           N  
ANISOU  159  N   ALA A1020    12912  18454  14244   2021   -270   1744       N  
ATOM    160  CA  ALA A1020      97.116  29.409  28.230  1.00118.40           C  
ANISOU  160  CA  ALA A1020    13049  17912  14026   2136    -73   1726       C  
ATOM    161  C   ALA A1020      97.199  29.497  26.712  1.00123.62           C  
ANISOU  161  C   ALA A1020    13647  18915  14407   2280   -218   1887       C  
ATOM    162  O   ALA A1020      96.823  28.555  26.007  1.00123.93           O  
ANISOU  162  O   ALA A1020    13497  19372  14219   2090   -564   1798       O  
ATOM    163  CB  ALA A1020      98.381  28.772  28.778  1.00115.32           C  
ANISOU  163  CB  ALA A1020    12944  17156  13715   1795   -111   1339       C  
ATOM    164  N   ASP A1021      97.703  30.641  26.221  1.00120.95           N  
ANISOU  164  N   ASP A1021    13497  18386  14073   2594     71   2115       N  
ATOM    165  CA  ASP A1021      97.864  30.935  24.800  1.00123.08           C  
ANISOU  165  CA  ASP A1021    13755  18940  14069   2799     12   2330       C  
ATOM    166  C   ASP A1021      99.297  30.666  24.354  1.00123.37           C  
ANISOU  166  C   ASP A1021    14124  18692  14059   2612     28   2066       C  
ATOM    167  O   ASP A1021      99.509  29.977  23.353  1.00123.41           O  
ANISOU  167  O   ASP A1021    14116  18984  13791   2481   -226   1955       O  
ATOM    168  CB  ASP A1021      97.482  32.407  24.511  1.00128.62           C  
ANISOU  168  CB  ASP A1021    14456  19590  14824   3318    390   2819       C  
ATOM    169  CG  ASP A1021      96.068  32.817  24.912  1.00146.62           C  
ANISOU  169  CG  ASP A1021    16386  22147  17177   3604    458   3173       C  
ATOM    170  OD1 ASP A1021      95.205  31.920  25.068  1.00148.81           O  
ANISOU  170  OD1 ASP A1021    16286  22935  17318   3450     92   3157       O  
ATOM    171  OD2 ASP A1021      95.810  34.037  25.010  1.00156.49           O  
ANISOU  171  OD2 ASP A1021    17728  23120  18610   3997    904   3497       O  
ATOM    172  N   ASN A1022     100.283  31.204  25.110  1.00116.92           N  
ANISOU  172  N   ASN A1022    13601  17324  13499   2577    341   1956       N  
ATOM    173  CA  ASN A1022     101.711  31.097  24.802  1.00114.39           C  
ANISOU  173  CA  ASN A1022    13556  16714  13194   2420    417   1759       C  
ATOM    174  C   ASN A1022     102.461  30.212  25.838  1.00113.83           C  
ANISOU  174  C   ASN A1022    13568  16389  13292   2025    314   1369       C  
ATOM    175  O   ASN A1022     101.931  29.914  26.914  1.00112.55           O  
ANISOU  175  O   ASN A1022    13315  16186  13262   1896    258   1266       O  
ATOM    176  CB  ASN A1022     102.347  32.496  24.744  1.00115.22           C  
ANISOU  176  CB  ASN A1022    13902  16427  13451   2642    858   1958       C  
ATOM    177  CG  ASN A1022     102.131  33.343  25.973  1.00133.92           C  
ANISOU  177  CG  ASN A1022    16371  18414  16097   2652   1160   1962       C  
ATOM    178  OD1 ASN A1022     102.755  33.144  27.014  1.00122.38           O  
ANISOU  178  OD1 ASN A1022    15046  16647  14805   2346   1201   1675       O  
ATOM    179  ND2 ASN A1022     101.306  34.368  25.844  1.00131.03           N  
ANISOU  179  ND2 ASN A1022    15955  18064  15766   3019   1410   2306       N  
ATOM    180  N   ALA A1023     103.699  29.796  25.480  1.00107.80           N  
ANISOU  180  N   ALA A1023    12965  15478  12517   1867    311   1196       N  
ATOM    181  CA  ALA A1023     104.583  28.944  26.277  1.00104.41           C  
ANISOU  181  CA  ALA A1023    12591  14854  12225   1552    229    902       C  
ATOM    182  C   ALA A1023     105.066  29.652  27.544  1.00106.70           C  
ANISOU  182  C   ALA A1023    12974  14801  12765   1436    432    846       C  
ATOM    183  O   ALA A1023     105.386  28.977  28.524  1.00104.55           O  
ANISOU  183  O   ALA A1023    12677  14456  12592   1195    326    654       O  
ATOM    184  CB  ALA A1023     105.779  28.522  25.441  1.00104.83           C  
ANISOU  184  CB  ALA A1023    12767  14856  12208   1501    250    826       C  
ATOM    185  N   ALA A1024     105.129  31.002  27.524  1.00104.35           N  
ANISOU  185  N   ALA A1024    12807  14293  12550   1594    742   1014       N  
ATOM    186  CA  ALA A1024     105.547  31.811  28.672  1.00103.75           C  
ANISOU  186  CA  ALA A1024    12877  13877  12669   1439    977    927       C  
ATOM    187  C   ALA A1024     104.514  31.734  29.810  1.00107.07           C  
ANISOU  187  C   ALA A1024    13229  14314  13141   1416    946    884       C  
ATOM    188  O   ALA A1024     104.910  31.728  30.976  1.00105.55           O  
ANISOU  188  O   ALA A1024    13116  13948  13041   1166    983    701       O  
ATOM    189  CB  ALA A1024     105.757  33.254  28.251  1.00106.97           C  
ANISOU  189  CB  ALA A1024    13489  14006  13148   1613   1378   1110       C  
ATOM    190  N   GLN A1025     103.198  31.651  29.471  1.00104.61           N  
ANISOU  190  N   GLN A1025    12746  14255  12746   1666    871   1067       N  
ATOM    191  CA  GLN A1025     102.113  31.503  30.455  1.00104.44           C  
ANISOU  191  CA  GLN A1025    12610  14295  12779   1677    852   1069       C  
ATOM    192  C   GLN A1025     102.208  30.152  31.153  1.00105.04           C  
ANISOU  192  C   GLN A1025    12570  14493  12849   1373    543    822       C  
ATOM    193  O   GLN A1025     102.035  30.077  32.371  1.00104.03           O  
ANISOU  193  O   GLN A1025    12476  14248  12804   1233    592    713       O  
ATOM    194  CB  GLN A1025     100.723  31.657  29.805  1.00108.42           C  
ANISOU  194  CB  GLN A1025    12873  15127  13194   2012    818   1370       C  
ATOM    195  CG  GLN A1025     100.429  33.037  29.224  1.00128.36           C  
ANISOU  195  CG  GLN A1025    15490  17538  15742   2405   1183   1708       C  
ATOM    196  CD  GLN A1025      99.038  33.144  28.636  1.00151.47           C  
ANISOU  196  CD  GLN A1025    18103  20878  18571   2761   1128   2069       C  
ATOM    197  OE1 GLN A1025      98.845  33.705  27.554  1.00149.98           O  
ANISOU  197  OE1 GLN A1025    17853  20876  18256   3070   1185   2377       O  
ATOM    198  NE2 GLN A1025      98.042  32.570  29.304  1.00143.61           N  
ANISOU  198  NE2 GLN A1025    16866  20084  17613   2723   1001   2066       N  
ATOM    199  N   VAL A1026     102.493  29.086  30.368  1.00100.22           N  
ANISOU  199  N   VAL A1026    11857  14095  12129   1278    264    741       N  
ATOM    200  CA  VAL A1026     102.644  27.702  30.834  1.00 98.04           C  
ANISOU  200  CA  VAL A1026    11500  13896  11855   1020     16    535       C  
ATOM    201  C   VAL A1026     103.884  27.614  31.746  1.00100.64           C  
ANISOU  201  C   VAL A1026    11973  13975  12289    799     76    377       C  
ATOM    202  O   VAL A1026     103.779  27.090  32.855  1.00 99.24           O  
ANISOU  202  O   VAL A1026    11769  13768  12168    638     20    279       O  
ATOM    203  CB  VAL A1026     102.731  26.698  29.646  1.00101.78           C  
ANISOU  203  CB  VAL A1026    11906  14589  12177    983   -208    478       C  
ATOM    204  CG1 VAL A1026     102.845  25.265  30.142  1.00100.17           C  
ANISOU  204  CG1 VAL A1026    11666  14386  12009    734   -382    278       C  
ATOM    205  CG2 VAL A1026     101.530  26.833  28.721  1.00104.03           C  
ANISOU  205  CG2 VAL A1026    12015  15217  12296   1150   -314    637       C  
ATOM    206  N   LYS A1027     105.039  28.162  31.286  1.00 97.49           N  
ANISOU  206  N   LYS A1027    11703  13435  11904    791    193    379       N  
ATOM    207  CA  LYS A1027     106.311  28.176  32.020  1.00 96.65           C  
ANISOU  207  CA  LYS A1027    11672  13173  11876    565    233    267       C  
ATOM    208  C   LYS A1027     106.147  28.880  33.380  1.00100.67           C  
ANISOU  208  C   LYS A1027    12276  13535  12438    425    368    201       C  
ATOM    209  O   LYS A1027     106.577  28.332  34.394  1.00 99.67           O  
ANISOU  209  O   LYS A1027    12123  13431  12318    207    268     94       O  
ATOM    210  CB  LYS A1027     107.404  28.871  31.185  1.00100.22           C  
ANISOU  210  CB  LYS A1027    12218  13516  12344    592    385    321       C  
ATOM    211  CG  LYS A1027     108.796  28.872  31.830  1.00117.10           C  
ANISOU  211  CG  LYS A1027    14358  15577  14559    330    398    233       C  
ATOM    212  CD  LYS A1027     109.805  29.786  31.101  1.00130.90           C  
ANISOU  212  CD  LYS A1027    16191  17189  16355    319    608    295       C  
ATOM    213  CE  LYS A1027     109.477  31.265  31.199  1.00147.73           C  
ANISOU  213  CE  LYS A1027    18523  19079  18527    332    905    323       C  
ATOM    214  NZ  LYS A1027     110.486  32.110  30.514  1.00160.12           N  
ANISOU  214  NZ  LYS A1027    20186  20487  20166    283   1140    383       N  
ATOM    215  N   ASP A1028     105.510  30.080  33.391  1.00 98.56           N  
ANISOU  215  N   ASP A1028    12138  13120  12192    567    622    281       N  
ATOM    216  CA  ASP A1028     105.260  30.888  34.593  1.00 99.37           C  
ANISOU  216  CA  ASP A1028    12410  13022  12323    455    842    200       C  
ATOM    217  C   ASP A1028     104.424  30.102  35.617  1.00101.67           C  
ANISOU  217  C   ASP A1028    12607  13437  12587    397    710    143       C  
ATOM    218  O   ASP A1028     104.819  30.016  36.782  1.00101.35           O  
ANISOU  218  O   ASP A1028    12656  13344  12510    149    717     -4       O  
ATOM    219  CB  ASP A1028     104.543  32.205  34.220  1.00103.75           C  
ANISOU  219  CB  ASP A1028    13123  13371  12926    721   1201    355       C  
ATOM    220  CG  ASP A1028     104.284  33.151  35.383  1.00117.15           C  
ANISOU  220  CG  ASP A1028    15076  14783  14655    625   1528    257       C  
ATOM    221  OD1 ASP A1028     105.206  33.348  36.207  1.00118.22           O  
ANISOU  221  OD1 ASP A1028    15372  14786  14759    267   1564     35       O  
ATOM    222  OD2 ASP A1028     103.206  33.788  35.400  1.00125.23           O  
ANISOU  222  OD2 ASP A1028    16148  15713  15722    912   1782    415       O  
ATOM    223  N   ALA A1029     103.291  29.505  35.170  1.00 96.94           N  
ANISOU  223  N   ALA A1029    11815  13031  11985    601    587    264       N  
ATOM    224  CA  ALA A1029     102.390  28.717  36.014  1.00 95.89           C  
ANISOU  224  CA  ALA A1029    11562  13021  11850    560    485    242       C  
ATOM    225  C   ALA A1029     103.113  27.504  36.628  1.00 97.32           C  
ANISOU  225  C   ALA A1029    11685  13287  12005    306    245    109       C  
ATOM    226  O   ALA A1029     102.993  27.289  37.832  1.00 97.34           O  
ANISOU  226  O   ALA A1029    11728  13275  11983    169    261     42       O  
ATOM    227  CB  ALA A1029     101.189  28.254  35.209  1.00 97.10           C  
ANISOU  227  CB  ALA A1029    11475  13412  12006    772    374    400       C  
ATOM    228  N   LEU A1030     103.902  26.756  35.817  1.00 91.70           N  
ANISOU  228  N   LEU A1030    10897  12655  11289    267     64     95       N  
ATOM    229  CA  LEU A1030     104.667  25.578  36.254  1.00 90.00           C  
ANISOU  229  CA  LEU A1030    10619  12504  11074     99   -114     33       C  
ATOM    230  C   LEU A1030     105.785  25.936  37.235  1.00 93.79           C  
ANISOU  230  C   LEU A1030    11185  12935  11517   -107    -84    -28       C  
ATOM    231  O   LEU A1030     106.149  25.098  38.057  1.00 93.39           O  
ANISOU  231  O   LEU A1030    11072  12972  11442   -229   -198    -30       O  
ATOM    232  CB  LEU A1030     105.288  24.853  35.054  1.00 89.53           C  
ANISOU  232  CB  LEU A1030    10498  12497  11025    152   -228     47       C  
ATOM    233  CG  LEU A1030     104.367  24.091  34.112  1.00 94.27           C  
ANISOU  233  CG  LEU A1030    11006  13208  11603    248   -329     56       C  
ATOM    234  CD1 LEU A1030     105.053  23.833  32.800  1.00 94.49           C  
ANISOU  234  CD1 LEU A1030    11065  13252  11586    313   -359     48       C  
ATOM    235  CD2 LEU A1030     103.853  22.807  34.749  1.00 96.15           C  
ANISOU  235  CD2 LEU A1030    11166  13487  11881    137   -430     13       C  
ATOM    236  N   THR A1031     106.358  27.151  37.126  1.00 91.20           N  
ANISOU  236  N   THR A1031    10990  12488  11176   -161     71    -64       N  
ATOM    237  CA  THR A1031     107.424  27.616  38.024  1.00 92.15           C  
ANISOU  237  CA  THR A1031    11180  12606  11229   -437     89   -152       C  
ATOM    238  C   THR A1031     106.825  27.853  39.420  1.00 97.67           C  
ANISOU  238  C   THR A1031    11998  13291  11820   -576    157   -243       C  
ATOM    239  O   THR A1031     107.445  27.503  40.427  1.00 97.85           O  
ANISOU  239  O   THR A1031    11993  13459  11727   -803     42   -286       O  
ATOM    240  CB  THR A1031     108.094  28.874  37.453  1.00 99.62           C  
ANISOU  240  CB  THR A1031    12258  13389  12203   -500    278   -189       C  
ATOM    241  OG1 THR A1031     108.623  28.568  36.165  1.00 98.65           O  
ANISOU  241  OG1 THR A1031    12028  13296  12160   -342    229    -85       O  
ATOM    242  CG2 THR A1031     109.212  29.381  38.326  1.00 98.57           C  
ANISOU  242  CG2 THR A1031    12168  13296  11988   -866    276   -304       C  
ATOM    243  N   LYS A1032     105.601  28.415  39.461  1.00 95.18           N  
ANISOU  243  N   LYS A1032    11798  12836  11530   -414    352   -240       N  
ATOM    244  CA  LYS A1032     104.851  28.669  40.693  1.00 96.28           C  
ANISOU  244  CA  LYS A1032    12076  12931  11576   -484    486   -312       C  
ATOM    245  C   LYS A1032     104.422  27.344  41.321  1.00100.26           C  
ANISOU  245  C   LYS A1032    12407  13634  12053   -478    283   -248       C  
ATOM    246  O   LYS A1032     104.425  27.213  42.546  1.00101.48           O  
ANISOU  246  O   LYS A1032    12639  13855  12065   -648    282   -309       O  
ATOM    247  CB  LYS A1032     103.628  29.566  40.414  1.00 99.31           C  
ANISOU  247  CB  LYS A1032    12581  13115  12037   -232    792   -256       C  
ATOM    248  CG  LYS A1032     103.976  30.956  39.883  1.00108.53           C  
ANISOU  248  CG  LYS A1032    13978  14015  13246   -209   1085   -292       C  
ATOM    249  CD  LYS A1032     102.733  31.717  39.464  1.00117.67           C  
ANISOU  249  CD  LYS A1032    15205  15001  14504    139   1406   -142       C  
ATOM    250  CE  LYS A1032     103.071  33.049  38.844  1.00126.21           C  
ANISOU  250  CE  LYS A1032    16530  15774  15652    214   1748   -126       C  
ATOM    251  NZ  LYS A1032     101.858  33.750  38.352  1.00133.85           N  
ANISOU  251  NZ  LYS A1032    17527  16600  16728    633   2085    104       N  
ATOM    252  N   MET A1033     104.095  26.350  40.472  1.00 95.62           N  
ANISOU  252  N   MET A1033    11608  13138  11585   -306    125   -131       N  
ATOM    253  CA  MET A1033     103.683  25.006  40.891  1.00 94.86           C  
ANISOU  253  CA  MET A1033    11360  13174  11509   -301    -27    -62       C  
ATOM    254  C   MET A1033     104.849  24.205  41.466  1.00 99.36           C  
ANISOU  254  C   MET A1033    11876  13868  12008   -459   -196    -39       C  
ATOM    255  O   MET A1033     104.651  23.497  42.453  1.00 99.44           O  
ANISOU  255  O   MET A1033    11862  13964  11957   -515   -234     10       O  
ATOM    256  CB  MET A1033     103.067  24.226  39.727  1.00 96.02           C  
ANISOU  256  CB  MET A1033    11338  13360  11786   -142   -124      9       C  
ATOM    257  CG  MET A1033     101.748  24.778  39.273  1.00100.25           C  
ANISOU  257  CG  MET A1033    11824  13892  12374     27     -6     60       C  
ATOM    258  SD  MET A1033     100.991  23.792  37.972  1.00104.16           S  
ANISOU  258  SD  MET A1033    12091  14536  12948    113   -176    115       S  
ATOM    259  CE  MET A1033     100.691  22.266  38.864  1.00100.55           C  
ANISOU  259  CE  MET A1033    11558  14108  12540    -50   -264    102       C  
ATOM    260  N   ARG A1034     106.056  24.302  40.855  1.00 96.30           N  
ANISOU  260  N   ARG A1034    11447  13510  11631   -504   -277    -33       N  
ATOM    261  CA  ARG A1034     107.242  23.581  41.336  1.00 96.97           C  
ANISOU  261  CA  ARG A1034    11418  13764  11662   -610   -426     56       C  
ATOM    262  C   ARG A1034     107.620  24.083  42.733  1.00104.36           C  
ANISOU  262  C   ARG A1034    12429  14844  12379   -850   -439      8       C  
ATOM    263  O   ARG A1034     108.036  23.291  43.577  1.00105.02           O  
ANISOU  263  O   ARG A1034    12413  15124  12364   -903   -556    130       O  
ATOM    264  CB  ARG A1034     108.426  23.727  40.367  1.00 95.94           C  
ANISOU  264  CB  ARG A1034    11199  13653  11601   -597   -473     94       C  
ATOM    265  CG  ARG A1034     109.474  22.643  40.561  1.00103.33           C  
ANISOU  265  CG  ARG A1034    11946  14763  12552   -580   -599    274       C  
ATOM    266  CD  ARG A1034     110.718  22.861  39.726  1.00110.97           C  
ANISOU  266  CD  ARG A1034    12799  15774  13593   -564   -609    338       C  
ATOM    267  NE  ARG A1034     111.566  21.667  39.716  1.00120.86           N  
ANISOU  267  NE  ARG A1034    13856  17156  14911   -444   -668    565       N  
ATOM    268  CZ  ARG A1034     112.504  21.375  40.614  1.00138.49           C  
ANISOU  268  CZ  ARG A1034    15893  19674  17052   -537   -776    744       C  
ATOM    269  NH1 ARG A1034     112.726  22.185  41.639  1.00127.09           N  
ANISOU  269  NH1 ARG A1034    14443  18438  15408   -822   -870    669       N  
ATOM    270  NH2 ARG A1034     113.209  20.257  40.505  1.00127.65           N  
ANISOU  270  NH2 ARG A1034    14336  18393  15773   -345   -775   1008       N  
ATOM    271  N   ALA A1035     107.434  25.397  42.980  1.00102.91           N  
ANISOU  271  N   ALA A1035    12445  14554  12101   -993   -291   -165       N  
ATOM    272  CA  ALA A1035     107.674  26.031  44.273  1.00105.57           C  
ANISOU  272  CA  ALA A1035    12935  14996  12182  -1279   -260   -287       C  
ATOM    273  C   ALA A1035     106.668  25.545  45.310  1.00111.64           C  
ANISOU  273  C   ALA A1035    13777  15794  12847  -1230   -208   -262       C  
ATOM    274  O   ALA A1035     107.058  25.209  46.426  1.00112.97           O  
ANISOU  274  O   ALA A1035    13930  16202  12792  -1392   -318   -222       O  
ATOM    275  CB  ALA A1035     107.591  27.539  44.133  1.00107.62           C  
ANISOU  275  CB  ALA A1035    13460  15027  12405  -1423    -22   -503       C  
ATOM    276  N   ALA A1036     105.374  25.489  44.922  1.00108.31           N  
ANISOU  276  N   ALA A1036    13405  15167  12581   -999    -42   -252       N  
ATOM    277  CA  ALA A1036     104.255  25.048  45.756  1.00109.10           C  
ANISOU  277  CA  ALA A1036    13550  15265  12640   -920     59   -208       C  
ATOM    278  C   ALA A1036     104.333  23.546  46.075  1.00113.80           C  
ANISOU  278  C   ALA A1036    13943  16029  13266   -857   -120    -12       C  
ATOM    279  O   ALA A1036     103.915  23.147  47.156  1.00114.82           O  
ANISOU  279  O   ALA A1036    14121  16246  13258   -894    -78     41       O  
ATOM    280  CB  ALA A1036     102.939  25.353  45.059  1.00109.09           C  
ANISOU  280  CB  ALA A1036    13549  15060  12838   -679    255   -193       C  
ATOM    281  N   ALA A1037     104.857  22.722  45.143  1.00109.97           N  
ANISOU  281  N   ALA A1037    13266  15562  12957   -751   -271    100       N  
ATOM    282  CA  ALA A1037     104.991  21.268  45.309  1.00110.25           C  
ANISOU  282  CA  ALA A1037    13150  15677  13064   -667   -371    295       C  
ATOM    283  C   ALA A1037     106.099  20.917  46.313  1.00117.63           C  
ANISOU  283  C   ALA A1037    14029  16877  13787   -780   -504    433       C  
ATOM    284  O   ALA A1037     105.905  20.025  47.145  1.00118.42           O  
ANISOU  284  O   ALA A1037    14088  17069  13839   -731   -508    611       O  
ATOM    285  CB  ALA A1037     105.282  20.614  43.967  1.00109.52           C  
ANISOU  285  CB  ALA A1037    12931  15477  13203   -529   -429    340       C  
ATOM    286  N   LEU A1038     107.255  21.616  46.237  1.00116.05           N  
ANISOU  286  N   LEU A1038    13809  16827  13459   -936   -609    376       N  
ATOM    287  CA  LEU A1038     108.394  21.409  47.138  1.00118.60           C  
ANISOU  287  CA  LEU A1038    14012  17506  13543  -1078   -779    526       C  
ATOM    288  C   LEU A1038     108.089  21.942  48.539  1.00126.70           C  
ANISOU  288  C   LEU A1038    15211  18711  14218  -1306   -761    432       C  
ATOM    289  O   LEU A1038     108.587  21.385  49.518  1.00128.82           O  
ANISOU  289  O   LEU A1038    15383  19314  14248  -1370   -893    621       O  
ATOM    290  CB  LEU A1038     109.661  22.084  46.588  1.00118.95           C  
ANISOU  290  CB  LEU A1038    13935  17687  13575  -1220   -899    490       C  
ATOM    291  CG  LEU A1038     110.279  21.502  45.312  1.00121.57           C  
ANISOU  291  CG  LEU A1038    14076  17922  14192   -999   -919    632       C  
ATOM    292  CD1 LEU A1038     111.330  22.415  44.767  1.00122.05           C  
ANISOU  292  CD1 LEU A1038    14051  18073  14248  -1163   -978    556       C  
ATOM    293  CD2 LEU A1038     110.863  20.115  45.546  1.00125.09           C  
ANISOU  293  CD2 LEU A1038    14303  18536  14691   -796   -987    980       C  
ATOM    294  N   ASP A1039     107.274  23.018  48.630  1.00124.52           N  
ANISOU  294  N   ASP A1039    15201  18219  13894  -1406   -573    161       N  
ATOM    295  CA  ASP A1039     106.850  23.643  49.889  1.00127.70           C  
ANISOU  295  CA  ASP A1039    15853  18707  13960  -1618   -469     14       C  
ATOM    296  C   ASP A1039     105.833  22.732  50.593  1.00133.77           C  
ANISOU  296  C   ASP A1039    16638  19465  14725  -1433   -372    181       C  
ATOM    297  O   ASP A1039     105.893  22.576  51.815  1.00136.28           O  
ANISOU  297  O   ASP A1039    17028  20039  14715  -1556   -405    244       O  
ATOM    298  CB  ASP A1039     106.261  25.051  49.615  1.00129.60           C  
ANISOU  298  CB  ASP A1039    16393  18632  14216  -1718   -207   -302       C  
ATOM    299  CG  ASP A1039     105.877  25.908  50.818  1.00143.62           C  
ANISOU  299  CG  ASP A1039    18519  20416  15635  -1974    -18   -531       C  
ATOM    300  OD1 ASP A1039     106.181  25.506  51.963  1.00146.92           O  
ANISOU  300  OD1 ASP A1039    18964  21090  15768  -2050    -78   -447       O  
ATOM    301  OD2 ASP A1039     105.326  27.010  50.608  1.00149.60           O  
ANISOU  301  OD2 ASP A1039    19551  20895  16396  -2077    234   -787       O  
ATOM    302  N   ALA A1040     104.932  22.097  49.813  1.00129.12           N  
ANISOU  302  N   ALA A1040    15966  18613  14483  -1162   -262    264       N  
ATOM    303  CA  ALA A1040     103.920  21.169  50.325  1.00129.68           C  
ANISOU  303  CA  ALA A1040    16017  18631  14624  -1002   -144    428       C  
ATOM    304  C   ALA A1040     104.559  19.857  50.792  1.00136.13           C  
ANISOU  304  C   ALA A1040    16657  19659  15409   -923   -292    739       C  
ATOM    305  O   ALA A1040     104.047  19.230  51.721  1.00137.37           O  
ANISOU  305  O   ALA A1040    16848  19874  15471   -870   -201    899       O  
ATOM    306  CB  ALA A1040     102.879  20.889  49.258  1.00128.08           C  
ANISOU  306  CB  ALA A1040    15732  18138  14794   -807    -21    413       C  
ATOM    307  N   GLN A1041     105.693  19.464  50.165  1.00133.39           N  
ANISOU  307  N   GLN A1041    16122  19416  15144   -890   -481    854       N  
ATOM    308  CA  GLN A1041     106.466  18.258  50.491  1.00135.33           C  
ANISOU  308  CA  GLN A1041    16179  19854  15385   -758   -586   1203       C  
ATOM    309  C   GLN A1041     107.057  18.357  51.911  1.00145.62           C  
ANISOU  309  C   GLN A1041    17490  21591  16247   -896   -701   1354       C  
ATOM    310  O   GLN A1041     107.192  17.339  52.595  1.00147.48           O  
ANISOU  310  O   GLN A1041    17646  21970  16418   -748   -688   1683       O  
ATOM    311  CB  GLN A1041     107.586  18.061  49.454  1.00135.63           C  
ANISOU  311  CB  GLN A1041    16020  19916  15596   -687   -722   1277       C  
ATOM    312  CG  GLN A1041     108.340  16.732  49.565  1.00148.17           C  
ANISOU  312  CG  GLN A1041    17404  21632  17262   -464   -754   1681       C  
ATOM    313  CD  GLN A1041     109.483  16.605  48.581  1.00164.40           C  
ANISOU  313  CD  GLN A1041    19264  23718  19483   -372   -841   1768       C  
ATOM    314  OE1 GLN A1041     110.007  17.592  48.051  1.00157.68           O  
ANISOU  314  OE1 GLN A1041    18393  22906  18612   -528   -937   1553       O  
ATOM    315  NE2 GLN A1041     109.957  15.383  48.386  1.00158.29           N  
ANISOU  315  NE2 GLN A1041    18345  22927  18872   -104   -771   2117       N  
ATOM    316  N   LYS A1042     107.394  19.591  52.344  1.00145.31           N  
ANISOU  316  N   LYS A1042    17564  21757  15889  -1194   -795   1110       N  
ATOM    317  CA  LYS A1042     107.969  19.890  53.660  1.00149.95           C  
ANISOU  317  CA  LYS A1042    18190  22815  15970  -1430   -937   1164       C  
ATOM    318  C   LYS A1042     106.881  19.921  54.753  1.00158.20           C  
ANISOU  318  C   LYS A1042    19502  23823  16785  -1450   -738   1118       C  
ATOM    319  O   LYS A1042     107.195  19.706  55.926  1.00161.10           O  
ANISOU  319  O   LYS A1042    19876  24584  16750  -1528   -826   1299       O  
ATOM    320  CB  LYS A1042     108.716  21.235  53.624  1.00153.47           C  
ANISOU  320  CB  LYS A1042    18717  23428  16169  -1817  -1063    841       C  
ATOM    321  CG  LYS A1042     109.905  21.257  52.664  1.00163.58           C  
ANISOU  321  CG  LYS A1042    19706  24815  17631  -1833  -1259    911       C  
ATOM    322  CD  LYS A1042     110.578  22.618  52.626  1.00174.20           C  
ANISOU  322  CD  LYS A1042    21153  26276  18760  -2265  -1339    567       C  
ATOM    323  N   ALA A1043     105.611  20.181  54.366  1.00155.15           N  
ANISOU  323  N   ALA A1043    19311  22999  16640  -1368   -464    905       N  
ATOM    324  CA  ALA A1043     104.463  20.251  55.281  1.00157.54           C  
ANISOU  324  CA  ALA A1043    19858  23209  16793  -1355   -207    857       C  
ATOM    325  C   ALA A1043     104.018  18.854  55.746  1.00165.40           C  
ANISOU  325  C   ALA A1043    20738  24221  17886  -1103   -130   1236       C  
ATOM    326  O   ALA A1043     104.250  17.865  55.048  1.00163.60           O  
ANISOU  326  O   ALA A1043    20283  23893  17986   -897   -187   1470       O  
ATOM    327  CB  ALA A1043     103.300  20.958  54.599  1.00155.89           C  
ANISOU  327  CB  ALA A1043    19796  22557  16877  -1289     64    593       C  
ATOM    328  N   THR A1044     103.373  18.783  56.928  1.00167.05           N  
ANISOU  328  N   THR A1044    21137  24526  17806  -1125     45   1290       N  
ATOM    329  CA  THR A1044     102.852  17.537  57.497  1.00169.13           C  
ANISOU  329  CA  THR A1044    21340  24784  18136   -905    185   1653       C  
ATOM    330  C   THR A1044     101.307  17.621  57.510  1.00174.80           C  
ANISOU  330  C   THR A1044    22194  25136  19087   -824    542   1539       C  
ATOM    331  O   THR A1044     100.755  18.579  58.060  1.00175.53           O  
ANISOU  331  O   THR A1044    22533  25208  18951   -948    714   1293       O  
ATOM    332  CB  THR A1044     103.452  17.280  58.895  1.00181.40           C  
ANISOU  332  CB  THR A1044    22962  26832  19129   -977     86   1892       C  
ATOM    333  OG1 THR A1044     104.877  17.302  58.806  1.00182.47           O  
ANISOU  333  OG1 THR A1044    22902  27368  19062  -1067   -267   2009       O  
ATOM    334  CG2 THR A1044     103.001  15.951  59.494  1.00181.28           C  
ANISOU  334  CG2 THR A1044    22891  26804  19183   -719    260   2328       C  
ATOM    335  N   PRO A1045     100.601  16.636  56.899  1.00171.92           N  
ANISOU  335  N   PRO A1045    21666  24482  19175   -631    681   1715       N  
ATOM    336  CA  PRO A1045      99.125  16.706  56.846  1.00172.19           C  
ANISOU  336  CA  PRO A1045    21743  24227  19455   -577    999   1633       C  
ATOM    337  C   PRO A1045      98.456  16.585  58.238  1.00181.85           C  
ANISOU  337  C   PRO A1045    23155  25562  20376   -564   1265   1769       C  
ATOM    338  O   PRO A1045      99.072  16.034  59.157  1.00184.11           O  
ANISOU  338  O   PRO A1045    23500  26126  20329   -552   1198   2016       O  
ATOM    339  CB  PRO A1045      98.748  15.507  55.966  1.00172.28           C  
ANISOU  339  CB  PRO A1045    21522  23977  19962   -453   1036   1806       C  
ATOM    340  CG  PRO A1045      99.913  14.584  56.044  1.00177.29           C  
ANISOU  340  CG  PRO A1045    22077  24751  20532   -374    861   2086       C  
ATOM    341  CD  PRO A1045     101.112  15.456  56.171  1.00172.69           C  
ANISOU  341  CD  PRO A1045    21537  24487  19592   -478    579   1974       C  
ATOM    342  N   PRO A1046      97.191  17.086  58.410  1.00180.43           N  
ANISOU  342  N   PRO A1046    23058  25195  20302   -541   1585   1649       N  
ATOM    343  CA  PRO A1046      96.518  16.979  59.729  1.00184.30           C  
ANISOU  343  CA  PRO A1046    23743  25775  20509   -512   1889   1784       C  
ATOM    344  C   PRO A1046      96.349  15.520  60.174  1.00191.27           C  
ANISOU  344  C   PRO A1046    24507  26662  21507   -393   1976   2190       C  
ATOM    345  O   PRO A1046      96.493  15.221  61.360  1.00193.99           O  
ANISOU  345  O   PRO A1046    25015  27236  21455   -373   2061   2398       O  
ATOM    346  CB  PRO A1046      95.155  17.643  59.496  1.00185.74           C  
ANISOU  346  CB  PRO A1046    23925  25704  20944   -453   2231   1631       C  
ATOM    347  CG  PRO A1046      94.963  17.645  58.017  1.00186.51           C  
ANISOU  347  CG  PRO A1046    23734  25592  21538   -424   2088   1533       C  
ATOM    348  CD  PRO A1046      96.330  17.779  57.428  1.00179.94           C  
ANISOU  348  CD  PRO A1046    22895  24868  20608   -511   1700   1429       C  
ATOM    349  N   LYS A1047      96.051  14.619  59.216  1.00187.26           N  
ANISOU  349  N   LYS A1047    23736  25895  21520   -330   1971   2298       N  
ATOM    350  CA  LYS A1047      95.980  13.172  59.426  1.00189.14           C  
ANISOU  350  CA  LYS A1047    23875  26036  21956   -234   2081   2664       C  
ATOM    351  C   LYS A1047      97.416  12.654  59.414  1.00194.52           C  
ANISOU  351  C   LYS A1047    24543  26909  22455   -172   1795   2855       C  
ATOM    352  O   LYS A1047      98.237  13.191  58.666  1.00191.79           O  
ANISOU  352  O   LYS A1047    24140  26637  22093   -227   1501   2660       O  
ATOM    353  CB  LYS A1047      95.078  12.513  58.355  1.00190.05           C  
ANISOU  353  CB  LYS A1047    23749  25788  22674   -264   2195   2630       C  
ATOM    354  CG  LYS A1047      94.925  10.997  58.469  1.00205.38           C  
ANISOU  354  CG  LYS A1047    25628  27522  24885   -214   2375   2961       C  
ATOM    355  CD  LYS A1047      94.092  10.432  57.329  1.00212.92           C  
ANISOU  355  CD  LYS A1047    26366  28141  26392   -343   2445   2840       C  
ATOM    356  CE  LYS A1047      93.981   8.931  57.413  1.00224.94           C  
ANISOU  356  CE  LYS A1047    27888  29385  28194   -337   2672   3128       C  
ATOM    357  NZ  LYS A1047      93.176   8.371  56.296  1.00232.64           N  
ANISOU  357  NZ  LYS A1047    28680  30044  29668   -549   2734   2954       N  
ATOM    358  N   LEU A1048      97.733  11.653  60.263  1.00195.48           N  
ANISOU  358  N   LEU A1048    24705  27136  22432    -37   1901   3269       N  
ATOM    359  CA  LEU A1048      99.074  11.087  60.490  1.00197.44           C  
ANISOU  359  CA  LEU A1048    24912  27645  22462     92   1681   3581       C  
ATOM    360  C   LEU A1048     100.066  12.257  60.809  1.00202.51           C  
ANISOU  360  C   LEU A1048    25615  28753  22575    -40   1328   3384       C  
ATOM    361  O   LEU A1048     101.158  12.353  60.237  1.00200.73           O  
ANISOU  361  O   LEU A1048    25252  28679  22337    -37   1029   3385       O  
ATOM    362  CB  LEU A1048      99.613  10.170  59.346  1.00195.85           C  
ANISOU  362  CB  LEU A1048    24528  27156  22731    202   1619   3693       C  
ATOM    363  CG  LEU A1048      99.717  10.619  57.875  1.00196.31           C  
ANISOU  363  CG  LEU A1048    24463  26992  23135     90   1431   3315       C  
ATOM    364  CD1 LEU A1048     100.918   9.993  57.196  1.00196.16           C  
ANISOU  364  CD1 LEU A1048    24322  26958  23252    237   1274   3500       C  
ATOM    365  CD2 LEU A1048      98.435  10.318  57.102  1.00196.97           C  
ANISOU  365  CD2 LEU A1048    24499  26637  23705    -14   1656   3110       C  
ATOM    366  N   GLU A1049      99.641  13.136  61.748  1.00201.74           N  
ANISOU  366  N   GLU A1049    25741  28867  22043   -178   1404   3208       N  
ATOM    367  CA  GLU A1049     100.394  14.296  62.227  1.00202.96           C  
ANISOU  367  CA  GLU A1049    26035  29436  21644   -390   1145   2963       C  
ATOM    368  C   GLU A1049     101.478  13.829  63.201  1.00211.47           C  
ANISOU  368  C   GLU A1049    27085  31068  22196   -345    932   3347       C  
ATOM    369  O   GLU A1049     102.660  14.098  62.974  1.00211.72           O  
ANISOU  369  O   GLU A1049    26979  31435  22031   -437    572   3341       O  
ATOM    370  CB  GLU A1049      99.439  15.317  62.886  1.00205.48           C  
ANISOU  370  CB  GLU A1049    26661  29714  21698   -544   1398   2638       C  
ATOM    371  CG  GLU A1049     100.103  16.597  63.375  1.00218.04           C  
ANISOU  371  CG  GLU A1049    28482  31654  22711   -833   1204   2302       C  
ATOM    372  CD  GLU A1049      99.194  17.606  64.058  1.00239.00           C  
ANISOU  372  CD  GLU A1049    31511  34213  25087   -970   1531   1972       C  
ATOM    373  OE1 GLU A1049      99.722  18.628  64.552  1.00236.87           O  
ANISOU  373  OE1 GLU A1049    31504  34219  24277  -1248   1426   1688       O  
ATOM    374  OE2 GLU A1049      97.965  17.374  64.119  1.00229.55           O  
ANISOU  374  OE2 GLU A1049    30346  32670  24202   -812   1914   2001       O  
ATOM    375  N   ASP A1050     101.077  13.103  64.268  1.00211.88           N  
ANISOU  375  N   ASP A1050    27236  31245  22025   -195   1158   3721       N  
ATOM    376  CA  ASP A1050     102.012  12.564  65.254  1.00216.70           C  
ANISOU  376  CA  ASP A1050    27798  32427  22112    -98    982   4180       C  
ATOM    377  C   ASP A1050     102.534  11.222  64.722  1.00220.06           C  
ANISOU  377  C   ASP A1050    27935  32712  22967    239    988   4686       C  
ATOM    378  O   ASP A1050     102.186  10.151  65.230  1.00221.67           O  
ANISOU  378  O   ASP A1050    28152  32801  23271    501   1275   5139       O  
ATOM    379  CB  ASP A1050     101.344  12.443  66.644  1.00223.32           C  
ANISOU  379  CB  ASP A1050    28909  33473  22470    -74   1253   4362       C  
ATOM    380  CG  ASP A1050     102.281  12.132  67.806  1.00233.50           C  
ANISOU  380  CG  ASP A1050    31100  33943  23678   -143    994   3949       C  
ATOM    381  OD1 ASP A1050     103.478  11.857  67.556  1.00233.43           O  
ANISOU  381  OD1 ASP A1050    30982  33998  23711    -64    645   4039       O  
ATOM    382  OD2 ASP A1050     101.819  12.176  68.967  1.00238.49           O  
ANISOU  382  OD2 ASP A1050    32670  33649  24296   -274   1144   3451       O  
ATOM    383  N   LYS A1051     103.344  11.305  63.652  1.00214.00           N  
ANISOU  383  N   LYS A1051    26934  31900  22477    235    723   4594       N  
ATOM    384  CA  LYS A1051     103.935  10.173  62.944  1.00213.40           C  
ANISOU  384  CA  LYS A1051    26607  31631  22843    543    746   4993       C  
ATOM    385  C   LYS A1051     105.417  10.447  62.673  1.00217.85           C  
ANISOU  385  C   LYS A1051    26903  32687  23184    536    323   5111       C  
ATOM    386  O   LYS A1051     105.765  11.557  62.262  1.00215.87           O  
ANISOU  386  O   LYS A1051    26642  32615  22764    231     39   4674       O  
ATOM    387  CB  LYS A1051     103.164   9.927  61.627  1.00211.00           C  
ANISOU  387  CB  LYS A1051    26296  30607  23266    541    953   4692       C  
ATOM    388  CG  LYS A1051     103.579   8.679  60.827  1.00224.47           C  
ANISOU  388  CG  LYS A1051    27843  31959  25488    835   1097   5033       C  
ATOM    389  CD  LYS A1051     103.121   7.336  61.412  1.00236.20           C  
ANISOU  389  CD  LYS A1051    29774  32717  27256    864   1369   4979       C  
ATOM    390  CE  LYS A1051     101.624   7.136  61.356  1.00244.06           C  
ANISOU  390  CE  LYS A1051    31159  32971  28602    513   1577   4350       C  
ATOM    391  NZ  LYS A1051     101.244   5.781  61.830  1.00252.93           N  
ANISOU  391  NZ  LYS A1051    32818  33336  29948    195   1591   3907       N  
ATOM    392  N   SER A1052     106.284   9.435  62.903  1.00218.38           N  
ANISOU  392  N   SER A1052    26742  32965  23268    883    314   5727       N  
ATOM    393  CA  SER A1052     107.736   9.523  62.694  1.00218.14           C  
ANISOU  393  CA  SER A1052    26632  33063  23190    884    -84   5671       C  
ATOM    394  C   SER A1052     108.071   9.785  61.210  1.00219.33           C  
ANISOU  394  C   SER A1052    26396  33213  23728    888   -137   5623       C  
ATOM    395  O   SER A1052     107.332   9.320  60.343  1.00215.29           O  
ANISOU  395  O   SER A1052    25999  32012  23791    985    163   5467       O  
ATOM    396  CB  SER A1052     108.423   8.244  63.167  1.00220.30           C  
ANISOU  396  CB  SER A1052    27455  32448  23801   1085   -103   5537       C  
ATOM    397  OG  SER A1052     107.964   7.101  62.465  1.00226.68           O  
ANISOU  397  OG  SER A1052    28472  32398  25259   1212    211   5429       O  
ATOM    398  N   PRO A1053     109.159  10.534  60.886  1.00216.21           N  
ANISOU  398  N   PRO A1053    25763  33259  23129    705   -531   5495       N  
ATOM    399  CA  PRO A1053     109.466  10.802  59.467  1.00211.92           C  
ANISOU  399  CA  PRO A1053    25113  32341  23067    670   -576   5189       C  
ATOM    400  C   PRO A1053     109.969   9.556  58.726  1.00216.23           C  
ANISOU  400  C   PRO A1053    25463  32593  24101   1125   -365   5653       C  
ATOM    401  O   PRO A1053     109.788   9.462  57.511  1.00211.98           O  
ANISOU  401  O   PRO A1053    24953  31531  24057   1154   -241   5398       O  
ATOM    402  CB  PRO A1053     110.566  11.873  59.529  1.00214.86           C  
ANISOU  402  CB  PRO A1053    25267  33341  23031    350  -1030   5017       C  
ATOM    403  CG  PRO A1053     110.596  12.348  60.957  1.00219.72           C  
ANISOU  403  CG  PRO A1053    26414  33855  23213    152  -1204   4622       C  
ATOM    404  CD  PRO A1053     110.139  11.190  61.773  1.00217.45           C  
ANISOU  404  CD  PRO A1053    26301  33391  22929    471   -955   5022       C  
ATOM    405  N   ASP A1054     110.570   8.592  59.458  1.00216.30           N  
ANISOU  405  N   ASP A1054    25554  32566  24062   1419   -324   6029       N  
ATOM    406  CA  ASP A1054     111.106   7.348  58.894  1.00215.50           C  
ANISOU  406  CA  ASP A1054    25579  31825  24477   1770   -123   6160       C  
ATOM    407  C   ASP A1054     109.986   6.317  58.605  1.00217.74           C  
ANISOU  407  C   ASP A1054    26114  31425  25192   1938    386   6235       C  
ATOM    408  O   ASP A1054     110.271   5.248  58.057  1.00216.84           O  
ANISOU  408  O   ASP A1054    26143  30746  25499   2161    611   6295       O  
ATOM    409  CB  ASP A1054     112.147   6.727  59.851  1.00217.89           C  
ANISOU  409  CB  ASP A1054    26306  31805  24676   1801   -404   5953       C  
ATOM    410  CG  ASP A1054     113.373   7.586  60.133  1.00226.93           C  
ANISOU  410  CG  ASP A1054    27740  32783  25700   1524   -963   5244       C  
ATOM    411  OD1 ASP A1054     113.381   8.771  59.723  1.00227.08           O  
ANISOU  411  OD1 ASP A1054    27584  33196  25502   1267  -1141   5031       O  
ATOM    412  OD2 ASP A1054     114.308   7.084  60.793  1.00232.55           O  
ANISOU  412  OD2 ASP A1054    28832  33008  26518   1577  -1206   4957       O  
ATOM    413  N   SER A1055     108.724   6.646  58.957  1.00215.61           N  
ANISOU  413  N   SER A1055    25692  31469  24762   1908    641   6502       N  
ATOM    414  CA  SER A1055     107.550   5.789  58.757  1.00214.35           C  
ANISOU  414  CA  SER A1055    25821  30583  25039   1980   1119   6457       C  
ATOM    415  C   SER A1055     107.233   5.614  57.248  1.00212.87           C  
ANISOU  415  C   SER A1055    25724  29713  25445   1901   1280   6038       C  
ATOM    416  O   SER A1055     107.419   6.567  56.484  1.00208.51           O  
ANISOU  416  O   SER A1055    25102  29234  24889   1652    990   5578       O  
ATOM    417  CB  SER A1055     106.346   6.380  59.484  1.00217.33           C  
ANISOU  417  CB  SER A1055    26429  30964  25182   1674   1141   6132       C  
ATOM    418  OG  SER A1055     105.202   5.549  59.397  1.00226.96           O  
ANISOU  418  OG  SER A1055    27888  31544  26802   1704   1591   6114       O  
ATOM    419  N   PRO A1056     106.748   4.418  56.801  1.00209.88           N  
ANISOU  419  N   PRO A1056    25520  28669  25556   2083   1753   6180       N  
ATOM    420  CA  PRO A1056     106.484   4.216  55.361  1.00206.06           C  
ANISOU  420  CA  PRO A1056    25140  27582  25570   1971   1896   5766       C  
ATOM    421  C   PRO A1056     105.380   5.126  54.797  1.00203.56           C  
ANISOU  421  C   PRO A1056    24933  27093  25318   1516   1746   5071       C  
ATOM    422  O   PRO A1056     105.470   5.497  53.627  1.00199.41           O  
ANISOU  422  O   PRO A1056    24398  26364  25005   1379   1645   4685       O  
ATOM    423  CB  PRO A1056     106.034   2.753  55.284  1.00211.05           C  
ANISOU  423  CB  PRO A1056    25998  27562  26630   2181   2472   6051       C  
ATOM    424  CG  PRO A1056     106.579   2.117  56.507  1.00219.38           C  
ANISOU  424  CG  PRO A1056    27097  28847  27412   2428   2486   6525       C  
ATOM    425  CD  PRO A1056     106.507   3.173  57.560  1.00216.12           C  
ANISOU  425  CD  PRO A1056    26435  29226  26454   2397   2201   6738       C  
ATOM    426  N   GLU A1057     104.349   5.478  55.603  1.00199.31           N  
ANISOU  426  N   GLU A1057    24488  26642  24598   1314   1756   4946       N  
ATOM    427  CA  GLU A1057     103.252   6.347  55.144  1.00194.83           C  
ANISOU  427  CA  GLU A1057    23984  25947  24095    939   1650   4364       C  
ATOM    428  C   GLU A1057     103.713   7.835  55.078  1.00195.03           C  
ANISOU  428  C   GLU A1057    23890  26447  23767    769   1203   4052       C  
ATOM    429  O   GLU A1057     103.109   8.612  54.332  1.00191.37           O  
ANISOU  429  O   GLU A1057    23442  25853  23419    532   1094   3584       O  
ATOM    430  CB  GLU A1057     101.967   6.221  56.000  1.00197.29           C  
ANISOU  430  CB  GLU A1057    24422  26165  24374    806   1876   4356       C  
ATOM    431  CG  GLU A1057     102.132   6.135  57.514  1.00210.51           C  
ANISOU  431  CG  GLU A1057    26125  28233  25628    966   1920   4787       C  
ATOM    432  CD  GLU A1057     102.522   4.782  58.089  1.00230.17           C  
ANISOU  432  CD  GLU A1057    28664  30576  28212   1304   2261   5396       C  
ATOM    433  OE1 GLU A1057     102.700   3.818  57.308  1.00221.85           O  
ANISOU  433  OE1 GLU A1057    27657  29039  27597   1425   2524   5489       O  
ATOM    434  OE2 GLU A1057     102.618   4.680  59.333  1.00226.31           O  
ANISOU  434  OE2 GLU A1057    28197  30441  27350   1450   2303   5784       O  
ATOM    435  N   MET A1058     104.797   8.209  55.805  1.00192.45           N  
ANISOU  435  N   MET A1058    23438  26667  23016    880    959   4321       N  
ATOM    436  CA  MET A1058     105.385   9.557  55.743  1.00189.84           C  
ANISOU  436  CA  MET A1058    23008  26769  22353    679    563   4036       C  
ATOM    437  C   MET A1058     106.347   9.662  54.571  1.00189.81           C  
ANISOU  437  C   MET A1058    22847  26713  22560    735    411   3954       C  
ATOM    438  O   MET A1058     106.445  10.724  53.952  1.00186.53           O  
ANISOU  438  O   MET A1058    22407  26366  22100    517    189   3557       O  
ATOM    439  CB  MET A1058     106.103   9.938  57.044  1.00195.85           C  
ANISOU  439  CB  MET A1058    23690  28187  22536    690    346   4325       C  
ATOM    440  CG  MET A1058     105.168  10.405  58.138  1.00200.81           C  
ANISOU  440  CG  MET A1058    24518  28955  22826    519    414   4212       C  
ATOM    441  SD  MET A1058     104.308  11.970  57.795  1.00201.49           S  
ANISOU  441  SD  MET A1058    24771  28971  22814    124    303   3518       S  
ATOM    442  CE  MET A1058     105.703  13.114  57.723  1.00198.78           C  
ANISOU  442  CE  MET A1058    24285  29193  22048    -75   -144   3392       C  
ATOM    443  N   LYS A1059     107.059   8.562  54.268  1.00186.73           N  
ANISOU  443  N   LYS A1059    22366  26177  22405   1048    576   4350       N  
ATOM    444  CA  LYS A1059     107.989   8.488  53.143  1.00184.68           C  
ANISOU  444  CA  LYS A1059    21970  25821  22379   1161    517   4332       C  
ATOM    445  C   LYS A1059     107.211   8.440  51.820  1.00183.08           C  
ANISOU  445  C   LYS A1059    21935  25035  22592   1021    670   3879       C  
ATOM    446  O   LYS A1059     107.686   8.981  50.825  1.00180.19           O  
ANISOU  446  O   LYS A1059    21502  24643  22319    959    527   3634       O  
ATOM    447  CB  LYS A1059     108.932   7.279  53.267  1.00191.23           C  
ANISOU  447  CB  LYS A1059    22673  26648  23339   1591    727   4940       C  
ATOM    448  CG  LYS A1059     109.967   7.414  54.381  1.00208.02           C  
ANISOU  448  CG  LYS A1059    24524  29493  25020   1749    493   5439       C  
ATOM    449  CD  LYS A1059     110.923   6.233  54.397  1.00221.42           C  
ANISOU  449  CD  LYS A1059    26048  31194  26887   2244    729   6100       C  
ATOM    450  CE  LYS A1059     112.026   6.413  55.408  1.00226.45           C  
ANISOU  450  CE  LYS A1059    27111  31735  27194   1962    158   5460       C  
ATOM    451  NZ  LYS A1059     112.947   5.248  55.434  1.00232.82           N  
ANISOU  451  NZ  LYS A1059    28378  31844  28237   2017     74   5090       N  
ATOM    452  N   ASP A1060     106.006   7.824  51.826  1.00178.22           N  
ANISOU  452  N   ASP A1060    21522  23995  22198    945    950   3772       N  
ATOM    453  CA  ASP A1060     105.111   7.738  50.665  1.00174.74           C  
ANISOU  453  CA  ASP A1060    21219  23075  22099    749   1074   3343       C  
ATOM    454  C   ASP A1060     104.531   9.119  50.335  1.00172.85           C  
ANISOU  454  C   ASP A1060    20951  23008  21718    456    794   2874       C  
ATOM    455  O   ASP A1060     104.389   9.452  49.157  1.00169.79           O  
ANISOU  455  O   ASP A1060    20576  22435  21504    340    735   2543       O  
ATOM    456  CB  ASP A1060     103.975   6.726  50.928  1.00178.45           C  
ANISOU  456  CB  ASP A1060    21865  23129  22809    696   1437   3392       C  
ATOM    457  CG  ASP A1060     102.988   6.529  49.787  1.00186.63           C  
ANISOU  457  CG  ASP A1060    23013  23730  24168    432   1555   2963       C  
ATOM    458  OD1 ASP A1060     103.411   6.607  48.613  1.00185.83           O  
ANISOU  458  OD1 ASP A1060    22921  23485  24200    405   1491   2738       O  
ATOM    459  OD2 ASP A1060     101.819   6.188  50.069  1.00192.64           O  
ANISOU  459  OD2 ASP A1060    23848  24299  25049    251   1735   2883       O  
ATOM    460  N   PHE A1061     104.199   9.916  51.381  1.00168.13           N  
ANISOU  460  N   PHE A1061    20336  22756  20790    354    655   2864       N  
ATOM    461  CA  PHE A1061     103.648  11.269  51.252  1.00164.60           C  
ANISOU  461  CA  PHE A1061    19897  22453  20191    119    465   2472       C  
ATOM    462  C   PHE A1061     104.623  12.177  50.503  1.00165.16           C  
ANISOU  462  C   PHE A1061    19872  22705  20174     82    200   2300       C  
ATOM    463  O   PHE A1061     104.218  12.844  49.549  1.00162.33           O  
ANISOU  463  O   PHE A1061    19530  22216  19931    -44    137   1961       O  
ATOM    464  CB  PHE A1061     103.317  11.866  52.634  1.00167.79           C  
ANISOU  464  CB  PHE A1061    20360  23173  20221     45    438   2534       C  
ATOM    465  CG  PHE A1061     102.844  13.307  52.599  1.00167.35           C  
ANISOU  465  CG  PHE A1061    20359  23230  19995   -163    317   2156       C  
ATOM    466  CD1 PHE A1061     101.511  13.614  52.345  1.00169.22           C  
ANISOU  466  CD1 PHE A1061    20649  23238  20409   -260    467   1924       C  
ATOM    467  CD2 PHE A1061     103.725  14.353  52.853  1.00169.54           C  
ANISOU  467  CD2 PHE A1061    20633  23847  19936   -266     84   2055       C  
ATOM    468  CE1 PHE A1061     101.075  14.947  52.315  1.00168.88           C  
ANISOU  468  CE1 PHE A1061    20668  23268  20232   -388    421   1629       C  
ATOM    469  CE2 PHE A1061     103.288  15.684  52.820  1.00171.14           C  
ANISOU  469  CE2 PHE A1061    20946  24076  20004   -448     51   1707       C  
ATOM    470  CZ  PHE A1061     101.964  15.971  52.562  1.00168.00           C  
ANISOU  470  CZ  PHE A1061    20616  23416  19801   -474    240   1516       C  
ATOM    471  N   ARG A1062     105.901  12.202  50.935  1.00161.94           N  
ANISOU  471  N   ARG A1062    19342  22628  19561    193     52   2562       N  
ATOM    472  CA  ARG A1062     106.939  13.021  50.308  1.00159.73           C  
ANISOU  472  CA  ARG A1062    18936  22551  19203    140   -184   2443       C  
ATOM    473  C   ARG A1062     107.317  12.448  48.931  1.00159.76           C  
ANISOU  473  C   ARG A1062    18902  22235  19565    280    -95   2417       C  
ATOM    474  O   ARG A1062     107.705  13.217  48.050  1.00157.51           O  
ANISOU  474  O   ARG A1062    18570  21969  19309    202   -228   2195       O  
ATOM    475  CB  ARG A1062     108.183  13.134  51.204  1.00163.21           C  
ANISOU  475  CB  ARG A1062    19194  23514  19303    183   -381   2762       C  
ATOM    476  CG  ARG A1062     107.924  13.857  52.529  1.00176.20           C  
ANISOU  476  CG  ARG A1062    20914  25531  20501    -23   -500   2720       C  
ATOM    477  CD  ARG A1062     109.176  13.995  53.380  1.00192.12           C  
ANISOU  477  CD  ARG A1062    22720  28154  22122    -43   -745   3023       C  
ATOM    478  NE  ARG A1062     109.748  12.695  53.750  1.00206.46           N  
ANISOU  478  NE  ARG A1062    24362  30085  23998    302   -655   3585       N  
ATOM    479  CZ  ARG A1062     109.449  12.026  54.860  1.00224.62           C  
ANISOU  479  CZ  ARG A1062    26709  32524  26111    434   -545   3921       C  
ATOM    480  NH1 ARG A1062     108.587  12.528  55.736  1.00211.46           N  
ANISOU  480  NH1 ARG A1062    25260  30916  24168    233   -521   3730       N  
ATOM    481  NH2 ARG A1062     110.017  10.852  55.106  1.00215.45           N  
ANISOU  481  NH2 ARG A1062    25390  31434  25038    796   -420   4475       N  
ATOM    482  N   HIS A1063     107.164  11.113  48.735  1.00155.35           N  
ANISOU  482  N   HIS A1063    18403  21349  19273    474    170   2627       N  
ATOM    483  CA  HIS A1063     107.444  10.443  47.457  1.00153.50           C  
ANISOU  483  CA  HIS A1063    18210  20749  19363    592    328   2575       C  
ATOM    484  C   HIS A1063     106.455  10.902  46.378  1.00150.82           C  
ANISOU  484  C   HIS A1063    17995  20140  19171    370    317   2106       C  
ATOM    485  O   HIS A1063     106.846  11.057  45.220  1.00149.27           O  
ANISOU  485  O   HIS A1063    17804  19825  19088    379    293   1938       O  
ATOM    486  CB  HIS A1063     107.394   8.916  47.609  1.00157.39           C  
ANISOU  486  CB  HIS A1063    18806  20902  20094    817    682   2888       C  
ATOM    487  CG  HIS A1063     107.654   8.176  46.335  1.00161.14           C  
ANISOU  487  CG  HIS A1063    19397  20948  20880    915    909   2800       C  
ATOM    488  ND1 HIS A1063     108.940   7.940  45.888  1.00164.29           N  
ANISOU  488  ND1 HIS A1063    19687  21402  21335   1175    951   3032       N  
ATOM    489  CD2 HIS A1063     106.779   7.628  45.460  1.00162.53           C  
ANISOU  489  CD2 HIS A1063    19795  20660  21301    766   1117   2503       C  
ATOM    490  CE1 HIS A1063     108.809   7.273  44.752  1.00163.95           C  
ANISOU  490  CE1 HIS A1063    19847  20887  21560   1194   1211   2851       C  
ATOM    491  NE2 HIS A1063     107.526   7.061  44.455  1.00163.36           N  
ANISOU  491  NE2 HIS A1063    19982  20499  21590    925   1303   2514       N  
ATOM    492  N   GLY A1064     105.202  11.133  46.777  1.00143.66           N  
ANISOU  492  N   GLY A1064    17163  19180  18241    189    338   1933       N  
ATOM    493  CA  GLY A1064     104.150  11.619  45.892  1.00139.91           C  
ANISOU  493  CA  GLY A1064    16739  18549  17869    -13    307   1552       C  
ATOM    494  C   GLY A1064     104.486  12.958  45.265  1.00138.02           C  
ANISOU  494  C   GLY A1064    16436  18506  17499    -80     75   1324       C  
ATOM    495  O   GLY A1064     104.147  13.197  44.103  1.00136.01           O  
ANISOU  495  O   GLY A1064    16202  18123  17353   -151     46   1079       O  
ATOM    496  N   PHE A1065     105.189  13.830  46.025  1.00132.36           N  
ANISOU  496  N   PHE A1065    15652  18109  16529    -77    -81   1406       N  
ATOM    497  CA  PHE A1065     105.615  15.139  45.541  1.00129.52           C  
ANISOU  497  CA  PHE A1065    15260  17905  16048   -162   -256   1204       C  
ATOM    498  C   PHE A1065     106.878  15.012  44.675  1.00131.32           C  
ANISOU  498  C   PHE A1065    15404  18144  16348    -54   -312   1270       C  
ATOM    499  O   PHE A1065     107.082  15.864  43.815  1.00129.73           O  
ANISOU  499  O   PHE A1065    15201  17940  16151   -108   -391   1074       O  
ATOM    500  CB  PHE A1065     105.848  16.130  46.688  1.00131.88           C  
ANISOU  500  CB  PHE A1065    15560  18512  16036   -277   -369   1211       C  
ATOM    501  CG  PHE A1065     104.563  16.528  47.370  1.00133.29           C  
ANISOU  501  CG  PHE A1065    15850  18654  16140   -375   -274   1088       C  
ATOM    502  CD1 PHE A1065     103.729  17.490  46.812  1.00134.70           C  
ANISOU  502  CD1 PHE A1065    16086  18731  16361   -447   -246    828       C  
ATOM    503  CD2 PHE A1065     104.195  15.956  48.579  1.00137.41           C  
ANISOU  503  CD2 PHE A1065    16409  19256  16544   -363   -184   1271       C  
ATOM    504  CE1 PHE A1065     102.527  17.841  47.430  1.00136.06           C  
ANISOU  504  CE1 PHE A1065    16335  18873  16490   -491   -112    758       C  
ATOM    505  CE2 PHE A1065     102.999  16.320  49.206  1.00140.53           C  
ANISOU  505  CE2 PHE A1065    16902  19613  16878   -434    -54   1173       C  
ATOM    506  CZ  PHE A1065     102.174  17.263  48.630  1.00137.08           C  
ANISOU  506  CZ  PHE A1065    16504  19069  16509   -493    -13    919       C  
ATOM    507  N   ASP A1066     107.693  13.942  44.854  1.00127.55           N  
ANISOU  507  N   ASP A1066    14859  17657  15946    129   -228   1571       N  
ATOM    508  CA  ASP A1066     108.858  13.701  43.989  1.00126.57           C  
ANISOU  508  CA  ASP A1066    14646  17516  15929    280   -214   1672       C  
ATOM    509  C   ASP A1066     108.376  13.302  42.588  1.00125.11           C  
ANISOU  509  C   ASP A1066    14608  16957  15971    296    -72   1442       C  
ATOM    510  O   ASP A1066     108.985  13.706  41.597  1.00123.53           O  
ANISOU  510  O   ASP A1066    14386  16740  15808    333    -98   1352       O  
ATOM    511  CB  ASP A1066     109.807  12.636  44.575  1.00131.93           C  
ANISOU  511  CB  ASP A1066    15200  18285  16641    529   -108   2114       C  
ATOM    512  CG  ASP A1066     110.634  13.090  45.775  1.00147.20           C  
ANISOU  512  CG  ASP A1066    16914  20723  18291    510   -312   2379       C  
ATOM    513  OD1 ASP A1066     110.843  14.319  45.929  1.00147.21           O  
ANISOU  513  OD1 ASP A1066    16857  20990  18087    282   -535   2186       O  
ATOM    514  OD2 ASP A1066     111.190  12.216  46.473  1.00157.04           O  
ANISOU  514  OD2 ASP A1066    18039  22111  19518    724   -237   2796       O  
ATOM    515  N   ILE A1067     107.248  12.564  42.512  1.00119.28           N  
ANISOU  515  N   ILE A1067    14019  15948  15355    231     71   1332       N  
ATOM    516  CA  ILE A1067     106.598  12.181  41.252  1.00117.58           C  
ANISOU  516  CA  ILE A1067    13951  15432  15292    153    174   1065       C  
ATOM    517  C   ILE A1067     105.991  13.439  40.610  1.00116.89           C  
ANISOU  517  C   ILE A1067    13837  15479  15097     -6    -20    773       C  
ATOM    518  O   ILE A1067     106.143  13.654  39.406  1.00115.65           O  
ANISOU  518  O   ILE A1067    13727  15255  14959    -10    -36    605       O  
ATOM    519  CB  ILE A1067     105.520  11.067  41.472  1.00122.19           C  
ANISOU  519  CB  ILE A1067    14670  15731  16024     55    376   1033       C  
ATOM    520  CG1 ILE A1067     106.119   9.815  42.161  1.00125.49           C  
ANISOU  520  CG1 ILE A1067    15143  15973  16565    259    635   1379       C  
ATOM    521  CG2 ILE A1067     104.813  10.700  40.146  1.00122.73           C  
ANISOU  521  CG2 ILE A1067    14886  15550  16197   -115    447    709       C  
ATOM    522  CD1 ILE A1067     105.098   8.702  42.507  1.00135.69           C  
ANISOU  522  CD1 ILE A1067    16591  16939  18024    147    891   1377       C  
ATOM    523  N   LEU A1068     105.325  14.274  41.437  1.00110.93           N  
ANISOU  523  N   LEU A1068    13019  14910  14218   -109   -134    741       N  
ATOM    524  CA  LEU A1068     104.645  15.509  41.045  1.00108.02           C  
ANISOU  524  CA  LEU A1068    12626  14657  13759   -210   -256    532       C  
ATOM    525  C   LEU A1068     105.644  16.537  40.486  1.00107.81           C  
ANISOU  525  C   LEU A1068    12570  14751  13642   -161   -358    495       C  
ATOM    526  O   LEU A1068     105.394  17.070  39.412  1.00106.45           O  
ANISOU  526  O   LEU A1068    12418  14556  13472   -172   -393    336       O  
ATOM    527  CB  LEU A1068     103.890  16.098  42.256  1.00108.19           C  
ANISOU  527  CB  LEU A1068    12622  14812  13672   -283   -268    560       C  
ATOM    528  CG  LEU A1068     102.958  17.292  42.003  1.00112.06           C  
ANISOU  528  CG  LEU A1068    13097  15377  14103   -341   -306    395       C  
ATOM    529  CD1 LEU A1068     101.763  16.882  41.173  1.00112.42           C  
ANISOU  529  CD1 LEU A1068    13092  15349  14275   -396   -286    281       C  
ATOM    530  CD2 LEU A1068     102.441  17.854  43.309  1.00115.20           C  
ANISOU  530  CD2 LEU A1068    13516  15876  14381   -382   -250    442       C  
ATOM    531  N   VAL A1069     106.775  16.790  41.191  1.00102.82           N  
ANISOU  531  N   VAL A1069    11871  14274  12923   -120   -405    661       N  
ATOM    532  CA  VAL A1069     107.827  17.730  40.755  1.00101.31           C  
ANISOU  532  CA  VAL A1069    11624  14207  12661   -121   -486    642       C  
ATOM    533  C   VAL A1069     108.452  17.207  39.434  1.00103.02           C  
ANISOU  533  C   VAL A1069    11849  14283  13012     10   -416    644       C  
ATOM    534  O   VAL A1069     108.751  18.006  38.542  1.00101.95           O  
ANISOU  534  O   VAL A1069    11722  14154  12860      9   -439    539       O  
ATOM    535  CB  VAL A1069     108.907  17.962  41.857  1.00106.57           C  
ANISOU  535  CB  VAL A1069    12168  15145  13180   -169   -576    828       C  
ATOM    536  CG1 VAL A1069     110.104  18.746  41.328  1.00106.70           C  
ANISOU  536  CG1 VAL A1069    12087  15292  13163   -207   -642    826       C  
ATOM    537  CG2 VAL A1069     108.312  18.669  43.069  1.00106.62           C  
ANISOU  537  CG2 VAL A1069    12232  15288  12992   -334   -624    763       C  
ATOM    538  N   GLY A1070     108.587  15.884  39.317  1.00 98.85           N  
ANISOU  538  N   GLY A1070    11353  13595  12612    125   -287    759       N  
ATOM    539  CA  GLY A1070     109.113  15.236  38.120  1.00 98.62           C  
ANISOU  539  CA  GLY A1070    11395  13376  12701    253   -150    744       C  
ATOM    540  C   GLY A1070     108.319  15.557  36.866  1.00 99.82           C  
ANISOU  540  C   GLY A1070    11680  13413  12835    173   -159    461       C  
ATOM    541  O   GLY A1070     108.891  15.999  35.868  1.00 98.76           O  
ANISOU  541  O   GLY A1070    11565  13282  12677    232   -148    404       O  
ATOM    542  N   GLN A1071     106.977  15.392  36.932  1.00 95.27           N  
ANISOU  542  N   GLN A1071    11166  12784  12249     33   -190    304       N  
ATOM    543  CA  GLN A1071     106.047  15.688  35.831  1.00 94.14           C  
ANISOU  543  CA  GLN A1071    11090  12632  12047    -66   -244     68       C  
ATOM    544  C   GLN A1071     106.023  17.200  35.512  1.00 94.83           C  
ANISOU  544  C   GLN A1071    11103  12912  12015    -47   -372     31       C  
ATOM    545  O   GLN A1071     105.793  17.566  34.357  1.00 94.41           O  
ANISOU  545  O   GLN A1071    11093  12890  11887    -43   -403    -89       O  
ATOM    546  CB  GLN A1071     104.631  15.200  36.165  1.00 96.21           C  
ANISOU  546  CB  GLN A1071    11349  12870  12335   -238   -261    -34       C  
ATOM    547  CG  GLN A1071     104.497  13.681  36.311  1.00111.31           C  
ANISOU  547  CG  GLN A1071    13389  14523  14380   -306    -82    -43       C  
ATOM    548  CD  GLN A1071     103.100  13.243  36.703  1.00128.88           C  
ANISOU  548  CD  GLN A1071    15581  16738  16648   -527    -90   -141       C  
ATOM    549  OE1 GLN A1071     102.372  13.936  37.427  1.00124.16           O  
ANISOU  549  OE1 GLN A1071    14834  16323  16019   -565   -191    -94       O  
ATOM    550  NE2 GLN A1071     102.737  12.030  36.324  1.00120.85           N  
ANISOU  550  NE2 GLN A1071    14716  15479  15721   -683     64   -267       N  
ATOM    551  N   ILE A1072     106.271  18.069  36.534  1.00 89.27           N  
ANISOU  551  N   ILE A1072    10314  12329  11275    -45   -421    134       N  
ATOM    552  CA  ILE A1072     106.371  19.535  36.394  1.00 87.28           C  
ANISOU  552  CA  ILE A1072    10043  12184  10935    -38   -466    106       C  
ATOM    553  C   ILE A1072     107.626  19.857  35.574  1.00 89.80           C  
ANISOU  553  C   ILE A1072    10369  12495  11256     42   -431    144       C  
ATOM    554  O   ILE A1072     107.567  20.708  34.689  1.00 89.12           O  
ANISOU  554  O   ILE A1072    10320  12423  11120     81   -418     90       O  
ATOM    555  CB  ILE A1072     106.376  20.272  37.780  1.00 89.89           C  
ANISOU  555  CB  ILE A1072    10343  12606  11206   -121   -483    157       C  
ATOM    556  CG1 ILE A1072     105.012  20.103  38.504  1.00 90.29           C  
ANISOU  556  CG1 ILE A1072    10389  12661  11254   -171   -472    126       C  
ATOM    557  CG2 ILE A1072     106.715  21.767  37.614  1.00 89.97           C  
ANISOU  557  CG2 ILE A1072    10393  12649  11144   -142   -457    112       C  
ATOM    558  CD1 ILE A1072     104.933  20.639  39.948  1.00 96.94           C  
ANISOU  558  CD1 ILE A1072    11253  13576  12006   -254   -447    161       C  
ATOM    559  N   ASP A1073     108.743  19.152  35.855  1.00 86.26           N  
ANISOU  559  N   ASP A1073     9869  12031  10873     92   -388    276       N  
ATOM    560  CA  ASP A1073     110.021  19.323  35.163  1.00 86.45           C  
ANISOU  560  CA  ASP A1073     9852  12067  10928    183   -324    359       C  
ATOM    561  C   ASP A1073     109.924  18.846  33.712  1.00 91.86           C  
ANISOU  561  C   ASP A1073    10670  12611  11622    289   -224    261       C  
ATOM    562  O   ASP A1073     110.525  19.475  32.833  1.00 91.34           O  
ANISOU  562  O   ASP A1073    10618  12558  11529    353   -171    262       O  
ATOM    563  CB  ASP A1073     111.135  18.575  35.899  1.00 89.24           C  
ANISOU  563  CB  ASP A1073    10061  12492  11356    246   -292    589       C  
ATOM    564  CG  ASP A1073     111.439  19.169  37.257  1.00 95.78           C  
ANISOU  564  CG  ASP A1073    10744  13548  12099    102   -421    684       C  
ATOM    565  OD1 ASP A1073     111.108  20.350  37.469  1.00 94.28           O  
ANISOU  565  OD1 ASP A1073    10592  13418  11814    -51   -485    554       O  
ATOM    566  OD2 ASP A1073     112.065  18.471  38.085  1.00102.28           O  
ANISOU  566  OD2 ASP A1073    11426  14499  12937    146   -436    903       O  
ATOM    567  N   ASP A1074     109.147  17.761  33.454  1.00 89.93           N  
ANISOU  567  N   ASP A1074    10543  12232  11394    277   -184    161       N  
ATOM    568  CA  ASP A1074     108.906  17.264  32.098  1.00 91.09           C  
ANISOU  568  CA  ASP A1074    10861  12265  11483    303   -100      5       C  
ATOM    569  C   ASP A1074     108.107  18.289  31.305  1.00 93.51           C  
ANISOU  569  C   ASP A1074    11186  12713  11631    255   -221   -122       C  
ATOM    570  O   ASP A1074     108.389  18.504  30.128  1.00 94.34           O  
ANISOU  570  O   ASP A1074    11395  12822  11628    314   -173   -191       O  
ATOM    571  CB  ASP A1074     108.180  15.907  32.111  1.00 94.97           C  
ANISOU  571  CB  ASP A1074    11488  12575  12020    216    -21   -107       C  
ATOM    572  CG  ASP A1074     108.988  14.735  32.646  1.00110.36           C  
ANISOU  572  CG  ASP A1074    13477  14318  14137    335    191     52       C  
ATOM    573  OD1 ASP A1074     110.240  14.784  32.557  1.00110.86           O  
ANISOU  573  OD1 ASP A1074    13470  14391  14262    519    296    238       O  
ATOM    574  OD2 ASP A1074     108.370  13.713  33.020  1.00119.40           O  
ANISOU  574  OD2 ASP A1074    14729  15279  15357    255    289      2       O  
ATOM    575  N   ALA A1075     107.151  18.961  31.970  1.00 87.91           N  
ANISOU  575  N   ALA A1075    10375  12126  10900    179   -348   -117       N  
ATOM    576  CA  ALA A1075     106.316  20.000  31.373  1.00 86.87           C  
ANISOU  576  CA  ALA A1075    10219  12143  10643    191   -431   -157       C  
ATOM    577  C   ALA A1075     107.126  21.290  31.142  1.00 88.45           C  
ANISOU  577  C   ALA A1075    10415  12366  10826    299   -370    -58       C  
ATOM    578  O   ALA A1075     106.989  21.907  30.083  1.00 88.15           O  
ANISOU  578  O   ALA A1075    10422  12398  10673    389   -358    -58       O  
ATOM    579  CB  ALA A1075     105.121  20.273  32.266  1.00 87.17           C  
ANISOU  579  CB  ALA A1075    10152  12266  10702    111   -514   -150       C  
ATOM    580  N   LEU A1076     107.993  21.673  32.117  1.00 83.83           N  
ANISOU  580  N   LEU A1076     9774  11739  10338    270   -328     31       N  
ATOM    581  CA  LEU A1076     108.886  22.837  32.025  1.00 83.25           C  
ANISOU  581  CA  LEU A1076     9699  11662  10272    293   -245    102       C  
ATOM    582  C   LEU A1076     109.871  22.664  30.881  1.00 87.80           C  
ANISOU  582  C   LEU A1076    10314  12204  10843    400   -145    141       C  
ATOM    583  O   LEU A1076     110.195  23.652  30.228  1.00 87.44           O  
ANISOU  583  O   LEU A1076    10308  12149  10766    456    -54    184       O  
ATOM    584  CB  LEU A1076     109.649  23.081  33.342  1.00 83.15           C  
ANISOU  584  CB  LEU A1076     9597  11670  10325    153   -255    159       C  
ATOM    585  CG  LEU A1076     108.902  23.821  34.471  1.00 87.38           C  
ANISOU  585  CG  LEU A1076    10158  12217  10826     38   -274    112       C  
ATOM    586  CD1 LEU A1076     109.584  23.619  35.815  1.00 87.66           C  
ANISOU  586  CD1 LEU A1076    10114  12336  10859   -138   -330    144       C  
ATOM    587  CD2 LEU A1076     108.747  25.318  34.158  1.00 89.88           C  
ANISOU  587  CD2 LEU A1076    10581  12455  11115     58   -140     94       C  
ATOM    588  N   LYS A1077     110.318  21.404  30.618  1.00 85.37           N  
ANISOU  588  N   LYS A1077    10020  11846  10572    443   -116    137       N  
ATOM    589  CA  LYS A1077     111.221  21.060  29.508  1.00 86.40           C  
ANISOU  589  CA  LYS A1077    10221  11913  10693    571     31    164       C  
ATOM    590  C   LYS A1077     110.573  21.449  28.179  1.00 90.72           C  
ANISOU  590  C   LYS A1077    10922  12494  11053    643     46     71       C  
ATOM    591  O   LYS A1077     111.193  22.141  27.377  1.00 90.86           O  
ANISOU  591  O   LYS A1077    10977  12517  11028    741    162    140       O  
ATOM    592  CB  LYS A1077     111.563  19.550  29.535  1.00 90.02           C  
ANISOU  592  CB  LYS A1077    10726  12253  11224    609    106    152       C  
ATOM    593  CG  LYS A1077     112.508  19.052  28.437  1.00107.39           C  
ANISOU  593  CG  LYS A1077    13058  14330  13417    762    328    160       C  
ATOM    594  CD  LYS A1077     113.992  19.155  28.769  1.00119.37           C  
ANISOU  594  CD  LYS A1077    14415  15873  15066    886    475    384       C  
ATOM    595  CE  LYS A1077     114.834  18.576  27.658  1.00131.49           C  
ANISOU  595  CE  LYS A1077    16090  17252  16620   1078    756    414       C  
ATOM    596  NZ  LYS A1077     114.610  17.113  27.438  1.00141.34           N  
ANISOU  596  NZ  LYS A1077    17451  18302  17950   1131    883    391       N  
ATOM    597  N   LEU A1078     109.298  21.049  27.988  1.00 87.23           N  
ANISOU  597  N   LEU A1078    10543  12113  10487    580    -78    -65       N  
ATOM    598  CA  LEU A1078     108.500  21.315  26.786  1.00 88.20           C  
ANISOU  598  CA  LEU A1078    10764  12372  10374    618   -129   -140       C  
ATOM    599  C   LEU A1078     108.161  22.805  26.659  1.00 93.15           C  
ANISOU  599  C   LEU A1078    11327  13116  10952    714   -143     -5       C  
ATOM    600  O   LEU A1078     108.232  23.342  25.551  1.00 94.41           O  
ANISOU  600  O   LEU A1078    11565  13364  10942    839    -89     48       O  
ATOM    601  CB  LEU A1078     107.205  20.482  26.812  1.00 88.65           C  
ANISOU  601  CB  LEU A1078    10826  12524  10334    461   -288   -301       C  
ATOM    602  CG  LEU A1078     107.389  18.962  26.774  1.00 93.71           C  
ANISOU  602  CG  LEU A1078    11604  12990  11010    344   -215   -464       C  
ATOM    603  CD1 LEU A1078     106.161  18.242  27.252  1.00 94.03           C  
ANISOU  603  CD1 LEU A1078    11599  13084  11044    130   -356   -598       C  
ATOM    604  CD2 LEU A1078     107.848  18.481  25.405  1.00 97.99           C  
ANISOU  604  CD2 LEU A1078    12381  13492  11360    380    -84   -586       C  
ATOM    605  N   ALA A1079     107.806  23.471  27.783  1.00 89.15           N  
ANISOU  605  N   ALA A1079    10706  12585  10581    670   -175     61       N  
ATOM    606  CA  ALA A1079     107.471  24.902  27.809  1.00 89.42           C  
ANISOU  606  CA  ALA A1079    10722  12644  10609    767   -109    191       C  
ATOM    607  C   ALA A1079     108.669  25.754  27.358  1.00 94.50           C  
ANISOU  607  C   ALA A1079    11437  13169  11300    843     89    294       C  
ATOM    608  O   ALA A1079     108.485  26.701  26.590  1.00 94.80           O  
ANISOU  608  O   ALA A1079    11536  13230  11253    995    197    414       O  
ATOM    609  CB  ALA A1079     107.026  25.316  29.208  1.00 89.10           C  
ANISOU  609  CB  ALA A1079    10606  12544  10703    670   -125    193       C  
ATOM    610  N   ASN A1080     109.894  25.384  27.804  1.00 91.48           N  
ANISOU  610  N   ASN A1080    11023  12680  11054    746    150    281       N  
ATOM    611  CA  ASN A1080     111.147  26.069  27.456  1.00 92.47           C  
ANISOU  611  CA  ASN A1080    11163  12717  11257    763    339    381       C  
ATOM    612  C   ASN A1080     111.563  25.780  26.001  1.00 96.67           C  
ANISOU  612  C   ASN A1080    11795  13277  11660    934    446    423       C  
ATOM    613  O   ASN A1080     112.333  26.552  25.427  1.00 97.35           O  
ANISOU  613  O   ASN A1080    11918  13302  11770    998    635    537       O  
ATOM    614  CB  ASN A1080     112.274  25.657  28.404  1.00 96.23           C  
ANISOU  614  CB  ASN A1080    11496  13164  11904    600    337    390       C  
ATOM    615  CG  ASN A1080     112.077  26.093  29.837  1.00136.17           C  
ANISOU  615  CG  ASN A1080    16483  18217  17039    396    259    350       C  
ATOM    616  OD1 ASN A1080     111.468  27.126  30.131  1.00133.07           O  
ANISOU  616  OD1 ASN A1080    16174  17749  16637    350    331    335       O  
ATOM    617  ND2 ASN A1080     112.666  25.349  30.761  1.00133.74           N  
ANISOU  617  ND2 ASN A1080    16033  17983  16801    275    152    350       N  
ATOM    618  N   GLU A1081     111.063  24.680  25.413  1.00 92.70           N  
ANISOU  618  N   GLU A1081    11360  12854  11008    981    350    317       N  
ATOM    619  CA  GLU A1081     111.345  24.327  24.021  1.00 94.19           C  
ANISOU  619  CA  GLU A1081    11700  13083  11005   1118    455    310       C  
ATOM    620  C   GLU A1081     110.326  24.999  23.075  1.00100.04           C  
ANISOU  620  C   GLU A1081    12528  14006  11478   1238    400    356       C  
ATOM    621  O   GLU A1081     110.515  24.985  21.859  1.00101.64           O  
ANISOU  621  O   GLU A1081    12870  14290  11457   1359    487    376       O  
ATOM    622  CB  GLU A1081     111.337  22.799  23.827  1.00 96.03           C  
ANISOU  622  CB  GLU A1081    12018  13287  11181   1069    423    140       C  
ATOM    623  CG  GLU A1081     112.494  22.090  24.510  1.00104.59           C  
ANISOU  623  CG  GLU A1081    13015  14210  12513   1052    546    185       C  
ATOM    624  CD  GLU A1081     112.492  20.575  24.440  1.00124.38           C  
ANISOU  624  CD  GLU A1081    15637  16604  15017   1037    598     51       C  
ATOM    625  OE1 GLU A1081     113.341  19.962  25.123  1.00126.26           O  
ANISOU  625  OE1 GLU A1081    15777  16725  15470   1078    720    152       O  
ATOM    626  OE2 GLU A1081     111.625  19.996  23.748  1.00114.76           O  
ANISOU  626  OE2 GLU A1081    14601  15419  13583    974    529   -143       O  
ATOM    627  N   GLY A1082     109.287  25.609  23.649  1.00 96.43           N  
ANISOU  627  N   GLY A1082    11977  13629  11034   1227    279    404       N  
ATOM    628  CA  GLY A1082     108.233  26.283  22.900  1.00 98.08           C  
ANISOU  628  CA  GLY A1082    12194  14062  11011   1382    222    526       C  
ATOM    629  C   GLY A1082     107.152  25.327  22.442  1.00103.88           C  
ANISOU  629  C   GLY A1082    12901  15076  11492   1305    -29    389       C  
ATOM    630  O   GLY A1082     106.481  25.575  21.436  1.00106.07           O  
ANISOU  630  O   GLY A1082    13177  15645  11481   1423   -109    486       O  
ATOM    631  N   LYS A1083     106.984  24.219  23.182  1.00 99.67           N  
ANISOU  631  N   LYS A1083    12338  14476  11054   1090   -149    175       N  
ATOM    632  CA  LYS A1083     106.003  23.173  22.896  1.00101.11           C  
ANISOU  632  CA  LYS A1083    12505  14874  11040    919   -367    -11       C  
ATOM    633  C   LYS A1083     104.844  23.304  23.888  1.00105.37           C  
ANISOU  633  C   LYS A1083    12822  15518  11695    840   -531     24       C  
ATOM    634  O   LYS A1083     104.835  22.640  24.926  1.00102.94           O  
ANISOU  634  O   LYS A1083    12473  15041  11601    685   -551    -85       O  
ATOM    635  CB  LYS A1083     106.675  21.786  22.959  1.00103.26           C  
ANISOU  635  CB  LYS A1083    12936  14933  11366    745   -306   -256       C  
ATOM    636  CG  LYS A1083     107.803  21.608  21.941  1.00113.82           C  
ANISOU  636  CG  LYS A1083    14498  16154  12593    852    -90   -278       C  
ATOM    637  CD  LYS A1083     108.487  20.264  22.075  1.00119.81           C  
ANISOU  637  CD  LYS A1083    15418  16645  13458    742     51   -470       C  
ATOM    638  CE  LYS A1083     109.593  20.097  21.069  1.00127.03           C  
ANISOU  638  CE  LYS A1083    16552  17433  14282    887    321   -467       C  
ATOM    639  NZ  LYS A1083     110.282  18.790  21.233  1.00133.50           N  
ANISOU  639  NZ  LYS A1083    17533  17950  15241    840    532   -608       N  
ATOM    640  N   VAL A1084     103.880  24.202  23.569  1.00104.95           N  
ANISOU  640  N   VAL A1084    12619  15753  11505    984   -615    220       N  
ATOM    641  CA  VAL A1084     102.723  24.571  24.403  1.00105.16           C  
ANISOU  641  CA  VAL A1084    12409  15907  11640    991   -711    330       C  
ATOM    642  C   VAL A1084     101.772  23.372  24.589  1.00110.47           C  
ANISOU  642  C   VAL A1084    12954  16780  12240    708   -948    132       C  
ATOM    643  O   VAL A1084     101.558  22.958  25.727  1.00108.14           O  
ANISOU  643  O   VAL A1084    12589  16327  12173    574   -951     57       O  
ATOM    644  CB  VAL A1084     101.947  25.777  23.806  1.00111.57           C  
ANISOU  644  CB  VAL A1084    13080  17001  12310   1284   -693    654       C  
ATOM    645  CG1 VAL A1084     100.841  26.240  24.751  1.00111.49           C  
ANISOU  645  CG1 VAL A1084    12835  17057  12467   1350   -700    807       C  
ATOM    646  CG2 VAL A1084     102.882  26.928  23.498  1.00111.04           C  
ANISOU  646  CG2 VAL A1084    13182  16704  12304   1539   -415    842       C  
ATOM    647  N   LYS A1085     101.188  22.844  23.480  1.00110.59           N  
ANISOU  647  N   LYS A1085    12942  17158  11920    593  -1138     50       N  
ATOM    648  CA  LYS A1085     100.228  21.728  23.495  1.00112.68           C  
ANISOU  648  CA  LYS A1085    13085  17656  12073    251  -1366   -162       C  
ATOM    649  C   LYS A1085     100.844  20.466  24.117  1.00115.85           C  
ANISOU  649  C   LYS A1085    13691  17660  12667    -21  -1279   -470       C  
ATOM    650  O   LYS A1085     100.120  19.707  24.761  1.00115.75           O  
ANISOU  650  O   LYS A1085    13562  17674  12744   -278  -1376   -596       O  
ATOM    651  CB  LYS A1085      99.705  21.407  22.079  1.00119.34           C  
ANISOU  651  CB  LYS A1085    13928  18961  12456    119  -1572   -243       C  
ATOM    652  CG  LYS A1085      98.598  22.349  21.556  1.00132.35           C  
ANISOU  652  CG  LYS A1085    15223  21193  13869    297  -1767     84       C  
ATOM    653  CD  LYS A1085      99.016  23.812  21.355  1.00137.58           C  
ANISOU  653  CD  LYS A1085    15865  21830  14581    785  -1581    485       C  
ATOM    654  CE  LYS A1085      97.859  24.678  20.924  1.00145.57           C  
ANISOU  654  CE  LYS A1085    16500  23415  15394   1008  -1735    867       C  
ATOM    655  NZ  LYS A1085      98.269  26.095  20.755  1.00150.49           N  
ANISOU  655  NZ  LYS A1085    17149  23932  16098   1505  -1475   1275       N  
ATOM    656  N   GLU A1086     102.171  20.265  23.957  1.00111.77           N  
ANISOU  656  N   GLU A1086    13454  16781  12232     58  -1069   -548       N  
ATOM    657  CA  GLU A1086     102.908  19.146  24.555  1.00110.79           C  
ANISOU  657  CA  GLU A1086    13521  16260  12315   -100   -924   -751       C  
ATOM    658  C   GLU A1086     103.007  19.332  26.075  1.00112.56           C  
ANISOU  658  C   GLU A1086    13612  16263  12892    -47   -860   -629       C  
ATOM    659  O   GLU A1086     102.782  18.379  26.823  1.00112.19           O  
ANISOU  659  O   GLU A1086    13575  16056  12998   -236   -845   -747       O  
ATOM    660  CB  GLU A1086     104.317  18.983  23.947  1.00111.97           C  
ANISOU  660  CB  GLU A1086    13951  16142  12449     29   -694   -797       C  
ATOM    661  CG  GLU A1086     104.397  18.648  22.462  1.00128.03           C  
ANISOU  661  CG  GLU A1086    16205  18334  14108    -29   -692   -955       C  
ATOM    662  CD  GLU A1086     104.211  19.747  21.426  1.00159.77           C  
ANISOU  662  CD  GLU A1086    20174  22692  17839    178   -766   -771       C  
ATOM    663  OE1 GLU A1086     104.766  19.585  20.316  1.00164.08           O  
ANISOU  663  OE1 GLU A1086    20962  23234  18149    234   -645   -841       O  
ATOM    664  OE2 GLU A1086     103.640  20.813  21.750  1.00156.35           O  
ANISOU  664  OE2 GLU A1086    19487  22475  17446    332   -879   -521       O  
ATOM    665  N   ALA A1087     103.348  20.568  26.524  1.00107.51           N  
ANISOU  665  N   ALA A1087    12880  15605  12364    195   -798   -398       N  
ATOM    666  CA  ALA A1087     103.465  20.938  27.938  1.00105.08           C  
ANISOU  666  CA  ALA A1087    12474  15128  12322    234   -735   -291       C  
ATOM    667  C   ALA A1087     102.104  20.875  28.634  1.00110.05           C  
ANISOU  667  C   ALA A1087    12894  15928  12992    134   -859   -265       C  
ATOM    668  O   ALA A1087     102.029  20.380  29.759  1.00108.30           O  
ANISOU  668  O   ALA A1087    12641  15558  12950     33   -828   -290       O  
ATOM    669  CB  ALA A1087     104.056  22.331  28.072  1.00104.55           C  
ANISOU  669  CB  ALA A1087    12407  15004  12313    456   -614   -100       C  
ATOM    670  N   GLN A1088     101.024  21.345  27.950  1.00109.26           N  
ANISOU  670  N   GLN A1088    12628  16174  12712    173   -992   -184       N  
ATOM    671  CA  GLN A1088      99.643  21.315  28.453  1.00110.29           C  
ANISOU  671  CA  GLN A1088    12492  16544  12871     94  -1107   -117       C  
ATOM    672  C   GLN A1088      99.167  19.867  28.610  1.00116.17           C  
ANISOU  672  C   GLN A1088    13222  17292  13625   -258  -1210   -349       C  
ATOM    673  O   GLN A1088      98.422  19.576  29.546  1.00115.41           O  
ANISOU  673  O   GLN A1088    12962  17213  13675   -367  -1223   -325       O  
ATOM    674  CB  GLN A1088      98.691  22.099  27.531  1.00114.20           C  
ANISOU  674  CB  GLN A1088    12766  17477  13149    247  -1229     80       C  
ATOM    675  CG  GLN A1088      98.936  23.612  27.522  1.00125.41           C  
ANISOU  675  CG  GLN A1088    14194  18847  14609    622  -1054    361       C  
ATOM    676  CD  GLN A1088      98.019  24.398  26.600  1.00142.88           C  
ANISOU  676  CD  GLN A1088    16179  21496  16612    850  -1133    637       C  
ATOM    677  OE1 GLN A1088      97.327  23.855  25.729  1.00140.22           O  
ANISOU  677  OE1 GLN A1088    15676  21582  16020    717  -1372    612       O  
ATOM    678  NE2 GLN A1088      98.039  25.715  26.737  1.00132.77           N  
ANISOU  678  NE2 GLN A1088    14902  20129  15417   1196   -915    918       N  
ATOM    679  N   ALA A1089      99.626  18.959  27.715  1.00115.16           N  
ANISOU  679  N   ALA A1089    13301  17104  13352   -438  -1233   -577       N  
ATOM    680  CA  ALA A1089      99.318  17.524  27.766  1.00117.23           C  
ANISOU  680  CA  ALA A1089    13645  17268  13628   -801  -1254   -839       C  
ATOM    681  C   ALA A1089     100.058  16.850  28.928  1.00119.87           C  
ANISOU  681  C   ALA A1089    14133  17154  14258   -811  -1050   -868       C  
ATOM    682  O   ALA A1089      99.485  15.995  29.604  1.00120.05           O  
ANISOU  682  O   ALA A1089    14117  17087  14411  -1041  -1031   -952       O  
ATOM    683  CB  ALA A1089      99.690  16.857  26.449  1.00120.48           C  
ANISOU  683  CB  ALA A1089    14302  17702  13773   -966  -1270  -1084       C  
ATOM    684  N   ALA A1090     101.332  17.242  29.155  1.00115.05           N  
ANISOU  684  N   ALA A1090    13676  16292  13746   -566   -896   -771       N  
ATOM    685  CA  ALA A1090     102.167  16.728  30.241  1.00113.64           C  
ANISOU  685  CA  ALA A1090    13598  15771  13808   -520   -722   -724       C  
ATOM    686  C   ALA A1090     101.630  17.184  31.590  1.00117.62           C  
ANISOU  686  C   ALA A1090    13912  16310  14467   -482   -742   -564       C  
ATOM    687  O   ALA A1090     101.637  16.406  32.543  1.00116.72           O  
ANISOU  687  O   ALA A1090    13822  16014  14512   -563   -653   -553       O  
ATOM    688  CB  ALA A1090     103.606  17.191  30.062  1.00112.78           C  
ANISOU  688  CB  ALA A1090    13619  15506  13726   -286   -594   -630       C  
ATOM    689  N   ALA A1091     101.126  18.438  31.654  1.00115.30           N  
ANISOU  689  N   ALA A1091    13451  16239  14119   -343   -820   -428       N  
ATOM    690  CA  ALA A1091     100.556  19.056  32.854  1.00115.06           C  
ANISOU  690  CA  ALA A1091    13274  16244  14199   -283   -794   -285       C  
ATOM    691  C   ALA A1091      99.213  18.422  33.235  1.00123.05           C  
ANISOU  691  C   ALA A1091    14108  17387  15260   -476   -854   -312       C  
ATOM    692  O   ALA A1091      98.774  18.555  34.381  1.00122.04           O  
ANISOU  692  O   ALA A1091    13898  17222  15248   -468   -784   -218       O  
ATOM    693  CB  ALA A1091     100.371  20.550  32.632  1.00115.41           C  
ANISOU  693  CB  ALA A1091    13238  16438  14174    -63   -787   -136       C  
ATOM    694  N   GLU A1092      98.563  17.735  32.283  1.00123.84           N  
ANISOU  694  N   GLU A1092    14148  17654  15250   -679   -975   -449       N  
ATOM    695  CA  GLU A1092      97.284  17.084  32.537  1.00126.74           C  
ANISOU  695  CA  GLU A1092    14311  18185  15661   -934  -1044   -493       C  
ATOM    696  C   GLU A1092      97.505  15.762  33.304  1.00131.70           C  
ANISOU  696  C   GLU A1092    15094  18482  16464  -1146   -904   -606       C  
ATOM    697  O   GLU A1092      96.585  15.292  33.974  1.00132.71           O  
ANISOU  697  O   GLU A1092    15068  18652  16705  -1325   -884   -590       O  
ATOM    698  CB  GLU A1092      96.535  16.849  31.223  1.00131.55           C  
ANISOU  698  CB  GLU A1092    14798  19137  16049  -1141  -1244   -620       C  
ATOM    699  CG  GLU A1092      95.134  17.451  31.209  1.00145.93           C  
ANISOU  699  CG  GLU A1092    16206  21418  17821  -1150  -1392   -450       C  
ATOM    700  CD  GLU A1092      94.945  18.955  31.301  1.00166.20           C  
ANISOU  700  CD  GLU A1092    18597  24185  20368   -750  -1373   -146       C  
ATOM    701  OE1 GLU A1092      95.944  19.705  31.221  1.00159.61           O  
ANISOU  701  OE1 GLU A1092    17972  23160  19512   -479  -1273    -87       O  
ATOM    702  OE2 GLU A1092      93.773  19.384  31.391  1.00160.99           O  
ANISOU  702  OE2 GLU A1092    17576  23879  19714   -712  -1437     45       O  
ATOM    703  N   GLN A1093      98.742  15.207  33.261  1.00127.64           N  
ANISOU  703  N   GLN A1093    14869  17638  15991  -1089   -772   -673       N  
ATOM    704  CA  GLN A1093      99.121  14.003  34.008  1.00128.15           C  
ANISOU  704  CA  GLN A1093    15105  17352  16232  -1195   -581   -704       C  
ATOM    705  C   GLN A1093      99.277  14.319  35.504  1.00130.73           C  
ANISOU  705  C   GLN A1093    15368  17607  16698  -1028   -491   -479       C  
ATOM    706  O   GLN A1093      99.271  13.395  36.319  1.00130.97           O  
ANISOU  706  O   GLN A1093    15470  17420  16872  -1106   -339   -436       O  
ATOM    707  CB  GLN A1093     100.417  13.384  33.462  1.00129.58           C  
ANISOU  707  CB  GLN A1093    15583  17237  16413  -1118   -435   -782       C  
ATOM    708  CG  GLN A1093     100.284  12.777  32.067  1.00148.53           C  
ANISOU  708  CG  GLN A1093    18147  19626  18663  -1339   -449  -1057       C  
ATOM    709  CD  GLN A1093     101.571  12.151  31.565  1.00168.48           C  
ANISOU  709  CD  GLN A1093    20992  21817  21208  -1219   -228  -1113       C  
ATOM    710  OE1 GLN A1093     102.678  12.436  32.046  1.00161.44           O  
ANISOU  710  OE1 GLN A1093    20125  20826  20391   -916   -142   -917       O  
ATOM    711  NE2 GLN A1093     101.456  11.322  30.541  1.00164.34           N  
ANISOU  711  NE2 GLN A1093    20710  21138  20594  -1466   -124  -1388       N  
ATOM    712  N   LEU A1094      99.410  15.620  35.862  1.00126.08           N  
ANISOU  712  N   LEU A1094    14673  17187  16046   -808   -558   -338       N  
ATOM    713  CA  LEU A1094      99.525  16.095  37.249  1.00125.00           C  
ANISOU  713  CA  LEU A1094    14503  17026  15966   -683   -480   -164       C  
ATOM    714  C   LEU A1094      98.222  15.842  38.010  1.00131.71           C  
ANISOU  714  C   LEU A1094    15189  17957  16899   -811   -439   -116       C  
ATOM    715  O   LEU A1094      98.255  15.629  39.223  1.00131.01           O  
ANISOU  715  O   LEU A1094    15131  17775  16873   -788   -322      0       O  
ATOM    716  CB  LEU A1094      99.886  17.597  37.292  1.00123.24           C  
ANISOU  716  CB  LEU A1094    14253  16931  15640   -479   -520    -86       C  
ATOM    717  CG  LEU A1094     101.252  18.004  36.725  1.00126.44           C  
ANISOU  717  CG  LEU A1094    14795  17267  15981   -354   -535    -97       C  
ATOM    718  CD1 LEU A1094     101.344  19.489  36.531  1.00125.66           C  
ANISOU  718  CD1 LEU A1094    14673  17276  15796   -211   -545    -52       C  
ATOM    719  CD2 LEU A1094     102.375  17.536  37.602  1.00128.24           C  
ANISOU  719  CD2 LEU A1094    15120  17351  16252   -321   -462    -10       C  
ATOM    720  N   LYS A1095      97.080  15.846  37.285  1.00131.25           N  
ANISOU  720  N   LYS A1095    14934  18110  16823   -953   -536   -185       N  
ATOM    721  CA  LYS A1095      95.744  15.578  37.829  1.00133.51           C  
ANISOU  721  CA  LYS A1095    14992  18531  17204  -1103   -503   -130       C  
ATOM    722  C   LYS A1095      95.656  14.144  38.359  1.00140.06           C  
ANISOU  722  C   LYS A1095    15921  19113  18183  -1341   -367   -182       C  
ATOM    723  O   LYS A1095      95.099  13.932  39.433  1.00140.38           O  
ANISOU  723  O   LYS A1095    15887  19121  18328  -1364   -235    -58       O  
ATOM    724  CB  LYS A1095      94.655  15.819  36.767  1.00138.32           C  
ANISOU  724  CB  LYS A1095    15323  19493  17740  -1234   -677   -180       C  
ATOM    725  CG  LYS A1095      94.574  17.257  36.270  1.00150.80           C  
ANISOU  725  CG  LYS A1095    16780  21325  19191   -950   -760    -53       C  
ATOM    726  CD  LYS A1095      93.473  17.427  35.250  1.00162.51           C  
ANISOU  726  CD  LYS A1095    17935  23234  20577  -1054   -945    -33       C  
ATOM    727  CE  LYS A1095      93.381  18.837  34.730  1.00171.04           C  
ANISOU  727  CE  LYS A1095    18898  24547  21541   -714   -980    157       C  
ATOM    728  NZ  LYS A1095      92.284  18.975  33.741  1.00182.27           N  
ANISOU  728  NZ  LYS A1095    19943  26471  22839   -783  -1179    245       N  
ATOM    729  N   THR A1096      96.235  13.168  37.615  1.00138.21           N  
ANISOU  729  N   THR A1096    15889  18668  17958  -1498   -349   -355       N  
ATOM    730  CA  THR A1096      96.275  11.745  37.983  1.00140.32           C  
ANISOU  730  CA  THR A1096    16326  18606  18385  -1708   -149   -409       C  
ATOM    731  C   THR A1096      97.037  11.590  39.314  1.00143.75           C  
ANISOU  731  C   THR A1096    16895  18823  18901  -1473     35   -178       C  
ATOM    732  O   THR A1096      96.603  10.831  40.182  1.00144.94           O  
ANISOU  732  O   THR A1096    17060  18820  19191  -1572    217    -83       O  
ATOM    733  CB  THR A1096      96.917  10.921  36.848  1.00149.37           C  
ANISOU  733  CB  THR A1096    17727  19529  19497  -1850   -112   -639       C  
ATOM    734  OG1 THR A1096      96.245  11.197  35.616  1.00150.55           O  
ANISOU  734  OG1 THR A1096    17747  19967  19486  -2063   -326   -847       O  
ATOM    735  CG2 THR A1096      96.897   9.419  37.121  1.00150.43           C  
ANISOU  735  CG2 THR A1096    18084  19257  19816  -2084    165   -714       C  
ATOM    736  N   THR A1097      98.143  12.345  39.479  1.00138.54           N  
ANISOU  736  N   THR A1097    16314  18192  18134  -1181    -18    -74       N  
ATOM    737  CA  THR A1097      98.962  12.353  40.692  1.00137.72           C  
ANISOU  737  CA  THR A1097    16298  18001  18029   -968     89    155       C  
ATOM    738  C   THR A1097      98.194  13.089  41.814  1.00142.43           C  
ANISOU  738  C   THR A1097    16748  18788  18579   -929     94    283       C  
ATOM    739  O   THR A1097      98.270  12.674  42.973  1.00142.61           O  
ANISOU  739  O   THR A1097    16823  18741  18621   -879    233    461       O  
ATOM    740  CB  THR A1097     100.333  12.998  40.393  1.00143.01           C  
ANISOU  740  CB  THR A1097    17048  18709  18580   -745     -1    194       C  
ATOM    741  OG1 THR A1097     100.936  12.320  39.289  1.00142.18           O  
ANISOU  741  OG1 THR A1097    17080  18423  18519   -767     38     72       O  
ATOM    742  CG2 THR A1097     101.283  12.969  41.590  1.00141.28           C  
ANISOU  742  CG2 THR A1097    16879  18485  18315   -563     65    439       C  
ATOM    743  N   ARG A1098      97.430  14.151  41.457  1.00139.58           N  
ANISOU  743  N   ARG A1098    16216  18667  18153   -931    -24    216       N  
ATOM    744  CA  ARG A1098      96.641  14.952  42.404  1.00140.08           C  
ANISOU  744  CA  ARG A1098    16159  18889  18176   -862     36    328       C  
ATOM    745  C   ARG A1098      95.472  14.109  42.965  1.00147.33           C  
ANISOU  745  C   ARG A1098    16950  19782  19247  -1041    180    387       C  
ATOM    746  O   ARG A1098      95.134  14.248  44.143  1.00147.62           O  
ANISOU  746  O   ARG A1098    16983  19836  19269   -979    327    534       O  
ATOM    747  CB  ARG A1098      96.122  16.244  41.730  1.00140.29           C  
ANISOU  747  CB  ARG A1098    16037  19141  18126   -766    -69    282       C  
ATOM    748  CG  ARG A1098      95.519  17.257  42.708  1.00152.40           C  
ANISOU  748  CG  ARG A1098    17519  20779  19606   -625     65    402       C  
ATOM    749  CD  ARG A1098      94.016  17.437  42.625  1.00166.98           C  
ANISOU  749  CD  ARG A1098    19075  22818  21553   -651    123    473       C  
ATOM    750  NE  ARG A1098      93.613  18.279  41.495  1.00179.08           N  
ANISOU  750  NE  ARG A1098    20436  24553  23054   -555      1    459       N  
ATOM    751  CZ  ARG A1098      93.234  17.822  40.306  1.00197.59           C  
ANISOU  751  CZ  ARG A1098    22599  27053  25423   -704   -183    382       C  
ATOM    752  NH1 ARG A1098      92.870  18.668  39.349  1.00187.23           N  
ANISOU  752  NH1 ARG A1098    21122  25976  24041   -574   -290    423       N  
ATOM    753  NH2 ARG A1098      93.188  16.516  40.071  1.00186.32           N  
ANISOU  753  NH2 ARG A1098    21169  25549  24075   -991   -240    268       N  
ATOM    754  N   ASN A1099      94.892  13.217  42.136  1.00146.21           N  
ANISOU  754  N   ASN A1099    16722  19597  19235  -1294    154    263       N  
ATOM    755  CA  ASN A1099      93.797  12.329  42.542  1.00149.17           C  
ANISOU  755  CA  ASN A1099    16962  19936  19782  -1540    298    294       C  
ATOM    756  C   ASN A1099      94.313  11.214  43.465  1.00153.83           C  
ANISOU  756  C   ASN A1099    17780  20198  20470  -1555    533    411       C  
ATOM    757  O   ASN A1099      93.572  10.759  44.337  1.00155.44           O  
ANISOU  757  O   ASN A1099    17913  20360  20785  -1646    721    538       O  
ATOM    758  CB  ASN A1099      93.103  11.726  41.318  1.00153.54           C  
ANISOU  758  CB  ASN A1099    17372  20559  20407  -1879    187     83       C  
ATOM    759  CG  ASN A1099      92.453  12.733  40.393  1.00182.18           C  
ANISOU  759  CG  ASN A1099    20711  24586  23924  -1864    -48     32       C  
ATOM    760  OD1 ASN A1099      92.291  13.920  40.713  1.00176.70           O  
ANISOU  760  OD1 ASN A1099    19892  24094  23152  -1591    -73    179       O  
ATOM    761  ND2 ASN A1099      92.079  12.279  39.211  1.00177.35           N  
ANISOU  761  ND2 ASN A1099    20005  24096  23285  -2157   -204   -169       N  
ATOM    762  N   ALA A1100      95.585  10.794  43.285  1.00148.99           N  
ANISOU  762  N   ALA A1100    17424  19367  19820  -1433    547    412       N  
ATOM    763  CA  ALA A1100      96.230   9.766  44.105  1.00175.09           C  
ANISOU  763  CA  ALA A1100    20942  22379  23205  -1361    783    596       C  
ATOM    764  C   ALA A1100      96.545  10.303  45.498  1.00207.86           C  
ANISOU  764  C   ALA A1100    25110  26661  27207  -1115    831    856       C  
ATOM    765  O   ALA A1100      96.842   9.531  46.406  1.00172.67           O  
ANISOU  765  O   ALA A1100    20783  22048  22775  -1024   1026   1082       O  
ATOM    766  CB  ALA A1100      97.504   9.280  43.429  1.00175.35           C  
ANISOU  766  CB  ALA A1100    21193  22191  23240  -1256    792    558       C  
ATOM    767  N   HIS A  43      86.160  -5.065  53.533  1.00183.15           N  
ANISOU  767  N   HIS A  43    20949  33045  15595   5542  -1199    815       N  
ATOM    768  CA  HIS A  43      85.490  -6.287  53.103  1.00181.34           C  
ANISOU  768  CA  HIS A  43    20886  32537  15479   5706   -901   1121       C  
ATOM    769  C   HIS A  43      84.359  -6.660  54.065  1.00184.79           C  
ANISOU  769  C   HIS A  43    21697  32720  15797   5962   -650   1306       C  
ATOM    770  O   HIS A  43      84.595  -6.827  55.266  1.00187.63           O  
ANISOU  770  O   HIS A  43    22219  33265  15806   6311   -703   1286       O  
ATOM    771  CB  HIS A  43      86.494  -7.453  52.993  1.00183.90           C  
ANISOU  771  CB  HIS A  43    21125  33125  15625   6034   -947   1218       C  
ATOM    772  CG  HIS A  43      85.864  -8.756  52.602  1.00186.29           C  
ANISOU  772  CG  HIS A  43    21632  33134  16017   6215   -648   1526       C  
ATOM    773  ND1 HIS A  43      85.379  -9.640  53.554  1.00188.50           N  
ANISOU  773  ND1 HIS A  43    22315  33080  16226   6436   -460   1698       N  
ATOM    774  CD2 HIS A  43      85.638  -9.272  51.372  1.00185.64           C  
ANISOU  774  CD2 HIS A  43    21484  32830  16221   6038   -521   1656       C  
ATOM    775  CE1 HIS A  43      84.877 -10.658  52.875  1.00187.62           C  
ANISOU  775  CE1 HIS A  43    22244  32914  16128   6646   -206   1968       C  
ATOM    776  NE2 HIS A  43      85.013 -10.485  51.560  1.00185.51           N  
ANISOU  776  NE2 HIS A  43    21753  32568  16164   6311   -252   1931       N  
ATOM    777  N   LEU A  44      83.142  -6.833  53.523  1.00178.53           N  
ANISOU  777  N   LEU A  44    21036  31506  15293   5802   -371   1496       N  
ATOM    778  CA  LEU A  44      81.973  -7.250  54.296  1.00178.23           C  
ANISOU  778  CA  LEU A  44    21326  31187  15205   6011    -84   1711       C  
ATOM    779  C   LEU A  44      81.500  -8.622  53.823  1.00179.15           C  
ANISOU  779  C   LEU A  44    21566  31057  15447   6147    186   2007       C  
ATOM    780  O   LEU A  44      81.366  -8.846  52.619  1.00176.41           O  
ANISOU  780  O   LEU A  44    21082  30544  15403   5886    225   2055       O  
ATOM    781  CB  LEU A  44      80.828  -6.219  54.205  1.00176.55           C  
ANISOU  781  CB  LEU A  44    21173  30685  15222   5702     23   1679       C  
ATOM    782  CG  LEU A  44      81.081  -4.842  54.840  1.00182.31           C  
ANISOU  782  CG  LEU A  44    21880  31586  15805   5592   -195   1409       C  
ATOM    783  CD1 LEU A  44      79.951  -3.893  54.538  1.00180.84           C  
ANISOU  783  CD1 LEU A  44    21748  31088  15874   5283    -64   1403       C  
ATOM    784  CD2 LEU A  44      81.287  -4.943  56.355  1.00188.06           C  
ANISOU  784  CD2 LEU A  44    22842  32505  16105   6019   -231   1396       C  
ATOM    785  N   ASP A  45      81.263  -9.544  54.775  1.00175.65           N  
ANISOU  785  N   ASP A  45    21402  30577  14760   6562    372   2202       N  
ATOM    786  CA  ASP A  45      80.801 -10.910  54.503  1.00174.30           C  
ANISOU  786  CA  ASP A  45    21403  30153  14669   6726    650   2493       C  
ATOM    787  C   ASP A  45      79.344 -10.925  54.017  1.00173.27           C  
ANISOU  787  C   ASP A  45    21362  29565  14908   6457    930   2666       C  
ATOM    788  O   ASP A  45      78.927 -11.898  53.387  1.00171.57           O  
ANISOU  788  O   ASP A  45    21215  29094  14880   6432   1121   2869       O  
ATOM    789  CB  ASP A  45      80.932 -11.783  55.765  1.00179.43           C  
ANISOU  789  CB  ASP A  45    22351  30895  14932   7258    782   2646       C  
ATOM    790  CG  ASP A  45      82.346 -11.939  56.303  1.00187.83           C  
ANISOU  790  CG  ASP A  45    23517  31679  16171   6842    420   2329       C  
ATOM    791  OD1 ASP A  45      83.305 -11.599  55.573  1.00188.14           O  
ANISOU  791  OD1 ASP A  45    23264  31998  16221   6732    168   2167       O  
ATOM    792  OD2 ASP A  45      82.495 -12.452  57.432  1.00191.94           O  
ANISOU  792  OD2 ASP A  45    24391  31699  16839   6608    402   2268       O  
ATOM    793  N   ALA A  46      78.578  -9.853  54.317  1.00167.31           N  
ANISOU  793  N   ALA A  46    20609  28710  14251   6262    948   2584       N  
ATOM    794  CA  ALA A  46      77.173  -9.697  53.939  1.00164.13           C  
ANISOU  794  CA  ALA A  46    20260  27914  14188   6011   1195   2728       C  
ATOM    795  C   ALA A  46      77.003  -9.566  52.421  1.00162.65           C  
ANISOU  795  C   ALA A  46    19845  27554  14399   5590   1144   2693       C  
ATOM    796  O   ALA A  46      76.061 -10.136  51.882  1.00160.97           O  
ANISOU  796  O   ALA A  46    19685  27009  14466   5458   1366   2884       O  
ATOM    797  CB  ALA A  46      76.584  -8.476  54.626  1.00165.01           C  
ANISOU  797  CB  ALA A  46    20413  28022  14259   5933   1184   2615       C  
ATOM    798  N   ILE A  47      77.911  -8.826  51.738  1.00156.42           N  
ANISOU  798  N   ILE A  47    18807  26990  13634   5383    856   2452       N  
ATOM    799  CA  ILE A  47      77.880  -8.572  50.288  1.00152.64           C  
ANISOU  799  CA  ILE A  47    18115  26380  13499   5001    783   2391       C  
ATOM    800  C   ILE A  47      77.795  -9.927  49.496  1.00154.82           C  
ANISOU  800  C   ILE A  47    18448  26460  13916   5055    924   2604       C  
ATOM    801  O   ILE A  47      76.809 -10.082  48.780  1.00152.61           O  
ANISOU  801  O   ILE A  47    18187  25847  13950   4836   1080   2724       O  
ATOM    802  CB  ILE A  47      79.104  -7.718  49.832  1.00155.18           C  
ANISOU  802  CB  ILE A  47    18178  27022  13762   4842    462   2110       C  
ATOM    803  CG1 ILE A  47      79.029  -6.267  50.391  1.00155.75           C  
ANISOU  803  CG1 ILE A  47    18205  27209  13765   4695    327   1888       C  
ATOM    804  CG2 ILE A  47      79.281  -7.711  48.303  1.00153.22           C  
ANISOU  804  CG2 ILE A  47    17733  26661  13823   4526    399   2075       C  
ATOM    805  CD1 ILE A  47      77.802  -5.410  49.929  1.00160.33           C  
ANISOU  805  CD1 ILE A  47    18793  27480  14646   4370    444   1886       C  
ATOM    806  N   PRO A  48      78.718 -10.926  49.611  1.00152.25           N  
ANISOU  806  N   PRO A  48    18169  26310  13368   5346    886   2664       N  
ATOM    807  CA  PRO A  48      78.541 -12.164  48.822  1.00151.22           C  
ANISOU  807  CA  PRO A  48    18130  25947  13378   5379   1031   2866       C  
ATOM    808  C   PRO A  48      77.239 -12.909  49.165  1.00154.31           C  
ANISOU  808  C   PRO A  48    18771  25964  13895   5435   1352   3127       C  
ATOM    809  O   PRO A  48      76.668 -13.542  48.278  1.00152.18           O  
ANISOU  809  O   PRO A  48    18547  25400  13877   5294   1472   3266       O  
ATOM    810  CB  PRO A  48      79.762 -13.006  49.204  1.00155.18           C  
ANISOU  810  CB  PRO A  48    18682  26746  13535   5761    947   2884       C  
ATOM    811  CG  PRO A  48      80.771 -12.023  49.667  1.00160.51           C  
ANISOU  811  CG  PRO A  48    19149  27836  14002   5777    667   2624       C  
ATOM    812  CD  PRO A  48      79.979 -10.973  50.381  1.00156.02           C  
ANISOU  812  CD  PRO A  48    18610  27207  13463   5649    693   2543       C  
ATOM    813  N   ILE A  49      76.751 -12.802  50.425  1.00152.52           N  
ANISOU  813  N   ILE A  49    18704  25740  13507   5624   1491   3192       N  
ATOM    814  CA  ILE A  49      75.504 -13.444  50.868  1.00153.03           C  
ANISOU  814  CA  ILE A  49    18988  25463  13694   5677   1818   3447       C  
ATOM    815  C   ILE A  49      74.302 -12.750  50.183  1.00155.01           C  
ANISOU  815  C   ILE A  49    19113  25430  14355   5263   1886   3446       C  
ATOM    816  O   ILE A  49      73.495 -13.436  49.555  1.00153.97           O  
ANISOU  816  O   ILE A  49    19017  24980  14506   5104   2043   3607       O  
ATOM    817  CB  ILE A  49      75.363 -13.439  52.421  1.00158.74           C  
ANISOU  817  CB  ILE A  49    19927  26288  14098   6037   1957   3521       C  
ATOM    818  CG1 ILE A  49      76.547 -14.177  53.118  1.00161.57           C  
ANISOU  818  CG1 ILE A  49    20418  26949  14024   6484   1877   3516       C  
ATOM    819  CG2 ILE A  49      74.008 -14.012  52.867  1.00160.39           C  
ANISOU  819  CG2 ILE A  49    20345  26133  14463   6070   2326   3799       C  
ATOM    820  CD1 ILE A  49      76.766 -15.711  52.780  1.00169.59           C  
ANISOU  820  CD1 ILE A  49    21608  27839  14989   6695   2019   3722       C  
ATOM    821  N   LEU A  50      74.212 -11.404  50.282  1.00150.59           N  
ANISOU  821  N   LEU A  50    18410  24989  13819   5092   1756   3258       N  
ATOM    822  CA  LEU A  50      73.155 -10.577  49.679  1.00148.14           C  
ANISOU  822  CA  LEU A  50    17974  24461  13851   4732   1797   3230       C  
ATOM    823  C   LEU A  50      73.074 -10.775  48.159  1.00148.81           C  
ANISOU  823  C   LEU A  50    17896  24377  14268   4405   1708   3198       C  
ATOM    824  O   LEU A  50      71.971 -10.847  47.623  1.00147.31           O  
ANISOU  824  O   LEU A  50    17674  23900  14398   4173   1835   3294       O  
ATOM    825  CB  LEU A  50      73.388  -9.085  49.989  1.00147.81           C  
ANISOU  825  CB  LEU A  50    17823  24628  13710   4636   1620   2992       C  
ATOM    826  CG  LEU A  50      72.683  -8.464  51.217  1.00154.10           C  
ANISOU  826  CG  LEU A  50    18767  25422  14363   4792   1770   3038       C  
ATOM    827  CD1 LEU A  50      72.978  -9.215  52.510  1.00157.30           C  
ANISOU  827  CD1 LEU A  50    19413  25935  14419   5232   1897   3172       C  
ATOM    828  CD2 LEU A  50      73.057  -6.996  51.370  1.00155.98           C  
ANISOU  828  CD2 LEU A  50    18909  25860  14496   4672   1556   2773       C  
ATOM    829  N   TYR A  51      74.232 -10.891  47.478  1.00144.18           N  
ANISOU  829  N   TYR A  51    17209  23973  13600   4402   1493   3070       N  
ATOM    830  CA  TYR A  51      74.324 -11.111  46.029  1.00141.61           C  
ANISOU  830  CA  TYR A  51    16756  23505  13543   4140   1399   3036       C  
ATOM    831  C   TYR A  51      73.715 -12.476  45.632  1.00146.06           C  
ANISOU  831  C   TYR A  51    17475  23750  14273   4165   1594   3278       C  
ATOM    832  O   TYR A  51      73.075 -12.552  44.584  1.00144.20           O  
ANISOU  832  O   TYR A  51    17174  23260  14354   3891   1602   3301       O  
ATOM    833  CB  TYR A  51      75.787 -11.017  45.561  1.00142.12           C  
ANISOU  833  CB  TYR A  51    16693  23866  13439   4189   1151   2865       C  
ATOM    834  CG  TYR A  51      76.260  -9.608  45.250  1.00141.92           C  
ANISOU  834  CG  TYR A  51    16449  24040  13434   3967    932   2603       C  
ATOM    835  CD1 TYR A  51      76.165  -8.593  46.201  1.00144.76           C  
ANISOU  835  CD1 TYR A  51    16798  24570  13636   3999    889   2482       C  
ATOM    836  CD2 TYR A  51      76.952  -9.329  44.076  1.00140.68           C  
ANISOU  836  CD2 TYR A  51    16116  23924  13411   3759    762   2472       C  
ATOM    837  CE1 TYR A  51      76.614  -7.302  45.929  1.00144.35           C  
ANISOU  837  CE1 TYR A  51    16568  24679  13598   3782    692   2237       C  
ATOM    838  CE2 TYR A  51      77.435  -8.050  43.806  1.00140.57           C  
ANISOU  838  CE2 TYR A  51    15913  24085  13412   3553    577   2235       C  
ATOM    839  CZ  TYR A  51      77.271  -7.041  44.741  1.00148.09           C  
ANISOU  839  CZ  TYR A  51    16860  25180  14226   3557    540   2115       C  
ATOM    840  OH  TYR A  51      77.741  -5.776  44.489  1.00147.56           O  
ANISOU  840  OH  TYR A  51    16630  25264  14172   3340    364   1878       O  
ATOM    841  N   TYR A  52      73.869 -13.528  46.469  1.00144.85           N  
ANISOU  841  N   TYR A  52    17538  23595  13904   4489   1752   3454       N  
ATOM    842  CA  TYR A  52      73.263 -14.833  46.178  1.00145.21           C  
ANISOU  842  CA  TYR A  52    17763  23315  14095   4513   1957   3689       C  
ATOM    843  C   TYR A  52      71.759 -14.830  46.512  1.00148.73           C  
ANISOU  843  C   TYR A  52    18261  23457  14794   4371   2204   3852       C  
ATOM    844  O   TYR A  52      71.009 -15.561  45.860  1.00147.94           O  
ANISOU  844  O   TYR A  52    18213  23034  14963   4210   2324   3994       O  
ATOM    845  CB  TYR A  52      73.961 -15.989  46.920  1.00148.93           C  
ANISOU  845  CB  TYR A  52    18473  23872  14242   4918   2060   3829       C  
ATOM    846  CG  TYR A  52      75.174 -16.534  46.195  1.00150.64           C  
ANISOU  846  CG  TYR A  52    18683  24229  14326   5024   1891   3769       C  
ATOM    847  CD1 TYR A  52      75.035 -17.453  45.157  1.00152.19           C  
ANISOU  847  CD1 TYR A  52    18976  24149  14702   4928   1938   3878       C  
ATOM    848  CD2 TYR A  52      76.462 -16.202  46.601  1.00152.15           C  
ANISOU  848  CD2 TYR A  52    18787  24828  14194   5247   1695   3615       C  
ATOM    849  CE1 TYR A  52      76.147 -17.966  44.490  1.00153.08           C  
ANISOU  849  CE1 TYR A  52    19102  24386  14676   5056   1799   3837       C  
ATOM    850  CE2 TYR A  52      77.584 -16.720  45.951  1.00153.19           C  
ANISOU  850  CE2 TYR A  52    18899  25107  14199   5369   1557   3578       C  
ATOM    851  CZ  TYR A  52      77.422 -17.602  44.894  1.00160.52           C  
ANISOU  851  CZ  TYR A  52    19935  25752  15303   5284   1618   3695       C  
ATOM    852  OH  TYR A  52      78.524 -18.111  44.248  1.00162.63           O  
ANISOU  852  OH  TYR A  52    20198  26162  15432   5429   1495   3669       O  
ATOM    853  N   ILE A  53      71.316 -14.009  47.501  1.00145.73           N  
ANISOU  853  N   ILE A  53    17863  23177  14330   4430   2278   3832       N  
ATOM    854  CA  ILE A  53      69.895 -13.902  47.886  1.00146.04           C  
ANISOU  854  CA  ILE A  53    17926  22966  14596   4317   2524   3991       C  
ATOM    855  C   ILE A  53      69.103 -13.292  46.702  1.00147.38           C  
ANISOU  855  C   ILE A  53    17881  22949  15168   3901   2442   3917       C  
ATOM    856  O   ILE A  53      68.086 -13.861  46.300  1.00147.23           O  
ANISOU  856  O   ILE A  53    17870  22625  15446   3734   2600   4078       O  
ATOM    857  CB  ILE A  53      69.701 -13.085  49.203  1.00150.44           C  
ANISOU  857  CB  ILE A  53    18529  23699  14931   4510   2607   3973       C  
ATOM    858  CG1 ILE A  53      70.363 -13.820  50.396  1.00153.62           C  
ANISOU  858  CG1 ILE A  53    19170  24275  14924   4952   2693   4056       C  
ATOM    859  CG2 ILE A  53      68.205 -12.838  49.489  1.00151.53           C  
ANISOU  859  CG2 ILE A  53    18663  23587  15324   4388   2871   4144       C  
ATOM    860  CD1 ILE A  53      70.363 -13.074  51.740  1.00164.30           C  
ANISOU  860  CD1 ILE A  53    20608  25829  15991   5197   2741   4017       C  
ATOM    861  N   ILE A  54      69.605 -12.179  46.117  1.00141.37           N  
ANISOU  861  N   ILE A  54    16933  22369  14412   3738   2191   3673       N  
ATOM    862  CA  ILE A  54      68.986 -11.491  44.975  1.00138.42           C  
ANISOU  862  CA  ILE A  54    16366  21854  14374   3377   2087   3575       C  
ATOM    863  C   ILE A  54      69.067 -12.403  43.728  1.00140.50           C  
ANISOU  863  C   ILE A  54    16628  21910  14844   3227   2022   3614       C  
ATOM    864  O   ILE A  54      68.140 -12.396  42.917  1.00138.95           O  
ANISOU  864  O   ILE A  54    16345  21471  14978   2963   2039   3648       O  
ATOM    865  CB  ILE A  54      69.664 -10.103  44.735  1.00139.89           C  
ANISOU  865  CB  ILE A  54    16395  22297  14461   3280   1844   3301       C  
ATOM    866  CG1 ILE A  54      69.545  -9.175  45.987  1.00141.44           C  
ANISOU  866  CG1 ILE A  54    16626  22674  14440   3428   1900   3254       C  
ATOM    867  CG2 ILE A  54      69.144  -9.396  43.472  1.00138.27           C  
ANISOU  867  CG2 ILE A  54    16013  21953  14572   2933   1727   3188       C  
ATOM    868  CD1 ILE A  54      68.078  -8.776  46.493  1.00148.53           C  
ANISOU  868  CD1 ILE A  54    17531  23388  15516   3365   2130   3391       C  
ATOM    869  N   PHE A  55      70.135 -13.219  43.615  1.00137.46           N  
ANISOU  869  N   PHE A  55    16356  21618  14255   3415   1955   3621       N  
ATOM    870  CA  PHE A  55      70.325 -14.153  42.505  1.00136.67           C  
ANISOU  870  CA  PHE A  55    16307  21327  14293   3328   1899   3665       C  
ATOM    871  C   PHE A  55      69.199 -15.197  42.432  1.00140.99           C  
ANISOU  871  C   PHE A  55    16983  21506  15082   3250   2120   3897       C  
ATOM    872  O   PHE A  55      68.603 -15.344  41.372  1.00139.06           O  
ANISOU  872  O   PHE A  55    16678  21020  15138   2987   2070   3897       O  
ATOM    873  CB  PHE A  55      71.685 -14.877  42.614  1.00139.45           C  
ANISOU  873  CB  PHE A  55    16782  21875  14330   3612   1821   3653       C  
ATOM    874  CG  PHE A  55      71.832 -16.063  41.686  1.00141.24           C  
ANISOU  874  CG  PHE A  55    17140  21877  14646   3597   1816   3747       C  
ATOM    875  CD1 PHE A  55      72.084 -15.880  40.333  1.00142.77           C  
ANISOU  875  CD1 PHE A  55    17234  22025  14988   3403   1622   3621       C  
ATOM    876  CD2 PHE A  55      71.748 -17.361  42.173  1.00145.48           C  
ANISOU  876  CD2 PHE A  55    17930  22241  15103   3792   2013   3961       C  
ATOM    877  CE1 PHE A  55      72.205 -16.973  39.473  1.00143.96           C  
ANISOU  877  CE1 PHE A  55    17538  21953  15208   3402   1616   3706       C  
ATOM    878  CE2 PHE A  55      71.878 -18.455  41.314  1.00148.65           C  
ANISOU  878  CE2 PHE A  55    18488  22414  15577   3778   2009   4043       C  
ATOM    879  CZ  PHE A  55      72.113 -18.254  39.971  1.00145.00           C  
ANISOU  879  CZ  PHE A  55    17927  21909  15257   3588   1803   3913       C  
ATOM    880  N   VAL A  56      68.942 -15.935  43.531  1.00139.84           N  
ANISOU  880  N   VAL A  56    17021  21314  14799   3480   2359   4091       N  
ATOM    881  CA  VAL A  56      67.960 -17.024  43.557  1.00141.04           C  
ANISOU  881  CA  VAL A  56    17315  21113  15159   3421   2595   4327       C  
ATOM    882  C   VAL A  56      66.513 -16.429  43.502  1.00143.82           C  
ANISOU  882  C   VAL A  56    17497  21282  15868   3135   2700   4377       C  
ATOM    883  O   VAL A  56      65.695 -16.951  42.743  1.00143.34           O  
ANISOU  883  O   VAL A  56    17411  20925  16127   2889   2730   4454       O  
ATOM    884  CB  VAL A  56      68.153 -17.973  44.786  1.00147.62           C  
ANISOU  884  CB  VAL A  56    18412  21951  15725   3771   2846   4527       C  
ATOM    885  CG1 VAL A  56      68.094 -17.230  46.122  1.00148.28           C  
ANISOU  885  CG1 VAL A  56    18482  22267  15591   3979   2951   4528       C  
ATOM    886  CG2 VAL A  56      67.171 -19.144  44.760  1.00149.31           C  
ANISOU  886  CG2 VAL A  56    18785  21774  16170   3684   3104   4775       C  
ATOM    887  N   ILE A  57      66.219 -15.338  44.250  1.00139.62           N  
ANISOU  887  N   ILE A  57    16846  20928  15276   3168   2740   4325       N  
ATOM    888  CA  ILE A  57      64.885 -14.710  44.251  1.00138.96           C  
ANISOU  888  CA  ILE A  57    16591  20708  15497   2939   2846   4376       C  
ATOM    889  C   ILE A  57      64.587 -14.170  42.836  1.00139.70           C  
ANISOU  889  C   ILE A  57    16483  20708  15887   2601   2620   4221       C  
ATOM    890  O   ILE A  57      63.551 -14.514  42.265  1.00139.66           O  
ANISOU  890  O   ILE A  57    16403  20441  16222   2365   2683   4316       O  
ATOM    891  CB  ILE A  57      64.762 -13.597  45.341  1.00142.22           C  
ANISOU  891  CB  ILE A  57    16950  21354  15733   3081   2912   4330       C  
ATOM    892  CG1 ILE A  57      64.804 -14.230  46.758  1.00145.37           C  
ANISOU  892  CG1 ILE A  57    17570  21799  15866   3424   3172   4516       C  
ATOM    893  CG2 ILE A  57      63.466 -12.774  45.160  1.00142.31           C  
ANISOU  893  CG2 ILE A  57    16761  21254  16057   2842   2988   4356       C  
ATOM    894  CD1 ILE A  57      64.775 -13.241  47.946  1.00153.66           C  
ANISOU  894  CD1 ILE A  57    18625  23076  16681   3621   3238   4475       C  
ATOM    895  N   GLY A  58      65.517 -13.393  42.283  1.00133.40           N  
ANISOU  895  N   GLY A  58    15609  20122  14955   2588   2363   3990       N  
ATOM    896  CA  GLY A  58      65.395 -12.805  40.954  1.00130.53           C  
ANISOU  896  CA  GLY A  58    15081  19699  14814   2313   2141   3825       C  
ATOM    897  C   GLY A  58      65.371 -13.800  39.813  1.00133.25           C  
ANISOU  897  C   GLY A  58    15484  19795  15350   2170   2059   3859       C  
ATOM    898  O   GLY A  58      64.715 -13.554  38.797  1.00131.47           O  
ANISOU  898  O   GLY A  58    15135  19408  15411   1911   1956   3803       O  
ATOM    899  N   PHE A  59      66.097 -14.925  39.958  1.00130.74           N  
ANISOU  899  N   PHE A  59    15371  19445  14858   2353   2095   3945       N  
ATOM    900  CA  PHE A  59      66.158 -15.943  38.913  1.00130.44           C  
ANISOU  900  CA  PHE A  59    15441  19159  14962   2248   2020   3981       C  
ATOM    901  C   PHE A  59      64.839 -16.705  38.853  1.00135.23           C  
ANISOU  901  C   PHE A  59    16070  19420  15890   2062   2190   4167       C  
ATOM    902  O   PHE A  59      64.332 -16.935  37.762  1.00133.72           O  
ANISOU  902  O   PHE A  59    15834  19004  15969   1820   2076   4136       O  
ATOM    903  CB  PHE A  59      67.336 -16.908  39.143  1.00133.31           C  
ANISOU  903  CB  PHE A  59    16038  19592  15020   2527   2026   4028       C  
ATOM    904  CG  PHE A  59      67.797 -17.629  37.898  1.00134.43           C  
ANISOU  904  CG  PHE A  59    16288  19566  15224   2458   1871   3990       C  
ATOM    905  CD1 PHE A  59      67.225 -18.838  37.521  1.00138.98           C  
ANISOU  905  CD1 PHE A  59    17034  19787  15984   2361   1960   4140       C  
ATOM    906  CD2 PHE A  59      68.812 -17.100  37.105  1.00134.91           C  
ANISOU  906  CD2 PHE A  59    16294  19817  15150   2495   1644   3807       C  
ATOM    907  CE1 PHE A  59      67.649 -19.498  36.361  1.00139.49           C  
ANISOU  907  CE1 PHE A  59    17230  19681  16088   2310   1810   4100       C  
ATOM    908  CE2 PHE A  59      69.232 -17.760  35.944  1.00137.22           C  
ANISOU  908  CE2 PHE A  59    16705  19949  15483   2458   1513   3781       C  
ATOM    909  CZ  PHE A  59      68.645 -18.952  35.579  1.00136.66           C  
ANISOU  909  CZ  PHE A  59    16824  19519  15583   2374   1591   3925       C  
ATOM    910  N   LEU A  60      64.263 -17.045  40.028  1.00134.12           N  
ANISOU  910  N   LEU A  60    15989  19244  15727   2172   2462   4357       N  
ATOM    911  CA  LEU A  60      63.006 -17.791  40.145  1.00136.02           C  
ANISOU  911  CA  LEU A  60    16240  19171  16270   2005   2668   4561       C  
ATOM    912  C   LEU A  60      61.775 -16.942  39.740  1.00139.55           C  
ANISOU  912  C   LEU A  60    16404  19549  17069   1712   2642   4527       C  
ATOM    913  O   LEU A  60      60.818 -17.519  39.216  1.00140.30           O  
ANISOU  913  O   LEU A  60    16451  19362  17493   1470   2677   4618       O  
ATOM    914  CB  LEU A  60      62.805 -18.318  41.578  1.00138.58           C  
ANISOU  914  CB  LEU A  60    16712  19501  16443   2239   2991   4779       C  
ATOM    915  CG  LEU A  60      63.347 -19.733  41.918  1.00145.35           C  
ANISOU  915  CG  LEU A  60    17893  20213  17121   2442   3133   4935       C  
ATOM    916  CD1 LEU A  60      64.846 -19.890  41.631  1.00144.25           C  
ANISOU  916  CD1 LEU A  60    17901  20270  16635   2675   2938   4798       C  
ATOM    917  CD2 LEU A  60      63.056 -20.089  43.358  1.00150.44           C  
ANISOU  917  CD2 LEU A  60    18672  20870  17619   2680   3466   5148       C  
ATOM    918  N   VAL A  61      61.791 -15.600  39.963  1.00134.32           N  
ANISOU  918  N   VAL A  61    15560  19137  16337   1732   2575   4395       N  
ATOM    919  CA  VAL A  61      60.651 -14.738  39.588  1.00133.20           C  
ANISOU  919  CA  VAL A  61    15158  18954  16499   1493   2555   4364       C  
ATOM    920  C   VAL A  61      60.643 -14.542  38.041  1.00134.57           C  
ANISOU  920  C   VAL A  61    15231  19020  16878   1244   2265   4189       C  
ATOM    921  O   VAL A  61      59.559 -14.419  37.464  1.00134.90           O  
ANISOU  921  O   VAL A  61    15107  18892  17255   1000   2246   4216       O  
ATOM    922  CB  VAL A  61      60.583 -13.365  40.327  1.00135.99           C  
ANISOU  922  CB  VAL A  61    15384  19581  16706   1602   2592   4287       C  
ATOM    923  CG1 VAL A  61      60.258 -13.545  41.806  1.00138.00           C  
ANISOU  923  CG1 VAL A  61    15726  19891  16819   1823   2900   4485       C  
ATOM    924  CG2 VAL A  61      61.850 -12.537  40.140  1.00133.49           C  
ANISOU  924  CG2 VAL A  61    15098  19529  16092   1723   2370   4053       C  
ATOM    925  N   ASN A  62      61.830 -14.549  37.379  1.00128.06           N  
ANISOU  925  N   ASN A  62    14509  18291  15855   1317   2047   4023       N  
ATOM    926  CA  ASN A  62      61.921 -14.427  35.919  1.00125.70           C  
ANISOU  926  CA  ASN A  62    14164  17884  15713   1126   1785   3866       C  
ATOM    927  C   ASN A  62      61.717 -15.807  35.246  1.00131.50           C  
ANISOU  927  C   ASN A  62    15054  18301  16607   1021   1767   3965       C  
ATOM    928  O   ASN A  62      61.402 -15.848  34.057  1.00130.04           O  
ANISOU  928  O   ASN A  62    14822  17944  16642    816   1585   3881       O  
ATOM    929  CB  ASN A  62      63.248 -13.803  35.483  1.00120.71           C  
ANISOU  929  CB  ASN A  62    13573  17478  14812   1248   1585   3663       C  
ATOM    930  CG  ASN A  62      63.328 -12.311  35.714  1.00125.97           C  
ANISOU  930  CG  ASN A  62    14074  18399  15388   1263   1539   3518       C  
ATOM    931  OD1 ASN A  62      62.576 -11.525  35.131  1.00114.94           O  
ANISOU  931  OD1 ASN A  62    12510  16965  14199   1087   1476   3446       O  
ATOM    932  ND2 ASN A  62      64.338 -11.874  36.437  1.00116.16           N  
ANISOU  932  ND2 ASN A  62    12886  17423  13827   1471   1540   3450       N  
ATOM    933  N   ILE A  63      61.852 -16.924  36.011  1.00131.10           N  
ANISOU  933  N   ILE A  63    15207  18161  16442   1167   1961   4144       N  
ATOM    934  CA  ILE A  63      61.602 -18.288  35.512  1.00133.11           C  
ANISOU  934  CA  ILE A  63    15652  18089  16834   1077   1987   4261       C  
ATOM    935  C   ILE A  63      60.092 -18.454  35.263  1.00139.61           C  
ANISOU  935  C   ILE A  63    16311  18656  18078    770   2046   4355       C  
ATOM    936  O   ILE A  63      59.703 -19.023  34.243  1.00139.54           O  
ANISOU  936  O   ILE A  63    16347  18386  18288    565   1907   4331       O  
ATOM    937  CB  ILE A  63      62.159 -19.392  36.481  1.00138.10           C  
ANISOU  937  CB  ILE A  63    16556  18699  17219   1334   2217   4442       C  
ATOM    938  CG1 ILE A  63      63.710 -19.494  36.403  1.00137.38           C  
ANISOU  938  CG1 ILE A  63    16670  18764  16763   1595   2089   4346       C  
ATOM    939  CG2 ILE A  63      61.532 -20.778  36.219  1.00141.54           C  
ANISOU  939  CG2 ILE A  63    17151  18754  17876   1194   2368   4635       C  
ATOM    940  CD1 ILE A  63      64.353 -19.881  34.977  1.00144.85           C  
ANISOU  940  CD1 ILE A  63    17764  19515  17757   1505   1852   4248       C  
ATOM    941  N   VAL A  64      59.256 -17.920  36.174  1.00137.96           N  
ANISOU  941  N   VAL A  64    15908  18534  17978    744   2240   4455       N  
ATOM    942  CA  VAL A  64      57.793 -17.994  36.089  1.00140.08           C  
ANISOU  942  CA  VAL A  64    15970  18607  18647    470   2326   4562       C  
ATOM    943  C   VAL A  64      57.298 -17.167  34.865  1.00142.78           C  
ANISOU  943  C   VAL A  64    16090  18934  19225    234   2041   4373       C  
ATOM    944  O   VAL A  64      56.316 -17.558  34.239  1.00143.56           O  
ANISOU  944  O   VAL A  64    16105  18789  19653    -28   1971   4401       O  
ATOM    945  CB  VAL A  64      57.127 -17.514  37.416  1.00145.53           C  
ANISOU  945  CB  VAL A  64    16507  19435  19353    554   2619   4719       C  
ATOM    946  CG1 VAL A  64      55.601 -17.578  37.340  1.00147.48           C  
ANISOU  946  CG1 VAL A  64    16502  19503  20029    272   2719   4842       C  
ATOM    947  CG2 VAL A  64      57.624 -18.332  38.608  1.00147.16           C  
ANISOU  947  CG2 VAL A  64    16957  19648  19311    812   2902   4906       C  
ATOM    948  N   VAL A  65      58.007 -16.078  34.502  1.00137.15           N  
ANISOU  948  N   VAL A  65    15303  18473  18336    329   1873   4178       N  
ATOM    949  CA  VAL A  65      57.633 -15.195  33.385  1.00135.54           C  
ANISOU  949  CA  VAL A  65    14912  18285  18300    158   1620   3993       C  
ATOM    950  C   VAL A  65      58.024 -15.846  32.020  1.00139.78           C  
ANISOU  950  C   VAL A  65    15599  18611  18900     45   1356   3876       C  
ATOM    951  O   VAL A  65      57.193 -15.861  31.108  1.00139.78           O  
ANISOU  951  O   VAL A  65    15479  18437  19193   -186   1206   3829       O  
ATOM    952  CB  VAL A  65      58.280 -13.787  33.540  1.00136.75           C  
ANISOU  952  CB  VAL A  65    14992  18756  18211    312   1549   3827       C  
ATOM    953  CG1 VAL A  65      57.959 -12.885  32.350  1.00134.86           C  
ANISOU  953  CG1 VAL A  65    14602  18522  18116    162   1298   3633       C  
ATOM    954  CG2 VAL A  65      57.830 -13.124  34.835  1.00137.22           C  
ANISOU  954  CG2 VAL A  65    14927  19002  18208    423   1793   3933       C  
ATOM    955  N   VAL A  66      59.274 -16.355  31.880  1.00136.25           N  
ANISOU  955  N   VAL A  66    15411  18188  18171    224   1296   3828       N  
ATOM    956  CA  VAL A  66      59.784 -16.964  30.636  1.00135.93           C  
ANISOU  956  CA  VAL A  66    15554  17958  18133    172   1063   3725       C  
ATOM    957  C   VAL A  66      58.939 -18.202  30.257  1.00143.56           C  
ANISOU  957  C   VAL A  66    16609  18560  19376    -35   1078   3848       C  
ATOM    958  O   VAL A  66      58.450 -18.278  29.127  1.00142.98           O  
ANISOU  958  O   VAL A  66    16513  18295  19516   -231    860   3753       O  
ATOM    959  CB  VAL A  66      61.291 -17.343  30.749  1.00138.90           C  
ANISOU  959  CB  VAL A  66    16188  18451  18136    440   1048   3691       C  
ATOM    960  CG1 VAL A  66      61.756 -18.184  29.560  1.00138.70           C  
ANISOU  960  CG1 VAL A  66    16394  18196  18108    411    850   3627       C  
ATOM    961  CG2 VAL A  66      62.164 -16.102  30.901  1.00136.29           C  
ANISOU  961  CG2 VAL A  66    15757  18465  17564    598    988   3540       C  
ATOM    962  N   THR A  67      58.769 -19.150  31.202  1.00143.71           N  
ANISOU  962  N   THR A  67    16736  18479  19387      7   1333   4055       N  
ATOM    963  CA  THR A  67      58.037 -20.408  30.994  1.00146.92           C  
ANISOU  963  CA  THR A  67    17255  18526  20042   -192   1388   4190       C  
ATOM    964  C   THR A  67      56.526 -20.167  30.739  1.00153.37           C  
ANISOU  964  C   THR A  67    17766  19221  21288   -512   1366   4216       C  
ATOM    965  O   THR A  67      55.882 -21.011  30.116  1.00154.96           O  
ANISOU  965  O   THR A  67    18016  19112  21750   -749   1289   4249       O  
ATOM    966  CB  THR A  67      58.210 -21.352  32.192  1.00156.55           C  
ANISOU  966  CB  THR A  67    18665  19685  21132    -47   1705   4414       C  
ATOM    967  OG1 THR A  67      57.765 -20.698  33.381  1.00155.64           O  
ANISOU  967  OG1 THR A  67    18341  19787  21006     30   1944   4519       O  
ATOM    968  CG2 THR A  67      59.654 -21.831  32.363  1.00153.83           C  
ANISOU  968  CG2 THR A  67    18649  19418  20382    265   1714   4403       C  
ATOM    969  N   LEU A  68      55.976 -19.029  31.218  1.00149.93           N  
ANISOU  969  N   LEU A  68    17021  19029  20918   -513   1431   4202       N  
ATOM    970  CA  LEU A  68      54.570 -18.642  31.045  1.00151.57           C  
ANISOU  970  CA  LEU A  68    16895  19189  21506   -773   1420   4228       C  
ATOM    971  C   LEU A  68      54.278 -18.355  29.566  1.00155.50           C  
ANISOU  971  C   LEU A  68    17318  19582  22181   -959   1064   4026       C  
ATOM    972  O   LEU A  68      53.317 -18.890  29.015  1.00156.85           O  
ANISOU  972  O   LEU A  68    17382  19526  22689  -1229    976   4050       O  
ATOM    973  CB  LEU A  68      54.273 -17.396  31.926  1.00150.69           C  
ANISOU  973  CB  LEU A  68    16522  19394  21338   -655   1578   4251       C  
ATOM    974  CG  LEU A  68      52.867 -16.760  31.931  1.00156.94           C  
ANISOU  974  CG  LEU A  68    16935  20214  22480   -858   1608   4295       C  
ATOM    975  CD1 LEU A  68      52.625 -15.998  33.218  1.00157.31           C  
ANISOU  975  CD1 LEU A  68    16829  20510  22431   -694   1892   4417       C  
ATOM    976  CD2 LEU A  68      52.633 -15.852  30.715  1.00157.71           C  
ANISOU  976  CD2 LEU A  68    16871  20360  22692   -970   1285   4073       C  
ATOM    977  N   PHE A  69      55.123 -17.514  28.941  1.00150.28           N  
ANISOU  977  N   PHE A  69    16719  19088  21292   -811    864   3828       N  
ATOM    978  CA  PHE A  69      55.023 -17.050  27.558  1.00149.38           C  
ANISOU  978  CA  PHE A  69    16563  18919  21275   -917    534   3620       C  
ATOM    979  C   PHE A  69      55.025 -18.208  26.535  1.00156.09           C  
ANISOU  979  C   PHE A  69    17640  19425  22243  -1066    332   3583       C  
ATOM    980  O   PHE A  69      54.361 -18.093  25.503  1.00156.33           O  
ANISOU  980  O   PHE A  69    17570  19328  22501  -1252     87   3468       O  
ATOM    981  CB  PHE A  69      56.211 -16.108  27.253  1.00147.72           C  
ANISOU  981  CB  PHE A  69    16450  18945  20733   -683    425   3448       C  
ATOM    982  CG  PHE A  69      56.253 -15.511  25.863  1.00147.60           C  
ANISOU  982  CG  PHE A  69    16416  18904  20762   -737    114   3231       C  
ATOM    983  CD1 PHE A  69      55.637 -14.295  25.591  1.00149.56           C  
ANISOU  983  CD1 PHE A  69    16406  19316  21106   -774     45   3132       C  
ATOM    984  CD2 PHE A  69      56.945 -16.144  24.836  1.00149.15           C  
ANISOU  984  CD2 PHE A  69    16879  18916  20876   -718    -98   3130       C  
ATOM    985  CE1 PHE A  69      55.682 -13.741  24.308  1.00149.05           C  
ANISOU  985  CE1 PHE A  69    16348  19221  21063   -799   -230   2935       C  
ATOM    986  CE2 PHE A  69      56.980 -15.595  23.551  1.00150.57           C  
ANISOU  986  CE2 PHE A  69    17063  19063  21082   -743   -373   2936       C  
ATOM    987  CZ  PHE A  69      56.358 -14.392  23.299  1.00147.67           C  
ANISOU  987  CZ  PHE A  69    16439  18857  20814   -782   -436   2838       C  
ATOM    988  N   CYS A  70      55.786 -19.289  26.798  1.00154.07           N  
ANISOU  988  N   CYS A  70    17704  19023  21812   -966    420   3669       N  
ATOM    989  CA  CYS A  70      55.970 -20.375  25.838  1.00155.30           C  
ANISOU  989  CA  CYS A  70    18142  18856  22009  -1058    224   3619       C  
ATOM    990  C   CYS A  70      54.842 -21.442  25.942  1.00164.12           C  
ANISOU  990  C   CYS A  70    19255  19645  23457  -1342    290   3762       C  
ATOM    991  O   CYS A  70      53.996 -21.509  25.049  1.00164.96           O  
ANISOU  991  O   CYS A  70    19319  19535  23823  -1580     50   3671       O  
ATOM    992  CB  CYS A  70      57.339 -21.025  26.027  1.00154.42           C  
ANISOU  992  CB  CYS A  70    18401  18747  21523   -787    275   3634       C  
ATOM    993  SG  CYS A  70      58.743 -19.906  25.765  1.00154.13           S  
ANISOU  993  SG  CYS A  70    18385  19057  21120   -489    166   3455       S  
ATOM    994  N   CYS A  71      54.876 -22.302  26.982  1.00163.56           N  
ANISOU  994  N   CYS A  71    19257  19522  23366  -1313    602   3976       N  
ATOM    995  CA  CYS A  71      54.005 -23.474  27.121  1.00167.58           C  
ANISOU  995  CA  CYS A  71    19827  19688  24156  -1571    695   4124       C  
ATOM    996  C   CYS A  71      52.629 -23.119  27.742  1.00174.07           C  
ANISOU  996  C   CYS A  71    20237  20553  25349  -1812    847   4243       C  
ATOM    997  O   CYS A  71      51.728 -23.959  27.666  1.00177.02           O  
ANISOU  997  O   CYS A  71    20573  20641  26045  -2104    861   4330       O  
ATOM    998  CB  CYS A  71      54.705 -24.535  27.968  1.00169.14           C  
ANISOU  998  CB  CYS A  71    20368  19775  24120  -1395    967   4302       C  
ATOM    999  SG  CYS A  71      56.254 -25.155  27.258  1.00171.30           S  
ANISOU  999  SG  CYS A  71    21139  19971  23976  -1111    812   4197       S  
ATOM   1000  N   GLN A  72      52.452 -21.926  28.357  1.00169.20           N  
ANISOU 1000  N   GLN A  72    19318  20276  24694  -1697    961   4250       N  
ATOM   1001  CA  GLN A  72      51.159 -21.632  28.995  1.00171.13           C  
ANISOU 1001  CA  GLN A  72    19175  20577  25270  -1888   1135   4385       C  
ATOM   1002  C   GLN A  72      50.489 -20.328  28.452  1.00173.69           C  
ANISOU 1002  C   GLN A  72    19122  21128  25744  -1951    937   4235       C  
ATOM   1003  O   GLN A  72      49.519 -19.858  29.060  1.00174.51           O  
ANISOU 1003  O   GLN A  72    18887  21365  26055  -2029   1104   4345       O  
ATOM   1004  CB  GLN A  72      51.313 -21.512  30.523  1.00172.55           C  
ANISOU 1004  CB  GLN A  72    19332  20936  25293  -1684   1541   4596       C  
ATOM   1005  CG  GLN A  72      51.772 -22.805  31.212  1.00182.27           C  
ANISOU 1005  CG  GLN A  72    20897  21939  26417  -1627   1793   4784       C  
ATOM   1006  CD  GLN A  72      51.730 -22.729  32.722  1.00195.67           C  
ANISOU 1006  CD  GLN A  72    22538  23775  28032  -1465   2207   5016       C  
ATOM   1007  OE1 GLN A  72      52.524 -23.365  33.418  1.00190.11           O  
ANISOU 1007  OE1 GLN A  72    22136  23049  27047  -1237   2414   5127       O  
ATOM   1008  NE2 GLN A  72      50.814 -21.940  33.266  1.00186.38           N  
ANISOU 1008  NE2 GLN A  72    20984  22747  27085  -1558   2340   5098       N  
ATOM   1009  N   LYS A  73      50.946 -19.789  27.299  1.00167.88           N  
ANISOU 1009  N   LYS A  73    18452  20422  24913  -1915    596   3997       N  
ATOM   1010  CA  LYS A  73      50.313 -18.596  26.725  1.00166.54           C  
ANISOU 1010  CA  LYS A  73    17962  20439  24875  -1965    404   3852       C  
ATOM   1011  C   LYS A  73      50.412 -18.646  25.184  1.00170.00           C  
ANISOU 1011  C   LYS A  73    18518  20717  25355  -2057     -5   3623       C  
ATOM   1012  O   LYS A  73      49.479 -19.118  24.532  1.00171.86           O  
ANISOU 1012  O   LYS A  73    18641  20744  25915  -2331   -181   3598       O  
ATOM   1013  CB  LYS A  73      50.939 -17.298  27.290  1.00165.71           C  
ANISOU 1013  CB  LYS A  73    17790  20698  24475  -1677    510   3805       C  
ATOM   1014  CG  LYS A  73      50.181 -16.017  26.909  1.00176.21           C  
ANISOU 1014  CG  LYS A  73    18779  22229  25944  -1712    384   3696       C  
ATOM   1015  CD  LYS A  73      50.818 -14.727  27.470  1.00180.71           C  
ANISOU 1015  CD  LYS A  73    19320  23131  26211  -1438    487   3639       C  
ATOM   1016  CE  LYS A  73      52.159 -14.349  26.870  1.00184.01           C  
ANISOU 1016  CE  LYS A  73    20017  23610  26288  -1243    315   3449       C  
ATOM   1017  NZ  LYS A  73      52.059 -14.039  25.417  1.00189.69           N  
ANISOU 1017  NZ  LYS A  73    20744  24236  27093  -1327    -34   3241       N  
ATOM   1018  N   GLY A  74      51.535 -18.170  24.636  1.00163.91           N  
ANISOU 1018  N   GLY A  74    17973  20047  24260  -1828   -148   3461       N  
ATOM   1019  CA  GLY A  74      51.789 -18.117  23.198  1.00162.90           C  
ANISOU 1019  CA  GLY A  74    17997  19789  24107  -1848   -512   3244       C  
ATOM   1020  C   GLY A  74      52.621 -16.918  22.759  1.00162.95           C  
ANISOU 1020  C   GLY A  74    18041  20040  23832  -1604   -620   3072       C  
ATOM   1021  O   GLY A  74      52.922 -16.039  23.577  1.00160.83           O  
ANISOU 1021  O   GLY A  74    17657  20051  23400  -1438   -425   3109       O  
ATOM   1022  N   PRO A  75      52.994 -16.829  21.452  1.00157.90           N  
ANISOU 1022  N   PRO A  75    17571  19292  23132  -1578   -931   2877       N  
ATOM   1023  CA  PRO A  75      53.821 -15.693  20.999  1.00153.93           C  
ANISOU 1023  CA  PRO A  75    17121  19004  22362  -1349  -1014   2718       C  
ATOM   1024  C   PRO A  75      52.975 -14.528  20.428  1.00155.07           C  
ANISOU 1024  C   PRO A  75    16981  19281  22658  -1398  -1169   2591       C  
ATOM   1025  O   PRO A  75      53.488 -13.716  19.648  1.00152.65           O  
ANISOU 1025  O   PRO A  75    16761  19048  22191  -1260  -1327   2423       O  
ATOM   1026  CB  PRO A  75      54.704 -16.323  19.909  1.00155.24           C  
ANISOU 1026  CB  PRO A  75    17663  18959  22364  -1269  -1236   2600       C  
ATOM   1027  CG  PRO A  75      53.981 -17.610  19.486  1.00163.13           C  
ANISOU 1027  CG  PRO A  75    18751  19609  23621  -1512  -1369   2642       C  
ATOM   1028  CD  PRO A  75      52.755 -17.779  20.347  1.00161.27           C  
ANISOU 1028  CD  PRO A  75    18188  19385  23703  -1740  -1208   2795       C  
ATOM   1029  N   LYS A  76      51.692 -14.426  20.846  1.00151.37           N  
ANISOU 1029  N   LYS A  76    16174  18852  22488  -1578  -1102   2680       N  
ATOM   1030  CA  LYS A  76      50.769 -13.370  20.410  1.00149.91           C  
ANISOU 1030  CA  LYS A  76    15693  18807  22460  -1615  -1228   2584       C  
ATOM   1031  C   LYS A  76      50.993 -12.078  21.229  1.00149.33           C  
ANISOU 1031  C   LYS A  76    15467  19062  22211  -1429  -1002   2610       C  
ATOM   1032  O   LYS A  76      51.706 -12.103  22.238  1.00148.16           O  
ANISOU 1032  O   LYS A  76    15398  19025  21870  -1311   -745   2720       O  
ATOM   1033  CB  LYS A  76      49.308 -13.843  20.527  1.00155.38           C  
ANISOU 1033  CB  LYS A  76    16072  19403  23563  -1891  -1265   2673       C  
ATOM   1034  CG  LYS A  76      48.951 -14.954  19.533  1.00165.53           C  
ANISOU 1034  CG  LYS A  76    17485  20363  25044  -2098  -1565   2593       C  
ATOM   1035  CD  LYS A  76      47.521 -15.492  19.694  1.00175.93           C  
ANISOU 1035  CD  LYS A  76    18474  21578  26792  -2408  -1603   2684       C  
ATOM   1036  CE  LYS A  76      47.281 -16.272  20.973  1.00185.76           C  
ANISOU 1036  CE  LYS A  76    19648  22759  28171  -2544  -1282   2931       C  
ATOM   1037  NZ  LYS A  76      48.125 -17.497  21.051  1.00193.41           N  
ANISOU 1037  NZ  LYS A  76    21018  23454  29014  -2563  -1258   2973       N  
ATOM   1038  N   LYS A  77      50.402 -10.946  20.755  1.00143.00           N  
ANISOU 1038  N   LYS A  77    14473  18405  21456  -1388  -1115   2495       N  
ATOM   1039  CA  LYS A  77      50.485  -9.573  21.302  1.00139.84           C  
ANISOU 1039  CA  LYS A  77    13944  18291  20897  -1214   -959   2478       C  
ATOM   1040  C   LYS A  77      51.884  -8.978  21.066  1.00137.37           C  
ANISOU 1040  C   LYS A  77    13920  18059  20216   -996   -962   2351       C  
ATOM   1041  O   LYS A  77      52.845  -9.724  20.889  1.00136.05           O  
ANISOU 1041  O   LYS A  77    14022  17765  19906   -963  -1001   2335       O  
ATOM   1042  CB  LYS A  77      50.125  -9.480  22.798  1.00143.33           C  
ANISOU 1042  CB  LYS A  77    14190  18898  21371  -1208   -619   2684       C  
ATOM   1043  CG  LYS A  77      48.664  -9.800  23.117  1.00161.23           C  
ANISOU 1043  CG  LYS A  77    16112  21138  24010  -1407   -572   2823       C  
ATOM   1044  CD  LYS A  77      48.293  -9.449  24.563  1.00172.08           C  
ANISOU 1044  CD  LYS A  77    17285  22713  25383  -1343   -223   3016       C  
ATOM   1045  CE  LYS A  77      48.348  -7.957  24.835  1.00181.90           C  
ANISOU 1045  CE  LYS A  77    18446  24216  26452  -1146   -160   2943       C  
ATOM   1046  NZ  LYS A  77      48.025  -7.634  26.246  1.00192.66           N  
ANISOU 1046  NZ  LYS A  77    19667  25764  27772  -1053    180   3127       N  
ATOM   1047  N   VAL A  78      51.990  -7.629  21.048  1.00130.04           N  
ANISOU 1047  N   VAL A  78    12936  17336  19137   -849   -920   2262       N  
ATOM   1048  CA  VAL A  78      53.267  -6.958  20.779  1.00125.89           C  
ANISOU 1048  CA  VAL A  78    12656  16891  18287   -666   -922   2134       C  
ATOM   1049  C   VAL A  78      53.984  -6.675  22.118  1.00125.92           C  
ANISOU 1049  C   VAL A  78    12685  17083  18075   -560   -635   2236       C  
ATOM   1050  O   VAL A  78      55.186  -6.922  22.221  1.00123.97           O  
ANISOU 1050  O   VAL A  78    12658  16842  17604   -470   -603   2212       O  
ATOM   1051  CB  VAL A  78      53.078  -5.659  19.939  1.00128.50           C  
ANISOU 1051  CB  VAL A  78    12963  17306  18554   -566  -1045   1964       C  
ATOM   1052  CG1 VAL A  78      54.416  -4.974  19.667  1.00125.44           C  
ANISOU 1052  CG1 VAL A  78    12826  16989  17848   -400  -1027   1839       C  
ATOM   1053  CG2 VAL A  78      52.353  -5.951  18.624  1.00129.62           C  
ANISOU 1053  CG2 VAL A  78    13087  17269  18894   -647  -1345   1858       C  
ATOM   1054  N   SER A  79      53.240  -6.184  23.135  1.00121.45           N  
ANISOU 1054  N   SER A  79    11897  16674  17575   -560   -431   2351       N  
ATOM   1055  CA  SER A  79      53.749  -5.859  24.474  1.00119.55           C  
ANISOU 1055  CA  SER A  79    11671  16617  17137   -450   -162   2449       C  
ATOM   1056  C   SER A  79      54.344  -7.091  25.168  1.00120.80           C  
ANISOU 1056  C   SER A  79    11948  16697  17254   -469    -50   2586       C  
ATOM   1057  O   SER A  79      55.342  -6.957  25.873  1.00118.84           O  
ANISOU 1057  O   SER A  79    11830  16572  16752   -341     85   2601       O  
ATOM   1058  CB  SER A  79      52.636  -5.273  25.338  1.00124.93           C  
ANISOU 1058  CB  SER A  79    12094  17440  17933   -449     23   2565       C  
ATOM   1059  OG  SER A  79      51.541  -6.168  25.456  1.00137.98           O  
ANISOU 1059  OG  SER A  79    13545  18982  19901   -608     44   2714       O  
ATOM   1060  N   SER A  80      53.747  -8.285  24.940  1.00117.36           N  
ANISOU 1060  N   SER A  80    11478  16053  17061   -627   -112   2679       N  
ATOM   1061  CA  SER A  80      54.188  -9.566  25.505  1.00117.26           C  
ANISOU 1061  CA  SER A  80    11601  15921  17032   -654     -8   2818       C  
ATOM   1062  C   SER A  80      55.579  -9.971  24.992  1.00117.40           C  
ANISOU 1062  C   SER A  80    11924  15881  16801   -548   -114   2721       C  
ATOM   1063  O   SER A  80      56.307 -10.667  25.706  1.00116.98           O  
ANISOU 1063  O   SER A  80    12017  15829  16601   -473     22   2821       O  
ATOM   1064  CB  SER A  80      53.187 -10.669  25.174  1.00123.45           C  
ANISOU 1064  CB  SER A  80    12289  16466  18151   -874    -80   2913       C  
ATOM   1065  OG  SER A  80      51.908 -10.399  25.723  1.00133.20           O  
ANISOU 1065  OG  SER A  80    13214  17764  19631   -973     44   3029       O  
ATOM   1066  N   ILE A  81      55.946  -9.539  23.763  1.00111.13           N  
ANISOU 1066  N   ILE A  81    11229  15043  15952   -525   -346   2536       N  
ATOM   1067  CA  ILE A  81      57.245  -9.846  23.155  1.00108.63           C  
ANISOU 1067  CA  ILE A  81    11189  14680  15406   -412   -448   2444       C  
ATOM   1068  C   ILE A  81      58.333  -9.081  23.913  1.00109.88           C  
ANISOU 1068  C   ILE A  81    11396  15094  15258   -233   -294   2419       C  
ATOM   1069  O   ILE A  81      59.373  -9.665  24.219  1.00109.47           O  
ANISOU 1069  O   ILE A  81    11519  15065  15009   -127   -241   2451       O  
ATOM   1070  CB  ILE A  81      57.281  -9.538  21.627  1.00110.65           C  
ANISOU 1070  CB  ILE A  81    11539  14811  15694   -424   -723   2261       C  
ATOM   1071  CG1 ILE A  81      56.034 -10.090  20.873  1.00112.98           C  
ANISOU 1071  CG1 ILE A  81    11740  14877  16308   -613   -908   2261       C  
ATOM   1072  CG2 ILE A  81      58.593  -9.995  20.973  1.00110.06           C  
ANISOU 1072  CG2 ILE A  81    11758  14670  15392   -298   -813   2189       C  
ATOM   1073  CD1 ILE A  81      55.728 -11.615  20.992  1.00121.88           C  
ANISOU 1073  CD1 ILE A  81    12953  15762  17592   -749   -918   2390       C  
ATOM   1074  N   TYR A  82      58.073  -7.800  24.268  1.00104.59           N  
ANISOU 1074  N   TYR A  82    10574  14619  14547   -197   -219   2366       N  
ATOM   1075  CA  TYR A  82      59.026  -6.990  25.032  1.00102.55           C  
ANISOU 1075  CA  TYR A  82    10350  14602  14011    -52    -83   2329       C  
ATOM   1076  C   TYR A  82      59.198  -7.570  26.446  1.00107.14           C  
ANISOU 1076  C   TYR A  82    10923  15277  14509      7    139   2498       C  
ATOM   1077  O   TYR A  82      60.315  -7.555  26.956  1.00106.49           O  
ANISOU 1077  O   TYR A  82    10949  15338  14173    137    207   2484       O  
ATOM   1078  CB  TYR A  82      58.604  -5.509  25.103  1.00102.66           C  
ANISOU 1078  CB  TYR A  82    10231  14769  14006    -35    -52   2236       C  
ATOM   1079  CG  TYR A  82      58.359  -4.862  23.755  1.00103.28           C  
ANISOU 1079  CG  TYR A  82    10330  14763  14150    -65   -252   2072       C  
ATOM   1080  CD1 TYR A  82      59.417  -4.553  22.904  1.00103.58           C  
ANISOU 1080  CD1 TYR A  82    10543  14800  14013      7   -360   1928       C  
ATOM   1081  CD2 TYR A  82      57.083  -4.446  23.382  1.00104.77           C  
ANISOU 1081  CD2 TYR A  82    10356  14896  14558   -144   -314   2062       C  
ATOM   1082  CE1 TYR A  82      59.197  -3.942  21.668  1.00103.32           C  
ANISOU 1082  CE1 TYR A  82    10556  14679  14024      3   -527   1783       C  
ATOM   1083  CE2 TYR A  82      56.855  -3.811  22.161  1.00104.81           C  
ANISOU 1083  CE2 TYR A  82    10395  14829  14599   -142   -497   1908       C  
ATOM   1084  CZ  TYR A  82      57.913  -3.565  21.304  1.00109.51           C  
ANISOU 1084  CZ  TYR A  82    11196  15399  15014    -65   -599   1769       C  
ATOM   1085  OH  TYR A  82      57.678  -2.958  20.090  1.00108.55           O  
ANISOU 1085  OH  TYR A  82    11134  15194  14917    -42   -766   1625       O  
ATOM   1086  N   ILE A  83      58.107  -8.127  27.050  1.00104.76           N  
ANISOU 1086  N   ILE A  83    10492  14892  14421    -85    251   2661       N  
ATOM   1087  CA  ILE A  83      58.117  -8.779  28.377  1.00105.38           C  
ANISOU 1087  CA  ILE A  83    10575  15021  14444    -26    483   2846       C  
ATOM   1088  C   ILE A  83      59.119  -9.946  28.372  1.00107.34           C  
ANISOU 1088  C   ILE A  83    11051  15183  14549     46    470   2890       C  
ATOM   1089  O   ILE A  83      59.957 -10.035  29.274  1.00106.45           O  
ANISOU 1089  O   ILE A  83    11028  15220  14197    202    604   2939       O  
ATOM   1090  CB  ILE A  83      56.692  -9.281  28.809  1.00111.09           C  
ANISOU 1090  CB  ILE A  83    11115  15625  15471   -165    600   3020       C  
ATOM   1091  CG1 ILE A  83      55.610  -8.169  28.778  1.00111.92           C  
ANISOU 1091  CG1 ILE A  83    10976  15823  15726   -219    617   2993       C  
ATOM   1092  CG2 ILE A  83      56.717  -9.987  30.179  1.00113.58           C  
ANISOU 1092  CG2 ILE A  83    11465  15969  15722    -88    864   3225       C  
ATOM   1093  CD1 ILE A  83      55.780  -7.020  29.731  1.00121.44           C  
ANISOU 1093  CD1 ILE A  83    12137  17278  16726    -68    782   2984       C  
ATOM   1094  N   PHE A  84      59.019 -10.834  27.355  1.00102.89           N  
ANISOU 1094  N   PHE A  84    10590  14380  14122    -53    304   2871       N  
ATOM   1095  CA  PHE A  84      59.881 -12.007  27.215  1.00102.47           C  
ANISOU 1095  CA  PHE A  84    10779  14209  13947     18    282   2917       C  
ATOM   1096  C   PHE A  84      61.357 -11.578  27.057  1.00104.01           C  
ANISOU 1096  C   PHE A  84    11113  14590  13817    208    236   2801       C  
ATOM   1097  O   PHE A  84      62.220 -12.098  27.771  1.00104.34           O  
ANISOU 1097  O   PHE A  84    11278  14719  13646    360    347   2876       O  
ATOM   1098  CB  PHE A  84      59.433 -12.872  26.025  1.00104.86           C  
ANISOU 1098  CB  PHE A  84    11177  14209  14455   -129     83   2889       C  
ATOM   1099  CG  PHE A  84      60.257 -14.125  25.840  1.00107.08           C  
ANISOU 1099  CG  PHE A  84    11739  14335  14613    -51     67   2947       C  
ATOM   1100  CD1 PHE A  84      59.988 -15.270  26.579  1.00112.62           C  
ANISOU 1100  CD1 PHE A  84    12521  14892  15377    -81    222   3131       C  
ATOM   1101  CD2 PHE A  84      61.292 -14.167  24.912  1.00107.83           C  
ANISOU 1101  CD2 PHE A  84    12030  14416  14524     63    -91   2827       C  
ATOM   1102  CE1 PHE A  84      60.757 -16.427  26.412  1.00114.36           C  
ANISOU 1102  CE1 PHE A  84    13031  14959  15462     12    217   3188       C  
ATOM   1103  CE2 PHE A  84      62.057 -15.326  24.743  1.00111.41           C  
ANISOU 1103  CE2 PHE A  84    12756  14730  14844    164    -97   2890       C  
ATOM   1104  CZ  PHE A  84      61.786 -16.447  25.495  1.00111.76           C  
ANISOU 1104  CZ  PHE A  84    12894  14631  14938    141     53   3067       C  
ATOM   1105  N   ASN A  85      61.633 -10.613  26.155  1.00 97.41           N  
ANISOU 1105  N   ASN A  85    10247  13821  12944    205     82   2622       N  
ATOM   1106  CA  ASN A  85      62.980 -10.100  25.920  1.00 94.78           C  
ANISOU 1106  CA  ASN A  85    10010  13663  12339    354     35   2503       C  
ATOM   1107  C   ASN A  85      63.529  -9.418  27.169  1.00 97.82           C  
ANISOU 1107  C   ASN A  85    10319  14338  12512    472    200   2516       C  
ATOM   1108  O   ASN A  85      64.729  -9.514  27.424  1.00 96.96           O  
ANISOU 1108  O   ASN A  85    10301  14381  12159    617    215   2490       O  
ATOM   1109  CB  ASN A  85      62.991  -9.143  24.750  1.00 92.58           C  
ANISOU 1109  CB  ASN A  85     9707  13371  12098    306   -135   2323       C  
ATOM   1110  CG  ASN A  85      62.872  -9.831  23.416  1.00107.04           C  
ANISOU 1110  CG  ASN A  85    11676  14939  14054    249   -328   2280       C  
ATOM   1111  OD1 ASN A  85      63.824 -10.429  22.911  1.00 97.84           O  
ANISOU 1111  OD1 ASN A  85    10704  13709  12759    345   -389   2275       O  
ATOM   1112  ND2 ASN A  85      61.734  -9.693  22.773  1.00 98.65           N  
ANISOU 1112  ND2 ASN A  85    10523  13733  13225    110   -440   2233       N  
ATOM   1113  N   LEU A  86      62.651  -8.767  27.964  1.00 94.77           N  
ANISOU 1113  N   LEU A  86     9767  14031  12211    419    320   2559       N  
ATOM   1114  CA  LEU A  86      63.037  -8.133  29.228  1.00 94.62           C  
ANISOU 1114  CA  LEU A  86     9693  14266  11991    534    477   2576       C  
ATOM   1115  C   LEU A  86      63.403  -9.219  30.248  1.00100.42           C  
ANISOU 1115  C   LEU A  86    10523  15023  12607    659    625   2741       C  
ATOM   1116  O   LEU A  86      64.431  -9.102  30.915  1.00 99.89           O  
ANISOU 1116  O   LEU A  86    10513  15162  12277    816    674   2721       O  
ATOM   1117  CB  LEU A  86      61.908  -7.213  29.764  1.00 94.90           C  
ANISOU 1117  CB  LEU A  86     9555  14353  12152    464    575   2592       C  
ATOM   1118  CG  LEU A  86      62.160  -6.470  31.090  1.00 99.84           C  
ANISOU 1118  CG  LEU A  86    10143  15217  12575    585    741   2613       C  
ATOM   1119  CD1 LEU A  86      63.376  -5.571  31.005  1.00 98.79           C  
ANISOU 1119  CD1 LEU A  86    10064  15292  12181    667    668   2442       C  
ATOM   1120  CD2 LEU A  86      60.958  -5.655  31.496  1.00102.36           C  
ANISOU 1120  CD2 LEU A  86    10309  15552  13031    527    837   2644       C  
ATOM   1121  N   ALA A  87      62.580 -10.297  30.323  1.00 98.66           N  
ANISOU 1121  N   ALA A  87    10326  14582  12576    588    690   2900       N  
ATOM   1122  CA  ALA A  87      62.783 -11.433  31.229  1.00 99.71           C  
ANISOU 1122  CA  ALA A  87    10579  14685  12619    701    851   3076       C  
ATOM   1123  C   ALA A  87      64.083 -12.171  30.895  1.00102.21           C  
ANISOU 1123  C   ALA A  87    11100  15018  12718    847    775   3052       C  
ATOM   1124  O   ALA A  87      64.812 -12.528  31.814  1.00102.00           O  
ANISOU 1124  O   ALA A  87    11162  15135  12459   1035    890   3123       O  
ATOM   1125  CB  ALA A  87      61.601 -12.386  31.154  1.00102.32           C  
ANISOU 1125  CB  ALA A  87    10896  14741  13239    551    922   3235       C  
ATOM   1126  N   VAL A  88      64.394 -12.351  29.587  1.00 97.84           N  
ANISOU 1126  N   VAL A  88    10622  14331  12221    783    581   2950       N  
ATOM   1127  CA  VAL A  88      65.635 -12.988  29.111  1.00 97.49           C  
ANISOU 1127  CA  VAL A  88    10769  14300  11972    932    501   2923       C  
ATOM   1128  C   VAL A  88      66.848 -12.111  29.526  1.00101.12           C  
ANISOU 1128  C   VAL A  88    11178  15095  12147   1090    492   2809       C  
ATOM   1129  O   VAL A  88      67.778 -12.625  30.154  1.00101.78           O  
ANISOU 1129  O   VAL A  88    11359  15321  11991   1286    552   2861       O  
ATOM   1130  CB  VAL A  88      65.604 -13.246  27.576  1.00100.39           C  
ANISOU 1130  CB  VAL A  88    11235  14437  12473    832    299   2837       C  
ATOM   1131  CG1 VAL A  88      66.994 -13.564  27.025  1.00 99.35           C  
ANISOU 1131  CG1 VAL A  88    11275  14371  12102   1012    217   2788       C  
ATOM   1132  CG2 VAL A  88      64.608 -14.349  27.222  1.00101.95           C  
ANISOU 1132  CG2 VAL A  88    11519  14299  12919    689    294   2953       C  
ATOM   1133  N   ALA A  89      66.804 -10.794  29.219  1.00 96.46           N  
ANISOU 1133  N   ALA A  89    10434  14633  11585   1005    423   2657       N  
ATOM   1134  CA  ALA A  89      67.857  -9.836  29.575  1.00 95.49           C  
ANISOU 1134  CA  ALA A  89    10243  14811  11226   1105    407   2532       C  
ATOM   1135  C   ALA A  89      68.084  -9.791  31.098  1.00101.21           C  
ANISOU 1135  C   ALA A  89    10937  15754  11763   1242    562   2607       C  
ATOM   1136  O   ALA A  89      69.237  -9.759  31.532  1.00100.64           O  
ANISOU 1136  O   ALA A  89    10884  15915  11441   1398    555   2565       O  
ATOM   1137  CB  ALA A  89      67.501  -8.449  29.061  1.00 94.70           C  
ANISOU 1137  CB  ALA A  89    10009  14753  11221    963    332   2373       C  
ATOM   1138  N   ASP A  90      66.987  -9.816  31.902  1.00 99.55           N  
ANISOU 1138  N   ASP A  90    10679  15473  11673   1196    703   2722       N  
ATOM   1139  CA  ASP A  90      67.053  -9.818  33.371  1.00100.77           C  
ANISOU 1139  CA  ASP A  90    10833  15801  11656   1344    869   2813       C  
ATOM   1140  C   ASP A  90      67.625 -11.128  33.893  1.00106.64           C  
ANISOU 1140  C   ASP A  90    11742  16534  12243   1535    950   2956       C  
ATOM   1141  O   ASP A  90      68.489 -11.109  34.770  1.00106.90           O  
ANISOU 1141  O   ASP A  90    11808  16805  12003   1731    987   2949       O  
ATOM   1142  CB  ASP A  90      65.667  -9.580  33.999  1.00103.34           C  
ANISOU 1142  CB  ASP A  90    11071  16024  12169   1252   1018   2919       C  
ATOM   1143  CG  ASP A  90      65.115  -8.178  33.851  1.00111.36           C  
ANISOU 1143  CG  ASP A  90    11934  17103  13274   1127    981   2795       C  
ATOM   1144  OD1 ASP A  90      65.908  -7.215  33.939  1.00109.70           O  
ANISOU 1144  OD1 ASP A  90    11695  17105  12881   1169    913   2641       O  
ATOM   1145  OD2 ASP A  90      63.872  -8.034  33.800  1.00119.64           O  
ANISOU 1145  OD2 ASP A  90    12892  18003  14563    999   1042   2863       O  
ATOM   1146  N   LEU A  91      67.139 -12.263  33.347  1.00104.14           N  
ANISOU 1146  N   LEU A  91    11538  15939  12093   1480    973   3082       N  
ATOM   1147  CA  LEU A  91      67.548 -13.614  33.720  1.00105.80           C  
ANISOU 1147  CA  LEU A  91    11947  16071  12180   1648   1063   3234       C  
ATOM   1148  C   LEU A  91      69.065 -13.792  33.519  1.00110.45           C  
ANISOU 1148  C   LEU A  91    12620  16866  12479   1852    964   3156       C  
ATOM   1149  O   LEU A  91      69.755 -14.254  34.435  1.00111.41           O  
ANISOU 1149  O   LEU A  91    12824  17161  12347   2085   1055   3226       O  
ATOM   1150  CB  LEU A  91      66.758 -14.636  32.874  1.00106.50           C  
ANISOU 1150  CB  LEU A  91    12144  15793  12527   1497   1045   3328       C  
ATOM   1151  CG  LEU A  91      66.782 -16.102  33.304  1.00113.37           C  
ANISOU 1151  CG  LEU A  91    13247  16490  13339   1620   1178   3517       C  
ATOM   1152  CD1 LEU A  91      65.996 -16.307  34.597  1.00115.28           C  
ANISOU 1152  CD1 LEU A  91    13481  16714  13606   1659   1426   3690       C  
ATOM   1153  CD2 LEU A  91      66.158 -16.973  32.239  1.00116.67           C  
ANISOU 1153  CD2 LEU A  91    13779  16546  14005   1440   1099   3556       C  
ATOM   1154  N   LEU A  92      69.584 -13.363  32.344  1.00105.65           N  
ANISOU 1154  N   LEU A  92    11978  16260  11904   1774    780   3011       N  
ATOM   1155  CA  LEU A  92      71.005 -13.477  32.000  1.00105.03           C  
ANISOU 1155  CA  LEU A  92    11948  16374  11583   1948    682   2937       C  
ATOM   1156  C   LEU A  92      71.862 -12.483  32.806  1.00109.91           C  
ANISOU 1156  C   LEU A  92    12417  17371  11972   2052    671   2824       C  
ATOM   1157  O   LEU A  92      73.036 -12.772  33.059  1.00110.37           O  
ANISOU 1157  O   LEU A  92    12509  17649  11776   2262    651   2819       O  
ATOM   1158  CB  LEU A  92      71.238 -13.256  30.491  1.00103.26           C  
ANISOU 1158  CB  LEU A  92    11727  16032  11473   1832    510   2820       C  
ATOM   1159  CG  LEU A  92      70.641 -14.296  29.526  1.00107.80           C  
ANISOU 1159  CG  LEU A  92    12487  16242  12228   1757    471   2903       C  
ATOM   1160  CD1 LEU A  92      70.848 -13.880  28.092  1.00106.03           C  
ANISOU 1160  CD1 LEU A  92    12257  15922  12108   1649    298   2767       C  
ATOM   1161  CD2 LEU A  92      71.238 -15.679  29.752  1.00111.87           C  
ANISOU 1161  CD2 LEU A  92    13239  16705  12564   1981    535   3044       C  
ATOM   1162  N   LEU A  93      71.286 -11.322  33.198  1.00106.36           N  
ANISOU 1162  N   LEU A  93    11805  16998  11607   1909    677   2732       N  
ATOM   1163  CA  LEU A  93      71.977 -10.306  34.006  1.00106.48           C  
ANISOU 1163  CA  LEU A  93    11692  17344  11419   1974    658   2612       C  
ATOM   1164  C   LEU A  93      72.209 -10.830  35.429  1.00113.42           C  
ANISOU 1164  C   LEU A  93    12640  18381  12074   2203    788   2724       C  
ATOM   1165  O   LEU A  93      73.317 -10.712  35.959  1.00113.69           O  
ANISOU 1165  O   LEU A  93    12643  18706  11847   2373    743   2662       O  
ATOM   1166  CB  LEU A  93      71.166  -8.992  34.037  1.00105.51           C  
ANISOU 1166  CB  LEU A  93    11430  17211  11446   1769    649   2501       C  
ATOM   1167  CG  LEU A  93      71.751  -7.813  34.836  1.00110.45           C  
ANISOU 1167  CG  LEU A  93    11945  18139  11884   1797    623   2358       C  
ATOM   1168  CD1 LEU A  93      73.024  -7.292  34.203  1.00109.95           C  
ANISOU 1168  CD1 LEU A  93    11807  18279  11691   1801    474   2197       C  
ATOM   1169  CD2 LEU A  93      70.756  -6.674  34.920  1.00112.83           C  
ANISOU 1169  CD2 LEU A  93    12160  18372  12338   1614    646   2283       C  
ATOM   1170  N   LEU A  94      71.155 -11.420  36.035  1.00111.56           N  
ANISOU 1170  N   LEU A  94    12496  17951  11943   2212    951   2894       N  
ATOM   1171  CA  LEU A  94      71.175 -12.003  37.380  1.00113.32           C  
ANISOU 1171  CA  LEU A  94    12821  18264  11971   2440   1112   3032       C  
ATOM   1172  C   LEU A  94      72.043 -13.264  37.425  1.00118.69           C  
ANISOU 1172  C   LEU A  94    13672  18970  12455   2681   1129   3135       C  
ATOM   1173  O   LEU A  94      72.556 -13.608  38.490  1.00119.50           O  
ANISOU 1173  O   LEU A  94    13850  19258  12297   2934   1207   3195       O  
ATOM   1174  CB  LEU A  94      69.743 -12.334  37.835  1.00114.22           C  
ANISOU 1174  CB  LEU A  94    12980  18126  12293   2356   1302   3200       C  
ATOM   1175  CG  LEU A  94      68.807 -11.144  38.082  1.00118.09           C  
ANISOU 1175  CG  LEU A  94    13317  18617  12937   2184   1333   3138       C  
ATOM   1176  CD1 LEU A  94      67.381 -11.563  38.026  1.00118.96           C  
ANISOU 1176  CD1 LEU A  94    13431  18436  13333   2045   1485   3299       C  
ATOM   1177  CD2 LEU A  94      69.140 -10.415  39.383  1.00121.08           C  
ANISOU 1177  CD2 LEU A  94    13673  19272  13061   2347   1387   3091       C  
ATOM   1178  N   ALA A  95      72.243 -13.922  36.262  1.00115.20           N  
ANISOU 1178  N   ALA A  95    13305  18350  12117   2624   1049   3147       N  
ATOM   1179  CA  ALA A  95      73.063 -15.127  36.121  1.00116.27           C  
ANISOU 1179  CA  ALA A  95    13625  18481  12070   2855   1060   3243       C  
ATOM   1180  C   ALA A  95      74.581 -14.830  36.325  1.00120.68           C  
ANISOU 1180  C   ALA A  95    14107  19423  12324   3064    940   3128       C  
ATOM   1181  O   ALA A  95      75.357 -15.774  36.490  1.00121.55           O  
ANISOU 1181  O   ALA A  95    14357  19601  12225   3314    959   3211       O  
ATOM   1182  CB  ALA A  95      72.838 -15.744  34.746  1.00116.28           C  
ANISOU 1182  CB  ALA A  95    13734  18177  12272   2721    992   3269       C  
ATOM   1183  N   THR A  96      74.998 -13.539  36.325  1.00116.42           N  
ANISOU 1183  N   THR A  96    13345  19132  11757   2964    822   2942       N  
ATOM   1184  CA  THR A  96      76.413 -13.168  36.512  1.00116.38           C  
ANISOU 1184  CA  THR A  96    13222  19504  11492   3122    699   2820       C  
ATOM   1185  C   THR A  96      76.738 -12.912  38.007  1.00122.38           C  
ANISOU 1185  C   THR A  96    13953  20554  11991   3322    745   2813       C  
ATOM   1186  O   THR A  96      77.919 -12.870  38.361  1.00122.93           O  
ANISOU 1186  O   THR A  96    13947  20953  11807   3510    654   2742       O  
ATOM   1187  CB  THR A  96      76.789 -11.926  35.679  1.00117.59           C  
ANISOU 1187  CB  THR A  96    13161  19760  11757   2893    541   2613       C  
ATOM   1188  OG1 THR A  96      76.025 -10.801  36.116  1.00114.76           O  
ANISOU 1188  OG1 THR A  96    12696  19398  11511   2701    554   2522       O  
ATOM   1189  CG2 THR A  96      76.624 -12.143  34.177  1.00112.35           C  
ANISOU 1189  CG2 THR A  96    12539  18839  11310   2738    481   2607       C  
ATOM   1190  N   LEU A  97      75.699 -12.764  38.876  1.00119.70           N  
ANISOU 1190  N   LEU A  97    13675  20098  11709   3295    885   2891       N  
ATOM   1191  CA  LEU A  97      75.852 -12.515  40.320  1.00121.18           C  
ANISOU 1191  CA  LEU A  97    13877  20515  11653   3494    945   2896       C  
ATOM   1192  C   LEU A  97      76.765 -13.572  41.005  1.00128.03           C  
ANISOU 1192  C   LEU A  97    14887  21559  12199   3872    986   3003       C  
ATOM   1193  O   LEU A  97      77.619 -13.140  41.785  1.00128.76           O  
ANISOU 1193  O   LEU A  97    14904  21993  12027   4047    903   2907       O  
ATOM   1194  CB  LEU A  97      74.498 -12.467  41.045  1.00121.49           C  
ANISOU 1194  CB  LEU A  97    14002  20334  11823   3433   1134   3016       C  
ATOM   1195  CG  LEU A  97      73.722 -11.157  40.900  1.00124.51           C  
ANISOU 1195  CG  LEU A  97    14233  20662  12412   3150   1102   2895       C  
ATOM   1196  CD1 LEU A  97      72.315 -11.291  41.410  1.00125.04           C  
ANISOU 1196  CD1 LEU A  97    14381  20476  12652   3091   1309   3051       C  
ATOM   1197  CD2 LEU A  97      74.419 -10.023  41.631  1.00127.33           C  
ANISOU 1197  CD2 LEU A  97    14472  21351  12558   3193    987   2710       C  
ATOM   1198  N   PRO A  98      76.701 -14.908  40.707  1.00125.91           N  
ANISOU 1198  N   PRO A  98    14825  21087  11927   4013   1094   3185       N  
ATOM   1199  CA  PRO A  98      77.639 -15.840  41.371  1.00128.14           C  
ANISOU 1199  CA  PRO A  98    15252  21564  11871   4403   1132   3278       C  
ATOM   1200  C   PRO A  98      79.118 -15.495  41.101  1.00133.03           C  
ANISOU 1200  C   PRO A  98    15694  22578  12271   4531    925   3123       C  
ATOM   1201  O   PRO A  98      79.957 -15.775  41.956  1.00134.81           O  
ANISOU 1201  O   PRO A  98    15936  23106  12179   4838    903   3123       O  
ATOM   1202  CB  PRO A  98      77.283 -17.197  40.757  1.00130.20           C  
ANISOU 1202  CB  PRO A  98    15758  21490  12221   4455   1258   3470       C  
ATOM   1203  CG  PRO A  98      75.870 -17.055  40.323  1.00133.25           C  
ANISOU 1203  CG  PRO A  98    16160  21495  12973   4128   1348   3520       C  
ATOM   1204  CD  PRO A  98      75.760 -15.645  39.834  1.00126.66           C  
ANISOU 1204  CD  PRO A  98    15052  20766  12306   3839   1186   3312       C  
ATOM   1205  N   LEU A  99      79.427 -14.857  39.943  1.00128.01           N  
ANISOU 1205  N   LEU A  99    14880  21951  11806   4296    774   2989       N  
ATOM   1206  CA  LEU A  99      80.791 -14.444  39.586  1.00128.12           C  
ANISOU 1206  CA  LEU A  99    14688  22328  11665   4367    587   2842       C  
ATOM   1207  C   LEU A  99      81.278 -13.275  40.433  1.00133.50           C  
ANISOU 1207  C   LEU A  99    15150  23360  12213   4338    462   2656       C  
ATOM   1208  O   LEU A  99      82.407 -13.321  40.924  1.00134.61           O  
ANISOU 1208  O   LEU A  99    15197  23870  12081   4572    363   2599       O  
ATOM   1209  CB  LEU A  99      80.900 -14.044  38.102  1.00126.04           C  
ANISOU 1209  CB  LEU A  99    14305  21942  11641   4105    487   2756       C  
ATOM   1210  CG  LEU A  99      80.716 -15.120  37.049  1.00130.22           C  
ANISOU 1210  CG  LEU A  99    15034  22164  12279   4135    553   2900       C  
ATOM   1211  CD1 LEU A  99      80.653 -14.500  35.671  1.00128.31           C  
ANISOU 1211  CD1 LEU A  99    14676  21790  12286   3854    453   2793       C  
ATOM   1212  CD2 LEU A  99      81.844 -16.153  37.110  1.00134.41           C  
ANISOU 1212  CD2 LEU A  99    15666  22884  12521   4508    558   3000       C  
ATOM   1213  N   TRP A 100      80.452 -12.209  40.573  1.00129.81           N  
ANISOU 1213  N   TRP A 100    14603  22787  11933   4055    459   2554       N  
ATOM   1214  CA  TRP A 100      80.850 -10.997  41.297  1.00130.66           C  
ANISOU 1214  CA  TRP A 100    14528  23188  11930   3990    332   2360       C  
ATOM   1215  C   TRP A 100      80.936 -11.277  42.793  1.00137.63           C  
ANISOU 1215  C   TRP A 100    15526  24249  12520   4291    387   2413       C  
ATOM   1216  O   TRP A 100      81.791 -10.698  43.458  1.00139.16           O  
ANISOU 1216  O   TRP A 100    15585  24792  12496   4380    242   2265       O  
ATOM   1217  CB  TRP A 100      79.898  -9.815  41.029  1.00127.76           C  
ANISOU 1217  CB  TRP A 100    14088  22633  11822   3634    333   2251       C  
ATOM   1218  CG  TRP A 100      79.516  -9.627  39.581  1.00126.64           C  
ANISOU 1218  CG  TRP A 100    13896  22236  11987   3353    319   2231       C  
ATOM   1219  CD1 TRP A 100      78.249  -9.602  39.078  1.00128.08           C  
ANISOU 1219  CD1 TRP A 100    14169  22052  12443   3155    427   2306       C  
ATOM   1220  CD2 TRP A 100      80.394  -9.693  38.441  1.00125.82           C  
ANISOU 1220  CD2 TRP A 100    13671  22205  11929   3296    208   2168       C  
ATOM   1221  NE1 TRP A 100      78.285  -9.504  37.706  1.00125.86           N  
ANISOU 1221  NE1 TRP A 100    13830  21621  12371   2963    366   2264       N  
ATOM   1222  CE2 TRP A 100      79.587  -9.596  37.285  1.00127.81           C  
ANISOU 1222  CE2 TRP A 100    13962  22119  12481   3054    245   2190       C  
ATOM   1223  CE3 TRP A 100      81.789  -9.797  38.284  1.00128.10           C  
ANISOU 1223  CE3 TRP A 100    13812  22824  12036   3431     82   2095       C  
ATOM   1224  CZ2 TRP A 100      80.126  -9.590  35.990  1.00126.14           C  
ANISOU 1224  CZ2 TRP A 100    13676  21873  12377   2956    167   2142       C  
ATOM   1225  CZ3 TRP A 100      82.320  -9.799  37.003  1.00128.58           C  
ANISOU 1225  CZ3 TRP A 100    13782  22856  12218   3327     21   2060       C  
ATOM   1226  CH2 TRP A 100      81.495  -9.683  35.874  1.00127.14           C  
ANISOU 1226  CH2 TRP A 100    13666  22319  12321   3096     65   2081       C  
ATOM   1227  N   ALA A 101      80.101 -12.199  43.313  1.00134.86           N  
ANISOU 1227  N   ALA A 101    15427  23658  12154   4456    593   2624       N  
ATOM   1228  CA  ALA A 101      80.154 -12.599  44.721  1.00137.10           C  
ANISOU 1228  CA  ALA A 101    15868  24077  12145   4787    679   2706       C  
ATOM   1229  C   ALA A 101      81.452 -13.371  45.013  1.00142.92           C  
ANISOU 1229  C   ALA A 101    16616  25131  12555   5152    599   2727       C  
ATOM   1230  O   ALA A 101      82.070 -13.141  46.051  1.00144.42           O  
ANISOU 1230  O   ALA A 101    16792  25631  12449   5392    524   2660       O  
ATOM   1231  CB  ALA A 101      78.940 -13.440  45.077  1.00138.13           C  
ANISOU 1231  CB  ALA A 101    16264  23841  12378   4846    947   2941       C  
ATOM   1232  N   THR A 102      81.884 -14.246  44.066  1.00139.00           N  
ANISOU 1232  N   THR A 102    16143  24566  12103   5202    603   2812       N  
ATOM   1233  CA  THR A 102      83.119 -15.040  44.158  1.00140.60           C  
ANISOU 1233  CA  THR A 102    16354  25059  12010   5557    538   2849       C  
ATOM   1234  C   THR A 102      84.332 -14.098  44.040  1.00145.31           C  
ANISOU 1234  C   THR A 102    16614  26093  12503   5506    275   2616       C  
ATOM   1235  O   THR A 102      85.244 -14.178  44.859  1.00146.99           O  
ANISOU 1235  O   THR A 102    16767  26679  12402   5796    173   2566       O  
ATOM   1236  CB  THR A 102      83.129 -16.143  43.076  1.00145.84           C  
ANISOU 1236  CB  THR A 102    17164  25474  12774   5601    632   3011       C  
ATOM   1237  OG1 THR A 102      81.994 -16.992  43.261  1.00144.76           O  
ANISOU 1237  OG1 THR A 102    17331  24928  12743   5618    870   3216       O  
ATOM   1238  CG2 THR A 102      84.389 -16.987  43.109  1.00146.16           C  
ANISOU 1238  CG2 THR A 102    17231  25802  12502   5993    584   3068       C  
ATOM   1239  N   TYR A 103      84.313 -13.188  43.043  1.00140.66           N  
ANISOU 1239  N   TYR A 103    15807  25455  12181   5134    169   2473       N  
ATOM   1240  CA  TYR A 103      85.364 -12.192  42.792  1.00141.11           C  
ANISOU 1240  CA  TYR A 103    15531  25876  12207   5005    -61   2249       C  
ATOM   1241  C   TYR A 103      85.528 -11.276  44.027  1.00146.82           C  
ANISOU 1241  C   TYR A 103    16156  26875  12752   5021   -183   2081       C  
ATOM   1242  O   TYR A 103      86.660 -11.005  44.425  1.00148.09           O  
ANISOU 1242  O   TYR A 103    16113  27451  12705   5143   -366   1950       O  
ATOM   1243  CB  TYR A 103      85.019 -11.386  41.523  1.00139.68           C  
ANISOU 1243  CB  TYR A 103    15208  25488  12374   4583    -96   2152       C  
ATOM   1244  CG  TYR A 103      85.971 -10.264  41.149  1.00141.63           C  
ANISOU 1244  CG  TYR A 103    15122  26040  12651   4374   -300   1920       C  
ATOM   1245  CD1 TYR A 103      87.282 -10.535  40.765  1.00145.10           C  
ANISOU 1245  CD1 TYR A 103    15360  26803  12969   4509   -415   1887       C  
ATOM   1246  CD2 TYR A 103      85.505  -8.966  40.968  1.00140.81           C  
ANISOU 1246  CD2 TYR A 103    14910  25850  12740   4012   -355   1751       C  
ATOM   1247  CE1 TYR A 103      88.142  -9.516  40.346  1.00146.31           C  
ANISOU 1247  CE1 TYR A 103    15193  27216  13184   4285   -584   1684       C  
ATOM   1248  CE2 TYR A 103      86.348  -7.944  40.530  1.00141.66           C  
ANISOU 1248  CE2 TYR A 103    14730  26194  12902   3788   -521   1544       C  
ATOM   1249  CZ  TYR A 103      87.666  -8.221  40.225  1.00150.42           C  
ANISOU 1249  CZ  TYR A 103    15624  27637  13893   3914   -634   1511       C  
ATOM   1250  OH  TYR A 103      88.492  -7.209  39.796  1.00150.87           O  
ANISOU 1250  OH  TYR A 103    15383  27920  14022   3672   -784   1313       O  
ATOM   1251  N   TYR A 104      84.408 -10.875  44.673  1.00143.25           N  
ANISOU 1251  N   TYR A 104    15861  26204  12364   4927    -79   2096       N  
ATOM   1252  CA  TYR A 104      84.436 -10.055  45.891  1.00144.85           C  
ANISOU 1252  CA  TYR A 104    16036  26621  12380   4969   -175   1953       C  
ATOM   1253  C   TYR A 104      84.996 -10.869  47.075  1.00152.66           C  
ANISOU 1253  C   TYR A 104    17156  27867  12980   5438   -175   2031       C  
ATOM   1254  O   TYR A 104      85.747 -10.314  47.882  1.00154.17           O  
ANISOU 1254  O   TYR A 104    17229  28413  12936   5544   -359   1867       O  
ATOM   1255  CB  TYR A 104      83.032  -9.518  46.224  1.00144.49           C  
ANISOU 1255  CB  TYR A 104    16149  26244  12504   4778    -30   1981       C  
ATOM   1256  CG  TYR A 104      82.983  -8.585  47.418  1.00147.46           C  
ANISOU 1256  CG  TYR A 104    16533  26800  12695   4810   -120   1832       C  
ATOM   1257  CD1 TYR A 104      83.118  -7.211  47.259  1.00148.73           C  
ANISOU 1257  CD1 TYR A 104    16507  27058  12946   4499   -287   1594       C  
ATOM   1258  CD2 TYR A 104      82.744  -9.072  48.700  1.00150.28           C  
ANISOU 1258  CD2 TYR A 104    17117  27194  12787   5150    -21   1935       C  
ATOM   1259  CE1 TYR A 104      83.049  -6.344  48.351  1.00150.82           C  
ANISOU 1259  CE1 TYR A 104    16814  27460  13032   4525   -373   1451       C  
ATOM   1260  CE2 TYR A 104      82.688  -8.217  49.801  1.00152.66           C  
ANISOU 1260  CE2 TYR A 104    17457  27646  12902   5198   -106   1798       C  
ATOM   1261  CZ  TYR A 104      82.828  -6.852  49.621  1.00159.20           C  
ANISOU 1261  CZ  TYR A 104    18104  28567  13819   4880   -287   1553       C  
ATOM   1262  OH  TYR A 104      82.760  -6.006  50.704  1.00161.55           O  
ANISOU 1262  OH  TYR A 104    18472  28991  13920   4929   -376   1412       O  
ATOM   1263  N   SER A 105      84.626 -12.178  47.174  1.00150.40           N  
ANISOU 1263  N   SER A 105    17129  27394  12624   5718     29   2277       N  
ATOM   1264  CA  SER A 105      85.068 -13.092  48.242  1.00153.44           C  
ANISOU 1264  CA  SER A 105    17696  27970  12636   6200     75   2389       C  
ATOM   1265  C   SER A 105      86.588 -13.288  48.236  1.00159.91           C  
ANISOU 1265  C   SER A 105    18304  29256  13199   6435   -140   2293       C  
ATOM   1266  O   SER A 105      87.192 -13.341  49.309  1.00162.62           O  
ANISOU 1266  O   SER A 105    18661  29922  13205   6753   -240   2241       O  
ATOM   1267  CB  SER A 105      84.390 -14.453  48.114  1.00156.88           C  
ANISOU 1267  CB  SER A 105    18452  28060  13094   6397    352   2675       C  
ATOM   1268  OG  SER A 105      82.987 -14.361  48.299  1.00163.94           O  
ANISOU 1268  OG  SER A 105    19537  28557  14197   6227    563   2781       O  
ATOM   1269  N   TYR A 106      87.204 -13.388  47.040  1.00155.21           N  
ANISOU 1269  N   TYR A 106    17509  28707  12755   6293   -214   2271       N  
ATOM   1270  CA  TYR A 106      88.651 -13.560  46.910  1.00157.05           C  
ANISOU 1270  CA  TYR A 106    17501  29391  12781   6495   -406   2192       C  
ATOM   1271  C   TYR A 106      89.374 -12.186  46.911  1.00160.87           C  
ANISOU 1271  C   TYR A 106    17604  30208  13311   6215   -681   1902       C  
ATOM   1272  O   TYR A 106      90.498 -12.087  46.418  1.00161.78           O  
ANISOU 1272  O   TYR A 106    17431  30640  13398   6215   -840   1815       O  
ATOM   1273  CB  TYR A 106      89.002 -14.359  45.637  1.00157.57           C  
ANISOU 1273  CB  TYR A 106    17553  29347  12970   6510   -333   2324       C  
ATOM   1274  CG  TYR A 106      88.655 -15.830  45.733  1.00160.50           C  
ANISOU 1274  CG  TYR A 106    18292  29479  13212   6858   -101   2595       C  
ATOM   1275  CD1 TYR A 106      89.527 -16.734  46.338  1.00165.51           C  
ANISOU 1275  CD1 TYR A 106    19007  30403  13478   7348   -109   2687       C  
ATOM   1276  CD2 TYR A 106      87.488 -16.332  45.167  1.00159.25           C  
ANISOU 1276  CD2 TYR A 106    18400  28805  13302   6695    124   2757       C  
ATOM   1277  CE1 TYR A 106      89.217 -18.090  46.426  1.00167.25           C  
ANISOU 1277  CE1 TYR A 106    19596  30381  13568   7672    119   2939       C  
ATOM   1278  CE2 TYR A 106      87.169 -17.687  45.247  1.00160.96           C  
ANISOU 1278  CE2 TYR A 106    18968  28778  13411   6990    341   3002       C  
ATOM   1279  CZ  TYR A 106      88.039 -18.564  45.873  1.00171.34           C  
ANISOU 1279  CZ  TYR A 106    20387  30365  14348   7478    346   3095       C  
ATOM   1280  OH  TYR A 106      87.734 -19.902  45.951  1.00173.31           O  
ANISOU 1280  OH  TYR A 106    21015  30354  14480   7772    574   3339       O  
ATOM   1281  N   ARG A 107      88.751 -11.156  47.542  1.00156.49           N  
ANISOU 1281  N   ARG A 107    17060  29592  12805   6002   -729   1760       N  
ATOM   1282  CA  ARG A 107      89.251  -9.778  47.695  1.00156.64           C  
ANISOU 1282  CA  ARG A 107    16789  29863  12865   5712   -973   1478       C  
ATOM   1283  C   ARG A 107      89.749  -9.227  46.339  1.00158.70           C  
ANISOU 1283  C   ARG A 107    16751  30130  13417   5343  -1051   1380       C  
ATOM   1284  O   ARG A 107      90.876  -8.742  46.230  1.00159.97           O  
ANISOU 1284  O   ARG A 107    16590  30668  13523   5282  -1265   1212       O  
ATOM   1285  CB  ARG A 107      90.365  -9.702  48.758  1.00160.68           C  
ANISOU 1285  CB  ARG A 107    17151  30890  13011   6005  -1210   1340       C  
ATOM   1286  N   TYR A 108      88.873  -9.315  45.317  1.00151.90           N  
ANISOU 1286  N   TYR A 108    16004  28843  12867   5101   -871   1490       N  
ATOM   1287  CA  TYR A 108      89.039  -8.849  43.936  1.00149.46           C  
ANISOU 1287  CA  TYR A 108    15503  28421  12865   4752   -885   1435       C  
ATOM   1288  C   TYR A 108      90.251  -9.538  43.262  1.00154.86           C  
ANISOU 1288  C   TYR A 108    15996  29367  13477   4932   -940   1491       C  
ATOM   1289  O   TYR A 108      91.069  -8.877  42.611  1.00154.59           O  
ANISOU 1289  O   TYR A 108    15655  29532  13549   4723  -1070   1353       O  
ATOM   1290  CB  TYR A 108      89.174  -7.318  43.872  1.00150.10           C  
ANISOU 1290  CB  TYR A 108    15353  28597  13082   4356  -1047   1172       C  
ATOM   1291  CG  TYR A 108      87.958  -6.615  44.420  1.00150.29           C  
ANISOU 1291  CG  TYR A 108    15575  28341  13188   4177   -977   1126       C  
ATOM   1292  CD1 TYR A 108      86.802  -6.490  43.662  1.00149.37           C  
ANISOU 1292  CD1 TYR A 108    15598  27788  13367   3922   -812   1198       C  
ATOM   1293  CD2 TYR A 108      87.962  -6.071  45.701  1.00152.90           C  
ANISOU 1293  CD2 TYR A 108    15956  28847  13290   4280  -1079   1011       C  
ATOM   1294  CE1 TYR A 108      85.672  -5.865  44.170  1.00149.10           C  
ANISOU 1294  CE1 TYR A 108    15736  27510  13403   3782   -734   1171       C  
ATOM   1295  CE2 TYR A 108      86.843  -5.425  46.212  1.00152.79           C  
ANISOU 1295  CE2 TYR A 108    16138  28576  13337   4142   -998    982       C  
ATOM   1296  CZ  TYR A 108      85.700  -5.324  45.442  1.00157.22           C  
ANISOU 1296  CZ  TYR A 108    16821  28716  14199   3895   -820   1067       C  
ATOM   1297  OH  TYR A 108      84.599  -4.687  45.935  1.00157.73           O  
ANISOU 1297  OH  TYR A 108    17065  28545  14321   3777   -733   1049       O  
ATOM   1298  N   ASP A 109      90.302 -10.886  43.363  1.00152.37           N  
ANISOU 1298  N   ASP A 109    15884  29015  12994   5316   -816   1709       N  
ATOM   1299  CA  ASP A 109      91.309 -11.709  42.698  1.00153.15           C  
ANISOU 1299  CA  ASP A 109    15871  29311  13009   5540   -826   1806       C  
ATOM   1300  C   ASP A 109      90.617 -12.525  41.621  1.00154.35           C  
ANISOU 1300  C   ASP A 109    16266  29024  13355   5513   -618   2007       C  
ATOM   1301  O   ASP A 109      89.966 -13.533  41.922  1.00153.81           O  
ANISOU 1301  O   ASP A 109    16529  28704  13207   5738   -450   2196       O  
ATOM   1302  CB  ASP A 109      92.073 -12.603  43.695  1.00158.33           C  
ANISOU 1302  CB  ASP A 109    16567  30325  13267   6045   -873   1882       C  
ATOM   1303  CG  ASP A 109      93.347 -13.232  43.149  1.00171.66           C  
ANISOU 1303  CG  ASP A 109    18050  32346  14825   6290   -935   1936       C  
ATOM   1304  OD1 ASP A 109      93.849 -12.756  42.103  1.00171.14           O  
ANISOU 1304  OD1 ASP A 109    17723  32338  14965   6039   -991   1863       O  
ATOM   1305  OD2 ASP A 109      93.914 -14.102  43.835  1.00181.05           O  
ANISOU 1305  OD2 ASP A 109    19314  33783  15692   6739   -940   2035       O  
ATOM   1306  N   TRP A 110      90.687 -12.038  40.372  1.00148.64           N  
ANISOU 1306  N   TRP A 110    15393  28183  12898   5218   -626   1960       N  
ATOM   1307  CA  TRP A 110      90.051 -12.678  39.230  1.00145.97           C  
ANISOU 1307  CA  TRP A 110    15272  27426  12765   5153   -461   2119       C  
ATOM   1308  C   TRP A 110      90.784 -13.989  38.916  1.00151.29           C  
ANISOU 1308  C   TRP A 110    16051  28198  13236   5558   -397   2306       C  
ATOM   1309  O   TRP A 110      91.946 -13.971  38.494  1.00151.78           O  
ANISOU 1309  O   TRP A 110    15867  28589  13214   5663   -487   2274       O  
ATOM   1310  CB  TRP A 110      90.034 -11.725  38.025  1.00142.48           C  
ANISOU 1310  CB  TRP A 110    14639  26865  12632   4753   -501   2001       C  
ATOM   1311  CG  TRP A 110      89.225 -12.228  36.868  1.00140.85           C  
ANISOU 1311  CG  TRP A 110    14669  26192  12654   4646   -354   2135       C  
ATOM   1312  CD1 TRP A 110      89.672 -12.963  35.811  1.00143.49           C  
ANISOU 1312  CD1 TRP A 110    15058  26454  13009   4771   -299   2254       C  
ATOM   1313  CD2 TRP A 110      87.810 -12.087  36.690  1.00138.42           C  
ANISOU 1313  CD2 TRP A 110    14593  25430  12569   4422   -247   2170       C  
ATOM   1314  NE1 TRP A 110      88.629 -13.256  34.964  1.00140.73           N  
ANISOU 1314  NE1 TRP A 110    14962  25624  12884   4618   -184   2342       N  
ATOM   1315  CE2 TRP A 110      87.473 -12.734  35.481  1.00140.87           C  
ANISOU 1315  CE2 TRP A 110    15077  25408  13036   4399   -153   2294       C  
ATOM   1316  CE3 TRP A 110      86.790 -11.473  37.436  1.00138.89           C  
ANISOU 1316  CE3 TRP A 110    14729  25336  12708   4246   -224   2110       C  
ATOM   1317  CZ2 TRP A 110      86.158 -12.782  34.997  1.00138.00           C  
ANISOU 1317  CZ2 TRP A 110    14936  24580  12916   4190    -55   2349       C  
ATOM   1318  CZ3 TRP A 110      85.490 -11.514  36.954  1.00138.22           C  
ANISOU 1318  CZ3 TRP A 110    14851  24800  12868   4048   -108   2178       C  
ATOM   1319  CH2 TRP A 110      85.183 -12.162  35.748  1.00137.50           C  
ANISOU 1319  CH2 TRP A 110    14907  24397  12939   4014    -33   2291       C  
ATOM   1320  N   LEU A 111      90.114 -15.124  39.199  1.00148.42           N  
ANISOU 1320  N   LEU A 111    16056  27562  12776   5799   -234   2503       N  
ATOM   1321  CA  LEU A 111      90.651 -16.476  39.013  1.00150.15           C  
ANISOU 1321  CA  LEU A 111    16469  27808  12774   6216   -141   2702       C  
ATOM   1322  C   LEU A 111      89.935 -17.210  37.854  1.00152.64           C  
ANISOU 1322  C   LEU A 111    17074  27630  13291   6134     16   2859       C  
ATOM   1323  O   LEU A 111      89.714 -18.421  37.934  1.00153.07           O  
ANISOU 1323  O   LEU A 111    17470  27469  13222   6399    162   3051       O  
ATOM   1324  CB  LEU A 111      90.497 -17.276  40.332  1.00152.51           C  
ANISOU 1324  CB  LEU A 111    17004  28176  12767   6590    -68   2811       C  
ATOM   1325  CG  LEU A 111      91.223 -16.739  41.592  1.00159.86           C  
ANISOU 1325  CG  LEU A 111    17707  29594  13439   6749   -230   2669       C  
ATOM   1326  CD1 LEU A 111      90.727 -17.436  42.844  1.00161.73           C  
ANISOU 1326  CD1 LEU A 111    18249  29773  13428   7064   -120   2784       C  
ATOM   1327  CD2 LEU A 111      92.747 -16.844  41.469  1.00164.70           C  
ANISOU 1327  CD2 LEU A 111    18021  30725  13833   7003   -382   2623       C  
ATOM   1328  N   PHE A 112      89.603 -16.479  36.766  1.00147.20           N  
ANISOU 1328  N   PHE A 112    16263  26760  12904   5772    -17   2772       N  
ATOM   1329  CA  PHE A 112      88.890 -17.041  35.613  1.00145.24           C  
ANISOU 1329  CA  PHE A 112    16273  26046  12866   5660     96   2887       C  
ATOM   1330  C   PHE A 112      89.609 -16.743  34.264  1.00146.55           C  
ANISOU 1330  C   PHE A 112    16262  26270  13150   5561     37   2842       C  
ATOM   1331  O   PHE A 112      89.089 -17.095  33.199  1.00144.39           O  
ANISOU 1331  O   PHE A 112    16183  25626  13054   5454    104   2911       O  
ATOM   1332  CB  PHE A 112      87.455 -16.479  35.557  1.00145.18           C  
ANISOU 1332  CB  PHE A 112    16374  25631  13156   5283    144   2841       C  
ATOM   1333  CG  PHE A 112      86.582 -16.801  36.748  1.00147.90           C  
ANISOU 1333  CG  PHE A 112    16917  25850  13429   5354    239   2909       C  
ATOM   1334  CD1 PHE A 112      85.802 -17.951  36.768  1.00151.69           C  
ANISOU 1334  CD1 PHE A 112    17767  25970  13898   5492    404   3105       C  
ATOM   1335  CD2 PHE A 112      86.493 -15.924  37.825  1.00150.99           C  
ANISOU 1335  CD2 PHE A 112    17138  26454  13775   5265    173   2778       C  
ATOM   1336  CE1 PHE A 112      84.973 -18.236  37.859  1.00153.58           C  
ANISOU 1336  CE1 PHE A 112    18187  26079  14086   5551    519   3182       C  
ATOM   1337  CE2 PHE A 112      85.661 -16.209  38.917  1.00154.70           C  
ANISOU 1337  CE2 PHE A 112    17805  26796  14177   5346    281   2854       C  
ATOM   1338  CZ  PHE A 112      84.905 -17.361  38.925  1.00153.12           C  
ANISOU 1338  CZ  PHE A 112    17956  26248  13975   5488    462   3061       C  
ATOM   1339  N   GLY A 113      90.785 -16.120  34.325  1.00143.06           N  
ANISOU 1339  N   GLY A 113    15460  26288  12609   5602    -84   2729       N  
ATOM   1340  CA  GLY A 113      91.551 -15.777  33.131  1.00142.05           C  
ANISOU 1340  CA  GLY A 113    15130  26261  12582   5522   -123   2690       C  
ATOM   1341  C   GLY A 113      91.168 -14.429  32.547  1.00143.02           C  
ANISOU 1341  C   GLY A 113    15059  26266  13016   5057   -183   2511       C  
ATOM   1342  O   GLY A 113      90.019 -14.006  32.682  1.00140.60           O  
ANISOU 1342  O   GLY A 113    14895  25627  12898   4797   -155   2469       O  
ATOM   1343  N   PRO A 114      92.098 -13.732  31.847  1.00139.86           N  
ANISOU 1343  N   PRO A 114    14338  26123  12681   4947   -251   2412       N  
ATOM   1344  CA  PRO A 114      91.778 -12.391  31.324  1.00137.85           C  
ANISOU 1344  CA  PRO A 114    13908  25759  12709   4507   -296   2236       C  
ATOM   1345  C   PRO A 114      90.779 -12.402  30.153  1.00139.28           C  
ANISOU 1345  C   PRO A 114    14350  25429  13142   4314   -207   2282       C  
ATOM   1346  O   PRO A 114      90.232 -11.344  29.824  1.00137.11           O  
ANISOU 1346  O   PRO A 114    14002  24997  13098   3960   -230   2147       O  
ATOM   1347  CB  PRO A 114      93.137 -11.867  30.844  1.00141.13           C  
ANISOU 1347  CB  PRO A 114    13947  26571  13105   4502   -358   2163       C  
ATOM   1348  CG  PRO A 114      94.155 -12.726  31.519  1.00148.62           C  
ANISOU 1348  CG  PRO A 114    14791  27937  13742   4907   -395   2249       C  
ATOM   1349  CD  PRO A 114      93.513 -14.066  31.605  1.00143.96           C  
ANISOU 1349  CD  PRO A 114    14616  27072  13011   5218   -286   2451       C  
ATOM   1350  N   VAL A 115      90.534 -13.573  29.532  1.00135.54           N  
ANISOU 1350  N   VAL A 115    14188  24694  12616   4547   -113   2465       N  
ATOM   1351  CA  VAL A 115      89.594 -13.695  28.414  1.00133.05           C  
ANISOU 1351  CA  VAL A 115    14142  23891  12518   4394    -50   2510       C  
ATOM   1352  C   VAL A 115      88.155 -13.549  28.963  1.00134.90           C  
ANISOU 1352  C   VAL A 115    14563  23791  12903   4176    -37   2481       C  
ATOM   1353  O   VAL A 115      87.377 -12.769  28.412  1.00132.16           O  
ANISOU 1353  O   VAL A 115    14233  23179  12801   3870    -47   2392       O  
ATOM   1354  CB  VAL A 115      89.790 -15.021  27.621  1.00137.83           C  
ANISOU 1354  CB  VAL A 115    15050  24316  13002   4718     33   2709       C  
ATOM   1355  CG1 VAL A 115      88.745 -15.173  26.513  1.00135.59           C  
ANISOU 1355  CG1 VAL A 115    15068  23512  12938   4556     72   2742       C  
ATOM   1356  CG2 VAL A 115      91.199 -15.107  27.035  1.00139.42           C  
ANISOU 1356  CG2 VAL A 115    15054  24857  13060   4945     37   2748       C  
ATOM   1357  N   MET A 116      87.835 -14.232  30.086  1.00132.47           N  
ANISOU 1357  N   MET A 116    14374  23517  12441   4341    -10   2555       N  
ATOM   1358  CA  MET A 116      86.502 -14.164  30.697  1.00130.99           C  
ANISOU 1358  CA  MET A 116    14352  23036  12381   4168     27   2553       C  
ATOM   1359  C   MET A 116      86.278 -12.807  31.395  1.00131.89           C  
ANISOU 1359  C   MET A 116    14212  23309  12589   3886    -45   2365       C  
ATOM   1360  O   MET A 116      85.132 -12.466  31.691  1.00130.63           O  
ANISOU 1360  O   MET A 116    14147  22897  12588   3682    -17   2339       O  
ATOM   1361  CB  MET A 116      86.278 -15.307  31.686  1.00135.34           C  
ANISOU 1361  CB  MET A 116    15130  23568  12727   4457    106   2708       C  
ATOM   1362  CG  MET A 116      86.282 -16.655  31.016  1.00140.33           C  
ANISOU 1362  CG  MET A 116    16078  23956  13283   4701    191   2893       C  
ATOM   1363  SD  MET A 116      85.844 -18.015  32.116  1.00147.38           S  
ANISOU 1363  SD  MET A 116    17298  24744  13955   5017    319   3088       S  
ATOM   1364  CE  MET A 116      86.192 -19.411  31.041  1.00144.79           C  
ANISOU 1364  CE  MET A 116    17323  24142  13551   5269    392   3270       C  
ATOM   1365  N   CYS A 117      87.353 -12.023  31.616  1.00127.19           N  
ANISOU 1365  N   CYS A 117    13299  23121  11908   3866   -138   2235       N  
ATOM   1366  CA  CYS A 117      87.260 -10.665  32.159  1.00125.45           C  
ANISOU 1366  CA  CYS A 117    12845  23050  11771   3585   -218   2039       C  
ATOM   1367  C   CYS A 117      86.587  -9.767  31.101  1.00126.61           C  
ANISOU 1367  C   CYS A 117    12989  22906  12211   3238   -211   1945       C  
ATOM   1368  O   CYS A 117      85.691  -8.991  31.437  1.00125.60           O  
ANISOU 1368  O   CYS A 117    12850  22656  12216   2989   -222   1840       O  
ATOM   1369  CB  CYS A 117      88.642 -10.151  32.570  1.00127.19           C  
ANISOU 1369  CB  CYS A 117    12731  23771  11824   3654   -327   1928       C  
ATOM   1370  SG  CYS A 117      88.689  -8.416  33.096  1.00130.51           S  
ANISOU 1370  SG  CYS A 117    12870  24376  12343   3285   -441   1666       S  
ATOM   1371  N   LYS A 118      86.953  -9.958  29.808  1.00121.46           N  
ANISOU 1371  N   LYS A 118    12382  22122  11645   3255   -183   1996       N  
ATOM   1372  CA  LYS A 118      86.370  -9.230  28.674  1.00118.73           C  
ANISOU 1372  CA  LYS A 118    12073  21486  11554   2982   -170   1925       C  
ATOM   1373  C   LYS A 118      85.002  -9.785  28.276  1.00121.74           C  
ANISOU 1373  C   LYS A 118    12763  21402  12088   2929   -113   2017       C  
ATOM   1374  O   LYS A 118      84.122  -9.006  27.917  1.00119.90           O  
ANISOU 1374  O   LYS A 118    12556  20938  12063   2666   -117   1930       O  
ATOM   1375  CB  LYS A 118      87.288  -9.273  27.437  1.00120.56           C  
ANISOU 1375  CB  LYS A 118    12237  21775  11797   3050   -158   1947       C  
ATOM   1376  CG  LYS A 118      88.611  -8.556  27.588  1.00127.52           C  
ANISOU 1376  CG  LYS A 118    12770  23096  12585   3041   -209   1847       C  
ATOM   1377  CD  LYS A 118      89.396  -8.558  26.284  1.00133.00           C  
ANISOU 1377  CD  LYS A 118    13400  23818  13316   3096   -167   1883       C  
ATOM   1378  CE  LYS A 118      90.714  -7.820  26.368  1.00141.58           C  
ANISOU 1378  CE  LYS A 118    14105  25341  14349   3047   -208   1781       C  
ATOM   1379  NZ  LYS A 118      90.539  -6.369  26.647  1.00146.68           N  
ANISOU 1379  NZ  LYS A 118    14567  26019  15145   2674   -255   1576       N  
ATOM   1380  N   VAL A 119      84.840 -11.131  28.283  1.00119.18           N  
ANISOU 1380  N   VAL A 119    12676  20942  11665   3178    -62   2191       N  
ATOM   1381  CA  VAL A 119      83.614 -11.811  27.845  1.00117.63           C  
ANISOU 1381  CA  VAL A 119    12775  20302  11615   3133    -15   2289       C  
ATOM   1382  C   VAL A 119      82.474 -11.561  28.866  1.00120.60           C  
ANISOU 1382  C   VAL A 119    13177  20571  12073   2985     11   2269       C  
ATOM   1383  O   VAL A 119      81.449 -11.003  28.470  1.00118.65           O  
ANISOU 1383  O   VAL A 119    12966  20066  12051   2738      6   2210       O  
ATOM   1384  CB  VAL A 119      83.832 -13.333  27.610  1.00122.56           C  
ANISOU 1384  CB  VAL A 119    13665  20804  12097   3438     40   2480       C  
ATOM   1385  CG1 VAL A 119      82.515 -14.042  27.294  1.00121.45           C  
ANISOU 1385  CG1 VAL A 119    13821  20201  12122   3355     80   2570       C  
ATOM   1386  CG2 VAL A 119      84.844 -13.573  26.491  1.00122.74           C  
ANISOU 1386  CG2 VAL A 119    13693  20896  12046   3596     29   2511       C  
ATOM   1387  N   PHE A 120      82.639 -11.958  30.151  1.00118.57           N  
ANISOU 1387  N   PHE A 120    12908  20512  11631   3151     43   2324       N  
ATOM   1388  CA  PHE A 120      81.569 -11.769  31.144  1.00118.18           C  
ANISOU 1388  CA  PHE A 120    12900  20361  11642   3048     92   2328       C  
ATOM   1389  C   PHE A 120      81.396 -10.290  31.502  1.00119.55           C  
ANISOU 1389  C   PHE A 120    12855  20669  11902   2795     36   2144       C  
ATOM   1390  O   PHE A 120      80.284  -9.889  31.852  1.00117.91           O  
ANISOU 1390  O   PHE A 120    12689  20280  11833   2631     76   2129       O  
ATOM   1391  CB  PHE A 120      81.802 -12.584  32.420  1.00122.23           C  
ANISOU 1391  CB  PHE A 120    13484  21048  11910   3322    153   2438       C  
ATOM   1392  CG  PHE A 120      81.655 -14.066  32.184  1.00125.04           C  
ANISOU 1392  CG  PHE A 120    14118  21199  12194   3554    238   2634       C  
ATOM   1393  CD1 PHE A 120      80.396 -14.636  31.992  1.00128.00           C  
ANISOU 1393  CD1 PHE A 120    14723  21164  12748   3459    322   2742       C  
ATOM   1394  CD2 PHE A 120      82.764 -14.903  32.207  1.00128.98           C  
ANISOU 1394  CD2 PHE A 120    14651  21915  12438   3873    238   2714       C  
ATOM   1395  CE1 PHE A 120      80.263 -16.007  31.767  1.00130.13           C  
ANISOU 1395  CE1 PHE A 120    15274  21218  12952   3654    402   2918       C  
ATOM   1396  CE2 PHE A 120      82.629 -16.275  31.996  1.00133.01           C  
ANISOU 1396  CE2 PHE A 120    15456  22216  12863   4099    326   2897       C  
ATOM   1397  CZ  PHE A 120      81.380 -16.819  31.780  1.00130.78           C  
ANISOU 1397  CZ  PHE A 120    15422  21502  12766   3980    408   2995       C  
ATOM   1398  N   GLY A 121      82.460  -9.500  31.359  1.00115.51           N  
ANISOU 1398  N   GLY A 121    12117  20454  11317   2759    -47   2010       N  
ATOM   1399  CA  GLY A 121      82.404  -8.058  31.564  1.00114.23           C  
ANISOU 1399  CA  GLY A 121    11765  20404  11234   2505   -103   1822       C  
ATOM   1400  C   GLY A 121      81.454  -7.415  30.568  1.00114.44           C  
ANISOU 1400  C   GLY A 121    11853  20099  11530   2239    -88   1768       C  
ATOM   1401  O   GLY A 121      80.621  -6.593  30.955  1.00113.10           O  
ANISOU 1401  O   GLY A 121    11670  19842  11462   2053    -78   1690       O  
ATOM   1402  N   SER A 122      81.539  -7.831  29.278  1.00108.88           N  
ANISOU 1402  N   SER A 122    11240  19200  10930   2246    -86   1817       N  
ATOM   1403  CA  SER A 122      80.673  -7.343  28.198  1.00106.21           C  
ANISOU 1403  CA  SER A 122    10984  18536  10833   2034    -85   1773       C  
ATOM   1404  C   SER A 122      79.289  -7.990  28.246  1.00108.84           C  
ANISOU 1404  C   SER A 122    11521  18530  11303   2013    -38   1885       C  
ATOM   1405  O   SER A 122      78.318  -7.333  27.882  1.00106.92           O  
ANISOU 1405  O   SER A 122    11300  18074  11251   1812    -39   1827       O  
ATOM   1406  CB  SER A 122      81.302  -7.603  26.839  1.00108.40           C  
ANISOU 1406  CB  SER A 122    11301  18739  11147   2080   -105   1785       C  
ATOM   1407  OG  SER A 122      82.521  -6.893  26.741  1.00117.55           O  
ANISOU 1407  OG  SER A 122    12242  20202  12220   2058   -134   1679       O  
ATOM   1408  N   PHE A 123      79.198  -9.274  28.685  1.00105.95           N  
ANISOU 1408  N   PHE A 123    11301  18114  10841   2218      9   2047       N  
ATOM   1409  CA  PHE A 123      77.929 -10.001  28.819  1.00105.30           C  
ANISOU 1409  CA  PHE A 123    11404  17715  10889   2194     67   2167       C  
ATOM   1410  C   PHE A 123      77.059  -9.323  29.887  1.00108.77           C  
ANISOU 1410  C   PHE A 123    11767  18182  11377   2074    118   2137       C  
ATOM   1411  O   PHE A 123      75.841  -9.236  29.724  1.00108.06           O  
ANISOU 1411  O   PHE A 123    11742  17831  11484   1932    151   2170       O  
ATOM   1412  CB  PHE A 123      78.189 -11.482  29.162  1.00108.54           C  
ANISOU 1412  CB  PHE A 123    11995  18091  11153   2452    123   2345       C  
ATOM   1413  CG  PHE A 123      76.959 -12.363  29.202  1.00110.25           C  
ANISOU 1413  CG  PHE A 123    12416  17961  11514   2418    192   2481       C  
ATOM   1414  CD1 PHE A 123      76.440 -12.916  28.035  1.00112.52           C  
ANISOU 1414  CD1 PHE A 123    12872  17908  11971   2345    154   2520       C  
ATOM   1415  CD2 PHE A 123      76.369 -12.709  30.414  1.00113.87           C  
ANISOU 1415  CD2 PHE A 123    12909  18432  11926   2472    296   2575       C  
ATOM   1416  CE1 PHE A 123      75.315 -13.753  28.073  1.00114.11           C  
ANISOU 1416  CE1 PHE A 123    13248  17789  12321   2289    208   2641       C  
ATOM   1417  CE2 PHE A 123      75.246 -13.551  30.452  1.00117.33           C  
ANISOU 1417  CE2 PHE A 123    13522  18545  12513   2426    376   2711       C  
ATOM   1418  CZ  PHE A 123      74.727 -14.066  29.280  1.00114.79           C  
ANISOU 1418  CZ  PHE A 123    13344  17892  12381   2321    326   2739       C  
ATOM   1419  N   LEU A 124      77.701  -8.810  30.955  1.00105.68           N  
ANISOU 1419  N   LEU A 124    11235  18116  10803   2137    118   2072       N  
ATOM   1420  CA  LEU A 124      77.064  -8.056  32.034  1.00105.48           C  
ANISOU 1420  CA  LEU A 124    11141  18160  10775   2053    161   2026       C  
ATOM   1421  C   LEU A 124      76.448  -6.758  31.508  1.00108.16           C  
ANISOU 1421  C   LEU A 124    11398  18398  11302   1786    127   1882       C  
ATOM   1422  O   LEU A 124      75.271  -6.503  31.743  1.00107.99           O  
ANISOU 1422  O   LEU A 124    11417  18188  11428   1675    185   1911       O  
ATOM   1423  CB  LEU A 124      78.106  -7.742  33.130  1.00106.79           C  
ANISOU 1423  CB  LEU A 124    11184  18716  10675   2193    131   1960       C  
ATOM   1424  CG  LEU A 124      77.731  -6.706  34.196  1.00111.38           C  
ANISOU 1424  CG  LEU A 124    11689  19420  11208   2109    146   1867       C  
ATOM   1425  CD1 LEU A 124      76.646  -7.223  35.125  1.00112.37           C  
ANISOU 1425  CD1 LEU A 124    11950  19413  11332   2204    274   2015       C  
ATOM   1426  CD2 LEU A 124      78.942  -6.306  34.984  1.00114.35           C  
ANISOU 1426  CD2 LEU A 124    11923  20186  11338   2208     62   1753       C  
ATOM   1427  N   THR A 125      77.261  -5.937  30.822  1.00103.26           N  
ANISOU 1427  N   THR A 125    10658  17908  10668   1693     45   1734       N  
ATOM   1428  CA  THR A 125      76.879  -4.634  30.281  1.00101.50           C  
ANISOU 1428  CA  THR A 125    10367  17614  10585   1458     17   1582       C  
ATOM   1429  C   THR A 125      75.820  -4.821  29.157  1.00102.95           C  
ANISOU 1429  C   THR A 125    10667  17438  11013   1347     24   1624       C  
ATOM   1430  O   THR A 125      74.868  -4.040  29.099  1.00101.58           O  
ANISOU 1430  O   THR A 125    10487  17134  10975   1189     40   1563       O  
ATOM   1431  CB  THR A 125      78.150  -3.924  29.781  1.00110.55           C  
ANISOU 1431  CB  THR A 125    11376  18976  11651   1412    -54   1443       C  
ATOM   1432  OG1 THR A 125      79.098  -3.886  30.848  1.00112.47           O  
ANISOU 1432  OG1 THR A 125    11504  19561  11670   1532    -82   1414       O  
ATOM   1433  CG2 THR A 125      77.893  -2.514  29.291  1.00108.40           C  
ANISOU 1433  CG2 THR A 125    11045  18654  11488   1175    -69   1276       C  
ATOM   1434  N   LEU A 126      75.970  -5.876  28.309  1.00 98.59           N  
ANISOU 1434  N   LEU A 126    10228  16728  10502   1446      6   1729       N  
ATOM   1435  CA  LEU A 126      75.061  -6.196  27.195  1.00 96.70           C  
ANISOU 1435  CA  LEU A 126    10115  16150  10478   1362    -16   1767       C  
ATOM   1436  C   LEU A 126      73.634  -6.392  27.718  1.00 99.37           C  
ANISOU 1436  C   LEU A 126    10496  16298  10964   1288     40   1846       C  
ATOM   1437  O   LEU A 126      72.723  -5.692  27.276  1.00 98.39           O  
ANISOU 1437  O   LEU A 126    10351  16027  11007   1129     28   1783       O  
ATOM   1438  CB  LEU A 126      75.559  -7.468  26.457  1.00 97.01           C  
ANISOU 1438  CB  LEU A 126    10299  16078  10484   1521    -44   1878       C  
ATOM   1439  CG  LEU A 126      74.921  -7.871  25.116  1.00100.58           C  
ANISOU 1439  CG  LEU A 126    10904  16193  11118   1464   -104   1896       C  
ATOM   1440  CD1 LEU A 126      75.745  -8.926  24.440  1.00101.41           C  
ANISOU 1440  CD1 LEU A 126    11157  16250  11125   1650   -130   1984       C  
ATOM   1441  CD2 LEU A 126      73.497  -8.369  25.271  1.00102.69           C  
ANISOU 1441  CD2 LEU A 126    11249  16192  11579   1366    -91   1973       C  
ATOM   1442  N   ASN A 127      73.451  -7.328  28.671  1.00 95.88           N  
ANISOU 1442  N   ASN A 127    10108  15867  10453   1413    112   1990       N  
ATOM   1443  CA  ASN A 127      72.146  -7.656  29.245  1.00 95.39           C  
ANISOU 1443  CA  ASN A 127    10081  15633  10530   1359    194   2098       C  
ATOM   1444  C   ASN A 127      71.658  -6.550  30.196  1.00 98.38           C  
ANISOU 1444  C   ASN A 127    10339  16145  10894   1281    256   2033       C  
ATOM   1445  O   ASN A 127      70.448  -6.428  30.377  1.00 98.11           O  
ANISOU 1445  O   ASN A 127    10295  15952  11029   1182    312   2081       O  
ATOM   1446  CB  ASN A 127      72.204  -8.988  29.970  1.00 95.88           C  
ANISOU 1446  CB  ASN A 127    10256  15677  10498   1532    277   2273       C  
ATOM   1447  CG  ASN A 127      72.456 -10.139  29.029  1.00113.72           C  
ANISOU 1447  CG  ASN A 127    12679  17745  12785   1606    229   2354       C  
ATOM   1448  OD1 ASN A 127      71.681 -10.399  28.102  1.00104.52           O  
ANISOU 1448  OD1 ASN A 127    11586  16302  11825   1486    173   2361       O  
ATOM   1449  ND2 ASN A 127      73.520 -10.880  29.270  1.00108.27           N  
ANISOU 1449  ND2 ASN A 127    12065  17194  11879   1819    247   2420       N  
ATOM   1450  N   MET A 128      72.573  -5.731  30.775  1.00 94.45           N  
ANISOU 1450  N   MET A 128     9751  15935  10200   1321    242   1921       N  
ATOM   1451  CA  MET A 128      72.168  -4.600  31.620  1.00 93.84           C  
ANISOU 1451  CA  MET A 128     9593  15975  10088   1248    288   1840       C  
ATOM   1452  C   MET A 128      71.446  -3.564  30.773  1.00 96.93           C  
ANISOU 1452  C   MET A 128     9952  16211  10665   1054    257   1734       C  
ATOM   1453  O   MET A 128      70.356  -3.128  31.142  1.00 97.06           O  
ANISOU 1453  O   MET A 128     9958  16130  10788    988    326   1764       O  
ATOM   1454  CB  MET A 128      73.358  -3.956  32.349  1.00 96.46           C  
ANISOU 1454  CB  MET A 128     9843  16632  10175   1309    249   1718       C  
ATOM   1455  CG  MET A 128      72.938  -2.786  33.222  1.00100.01           C  
ANISOU 1455  CG  MET A 128    10250  17179  10572   1239    289   1627       C  
ATOM   1456  SD  MET A 128      74.278  -1.729  33.804  1.00104.71           S  
ANISOU 1456  SD  MET A 128    10743  18115  10925   1224    201   1426       S  
ATOM   1457  CE  MET A 128      74.836  -1.023  32.272  1.00 99.95           C  
ANISOU 1457  CE  MET A 128    10084  17443  10449   1039    111   1280       C  
ATOM   1458  N   PHE A 129      72.055  -3.177  29.630  1.00 92.12           N  
ANISOU 1458  N   PHE A 129     9334  15581  10087    980    163   1619       N  
ATOM   1459  CA  PHE A 129      71.457  -2.217  28.713  1.00 90.56           C  
ANISOU 1459  CA  PHE A 129     9132  15229  10046    821    130   1515       C  
ATOM   1460  C   PHE A 129      70.253  -2.828  28.007  1.00 93.42           C  
ANISOU 1460  C   PHE A 129     9556  15300  10638    780    123   1613       C  
ATOM   1461  O   PHE A 129      69.272  -2.117  27.813  1.00 92.80           O  
ANISOU 1461  O   PHE A 129     9457  15107  10694    678    139   1580       O  
ATOM   1462  CB  PHE A 129      72.460  -1.686  27.684  1.00 91.55           C  
ANISOU 1462  CB  PHE A 129     9249  15398  10137    773     52   1381       C  
ATOM   1463  CG  PHE A 129      73.387  -0.634  28.240  1.00 93.15           C  
ANISOU 1463  CG  PHE A 129     9366  15852  10175    728     53   1237       C  
ATOM   1464  CD1 PHE A 129      72.921   0.643  28.526  1.00 95.83           C  
ANISOU 1464  CD1 PHE A 129     9691  16194  10527    602     84   1121       C  
ATOM   1465  CD2 PHE A 129      74.744  -0.882  28.373  1.00 95.91           C  
ANISOU 1465  CD2 PHE A 129     9651  16428  10363    803     15   1208       C  
ATOM   1466  CE1 PHE A 129      73.779   1.623  29.027  1.00 97.22           C  
ANISOU 1466  CE1 PHE A 129     9804  16581  10554    537     76    976       C  
ATOM   1467  CE2 PHE A 129      75.607   0.106  28.853  1.00 99.45           C  
ANISOU 1467  CE2 PHE A 129    10001  17108  10677    732      0   1062       C  
ATOM   1468  CZ  PHE A 129      75.118   1.349  29.186  1.00 97.32           C  
ANISOU 1468  CZ  PHE A 129     9733  16821  10422    590     27    943       C  
ATOM   1469  N   ALA A 130      70.283  -4.138  27.684  1.00 89.94           N  
ANISOU 1469  N   ALA A 130     9192  14742  10239    860     99   1736       N  
ATOM   1470  CA  ALA A 130      69.129  -4.792  27.057  1.00 90.09           C  
ANISOU 1470  CA  ALA A 130     9268  14478  10484    802     76   1825       C  
ATOM   1471  C   ALA A 130      67.911  -4.729  27.991  1.00 96.27           C  
ANISOU 1471  C   ALA A 130     9987  15219  11371    759    181   1920       C  
ATOM   1472  O   ALA A 130      66.796  -4.512  27.522  1.00 95.67           O  
ANISOU 1472  O   ALA A 130     9884  14963  11502    654    163   1932       O  
ATOM   1473  CB  ALA A 130      69.460  -6.225  26.697  1.00 91.46           C  
ANISOU 1473  CB  ALA A 130     9562  14537  10651    901     42   1940       C  
ATOM   1474  N   SER A 131      68.145  -4.813  29.320  1.00 94.79           N  
ANISOU 1474  N   SER A 131     9768  15218  11032    849    291   1978       N  
ATOM   1475  CA  SER A 131      67.095  -4.686  30.332  1.00 95.81           C  
ANISOU 1475  CA  SER A 131     9841  15335  11228    837    419   2075       C  
ATOM   1476  C   SER A 131      66.528  -3.261  30.348  1.00 98.83           C  
ANISOU 1476  C   SER A 131    10146  15756  11650    740    431   1959       C  
ATOM   1477  O   SER A 131      65.325  -3.082  30.174  1.00 98.43           O  
ANISOU 1477  O   SER A 131    10045  15559  11795    658    458   2002       O  
ATOM   1478  CB  SER A 131      67.631  -5.057  31.713  1.00101.11           C  
ANISOU 1478  CB  SER A 131    10532  16199  11688    992    531   2159       C  
ATOM   1479  OG  SER A 131      66.648  -4.893  32.722  1.00111.75           O  
ANISOU 1479  OG  SER A 131    11840  17537  13083   1003    677   2262       O  
ATOM   1480  N   ILE A 132      67.414  -2.252  30.499  1.00 94.13           N  
ANISOU 1480  N   ILE A 132     9542  15351  10871    747    403   1808       N  
ATOM   1481  CA  ILE A 132      67.070  -0.827  30.576  1.00 92.90           C  
ANISOU 1481  CA  ILE A 132     9354  15242  10702    669    421   1682       C  
ATOM   1482  C   ILE A 132      66.374  -0.362  29.263  1.00 94.57           C  
ANISOU 1482  C   ILE A 132     9563  15254  11114    552    345   1614       C  
ATOM   1483  O   ILE A 132      65.403   0.395  29.342  1.00 94.17           O  
ANISOU 1483  O   ILE A 132     9482  15154  11146    505    393   1598       O  
ATOM   1484  CB  ILE A 132      68.352   0.018  30.871  1.00 95.71           C  
ANISOU 1484  CB  ILE A 132     9719  15823  10825    678    382   1520       C  
ATOM   1485  CG1 ILE A 132      68.990  -0.413  32.227  1.00 97.48           C  
ANISOU 1485  CG1 ILE A 132     9942  16260  10834    815    437   1577       C  
ATOM   1486  CG2 ILE A 132      68.039   1.516  30.885  1.00 95.79           C  
ANISOU 1486  CG2 ILE A 132     9734  15852  10811    588    404   1381       C  
ATOM   1487  CD1 ILE A 132      70.341   0.221  32.577  1.00104.59           C  
ANISOU 1487  CD1 ILE A 132    10827  17409  11505    825    374   1423       C  
ATOM   1488  N   PHE A 133      66.844  -0.819  28.083  1.00 89.47           N  
ANISOU 1488  N   PHE A 133     8963  14499  10535    527    230   1581       N  
ATOM   1489  CA  PHE A 133      66.247  -0.387  26.821  1.00 87.73           C  
ANISOU 1489  CA  PHE A 133     8763  14091  10479    443    146   1510       C  
ATOM   1490  C   PHE A 133      64.883  -1.034  26.613  1.00 92.99           C  
ANISOU 1490  C   PHE A 133     9386  14567  11380    407    144   1631       C  
ATOM   1491  O   PHE A 133      64.007  -0.372  26.058  1.00 92.98           O  
ANISOU 1491  O   PHE A 133     9354  14472  11502    350    123   1583       O  
ATOM   1492  CB  PHE A 133      67.143  -0.673  25.609  1.00 88.16           C  
ANISOU 1492  CB  PHE A 133     8900  14076  10520    448     29   1441       C  
ATOM   1493  CG  PHE A 133      68.521  -0.050  25.624  1.00 88.67           C  
ANISOU 1493  CG  PHE A 133     8980  14321  10388    463     26   1319       C  
ATOM   1494  CD1 PHE A 133      68.717   1.233  26.121  1.00 91.59           C  
ANISOU 1494  CD1 PHE A 133     9324  14821  10656    409     81   1199       C  
ATOM   1495  CD2 PHE A 133      69.584  -0.667  24.975  1.00 89.96           C  
ANISOU 1495  CD2 PHE A 133     9193  14502  10484    521    -37   1315       C  
ATOM   1496  CE1 PHE A 133      69.986   1.821  26.103  1.00 92.18           C  
ANISOU 1496  CE1 PHE A 133     9397  15055  10571    391     73   1080       C  
ATOM   1497  CE2 PHE A 133      70.846  -0.066  24.927  1.00 92.36           C  
ANISOU 1497  CE2 PHE A 133     9480  14982  10630    521    -36   1206       C  
ATOM   1498  CZ  PHE A 133      71.040   1.172  25.491  1.00 90.52           C  
ANISOU 1498  CZ  PHE A 133     9200  14884  10310    443     15   1086       C  
ATOM   1499  N   PHE A 134      64.670  -2.291  27.075  1.00 90.92           N  
ANISOU 1499  N   PHE A 134     9116  14249  11179    441    172   1787       N  
ATOM   1500  CA  PHE A 134      63.347  -2.912  26.936  1.00 92.07           C  
ANISOU 1500  CA  PHE A 134     9198  14215  11568    379    177   1906       C  
ATOM   1501  C   PHE A 134      62.361  -2.311  27.982  1.00 97.79           C  
ANISOU 1501  C   PHE A 134     9806  15024  12328    377    329   1976       C  
ATOM   1502  O   PHE A 134      61.161  -2.263  27.704  1.00 98.04           O  
ANISOU 1502  O   PHE A 134     9742  14940  12569    310    330   2029       O  
ATOM   1503  CB  PHE A 134      63.385  -4.446  27.030  1.00 94.83           C  
ANISOU 1503  CB  PHE A 134     9598  14448  11987    397    173   2053       C  
ATOM   1504  CG  PHE A 134      63.868  -5.108  25.755  1.00 95.86           C  
ANISOU 1504  CG  PHE A 134     9851  14419  12153    388     11   2004       C  
ATOM   1505  CD1 PHE A 134      63.074  -5.112  24.609  1.00 98.74           C  
ANISOU 1505  CD1 PHE A 134    10219  14578  12721    296   -126   1958       C  
ATOM   1506  CD2 PHE A 134      65.053  -5.836  25.735  1.00 97.66           C  
ANISOU 1506  CD2 PHE A 134    10198  14697  12210    490     -4   2019       C  
ATOM   1507  CE1 PHE A 134      63.513  -5.732  23.434  1.00 99.23           C  
ANISOU 1507  CE1 PHE A 134    10426  14480  12797    308   -278   1913       C  
ATOM   1508  CE2 PHE A 134      65.484  -6.472  24.566  1.00100.11           C  
ANISOU 1508  CE2 PHE A 134    10644  14853  12539    506   -141   1986       C  
ATOM   1509  CZ  PHE A 134      64.710  -6.417  23.422  1.00 98.06           C  
ANISOU 1509  CZ  PHE A 134    10409  14377  12471    414   -278   1932       C  
ATOM   1510  N   ILE A 135      62.873  -1.784  29.127  1.00 95.18           N  
ANISOU 1510  N   ILE A 135     9483  14897  11787    458    445   1965       N  
ATOM   1511  CA  ILE A 135      62.074  -1.044  30.128  1.00 95.89           C  
ANISOU 1511  CA  ILE A 135     9499  15075  11859    487    594   2014       C  
ATOM   1512  C   ILE A 135      61.557   0.239  29.459  1.00 98.24           C  
ANISOU 1512  C   ILE A 135     9775  15348  12205    432    551   1883       C  
ATOM   1513  O   ILE A 135      60.388   0.598  29.617  1.00 99.35           O  
ANISOU 1513  O   ILE A 135     9824  15450  12475    421    623   1946       O  
ATOM   1514  CB  ILE A 135      62.901  -0.745  31.430  1.00 99.60           C  
ANISOU 1514  CB  ILE A 135    10023  15764  12055    601    699   2008       C  
ATOM   1515  CG1 ILE A 135      63.204  -2.043  32.213  1.00101.27           C  
ANISOU 1515  CG1 ILE A 135    10263  15997  12219    691    768   2164       C  
ATOM   1516  CG2 ILE A 135      62.180   0.274  32.344  1.00100.69           C  
ANISOU 1516  CG2 ILE A 135    10130  15991  12138    647    840   2024       C  
ATOM   1517  CD1 ILE A 135      64.178  -1.889  33.392  1.00108.29           C  
ANISOU 1517  CD1 ILE A 135    11218  17112  12816    828    833   2145       C  
ATOM   1518  N   THR A 136      62.438   0.897  28.680  1.00 92.30           N  
ANISOU 1518  N   THR A 136     9107  14614  11347    405    444   1709       N  
ATOM   1519  CA  THR A 136      62.161   2.123  27.936  1.00 90.87           C  
ANISOU 1519  CA  THR A 136     8954  14397  11177    366    403   1568       C  
ATOM   1520  C   THR A 136      61.106   1.837  26.850  1.00 96.12           C  
ANISOU 1520  C   THR A 136     9560  14868  12094    313    307   1595       C  
ATOM   1521  O   THR A 136      60.188   2.643  26.688  1.00 96.38           O  
ANISOU 1521  O   THR A 136     9551  14874  12196    312    332   1570       O  
ATOM   1522  CB  THR A 136      63.465   2.676  27.344  1.00 89.35           C  
ANISOU 1522  CB  THR A 136     8873  14258  10820    346    325   1397       C  
ATOM   1523  OG1 THR A 136      64.411   2.866  28.398  1.00 87.25           O  
ANISOU 1523  OG1 THR A 136     8633  14185  10334    385    395   1370       O  
ATOM   1524  CG2 THR A 136      63.264   3.976  26.604  1.00 85.00           C  
ANISOU 1524  CG2 THR A 136     8384  13652  10261    311    302   1250       C  
ATOM   1525  N   CYS A 137      61.212   0.680  26.141  1.00 92.80           N  
ANISOU 1525  N   CYS A 137     9143  14316  11801    278    195   1647       N  
ATOM   1526  CA  CYS A 137      60.241   0.274  25.115  1.00 92.78           C  
ANISOU 1526  CA  CYS A 137     9090  14123  12040    220     74   1666       C  
ATOM   1527  C   CYS A 137      58.856   0.130  25.733  1.00 97.94           C  
ANISOU 1527  C   CYS A 137     9572  14764  12877    197    162   1805       C  
ATOM   1528  O   CYS A 137      57.892   0.629  25.155  1.00 97.99           O  
ANISOU 1528  O   CYS A 137     9502  14705  13026    174    108   1777       O  
ATOM   1529  CB  CYS A 137      60.665  -1.019  24.426  1.00 93.19           C  
ANISOU 1529  CB  CYS A 137     9206  14035  12166    192    -51   1704       C  
ATOM   1530  SG  CYS A 137      62.083  -0.838  23.314  1.00 95.47           S  
ANISOU 1530  SG  CYS A 137     9684  14302  12288    231   -174   1546       S  
ATOM   1531  N   MET A 138      58.762  -0.524  26.913  1.00 95.69           N  
ANISOU 1531  N   MET A 138     9226  14549  12581    216    306   1959       N  
ATOM   1532  CA  MET A 138      57.503  -0.738  27.642  1.00 97.23           C  
ANISOU 1532  CA  MET A 138     9251  14743  12947    202    432   2121       C  
ATOM   1533  C   MET A 138      56.783   0.582  27.961  1.00101.46           C  
ANISOU 1533  C   MET A 138     9719  15381  13448    257    527   2088       C  
ATOM   1534  O   MET A 138      55.561   0.642  27.823  1.00102.66           O  
ANISOU 1534  O   MET A 138     9713  15488  13803    228    540   2159       O  
ATOM   1535  CB  MET A 138      57.732  -1.505  28.959  1.00100.50           C  
ANISOU 1535  CB  MET A 138     9662  15233  13292    251    605   2284       C  
ATOM   1536  CG  MET A 138      58.031  -2.990  28.780  1.00104.53           C  
ANISOU 1536  CG  MET A 138    10216  15613  13887    201    553   2376       C  
ATOM   1537  SD  MET A 138      56.729  -3.915  27.906  1.00109.98           S  
ANISOU 1537  SD  MET A 138    10767  16064  14957     40    443   2466       S  
ATOM   1538  CE  MET A 138      55.269  -3.521  28.923  1.00108.63           C  
ANISOU 1538  CE  MET A 138    10359  15966  14949     37    659   2638       C  
ATOM   1539  N   SER A 139      57.524   1.622  28.394  1.00 96.80           N  
ANISOU 1539  N   SER A 139     9248  14927  12603    337    593   1982       N  
ATOM   1540  CA  SER A 139      56.936   2.919  28.732  1.00 96.89           C  
ANISOU 1540  CA  SER A 139     9247  15026  12541    407    694   1944       C  
ATOM   1541  C   SER A 139      56.418   3.632  27.467  1.00100.11           C  
ANISOU 1541  C   SER A 139     9650  15342  13044    384    565   1823       C  
ATOM   1542  O   SER A 139      55.348   4.241  27.513  1.00100.66           O  
ANISOU 1542  O   SER A 139     9624  15431  13191    430    627   1861       O  
ATOM   1543  CB  SER A 139      57.946   3.797  29.465  1.00 99.65           C  
ANISOU 1543  CB  SER A 139     9757  15517  12587    476    772   1841       C  
ATOM   1544  OG  SER A 139      58.309   3.212  30.707  1.00108.12           O  
ANISOU 1544  OG  SER A 139    10836  16689  13554    530    893   1954       O  
ATOM   1545  N   VAL A 140      57.153   3.516  26.340  1.00 95.25           N  
ANISOU 1545  N   VAL A 140     9139  14630  12420    332    392   1689       N  
ATOM   1546  CA  VAL A 140      56.780   4.097  25.044  1.00 94.43           C  
ANISOU 1546  CA  VAL A 140     9067  14423  12388    330    256   1567       C  
ATOM   1547  C   VAL A 140      55.544   3.344  24.496  1.00100.14           C  
ANISOU 1547  C   VAL A 140     9606  15036  13406    279    155   1663       C  
ATOM   1548  O   VAL A 140      54.649   3.980  23.934  1.00 99.98           O  
ANISOU 1548  O   VAL A 140     9518  14994  13475    316    113   1630       O  
ATOM   1549  CB  VAL A 140      57.973   4.071  24.043  1.00 96.57           C  
ANISOU 1549  CB  VAL A 140     9519  14619  12552    305    120   1411       C  
ATOM   1550  CG1 VAL A 140      57.546   4.502  22.639  1.00 95.99           C  
ANISOU 1550  CG1 VAL A 140     9495  14414  12564    320    -29   1299       C  
ATOM   1551  CG2 VAL A 140      59.134   4.936  24.541  1.00 95.32           C  
ANISOU 1551  CG2 VAL A 140     9511  14580  12126    332    216   1305       C  
ATOM   1552  N   ASP A 141      55.486   2.004  24.704  1.00 98.47           N  
ANISOU 1552  N   ASP A 141     9314  14760  13341    197    121   1783       N  
ATOM   1553  CA  ASP A 141      54.379   1.144  24.260  1.00100.41           C  
ANISOU 1553  CA  ASP A 141     9381  14890  13882    111     21   1878       C  
ATOM   1554  C   ASP A 141      53.102   1.441  25.072  1.00107.20           C  
ANISOU 1554  C   ASP A 141    10013  15842  14876    131    173   2021       C  
ATOM   1555  O   ASP A 141      52.035   1.623  24.477  1.00107.61           O  
ANISOU 1555  O   ASP A 141     9908  15857  15122    111     85   2025       O  
ATOM   1556  CB  ASP A 141      54.752  -0.348  24.378  1.00102.69           C  
ANISOU 1556  CB  ASP A 141     9678  15073  14267     15    -22   1974       C  
ATOM   1557  CG  ASP A 141      53.700  -1.289  23.815  1.00114.51           C  
ANISOU 1557  CG  ASP A 141    11009  16424  16077   -106   -145   2056       C  
ATOM   1558  OD1 ASP A 141      53.588  -1.377  22.573  1.00113.96           O  
ANISOU 1558  OD1 ASP A 141    10982  16221  16097   -143   -366   1945       O  
ATOM   1559  OD2 ASP A 141      53.021  -1.971  24.616  1.00123.75           O  
ANISOU 1559  OD2 ASP A 141    12013  17605  17402   -167    -19   2230       O  
ATOM   1560  N   ARG A 142      53.218   1.499  26.423  1.00105.17           N  
ANISOU 1560  N   ARG A 142     9737  15713  14509    186    399   2139       N  
ATOM   1561  CA  ARG A 142      52.090   1.819  27.304  1.00107.15           C  
ANISOU 1561  CA  ARG A 142     9793  16064  14856    236    583   2292       C  
ATOM   1562  C   ARG A 142      51.560   3.225  27.023  1.00111.89           C  
ANISOU 1562  C   ARG A 142    10389  16743  15381    349    597   2202       C  
ATOM   1563  O   ARG A 142      50.346   3.417  27.063  1.00113.60           O  
ANISOU 1563  O   ARG A 142    10395  16992  15776    369    634   2292       O  
ATOM   1564  CB  ARG A 142      52.455   1.692  28.792  1.00107.29           C  
ANISOU 1564  CB  ARG A 142     9850  16197  14719    309    824   2422       C  
ATOM   1565  CG  ARG A 142      52.537   0.263  29.309  1.00115.85           C  
ANISOU 1565  CG  ARG A 142    10884  17212  15921    224    875   2580       C  
ATOM   1566  CD  ARG A 142      52.774   0.265  30.803  1.00123.19           C  
ANISOU 1566  CD  ARG A 142    11852  18266  16688    336   1129   2715       C  
ATOM   1567  NE  ARG A 142      52.624  -1.066  31.389  1.00132.39           N  
ANISOU 1567  NE  ARG A 142    12965  19359  17977    276   1219   2895       N  
ATOM   1568  CZ  ARG A 142      52.741  -1.328  32.688  1.00148.31           C  
ANISOU 1568  CZ  ARG A 142    15011  21455  19884    376   1447   3046       C  
ATOM   1569  NH1 ARG A 142      53.020  -0.355  33.548  1.00137.06           N  
ANISOU 1569  NH1 ARG A 142    13668  20186  18221    538   1593   3033       N  
ATOM   1570  NH2 ARG A 142      52.584  -2.566  33.136  1.00135.72           N  
ANISOU 1570  NH2 ARG A 142    13389  19772  18407    322   1532   3210       N  
ATOM   1571  N   TYR A 143      52.457   4.196  26.714  1.00106.80           N  
ANISOU 1571  N   TYR A 143     9975  16127  14479    422    571   2027       N  
ATOM   1572  CA  TYR A 143      52.063   5.568  26.389  1.00106.69           C  
ANISOU 1572  CA  TYR A 143    10019  16162  14357    539    591   1925       C  
ATOM   1573  C   TYR A 143      51.279   5.595  25.076  1.00111.73           C  
ANISOU 1573  C   TYR A 143    10556  16707  15188    521    396   1861       C  
ATOM   1574  O   TYR A 143      50.214   6.206  25.027  1.00112.86           O  
ANISOU 1574  O   TYR A 143    10568  16910  15403    609    437   1900       O  
ATOM   1575  CB  TYR A 143      53.282   6.510  26.311  1.00106.14           C  
ANISOU 1575  CB  TYR A 143    10235  16109  13986    584    597   1745       C  
ATOM   1576  CG  TYR A 143      52.955   7.880  25.751  1.00108.18           C  
ANISOU 1576  CG  TYR A 143    10603  16370  14129    694    599   1618       C  
ATOM   1577  CD1 TYR A 143      52.274   8.824  26.515  1.00111.26           C  
ANISOU 1577  CD1 TYR A 143    11003  16866  14406    827    781   1666       C  
ATOM   1578  CD2 TYR A 143      53.368   8.249  24.474  1.00108.15           C  
ANISOU 1578  CD2 TYR A 143    10730  16255  14106    683    432   1452       C  
ATOM   1579  CE1 TYR A 143      51.947  10.075  25.994  1.00112.52           C  
ANISOU 1579  CE1 TYR A 143    11292  17017  14446    943    793   1554       C  
ATOM   1580  CE2 TYR A 143      53.065   9.505  23.950  1.00109.09           C  
ANISOU 1580  CE2 TYR A 143    10977  16363  14107    799    448   1340       C  
ATOM   1581  CZ  TYR A 143      52.359  10.418  24.717  1.00118.34           C  
ANISOU 1581  CZ  TYR A 143    12155  17638  15170    927    629   1390       C  
ATOM   1582  OH  TYR A 143      52.055  11.659  24.213  1.00119.84           O  
ANISOU 1582  OH  TYR A 143    12499  17807  15226   1057    657   1283       O  
ATOM   1583  N   GLN A 144      51.781   4.897  24.039  1.00107.72           N  
ANISOU 1583  N   GLN A 144    10110  16060  14758    423    183   1769       N  
ATOM   1584  CA  GLN A 144      51.162   4.816  22.712  1.00107.97           C  
ANISOU 1584  CA  GLN A 144    10085  15983  14954    408    -41   1686       C  
ATOM   1585  C   GLN A 144      49.792   4.084  22.798  1.00115.58           C  
ANISOU 1585  C   GLN A 144    10726  16951  16237    338    -81   1837       C  
ATOM   1586  O   GLN A 144      48.923   4.316  21.955  1.00115.98           O  
ANISOU 1586  O   GLN A 144    10666  16974  16428    363   -233   1789       O  
ATOM   1587  CB  GLN A 144      52.123   4.099  21.748  1.00107.57           C  
ANISOU 1587  CB  GLN A 144    10205  15777  14891    327   -237   1572       C  
ATOM   1588  CG  GLN A 144      51.753   4.181  20.268  1.00110.54           C  
ANISOU 1588  CG  GLN A 144    10618  16028  15357    350   -480   1442       C  
ATOM   1589  CD  GLN A 144      52.816   3.597  19.356  1.00123.05           C  
ANISOU 1589  CD  GLN A 144    12416  17458  16879    307   -644   1331       C  
ATOM   1590  OE1 GLN A 144      52.813   3.839  18.151  1.00117.18           O  
ANISOU 1590  OE1 GLN A 144    11796  16611  16117    367   -811   1198       O  
ATOM   1591  NE2 GLN A 144      53.798   2.888  19.906  1.00115.15           N  
ANISOU 1591  NE2 GLN A 144    11488  16446  15819    231   -586   1383       N  
ATOM   1592  N   SER A 145      49.596   3.244  23.840  1.00114.50           N  
ANISOU 1592  N   SER A 145    10439  16856  16211    257     63   2019       N  
ATOM   1593  CA  SER A 145      48.343   2.525  24.098  1.00117.51           C  
ANISOU 1593  CA  SER A 145    10498  17246  16903    169     74   2187       C  
ATOM   1594  C   SER A 145      47.312   3.430  24.783  1.00123.42           C  
ANISOU 1594  C   SER A 145    11065  18168  17662    303    260   2289       C  
ATOM   1595  O   SER A 145      46.112   3.223  24.612  1.00125.33           O  
ANISOU 1595  O   SER A 145    11022  18442  18157    272    219   2376       O  
ATOM   1596  CB  SER A 145      48.599   1.293  24.963  1.00122.42           C  
ANISOU 1596  CB  SER A 145    11066  17826  17623     41    183   2350       C  
ATOM   1597  OG  SER A 145      49.487   0.389  24.326  1.00131.77           O  
ANISOU 1597  OG  SER A 145    12417  18848  18801    -68     15   2270       O  
ATOM   1598  N   VAL A 146      47.783   4.418  25.568  1.00119.25           N  
ANISOU 1598  N   VAL A 146    10702  17752  16856    454    464   2281       N  
ATOM   1599  CA  VAL A 146      46.929   5.357  26.295  1.00120.56           C  
ANISOU 1599  CA  VAL A 146    10762  18078  16969    618    670   2378       C  
ATOM   1600  C   VAL A 146      46.477   6.492  25.342  1.00125.55           C  
ANISOU 1600  C   VAL A 146    11429  18733  17540    754    556   2236       C  
ATOM   1601  O   VAL A 146      45.272   6.674  25.167  1.00127.14           O  
ANISOU 1601  O   VAL A 146    11375  19010  17921    807    547   2315       O  
ATOM   1602  CB  VAL A 146      47.639   5.920  27.560  1.00123.28           C  
ANISOU 1602  CB  VAL A 146    11313  18511  17016    730    918   2411       C  
ATOM   1603  CG1 VAL A 146      46.851   7.069  28.182  1.00124.19           C  
ANISOU 1603  CG1 VAL A 146    11401  18772  17015    936   1118   2476       C  
ATOM   1604  CG2 VAL A 146      47.886   4.820  28.590  1.00123.62           C  
ANISOU 1604  CG2 VAL A 146    11296  18552  17122    641   1055   2580       C  
ATOM   1605  N   ILE A 147      47.432   7.242  24.737  1.00121.05           N  
ANISOU 1605  N   ILE A 147    11171  18104  16718    816    480   2036       N  
ATOM   1606  CA  ILE A 147      47.147   8.384  23.855  1.00121.21           C  
ANISOU 1606  CA  ILE A 147    11300  18128  16627    968    400   1892       C  
ATOM   1607  C   ILE A 147      46.385   7.880  22.572  1.00126.98           C  
ANISOU 1607  C   ILE A 147    11846  18785  17614    915    127   1842       C  
ATOM   1608  O   ILE A 147      45.439   8.553  22.150  1.00127.96           O  
ANISOU 1608  O   ILE A 147    11856  18983  17780   1053     96   1835       O  
ATOM   1609  CB  ILE A 147      48.450   9.189  23.497  1.00122.17           C  
ANISOU 1609  CB  ILE A 147    11809  18172  16437   1009    391   1694       C  
ATOM   1610  CG1 ILE A 147      48.161  10.479  22.679  1.00122.93           C  
ANISOU 1610  CG1 ILE A 147    12066  18260  16382   1190    359   1554       C  
ATOM   1611  CG2 ILE A 147      49.534   8.347  22.826  1.00121.45           C  
ANISOU 1611  CG2 ILE A 147    11842  17936  16366    851    213   1591       C  
ATOM   1612  CD1 ILE A 147      47.376  11.600  23.413  1.00135.23           C  
ANISOU 1612  CD1 ILE A 147    13632  19951  17796   1393    577   1620       C  
ATOM   1613  N   TYR A 148      46.744   6.697  22.012  1.00123.80           N  
ANISOU 1613  N   TYR A 148    11415  18248  17377    730    -69   1813       N  
ATOM   1614  CA  TYR A 148      46.043   6.127  20.847  1.00125.13           C  
ANISOU 1614  CA  TYR A 148    11425  18333  17788    665   -349   1759       C  
ATOM   1615  C   TYR A 148      45.428   4.760  21.234  1.00132.85           C  
ANISOU 1615  C   TYR A 148    12096  19289  19093    459   -386   1924       C  
ATOM   1616  O   TYR A 148      46.130   3.742  21.191  1.00131.84           O  
ANISOU 1616  O   TYR A 148    12049  19027  19017    299   -463   1920       O  
ATOM   1617  CB  TYR A 148      46.971   5.993  19.618  1.00124.13           C  
ANISOU 1617  CB  TYR A 148    11578  18027  17559    642   -577   1559       C  
ATOM   1618  CG  TYR A 148      47.629   7.289  19.192  1.00123.85           C  
ANISOU 1618  CG  TYR A 148    11860  17986  17212    820   -524   1400       C  
ATOM   1619  CD1 TYR A 148      46.951   8.211  18.400  1.00126.64           C  
ANISOU 1619  CD1 TYR A 148    12234  18371  17512   1003   -591   1312       C  
ATOM   1620  CD2 TYR A 148      48.957   7.556  19.508  1.00122.27           C  
ANISOU 1620  CD2 TYR A 148    11945  17737  16774    801   -421   1331       C  
ATOM   1621  CE1 TYR A 148      47.554   9.406  18.001  1.00126.09           C  
ANISOU 1621  CE1 TYR A 148    12482  18273  17154   1163   -522   1172       C  
ATOM   1622  CE2 TYR A 148      49.568   8.749  19.123  1.00121.66           C  
ANISOU 1622  CE2 TYR A 148    12157  17641  16427    938   -360   1188       C  
ATOM   1623  CZ  TYR A 148      48.861   9.674  18.373  1.00129.37           C  
ANISOU 1623  CZ  TYR A 148    13173  18632  17351   1117   -402   1110       C  
ATOM   1624  OH  TYR A 148      49.471  10.838  17.967  1.00128.25           O  
ANISOU 1624  OH  TYR A 148    13341  18446  16942   1248   -327    972       O  
ATOM   1625  N   PRO A 149      44.130   4.717  21.652  1.00133.56           N  
ANISOU 1625  N   PRO A 149    11835  19508  19403    465   -313   2078       N  
ATOM   1626  CA  PRO A 149      43.537   3.432  22.089  1.00136.12           C  
ANISOU 1626  CA  PRO A 149    11866  19805  20050    251   -312   2249       C  
ATOM   1627  C   PRO A 149      43.420   2.394  20.955  1.00142.16           C  
ANISOU 1627  C   PRO A 149    12566  20396  21052     64   -643   2160       C  
ATOM   1628  O   PRO A 149      43.430   1.194  21.243  1.00142.82           O  
ANISOU 1628  O   PRO A 149    12540  20381  21343   -146   -657   2261       O  
ATOM   1629  CB  PRO A 149      42.141   3.833  22.590  1.00140.62           C  
ANISOU 1629  CB  PRO A 149    12071  20567  20791    329   -173   2412       C  
ATOM   1630  CG  PRO A 149      42.220   5.309  22.839  1.00143.69           C  
ANISOU 1630  CG  PRO A 149    12628  21092  20876    602    -10   2365       C  
ATOM   1631  CD  PRO A 149      43.166   5.826  21.802  1.00136.59           C  
ANISOU 1631  CD  PRO A 149    12080  20072  19745    671   -199   2120       C  
ATOM   1632  N   PHE A 150      43.302   2.848  19.689  1.00139.13           N  
ANISOU 1632  N   PHE A 150    12271  19963  20628    148   -903   1972       N  
ATOM   1633  CA  PHE A 150      43.202   1.982  18.506  1.00178.48           C  
ANISOU 1633  CA  PHE A 150    17242  24774  25797      8  -1247   1857       C  
ATOM   1634  C   PHE A 150      44.539   1.272  18.201  1.00206.53           C  
ANISOU 1634  C   PHE A 150    21126  28118  29230    -93  -1326   1773       C  
ATOM   1635  O   PHE A 150      45.607   1.800  18.507  1.00163.79           O  
ANISOU 1635  O   PHE A 150    16007  22700  23525     14  -1195   1716       O  
ATOM   1636  CB  PHE A 150      42.762   2.796  17.280  1.00180.60           C  
ANISOU 1636  CB  PHE A 150    17557  25060  26001    183  -1481   1677       C  
ATOM   1637  CG  PHE A 150      43.619   3.985  16.901  1.00179.47           C  
ANISOU 1637  CG  PHE A 150    17783  24919  25489    416  -1417   1529       C  
ATOM   1638  CD1 PHE A 150      44.677   3.846  16.009  1.00180.56           C  
ANISOU 1638  CD1 PHE A 150    18271  24873  25462    428  -1574   1360       C  
ATOM   1639  CD2 PHE A 150      43.317   5.258  17.372  1.00181.37           C  
ANISOU 1639  CD2 PHE A 150    18024  25335  25552    629  -1201   1559       C  
ATOM   1640  CE1 PHE A 150      45.449   4.950  15.636  1.00179.24           C  
ANISOU 1640  CE1 PHE A 150    18432  24697  24973    628  -1501   1230       C  
ATOM   1641  CE2 PHE A 150      44.088   6.363  16.995  1.00181.93           C  
ANISOU 1641  CE2 PHE A 150    18449  25386  25292    825  -1138   1419       C  
ATOM   1642  CZ  PHE A 150      45.144   6.202  16.125  1.00178.09           C  
ANISOU 1642  CZ  PHE A 150    18288  24715  24662    814  -1286   1256       C  
ATOM   1643  N   PRO A 157      51.731  -4.733  14.662  1.00128.89           N  
ANISOU 1643  N   PRO A 157    13291  16901  18780   -450  -2107   1343       N  
ATOM   1644  CA  PRO A 157      52.079  -6.106  14.273  1.00129.81           C  
ANISOU 1644  CA  PRO A 157    13575  16783  18962   -557  -2248   1363       C  
ATOM   1645  C   PRO A 157      53.495  -6.199  13.692  1.00132.22           C  
ANISOU 1645  C   PRO A 157    14252  16992  18994   -408  -2280   1275       C  
ATOM   1646  O   PRO A 157      54.247  -7.114  14.047  1.00131.58           O  
ANISOU 1646  O   PRO A 157    14330  16808  18858   -443  -2237   1346       O  
ATOM   1647  CB  PRO A 157      51.022  -6.457  13.214  1.00133.97           C  
ANISOU 1647  CB  PRO A 157    14015  17157  19729   -652  -2565   1277       C  
ATOM   1648  CG  PRO A 157      50.412  -5.144  12.804  1.00137.93           C  
ANISOU 1648  CG  PRO A 157    14395  17806  20206   -520  -2617   1170       C  
ATOM   1649  CD  PRO A 157      50.486  -4.283  14.015  1.00132.10           C  
ANISOU 1649  CD  PRO A 157    13502  17320  19372   -462  -2296   1271       C  
ATOM   1650  N   TRP A 158      53.855  -5.244  12.804  1.00127.44           N  
ANISOU 1650  N   TRP A 158    13788  16420  18214   -231  -2342   1129       N  
ATOM   1651  CA  TRP A 158      55.146  -5.192  12.116  1.00125.26           C  
ANISOU 1651  CA  TRP A 158    13849  16061  17684    -73  -2366   1041       C  
ATOM   1652  C   TRP A 158      56.260  -4.721  13.068  1.00124.72           C  
ANISOU 1652  C   TRP A 158    13821  16175  17391      0  -2078   1102       C  
ATOM   1653  O   TRP A 158      57.290  -5.387  13.173  1.00124.05           O  
ANISOU 1653  O   TRP A 158    13927  16038  17167     41  -2031   1135       O  
ATOM   1654  CB  TRP A 158      55.053  -4.242  10.897  1.00123.91           C  
ANISOU 1654  CB  TRP A 158    13804  15849  17425     89  -2525    869       C  
ATOM   1655  CG  TRP A 158      55.884  -4.649   9.710  1.00124.74           C  
ANISOU 1655  CG  TRP A 158    14261  15748  17386    217  -2692    769       C  
ATOM   1656  CD1 TRP A 158      55.431  -5.239   8.566  1.00129.37           C  
ANISOU 1656  CD1 TRP A 158    14984  16109  18061    225  -2992    680       C  
ATOM   1657  CD2 TRP A 158      57.315  -4.572   9.583  1.00122.73           C  
ANISOU 1657  CD2 TRP A 158    14267  15491  16875    356  -2567    760       C  
ATOM   1658  NE1 TRP A 158      56.482  -5.489   7.713  1.00128.07           N  
ANISOU 1658  NE1 TRP A 158    15173  15794  17694    383  -3052    616       N  
ATOM   1659  CE2 TRP A 158      57.652  -5.103   8.318  1.00127.27           C  
ANISOU 1659  CE2 TRP A 158    15141  15830  17387    464  -2787    671       C  
ATOM   1660  CE3 TRP A 158      58.345  -4.082  10.405  1.00122.05           C  
ANISOU 1660  CE3 TRP A 158    14185  15585  16604    404  -2296    814       C  
ATOM   1661  CZ2 TRP A 158      58.975  -5.167   7.860  1.00125.22           C  
ANISOU 1661  CZ2 TRP A 158    15172  15514  16890    626  -2721    652       C  
ATOM   1662  CZ3 TRP A 158      59.655  -4.151   9.952  1.00122.26           C  
ANISOU 1662  CZ3 TRP A 158    14475  15566  16411    544  -2246    787       C  
ATOM   1663  CH2 TRP A 158      59.960  -4.690   8.696  1.00123.43           C  
ANISOU 1663  CH2 TRP A 158    14910  15484  16506    658  -2446    715       C  
ATOM   1664  N   GLN A 159      56.028  -3.589  13.781  1.00117.90           N  
ANISOU 1664  N   GLN A 159    12774  15530  16491     20  -1892   1119       N  
ATOM   1665  CA  GLN A 159      56.953  -2.860  14.669  1.00114.57           C  
ANISOU 1665  CA  GLN A 159    12367  15305  15858     85  -1636   1148       C  
ATOM   1666  C   GLN A 159      57.780  -3.807  15.602  1.00114.70           C  
ANISOU 1666  C   GLN A 159    12415  15353  15814     35  -1500   1277       C  
ATOM   1667  O   GLN A 159      58.934  -3.489  15.885  1.00113.20           O  
ANISOU 1667  O   GLN A 159    12334  15267  15409    118  -1368   1266       O  
ATOM   1668  CB  GLN A 159      56.194  -1.831  15.544  1.00115.96           C  
ANISOU 1668  CB  GLN A 159    12309  15683  16068     72  -1473   1180       C  
ATOM   1669  CG  GLN A 159      55.144  -2.397  16.515  1.00134.38           C  
ANISOU 1669  CG  GLN A 159    14367  18069  18621    -67  -1404   1332       C  
ATOM   1670  CD  GLN A 159      54.436  -1.333  17.331  1.00155.52           C  
ANISOU 1670  CD  GLN A 159    16843  20946  21303    -42  -1231   1367       C  
ATOM   1671  OE1 GLN A 159      54.211  -0.201  16.882  1.00150.28           O  
ANISOU 1671  OE1 GLN A 159    16194  20334  20572     57  -1249   1264       O  
ATOM   1672  NE2 GLN A 159      53.972  -1.710  18.513  1.00149.78           N  
ANISOU 1672  NE2 GLN A 159    15930  20318  20660   -120  -1061   1523       N  
ATOM   1673  N   ALA A 160      57.220  -4.962  16.022  1.00109.27           N  
ANISOU 1673  N   ALA A 160    11641  14567  15308    -92  -1538   1394       N  
ATOM   1674  CA  ALA A 160      57.894  -5.907  16.916  1.00107.44           C  
ANISOU 1674  CA  ALA A 160    11453  14351  15020   -123  -1405   1527       C  
ATOM   1675  C   ALA A 160      59.044  -6.664  16.220  1.00107.02           C  
ANISOU 1675  C   ALA A 160    11690  14163  14811    -33  -1490   1494       C  
ATOM   1676  O   ALA A 160      60.048  -6.952  16.872  1.00105.71           O  
ANISOU 1676  O   ALA A 160    11598  14093  14473     31  -1346   1557       O  
ATOM   1677  CB  ALA A 160      56.893  -6.906  17.456  1.00110.40           C  
ANISOU 1677  CB  ALA A 160    11672  14631  15645   -288  -1413   1661       C  
ATOM   1678  N   SER A 161      58.902  -6.991  14.914  1.00101.39           N  
ANISOU 1678  N   SER A 161    11144  13236  14143     -9  -1725   1396       N  
ATOM   1679  CA  SER A 161      59.918  -7.745  14.155  1.00 99.53           C  
ANISOU 1679  CA  SER A 161    11209  12847  13759     97  -1814   1371       C  
ATOM   1680  C   SER A 161      61.194  -6.929  13.913  1.00 97.78           C  
ANISOU 1680  C   SER A 161    11121  12757  13273    273  -1718   1295       C  
ATOM   1681  O   SER A 161      62.233  -7.507  13.590  1.00 97.14           O  
ANISOU 1681  O   SER A 161    11265  12605  13038    386  -1733   1299       O  
ATOM   1682  CB  SER A 161      59.358  -8.185  12.806  1.00104.27           C  
ANISOU 1682  CB  SER A 161    11964  13180  14475     87  -2098   1277       C  
ATOM   1683  OG  SER A 161      59.032  -7.067  11.995  1.00112.69           O  
ANISOU 1683  OG  SER A 161    13013  14263  15540    155  -2201   1136       O  
ATOM   1684  N   TYR A 162      61.096  -5.592  14.025  1.00 89.95           N  
ANISOU 1684  N   TYR A 162     9996  11951  12231    295  -1612   1231       N  
ATOM   1685  CA  TYR A 162      62.184  -4.648  13.787  1.00 86.37           C  
ANISOU 1685  CA  TYR A 162     9638  11624  11556    424  -1509   1151       C  
ATOM   1686  C   TYR A 162      62.817  -4.134  15.101  1.00 88.80           C  
ANISOU 1686  C   TYR A 162     9798  12198  11743    408  -1271   1210       C  
ATOM   1687  O   TYR A 162      64.042  -3.974  15.149  1.00 87.63           O  
ANISOU 1687  O   TYR A 162     9739  12151  11404    496  -1178   1200       O  
ATOM   1688  CB  TYR A 162      61.655  -3.450  12.969  1.00 85.74           C  
ANISOU 1688  CB  TYR A 162     9562  11523  11493    467  -1578   1013       C  
ATOM   1689  CG  TYR A 162      62.621  -2.292  12.864  1.00 83.77           C  
ANISOU 1689  CG  TYR A 162     9372  11414  11043    562  -1432    934       C  
ATOM   1690  CD1 TYR A 162      63.676  -2.318  11.957  1.00 84.71           C  
ANISOU 1690  CD1 TYR A 162     9719  11463  11005    694  -1447    877       C  
ATOM   1691  CD2 TYR A 162      62.468  -1.159  13.654  1.00 83.30           C  
ANISOU 1691  CD2 TYR A 162     9151  11546  10953    519  -1273    915       C  
ATOM   1692  CE1 TYR A 162      64.584  -1.266  11.876  1.00 83.53           C  
ANISOU 1692  CE1 TYR A 162     9611  11436  10690    758  -1299    810       C  
ATOM   1693  CE2 TYR A 162      63.367  -0.100  13.580  1.00 82.74           C  
ANISOU 1693  CE2 TYR A 162     9144  11587  10706    579  -1138    837       C  
ATOM   1694  CZ  TYR A 162      64.424  -0.155  12.687  1.00 88.01           C  
ANISOU 1694  CZ  TYR A 162    10016  12186  11237    687  -1149    784       C  
ATOM   1695  OH  TYR A 162      65.308   0.892  12.614  1.00 86.21           O  
ANISOU 1695  OH  TYR A 162     9838  12063  10855    723  -1004    710       O  
ATOM   1696  N   ILE A 163      61.996  -3.842  16.136  1.00 84.58           N  
ANISOU 1696  N   ILE A 163     9041  11782  11314    306  -1176   1268       N  
ATOM   1697  CA  ILE A 163      62.467  -3.248  17.396  1.00 83.06           C  
ANISOU 1697  CA  ILE A 163     8719  11836  11004    298   -965   1310       C  
ATOM   1698  C   ILE A 163      63.301  -4.270  18.208  1.00 86.70           C  
ANISOU 1698  C   ILE A 163     9205  12364  11374    318   -877   1430       C  
ATOM   1699  O   ILE A 163      64.395  -3.900  18.633  1.00 85.76           O  
ANISOU 1699  O   ILE A 163     9107  12415  11062    383   -768   1414       O  
ATOM   1700  CB  ILE A 163      61.283  -2.702  18.231  1.00 86.39           C  
ANISOU 1700  CB  ILE A 163     8920  12343  11560    210   -889   1351       C  
ATOM   1701  CG1 ILE A 163      60.671  -1.495  17.489  1.00 86.06           C  
ANISOU 1701  CG1 ILE A 163     8873  12283  11545    234   -944   1222       C  
ATOM   1702  CG2 ILE A 163      61.732  -2.278  19.645  1.00 86.49           C  
ANISOU 1702  CG2 ILE A 163     8824  12591  11446    210   -676   1413       C  
ATOM   1703  CD1 ILE A 163      59.510  -0.964  18.062  1.00 94.10           C  
ANISOU 1703  CD1 ILE A 163     9697  13363  12693    181   -895   1255       C  
ATOM   1704  N   VAL A 164      62.817  -5.521  18.410  1.00 83.88           N  
ANISOU 1704  N   VAL A 164     8851  11874  11145    265   -924   1547       N  
ATOM   1705  CA  VAL A 164      63.548  -6.549  19.184  1.00 83.88           C  
ANISOU 1705  CA  VAL A 164     8902  11922  11048    307   -832   1671       C  
ATOM   1706  C   VAL A 164      65.026  -6.646  18.663  1.00 85.77           C  
ANISOU 1706  C   VAL A 164     9319  12212  11058    452   -837   1623       C  
ATOM   1707  O   VAL A 164      65.924  -6.463  19.488  1.00 83.82           O  
ANISOU 1707  O   VAL A 164     9026  12184  10640    514   -702   1647       O  
ATOM   1708  CB  VAL A 164      62.847  -7.940  19.171  1.00 89.59           C  
ANISOU 1708  CB  VAL A 164     9672  12426  11942    232   -902   1788       C  
ATOM   1709  CG1 VAL A 164      63.697  -9.006  19.863  1.00 89.84           C  
ANISOU 1709  CG1 VAL A 164     9805  12491  11837    310   -799   1914       C  
ATOM   1710  CG2 VAL A 164      61.464  -7.860  19.811  1.00 90.62           C  
ANISOU 1710  CG2 VAL A 164     9588  12540  12303     85   -864   1855       C  
ATOM   1711  N   PRO A 165      65.318  -6.827  17.333  1.00 82.60           N  
ANISOU 1711  N   PRO A 165     9107  11638  10641    517   -983   1550       N  
ATOM   1712  CA  PRO A 165      66.731  -6.875  16.900  1.00 81.77           C  
ANISOU 1712  CA  PRO A 165     9145  11604  10318    667   -957   1522       C  
ATOM   1713  C   PRO A 165      67.464  -5.547  17.125  1.00 85.33           C  
ANISOU 1713  C   PRO A 165     9499  12289  10634    690   -847   1427       C  
ATOM   1714  O   PRO A 165      68.619  -5.570  17.542  1.00 85.48           O  
ANISOU 1714  O   PRO A 165     9513  12489  10476    772   -751   1446       O  
ATOM   1715  CB  PRO A 165      66.641  -7.189  15.400  1.00 83.45           C  
ANISOU 1715  CB  PRO A 165     9581  11561  10566    729  -1134   1458       C  
ATOM   1716  CG  PRO A 165      65.287  -7.746  15.195  1.00 89.02           C  
ANISOU 1716  CG  PRO A 165    10280  12046  11497    610  -1270   1484       C  
ATOM   1717  CD  PRO A 165      64.414  -7.056  16.186  1.00 84.61           C  
ANISOU 1717  CD  PRO A 165     9461  11626  11064    473  -1180   1496       C  
ATOM   1718  N   LEU A 166      66.792  -4.401  16.880  1.00 81.12           N  
ANISOU 1718  N   LEU A 166     8887  11755  10181    616   -858   1325       N  
ATOM   1719  CA  LEU A 166      67.377  -3.067  17.040  1.00 79.77           C  
ANISOU 1719  CA  LEU A 166     8648  11767   9893    615   -753   1224       C  
ATOM   1720  C   LEU A 166      67.781  -2.803  18.507  1.00 83.71           C  
ANISOU 1720  C   LEU A 166     8981  12529  10295    578   -599   1271       C  
ATOM   1721  O   LEU A 166      68.818  -2.176  18.745  1.00 82.99           O  
ANISOU 1721  O   LEU A 166     8862  12620  10050    603   -513   1215       O  
ATOM   1722  CB  LEU A 166      66.381  -1.992  16.565  1.00 79.36           C  
ANISOU 1722  CB  LEU A 166     8565  11638   9950    553   -791   1122       C  
ATOM   1723  CG  LEU A 166      66.850  -0.527  16.592  1.00 83.07           C  
ANISOU 1723  CG  LEU A 166     9006  12247  10310    542   -681   1006       C  
ATOM   1724  CD1 LEU A 166      67.969  -0.278  15.590  1.00 82.43           C  
ANISOU 1724  CD1 LEU A 166     9084  12128  10109    632   -683    930       C  
ATOM   1725  CD2 LEU A 166      65.709   0.398  16.280  1.00 86.12           C  
ANISOU 1725  CD2 LEU A 166     9357  12561  10803    496   -706    936       C  
ATOM   1726  N   VAL A 167      66.981  -3.291  19.476  1.00 80.66           N  
ANISOU 1726  N   VAL A 167     8489  12160  10000    522   -565   1373       N  
ATOM   1727  CA  VAL A 167      67.264  -3.099  20.897  1.00 80.85           C  
ANISOU 1727  CA  VAL A 167     8378  12416   9926    510   -424   1424       C  
ATOM   1728  C   VAL A 167      68.487  -3.963  21.272  1.00 87.01           C  
ANISOU 1728  C   VAL A 167     9205  13317  10539    616   -389   1492       C  
ATOM   1729  O   VAL A 167      69.407  -3.452  21.920  1.00 86.87           O  
ANISOU 1729  O   VAL A 167     9120  13530  10357    645   -308   1454       O  
ATOM   1730  CB  VAL A 167      66.040  -3.392  21.803  1.00 85.06           C  
ANISOU 1730  CB  VAL A 167     8795  12921  10601    439   -376   1528       C  
ATOM   1731  CG1 VAL A 167      66.406  -3.279  23.276  1.00 85.15           C  
ANISOU 1731  CG1 VAL A 167     8707  13164  10482    464   -228   1589       C  
ATOM   1732  CG2 VAL A 167      64.894  -2.445  21.482  1.00 84.55           C  
ANISOU 1732  CG2 VAL A 167     8659  12784  10680    357   -398   1462       C  
ATOM   1733  N   TRP A 168      68.535  -5.234  20.810  1.00 84.86           N  
ANISOU 1733  N   TRP A 168     9055  12888  10298    681   -458   1584       N  
ATOM   1734  CA  TRP A 168      69.682  -6.101  21.090  1.00 85.47           C  
ANISOU 1734  CA  TRP A 168     9197  13073  10203    816   -423   1658       C  
ATOM   1735  C   TRP A 168      70.937  -5.586  20.382  1.00 88.74           C  
ANISOU 1735  C   TRP A 168     9647  13605  10467    894   -429   1564       C  
ATOM   1736  O   TRP A 168      72.035  -5.760  20.913  1.00 89.27           O  
ANISOU 1736  O   TRP A 168     9665  13895  10359    983   -363   1586       O  
ATOM   1737  CB  TRP A 168      69.420  -7.562  20.697  1.00 85.33           C  
ANISOU 1737  CB  TRP A 168     9346  12832  10243    875   -492   1773       C  
ATOM   1738  CG  TRP A 168      68.487  -8.279  21.629  1.00 87.49           C  
ANISOU 1738  CG  TRP A 168     9578  13032  10631    813   -442   1898       C  
ATOM   1739  CD1 TRP A 168      67.168  -8.553  21.421  1.00 91.01           C  
ANISOU 1739  CD1 TRP A 168    10021  13253  11308    686   -504   1928       C  
ATOM   1740  CD2 TRP A 168      68.789  -8.737  22.957  1.00 88.08           C  
ANISOU 1740  CD2 TRP A 168     9592  13273  10599    873   -308   2009       C  
ATOM   1741  NE1 TRP A 168      66.639  -9.194  22.519  1.00 91.77           N  
ANISOU 1741  NE1 TRP A 168    10059  13352  11459    654   -401   2064       N  
ATOM   1742  CE2 TRP A 168      67.614  -9.318  23.478  1.00 93.17           C  
ANISOU 1742  CE2 TRP A 168    10217  13762  11423    778   -275   2117       C  
ATOM   1743  CE3 TRP A 168      69.950  -8.737  23.749  1.00 89.40           C  
ANISOU 1743  CE3 TRP A 168     9723  13711  10535   1006   -216   2029       C  
ATOM   1744  CZ2 TRP A 168      67.564  -9.895  24.754  1.00 93.53           C  
ANISOU 1744  CZ2 TRP A 168    10230  13895  11413    824   -134   2251       C  
ATOM   1745  CZ3 TRP A 168      69.902  -9.318  25.008  1.00 91.88           C  
ANISOU 1745  CZ3 TRP A 168    10009  14120  10783   1063    -98   2152       C  
ATOM   1746  CH2 TRP A 168      68.719  -9.878  25.502  1.00 93.48           C  
ANISOU 1746  CH2 TRP A 168    10214  14147  11157    978    -48   2265       C  
ATOM   1747  N   CYS A 169      70.777  -4.919  19.220  1.00 83.83           N  
ANISOU 1747  N   CYS A 169     9099  12843   9909    865   -501   1461       N  
ATOM   1748  CA  CYS A 169      71.893  -4.351  18.466  1.00 82.90           C  
ANISOU 1748  CA  CYS A 169     9019  12805   9673    929   -487   1375       C  
ATOM   1749  C   CYS A 169      72.509  -3.186  19.248  1.00 86.42           C  
ANISOU 1749  C   CYS A 169     9292  13525  10021    858   -381   1291       C  
ATOM   1750  O   CYS A 169      73.733  -3.140  19.385  1.00 86.37           O  
ANISOU 1750  O   CYS A 169     9236  13714   9867    923   -330   1282       O  
ATOM   1751  CB  CYS A 169      71.447  -3.908  17.077  1.00 82.41           C  
ANISOU 1751  CB  CYS A 169     9095  12510   9708    919   -575   1289       C  
ATOM   1752  SG  CYS A 169      72.769  -3.178  16.079  1.00 85.66           S  
ANISOU 1752  SG  CYS A 169     9570  12987   9988    999   -526   1195       S  
ATOM   1753  N   MET A 170      71.662  -2.270  19.784  1.00 82.75           N  
ANISOU 1753  N   MET A 170     8732  13075   9634    729   -350   1232       N  
ATOM   1754  CA  MET A 170      72.113  -1.109  20.567  1.00 82.86           C  
ANISOU 1754  CA  MET A 170     8612  13315   9556    647   -258   1140       C  
ATOM   1755  C   MET A 170      72.743  -1.555  21.893  1.00 87.99           C  
ANISOU 1755  C   MET A 170     9145  14219  10070    689   -201   1205       C  
ATOM   1756  O   MET A 170      73.657  -0.888  22.373  1.00 88.02           O  
ANISOU 1756  O   MET A 170     9050  14447   9947    659   -151   1129       O  
ATOM   1757  CB  MET A 170      70.971  -0.121  20.836  1.00 84.92           C  
ANISOU 1757  CB  MET A 170     8836  13509   9919    531   -237   1079       C  
ATOM   1758  CG  MET A 170      70.428   0.531  19.574  1.00 87.90           C  
ANISOU 1758  CG  MET A 170     9324  13678  10396    503   -285    989       C  
ATOM   1759  SD  MET A 170      69.117   1.747  19.843  1.00 91.86           S  
ANISOU 1759  SD  MET A 170     9791  14115  10998    403   -254    920       S  
ATOM   1760  CE  MET A 170      67.841   0.714  20.572  1.00 89.08           C  
ANISOU 1760  CE  MET A 170     9369  13676  10800    405   -299   1070       C  
ATOM   1761  N   ALA A 171      72.301  -2.711  22.440  1.00 85.37           N  
ANISOU 1761  N   ALA A 171     8832  13847   9756    763   -212   1343       N  
ATOM   1762  CA  ALA A 171      72.852  -3.310  23.659  1.00 86.03           C  
ANISOU 1762  CA  ALA A 171     8840  14151   9696    846   -158   1422       C  
ATOM   1763  C   ALA A 171      74.282  -3.850  23.408  1.00 91.69           C  
ANISOU 1763  C   ALA A 171     9563  15022  10253    978   -169   1436       C  
ATOM   1764  O   ALA A 171      75.148  -3.702  24.277  1.00 91.53           O  
ANISOU 1764  O   ALA A 171     9424  15277  10077   1011   -133   1407       O  
ATOM   1765  CB  ALA A 171      71.942  -4.424  24.151  1.00 87.14           C  
ANISOU 1765  CB  ALA A 171     9033  14162   9913    892   -148   1573       C  
ATOM   1766  N   CYS A 172      74.528  -4.448  22.208  1.00 89.15           N  
ANISOU 1766  N   CYS A 172     9379  14526   9967   1061   -225   1477       N  
ATOM   1767  CA  CYS A 172      75.837  -4.988  21.808  1.00 89.94           C  
ANISOU 1767  CA  CYS A 172     9505  14743   9924   1213   -228   1508       C  
ATOM   1768  C   CYS A 172      76.826  -3.858  21.571  1.00 92.51           C  
ANISOU 1768  C   CYS A 172     9705  15265  10179   1155   -197   1380       C  
ATOM   1769  O   CYS A 172      78.005  -4.020  21.883  1.00 92.86           O  
ANISOU 1769  O   CYS A 172     9654  15555  10073   1250   -172   1394       O  
ATOM   1770  CB  CYS A 172      75.719  -5.864  20.565  1.00 90.73           C  
ANISOU 1770  CB  CYS A 172     9815  14572  10087   1308   -292   1570       C  
ATOM   1771  SG  CYS A 172      74.776  -7.385  20.813  1.00 95.81           S  
ANISOU 1771  SG  CYS A 172    10624  14973  10806   1371   -331   1726       S  
ATOM   1772  N   LEU A 173      76.359  -2.731  20.986  1.00 86.94           N  
ANISOU 1772  N   LEU A 173     9001  14450   9580   1003   -195   1260       N  
ATOM   1773  CA  LEU A 173      77.223  -1.585  20.684  1.00 85.55           C  
ANISOU 1773  CA  LEU A 173     8729  14418   9358    919   -149   1134       C  
ATOM   1774  C   LEU A 173      77.598  -0.833  21.966  1.00 90.00           C  
ANISOU 1774  C   LEU A 173     9103  15266   9827    821   -110   1061       C  
ATOM   1775  O   LEU A 173      78.703  -0.299  22.053  1.00 90.37           O  
ANISOU 1775  O   LEU A 173     9021  15534   9780    796    -81    996       O  
ATOM   1776  CB  LEU A 173      76.556  -0.624  19.684  1.00 84.00           C  
ANISOU 1776  CB  LEU A 173     8632  13994   9292    804   -147   1033       C  
ATOM   1777  CG  LEU A 173      76.175  -1.194  18.311  1.00 87.01           C  
ANISOU 1777  CG  LEU A 173     9220  14082   9760    899   -203   1075       C  
ATOM   1778  CD1 LEU A 173      75.439  -0.174  17.494  1.00 85.82           C  
ANISOU 1778  CD1 LEU A 173     9158  13729   9719    798   -204    968       C  
ATOM   1779  CD2 LEU A 173      77.383  -1.688  17.552  1.00 89.91           C  
ANISOU 1779  CD2 LEU A 173     9631  14495  10034   1044   -183   1118       C  
ATOM   1780  N   SER A 174      76.694  -0.821  22.965  1.00 86.80           N  
ANISOU 1780  N   SER A 174     8679  14856   9445    769   -109   1074       N  
ATOM   1781  CA  SER A 174      76.918  -0.175  24.264  1.00 87.63           C  
ANISOU 1781  CA  SER A 174     8643  15207   9445    698    -82   1008       C  
ATOM   1782  C   SER A 174      77.934  -0.954  25.122  1.00 93.52           C  
ANISOU 1782  C   SER A 174     9282  16233  10019    840    -96   1076       C  
ATOM   1783  O   SER A 174      78.590  -0.355  25.982  1.00 94.35           O  
ANISOU 1783  O   SER A 174     9244  16601  10003    794    -96    991       O  
ATOM   1784  CB  SER A 174      75.603  -0.047  25.030  1.00 90.57           C  
ANISOU 1784  CB  SER A 174     9053  15477   9884    649    -64   1034       C  
ATOM   1785  OG  SER A 174      74.650   0.733  24.329  1.00 97.28           O  
ANISOU 1785  OG  SER A 174     9985  16100  10878    534    -55    970       O  
ATOM   1786  N   SER A 175      78.056  -2.284  24.889  1.00 90.16           N  
ANISOU 1786  N   SER A 175     8938  15745   9574   1020   -112   1224       N  
ATOM   1787  CA  SER A 175      78.948  -3.165  25.650  1.00 91.13           C  
ANISOU 1787  CA  SER A 175     8996  16106   9522   1202   -118   1312       C  
ATOM   1788  C   SER A 175      80.312  -3.383  24.945  1.00 94.37           C  
ANISOU 1788  C   SER A 175     9346  16661   9849   1303   -129   1315       C  
ATOM   1789  O   SER A 175      81.100  -4.198  25.424  1.00 95.47           O  
ANISOU 1789  O   SER A 175     9461  16967   9845   1499   -135   1411       O  
ATOM   1790  CB  SER A 175      78.281  -4.520  25.882  1.00 95.30           C  
ANISOU 1790  CB  SER A 175     9674  16473  10064   1351   -110   1481       C  
ATOM   1791  OG  SER A 175      78.034  -5.207  24.666  1.00103.75           O  
ANISOU 1791  OG  SER A 175    10908  17271  11242   1398   -131   1549       O  
ATOM   1792  N   LEU A 176      80.595  -2.666  23.831  1.00 88.93           N  
ANISOU 1792  N   LEU A 176     8638  15910   9241   1187   -119   1218       N  
ATOM   1793  CA  LEU A 176      81.871  -2.797  23.109  1.00 88.64           C  
ANISOU 1793  CA  LEU A 176     8529  16011   9140   1275   -105   1226       C  
ATOM   1794  C   LEU A 176      83.006  -2.059  23.842  1.00 94.51           C  
ANISOU 1794  C   LEU A 176     9012  17127   9770   1203   -106   1123       C  
ATOM   1795  O   LEU A 176      84.043  -2.696  24.046  1.00 95.18           O  
ANISOU 1795  O   LEU A 176     8985  17461   9720   1368   -116   1186       O  
ATOM   1796  CB  LEU A 176      81.781  -2.294  21.665  1.00 87.28           C  
ANISOU 1796  CB  LEU A 176     8467  15600   9097   1206    -75   1184       C  
ATOM   1797  CG  LEU A 176      80.948  -3.127  20.710  1.00 90.58           C  
ANISOU 1797  CG  LEU A 176     9139  15673   9603   1314    -98   1284       C  
ATOM   1798  CD1 LEU A 176      80.574  -2.340  19.515  1.00 89.90           C  
ANISOU 1798  CD1 LEU A 176     9163  15349   9644   1215    -78   1206       C  
ATOM   1799  CD2 LEU A 176      81.628  -4.443  20.354  1.00 92.67           C  
ANISOU 1799  CD2 LEU A 176     9483  15972   9757   1572   -102   1431       C  
ATOM   1800  N   PRO A 177      82.865  -0.768  24.297  1.00 91.82           N  
ANISOU 1800  N   PRO A 177     8573  16847   9469    971   -104    966       N  
ATOM   1801  CA  PRO A 177      83.985  -0.123  25.020  1.00 93.31           C  
ANISOU 1801  CA  PRO A 177     8511  17395   9548    890   -128    858       C  
ATOM   1802  C   PRO A 177      84.382  -0.903  26.281  1.00 98.94           C  
ANISOU 1802  C   PRO A 177     9126  18384  10081   1058   -189    917       C  
ATOM   1803  O   PRO A 177      85.473  -0.703  26.810  1.00100.33           O  
ANISOU 1803  O   PRO A 177     9084  18895  10140   1053   -234    851       O  
ATOM   1804  CB  PRO A 177      83.429   1.257  25.377  1.00 94.64           C  
ANISOU 1804  CB  PRO A 177     8677  17494   9788    624   -119    692       C  
ATOM   1805  CG  PRO A 177      82.375   1.513  24.353  1.00 97.36           C  
ANISOU 1805  CG  PRO A 177     9237  17461  10296    565    -66    705       C  
ATOM   1806  CD  PRO A 177      81.731   0.172  24.152  1.00 92.21           C  
ANISOU 1806  CD  PRO A 177     8735  16648   9653    777    -84    875       C  
ATOM   1807  N   THR A 178      83.511  -1.827  26.723  1.00 95.26           N  
ANISOU 1807  N   THR A 178     8826  17775   9595   1215   -190   1046       N  
ATOM   1808  CA  THR A 178      83.756  -2.727  27.846  1.00 96.30           C  
ANISOU 1808  CA  THR A 178     8931  18107   9551   1421   -224   1135       C  
ATOM   1809  C   THR A 178      84.757  -3.808  27.403  1.00101.11           C  
ANISOU 1809  C   THR A 178     9503  18867  10048   1671   -224   1258       C  
ATOM   1810  O   THR A 178      85.746  -4.045  28.093  1.00102.79           O  
ANISOU 1810  O   THR A 178     9549  19420  10085   1800   -268   1258       O  
ATOM   1811  CB  THR A 178      82.426  -3.328  28.331  1.00104.39           C  
ANISOU 1811  CB  THR A 178    10166  18873  10624   1474   -193   1237       C  
ATOM   1812  OG1 THR A 178      81.449  -2.295  28.494  1.00105.73           O  
ANISOU 1812  OG1 THR A 178    10372  18889  10913   1253   -179   1131       O  
ATOM   1813  CG2 THR A 178      82.579  -4.155  29.595  1.00103.04           C  
ANISOU 1813  CG2 THR A 178    10000  18882  10269   1686   -203   1331       C  
ATOM   1814  N   PHE A 179      84.513  -4.428  26.226  1.00 96.21           N  
ANISOU 1814  N   PHE A 179     9043  17996   9516   1751   -180   1360       N  
ATOM   1815  CA  PHE A 179      85.343  -5.492  25.656  1.00 96.87           C  
ANISOU 1815  CA  PHE A 179     9149  18163   9493   2011   -164   1494       C  
ATOM   1816  C   PHE A 179      86.748  -4.976  25.306  1.00102.30           C  
ANISOU 1816  C   PHE A 179     9582  19159  10127   2002   -165   1429       C  
ATOM   1817  O   PHE A 179      87.718  -5.737  25.386  1.00103.77           O  
ANISOU 1817  O   PHE A 179     9685  19581  10160   2238   -165   1522       O  
ATOM   1818  CB  PHE A 179      84.670  -6.073  24.394  1.00 97.26           C  
ANISOU 1818  CB  PHE A 179     9466  17825   9665   2066   -125   1593       C  
ATOM   1819  CG  PHE A 179      85.214  -7.413  23.954  1.00 99.97           C  
ANISOU 1819  CG  PHE A 179     9937  18168   9879   2373   -104   1763       C  
ATOM   1820  CD1 PHE A 179      86.334  -7.494  23.129  1.00104.18           C  
ANISOU 1820  CD1 PHE A 179    10395  18836  10352   2499    -74   1796       C  
ATOM   1821  CD2 PHE A 179      84.590  -8.594  24.336  1.00102.41           C  
ANISOU 1821  CD2 PHE A 179    10462  18317  10131   2539   -100   1898       C  
ATOM   1822  CE1 PHE A 179      86.849  -8.736  22.738  1.00106.11           C  
ANISOU 1822  CE1 PHE A 179    10783  19076  10458   2809    -46   1960       C  
ATOM   1823  CE2 PHE A 179      85.098  -9.836  23.935  1.00106.48           C  
ANISOU 1823  CE2 PHE A 179    11135  18811  10513   2830    -74   2055       C  
ATOM   1824  CZ  PHE A 179      86.226  -9.899  23.141  1.00105.41           C  
ANISOU 1824  CZ  PHE A 179    10930  18822  10298   2973    -50   2085       C  
ATOM   1825  N   TYR A 180      86.860  -3.691  24.933  1.00 97.79           N  
ANISOU 1825  N   TYR A 180     8887  18588   9682   1735   -155   1278       N  
ATOM   1826  CA  TYR A 180      88.140  -3.126  24.535  1.00 98.77           C  
ANISOU 1826  CA  TYR A 180     8761  18976   9790   1689   -137   1218       C  
ATOM   1827  C   TYR A 180      89.004  -2.701  25.730  1.00105.93           C  
ANISOU 1827  C   TYR A 180     9366  20311  10573   1633   -216   1113       C  
ATOM   1828  O   TYR A 180      90.231  -2.691  25.595  1.00107.78           O  
ANISOU 1828  O   TYR A 180     9352  20842  10759   1657   -216   1096       O  
ATOM   1829  CB  TYR A 180      87.951  -1.904  23.624  1.00 98.29           C  
ANISOU 1829  CB  TYR A 180     8710  18719   9917   1422    -75   1103       C  
ATOM   1830  CG  TYR A 180      87.028  -2.115  22.444  1.00 97.28           C  
ANISOU 1830  CG  TYR A 180     8883  18158   9921   1442    -19   1168       C  
ATOM   1831  CD1 TYR A 180      87.209  -3.190  21.576  1.00 98.96           C  
ANISOU 1831  CD1 TYR A 180     9263  18241  10096   1697     11   1328       C  
ATOM   1832  CD2 TYR A 180      86.107  -1.139  22.077  1.00 96.11           C  
ANISOU 1832  CD2 TYR A 180     8849  17742   9929   1207      4   1058       C  
ATOM   1833  CE1 TYR A 180      86.374  -3.378  20.477  1.00 97.03           C  
ANISOU 1833  CE1 TYR A 180     9302  17599   9966   1715     37   1372       C  
ATOM   1834  CE2 TYR A 180      85.309  -1.284  20.944  1.00 95.03           C  
ANISOU 1834  CE2 TYR A 180     8974  17226   9907   1233     37   1105       C  
ATOM   1835  CZ  TYR A 180      85.449  -2.404  20.144  1.00100.57           C  
ANISOU 1835  CZ  TYR A 180     9841  17800  10572   1481     45   1257       C  
ATOM   1836  OH  TYR A 180      84.650  -2.552  19.043  1.00 99.09           O  
ANISOU 1836  OH  TYR A 180     9920  17237  10491   1507     53   1290       O  
ATOM   1837  N   PHE A 181      88.394  -2.313  26.871  1.00102.63           N  
ANISOU 1837  N   PHE A 181     8961  19931  10102   1560   -285   1039       N  
ATOM   1838  CA  PHE A 181      89.189  -1.801  27.984  1.00104.70           C  
ANISOU 1838  CA  PHE A 181     8956  20586  10240   1498   -382    917       C  
ATOM   1839  C   PHE A 181      89.231  -2.774  29.184  1.00110.85           C  
ANISOU 1839  C   PHE A 181     9751  21566  10802   1766   -452    999       C  
ATOM   1840  O   PHE A 181      90.258  -2.797  29.859  1.00112.66           O  
ANISOU 1840  O   PHE A 181     9740  22188  10879   1851   -536    957       O  
ATOM   1841  CB  PHE A 181      88.665  -0.439  28.447  1.00106.01           C  
ANISOU 1841  CB  PHE A 181     9105  20681  10496   1172   -412    723       C  
ATOM   1842  CG  PHE A 181      88.866   0.622  27.388  1.00107.05           C  
ANISOU 1842  CG  PHE A 181     9186  20680  10809    905   -343    622       C  
ATOM   1843  CD1 PHE A 181      90.093   1.264  27.245  1.00111.96           C  
ANISOU 1843  CD1 PHE A 181     9518  21585  11437    767   -361    519       C  
ATOM   1844  CD2 PHE A 181      87.837   0.963  26.516  1.00106.64           C  
ANISOU 1844  CD2 PHE A 181     9375  20222  10921    796   -255    631       C  
ATOM   1845  CE1 PHE A 181      90.288   2.220  26.245  1.00112.51           C  
ANISOU 1845  CE1 PHE A 181     9560  21514  11676    524   -271    437       C  
ATOM   1846  CE2 PHE A 181      88.033   1.921  25.517  1.00109.05           C  
ANISOU 1846  CE2 PHE A 181     9662  20395  11377    576   -176    544       C  
ATOM   1847  CZ  PHE A 181      89.260   2.534  25.382  1.00109.19           C  
ANISOU 1847  CZ  PHE A 181     9410  20678  11399    442   -173    453       C  
ATOM   1848  N   ARG A 182      88.174  -3.578  29.449  1.00107.38           N  
ANISOU 1848  N   ARG A 182     9583  20872  10346   1904   -415   1117       N  
ATOM   1849  CA  ARG A 182      88.228  -4.545  30.562  1.00108.94           C  
ANISOU 1849  CA  ARG A 182     9824  21238  10329   2178   -454   1210       C  
ATOM   1850  C   ARG A 182      89.324  -5.583  30.296  1.00115.82           C  
ANISOU 1850  C   ARG A 182    10617  22343  11045   2490   -451   1344       C  
ATOM   1851  O   ARG A 182      89.406  -6.116  29.193  1.00114.93           O  
ANISOU 1851  O   ARG A 182    10627  22046  10997   2589   -374   1465       O  
ATOM   1852  CB  ARG A 182      86.869  -5.237  30.808  1.00107.57           C  
ANISOU 1852  CB  ARG A 182     9960  20717  10193   2249   -387   1326       C  
ATOM   1853  CG  ARG A 182      85.846  -4.384  31.568  1.00116.67           C  
ANISOU 1853  CG  ARG A 182    11168  21751  11411   2036   -398   1214       C  
ATOM   1854  CD  ARG A 182      86.228  -4.236  33.032  1.00130.50           C  
ANISOU 1854  CD  ARG A 182    12811  23826  12948   2129   -482   1147       C  
ATOM   1855  NE  ARG A 182      85.328  -3.356  33.773  1.00142.42           N  
ANISOU 1855  NE  ARG A 182    14374  25244  14497   1937   -492   1031       N  
ATOM   1856  CZ  ARG A 182      85.458  -3.081  35.068  1.00166.70           C  
ANISOU 1856  CZ  ARG A 182    17407  28541  17391   1999   -562    960       C  
ATOM   1857  NH1 ARG A 182      86.439  -3.628  35.774  1.00161.23           N  
ANISOU 1857  NH1 ARG A 182    16613  28180  16468   2251   -635    993       N  
ATOM   1858  NH2 ARG A 182      84.605  -2.264  35.668  1.00155.55           N  
ANISOU 1858  NH2 ARG A 182    16071  27019  16013   1833   -559    861       N  
ATOM   1859  N   ASP A 183      90.225  -5.780  31.277  1.00115.52           N  
ANISOU 1859  N   ASP A 183    10365  22728  10797   2642   -543   1311       N  
ATOM   1860  CA  ASP A 183      91.356  -6.712  31.196  1.00117.44           C  
ANISOU 1860  CA  ASP A 183    10494  23271  10858   2966   -553   1428       C  
ATOM   1861  C   ASP A 183      91.934  -6.958  32.597  1.00123.55           C  
ANISOU 1861  C   ASP A 183    11123  24447  11373   3162   -666   1393       C  
ATOM   1862  O   ASP A 183      91.773  -6.114  33.481  1.00123.89           O  
ANISOU 1862  O   ASP A 183    11054  24615  11403   2979   -763   1228       O  
ATOM   1863  CB  ASP A 183      92.447  -6.169  30.241  1.00120.23           C  
ANISOU 1863  CB  ASP A 183    10573  23808  11300   2863   -549   1379       C  
ATOM   1864  CG  ASP A 183      93.513  -7.177  29.840  1.00132.41           C  
ANISOU 1864  CG  ASP A 183    12033  25590  12689   3210   -519   1535       C  
ATOM   1865  OD1 ASP A 183      93.164  -8.363  29.635  1.00132.84           O  
ANISOU 1865  OD1 ASP A 183    12359  25476  12640   3502   -449   1717       O  
ATOM   1866  OD2 ASP A 183      94.657  -6.754  29.585  1.00139.01           O  
ANISOU 1866  OD2 ASP A 183    12548  26739  13528   3174   -546   1485       O  
ATOM   1867  N   VAL A 184      92.586  -8.118  32.801  1.00120.72           N  
ANISOU 1867  N   VAL A 184    10792  24281  10795   3551   -656   1547       N  
ATOM   1868  CA  VAL A 184      93.212  -8.479  34.075  1.00122.65           C  
ANISOU 1868  CA  VAL A 184    10916  24925  10760   3806   -763   1532       C  
ATOM   1869  C   VAL A 184      94.580  -7.793  34.164  1.00128.40           C  
ANISOU 1869  C   VAL A 184    11203  26140  11441   3743   -897   1393       C  
ATOM   1870  O   VAL A 184      95.413  -7.950  33.269  1.00128.82           O  
ANISOU 1870  O   VAL A 184    11091  26320  11535   3797   -861   1450       O  
ATOM   1871  CB  VAL A 184      93.322 -10.019  34.257  1.00127.36           C  
ANISOU 1871  CB  VAL A 184    11736  25527  11129   4266   -686   1757       C  
ATOM   1872  CG1 VAL A 184      94.251 -10.391  35.420  1.00130.41           C  
ANISOU 1872  CG1 VAL A 184    11947  26401  11202   4579   -803   1745       C  
ATOM   1873  CG2 VAL A 184      91.944 -10.638  34.443  1.00125.22           C  
ANISOU 1873  CG2 VAL A 184    11875  24809  10895   4301   -570   1872       C  
ATOM   1874  N   ARG A 185      94.785  -7.005  35.234  1.00126.24           N  
ANISOU 1874  N   ARG A 185    10746  26130  11091   3617  -1052   1208       N  
ATOM   1875  CA  ARG A 185      96.036  -6.293  35.511  1.00128.85           C  
ANISOU 1875  CA  ARG A 185    10643  26940  11376   3521  -1213   1046       C  
ATOM   1876  C   ARG A 185      96.410  -6.449  36.977  1.00136.65           C  
ANISOU 1876  C   ARG A 185    11546  28292  12083   3723  -1385    965       C  
ATOM   1877  O   ARG A 185      95.531  -6.441  37.845  1.00135.70           O  
ANISOU 1877  O   ARG A 185    11654  28006  11900   3708  -1402    923       O  
ATOM   1878  CB  ARG A 185      95.934  -4.797  35.139  1.00126.55           C  
ANISOU 1878  CB  ARG A 185    10185  26555  11343   3023  -1250    836       C  
ATOM   1879  CG  ARG A 185      95.695  -4.512  33.656  1.00130.37           C  
ANISOU 1879  CG  ARG A 185    10732  26705  12099   2816  -1089    895       C  
ATOM   1880  CD  ARG A 185      96.844  -4.941  32.752  1.00136.31           C  
ANISOU 1880  CD  ARG A 185    11248  27682  12862   2956  -1036    998       C  
ATOM   1881  NE  ARG A 185      96.496  -4.808  31.337  1.00135.01           N  
ANISOU 1881  NE  ARG A 185    11218  27150  12930   2809   -868   1073       N  
ATOM   1882  CZ  ARG A 185      96.684  -3.706  30.618  1.00146.50           C  
ANISOU 1882  CZ  ARG A 185    12520  28532  14612   2447   -837    950       C  
ATOM   1883  NH1 ARG A 185      96.325  -3.671  29.342  1.00134.83           N  
ANISOU 1883  NH1 ARG A 185    11205  26706  13318   2365   -679   1031       N  
ATOM   1884  NH2 ARG A 185      97.219  -2.626  31.173  1.00131.24           N  
ANISOU 1884  NH2 ARG A 185    10289  26858  12717   2166   -962    741       N  
ATOM   1885  N   THR A 186      97.715  -6.593  37.257  1.00137.39           N  
ANISOU 1885  N   THR A 186    11310  28889  12003   3927  -1510    946       N  
ATOM   1886  CA  THR A 186      98.210  -6.772  38.624  1.00140.65           C  
ANISOU 1886  CA  THR A 186    11614  29706  12122   4164  -1697    866       C  
ATOM   1887  C   THR A 186      98.213  -5.416  39.347  1.00145.60           C  
ANISOU 1887  C   THR A 186    12062  30453  12807   3795  -1885    585       C  
ATOM   1888  O   THR A 186      98.824  -4.455  38.875  1.00145.99           O  
ANISOU 1888  O   THR A 186    11799  30630  13042   3451  -1955    433       O  
ATOM   1889  CB  THR A 186      99.610  -7.421  38.629  1.00153.26           C  
ANISOU 1889  CB  THR A 186    12882  31822  13526   4492  -1781    929       C  
ATOM   1890  OG1 THR A 186     100.549  -6.537  38.021  1.00155.81           O  
ANISOU 1890  OG1 THR A 186    12769  32397  14033   4191  -1860    795       O  
ATOM   1891  CG2 THR A 186      99.636  -8.775  37.921  1.00151.31           C  
ANISOU 1891  CG2 THR A 186    12843  31455  13191   4887  -1591   1211       C  
ATOM   1892  N   ILE A 187      97.477  -5.340  40.463  1.00142.55           N  
ANISOU 1892  N   ILE A 187    11904  29994  12264   3864  -1950    523       N  
ATOM   1893  CA  ILE A 187      97.380  -4.140  41.290  1.00143.74           C  
ANISOU 1893  CA  ILE A 187    11963  30231  12420   3565  -2131    262       C  
ATOM   1894  C   ILE A 187      98.475  -4.259  42.340  1.00152.61           C  
ANISOU 1894  C   ILE A 187    12807  31921  13257   3796  -2385    147       C  
ATOM   1895  O   ILE A 187      98.291  -4.948  43.342  1.00153.43           O  
ANISOU 1895  O   ILE A 187    13097  32124  13075   4156  -2432    198       O  
ATOM   1896  CB  ILE A 187      95.940  -3.975  41.883  1.00144.51           C  
ANISOU 1896  CB  ILE A 187    12484  29910  12513   3517  -2044    267       C  
ATOM   1897  CG1 ILE A 187      94.837  -4.100  40.808  1.00140.89           C  
ANISOU 1897  CG1 ILE A 187    12302  28908  12323   3355  -1791    414       C  
ATOM   1898  CG2 ILE A 187      95.786  -2.688  42.677  1.00145.97           C  
ANISOU 1898  CG2 ILE A 187    12617  30147  12697   3209  -2219     -1       C  
ATOM   1899  CD1 ILE A 187      94.874  -3.074  39.608  1.00146.51           C  
ANISOU 1899  CD1 ILE A 187    12858  29439  13369   2891  -1745    309       C  
ATOM   1900  N   GLU A 188      99.642  -3.646  42.054  1.00152.28           N  
ANISOU 1900  N   GLU A 188    12310  32254  13293   3602  -2538      3       N  
ATOM   1901  CA  GLU A 188     100.887  -3.700  42.826  1.00156.42           C  
ANISOU 1901  CA  GLU A 188    12460  33377  13595   3772  -2801   -120       C  
ATOM   1902  C   GLU A 188     100.696  -3.433  44.338  1.00163.09           C  
ANISOU 1902  C   GLU A 188    13425  34374  14166   3888  -3018   -285       C  
ATOM   1903  O   GLU A 188     101.280  -4.164  45.141  1.00165.56           O  
ANISOU 1903  O   GLU A 188    13690  35047  14168   4313  -3140   -245       O  
ATOM   1904  CB  GLU A 188     101.892  -2.676  42.284  1.00159.61           C  
ANISOU 1904  CB  GLU A 188    12384  34041  14220   3355  -2931   -312       C  
ATOM   1905  N   TYR A 189      99.906  -2.407  44.726  1.00159.22           N  
ANISOU 1905  N   TYR A 189    13109  33617  13770   3544  -3061   -464       N  
ATOM   1906  CA  TYR A 189      99.733  -2.056  46.142  1.00161.52           C  
ANISOU 1906  CA  TYR A 189    13530  34039  13800   3639  -3271   -634       C  
ATOM   1907  C   TYR A 189      98.754  -3.028  46.866  1.00163.52           C  
ANISOU 1907  C   TYR A 189    14263  34047  13820   4066  -3122   -442       C  
ATOM   1908  O   TYR A 189      98.625  -2.941  48.090  1.00165.27           O  
ANISOU 1908  O   TYR A 189    14652  34344  13799   4209  -3260   -548       O  
ATOM   1909  CB  TYR A 189      99.246  -0.603  46.316  1.00162.67           C  
ANISOU 1909  CB  TYR A 189    13721  33976  14111   3137  -3360   -889       C  
ATOM   1910  CG  TYR A 189      97.928  -0.267  45.652  1.00160.40           C  
ANISOU 1910  CG  TYR A 189    13783  33093  14070   2889  -3095   -803       C  
ATOM   1911  CD1 TYR A 189      97.889   0.234  44.353  1.00160.24           C  
ANISOU 1911  CD1 TYR A 189    13642  32852  14392   2519  -2951   -788       C  
ATOM   1912  CD2 TYR A 189      96.731  -0.333  46.360  1.00159.62           C  
ANISOU 1912  CD2 TYR A 189    14123  32663  13860   3013  -2998   -751       C  
ATOM   1913  CE1 TYR A 189      96.683   0.597  43.753  1.00157.48           C  
ANISOU 1913  CE1 TYR A 189    13605  31972  14259   2300  -2726   -722       C  
ATOM   1914  CE2 TYR A 189      95.518   0.018  45.768  1.00156.82           C  
ANISOU 1914  CE2 TYR A 189    14062  31788  13736   2788  -2766   -675       C  
ATOM   1915  CZ  TYR A 189      95.498   0.483  44.463  1.00162.09           C  
ANISOU 1915  CZ  TYR A 189    14602  32250  14733   2434  -2640   -666       C  
ATOM   1916  OH  TYR A 189      94.304   0.832  43.877  1.00158.70           O  
ANISOU 1916  OH  TYR A 189    14456  31324  14518   2230  -2426   -598       O  
ATOM   1917  N   LEU A 190      98.103  -3.955  46.132  1.00156.81           N  
ANISOU 1917  N   LEU A 190    13632  32913  13035   4274  -2847   -162       N  
ATOM   1918  CA  LEU A 190      97.209  -4.961  46.721  1.00155.17           C  
ANISOU 1918  CA  LEU A 190    13862  32466  12629   4669  -2679     43       C  
ATOM   1919  C   LEU A 190      97.746  -6.384  46.505  1.00159.75           C  
ANISOU 1919  C   LEU A 190    14446  33217  13036   5146  -2583    284       C  
ATOM   1920  O   LEU A 190      97.307  -7.313  47.188  1.00159.85           O  
ANISOU 1920  O   LEU A 190    14767  33167  12800   5555  -2494    436       O  
ATOM   1921  CB  LEU A 190      95.788  -4.860  46.146  1.00150.77           C  
ANISOU 1921  CB  LEU A 190    13664  31304  12319   4456  -2411    161       C  
ATOM   1922  CG  LEU A 190      94.962  -3.619  46.496  1.00153.87           C  
ANISOU 1922  CG  LEU A 190    14177  31442  12847   4064  -2447    -28       C  
ATOM   1923  CD1 LEU A 190      93.689  -3.579  45.688  1.00149.60           C  
ANISOU 1923  CD1 LEU A 190    13933  30341  12565   3883  -2173    117       C  
ATOM   1924  CD2 LEU A 190      94.636  -3.565  47.985  1.00158.17           C  
ANISOU 1924  CD2 LEU A 190    14919  32092  13089   4274  -2574   -124       C  
ATOM   1925  N   GLY A 191      98.687  -6.530  45.568  1.00156.28           N  
ANISOU 1925  N   GLY A 191    13679  32982  12719   5097  -2588    321       N  
ATOM   1926  CA  GLY A 191      99.293  -7.805  45.192  1.00156.55           C  
ANISOU 1926  CA  GLY A 191    13695  33181  12607   5527  -2489    549       C  
ATOM   1927  C   GLY A 191      98.275  -8.804  44.681  1.00157.19           C  
ANISOU 1927  C   GLY A 191    14215  32769  12743   5693  -2183    821       C  
ATOM   1928  O   GLY A 191      98.372  -9.988  44.985  1.00157.00           O  
ANISOU 1928  O   GLY A 191    14397  32787  12470   6158  -2093   1011       O  
ATOM   1929  N   VAL A 192      97.283  -8.326  43.907  1.00150.50           N  
ANISOU 1929  N   VAL A 192    13522  31445  12218   5314  -2023    835       N  
ATOM   1930  CA  VAL A 192      96.163  -9.141  43.443  1.00147.14           C  
ANISOU 1930  CA  VAL A 192    13514  30510  11883   5399  -1750   1065       C  
ATOM   1931  C   VAL A 192      95.920  -8.901  41.926  1.00148.11           C  
ANISOU 1931  C   VAL A 192    13589  30325  12359   5073  -1610   1118       C  
ATOM   1932  O   VAL A 192      96.208  -7.807  41.432  1.00147.54           O  
ANISOU 1932  O   VAL A 192    13245  30315  12499   4685  -1701    944       O  
ATOM   1933  CB  VAL A 192      94.931  -8.752  44.309  1.00149.64           C  
ANISOU 1933  CB  VAL A 192    14148  30511  12196   5296  -1704   1019       C  
ATOM   1934  CG1 VAL A 192      94.353  -7.381  43.921  1.00147.52           C  
ANISOU 1934  CG1 VAL A 192    13792  30039  12221   4762  -1748    822       C  
ATOM   1935  CG2 VAL A 192      93.868  -9.825  44.266  1.00147.30           C  
ANISOU 1935  CG2 VAL A 192    14288  29772  11908   5491  -1442   1270       C  
ATOM   1936  N   ASN A 193      95.428  -9.929  41.189  1.00142.50           N  
ANISOU 1936  N   ASN A 193    13156  29286  11701   5240  -1391   1355       N  
ATOM   1937  CA  ASN A 193      95.114  -9.784  39.758  1.00139.42           C  
ANISOU 1937  CA  ASN A 193    12786  28563  11625   4971  -1254   1415       C  
ATOM   1938  C   ASN A 193      93.648  -9.431  39.610  1.00140.63           C  
ANISOU 1938  C   ASN A 193    13250  28193  11989   4708  -1125   1427       C  
ATOM   1939  O   ASN A 193      92.779 -10.294  39.748  1.00139.19           O  
ANISOU 1939  O   ASN A 193    13418  27707  11760   4895   -973   1600       O  
ATOM   1940  CB  ASN A 193      95.468 -11.037  38.945  1.00140.02           C  
ANISOU 1940  CB  ASN A 193    12969  28594  11640   5289  -1115   1649       C  
ATOM   1941  CG  ASN A 193      96.946 -11.303  38.819  1.00164.80           C  
ANISOU 1941  CG  ASN A 193    15757  32245  14614   5518  -1224   1647       C  
ATOM   1942  OD1 ASN A 193      97.769 -10.788  39.585  1.00166.72           O  
ANISOU 1942  OD1 ASN A 193    15717  32940  14690   5582  -1416   1504       O  
ATOM   1943  ND2 ASN A 193      97.314 -12.132  37.855  1.00152.97           N  
ANISOU 1943  ND2 ASN A 193    14277  30693  13151   5668  -1105   1810       N  
ATOM   1944  N   ALA A 194      93.373  -8.141  39.380  1.00136.60           N  
ANISOU 1944  N   ALA A 194    12608  27589  11704   4276  -1185   1239       N  
ATOM   1945  CA  ALA A 194      92.015  -7.633  39.292  1.00134.01           C  
ANISOU 1945  CA  ALA A 194    12529  26815  11575   4010  -1084   1222       C  
ATOM   1946  C   ALA A 194      91.577  -7.418  37.849  1.00136.47           C  
ANISOU 1946  C   ALA A 194    12884  26770  12199   3739   -963   1263       C  
ATOM   1947  O   ALA A 194      92.373  -7.007  36.999  1.00135.99           O  
ANISOU 1947  O   ALA A 194    12575  26840  12257   3580  -1005   1193       O  
ATOM   1948  CB  ALA A 194      91.906  -6.324  40.053  1.00135.36           C  
ANISOU 1948  CB  ALA A 194    12578  27097  11756   3738  -1228    983       C  
ATOM   1949  N   CYS A 195      90.291  -7.706  37.588  1.00132.14           N  
ANISOU 1949  N   CYS A 195    12653  25770  11783   3693   -810   1379       N  
ATOM   1950  CA  CYS A 195      89.615  -7.504  36.306  1.00129.96           C  
ANISOU 1950  CA  CYS A 195    12477  25103  11799   3445   -700   1417       C  
ATOM   1951  C   CYS A 195      89.180  -6.046  36.236  1.00132.27           C  
ANISOU 1951  C   CYS A 195    12670  25303  12282   3038   -751   1215       C  
ATOM   1952  O   CYS A 195      88.061  -5.713  36.629  1.00131.23           O  
ANISOU 1952  O   CYS A 195    12718  24927  12217   2921   -704   1196       O  
ATOM   1953  CB  CYS A 195      88.444  -8.479  36.168  1.00129.16           C  
ANISOU 1953  CB  CYS A 195    12736  24588  11751   3566   -539   1612       C  
ATOM   1954  SG  CYS A 195      87.429  -8.253  34.680  1.00130.21           S  
ANISOU 1954  SG  CYS A 195    13022  24217  12235   3273   -427   1650       S  
ATOM   1955  N   ILE A 196      90.116  -5.157  35.859  1.00128.55           N  
ANISOU 1955  N   ILE A 196    11907  25062  11875   2837   -848   1060       N  
ATOM   1956  CA  ILE A 196      89.875  -3.710  35.852  1.00127.40           C  
ANISOU 1956  CA  ILE A 196    11663  24864  11880   2454   -903    851       C  
ATOM   1957  C   ILE A 196      89.537  -3.192  34.444  1.00128.10           C  
ANISOU 1957  C   ILE A 196    11766  24656  12248   2184   -809    840       C  
ATOM   1958  O   ILE A 196      89.528  -3.949  33.477  1.00126.35           O  
ANISOU 1958  O   ILE A 196    11617  24292  12100   2296   -717    986       O  
ATOM   1959  CB  ILE A 196      91.100  -2.927  36.406  1.00133.34           C  
ANISOU 1959  CB  ILE A 196    12078  26066  12518   2363  -1085    654       C  
ATOM   1960  CG1 ILE A 196      92.343  -3.047  35.471  1.00134.72           C  
ANISOU 1960  CG1 ILE A 196    11959  26491  12738   2366  -1107    662       C  
ATOM   1961  CG2 ILE A 196      91.407  -3.325  37.851  1.00136.80           C  
ANISOU 1961  CG2 ILE A 196    12512  26804  12662   2631  -1202    638       C  
ATOM   1962  CD1 ILE A 196      93.461  -2.068  35.761  1.00143.91           C  
ANISOU 1962  CD1 ILE A 196    12756  28048  13875   2169  -1274    449       C  
ATOM   1963  N   MET A 197      89.293  -1.877  34.355  1.00123.86           N  
ANISOU 1963  N   MET A 197    11177  24035  11850   1841   -837    659       N  
ATOM   1964  CA  MET A 197      89.037  -1.136  33.130  1.00122.04           C  
ANISOU 1964  CA  MET A 197    10954  23549  11868   1555   -760    606       C  
ATOM   1965  C   MET A 197      90.384  -0.531  32.682  1.00127.99           C  
ANISOU 1965  C   MET A 197    11380  24603  12648   1418   -824    492       C  
ATOM   1966  O   MET A 197      90.686   0.619  33.006  1.00128.42           O  
ANISOU 1966  O   MET A 197    11286  24778  12731   1153   -903    297       O  
ATOM   1967  CB  MET A 197      87.941  -0.086  33.414  1.00123.16           C  
ANISOU 1967  CB  MET A 197    11247  23438  12109   1295   -743    481       C  
ATOM   1968  CG  MET A 197      87.252   0.468  32.189  1.00124.62           C  
ANISOU 1968  CG  MET A 197    11541  23270  12539   1057   -636    462       C  
ATOM   1969  SD  MET A 197      86.079  -0.650  31.397  1.00126.02           S  
ANISOU 1969  SD  MET A 197    12009  23024  12848   1207   -497    679       S  
ATOM   1970  CE  MET A 197      85.413   0.432  30.153  1.00120.78           C  
ANISOU 1970  CE  MET A 197    11424  22033  12435    886   -419    576       C  
ATOM   1971  N   ALA A 198      91.235  -1.361  32.033  1.00125.99           N  
ANISOU 1971  N   ALA A 198    11012  24490  12368   1617   -791    621       N  
ATOM   1972  CA  ALA A 198      92.625  -1.060  31.649  1.00128.62           C  
ANISOU 1972  CA  ALA A 198    11003  25160  12707   1561   -836    561       C  
ATOM   1973  C   ALA A 198      92.728   0.062  30.608  1.00134.20           C  
ANISOU 1973  C   ALA A 198    11637  25702  13650   1210   -762    454       C  
ATOM   1974  O   ALA A 198      93.033  -0.189  29.435  1.00133.13           O  
ANISOU 1974  O   ALA A 198    11505  25451  13628   1241   -647    554       O  
ATOM   1975  CB  ALA A 198      93.298  -2.311  31.100  1.00129.80           C  
ANISOU 1975  CB  ALA A 198    11114  25433  12770   1901   -781    762       C  
ATOM   1976  N   PHE A 199      92.588   1.308  31.069  1.00133.15           N  
ANISOU 1976  N   PHE A 199    11436  25582  13574    892   -828    247       N  
ATOM   1977  CA  PHE A 199      92.750   2.483  30.217  1.00133.67           C  
ANISOU 1977  CA  PHE A 199    11428  25516  13846    543   -758    125       C  
ATOM   1978  C   PHE A 199      94.235   2.794  30.014  1.00142.15           C  
ANISOU 1978  C   PHE A 199    12105  26971  14933    461   -800     67       C  
ATOM   1979  O   PHE A 199      95.033   2.329  30.831  1.00144.12           O  
ANISOU 1979  O   PHE A 199    12130  27616  15014    636   -929     70       O  
ATOM   1980  CB  PHE A 199      92.037   3.700  30.827  1.00135.36           C  
ANISOU 1980  CB  PHE A 199    11745  25587  14098    237   -808    -75       C  
ATOM   1981  CG  PHE A 199      90.564   3.587  31.130  1.00134.68           C  
ANISOU 1981  CG  PHE A 199    12011  25159  14003    284   -769    -38       C  
ATOM   1982  CD1 PHE A 199      89.634   3.479  30.099  1.00135.22           C  
ANISOU 1982  CD1 PHE A 199    12334  24818  14227    271   -621     58       C  
ATOM   1983  CD2 PHE A 199      90.088   3.816  32.417  1.00137.49           C  
ANISOU 1983  CD2 PHE A 199    12436  25591  14211    294   -879   -128       C  
ATOM   1984  CE1 PHE A 199      88.263   3.478  30.368  1.00134.05           C  
ANISOU 1984  CE1 PHE A 199    12472  24368  14091    284   -586     82       C  
ATOM   1985  CE2 PHE A 199      88.718   3.824  32.684  1.00138.25           C  
ANISOU 1985  CE2 PHE A 199    12838  25374  14315    318   -824    -94       C  
ATOM   1986  CZ  PHE A 199      87.814   3.674  31.656  1.00133.75           C  
ANISOU 1986  CZ  PHE A 199    12486  24419  13912    301   -677      9       C  
ATOM   1987  N   PRO A 200      94.658   3.604  28.997  1.00140.51           N  
ANISOU 1987  N   PRO A 200    11789  26679  14919    194   -696      6       N  
ATOM   1988  CA  PRO A 200      96.087   3.953  28.898  1.00144.16           C  
ANISOU 1988  CA  PRO A 200    11833  27532  15407     88   -736    -56       C  
ATOM   1989  C   PRO A 200      96.546   4.647  30.188  1.00152.28           C  
ANISOU 1989  C   PRO A 200    12637  28892  16332    -86   -947   -268       C  
ATOM   1990  O   PRO A 200      95.861   5.560  30.642  1.00151.12           O  
ANISOU 1990  O   PRO A 200    12647  28562  16209   -332   -992   -430       O  
ATOM   1991  CB  PRO A 200      96.143   4.876  27.672  1.00145.35           C  
ANISOU 1991  CB  PRO A 200    11995  27435  15797   -210   -563    -98       C  
ATOM   1992  CG  PRO A 200      94.908   4.583  26.904  1.00146.01           C  
ANISOU 1992  CG  PRO A 200    12495  27031  15950   -128   -424      8       C  
ATOM   1993  CD  PRO A 200      93.876   4.272  27.935  1.00140.03           C  
ANISOU 1993  CD  PRO A 200    11967  26180  15057    -21   -537    -12       C  
ATOM   1994  N   PRO A 201      97.608   4.150  30.869  1.00153.22           N  
ANISOU 1994  N   PRO A 201    12422  29489  16304     79  -1093   -266       N  
ATOM   1995  CA  PRO A 201      97.993   4.739  32.169  1.00156.21           C  
ANISOU 1995  CA  PRO A 201    12611  30185  16557    -57  -1327   -477       C  
ATOM   1996  C   PRO A 201      98.383   6.222  32.074  1.00162.44           C  
ANISOU 1996  C   PRO A 201    13226  30981  17515   -547  -1358   -713       C  
ATOM   1997  O   PRO A 201      98.100   6.975  33.010  1.00162.71           O  
ANISOU 1997  O   PRO A 201    13307  31035  17480   -740  -1512   -914       O  
ATOM   1998  CB  PRO A 201      99.202   3.899  32.600  1.00161.12           C  
ANISOU 1998  CB  PRO A 201    12871  31327  17020    227  -1449   -406       C  
ATOM   1999  CG  PRO A 201      99.698   3.249  31.351  1.00164.95           C  
ANISOU 1999  CG  PRO A 201    13270  31792  17610    384  -1258   -199       C  
ATOM   2000  CD  PRO A 201      98.483   3.016  30.513  1.00156.19           C  
ANISOU 2000  CD  PRO A 201    12598  30144  16602    421  -1060    -73       C  
ATOM   2001  N   GLU A 202      99.003   6.648  30.943  1.00160.03           N  
ANISOU 2001  N   GLU A 202    12749  30632  17424   -745  -1201   -687       N  
ATOM   2002  CA  GLU A 202      99.418   8.043  30.720  1.00161.74           C  
ANISOU 2002  CA  GLU A 202    12811  30819  17823  -1225  -1190   -894       C  
ATOM   2003  C   GLU A 202      98.174   8.965  30.609  1.00162.28           C  
ANISOU 2003  C   GLU A 202    13297  30393  17967  -1468  -1108   -999       C  
ATOM   2004  O   GLU A 202      98.263  10.175  30.841  1.00163.94           O  
ANISOU 2004  O   GLU A 202    13482  30547  18259  -1855  -1150  -1212       O  
ATOM   2005  CB  GLU A 202     100.319   8.191  29.465  1.00164.30           C  
ANISOU 2005  CB  GLU A 202    12878  31191  18359  -1341   -999   -805       C  
ATOM   2006  CG  GLU A 202      99.742   7.732  28.122  1.00171.79           C  
ANISOU 2006  CG  GLU A 202    14103  31751  19417  -1179   -730   -591       C  
ATOM   2007  CD  GLU A 202      99.630   6.244  27.831  1.00187.95           C  
ANISOU 2007  CD  GLU A 202    16238  33837  21335   -688   -681   -334       C  
ATOM   2008  OE1 GLU A 202     100.089   5.426  28.662  1.00183.94           O  
ANISOU 2008  OE1 GLU A 202    15556  33694  20638   -420   -843   -293       O  
ATOM   2009  OE2 GLU A 202      99.152   5.900  26.726  1.00175.95           O  
ANISOU 2009  OE2 GLU A 202    14961  31989  19902   -568   -479   -175       O  
ATOM   2010  N   LYS A 203      97.023   8.359  30.258  1.00153.60           N  
ANISOU 2010  N   LYS A 203    12582  28944  16837  -1227   -993   -845       N  
ATOM   2011  CA  LYS A 203      95.728   9.009  30.119  1.00149.94           C  
ANISOU 2011  CA  LYS A 203    12530  28013  16426  -1361   -902   -895       C  
ATOM   2012  C   LYS A 203      94.664   8.184  30.860  1.00149.97           C  
ANISOU 2012  C   LYS A 203    12822  27905  16253  -1045   -964   -801       C  
ATOM   2013  O   LYS A 203      93.753   7.648  30.226  1.00146.46           O  
ANISOU 2013  O   LYS A 203    12645  27156  15849   -859   -827   -637       O  
ATOM   2014  CB  LYS A 203      95.380   9.180  28.624  1.00150.13           C  
ANISOU 2014  CB  LYS A 203    12721  27671  16652  -1419   -646   -783       C  
ATOM   2015  N   TYR A 204      94.816   8.016  32.197  1.00146.79           N  
ANISOU 2015  N   TYR A 204    12357  27762  15654   -969  -1171   -898       N  
ATOM   2016  CA  TYR A 204      93.888   7.174  32.948  1.00144.05           C  
ANISOU 2016  CA  TYR A 204    12266  27334  15133   -656  -1216   -797       C  
ATOM   2017  C   TYR A 204      92.763   8.018  33.587  1.00147.60           C  
ANISOU 2017  C   TYR A 204    13028  27505  15549   -815  -1234   -929       C  
ATOM   2018  O   TYR A 204      91.612   7.582  33.577  1.00144.09           O  
ANISOU 2018  O   TYR A 204    12888  26775  15086   -648  -1145   -812       O  
ATOM   2019  CB  TYR A 204      94.627   6.367  34.033  1.00146.45           C  
ANISOU 2019  CB  TYR A 204    12352  28085  15207   -391  -1411   -786       C  
ATOM   2020  CG  TYR A 204      93.827   5.192  34.552  1.00144.52           C  
ANISOU 2020  CG  TYR A 204    12349  27764  14797      5  -1399   -608       C  
ATOM   2021  CD1 TYR A 204      93.929   3.937  33.959  1.00144.84           C  
ANISOU 2021  CD1 TYR A 204    12400  27803  14828    322  -1298   -374       C  
ATOM   2022  CD2 TYR A 204      92.962   5.335  35.633  1.00144.37           C  
ANISOU 2022  CD2 TYR A 204    12563  27662  14628     65  -1476   -669       C  
ATOM   2023  CE1 TYR A 204      93.174   2.860  34.413  1.00143.27           C  
ANISOU 2023  CE1 TYR A 204    12442  27503  14490    663  -1272   -209       C  
ATOM   2024  CE2 TYR A 204      92.214   4.259  36.107  1.00143.36           C  
ANISOU 2024  CE2 TYR A 204    12658  27449  14363    417  -1440   -495       C  
ATOM   2025  CZ  TYR A 204      92.318   3.026  35.488  1.00147.56           C  
ANISOU 2025  CZ  TYR A 204    13198  27965  14903    702  -1337   -268       C  
ATOM   2026  OH  TYR A 204      91.582   1.959  35.930  1.00145.08           O  
ANISOU 2026  OH  TYR A 204    13116  27544  14463   1029  -1289    -95       O  
ATOM   2027  N   ALA A 205      93.102   9.200  34.159  1.00147.32           N  
ANISOU 2027  N   ALA A 205    12917  27555  15503  -1132  -1348  -1169       N  
ATOM   2028  CA  ALA A 205      92.151  10.092  34.844  1.00146.80           C  
ANISOU 2028  CA  ALA A 205    13147  27251  15378  -1281  -1374  -1311       C  
ATOM   2029  C   ALA A 205      91.085  10.650  33.884  1.00148.33           C  
ANISOU 2029  C   ALA A 205    13646  26967  15746  -1418  -1158  -1270       C  
ATOM   2030  O   ALA A 205      89.937  10.821  34.299  1.00146.22           O  
ANISOU 2030  O   ALA A 205    13688  26449  15420  -1370  -1123  -1269       O  
ATOM   2031  CB  ALA A 205      92.892  11.244  35.499  1.00150.96           C  
ANISOU 2031  CB  ALA A 205    13521  27970  15866  -1609  -1543  -1582       C  
ATOM   2032  N   GLN A 206      91.461  10.945  32.620  1.00144.94           N  
ANISOU 2032  N   GLN A 206    13130  26421  15521  -1574  -1011  -1235       N  
ATOM   2033  CA  GLN A 206      90.527  11.469  31.622  1.00142.31           C  
ANISOU 2033  CA  GLN A 206    13075  25649  15349  -1687   -806  -1196       C  
ATOM   2034  C   GLN A 206      89.514  10.375  31.198  1.00142.55           C  
ANISOU 2034  C   GLN A 206    13323  25455  15385  -1360   -702   -966       C  
ATOM   2035  O   GLN A 206      88.307  10.643  31.115  1.00140.43           O  
ANISOU 2035  O   GLN A 206    13358  24857  15143  -1356   -614   -947       O  
ATOM   2036  CB  GLN A 206      91.236  12.063  30.373  1.00144.54           C  
ANISOU 2036  CB  GLN A 206    13212  25871  15834  -1921   -668  -1216       C  
ATOM   2037  CG  GLN A 206      92.528  11.404  29.811  1.00165.96           C  
ANISOU 2037  CG  GLN A 206    15550  28907  18600  -1847   -676  -1127       C  
ATOM   2038  CD  GLN A 206      93.800  11.814  30.534  1.00188.93           C  
ANISOU 2038  CD  GLN A 206    18097  32228  21460  -2039   -851  -1294       C  
ATOM   2039  OE1 GLN A 206      93.964  11.581  31.741  1.00186.01           O  
ANISOU 2039  OE1 GLN A 206    17653  32111  20910  -1957  -1054  -1373       O  
ATOM   2040  NE2 GLN A 206      94.797  12.264  29.777  1.00181.91           N  
ANISOU 2040  NE2 GLN A 206    16943  31449  20725  -2257   -777  -1328       N  
ATOM   2041  N   TRP A 207      90.014   9.151  30.971  1.00138.09           N  
ANISOU 2041  N   TRP A 207    12600  25077  14791  -1089   -717   -797       N  
ATOM   2042  CA  TRP A 207      89.213   7.998  30.586  1.00134.79           C  
ANISOU 2042  CA  TRP A 207    12358  24479  14378   -784   -636   -578       C  
ATOM   2043  C   TRP A 207      88.249   7.567  31.684  1.00136.34           C  
ANISOU 2043  C   TRP A 207    12747  24630  14425   -596   -701   -539       C  
ATOM   2044  O   TRP A 207      87.108   7.225  31.375  1.00133.58           O  
ANISOU 2044  O   TRP A 207    12647  23978  14130   -491   -603   -427       O  
ATOM   2045  CB  TRP A 207      90.110   6.822  30.230  1.00134.29           C  
ANISOU 2045  CB  TRP A 207    12078  24659  14287   -543   -649   -423       C  
ATOM   2046  CG  TRP A 207      90.486   6.767  28.787  1.00134.67           C  
ANISOU 2046  CG  TRP A 207    12078  24586  14506   -587   -504   -345       C  
ATOM   2047  CD1 TRP A 207      91.672   7.137  28.227  1.00139.67           C  
ANISOU 2047  CD1 TRP A 207    12443  25410  15217   -746   -479   -402       C  
ATOM   2048  CD2 TRP A 207      89.630   6.393  27.707  1.00131.81           C  
ANISOU 2048  CD2 TRP A 207    11958  23864  14259   -482   -357   -203       C  
ATOM   2049  NE1 TRP A 207      91.625   6.966  26.866  1.00137.82           N  
ANISOU 2049  NE1 TRP A 207    12281  24956  15127   -716   -311   -288       N  
ATOM   2050  CE2 TRP A 207      90.376   6.523  26.517  1.00136.29           C  
ANISOU 2050  CE2 TRP A 207    12410  24421  14954   -555   -245   -173       C  
ATOM   2051  CE3 TRP A 207      88.298   5.955  27.628  1.00130.43           C  
ANISOU 2051  CE3 TRP A 207    12082  23379  14095   -331   -313    -97       C  
ATOM   2052  CZ2 TRP A 207      89.836   6.229  25.264  1.00133.55           C  
ANISOU 2052  CZ2 TRP A 207    12262  23756  14723   -463   -101    -49       C  
ATOM   2053  CZ3 TRP A 207      87.764   5.662  26.385  1.00129.87           C  
ANISOU 2053  CZ3 TRP A 207    12185  23005  14153   -262   -187     18       C  
ATOM   2054  CH2 TRP A 207      88.523   5.814  25.221  1.00130.99           C  
ANISOU 2054  CH2 TRP A 207    12234  23134  14401   -321    -87     37       C  
ATOM   2055  N   SER A 208      88.701   7.562  32.951  1.00134.00           N  
ANISOU 2055  N   SER A 208    12336  24635  13943   -546   -862   -625       N  
ATOM   2056  CA  SER A 208      87.875   7.169  34.093  1.00133.06           C  
ANISOU 2056  CA  SER A 208    12396  24501  13659   -348   -915   -585       C  
ATOM   2057  C   SER A 208      86.712   8.137  34.278  1.00134.88           C  
ANISOU 2057  C   SER A 208    12907  24415  13925   -504   -849   -667       C  
ATOM   2058  O   SER A 208      85.603   7.702  34.580  1.00132.34           O  
ANISOU 2058  O   SER A 208    12802  23911  13571   -331   -789   -553       O  
ATOM   2059  CB  SER A 208      88.713   7.104  35.363  1.00139.48           C  
ANISOU 2059  CB  SER A 208    13030  25712  14256   -279  -1111   -690       C  
ATOM   2060  OG  SER A 208      89.756   6.157  35.215  1.00149.62           O  
ANISOU 2060  OG  SER A 208    14054  27305  15490    -95  -1168   -600       O  
ATOM   2061  N   ALA A 209      86.960   9.443  34.053  1.00132.38           N  
ANISOU 2061  N   ALA A 209    12592  24026  13681   -826   -845   -855       N  
ATOM   2062  CA  ALA A 209      85.950  10.495  34.146  1.00131.32           C  
ANISOU 2062  CA  ALA A 209    12732  23591  13572   -986   -773   -948       C  
ATOM   2063  C   ALA A 209      84.983  10.433  32.960  1.00132.09           C  
ANISOU 2063  C   ALA A 209    13015  23316  13857   -981   -586   -825       C  
ATOM   2064  O   ALA A 209      83.787  10.643  33.138  1.00130.23           O  
ANISOU 2064  O   ALA A 209    13028  22830  13625   -950   -511   -800       O  
ATOM   2065  CB  ALA A 209      86.621  11.860  34.204  1.00134.30           C  
ANISOU 2065  CB  ALA A 209    13057  24016  13956  -1332   -829  -1191       C  
ATOM   2066  N   GLY A 210      85.511  10.118  31.778  1.00127.92           N  
ANISOU 2066  N   GLY A 210    12363  22766  13475   -994   -517   -749       N  
ATOM   2067  CA  GLY A 210      84.744  10.027  30.540  1.00125.08           C  
ANISOU 2067  CA  GLY A 210    12164  22073  13287   -978   -361   -641       C  
ATOM   2068  C   GLY A 210      83.754   8.879  30.467  1.00125.94           C  
ANISOU 2068  C   GLY A 210    12402  22040  13409   -697   -320   -436       C  
ATOM   2069  O   GLY A 210      82.592   9.093  30.111  1.00123.70           O  
ANISOU 2069  O   GLY A 210    12337  21460  13203   -686   -230   -392       O  
ATOM   2070  N   ILE A 211      84.203   7.647  30.789  1.00122.35           N  
ANISOU 2070  N   ILE A 211    11814  21795  12878   -466   -386   -308       N  
ATOM   2071  CA  ILE A 211      83.364   6.441  30.747  1.00120.47           C  
ANISOU 2071  CA  ILE A 211    11690  21435  12650   -202   -350   -105       C  
ATOM   2072  C   ILE A 211      82.342   6.486  31.926  1.00125.64           C  
ANISOU 2072  C   ILE A 211    12503  22030  13205   -124   -360    -94       C  
ATOM   2073  O   ILE A 211      81.249   5.940  31.779  1.00123.90           O  
ANISOU 2073  O   ILE A 211    12437  21589  13052     -1   -288     42       O  
ATOM   2074  CB  ILE A 211      84.236   5.146  30.763  1.00124.10           C  
ANISOU 2074  CB  ILE A 211    11979  22144  13031     25   -407     21       C  
ATOM   2075  CG1 ILE A 211      85.169   5.096  29.523  1.00124.66           C  
ANISOU 2075  CG1 ILE A 211    11908  22252  13205    -26   -370     34       C  
ATOM   2076  CG2 ILE A 211      83.402   3.857  30.856  1.00123.15           C  
ANISOU 2076  CG2 ILE A 211    11995  21899  12898    295   -373    226       C  
ATOM   2077  CD1 ILE A 211      84.471   5.100  28.082  1.00128.49           C  
ANISOU 2077  CD1 ILE A 211    12564  22374  13881    -44   -245    116       C  
ATOM   2078  N   ALA A 212      82.660   7.188  33.042  1.00124.63           N  
ANISOU 2078  N   ALA A 212    12344  22084  12925   -203   -444   -239       N  
ATOM   2079  CA  ALA A 212      81.713   7.355  34.157  1.00124.58           C  
ANISOU 2079  CA  ALA A 212    12506  22019  12808   -124   -439   -235       C  
ATOM   2080  C   ALA A 212      80.517   8.217  33.714  1.00126.99           C  
ANISOU 2080  C   ALA A 212    13027  21988  13233   -248   -322   -257       C  
ATOM   2081  O   ALA A 212      79.379   7.906  34.072  1.00125.74           O  
ANISOU 2081  O   ALA A 212    13018  21677  13080   -116   -254   -145       O  
ATOM   2082  CB  ALA A 212      82.403   7.974  35.367  1.00127.79           C  
ANISOU 2082  CB  ALA A 212    12849  22691  13014   -185   -569   -404       C  
ATOM   2083  N   LEU A 213      80.777   9.268  32.892  1.00123.22           N  
ANISOU 2083  N   LEU A 213    12564  21398  12855   -490   -289   -392       N  
ATOM   2084  CA  LEU A 213      79.733  10.126  32.320  1.00121.55           C  
ANISOU 2084  CA  LEU A 213    12561  20870  12751   -595   -173   -418       C  
ATOM   2085  C   LEU A 213      78.875   9.340  31.314  1.00122.04           C  
ANISOU 2085  C   LEU A 213    12686  20701  12984   -467    -85   -240       C  
ATOM   2086  O   LEU A 213      77.669   9.571  31.249  1.00121.05           O  
ANISOU 2086  O   LEU A 213    12725  20354  12915   -428     -6   -186       O  
ATOM   2087  CB  LEU A 213      80.319  11.388  31.644  1.00122.49           C  
ANISOU 2087  CB  LEU A 213    12691  20925  12925   -873   -148   -600       C  
ATOM   2088  CG  LEU A 213      80.468  12.692  32.486  1.00129.50           C  
ANISOU 2088  CG  LEU A 213    13681  21842  13683  -1061   -181   -804       C  
ATOM   2089  CD1 LEU A 213      79.110  13.249  32.930  1.00129.03           C  
ANISOU 2089  CD1 LEU A 213    13889  21544  13592  -1013    -92   -791       C  
ATOM   2090  CD2 LEU A 213      81.380  12.524  33.672  1.00134.33           C  
ANISOU 2090  CD2 LEU A 213    14153  22777  14110  -1043   -336   -885       C  
ATOM   2091  N   MET A 214      79.487   8.388  30.567  1.00116.78           N  
ANISOU 2091  N   MET A 214    11887  20093  12389   -391   -104   -146       N  
ATOM   2092  CA  MET A 214      78.791   7.509  29.614  1.00114.29           C  
ANISOU 2092  CA  MET A 214    11630  19573  12221   -260    -49     20       C  
ATOM   2093  C   MET A 214      77.743   6.666  30.348  1.00115.43           C  
ANISOU 2093  C   MET A 214    11846  19667  12346    -67    -38    173       C  
ATOM   2094  O   MET A 214      76.625   6.517  29.859  1.00113.56           O  
ANISOU 2094  O   MET A 214    11724  19189  12236    -23     23    264       O  
ATOM   2095  CB  MET A 214      79.802   6.604  28.872  1.00117.03           C  
ANISOU 2095  CB  MET A 214    11831  20037  12600   -188    -83     87       C  
ATOM   2096  CG  MET A 214      79.165   5.594  27.914  1.00119.30           C  
ANISOU 2096  CG  MET A 214    12197  20113  13017    -43    -47    252       C  
ATOM   2097  SD  MET A 214      80.390   4.504  27.138  1.00124.16           S  
ANISOU 2097  SD  MET A 214    12670  20879  13625     83    -81    341       S  
ATOM   2098  CE  MET A 214      79.314   3.404  26.243  1.00119.05           C  
ANISOU 2098  CE  MET A 214    12194  19922  13117    245    -50    519       C  
ATOM   2099  N   LYS A 215      78.103   6.157  31.539  1.00111.72           N  
ANISOU 2099  N   LYS A 215    11307  19428  11716     46    -95    198       N  
ATOM   2100  CA  LYS A 215      77.231   5.343  32.392  1.00110.80           C  
ANISOU 2100  CA  LYS A 215    11255  19288  11556    236    -66    348       C  
ATOM   2101  C   LYS A 215      75.979   6.117  32.804  1.00112.42           C  
ANISOU 2101  C   LYS A 215    11613  19315  11786    195     14    334       C  
ATOM   2102  O   LYS A 215      74.875   5.583  32.718  1.00110.82           O  
ANISOU 2102  O   LYS A 215    11483  18938  11684    291     84    478       O  
ATOM   2103  CB  LYS A 215      77.991   4.878  33.654  1.00115.20           C  
ANISOU 2103  CB  LYS A 215    11725  20147  11900    368   -141    348       C  
ATOM   2104  CG  LYS A 215      79.234   4.045  33.369  1.00126.75           C  
ANISOU 2104  CG  LYS A 215    13027  21818  13315    455   -216    382       C  
ATOM   2105  CD  LYS A 215      79.955   3.672  34.644  1.00135.25           C  
ANISOU 2105  CD  LYS A 215    14018  23209  14163    597   -302    365       C  
ATOM   2106  CE  LYS A 215      81.177   2.845  34.357  1.00143.62           C  
ANISOU 2106  CE  LYS A 215    14911  24493  15164    711   -372    408       C  
ATOM   2107  NZ  LYS A 215      81.848   2.418  35.608  1.00151.71           N  
ANISOU 2107  NZ  LYS A 215    15856  25836  15951    883   -463    397       N  
ATOM   2108  N   ASN A 216      76.159   7.388  33.224  1.00108.39           N  
ANISOU 2108  N   ASN A 216    11151  18845  11188     48      4    161       N  
ATOM   2109  CA  ASN A 216      75.094   8.268  33.704  1.00107.06           C  
ANISOU 2109  CA  ASN A 216    11145  18533  11002     17     82    127       C  
ATOM   2110  C   ASN A 216      74.144   8.689  32.576  1.00107.20           C  
ANISOU 2110  C   ASN A 216    11257  18263  11210    -48    168    156       C  
ATOM   2111  O   ASN A 216      72.936   8.561  32.748  1.00106.24           O  
ANISOU 2111  O   ASN A 216    11218  18001  11149     42    248    264       O  
ATOM   2112  CB  ASN A 216      75.689   9.520  34.366  1.00106.97           C  
ANISOU 2112  CB  ASN A 216    11180  18629  10833   -136     36    -85       C  
ATOM   2113  CG  ASN A 216      76.460   9.262  35.646  1.00117.34           C  
ANISOU 2113  CG  ASN A 216    12429  20225  11928    -66    -66   -139       C  
ATOM   2114  OD1 ASN A 216      77.313  10.061  36.047  1.00113.21           O  
ANISOU 2114  OD1 ASN A 216    11896  19832  11286   -211   -147   -326       O  
ATOM   2115  ND2 ASN A 216      76.200   8.135  36.310  1.00101.71           N  
ANISOU 2115  ND2 ASN A 216    10414  18345   9888    158    -67     17       N  
ATOM   2116  N   ILE A 217      74.678   9.176  31.439  1.00101.70           N  
ANISOU 2116  N   ILE A 217    10547  17489  10606   -194    157     62       N  
ATOM   2117  CA  ILE A 217      73.895   9.658  30.298  1.00 99.57           C  
ANISOU 2117  CA  ILE A 217    10383  16955  10495   -250    228     64       C  
ATOM   2118  C   ILE A 217      73.126   8.492  29.611  1.00101.17           C  
ANISOU 2118  C   ILE A 217    10558  17017  10864   -115    237    247       C  
ATOM   2119  O   ILE A 217      71.904   8.557  29.509  1.00100.17           O  
ANISOU 2119  O   ILE A 217    10510  16724  10828    -62    295    321       O  
ATOM   2120  CB  ILE A 217      74.811  10.386  29.270  1.00102.51           C  
ANISOU 2120  CB  ILE A 217    10753  17293  10905   -425    223    -79       C  
ATOM   2121  CG1 ILE A 217      75.559  11.565  29.929  1.00104.63           C  
ANISOU 2121  CG1 ILE A 217    11050  17681  11024   -595    211   -270       C  
ATOM   2122  CG2 ILE A 217      73.996  10.870  28.058  1.00101.78           C  
ANISOU 2122  CG2 ILE A 217    10795  16921  10957   -451    297    -76       C  
ATOM   2123  CD1 ILE A 217      76.659  12.221  29.054  1.00113.05           C  
ANISOU 2123  CD1 ILE A 217    12077  18753  12125   -790    213   -408       C  
ATOM   2124  N   LEU A 218      73.839   7.455  29.143  1.00 96.67           N  
ANISOU 2124  N   LEU A 218     9882  16514  10334    -61    177    316       N  
ATOM   2125  CA  LEU A 218      73.268   6.342  28.375  1.00 95.04           C  
ANISOU 2125  CA  LEU A 218     9674  16157  10281     47    169    470       C  
ATOM   2126  C   LEU A 218      72.452   5.363  29.251  1.00 98.66           C  
ANISOU 2126  C   LEU A 218    10115  16624  10745    191    188    634       C  
ATOM   2127  O   LEU A 218      71.457   4.816  28.773  1.00 97.21           O  
ANISOU 2127  O   LEU A 218     9966  16257  10713    241    207    747       O  
ATOM   2128  CB  LEU A 218      74.420   5.572  27.686  1.00 95.00           C  
ANISOU 2128  CB  LEU A 218     9583  16233  10279     77    107    491       C  
ATOM   2129  CG  LEU A 218      74.089   4.464  26.679  1.00 98.41           C  
ANISOU 2129  CG  LEU A 218    10050  16485  10858    170     83    617       C  
ATOM   2130  CD1 LEU A 218      73.337   5.011  25.473  1.00 97.61           C  
ANISOU 2130  CD1 LEU A 218    10060  16135  10894    100    102    563       C  
ATOM   2131  CD2 LEU A 218      75.355   3.802  26.188  1.00100.20           C  
ANISOU 2131  CD2 LEU A 218    10201  16834  11036    231     35    642       C  
ATOM   2132  N   GLY A 219      72.889   5.135  30.491  1.00 96.44           N  
ANISOU 2132  N   GLY A 219     9785  16554  10303    257    183    647       N  
ATOM   2133  CA  GLY A 219      72.258   4.165  31.385  1.00 96.53           C  
ANISOU 2133  CA  GLY A 219     9791  16587  10297    409    222    810       C  
ATOM   2134  C   GLY A 219      71.239   4.680  32.383  1.00100.17           C  
ANISOU 2134  C   GLY A 219    10317  17024  10719    441    311    839       C  
ATOM   2135  O   GLY A 219      70.559   3.873  33.027  1.00100.29           O  
ANISOU 2135  O   GLY A 219    10333  17022  10751    566    371    995       O  
ATOM   2136  N   PHE A 220      71.116   6.016  32.541  1.00 95.85           N  
ANISOU 2136  N   PHE A 220     9838  16467  10113    338    334    697       N  
ATOM   2137  CA  PHE A 220      70.145   6.551  33.492  1.00 95.50           C  
ANISOU 2137  CA  PHE A 220     9875  16398  10013    394    430    730       C  
ATOM   2138  C   PHE A 220      69.446   7.800  32.926  1.00 97.74           C  
ANISOU 2138  C   PHE A 220    10257  16522  10356    290    479    633       C  
ATOM   2139  O   PHE A 220      68.227   7.772  32.795  1.00 96.41           O  
ANISOU 2139  O   PHE A 220    10114  16209  10310    340    558    735       O  
ATOM   2140  CB  PHE A 220      70.810   6.879  34.845  1.00 98.70           C  
ANISOU 2140  CB  PHE A 220    10308  17025  10167    448    415    661       C  
ATOM   2141  CG  PHE A 220      69.851   7.296  35.939  1.00100.76           C  
ANISOU 2141  CG  PHE A 220    10672  17272  10342    554    525    722       C  
ATOM   2142  CD1 PHE A 220      69.132   6.345  36.656  1.00103.99           C  
ANISOU 2142  CD1 PHE A 220    11064  17675  10772    726    612    922       C  
ATOM   2143  CD2 PHE A 220      69.715   8.634  36.294  1.00103.17           C  
ANISOU 2143  CD2 PHE A 220    11106  17567  10527    492    552    584       C  
ATOM   2144  CE1 PHE A 220      68.254   6.729  37.672  1.00106.01           C  
ANISOU 2144  CE1 PHE A 220    11416  17921  10944    842    735    994       C  
ATOM   2145  CE2 PHE A 220      68.839   9.017  37.312  1.00106.97           C  
ANISOU 2145  CE2 PHE A 220    11700  18035  10909    617    664    649       C  
ATOM   2146  CZ  PHE A 220      68.114   8.061  37.994  1.00105.70           C  
ANISOU 2146  CZ  PHE A 220    11505  17876  10778    797    759    859       C  
ATOM   2147  N   ILE A 221      70.203   8.876  32.596  1.00 94.63           N  
ANISOU 2147  N   ILE A 221     9920  16157   9879    149    439    441       N  
ATOM   2148  CA  ILE A 221      69.665  10.164  32.133  1.00 94.79           C  
ANISOU 2148  CA  ILE A 221    10074  16029   9912     59    497    332       C  
ATOM   2149  C   ILE A 221      68.716   9.955  30.924  1.00 98.42           C  
ANISOU 2149  C   ILE A 221    10535  16269  10591     69    526    410       C  
ATOM   2150  O   ILE A 221      67.527  10.243  31.066  1.00 98.35           O  
ANISOU 2150  O   ILE A 221    10582  16153  10632    136    608    476       O  
ATOM   2151  CB  ILE A 221      70.785  11.191  31.779  1.00 98.46           C  
ANISOU 2151  CB  ILE A 221    10593  16539  10280   -120    450    119       C  
ATOM   2152  CG1 ILE A 221      71.779  11.429  32.962  1.00100.97           C  
ANISOU 2152  CG1 ILE A 221    10894  17089  10381   -149    388     17       C  
ATOM   2153  CG2 ILE A 221      70.208  12.515  31.251  1.00 98.91           C  
ANISOU 2153  CG2 ILE A 221    10825  16413  10341   -202    529     12       C  
ATOM   2154  CD1 ILE A 221      71.178  11.949  34.337  1.00112.53           C  
ANISOU 2154  CD1 ILE A 221    12486  18603  11669    -55    443     18       C  
ATOM   2155  N   ILE A 222      69.225   9.457  29.768  1.00 94.07           N  
ANISOU 2155  N   ILE A 222     9924  15658  10162     19    456    404       N  
ATOM   2156  CA  ILE A 222      68.426   9.256  28.541  1.00 92.52           C  
ANISOU 2156  CA  ILE A 222     9743  15252  10158     34    454    458       C  
ATOM   2157  C   ILE A 222      67.232   8.281  28.827  1.00 96.25           C  
ANISOU 2157  C   ILE A 222    10139  15666  10765    156    476    650       C  
ATOM   2158  O   ILE A 222      66.098   8.706  28.600  1.00 95.57           O  
ANISOU 2158  O   ILE A 222    10091  15457  10765    187    529    683       O  
ATOM   2159  CB  ILE A 222      69.287   8.757  27.336  1.00 94.37           C  
ANISOU 2159  CB  ILE A 222     9944  15438  10474    -15    372    426       C  
ATOM   2160  CG1 ILE A 222      70.304   9.846  26.914  1.00 94.73           C  
ANISOU 2160  CG1 ILE A 222    10060  15514  10420   -151    381    244       C  
ATOM   2161  CG2 ILE A 222      68.392   8.350  26.144  1.00 93.60           C  
ANISOU 2161  CG2 ILE A 222     9873  15123  10568     29    347    491       C  
ATOM   2162  CD1 ILE A 222      71.270   9.454  25.827  1.00103.65           C  
ANISOU 2162  CD1 ILE A 222    11156  16619  11608   -190    326    216       C  
ATOM   2163  N   PRO A 223      67.409   7.031  29.345  1.00 93.16           N  
ANISOU 2163  N   PRO A 223     9645  15358  10394    226    449    782       N  
ATOM   2164  CA  PRO A 223      66.226   6.174  29.570  1.00 93.36           C  
ANISOU 2164  CA  PRO A 223     9603  15300  10569    313    488    964       C  
ATOM   2165  C   PRO A 223      65.217   6.790  30.550  1.00 98.31           C  
ANISOU 2165  C   PRO A 223    10252  15947  11153    376    611   1017       C  
ATOM   2166  O   PRO A 223      64.020   6.629  30.333  1.00 98.35           O  
ANISOU 2166  O   PRO A 223    10212  15838  11317    412    654   1122       O  
ATOM   2167  CB  PRO A 223      66.812   4.885  30.149  1.00 95.45           C  
ANISOU 2167  CB  PRO A 223     9795  15668  10805    379    462   1076       C  
ATOM   2168  CG  PRO A 223      68.186   5.224  30.564  1.00 99.95           C  
ANISOU 2168  CG  PRO A 223    10381  16425  11170    356    423    956       C  
ATOM   2169  CD  PRO A 223      68.656   6.312  29.681  1.00 94.68           C  
ANISOU 2169  CD  PRO A 223     9776  15712  10484    236    387    779       C  
ATOM   2170  N   LEU A 224      65.685   7.527  31.587  1.00 95.29           N  
ANISOU 2170  N   LEU A 224     9942  15708  10557    391    662    941       N  
ATOM   2171  CA  LEU A 224      64.791   8.158  32.563  1.00 95.86           C  
ANISOU 2171  CA  LEU A 224    10069  15799  10556    476    789    989       C  
ATOM   2172  C   LEU A 224      63.997   9.285  31.879  1.00 97.69           C  
ANISOU 2172  C   LEU A 224    10379  15892  10848    447    830    923       C  
ATOM   2173  O   LEU A 224      62.831   9.453  32.215  1.00 97.77           O  
ANISOU 2173  O   LEU A 224    10369  15852  10927    535    928   1034       O  
ATOM   2174  CB  LEU A 224      65.569   8.683  33.801  1.00 97.16           C  
ANISOU 2174  CB  LEU A 224    10327  16137  10453    503    811    900       C  
ATOM   2175  CG  LEU A 224      64.787   9.176  35.059  1.00103.07           C  
ANISOU 2175  CG  LEU A 224    11166  16927  11071    630    947    961       C  
ATOM   2176  CD1 LEU A 224      64.391  10.642  34.977  1.00103.65           C  
ANISOU 2176  CD1 LEU A 224    11394  16920  11068    599   1003    840       C  
ATOM   2177  CD2 LEU A 224      63.667   8.218  35.474  1.00104.94           C  
ANISOU 2177  CD2 LEU A 224    11301  17133  11440    765   1057   1199       C  
ATOM   2178  N   ILE A 225      64.594  10.005  30.887  1.00 92.47           N  
ANISOU 2178  N   ILE A 225     9802  15166  10167    338    765    756       N  
ATOM   2179  CA  ILE A 225      63.880  11.051  30.132  1.00 91.53           C  
ANISOU 2179  CA  ILE A 225     9783  14904  10091    328    804    687       C  
ATOM   2180  C   ILE A 225      62.641  10.411  29.493  1.00 94.49           C  
ANISOU 2180  C   ILE A 225    10040  15159  10703    393    798    830       C  
ATOM   2181  O   ILE A 225      61.541  10.910  29.707  1.00 94.92           O  
ANISOU 2181  O   ILE A 225    10106  15172  10788    477    886    888       O  
ATOM   2182  CB  ILE A 225      64.772  11.779  29.079  1.00 93.77           C  
ANISOU 2182  CB  ILE A 225    10177  15118  10333    203    743    500       C  
ATOM   2183  CG1 ILE A 225      65.875  12.613  29.779  1.00 95.08           C  
ANISOU 2183  CG1 ILE A 225    10461  15396  10270    116    760    346       C  
ATOM   2184  CG2 ILE A 225      63.918  12.686  28.176  1.00 94.11           C  
ANISOU 2184  CG2 ILE A 225    10329  14990  10439    227    784    453       C  
ATOM   2185  CD1 ILE A 225      66.918  13.316  28.838  1.00102.70           C  
ANISOU 2185  CD1 ILE A 225    11519  16309  11193    -37    719    163       C  
ATOM   2186  N   PHE A 226      62.814   9.264  28.796  1.00 89.51           N  
ANISOU 2186  N   PHE A 226     9292  14486  10232    361    694    893       N  
ATOM   2187  CA  PHE A 226      61.731   8.504  28.163  1.00 88.89           C  
ANISOU 2187  CA  PHE A 226     9091  14290  10391    394    655   1018       C  
ATOM   2188  C   PHE A 226      60.690   8.016  29.175  1.00 94.87           C  
ANISOU 2188  C   PHE A 226     9727  15093  11224    480    758   1202       C  
ATOM   2189  O   PHE A 226      59.500   8.244  28.962  1.00 95.99           O  
ANISOU 2189  O   PHE A 226     9810  15170  11494    529    796   1267       O  
ATOM   2190  CB  PHE A 226      62.290   7.291  27.408  1.00 89.58           C  
ANISOU 2190  CB  PHE A 226     9112  14327  10597    343    524   1048       C  
ATOM   2191  CG  PHE A 226      62.972   7.606  26.102  1.00 89.51           C  
ANISOU 2191  CG  PHE A 226     9199  14222  10591    284    423    907       C  
ATOM   2192  CD1 PHE A 226      64.296   8.024  26.073  1.00 91.82           C  
ANISOU 2192  CD1 PHE A 226     9583  14589  10718    225    417    776       C  
ATOM   2193  CD2 PHE A 226      62.311   7.421  24.893  1.00 90.75           C  
ANISOU 2193  CD2 PHE A 226     9346  14214  10919    292    329    911       C  
ATOM   2194  CE1 PHE A 226      64.930   8.303  24.861  1.00 91.80           C  
ANISOU 2194  CE1 PHE A 226     9667  14490  10721    178    349    662       C  
ATOM   2195  CE2 PHE A 226      62.944   7.698  23.682  1.00 92.45           C  
ANISOU 2195  CE2 PHE A 226     9673  14332  11123    263    248    790       C  
ATOM   2196  CZ  PHE A 226      64.251   8.134  23.672  1.00 90.25           C  
ANISOU 2196  CZ  PHE A 226     9488  14122  10681    209    272    674       C  
ATOM   2197  N   ILE A 227      61.133   7.358  30.269  1.00 91.86           N  
ANISOU 2197  N   ILE A 227     9310  14830  10761    511    811   1290       N  
ATOM   2198  CA  ILE A 227      60.256   6.791  31.302  1.00 93.17           C  
ANISOU 2198  CA  ILE A 227     9372  15039  10990    600    935   1483       C  
ATOM   2199  C   ILE A 227      59.423   7.922  31.973  1.00 98.55           C  
ANISOU 2199  C   ILE A 227    10111  15758  11576    697   1081   1493       C  
ATOM   2200  O   ILE A 227      58.209   7.753  32.136  1.00 98.80           O  
ANISOU 2200  O   ILE A 227    10028  15755  11756    760   1167   1636       O  
ATOM   2201  CB  ILE A 227      61.080   5.986  32.353  1.00 96.79           C  
ANISOU 2201  CB  ILE A 227     9830  15619  11326    638    966   1553       C  
ATOM   2202  CG1 ILE A 227      61.834   4.813  31.663  1.00 96.42           C  
ANISOU 2202  CG1 ILE A 227     9737  15528  11369    568    832   1559       C  
ATOM   2203  CG2 ILE A 227      60.169   5.453  33.474  1.00 99.08           C  
ANISOU 2203  CG2 ILE A 227    10036  15942  11667    746   1126   1764       C  
ATOM   2204  CD1 ILE A 227      62.821   4.032  32.538  1.00104.52           C  
ANISOU 2204  CD1 ILE A 227    10784  16684  12246    619    839   1599       C  
ATOM   2205  N   ALA A 228      60.060   9.067  32.320  1.00 95.64           N  
ANISOU 2205  N   ALA A 228     9920  15454  10965    706   1108   1343       N  
ATOM   2206  CA  ALA A 228      59.381  10.199  32.967  1.00 96.46           C  
ANISOU 2206  CA  ALA A 228    10133  15582  10934    811   1247   1336       C  
ATOM   2207  C   ALA A 228      58.390  10.870  32.021  1.00 99.13           C  
ANISOU 2207  C   ALA A 228    10463  15806  11394    830   1253   1318       C  
ATOM   2208  O   ALA A 228      57.262  11.123  32.435  1.00100.11           O  
ANISOU 2208  O   ALA A 228    10544  15938  11556    951   1379   1436       O  
ATOM   2209  CB  ALA A 228      60.392  11.223  33.457  1.00 97.31           C  
ANISOU 2209  CB  ALA A 228    10456  15757  10759    785   1245   1154       C  
ATOM   2210  N   THR A 229      58.794  11.133  30.753  1.00 93.18           N  
ANISOU 2210  N   THR A 229     9752  14954  10700    732   1125   1180       N  
ATOM   2211  CA  THR A 229      57.945  11.785  29.749  1.00 92.45           C  
ANISOU 2211  CA  THR A 229     9672  14749  10705    766   1110   1144       C  
ATOM   2212  C   THR A 229      56.720  10.911  29.454  1.00 97.27           C  
ANISOU 2212  C   THR A 229    10043  15327  11586    808   1095   1320       C  
ATOM   2213  O   THR A 229      55.619  11.450  29.332  1.00 97.93           O  
ANISOU 2213  O   THR A 229    10087  15395  11727    910   1162   1374       O  
ATOM   2214  CB  THR A 229      58.734  12.084  28.468  1.00 95.30           C  
ANISOU 2214  CB  THR A 229    10139  15006  11062    660    978    968       C  
ATOM   2215  OG1 THR A 229      59.890  12.851  28.802  1.00 91.70           O  
ANISOU 2215  OG1 THR A 229     9880  14588  10374    597   1002    811       O  
ATOM   2216  CG2 THR A 229      57.905  12.843  27.428  1.00 93.73           C  
ANISOU 2216  CG2 THR A 229     9990  14689  10934    723    962    919       C  
ATOM   2217  N   CYS A 230      56.898   9.573  29.382  1.00 93.35           N  
ANISOU 2217  N   CYS A 230     9390  14826  11254    732   1015   1415       N  
ATOM   2218  CA  CYS A 230      55.785   8.662  29.128  1.00 94.04           C  
ANISOU 2218  CA  CYS A 230     9246  14871  11615    736    993   1579       C  
ATOM   2219  C   CYS A 230      54.856   8.610  30.346  1.00101.13           C  
ANISOU 2219  C   CYS A 230    10031  15863  12529    843   1183   1767       C  
ATOM   2220  O   CYS A 230      53.661   8.418  30.152  1.00101.78           O  
ANISOU 2220  O   CYS A 230     9925  15926  12819    875   1209   1894       O  
ATOM   2221  CB  CYS A 230      56.277   7.270  28.753  1.00 93.46           C  
ANISOU 2221  CB  CYS A 230     9080  14742  11690    623    864   1621       C  
ATOM   2222  SG  CYS A 230      57.107   7.192  27.147  1.00 95.43           S  
ANISOU 2222  SG  CYS A 230     9432  14857  11970    527    643   1439       S  
ATOM   2223  N   TYR A 231      55.377   8.815  31.579  1.00 99.52           N  
ANISOU 2223  N   TYR A 231     9942  15764  12108    907   1315   1786       N  
ATOM   2224  CA  TYR A 231      54.526   8.825  32.769  1.00102.06           C  
ANISOU 2224  CA  TYR A 231    10193  16171  12415   1039   1517   1969       C  
ATOM   2225  C   TYR A 231      53.622  10.049  32.779  1.00109.00           C  
ANISOU 2225  C   TYR A 231    11115  17065  13236   1173   1625   1967       C  
ATOM   2226  O   TYR A 231      52.410   9.897  32.918  1.00109.58           O  
ANISOU 2226  O   TYR A 231    10998  17152  13484   1246   1715   2130       O  
ATOM   2227  CB  TYR A 231      55.330   8.770  34.075  1.00103.86           C  
ANISOU 2227  CB  TYR A 231    10564  16502  12397   1098   1616   1979       C  
ATOM   2228  CG  TYR A 231      54.475   9.076  35.294  1.00107.89           C  
ANISOU 2228  CG  TYR A 231    11076  17093  12824   1278   1844   2140       C  
ATOM   2229  CD1 TYR A 231      53.499   8.182  35.730  1.00111.20           C  
ANISOU 2229  CD1 TYR A 231    11286  17524  13443   1328   1972   2380       C  
ATOM   2230  CD2 TYR A 231      54.648  10.256  36.015  1.00109.39           C  
ANISOU 2230  CD2 TYR A 231    11491  17340  12733   1399   1941   2057       C  
ATOM   2231  CE1 TYR A 231      52.684   8.476  36.823  1.00113.85           C  
ANISOU 2231  CE1 TYR A 231    11620  17932  13705   1511   2204   2545       C  
ATOM   2232  CE2 TYR A 231      53.854  10.550  37.125  1.00112.24           C  
ANISOU 2232  CE2 TYR A 231    11879  17769  13000   1592   2159   2211       C  
ATOM   2233  CZ  TYR A 231      52.877   9.653  37.529  1.00121.32           C  
ANISOU 2233  CZ  TYR A 231    12805  18937  14353   1656   2296   2461       C  
ATOM   2234  OH  TYR A 231      52.092   9.932  38.622  1.00125.37           O  
ANISOU 2234  OH  TYR A 231    13344  19518  14772   1862   2532   2629       O  
ATOM   2235  N   PHE A 232      54.205  11.256  32.658  1.00107.18           N  
ANISOU 2235  N   PHE A 232    11132  16831  12761   1207   1623   1788       N  
ATOM   2236  CA  PHE A 232      53.441  12.500  32.674  1.00109.03           C  
ANISOU 2236  CA  PHE A 232    11466  17068  12894   1355   1733   1772       C  
ATOM   2237  C   PHE A 232      52.606  12.633  31.384  1.00114.57           C  
ANISOU 2237  C   PHE A 232    12038  17691  13802   1348   1634   1754       C  
ATOM   2238  O   PHE A 232      51.591  13.325  31.395  1.00115.42           O  
ANISOU 2238  O   PHE A 232    12124  17821  13911   1497   1733   1813       O  
ATOM   2239  CB  PHE A 232      54.358  13.718  32.868  1.00110.47           C  
ANISOU 2239  CB  PHE A 232    11976  17239  12758   1369   1750   1573       C  
ATOM   2240  CG  PHE A 232      55.030  13.726  34.224  1.00112.82           C  
ANISOU 2240  CG  PHE A 232    12410  17627  12830   1406   1842   1583       C  
ATOM   2241  CD1 PHE A 232      54.325  14.089  35.367  1.00117.75           C  
ANISOU 2241  CD1 PHE A 232    13092  18322  13324   1597   2039   1713       C  
ATOM   2242  CD2 PHE A 232      56.379  13.426  34.352  1.00114.14           C  
ANISOU 2242  CD2 PHE A 232    12656  17815  12896   1268   1729   1460       C  
ATOM   2243  CE1 PHE A 232      54.944  14.092  36.621  1.00119.35           C  
ANISOU 2243  CE1 PHE A 232    13443  18603  13299   1651   2110   1715       C  
ATOM   2244  CE2 PHE A 232      57.000  13.436  35.605  1.00117.69           C  
ANISOU 2244  CE2 PHE A 232    13230  18361  13126   1316   1791   1458       C  
ATOM   2245  CZ  PHE A 232      56.280  13.776  36.730  1.00117.36           C  
ANISOU 2245  CZ  PHE A 232    13263  18377  12951   1508   1976   1580       C  
ATOM   2246  N   GLY A 233      53.000  11.914  30.330  1.00111.01           N  
ANISOU 2246  N   GLY A 233    11500  17159  13521   1196   1441   1687       N  
ATOM   2247  CA  GLY A 233      52.260  11.845  29.076  1.00111.30           C  
ANISOU 2247  CA  GLY A 233    11407  17118  13766   1183   1311   1667       C  
ATOM   2248  C   GLY A 233      50.976  11.061  29.262  1.00118.55           C  
ANISOU 2248  C   GLY A 233    12006  18080  14959   1213   1345   1878       C  
ATOM   2249  O   GLY A 233      49.920  11.471  28.770  1.00119.54           O  
ANISOU 2249  O   GLY A 233    12012  18207  15200   1298   1329   1908       O  
ATOM   2250  N   ILE A 234      51.060   9.938  30.014  1.00116.50           N  
ANISOU 2250  N   ILE A 234    11604  17858  14801   1148   1400   2028       N  
ATOM   2251  CA  ILE A 234      49.920   9.091  30.391  1.00118.64           C  
ANISOU 2251  CA  ILE A 234    11569  18169  15338   1153   1473   2251       C  
ATOM   2252  C   ILE A 234      49.070   9.856  31.422  1.00125.00           C  
ANISOU 2252  C   ILE A 234    12357  19095  16043   1353   1721   2389       C  
ATOM   2253  O   ILE A 234      47.863   9.983  31.233  1.00126.70           O  
ANISOU 2253  O   ILE A 234    12358  19353  16427   1430   1767   2501       O  
ATOM   2254  CB  ILE A 234      50.389   7.697  30.926  1.00121.86           C  
ANISOU 2254  CB  ILE A 234    11882  18555  15862   1022   1471   2363       C  
ATOM   2255  CG1 ILE A 234      51.050   6.864  29.795  1.00120.81           C  
ANISOU 2255  CG1 ILE A 234    11749  18294  15858    843   1221   2248       C  
ATOM   2256  CG2 ILE A 234      49.212   6.918  31.547  1.00125.03           C  
ANISOU 2256  CG2 ILE A 234    11989  18999  16516   1033   1610   2617       C  
ATOM   2257  CD1 ILE A 234      51.723   5.529  30.236  1.00128.14           C  
ANISOU 2257  CD1 ILE A 234    12658  19185  16846    727   1207   2328       C  
ATOM   2258  N   ARG A 235      49.723  10.413  32.471  1.00121.44           N  
ANISOU 2258  N   ARG A 235    12138  18700  15302   1447   1870   2370       N  
ATOM   2259  CA  ARG A 235      49.116  11.200  33.555  1.00122.98           C  
ANISOU 2259  CA  ARG A 235    12398  18997  15333   1662   2115   2486       C  
ATOM   2260  C   ARG A 235      48.270  12.352  32.982  1.00127.84           C  
ANISOU 2260  C   ARG A 235    13042  19626  15905   1812   2141   2441       C  
ATOM   2261  O   ARG A 235      47.209  12.643  33.524  1.00129.57           O  
ANISOU 2261  O   ARG A 235    13145  19934  16154   1985   2322   2609       O  
ATOM   2262  CB  ARG A 235      50.228  11.743  34.478  1.00122.56           C  
ANISOU 2262  CB  ARG A 235    12666  18968  14935   1709   2189   2389       C  
ATOM   2263  CG  ARG A 235      49.793  12.560  35.697  1.00135.19           C  
ANISOU 2263  CG  ARG A 235    14407  20654  16305   1941   2436   2489       C  
ATOM   2264  CD  ARG A 235      51.016  12.915  36.533  1.00145.46           C  
ANISOU 2264  CD  ARG A 235    16014  21968  17285   1948   2451   2368       C  
ATOM   2265  NE  ARG A 235      50.713  13.784  37.673  1.00156.19           N  
ANISOU 2265  NE  ARG A 235    17579  23389  18377   2177   2663   2426       N  
ATOM   2266  CZ  ARG A 235      50.824  15.110  37.659  1.00170.08           C  
ANISOU 2266  CZ  ARG A 235    19621  25121  19879   2271   2688   2279       C  
ATOM   2267  NH1 ARG A 235      51.237  15.736  36.562  1.00155.45           N  
ANISOU 2267  NH1 ARG A 235    17875  23182  18007   2152   2526   2068       N  
ATOM   2268  NH2 ARG A 235      50.536  15.819  38.742  1.00157.85           N  
ANISOU 2268  NH2 ARG A 235    18276  23618  18081   2491   2883   2343       N  
ATOM   2269  N   LYS A 236      48.713  12.957  31.861  1.00122.98           N  
ANISOU 2269  N   LYS A 236    12577  18925  15224   1760   1970   2228       N  
ATOM   2270  CA  LYS A 236      48.018  14.050  31.176  1.00123.18           C  
ANISOU 2270  CA  LYS A 236    12665  18945  15191   1909   1975   2163       C  
ATOM   2271  C   LYS A 236      46.687  13.578  30.573  1.00127.94           C  
ANISOU 2271  C   LYS A 236    12909  19595  16107   1944   1932   2301       C  
ATOM   2272  O   LYS A 236      45.660  14.210  30.811  1.00128.89           O  
ANISOU 2272  O   LYS A 236    12958  19805  16208   2146   2073   2406       O  
ATOM   2273  CB  LYS A 236      48.914  14.635  30.062  1.00123.93           C  
ANISOU 2273  CB  LYS A 236    13003  18916  15168   1822   1796   1906       C  
ATOM   2274  CG  LYS A 236      48.305  15.827  29.308  1.00139.04           C  
ANISOU 2274  CG  LYS A 236    15031  20804  16996   1988   1799   1822       C  
ATOM   2275  CD  LYS A 236      49.110  16.239  28.064  1.00148.09           C  
ANISOU 2275  CD  LYS A 236    16383  21809  18075   1895   1619   1590       C  
ATOM   2276  CE  LYS A 236      49.116  15.194  26.960  1.00157.25           C  
ANISOU 2276  CE  LYS A 236    17319  22910  19519   1740   1386   1571       C  
ATOM   2277  NZ  LYS A 236      49.914  15.638  25.787  1.00164.49           N  
ANISOU 2277  NZ  LYS A 236    18457  23687  20355   1681   1235   1358       N  
ATOM   2278  N   HIS A 237      46.719  12.479  29.786  1.00124.34           N  
ANISOU 2278  N   HIS A 237    12234  19080  15931   1751   1729   2294       N  
ATOM   2279  CA  HIS A 237      45.570  11.937  29.056  1.00125.88           C  
ANISOU 2279  CA  HIS A 237    12084  19300  16446   1733   1620   2382       C  
ATOM   2280  C   HIS A 237      44.484  11.413  30.022  1.00131.97           C  
ANISOU 2280  C   HIS A 237    12529  20199  17413   1792   1809   2655       C  
ATOM   2281  O   HIS A 237      43.298  11.517  29.706  1.00133.47           O  
ANISOU 2281  O   HIS A 237    12439  20463  17809   1856   1789   2747       O  
ATOM   2282  CB  HIS A 237      46.018  10.812  28.105  1.00125.72           C  
ANISOU 2282  CB  HIS A 237    11961  19159  16647   1494   1359   2302       C  
ATOM   2283  CG  HIS A 237      44.979  10.422  27.094  1.00130.61           C  
ANISOU 2283  CG  HIS A 237    12297  19772  17555   1463   1176   2316       C  
ATOM   2284  ND1 HIS A 237      44.030   9.447  27.364  1.00134.50           N  
ANISOU 2284  ND1 HIS A 237    12418  20309  18377   1361   1168   2498       N  
ATOM   2285  CD2 HIS A 237      44.769  10.900  25.844  1.00132.03           C  
ANISOU 2285  CD2 HIS A 237    12529  19906  17732   1521    994   2164       C  
ATOM   2286  CE1 HIS A 237      43.284   9.360  26.273  1.00134.71           C  
ANISOU 2286  CE1 HIS A 237    12268  20323  18594   1351    961   2441       C  
ATOM   2287  NE2 HIS A 237      43.690  10.214  25.331  1.00133.61           N  
ANISOU 2287  NE2 HIS A 237    12379  20132  18256   1460    849   2242       N  
ATOM   2288  N   LEU A 238      44.875  10.874  31.186  1.00128.62           N  
ANISOU 2288  N   LEU A 238    12139  19808  16923   1782   1995   2785       N  
ATOM   2289  CA  LEU A 238      43.901  10.371  32.161  1.00131.03           C  
ANISOU 2289  CA  LEU A 238    12157  20222  17405   1844   2208   3058       C  
ATOM   2290  C   LEU A 238      43.244  11.506  32.962  1.00135.91           C  
ANISOU 2290  C   LEU A 238    12875  20965  17799   2135   2477   3162       C  
ATOM   2291  O   LEU A 238      42.059  11.383  33.263  1.00138.37           O  
ANISOU 2291  O   LEU A 238    12900  21389  18284   2240   2629   3373       O  
ATOM   2292  CB  LEU A 238      44.521   9.365  33.153  1.00131.11           C  
ANISOU 2292  CB  LEU A 238    12147  20198  17469   1712   2295   3177       C  
ATOM   2293  CG  LEU A 238      44.679   7.879  32.734  1.00135.61           C  
ANISOU 2293  CG  LEU A 238    12508  20665  18354   1440   2110   3194       C  
ATOM   2294  CD1 LEU A 238      43.337   7.207  32.468  1.00138.35           C  
ANISOU 2294  CD1 LEU A 238    12432  21049  19086   1374   2081   3347       C  
ATOM   2295  CD2 LEU A 238      45.618   7.686  31.571  1.00135.18           C  
ANISOU 2295  CD2 LEU A 238    12634  20482  18247   1294   1825   2945       C  
ATOM   2296  N   LEU A 239      44.007  12.546  33.373  1.00130.46           N  
ANISOU 2296  N   LEU A 239    12582  20253  16734   2263   2541   3022       N  
ATOM   2297  CA  LEU A 239      43.470  13.640  34.191  1.00131.68           C  
ANISOU 2297  CA  LEU A 239    12879  20505  16647   2554   2795   3113       C  
ATOM   2298  C   LEU A 239      42.575  14.585  33.359  1.00136.28           C  
ANISOU 2298  C   LEU A 239    13403  21142  17237   2728   2770   3082       C  
ATOM   2299  O   LEU A 239      41.641  15.155  33.932  1.00138.10           O  
ANISOU 2299  O   LEU A 239    13585  21489  17398   2979   2989   3240       O  
ATOM   2300  CB  LEU A 239      44.583  14.459  34.880  1.00130.33           C  
ANISOU 2300  CB  LEU A 239    13172  20282  16066   2629   2867   2968       C  
ATOM   2301  CG  LEU A 239      45.402  13.755  35.986  1.00134.35           C  
ANISOU 2301  CG  LEU A 239    13790  20775  16482   2543   2934   3008       C  
ATOM   2302  CD1 LEU A 239      46.531  14.637  36.468  1.00133.34           C  
ANISOU 2302  CD1 LEU A 239    14110  20607  15945   2621   2972   2837       C  
ATOM   2303  CD2 LEU A 239      44.530  13.344  37.169  1.00139.43           C  
ANISOU 2303  CD2 LEU A 239    14229  21521  17227   2669   3191   3303       C  
ATOM   2304  N   LYS A 240      42.831  14.738  32.029  1.00130.84           N  
ANISOU 2304  N   LYS A 240    12723  20371  16619   2620   2513   2888       N  
ATOM   2305  CA  LYS A 240      41.991  15.600  31.180  1.00131.38           C  
ANISOU 2305  CA  LYS A 240    12744  20488  16688   2796   2465   2846       C  
ATOM   2306  C   LYS A 240      40.605  14.930  30.994  1.00138.20           C  
ANISOU 2306  C   LYS A 240    13100  21488  17920   2812   2464   3054       C  
ATOM   2307  O   LYS A 240      39.588  15.629  30.936  1.00139.82           O  
ANISOU 2307  O   LYS A 240    13196  21819  18111   3052   2565   3144       O  
ATOM   2308  CB  LYS A 240      42.651  15.933  29.818  1.00131.34           C  
ANISOU 2308  CB  LYS A 240    12926  20345  16633   2694   2199   2578       C  
ATOM   2309  CG  LYS A 240      42.951  14.743  28.897  1.00140.70           C  
ANISOU 2309  CG  LYS A 240    13910  21441  18108   2406   1926   2507       C  
ATOM   2310  CD  LYS A 240      43.561  15.147  27.533  1.00146.17           C  
ANISOU 2310  CD  LYS A 240    14816  21996  18724   2350   1686   2252       C  
ATOM   2311  CE  LYS A 240      44.935  15.781  27.610  1.00150.18           C  
ANISOU 2311  CE  LYS A 240    15774  22382  18905   2319   1712   2062       C  
ATOM   2312  NZ  LYS A 240      45.470  16.112  26.264  1.00153.63           N  
ANISOU 2312  NZ  LYS A 240    16399  22682  19293   2269   1504   1838       N  
ATOM   2313  N   THR A 241      40.574  13.576  30.967  1.00134.93           N  
ANISOU 2313  N   THR A 241    12383  21052  17832   2559   2361   3137       N  
ATOM   2314  CA  THR A 241      39.339  12.796  30.908  1.00137.43           C  
ANISOU 2314  CA  THR A 241    12202  21486  18530   2518   2365   3342       C  
ATOM   2315  C   THR A 241      38.739  12.814  32.318  1.00143.24           C  
ANISOU 2315  C   THR A 241    12826  22348  19251   2666   2709   3615       C  
ATOM   2316  O   THR A 241      39.352  12.288  33.252  1.00142.83           O  
ANISOU 2316  O   THR A 241    12847  22244  19178   2564   2825   3694       O  
ATOM   2317  CB  THR A 241      39.628  11.388  30.365  1.00144.50           C  
ANISOU 2317  CB  THR A 241    12877  22274  19752   2183   2127   3309       C  
ATOM   2318  N   ASN A 242      37.594  13.492  32.494  1.00141.24           N  
ANISOU 2318  N   ASN A 242    12438  22259  18966   2942   2887   3756       N  
ATOM   2319  CA  ASN A 242      36.984  13.662  33.812  1.00143.01           C  
ANISOU 2319  CA  ASN A 242    12597  22610  19131   3145   3243   4022       C  
ATOM   2320  C   ASN A 242      36.409  12.332  34.354  1.00148.20           C  
ANISOU 2320  C   ASN A 242    12819  23313  20177   2961   3334   4270       C  
ATOM   2321  O   ASN A 242      35.412  11.813  33.843  1.00149.70           O  
ANISOU 2321  O   ASN A 242    12561  23589  20728   2868   3246   4366       O  
ATOM   2322  CB  ASN A 242      35.882  14.723  33.764  1.00145.85           C  
ANISOU 2322  CB  ASN A 242    12880  23144  19394   3489   3396   4122       C  
ATOM   2323  CG  ASN A 242      35.229  15.035  35.095  1.00168.33           C  
ANISOU 2323  CG  ASN A 242    15687  26125  22147   3748   3782   4403       C  
ATOM   2324  OD1 ASN A 242      34.039  15.312  35.160  1.00162.49           O  
ANISOU 2324  OD1 ASN A 242    14646  25568  21524   3953   3927   4594       O  
ATOM   2325  ND2 ASN A 242      35.967  14.941  36.195  1.00161.17           N  
ANISOU 2325  ND2 ASN A 242    15060  25139  21039   3751   3959   4447       N  
ATOM   2326  N   SER A 243      37.048  11.817  35.420  1.00144.02           N  
ANISOU 2326  N   SER A 243    12440  22721  19558   2916   3516   4368       N  
ATOM   2327  CA  SER A 243      36.653  10.608  36.146  1.00145.67           C  
ANISOU 2327  CA  SER A 243    12342  22944  20064   2772   3672   4616       C  
ATOM   2328  C   SER A 243      36.148  10.996  37.546  1.00151.23           C  
ANISOU 2328  C   SER A 243    13105  23757  20597   3060   4078   4873       C  
ATOM   2329  O   SER A 243      36.730  11.893  38.162  1.00149.23           O  
ANISOU 2329  O   SER A 243    13281  23480  19940   3266   4193   4799       O  
ATOM   2330  CB  SER A 243      37.822   9.632  36.223  1.00146.75           C  
ANISOU 2330  CB  SER A 243    12633  22899  20225   2488   3531   4509       C  
ATOM   2331  N   TYR A 244      35.056  10.361  38.040  1.00151.30           N  
ANISOU 2331  N   TYR A 244    12691  23887  20908   3086   4299   5173       N  
ATOM   2332  CA  TYR A 244      34.475  10.769  39.326  1.00154.08           C  
ANISOU 2332  CA  TYR A 244    13071  24359  21113   3399   4708   5445       C  
ATOM   2333  C   TYR A 244      33.760   9.614  40.091  1.00161.63           C  
ANISOU 2333  C   TYR A 244    13658  25345  22410   3295   4959   5767       C  
ATOM   2334  O   TYR A 244      33.707   9.665  41.324  1.00162.24           O  
ANISOU 2334  O   TYR A 244    13900  25432  22314   3484   5281   5955       O  
ATOM   2335  CB  TYR A 244      33.460  11.914  39.113  1.00157.58           C  
ANISOU 2335  CB  TYR A 244    13385  24995  21493   3711   4811   5520       C  
ATOM   2336  CG  TYR A 244      32.492  11.721  37.959  1.00160.65           C  
ANISOU 2336  CG  TYR A 244    13293  25488  22260   3579   4593   5506       C  
ATOM   2337  CD1 TYR A 244      32.820  12.140  36.671  1.00160.42           C  
ANISOU 2337  CD1 TYR A 244    13366  25412  22176   3506   4243   5214       C  
ATOM   2338  CD2 TYR A 244      31.215  11.212  38.171  1.00165.04           C  
ANISOU 2338  CD2 TYR A 244    13294  26196  23216   3545   4744   5787       C  
ATOM   2339  CE1 TYR A 244      31.925  11.999  35.613  1.00162.53           C  
ANISOU 2339  CE1 TYR A 244    13208  25781  22767   3409   4025   5190       C  
ATOM   2340  CE2 TYR A 244      30.308  11.068  37.120  1.00167.41           C  
ANISOU 2340  CE2 TYR A 244    13138  26607  23862   3423   4521   5763       C  
ATOM   2341  CZ  TYR A 244      30.668  11.466  35.842  1.00171.81           C  
ANISOU 2341  CZ  TYR A 244    13820  27116  24342   3365   4152   5459       C  
ATOM   2342  OH  TYR A 244      29.785  11.333  34.797  1.00173.55           O  
ANISOU 2342  OH  TYR A 244    13610  27449  24882   3266   3912   5422       O  
ATOM   2343  N   GLY A 245      33.211   8.628  39.383  1.00160.20           N  
ANISOU 2343  N   GLY A 245    13005  25171  22693   3008   4819   5828       N  
ATOM   2344  CA  GLY A 245      32.516   7.509  40.019  1.00163.35           C  
ANISOU 2344  CA  GLY A 245    13033  25580  23453   2871   5052   6130       C  
ATOM   2345  C   GLY A 245      33.405   6.296  40.196  1.00166.38           C  
ANISOU 2345  C   GLY A 245    13540  25751  23925   2568   4968   6081       C  
ATOM   2346  O   GLY A 245      34.438   6.373  40.870  1.00164.03           O  
ANISOU 2346  O   GLY A 245    13686  25349  23290   2649   5021   6000       O  
ATOM   2347  N   LYS A 246      33.008   5.161  39.579  1.00164.26           N  
ANISOU 2347  N   LYS A 246    12882  25420  24111   2220   4829   6129       N  
ATOM   2348  CA  LYS A 246      33.779   3.909  39.553  1.00162.68           C  
ANISOU 2348  CA  LYS A 246    12760  25003  24047   1901   4716   6080       C  
ATOM   2349  C   LYS A 246      35.022   4.135  38.685  1.00161.61           C  
ANISOU 2349  C   LYS A 246    12993  24735  23677   1793   4332   5714       C  
ATOM   2350  O   LYS A 246      36.098   3.622  38.992  1.00158.83           O  
ANISOU 2350  O   LYS A 246    12950  24227  23171   1702   4294   5630       O  
ATOM   2351  CB  LYS A 246      32.885   2.746  39.033  1.00168.17           C  
ANISOU 2351  CB  LYS A 246    12927  25670  25301   1560   4649   6215       C  
ATOM   2352  CG  LYS A 246      33.525   1.341  38.914  1.00180.54           C  
ANISOU 2352  CG  LYS A 246    14533  26995  27067   1201   4528   6182       C  
ATOM   2353  CD  LYS A 246      34.388   1.134  37.651  1.00184.79           C  
ANISOU 2353  CD  LYS A 246    15228  27390  27593    966   4056   5838       C  
ATOM   2354  CE  LYS A 246      34.982  -0.250  37.559  1.00192.22           C  
ANISOU 2354  CE  LYS A 246    16218  28093  28722    638   3955   5823       C  
ATOM   2355  NZ  LYS A 246      35.833  -0.402  36.346  1.00196.84           N  
ANISOU 2355  NZ  LYS A 246    16973  28543  29273    445   3511   5500       N  
ATOM   2356  N   ASN A 247      34.862   4.959  37.628  1.00156.92           N  
ANISOU 2356  N   ASN A 247    12372  24213  23037   1834   4067   5506       N  
ATOM   2357  CA  ASN A 247      35.891   5.348  36.667  1.00152.86           C  
ANISOU 2357  CA  ASN A 247    12175  23594  22311   1761   3711   5162       C  
ATOM   2358  C   ASN A 247      37.060   6.076  37.348  1.00153.52           C  
ANISOU 2358  C   ASN A 247    12794  23634  21904   1964   3795   5040       C  
ATOM   2359  O   ASN A 247      38.171   6.033  36.821  1.00150.48           O  
ANISOU 2359  O   ASN A 247    12696  23119  21361   1844   3554   4796       O  
ATOM   2360  CB  ASN A 247      35.284   6.253  35.583  1.00154.43           C  
ANISOU 2360  CB  ASN A 247    12235  23908  22534   1847   3497   5018       C  
ATOM   2361  CG  ASN A 247      34.147   5.641  34.788  1.00183.22           C  
ANISOU 2361  CG  ASN A 247    15351  27614  26650   1649   3351   5093       C  
ATOM   2362  OD1 ASN A 247      33.981   4.417  34.706  1.00179.13           O  
ANISOU 2362  OD1 ASN A 247    14599  26992  26471   1350   3291   5169       O  
ATOM   2363  ND2 ASN A 247      33.371   6.489  34.130  1.00177.16           N  
ANISOU 2363  ND2 ASN A 247    14399  27009  25904   1808   3267   5055       N  
ATOM   2364  N   ARG A 248      36.817   6.746  38.504  1.00150.56           N  
ANISOU 2364  N   ARG A 248    12550  23368  21286   2272   4131   5207       N  
ATOM   2365  CA  ARG A 248      37.865   7.464  39.242  1.00147.93           C  
ANISOU 2365  CA  ARG A 248    12723  23002  20483   2473   4216   5097       C  
ATOM   2366  C   ARG A 248      38.792   6.463  39.920  1.00150.80           C  
ANISOU 2366  C   ARG A 248    13264  23232  20802   2340   4265   5127       C  
ATOM   2367  O   ARG A 248      40.008   6.672  39.952  1.00147.86           O  
ANISOU 2367  O   ARG A 248    13271  22778  20131   2336   4138   4921       O  
ATOM   2368  CB  ARG A 248      37.262   8.436  40.270  1.00149.97           C  
ANISOU 2368  CB  ARG A 248    13074  23407  20502   2851   4558   5278       C  
ATOM   2369  CG  ARG A 248      38.296   9.374  40.884  1.00157.02           C  
ANISOU 2369  CG  ARG A 248    14506  24267  20888   3065   4597   5120       C  
ATOM   2370  CD  ARG A 248      37.682  10.388  41.825  1.00168.35           C  
ANISOU 2370  CD  ARG A 248    16063  25831  22071   3453   4916   5284       C  
ATOM   2371  NE  ARG A 248      38.684  11.348  42.291  1.00175.54           N  
ANISOU 2371  NE  ARG A 248    17506  26696  22494   3635   4906   5092       N  
ATOM   2372  CZ  ARG A 248      38.965  12.496  41.679  1.00189.54           C  
ANISOU 2372  CZ  ARG A 248    19513  28467  24036   3720   4752   4865       C  
ATOM   2373  NH1 ARG A 248      38.312  12.847  40.577  1.00176.95           N  
ANISOU 2373  NH1 ARG A 248    17678  26921  22633   3670   4595   4802       N  
ATOM   2374  NH2 ARG A 248      39.895  13.304  42.167  1.00176.19           N  
ANISOU 2374  NH2 ARG A 248    18308  26721  21917   3857   4752   4697       N  
ATOM   2375  N   ILE A 249      38.214   5.361  40.436  1.00149.47           N  
ANISOU 2375  N   ILE A 249    12812  23042  20937   2230   4450   5383       N  
ATOM   2376  CA  ILE A 249      38.951   4.269  41.075  1.00148.66           C  
ANISOU 2376  CA  ILE A 249    12840  22808  20834   2108   4524   5451       C  
ATOM   2377  C   ILE A 249      39.780   3.553  39.990  1.00149.11           C  
ANISOU 2377  C   ILE A 249    12933  22710  21012   1787   4154   5215       C  
ATOM   2378  O   ILE A 249      40.943   3.230  40.225  1.00146.57           O  
ANISOU 2378  O   ILE A 249    12924  22293  20475   1753   4080   5096       O  
ATOM   2379  CB  ILE A 249      37.977   3.306  41.827  1.00155.53           C  
ANISOU 2379  CB  ILE A 249    13377  23688  22031   2075   4844   5806       C  
ATOM   2380  CG1 ILE A 249      37.060   4.086  42.820  1.00158.56           C  
ANISOU 2380  CG1 ILE A 249    13702  24241  22302   2421   5220   6051       C  
ATOM   2381  CG2 ILE A 249      38.751   2.177  42.534  1.00156.18           C  
ANISOU 2381  CG2 ILE A 249    13631  23621  22090   1977   4947   5887       C  
ATOM   2382  CD1 ILE A 249      35.927   3.258  43.512  1.00169.83           C  
ANISOU 2382  CD1 ILE A 249    14739  25705  24083   2406   5569   6428       C  
ATOM   2383  N   THR A 250      39.188   3.383  38.782  1.00145.34           N  
ANISOU 2383  N   THR A 250    12147  22220  20858   1577   3914   5142       N  
ATOM   2384  CA  THR A 250      39.811   2.748  37.615  1.00142.78           C  
ANISOU 2384  CA  THR A 250    11835  21747  20668   1286   3550   4922       C  
ATOM   2385  C   THR A 250      40.951   3.639  37.073  1.00141.56           C  
ANISOU 2385  C   THR A 250    12060  21574  20152   1358   3312   4609       C  
ATOM   2386  O   THR A 250      41.977   3.104  36.651  1.00139.02           O  
ANISOU 2386  O   THR A 250    11922  21122  19778   1197   3102   4442       O  
ATOM   2387  CB  THR A 250      38.738   2.479  36.533  1.00154.52           C  
ANISOU 2387  CB  THR A 250    12894  23244  22572   1088   3366   4931       C  
ATOM   2388  OG1 THR A 250      37.670   1.723  37.105  1.00157.69           O  
ANISOU 2388  OG1 THR A 250    12930  23676  23308   1019   3614   5231       O  
ATOM   2389  CG2 THR A 250      39.287   1.736  35.313  1.00152.13           C  
ANISOU 2389  CG2 THR A 250    12605  22770  22429    789   2996   4724       C  
ATOM   2390  N   ARG A 251      40.772   4.982  37.098  1.00136.56           N  
ANISOU 2390  N   ARG A 251    11551  21066  19270   1602   3363   4540       N  
ATOM   2391  CA  ARG A 251      41.765   5.950  36.609  1.00132.89           C  
ANISOU 2391  CA  ARG A 251    11443  20584  18467   1676   3172   4255       C  
ATOM   2392  C   ARG A 251      43.024   5.961  37.492  1.00134.62           C  
ANISOU 2392  C   ARG A 251    12052  20760  18339   1747   3246   4190       C  
ATOM   2393  O   ARG A 251      44.137   5.911  36.964  1.00131.42           O  
ANISOU 2393  O   ARG A 251    11870  20267  17797   1635   3022   3966       O  
ATOM   2394  CB  ARG A 251      41.162   7.366  36.561  1.00132.74           C  
ANISOU 2394  CB  ARG A 251    11463  20699  18274   1934   3251   4230       C  
ATOM   2395  CG  ARG A 251      42.066   8.418  35.915  1.00137.88           C  
ANISOU 2395  CG  ARG A 251    12463  21314  18612   1988   3052   3932       C  
ATOM   2396  CD  ARG A 251      41.588   9.826  36.208  1.00145.36           C  
ANISOU 2396  CD  ARG A 251    13550  22374  19307   2284   3200   3930       C  
ATOM   2397  NE  ARG A 251      41.727  10.154  37.631  1.00153.25           N  
ANISOU 2397  NE  ARG A 251    14760  23428  20039   2499   3495   4063       N  
ATOM   2398  CZ  ARG A 251      41.343  11.299  38.184  1.00169.85           C  
ANISOU 2398  CZ  ARG A 251    17045  25617  21874   2786   3677   4092       C  
ATOM   2399  NH1 ARG A 251      40.759  12.238  37.448  1.00160.62           N  
ANISOU 2399  NH1 ARG A 251    15866  24495  20667   2899   3609   4005       N  
ATOM   2400  NH2 ARG A 251      41.521  11.508  39.481  1.00156.28           N  
ANISOU 2400  NH2 ARG A 251    15538  23932  19908   2980   3932   4210       N  
ATOM   2401  N   ASP A 252      42.843   6.058  38.829  1.00132.55           N  
ANISOU 2401  N   ASP A 252    11871  20568  17924   1950   3558   4383       N  
ATOM   2402  CA  ASP A 252      43.938   6.139  39.795  1.00131.13           C  
ANISOU 2402  CA  ASP A 252    12058  20374  17392   2060   3642   4333       C  
ATOM   2403  C   ASP A 252      44.743   4.832  39.856  1.00133.79           C  
ANISOU 2403  C   ASP A 252    12425  20595  17813   1864   3558   4332       C  
ATOM   2404  O   ASP A 252      45.958   4.912  40.034  1.00131.54           O  
ANISOU 2404  O   ASP A 252    12440  20284  17257   1871   3458   4168       O  
ATOM   2405  CB  ASP A 252      43.420   6.491  41.197  1.00135.34           C  
ANISOU 2405  CB  ASP A 252    12660  21003  17759   2346   4004   4563       C  
ATOM   2406  CG  ASP A 252      42.831   7.891  41.329  1.00146.32           C  
ANISOU 2406  CG  ASP A 252    14128  22506  18962   2600   4112   4555       C  
ATOM   2407  OD1 ASP A 252      42.662   8.570  40.288  1.00145.69           O  
ANISOU 2407  OD1 ASP A 252    13979  22436  18940   2550   3926   4404       O  
ATOM   2408  OD2 ASP A 252      42.545   8.310  42.473  1.00154.53           O  
ANISOU 2408  OD2 ASP A 252    15314  23616  19785   2865   4388   4702       O  
ATOM   2409  N   GLN A 253      44.102   3.649  39.671  1.00131.15           N  
ANISOU 2409  N   GLN A 253    11790  20193  17849   1686   3591   4505       N  
ATOM   2410  CA  GLN A 253      44.834   2.372  39.695  1.00130.06           C  
ANISOU 2410  CA  GLN A 253    11702  19928  17788   1509   3520   4511       C  
ATOM   2411  C   GLN A 253      45.762   2.257  38.467  1.00131.00           C  
ANISOU 2411  C   GLN A 253    11925  19955  17895   1311   3154   4231       C  
ATOM   2412  O   GLN A 253      46.836   1.671  38.585  1.00129.55           O  
ANISOU 2412  O   GLN A 253    11942  19705  17575   1258   3072   4149       O  
ATOM   2413  CB  GLN A 253      43.898   1.156  39.770  1.00134.01           C  
ANISOU 2413  CB  GLN A 253    11876  20352  18691   1352   3651   4762       C  
ATOM   2414  CG  GLN A 253      43.145   1.047  41.103  1.00152.52           C  
ANISOU 2414  CG  GLN A 253    14145  22765  21041   1545   4051   5068       C  
ATOM   2415  CD  GLN A 253      42.366  -0.247  41.255  1.00173.49           C  
ANISOU 2415  CD  GLN A 253    16512  25323  24084   1371   4207   5322       C  
ATOM   2416  OE1 GLN A 253      42.813  -1.330  40.864  1.00170.18           O  
ANISOU 2416  OE1 GLN A 253    16063  24751  23845   1128   4054   5283       O  
ATOM   2417  NE2 GLN A 253      41.239  -0.185  41.942  1.00166.11           N  
ANISOU 2417  NE2 GLN A 253    15385  24463  23265   1504   4540   5598       N  
ATOM   2418  N   VAL A 254      45.377   2.857  37.317  1.00126.12           N  
ANISOU 2418  N   VAL A 254    11186  19342  17392   1234   2946   4086       N  
ATOM   2419  CA  VAL A 254      46.209   2.897  36.103  1.00122.77           C  
ANISOU 2419  CA  VAL A 254    10876  18833  16939   1081   2614   3820       C  
ATOM   2420  C   VAL A 254      47.419   3.817  36.381  1.00123.00           C  
ANISOU 2420  C   VAL A 254    11269  18915  16552   1216   2571   3619       C  
ATOM   2421  O   VAL A 254      48.545   3.478  36.011  1.00120.28           O  
ANISOU 2421  O   VAL A 254    11100  18504  16096   1120   2393   3457       O  
ATOM   2422  CB  VAL A 254      45.394   3.347  34.850  1.00126.82           C  
ANISOU 2422  CB  VAL A 254    11169  19339  17677    996   2421   3733       C  
ATOM   2423  CG1 VAL A 254      46.284   3.545  33.625  1.00123.83           C  
ANISOU 2423  CG1 VAL A 254    10955  18873  17219    886   2102   3454       C  
ATOM   2424  CG2 VAL A 254      44.279   2.359  34.536  1.00129.17           C  
ANISOU 2424  CG2 VAL A 254    11095  19582  18403    823   2425   3910       C  
ATOM   2425  N   LEU A 255      47.181   4.944  37.091  1.00119.79           N  
ANISOU 2425  N   LEU A 255    10975  18624  15916   1441   2747   3642       N  
ATOM   2426  CA  LEU A 255      48.219   5.903  37.481  1.00117.93           C  
ANISOU 2426  CA  LEU A 255    11085  18438  15284   1568   2728   3462       C  
ATOM   2427  C   LEU A 255      49.168   5.294  38.511  1.00121.46           C  
ANISOU 2427  C   LEU A 255    11721  18890  15538   1603   2804   3493       C  
ATOM   2428  O   LEU A 255      50.358   5.608  38.477  1.00119.01           O  
ANISOU 2428  O   LEU A 255    11651  18583  14985   1585   2667   3295       O  
ATOM   2429  CB  LEU A 255      47.608   7.199  38.039  1.00119.04           C  
ANISOU 2429  CB  LEU A 255    11315  18685  15232   1809   2914   3499       C  
ATOM   2430  CG  LEU A 255      46.843   8.083  37.050  1.00123.76           C  
ANISOU 2430  CG  LEU A 255    11797  19300  15925   1837   2842   3434       C  
ATOM   2431  CD1 LEU A 255      46.117   9.205  37.769  1.00125.58           C  
ANISOU 2431  CD1 LEU A 255    12122  19636  15958   2110   3075   3521       C  
ATOM   2432  CD2 LEU A 255      47.768   8.649  35.974  1.00122.85           C  
ANISOU 2432  CD2 LEU A 255    11858  19117  15701   1730   2571   3144       C  
ATOM   2433  N   LYS A 256      48.650   4.423  39.418  1.00120.25           N  
ANISOU 2433  N   LYS A 256    11456  18741  15492   1656   3025   3744       N  
ATOM   2434  CA  LYS A 256      49.462   3.723  40.423  1.00120.30           C  
ANISOU 2434  CA  LYS A 256    11635  18751  15322   1718   3116   3803       C  
ATOM   2435  C   LYS A 256      50.432   2.762  39.734  1.00122.32           C  
ANISOU 2435  C   LYS A 256    11912  18911  15652   1515   2890   3690       C  
ATOM   2436  O   LYS A 256      51.600   2.702  40.120  1.00121.07           O  
ANISOU 2436  O   LYS A 256    11977  18783  15242   1557   2832   3586       O  
ATOM   2437  CB  LYS A 256      48.596   2.965  41.449  1.00125.85           C  
ANISOU 2437  CB  LYS A 256    12208  19457  16151   1823   3423   4114       C  
ATOM   2438  CG  LYS A 256      47.810   3.856  42.404  1.00145.89           C  
ANISOU 2438  CG  LYS A 256    14786  22103  18544   2084   3692   4252       C  
ATOM   2439  CD  LYS A 256      46.979   3.024  43.389  1.00160.92           C  
ANISOU 2439  CD  LYS A 256    16554  23999  20588   2187   4017   4579       C  
ATOM   2440  CE  LYS A 256      46.146   3.851  44.351  1.00172.25           C  
ANISOU 2440  CE  LYS A 256    18021  25539  21889   2468   4309   4743       C  
ATOM   2441  NZ  LYS A 256      45.107   4.665  43.659  1.00179.04           N  
ANISOU 2441  NZ  LYS A 256    18656  26448  22924   2461   4299   4751       N  
ATOM   2442  N   MET A 257      49.958   2.047  38.686  1.00118.22           N  
ANISOU 2442  N   MET A 257    11167  18283  15467   1305   2754   3703       N  
ATOM   2443  CA  MET A 257      50.776   1.128  37.882  1.00116.45           C  
ANISOU 2443  CA  MET A 257    10969  17948  15330   1117   2531   3598       C  
ATOM   2444  C   MET A 257      51.810   1.900  37.051  1.00117.81           C  
ANISOU 2444  C   MET A 257    11313  18136  15313   1073   2277   3309       C  
ATOM   2445  O   MET A 257      52.898   1.384  36.785  1.00115.51           O  
ANISOU 2445  O   MET A 257    11140  17804  14946    996   2126   3201       O  
ATOM   2446  CB  MET A 257      49.894   0.274  36.958  1.00119.57           C  
ANISOU 2446  CB  MET A 257    11089  18211  16132    911   2452   3687       C  
ATOM   2447  CG  MET A 257      48.985  -0.663  37.701  1.00125.92           C  
ANISOU 2447  CG  MET A 257    11713  18973  17157    905   2697   3973       C  
ATOM   2448  SD  MET A 257      47.936  -1.621  36.602  1.00131.64           S  
ANISOU 2448  SD  MET A 257    12101  19540  18375    629   2579   4056       S  
ATOM   2449  CE  MET A 257      47.024  -2.541  37.792  1.00131.83           C  
ANISOU 2449  CE  MET A 257    11965  19536  18587    656   2936   4402       C  
ATOM   2450  N   ALA A 258      51.457   3.137  36.650  1.00114.62           N  
ANISOU 2450  N   ALA A 258    10928  17790  14832   1131   2246   3195       N  
ATOM   2451  CA  ALA A 258      52.295   4.033  35.858  1.00112.55           C  
ANISOU 2451  CA  ALA A 258    10833  17536  14396   1097   2043   2932       C  
ATOM   2452  C   ALA A 258      53.403   4.665  36.716  1.00116.25           C  
ANISOU 2452  C   ALA A 258    11571  18107  14490   1218   2083   2820       C  
ATOM   2453  O   ALA A 258      54.542   4.769  36.261  1.00114.03           O  
ANISOU 2453  O   ALA A 258    11433  17825  14069   1148   1914   2629       O  
ATOM   2454  CB  ALA A 258      51.436   5.124  35.229  1.00113.32           C  
ANISOU 2454  CB  ALA A 258    10859  17643  14555   1129   2022   2872       C  
ATOM   2455  N   ALA A 259      53.068   5.088  37.949  1.00114.64           N  
ANISOU 2455  N   ALA A 259    11436  17994  14126   1402   2306   2939       N  
ATOM   2456  CA  ALA A 259      54.017   5.715  38.870  1.00114.35           C  
ANISOU 2456  CA  ALA A 259    11661  18059  13728   1530   2343   2838       C  
ATOM   2457  C   ALA A 259      54.985   4.690  39.450  1.00118.86           C  
ANISOU 2457  C   ALA A 259    12302  18655  14203   1531   2326   2869       C  
ATOM   2458  O   ALA A 259      56.058   5.063  39.915  1.00118.01           O  
ANISOU 2458  O   ALA A 259    12392  18632  13814   1583   2265   2730       O  
ATOM   2459  CB  ALA A 259      53.268   6.412  39.994  1.00116.87           C  
ANISOU 2459  CB  ALA A 259    12049  18454  13904   1751   2587   2965       C  
ATOM   2460  N   ALA A 260      54.604   3.406  39.432  1.00116.24           N  
ANISOU 2460  N   ALA A 260    11812  18252  14103   1476   2378   3050       N  
ATOM   2461  CA  ALA A 260      55.418   2.331  39.978  1.00116.21           C  
ANISOU 2461  CA  ALA A 260    11878  18258  14019   1499   2385   3108       C  
ATOM   2462  C   ALA A 260      56.601   1.986  39.059  1.00118.22           C  
ANISOU 2462  C   ALA A 260    12180  18486  14252   1352   2130   2921       C  
ATOM   2463  O   ALA A 260      57.635   1.562  39.570  1.00117.63           O  
ANISOU 2463  O   ALA A 260    12228  18478  13989   1410   2098   2890       O  
ATOM   2464  CB  ALA A 260      54.565   1.099  40.200  1.00118.66           C  
ANISOU 2464  CB  ALA A 260    12022  18473  14592   1481   2545   3369       C  
ATOM   2465  N   VAL A 261      56.469   2.166  37.723  1.00113.41           N  
ANISOU 2465  N   VAL A 261    11480  17790  13821   1184   1953   2801       N  
ATOM   2466  CA  VAL A 261      57.560   1.812  36.800  1.00111.45           C  
ANISOU 2466  CA  VAL A 261    11281  17508  13558   1059   1726   2638       C  
ATOM   2467  C   VAL A 261      58.665   2.906  36.842  1.00113.27           C  
ANISOU 2467  C   VAL A 261    11684  17859  13496   1085   1622   2407       C  
ATOM   2468  O   VAL A 261      59.839   2.565  36.680  1.00112.25           O  
ANISOU 2468  O   VAL A 261    11630  17777  13242   1058   1501   2305       O  
ATOM   2469  CB  VAL A 261      57.109   1.544  35.329  1.00114.76           C  
ANISOU 2469  CB  VAL A 261    11566  17776  14262    883   1567   2594       C  
ATOM   2470  CG1 VAL A 261      56.156   0.355  35.250  1.00115.92           C  
ANISOU 2470  CG1 VAL A 261    11544  17796  14705    819   1636   2804       C  
ATOM   2471  CG2 VAL A 261      56.491   2.776  34.671  1.00114.22           C  
ANISOU 2471  CG2 VAL A 261    11466  17698  14234    860   1529   2486       C  
ATOM   2472  N   VAL A 262      58.301   4.190  37.082  1.00109.04           N  
ANISOU 2472  N   VAL A 262    11212  17370  12849   1138   1676   2329       N  
ATOM   2473  CA  VAL A 262      59.274   5.288  37.125  1.00107.55           C  
ANISOU 2473  CA  VAL A 262    11195  17272  12398   1136   1586   2106       C  
ATOM   2474  C   VAL A 262      59.966   5.289  38.519  1.00112.69           C  
ANISOU 2474  C   VAL A 262    11986  18072  12759   1282   1662   2114       C  
ATOM   2475  O   VAL A 262      61.194   5.358  38.560  1.00111.77           O  
ANISOU 2475  O   VAL A 262    11957  18045  12467   1250   1535   1964       O  
ATOM   2476  CB  VAL A 262      58.664   6.680  36.775  1.00110.95           C  
ANISOU 2476  CB  VAL A 262    11681  17673  12802   1138   1611   2007       C  
ATOM   2477  CG1 VAL A 262      57.442   7.016  37.625  1.00112.71           C  
ANISOU 2477  CG1 VAL A 262    11882  17910  13034   1293   1826   2176       C  
ATOM   2478  CG2 VAL A 262      59.703   7.795  36.841  1.00109.97           C  
ANISOU 2478  CG2 VAL A 262    11754  17620  12410   1112   1526   1773       C  
ATOM   2479  N   LEU A 263      59.197   5.167  39.633  1.00110.91           N  
ANISOU 2479  N   LEU A 263    11775  17878  12488   1450   1866   2294       N  
ATOM   2480  CA  LEU A 263      59.738   5.156  41.004  1.00111.84           C  
ANISOU 2480  CA  LEU A 263    12047  18129  12319   1624   1946   2314       C  
ATOM   2481  C   LEU A 263      60.690   3.967  41.238  1.00115.27           C  
ANISOU 2481  C   LEU A 263    12473  18619  12707   1638   1877   2347       C  
ATOM   2482  O   LEU A 263      61.740   4.173  41.841  1.00115.18           O  
ANISOU 2482  O   LEU A 263    12589  18744  12430   1703   1800   2227       O  
ATOM   2483  CB  LEU A 263      58.619   5.121  42.064  1.00113.84           C  
ANISOU 2483  CB  LEU A 263    12315  18382  12557   1820   2204   2533       C  
ATOM   2484  CG  LEU A 263      58.148   6.468  42.662  1.00119.26           C  
ANISOU 2484  CG  LEU A 263    13154  19107  13053   1942   2303   2479       C  
ATOM   2485  CD1 LEU A 263      57.657   7.453  41.597  1.00118.37           C  
ANISOU 2485  CD1 LEU A 263    12988  18909  13077   1820   2247   2379       C  
ATOM   2486  CD2 LEU A 263      57.072   6.248  43.697  1.00123.81           C  
ANISOU 2486  CD2 LEU A 263    13739  19688  13613   2162   2575   2726       C  
ATOM   2487  N   ALA A 264      60.342   2.749  40.759  1.00111.17           N  
ANISOU 2487  N   ALA A 264    11811  17995  12433   1579   1896   2499       N  
ATOM   2488  CA  ALA A 264      61.183   1.556  40.920  1.00110.94           C  
ANISOU 2488  CA  ALA A 264    11791  17997  12362   1607   1845   2546       C  
ATOM   2489  C   ALA A 264      62.532   1.727  40.211  1.00113.52           C  
ANISOU 2489  C   ALA A 264    12151  18403  12580   1503   1608   2323       C  
ATOM   2490  O   ALA A 264      63.561   1.373  40.783  1.00114.21           O  
ANISOU 2490  O   ALA A 264    12311  18619  12463   1595   1555   2286       O  
ATOM   2491  CB  ALA A 264      60.471   0.324  40.386  1.00111.79           C  
ANISOU 2491  CB  ALA A 264    11760  17940  12774   1532   1902   2735       C  
ATOM   2492  N   PHE A 265      62.531   2.302  38.991  1.00107.72           N  
ANISOU 2492  N   PHE A 265    11359  17597  11972   1327   1475   2178       N  
ATOM   2493  CA  PHE A 265      63.748   2.535  38.215  1.00105.82           C  
ANISOU 2493  CA  PHE A 265    11136  17416  11654   1216   1272   1974       C  
ATOM   2494  C   PHE A 265      64.656   3.549  38.934  1.00110.77           C  
ANISOU 2494  C   PHE A 265    11886  18224  11979   1263   1221   1796       C  
ATOM   2495  O   PHE A 265      65.866   3.335  38.988  1.00110.89           O  
ANISOU 2495  O   PHE A 265    11919  18371  11845   1262   1099   1691       O  
ATOM   2496  CB  PHE A 265      63.397   3.026  36.796  1.00105.71           C  
ANISOU 2496  CB  PHE A 265    11054  17260  11849   1039   1175   1879       C  
ATOM   2497  CG  PHE A 265      64.565   3.146  35.839  1.00105.36           C  
ANISOU 2497  CG  PHE A 265    11015  17242  11775    921    990   1702       C  
ATOM   2498  CD1 PHE A 265      64.989   2.053  35.092  1.00107.41           C  
ANISOU 2498  CD1 PHE A 265    11220  17440  12153    883    903   1750       C  
ATOM   2499  CD2 PHE A 265      65.194   4.368  35.633  1.00106.46           C  
ANISOU 2499  CD2 PHE A 265    11223  17449  11778    846    914   1494       C  
ATOM   2500  CE1 PHE A 265      66.055   2.168  34.196  1.00107.04           C  
ANISOU 2500  CE1 PHE A 265    11176  17417  12076    795    751   1602       C  
ATOM   2501  CE2 PHE A 265      66.261   4.482  34.736  1.00108.04           C  
ANISOU 2501  CE2 PHE A 265    11415  17670  11966    735    766   1345       C  
ATOM   2502  CZ  PHE A 265      66.684   3.382  34.024  1.00105.54           C  
ANISOU 2502  CZ  PHE A 265    11033  17308  11761    720    690   1405       C  
ATOM   2503  N   ILE A 266      64.072   4.623  39.511  1.00107.99           N  
ANISOU 2503  N   ILE A 266    11620  17881  11530   1313   1314   1766       N  
ATOM   2504  CA  ILE A 266      64.822   5.664  40.231  1.00108.54           C  
ANISOU 2504  CA  ILE A 266    11835  18095  11312   1348   1267   1590       C  
ATOM   2505  C   ILE A 266      65.390   5.072  41.548  1.00113.98           C  
ANISOU 2505  C   ILE A 266    12598  18947  11763   1542   1299   1652       C  
ATOM   2506  O   ILE A 266      66.589   5.193  41.776  1.00114.44           O  
ANISOU 2506  O   ILE A 266    12697  19163  11624   1533   1159   1497       O  
ATOM   2507  CB  ILE A 266      63.958   6.937  40.499  1.00112.10           C  
ANISOU 2507  CB  ILE A 266    12392  18483  11718   1372   1374   1560       C  
ATOM   2508  CG1 ILE A 266      63.511   7.583  39.162  1.00110.99           C  
ANISOU 2508  CG1 ILE A 266    12201  18198  11773   1196   1322   1469       C  
ATOM   2509  CG2 ILE A 266      64.726   7.960  41.356  1.00113.58           C  
ANISOU 2509  CG2 ILE A 266    12768  18803  11584   1422   1330   1386       C  
ATOM   2510  CD1 ILE A 266      62.523   8.762  39.272  1.00116.61           C  
ANISOU 2510  CD1 ILE A 266    13011  18828  12468   1233   1438   1459       C  
ATOM   2511  N   ILE A 267      64.560   4.407  42.377  1.00111.01           N  
ANISOU 2511  N   ILE A 267    12232  18537  11411   1717   1481   1877       N  
ATOM   2512  CA  ILE A 267      65.014   3.828  43.652  1.00112.63           C  
ANISOU 2512  CA  ILE A 267    12534  18880  11381   1938   1536   1955       C  
ATOM   2513  C   ILE A 267      66.178   2.831  43.411  1.00117.02           C  
ANISOU 2513  C   ILE A 267    13030  19541  11893   1934   1393   1923       C  
ATOM   2514  O   ILE A 267      67.159   2.872  44.154  1.00117.70           O  
ANISOU 2514  O   ILE A 267    13198  19813  11711   2050   1311   1835       O  
ATOM   2515  CB  ILE A 267      63.847   3.135  44.427  1.00116.84           C  
ANISOU 2515  CB  ILE A 267    13077  19321  11997   2116   1791   2236       C  
ATOM   2516  CG1 ILE A 267      62.797   4.176  44.868  1.00117.87           C  
ANISOU 2516  CG1 ILE A 267    13288  19396  12103   2179   1944   2269       C  
ATOM   2517  CG2 ILE A 267      64.368   2.356  45.658  1.00118.92           C  
ANISOU 2517  CG2 ILE A 267    13450  19706  12028   2362   1859   2338       C  
ATOM   2518  CD1 ILE A 267      61.528   3.592  45.483  1.00126.43           C  
ANISOU 2518  CD1 ILE A 267    14342  20379  13315   2331   2218   2557       C  
ATOM   2519  N   CYS A 268      66.088   1.985  42.366  1.00112.51           N  
ANISOU 2519  N   CYS A 268    12324  18855  11568   1810   1354   1986       N  
ATOM   2520  CA  CYS A 268      67.069   0.933  42.099  1.00112.20           C  
ANISOU 2520  CA  CYS A 268    12241  18893  11498   1834   1248   1992       C  
ATOM   2521  C   CYS A 268      68.346   1.468  41.406  1.00115.54           C  
ANISOU 2521  C   CYS A 268    12616  19447  11837   1694   1022   1751       C  
ATOM   2522  O   CYS A 268      69.414   0.917  41.674  1.00115.50           O  
ANISOU 2522  O   CYS A 268    12607  19611  11665   1783    926   1710       O  
ATOM   2523  CB  CYS A 268      66.447  -0.169  41.253  1.00111.59           C  
ANISOU 2523  CB  CYS A 268    12071  18620  11707   1768   1305   2162       C  
ATOM   2524  SG  CYS A 268      65.183  -1.138  42.112  1.00117.02           S  
ANISOU 2524  SG  CYS A 268    12791  19169  12501   1926   1577   2469       S  
ATOM   2525  N   TRP A 269      68.260   2.463  40.505  1.00111.37           N  
ANISOU 2525  N   TRP A 269    12047  18842  11427   1490    946   1604       N  
ATOM   2526  CA  TRP A 269      69.461   2.883  39.780  1.00110.89           C  
ANISOU 2526  CA  TRP A 269    11930  18886  11316   1348    759   1399       C  
ATOM   2527  C   TRP A 269      70.026   4.269  40.206  1.00115.81           C  
ANISOU 2527  C   TRP A 269    12622  19639  11741   1279    678   1176       C  
ATOM   2528  O   TRP A 269      71.211   4.494  39.962  1.00115.63           O  
ANISOU 2528  O   TRP A 269    12548  19770  11618   1203    527   1017       O  
ATOM   2529  CB  TRP A 269      69.197   2.935  38.270  1.00108.02           C  
ANISOU 2529  CB  TRP A 269    11484  18343  11215   1158    713   1372       C  
ATOM   2530  CG  TRP A 269      69.108   1.578  37.638  1.00108.67           C  
ANISOU 2530  CG  TRP A 269    11502  18328  11461   1189    717   1526       C  
ATOM   2531  CD1 TRP A 269      67.974   0.905  37.289  1.00111.40           C  
ANISOU 2531  CD1 TRP A 269    11829  18469  12028   1193    820   1703       C  
ATOM   2532  CD2 TRP A 269      70.200   0.685  37.382  1.00108.59           C  
ANISOU 2532  CD2 TRP A 269    11448  18425  11385   1238    620   1525       C  
ATOM   2533  NE1 TRP A 269      68.297  -0.328  36.767  1.00110.76           N  
ANISOU 2533  NE1 TRP A 269    11719  18338  12028   1222    784   1799       N  
ATOM   2534  CE2 TRP A 269      69.656  -0.495  36.826  1.00112.25           C  
ANISOU 2534  CE2 TRP A 269    11900  18716  12033   1267    669   1700       C  
ATOM   2535  CE3 TRP A 269      71.593   0.774  37.557  1.00110.23           C  
ANISOU 2535  CE3 TRP A 269    11621  18864  11397   1261    492   1392       C  
ATOM   2536  CZ2 TRP A 269      70.455  -1.575  36.436  1.00111.41           C  
ANISOU 2536  CZ2 TRP A 269    11780  18646  11903   1335    605   1749       C  
ATOM   2537  CZ3 TRP A 269      72.380  -0.298  37.177  1.00111.63           C  
ANISOU 2537  CZ3 TRP A 269    11755  19102  11558   1337    432   1448       C  
ATOM   2538  CH2 TRP A 269      71.813  -1.453  36.616  1.00111.78           C  
ANISOU 2538  CH2 TRP A 269    11794  18931  11745   1381    492   1626       C  
ATOM   2539  N   LEU A 270      69.234   5.178  40.818  1.00113.16           N  
ANISOU 2539  N   LEU A 270    12403  19245  11348   1303    775   1163       N  
ATOM   2540  CA  LEU A 270      69.754   6.507  41.191  1.00113.86           C  
ANISOU 2540  CA  LEU A 270    12593  19427  11243   1226    696    944       C  
ATOM   2541  C   LEU A 270      70.950   6.396  42.187  1.00120.37           C  
ANISOU 2541  C   LEU A 270    13440  20511  11783   1326    572    840       C  
ATOM   2542  O   LEU A 270      71.940   7.084  41.931  1.00120.56           O  
ANISOU 2542  O   LEU A 270    13438  20645  11723   1175    420    629       O  
ATOM   2543  CB  LEU A 270      68.668   7.423  41.790  1.00114.53           C  
ANISOU 2543  CB  LEU A 270    12835  19406  11276   1288    837    970       C  
ATOM   2544  CG  LEU A 270      69.071   8.870  42.141  1.00120.03           C  
ANISOU 2544  CG  LEU A 270    13686  20149  11771   1203    771    744       C  
ATOM   2545  CD1 LEU A 270      69.593   9.625  40.922  1.00118.66           C  
ANISOU 2545  CD1 LEU A 270    13466  19912  11708    940    664    556       C  
ATOM   2546  CD2 LEU A 270      67.908   9.623  42.746  1.00123.50           C  
ANISOU 2546  CD2 LEU A 270    14297  20472  12156   1312    937    810       C  
ATOM   2547  N   PRO A 271      70.943   5.544  43.265  1.00118.19           N  
ANISOU 2547  N   PRO A 271    13203  20342  11360   1570    625    977       N  
ATOM   2548  CA  PRO A 271      72.117   5.491  44.161  1.00119.60           C  
ANISOU 2548  CA  PRO A 271    13402  20785  11255   1674    481    859       C  
ATOM   2549  C   PRO A 271      73.429   5.187  43.414  1.00122.68           C  
ANISOU 2549  C   PRO A 271    13614  21330  11668   1549    295    738       C  
ATOM   2550  O   PRO A 271      74.428   5.862  43.672  1.00123.22           O  
ANISOU 2550  O   PRO A 271    13661  21585  11571   1471    130    531       O  
ATOM   2551  CB  PRO A 271      71.772   4.353  45.126  1.00122.53           C  
ANISOU 2551  CB  PRO A 271    13835  21197  11525   1971    602   1076       C  
ATOM   2552  CG  PRO A 271      70.307   4.321  45.154  1.00126.48           C  
ANISOU 2552  CG  PRO A 271    14407  21464  12186   2017    826   1265       C  
ATOM   2553  CD  PRO A 271      69.875   4.645  43.757  1.00119.97           C  
ANISOU 2553  CD  PRO A 271    13467  20458  11658   1766    821   1240       C  
ATOM   2554  N   PHE A 272      73.416   4.226  42.461  1.00117.63           N  
ANISOU 2554  N   PHE A 272    12847  20608  11238   1521    320    862       N  
ATOM   2555  CA  PHE A 272      74.603   3.863  41.685  1.00117.06           C  
ANISOU 2555  CA  PHE A 272    12610  20672  11197   1430    171    778       C  
ATOM   2556  C   PHE A 272      75.131   5.046  40.847  1.00120.26           C  
ANISOU 2556  C   PHE A 272    12951  21070  11670   1147     63    555       C  
ATOM   2557  O   PHE A 272      76.341   5.284  40.840  1.00120.93           O  
ANISOU 2557  O   PHE A 272    12931  21370  11646   1078    -92    399       O  
ATOM   2558  CB  PHE A 272      74.316   2.666  40.748  1.00117.40           C  
ANISOU 2558  CB  PHE A 272    12578  20575  11456   1459    237    962       C  
ATOM   2559  CG  PHE A 272      75.487   2.325  39.854  1.00118.63           C  
ANISOU 2559  CG  PHE A 272    12577  20851  11644   1380    103    888       C  
ATOM   2560  CD1 PHE A 272      76.518   1.519  40.310  1.00123.22           C  
ANISOU 2560  CD1 PHE A 272    13090  21675  12051   1552     19    907       C  
ATOM   2561  CD2 PHE A 272      75.579   2.846  38.568  1.00119.29           C  
ANISOU 2561  CD2 PHE A 272    12589  20815  11919   1153     67    799       C  
ATOM   2562  CE1 PHE A 272      77.622   1.242  39.498  1.00124.08           C  
ANISOU 2562  CE1 PHE A 272    13045  21916  12182   1494    -96    844       C  
ATOM   2563  CE2 PHE A 272      76.685   2.574  37.761  1.00121.85           C  
ANISOU 2563  CE2 PHE A 272    12773  21259  12266   1093    -40    737       C  
ATOM   2564  CZ  PHE A 272      77.699   1.775  38.230  1.00121.38           C  
ANISOU 2564  CZ  PHE A 272    12630  21450  12038   1262   -119    763       C  
ATOM   2565  N   HIS A 273      74.243   5.743  40.115  1.00115.11           N  
ANISOU 2565  N   HIS A 273    12356  20177  11203    991    149    547       N  
ATOM   2566  CA  HIS A 273      74.646   6.824  39.219  1.00113.97           C  
ANISOU 2566  CA  HIS A 273    12180  19982  11141    732     82    357       C  
ATOM   2567  C   HIS A 273      75.028   8.086  40.007  1.00118.94           C  
ANISOU 2567  C   HIS A 273    12911  20710  11572    642     12    149       C  
ATOM   2568  O   HIS A 273      75.818   8.877  39.492  1.00118.19           O  
ANISOU 2568  O   HIS A 273    12765  20654  11488    427    -80    -37       O  
ATOM   2569  CB  HIS A 273      73.544   7.132  38.207  1.00112.57           C  
ANISOU 2569  CB  HIS A 273    12052  19516  11204    629    197    421       C  
ATOM   2570  CG  HIS A 273      73.350   5.999  37.249  1.00114.22           C  
ANISOU 2570  CG  HIS A 273    12163  19620  11616    667    225    580       C  
ATOM   2571  ND1 HIS A 273      74.138   5.869  36.122  1.00114.98           N  
ANISOU 2571  ND1 HIS A 273    12149  19727  11813    551    144    521       N  
ATOM   2572  CD2 HIS A 273      72.532   4.924  37.334  1.00115.17           C  
ANISOU 2572  CD2 HIS A 273    12291  19629  11839    813    321    792       C  
ATOM   2573  CE1 HIS A 273      73.747   4.748  35.538  1.00113.24           C  
ANISOU 2573  CE1 HIS A 273    11893  19391  11741    637    185    692       C  
ATOM   2574  NE2 HIS A 273      72.785   4.144  36.232  1.00113.71           N  
ANISOU 2574  NE2 HIS A 273    12017  19371  11815    781    287    855       N  
ATOM   2575  N   VAL A 274      74.547   8.244  41.264  1.00117.10           N  
ANISOU 2575  N   VAL A 274    12824  20518  11149    806     54    176       N  
ATOM   2576  CA  VAL A 274      74.958   9.372  42.112  1.00118.80           C  
ANISOU 2576  CA  VAL A 274    13164  20833  11143    741    -34    -30       C  
ATOM   2577  C   VAL A 274      76.443   9.181  42.451  1.00124.35           C  
ANISOU 2577  C   VAL A 274    13719  21832  11695    705   -239   -178       C  
ATOM   2578  O   VAL A 274      77.237  10.092  42.221  1.00124.87           O  
ANISOU 2578  O   VAL A 274    13747  21960  11739    476   -357   -393       O  
ATOM   2579  CB  VAL A 274      74.080   9.551  43.384  1.00123.96           C  
ANISOU 2579  CB  VAL A 274    14035  21457  11609    959     64     44       C  
ATOM   2580  CG1 VAL A 274      74.729  10.495  44.394  1.00126.25           C  
ANISOU 2580  CG1 VAL A 274    14454  21897  11619    934    -72   -175       C  
ATOM   2581  CG2 VAL A 274      72.685  10.041  43.022  1.00122.48           C  
ANISOU 2581  CG2 VAL A 274    13982  20995  11560    953    255    146       C  
ATOM   2582  N   LEU A 275      76.817   7.968  42.912  1.00121.11           N  
ANISOU 2582  N   LEU A 275    13215  21600  11200    928   -273    -55       N  
ATOM   2583  CA  LEU A 275      78.191   7.607  43.275  1.00122.52           C  
ANISOU 2583  CA  LEU A 275    13232  22094  11225    959   -465   -162       C  
ATOM   2584  C   LEU A 275      79.127   7.649  42.063  1.00125.19           C  
ANISOU 2584  C   LEU A 275    13343  22490  11732    735   -549   -246       C  
ATOM   2585  O   LEU A 275      80.285   8.039  42.217  1.00126.25           O  
ANISOU 2585  O   LEU A 275    13345  22857  11769    621   -721   -427       O  
ATOM   2586  CB  LEU A 275      78.232   6.200  43.906  1.00123.18           C  
ANISOU 2586  CB  LEU A 275    13290  22311  11201   1283   -438     32       C  
ATOM   2587  CG  LEU A 275      77.399   5.978  45.179  1.00128.82           C  
ANISOU 2587  CG  LEU A 275    14223  22992  11731   1554   -335    147       C  
ATOM   2588  CD1 LEU A 275      77.394   4.521  45.571  1.00129.14           C  
ANISOU 2588  CD1 LEU A 275    14243  23113  11713   1853   -270    364       C  
ATOM   2589  CD2 LEU A 275      77.878   6.850  46.333  1.00133.49           C  
ANISOU 2589  CD2 LEU A 275    14931  23756  12033   1580   -477    -54       C  
ATOM   2590  N   THR A 276      78.621   7.259  40.862  1.00119.15           N  
ANISOU 2590  N   THR A 276    12534  21516  11221    677   -430   -114       N  
ATOM   2591  CA  THR A 276      79.365   7.243  39.595  1.00117.82           C  
ANISOU 2591  CA  THR A 276    12182  21357  11228    496   -471   -159       C  
ATOM   2592  C   THR A 276      79.663   8.692  39.152  1.00122.50           C  
ANISOU 2592  C   THR A 276    12788  21886  11869    184   -513   -382       C  
ATOM   2593  O   THR A 276      80.760   8.962  38.655  1.00122.52           O  
ANISOU 2593  O   THR A 276    12615  22035  11902     19   -613   -506       O  
ATOM   2594  CB  THR A 276      78.562   6.465  38.519  1.00121.96           C  
ANISOU 2594  CB  THR A 276    12716  21635  11988    543   -330     42       C  
ATOM   2595  OG1 THR A 276      78.343   5.129  38.971  1.00121.00           O  
ANISOU 2595  OG1 THR A 276    12599  21561  11814    815   -287    242       O  
ATOM   2596  CG2 THR A 276      79.265   6.415  37.169  1.00118.51           C  
ANISOU 2596  CG2 THR A 276    12123  21187  11720    394   -358     14       C  
ATOM   2597  N   PHE A 277      78.692   9.615  39.338  1.00119.74           N  
ANISOU 2597  N   PHE A 277    12653  21322  11523    111   -425   -427       N  
ATOM   2598  CA  PHE A 277      78.869  11.023  38.978  1.00120.49           C  
ANISOU 2598  CA  PHE A 277    12819  21321  11642   -171   -442   -635       C  
ATOM   2599  C   PHE A 277      79.864  11.682  39.943  1.00128.97           C  
ANISOU 2599  C   PHE A 277    13870  22638  12495   -258   -617   -851       C  
ATOM   2600  O   PHE A 277      80.706  12.462  39.494  1.00129.26           O  
ANISOU 2600  O   PHE A 277    13827  22721  12566   -521   -695  -1036       O  
ATOM   2601  CB  PHE A 277      77.526  11.778  38.963  1.00120.94           C  
ANISOU 2601  CB  PHE A 277    13129  21081  11741   -183   -291   -607       C  
ATOM   2602  CG  PHE A 277      77.643  13.240  38.615  1.00122.86           C  
ANISOU 2602  CG  PHE A 277    13493  21196  11992   -454   -288   -814       C  
ATOM   2603  CD1 PHE A 277      77.836  13.645  37.301  1.00124.78           C  
ANISOU 2603  CD1 PHE A 277    13684  21296  12430   -654   -237   -855       C  
ATOM   2604  CD2 PHE A 277      77.514  14.217  39.595  1.00126.72           C  
ANISOU 2604  CD2 PHE A 277    14183  21682  12283   -494   -322   -960       C  
ATOM   2605  CE1 PHE A 277      77.962  15.000  36.983  1.00126.37           C  
ANISOU 2605  CE1 PHE A 277    14021  21362  12633   -902   -215  -1041       C  
ATOM   2606  CE2 PHE A 277      77.624  15.573  39.274  1.00130.19           C  
ANISOU 2606  CE2 PHE A 277    14766  21979  12722   -749   -310  -1152       C  
ATOM   2607  CZ  PHE A 277      77.848  15.955  37.971  1.00127.15           C  
ANISOU 2607  CZ  PHE A 277    14320  21455  12537   -955   -250  -1189       C  
ATOM   2608  N   LEU A 278      79.791  11.340  41.254  1.00128.65           N  
ANISOU 2608  N   LEU A 278    13898  22754  12230    -37   -681   -827       N  
ATOM   2609  CA  LEU A 278      80.724  11.846  42.269  1.00132.11           C  
ANISOU 2609  CA  LEU A 278    14316  23446  12432    -81   -878  -1030       C  
ATOM   2610  C   LEU A 278      82.133  11.326  41.997  1.00138.72           C  
ANISOU 2610  C   LEU A 278    14837  24588  13281   -138  -1041  -1092       C  
ATOM   2611  O   LEU A 278      83.099  12.072  42.175  1.00140.41           O  
ANISOU 2611  O   LEU A 278    14953  24963  13433   -354  -1200  -1313       O  
ATOM   2612  CB  LEU A 278      80.283  11.463  43.692  1.00133.50           C  
ANISOU 2612  CB  LEU A 278    14657  23712  12355    221   -897   -966       C  
ATOM   2613  CG  LEU A 278      78.988  12.070  44.224  1.00137.83           C  
ANISOU 2613  CG  LEU A 278    15524  24010  12836    308   -749   -919       C  
ATOM   2614  CD1 LEU A 278      78.619  11.447  45.555  1.00139.23           C  
ANISOU 2614  CD1 LEU A 278    15833  24294  12773    651   -744   -811       C  
ATOM   2615  CD2 LEU A 278      79.084  13.591  44.344  1.00141.81           C  
ANISOU 2615  CD2 LEU A 278    16203  24409  13268     52   -802  -1162       C  
ATOM   2616  N   ASP A 279      82.241  10.051  41.539  1.00135.32           N  
ANISOU 2616  N   ASP A 279    14249  24230  12937     50   -995   -894       N  
ATOM   2617  CA  ASP A 279      83.500   9.404  41.154  1.00136.67           C  
ANISOU 2617  CA  ASP A 279    14116  24681  13131     47  -1114   -904       C  
ATOM   2618  C   ASP A 279      84.151  10.152  39.993  1.00142.34           C  
ANISOU 2618  C   ASP A 279    14683  25354  14048   -286  -1117  -1028       C  
ATOM   2619  O   ASP A 279      85.355  10.408  40.031  1.00144.07           O  
ANISOU 2619  O   ASP A 279    14669  25835  14234   -419  -1268  -1169       O  
ATOM   2620  CB  ASP A 279      83.263   7.926  40.768  1.00136.63           C  
ANISOU 2620  CB  ASP A 279    14047  24673  13192    321  -1017   -644       C  
ATOM   2621  CG  ASP A 279      84.498   7.187  40.284  1.00145.68           C  
ANISOU 2621  CG  ASP A 279    14902  26094  14357    363  -1113   -622       C  
ATOM   2622  OD1 ASP A 279      85.583   7.379  40.884  1.00148.28           O  
ANISOU 2622  OD1 ASP A 279    15057  26743  14539    330  -1298   -775       O  
ATOM   2623  OD2 ASP A 279      84.363   6.352  39.367  1.00149.85           O  
ANISOU 2623  OD2 ASP A 279    15380  26528  15027    458  -1008   -445       O  
ATOM   2624  N   ALA A 280      83.343  10.509  38.971  1.00138.01           N  
ANISOU 2624  N   ALA A 280    14263  24474  13701   -413   -946   -973       N  
ATOM   2625  CA  ALA A 280      83.778  11.247  37.787  1.00138.01           C  
ANISOU 2625  CA  ALA A 280    14178  24364  13896   -710   -903  -1068       C  
ATOM   2626  C   ALA A 280      84.352  12.616  38.167  1.00145.57           C  
ANISOU 2626  C   ALA A 280    15154  25372  14783  -1009  -1006  -1335       C  
ATOM   2627  O   ALA A 280      85.371  13.016  37.607  1.00146.49           O  
ANISOU 2627  O   ALA A 280    15069  25600  14990  -1240  -1059  -1451       O  
ATOM   2628  CB  ALA A 280      82.616  11.418  36.830  1.00135.96           C  
ANISOU 2628  CB  ALA A 280    14110  23727  13819   -732   -705   -956       C  
ATOM   2629  N   LEU A 281      83.723  13.308  39.149  1.00143.83           N  
ANISOU 2629  N   LEU A 281    15177  25073  14398  -1000  -1033  -1430       N  
ATOM   2630  CA  LEU A 281      84.175  14.615  39.644  1.00146.38           C  
ANISOU 2630  CA  LEU A 281    15576  25417  14623  -1273  -1142  -1693       C  
ATOM   2631  C   LEU A 281      85.516  14.486  40.382  1.00153.60           C  
ANISOU 2631  C   LEU A 281    16238  26729  15395  -1312  -1387  -1841       C  
ATOM   2632  O   LEU A 281      86.336  15.400  40.304  1.00155.43           O  
ANISOU 2632  O   LEU A 281    16398  27031  15628  -1616  -1496  -2064       O  
ATOM   2633  CB  LEU A 281      83.128  15.265  40.567  1.00146.65           C  
ANISOU 2633  CB  LEU A 281    15968  25262  14490  -1197  -1102  -1734       C  
ATOM   2634  CG  LEU A 281      81.784  15.660  39.943  1.00148.79           C  
ANISOU 2634  CG  LEU A 281    16505  25149  14881  -1185   -873  -1628       C  
ATOM   2635  CD1 LEU A 281      80.801  16.087  41.016  1.00149.51           C  
ANISOU 2635  CD1 LEU A 281    16916  25118  14774  -1028   -837  -1629       C  
ATOM   2636  CD2 LEU A 281      81.950  16.753  38.879  1.00150.94           C  
ANISOU 2636  CD2 LEU A 281    16824  25213  15315  -1521   -793  -1759       C  
ATOM   2637  N   ALA A 282      85.755  13.335  41.052  1.00150.59           N  
ANISOU 2637  N   ALA A 282    15715  26606  14895  -1009  -1473  -1717       N  
ATOM   2638  CA  ALA A 282      87.015  13.061  41.743  1.00153.63           C  
ANISOU 2638  CA  ALA A 282    15836  27401  15136   -991  -1712  -1836       C  
ATOM   2639  C   ALA A 282      88.164  12.927  40.730  1.00158.49           C  
ANISOU 2639  C   ALA A 282    16091  28187  15939  -1192  -1743  -1865       C  
ATOM   2640  O   ALA A 282      89.241  13.478  40.967  1.00161.08           O  
ANISOU 2640  O   ALA A 282    16216  28752  16236  -1414  -1921  -2069       O  
ATOM   2641  CB  ALA A 282      86.894  11.802  42.587  1.00154.36           C  
ANISOU 2641  CB  ALA A 282    15909  27693  15048   -575  -1759  -1669       C  
ATOM   2642  N   TRP A 283      87.916  12.244  39.578  1.00152.57           N  
ANISOU 2642  N   TRP A 283    15272  27305  15393  -1125  -1564  -1665       N  
ATOM   2643  CA  TRP A 283      88.909  12.090  38.508  1.00152.76           C  
ANISOU 2643  CA  TRP A 283    14984  27455  15602  -1279  -1548  -1657       C  
ATOM   2644  C   TRP A 283      89.143  13.417  37.770  1.00159.10           C  
ANISOU 2644  C   TRP A 283    15803  28074  16575  -1698  -1487  -1829       C  
ATOM   2645  O   TRP A 283      90.249  13.645  37.276  1.00160.69           O  
ANISOU 2645  O   TRP A 283    15715  28449  16889  -1902  -1527  -1903       O  
ATOM   2646  CB  TRP A 283      88.517  11.005  37.497  1.00148.08           C  
ANISOU 2646  CB  TRP A 283    14370  26739  15153  -1064  -1374  -1395       C  
ATOM   2647  CG  TRP A 283      88.568   9.609  38.041  1.00148.57           C  
ANISOU 2647  CG  TRP A 283    14375  27003  15072   -674  -1422  -1218       C  
ATOM   2648  CD1 TRP A 283      87.510   8.824  38.385  1.00149.44           C  
ANISOU 2648  CD1 TRP A 283    14718  26949  15114   -391  -1332  -1044       C  
ATOM   2649  CD2 TRP A 283      89.746   8.865  38.378  1.00150.50           C  
ANISOU 2649  CD2 TRP A 283    14316  27656  15210   -520  -1570  -1203       C  
ATOM   2650  NE1 TRP A 283      87.953   7.611  38.858  1.00149.50           N  
ANISOU 2650  NE1 TRP A 283    14609  27212  14982    -73  -1400   -915       N  
ATOM   2651  CE2 TRP A 283      89.322   7.614  38.879  1.00153.43           C  
ANISOU 2651  CE2 TRP A 283    14785  28073  15440   -130  -1552  -1012       C  
ATOM   2652  CE3 TRP A 283      91.126   9.124  38.284  1.00154.46           C  
ANISOU 2652  CE3 TRP A 283    14465  28498  15727   -670  -1709  -1326       C  
ATOM   2653  CZ2 TRP A 283      90.225   6.622  39.282  1.00154.38           C  
ANISOU 2653  CZ2 TRP A 283    14687  28555  15416    135  -1665   -939       C  
ATOM   2654  CZ3 TRP A 283      92.019   8.143  38.689  1.00157.49           C  
ANISOU 2654  CZ3 TRP A 283    14602  29263  15976   -406  -1829  -1252       C  
ATOM   2655  CH2 TRP A 283      91.568   6.909  39.181  1.00157.08           C  
ANISOU 2655  CH2 TRP A 283    14679  29239  15766      2  -1806  -1061       C  
ATOM   2656  N   MET A 284      88.116  14.290  37.705  1.00155.54           N  
ANISOU 2656  N   MET A 284    15687  27273  16138  -1817  -1377  -1885       N  
ATOM   2657  CA  MET A 284      88.216  15.612  37.071  1.00156.54           C  
ANISOU 2657  CA  MET A 284    15899  27181  16398  -2199  -1299  -2050       C  
ATOM   2658  C   MET A 284      88.969  16.614  37.967  1.00165.51           C  
ANISOU 2658  C   MET A 284    16996  28483  17408  -2469  -1501  -2330       C  
ATOM   2659  O   MET A 284      89.323  17.704  37.509  1.00166.54           O  
ANISOU 2659  O   MET A 284    17126  28502  17648  -2828  -1469  -2493       O  
ATOM   2660  CB  MET A 284      86.822  16.164  36.741  1.00156.33           C  
ANISOU 2660  CB  MET A 284    16263  26721  16413  -2188  -1103  -1996       C  
ATOM   2661  CG  MET A 284      86.132  15.428  35.630  1.00156.67           C  
ANISOU 2661  CG  MET A 284    16342  26565  16619  -2002   -910  -1756       C  
ATOM   2662  SD  MET A 284      84.463  16.049  35.352  1.00158.24           S  
ANISOU 2662  SD  MET A 284    16971  26301  16853  -1960   -706  -1695       S  
ATOM   2663  CE  MET A 284      84.010  15.077  33.971  1.00151.65           C  
ANISOU 2663  CE  MET A 284    16076  25327  16218  -1760   -548  -1437       C  
ATOM   2664  N   GLY A 285      89.199  16.235  39.223  1.00164.57           N  
ANISOU 2664  N   GLY A 285    16859  28615  17057  -2291  -1703  -2384       N  
ATOM   2665  CA  GLY A 285      89.892  17.063  40.202  1.00168.55           C  
ANISOU 2665  CA  GLY A 285    17337  29300  17404  -2500  -1936  -2653       C  
ATOM   2666  C   GLY A 285      88.982  18.007  40.957  1.00173.59           C  
ANISOU 2666  C   GLY A 285    18401  29673  17882  -2541  -1932  -2775       C  
ATOM   2667  O   GLY A 285      89.462  18.890  41.672  1.00176.22           O  
ANISOU 2667  O   GLY A 285    18784  30080  18092  -2759  -2111  -3021       O  
ATOM   2668  N   VAL A 286      87.660  17.821  40.804  1.00167.67           N  
ANISOU 2668  N   VAL A 286    17960  28617  17129  -2325  -1731  -2601       N  
ATOM   2669  CA  VAL A 286      86.631  18.628  41.462  1.00167.53           C  
ANISOU 2669  CA  VAL A 286    18367  28329  16956  -2302  -1683  -2670       C  
ATOM   2670  C   VAL A 286      86.556  18.207  42.937  1.00173.05           C  
ANISOU 2670  C   VAL A 286    19145  29243  17361  -2020  -1866  -2692       C  
ATOM   2671  O   VAL A 286      86.576  19.070  43.816  1.00175.11           O  
ANISOU 2671  O   VAL A 286    19619  29482  17431  -2117  -1994  -2892       O  
ATOM   2672  CB  VAL A 286      85.257  18.498  40.742  1.00167.73           C  
ANISOU 2672  CB  VAL A 286    18652  27984  17094  -2154  -1402  -2463       C  
ATOM   2673  CG1 VAL A 286      84.182  19.330  41.439  1.00167.77           C  
ANISOU 2673  CG1 VAL A 286    19090  27722  16931  -2119  -1340  -2529       C  
ATOM   2674  CG2 VAL A 286      85.367  18.893  39.271  1.00166.01           C  
ANISOU 2674  CG2 VAL A 286    18358  27567  17150  -2397  -1228  -2438       C  
ATOM   2675  N   ILE A 287      86.502  16.882  43.201  1.00169.14           N  
ANISOU 2675  N   ILE A 287    18496  28951  16820  -1668  -1879  -2491       N  
ATOM   2676  CA  ILE A 287      86.453  16.346  44.561  1.00170.89           C  
ANISOU 2676  CA  ILE A 287    18791  29384  16755  -1365  -2037  -2492       C  
ATOM   2677  C   ILE A 287      87.866  15.931  44.967  1.00178.32           C  
ANISOU 2677  C   ILE A 287    19366  30765  17624  -1395  -2304  -2613       C  
ATOM   2678  O   ILE A 287      88.452  15.016  44.372  1.00177.19           O  
ANISOU 2678  O   ILE A 287    18898  30815  17611  -1332  -2296  -2492       O  
ATOM   2679  CB  ILE A 287      85.438  15.177  44.722  1.00171.32           C  
ANISOU 2679  CB  ILE A 287    18962  29368  16764   -938  -1877  -2201       C  
ATOM   2680  CG1 ILE A 287      84.035  15.505  44.135  1.00168.57           C  
ANISOU 2680  CG1 ILE A 287    18906  28603  16540   -920  -1601  -2059       C  
ATOM   2681  CG2 ILE A 287      85.350  14.704  46.164  1.00174.01           C  
ANISOU 2681  CG2 ILE A 287    19430  29898  16788   -624  -2018  -2211       C  
ATOM   2682  CD1 ILE A 287      83.299  16.686  44.597  1.00176.52           C  
ANISOU 2682  CD1 ILE A 287    20296  29342  17432  -1027  -1552  -2192       C  
ATOM   2683  N   ASN A 288      88.391  16.629  45.995  1.00179.11           N  
ANISOU 2683  N   ASN A 288    19531  31013  17509  -1499  -2546  -2864       N  
ATOM   2684  CA  ASN A 288      89.729  16.471  46.566  1.00183.12           C  
ANISOU 2684  CA  ASN A 288    19731  31944  17903  -1567  -2856  -3050       C  
ATOM   2685  C   ASN A 288      89.692  15.771  47.941  1.00189.16           C  
ANISOU 2685  C   ASN A 288    20568  32961  18343  -1152  -3024  -3020       C  
ATOM   2686  O   ASN A 288      90.689  15.155  48.329  1.00190.66           O  
ANISOU 2686  O   ASN A 288    20441  33543  18458  -1029  -3215  -3037       O  
ATOM   2687  CB  ASN A 288      90.409  17.845  46.709  1.00187.09           C  
ANISOU 2687  CB  ASN A 288    20281  32416  18388  -2003  -3030  -3381       C  
ATOM   2688  CG  ASN A 288      89.664  18.864  47.557  1.00208.29           C  
ANISOU 2688  CG  ASN A 288    23454  34818  20869  -2014  -3029  -3508       C  
ATOM   2689  OD1 ASN A 288      88.459  18.751  47.824  1.00198.56           O  
ANISOU 2689  OD1 ASN A 288    22552  33336  19554  -1740  -2836  -3336       O  
ATOM   2690  ND2 ASN A 288      90.357  19.928  47.938  1.00203.12           N  
ANISOU 2690  ND2 ASN A 288    22860  34169  20148  -2356  -3224  -3810       N  
ATOM   2691  N   SER A 289      88.566  15.891  48.684  1.00184.95           N  
ANISOU 2691  N   SER A 289    20453  32208  17610   -920  -2942  -2969       N  
ATOM   2692  CA  SER A 289      88.403  15.266  50.003  1.00186.00           C  
ANISOU 2692  CA  SER A 289    20727  32525  17419   -500  -3060  -2926       C  
ATOM   2693  C   SER A 289      88.292  13.747  49.852  1.00187.33           C  
ANISOU 2693  C   SER A 289    20735  32828  17614   -118  -2937  -2630       C  
ATOM   2694  O   SER A 289      87.386  13.266  49.175  1.00182.84           O  
ANISOU 2694  O   SER A 289    20251  32001  17219    -28  -2657  -2390       O  
ATOM   2695  CB  SER A 289      87.182  15.833  50.722  1.00188.64           C  
ANISOU 2695  CB  SER A 289    21557  32546  17571   -357  -2944  -2912       C  
ATOM   2696  N   CYS A 290      89.241  12.999  50.449  1.00186.11           N  
ANISOU 2696  N   CYS A 290    20346  33078  17290     99  -3152  -2652       N  
ATOM   2697  CA  CYS A 290      89.313  11.537  50.348  1.00184.17           C  
ANISOU 2697  CA  CYS A 290    19941  32998  17037    470  -3063  -2391       C  
ATOM   2698  C   CYS A 290      88.233  10.872  51.227  1.00186.61           C  
ANISOU 2698  C   CYS A 290    20606  33160  17138    910  -2907  -2186       C  
ATOM   2699  O   CYS A 290      87.910   9.704  50.988  1.00183.87           O  
ANISOU 2699  O   CYS A 290    20219  32811  16834   1195  -2740  -1923       O  
ATOM   2700  CB  CYS A 290      90.704  11.037  50.727  1.00187.76           C  
ANISOU 2700  CB  CYS A 290    20038  33946  17356    565  -3350  -2497       C  
ATOM   2701  SG  CYS A 290      91.199  11.418  52.427  1.00196.52           S  
ANISOU 2701  SG  CYS A 290    21298  35341  18030    761  -3698  -2743       S  
ATOM   2702  N   GLU A 291      87.688  11.600  52.235  1.00184.92           N  
ANISOU 2702  N   GLU A 291    20743  32825  16693    971  -2959  -2304       N  
ATOM   2703  CA  GLU A 291      86.635  11.090  53.121  1.00184.08           C  
ANISOU 2703  CA  GLU A 291    20992  32571  16378   1383  -2799  -2117       C  
ATOM   2704  C   GLU A 291      85.404  10.684  52.305  1.00183.77           C  
ANISOU 2704  C   GLU A 291    21069  32169  16585   1426  -2432  -1829       C  
ATOM   2705  O   GLU A 291      84.942   9.550  52.449  1.00182.26           O  
ANISOU 2705  O   GLU A 291    20923  31968  16359   1770  -2270  -1573       O  
ATOM   2706  CB  GLU A 291      86.236  12.117  54.212  1.00187.74           C  
ANISOU 2706  CB  GLU A 291    21830  32925  16576   1391  -2899  -2306       C  
ATOM   2707  CG  GLU A 291      87.230  12.328  55.352  1.00202.41           C  
ANISOU 2707  CG  GLU A 291    23670  35133  18102   1487  -3263  -2560       C  
ATOM   2708  CD  GLU A 291      88.540  13.069  55.142  1.00215.27           C  
ANISOU 2708  CD  GLU A 291    25897  35253  20641    726  -3523  -2358       C  
ATOM   2709  OE1 GLU A 291      89.208  13.361  56.160  1.00210.31           O  
ANISOU 2709  OE1 GLU A 291    25338  34801  19769    764  -3818  -2517       O  
ATOM   2710  OE2 GLU A 291      88.896  13.372  53.979  1.00209.46           O  
ANISOU 2710  OE2 GLU A 291    24504  35243  19838    564  -3519  -2618       O  
ATOM   2711  N   VAL A 292      84.909  11.575  51.411  1.00177.99           N  
ANISOU 2711  N   VAL A 292    20378  31146  16105   1075  -2303  -1870       N  
ATOM   2712  CA  VAL A 292      83.743  11.291  50.558  1.00173.64           C  
ANISOU 2712  CA  VAL A 292    19915  30256  15805   1083  -1980  -1621       C  
ATOM   2713  C   VAL A 292      84.126  10.238  49.479  1.00174.34           C  
ANISOU 2713  C   VAL A 292    19679  30430  16132   1086  -1908  -1448       C  
ATOM   2714  O   VAL A 292      83.246   9.511  49.022  1.00171.14           O  
ANISOU 2714  O   VAL A 292    19330  29833  15863   1242  -1672  -1193       O  
ATOM   2715  CB  VAL A 292      83.114  12.556  49.898  1.00176.17           C  
ANISOU 2715  CB  VAL A 292    20389  30245  16301    739  -1868  -1717       C  
ATOM   2716  CG1 VAL A 292      82.453  13.460  50.933  1.00177.29           C  
ANISOU 2716  CG1 VAL A 292    20929  30220  16214    823  -1847  -1798       C  
ATOM   2717  CG2 VAL A 292      84.126  13.331  49.068  1.00176.94           C  
ANISOU 2717  CG2 VAL A 292    20256  30430  16543    312  -2035  -1960       C  
ATOM   2718  N   ILE A 293      85.428  10.142  49.107  1.00171.84           N  
ANISOU 2718  N   ILE A 293    19031  30404  15858    926  -2110  -1585       N  
ATOM   2719  CA  ILE A 293      85.930   9.158  48.132  1.00169.96           C  
ANISOU 2719  CA  ILE A 293    18488  30276  15813    948  -2059  -1435       C  
ATOM   2720  C   ILE A 293      85.892   7.752  48.785  1.00173.50           C  
ANISOU 2720  C   ILE A 293    18940  30901  16080   1405  -2035  -1228       C  
ATOM   2721  O   ILE A 293      85.574   6.771  48.105  1.00171.03           O  
ANISOU 2721  O   ILE A 293    18553  30516  15913   1535  -1871   -999       O  
ATOM   2722  CB  ILE A 293      87.357   9.532  47.614  1.00174.95           C  
ANISOU 2722  CB  ILE A 293    18759  31187  16527    655  -2276  -1643       C  
ATOM   2723  CG1 ILE A 293      87.355  10.941  46.961  1.00175.22           C  
ANISOU 2723  CG1 ILE A 293    18826  31012  16736    198  -2274  -1844       C  
ATOM   2724  CG2 ILE A 293      87.890   8.471  46.624  1.00174.17           C  
ANISOU 2724  CG2 ILE A 293    18360  31206  16612    713  -2208  -1472       C  
ATOM   2725  CD1 ILE A 293      88.745  11.514  46.548  1.00185.51           C  
ANISOU 2725  CD1 ILE A 293    19788  32572  18124   -143  -2485  -2076       C  
ATOM   2726  N   ALA A 294      86.178   7.670  50.105  1.00171.98           N  
ANISOU 2726  N   ALA A 294    18866  30916  15560   1654  -2191  -1308       N  
ATOM   2727  CA  ALA A 294      86.142   6.418  50.872  1.00172.10           C  
ANISOU 2727  CA  ALA A 294    18938  31095  15358   2113  -2166  -1126       C  
ATOM   2728  C   ALA A 294      84.698   5.912  51.031  1.00172.36           C  
ANISOU 2728  C   ALA A 294    19276  30793  15419   2343  -1862   -859       C  
ATOM   2729  O   ALA A 294      84.470   4.699  51.030  1.00171.05           O  
ANISOU 2729  O   ALA A 294    19123  30642  15225   2647  -1733   -626       O  
ATOM   2730  CB  ALA A 294      86.781   6.623  52.236  1.00176.73           C  
ANISOU 2730  CB  ALA A 294    19589  31983  15579   2302  -2427  -1311       C  
ATOM   2731  N   VAL A 295      83.730   6.855  51.148  1.00167.02           N  
ANISOU 2731  N   VAL A 295    18845  29812  14802   2194  -1743   -891       N  
ATOM   2732  CA  VAL A 295      82.289   6.590  51.266  1.00164.41           C  
ANISOU 2732  CA  VAL A 295    18786  29152  14529   2360  -1448   -654       C  
ATOM   2733  C   VAL A 295      81.815   5.894  49.978  1.00163.85           C  
ANISOU 2733  C   VAL A 295    18581  28879  14795   2267  -1241   -441       C  
ATOM   2734  O   VAL A 295      81.194   4.836  50.067  1.00162.47           O  
ANISOU 2734  O   VAL A 295    18482  28607  14642   2524  -1054   -188       O  
ATOM   2735  CB  VAL A 295      81.470   7.890  51.565  1.00168.28           C  
ANISOU 2735  CB  VAL A 295    19546  29395  14999   2206  -1390   -762       C  
ATOM   2736  CG1 VAL A 295      79.961   7.636  51.525  1.00165.89           C  
ANISOU 2736  CG1 VAL A 295    19465  28756  14807   2346  -1070   -503       C  
ATOM   2737  CG2 VAL A 295      81.871   8.501  52.904  1.00171.58           C  
ANISOU 2737  CG2 VAL A 295    20150  29988  15055   2341  -1590   -959       C  
ATOM   2738  N   ILE A 296      82.168   6.456  48.790  1.00157.91           N  
ANISOU 2738  N   ILE A 296    17637  28065  14297   1905  -1279   -546       N  
ATOM   2739  CA  ILE A 296      81.823   5.913  47.463  1.00154.26           C  
ANISOU 2739  CA  ILE A 296    17049  27412  14151   1791  -1115   -379       C  
ATOM   2740  C   ILE A 296      82.260   4.435  47.371  1.00158.11           C  
ANISOU 2740  C   ILE A 296    17404  28060  14612   2058  -1096   -194       C  
ATOM   2741  O   ILE A 296      81.456   3.598  46.965  1.00155.71           O  
ANISOU 2741  O   ILE A 296    17169  27549  14444   2179   -893     42       O  
ATOM   2742  CB  ILE A 296      82.462   6.758  46.309  1.00156.20           C  
ANISOU 2742  CB  ILE A 296    17095  27639  14617   1389  -1199   -554       C  
ATOM   2743  CG1 ILE A 296      81.984   8.230  46.354  1.00156.59           C  
ANISOU 2743  CG1 ILE A 296    17312  27502  14683   1126  -1201   -737       C  
ATOM   2744  CG2 ILE A 296      82.169   6.130  44.928  1.00153.69           C  
ANISOU 2744  CG2 ILE A 296    16668  27126  14603   1309  -1038   -379       C  
ATOM   2745  CD1 ILE A 296      82.712   9.196  45.389  1.00163.23           C  
ANISOU 2745  CD1 ILE A 296    17984  28337  15699    725  -1293   -939       C  
ATOM   2746  N   ASP A 297      83.511   4.123  47.785  1.00157.08           N  
ANISOU 2746  N   ASP A 297    17096  28295  14293   2161  -1309   -300       N  
ATOM   2747  CA  ASP A 297      84.086   2.772  47.722  1.00157.20           C  
ANISOU 2747  CA  ASP A 297    16985  28502  14242   2436  -1311   -144       C  
ATOM   2748  C   ASP A 297      83.263   1.741  48.502  1.00160.71           C  
ANISOU 2748  C   ASP A 297    17670  28845  14547   2820  -1135     97       C  
ATOM   2749  O   ASP A 297      83.052   0.648  47.984  1.00158.97           O  
ANISOU 2749  O   ASP A 297    17433  28554  14414   2971  -1001    309       O  
ATOM   2750  CB  ASP A 297      85.533   2.744  48.265  1.00162.16           C  
ANISOU 2750  CB  ASP A 297    17399  29576  14641   2514  -1589   -321       C  
ATOM   2751  CG  ASP A 297      86.574   3.478  47.440  1.00171.98           C  
ANISOU 2751  CG  ASP A 297    18342  30979  16023   2158  -1765   -536       C  
ATOM   2752  OD1 ASP A 297      86.240   3.934  46.324  1.00170.38           O  
ANISOU 2752  OD1 ASP A 297    18098  30537  16103   1860  -1660   -537       O  
ATOM   2753  OD2 ASP A 297      87.742   3.533  47.877  1.00179.67           O  
ANISOU 2753  OD2 ASP A 297    19113  32327  16829   2190  -2002   -695       O  
ATOM   2754  N   LEU A 298      82.829   2.060  49.740  1.00158.63           N  
ANISOU 2754  N   LEU A 298    17641  28571  14059   2984  -1128     68       N  
ATOM   2755  CA  LEU A 298      82.095   1.084  50.543  1.00158.78           C  
ANISOU 2755  CA  LEU A 298    17896  28502  13932   3363   -943    301       C  
ATOM   2756  C   LEU A 298      80.598   1.085  50.161  1.00159.42           C  
ANISOU 2756  C   LEU A 298    18156  28169  14247   3290   -655    493       C  
ATOM   2757  O   LEU A 298      79.943   0.059  50.336  1.00158.62           O  
ANISOU 2757  O   LEU A 298    18182  27932  14155   3528   -450    740       O  
ATOM   2758  CB  LEU A 298      82.278   1.332  52.067  1.00162.14           C  
ANISOU 2758  CB  LEU A 298    18505  29122  13980   3632  -1056    203       C  
ATOM   2759  CG  LEU A 298      81.885   2.691  52.701  1.00167.98           C  
ANISOU 2759  CG  LEU A 298    19405  29794  14626   3481  -1132      5       C  
ATOM   2760  CD1 LEU A 298      80.383   2.766  52.982  1.00166.84           C  
ANISOU 2760  CD1 LEU A 298    19544  29296  14553   3550   -846    186       C  
ATOM   2761  CD2 LEU A 298      82.563   2.854  54.052  1.00174.10           C  
ANISOU 2761  CD2 LEU A 298    20283  30865  15003   3739  -1344   -147       C  
ATOM   2762  N   ALA A 299      80.071   2.212  49.633  1.00153.90           N  
ANISOU 2762  N   ALA A 299    17462  27274  13738   2965   -637    382       N  
ATOM   2763  CA  ALA A 299      78.654   2.330  49.265  1.00151.27           C  
ANISOU 2763  CA  ALA A 299    17273  26575  13627   2886   -385    543       C  
ATOM   2764  C   ALA A 299      78.380   1.808  47.839  1.00151.48           C  
ANISOU 2764  C   ALA A 299    17149  26410  13996   2702   -283    667       C  
ATOM   2765  O   ALA A 299      77.218   1.591  47.489  1.00149.67           O  
ANISOU 2765  O   ALA A 299    17011  25895  13963   2682    -72    841       O  
ATOM   2766  CB  ALA A 299      78.207   3.781  49.370  1.00151.94           C  
ANISOU 2766  CB  ALA A 299    17459  26544  13726   2660   -413    368       C  
ATOM   2767  N   LEU A 300      79.438   1.605  47.030  1.00146.63           N  
ANISOU 2767  N   LEU A 300    16307  25957  13450   2578   -433    577       N  
ATOM   2768  CA  LEU A 300      79.327   1.137  45.647  1.00143.55           C  
ANISOU 2768  CA  LEU A 300    15784  25407  13352   2419   -364    672       C  
ATOM   2769  C   LEU A 300      78.866  -0.355  45.566  1.00145.35           C  
ANISOU 2769  C   LEU A 300    16078  25522  13625   2666   -196    949       C  
ATOM   2770  O   LEU A 300      77.956  -0.614  44.779  1.00143.07           O  
ANISOU 2770  O   LEU A 300    15826  24945  13590   2565    -42   1086       O  
ATOM   2771  CB  LEU A 300      80.660   1.305  44.901  1.00143.88           C  
ANISOU 2771  CB  LEU A 300    15574  25677  13417   2262   -560    511       C  
ATOM   2772  N   PRO A 301      79.408  -1.346  46.340  1.00142.27           N  
ANISOU 2772  N   PRO A 301    15724  25333  13001   2988   -214   1040       N  
ATOM   2773  CA  PRO A 301      78.909  -2.734  46.195  1.00141.05           C  
ANISOU 2773  CA  PRO A 301    15665  25023  12903   3199    -31   1307       C  
ATOM   2774  C   PRO A 301      77.416  -2.868  46.508  1.00142.47           C  
ANISOU 2774  C   PRO A 301    16042  24886  13203   3231    213   1490       C  
ATOM   2775  O   PRO A 301      76.746  -3.710  45.912  1.00140.50           O  
ANISOU 2775  O   PRO A 301    15836  24404  13143   3243    372   1688       O  
ATOM   2776  CB  PRO A 301      79.736  -3.519  47.213  1.00145.57           C  
ANISOU 2776  CB  PRO A 301    16283  25884  13142   3560    -95   1340       C  
ATOM   2777  CG  PRO A 301      80.945  -2.696  47.441  1.00151.63           C  
ANISOU 2777  CG  PRO A 301    16873  26993  13745   3484   -362   1079       C  
ATOM   2778  CD  PRO A 301      80.491  -1.280  47.342  1.00146.43           C  
ANISOU 2778  CD  PRO A 301    16211  26227  13199   3178   -403    904       C  
ATOM   2779  N   PHE A 302      76.893  -2.025  47.423  1.00139.10           N  
ANISOU 2779  N   PHE A 302    15731  24447  12672   3239    241   1424       N  
ATOM   2780  CA  PHE A 302      75.477  -2.010  47.791  1.00138.18           C  
ANISOU 2780  CA  PHE A 302    15783  24058  12663   3271    478   1591       C  
ATOM   2781  C   PHE A 302      74.628  -1.373  46.686  1.00137.65           C  
ANISOU 2781  C   PHE A 302    15640  23728  12932   2946    534   1576       C  
ATOM   2782  O   PHE A 302      73.561  -1.898  46.365  1.00135.93           O  
ANISOU 2782  O   PHE A 302    15466  23253  12929   2929    726   1771       O  
ATOM   2783  CB  PHE A 302      75.266  -1.257  49.113  1.00142.26           C  
ANISOU 2783  CB  PHE A 302    16466  24665  12920   3426    487   1524       C  
ATOM   2784  CG  PHE A 302      75.879  -1.919  50.323  1.00147.00           C  
ANISOU 2784  CG  PHE A 302    17188  25489  13176   3797    466   1569       C  
ATOM   2785  CD1 PHE A 302      75.150  -2.828  51.082  1.00151.62           C  
ANISOU 2785  CD1 PHE A 302    17958  25951  13698   4082    705   1823       C  
ATOM   2786  CD2 PHE A 302      77.170  -1.603  50.730  1.00151.10           C  
ANISOU 2786  CD2 PHE A 302    17639  26342  13430   3867    209   1358       C  
ATOM   2787  CE1 PHE A 302      75.706  -3.420  52.219  1.00155.20           C  
ANISOU 2787  CE1 PHE A 302    18551  26605  13812   4454    695   1867       C  
ATOM   2788  CE2 PHE A 302      77.729  -2.201  51.864  1.00156.67           C  
ANISOU 2788  CE2 PHE A 302    18462  27266  13798   4237    176   1394       C  
ATOM   2789  CZ  PHE A 302      76.990  -3.099  52.604  1.00155.77           C  
ANISOU 2789  CZ  PHE A 302    18559  27019  13609   4540    423   1649       C  
ATOM   2790  N   ALA A 303      75.103  -0.244  46.105  1.00132.14           N  
ANISOU 2790  N   ALA A 303    14830  23097  12281   2688    367   1345       N  
ATOM   2791  CA  ALA A 303      74.415   0.483  45.037  1.00129.14           C  
ANISOU 2791  CA  ALA A 303    14390  22492  12187   2391    400   1301       C  
ATOM   2792  C   ALA A 303      74.312  -0.366  43.766  1.00130.50           C  
ANISOU 2792  C   ALA A 303    14454  22506  12625   2290    435   1416       C  
ATOM   2793  O   ALA A 303      73.332  -0.236  43.026  1.00128.62           O  
ANISOU 2793  O   ALA A 303    14214  22015  12641   2139    537   1486       O  
ATOM   2794  CB  ALA A 303      75.145   1.779  44.740  1.00129.69           C  
ANISOU 2794  CB  ALA A 303    14378  22686  12211   2164    212   1027       C  
ATOM   2795  N   ILE A 304      75.323  -1.238  43.527  1.00126.76           N  
ANISOU 2795  N   ILE A 304    13900  22186  12078   2390    345   1434       N  
ATOM   2796  CA  ILE A 304      75.392  -2.178  42.398  1.00124.72           C  
ANISOU 2796  CA  ILE A 304    13573  21797  12018   2345    365   1545       C  
ATOM   2797  C   ILE A 304      74.315  -3.270  42.590  1.00128.64           C  
ANISOU 2797  C   ILE A 304    14197  22062  12618   2487    573   1807       C  
ATOM   2798  O   ILE A 304      73.690  -3.683  41.611  1.00127.21           O  
ANISOU 2798  O   ILE A 304    13999  21641  12692   2365    636   1905       O  
ATOM   2799  CB  ILE A 304      76.827  -2.784  42.257  1.00128.23           C  
ANISOU 2799  CB  ILE A 304    13911  22503  12307   2456    217   1493       C  
ATOM   2800  CG1 ILE A 304      77.832  -1.692  41.791  1.00128.29           C  
ANISOU 2800  CG1 ILE A 304    13752  22710  12280   2255     22   1239       C  
ATOM   2801  CG2 ILE A 304      76.842  -3.977  41.280  1.00127.49           C  
ANISOU 2801  CG2 ILE A 304    13805  22258  12376   2476    263   1643       C  
ATOM   2802  CD1 ILE A 304      79.306  -2.096  41.737  1.00134.27           C  
ANISOU 2802  CD1 ILE A 304    14361  23778  12879   2354   -136   1167       C  
ATOM   2803  N   LEU A 305      74.077  -3.697  43.844  1.00126.57           N  
ANISOU 2803  N   LEU A 305    14068  21862  12160   2737    681   1917       N  
ATOM   2804  CA  LEU A 305      73.081  -4.721  44.157  1.00126.79           C  
ANISOU 2804  CA  LEU A 305    14224  21676  12275   2876    903   2174       C  
ATOM   2805  C   LEU A 305      71.657  -4.230  43.820  1.00130.22           C  
ANISOU 2805  C   LEU A 305    14662  21834  12980   2692   1045   2246       C  
ATOM   2806  O   LEU A 305      70.875  -5.008  43.271  1.00129.37           O  
ANISOU 2806  O   LEU A 305    14567  21487  13101   2643   1169   2417       O  
ATOM   2807  CB  LEU A 305      73.171  -5.120  45.641  1.00129.21           C  
ANISOU 2807  CB  LEU A 305    14685  22124  12285   3200    996   2264       C  
ATOM   2808  CG  LEU A 305      72.294  -6.288  46.098  1.00134.83           C  
ANISOU 2808  CG  LEU A 305    15548  22633  13050   3379   1248   2543       C  
ATOM   2809  CD1 LEU A 305      72.697  -7.586  45.406  1.00134.59           C  
ANISOU 2809  CD1 LEU A 305    15524  22518  13097   3420   1255   2662       C  
ATOM   2810  CD2 LEU A 305      72.388  -6.467  47.584  1.00140.04           C  
ANISOU 2810  CD2 LEU A 305    16376  23440  13393   3707   1341   2611       C  
ATOM   2811  N   LEU A 306      71.334  -2.941  44.116  1.00126.92           N  
ANISOU 2811  N   LEU A 306    14235  21450  12538   2589   1020   2111       N  
ATOM   2812  CA  LEU A 306      70.021  -2.346  43.820  1.00125.91           C  
ANISOU 2812  CA  LEU A 306    14101  21095  12644   2433   1146   2165       C  
ATOM   2813  C   LEU A 306      69.743  -2.331  42.309  1.00127.43           C  
ANISOU 2813  C   LEU A 306    14169  21102  13146   2174   1085   2138       C  
ATOM   2814  O   LEU A 306      68.585  -2.424  41.906  1.00126.51           O  
ANISOU 2814  O   LEU A 306    14034  20761  13274   2080   1207   2258       O  
ATOM   2815  CB  LEU A 306      69.895  -0.920  44.379  1.00126.38           C  
ANISOU 2815  CB  LEU A 306    14200  21243  12576   2391   1111   2004       C  
ATOM   2816  CG  LEU A 306      69.794  -0.758  45.902  1.00133.34           C  
ANISOU 2816  CG  LEU A 306    15241  22251  13172   2647   1201   2041       C  
ATOM   2817  CD1 LEU A 306      69.834   0.710  46.290  1.00133.83           C  
ANISOU 2817  CD1 LEU A 306    15357  22397  13094   2577   1121   1841       C  
ATOM   2818  CD2 LEU A 306      68.521  -1.409  46.456  1.00136.17           C  
ANISOU 2818  CD2 LEU A 306    15687  22427  13625   2792   1475   2310       C  
ATOM   2819  N   GLY A 307      70.801  -2.237  41.501  1.00122.59           N  
ANISOU 2819  N   GLY A 307    13471  20591  12516   2074    899   1986       N  
ATOM   2820  CA  GLY A 307      70.711  -2.298  40.046  1.00120.06           C  
ANISOU 2820  CA  GLY A 307    13058  20112  12448   1864    826   1952       C  
ATOM   2821  C   GLY A 307      70.189  -3.648  39.596  1.00122.64           C  
ANISOU 2821  C   GLY A 307    13408  20237  12953   1901    915   2157       C  
ATOM   2822  O   GLY A 307      69.273  -3.716  38.772  1.00121.25           O  
ANISOU 2822  O   GLY A 307    13198  19829  13043   1750    953   2214       O  
ATOM   2823  N   PHE A 308      70.739  -4.738  40.182  1.00119.63           N  
ANISOU 2823  N   PHE A 308    13098  19941  12416   2112    950   2269       N  
ATOM   2824  CA  PHE A 308      70.298  -6.116  39.930  1.00119.47           C  
ANISOU 2824  CA  PHE A 308    13145  19723  12524   2174   1053   2475       C  
ATOM   2825  C   PHE A 308      68.919  -6.373  40.530  1.00122.93           C  
ANISOU 2825  C   PHE A 308    13636  19967  13106   2186   1267   2663       C  
ATOM   2826  O   PHE A 308      68.186  -7.217  40.020  1.00122.07           O  
ANISOU 2826  O   PHE A 308    13538  19616  13227   2109   1343   2805       O  
ATOM   2827  CB  PHE A 308      71.295  -7.151  40.494  1.00122.83           C  
ANISOU 2827  CB  PHE A 308    13662  20303  12705   2428   1052   2546       C  
ATOM   2828  CG  PHE A 308      72.634  -7.248  39.804  1.00123.96           C  
ANISOU 2828  CG  PHE A 308    13744  20617  12738   2440    866   2416       C  
ATOM   2829  CD1 PHE A 308      72.783  -8.004  38.645  1.00126.21           C  
ANISOU 2829  CD1 PHE A 308    14037  20746  13172   2374    819   2461       C  
ATOM   2830  CD2 PHE A 308      73.770  -6.688  40.375  1.00126.86           C  
ANISOU 2830  CD2 PHE A 308    14054  21307  12839   2542    744   2265       C  
ATOM   2831  CE1 PHE A 308      74.029  -8.128  38.026  1.00126.73           C  
ANISOU 2831  CE1 PHE A 308    14047  20976  13127   2414    670   2362       C  
ATOM   2832  CE2 PHE A 308      75.020  -6.829  39.766  1.00129.42           C  
ANISOU 2832  CE2 PHE A 308    14295  21808  13069   2564    588   2164       C  
ATOM   2833  CZ  PHE A 308      75.139  -7.541  38.590  1.00126.46           C  
ANISOU 2833  CZ  PHE A 308    13925  21276  12846   2507    562   2219       C  
ATOM   2834  N   THR A 309      68.577  -5.659  41.626  1.00120.17           N  
ANISOU 2834  N   THR A 309    13320  19721  12617   2286   1364   2665       N  
ATOM   2835  CA  THR A 309      67.298  -5.789  42.334  1.00120.94           C  
ANISOU 2835  CA  THR A 309    13459  19669  12822   2329   1592   2850       C  
ATOM   2836  C   THR A 309      66.160  -5.274  41.423  1.00122.72           C  
ANISOU 2836  C   THR A 309    13565  19685  13379   2077   1607   2852       C  
ATOM   2837  O   THR A 309      65.039  -5.765  41.532  1.00123.06           O  
ANISOU 2837  O   THR A 309    13594  19538  13625   2049   1778   3037       O  
ATOM   2838  CB  THR A 309      67.359  -5.042  43.679  1.00130.38           C  
ANISOU 2838  CB  THR A 309    14736  21050  13754   2510   1665   2820       C  
ATOM   2839  OG1 THR A 309      68.463  -5.546  44.426  1.00131.15           O  
ANISOU 2839  OG1 THR A 309    14936  21352  13542   2750   1622   2805       O  
ATOM   2840  CG2 THR A 309      66.092  -5.204  44.509  1.00130.90           C  
ANISOU 2840  CG2 THR A 309    14855  20978  13905   2594   1929   3030       C  
ATOM   2841  N   ASN A 310      66.463  -4.347  40.483  1.00116.83           N  
ANISOU 2841  N   ASN A 310    12727  18969  12694   1896   1430   2651       N  
ATOM   2842  CA  ASN A 310      65.472  -3.844  39.521  1.00114.86           C  
ANISOU 2842  CA  ASN A 310    12370  18535  12737   1678   1417   2632       C  
ATOM   2843  C   ASN A 310      64.976  -4.993  38.618  1.00116.65           C  
ANISOU 2843  C   ASN A 310    12562  18526  13232   1573   1421   2760       C  
ATOM   2844  O   ASN A 310      63.825  -4.976  38.190  1.00116.41           O  
ANISOU 2844  O   ASN A 310    12449  18317  13465   1444   1481   2837       O  
ATOM   2845  CB  ASN A 310      66.058  -2.704  38.674  1.00114.57           C  
ANISOU 2845  CB  ASN A 310    12279  18575  12678   1531   1228   2390       C  
ATOM   2846  CG  ASN A 310      65.072  -2.016  37.749  1.00138.14           C  
ANISOU 2846  CG  ASN A 310    15176  21398  15914   1344   1215   2352       C  
ATOM   2847  OD1 ASN A 310      65.301  -1.903  36.542  1.00132.95           O  
ANISOU 2847  OD1 ASN A 310    14472  20662  15379   1200   1075   2245       O  
ATOM   2848  ND2 ASN A 310      63.938  -1.571  38.281  1.00129.75           N  
ANISOU 2848  ND2 ASN A 310    14091  20279  14929   1363   1368   2448       N  
ATOM   2849  N   SER A 311      65.834  -6.013  38.382  1.00111.77           N  
ANISOU 2849  N   SER A 311    12016  17912  12539   1643   1360   2789       N  
ATOM   2850  CA  SER A 311      65.507  -7.197  37.580  1.00110.76           C  
ANISOU 2850  CA  SER A 311    11906  17553  12624   1565   1355   2905       C  
ATOM   2851  C   SER A 311      64.580  -8.153  38.359  1.00114.40           C  
ANISOU 2851  C   SER A 311    12415  17863  13189   1629   1581   3151       C  
ATOM   2852  O   SER A 311      64.003  -9.065  37.761  1.00113.64           O  
ANISOU 2852  O   SER A 311    12324  17534  13321   1524   1602   3263       O  
ATOM   2853  CB  SER A 311      66.780  -7.924  37.154  1.00113.67           C  
ANISOU 2853  CB  SER A 311    12364  17988  12838   1654   1233   2859       C  
ATOM   2854  OG  SER A 311      67.613  -7.084  36.369  1.00117.90           O  
ANISOU 2854  OG  SER A 311    12841  18652  13303   1582   1043   2647       O  
ATOM   2855  N   CYS A 312      64.442  -7.936  39.686  1.00111.97           N  
ANISOU 2855  N   CYS A 312    12151  17678  12712   1801   1752   3235       N  
ATOM   2856  CA  CYS A 312      63.547  -8.702  40.566  1.00113.78           C  
ANISOU 2856  CA  CYS A 312    12428  17783  13021   1884   2006   3478       C  
ATOM   2857  C   CYS A 312      62.176  -8.042  40.593  1.00117.92           C  
ANISOU 2857  C   CYS A 312    12806  18212  13785   1751   2118   3537       C  
ATOM   2858  O   CYS A 312      61.174  -8.708  40.849  1.00119.17           O  
ANISOU 2858  O   CYS A 312    12932  18195  14154   1708   2301   3737       O  
ATOM   2859  CB  CYS A 312      64.127  -8.815  41.976  1.00115.37           C  
ANISOU 2859  CB  CYS A 312    12775  18168  12891   2175   2139   3542       C  
ATOM   2860  SG  CYS A 312      65.800  -9.503  42.048  1.00118.94           S  
ANISOU 2860  SG  CYS A 312    13377  18795  13019   2376   1998   3462       S  
ATOM   2861  N   VAL A 313      62.149  -6.715  40.358  1.00112.86           N  
ANISOU 2861  N   VAL A 313    12082  17696  13104   1694   2016   3366       N  
ATOM   2862  CA  VAL A 313      60.954  -5.874  40.370  1.00112.51           C  
ANISOU 2862  CA  VAL A 313    11905  17608  13234   1602   2103   3392       C  
ATOM   2863  C   VAL A 313      60.204  -6.003  39.028  1.00115.60           C  
ANISOU 2863  C   VAL A 313    12143  17805  13974   1347   1991   3369       C  
ATOM   2864  O   VAL A 313      58.985  -6.158  39.046  1.00116.03           O  
ANISOU 2864  O   VAL A 313    12071  17738  14276   1264   2118   3504       O  
ATOM   2865  CB  VAL A 313      61.326  -4.393  40.667  1.00115.35           C  
ANISOU 2865  CB  VAL A 313    12283  18172  13373   1661   2031   3204       C  
ATOM   2866  CG1 VAL A 313      60.093  -3.488  40.643  1.00115.29           C  
ANISOU 2866  CG1 VAL A 313    12160  18122  13522   1597   2130   3234       C  
ATOM   2867  CG2 VAL A 313      62.056  -4.267  42.004  1.00116.42           C  
ANISOU 2867  CG2 VAL A 313    12577  18502  13155   1914   2112   3209       C  
ATOM   2868  N   ASN A 314      60.932  -5.947  37.880  1.00111.21           N  
ANISOU 2868  N   ASN A 314    11596  17227  13433   1236   1755   3201       N  
ATOM   2869  CA  ASN A 314      60.389  -6.001  36.508  1.00110.47           C  
ANISOU 2869  CA  ASN A 314    11392  16960  13623   1018   1604   3141       C  
ATOM   2870  C   ASN A 314      59.353  -7.163  36.290  1.00117.32           C  
ANISOU 2870  C   ASN A 314    12190  17584  14801    900   1690   3335       C  
ATOM   2871  O   ASN A 314      58.325  -6.877  35.676  1.00117.14           O  
ANISOU 2871  O   ASN A 314    12013  17454  15041    744   1656   3338       O  
ATOM   2872  CB  ASN A 314      61.509  -6.147  35.460  1.00107.89           C  
ANISOU 2872  CB  ASN A 314    11140  16637  13217    972   1371   2968       C  
ATOM   2873  CG  ASN A 314      62.371  -4.910  35.265  1.00123.16           C  
ANISOU 2873  CG  ASN A 314    13092  18762  14942    998   1246   2748       C  
ATOM   2874  OD1 ASN A 314      62.019  -3.785  35.651  1.00113.02           O  
ANISOU 2874  OD1 ASN A 314    11763  17575  13605   1008   1293   2687       O  
ATOM   2875  ND2 ASN A 314      63.481  -5.079  34.562  1.00113.16           N  
ANISOU 2875  ND2 ASN A 314    11893  17533  13568    996   1084   2624       N  
ATOM   2876  N   PRO A 315      59.542  -8.433  36.749  1.00115.99           N  
ANISOU 2876  N   PRO A 315    12129  17320  14623    960   1795   3493       N  
ATOM   2877  CA  PRO A 315      58.516  -9.462  36.474  1.00117.81           C  
ANISOU 2877  CA  PRO A 315    12292  17297  15174    805   1867   3661       C  
ATOM   2878  C   PRO A 315      57.133  -9.094  37.047  1.00124.25           C  
ANISOU 2878  C   PRO A 315    12921  18083  16205    751   2065   3813       C  
ATOM   2879  O   PRO A 315      56.137  -9.208  36.325  1.00124.95           O  
ANISOU 2879  O   PRO A 315    12851  18009  16616    551   2026   3856       O  
ATOM   2880  CB  PRO A 315      59.071 -10.713  37.164  1.00120.98           C  
ANISOU 2880  CB  PRO A 315    12885  17635  15448    934   1995   3809       C  
ATOM   2881  CG  PRO A 315      60.103 -10.221  38.098  1.00124.94           C  
ANISOU 2881  CG  PRO A 315    13508  18388  15576   1186   2052   3762       C  
ATOM   2882  CD  PRO A 315      60.691  -9.020  37.464  1.00118.03           C  
ANISOU 2882  CD  PRO A 315    12578  17683  14584   1163   1844   3521       C  
ATOM   2883  N   PHE A 316      57.076  -8.625  38.318  1.00121.30           N  
ANISOU 2883  N   PHE A 316    12563  17874  15649    935   2269   3889       N  
ATOM   2884  CA  PHE A 316      55.836  -8.219  38.990  1.00122.53           C  
ANISOU 2884  CA  PHE A 316    12555  18029  15972    930   2490   4050       C  
ATOM   2885  C   PHE A 316      55.231  -6.966  38.350  1.00124.35           C  
ANISOU 2885  C   PHE A 316    12609  18334  16303    843   2380   3918       C  
ATOM   2886  O   PHE A 316      54.040  -6.929  38.058  1.00125.14           O  
ANISOU 2886  O   PHE A 316    12501  18352  16694    716   2440   4013       O  
ATOM   2887  CB  PHE A 316      56.087  -7.945  40.491  1.00125.61           C  
ANISOU 2887  CB  PHE A 316    13064  18571  16091   1195   2742   4167       C  
ATOM   2888  CG  PHE A 316      56.660  -9.070  41.325  1.00128.54           C  
ANISOU 2888  CG  PHE A 316    13638  18900  16301   1345   2881   4303       C  
ATOM   2889  CD1 PHE A 316      55.833 -10.054  41.857  1.00133.94           C  
ANISOU 2889  CD1 PHE A 316    14305  19392  17193   1300   3104   4549       C  
ATOM   2890  CD2 PHE A 316      58.001  -9.067  41.696  1.00129.77           C  
ANISOU 2890  CD2 PHE A 316    14001  19222  16085   1552   2814   4195       C  
ATOM   2891  CE1 PHE A 316      56.354 -11.067  42.668  1.00136.19           C  
ANISOU 2891  CE1 PHE A 316    14808  19629  17309   1464   3255   4682       C  
ATOM   2892  CE2 PHE A 316      58.521 -10.078  42.513  1.00133.95           C  
ANISOU 2892  CE2 PHE A 316    14727  19727  16440   1729   2949   4325       C  
ATOM   2893  CZ  PHE A 316      57.694 -11.071  42.993  1.00134.33           C  
ANISOU 2893  CZ  PHE A 316    14786  19567  16687   1693   3176   4571       C  
ATOM   2894  N   LEU A 317      56.081  -5.958  38.120  1.00118.40           N  
ANISOU 2894  N   LEU A 317    11942  17740  15305    916   2223   3703       N  
ATOM   2895  CA  LEU A 317      55.790  -4.613  37.630  1.00116.80           C  
ANISOU 2895  CA  LEU A 317    11648  17630  15099    886   2126   3550       C  
ATOM   2896  C   LEU A 317      55.237  -4.575  36.170  1.00119.57           C  
ANISOU 2896  C   LEU A 317    11850  17846  15734    666   1915   3453       C  
ATOM   2897  O   LEU A 317      54.644  -3.559  35.795  1.00118.40           O  
ANISOU 2897  O   LEU A 317    11592  17746  15647    640   1875   3376       O  
ATOM   2898  CB  LEU A 317      57.119  -3.830  37.686  1.00114.92           C  
ANISOU 2898  CB  LEU A 317    11586  17564  14515    998   1997   3338       C  
ATOM   2899  CG  LEU A 317      57.108  -2.315  37.533  1.00118.42           C  
ANISOU 2899  CG  LEU A 317    12024  18134  14837   1027   1942   3173       C  
ATOM   2900  CD1 LEU A 317      56.336  -1.658  38.651  1.00120.07           C  
ANISOU 2900  CD1 LEU A 317    12206  18426  14987   1170   2178   3301       C  
ATOM   2901  CD2 LEU A 317      58.521  -1.774  37.547  1.00119.70           C  
ANISOU 2901  CD2 LEU A 317    12357  18441  14682   1098   1808   2971       C  
ATOM   2902  N   TYR A 318      55.422  -5.645  35.358  1.00116.37           N  
ANISOU 2902  N   TYR A 318    11459  17270  15485    528   1782   3454       N  
ATOM   2903  CA  TYR A 318      54.962  -5.617  33.961  1.00115.48           C  
ANISOU 2903  CA  TYR A 318    11238  17025  15613    339   1558   3347       C  
ATOM   2904  C   TYR A 318      54.140  -6.858  33.563  1.00122.87           C  
ANISOU 2904  C   TYR A 318    12071  17735  16877    161   1551   3488       C  
ATOM   2905  O   TYR A 318      53.123  -6.697  32.894  1.00122.95           O  
ANISOU 2905  O   TYR A 318    11902  17660  17153     12   1447   3468       O  
ATOM   2906  CB  TYR A 318      56.156  -5.503  32.988  1.00113.62           C  
ANISOU 2906  CB  TYR A 318    11165  16791  15215    331   1315   3131       C  
ATOM   2907  CG  TYR A 318      56.981  -4.248  33.163  1.00112.34           C  
ANISOU 2907  CG  TYR A 318    11091  16826  14768    451   1281   2961       C  
ATOM   2908  CD1 TYR A 318      56.609  -3.055  32.553  1.00112.99           C  
ANISOU 2908  CD1 TYR A 318    11103  16947  14880    416   1190   2823       C  
ATOM   2909  CD2 TYR A 318      58.155  -4.262  33.906  1.00112.28           C  
ANISOU 2909  CD2 TYR A 318    11245  16959  14456    596   1328   2927       C  
ATOM   2910  CE1 TYR A 318      57.364  -1.896  32.714  1.00112.07           C  
ANISOU 2910  CE1 TYR A 318    11088  16987  14507    506   1167   2663       C  
ATOM   2911  CE2 TYR A 318      58.915  -3.108  34.080  1.00111.71           C  
ANISOU 2911  CE2 TYR A 318    11249  17061  14136    677   1286   2760       C  
ATOM   2912  CZ  TYR A 318      58.515  -1.926  33.484  1.00118.40           C  
ANISOU 2912  CZ  TYR A 318    12037  17923  15025    622   1211   2629       C  
ATOM   2913  OH  TYR A 318      59.268  -0.791  33.653  1.00119.30           O  
ANISOU 2913  OH  TYR A 318    12244  18184  14899    684   1178   2462       O  
ATOM   2914  N   CYS A 319      54.601  -8.080  33.897  1.00122.07           N  
ANISOU 2914  N   CYS A 319    12096  17531  16755    173   1639   3613       N  
ATOM   2915  CA  CYS A 319      53.910  -9.299  33.466  1.00124.63           C  
ANISOU 2915  CA  CYS A 319    12362  17611  17379    -15   1622   3732       C  
ATOM   2916  C   CYS A 319      52.705  -9.598  34.365  1.00134.09           C  
ANISOU 2916  C   CYS A 319    13373  18770  18807    -63   1888   3974       C  
ATOM   2917  O   CYS A 319      51.636  -9.918  33.840  1.00135.35           O  
ANISOU 2917  O   CYS A 319    13344  18776  19305   -270   1844   4036       O  
ATOM   2918  CB  CYS A 319      54.861 -10.491  33.440  1.00124.73           C  
ANISOU 2918  CB  CYS A 319    12624  17506  17262     21   1598   3756       C  
ATOM   2919  SG  CYS A 319      54.081 -12.051  32.936  1.00131.01           S  
ANISOU 2919  SG  CYS A 319    13413  17964  18403   -217   1578   3896       S  
ATOM   2920  N   PHE A 320      52.883  -9.563  35.699  1.00133.57           N  
ANISOU 2920  N   PHE A 320    13360  18832  18560    126   2162   4114       N  
ATOM   2921  CA  PHE A 320      51.822  -9.952  36.625  1.00137.32           C  
ANISOU 2921  CA  PHE A 320    13679  19259  19236    104   2452   4369       C  
ATOM   2922  C   PHE A 320      50.825  -8.784  36.863  1.00144.86           C  
ANISOU 2922  C   PHE A 320    14390  20371  20280    137   2541   4392       C  
ATOM   2923  O   PHE A 320      49.669  -8.909  36.452  1.00146.36           O  
ANISOU 2923  O   PHE A 320    14318  20483  20810    -42   2537   4465       O  
ATOM   2924  CB  PHE A 320      52.412 -10.443  37.966  1.00139.91           C  
ANISOU 2924  CB  PHE A 320    14211  19625  19323    317   2726   4533       C  
ATOM   2925  CG  PHE A 320      53.374 -11.607  37.819  1.00140.85           C  
ANISOU 2925  CG  PHE A 320    14583  19602  19329    323   2662   4526       C  
ATOM   2926  CD1 PHE A 320      52.904 -12.899  37.610  1.00145.61           C  
ANISOU 2926  CD1 PHE A 320    15187  19942  20195    137   2702   4660       C  
ATOM   2927  CD2 PHE A 320      54.744 -11.418  37.935  1.00140.47           C  
ANISOU 2927  CD2 PHE A 320    14777  19686  18909    520   2573   4394       C  
ATOM   2928  CE1 PHE A 320      53.793 -13.968  37.460  1.00146.19           C  
ANISOU 2928  CE1 PHE A 320    15526  19876  20143    164   2649   4656       C  
ATOM   2929  CE2 PHE A 320      55.632 -12.487  37.794  1.00142.98           C  
ANISOU 2929  CE2 PHE A 320    15328  19890  19110    554   2519   4396       C  
ATOM   2930  CZ  PHE A 320      55.151 -13.756  37.562  1.00142.97           C  
ANISOU 2930  CZ  PHE A 320    15352  19617  19354    387   2564   4530       C  
ATOM   2931  N   VAL A 321      51.261  -7.669  37.506  1.00142.31           N  
ANISOU 2931  N   VAL A 321    14153  20265  19652    363   2611   4326       N  
ATOM   2932  CA  VAL A 321      50.395  -6.513  37.832  1.00143.47           C  
ANISOU 2932  CA  VAL A 321    14124  20566  19823    441   2713   4347       C  
ATOM   2933  C   VAL A 321      50.023  -5.750  36.519  1.00147.44           C  
ANISOU 2933  C   VAL A 321    14480  21074  20468    301   2431   4148       C  
ATOM   2934  O   VAL A 321      48.932  -5.179  36.432  1.00148.10           O  
ANISOU 2934  O   VAL A 321    14333  21214  20724    279   2480   4196       O  
ATOM   2935  CB  VAL A 321      51.066  -5.563  38.881  1.00146.55           C  
ANISOU 2935  CB  VAL A 321    14705  21163  19814    724   2844   4310       C  
ATOM   2936  CG1 VAL A 321      50.192  -4.346  39.194  1.00146.89           C  
ANISOU 2936  CG1 VAL A 321    14603  21348  19862    825   2962   4340       C  
ATOM   2937  CG2 VAL A 321      51.398  -6.316  40.171  1.00147.94           C  
ANISOU 2937  CG2 VAL A 321    15045  21334  19832    889   3106   4500       C  
ATOM   2938  N   GLY A 322      50.901  -5.806  35.517  1.00143.06           N  
ANISOU 2938  N   GLY A 322    14059  20455  19844    220   2152   3943       N  
ATOM   2939  CA  GLY A 322      50.696  -5.153  34.228  1.00142.06           C  
ANISOU 2939  CA  GLY A 322    13848  20310  19818    107   1877   3745       C  
ATOM   2940  C   GLY A 322      49.625  -5.758  33.337  1.00149.19           C  
ANISOU 2940  C   GLY A 322    14505  21057  21122   -122   1765   3795       C  
ATOM   2941  O   GLY A 322      49.271  -5.162  32.316  1.00148.07           O  
ANISOU 2941  O   GLY A 322    14265  20917  21079   -191   1554   3648       O  
ATOM   2942  N   ASN A 323      49.102  -6.948  33.702  1.00149.39           N  
ANISOU 2942  N   ASN A 323    14439  20943  21380   -243   1900   3996       N  
ATOM   2943  CA  ASN A 323      48.040  -7.619  32.941  1.00151.97           C  
ANISOU 2943  CA  ASN A 323    14514  21114  22113   -491   1796   4052       C  
ATOM   2944  C   ASN A 323      46.688  -6.907  33.172  1.00158.70           C  
ANISOU 2944  C   ASN A 323    15036  22095  23170   -486   1926   4162       C  
ATOM   2945  O   ASN A 323      45.835  -6.903  32.280  1.00159.38           O  
ANISOU 2945  O   ASN A 323    14884  22137  23536   -647   1754   4118       O  
ATOM   2946  CB  ASN A 323      47.950  -9.105  33.329  1.00156.04           C  
ANISOU 2946  CB  ASN A 323    15059  21422  22807   -636   1913   4232       C  
ATOM   2947  CG  ASN A 323      46.951  -9.926  32.530  1.00186.38           C  
ANISOU 2947  CG  ASN A 323    18668  25076  27071   -928   1771   4266       C  
ATOM   2948  OD1 ASN A 323      46.593  -9.607  31.386  1.00180.67           O  
ANISOU 2948  OD1 ASN A 323    17923  24279  26443  -1049   1455   4081       O  
ATOM   2949  ND2 ASN A 323      46.550 -11.057  33.086  1.00182.71           N  
ANISOU 2949  ND2 ASN A 323    18048  24511  26861  -1051   1998   4502       N  
ATOM   2950  N   ARG A 324      46.506  -6.300  34.369  1.00156.24           N  
ANISOU 2950  N   ARG A 324    14712  21944  22706   -285   2228   4307       N  
ATOM   2951  CA  ARG A 324      45.291  -5.559  34.727  1.00157.88           C  
ANISOU 2951  CA  ARG A 324    14631  22297  23058   -225   2394   4431       C  
ATOM   2952  C   ARG A 324      45.256  -4.201  34.016  1.00160.07           C  
ANISOU 2952  C   ARG A 324    14894  22722  23204   -121   2214   4227       C  
ATOM   2953  O   ARG A 324      44.171  -3.674  33.763  1.00161.01           O  
ANISOU 2953  O   ARG A 324    14741  22933  23503   -120   2235   4275       O  
ATOM   2954  CB  ARG A 324      45.183  -5.358  36.248  1.00158.85           C  
ANISOU 2954  CB  ARG A 324    14801  22534  23022    -10   2779   4649       C  
ATOM   2955  CG  ARG A 324      45.139  -6.643  37.073  1.00170.44           C  
ANISOU 2955  CG  ARG A 324    16294  23859  24605    -77   3015   4881       C  
ATOM   2956  CD  ARG A 324      44.955  -6.350  38.554  1.00182.66           C  
ANISOU 2956  CD  ARG A 324    17880  25529  25992    168   3404   5101       C  
ATOM   2957  NE  ARG A 324      46.044  -5.543  39.111  1.00190.36           N  
ANISOU 2957  NE  ARG A 324    19171  26646  26513    439   3417   4976       N  
ATOM   2958  CZ  ARG A 324      46.086  -5.098  40.364  1.00206.52           C  
ANISOU 2958  CZ  ARG A 324    21322  28817  28328    700   3705   5110       C  
ATOM   2959  NH1 ARG A 324      45.095  -5.371  41.206  1.00197.70           N  
ANISOU 2959  NH1 ARG A 324    20022  27706  27389    745   4030   5389       N  
ATOM   2960  NH2 ARG A 324      47.111  -4.368  40.782  1.00191.16           N  
ANISOU 2960  NH2 ARG A 324    19666  26992  25976    918   3671   4966       N  
ATOM   2961  N   PHE A 325      46.449  -3.643  33.685  1.00154.02           N  
ANISOU 2961  N   PHE A 325    14422  21978  22122    -28   2045   4005       N  
ATOM   2962  CA  PHE A 325      46.614  -2.365  32.977  1.00152.08           C  
ANISOU 2962  CA  PHE A 325    14230  21838  21716     68   1871   3790       C  
ATOM   2963  C   PHE A 325      45.903  -2.426  31.617  1.00158.73           C  
ANISOU 2963  C   PHE A 325    14868  22600  22841   -106   1599   3687       C  
ATOM   2964  O   PHE A 325      45.372  -1.421  31.157  1.00158.25           O  
ANISOU 2964  O   PHE A 325    14696  22644  22787    -31   1537   3613       O  
ATOM   2965  CB  PHE A 325      48.117  -2.043  32.802  1.00150.33           C  
ANISOU 2965  CB  PHE A 325    14357  21620  21141    151   1746   3586       C  
ATOM   2966  CG  PHE A 325      48.464  -0.645  32.330  1.00149.25           C  
ANISOU 2966  CG  PHE A 325    14335  21591  20780    273   1631   3377       C  
ATOM   2967  CD1 PHE A 325      48.500  -0.337  30.975  1.00150.64           C  
ANISOU 2967  CD1 PHE A 325    14520  21698  21017    186   1348   3181       C  
ATOM   2968  CD2 PHE A 325      48.849   0.336  33.237  1.00150.28           C  
ANISOU 2968  CD2 PHE A 325    14606  21876  20618    479   1804   3370       C  
ATOM   2969  CE1 PHE A 325      48.846   0.947  30.540  1.00149.51           C  
ANISOU 2969  CE1 PHE A 325    14510  21637  20661    301   1264   2994       C  
ATOM   2970  CE2 PHE A 325      49.211   1.614  32.800  1.00151.02           C  
ANISOU 2970  CE2 PHE A 325    14836  22045  20501    576   1706   3174       C  
ATOM   2971  CZ  PHE A 325      49.199   1.914  31.456  1.00147.80           C  
ANISOU 2971  CZ  PHE A 325    14425  21564  20169    485   1447   2992       C  
ATOM   2972  N   GLN A 326      45.874  -3.626  31.004  1.00157.73           N  
ANISOU 2972  N   GLN A 326    14703  22284  22943   -326   1441   3689       N  
ATOM   2973  CA  GLN A 326      45.224  -3.938  29.728  1.00159.08           C  
ANISOU 2973  CA  GLN A 326    14692  22344  23406   -518   1160   3598       C  
ATOM   2974  C   GLN A 326      43.694  -3.793  29.832  1.00167.02           C  
ANISOU 2974  C   GLN A 326    15296  23433  24733   -577   1245   3748       C  
ATOM   2975  O   GLN A 326      43.075  -3.168  28.970  1.00166.53           O  
ANISOU 2975  O   GLN A 326    15078  23436  24762   -569   1067   3641       O  
ATOM   2976  CB  GLN A 326      45.595  -5.381  29.316  1.00161.17           C  
ANISOU 2976  CB  GLN A 326    15042  22371  23826   -735   1031   3607       C  
ATOM   2977  CG  GLN A 326      44.979  -5.876  28.003  1.00180.29           C  
ANISOU 2977  CG  GLN A 326    17290  24644  26566   -959    729   3521       C  
ATOM   2978  CD  GLN A 326      45.186  -7.360  27.755  1.00201.43           C  
ANISOU 2978  CD  GLN A 326    20040  27070  29423  -1183    648   3570       C  
ATOM   2979  OE1 GLN A 326      45.159  -7.824  26.612  1.00197.29           O  
ANISOU 2979  OE1 GLN A 326    19545  26385  29031  -1332    348   3432       O  
ATOM   2980  NE2 GLN A 326      45.416  -8.142  28.809  1.00194.64           N  
ANISOU 2980  NE2 GLN A 326    19240  26158  28558  -1200    913   3764       N  
ATOM   2981  N   GLN A 327      43.098  -4.393  30.881  1.00167.32           N  
ANISOU 2981  N   GLN A 327    15166  23469  24941   -629   1521   4003       N  
ATOM   2982  CA  GLN A 327      41.655  -4.434  31.122  1.00171.21           C  
ANISOU 2982  CA  GLN A 327    15246  24031  25774   -710   1649   4192       C  
ATOM   2983  C   GLN A 327      41.116  -3.078  31.631  1.00176.48           C  
ANISOU 2983  C   GLN A 327    15788  24951  26317   -458   1823   4242       C  
ATOM   2984  O   GLN A 327      40.013  -2.687  31.245  1.00177.97           O  
ANISOU 2984  O   GLN A 327    15652  25236  26734   -487   1760   4266       O  
ATOM   2985  CB  GLN A 327      41.344  -5.542  32.155  1.00175.22           C  
ANISOU 2985  CB  GLN A 327    15674  24448  26454   -815   1943   4462       C  
ATOM   2986  CG  GLN A 327      39.854  -5.858  32.389  1.00195.94           C  
ANISOU 2986  CG  GLN A 327    17843  27111  29494   -958   2089   4685       C  
ATOM   2987  CD  GLN A 327      39.146  -6.536  31.229  1.00218.01           C  
ANISOU 2987  CD  GLN A 327    20376  29778  32679  -1264   1784   4610       C  
ATOM   2988  OE1 GLN A 327      39.757  -7.011  30.261  1.00212.97           O  
ANISOU 2988  OE1 GLN A 327    19920  28969  32029  -1399   1469   4410       O  
ATOM   2989  NE2 GLN A 327      37.838  -6.696  31.363  1.00213.45           N  
ANISOU 2989  NE2 GLN A 327    19362  29273  32466  -1385   1881   4780       N  
ATOM   2990  N   LYS A 328      41.880  -2.383  32.501  1.00172.24           N  
ANISOU 2990  N   LYS A 328    15505  24520  25417   -209   2036   4259       N  
ATOM   2991  CA  LYS A 328      41.481  -1.115  33.124  1.00172.79           C  
ANISOU 2991  CA  LYS A 328    15512  24809  25332     49   2232   4319       C  
ATOM   2992  C   LYS A 328      41.685   0.082  32.165  1.00175.60           C  
ANISOU 2992  C   LYS A 328    15988  25245  25487    174   1998   4066       C  
ATOM   2993  O   LYS A 328      41.081   1.136  32.385  1.00175.56           O  
ANISOU 2993  O   LYS A 328    15905  25409  25391    374   2115   4098       O  
ATOM   2994  CB  LYS A 328      42.259  -0.879  34.432  1.00174.56           C  
ANISOU 2994  CB  LYS A 328    15986  25099  25238    268   2547   4434       C  
ATOM   2995  CG  LYS A 328      41.879  -1.844  35.564  1.00190.99           C  
ANISOU 2995  CG  LYS A 328    17947  27129  27493    214   2852   4724       C  
ATOM   2996  CD  LYS A 328      40.422  -1.697  36.018  1.00204.25           C  
ANISOU 2996  CD  LYS A 328    19195  28905  29506    192   3045   4960       C  
ATOM   2997  CE  LYS A 328      40.023  -2.718  37.053  1.00217.00           C  
ANISOU 2997  CE  LYS A 328    20689  30450  31313    124   3363   5255       C  
ATOM   2998  NZ  LYS A 328      38.628  -2.489  37.518  1.00222.68           N  
ANISOU 2998  NZ  LYS A 328    21690  31102  31817   -153   3261   4344       N  
ATOM   2999  N   LEU A 329      42.478  -0.094  31.091  1.00171.00           N  
ANISOU 2999  N   LEU A 329    15597  24537  24839     68   1686   3828       N  
ATOM   3000  CA  LEU A 329      42.691   0.956  30.091  1.00169.36           C  
ANISOU 3000  CA  LEU A 329    15509  24377  24464    172   1465   3591       C  
ATOM   3001  C   LEU A 329      41.549   0.922  29.058  1.00176.87           C  
ANISOU 3001  C   LEU A 329    16132  25341  25730     74   1255   3562       C  
ATOM   3002  O   LEU A 329      41.155   1.970  28.540  1.00176.08           O  
ANISOU 3002  O   LEU A 329    16002  25354  25547    226   1184   3465       O  
ATOM   3003  CB  LEU A 329      44.068   0.791  29.414  1.00166.17           C  
ANISOU 3003  CB  LEU A 329    15456  23837  23845    123   1246   3362       C  
ATOM   3004  CG  LEU A 329      44.536   1.882  28.449  1.00168.32           C  
ANISOU 3004  CG  LEU A 329    15929  24137  23887    244   1059   3116       C  
ATOM   3005  CD1 LEU A 329      44.577   3.242  29.139  1.00167.77           C  
ANISOU 3005  CD1 LEU A 329    15992  24231  23522    496   1275   3121       C  
ATOM   3006  CD2 LEU A 329      45.907   1.537  27.877  1.00168.02           C  
ANISOU 3006  CD2 LEU A 329    16204  23959  23676    175    874   2928       C  
ATOM   3007  N   ARG A 330      41.002  -0.282  28.787  1.00177.05           N  
ANISOU 3007  N   ARG A 330    15910  25250  26112   -177   1160   3649       N  
ATOM   3008  CA  ARG A 330      39.876  -0.473  27.871  1.00179.89           C  
ANISOU 3008  CA  ARG A 330    15918  25621  26810   -306    947   3632       C  
ATOM   3009  C   ARG A 330      38.557  -0.065  28.554  1.00188.35           C  
ANISOU 3009  C   ARG A 330    16602  26896  28066   -218   1186   3856       C  
ATOM   3010  O   ARG A 330      37.583   0.236  27.863  1.00189.85           O  
ANISOU 3010  O   ARG A 330    16493  27178  28461   -229   1035   3832       O  
ATOM   3011  CB  ARG A 330      39.809  -1.930  27.384  1.00181.68           C  
ANISOU 3011  CB  ARG A 330    16046  25635  27349   -625    762   3641       C  
ATOM   3012  N   SER A 331      38.532  -0.050  29.910  1.00186.65           N  
ANISOU 3012  N   SER A 331    16397  26758  27765   -109   1559   4075       N  
ATOM   3013  CA  SER A 331      37.362   0.337  30.709  1.00189.94           C  
ANISOU 3013  CA  SER A 331    16481  27370  28319     13   1845   4318       C  
ATOM   3014  C   SER A 331      37.147   1.856  30.675  1.00193.59           C  
ANISOU 3014  C   SER A 331    17006  28033  28517    331   1892   4248       C  
ATOM   3015  O   SER A 331      36.006   2.301  30.532  1.00195.71           O  
ANISOU 3015  O   SER A 331    16936  28463  28961    404   1906   4327       O  
ATOM   3016  CB  SER A 331      37.508  -0.133  32.154  1.00194.63           C  
ANISOU 3016  CB  SER A 331    17130  27959  28863     56   2232   4566       C  
ATOM   3017  OG  SER A 331      37.529  -1.549  32.248  1.00205.25           O  
ANISOU 3017  OG  SER A 331    18393  29119  30474   -228   2231   4665       O  
ATOM   3018  N   VAL A 332      38.238   2.647  30.799  1.00187.35           N  
ANISOU 3018  N   VAL A 332    16646  27230  27307    518   1915   4099       N  
ATOM   3019  CA  VAL A 332      38.173   4.115  30.773  1.00186.37           C  
ANISOU 3019  CA  VAL A 332    16666  27258  26888    818   1966   4014       C  
ATOM   3020  C   VAL A 332      37.931   4.598  29.320  1.00190.09           C  
ANISOU 3020  C   VAL A 332    17102  27726  27398    811   1619   3784       C  
ATOM   3021  O   VAL A 332      37.324   5.654  29.129  1.00189.93           O  
ANISOU 3021  O   VAL A 332    17053  27853  27261   1039   1642   3754       O  
ATOM   3022  CB  VAL A 332      39.426   4.807  31.390  1.00187.23           C  
ANISOU 3022  CB  VAL A 332    17253  27338  26546    990   2091   3917       C  
ATOM   3023  CG1 VAL A 332      39.464   4.633  32.904  1.00188.18           C  
ANISOU 3023  CG1 VAL A 332    17408  27515  26576   1099   2463   4154       C  
ATOM   3024  CG2 VAL A 332      40.733   4.333  30.744  1.00183.96           C  
ANISOU 3024  CG2 VAL A 332    17145  26736  26016    825   1853   3699       C  
ATOM   3025  N   PHE A 333      38.382   3.815  28.314  1.00186.42           N  
ANISOU 3025  N   PHE A 333    16656  27091  27086    568   1305   3629       N  
ATOM   3026  CA  PHE A 333      38.219   4.140  26.893  1.00185.95           C  
ANISOU 3026  CA  PHE A 333    16584  27003  27067    556    958   3408       C  
ATOM   3027  C   PHE A 333      36.797   3.781  26.410  1.00193.55           C  
ANISOU 3027  C   PHE A 333    17052  28060  28429    457    835   3499       C  
ATOM   3028  O   PHE A 333      36.128   4.636  25.826  1.00193.98           O  
ANISOU 3028  O   PHE A 333    16991  28246  28467    624    727   3428       O  
ATOM   3029  CB  PHE A 333      39.276   3.411  26.043  1.00185.39           C  
ANISOU 3029  CB  PHE A 333    16776  26700  26962    362    680   3206       C  
ATOM   3030  N   ARG A 334      36.343   2.523  26.675  1.00192.40           N  
ANISOU 3030  N   ARG A 334    16616  27847  28639    189    856   3658       N  
ATOM   3031  CA  ARG A 334      35.026   1.961  26.319  1.00225.19           C  
ANISOU 3031  CA  ARG A 334    20261  32071  33228     23    746   3763       C  
ATOM   3032  C   ARG A 334      34.746   2.115  24.814  1.00237.68           C  
ANISOU 3032  C   ARG A 334    22917  33360  34032    -56    279   1856       C  
ATOM   3033  O   ARG A 334      33.885   1.427  24.268  1.00208.72           O  
ANISOU 3033  O   ARG A 334    17798  29909  31597   -266     99   3529       O  
ATOM   3034  CB  ARG A 334      33.899   2.621  27.133  1.00225.70           C  
ANISOU 3034  CB  ARG A 334    20323  32299  33133    184    988   3479       C  
TER    3035      ARG A 334                                                      
ATOM   3036  N   ALA B1001      45.030  41.773  -2.640  1.00110.43           N  
ANISOU 3036  N   ALA B1001    12410  11602  17944   -953   1995   1905       N  
ATOM   3037  CA  ALA B1001      44.277  41.103  -3.699  1.00108.88           C  
ANISOU 3037  CA  ALA B1001    12406  11798  17163   -562   2050   2123       C  
ATOM   3038  C   ALA B1001      44.954  39.775  -4.118  1.00110.45           C  
ANISOU 3038  C   ALA B1001    12419  12487  17059   -483   2096   2018       C  
ATOM   3039  O   ALA B1001      44.320  38.948  -4.785  1.00109.38           O  
ANISOU 3039  O   ALA B1001    12439  12714  16405   -188   2084   2047       O  
ATOM   3040  CB  ALA B1001      44.136  42.024  -4.903  1.00114.36           C  
ANISOU 3040  CB  ALA B1001    13276  12364  17813   -427   2419   2704       C  
ATOM   3041  N   ASP B1002      46.230  39.573  -3.713  1.00106.27           N  
ANISOU 3041  N   ASP B1002    11547  11971  16861   -736   2136   1868       N  
ATOM   3042  CA  ASP B1002      47.017  38.361  -3.985  1.00105.13           C  
ANISOU 3042  CA  ASP B1002    11183  12228  16535   -633   2208   1758       C  
ATOM   3043  C   ASP B1002      46.491  37.182  -3.154  1.00103.46           C  
ANISOU 3043  C   ASP B1002    11014  12166  16131   -503   1819   1329       C  
ATOM   3044  O   ASP B1002      46.004  37.399  -2.044  1.00101.54           O  
ANISOU 3044  O   ASP B1002    10791  11734  16055   -625   1510   1099       O  
ATOM   3045  CB  ASP B1002      48.506  38.622  -3.671  1.00110.26           C  
ANISOU 3045  CB  ASP B1002    11374  12848  17670   -940   2391   1816       C  
ATOM   3046  CG  ASP B1002      49.463  37.468  -3.936  1.00119.13           C  
ANISOU 3046  CG  ASP B1002    12196  14374  18693   -797   2521   1749       C  
ATOM   3047  OD1 ASP B1002      49.142  36.607  -4.791  1.00119.05           O  
ANISOU 3047  OD1 ASP B1002    12379  14645  18209   -450   2650   1760       O  
ATOM   3048  OD2 ASP B1002      50.569  37.477  -3.361  1.00126.11           O  
ANISOU 3048  OD2 ASP B1002    12635  15302  19978  -1024   2520   1694       O  
ATOM   3049  N   LEU B1003      46.601  35.938  -3.682  1.00 97.57           N  
ANISOU 3049  N   LEU B1003    10296  11737  15039   -250   1865   1224       N  
ATOM   3050  CA  LEU B1003      46.114  34.715  -3.018  1.00 92.83           C  
ANISOU 3050  CA  LEU B1003     9759  11221  14289   -119   1561    874       C  
ATOM   3051  C   LEU B1003      46.880  34.431  -1.700  1.00 94.06           C  
ANISOU 3051  C   LEU B1003     9600  11327  14810   -271   1366    696       C  
ATOM   3052  O   LEU B1003      46.254  34.075  -0.702  1.00 89.98           O  
ANISOU 3052  O   LEU B1003     9156  10741  14292   -282   1050    492       O  
ATOM   3053  CB  LEU B1003      46.247  33.507  -3.963  1.00 93.69           C  
ANISOU 3053  CB  LEU B1003     9959  11595  14044    161   1724    784       C  
ATOM   3054  CG  LEU B1003      45.702  32.160  -3.467  1.00 95.58           C  
ANISOU 3054  CG  LEU B1003    10313  11835  14167    295   1472    445       C  
ATOM   3055  CD1 LEU B1003      44.191  32.201  -3.312  1.00 93.03           C  
ANISOU 3055  CD1 LEU B1003    10271  11443  13634    277   1179    332       C  
ATOM   3056  CD2 LEU B1003      46.058  31.055  -4.426  1.00100.00           C  
ANISOU 3056  CD2 LEU B1003    10963  12573  14459    558   1693    310       C  
ATOM   3057  N   GLU B1004      48.215  34.591  -1.705  1.00 93.76           N  
ANISOU 3057  N   GLU B1004     9186  11380  15059   -376   1556    802       N  
ATOM   3058  CA  GLU B1004      49.075  34.371  -0.536  1.00 94.01           C  
ANISOU 3058  CA  GLU B1004     8836  11470  15412   -510   1355    669       C  
ATOM   3059  C   GLU B1004      48.745  35.380   0.588  1.00 97.74           C  
ANISOU 3059  C   GLU B1004     9300  11724  16113   -821   1062    542       C  
ATOM   3060  O   GLU B1004      48.688  34.999   1.761  1.00 96.26           O  
ANISOU 3060  O   GLU B1004     9014  11602  15959   -843    739    331       O  
ATOM   3061  CB  GLU B1004      50.554  34.490  -0.952  1.00 99.86           C  
ANISOU 3061  CB  GLU B1004     9112  12404  16429   -581   1654    855       C  
ATOM   3062  CG  GLU B1004      51.554  34.243   0.169  1.00112.26           C  
ANISOU 3062  CG  GLU B1004    10190  14143  18319   -702   1427    747       C  
ATOM   3063  CD  GLU B1004      53.019  34.422  -0.186  1.00137.40           C  
ANISOU 3063  CD  GLU B1004    12804  17563  21839   -817   1697    944       C  
ATOM   3064  OE1 GLU B1004      53.859  34.305   0.734  1.00141.38           O  
ANISOU 3064  OE1 GLU B1004    12840  18259  22619   -957   1461    860       O  
ATOM   3065  OE2 GLU B1004      53.329  34.705  -1.367  1.00130.13           O  
ANISOU 3065  OE2 GLU B1004    11870  16678  20894   -774   2140   1198       O  
ATOM   3066  N   ASP B1005      48.523  36.658   0.213  1.00 95.67           N  
ANISOU 3066  N   ASP B1005     9164  11196  15990  -1028   1199    678       N  
ATOM   3067  CA  ASP B1005      48.221  37.764   1.123  1.00 95.90           C  
ANISOU 3067  CA  ASP B1005     9244  10922  16271  -1315    996    526       C  
ATOM   3068  C   ASP B1005      46.796  37.650   1.681  1.00 96.79           C  
ANISOU 3068  C   ASP B1005     9734  10937  16103  -1145    739    343       C  
ATOM   3069  O   ASP B1005      46.562  38.085   2.811  1.00 96.48           O  
ANISOU 3069  O   ASP B1005     9698  10799  16161  -1280    475     82       O  
ATOM   3070  CB  ASP B1005      48.401  39.098   0.393  1.00101.17           C  
ANISOU 3070  CB  ASP B1005     9967  11251  17220  -1537   1305    792       C  
ATOM   3071  CG  ASP B1005      49.810  39.314  -0.131  1.00113.02           C  
ANISOU 3071  CG  ASP B1005    11035  12839  19067  -1773   1597   1010       C  
ATOM   3072  OD1 ASP B1005      50.759  38.756   0.464  1.00113.72           O  
ANISOU 3072  OD1 ASP B1005    10701  13197  19311  -1877   1455    854       O  
ATOM   3073  OD2 ASP B1005      49.968  40.073  -1.101  1.00122.48           O  
ANISOU 3073  OD2 ASP B1005    12286  13852  20397  -1852   1973   1371       O  
ATOM   3074  N   ASN B1006      45.851  37.062   0.900  1.00 91.09           N  
ANISOU 3074  N   ASN B1006     9303  10286  15019   -855    814    459       N  
ATOM   3075  CA  ASN B1006      44.473  36.814   1.338  1.00 87.52           C  
ANISOU 3075  CA  ASN B1006     9130   9808  14315   -693    592    325       C  
ATOM   3076  C   ASN B1006      44.444  35.683   2.352  1.00 90.68           C  
ANISOU 3076  C   ASN B1006     9433  10416  14604   -615    334    105       C  
ATOM   3077  O   ASN B1006      43.681  35.772   3.313  1.00 88.94           O  
ANISOU 3077  O   ASN B1006     9302  10163  14327   -611    117    -58       O  
ATOM   3078  CB  ASN B1006      43.547  36.503   0.168  1.00 85.01           C  
ANISOU 3078  CB  ASN B1006     9071   9568  13662   -454    707    500       C  
ATOM   3079  CG  ASN B1006      43.151  37.710  -0.638  1.00107.73           C  
ANISOU 3079  CG  ASN B1006    12108  12242  16581   -449    915    778       C  
ATOM   3080  OD1 ASN B1006      43.035  38.828  -0.121  1.00104.64           O  
ANISOU 3080  OD1 ASN B1006    11738  11527  16492   -604    935    794       O  
ATOM   3081  ND2 ASN B1006      42.803  37.489  -1.895  1.00100.73           N  
ANISOU 3081  ND2 ASN B1006    11373  11535  15366   -242   1053    992       N  
ATOM   3082  N   TRP B1007      45.298  34.638   2.174  1.00 88.98           N  
ANISOU 3082  N   TRP B1007     9030  10411  14369   -525    388    126       N  
ATOM   3083  CA  TRP B1007      45.400  33.555   3.156  1.00 88.52           C  
ANISOU 3083  CA  TRP B1007     8865  10515  14255   -419    176      0       C  
ATOM   3084  C   TRP B1007      46.049  34.070   4.436  1.00 93.22           C  
ANISOU 3084  C   TRP B1007     9206  11182  15031   -598    -45   -133       C  
ATOM   3085  O   TRP B1007      45.733  33.575   5.517  1.00 92.14           O  
ANISOU 3085  O   TRP B1007     9070  11167  14771   -523   -279   -234       O  
ATOM   3086  CB  TRP B1007      46.160  32.331   2.630  1.00 88.97           C  
ANISOU 3086  CB  TRP B1007     8792  10718  14293   -224    320     68       C  
ATOM   3087  CG  TRP B1007      45.302  31.413   1.815  1.00 89.24           C  
ANISOU 3087  CG  TRP B1007     9120  10708  14080    -29    404     52       C  
ATOM   3088  CD1 TRP B1007      45.274  31.306   0.457  1.00 93.41           C  
ANISOU 3088  CD1 TRP B1007     9790  11249  14451     59    643    100       C  
ATOM   3089  CD2 TRP B1007      44.255  30.562   2.309  1.00 87.32           C  
ANISOU 3089  CD2 TRP B1007     9065  10412  13702     61    234    -37       C  
ATOM   3090  NE1 TRP B1007      44.311  30.399   0.074  1.00 92.19           N  
ANISOU 3090  NE1 TRP B1007     9896  11061  14069    182    589    -21       N  
ATOM   3091  CE2 TRP B1007      43.662  29.936   1.191  1.00 91.73           C  
ANISOU 3091  CE2 TRP B1007     9857  10930  14065    161    350    -92       C  
ATOM   3092  CE3 TRP B1007      43.762  30.262   3.593  1.00 87.48           C  
ANISOU 3092  CE3 TRP B1007     9069  10438  13733     59      6    -66       C  
ATOM   3093  CZ2 TRP B1007      42.605  29.025   1.316  1.00 90.19           C  
ANISOU 3093  CZ2 TRP B1007     9849  10651  13769    198    231   -198       C  
ATOM   3094  CZ3 TRP B1007      42.697  29.382   3.712  1.00 87.90           C  
ANISOU 3094  CZ3 TRP B1007     9311  10409  13676    125    -59    -95       C  
ATOM   3095  CH2 TRP B1007      42.146  28.756   2.587  1.00 88.87           C  
ANISOU 3095  CH2 TRP B1007     9635  10443  13689    166     46   -172       C  
ATOM   3096  N   GLU B1008      46.906  35.098   4.323  1.00 91.92           N  
ANISOU 3096  N   GLU B1008     8828  10953  15144   -853     26   -135       N  
ATOM   3097  CA  GLU B1008      47.522  35.730   5.481  1.00 94.26           C  
ANISOU 3097  CA  GLU B1008     8874  11320  15619  -1096   -222   -344       C  
ATOM   3098  C   GLU B1008      46.443  36.516   6.242  1.00 97.07           C  
ANISOU 3098  C   GLU B1008     9528  11480  15873  -1163   -391   -568       C  
ATOM   3099  O   GLU B1008      46.401  36.453   7.468  1.00 97.63           O  
ANISOU 3099  O   GLU B1008     9541  11728  15825  -1179   -674   -793       O  
ATOM   3100  CB  GLU B1008      48.701  36.620   5.055  1.00 99.97           C  
ANISOU 3100  CB  GLU B1008     9270  11976  16738  -1416    -76   -296       C  
ATOM   3101  CG  GLU B1008      49.520  37.159   6.215  1.00115.60           C  
ANISOU 3101  CG  GLU B1008    10907  14091  18927  -1726   -381   -571       C  
ATOM   3102  CD  GLU B1008      50.804  37.877   5.840  1.00149.64           C  
ANISOU 3102  CD  GLU B1008    14786  18370  23699  -2107   -254   -523       C  
ATOM   3103  OE1 GLU B1008      51.267  37.730   4.684  1.00146.09           O  
ANISOU 3103  OE1 GLU B1008    14231  17891  23386  -2066    116   -203       O  
ATOM   3104  OE2 GLU B1008      51.393  38.524   6.736  1.00151.77           O  
ANISOU 3104  OE2 GLU B1008    14791  18696  24180  -2452   -529   -816       O  
ATOM   3105  N   THR B1009      45.515  37.173   5.504  1.00 91.81           N  
ANISOU 3105  N   THR B1009     9186  10498  15199  -1135   -205   -483       N  
ATOM   3106  CA  THR B1009      44.393  37.930   6.073  1.00 90.72           C  
ANISOU 3106  CA  THR B1009     9343  10148  14978  -1111   -291   -656       C  
ATOM   3107  C   THR B1009      43.420  36.947   6.764  1.00 91.14           C  
ANISOU 3107  C   THR B1009     9518  10449  14661   -845   -455   -699       C  
ATOM   3108  O   THR B1009      42.895  37.258   7.834  1.00 91.31           O  
ANISOU 3108  O   THR B1009     9619  10517  14557   -827   -626   -928       O  
ATOM   3109  CB  THR B1009      43.697  38.763   4.976  1.00 97.93           C  
ANISOU 3109  CB  THR B1009    10519  10713  15978  -1064    -26   -448       C  
ATOM   3110  OG1 THR B1009      44.667  39.546   4.283  1.00101.07           O  
ANISOU 3110  OG1 THR B1009    10786  10884  16734  -1313    181   -317       O  
ATOM   3111  CG2 THR B1009      42.616  39.677   5.527  1.00 97.90           C  
ANISOU 3111  CG2 THR B1009    10794  10448  15954   -991    -68   -606       C  
ATOM   3112  N   LEU B1010      43.213  35.753   6.162  1.00 84.69           N  
ANISOU 3112  N   LEU B1010     8712   9786  13680   -650   -383   -489       N  
ATOM   3113  CA  LEU B1010      42.342  34.707   6.712  1.00 81.77           C  
ANISOU 3113  CA  LEU B1010     8426   9600  13043   -447   -492   -467       C  
ATOM   3114  C   LEU B1010      42.934  34.100   7.976  1.00 85.05           C  
ANISOU 3114  C   LEU B1010     8654  10286  13375   -426   -704   -555       C  
ATOM   3115  O   LEU B1010      42.199  33.874   8.932  1.00 84.54           O  
ANISOU 3115  O   LEU B1010     8672  10353  13097   -331   -825   -617       O  
ATOM   3116  CB  LEU B1010      42.086  33.586   5.680  1.00 80.14           C  
ANISOU 3116  CB  LEU B1010     8270   9421  12759   -308   -363   -279       C  
ATOM   3117  CG  LEU B1010      41.135  33.904   4.522  1.00 84.41           C  
ANISOU 3117  CG  LEU B1010     9015   9837  13222   -256   -222   -181       C  
ATOM   3118  CD1 LEU B1010      41.209  32.853   3.457  1.00 84.49           C  
ANISOU 3118  CD1 LEU B1010     9052   9902  13149   -167   -113    -98       C  
ATOM   3119  CD2 LEU B1010      39.713  34.028   5.002  1.00 85.98           C  
ANISOU 3119  CD2 LEU B1010     9353  10049  13267   -172   -308   -202       C  
ATOM   3120  N   ASN B1011      44.255  33.842   7.981  1.00 81.87           N  
ANISOU 3120  N   ASN B1011     7973  10017  13116   -487   -738   -526       N  
ATOM   3121  CA  ASN B1011      44.935  33.206   9.103  1.00 82.49           C  
ANISOU 3121  CA  ASN B1011     7817  10427  13098   -415   -960   -543       C  
ATOM   3122  C   ASN B1011      45.217  34.208  10.237  1.00 87.72           C  
ANISOU 3122  C   ASN B1011     8394  11231  13704   -595  -1209   -845       C  
ATOM   3123  O   ASN B1011      45.187  33.796  11.393  1.00 87.98           O  
ANISOU 3123  O   ASN B1011     8370  11588  13471   -475  -1425   -887       O  
ATOM   3124  CB  ASN B1011      46.231  32.549   8.645  1.00 82.68           C  
ANISOU 3124  CB  ASN B1011     7520  10581  13313   -375   -906   -394       C  
ATOM   3125  CG  ASN B1011      46.015  31.333   7.759  1.00 95.71           C  
ANISOU 3125  CG  ASN B1011     9279  12118  14968   -141   -684   -169       C  
ATOM   3126  OD1 ASN B1011      45.252  30.413   8.083  1.00 84.84           O  
ANISOU 3126  OD1 ASN B1011     8089  10711  13435     39   -691    -72       O  
ATOM   3127  ND2 ASN B1011      46.773  31.243   6.679  1.00 89.00           N  
ANISOU 3127  ND2 ASN B1011     8295  11213  14309   -141   -472    -91       N  
ATOM   3128  N   ASP B1012      45.460  35.500   9.936  1.00 86.00           N  
ANISOU 3128  N   ASP B1012     8193  10766  13718   -872  -1172  -1059       N  
ATOM   3129  CA  ASP B1012      45.690  36.490  10.998  1.00 89.75           C  
ANISOU 3129  CA  ASP B1012     8631  11303  14167  -1082  -1412  -1450       C  
ATOM   3130  C   ASP B1012      44.370  36.789  11.750  1.00 92.85           C  
ANISOU 3130  C   ASP B1012     9374  11660  14244   -922  -1442  -1621       C  
ATOM   3131  O   ASP B1012      44.389  36.874  12.981  1.00 95.01           O  
ANISOU 3131  O   ASP B1012     9626  12245  14227   -890  -1686  -1869       O  
ATOM   3132  CB  ASP B1012      46.308  37.793  10.452  1.00 94.97           C  
ANISOU 3132  CB  ASP B1012     9230  11596  15257  -1458  -1326  -1632       C  
ATOM   3133  CG  ASP B1012      47.747  37.690   9.935  1.00112.80           C  
ANISOU 3133  CG  ASP B1012    11042  13968  17848  -1682  -1312  -1517       C  
ATOM   3134  OD1 ASP B1012      48.298  36.556   9.901  1.00113.50           O  
ANISOU 3134  OD1 ASP B1012    10868  14423  17832  -1486  -1358  -1287       O  
ATOM   3135  OD2 ASP B1012      48.318  38.740   9.555  1.00122.52           O  
ANISOU 3135  OD2 ASP B1012    12174  14902  19476  -2039  -1225  -1630       O  
ATOM   3136  N   ASN B1013      43.228  36.899  11.014  1.00 85.83           N  
ANISOU 3136  N   ASN B1013     8777  10462  13371   -790  -1194  -1472       N  
ATOM   3137  CA  ASN B1013      41.897  37.143  11.590  1.00 84.34           C  
ANISOU 3137  CA  ASN B1013     8867  10257  12920   -593  -1160  -1571       C  
ATOM   3138  C   ASN B1013      41.351  35.898  12.296  1.00 85.86           C  
ANISOU 3138  C   ASN B1013     9036  10849  12738   -333  -1222  -1371       C  
ATOM   3139  O   ASN B1013      40.549  36.036  13.215  1.00 86.38           O  
ANISOU 3139  O   ASN B1013     9236  11077  12508   -180  -1246  -1488       O  
ATOM   3140  CB  ASN B1013      40.904  37.601  10.529  1.00 81.02           C  
ANISOU 3140  CB  ASN B1013     8674   9463  12649   -509   -897  -1409       C  
ATOM   3141  CG  ASN B1013      41.033  39.055  10.160  1.00 97.67           C  
ANISOU 3141  CG  ASN B1013    10901  11115  15094   -692   -788  -1579       C  
ATOM   3142  OD1 ASN B1013      40.722  39.941  10.957  1.00 97.73           O  
ANISOU 3142  OD1 ASN B1013    11039  10974  15121   -749   -847  -1941       O  
ATOM   3143  ND2 ASN B1013      41.354  39.335   8.909  1.00 83.41           N  
ANISOU 3143  ND2 ASN B1013     9103   9048  13541   -746   -589  -1309       N  
ATOM   3144  N   LEU B1014      41.791  34.698  11.891  1.00 80.79           N  
ANISOU 3144  N   LEU B1014     8230  10345  12124   -269  -1214  -1061       N  
ATOM   3145  CA  LEU B1014      41.377  33.444  12.528  1.00 79.98           C  
ANISOU 3145  CA  LEU B1014     8104  10534  11753    -43  -1240   -807       C  
ATOM   3146  C   LEU B1014      41.996  33.355  13.937  1.00 87.83           C  
ANISOU 3146  C   LEU B1014     8957  11975  12440     20  -1498   -923       C  
ATOM   3147  O   LEU B1014      41.371  32.814  14.851  1.00 88.55           O  
ANISOU 3147  O   LEU B1014     9104  12348  12193    225  -1512   -780       O  
ATOM   3148  CB  LEU B1014      41.787  32.240  11.654  1.00 78.20           C  
ANISOU 3148  CB  LEU B1014     7776  10224  11711     14  -1137   -486       C  
ATOM   3149  CG  LEU B1014      41.160  30.885  11.976  1.00 82.20           C  
ANISOU 3149  CG  LEU B1014     8317  10834  12081    216  -1078   -169       C  
ATOM   3150  CD1 LEU B1014      39.666  30.892  11.678  1.00 80.35           C  
ANISOU 3150  CD1 LEU B1014     8276  10475  11778    239   -928   -113       C  
ATOM   3151  CD2 LEU B1014      41.800  29.796  11.149  1.00 83.29           C  
ANISOU 3151  CD2 LEU B1014     8382  10809  12455    268   -976     46       C  
ATOM   3152  N   LYS B1015      43.212  33.933  14.108  1.00 87.17           N  
ANISOU 3152  N   LYS B1015     8672  11990  12460   -170  -1703  -1175       N  
ATOM   3153  CA  LYS B1015      43.926  34.025  15.384  1.00 91.52           C  
ANISOU 3153  CA  LYS B1015     9045  13033  12697   -155  -2025  -1371       C  
ATOM   3154  C   LYS B1015      43.222  35.002  16.322  1.00 98.24           C  
ANISOU 3154  C   LYS B1015    10132  13973  13223   -158  -2098  -1781       C  
ATOM   3155  O   LYS B1015      43.195  34.768  17.531  1.00101.55           O  
ANISOU 3155  O   LYS B1015    10543  14882  13159     22  -2273  -1828       O  
ATOM   3156  CB  LYS B1015      45.390  34.459  15.178  1.00 97.22           C  
ANISOU 3156  CB  LYS B1015     9420  13826  13693   -425  -2234  -1561       C  
ATOM   3157  CG  LYS B1015      46.260  33.454  14.427  1.00111.79           C  
ANISOU 3157  CG  LYS B1015    10979  15687  15811   -348  -2155  -1167       C  
ATOM   3158  CD  LYS B1015      47.667  33.997  14.214  1.00125.01           C  
ANISOU 3158  CD  LYS B1015    12246  17447  17804   -636  -2312  -1338       C  
ATOM   3159  CE  LYS B1015      48.532  33.067  13.404  1.00133.18           C  
ANISOU 3159  CE  LYS B1015    12995  18489  19117   -506  -2161   -953       C  
ATOM   3160  NZ  LYS B1015      49.882  33.646  13.173  1.00145.85           N  
ANISOU 3160  NZ  LYS B1015    14136  20213  21069   -797  -2268  -1082       N  
ATOM   3161  N   VAL B1016      42.663  36.105  15.763  1.00 93.56           N  
ANISOU 3161  N   VAL B1016     9764  12908  12876   -317  -1938  -2056       N  
ATOM   3162  CA  VAL B1016      41.929  37.147  16.501  1.00 95.79           C  
ANISOU 3162  CA  VAL B1016    10320  13135  12942   -287  -1930  -2491       C  
ATOM   3163  C   VAL B1016      40.702  36.508  17.192  1.00 98.21           C  
ANISOU 3163  C   VAL B1016    10793  13723  12801     81  -1779  -2264       C  
ATOM   3164  O   VAL B1016      40.481  36.760  18.377  1.00102.09           O  
ANISOU 3164  O   VAL B1016    11392  14561  12836    221  -1873  -2545       O  
ATOM   3165  CB  VAL B1016      41.515  38.331  15.572  1.00 98.74           C  
ANISOU 3165  CB  VAL B1016    10905  12847  13765   -454  -1709  -2678       C  
ATOM   3166  CG1 VAL B1016      40.644  39.350  16.305  1.00101.89           C  
ANISOU 3166  CG1 VAL B1016    11614  13120  13978   -351  -1651  -3128       C  
ATOM   3167  CG2 VAL B1016      42.739  39.015  14.969  1.00100.29           C  
ANISOU 3167  CG2 VAL B1016    10917  12753  14434   -850  -1804  -2842       C  
ATOM   3168  N   ILE B1017      39.953  35.646  16.457  1.00 89.09           N  
ANISOU 3168  N   ILE B1017     9636  12447  11768    218  -1544  -1768       N  
ATOM   3169  CA  ILE B1017      38.755  34.937  16.932  1.00 87.52           C  
ANISOU 3169  CA  ILE B1017     9522  12464  11268    500  -1355  -1464       C  
ATOM   3170  C   ILE B1017      39.096  34.091  18.182  1.00 95.96           C  
ANISOU 3170  C   ILE B1017    10484  14131  11847    686  -1508  -1296       C  
ATOM   3171  O   ILE B1017      38.346  34.133  19.157  1.00 97.94           O  
ANISOU 3171  O   ILE B1017    10842  14713  11658    909  -1425  -1310       O  
ATOM   3172  CB  ILE B1017      38.152  34.049  15.801  1.00 85.35           C  
ANISOU 3172  CB  ILE B1017     9208  11910  11310    502  -1138  -1008       C  
ATOM   3173  CG1 ILE B1017      37.788  34.905  14.555  1.00 83.18           C  
ANISOU 3173  CG1 ILE B1017     9038  11143  11425    375  -1001  -1129       C  
ATOM   3174  CG2 ILE B1017      36.933  33.268  16.303  1.00 85.17           C  
ANISOU 3174  CG2 ILE B1017     9205  12106  11052    718   -943   -667       C  
ATOM   3175  CD1 ILE B1017      37.345  34.125  13.291  1.00 84.74           C  
ANISOU 3175  CD1 ILE B1017     9191  11107  11900    337   -855   -777       C  
ATOM   3176  N   GLU B1018      40.226  33.349  18.154  1.00 94.48           N  
ANISOU 3176  N   GLU B1018    10075  14111  11713    638  -1708  -1108       N  
ATOM   3177  CA  GLU B1018      40.674  32.494  19.269  1.00 98.32           C  
ANISOU 3177  CA  GLU B1018    10431  15182  11745    862  -1871   -853       C  
ATOM   3178  C   GLU B1018      40.915  33.299  20.548  1.00107.91           C  
ANISOU 3178  C   GLU B1018    11690  16909  12404    920  -2127  -1315       C  
ATOM   3179  O   GLU B1018      40.554  32.842  21.634  1.00110.66           O  
ANISOU 3179  O   GLU B1018    12068  17789  12189   1200  -2137  -1128       O  
ATOM   3180  CB  GLU B1018      41.970  31.740  18.908  1.00 99.93           C  
ANISOU 3180  CB  GLU B1018    10352  15440  12178    828  -2051   -602       C  
ATOM   3181  CG  GLU B1018      41.871  30.787  17.725  1.00107.97           C  
ANISOU 3181  CG  GLU B1018    11347  15996  13681    816  -1808   -185       C  
ATOM   3182  CD  GLU B1018      43.159  30.054  17.379  1.00136.11           C  
ANISOU 3182  CD  GLU B1018    14637  19595  17482    850  -1931     42       C  
ATOM   3183  OE1 GLU B1018      43.292  29.633  16.208  1.00128.08           O  
ANISOU 3183  OE1 GLU B1018    13608  18141  16916    758  -1761    147       O  
ATOM   3184  OE2 GLU B1018      44.060  29.961  18.246  1.00138.96           O  
ANISOU 3184  OE2 GLU B1018    14777  20456  17564    980  -2206     82       O  
ATOM   3185  N   LYS B1019      41.536  34.489  20.413  1.00106.75           N  
ANISOU 3185  N   LYS B1019    11554  16595  12413    645  -2322  -1919       N  
ATOM   3186  CA  LYS B1019      41.897  35.361  21.533  1.00113.10           C  
ANISOU 3186  CA  LYS B1019    12411  17811  12752    614  -2616  -2517       C  
ATOM   3187  C   LYS B1019      40.875  36.510  21.721  1.00118.11           C  
ANISOU 3187  C   LYS B1019    13404  18163  13308    637  -2407  -2998       C  
ATOM   3188  O   LYS B1019      41.153  37.456  22.465  1.00123.29           O  
ANISOU 3188  O   LYS B1019    14175  18951  13718    539  -2616  -3655       O  
ATOM   3189  CB  LYS B1019      43.307  35.946  21.310  1.00118.50           C  
ANISOU 3189  CB  LYS B1019    12837  18455  13732    237  -2986  -2919       C  
ATOM   3190  CG  LYS B1019      44.414  34.895  21.222  1.00135.34           C  
ANISOU 3190  CG  LYS B1019    14558  20944  15919    272  -3209  -2480       C  
ATOM   3191  CD  LYS B1019      45.779  35.533  21.021  1.00149.18           C  
ANISOU 3191  CD  LYS B1019    15976  22690  18015   -125  -3547  -2862       C  
ATOM   3192  CE  LYS B1019      46.875  34.502  20.959  1.00162.93           C  
ANISOU 3192  CE  LYS B1019    17262  24820  19823    -19  -3739  -2397       C  
ATOM   3193  NZ  LYS B1019      48.209  35.129  20.773  1.00177.05           N  
ANISOU 3193  NZ  LYS B1019    18634  26650  21987   -423  -4047  -2734       N  
ATOM   3194  N   ALA B1020      39.693  36.409  21.083  1.00110.18           N  
ANISOU 3194  N   ALA B1020    12562  16790  12511    780  -2003  -2693       N  
ATOM   3195  CA  ALA B1020      38.652  37.433  21.183  1.00111.08           C  
ANISOU 3195  CA  ALA B1020    12975  16630  12599    887  -1752  -3052       C  
ATOM   3196  C   ALA B1020      37.926  37.357  22.520  1.00119.88           C  
ANISOU 3196  C   ALA B1020    14234  18344  12973   1251  -1672  -3151       C  
ATOM   3197  O   ALA B1020      37.725  36.267  23.064  1.00119.37           O  
ANISOU 3197  O   ALA B1020    14051  18786  12517   1479  -1624  -2648       O  
ATOM   3198  CB  ALA B1020      37.653  37.289  20.049  1.00106.35           C  
ANISOU 3198  CB  ALA B1020    12412  15540  12456    935  -1388  -2646       C  
ATOM   3199  N   ASP B1021      37.529  38.529  23.039  1.00121.48           N  
ANISOU 3199  N   ASP B1021    14709  18457  12990   1324  -1620  -3793       N  
ATOM   3200  CA  ASP B1021      36.823  38.677  24.309  1.00127.19           C  
ANISOU 3200  CA  ASP B1021    15619  19741  12967   1702  -1502  -4021       C  
ATOM   3201  C   ASP B1021      35.321  38.812  24.077  1.00129.79           C  
ANISOU 3201  C   ASP B1021    16074  19866  13373   2016   -997  -3797       C  
ATOM   3202  O   ASP B1021      34.536  38.103  24.712  1.00130.16           O  
ANISOU 3202  O   ASP B1021    16059  20412  12984   2336   -752  -3358       O  
ATOM   3203  CB  ASP B1021      37.358  39.908  25.079  1.00136.42           C  
ANISOU 3203  CB  ASP B1021    17027  20948  13858   1603  -1765  -4975       C  
ATOM   3204  CG  ASP B1021      38.851  39.908  25.383  1.00151.39           C  
ANISOU 3204  CG  ASP B1021    18735  23114  15673   1251  -2318  -5290       C  
ATOM   3205  OD1 ASP B1021      39.469  38.816  25.358  1.00151.20           O  
ANISOU 3205  OD1 ASP B1021    18422  23620  15408   1287  -2514  -4770       O  
ATOM   3206  OD2 ASP B1021      39.388  40.987  25.707  1.00162.10           O  
ANISOU 3206  OD2 ASP B1021    20224  24188  17180    962  -2554  -6070       O  
ATOM   3207  N   ASN B1022      34.925  39.719  23.153  1.00124.80           N  
ANISOU 3207  N   ASN B1022    15584  18511  13323   1931   -830  -4047       N  
ATOM   3208  CA  ASN B1022      33.527  40.024  22.837  1.00123.68           C  
ANISOU 3208  CA  ASN B1022    15523  18140  13330   2244   -379  -3883       C  
ATOM   3209  C   ASN B1022      33.142  39.552  21.408  1.00119.71           C  
ANISOU 3209  C   ASN B1022    14810  17187  13488   2103   -243  -3275       C  
ATOM   3210  O   ASN B1022      34.013  39.240  20.591  1.00115.57           O  
ANISOU 3210  O   ASN B1022    14162  16392  13356   1755   -471  -3115       O  
ATOM   3211  CB  ASN B1022      33.271  41.534  22.982  1.00129.89           C  
ANISOU 3211  CB  ASN B1022    16654  18457  14241   2352   -272  -4622       C  
ATOM   3212  CG  ASN B1022      34.199  42.419  22.188  1.00152.75           C  
ANISOU 3212  CG  ASN B1022    19650  20617  17771   1938   -494  -4986       C  
ATOM   3213  OD1 ASN B1022      34.079  42.553  20.971  1.00143.87           O  
ANISOU 3213  OD1 ASN B1022    18471  18923  17272   1830   -369  -4679       O  
ATOM   3214  ND2 ASN B1022      35.088  43.113  22.880  1.00149.00           N  
ANISOU 3214  ND2 ASN B1022    19318  20159  17135   1697   -820  -5659       N  
ATOM   3215  N   ALA B1023      31.817  39.499  21.137  1.00114.58           N  
ANISOU 3215  N   ALA B1023    14099  16516  12923   2393    130  -2959       N  
ATOM   3216  CA  ALA B1023      31.215  39.072  19.868  1.00108.59           C  
ANISOU 3216  CA  ALA B1023    13123  15451  12684   2314    262  -2419       C  
ATOM   3217  C   ALA B1023      31.527  40.046  18.733  1.00109.69           C  
ANISOU 3217  C   ALA B1023    13386  14877  13416   2140    200  -2616       C  
ATOM   3218  O   ALA B1023      31.537  39.633  17.574  1.00104.81           O  
ANISOU 3218  O   ALA B1023    12605  14022  13195   1957    167  -2224       O  
ATOM   3219  CB  ALA B1023      29.709  38.943  20.025  1.00110.72           C  
ANISOU 3219  CB  ALA B1023    13256  15961  12850   2687    651  -2124       C  
ATOM   3220  N   ALA B1024      31.772  41.334  19.060  1.00109.88           N  
ANISOU 3220  N   ALA B1024    13711  14547  13492   2200    201  -3218       N  
ATOM   3221  CA  ALA B1024      32.107  42.369  18.079  1.00109.01           C  
ANISOU 3221  CA  ALA B1024    13753  13699  13966   2040    188  -3384       C  
ATOM   3222  C   ALA B1024      33.489  42.114  17.461  1.00109.42           C  
ANISOU 3222  C   ALA B1024    13727  13557  14290   1547   -133  -3363       C  
ATOM   3223  O   ALA B1024      33.666  42.375  16.272  1.00106.83           O  
ANISOU 3223  O   ALA B1024    13376  12763  14451   1383   -113  -3148       O  
ATOM   3224  CB  ALA B1024      32.068  43.742  18.724  1.00116.18           C  
ANISOU 3224  CB  ALA B1024    15027  14227  14889   2209    294  -4062       C  
ATOM   3225  N   GLN B1025      34.456  41.582  18.257  1.00105.79           N  
ANISOU 3225  N   GLN B1025    13197  13512  13487   1347   -415  -3544       N  
ATOM   3226  CA  GLN B1025      35.801  41.228  17.774  1.00102.92           C  
ANISOU 3226  CA  GLN B1025    12677  13080  13350    921   -717  -3496       C  
ATOM   3227  C   GLN B1025      35.723  40.070  16.784  1.00 99.87           C  
ANISOU 3227  C   GLN B1025    12032  12765  13148    854   -686  -2832       C  
ATOM   3228  O   GLN B1025      36.402  40.096  15.755  1.00 96.95           O  
ANISOU 3228  O   GLN B1025    11582  12063  13191    589   -751  -2695       O  
ATOM   3229  CB  GLN B1025      36.748  40.861  18.932  1.00107.45           C  
ANISOU 3229  CB  GLN B1025    13181  14194  13453    809  -1040  -3797       C  
ATOM   3230  CG  GLN B1025      37.056  42.000  19.899  1.00129.82           C  
ANISOU 3230  CG  GLN B1025    16267  16977  16081    778  -1166  -4588       C  
ATOM   3231  CD  GLN B1025      38.020  41.599  20.994  1.00153.86           C  
ANISOU 3231  CD  GLN B1025    19193  20660  18607    658  -1555  -4874       C  
ATOM   3232  OE1 GLN B1025      37.831  41.933  22.169  1.00156.27           O  
ANISOU 3232  OE1 GLN B1025    19668  21371  18336    859  -1613  -5325       O  
ATOM   3233  NE2 GLN B1025      39.050  40.833  20.650  1.00142.67           N  
ANISOU 3233  NE2 GLN B1025    17465  19411  17331    379  -1825  -4599       N  
ATOM   3234  N   VAL B1026      34.877  39.058  17.101  1.00 93.90           N  
ANISOU 3234  N   VAL B1026    11150  12433  12094   1088   -561  -2434       N  
ATOM   3235  CA  VAL B1026      34.642  37.860  16.286  1.00 88.22           C  
ANISOU 3235  CA  VAL B1026    10210  11780  11529   1028   -520  -1860       C  
ATOM   3236  C   VAL B1026      33.957  38.279  14.971  1.00 89.14           C  
ANISOU 3236  C   VAL B1026    10340  11463  12065   1037   -353  -1675       C  
ATOM   3237  O   VAL B1026      34.421  37.892  13.900  1.00 85.76           O  
ANISOU 3237  O   VAL B1026     9825  10835  11926    835   -415  -1455       O  
ATOM   3238  CB  VAL B1026      33.809  36.792  17.056  1.00 91.87           C  
ANISOU 3238  CB  VAL B1026    10542  12748  11616   1243   -394  -1506       C  
ATOM   3239  CG1 VAL B1026      33.605  35.536  16.214  1.00 87.45           C  
ANISOU 3239  CG1 VAL B1026     9778  12161  11286   1121   -362   -984       C  
ATOM   3240  CG2 VAL B1026      34.459  36.432  18.388  1.00 94.95           C  
ANISOU 3240  CG2 VAL B1026    10935  13629  11512   1300   -551  -1624       C  
ATOM   3241  N   LYS B1027      32.882  39.101  15.062  1.00 87.36           N  
ANISOU 3241  N   LYS B1027    10222  11129  11842   1313   -136  -1765       N  
ATOM   3242  CA  LYS B1027      32.115  39.605  13.916  1.00 86.25           C  
ANISOU 3242  CA  LYS B1027    10078  10658  12035   1418     19  -1559       C  
ATOM   3243  C   LYS B1027      33.024  40.390  12.950  1.00 90.56           C  
ANISOU 3243  C   LYS B1027    10758  10671  12978   1195    -51  -1663       C  
ATOM   3244  O   LYS B1027      32.985  40.139  11.744  1.00 87.21           O  
ANISOU 3244  O   LYS B1027    10249  10108  12779   1119    -41  -1339       O  
ATOM   3245  CB  LYS B1027      30.954  40.494  14.396  1.00 92.41           C  
ANISOU 3245  CB  LYS B1027    10957  11418  12737   1823    269  -1696       C  
ATOM   3246  CG  LYS B1027      30.042  41.015  13.278  1.00105.56           C  
ANISOU 3246  CG  LYS B1027    12565  12837  14707   2026    426  -1409       C  
ATOM   3247  CD  LYS B1027      29.040  42.081  13.757  1.00119.82           C  
ANISOU 3247  CD  LYS B1027    14493  14525  16507   2487    697  -1580       C  
ATOM   3248  CE  LYS B1027      29.687  43.384  14.176  1.00136.93           C  
ANISOU 3248  CE  LYS B1027    17047  16145  18836   2510    740  -2097       C  
ATOM   3249  NZ  LYS B1027      28.676  44.383  14.611  1.00153.62           N  
ANISOU 3249  NZ  LYS B1027    19310  18081  20976   3018   1044  -2274       N  
ATOM   3250  N   ASP B1028      33.849  41.319  13.491  1.00 91.51           N  
ANISOU 3250  N   ASP B1028    11080  10518  13171   1075   -116  -2119       N  
ATOM   3251  CA  ASP B1028      34.787  42.153  12.727  1.00 93.07           C  
ANISOU 3251  CA  ASP B1028    11394  10175  13795    813   -146  -2235       C  
ATOM   3252  C   ASP B1028      35.791  41.282  11.955  1.00 94.16           C  
ANISOU 3252  C   ASP B1028    11327  10399  14051    487   -300  -1968       C  
ATOM   3253  O   ASP B1028      35.952  41.473  10.748  1.00 93.02           O  
ANISOU 3253  O   ASP B1028    11179   9956  14209    400   -214  -1710       O  
ATOM   3254  CB  ASP B1028      35.538  43.121  13.665  1.00100.49           C  
ANISOU 3254  CB  ASP B1028    12533  10883  14768    661   -237  -2848       C  
ATOM   3255  CG  ASP B1028      36.494  44.081  12.975  1.00118.63           C  
ANISOU 3255  CG  ASP B1028    14927  12565  17580    326   -241  -2987       C  
ATOM   3256  OD1 ASP B1028      36.108  44.659  11.931  1.00119.72           O  
ANISOU 3256  OD1 ASP B1028    15163  12252  18075    416    -23  -2698       O  
ATOM   3257  OD2 ASP B1028      37.576  44.352  13.545  1.00129.86           O  
ANISOU 3257  OD2 ASP B1028    16326  13963  19051    -16   -452  -3392       O  
ATOM   3258  N   ALA B1029      36.434  40.310  12.646  1.00 89.11           N  
ANISOU 3258  N   ALA B1029    10519  10191  13148    357   -502  -2003       N  
ATOM   3259  CA  ALA B1029      37.407  39.391  12.059  1.00 86.00           C  
ANISOU 3259  CA  ALA B1029     9917   9914  12846    118   -629  -1774       C  
ATOM   3260  C   ALA B1029      36.777  38.557  10.927  1.00 85.98           C  
ANISOU 3260  C   ALA B1029     9827   9951  12888    207   -516  -1314       C  
ATOM   3261  O   ALA B1029      37.372  38.473   9.856  1.00 84.93           O  
ANISOU 3261  O   ALA B1029     9641   9650  12980     57   -490  -1144       O  
ATOM   3262  CB  ALA B1029      37.975  38.475  13.130  1.00 87.06           C  
ANISOU 3262  CB  ALA B1029     9897  10524  12656     83   -842  -1847       C  
ATOM   3263  N   LEU B1030      35.562  37.993  11.146  1.00 80.55           N  
ANISOU 3263  N   LEU B1030     9114   9504  11987    438   -441  -1136       N  
ATOM   3264  CA  LEU B1030      34.829  37.179  10.159  1.00 77.45           C  
ANISOU 3264  CA  LEU B1030     8617   9192  11618    486   -381   -774       C  
ATOM   3265  C   LEU B1030      34.388  37.993   8.934  1.00 81.86           C  
ANISOU 3265  C   LEU B1030     9254   9468  12381    560   -263   -639       C  
ATOM   3266  O   LEU B1030      34.260  37.424   7.848  1.00 79.55           O  
ANISOU 3266  O   LEU B1030     8889   9215  12120    515   -268   -401       O  
ATOM   3267  CB  LEU B1030      33.584  36.542  10.795  1.00 77.40           C  
ANISOU 3267  CB  LEU B1030     8511   9512  11383    670   -324   -637       C  
ATOM   3268  CG  LEU B1030      33.779  35.416  11.799  1.00 81.51           C  
ANISOU 3268  CG  LEU B1030     8930  10362  11679    637   -393   -579       C  
ATOM   3269  CD1 LEU B1030      32.537  35.222  12.634  1.00 82.68           C  
ANISOU 3269  CD1 LEU B1030     9002  10806  11606    844   -260   -473       C  
ATOM   3270  CD2 LEU B1030      34.225  34.116  11.116  1.00 81.61           C  
ANISOU 3270  CD2 LEU B1030     8831  10380  11796    463   -463   -346       C  
ATOM   3271  N   THR B1031      34.112  39.302   9.111  1.00 81.38           N  
ANISOU 3271  N   THR B1031     9356   9130  12437    702   -152   -784       N  
ATOM   3272  CA  THR B1031      33.706  40.191   8.015  1.00 82.03           C  
ANISOU 3272  CA  THR B1031     9531   8916  12721    837    -15   -586       C  
ATOM   3273  C   THR B1031      34.907  40.404   7.079  1.00 84.86           C  
ANISOU 3273  C   THR B1031     9934   9005  13304    585     -7   -507       C  
ATOM   3274  O   THR B1031      34.748  40.400   5.854  1.00 83.69           O  
ANISOU 3274  O   THR B1031     9777   8831  13191    633     57   -200       O  
ATOM   3275  CB  THR B1031      33.163  41.509   8.577  1.00 94.39           C  
ANISOU 3275  CB  THR B1031    11285  10178  14400   1091    140   -766       C  
ATOM   3276  OG1 THR B1031      32.061  41.220   9.434  1.00 94.80           O  
ANISOU 3276  OG1 THR B1031    11251  10565  14204   1346    171   -823       O  
ATOM   3277  CG2 THR B1031      32.713  42.467   7.490  1.00 97.03           C  
ANISOU 3277  CG2 THR B1031    11719  10192  14957   1311    306   -475       C  
ATOM   3278  N   LYS B1032      36.110  40.558   7.671  1.00 81.76           N  
ANISOU 3278  N   LYS B1032     9553   8483  13029    319    -77   -777       N  
ATOM   3279  CA  LYS B1032      37.369  40.727   6.944  1.00 81.81           C  
ANISOU 3279  CA  LYS B1032     9523   8287  13276     43    -50   -711       C  
ATOM   3280  C   LYS B1032      37.725  39.436   6.225  1.00 82.50           C  
ANISOU 3280  C   LYS B1032     9435   8703  13208    -22   -111   -490       C  
ATOM   3281  O   LYS B1032      38.253  39.479   5.115  1.00 82.40           O  
ANISOU 3281  O   LYS B1032     9407   8607  13294    -89      0   -264       O  
ATOM   3282  CB  LYS B1032      38.505  41.150   7.902  1.00 85.97           C  
ANISOU 3282  CB  LYS B1032    10020   8683  13964   -242   -159  -1094       C  
ATOM   3283  CG  LYS B1032      38.286  42.499   8.580  1.00 87.68           C  
ANISOU 3283  CG  LYS B1032    10457   8480  14378   -229    -95  -1422       C  
ATOM   3284  CD  LYS B1032      39.344  42.764   9.628  1.00 91.20           C  
ANISOU 3284  CD  LYS B1032    10838   8901  14914   -552   -283  -1885       C  
ATOM   3285  CE  LYS B1032      39.088  44.036  10.388  1.00 99.64           C  
ANISOU 3285  CE  LYS B1032    12169   9535  16156   -551   -236  -2325       C  
ATOM   3286  NZ  LYS B1032      40.076  44.223  11.480  1.00112.25           N  
ANISOU 3286  NZ  LYS B1032    13681  11193  17774   -897   -489  -2861       N  
ATOM   3287  N   MET B1033      37.406  38.287   6.856  1.00 76.67           N  
ANISOU 3287  N   MET B1033     8585   8325  12223     21   -254   -543       N  
ATOM   3288  CA  MET B1033      37.658  36.948   6.318  1.00 73.80           C  
ANISOU 3288  CA  MET B1033     8091   8209  11739    -18   -305   -389       C  
ATOM   3289  C   MET B1033      36.742  36.631   5.141  1.00 76.11           C  
ANISOU 3289  C   MET B1033     8418   8576  11925    111   -243   -153       C  
ATOM   3290  O   MET B1033      37.210  36.031   4.175  1.00 75.12           O  
ANISOU 3290  O   MET B1033     8263   8504  11774     55   -211    -46       O  
ATOM   3291  CB  MET B1033      37.483  35.870   7.393  1.00 74.88           C  
ANISOU 3291  CB  MET B1033     8130   8630  11691      9   -440   -461       C  
ATOM   3292  CG  MET B1033      38.524  35.923   8.468  1.00 79.73           C  
ANISOU 3292  CG  MET B1033     8660   9314  12319   -103   -560   -661       C  
ATOM   3293  SD  MET B1033      38.371  34.589   9.671  1.00 83.79           S  
ANISOU 3293  SD  MET B1033     9065  10199  12572     -9   -690   -613       S  
ATOM   3294  CE  MET B1033      38.702  33.155   8.613  1.00 78.44           C  
ANISOU 3294  CE  MET B1033     8307   9511  11985    -27   -638   -359       C  
ATOM   3295  N   ARG B1034      35.438  37.015   5.217  1.00 72.10           N  
ANISOU 3295  N   ARG B1034     7948   8116  11330    301   -232    -88       N  
ATOM   3296  CA  ARG B1034      34.484  36.756   4.134  1.00 71.19           C  
ANISOU 3296  CA  ARG B1034     7806   8162  11083    422   -236    124       C  
ATOM   3297  C   ARG B1034      34.906  37.533   2.875  1.00 77.16           C  
ANISOU 3297  C   ARG B1034     8668   8760  11889    461   -115    314       C  
ATOM   3298  O   ARG B1034      34.773  37.021   1.761  1.00 77.33           O  
ANISOU 3298  O   ARG B1034     8673   8967  11741    475   -136    447       O  
ATOM   3299  CB  ARG B1034      33.051  37.120   4.548  1.00 69.35           C  
ANISOU 3299  CB  ARG B1034     7512   8061  10775    643   -246    183       C  
ATOM   3300  CG  ARG B1034      32.008  36.455   3.660  1.00 71.27           C  
ANISOU 3300  CG  ARG B1034     7611   8616  10852    698   -345    349       C  
ATOM   3301  CD  ARG B1034      30.596  36.930   3.935  1.00 73.70           C  
ANISOU 3301  CD  ARG B1034     7773   9110  11118    939   -345    458       C  
ATOM   3302  NE  ARG B1034      29.611  36.043   3.310  1.00 74.33           N  
ANISOU 3302  NE  ARG B1034     7623   9563  11056    895   -503    556       N  
ATOM   3303  CZ  ARG B1034      29.164  36.149   2.064  1.00 86.88           C  
ANISOU 3303  CZ  ARG B1034     9156  11348  12508    994   -597    720       C  
ATOM   3304  NH1 ARG B1034      29.620  37.108   1.266  1.00 74.85           N  
ANISOU 3304  NH1 ARG B1034     7809   9660  10969   1179   -504    885       N  
ATOM   3305  NH2 ARG B1034      28.273  35.286   1.599  1.00 76.35           N  
ANISOU 3305  NH2 ARG B1034     7580  10385  11045    893   -791    729       N  
ATOM   3306  N   ALA B1035      35.454  38.746   3.070  1.00 75.23           N  
ANISOU 3306  N   ALA B1035     8542   8169  11875    461     22    318       N  
ATOM   3307  CA  ALA B1035      35.961  39.589   1.997  1.00 77.51           C  
ANISOU 3307  CA  ALA B1035     8937   8241  12273    479    201    567       C  
ATOM   3308  C   ALA B1035      37.213  38.969   1.363  1.00 81.15           C  
ANISOU 3308  C   ALA B1035     9336   8767  12729    265    255    584       C  
ATOM   3309  O   ALA B1035      37.317  38.930   0.137  1.00 81.72           O  
ANISOU 3309  O   ALA B1035     9439   8966  12643    336    353    825       O  
ATOM   3310  CB  ALA B1035      36.270  40.976   2.534  1.00 81.25           C  
ANISOU 3310  CB  ALA B1035     9549   8231  13090    465    350    523       C  
ATOM   3311  N   ALA B1036      38.141  38.451   2.201  1.00 76.71           N  
ANISOU 3311  N   ALA B1036     8666   8180  12298     45    190    334       N  
ATOM   3312  CA  ALA B1036      39.394  37.832   1.764  1.00 76.37           C  
ANISOU 3312  CA  ALA B1036     8503   8218  12296   -122    253    335       C  
ATOM   3313  C   ALA B1036      39.143  36.492   1.082  1.00 79.88           C  
ANISOU 3313  C   ALA B1036     8920   8984  12447    -33    197    351       C  
ATOM   3314  O   ALA B1036      39.872  36.146   0.156  1.00 80.61           O  
ANISOU 3314  O   ALA B1036     8990   9161  12477    -43    338    449       O  
ATOM   3315  CB  ALA B1036      40.326  37.640   2.951  1.00 76.71           C  
ANISOU 3315  CB  ALA B1036     8391   8229  12525   -319    142     74       C  
ATOM   3316  N   ALA B1037      38.120  35.741   1.536  1.00 75.83           N  
ANISOU 3316  N   ALA B1037     8408   8635  11768     45     16    242       N  
ATOM   3317  CA  ALA B1037      37.775  34.433   0.979  1.00 75.32           C  
ANISOU 3317  CA  ALA B1037     8335   8796  11488     74    -59    190       C  
ATOM   3318  C   ALA B1037      37.216  34.566  -0.448  1.00 81.46           C  
ANISOU 3318  C   ALA B1037     9207   9743  12000    196    -22    335       C  
ATOM   3319  O   ALA B1037      37.593  33.780  -1.319  1.00 81.85           O  
ANISOU 3319  O   ALA B1037     9292   9938  11871    200      8    273       O  
ATOM   3320  CB  ALA B1037      36.769  33.729   1.871  1.00 74.53           C  
ANISOU 3320  CB  ALA B1037     8180   8786  11353     70   -237     76       C  
ATOM   3321  N   LEU B1038      36.334  35.559  -0.683  1.00 79.60           N  
ANISOU 3321  N   LEU B1038     9020   9509  11716    332    -21    523       N  
ATOM   3322  CA  LEU B1038      35.732  35.824  -1.995  1.00 82.01           C  
ANISOU 3322  CA  LEU B1038     9393  10053  11715    502    -17    726       C  
ATOM   3323  C   LEU B1038      36.761  36.420  -2.964  1.00 90.57           C  
ANISOU 3323  C   LEU B1038    10576  11079  12757    544    244    960       C  
ATOM   3324  O   LEU B1038      36.679  36.169  -4.166  1.00 92.41           O  
ANISOU 3324  O   LEU B1038    10876  11603  12632    664    273   1073       O  
ATOM   3325  CB  LEU B1038      34.523  36.771  -1.865  1.00 82.99           C  
ANISOU 3325  CB  LEU B1038     9498  10208  11825    704    -89    920       C  
ATOM   3326  CG  LEU B1038      33.277  36.233  -1.143  1.00 85.85           C  
ANISOU 3326  CG  LEU B1038     9703  10755  12161    707   -318    770       C  
ATOM   3327  CD1 LEU B1038      32.307  37.339  -0.855  1.00 87.30           C  
ANISOU 3327  CD1 LEU B1038     9843  10917  12410    958   -310    976       C  
ATOM   3328  CD2 LEU B1038      32.599  35.119  -1.936  1.00 88.55           C  
ANISOU 3328  CD2 LEU B1038     9957  11491  12197    647   -528    653       C  
ATOM   3329  N   ASP B1039      37.724  37.207  -2.437  1.00 89.10           N  
ANISOU 3329  N   ASP B1039    10381  10551  12922    429    433   1026       N  
ATOM   3330  CA  ASP B1039      38.809  37.835  -3.205  1.00 92.11           C  
ANISOU 3330  CA  ASP B1039    10796  10828  13374    404    735   1285       C  
ATOM   3331  C   ASP B1039      39.826  36.763  -3.619  1.00 95.08           C  
ANISOU 3331  C   ASP B1039    11096  11399  13632    323    822   1134       C  
ATOM   3332  O   ASP B1039      40.317  36.793  -4.749  1.00 98.03           O  
ANISOU 3332  O   ASP B1039    11521  11961  13764    421   1037   1331       O  
ATOM   3333  CB  ASP B1039      39.475  38.957  -2.367  1.00 95.48           C  
ANISOU 3333  CB  ASP B1039    11190  10791  14298    228    871   1334       C  
ATOM   3334  CG  ASP B1039      40.573  39.794  -3.029  1.00113.85           C  
ANISOU 3334  CG  ASP B1039    13512  12906  16839    132   1219   1660       C  
ATOM   3335  OD1 ASP B1039      40.781  39.650  -4.257  1.00116.91           O  
ANISOU 3335  OD1 ASP B1039    13893  13562  16967    206   1407   1855       O  
ATOM   3336  OD2 ASP B1039      41.179  40.639  -2.327  1.00121.99           O  
ANISOU 3336  OD2 ASP B1039    14539  13499  18314    -39   1320   1693       O  
ATOM   3337  N   ALA B1040      40.109  35.793  -2.715  1.00 87.97           N  
ANISOU 3337  N   ALA B1040    10079  10476  12869    194    673    806       N  
ATOM   3338  CA  ALA B1040      41.036  34.683  -2.970  1.00 87.19           C  
ANISOU 3338  CA  ALA B1040     9902  10511  12714    177    755    643       C  
ATOM   3339  C   ALA B1040      40.440  33.695  -3.975  1.00 90.89           C  
ANISOU 3339  C   ALA B1040    10514  11270  12749    326    688    505       C  
ATOM   3340  O   ALA B1040      41.187  33.074  -4.729  1.00 91.85           O  
ANISOU 3340  O   ALA B1040    10652  11530  12715    401    863    433       O  
ATOM   3341  CB  ALA B1040      41.378  33.971  -1.672  1.00 85.28           C  
ANISOU 3341  CB  ALA B1040     9510  10152  12738     57    597    399       C  
ATOM   3342  N   GLN B1041      39.093  33.577  -4.000  1.00 86.97           N  
ANISOU 3342  N   GLN B1041    10102  10882  12060    369    439    443       N  
ATOM   3343  CA  GLN B1041      38.335  32.708  -4.910  1.00 88.35           C  
ANISOU 3343  CA  GLN B1041    10389  11352  11827    446    293    255       C  
ATOM   3344  C   GLN B1041      38.515  33.161  -6.372  1.00 97.71           C  
ANISOU 3344  C   GLN B1041    11701  12847  12579    631    470    448       C  
ATOM   3345  O   GLN B1041      38.514  32.328  -7.278  1.00 99.37           O  
ANISOU 3345  O   GLN B1041    12021  13308  12426    701    471    220       O  
ATOM   3346  CB  GLN B1041      36.844  32.720  -4.523  1.00 88.27           C  
ANISOU 3346  CB  GLN B1041    10340  11429  11769    422    -15    217       C  
ATOM   3347  CG  GLN B1041      35.980  31.700  -5.268  1.00 93.25           C  
ANISOU 3347  CG  GLN B1041    11019  12363  12050    405   -246    -53       C  
ATOM   3348  CD  GLN B1041      34.508  31.790  -4.921  1.00104.26           C  
ANISOU 3348  CD  GLN B1041    12278  13904  13432    364   -540    -41       C  
ATOM   3349  OE1 GLN B1041      34.004  32.811  -4.430  1.00100.46           O  
ANISOU 3349  OE1 GLN B1041    11703  13365  13101    448   -545    225       O  
ATOM   3350  NE2 GLN B1041      33.766  30.748  -5.253  1.00 90.89           N  
ANISOU 3350  NE2 GLN B1041    10557  12416  11562    239   -782   -342       N  
ATOM   3351  N   LYS B1042      38.679  34.481  -6.585  1.00 97.37           N  
ANISOU 3351  N   LYS B1042    11660  12765  12572    719    640    870       N  
ATOM   3352  CA  LYS B1042      38.864  35.101  -7.901  1.00102.36           C  
ANISOU 3352  CA  LYS B1042    12406  13684  12800    926    861   1205       C  
ATOM   3353  C   LYS B1042      40.318  34.945  -8.396  1.00111.40           C  
ANISOU 3353  C   LYS B1042    13538  14838  13952    931   1250   1261       C  
ATOM   3354  O   LYS B1042      40.555  34.980  -9.606  1.00115.19           O  
ANISOU 3354  O   LYS B1042    14134  15680  13954   1123   1441   1391       O  
ATOM   3355  CB  LYS B1042      38.483  36.592  -7.846  1.00105.50           C  
ANISOU 3355  CB  LYS B1042    12814  13920  13353   1021    954   1702       C  
ATOM   3356  CG  LYS B1042      37.013  36.837  -7.509  1.00115.30           C  
ANISOU 3356  CG  LYS B1042    14038  15227  14544   1114    621   1714       C  
ATOM   3357  CD  LYS B1042      36.690  38.315  -7.417  1.00126.65           C  
ANISOU 3357  CD  LYS B1042    15511  16412  16200   1266    762   2203       C  
ATOM   3358  N   ALA B1043      41.281  34.767  -7.461  1.00107.88           N  
ANISOU 3358  N   ALA B1043    12922  14054  14015    742   1365   1171       N  
ATOM   3359  CA  ALA B1043      42.713  34.610  -7.759  1.00110.46           C  
ANISOU 3359  CA  ALA B1043    13124  14387  14457    731   1734   1239       C  
ATOM   3360  C   ALA B1043      43.029  33.217  -8.334  1.00116.95           C  
ANISOU 3360  C   ALA B1043    14018  15462  14956    873   1775    858       C  
ATOM   3361  O   ALA B1043      42.300  32.260  -8.074  1.00115.03           O  
ANISOU 3361  O   ALA B1043    13877  15221  14609    865   1475    469       O  
ATOM   3362  CB  ALA B1043      43.534  34.839  -6.494  1.00108.78           C  
ANISOU 3362  CB  ALA B1043    12654  13806  14873    486   1742   1207       C  
ATOM   3363  N   THR B1044      44.126  33.112  -9.109  1.00118.03           N  
ANISOU 3363  N   THR B1044    14096  15782  14968   1002   2182    975       N  
ATOM   3364  CA  THR B1044      44.596  31.853  -9.698  1.00120.25           C  
ANISOU 3364  CA  THR B1044    14456  16268  14965   1196   2319    611       C  
ATOM   3365  C   THR B1044      45.945  31.486  -9.037  1.00124.20           C  
ANISOU 3365  C   THR B1044    14645  16583  15961   1159   2554    594       C  
ATOM   3366  O   THR B1044      46.866  32.312  -9.042  1.00125.30           O  
ANISOU 3366  O   THR B1044    14526  16716  16367   1080   2851    975       O  
ATOM   3367  CB  THR B1044      44.692  31.975 -11.229  1.00133.53           C  
ANISOU 3367  CB  THR B1044    16328  18429  15977   1470   2624    748       C  
ATOM   3368  OG1 THR B1044      43.426  32.395 -11.745  1.00134.15           O  
ANISOU 3368  OG1 THR B1044    16633  18732  15604   1514   2344    810       O  
ATOM   3369  CG2 THR B1044      45.116  30.670 -11.898  1.00135.25           C  
ANISOU 3369  CG2 THR B1044    16686  18857  15847   1711   2785    285       C  
ATOM   3370  N   PRO B1045      46.074  30.263  -8.454  1.00119.64           N  
ANISOU 3370  N   PRO B1045    14062  15850  15544   1211   2424    186       N  
ATOM   3371  CA  PRO B1045      47.330  29.895  -7.760  1.00119.82           C  
ANISOU 3371  CA  PRO B1045    13744  15746  16039   1230   2603    212       C  
ATOM   3372  C   PRO B1045      48.548  29.801  -8.703  1.00130.07           C  
ANISOU 3372  C   PRO B1045    14886  17333  17201   1478   3134    351       C  
ATOM   3373  O   PRO B1045      48.362  29.594  -9.904  1.00133.12           O  
ANISOU 3373  O   PRO B1045    15532  18006  17040   1702   3348    274       O  
ATOM   3374  CB  PRO B1045      47.014  28.518  -7.163  1.00119.79           C  
ANISOU 3374  CB  PRO B1045    13862  15512  16142   1316   2370   -218       C  
ATOM   3375  CG  PRO B1045      45.873  28.004  -7.942  1.00124.97           C  
ANISOU 3375  CG  PRO B1045    14929  16245  16311   1378   2216   -543       C  
ATOM   3376  CD  PRO B1045      45.064  29.194  -8.333  1.00119.74           C  
ANISOU 3376  CD  PRO B1045    14350  15767  15380   1236   2094   -278       C  
ATOM   3377  N   PRO B1046      49.805  29.951  -8.181  1.00129.25           N  
ANISOU 3377  N   PRO B1046    14329  17217  17561   1454   3351    552       N  
ATOM   3378  CA  PRO B1046      50.994  29.878  -9.066  1.00135.49           C  
ANISOU 3378  CA  PRO B1046    14896  18328  18255   1705   3906    724       C  
ATOM   3379  C   PRO B1046      51.103  28.522  -9.769  1.00143.84           C  
ANISOU 3379  C   PRO B1046    16211  19495  18946   2138   4096    306       C  
ATOM   3380  O   PRO B1046      51.493  28.463 -10.936  1.00148.30           O  
ANISOU 3380  O   PRO B1046    16878  20402  19065   2408   4522    334       O  
ATOM   3381  CB  PRO B1046      52.173  30.101  -8.109  1.00137.57           C  
ANISOU 3381  CB  PRO B1046    14568  18538  19164   1565   3960    935       C  
ATOM   3382  CG  PRO B1046      51.632  29.813  -6.745  1.00136.59           C  
ANISOU 3382  CG  PRO B1046    14452  18083  19364   1382   3426    728       C  
ATOM   3383  CD  PRO B1046      50.198  30.218  -6.781  1.00128.02           C  
ANISOU 3383  CD  PRO B1046    13811  16830  18000   1205   3095    633       C  
ATOM   3384  N   LYS B1047      50.746  27.440  -9.056  1.00139.22           N  
ANISOU 3384  N   LYS B1047    15753  18598  18545   2211   3799    -82       N  
ATOM   3385  CA  LYS B1047      50.680  26.091  -9.608  1.00142.49           C  
ANISOU 3385  CA  LYS B1047    16491  18949  18698   2579   3920   -564       C  
ATOM   3386  C   LYS B1047      49.323  25.964 -10.307  1.00147.12           C  
ANISOU 3386  C   LYS B1047    17614  19560  18724   2502   3670   -894       C  
ATOM   3387  O   LYS B1047      48.350  26.580  -9.856  1.00142.73           O  
ANISOU 3387  O   LYS B1047    17132  18913  18185   2174   3275   -790       O  
ATOM   3388  CB  LYS B1047      50.917  25.031  -8.517  1.00143.27           C  
ANISOU 3388  CB  LYS B1047    16496  18644  19298   2673   3729   -759       C  
ATOM   3389  CG  LYS B1047      52.339  25.098  -7.942  1.00154.35           C  
ANISOU 3389  CG  LYS B1047    17309  20149  21187   2821   3973   -430       C  
ATOM   3390  CD  LYS B1047      52.608  24.055  -6.868  1.00161.31           C  
ANISOU 3390  CD  LYS B1047    18078  20686  22525   2991   3793   -533       C  
ATOM   3391  CE  LYS B1047      54.008  24.191  -6.316  1.00169.80           C  
ANISOU 3391  CE  LYS B1047    18500  21981  24036   3158   3994   -182       C  
ATOM   3392  NZ  LYS B1047      54.295  23.172  -5.276  1.00175.59           N  
ANISOU 3392  NZ  LYS B1047    19106  22434  25176   3400   3823   -203       N  
ATOM   3393  N   LEU B1048      49.278  25.246 -11.456  1.00149.32           N  
ANISOU 3393  N   LEU B1048    18237  20025  18473   2816   3911  -1288       N  
ATOM   3394  CA  LEU B1048      48.112  25.120 -12.356  1.00150.86           C  
ANISOU 3394  CA  LEU B1048    18909  20400  18013   2780   3698  -1646       C  
ATOM   3395  C   LEU B1048      47.629  26.551 -12.747  1.00152.86           C  
ANISOU 3395  C   LEU B1048    19107  21025  17949   2577   3624  -1155       C  
ATOM   3396  O   LEU B1048      46.438  26.868 -12.672  1.00149.45           O  
ANISOU 3396  O   LEU B1048    18857  20590  17337   2346   3197  -1207       O  
ATOM   3397  CB  LEU B1048      46.957  24.263 -11.774  1.00148.28           C  
ANISOU 3397  CB  LEU B1048    18864  19642  17834   2560   3183  -2124       C  
ATOM   3398  N   GLU B1049      48.597  27.407 -13.151  1.00151.83           N  
ANISOU 3398  N   GLU B1049    18691  21195  17802   2679   4075   -638       N  
ATOM   3399  CA  GLU B1049      48.382  28.788 -13.587  1.00151.79           C  
ANISOU 3399  CA  GLU B1049    18620  21481  17571   2542   4144    -72       C  
ATOM   3400  C   GLU B1049      47.836  28.790 -15.013  1.00160.66           C  
ANISOU 3400  C   GLU B1049    20132  23137  17773   2792   4247   -187       C  
ATOM   3401  O   GLU B1049      46.766  29.351 -15.252  1.00159.38           O  
ANISOU 3401  O   GLU B1049    20156  23117  17286   2668   3921    -71       O  
ATOM   3402  CB  GLU B1049      49.693  29.593 -13.484  1.00155.00           C  
ANISOU 3402  CB  GLU B1049    18559  21971  18361   2527   4632    513       C  
ATOM   3403  CG  GLU B1049      49.572  31.063 -13.860  1.00166.80           C  
ANISOU 3403  CG  GLU B1049    19979  23641  19755   2361   4771   1164       C  
ATOM   3404  CD  GLU B1049      50.845  31.887 -13.783  1.00191.40           C  
ANISOU 3404  CD  GLU B1049    22610  26797  23317   2259   5265   1746       C  
ATOM   3405  OE1 GLU B1049      50.788  33.084 -14.144  1.00187.81           O  
ANISOU 3405  OE1 GLU B1049    22126  26455  22777   2150   5477   2315       O  
ATOM   3406  OE2 GLU B1049      51.899  31.343 -13.377  1.00186.42           O  
ANISOU 3406  OE2 GLU B1049    21607  26088  23134   2294   5454   1660       O  
ATOM   3407  N   ASP B1050      48.555  28.135 -15.953  1.00163.29           N  
ANISOU 3407  N   ASP B1050    20581  23807  17654   3180   4696   -427       N  
ATOM   3408  CA  ASP B1050      48.130  28.002 -17.344  1.00169.75           C  
ANISOU 3408  CA  ASP B1050    21793  25217  17488   3473   4811   -628       C  
ATOM   3409  C   ASP B1050      47.149  26.819 -17.444  1.00174.55           C  
ANISOU 3409  C   ASP B1050    22819  25698  17804   3467   4337  -1487       C  
ATOM   3410  O   ASP B1050      47.468  25.769 -18.008  1.00178.84           O  
ANISOU 3410  O   ASP B1050    23604  26300  18047   3755   4532  -2085       O  
ATOM   3411  CB  ASP B1050      49.349  27.835 -18.270  1.00178.92           C  
ANISOU 3411  CB  ASP B1050    22889  26816  18276   3907   5544   -522       C  
ATOM   3412  N   LYS B1051      45.964  26.995 -16.834  1.00166.80           N  
ANISOU 3412  N   LYS B1051    21897  24492  16989   3116   3726  -1549       N  
ATOM   3413  CA  LYS B1051      44.889  26.006 -16.749  1.00166.49           C  
ANISOU 3413  CA  LYS B1051    22159  24270  16831   2965   3199  -2279       C  
ATOM   3414  C   LYS B1051      43.543  26.673 -17.055  1.00170.85           C  
ANISOU 3414  C   LYS B1051    22811  25176  16929   2781   2706  -2155       C  
ATOM   3415  O   LYS B1051      43.277  27.770 -16.554  1.00166.78           O  
ANISOU 3415  O   LYS B1051    22065  24654  16651   2635   2625  -1508       O  
ATOM   3416  CB  LYS B1051      44.887  25.370 -15.337  1.00162.57           C  
ANISOU 3416  CB  LYS B1051    21494  23015  17261   2690   2960  -2443       C  
ATOM   3417  CG  LYS B1051      43.895  24.217 -15.117  1.00172.01           C  
ANISOU 3417  CG  LYS B1051    22963  23875  18520   2488   2494  -3177       C  
ATOM   3418  CD  LYS B1051      44.290  22.884 -15.771  1.00184.94           C  
ANISOU 3418  CD  LYS B1051    24933  25382  19954   2747   2713  -3928       C  
ATOM   3419  CE  LYS B1051      45.506  22.247 -15.136  1.00190.07           C  
ANISOU 3419  CE  LYS B1051    25423  25533  21261   2959   3122  -3887       C  
ATOM   3420  NZ  LYS B1051      45.791  20.913 -15.719  1.00203.32           N  
ANISOU 3420  NZ  LYS B1051    27466  26976  22812   3239   3333  -4649       N  
ATOM   3421  N   SER B1052      42.698  26.010 -17.870  1.00172.98           N  
ANISOU 3421  N   SER B1052    23408  25753  16564   2796   2372  -2791       N  
ATOM   3422  CA  SER B1052      41.372  26.504 -18.264  1.00173.88           C  
ANISOU 3422  CA  SER B1052    23577  26307  16182   2656   1850  -2741       C  
ATOM   3423  C   SER B1052      40.440  26.653 -17.033  1.00170.75           C  
ANISOU 3423  C   SER B1052    22946  25421  16508   2233   1356  -2629       C  
ATOM   3424  O   SER B1052      40.573  25.876 -16.085  1.00166.56           O  
ANISOU 3424  O   SER B1052    22366  24257  16664   2018   1285  -2948       O  
ATOM   3425  CB  SER B1052      40.740  25.567 -19.292  1.00184.56           C  
ANISOU 3425  CB  SER B1052    25293  28086  16746   2715   1563  -3578       C  
ATOM   3426  OG  SER B1052      40.575  24.253 -18.783  1.00193.04           O  
ANISOU 3426  OG  SER B1052    26498  28560  18291   2475   1360  -4363       O  
ATOM   3427  N   PRO B1053      39.507  27.641 -17.011  1.00165.99           N  
ANISOU 3427  N   PRO B1053    22196  25108  15766   2150   1043  -2150       N  
ATOM   3428  CA  PRO B1053      38.625  27.788 -15.834  1.00159.60           C  
ANISOU 3428  CA  PRO B1053    21152  23871  15617   1793    623  -2058       C  
ATOM   3429  C   PRO B1053      37.587  26.660 -15.729  1.00164.85           C  
ANISOU 3429  C   PRO B1053    21898  24468  16268   1500    102  -2802       C  
ATOM   3430  O   PRO B1053      37.141  26.350 -14.624  1.00159.89           O  
ANISOU 3430  O   PRO B1053    21099  23348  16303   1186   -136  -2866       O  
ATOM   3431  CB  PRO B1053      37.930  29.139 -16.070  1.00161.29           C  
ANISOU 3431  CB  PRO B1053    21220  24492  15573   1891    488  -1367       C  
ATOM   3432  CG  PRO B1053      38.676  29.791 -17.202  1.00171.10           C  
ANISOU 3432  CG  PRO B1053    22596  26248  16165   2280    928   -959       C  
ATOM   3433  CD  PRO B1053      39.217  28.674 -18.024  1.00172.05           C  
ANISOU 3433  CD  PRO B1053    22995  26597  15777   2422   1086  -1630       C  
ATOM   3434  N   ASP B1054      37.224  26.033 -16.868  1.00168.24           N  
ANISOU 3434  N   ASP B1054    22587  25394  15944   1586    -58  -3380       N  
ATOM   3435  CA  ASP B1054      36.247  24.940 -16.926  1.00171.08           C  
ANISOU 3435  CA  ASP B1054    23032  25717  16253   1258   -561  -4170       C  
ATOM   3436  C   ASP B1054      36.866  23.591 -16.471  1.00174.33           C  
ANISOU 3436  C   ASP B1054    23648  25403  17188   1121   -373  -4825       C  
ATOM   3437  O   ASP B1054      36.151  22.588 -16.401  1.00177.06           O  
ANISOU 3437  O   ASP B1054    24082  25527  17664    791   -731  -5504       O  
ATOM   3438  CB  ASP B1054      35.683  24.800 -18.357  1.00181.82           C  
ANISOU 3438  CB  ASP B1054    24594  27945  16542   1399   -843  -4582       C  
ATOM   3439  CG  ASP B1054      34.940  26.019 -18.889  1.00193.21           C  
ANISOU 3439  CG  ASP B1054    25835  30160  17415   1568  -1103  -3953       C  
ATOM   3440  OD1 ASP B1054      34.979  27.081 -18.226  1.00187.92           O  
ANISOU 3440  OD1 ASP B1054    24957  29370  17074   1707   -872  -3109       O  
ATOM   3441  OD2 ASP B1054      34.343  25.918 -19.980  1.00206.08           O  
ANISOU 3441  OD2 ASP B1054    27530  32528  18241   1593  -1518  -4303       O  
ATOM   3442  N   SER B1055      38.179  23.578 -16.152  1.00167.32           N  
ANISOU 3442  N   SER B1055    22803  24130  16643   1371    187  -4591       N  
ATOM   3443  CA  SER B1055      38.921  22.393 -15.702  1.00167.04           C  
ANISOU 3443  CA  SER B1055    22934  23395  17138   1363    445  -5069       C  
ATOM   3444  C   SER B1055      38.438  21.926 -14.306  1.00163.67           C  
ANISOU 3444  C   SER B1055    22310  22241  17635    966    207  -5033       C  
ATOM   3445  O   SER B1055      38.101  22.776 -13.476  1.00156.91           O  
ANISOU 3445  O   SER B1055    21139  21365  17113    835     83  -4428       O  
ATOM   3446  CB  SER B1055      40.415  22.698 -15.668  1.00169.78           C  
ANISOU 3446  CB  SER B1055    23253  23650  17607   1766   1084  -4679       C  
ATOM   3447  OG  SER B1055      41.189  21.564 -15.321  1.00180.66           O  
ANISOU 3447  OG  SER B1055    24781  24413  19448   1863   1366  -5104       O  
ATOM   3448  N   PRO B1056      38.405  20.590 -14.023  1.00161.86           N  
ANISOU 3448  N   PRO B1056    22279  21393  17827    791    172  -5656       N  
ATOM   3449  CA  PRO B1056      37.902  20.120 -12.714  1.00156.76           C  
ANISOU 3449  CA  PRO B1056    21450  20089  18024    419    -27  -5555       C  
ATOM   3450  C   PRO B1056      38.753  20.577 -11.519  1.00151.99           C  
ANISOU 3450  C   PRO B1056    20590  19119  18040    562    278  -4866       C  
ATOM   3451  O   PRO B1056      38.186  20.788 -10.447  1.00146.64           O  
ANISOU 3451  O   PRO B1056    19667  18200  17852    295     72  -4535       O  
ATOM   3452  CB  PRO B1056      37.963  18.594 -12.834  1.00164.33           C  
ANISOU 3452  CB  PRO B1056    22743  20417  19278    304     12  -6329       C  
ATOM   3453  CG  PRO B1056      37.956  18.323 -14.294  1.00176.98           C  
ANISOU 3453  CG  PRO B1056    24687  22490  20067    459     -5  -6999       C  
ATOM   3454  CD  PRO B1056      38.729  19.447 -14.902  1.00171.28           C  
ANISOU 3454  CD  PRO B1056    23894  22448  18737    915    306  -6494       C  
ATOM   3455  N   GLU B1057      40.089  20.722 -11.688  1.00147.40           N  
ANISOU 3455  N   GLU B1057    20037  18542  17429    974    756  -4665       N  
ATOM   3456  CA  GLU B1057      40.980  21.154 -10.597  1.00140.91           C  
ANISOU 3456  CA  GLU B1057    18927  17450  17163   1098   1007  -4055       C  
ATOM   3457  C   GLU B1057      40.843  22.677 -10.338  1.00137.50           C  
ANISOU 3457  C   GLU B1057    18189  17454  16603   1053    927  -3392       C  
ATOM   3458  O   GLU B1057      41.149  23.114  -9.227  1.00131.36           O  
ANISOU 3458  O   GLU B1057    17147  16450  16316    987    940  -2945       O  
ATOM   3459  CB  GLU B1057      42.470  20.790 -10.832  1.00144.76           C  
ANISOU 3459  CB  GLU B1057    19457  17816  17730   1539   1538  -4050       C  
ATOM   3460  CG  GLU B1057      43.035  20.969 -12.239  1.00161.07           C  
ANISOU 3460  CG  GLU B1057    21716  20393  19089   1882   1852  -4268       C  
ATOM   3461  CD  GLU B1057      42.710  19.874 -13.246  1.00189.94           C  
ANISOU 3461  CD  GLU B1057    25820  23992  22355   1953   1840  -5107       C  
ATOM   3462  OE1 GLU B1057      41.996  18.908 -12.890  1.00186.48           O  
ANISOU 3462  OE1 GLU B1057    25558  23035  22263   1682   1573  -5569       O  
ATOM   3463  OE2 GLU B1057      43.201  19.971 -14.393  1.00190.26           O  
ANISOU 3463  OE2 GLU B1057    26044  24496  21750   2280   2127  -5315       O  
ATOM   3464  N   MET B1058      40.360  23.467 -11.318  1.00135.03           N  
ANISOU 3464  N   MET B1058    17923  17740  15641   1096    836  -3330       N  
ATOM   3465  CA  MET B1058      40.117  24.895 -11.084  1.00130.30           C  
ANISOU 3465  CA  MET B1058    17074  17453  14978   1062    766  -2700       C  
ATOM   3466  C   MET B1058      38.718  25.096 -10.489  1.00130.16           C  
ANISOU 3466  C   MET B1058    16934  17417  15104    732    285  -2663       C  
ATOM   3467  O   MET B1058      38.541  25.988  -9.655  1.00124.69           O  
ANISOU 3467  O   MET B1058    16005  16671  14700    656    227  -2182       O  
ATOM   3468  CB  MET B1058      40.297  25.742 -12.349  1.00136.26           C  
ANISOU 3468  CB  MET B1058    17912  18844  15016   1312    933  -2497       C  
ATOM   3469  CG  MET B1058      41.754  26.057 -12.657  1.00140.91           C  
ANISOU 3469  CG  MET B1058    18454  19495  15590   1620   1488  -2219       C  
ATOM   3470  SD  MET B1058      42.604  27.024 -11.359  1.00138.43           S  
ANISOU 3470  SD  MET B1058    17738  18833  16027   1537   1690  -1543       S  
ATOM   3471  CE  MET B1058      41.684  28.569 -11.422  1.00132.95           C  
ANISOU 3471  CE  MET B1058    16942  18419  15154   1415   1469   -991       C  
ATOM   3472  N   LYS B1059      37.736  24.248 -10.886  1.00129.57           N  
ANISOU 3472  N   LYS B1059    17000  17372  14860    527    -48  -3197       N  
ATOM   3473  CA  LYS B1059      36.377  24.288 -10.332  1.00127.28           C  
ANISOU 3473  CA  LYS B1059    16530  17082  14750    189   -492  -3195       C  
ATOM   3474  C   LYS B1059      36.388  23.829  -8.860  1.00125.15           C  
ANISOU 3474  C   LYS B1059    16109  16192  15249    -16   -481  -3072       C  
ATOM   3475  O   LYS B1059      35.608  24.344  -8.057  1.00121.01           O  
ANISOU 3475  O   LYS B1059    15341  15669  14966   -190   -687  -2772       O  
ATOM   3476  CB  LYS B1059      35.399  23.434 -11.159  1.00135.53           C  
ANISOU 3476  CB  LYS B1059    17714  18341  15439    -32   -858  -3837       C  
ATOM   3477  CG  LYS B1059      35.071  24.022 -12.527  1.00147.81           C  
ANISOU 3477  CG  LYS B1059    19359  20673  16131    159   -993  -3899       C  
ATOM   3478  CD  LYS B1059      34.031  23.189 -13.251  1.00161.26           C  
ANISOU 3478  CD  LYS B1059    21140  22646  17484   -120  -1449  -4579       C  
ATOM   3479  CE  LYS B1059      33.606  23.831 -14.545  1.00175.45           C  
ANISOU 3479  CE  LYS B1059    22981  25331  18353     94  -1650  -4580       C  
ATOM   3480  NZ  LYS B1059      32.596  23.012 -15.261  1.00191.45           N  
ANISOU 3480  NZ  LYS B1059    25041  27698  20003   -211  -2164  -5301       N  
ATOM   3481  N   ASP B1060      37.300  22.892  -8.510  1.00121.37           N  
ANISOU 3481  N   ASP B1060    15771  15218  15125     61   -212  -3264       N  
ATOM   3482  CA  ASP B1060      37.490  22.392  -7.146  1.00117.48           C  
ANISOU 3482  CA  ASP B1060    15162  14168  15308    -48   -151  -3089       C  
ATOM   3483  C   ASP B1060      38.100  23.484  -6.256  1.00114.86           C  
ANISOU 3483  C   ASP B1060    14580  13891  15170     90     -9  -2482       C  
ATOM   3484  O   ASP B1060      37.725  23.602  -5.088  1.00111.23           O  
ANISOU 3484  O   ASP B1060    13940  13233  15092    -54   -112  -2224       O  
ATOM   3485  CB  ASP B1060      38.389  21.135  -7.151  1.00122.47           C  
ANISOU 3485  CB  ASP B1060    16023  14294  16218     97    125  -3420       C  
ATOM   3486  CG  ASP B1060      38.647  20.506  -5.787  1.00130.20           C  
ANISOU 3486  CG  ASP B1060    16904  14705  17863     53    210  -3191       C  
ATOM   3487  OD1 ASP B1060      37.733  20.547  -4.926  1.00128.58           O  
ANISOU 3487  OD1 ASP B1060    16533  14397  17923   -231    -18  -3001       O  
ATOM   3488  OD2 ASP B1060      39.717  19.881  -5.617  1.00137.04           O  
ANISOU 3488  OD2 ASP B1060    17858  15241  18967    324    513  -3210       O  
ATOM   3489  N   PHE B1061      39.040  24.279  -6.819  1.00110.14           N  
ANISOU 3489  N   PHE B1061    13971  13573  14302    356    239  -2270       N  
ATOM   3490  CA  PHE B1061      39.718  25.380  -6.133  1.00105.44           C  
ANISOU 3490  CA  PHE B1061    13145  13028  13890    447    383  -1760       C  
ATOM   3491  C   PHE B1061      38.711  26.426  -5.670  1.00105.30           C  
ANISOU 3491  C   PHE B1061    12972  13187  13851    289    131  -1466       C  
ATOM   3492  O   PHE B1061      38.742  26.811  -4.502  1.00101.38           O  
ANISOU 3492  O   PHE B1061    12298  12519  13702    221    100  -1205       O  
ATOM   3493  CB  PHE B1061      40.775  26.026  -7.049  1.00109.14           C  
ANISOU 3493  CB  PHE B1061    13627  13776  14063    706    716  -1609       C  
ATOM   3494  CG  PHE B1061      41.455  27.240  -6.466  1.00107.65           C  
ANISOU 3494  CG  PHE B1061    13188  13619  14093    729    861  -1119       C  
ATOM   3495  CD1 PHE B1061      42.543  27.104  -5.613  1.00109.45           C  
ANISOU 3495  CD1 PHE B1061    13219  13616  14749    776   1023   -986       C  
ATOM   3496  CD2 PHE B1061      41.030  28.520  -6.796  1.00109.11           C  
ANISOU 3496  CD2 PHE B1061    13328  14061  14067    707    833   -796       C  
ATOM   3497  CE1 PHE B1061      43.168  28.225  -5.073  1.00108.48           C  
ANISOU 3497  CE1 PHE B1061    12845  13526  14846    730   1114   -609       C  
ATOM   3498  CE2 PHE B1061      41.654  29.640  -6.253  1.00110.00           C  
ANISOU 3498  CE2 PHE B1061    13235  14111  14450    676    973   -399       C  
ATOM   3499  CZ  PHE B1061      42.727  29.487  -5.405  1.00106.88           C  
ANISOU 3499  CZ  PHE B1061    12634  13497  14480    657   1100   -342       C  
ATOM   3500  N   ARG B1062      37.824  26.882  -6.578  1.00103.15           N  
ANISOU 3500  N   ARG B1062    12760  13286  13148    269    -48  -1514       N  
ATOM   3501  CA  ARG B1062      36.799  27.880  -6.262  1.00100.78           C  
ANISOU 3501  CA  ARG B1062    12303  13176  12812    194   -271  -1225       C  
ATOM   3502  C   ARG B1062      35.712  27.270  -5.364  1.00102.50           C  
ANISOU 3502  C   ARG B1062    12399  13227  13318    -61   -551  -1356       C  
ATOM   3503  O   ARG B1062      35.118  27.994  -4.564  1.00 99.69           O  
ANISOU 3503  O   ARG B1062    11865  12894  13120   -101   -653  -1083       O  
ATOM   3504  CB  ARG B1062      36.175  28.467  -7.537  1.00104.39           C  
ANISOU 3504  CB  ARG B1062    12827  14141  12694    312   -382  -1182       C  
ATOM   3505  CG  ARG B1062      37.163  29.256  -8.396  1.00117.53           C  
ANISOU 3505  CG  ARG B1062    14588  16006  14062    574    -56   -911       C  
ATOM   3506  CD  ARG B1062      36.510  29.872  -9.625  1.00136.26           C  
ANISOU 3506  CD  ARG B1062    17033  18930  15808    744   -161   -778       C  
ATOM   3507  NE  ARG B1062      35.950  28.860 -10.523  1.00154.21           N  
ANISOU 3507  NE  ARG B1062    19449  21516  17629    698   -398  -1292       N  
ATOM   3508  CZ  ARG B1062      36.613  28.301 -11.530  1.00173.13           C  
ANISOU 3508  CZ  ARG B1062    22072  24099  19609    840   -218  -1592       C  
ATOM   3509  NH1 ARG B1062      37.866  28.657 -11.790  1.00161.38           N  
ANISOU 3509  NH1 ARG B1062    20652  22552  18113   1051    230  -1364       N  
ATOM   3510  NH2 ARG B1062      36.027  27.387 -12.290  1.00163.35           N  
ANISOU 3510  NH2 ARG B1062    20980  23123  17962    763   -478  -2145       N  
ATOM   3511  N   HIS B1063      35.484  25.938  -5.467  1.00100.65           N  
ANISOU 3511  N   HIS B1063    12264  12792  13186   -227   -633  -1765       N  
ATOM   3512  CA  HIS B1063      34.505  25.222  -4.642  1.00100.08           C  
ANISOU 3512  CA  HIS B1063    12064  12513  13447   -513   -843  -1863       C  
ATOM   3513  C   HIS B1063      34.938  25.226  -3.167  1.00 98.13           C  
ANISOU 3513  C   HIS B1063    11702  11917  13667   -509   -702  -1566       C  
ATOM   3514  O   HIS B1063      34.087  25.339  -2.279  1.00 96.49           O  
ANISOU 3514  O   HIS B1063    11305  11701  13656   -652   -826  -1396       O  
ATOM   3515  CB  HIS B1063      34.312  23.780  -5.140  1.00105.54           C  
ANISOU 3515  CB  HIS B1063    12930  12972  14200   -714   -918  -2383       C  
ATOM   3516  CG  HIS B1063      33.334  22.995  -4.325  1.00109.84           C  
ANISOU 3516  CG  HIS B1063    13328  13248  15157  -1060  -1088  -2445       C  
ATOM   3517  ND1 HIS B1063      31.971  23.108  -4.530  1.00113.72           N  
ANISOU 3517  ND1 HIS B1063    13598  14054  15556  -1318  -1409  -2509       N  
ATOM   3518  CD2 HIS B1063      33.555  22.108  -3.329  1.00111.41           C  
ANISOU 3518  CD2 HIS B1063    13546  12923  15861  -1170   -955  -2401       C  
ATOM   3519  CE1 HIS B1063      31.407  22.299  -3.647  1.00113.98           C  
ANISOU 3519  CE1 HIS B1063    13509  13733  16064  -1613  -1437  -2503       C  
ATOM   3520  NE2 HIS B1063      32.320  21.672  -2.904  1.00112.97           N  
ANISOU 3520  NE2 HIS B1063    13546  13080  16299  -1528  -1161  -2422       N  
ATOM   3521  N   GLY B1064      36.247  25.125  -2.932  1.00 91.45           N  
ANISOU 3521  N   GLY B1064    10942  10855  12950   -323   -445  -1497       N  
ATOM   3522  CA  GLY B1064      36.833  25.157  -1.597  1.00 87.52           C  
ANISOU 3522  CA  GLY B1064    10328  10119  12807   -272   -334  -1224       C  
ATOM   3523  C   GLY B1064      36.515  26.439  -0.850  1.00 86.67           C  
ANISOU 3523  C   GLY B1064    10039  10207  12685   -251   -394   -897       C  
ATOM   3524  O   GLY B1064      36.309  26.411   0.368  1.00 84.56           O  
ANISOU 3524  O   GLY B1064     9652   9837  12639   -296   -423   -726       O  
ATOM   3525  N   PHE B1065      36.438  27.574  -1.588  1.00 81.30           N  
ANISOU 3525  N   PHE B1065     9359   9804  11729   -161   -395   -805       N  
ATOM   3526  CA  PHE B1065      36.113  28.875  -1.009  1.00 77.92           C  
ANISOU 3526  CA  PHE B1065     8806   9488  11310   -115   -425   -532       C  
ATOM   3527  C   PHE B1065      34.598  29.016  -0.812  1.00 81.18           C  
ANISOU 3527  C   PHE B1065     9104  10068  11674   -206   -635   -500       C  
ATOM   3528  O   PHE B1065      34.188  29.767   0.071  1.00 79.04           O  
ANISOU 3528  O   PHE B1065     8718   9807  11505   -169   -649   -318       O  
ATOM   3529  CB  PHE B1065      36.654  30.027  -1.861  1.00 79.91           C  
ANISOU 3529  CB  PHE B1065     9112   9886  11365     33   -293   -376       C  
ATOM   3530  CG  PHE B1065      38.159  30.110  -1.820  1.00 80.75           C  
ANISOU 3530  CG  PHE B1065     9222   9855  11606     99    -59   -326       C  
ATOM   3531  CD1 PHE B1065      38.810  30.696  -0.740  1.00 81.70           C  
ANISOU 3531  CD1 PHE B1065     9216   9828  11996     73    -10   -191       C  
ATOM   3532  CD2 PHE B1065      38.927  29.620  -2.865  1.00 84.93           C  
ANISOU 3532  CD2 PHE B1065     9851  10448  11971    191    113   -433       C  
ATOM   3533  CE1 PHE B1065      40.203  30.746  -0.686  1.00 82.87           C  
ANISOU 3533  CE1 PHE B1065     9282   9908  12297    102    173   -147       C  
ATOM   3534  CE2 PHE B1065      40.322  29.691  -2.820  1.00 88.03           C  
ANISOU 3534  CE2 PHE B1065    10168  10764  12517    263    353   -355       C  
ATOM   3535  CZ  PHE B1065      40.950  30.255  -1.731  1.00 84.10           C  
ANISOU 3535  CZ  PHE B1065     9489  10134  12333    201    367   -200       C  
ATOM   3536  N   ASP B1066      33.769  28.269  -1.578  1.00 79.74           N  
ANISOU 3536  N   ASP B1066     8925  10027  11346   -330   -801   -706       N  
ATOM   3537  CA  ASP B1066      32.314  28.269  -1.372  1.00 80.12           C  
ANISOU 3537  CA  ASP B1066     8770  10280  11393   -452  -1015   -675       C  
ATOM   3538  C   ASP B1066      31.991  27.564  -0.048  1.00 81.88           C  
ANISOU 3538  C   ASP B1066     8868  10275  11967   -616   -995   -630       C  
ATOM   3539  O   ASP B1066      31.086  27.995   0.668  1.00 81.30           O  
ANISOU 3539  O   ASP B1066     8585  10344  11962   -626  -1048   -454       O  
ATOM   3540  CB  ASP B1066      31.559  27.616  -2.551  1.00 85.76           C  
ANISOU 3540  CB  ASP B1066     9473  11248  11862   -598  -1243   -954       C  
ATOM   3541  CG  ASP B1066      31.499  28.444  -3.828  1.00 94.91           C  
ANISOU 3541  CG  ASP B1066    10694  12804  12566   -394  -1312   -903       C  
ATOM   3542  OD1 ASP B1066      31.636  29.689  -3.740  1.00 93.03           O  
ANISOU 3542  OD1 ASP B1066    10436  12650  12263   -152  -1206   -566       O  
ATOM   3543  OD2 ASP B1066      31.174  27.870  -4.889  1.00104.31           O  
ANISOU 3543  OD2 ASP B1066    11936  14239  13458   -479  -1491  -1192       O  
ATOM   3544  N   ILE B1067      32.779  26.516   0.299  1.00 77.45           N  
ANISOU 3544  N   ILE B1067     8436   9372  11619   -692   -880   -741       N  
ATOM   3545  CA  ILE B1067      32.669  25.791   1.571  1.00 76.41           C  
ANISOU 3545  CA  ILE B1067     8226   9004  11804   -796   -811   -612       C  
ATOM   3546  C   ILE B1067      33.138  26.715   2.704  1.00 76.22           C  
ANISOU 3546  C   ILE B1067     8147   9025  11789   -597   -703   -343       C  
ATOM   3547  O   ILE B1067      32.483  26.797   3.740  1.00 75.07           O  
ANISOU 3547  O   ILE B1067     7852   8950  11722   -619   -694   -162       O  
ATOM   3548  CB  ILE B1067      33.477  24.450   1.544  1.00 81.08           C  
ANISOU 3548  CB  ILE B1067     8998   9186  12624   -859   -701   -766       C  
ATOM   3549  CG1 ILE B1067      33.033  23.537   0.375  1.00 85.14           C  
ANISOU 3549  CG1 ILE B1067     9619   9611  13118  -1073   -813  -1152       C  
ATOM   3550  CG2 ILE B1067      33.389  23.710   2.899  1.00 82.34           C  
ANISOU 3550  CG2 ILE B1067     9084   9101  13102   -921   -601   -523       C  
ATOM   3551  CD1 ILE B1067      33.852  22.223   0.218  1.00 94.56           C  
ANISOU 3551  CD1 ILE B1067    11050  10314  14565  -1091   -666  -1367       C  
ATOM   3552  N   LEU B1068      34.264  27.421   2.475  1.00 71.45           N  
ANISOU 3552  N   LEU B1068     7651   8405  11090   -418   -617   -340       N  
ATOM   3553  CA  LEU B1068      34.915  28.330   3.419  1.00 69.41           C  
ANISOU 3553  CA  LEU B1068     7359   8169  10846   -274   -546   -187       C  
ATOM   3554  C   LEU B1068      34.005  29.525   3.756  1.00 72.92           C  
ANISOU 3554  C   LEU B1068     7712   8810  11186   -207   -591    -86       C  
ATOM   3555  O   LEU B1068      33.825  29.811   4.936  1.00 72.86           O  
ANISOU 3555  O   LEU B1068     7638   8837  11207   -151   -566      5       O  
ATOM   3556  CB  LEU B1068      36.252  28.823   2.829  1.00 69.11           C  
ANISOU 3556  CB  LEU B1068     7409   8075  10776   -171   -447   -233       C  
ATOM   3557  CG  LEU B1068      37.179  29.632   3.745  1.00 72.89           C  
ANISOU 3557  CG  LEU B1068     7826   8546  11323    -93   -401   -148       C  
ATOM   3558  CD1 LEU B1068      37.725  28.768   4.876  1.00 73.24           C  
ANISOU 3558  CD1 LEU B1068     7801   8538  11490    -68   -410    -85       C  
ATOM   3559  CD2 LEU B1068      38.352  30.177   2.959  1.00 76.00           C  
ANISOU 3559  CD2 LEU B1068     8241   8908  11727    -51   -286   -169       C  
ATOM   3560  N   VAL B1069      33.418  30.196   2.736  1.00 69.75           N  
ANISOU 3560  N   VAL B1069     7309   8556  10636   -171   -648    -96       N  
ATOM   3561  CA  VAL B1069      32.502  31.338   2.927  1.00 70.01           C  
ANISOU 3561  CA  VAL B1069     7253   8750  10599    -36   -667     30       C  
ATOM   3562  C   VAL B1069      31.232  30.857   3.696  1.00 75.72           C  
ANISOU 3562  C   VAL B1069     7765   9633  11373    -98   -723     94       C  
ATOM   3563  O   VAL B1069      30.733  31.577   4.564  1.00 75.80           O  
ANISOU 3563  O   VAL B1069     7692   9724  11383     43   -662    193       O  
ATOM   3564  CB  VAL B1069      32.129  32.027   1.576  1.00 75.02           C  
ANISOU 3564  CB  VAL B1069     7919   9540  11045     72   -716     83       C  
ATOM   3565  CG1 VAL B1069      31.010  33.052   1.744  1.00 75.77           C  
ANISOU 3565  CG1 VAL B1069     7890   9798  11101    268   -733    254       C  
ATOM   3566  CG2 VAL B1069      33.347  32.677   0.934  1.00 74.42           C  
ANISOU 3566  CG2 VAL B1069     8026   9314  10936    145   -585    106       C  
ATOM   3567  N   GLY B1070      30.761  29.648   3.390  1.00 73.82           N  
ANISOU 3567  N   GLY B1070     7439   9414  11194   -315   -810     25       N  
ATOM   3568  CA  GLY B1070      29.609  29.036   4.052  1.00 75.48           C  
ANISOU 3568  CA  GLY B1070     7403   9756  11519   -450   -835    117       C  
ATOM   3569  C   GLY B1070      29.819  28.793   5.536  1.00 78.78           C  
ANISOU 3569  C   GLY B1070     7800  10095  12038   -415   -679    266       C  
ATOM   3570  O   GLY B1070      28.899  28.983   6.336  1.00 79.44           O  
ANISOU 3570  O   GLY B1070     7678  10380  12128   -370   -614    422       O  
ATOM   3571  N   GLN B1071      31.043  28.388   5.915  1.00 74.38           N  
ANISOU 3571  N   GLN B1071     7434   9301  11526   -398   -610    237       N  
ATOM   3572  CA  GLN B1071      31.412  28.159   7.311  1.00 74.22           C  
ANISOU 3572  CA  GLN B1071     7417   9266  11519   -320   -493    393       C  
ATOM   3573  C   GLN B1071      31.543  29.504   8.041  1.00 77.58           C  
ANISOU 3573  C   GLN B1071     7868   9852  11756    -80   -452    381       C  
ATOM   3574  O   GLN B1071      31.127  29.608   9.200  1.00 78.50           O  
ANISOU 3574  O   GLN B1071     7915  10134  11777     22   -361    499       O  
ATOM   3575  CB  GLN B1071      32.709  27.347   7.406  1.00 75.08           C  
ANISOU 3575  CB  GLN B1071     7683   9121  11725   -333   -468    379       C  
ATOM   3576  CG  GLN B1071      32.601  25.928   6.836  1.00 93.60           C  
ANISOU 3576  CG  GLN B1071    10058  11201  14303   -544   -464    355       C  
ATOM   3577  CD  GLN B1071      33.911  25.170   6.838  1.00113.18           C  
ANISOU 3577  CD  GLN B1071    12696  13405  16903   -471   -407    348       C  
ATOM   3578  OE1 GLN B1071      34.968  25.668   7.251  1.00107.02           O  
ANISOU 3578  OE1 GLN B1071    11949  12686  16027   -280   -394    389       O  
ATOM   3579  NE2 GLN B1071      33.872  23.945   6.341  1.00108.83           N  
ANISOU 3579  NE2 GLN B1071    12227  12538  16584   -620   -374    274       N  
ATOM   3580  N   ILE B1072      32.074  30.544   7.337  1.00 72.06           N  
ANISOU 3580  N   ILE B1072     7283   9092  11005     10   -497    234       N  
ATOM   3581  CA  ILE B1072      32.212  31.921   7.838  1.00 71.27           C  
ANISOU 3581  CA  ILE B1072     7252   9022  10807    201   -454    159       C  
ATOM   3582  C   ILE B1072      30.809  32.502   8.145  1.00 76.34           C  
ANISOU 3582  C   ILE B1072     7752   9871  11382    354   -389    240       C  
ATOM   3583  O   ILE B1072      30.624  33.119   9.195  1.00 77.86           O  
ANISOU 3583  O   ILE B1072     7960  10156  11467    522   -297    204       O  
ATOM   3584  CB  ILE B1072      32.994  32.813   6.820  1.00 73.52           C  
ANISOU 3584  CB  ILE B1072     7679   9120  11137    219   -475     56       C  
ATOM   3585  CG1 ILE B1072      34.476  32.357   6.715  1.00 72.49           C  
ANISOU 3585  CG1 ILE B1072     7628   8838  11077    111   -494    -20       C  
ATOM   3586  CG2 ILE B1072      32.921  34.303   7.217  1.00 76.01           C  
ANISOU 3586  CG2 ILE B1072     8078   9364  11438    396   -407    -19       C  
ATOM   3587  CD1 ILE B1072      35.336  33.035   5.603  1.00 76.53           C  
ANISOU 3587  CD1 ILE B1072     8235   9190  11654     87   -460    -61       C  
ATOM   3588  N   ASP B1073      29.826  32.267   7.258  1.00 72.35           N  
ANISOU 3588  N   ASP B1073     7087   9483  10918    310   -441    333       N  
ATOM   3589  CA  ASP B1073      28.462  32.759   7.428  1.00 73.67           C  
ANISOU 3589  CA  ASP B1073     7032   9908  11053    474   -386    452       C  
ATOM   3590  C   ASP B1073      27.762  32.094   8.629  1.00 80.03           C  
ANISOU 3590  C   ASP B1073     7641  10924  11843    446   -263    587       C  
ATOM   3591  O   ASP B1073      26.955  32.749   9.288  1.00 81.88           O  
ANISOU 3591  O   ASP B1073     7757  11360  11994    686   -120    647       O  
ATOM   3592  CB  ASP B1073      27.648  32.528   6.151  1.00 76.22           C  
ANISOU 3592  CB  ASP B1073     7165  10386  11407    392   -534    520       C  
ATOM   3593  CG  ASP B1073      28.032  33.466   5.020  1.00 82.81           C  
ANISOU 3593  CG  ASP B1073     8167  11119  12179    536   -600    490       C  
ATOM   3594  OD1 ASP B1073      28.553  34.562   5.311  1.00 82.58           O  
ANISOU 3594  OD1 ASP B1073     8319  10911  12148    763   -483    471       O  
ATOM   3595  OD2 ASP B1073      27.680  33.169   3.859  1.00 88.72           O  
ANISOU 3595  OD2 ASP B1073     8850  11991  12870    436   -760    498       O  
ATOM   3596  N   ASP B1074      28.085  30.827   8.931  1.00 77.10           N  
ANISOU 3596  N   ASP B1074     7250  10488  11555    192   -275    656       N  
ATOM   3597  CA  ASP B1074      27.505  30.108  10.073  1.00 79.32           C  
ANISOU 3597  CA  ASP B1074     7361  10944  11832    152   -115    873       C  
ATOM   3598  C   ASP B1074      28.037  30.689  11.388  1.00 84.15           C  
ANISOU 3598  C   ASP B1074     8134  11646  12195    407     21    848       C  
ATOM   3599  O   ASP B1074      27.280  30.812  12.353  1.00 87.32           O  
ANISOU 3599  O   ASP B1074     8388  12330  12460    549    210   1005       O  
ATOM   3600  CB  ASP B1074      27.804  28.600   9.982  1.00 81.66           C  
ANISOU 3600  CB  ASP B1074     7652  11042  12331   -168   -141    984       C  
ATOM   3601  CG  ASP B1074      27.132  27.879   8.817  1.00 92.67           C  
ANISOU 3601  CG  ASP B1074     8872  12374  13966   -477   -280    945       C  
ATOM   3602  OD1 ASP B1074      26.080  28.368   8.336  1.00 94.05           O  
ANISOU 3602  OD1 ASP B1074     8787  12810  14139   -461   -335    952       O  
ATOM   3603  OD2 ASP B1074      27.593  26.769   8.460  1.00 99.11           O  
ANISOU 3603  OD2 ASP B1074     9790  12895  14973   -728   -332    903       O  
ATOM   3604  N   ALA B1075      29.334  31.063  11.411  1.00 77.94           N  
ANISOU 3604  N   ALA B1075     7622  10661  11330    459    -76    638       N  
ATOM   3605  CA  ALA B1075      29.990  31.694  12.556  1.00 78.17           C  
ANISOU 3605  CA  ALA B1075     7811  10791  11099    661    -30    511       C  
ATOM   3606  C   ALA B1075      29.536  33.142  12.703  1.00 82.80           C  
ANISOU 3606  C   ALA B1075     8460  11422  11577    919     41    295       C  
ATOM   3607  O   ALA B1075      29.491  33.652  13.820  1.00 85.46           O  
ANISOU 3607  O   ALA B1075     8871  11945  11654   1128    144    180       O  
ATOM   3608  CB  ALA B1075      31.500  31.630  12.400  1.00 77.18           C  
ANISOU 3608  CB  ALA B1075     7876  10457  10994    571   -190    355       C  
ATOM   3609  N   LEU B1076      29.224  33.813  11.570  1.00 77.24           N  
ANISOU 3609  N   LEU B1076     7748  10544  11055    935     -4    239       N  
ATOM   3610  CA  LEU B1076      28.715  35.189  11.550  1.00 78.39           C  
ANISOU 3610  CA  LEU B1076     7958  10645  11183   1224     96     97       C  
ATOM   3611  C   LEU B1076      27.330  35.260  12.139  1.00 85.25           C  
ANISOU 3611  C   LEU B1076     8573  11857  11962   1457    294    264       C  
ATOM   3612  O   LEU B1076      26.972  36.262  12.764  1.00 87.95           O  
ANISOU 3612  O   LEU B1076     8988  12231  12199   1783    456    120       O  
ATOM   3613  CB  LEU B1076      28.690  35.753  10.126  1.00 77.20           C  
ANISOU 3613  CB  LEU B1076     7850  10241  11241   1212      6    108       C  
ATOM   3614  CG  LEU B1076      29.955  36.388   9.623  1.00 80.44           C  
ANISOU 3614  CG  LEU B1076     8535  10278  11751   1116    -78    -89       C  
ATOM   3615  CD1 LEU B1076      29.889  36.591   8.134  1.00 80.14           C  
ANISOU 3615  CD1 LEU B1076     8501  10086  11864   1083   -141     46       C  
ATOM   3616  CD2 LEU B1076      30.221  37.713  10.333  1.00 85.06           C  
ANISOU 3616  CD2 LEU B1076     9341  10660  12318   1318     28   -368       C  
ATOM   3617  N   LYS B1077      26.536  34.205  11.902  1.00 81.68           N  
ANISOU 3617  N   LYS B1077     7810  11643  11582   1284    301    555       N  
ATOM   3618  CA  LYS B1077      25.187  34.057  12.422  1.00 85.04           C  
ANISOU 3618  CA  LYS B1077     7893  12453  11965   1444    509    778       C  
ATOM   3619  C   LYS B1077      25.226  34.068  13.954  1.00 91.13           C  
ANISOU 3619  C   LYS B1077     8740  13458  12428   1636    738    757       C  
ATOM   3620  O   LYS B1077      24.478  34.814  14.582  1.00 94.05           O  
ANISOU 3620  O   LYS B1077     9049  14046  12641   1996    966    712       O  
ATOM   3621  CB  LYS B1077      24.558  32.761  11.884  1.00 88.28           C  
ANISOU 3621  CB  LYS B1077     7948  13010  12585   1099    440   1067       C  
ATOM   3622  CG  LYS B1077      23.120  32.538  12.347  1.00115.58           C  
ANISOU 3622  CG  LYS B1077    10934  16899  16080   1203    645   1339       C  
ATOM   3623  CD  LYS B1077      22.488  31.212  11.915  1.00131.84           C  
ANISOU 3623  CD  LYS B1077    12605  19074  18412    760    571   1599       C  
ATOM   3624  CE  LYS B1077      22.888  29.952  12.685  1.00145.18           C  
ANISOU 3624  CE  LYS B1077    14323  20704  20136    476    695   1801       C  
ATOM   3625  NZ  LYS B1077      24.357  29.675  12.660  1.00148.81           N  
ANISOU 3625  NZ  LYS B1077    15224  20759  20557    343    541   1636       N  
ATOM   3626  N   LEU B1078      26.154  33.280  14.541  1.00 85.85           N  
ANISOU 3626  N   LEU B1078     8231  12750  11637   1446    674    772       N  
ATOM   3627  CA  LEU B1078      26.346  33.143  15.984  1.00 87.79           C  
ANISOU 3627  CA  LEU B1078     8569  13282  11504   1612    840    789       C  
ATOM   3628  C   LEU B1078      26.915  34.432  16.598  1.00 93.39           C  
ANISOU 3628  C   LEU B1078     9604  13947  11931   1906    836    335       C  
ATOM   3629  O   LEU B1078      26.471  34.826  17.678  1.00 97.21           O  
ANISOU 3629  O   LEU B1078    10116  14764  12056   2208   1057    261       O  
ATOM   3630  CB  LEU B1078      27.282  31.959  16.279  1.00 86.13           C  
ANISOU 3630  CB  LEU B1078     8439  13012  11274   1351    718    965       C  
ATOM   3631  CG  LEU B1078      26.758  30.580  15.866  1.00 90.17           C  
ANISOU 3631  CG  LEU B1078     8683  13488  12089   1039    762   1390       C  
ATOM   3632  CD1 LEU B1078      27.869  29.580  15.756  1.00 88.39           C  
ANISOU 3632  CD1 LEU B1078     8610  13009  11964    814    604   1486       C  
ATOM   3633  CD2 LEU B1078      25.632  30.106  16.774  1.00 96.35           C  
ANISOU 3633  CD2 LEU B1078     9177  14678  12753   1125   1093   1778       C  
ATOM   3634  N   ALA B1079      27.881  35.090  15.913  1.00 87.19           N  
ANISOU 3634  N   ALA B1079     9063  12751  11316   1810    608     17       N  
ATOM   3635  CA  ALA B1079      28.494  36.342  16.372  1.00 88.70           C  
ANISOU 3635  CA  ALA B1079     9570  12776  11357   1989    574   -466       C  
ATOM   3636  C   ALA B1079      27.452  37.454  16.493  1.00 97.05           C  
ANISOU 3636  C   ALA B1079    10641  13830  12402   2377    821   -620       C  
ATOM   3637  O   ALA B1079      27.475  38.201  17.472  1.00100.65           O  
ANISOU 3637  O   ALA B1079    11307  14370  12565   2636    935   -978       O  
ATOM   3638  CB  ALA B1079      29.599  36.768  15.419  1.00 86.47           C  
ANISOU 3638  CB  ALA B1079     9464  12017  11373   1745    326   -667       C  
ATOM   3639  N   ASN B1080      26.513  37.531  15.515  1.00 93.78           N  
ANISOU 3639  N   ASN B1080     9994  13352  12285   2444    898   -359       N  
ATOM   3640  CA  ASN B1080      25.427  38.519  15.481  1.00 97.58           C  
ANISOU 3640  CA  ASN B1080    10416  13841  12818   2874   1145   -405       C  
ATOM   3641  C   ASN B1080      24.348  38.203  16.528  1.00105.50           C  
ANISOU 3641  C   ASN B1080    11171  15395  13521   3167   1465   -244       C  
ATOM   3642  O   ASN B1080      23.602  39.105  16.916  1.00109.68           O  
ANISOU 3642  O   ASN B1080    11717  15984  13973   3617   1732   -389       O  
ATOM   3643  CB  ASN B1080      24.795  38.583  14.088  1.00 98.40           C  
ANISOU 3643  CB  ASN B1080    10283  13812  13293   2859   1076   -111       C  
ATOM   3644  CG  ASN B1080      25.717  39.104  13.009  1.00125.30           C  
ANISOU 3644  CG  ASN B1080    13949  16698  16962   2683    854   -235       C  
ATOM   3645  OD1 ASN B1080      26.599  39.939  13.243  1.00120.54           O  
ANISOU 3645  OD1 ASN B1080    13708  15700  16390   2739    853   -589       O  
ATOM   3646  ND2 ASN B1080      25.476  38.681  11.782  1.00118.16           N  
ANISOU 3646  ND2 ASN B1080    12850  15790  16256   2471    680     51       N  
ATOM   3647  N   GLU B1081      24.267  36.938  16.984  1.00100.84           N  
ANISOU 3647  N   GLU B1081    10353  15182  12780   2937   1479     79       N  
ATOM   3648  CA  GLU B1081      23.311  36.527  18.015  1.00104.47           C  
ANISOU 3648  CA  GLU B1081    10548  16200  12944   3166   1822    322       C  
ATOM   3649  C   GLU B1081      23.911  36.736  19.426  1.00111.16           C  
ANISOU 3649  C   GLU B1081    11719  17281  13237   3361   1929     24       C  
ATOM   3650  O   GLU B1081      23.189  36.631  20.422  1.00115.68           O  
ANISOU 3650  O   GLU B1081    12151  18354  13448   3643   2266    165       O  
ATOM   3651  CB  GLU B1081      22.886  35.061  17.820  1.00104.47           C  
ANISOU 3651  CB  GLU B1081    10147  16447  13101   2798   1820    866       C  
ATOM   3652  CG  GLU B1081      22.044  34.827  16.574  1.00111.26           C  
ANISOU 3652  CG  GLU B1081    10608  17244  14421   2635   1735   1127       C  
ATOM   3653  CD  GLU B1081      21.679  33.386  16.264  1.00130.72           C  
ANISOU 3653  CD  GLU B1081    12697  19840  17132   2181   1685   1566       C  
ATOM   3654  OE1 GLU B1081      21.146  33.140  15.158  1.00121.69           O  
ANISOU 3654  OE1 GLU B1081    11230  18669  16340   1994   1544   1705       O  
ATOM   3655  OE2 GLU B1081      21.966  32.499  17.101  1.00128.06           O  
ANISOU 3655  OE2 GLU B1081    12399  19616  16643   2006   1772   1766       O  
ATOM   3656  N   GLY B1082      25.203  37.066  19.483  1.00105.06           N  
ANISOU 3656  N   GLY B1082    11345  16192  12380   3217   1643   -388       N  
ATOM   3657  CA  GLY B1082      25.928  37.291  20.730  1.00107.81           C  
ANISOU 3657  CA  GLY B1082    12002  16780  12181   3350   1629   -750       C  
ATOM   3658  C   GLY B1082      26.441  36.003  21.339  1.00110.56           C  
ANISOU 3658  C   GLY B1082    12269  17492  12249   3128   1535   -396       C  
ATOM   3659  O   GLY B1082      26.622  35.916  22.558  1.00114.61           O  
ANISOU 3659  O   GLY B1082    12924  18443  12179   3319   1600   -515       O  
ATOM   3660  N   LYS B1083      26.673  34.991  20.484  1.00101.38           N  
ANISOU 3660  N   LYS B1083    10891  16146  11482   2752   1387     42       N  
ATOM   3661  CA  LYS B1083      27.153  33.669  20.875  1.00 99.98           C  
ANISOU 3661  CA  LYS B1083    10630  16176  11181   2537   1316    462       C  
ATOM   3662  C   LYS B1083      28.633  33.554  20.497  1.00100.17           C  
ANISOU 3662  C   LYS B1083    10871  15875  11316   2272    906    236       C  
ATOM   3663  O   LYS B1083      28.962  33.047  19.421  1.00 95.85           O  
ANISOU 3663  O   LYS B1083    10248  14932  11240   1966    736    374       O  
ATOM   3664  CB  LYS B1083      26.289  32.576  20.211  1.00100.49           C  
ANISOU 3664  CB  LYS B1083    10318  16199  11666   2295   1458   1053       C  
ATOM   3665  CG  LYS B1083      24.815  32.634  20.615  1.00113.89           C  
ANISOU 3665  CG  LYS B1083    11694  18280  13297   2524   1873   1328       C  
ATOM   3666  CD  LYS B1083      23.980  31.591  19.898  1.00120.19           C  
ANISOU 3666  CD  LYS B1083    12074  19004  14589   2193   1956   1842       C  
ATOM   3667  CE  LYS B1083      22.532  31.662  20.313  1.00131.01           C  
ANISOU 3667  CE  LYS B1083    13036  20805  15936   2398   2367   2130       C  
ATOM   3668  NZ  LYS B1083      21.707  30.661  19.591  1.00140.19           N  
ANISOU 3668  NZ  LYS B1083    13738  21897  17632   1997   2402   2579       N  
ATOM   3669  N   VAL B1084      29.523  34.064  21.385  1.00 98.62           N  
ANISOU 3669  N   VAL B1084    10925  15883  10663   2400    745   -147       N  
ATOM   3670  CA  VAL B1084      30.984  34.153  21.199  1.00 95.95           C  
ANISOU 3670  CA  VAL B1084    10742  15333  10382   2181    349   -431       C  
ATOM   3671  C   VAL B1084      31.618  32.749  21.117  1.00 97.01           C  
ANISOU 3671  C   VAL B1084    10735  15527  10598   1995    227     79       C  
ATOM   3672  O   VAL B1084      32.216  32.430  20.090  1.00 92.34           O  
ANISOU 3672  O   VAL B1084    10101  14517  10467   1726     47    128       O  
ATOM   3673  CB  VAL B1084      31.659  34.974  22.333  1.00104.40           C  
ANISOU 3673  CB  VAL B1084    12055  16721  10889   2358    190   -990       C  
ATOM   3674  CG1 VAL B1084      33.146  35.181  22.048  1.00102.68           C  
ANISOU 3674  CG1 VAL B1084    11914  16268  10830   2078   -235  -1319       C  
ATOM   3675  CG2 VAL B1084      30.970  36.319  22.522  1.00107.14           C  
ANISOU 3675  CG2 VAL B1084    12588  16970  11148   2599    376  -1510       C  
ATOM   3676  N   LYS B1085      31.506  31.935  22.199  1.00 97.02           N  
ANISOU 3676  N   LYS B1085    10681  16043  10141   2178    352    466       N  
ATOM   3677  CA  LYS B1085      32.085  30.585  22.295  1.00 96.74           C  
ANISOU 3677  CA  LYS B1085    10540  16066  10152   2091    287   1015       C  
ATOM   3678  C   LYS B1085      31.545  29.661  21.194  1.00 96.59           C  
ANISOU 3678  C   LYS B1085    10347  15566  10785   1820    420   1442       C  
ATOM   3679  O   LYS B1085      32.284  28.794  20.727  1.00 94.82           O  
ANISOU 3679  O   LYS B1085    10094  15095  10837   1667    285   1691       O  
ATOM   3680  CB  LYS B1085      31.824  29.951  23.676  1.00105.31           C  
ANISOU 3680  CB  LYS B1085    11601  17799  10614   2390    493   1450       C  
ATOM   3681  CG  LYS B1085      32.771  30.421  24.800  1.00129.84           C  
ANISOU 3681  CG  LYS B1085    14861  21466  13006   2628    225   1150       C  
ATOM   3682  CD  LYS B1085      32.660  31.904  25.173  1.00147.31           C  
ANISOU 3682  CD  LYS B1085    17272  23831  14869   2746    123    346       C  
ATOM   3683  CE  LYS B1085      33.674  32.297  26.219  1.00169.12           C  
ANISOU 3683  CE  LYS B1085    20158  27151  16949   2901   -223     -8       C  
ATOM   3684  NZ  LYS B1085      33.576  33.740  26.563  1.00184.07           N  
ANISOU 3684  NZ  LYS B1085    22281  29098  18559   2964   -332   -881       N  
ATOM   3685  N   GLU B1086      30.285  29.869  20.758  1.00 91.89           N  
ANISOU 3685  N   GLU B1086     9625  14853  10436   1771    668   1491       N  
ATOM   3686  CA  GLU B1086      29.667  29.112  19.664  1.00 88.61           C  
ANISOU 3686  CA  GLU B1086     9023  14027  10617   1475    751   1786       C  
ATOM   3687  C   GLU B1086      30.309  29.498  18.325  1.00 87.46           C  
ANISOU 3687  C   GLU B1086     8959  13377  10895   1247    470   1423       C  
ATOM   3688  O   GLU B1086      30.623  28.617  17.519  1.00 84.53           O  
ANISOU 3688  O   GLU B1086     8546  12654  10916   1004    393   1599       O  
ATOM   3689  CB  GLU B1086      28.140  29.322  19.600  1.00 91.32           C  
ANISOU 3689  CB  GLU B1086     9130  14509  11058   1503   1061   1933       C  
ATOM   3690  CG  GLU B1086      27.329  28.850  20.800  1.00103.76           C  
ANISOU 3690  CG  GLU B1086    10555  16594  12273   1706   1433   2380       C  
ATOM   3691  CD  GLU B1086      27.268  29.705  22.054  1.00116.66           C  
ANISOU 3691  CD  GLU B1086    12322  18781  13223   2134   1572   2155       C  
ATOM   3692  OE1 GLU B1086      26.241  29.600  22.755  1.00107.94           O  
ANISOU 3692  OE1 GLU B1086    11023  18075  11912   2319   1954   2432       O  
ATOM   3693  OE2 GLU B1086      28.146  30.572  22.263  1.00107.42           O  
ANISOU 3693  OE2 GLU B1086    11427  17633  11757   2272   1316   1644       O  
ATOM   3694  N   ALA B1087      30.498  30.826  18.094  1.00 82.88           N  
ANISOU 3694  N   ALA B1087     8512  12745  10235   1339    352    920       N  
ATOM   3695  CA  ALA B1087      31.116  31.379  16.889  1.00 78.95           C  
ANISOU 3695  CA  ALA B1087     8102  11812  10082   1162    134    601       C  
ATOM   3696  C   ALA B1087      32.588  30.977  16.798  1.00 82.52           C  
ANISOU 3696  C   ALA B1087     8648  12137  10567   1050   -113    539       C  
ATOM   3697  O   ALA B1087      33.045  30.620  15.711  1.00 79.82           O  
ANISOU 3697  O   ALA B1087     8296  11444  10587    849   -217    546       O  
ATOM   3698  CB  ALA B1087      30.984  32.891  16.876  1.00 80.07           C  
ANISOU 3698  CB  ALA B1087     8379  11907  10136   1316    126    148       C  
ATOM   3699  N   GLN B1088      33.317  31.000  17.945  1.00 81.50           N  
ANISOU 3699  N   GLN B1088     8583  12353  10029   1205   -205    489       N  
ATOM   3700  CA  GLN B1088      34.726  30.597  18.041  1.00 81.16           C  
ANISOU 3700  CA  GLN B1088     8549  12316   9970   1153   -456    474       C  
ATOM   3701  C   GLN B1088      34.872  29.098  17.746  1.00 86.62           C  
ANISOU 3701  C   GLN B1088     9141  12870  10900   1092   -392    986       C  
ATOM   3702  O   GLN B1088      35.872  28.699  17.153  1.00 86.22           O  
ANISOU 3702  O   GLN B1088     9068  12606  11085   1004   -545    990       O  
ATOM   3703  CB  GLN B1088      35.315  30.936  19.422  1.00 86.46           C  
ANISOU 3703  CB  GLN B1088     9272  13505  10073   1359   -598    312       C  
ATOM   3704  CG  GLN B1088      35.442  32.441  19.693  1.00 95.18           C  
ANISOU 3704  CG  GLN B1088    10521  14645  11000   1373   -711   -322       C  
ATOM   3705  CD  GLN B1088      35.998  32.791  21.057  1.00115.78           C  
ANISOU 3705  CD  GLN B1088    13193  17805  12992   1551   -894   -589       C  
ATOM   3706  OE1 GLN B1088      36.083  31.961  21.968  1.00116.50           O  
ANISOU 3706  OE1 GLN B1088    13225  18380  12661   1748   -890   -239       O  
ATOM   3707  NE2 GLN B1088      36.339  34.057  21.245  1.00106.96           N  
ANISOU 3707  NE2 GLN B1088    12214  16632  11795   1491  -1049  -1223       N  
ATOM   3708  N   ALA B1089      33.862  28.278  18.128  1.00 85.23           N  
ANISOU 3708  N   ALA B1089     8895  12774  10713   1133   -135   1415       N  
ATOM   3709  CA  ALA B1089      33.820  26.836  17.851  1.00 85.71           C  
ANISOU 3709  CA  ALA B1089     8890  12588  11086   1043    -18   1904       C  
ATOM   3710  C   ALA B1089      33.553  26.572  16.358  1.00 88.04           C  
ANISOU 3710  C   ALA B1089     9170  12349  11931    755    -18   1793       C  
ATOM   3711  O   ALA B1089      34.154  25.669  15.771  1.00 87.31           O  
ANISOU 3711  O   ALA B1089     9100  11922  12151    667    -47   1933       O  
ATOM   3712  CB  ALA B1089      32.753  26.170  18.699  1.00 89.95           C  
ANISOU 3712  CB  ALA B1089     9338  13357  11480   1120    286   2386       C  
ATOM   3713  N   ALA B1090      32.656  27.371  15.748  1.00 84.34           N  
ANISOU 3713  N   ALA B1090     8666  11828  11550    648     16   1539       N  
ATOM   3714  CA  ALA B1090      32.316  27.280  14.328  1.00 82.22           C  
ANISOU 3714  CA  ALA B1090     8373  11177  11688    403    -20   1397       C  
ATOM   3715  C   ALA B1090      33.496  27.701  13.466  1.00 84.83           C  
ANISOU 3715  C   ALA B1090     8824  11280  12128    365   -221   1080       C  
ATOM   3716  O   ALA B1090      33.746  27.090  12.428  1.00 83.98           O  
ANISOU 3716  O   ALA B1090     8742  10848  12319    207   -253   1052       O  
ATOM   3717  CB  ALA B1090      31.103  28.150  14.023  1.00 82.70           C  
ANISOU 3717  CB  ALA B1090     8328  11359  11734    387     52   1263       C  
ATOM   3718  N   ALA B1091      34.243  28.730  13.924  1.00 81.48           N  
ANISOU 3718  N   ALA B1091     8467  11031  11460    500   -343    827       N  
ATOM   3719  CA  ALA B1091      35.419  29.284  13.247  1.00 79.53           C  
ANISOU 3719  CA  ALA B1091     8282  10617  11320    448   -507    550       C  
ATOM   3720  C   ALA B1091      36.602  28.317  13.297  1.00 84.23           C  
ANISOU 3720  C   ALA B1091     8845  11145  12013    473   -577    708       C  
ATOM   3721  O   ALA B1091      37.530  28.451  12.504  1.00 82.61           O  
ANISOU 3721  O   ALA B1091     8639  10757  11992    408   -652    562       O  
ATOM   3722  CB  ALA B1091      35.813  30.608  13.884  1.00 81.07           C  
ANISOU 3722  CB  ALA B1091     8527  11002  11272    534   -612    231       C  
ATOM   3723  N   GLU B1092      36.570  27.344  14.218  1.00 83.92           N  
ANISOU 3723  N   GLU B1092     8766  11262  11856    602   -522   1052       N  
ATOM   3724  CA  GLU B1092      37.632  26.351  14.348  1.00 85.27           C  
ANISOU 3724  CA  GLU B1092     8897  11371  12130    710   -562   1288       C  
ATOM   3725  C   GLU B1092      37.494  25.283  13.239  1.00 87.99           C  
ANISOU 3725  C   GLU B1092     9296  11228  12908    588   -430   1396       C  
ATOM   3726  O   GLU B1092      38.483  24.645  12.893  1.00 88.64           O  
ANISOU 3726  O   GLU B1092     9369  11137  13174    677   -444   1466       O  
ATOM   3727  CB  GLU B1092      37.611  25.716  15.746  1.00 90.53           C  
ANISOU 3727  CB  GLU B1092     9523  12373  12500    937   -523   1690       C  
ATOM   3728  CG  GLU B1092      38.944  25.819  16.488  1.00106.60           C  
ANISOU 3728  CG  GLU B1092    11456  14763  14283   1154   -744   1716       C  
ATOM   3729  CD  GLU B1092      39.494  27.191  16.871  1.00135.01           C  
ANISOU 3729  CD  GLU B1092    15002  18723  17573   1132   -996   1262       C  
ATOM   3730  OE1 GLU B1092      38.780  28.211  16.711  1.00137.01           O  
ANISOU 3730  OE1 GLU B1092    15345  18965  17746   1003   -970    929       O  
ATOM   3731  OE2 GLU B1092      40.637  27.234  17.383  1.00128.84           O  
ANISOU 3731  OE2 GLU B1092    14074  18242  16638   1254  -1223   1247       O  
ATOM   3732  N   GLN B1093      36.297  25.150  12.635  1.00 83.66           N  
ANISOU 3732  N   GLN B1093     8789  10480  12517    388   -315   1359       N  
ATOM   3733  CA  GLN B1093      36.051  24.237  11.509  1.00 83.37           C  
ANISOU 3733  CA  GLN B1093     8822   9998  12856    214   -230   1333       C  
ATOM   3734  C   GLN B1093      36.674  24.789  10.200  1.00 83.90           C  
ANISOU 3734  C   GLN B1093     8946   9926  13007    149   -318    960       C  
ATOM   3735  O   GLN B1093      36.860  24.032   9.242  1.00 84.14           O  
ANISOU 3735  O   GLN B1093     9063   9625  13280     74   -265    870       O  
ATOM   3736  CB  GLN B1093      34.548  23.987  11.312  1.00 85.60           C  
ANISOU 3736  CB  GLN B1093     9063  10209  13253    -15   -131   1389       C  
ATOM   3737  CG  GLN B1093      33.892  23.198  12.446  1.00114.00           C  
ANISOU 3737  CG  GLN B1093    12590  13862  16862      4     42   1836       C  
ATOM   3738  CD  GLN B1093      32.416  22.948  12.220  1.00146.22           C  
ANISOU 3738  CD  GLN B1093    16546  17894  21118   -273    148   1899       C  
ATOM   3739  OE1 GLN B1093      31.739  23.628  11.434  1.00143.25           O  
ANISOU 3739  OE1 GLN B1093    16087  17644  20700   -397     63   1629       O  
ATOM   3740  NE2 GLN B1093      31.863  22.003  12.964  1.00144.56           N  
ANISOU 3740  NE2 GLN B1093    16282  17536  21108   -362    348   2308       N  
ATOM   3741  N   LEU B1094      37.010  26.100  10.177  1.00 77.28           N  
ANISOU 3741  N   LEU B1094     8074   9325  11966    182   -427    744       N  
ATOM   3742  CA  LEU B1094      37.656  26.769   9.041  1.00 74.72           C  
ANISOU 3742  CA  LEU B1094     7784   8911  11696    135   -469    474       C  
ATOM   3743  C   LEU B1094      39.079  26.240   8.846  1.00 77.95           C  
ANISOU 3743  C   LEU B1094     8159   9228  12232    257   -458    497       C  
ATOM   3744  O   LEU B1094      39.577  26.227   7.719  1.00 76.71           O  
ANISOU 3744  O   LEU B1094     8046   8914  12189    230   -402    345       O  
ATOM   3745  CB  LEU B1094      37.680  28.300   9.243  1.00 73.64           C  
ANISOU 3745  CB  LEU B1094     7620   8979  11381    132   -552    297       C  
ATOM   3746  CG  LEU B1094      36.319  29.019   9.282  1.00 78.03           C  
ANISOU 3746  CG  LEU B1094     8198   9623  11826     88   -535    253       C  
ATOM   3747  CD1 LEU B1094      36.456  30.421   9.782  1.00 78.14           C  
ANISOU 3747  CD1 LEU B1094     8224   9768  11698    144   -586     84       C  
ATOM   3748  CD2 LEU B1094      35.671  29.039   7.926  1.00 80.84           C  
ANISOU 3748  CD2 LEU B1094     8599   9838  12277    -20   -508    177       C  
ATOM   3749  N   LYS B1095      39.722  25.792   9.949  1.00 75.83           N  
ANISOU 3749  N   LYS B1095     7791   9108  11913    428   -500    713       N  
ATOM   3750  CA  LYS B1095      41.064  25.204   9.950  1.00 77.28           C  
ANISOU 3750  CA  LYS B1095     7868   9273  12220    617   -497    813       C  
ATOM   3751  C   LYS B1095      41.088  23.908   9.145  1.00 83.79           C  
ANISOU 3751  C   LYS B1095     8820   9682  13334    672   -318    877       C  
ATOM   3752  O   LYS B1095      42.030  23.688   8.389  1.00 84.39           O  
ANISOU 3752  O   LYS B1095     8862   9648  13552    775   -246    782       O  
ATOM   3753  CB  LYS B1095      41.552  24.935  11.380  1.00 81.64           C  
ANISOU 3753  CB  LYS B1095     8280  10138  12602    828   -607   1094       C  
ATOM   3754  CG  LYS B1095      41.708  26.174  12.236  1.00 91.38           C  
ANISOU 3754  CG  LYS B1095     9398  11801  13521    784   -812    936       C  
ATOM   3755  CD  LYS B1095      42.221  25.797  13.611  1.00102.68           C  
ANISOU 3755  CD  LYS B1095    10687  13630  14698   1021   -953   1202       C  
ATOM   3756  CE  LYS B1095      42.383  27.009  14.476  1.00111.26           C  
ANISOU 3756  CE  LYS B1095    11684  15153  15436    956  -1185    941       C  
ATOM   3757  NZ  LYS B1095      42.902  26.660  15.821  1.00124.80           N  
ANISOU 3757  NZ  LYS B1095    13251  17366  16800   1205  -1369   1172       N  
ATOM   3758  N   THR B1096      40.039  23.062   9.293  1.00 82.43           N  
ANISOU 3758  N   THR B1096     8789   9264  13266    590   -226   1014       N  
ATOM   3759  CA  THR B1096      39.875  21.790   8.571  1.00 85.03           C  
ANISOU 3759  CA  THR B1096     9288   9104  13917    576    -58   1009       C  
ATOM   3760  C   THR B1096      39.828  22.071   7.055  1.00 89.11           C  
ANISOU 3760  C   THR B1096     9917   9478  14463    428    -32    593       C  
ATOM   3761  O   THR B1096      40.459  21.352   6.275  1.00 90.90           O  
ANISOU 3761  O   THR B1096    10249   9416  14872    539     97    464       O  
ATOM   3762  CB  THR B1096      38.603  21.060   9.065  1.00 94.61           C  
ANISOU 3762  CB  THR B1096    10581  10114  15252    402     15   1213       C  
ATOM   3763  OG1 THR B1096      38.649  20.931  10.485  1.00 97.30           O  
ANISOU 3763  OG1 THR B1096    10817  10692  15461    571     13   1639       O  
ATOM   3764  CG2 THR B1096      38.429  19.686   8.434  1.00 97.02           C  
ANISOU 3764  CG2 THR B1096    11077   9825  15962    340    186   1190       C  
ATOM   3765  N   THR B1097      39.114  23.145   6.658  1.00 83.52           N  
ANISOU 3765  N   THR B1097     9189   9003  13542    230   -140    402       N  
ATOM   3766  CA  THR B1097      38.988  23.580   5.268  1.00 82.43           C  
ANISOU 3766  CA  THR B1097     9144   8849  13327    118   -137     76       C  
ATOM   3767  C   THR B1097      40.330  24.193   4.810  1.00 86.64           C  
ANISOU 3767  C   THR B1097     9600   9521  13799    289    -84      8       C  
ATOM   3768  O   THR B1097      40.729  23.989   3.660  1.00 87.72           O  
ANISOU 3768  O   THR B1097     9834   9564  13931    325     26   -195       O  
ATOM   3769  CB  THR B1097      37.809  24.572   5.134  1.00 84.36           C  
ANISOU 3769  CB  THR B1097     9354   9325  13372    -77   -262      6       C  
ATOM   3770  OG1 THR B1097      36.630  23.968   5.670  1.00 84.48           O  
ANISOU 3770  OG1 THR B1097     9353   9265  13478   -233   -286    118       O  
ATOM   3771  CG2 THR B1097      37.551  24.995   3.689  1.00 80.37           C  
ANISOU 3771  CG2 THR B1097     8943   8864  12729   -162   -279   -263       C  
ATOM   3772  N   ARG B1098      41.034  24.909   5.721  1.00 82.42           N  
ANISOU 3772  N   ARG B1098     8871   9236  13210    382   -156    167       N  
ATOM   3773  CA  ARG B1098      42.324  25.556   5.438  1.00 82.57           C  
ANISOU 3773  CA  ARG B1098     8724   9420  13230    480   -120    136       C  
ATOM   3774  C   ARG B1098      43.421  24.489   5.216  1.00 90.36           C  
ANISOU 3774  C   ARG B1098     9652  10267  14412    737     32    204       C  
ATOM   3775  O   ARG B1098      44.304  24.689   4.379  1.00 90.72           O  
ANISOU 3775  O   ARG B1098     9617  10361  14491    822    170    115       O  
ATOM   3776  CB  ARG B1098      42.715  26.520   6.583  1.00 80.77           C  
ANISOU 3776  CB  ARG B1098     8284   9493  12911    453   -290    226       C  
ATOM   3777  CG  ARG B1098      43.882  27.443   6.249  1.00 84.35           C  
ANISOU 3777  CG  ARG B1098     8525  10114  13412    427   -275    158       C  
ATOM   3778  CD  ARG B1098      45.162  27.150   6.989  1.00 90.06           C  
ANISOU 3778  CD  ARG B1098     8940  11050  14230    586   -349    291       C  
ATOM   3779  NE  ARG B1098      45.155  27.649   8.367  1.00 88.90           N  
ANISOU 3779  NE  ARG B1098     8665  11175  13937    540   -601    324       N  
ATOM   3780  CZ  ARG B1098      44.852  26.920   9.434  1.00 94.60           C  
ANISOU 3780  CZ  ARG B1098     9406  11997  14542    696   -705    511       C  
ATOM   3781  NH1 ARG B1098      44.912  27.455  10.644  1.00 78.31           N  
ANISOU 3781  NH1 ARG B1098     7229  10263  12260    674   -935    504       N  
ATOM   3782  NH2 ARG B1098      44.518  25.642   9.303  1.00 78.11           N  
ANISOU 3782  NH2 ARG B1098     7456   9672  12550    880   -567    708       N  
ATOM   3783  N   ASN B1099      43.340  23.353   5.939  1.00 90.27           N  
ANISOU 3783  N   ASN B1099     9682  10072  14544    889     47    395       N  
ATOM   3784  CA  ASN B1099      44.286  22.241   5.808  1.00 94.35           C  
ANISOU 3784  CA  ASN B1099    10171  10385  15294   1204    217    502       C  
ATOM   3785  C   ASN B1099      44.061  21.485   4.493  1.00101.26           C  
ANISOU 3785  C   ASN B1099    11322  10872  16280   1215    432    218       C  
ATOM   3786  O   ASN B1099      45.022  20.973   3.920  1.00103.68           O  
ANISOU 3786  O   ASN B1099    11601  11073  16719   1487    631    169       O  
ATOM   3787  CB  ASN B1099      44.173  21.286   6.991  1.00 98.65           C  
ANISOU 3787  CB  ASN B1099    10710  10805  15967   1382    189    855       C  
ATOM   3788  CG  ASN B1099      44.506  21.903   8.334  1.00125.52           C  
ANISOU 3788  CG  ASN B1099    13842  14669  19179   1443    -33   1121       C  
ATOM   3789  OD1 ASN B1099      45.036  23.019   8.442  1.00115.44           O  
ANISOU 3789  OD1 ASN B1099    12340  13780  17740   1359   -179   1012       O  
ATOM   3790  ND2 ASN B1099      44.186  21.185   9.398  1.00123.19           N  
ANISOU 3790  ND2 ASN B1099    13573  14339  18893   1578    -60   1473       N  
ATOM   3791  N   ALA B1100      42.801  21.449   4.001  1.00 97.49           N  
ANISOU 3791  N   ALA B1100    11087  10232  15723    931    385      2       N  
ATOM   3792  CA  ALA B1100      42.437  20.825   2.725  1.00 99.37           C  
ANISOU 3792  CA  ALA B1100    11602  10171  15983    876    518   -362       C  
ATOM   3793  C   ALA B1100      42.985  21.646   1.538  1.00103.21           C  
ANISOU 3793  C   ALA B1100    12068  10937  16210    905    601   -593       C  
ATOM   3794  O   ALA B1100      43.011  21.156   0.415  1.00105.13           O  
ANISOU 3794  O   ALA B1100    12531  11044  16370    927    729   -920       O  
ATOM   3795  CB  ALA B1100      40.928  20.687   2.624  1.00 99.53           C  
ANISOU 3795  CB  ALA B1100    11790  10051  15974    527    377   -503       C  
ATOM   3796  N   TYR B1101      43.450  22.883   1.808  1.00 98.19           N  
ANISOU 3796  N   TYR B1101    11172  10688  15447    903    545   -420       N  
ATOM   3797  CA  TYR B1101      44.066  23.775   0.828  1.00 98.36           C  
ANISOU 3797  CA  TYR B1101    11120  10981  15274    921    665   -508       C  
ATOM   3798  C   TYR B1101      45.594  23.627   0.825  1.00104.60           C  
ANISOU 3798  C   TYR B1101    11644  11883  16217   1207    870   -375       C  
ATOM   3799  O   TYR B1101      46.188  23.567  -0.254  1.00106.85           O  
ANISOU 3799  O   TYR B1101    11950  12237  16410   1352   1120   -502       O  
ATOM   3800  CB  TYR B1101      43.688  25.252   1.103  1.00 96.84           C  
ANISOU 3800  CB  TYR B1101    10808  11067  14919    682    494   -398       C  
ATOM   3801  CG  TYR B1101      44.506  26.252   0.305  1.00100.24           C  
ANISOU 3801  CG  TYR B1101    11107  11740  15241    689    650   -361       C  
ATOM   3802  CD1 TYR B1101      44.112  26.650  -0.970  1.00103.34           C  
ANISOU 3802  CD1 TYR B1101    11685  12218  15360    660    763   -488       C  
ATOM   3803  CD2 TYR B1101      45.681  26.795   0.824  1.00101.79           C  
ANISOU 3803  CD2 TYR B1101    10969  12105  15603    711    682   -177       C  
ATOM   3804  CE1 TYR B1101      44.876  27.549  -1.717  1.00105.77           C  
ANISOU 3804  CE1 TYR B1101    11874  12738  15576    678    966   -370       C  
ATOM   3805  CE2 TYR B1101      46.458  27.685   0.082  1.00104.11           C  
ANISOU 3805  CE2 TYR B1101    11108  12580  15868    670    869   -102       C  
ATOM   3806  CZ  TYR B1101      46.054  28.057  -1.190  1.00112.99           C  
ANISOU 3806  CZ  TYR B1101    12447  13751  16733    664   1039   -167       C  
ATOM   3807  OH  TYR B1101      46.809  28.952  -1.911  1.00116.40           O  
ANISOU 3807  OH  TYR B1101    12729  14356  17143    627   1271    -11       O  
ATOM   3808  N   ILE B1102      46.235  23.644   2.020  1.00100.52           N  
ANISOU 3808  N   ILE B1102    10842  11458  15893   1298    761   -109       N  
ATOM   3809  CA  ILE B1102      47.698  23.612   2.140  1.00102.81           C  
ANISOU 3809  CA  ILE B1102    10766  11950  16347   1556    898     55       C  
ATOM   3810  C   ILE B1102      48.244  22.249   1.594  1.00109.78           C  
ANISOU 3810  C   ILE B1102    11757  12560  17393   1956   1193    -17       C  
ATOM   3811  O   ILE B1102      49.367  22.232   1.086  1.00112.38           O  
ANISOU 3811  O   ILE B1102    11851  13062  17788   2196   1437     12       O  
ATOM   3812  CB  ILE B1102      48.211  23.901   3.602  1.00106.01           C  
ANISOU 3812  CB  ILE B1102    10816  12596  16865   1573    643    338       C  
ATOM   3813  CG1 ILE B1102      47.788  22.841   4.670  1.00107.52           C  
ANISOU 3813  CG1 ILE B1102    11133  12573  17148   1730    518    517       C  
ATOM   3814  CG2 ILE B1102      47.812  25.301   4.063  1.00103.34           C  
ANISOU 3814  CG2 ILE B1102    10371  12510  16382   1208    403    321       C  
ATOM   3815  CD1 ILE B1102      48.669  21.527   4.799  1.00119.89           C  
ANISOU 3815  CD1 ILE B1102    12639  13934  18979   2203    708    703       C  
ATOM   3816  N   GLN B1103      47.448  21.146   1.643  1.00106.00           N  
ANISOU 3816  N   GLN B1103    11635  11636  17005   2017   1204   -128       N  
ATOM   3817  CA  GLN B1103      47.921  19.852   1.138  1.00109.84           C  
ANISOU 3817  CA  GLN B1103    12288  11749  17696   2400   1501   -247       C  
ATOM   3818  C   GLN B1103      47.436  19.631  -0.323  1.00114.05           C  
ANISOU 3818  C   GLN B1103    13206  12110  18017   2336   1694   -724       C  
ATOM   3819  O   GLN B1103      47.574  18.527  -0.854  1.00118.04           O  
ANISOU 3819  O   GLN B1103    13962  12230  18658   2607   1940   -961       O  
ATOM   3820  CB  GLN B1103      47.488  18.671   2.049  1.00112.81           C  
ANISOU 3820  CB  GLN B1103    12839  11652  18373   2523   1449    -81       C  
ATOM   3821  CG  GLN B1103      45.990  18.366   2.139  1.00119.14           C  
ANISOU 3821  CG  GLN B1103    14006  12111  19152   2143   1288   -244       C  
ATOM   3822  CD  GLN B1103      45.688  17.161   3.015  1.00137.52           C  
ANISOU 3822  CD  GLN B1103    16475  13941  21837   2264   1308      6       C  
ATOM   3823  OE1 GLN B1103      46.537  16.651   3.757  1.00134.37           O  
ANISOU 3823  OE1 GLN B1103    15885  13515  21654   2645   1380    390       O  
ATOM   3824  NE2 GLN B1103      44.453  16.692   2.967  1.00130.38           N  
ANISOU 3824  NE2 GLN B1103    15874  12657  21008   1934   1240   -157       N  
ATOM   3825  N   LYS B1104      46.954  20.695  -0.987  1.00107.04           N  
ANISOU 3825  N   LYS B1104    12359  11530  16781   2024   1597   -862       N  
ATOM   3826  CA  LYS B1104      46.495  20.616  -2.369  1.00108.46           C  
ANISOU 3826  CA  LYS B1104    12870  11696  16645   1973   1728  -1282       C  
ATOM   3827  C   LYS B1104      47.206  21.642  -3.258  1.00113.58           C  
ANISOU 3827  C   LYS B1104    13339  12823  16993   2033   1929  -1237       C  
ATOM   3828  O   LYS B1104      48.025  21.254  -4.086  1.00117.62           O  
ANISOU 3828  O   LYS B1104    13849  13391  17451   2364   2280  -1358       O  
ATOM   3829  CB  LYS B1104      44.967  20.822  -2.461  1.00108.06           C  
ANISOU 3829  CB  LYS B1104    13072  11582  16404   1557   1422  -1463       C  
ATOM   3830  CG  LYS B1104      44.094  19.619  -2.095  1.00120.78           C  
ANISOU 3830  CG  LYS B1104    14964  12666  18261   1446   1315  -1662       C  
ATOM   3831  CD  LYS B1104      44.044  18.583  -3.208  1.00136.02           C  
ANISOU 3831  CD  LYS B1104    17270  14289  20121   1566   1508  -2193       C  
ATOM   3832  CE  LYS B1104      43.099  17.448  -2.921  1.00146.61           C  
ANISOU 3832  CE  LYS B1104    18900  15059  21747   1343   1387  -2448       C  
ATOM   3833  NZ  LYS B1104      43.027  16.511  -4.072  1.00158.99           N  
ANISOU 3833  NZ  LYS B1104    20863  16329  23216   1416   1546  -3079       N  
ATOM   3834  N   TYR B1105      46.912  22.941  -3.079  1.00107.14           N  
ANISOU 3834  N   TYR B1105    12374  12329  16006   1734   1747  -1040       N  
ATOM   3835  CA  TYR B1105      47.392  24.002  -3.965  1.00107.87           C  
ANISOU 3835  CA  TYR B1105    12339  12823  15825   1716   1937   -936       C  
ATOM   3836  C   TYR B1105      48.703  24.636  -3.474  1.00114.39           C  
ANISOU 3836  C   TYR B1105    12669  13885  16911   1787   2078   -576       C  
ATOM   3837  O   TYR B1105      49.512  25.021  -4.323  1.00117.06           O  
ANISOU 3837  O   TYR B1105    12855  14495  17126   1902   2400   -490       O  
ATOM   3838  CB  TYR B1105      46.317  25.092  -4.109  1.00105.08           C  
ANISOU 3838  CB  TYR B1105    12095  12617  15214   1372   1685   -881       C  
ATOM   3839  CG  TYR B1105      45.023  24.508  -4.632  1.00106.17           C  
ANISOU 3839  CG  TYR B1105    12628  12619  15093   1267   1500  -1227       C  
ATOM   3840  CD1 TYR B1105      44.853  24.245  -5.988  1.00111.59           C  
ANISOU 3840  CD1 TYR B1105    13583  13473  15343   1372   1646  -1515       C  
ATOM   3841  CD2 TYR B1105      44.011  24.113  -3.761  1.00104.13           C  
ANISOU 3841  CD2 TYR B1105    12450  12096  15020   1064   1186  -1283       C  
ATOM   3842  CE1 TYR B1105      43.705  23.617  -6.465  1.00113.66           C  
ANISOU 3842  CE1 TYR B1105    14167  13644  15373   1242   1427  -1900       C  
ATOM   3843  CE2 TYR B1105      42.858  23.485  -4.226  1.00105.97           C  
ANISOU 3843  CE2 TYR B1105    12975  12205  15085    919   1011  -1618       C  
ATOM   3844  CZ  TYR B1105      42.705  23.248  -5.581  1.00117.67           C  
ANISOU 3844  CZ  TYR B1105    14702  13860  16145    989   1103  -1950       C  
ATOM   3845  OH  TYR B1105      41.565  22.646  -6.053  1.00121.81           O  
ANISOU 3845  OH  TYR B1105    15475  14311  16496    800    873  -2332       O  
ATOM   3846  N   LEU B1106      48.931  24.732  -2.141  1.00110.11           N  
ANISOU 3846  N   LEU B1106    11851  13286  16701   1712   1842   -367       N  
ATOM   3847  CA  LEU B1106      50.169  25.312  -1.590  1.00111.27           C  
ANISOU 3847  CA  LEU B1106    11469  13701  17109   1730   1893    -73       C  
ATOM   3848  C   LEU B1106      51.390  24.434  -1.921  1.00120.72           C  
ANISOU 3848  C   LEU B1106    12426  14956  18487   2172   2220    -34       C  
ATOM   3849  O   LEU B1106      52.464  24.965  -2.213  1.00122.93           O  
ANISOU 3849  O   LEU B1106    12262  15553  18894   2229   2427    164       O  
ATOM   3850  CB  LEU B1106      50.067  25.507  -0.072  1.00108.57           C  
ANISOU 3850  CB  LEU B1106    10924  13352  16975   1549   1503     83       C  
ATOM   3851  N   GLY B1107      51.202  23.114  -1.904  1.00119.75           N  
ANISOU 3851  N   GLY B1107    12587  14504  18410   2479   2286   -218       N  
ATOM   3852  CA  GLY B1107      52.265  22.158  -2.194  1.00125.30           C  
ANISOU 3852  CA  GLY B1107    13133  15167  19309   2986   2622   -207       C  
ATOM   3853  C   GLY B1107      52.150  21.438  -3.522  1.00133.65           C  
ANISOU 3853  C   GLY B1107    14569  16083  20129   3266   3018   -565       C  
ATOM   3854  O   GLY B1107      51.278  21.750  -4.342  1.00132.18           O  
ANISOU 3854  O   GLY B1107    14738  15923  19561   3050   3024   -812       O  
ATOM   3855  N   SER B1108      53.025  20.442  -3.728  1.00135.88           N  
ANISOU 3855  N   SER B1108    14781  16236  20613   3790   3348   -606       N  
ATOM   3856  CA  SER B1108      53.066  19.626  -4.942  1.00141.14           C  
ANISOU 3856  CA  SER B1108    15814  16746  21065   4149   3772  -1012       C  
ATOM   3857  C   SER B1108      51.953  18.530  -4.936  1.00146.27           C  
ANISOU 3857  C   SER B1108    17103  16747  21728   4146   3648  -1452       C  
ATOM   3858  O   SER B1108      52.085  17.512  -5.629  1.00151.37           O  
ANISOU 3858  O   SER B1108    18077  17092  22346   4522   3976  -1838       O  
ATOM   3859  CB  SER B1108      54.442  18.980  -5.094  1.00151.30           C  
ANISOU 3859  CB  SER B1108    16726  18153  22608   4756   4219   -870       C  
ATOM   3860  OG  SER B1108      54.776  18.153  -3.992  1.00161.83           O  
ANISOU 3860  OG  SER B1108    17885  19187  24417   5044   4102   -641       O  
ATOM   3861  N   GLY B1109      50.869  18.775  -4.181  1.00137.86           N  
ANISOU 3861  N   GLY B1109    16197  15473  20709   3705   3196  -1410       N  
ATOM   3862  CA  GLY B1109      49.715  17.881  -4.085  1.00137.80           C  
ANISOU 3862  CA  GLY B1109    16714  14878  20767   3560   3031  -1768       C  
ATOM   3863  C   GLY B1109      48.926  17.898  -5.375  1.00141.62           C  
ANISOU 3863  C   GLY B1109    17634  15409  20765   3356   3048  -2301       C  
ATOM   3864  O   GLY B1109      48.793  16.869  -6.047  1.00146.55           O  
ANISOU 3864  O   GLY B1109    18677  15655  21352   3539   3235  -2803       O  
ATOM   3865  N   SER B1110      48.432  19.092  -5.739  1.00132.71           N  
ANISOU 3865  N   SER B1110    16412  14758  19252   2993   2850  -2200       N  
ATOM   3866  CA  SER B1110      47.754  19.361  -7.001  1.00133.06           C  
ANISOU 3866  CA  SER B1110    16784  15040  18732   2834   2843  -2595       C  
ATOM   3867  C   SER B1110      48.746  20.076  -7.914  1.00136.72           C  
ANISOU 3867  C   SER B1110    17039  16060  18848   3086   3222  -2453       C  
ATOM   3868  O   SER B1110      48.655  21.286  -8.151  1.00133.61           O  
ANISOU 3868  O   SER B1110    16457  16113  18195   2868   3153  -2159       O  
ATOM   3869  CB  SER B1110      46.468  20.155  -6.788  1.00132.00           C  
ANISOU 3869  CB  SER B1110    16700  15035  18418   2320   2389  -2528       C  
ATOM   3870  OG  SER B1110      45.534  19.406  -6.030  1.00141.47           O  
ANISOU 3870  OG  SER B1110    18104  15736  19912   2090   2105  -2702       O  
ATOM   3871  N   CYS B  35      49.766  19.308  -8.335  1.00101.99           N  
ANISOU 3871  N   CYS B  35    10749  13086  14916    404  -1443   1185       N  
ATOM   3872  CA  CYS B  35      50.889  19.708  -9.184  1.00 99.90           C  
ANISOU 3872  CA  CYS B  35    10683  12792  14483    471  -1426   1188       C  
ATOM   3873  C   CYS B  35      51.568  18.448  -9.703  1.00107.41           C  
ANISOU 3873  C   CYS B  35    11752  13754  15305    355  -1536   1060       C  
ATOM   3874  O   CYS B  35      51.228  17.972 -10.792  1.00108.26           O  
ANISOU 3874  O   CYS B  35    11872  13968  15295    367  -1714   1045       O  
ATOM   3875  CB  CYS B  35      51.858  20.613  -8.416  1.00 96.42           C  
ANISOU 3875  CB  CYS B  35    10353  12208  14075    519  -1204   1205       C  
ATOM   3876  SG  CYS B  35      53.376  21.039  -9.316  1.00 97.93           S  
ANISOU 3876  SG  CYS B  35    10776  12338  14095    579  -1149   1212       S  
ATOM   3877  N   SER B  36      52.468  17.863  -8.878  1.00105.38           N  
ANISOU 3877  N   SER B  36    11577  13392  15072    249  -1435    963       N  
ATOM   3878  CA  SER B  36      53.194  16.626  -9.173  1.00106.01           C  
ANISOU 3878  CA  SER B  36    11773  13452  15056    138  -1505    836       C  
ATOM   3879  C   SER B  36      52.267  15.393  -9.042  1.00113.43           C  
ANISOU 3879  C   SER B  36    12582  14429  16085      1  -1640    759       C  
ATOM   3880  O   SER B  36      51.174  15.487  -8.461  1.00114.19           O  
ANISOU 3880  O   SER B  36    12498  14549  16339    -21  -1634    807       O  
ATOM   3881  CB  SER B  36      54.398  16.485  -8.244  1.00107.27           C  
ANISOU 3881  CB  SER B  36    12059  13481  15217     96  -1335    782       C  
ATOM   3882  N   GLN B  37      52.712  14.243  -9.594  1.00110.79           N  
ANISOU 3882  N   GLN B  37    12342  14093  15661    -89  -1752    640       N  
ATOM   3883  CA  GLN B  37      51.971  12.980  -9.587  1.00111.69           C  
ANISOU 3883  CA  GLN B  37    12358  14219  15861   -233  -1892    546       C  
ATOM   3884  C   GLN B  37      51.916  12.357  -8.173  1.00113.65           C  
ANISOU 3884  C   GLN B  37    12535  14364  16284   -343  -1761    534       C  
ATOM   3885  O   GLN B  37      52.733  12.693  -7.310  1.00111.22           O  
ANISOU 3885  O   GLN B  37    12304  13975  15981   -314  -1579    560       O  
ATOM   3886  CB  GLN B  37      52.617  11.989 -10.569  1.00113.60           C  
ANISOU 3886  CB  GLN B  37    12758  14453  15950   -286  -2012    410       C  
ATOM   3887  N   LYS B  38      50.933  11.451  -7.954  1.00110.89           N  
ANISOU 3887  N   LYS B  38    12033  14022  16079   -467  -1860    497       N  
ATOM   3888  CA  LYS B  38      50.705  10.726  -6.698  1.00109.66           C  
ANISOU 3888  CA  LYS B  38    11790  13779  16098   -576  -1750    501       C  
ATOM   3889  C   LYS B  38      51.804   9.661  -6.460  1.00111.32           C  
ANISOU 3889  C   LYS B  38    12168  13869  16260   -661  -1698    400       C  
ATOM   3890  O   LYS B  38      52.412   9.213  -7.435  1.00111.17           O  
ANISOU 3890  O   LYS B  38    12290  13844  16105   -669  -1800    302       O  
ATOM   3891  CB  LYS B  38      49.318  10.060  -6.728  1.00114.00           C  
ANISOU 3891  CB  LYS B  38    12113  14370  16830   -686  -1882    501       C  
ATOM   3892  N   PRO B  39      52.060   9.214  -5.193  1.00105.92           N  
ANISOU 3892  N   PRO B  39    11473  13095  15679   -714  -1540    425       N  
ATOM   3893  CA  PRO B  39      53.099   8.186  -4.959  1.00104.37           C  
ANISOU 3893  CA  PRO B  39    11429  12784  15442   -782  -1490    343       C  
ATOM   3894  C   PRO B  39      52.844   6.883  -5.728  1.00108.27           C  
ANISOU 3894  C   PRO B  39    11934  13235  15971   -908  -1653    227       C  
ATOM   3895  O   PRO B  39      53.797   6.205  -6.117  1.00107.17           O  
ANISOU 3895  O   PRO B  39    11957  13016  15745   -932  -1654    136       O  
ATOM   3896  CB  PRO B  39      53.009   7.931  -3.451  1.00105.57           C  
ANISOU 3896  CB  PRO B  39    11511  12875  15724   -814  -1318    417       C  
ATOM   3897  CG  PRO B  39      51.679   8.455  -3.034  1.00111.18           C  
ANISOU 3897  CG  PRO B  39    12005  13660  16578   -808  -1312    515       C  
ATOM   3898  CD  PRO B  39      51.446   9.633  -3.917  1.00107.17           C  
ANISOU 3898  CD  PRO B  39    11486  13255  15978   -698  -1393    535       C  
ATOM   3899  N   SER B  40      51.556   6.548  -5.954  1.00105.86           N  
ANISOU 3899  N   SER B  40    11447  12974  15800   -988  -1790    224       N  
ATOM   3900  CA  SER B  40      51.114   5.380  -6.719  1.00106.63           C  
ANISOU 3900  CA  SER B  40    11526  13032  15957  -1118  -1974     97       C  
ATOM   3901  C   SER B  40      51.598   5.478  -8.171  1.00109.10           C  
ANISOU 3901  C   SER B  40    11994  13407  16054  -1059  -2136    -19       C  
ATOM   3902  O   SER B  40      52.010   4.471  -8.752  1.00109.25           O  
ANISOU 3902  O   SER B  40    12133  13350  16026  -1127  -2219   -157       O  
ATOM   3903  CB  SER B  40      49.593   5.266  -6.669  1.00111.73           C  
ANISOU 3903  CB  SER B  40    11913  13730  16809  -1207  -2085    132       C  
ATOM   3904  OG  SER B  40      49.135   5.203  -5.328  1.00119.43           O  
ANISOU 3904  OG  SER B  40    12746  14655  17977  -1249  -1914    254       O  
ATOM   3905  N   ASP B  41      51.591   6.715  -8.727  1.00103.89           N  
ANISOU 3905  N   ASP B  41    11340  12876  15255   -920  -2162     44       N  
ATOM   3906  CA  ASP B  41      52.028   7.042 -10.089  1.00103.09           C  
ANISOU 3906  CA  ASP B  41    11385  12860  14924   -828  -2290    -26       C  
ATOM   3907  C   ASP B  41      53.561   7.044 -10.218  1.00101.42           C  
ANISOU 3907  C   ASP B  41    11417  12579  14539   -761  -2166    -64       C  
ATOM   3908  O   ASP B  41      54.073   6.859 -11.325  1.00101.77           O  
ANISOU 3908  O   ASP B  41    11611  12651  14406   -723  -2265   -163       O  
ATOM   3909  CB  ASP B  41      51.482   8.423 -10.521  1.00105.31           C  
ANISOU 3909  CB  ASP B  41    11591  13289  15131   -686  -2319     92       C  
ATOM   3910  CG  ASP B  41      49.970   8.538 -10.634  1.00117.80           C  
ANISOU 3910  CG  ASP B  41    12929  14975  16856   -719  -2466    136       C  
ATOM   3911  OD1 ASP B  41      49.279   7.493 -10.539  1.00119.43           O  
ANISOU 3911  OD1 ASP B  41    13009  15143  17227   -869  -2572     61       O  
ATOM   3912  OD2 ASP B  41      49.480   9.660 -10.885  1.00124.58           O  
ANISOU 3912  OD2 ASP B  41    13718  15949  17668   -594  -2482    245       O  
ATOM   3913  N   LYS B  42      54.287   7.273  -9.110  1.00 92.81           N  
ANISOU 3913  N   LYS B  42    10362  11408  13494   -738  -1954     14       N  
ATOM   3914  CA  LYS B  42      55.745   7.339  -9.152  1.00 89.45           C  
ANISOU 3914  CA  LYS B  42    10137  10921  12930   -673  -1829     -8       C  
ATOM   3915  C   LYS B  42      56.358   6.277  -8.194  1.00 90.32           C  
ANISOU 3915  C   LYS B  42    10290  10886  13140   -767  -1721    -50       C  
ATOM   3916  O   LYS B  42      57.324   6.563  -7.475  1.00 89.14           O  
ANISOU 3916  O   LYS B  42    10224  10684  12960   -719  -1561     -9       O  
ATOM   3917  CB  LYS B  42      56.235   8.771  -8.810  1.00 89.59           C  
ANISOU 3917  CB  LYS B  42    10171  10978  12892   -542  -1680    117       C  
ATOM   3918  CG  LYS B  42      55.799   9.347  -7.461  1.00 93.38           C  
ANISOU 3918  CG  LYS B  42    10511  11440  13528   -547  -1550    224       C  
ATOM   3919  CD  LYS B  42      56.292  10.784  -7.306  1.00101.07           C  
ANISOU 3919  CD  LYS B  42    11517  12441  14445   -416  -1424    319       C  
ATOM   3920  CE  LYS B  42      56.026  11.384  -5.943  1.00113.65           C  
ANISOU 3920  CE  LYS B  42    13002  14010  16169   -406  -1283    402       C  
ATOM   3921  NZ  LYS B  42      54.579  11.471  -5.621  1.00124.80           N  
ANISOU 3921  NZ  LYS B  42    14220  15484  17716   -433  -1341    459       N  
ATOM   3922  N   HIS B  43      55.835   5.031  -8.244  1.00 85.42           N  
ANISOU 3922  N   HIS B  43     9620  10199  12639   -899  -1817   -135       N  
ATOM   3923  CA  HIS B  43      56.346   3.947  -7.401  1.00 83.26           C  
ANISOU 3923  CA  HIS B  43     9388   9779  12469   -984  -1719   -162       C  
ATOM   3924  C   HIS B  43      57.250   3.006  -8.204  1.00 86.04           C  
ANISOU 3924  C   HIS B  43     9927  10052  12713   -995  -1769   -304       C  
ATOM   3925  O   HIS B  43      56.814   2.425  -9.202  1.00 88.21           O  
ANISOU 3925  O   HIS B  43    10225  10338  12954  -1040  -1941   -426       O  
ATOM   3926  CB  HIS B  43      55.199   3.147  -6.755  1.00 84.72           C  
ANISOU 3926  CB  HIS B  43     9397   9906  12888  -1125  -1755   -147       C  
ATOM   3927  CG  HIS B  43      55.671   2.010  -5.901  1.00 87.56           C  
ANISOU 3927  CG  HIS B  43     9798  10108  13361  -1204  -1647   -154       C  
ATOM   3928  ND1 HIS B  43      55.873   0.744  -6.430  1.00 90.24           N  
ANISOU 3928  ND1 HIS B  43    10227  10329  13732  -1292  -1728   -286       N  
ATOM   3929  CD2 HIS B  43      55.988   1.989  -4.585  1.00 88.20           C  
ANISOU 3929  CD2 HIS B  43     9853  10138  13520  -1195  -1466    -43       C  
ATOM   3930  CE1 HIS B  43      56.309  -0.001  -5.426  1.00 89.23           C  
ANISOU 3930  CE1 HIS B  43    10118  10074  13711  -1332  -1587   -237       C  
ATOM   3931  NE2 HIS B  43      56.394   0.701  -4.296  1.00 88.35           N  
ANISOU 3931  NE2 HIS B  43     9939  10006  13621  -1273  -1430    -88       N  
ATOM   3932  N   LEU B  44      58.496   2.823  -7.730  1.00 78.90           N  
ANISOU 3932  N   LEU B  44     9150   9066  11761   -952  -1622   -294       N  
ATOM   3933  CA  LEU B  44      59.458   1.906  -8.339  1.00 77.91           C  
ANISOU 3933  CA  LEU B  44     9201   8850  11550   -949  -1631   -415       C  
ATOM   3934  C   LEU B  44      59.777   0.771  -7.372  1.00 78.78           C  
ANISOU 3934  C   LEU B  44     9319   8804  11810  -1029  -1536   -413       C  
ATOM   3935  O   LEU B  44      60.048   1.019  -6.199  1.00 76.09           O  
ANISOU 3935  O   LEU B  44     8929   8446  11537  -1012  -1392   -297       O  
ATOM   3936  CB  LEU B  44      60.751   2.632  -8.769  1.00 76.72           C  
ANISOU 3936  CB  LEU B  44     9201   8746  11203   -809  -1540   -401       C  
ATOM   3937  CG  LEU B  44      60.625   3.670  -9.896  1.00 81.80           C  
ANISOU 3937  CG  LEU B  44     9879   9531  11672   -710  -1618   -399       C  
ATOM   3938  CD1 LEU B  44      61.924   4.405 -10.101  1.00 80.31           C  
ANISOU 3938  CD1 LEU B  44     9815   9363  11336   -584  -1487   -356       C  
ATOM   3939  CD2 LEU B  44      60.176   3.030 -11.206  1.00 86.79           C  
ANISOU 3939  CD2 LEU B  44    10577  10189  12211   -734  -1805   -545       C  
ATOM   3940  N   ASP B  45      59.727  -0.479  -7.869  1.00 76.30           N  
ANISOU 3940  N   ASP B  45     9071   8373  11545  -1110  -1617   -543       N  
ATOM   3941  CA  ASP B  45      60.005  -1.688  -7.086  1.00 76.15           C  
ANISOU 3941  CA  ASP B  45     9071   8182  11680  -1185  -1533   -544       C  
ATOM   3942  C   ASP B  45      61.494  -1.803  -6.738  1.00 76.51           C  
ANISOU 3942  C   ASP B  45     9265   8178  11629  -1083  -1381   -520       C  
ATOM   3943  O   ASP B  45      61.838  -2.502  -5.787  1.00 76.09           O  
ANISOU 3943  O   ASP B  45     9211   8013  11687  -1107  -1270   -461       O  
ATOM   3944  CB  ASP B  45      59.558  -2.945  -7.857  1.00 80.86           C  
ANISOU 3944  CB  ASP B  45     9704   8654  12364  -1299  -1674   -710       C  
ATOM   3945  CG  ASP B  45      58.076  -3.013  -8.186  1.00 97.83           C  
ANISOU 3945  CG  ASP B  45    11689  10838  14643  -1421  -1844   -751       C  
ATOM   3946  OD1 ASP B  45      57.295  -2.232  -7.591  1.00 99.95           O  
ANISOU 3946  OD1 ASP B  45    11791  11209  14978  -1427  -1826   -623       O  
ATOM   3947  OD2 ASP B  45      57.689  -3.879  -9.004  1.00105.60           O  
ANISOU 3947  OD2 ASP B  45    12705  11743  15677  -1510  -1994   -915       O  
ATOM   3948  N   ALA B  46      62.369  -1.125  -7.515  1.00 70.13           N  
ANISOU 3948  N   ALA B  46     8575   7455  10618   -964  -1375   -554       N  
ATOM   3949  CA  ALA B  46      63.820  -1.120  -7.334  1.00 67.29           C  
ANISOU 3949  CA  ALA B  46     8340   7066  10162   -860  -1240   -534       C  
ATOM   3950  C   ALA B  46      64.230  -0.431  -6.026  1.00 68.27           C  
ANISOU 3950  C   ALA B  46     8389   7226  10326   -815  -1094   -380       C  
ATOM   3951  O   ALA B  46      65.138  -0.914  -5.364  1.00 66.85           O  
ANISOU 3951  O   ALA B  46     8263   6975  10163   -777   -985   -348       O  
ATOM   3952  CB  ALA B  46      64.483  -0.425  -8.507  1.00 67.54           C  
ANISOU 3952  CB  ALA B  46     8484   7195   9984   -749  -1264   -588       C  
ATOM   3953  N   ILE B  47      63.563   0.688  -5.657  1.00 64.02           N  
ANISOU 3953  N   ILE B  47     7727   6799   9799   -811  -1098   -291       N  
ATOM   3954  CA  ILE B  47      63.848   1.487  -4.453  1.00 62.31           C  
ANISOU 3954  CA  ILE B  47     7440   6631   9606   -764   -975   -166       C  
ATOM   3955  C   ILE B  47      63.834   0.575  -3.176  1.00 66.51           C  
ANISOU 3955  C   ILE B  47     7933   7063  10273   -814   -890   -104       C  
ATOM   3956  O   ILE B  47      64.875   0.518  -2.534  1.00 64.51           O  
ANISOU 3956  O   ILE B  47     7735   6787   9987   -749   -790    -67       O  
ATOM   3957  CB  ILE B  47      62.850   2.685  -4.310  1.00 65.08           C  
ANISOU 3957  CB  ILE B  47     7660   7099   9968   -761  -1005    -97       C  
ATOM   3958  CG1 ILE B  47      63.067   3.743  -5.423  1.00 64.81           C  
ANISOU 3958  CG1 ILE B  47     7672   7164   9790   -683  -1056   -122       C  
ATOM   3959  CG2 ILE B  47      62.898   3.338  -2.920  1.00 65.01           C  
ANISOU 3959  CG2 ILE B  47     7570   7123  10006   -728   -885     16       C  
ATOM   3960  CD1 ILE B  47      64.472   4.433  -5.453  1.00 70.78           C  
ANISOU 3960  CD1 ILE B  47     8520   7939  10434   -576   -953   -103       C  
ATOM   3961  N   PRO B  48      62.758  -0.174  -2.794  1.00 66.14           N  
ANISOU 3961  N   PRO B  48     7796   6955  10380   -920   -922    -84       N  
ATOM   3962  CA  PRO B  48      62.854  -1.003  -1.574  1.00 66.28           C  
ANISOU 3962  CA  PRO B  48     7789   6878  10515   -947   -816      1       C  
ATOM   3963  C   PRO B  48      63.954  -2.073  -1.662  1.00 71.16           C  
ANISOU 3963  C   PRO B  48     8542   7369  11125   -923   -773    -45       C  
ATOM   3964  O   PRO B  48      64.543  -2.400  -0.633  1.00 71.19           O  
ANISOU 3964  O   PRO B  48     8555   7330  11162   -886   -663     44       O  
ATOM   3965  CB  PRO B  48      61.477  -1.659  -1.482  1.00 69.40           C  
ANISOU 3965  CB  PRO B  48     8065   7215  11089  -1076   -873     14       C  
ATOM   3966  CG  PRO B  48      60.577  -0.765  -2.239  1.00 74.03           C  
ANISOU 3966  CG  PRO B  48     8565   7920  11645  -1093   -983    -18       C  
ATOM   3967  CD  PRO B  48      61.405  -0.269  -3.381  1.00 69.27           C  
ANISOU 3967  CD  PRO B  48     8089   7369  10860  -1016  -1048   -120       C  
ATOM   3968  N   ILE B  49      64.257  -2.587  -2.883  1.00 67.53           N  
ANISOU 3968  N   ILE B  49     8192   6857  10610   -927   -856   -180       N  
ATOM   3969  CA  ILE B  49      65.310  -3.592  -3.107  1.00 67.03           C  
ANISOU 3969  CA  ILE B  49     8264   6669  10534   -889   -812   -236       C  
ATOM   3970  C   ILE B  49      66.691  -2.941  -2.857  1.00 69.61           C  
ANISOU 3970  C   ILE B  49     8653   7071  10726   -754   -717   -192       C  
ATOM   3971  O   ILE B  49      67.462  -3.469  -2.057  1.00 69.82           O  
ANISOU 3971  O   ILE B  49     8702   7044  10784   -707   -618   -122       O  
ATOM   3972  CB  ILE B  49      65.222  -4.225  -4.531  1.00 70.84           C  
ANISOU 3972  CB  ILE B  49     8852   7081  10983   -924   -929   -410       C  
ATOM   3973  CG1 ILE B  49      63.854  -4.932  -4.746  1.00 72.50           C  
ANISOU 3973  CG1 ILE B  49     8983   7212  11349  -1073  -1045   -470       C  
ATOM   3974  CG2 ILE B  49      66.392  -5.193  -4.771  1.00 71.51           C  
ANISOU 3974  CG2 ILE B  49     9085   7034  11052   -865   -865   -468       C  
ATOM   3975  CD1 ILE B  49      63.538  -5.405  -6.189  1.00 77.34           C  
ANISOU 3975  CD1 ILE B  49     9685   7787  11915  -1117  -1202   -666       C  
ATOM   3976  N   LEU B  50      66.977  -1.790  -3.515  1.00 64.63           N  
ANISOU 3976  N   LEU B  50     8037   6564   9954   -692   -746   -223       N  
ATOM   3977  CA  LEU B  50      68.230  -1.030  -3.392  1.00 62.96           C  
ANISOU 3977  CA  LEU B  50     7864   6425   9632   -578   -666   -190       C  
ATOM   3978  C   LEU B  50      68.502  -0.619  -1.943  1.00 64.73           C  
ANISOU 3978  C   LEU B  50     8006   6698   9890   -544   -577    -69       C  
ATOM   3979  O   LEU B  50      69.644  -0.701  -1.503  1.00 63.63           O  
ANISOU 3979  O   LEU B  50     7900   6560   9715   -465   -504    -40       O  
ATOM   3980  CB  LEU B  50      68.195   0.223  -4.284  1.00 62.80           C  
ANISOU 3980  CB  LEU B  50     7845   6524   9490   -537   -711   -219       C  
ATOM   3981  CG  LEU B  50      68.806   0.139  -5.704  1.00 68.56           C  
ANISOU 3981  CG  LEU B  50     8702   7249  10099   -483   -741   -321       C  
ATOM   3982  CD1 LEU B  50      68.207  -0.986  -6.542  1.00 71.06           C  
ANISOU 3982  CD1 LEU B  50     9090   7472  10438   -549   -837   -440       C  
ATOM   3983  CD2 LEU B  50      68.645   1.455  -6.436  1.00 69.59           C  
ANISOU 3983  CD2 LEU B  50     8818   7505  10118   -438   -771   -311       C  
ATOM   3984  N   TYR B  51      67.458  -0.211  -1.204  1.00 61.55           N  
ANISOU 3984  N   TYR B  51     7495   6339   9553   -598   -585     -1       N  
ATOM   3985  CA  TYR B  51      67.549   0.192   0.204  1.00 61.19           C  
ANISOU 3985  CA  TYR B  51     7377   6349   9523   -561   -505    105       C  
ATOM   3986  C   TYR B  51      67.984  -0.994   1.099  1.00 65.88           C  
ANISOU 3986  C   TYR B  51     8001   6852  10180   -548   -433    166       C  
ATOM   3987  O   TYR B  51      68.752  -0.774   2.032  1.00 65.82           O  
ANISOU 3987  O   TYR B  51     7987   6892  10129   -470   -367    227       O  
ATOM   3988  CB  TYR B  51      66.203   0.767   0.689  1.00 62.56           C  
ANISOU 3988  CB  TYR B  51     7433   6585   9753   -616   -521    161       C  
ATOM   3989  CG  TYR B  51      66.016   2.250   0.410  1.00 62.71           C  
ANISOU 3989  CG  TYR B  51     7405   6722   9700   -581   -545    151       C  
ATOM   3990  CD1 TYR B  51      66.134   2.757  -0.881  1.00 63.99           C  
ANISOU 3990  CD1 TYR B  51     7606   6908   9798   -576   -617     77       C  
ATOM   3991  CD2 TYR B  51      65.554   3.110   1.401  1.00 62.87           C  
ANISOU 3991  CD2 TYR B  51     7342   6825   9722   -552   -495    220       C  
ATOM   3992  CE1 TYR B  51      65.943   4.109  -1.146  1.00 63.03           C  
ANISOU 3992  CE1 TYR B  51     7443   6880   9625   -538   -628     86       C  
ATOM   3993  CE2 TYR B  51      65.325   4.460   1.140  1.00 62.90           C  
ANISOU 3993  CE2 TYR B  51     7304   6915   9681   -519   -511    211       C  
ATOM   3994  CZ  TYR B  51      65.514   4.953  -0.139  1.00 68.57           C  
ANISOU 3994  CZ  TYR B  51     8059   7645  10349   -514   -576    151       C  
ATOM   3995  OH  TYR B  51      65.295   6.280  -0.404  1.00 69.20           O  
ANISOU 3995  OH  TYR B  51     8099   7797  10395   -475   -582    159       O  
ATOM   3996  N   TYR B  52      67.542  -2.236   0.799  1.00 63.23           N  
ANISOU 3996  N   TYR B  52     7696   6382   9947   -618   -449    148       N  
ATOM   3997  CA  TYR B  52      67.968  -3.409   1.570  1.00 63.48           C  
ANISOU 3997  CA  TYR B  52     7763   6304  10051   -598   -371    218       C  
ATOM   3998  C   TYR B  52      69.385  -3.849   1.165  1.00 69.43           C  
ANISOU 3998  C   TYR B  52     8627   7010  10744   -509   -345    171       C  
ATOM   3999  O   TYR B  52      70.100  -4.387   2.012  1.00 69.41           O  
ANISOU 3999  O   TYR B  52     8644   6977  10753   -440   -269    251       O  
ATOM   4000  CB  TYR B  52      66.998  -4.594   1.436  1.00 65.18           C  
ANISOU 4000  CB  TYR B  52     7969   6368  10429   -709   -387    219       C  
ATOM   4001  CG  TYR B  52      65.839  -4.545   2.408  1.00 66.25           C  
ANISOU 4001  CG  TYR B  52     7983   6523  10665   -769   -345    338       C  
ATOM   4002  CD1 TYR B  52      65.988  -4.974   3.724  1.00 68.31           C  
ANISOU 4002  CD1 TYR B  52     8227   6764  10964   -722   -230    485       C  
ATOM   4003  CD2 TYR B  52      64.572  -4.151   1.993  1.00 66.76           C  
ANISOU 4003  CD2 TYR B  52     7950   6623  10792   -867   -415    313       C  
ATOM   4004  CE1 TYR B  52      64.928  -4.932   4.624  1.00 68.72           C  
ANISOU 4004  CE1 TYR B  52     8170   6838  11101   -765   -171    608       C  
ATOM   4005  CE2 TYR B  52      63.498  -4.125   2.879  1.00 67.91           C  
ANISOU 4005  CE2 TYR B  52     7974   6786  11044   -917   -361    432       C  
ATOM   4006  CZ  TYR B  52      63.682  -4.514   4.196  1.00 76.07           C  
ANISOU 4006  CZ  TYR B  52     8997   7801  12105   -865   -230    580       C  
ATOM   4007  OH  TYR B  52      62.634  -4.492   5.087  1.00 80.16           O  
ANISOU 4007  OH  TYR B  52     9398   8342  12719   -902   -155    711       O  
ATOM   4008  N   ILE B  53      69.801  -3.607  -0.109  1.00 66.82           N  
ANISOU 4008  N   ILE B  53     8364   6682  10342   -498   -400     51       N  
ATOM   4009  CA  ILE B  53      71.148  -3.962  -0.597  1.00 66.70           C  
ANISOU 4009  CA  ILE B  53     8447   6629  10268   -405   -363      4       C  
ATOM   4010  C   ILE B  53      72.191  -3.109   0.162  1.00 70.79           C  
ANISOU 4010  C   ILE B  53     8922   7268  10708   -303   -307     74       C  
ATOM   4011  O   ILE B  53      73.145  -3.670   0.701  1.00 71.43           O  
ANISOU 4011  O   ILE B  53     9028   7316  10799   -225   -246    122       O  
ATOM   4012  CB  ILE B  53      71.274  -3.801  -2.146  1.00 69.46           C  
ANISOU 4012  CB  ILE B  53     8878   6972  10540   -407   -425   -133       C  
ATOM   4013  CG1 ILE B  53      70.336  -4.797  -2.871  1.00 70.99           C  
ANISOU 4013  CG1 ILE B  53     9117   7044  10811   -509   -503   -227       C  
ATOM   4014  CG2 ILE B  53      72.730  -4.006  -2.608  1.00 69.33           C  
ANISOU 4014  CG2 ILE B  53     8952   6930  10461   -296   -363   -167       C  
ATOM   4015  CD1 ILE B  53      70.261  -4.668  -4.396  1.00 76.68           C  
ANISOU 4015  CD1 ILE B  53     9926   7778  11431   -510   -585   -374       C  
ATOM   4016  N   ILE B  54      71.966  -1.777   0.256  1.00 66.17           N  
ANISOU 4016  N   ILE B  54     8267   6817  10060   -305   -332     80       N  
ATOM   4017  CA  ILE B  54      72.849  -0.834   0.955  1.00 65.29           C  
ANISOU 4017  CA  ILE B  54     8102   6817   9887   -227   -296    123       C  
ATOM   4018  C   ILE B  54      72.811  -1.128   2.472  1.00 70.83           C  
ANISOU 4018  C   ILE B  54     8754   7543  10618   -200   -256    227       C  
ATOM   4019  O   ILE B  54      73.841  -0.993   3.140  1.00 70.82           O  
ANISOU 4019  O   ILE B  54     8736   7594  10580   -117   -225    261       O  
ATOM   4020  CB  ILE B  54      72.452   0.641   0.636  1.00 67.27           C  
ANISOU 4020  CB  ILE B  54     8296   7178  10087   -247   -333     96       C  
ATOM   4021  CG1 ILE B  54      72.530   0.943  -0.896  1.00 67.96           C  
ANISOU 4021  CG1 ILE B  54     8442   7254  10124   -254   -366     13       C  
ATOM   4022  CG2 ILE B  54      73.270   1.665   1.444  1.00 66.58           C  
ANISOU 4022  CG2 ILE B  54     8145   7192   9962   -184   -305    126       C  
ATOM   4023  CD1 ILE B  54      73.946   0.790  -1.626  1.00 73.20           C  
ANISOU 4023  CD1 ILE B  54     9173   7898  10743   -171   -318    -24       C  
ATOM   4024  N   PHE B  55      71.651  -1.585   2.993  1.00 67.67           N  
ANISOU 4024  N   PHE B  55     8327   7104  10282   -266   -253    280       N  
ATOM   4025  CA  PHE B  55      71.484  -1.931   4.405  1.00 67.64           C  
ANISOU 4025  CA  PHE B  55     8284   7121  10294   -234   -199    396       C  
ATOM   4026  C   PHE B  55      72.425  -3.069   4.835  1.00 71.94           C  
ANISOU 4026  C   PHE B  55     8885   7589  10861   -159   -147    453       C  
ATOM   4027  O   PHE B  55      73.140  -2.901   5.814  1.00 70.88           O  
ANISOU 4027  O   PHE B  55     8729   7535  10667    -68   -119    518       O  
ATOM   4028  CB  PHE B  55      70.027  -2.335   4.706  1.00 70.03           C  
ANISOU 4028  CB  PHE B  55     8544   7378  10688   -326   -190    451       C  
ATOM   4029  CG  PHE B  55      69.837  -2.988   6.058  1.00 72.22           C  
ANISOU 4029  CG  PHE B  55     8798   7649  10992   -289   -110    592       C  
ATOM   4030  CD1 PHE B  55      69.827  -2.229   7.221  1.00 74.88           C  
ANISOU 4030  CD1 PHE B  55     9080   8125  11247   -228    -78    659       C  
ATOM   4031  CD2 PHE B  55      69.635  -4.359   6.164  1.00 75.33           C  
ANISOU 4031  CD2 PHE B  55     9232   7895  11494   -309    -61    659       C  
ATOM   4032  CE1 PHE B  55      69.665  -2.833   8.472  1.00 76.45           C  
ANISOU 4032  CE1 PHE B  55     9268   8335  11444   -175      5    799       C  
ATOM   4033  CE2 PHE B  55      69.463  -4.962   7.415  1.00 78.92           C  
ANISOU 4033  CE2 PHE B  55     9669   8346  11971   -263     29    812       C  
ATOM   4034  CZ  PHE B  55      69.473  -4.194   8.560  1.00 76.57           C  
ANISOU 4034  CZ  PHE B  55     9321   8207  11567   -192     62    886       C  
ATOM   4035  N   VAL B  56      72.393  -4.223   4.136  1.00 70.05           N  
ANISOU 4035  N   VAL B  56     8717   7193  10707   -192   -138    428       N  
ATOM   4036  CA  VAL B  56      73.165  -5.411   4.509  1.00 71.00           C  
ANISOU 4036  CA  VAL B  56     8895   7210  10873   -120    -78    491       C  
ATOM   4037  C   VAL B  56      74.680  -5.162   4.206  1.00 74.11           C  
ANISOU 4037  C   VAL B  56     9314   7655  11191     -8    -76    452       C  
ATOM   4038  O   VAL B  56      75.505  -5.492   5.055  1.00 74.23           O  
ANISOU 4038  O   VAL B  56     9318   7701  11184     93    -37    539       O  
ATOM   4039  CB  VAL B  56      72.630  -6.710   3.818  1.00 76.43           C  
ANISOU 4039  CB  VAL B  56     9655   7692  11693   -194    -68    458       C  
ATOM   4040  CG1 VAL B  56      72.604  -6.597   2.295  1.00 76.52           C  
ANISOU 4040  CG1 VAL B  56     9724   7656  11692   -247   -135    295       C  
ATOM   4041  CG2 VAL B  56      73.400  -7.948   4.263  1.00 77.24           C  
ANISOU 4041  CG2 VAL B  56     9820   7670  11857   -108      8    537       C  
ATOM   4042  N   ILE B  57      75.032  -4.552   3.049  1.00 69.58           N  
ANISOU 4042  N   ILE B  57     8762   7101  10575    -21   -114    333       N  
ATOM   4043  CA  ILE B  57      76.433  -4.276   2.690  1.00 68.57           C  
ANISOU 4043  CA  ILE B  57     8641   7020  10394     77    -99    301       C  
ATOM   4044  C   ILE B  57      77.026  -3.287   3.716  1.00 70.33           C  
ANISOU 4044  C   ILE B  57     8767   7404  10551    138   -110    354       C  
ATOM   4045  O   ILE B  57      78.067  -3.575   4.304  1.00 69.98           O  
ANISOU 4045  O   ILE B  57     8704   7388  10498    238    -86    407       O  
ATOM   4046  CB  ILE B  57      76.568  -3.755   1.223  1.00 71.37           C  
ANISOU 4046  CB  ILE B  57     9035   7374  10710     51   -124    179       C  
ATOM   4047  CG1 ILE B  57      76.213  -4.892   0.223  1.00 72.88           C  
ANISOU 4047  CG1 ILE B  57     9337   7404  10949     13   -121    104       C  
ATOM   4048  CG2 ILE B  57      77.991  -3.218   0.941  1.00 71.86           C  
ANISOU 4048  CG2 ILE B  57     9074   7504  10727    149    -92    165       C  
ATOM   4049  CD1 ILE B  57      76.223  -4.513  -1.269  1.00 82.57           C  
ANISOU 4049  CD1 ILE B  57    10625   8637  12110     -2   -149    -18       C  
ATOM   4050  N   GLY B  58      76.330  -2.179   3.951  1.00 66.23           N  
ANISOU 4050  N   GLY B  58     8189   6983   9991     80   -150    337       N  
ATOM   4051  CA  GLY B  58      76.746  -1.148   4.894  1.00 65.55           C  
ANISOU 4051  CA  GLY B  58     8019   7044   9844    123   -172    357       C  
ATOM   4052  C   GLY B  58      76.778  -1.578   6.347  1.00 69.93           C  
ANISOU 4052  C   GLY B  58     8549   7649  10373    187   -157    461       C  
ATOM   4053  O   GLY B  58      77.611  -1.091   7.117  1.00 69.59           O  
ANISOU 4053  O   GLY B  58     8452   7716  10274    262   -179    473       O  
ATOM   4054  N   PHE B  59      75.868  -2.488   6.739  1.00 66.48           N  
ANISOU 4054  N   PHE B  59     8147   7135   9976    158   -120    540       N  
ATOM   4055  CA  PHE B  59      75.802  -2.962   8.116  1.00 66.63           C  
ANISOU 4055  CA  PHE B  59     8154   7202   9962    229    -87    664       C  
ATOM   4056  C   PHE B  59      76.972  -3.897   8.398  1.00 71.19           C  
ANISOU 4056  C   PHE B  59     8758   7745  10545    342    -62    727       C  
ATOM   4057  O   PHE B  59      77.595  -3.775   9.445  1.00 71.85           O  
ANISOU 4057  O   PHE B  59     8806   7942  10550    444    -74    789       O  
ATOM   4058  CB  PHE B  59      74.464  -3.662   8.400  1.00 68.92           C  
ANISOU 4058  CB  PHE B  59     8463   7406  10317    161    -35    748       C  
ATOM   4059  CG  PHE B  59      74.089  -3.697   9.861  1.00 71.25           C  
ANISOU 4059  CG  PHE B  59     8730   7794  10546    225      7    876       C  
ATOM   4060  CD1 PHE B  59      74.512  -4.738  10.682  1.00 75.48           C  
ANISOU 4060  CD1 PHE B  59     9298   8306  11075    327     62   1010       C  
ATOM   4061  CD2 PHE B  59      73.299  -2.694  10.416  1.00 72.71           C  
ANISOU 4061  CD2 PHE B  59     8864   8091  10672    196      1    871       C  
ATOM   4062  CE1 PHE B  59      74.172  -4.762  12.039  1.00 77.01           C  
ANISOU 4062  CE1 PHE B  59     9476   8601  11184    403    108   1139       C  
ATOM   4063  CE2 PHE B  59      72.964  -2.716  11.773  1.00 76.41           C  
ANISOU 4063  CE2 PHE B  59     9317   8657  11058    271     51    989       C  
ATOM   4064  CZ  PHE B  59      73.402  -3.752  12.575  1.00 75.65           C  
ANISOU 4064  CZ  PHE B  59     9258   8548  10938    375    104   1124       C  
ATOM   4065  N   LEU B  60      77.305  -4.787   7.440  1.00 67.49           N  
ANISOU 4065  N   LEU B  60     8353   7129  10164    335    -33    702       N  
ATOM   4066  CA  LEU B  60      78.391  -5.764   7.562  1.00 68.07           C  
ANISOU 4066  CA  LEU B  60     8456   7142  10264    448      4    761       C  
ATOM   4067  C   LEU B  60      79.792  -5.112   7.477  1.00 72.15           C  
ANISOU 4067  C   LEU B  60     8914   7772  10729    536    -37    712       C  
ATOM   4068  O   LEU B  60      80.701  -5.619   8.138  1.00 73.14           O  
ANISOU 4068  O   LEU B  60     9018   7933  10838    657    -28    793       O  
ATOM   4069  CB  LEU B  60      78.281  -6.853   6.477  1.00 68.63           C  
ANISOU 4069  CB  LEU B  60     8619   7009  10447    412     51    725       C  
ATOM   4070  CG  LEU B  60      77.465  -8.140   6.804  1.00 74.27           C  
ANISOU 4070  CG  LEU B  60     9396   7557  11265    385    117    823       C  
ATOM   4071  CD1 LEU B  60      76.025  -7.852   7.252  1.00 73.86           C  
ANISOU 4071  CD1 LEU B  60     9314   7522  11227    275    114    860       C  
ATOM   4072  CD2 LEU B  60      77.466  -9.094   5.622  1.00 77.09           C  
ANISOU 4072  CD2 LEU B  60     9848   7710  11734    346    146    743       C  
ATOM   4073  N   VAL B  61      79.992  -4.024   6.680  1.00 66.95           N  
ANISOU 4073  N   VAL B  61     8220   7166  10054    480    -77    590       N  
ATOM   4074  CA  VAL B  61      81.335  -3.407   6.592  1.00 65.90           C  
ANISOU 4074  CA  VAL B  61     8010   7127   9900    551   -106    549       C  
ATOM   4075  C   VAL B  61      81.614  -2.618   7.897  1.00 68.54           C  
ANISOU 4075  C   VAL B  61     8252   7636  10154    599   -173    577       C  
ATOM   4076  O   VAL B  61      82.764  -2.592   8.339  1.00 69.86           O  
ANISOU 4076  O   VAL B  61     8350   7881  10310    693   -202    593       O  
ATOM   4077  CB  VAL B  61      81.597  -2.518   5.340  1.00 68.47           C  
ANISOU 4077  CB  VAL B  61     8322   7452  10244    488   -111    431       C  
ATOM   4078  CG1 VAL B  61      81.692  -3.359   4.077  1.00 67.98           C  
ANISOU 4078  CG1 VAL B  61     8355   7240  10235    482    -49    394       C  
ATOM   4079  CG2 VAL B  61      80.561  -1.403   5.188  1.00 67.54           C  
ANISOU 4079  CG2 VAL B  61     8187   7385  10091    379   -151    372       C  
ATOM   4080  N   ASN B  62      80.573  -2.018   8.523  1.00 62.22           N  
ANISOU 4080  N   ASN B  62     7447   6897   9295    540   -198    579       N  
ATOM   4081  CA  ASN B  62      80.733  -1.302   9.792  1.00 61.24           C  
ANISOU 4081  CA  ASN B  62     7256   6936   9074    591   -261    590       C  
ATOM   4082  C   ASN B  62      80.881  -2.319  10.966  1.00 65.48           C  
ANISOU 4082  C   ASN B  62     7817   7506   9556    708   -244    730       C  
ATOM   4083  O   ASN B  62      81.551  -1.996  11.953  1.00 64.69           O  
ANISOU 4083  O   ASN B  62     7659   7551   9369    799   -307    745       O  
ATOM   4084  CB  ASN B  62      79.590  -0.331  10.037  1.00 57.89           C  
ANISOU 4084  CB  ASN B  62     6827   6563   8605    505   -278    543       C  
ATOM   4085  CG  ASN B  62      79.718   0.943   9.232  1.00 78.55           C  
ANISOU 4085  CG  ASN B  62     9395   9197  11252    426   -314    415       C  
ATOM   4086  OD1 ASN B  62      80.552   1.809   9.527  1.00 84.65           O  
ANISOU 4086  OD1 ASN B  62    10091  10064  12009    452   -374    349       O  
ATOM   4087  ND2 ASN B  62      78.857   1.133   8.250  1.00 60.17           N  
ANISOU 4087  ND2 ASN B  62     7106   6786   8971    328   -284    379       N  
ATOM   4088  N   ILE B  63      80.336  -3.566  10.818  1.00 62.49           N  
ANISOU 4088  N   ILE B  63     7521   6989   9235    710   -160    832       N  
ATOM   4089  CA  ILE B  63      80.523  -4.653  11.795  1.00 63.79           C  
ANISOU 4089  CA  ILE B  63     7716   7151   9369    829   -120    991       C  
ATOM   4090  C   ILE B  63      82.020  -5.021  11.809  1.00 69.03           C  
ANISOU 4090  C   ILE B  63     8338   7850  10040    955   -151   1010       C  
ATOM   4091  O   ILE B  63      82.567  -5.296  12.881  1.00 69.56           O  
ANISOU 4091  O   ILE B  63     8378   8031  10022   1084   -182   1104       O  
ATOM   4092  CB  ILE B  63      79.605  -5.901  11.518  1.00 67.28           C  
ANISOU 4092  CB  ILE B  63     8250   7399   9913    786    -16   1088       C  
ATOM   4093  CG1 ILE B  63      78.101  -5.599  11.776  1.00 67.52           C  
ANISOU 4093  CG1 ILE B  63     8296   7425   9934    684     17   1110       C  
ATOM   4094  CG2 ILE B  63      80.038  -7.137  12.330  1.00 68.94           C  
ANISOU 4094  CG2 ILE B  63     8497   7567  10129    925     42   1262       C  
ATOM   4095  CD1 ILE B  63      77.662  -5.154  13.268  1.00 75.41           C  
ANISOU 4095  CD1 ILE B  63     9268   8601  10783    760     14   1206       C  
ATOM   4096  N   VAL B  64      82.683  -4.978  10.625  1.00 65.78           N  
ANISOU 4096  N   VAL B  64     7915   7357   9722    927   -144    922       N  
ATOM   4097  CA  VAL B  64      84.115  -5.264  10.495  1.00 66.87           C  
ANISOU 4097  CA  VAL B  64     7994   7522   9890   1040   -163    932       C  
ATOM   4098  C   VAL B  64      84.896  -4.200  11.278  1.00 72.71           C  
ANISOU 4098  C   VAL B  64     8610   8473  10543   1089   -279    884       C  
ATOM   4099  O   VAL B  64      85.726  -4.569  12.107  1.00 73.92           O  
ANISOU 4099  O   VAL B  64     8715   8724  10648   1223   -321    966       O  
ATOM   4100  CB  VAL B  64      84.594  -5.357   9.013  1.00 69.78           C  
ANISOU 4100  CB  VAL B  64     8377   7767  10368    994   -116    839       C  
ATOM   4101  CG1 VAL B  64      86.119  -5.416   8.917  1.00 70.15           C  
ANISOU 4101  CG1 VAL B  64     8328   7874  10451   1106   -136    838       C  
ATOM   4102  CG2 VAL B  64      83.966  -6.552   8.304  1.00 69.73           C  
ANISOU 4102  CG2 VAL B  64     8498   7549  10447    970    -16    874       C  
ATOM   4103  N   VAL B  65      84.578  -2.891  11.056  1.00 68.07           N  
ANISOU 4103  N   VAL B  65     7973   7953   9936    981   -333    753       N  
ATOM   4104  CA  VAL B  65      85.219  -1.723  11.703  1.00 67.38           C  
ANISOU 4104  CA  VAL B  65     7769   8043   9790    994   -449    669       C  
ATOM   4105  C   VAL B  65      85.226  -1.893  13.237  1.00 72.79           C  
ANISOU 4105  C   VAL B  65     8445   8881  10332   1104   -518    747       C  
ATOM   4106  O   VAL B  65      86.266  -1.736  13.862  1.00 73.49           O  
ANISOU 4106  O   VAL B  65     8439   9102  10383   1198   -612    739       O  
ATOM   4107  CB  VAL B  65      84.504  -0.402  11.302  1.00 68.98           C  
ANISOU 4107  CB  VAL B  65     7960   8255   9996    853   -471    538       C  
ATOM   4108  CG1 VAL B  65      85.105   0.802  12.016  1.00 68.96           C  
ANISOU 4108  CG1 VAL B  65     7845   8413   9945    857   -591    437       C  
ATOM   4109  CG2 VAL B  65      84.543  -0.195   9.802  1.00 67.58           C  
ANISOU 4109  CG2 VAL B  65     7792   7949   9936    763   -408    472       C  
ATOM   4110  N   VAL B  66      84.073  -2.234  13.815  1.00 70.32           N  
ANISOU 4110  N   VAL B  66     8225   8552   9941   1097   -468    824       N  
ATOM   4111  CA  VAL B  66      83.860  -2.415  15.247  1.00 71.55           C  
ANISOU 4111  CA  VAL B  66     8399   8849   9938   1205   -504    914       C  
ATOM   4112  C   VAL B  66      84.604  -3.686  15.770  1.00 79.88           C  
ANISOU 4112  C   VAL B  66     9464   9913  10972   1371   -487   1079       C  
ATOM   4113  O   VAL B  66      85.348  -3.570  16.740  1.00 81.32           O  
ANISOU 4113  O   VAL B  66     9590  10269  11040   1496   -585   1103       O  
ATOM   4114  CB  VAL B  66      82.345  -2.498  15.519  1.00 74.17           C  
ANISOU 4114  CB  VAL B  66     8825   9128  10227   1139   -418    967       C  
ATOM   4115  CG1 VAL B  66      82.055  -3.112  16.866  1.00 75.76           C  
ANISOU 4115  CG1 VAL B  66     9076   9425  10284   1270   -393   1125       C  
ATOM   4116  CG2 VAL B  66      81.687  -1.132  15.378  1.00 72.36           C  
ANISOU 4116  CG2 VAL B  66     8572   8949   9975   1021   -458    816       C  
ATOM   4117  N   THR B  67      84.422  -4.869  15.139  1.00 78.02           N  
ANISOU 4117  N   THR B  67     9301   9492  10850   1378   -370   1187       N  
ATOM   4118  CA  THR B  67      85.065  -6.120  15.597  1.00 80.17           C  
ANISOU 4118  CA  THR B  67     9593   9742  11125   1540   -334   1358       C  
ATOM   4119  C   THR B  67      86.588  -6.108  15.328  1.00 86.64           C  
ANISOU 4119  C   THR B  67    10303  10618  11999   1628   -409   1319       C  
ATOM   4120  O   THR B  67      87.315  -6.909  15.920  1.00 87.80           O  
ANISOU 4120  O   THR B  67    10434  10802  12125   1789   -414   1452       O  
ATOM   4121  CB  THR B  67      84.426  -7.348  14.919  1.00 86.98           C  
ANISOU 4121  CB  THR B  67    10567  10361  12120   1508   -183   1463       C  
ATOM   4122  OG1 THR B  67      84.501  -7.197  13.501  1.00 87.53           O  
ANISOU 4122  OG1 THR B  67    10641  10281  12334   1389   -150   1336       O  
ATOM   4123  CG2 THR B  67      82.975  -7.566  15.343  1.00 83.98           C  
ANISOU 4123  CG2 THR B  67    10275   9926  11707   1441   -101   1542       C  
ATOM   4124  N   LEU B  68      87.070  -5.177  14.481  1.00 83.87           N  
ANISOU 4124  N   LEU B  68     9868  10279  11721   1530   -463   1151       N  
ATOM   4125  CA  LEU B  68      88.485  -5.058  14.119  1.00 84.80           C  
ANISOU 4125  CA  LEU B  68     9859  10444  11916   1595   -521   1109       C  
ATOM   4126  C   LEU B  68      89.321  -4.602  15.321  1.00 92.46           C  
ANISOU 4126  C   LEU B  68    10713  11651  12766   1714   -676   1114       C  
ATOM   4127  O   LEU B  68      90.513  -4.903  15.375  1.00 93.49           O  
ANISOU 4127  O   LEU B  68    10740  11839  12943   1827   -725   1151       O  
ATOM   4128  CB  LEU B  68      88.650  -4.075  12.958  1.00 83.17           C  
ANISOU 4128  CB  LEU B  68     9594  10191  11816   1449   -524    939       C  
ATOM   4129  CG  LEU B  68      89.868  -4.252  12.088  1.00 87.97           C  
ANISOU 4129  CG  LEU B  68    10108  10756  12563   1488   -502    917       C  
ATOM   4130  CD1 LEU B  68      89.732  -5.484  11.211  1.00 87.60           C  
ANISOU 4130  CD1 LEU B  68    10172  10498  12612   1511   -351    989       C  
ATOM   4131  CD2 LEU B  68      90.011  -3.094  11.183  1.00 90.80           C  
ANISOU 4131  CD2 LEU B  68    10389  11116  12995   1356   -520    762       C  
ATOM   4132  N   PHE B  69      88.695  -3.886  16.285  1.00 90.86           N  
ANISOU 4132  N   PHE B  69    10525  11589  12406   1695   -757   1072       N  
ATOM   4133  CA  PHE B  69      89.360  -3.462  17.521  1.00 93.20           C  
ANISOU 4133  CA  PHE B  69    10736  12125  12551   1812   -918   1061       C  
ATOM   4134  C   PHE B  69      89.547  -4.659  18.478  1.00102.37           C  
ANISOU 4134  C   PHE B  69    11950  13344  13603   2012   -901   1274       C  
ATOM   4135  O   PHE B  69      90.550  -4.716  19.190  1.00103.54           O  
ANISOU 4135  O   PHE B  69    11998  13657  13685   2154  -1024   1306       O  
ATOM   4136  CB  PHE B  69      88.576  -2.343  18.230  1.00 94.13           C  
ANISOU 4136  CB  PHE B  69    10879  12362  12523   1738   -991    944       C  
ATOM   4137  CG  PHE B  69      88.306  -1.069  17.468  1.00 93.59           C  
ANISOU 4137  CG  PHE B  69    10762  12248  12548   1555  -1014    743       C  
ATOM   4138  CD1 PHE B  69      89.230  -0.032  17.468  1.00 96.92           C  
ANISOU 4138  CD1 PHE B  69    11036  12780  13010   1523  -1159    583       C  
ATOM   4139  CD2 PHE B  69      87.069  -0.845  16.879  1.00 93.84           C  
ANISOU 4139  CD2 PHE B  69    10895  12138  12623   1418   -899    716       C  
ATOM   4140  CE1 PHE B  69      88.957   1.172  16.809  1.00 96.47           C  
ANISOU 4140  CE1 PHE B  69    10938  12668  13048   1359  -1169    412       C  
ATOM   4141  CE2 PHE B  69      86.794   0.361  16.223  1.00 95.35           C  
ANISOU 4141  CE2 PHE B  69    11045  12292  12892   1265   -918    547       C  
ATOM   4142  CZ  PHE B  69      87.742   1.359  16.188  1.00 93.88           C  
ANISOU 4142  CZ  PHE B  69    10719  12198  12753   1238  -1045    401       C  
ATOM   4143  N   CYS B  70      88.570  -5.610  18.488  1.00101.36           N  
ANISOU 4143  N   CYS B  70    11972  13076  13465   2021   -747   1426       N  
ATOM   4144  CA  CYS B  70      88.549  -6.812  19.338  1.00104.10           C  
ANISOU 4144  CA  CYS B  70    12393  13431  13731   2200   -687   1659       C  
ATOM   4145  C   CYS B  70      89.741  -7.729  19.022  1.00111.49           C  
ANISOU 4145  C   CYS B  70    13263  14316  14782   2333   -680   1756       C  
ATOM   4146  O   CYS B  70      90.509  -8.066  19.930  1.00113.20           O  
ANISOU 4146  O   CYS B  70    13420  14696  14894   2516   -773   1855       O  
ATOM   4147  CB  CYS B  70      87.236  -7.575  19.171  1.00103.87           C  
ANISOU 4147  CB  CYS B  70    12519  13207  13742   2140   -505   1780       C  
ATOM   4148  SG  CYS B  70      85.757  -6.629  19.602  1.00106.74           S  
ANISOU 4148  SG  CYS B  70    12955  13633  13969   2017   -488   1713       S  
ATOM   4149  N   CYS B  71      89.863  -8.169  17.746  1.00108.67           N  
ANISOU 4149  N   CYS B  71    12924  13735  14632   2251   -567   1731       N  
ATOM   4150  CA  CYS B  71      90.910  -9.098  17.311  1.00110.25           C  
ANISOU 4150  CA  CYS B  71    13078  13846  14966   2372   -524   1819       C  
ATOM   4151  C   CYS B  71      92.299  -8.388  17.272  1.00116.20           C  
ANISOU 4151  C   CYS B  71    13636  14776  15740   2427   -679   1718       C  
ATOM   4152  O   CYS B  71      93.318  -9.084  17.301  1.00117.97           O  
ANISOU 4152  O   CYS B  71    13788  15013  16022   2585   -684   1822       O  
ATOM   4153  CB  CYS B  71      90.576  -9.724  15.957  1.00109.15           C  
ANISOU 4153  CB  CYS B  71    13021  13429  15023   2264   -365   1786       C  
ATOM   4154  SG  CYS B  71      90.388  -8.537  14.600  1.00110.50           S  
ANISOU 4154  SG  CYS B  71    13138  13556  15291   2039   -382   1530       S  
ATOM   4155  N   GLN B  72      92.336  -7.031  17.232  1.00111.63           N  
ANISOU 4155  N   GLN B  72    12962  14320  15130   2299   -798   1523       N  
ATOM   4156  CA  GLN B  72      93.582  -6.248  17.224  1.00136.62           C  
ANISOU 4156  CA  GLN B  72    15925  17644  18339   2322   -950   1413       C  
ATOM   4157  C   GLN B  72      93.565  -5.197  18.337  1.00148.58           C  
ANISOU 4157  C   GLN B  72    17372  19406  19676   2321  -1143   1313       C  
ATOM   4158  O   GLN B  72      94.530  -4.453  18.504  1.00105.54           O  
ANISOU 4158  O   GLN B  72    11744  14103  14252   2329  -1297   1204       O  
ATOM   4159  CB  GLN B  72      93.815  -5.570  15.861  1.00136.35           C  
ANISOU 4159  CB  GLN B  72    15822  17493  18492   2159   -901   1254       C  
ATOM   4160  CG  GLN B  72      94.106  -6.532  14.710  1.00149.64           C  
ANISOU 4160  CG  GLN B  72    17549  18959  20348   2181   -730   1324       C  
ATOM   4161  CD  GLN B  72      94.337  -5.830  13.386  1.00165.42           C  
ANISOU 4161  CD  GLN B  72    19489  20862  22502   2036   -674   1177       C  
ATOM   4162  OE1 GLN B  72      95.026  -6.350  12.504  1.00160.65           O  
ANISOU 4162  OE1 GLN B  72    18867  20135  22037   2076   -566   1205       O  
ATOM   4163  NE2 GLN B  72      93.814  -4.616  13.225  1.00155.04           N  
ANISOU 4163  NE2 GLN B  72    18142  19600  21165   1876   -739   1022       N  
ATOM   4164  N   LYS B  77      95.132   5.686  20.579  1.00115.83           N  
ANISOU 4164  N   LYS B  77    12387  16045  15579   1452  -2363   -426       N  
ATOM   4165  CA  LYS B  77      94.891   6.716  19.569  1.00114.06           C  
ANISOU 4165  CA  LYS B  77    12118  15645  15574   1246  -2288   -560       C  
ATOM   4166  C   LYS B  77      93.529   7.395  19.782  1.00115.41           C  
ANISOU 4166  C   LYS B  77    12466  15762  15621   1167  -2232   -651       C  
ATOM   4167  O   LYS B  77      92.498   6.719  19.866  1.00113.49           O  
ANISOU 4167  O   LYS B  77    12412  15490  15219   1224  -2105   -524       O  
ATOM   4168  CB  LYS B  77      94.958   6.124  18.141  1.00115.15           C  
ANISOU 4168  CB  LYS B  77    12250  15580  15920   1188  -2072   -419       C  
ATOM   4169  CG  LYS B  77      96.319   5.526  17.725  1.00136.23           C  
ANISOU 4169  CG  LYS B  77    14729  18272  18762   1252  -2092   -335       C  
ATOM   4170  CD  LYS B  77      97.472   6.555  17.569  1.00150.03           C  
ANISOU 4170  CD  LYS B  77    16216  20051  20736   1151  -2230   -499       C  
ATOM   4171  CE  LYS B  77      97.293   7.562  16.443  1.00161.45           C  
ANISOU 4171  CE  LYS B  77    17626  21307  22411    954  -2111   -590       C  
ATOM   4172  NZ  LYS B  77      97.236   6.916  15.101  1.00168.55           N  
ANISOU 4172  NZ  LYS B  77    18568  22033  23441    939  -1873   -432       N  
ATOM   4173  N   VAL B  78      93.547   8.740  19.876  1.00111.54           N  
ANISOU 4173  N   VAL B  78    11906  15252  15224   1035  -2324   -872       N  
ATOM   4174  CA  VAL B  78      92.378   9.631  20.003  1.00109.73           C  
ANISOU 4174  CA  VAL B  78    11811  14956  14924    947  -2279   -991       C  
ATOM   4175  C   VAL B  78      91.518   9.508  18.729  1.00108.22           C  
ANISOU 4175  C   VAL B  78    11725  14545  14846    849  -2036   -877       C  
ATOM   4176  O   VAL B  78      90.290   9.498  18.813  1.00106.19           O  
ANISOU 4176  O   VAL B  78    11640  14250  14458    850  -1936   -844       O  
ATOM   4177  CB  VAL B  78      92.836  11.104  20.259  1.00115.20           C  
ANISOU 4177  CB  VAL B  78    12373  15648  15750    822  -2436  -1258       C  
ATOM   4178  CG1 VAL B  78      91.653  12.075  20.302  1.00114.00           C  
ANISOU 4178  CG1 VAL B  78    12358  15405  15552    734  -2373  -1381       C  
ATOM   4179  CG2 VAL B  78      93.663  11.214  21.541  1.00117.92           C  
ANISOU 4179  CG2 VAL B  78    12615  16222  15968    920  -2700  -1392       C  
ATOM   4180  N   SER B  79      92.183   9.377  17.556  1.00102.45           N  
ANISOU 4180  N   SER B  79    10888  13683  14354    776  -1942   -811       N  
ATOM   4181  CA  SER B  79      91.552   9.230  16.237  1.00 98.89           C  
ANISOU 4181  CA  SER B  79    10521  13036  14015    692  -1727   -707       C  
ATOM   4182  C   SER B  79      90.676   7.981  16.169  1.00 98.96           C  
ANISOU 4182  C   SER B  79    10707  13028  13864    787  -1597   -517       C  
ATOM   4183  O   SER B  79      89.626   8.022  15.533  1.00 96.91           O  
ANISOU 4183  O   SER B  79    10573  12644  13604    724  -1455   -472       O  
ATOM   4184  CB  SER B  79      92.609   9.170  15.139  1.00102.29           C  
ANISOU 4184  CB  SER B  79    10799  13367  14699    634  -1662   -663       C  
ATOM   4185  OG  SER B  79      93.500   8.082  15.322  1.00111.90           O  
ANISOU 4185  OG  SER B  79    11941  14669  15909    758  -1692   -547       O  
ATOM   4186  N   SER B  80      91.096   6.884  16.846  1.00 94.54           N  
ANISOU 4186  N   SER B  80    10152  12592  13177    939  -1651   -407       N  
ATOM   4187  CA  SER B  80      90.375   5.607  16.901  1.00 92.51           C  
ANISOU 4187  CA  SER B  80    10049  12315  12784   1039  -1534   -217       C  
ATOM   4188  C   SER B  80      89.021   5.747  17.615  1.00 93.36           C  
ANISOU 4188  C   SER B  80    10322  12457  12693   1052  -1507   -221       C  
ATOM   4189  O   SER B  80      88.093   4.995  17.303  1.00 92.60           O  
ANISOU 4189  O   SER B  80    10361  12275  12547   1065  -1366    -86       O  
ATOM   4190  CB  SER B  80      91.213   4.547  17.609  1.00 97.27           C  
ANISOU 4190  CB  SER B  80    10604  13051  13305   1209  -1611   -102       C  
ATOM   4191  OG  SER B  80      92.422   4.291  16.915  1.00107.38           O  
ANISOU 4191  OG  SER B  80    11730  14294  14774   1212  -1614    -76       O  
ATOM   4192  N   ILE B  81      88.905   6.708  18.563  1.00 87.53           N  
ANISOU 4192  N   ILE B  81     9570  11838  11851   1047  -1639   -379       N  
ATOM   4193  CA  ILE B  81      87.669   6.945  19.317  1.00 85.63           C  
ANISOU 4193  CA  ILE B  81     9476  11645  11416   1072  -1611   -395       C  
ATOM   4194  C   ILE B  81      86.630   7.548  18.371  1.00 84.24           C  
ANISOU 4194  C   ILE B  81     9367  11292  11350    927  -1470   -423       C  
ATOM   4195  O   ILE B  81      85.477   7.124  18.402  1.00 82.88           O  
ANISOU 4195  O   ILE B  81     9326  11081  11084    940  -1353   -327       O  
ATOM   4196  CB  ILE B  81      87.898   7.842  20.573  1.00 90.86           C  
ANISOU 4196  CB  ILE B  81    10108  12488  11928   1120  -1797   -577       C  
ATOM   4197  CG1 ILE B  81      89.144   7.392  21.414  1.00 94.04           C  
ANISOU 4197  CG1 ILE B  81    10407  13081  12244   1257  -1976   -574       C  
ATOM   4198  CG2 ILE B  81      86.631   7.967  21.435  1.00 91.37           C  
ANISOU 4198  CG2 ILE B  81    10333  12619  11765   1177  -1750   -577       C  
ATOM   4199  CD1 ILE B  81      89.172   5.898  21.912  1.00102.78           C  
ANISOU 4199  CD1 ILE B  81    11589  14273  13188   1436  -1927   -334       C  
ATOM   4200  N   TYR B  82      87.047   8.489  17.491  1.00 78.03           N  
ANISOU 4200  N   TYR B  82     8481  10395  10770    794  -1474   -538       N  
ATOM   4201  CA  TYR B  82      86.145   9.103  16.510  1.00 74.86           C  
ANISOU 4201  CA  TYR B  82     8134   9829  10482    666  -1346   -557       C  
ATOM   4202  C   TYR B  82      85.688   8.057  15.483  1.00 75.07           C  
ANISOU 4202  C   TYR B  82     8234   9731  10558    656  -1185   -379       C  
ATOM   4203  O   TYR B  82      84.533   8.100  15.074  1.00 73.51           O  
ANISOU 4203  O   TYR B  82     8134   9445  10349    603  -1078   -342       O  
ATOM   4204  CB  TYR B  82      86.789  10.306  15.798  1.00 75.89           C  
ANISOU 4204  CB  TYR B  82     8138   9870  10827    540  -1379   -699       C  
ATOM   4205  CG  TYR B  82      87.315  11.373  16.734  1.00 79.69           C  
ANISOU 4205  CG  TYR B  82     8536  10447  11297    529  -1546   -901       C  
ATOM   4206  CD1 TYR B  82      86.446  12.210  17.427  1.00 82.24           C  
ANISOU 4206  CD1 TYR B  82     8940  10792  11515    518  -1569  -1020       C  
ATOM   4207  CD2 TYR B  82      88.676  11.630  16.832  1.00 82.08           C  
ANISOU 4207  CD2 TYR B  82     8669  10799  11718    519  -1677   -987       C  
ATOM   4208  CE1 TYR B  82      86.924  13.206  18.280  1.00 84.74           C  
ANISOU 4208  CE1 TYR B  82     9191  11185  11821    508  -1728  -1230       C  
ATOM   4209  CE2 TYR B  82      89.165  12.640  17.660  1.00 84.78           C  
ANISOU 4209  CE2 TYR B  82     8928  11219  12067    495  -1847  -1196       C  
ATOM   4210  CZ  TYR B  82      88.284  13.422  18.387  1.00 91.10           C  
ANISOU 4210  CZ  TYR B  82     9829  12040  12744    490  -1874  -1324       C  
ATOM   4211  OH  TYR B  82      88.757  14.413  19.206  1.00 93.78           O  
ANISOU 4211  OH  TYR B  82    10099  12447  13088    468  -2046  -1552       O  
ATOM   4212  N   ILE B  83      86.577   7.090  15.111  1.00 70.74           N  
ANISOU 4212  N   ILE B  83     7639   9178  10062    713  -1174   -274       N  
ATOM   4213  CA  ILE B  83      86.274   5.974  14.186  1.00 68.64           C  
ANISOU 4213  CA  ILE B  83     7448   8792   9840    719  -1033   -118       C  
ATOM   4214  C   ILE B  83      85.107   5.147  14.740  1.00 69.84           C  
ANISOU 4214  C   ILE B  83     7744   8955   9837    777   -966     -4       C  
ATOM   4215  O   ILE B  83      84.154   4.875  14.010  1.00 67.74           O  
ANISOU 4215  O   ILE B  83     7566   8570   9604    715   -851     54       O  
ATOM   4216  CB  ILE B  83      87.520   5.053  13.928  1.00 72.69           C  
ANISOU 4216  CB  ILE B  83     7881   9315  10423    801  -1043    -34       C  
ATOM   4217  CG1 ILE B  83      88.769   5.832  13.426  1.00 73.57           C  
ANISOU 4217  CG1 ILE B  83     7823   9422  10708    748  -1101   -132       C  
ATOM   4218  CG2 ILE B  83      87.184   3.873  12.991  1.00 72.23           C  
ANISOU 4218  CG2 ILE B  83     7918   9122  10405    815   -897    110       C  
ATOM   4219  CD1 ILE B  83      88.668   6.509  12.097  1.00 77.66           C  
ANISOU 4219  CD1 ILE B  83     8325   9792  11390    622  -1000   -171       C  
ATOM   4220  N   PHE B  84      85.195   4.749  16.031  1.00 66.87           N  
ANISOU 4220  N   PHE B  84     7386   8727   9294    897  -1041     32       N  
ATOM   4221  CA  PHE B  84      84.180   3.943  16.703  1.00 66.50           C  
ANISOU 4221  CA  PHE B  84     7463   8705   9097    969   -970    161       C  
ATOM   4222  C   PHE B  84      82.835   4.695  16.742  1.00 69.34           C  
ANISOU 4222  C   PHE B  84     7896   9030   9419    887   -910    108       C  
ATOM   4223  O   PHE B  84      81.812   4.123  16.359  1.00 68.43           O  
ANISOU 4223  O   PHE B  84     7865   8819   9315    856   -790    212       O  
ATOM   4224  CB  PHE B  84      84.634   3.562  18.122  1.00 70.01           C  
ANISOU 4224  CB  PHE B  84     7907   9342   9354   1128  -1070    200       C  
ATOM   4225  CG  PHE B  84      83.645   2.696  18.866  1.00 72.23           C  
ANISOU 4225  CG  PHE B  84     8311   9651   9481   1218   -979    363       C  
ATOM   4226  CD1 PHE B  84      83.614   1.321  18.670  1.00 75.57           C  
ANISOU 4226  CD1 PHE B  84     8784   9998   9931   1283   -883    555       C  
ATOM   4227  CD2 PHE B  84      82.757   3.253  19.782  1.00 74.83           C  
ANISOU 4227  CD2 PHE B  84     8705  10078   9647   1245   -978    329       C  
ATOM   4228  CE1 PHE B  84      82.687   0.525  19.343  1.00 77.30           C  
ANISOU 4228  CE1 PHE B  84     9110  10225  10036   1358   -783    719       C  
ATOM   4229  CE2 PHE B  84      81.847   2.453  20.472  1.00 78.39           C  
ANISOU 4229  CE2 PHE B  84     9262  10556   9969   1331   -873    498       C  
ATOM   4230  CZ  PHE B  84      81.815   1.094  20.247  1.00 76.84           C  
ANISOU 4230  CZ  PHE B  84     9106  10272   9817   1382   -775    697       C  
ATOM   4231  N   ASN B  85      82.847   5.980  17.163  1.00 64.66           N  
ANISOU 4231  N   ASN B  85     7262   8506   8800    849   -995    -58       N  
ATOM   4232  CA  ASN B  85      81.652   6.814  17.228  1.00 62.52           C  
ANISOU 4232  CA  ASN B  85     7047   8208   8498    785   -943   -122       C  
ATOM   4233  C   ASN B  85      81.064   7.030  15.839  1.00 63.28           C  
ANISOU 4233  C   ASN B  85     7153   8128   8765    652   -842   -114       C  
ATOM   4234  O   ASN B  85      79.845   7.092  15.712  1.00 61.34           O  
ANISOU 4234  O   ASN B  85     6973   7834   8501    614   -755    -77       O  
ATOM   4235  CB  ASN B  85      81.957   8.139  17.882  1.00 61.81           C  
ANISOU 4235  CB  ASN B  85     6908   8209   8369    777  -1061   -317       C  
ATOM   4236  CG  ASN B  85      82.133   8.039  19.375  1.00 81.28           C  
ANISOU 4236  CG  ASN B  85     9397  10870  10615    917  -1160   -342       C  
ATOM   4237  OD1 ASN B  85      81.161   7.913  20.126  1.00 73.10           O  
ANISOU 4237  OD1 ASN B  85     8457   9904   9414    992  -1102   -279       O  
ATOM   4238  ND2 ASN B  85      83.362   8.183  19.846  1.00 73.19           N  
ANISOU 4238  ND2 ASN B  85     8280   9945   9584    956  -1315   -446       N  
ATOM   4239  N   LEU B  86      81.917   7.104  14.797  1.00 59.51           N  
ANISOU 4239  N   LEU B  86     6604   7562   8445    589   -850   -141       N  
ATOM   4240  CA  LEU B  86      81.473   7.236  13.405  1.00 57.26           C  
ANISOU 4240  CA  LEU B  86     6333   7122   8302    480   -757   -125       C  
ATOM   4241  C   LEU B  86      80.801   5.926  12.963  1.00 62.39           C  
ANISOU 4241  C   LEU B  86     7069   7694   8942    491   -656     28       C  
ATOM   4242  O   LEU B  86      79.726   5.970  12.367  1.00 61.19           O  
ANISOU 4242  O   LEU B  86     6969   7458   8821    423   -581     53       O  
ATOM   4243  CB  LEU B  86      82.653   7.608  12.471  1.00 56.43           C  
ANISOU 4243  CB  LEU B  86     6131   6957   8352    431   -780   -182       C  
ATOM   4244  CG  LEU B  86      82.344   7.784  10.970  1.00 59.20           C  
ANISOU 4244  CG  LEU B  86     6500   7161   8832    337   -684   -160       C  
ATOM   4245  CD1 LEU B  86      81.318   8.873  10.733  1.00 58.88           C  
ANISOU 4245  CD1 LEU B  86     6489   7075   8808    259   -653   -219       C  
ATOM   4246  CD2 LEU B  86      83.594   8.091  10.186  1.00 59.32           C  
ANISOU 4246  CD2 LEU B  86     6415   7136   8987    311   -692   -198       C  
ATOM   4247  N   ALA B  87      81.414   4.766  13.309  1.00 60.42           N  
ANISOU 4247  N   ALA B  87     6829   7472   8655    581   -659    127       N  
ATOM   4248  CA  ALA B  87      80.900   3.433  12.983  1.00 60.27           C  
ANISOU 4248  CA  ALA B  87     6890   7364   8645    598   -565    269       C  
ATOM   4249  C   ALA B  87      79.560   3.185  13.666  1.00 65.57           C  
ANISOU 4249  C   ALA B  87     7636   8052   9224    605   -509    343       C  
ATOM   4250  O   ALA B  87      78.664   2.643  13.027  1.00 65.49           O  
ANISOU 4250  O   ALA B  87     7681   7930   9272    545   -425    408       O  
ATOM   4251  CB  ALA B  87      81.900   2.367  13.392  1.00 62.15           C  
ANISOU 4251  CB  ALA B  87     7117   7634   8864    711   -583    360       C  
ATOM   4252  N   VAL B  88      79.408   3.618  14.947  1.00 62.89           N  
ANISOU 4252  N   VAL B  88     7294   7856   8744    679   -555    327       N  
ATOM   4253  CA  VAL B  88      78.160   3.503  15.720  1.00 62.96           C  
ANISOU 4253  CA  VAL B  88     7365   7903   8653    702   -488    401       C  
ATOM   4254  C   VAL B  88      77.071   4.370  15.042  1.00 66.19           C  
ANISOU 4254  C   VAL B  88     7775   8243   9131    586   -445    330       C  
ATOM   4255  O   VAL B  88      75.993   3.852  14.750  1.00 66.72           O  
ANISOU 4255  O   VAL B  88     7882   8236   9234    542   -355    419       O  
ATOM   4256  CB  VAL B  88      78.359   3.886  17.216  1.00 68.31           C  
ANISOU 4256  CB  VAL B  88     8047   8767   9139    827   -551    383       C  
ATOM   4257  CG1 VAL B  88      77.033   4.130  17.932  1.00 68.52           C  
ANISOU 4257  CG1 VAL B  88     8130   8842   9064    847   -469    433       C  
ATOM   4258  CG2 VAL B  88      79.179   2.833  17.947  1.00 69.48           C  
ANISOU 4258  CG2 VAL B  88     8205   8989   9205    960   -578    499       C  
ATOM   4259  N   ALA B  89      77.374   5.661  14.756  1.00 60.80           N  
ANISOU 4259  N   ALA B  89     7042   7575   8486    534   -510    176       N  
ATOM   4260  CA  ALA B  89      76.457   6.594  14.092  1.00 59.20           C  
ANISOU 4260  CA  ALA B  89     6832   7306   8353    438   -476    110       C  
ATOM   4261  C   ALA B  89      76.034   6.067  12.715  1.00 62.16           C  
ANISOU 4261  C   ALA B  89     7223   7535   8861    344   -415    166       C  
ATOM   4262  O   ALA B  89      74.853   6.165  12.381  1.00 62.03           O  
ANISOU 4262  O   ALA B  89     7223   7471   8876    288   -359    193       O  
ATOM   4263  CB  ALA B  89      77.103   7.962  13.949  1.00 59.67           C  
ANISOU 4263  CB  ALA B  89     6833   7385   8454    406   -553    -53       C  
ATOM   4264  N   ASP B  90      76.984   5.484  11.933  1.00 57.57           N  
ANISOU 4264  N   ASP B  90     6633   6889   8351    336   -429    180       N  
ATOM   4265  CA  ASP B  90      76.706   4.907  10.611  1.00 56.44           C  
ANISOU 4265  CA  ASP B  90     6518   6614   8312    262   -380    217       C  
ATOM   4266  C   ASP B  90      75.859   3.658  10.724  1.00 62.40           C  
ANISOU 4266  C   ASP B  90     7332   7313   9064    263   -314    339       C  
ATOM   4267  O   ASP B  90      74.894   3.506   9.984  1.00 61.83           O  
ANISOU 4267  O   ASP B  90     7280   7162   9050    186   -276    356       O  
ATOM   4268  CB  ASP B  90      78.005   4.569   9.854  1.00 57.35           C  
ANISOU 4268  CB  ASP B  90     6615   6684   8491    275   -399    198       C  
ATOM   4269  CG  ASP B  90      78.797   5.757   9.359  1.00 61.67           C  
ANISOU 4269  CG  ASP B  90     7094   7245   9094    246   -442     89       C  
ATOM   4270  OD1 ASP B  90      78.169   6.748   8.918  1.00 59.09           O  
ANISOU 4270  OD1 ASP B  90     6757   6894   8801    180   -434     33       O  
ATOM   4271  OD2 ASP B  90      80.042   5.642   9.273  1.00 68.63           O  
ANISOU 4271  OD2 ASP B  90     7926   8145  10006    287   -473     72       O  
ATOM   4272  N   LEU B  91      76.222   2.767  11.647  1.00 61.29           N  
ANISOU 4272  N   LEU B  91     7212   7214   8863    351   -303    428       N  
ATOM   4273  CA  LEU B  91      75.563   1.486  11.858  1.00 62.70           C  
ANISOU 4273  CA  LEU B  91     7443   7325   9057    362   -230    563       C  
ATOM   4274  C   LEU B  91      74.089   1.691  12.333  1.00 68.86           C  
ANISOU 4274  C   LEU B  91     8225   8119   9818    324   -173    612       C  
ATOM   4275  O   LEU B  91      73.209   0.980  11.853  1.00 69.74           O  
ANISOU 4275  O   LEU B  91     8357   8124  10017    257   -117    678       O  
ATOM   4276  CB  LEU B  91      76.389   0.705  12.885  1.00 63.94           C  
ANISOU 4276  CB  LEU B  91     7613   7548   9133    491   -233    654       C  
ATOM   4277  CG  LEU B  91      76.263  -0.796  12.934  1.00 69.17           C  
ANISOU 4277  CG  LEU B  91     8330   8110   9840    523   -158    802       C  
ATOM   4278  CD1 LEU B  91      76.440  -1.408  11.563  1.00 68.72           C  
ANISOU 4278  CD1 LEU B  91     8301   7887   9921    451   -140    776       C  
ATOM   4279  CD2 LEU B  91      77.311  -1.367  13.867  1.00 71.30           C  
ANISOU 4279  CD2 LEU B  91     8603   8465  10023    669   -178    883       C  
ATOM   4280  N   LEU B  92      73.820   2.700  13.195  1.00 65.28           N  
ANISOU 4280  N   LEU B  92     7746   7792   9266    362   -190    569       N  
ATOM   4281  CA  LEU B  92      72.465   3.028  13.652  1.00 65.40           C  
ANISOU 4281  CA  LEU B  92     7753   7834   9263    339   -128    609       C  
ATOM   4282  C   LEU B  92      71.672   3.773  12.560  1.00 69.25           C  
ANISOU 4282  C   LEU B  92     8208   8251   9853    224   -135    532       C  
ATOM   4283  O   LEU B  92      70.444   3.665  12.533  1.00 69.17           O  
ANISOU 4283  O   LEU B  92     8181   8209   9890    175    -75    591       O  
ATOM   4284  CB  LEU B  92      72.488   3.872  14.940  1.00 66.04           C  
ANISOU 4284  CB  LEU B  92     7828   8075   9190    436   -140    573       C  
ATOM   4285  CG  LEU B  92      73.033   3.205  16.211  1.00 71.57           C  
ANISOU 4285  CG  LEU B  92     8564   8882   9747    572   -130    666       C  
ATOM   4286  CD1 LEU B  92      73.099   4.198  17.347  1.00 72.26           C  
ANISOU 4286  CD1 LEU B  92     8652   9135   9668    664   -170    583       C  
ATOM   4287  CD2 LEU B  92      72.193   1.992  16.620  1.00 73.65           C  
ANISOU 4287  CD2 LEU B  92     8858   9103  10023    591     -8    858       C  
ATOM   4288  N   LEU B  93      72.363   4.535  11.679  1.00 65.14           N  
ANISOU 4288  N   LEU B  93     7670   7711   9370    187   -203    412       N  
ATOM   4289  CA  LEU B  93      71.736   5.258  10.561  1.00 64.12           C  
ANISOU 4289  CA  LEU B  93     7516   7520   9327     95   -214    348       C  
ATOM   4290  C   LEU B  93      71.220   4.268   9.514  1.00 68.29           C  
ANISOU 4290  C   LEU B  93     8066   7927   9954     16   -196    399       C  
ATOM   4291  O   LEU B  93      70.081   4.388   9.065  1.00 68.05           O  
ANISOU 4291  O   LEU B  93     8012   7862   9982    -52   -181    410       O  
ATOM   4292  CB  LEU B  93      72.737   6.246   9.920  1.00 63.54           C  
ANISOU 4292  CB  LEU B  93     7423   7448   9270     87   -276    229       C  
ATOM   4293  CG  LEU B  93      72.239   7.097   8.739  1.00 67.35           C  
ANISOU 4293  CG  LEU B  93     7886   7874   9830     11   -285    173       C  
ATOM   4294  CD1 LEU B  93      71.167   8.081   9.178  1.00 67.33           C  
ANISOU 4294  CD1 LEU B  93     7851   7913   9818      6   -262    161       C  
ATOM   4295  CD2 LEU B  93      73.381   7.867   8.116  1.00 69.57           C  
ANISOU 4295  CD2 LEU B  93     8148   8144  10140     10   -325     85       C  
ATOM   4296  N   LEU B  94      72.066   3.278   9.145  1.00 64.80           N  
ANISOU 4296  N   LEU B  94     7665   7422   9534     29   -201    423       N  
ATOM   4297  CA  LEU B  94      71.761   2.218   8.179  1.00 64.39           C  
ANISOU 4297  CA  LEU B  94     7650   7243   9572    -36   -189    451       C  
ATOM   4298  C   LEU B  94      70.710   1.259   8.733  1.00 71.97           C  
ANISOU 4298  C   LEU B  94     8610   8158  10576    -62   -129    563       C  
ATOM   4299  O   LEU B  94      70.001   0.626   7.954  1.00 73.00           O  
ANISOU 4299  O   LEU B  94     8748   8186  10803   -146   -128    570       O  
ATOM   4300  CB  LEU B  94      73.039   1.442   7.812  1.00 63.74           C  
ANISOU 4300  CB  LEU B  94     7615   7105   9497      7   -198    444       C  
ATOM   4301  CG  LEU B  94      74.106   2.203   7.023  1.00 66.20           C  
ANISOU 4301  CG  LEU B  94     7920   7435   9800     20   -241    347       C  
ATOM   4302  CD1 LEU B  94      75.430   1.549   7.152  1.00 66.10           C  
ANISOU 4302  CD1 LEU B  94     7927   7407   9781     95   -237    362       C  
ATOM   4303  CD2 LEU B  94      73.710   2.400   5.565  1.00 67.19           C  
ANISOU 4303  CD2 LEU B  94     8066   7488   9975    -57   -257    284       C  
ATOM   4304  N   ALA B  95      70.580   1.184  10.077  1.00 69.56           N  
ANISOU 4304  N   ALA B  95     8293   7935  10203     11    -79    649       N  
ATOM   4305  CA  ALA B  95      69.604   0.336  10.771  1.00 70.11           C  
ANISOU 4305  CA  ALA B  95     8353   7972  10314      1      4    782       C  
ATOM   4306  C   ALA B  95      68.145   0.837  10.567  1.00 73.18           C  
ANISOU 4306  C   ALA B  95     8675   8367  10762    -78     26    787       C  
ATOM   4307  O   ALA B  95      67.217   0.091  10.871  1.00 74.35           O  
ANISOU 4307  O   ALA B  95     8796   8471  10984   -112     98    896       O  
ATOM   4308  CB  ALA B  95      69.923   0.286  12.257  1.00 71.52           C  
ANISOU 4308  CB  ALA B  95     8543   8260  10369    125     55    874       C  
ATOM   4309  N   THR B  96      67.943   2.075  10.046  1.00 66.77           N  
ANISOU 4309  N   THR B  96     7829   7605   9934   -106    -30    680       N  
ATOM   4310  CA  THR B  96      66.600   2.619   9.812  1.00 65.98           C  
ANISOU 4310  CA  THR B  96     7656   7518   9894   -169    -16    684       C  
ATOM   4311  C   THR B  96      66.105   2.308   8.377  1.00 69.89           C  
ANISOU 4311  C   THR B  96     8138   7907  10510   -284    -78    636       C  
ATOM   4312  O   THR B  96      64.909   2.441   8.120  1.00 69.36           O  
ANISOU 4312  O   THR B  96     7999   7834  10522   -348    -75    658       O  
ATOM   4313  CB  THR B  96      66.551   4.135  10.060  1.00 68.06           C  
ANISOU 4313  CB  THR B  96     7891   7890  10078   -122    -35    606       C  
ATOM   4314  OG1 THR B  96      67.405   4.802   9.134  1.00 64.05           O  
ANISOU 4314  OG1 THR B  96     7411   7367   9560   -134   -115    491       O  
ATOM   4315  CG2 THR B  96      66.898   4.516  11.495  1.00 67.41           C  
ANISOU 4315  CG2 THR B  96     7825   7924   9864     -7     14    630       C  
ATOM   4316  N   LEU B  97      67.013   1.876   7.458  1.00 66.20           N  
ANISOU 4316  N   LEU B  97     7737   7365  10052   -302   -135    570       N  
ATOM   4317  CA  LEU B  97      66.688   1.546   6.062  1.00 65.52           C  
ANISOU 4317  CA  LEU B  97     7661   7186  10046   -394   -203    506       C  
ATOM   4318  C   LEU B  97      65.532   0.514   5.958  1.00 68.98           C  
ANISOU 4318  C   LEU B  97     8059   7530  10620   -489   -189    567       C  
ATOM   4319  O   LEU B  97      64.650   0.758   5.129  1.00 68.79           O  
ANISOU 4319  O   LEU B  97     7987   7490  10659   -568   -251    523       O  
ATOM   4320  CB  LEU B  97      67.906   1.022   5.293  1.00 65.35           C  
ANISOU 4320  CB  LEU B  97     7732   7098  10001   -375   -238    440       C  
ATOM   4321  CG  LEU B  97      68.890   2.093   4.813  1.00 69.41           C  
ANISOU 4321  CG  LEU B  97     8269   7678  10427   -320   -273    357       C  
ATOM   4322  CD1 LEU B  97      70.172   1.479   4.311  1.00 70.00           C  
ANISOU 4322  CD1 LEU B  97     8421   7695  10482   -281   -277    320       C  
ATOM   4323  CD2 LEU B  97      68.279   2.948   3.721  1.00 70.73           C  
ANISOU 4323  CD2 LEU B  97     8413   7862  10599   -368   -331    291       C  
ATOM   4324  N   PRO B  98      65.429  -0.571   6.790  1.00 65.12           N  
ANISOU 4324  N   PRO B  98     7574   6978  10188   -486   -110    674       N  
ATOM   4325  CA  PRO B  98      64.271  -1.482   6.650  1.00 65.78           C  
ANISOU 4325  CA  PRO B  98     7602   6956  10436   -593    -94    731       C  
ATOM   4326  C   PRO B  98      62.924  -0.766   6.854  1.00 69.65           C  
ANISOU 4326  C   PRO B  98     7966   7517  10980   -641    -88    766       C  
ATOM   4327  O   PRO B  98      61.934  -1.190   6.261  1.00 69.73           O  
ANISOU 4327  O   PRO B  98     7909   7458  11126   -752   -135    750       O  
ATOM   4328  CB  PRO B  98      64.499  -2.523   7.751  1.00 68.21           C  
ANISOU 4328  CB  PRO B  98     7932   7209  10775   -550     19    870       C  
ATOM   4329  CG  PRO B  98      65.952  -2.502   7.995  1.00 71.86           C  
ANISOU 4329  CG  PRO B  98     8492   7708  11106   -436     21    848       C  
ATOM   4330  CD  PRO B  98      66.359  -1.067   7.828  1.00 66.35           C  
ANISOU 4330  CD  PRO B  98     7784   7151  10275   -385    -36    754       C  
ATOM   4331  N   LEU B  99      62.895   0.336   7.648  1.00 65.42           N  
ANISOU 4331  N   LEU B  99     7395   7121  10340   -555    -37    801       N  
ATOM   4332  CA  LEU B  99      61.685   1.125   7.893  1.00 65.34           C  
ANISOU 4332  CA  LEU B  99     7267   7189  10369   -573    -14    836       C  
ATOM   4333  C   LEU B  99      61.266   1.925   6.669  1.00 67.94           C  
ANISOU 4333  C   LEU B  99     7560   7539  10716   -625   -131    726       C  
ATOM   4334  O   LEU B  99      60.088   1.907   6.323  1.00 68.77           O  
ANISOU 4334  O   LEU B  99     7558   7633  10938   -704   -158    746       O  
ATOM   4335  CB  LEU B  99      61.866   2.100   9.069  1.00 65.28           C  
ANISOU 4335  CB  LEU B  99     7256   7319  10227   -450     69    877       C  
ATOM   4336  CG  LEU B  99      62.059   1.528  10.459  1.00 71.91           C  
ANISOU 4336  CG  LEU B  99     8121   8186  11015   -370    195   1004       C  
ATOM   4337  CD1 LEU B  99      62.402   2.622  11.433  1.00 71.95           C  
ANISOU 4337  CD1 LEU B  99     8145   8338  10854   -241    241    992       C  
ATOM   4338  CD2 LEU B  99      60.819   0.786  10.936  1.00 77.86           C  
ANISOU 4338  CD2 LEU B  99     8777   8894  11913   -427    296   1149       C  
ATOM   4339  N   TRP B 100      62.209   2.652   6.032  1.00 62.79           N  
ANISOU 4339  N   TRP B 100     6987   6921   9951   -577   -198    621       N  
ATOM   4340  CA  TRP B 100      61.898   3.521   4.893  1.00 62.35           C  
ANISOU 4340  CA  TRP B 100     6908   6894   9888   -603   -297    535       C  
ATOM   4341  C   TRP B 100      61.548   2.685   3.668  1.00 67.95           C  
ANISOU 4341  C   TRP B 100     7626   7512  10682   -705   -398    478       C  
ATOM   4342  O   TRP B 100      60.697   3.106   2.888  1.00 69.29           O  
ANISOU 4342  O   TRP B 100     7730   7707  10891   -750   -479    445       O  
ATOM   4343  CB  TRP B 100      63.054   4.495   4.562  1.00 59.46           C  
ANISOU 4343  CB  TRP B 100     6624   6576   9392   -523   -322    454       C  
ATOM   4344  CG  TRP B 100      63.672   5.172   5.759  1.00 59.58           C  
ANISOU 4344  CG  TRP B 100     6655   6665   9318   -425   -242    476       C  
ATOM   4345  CD1 TRP B 100      64.989   5.139   6.112  1.00 61.94           C  
ANISOU 4345  CD1 TRP B 100     7034   6967   9531   -364   -228    445       C  
ATOM   4346  CD2 TRP B 100      62.974   5.747   6.882  1.00 59.54           C  
ANISOU 4346  CD2 TRP B 100     6582   6738   9305   -377   -164    537       C  
ATOM   4347  NE1 TRP B 100      65.175   5.787   7.313  1.00 61.34           N  
ANISOU 4347  NE1 TRP B 100     6947   6974   9385   -283   -167    465       N  
ATOM   4348  CE2 TRP B 100      63.951   6.139   7.825  1.00 63.12           C  
ANISOU 4348  CE2 TRP B 100     7091   7244   9648   -285   -119    521       C  
ATOM   4349  CE3 TRP B 100      61.621   5.995   7.171  1.00 61.19           C  
ANISOU 4349  CE3 TRP B 100     6682   6981   9586   -396   -126    600       C  
ATOM   4350  CZ2 TRP B 100      63.620   6.773   9.029  1.00 62.40           C  
ANISOU 4350  CZ2 TRP B 100     6970   7241   9500   -208    -42    552       C  
ATOM   4351  CZ3 TRP B 100      61.295   6.616   8.367  1.00 62.83           C  
ANISOU 4351  CZ3 TRP B 100     6856   7272   9746   -315    -32    645       C  
ATOM   4352  CH2 TRP B 100      62.287   7.008   9.275  1.00 63.04           C  
ANISOU 4352  CH2 TRP B 100     6957   7350   9644   -220      8    614       C  
ATOM   4353  N   ALA B 101      62.150   1.489   3.524  1.00 63.65           N  
ANISOU 4353  N   ALA B 101     7158   6859  10166   -737   -398    464       N  
ATOM   4354  CA  ALA B 101      61.826   0.575   2.427  1.00 63.68           C  
ANISOU 4354  CA  ALA B 101     7182   6758  10255   -836   -493    392       C  
ATOM   4355  C   ALA B 101      60.404   0.026   2.586  1.00 67.73           C  
ANISOU 4355  C   ALA B 101     7565   7228  10943   -945   -503    447       C  
ATOM   4356  O   ALA B 101      59.682  -0.067   1.596  1.00 68.47           O  
ANISOU 4356  O   ALA B 101     7615   7299  11101  -1028   -620    375       O  
ATOM   4357  CB  ALA B 101      62.831  -0.563   2.375  1.00 64.58           C  
ANISOU 4357  CB  ALA B 101     7416   6756  10367   -829   -469    367       C  
ATOM   4358  N   THR B 102      59.991  -0.289   3.843  1.00 63.90           N  
ANISOU 4358  N   THR B 102     7009   6741  10530   -939   -380    580       N  
ATOM   4359  CA  THR B 102      58.654  -0.797   4.184  1.00 65.30           C  
ANISOU 4359  CA  THR B 102     7041   6877  10894  -1037   -355    663       C  
ATOM   4360  C   THR B 102      57.625   0.325   3.985  1.00 68.65           C  
ANISOU 4360  C   THR B 102     7330   7423  11330  -1038   -396    670       C  
ATOM   4361  O   THR B 102      56.605   0.102   3.343  1.00 69.41           O  
ANISOU 4361  O   THR B 102     7316   7496  11561  -1141   -485    646       O  
ATOM   4362  CB  THR B 102      58.639  -1.348   5.627  1.00 75.33           C  
ANISOU 4362  CB  THR B 102     8290   8122  12210  -1001   -185    823       C  
ATOM   4363  OG1 THR B 102      59.585  -2.408   5.732  1.00 78.62           O  
ANISOU 4363  OG1 THR B 102     8830   8420  12621   -992   -155    821       O  
ATOM   4364  CG2 THR B 102      57.288  -1.878   6.043  1.00 74.55           C  
ANISOU 4364  CG2 THR B 102     8031   7973  12321  -1101   -130    932       C  
ATOM   4365  N   TYR B 103      57.920   1.532   4.503  1.00 63.89           N  
ANISOU 4365  N   TYR B 103     6737   6948  10592   -922   -339    695       N  
ATOM   4366  CA  TYR B 103      57.085   2.730   4.382  1.00 63.21           C  
ANISOU 4366  CA  TYR B 103     6539   6976  10501   -892   -359    706       C  
ATOM   4367  C   TYR B 103      56.874   3.083   2.892  1.00 65.73           C  
ANISOU 4367  C   TYR B 103     6855   7309  10813   -937   -529    592       C  
ATOM   4368  O   TYR B 103      55.743   3.376   2.506  1.00 66.23           O  
ANISOU 4368  O   TYR B 103     6779   7415  10969   -980   -588    608       O  
ATOM   4369  CB  TYR B 103      57.739   3.898   5.156  1.00 63.22           C  
ANISOU 4369  CB  TYR B 103     6596   7081  10346   -752   -272    720       C  
ATOM   4370  CG  TYR B 103      57.025   5.231   5.098  1.00 65.06           C  
ANISOU 4370  CG  TYR B 103     6740   7418  10561   -697   -278    724       C  
ATOM   4371  CD1 TYR B 103      55.761   5.390   5.659  1.00 68.52           C  
ANISOU 4371  CD1 TYR B 103     7023   7903  11108   -703   -210    821       C  
ATOM   4372  CD2 TYR B 103      57.693   6.377   4.681  1.00 64.57           C  
ANISOU 4372  CD2 TYR B 103     6752   7407  10376   -620   -320    647       C  
ATOM   4373  CE1 TYR B 103      55.125   6.629   5.673  1.00 69.23           C  
ANISOU 4373  CE1 TYR B 103     7034   8085  11185   -635   -201    830       C  
ATOM   4374  CE2 TYR B 103      57.079   7.626   4.710  1.00 65.38           C  
ANISOU 4374  CE2 TYR B 103     6781   7589  10470   -556   -309    659       C  
ATOM   4375  CZ  TYR B 103      55.791   7.747   5.201  1.00 71.76           C  
ANISOU 4375  CZ  TYR B 103     7439   8443  11386   -560   -252    747       C  
ATOM   4376  OH  TYR B 103      55.186   8.975   5.229  1.00 71.25           O  
ANISOU 4376  OH  TYR B 103     7301   8450  11319   -485   -235    761       O  
ATOM   4377  N   TYR B 104      57.935   2.972   2.053  1.00 60.19           N  
ANISOU 4377  N   TYR B 104     6296   6570  10001   -922   -607    485       N  
ATOM   4378  CA  TYR B 104      57.847   3.223   0.612  1.00 59.74           C  
ANISOU 4378  CA  TYR B 104     6263   6532   9905   -948   -762    380       C  
ATOM   4379  C   TYR B 104      57.004   2.133  -0.074  1.00 67.32           C  
ANISOU 4379  C   TYR B 104     7158   7413  11009  -1083   -877    332       C  
ATOM   4380  O   TYR B 104      56.227   2.459  -0.975  1.00 67.97           O  
ANISOU 4380  O   TYR B 104     7170   7547  11110  -1117  -1009    283       O  
ATOM   4381  CB  TYR B 104      59.250   3.295  -0.015  1.00 58.67           C  
ANISOU 4381  CB  TYR B 104     6302   6376   9614   -886   -784    291       C  
ATOM   4382  CG  TYR B 104      59.266   3.646  -1.489  1.00 59.10           C  
ANISOU 4382  CG  TYR B 104     6403   6465   9589   -884   -924    193       C  
ATOM   4383  CD1 TYR B 104      59.373   4.968  -1.909  1.00 60.00           C  
ANISOU 4383  CD1 TYR B 104     6514   6679   9603   -798   -939    201       C  
ATOM   4384  CD2 TYR B 104      59.240   2.654  -2.462  1.00 60.30           C  
ANISOU 4384  CD2 TYR B 104     6614   6543   9754   -957  -1035     93       C  
ATOM   4385  CE1 TYR B 104      59.425   5.295  -3.264  1.00 59.55           C  
ANISOU 4385  CE1 TYR B 104     6511   6662   9454   -778  -1055    130       C  
ATOM   4386  CE2 TYR B 104      59.271   2.970  -3.818  1.00 61.04           C  
ANISOU 4386  CE2 TYR B 104     6764   6684   9744   -937  -1163      2       C  
ATOM   4387  CZ  TYR B 104      59.381   4.291  -4.215  1.00 65.10           C  
ANISOU 4387  CZ  TYR B 104     7277   7312  10148   -843  -1169     30       C  
ATOM   4388  OH  TYR B 104      59.419   4.606  -5.551  1.00 65.51           O  
ANISOU 4388  OH  TYR B 104     7391   7418  10081   -808  -1285    -40       O  
ATOM   4389  N   SER B 105      57.160   0.846   0.356  1.00 65.62           N  
ANISOU 4389  N   SER B 105     6965   7068  10899  -1157   -830    345       N  
ATOM   4390  CA  SER B 105      56.436  -0.314  -0.193  1.00 67.77           C  
ANISOU 4390  CA  SER B 105     7181   7229  11340  -1300   -928    290       C  
ATOM   4391  C   SER B 105      54.927  -0.196   0.007  1.00 74.80           C  
ANISOU 4391  C   SER B 105     7853   8157  12410  -1383   -956    360       C  
ATOM   4392  O   SER B 105      54.169  -0.552  -0.898  1.00 75.69           O  
ANISOU 4392  O   SER B 105     7891   8249  12617  -1484  -1112    275       O  
ATOM   4393  CB  SER B 105      56.916  -1.614   0.444  1.00 72.05           C  
ANISOU 4393  CB  SER B 105     7788   7613  11977  -1347   -834    322       C  
ATOM   4394  OG  SER B 105      58.272  -1.883   0.137  1.00 83.28           O  
ANISOU 4394  OG  SER B 105     9399   8986  13256  -1279   -825    247       O  
ATOM   4395  N   TYR B 106      54.488   0.303   1.183  1.00 72.80           N  
ANISOU 4395  N   TYR B 106     7494   7965  12201  -1336   -808    509       N  
ATOM   4396  CA  TYR B 106      53.068   0.467   1.490  1.00 74.73           C  
ANISOU 4396  CA  TYR B 106     7516   8255  12622  -1397   -802    598       C  
ATOM   4397  C   TYR B 106      52.550   1.838   0.976  1.00 78.57           C  
ANISOU 4397  C   TYR B 106     7926   8901  13026  -1321   -877    587       C  
ATOM   4398  O   TYR B 106      51.538   2.332   1.472  1.00 79.16           O  
ANISOU 4398  O   TYR B 106     7828   9049  13199  -1310   -820    690       O  
ATOM   4399  CB  TYR B 106      52.810   0.315   3.002  1.00 76.62           C  
ANISOU 4399  CB  TYR B 106     7682   8485  12943  -1368   -588    771       C  
ATOM   4400  CG  TYR B 106      52.927  -1.112   3.497  1.00 80.93           C  
ANISOU 4400  CG  TYR B 106     8251   8866  13633  -1459   -511    819       C  
ATOM   4401  CD1 TYR B 106      51.854  -1.996   3.397  1.00 86.14           C  
ANISOU 4401  CD1 TYR B 106     8747   9426  14556  -1612   -535    855       C  
ATOM   4402  CD2 TYR B 106      54.081  -1.561   4.125  1.00 80.68           C  
ANISOU 4402  CD2 TYR B 106     8391   8772  13490  -1390   -408    839       C  
ATOM   4403  CE1 TYR B 106      51.952  -3.311   3.854  1.00 89.31           C  
ANISOU 4403  CE1 TYR B 106     9169   9653  15112  -1697   -452    910       C  
ATOM   4404  CE2 TYR B 106      54.192  -2.872   4.589  1.00 83.07           C  
ANISOU 4404  CE2 TYR B 106     8719   8914  13930  -1461   -329    899       C  
ATOM   4405  CZ  TYR B 106      53.124  -3.745   4.453  1.00 96.45           C  
ANISOU 4405  CZ  TYR B 106    10259  10495  15892  -1615   -345    937       C  
ATOM   4406  OH  TYR B 106      53.225  -5.039   4.914  1.00101.60           O  
ANISOU 4406  OH  TYR B 106    10936  10968  16701  -1686   -254   1006       O  
ATOM   4407  N   ARG B 107      53.210   2.400  -0.075  1.00 73.51           N  
ANISOU 4407  N   ARG B 107     7410   8308  12214  -1266  -1001    470       N  
ATOM   4408  CA  ARG B 107      52.886   3.669  -0.747  1.00 72.12           C  
ANISOU 4408  CA  ARG B 107     7195   8267  11939  -1183  -1083    455       C  
ATOM   4409  C   ARG B 107      52.670   4.791   0.294  1.00 76.81           C  
ANISOU 4409  C   ARG B 107     7726   8951  12507  -1067   -926    578       C  
ATOM   4410  O   ARG B 107      51.647   5.476   0.289  1.00 77.90           O  
ANISOU 4410  O   ARG B 107     7707   9177  12716  -1044   -941    638       O  
ATOM   4411  CB  ARG B 107      51.659   3.532  -1.669  1.00 69.81           C  
ANISOU 4411  CB  ARG B 107     6738   8017  11769  -1271  -1263    419       C  
ATOM   4412  CG  ARG B 107      51.923   2.891  -3.038  1.00 73.42           C  
ANISOU 4412  CG  ARG B 107     7289   8440  12168  -1335  -1466    258       C  
ATOM   4413  CD  ARG B 107      52.433   1.459  -3.002  1.00 78.28           C  
ANISOU 4413  CD  ARG B 107     7997   8892  12854  -1446  -1472    177       C  
ATOM   4414  NE  ARG B 107      52.530   0.879  -4.343  1.00 80.44           N  
ANISOU 4414  NE  ARG B 107     8360   9142  13061  -1497  -1673      6       N  
ATOM   4415  CZ  ARG B 107      53.016  -0.331  -4.601  1.00 89.68           C  
ANISOU 4415  CZ  ARG B 107     9642  10168  14265  -1580  -1710   -104       C  
ATOM   4416  NH1 ARG B 107      53.512  -1.080  -3.623  1.00 67.04           N  
ANISOU 4416  NH1 ARG B 107     6810   7164  11498  -1618  -1556    -45       N  
ATOM   4417  NH2 ARG B 107      53.051  -0.784  -5.847  1.00 82.06           N  
ANISOU 4417  NH2 ARG B 107     8764   9195  13220  -1611  -1897   -273       N  
ATOM   4418  N   TYR B 108      53.669   4.958   1.176  1.00 73.01           N  
ANISOU 4418  N   TYR B 108     7373   8448  11920   -988   -781    604       N  
ATOM   4419  CA  TYR B 108      53.780   5.959   2.238  1.00 72.14           C  
ANISOU 4419  CA  TYR B 108     7257   8407  11746   -867   -628    685       C  
ATOM   4420  C   TYR B 108      52.596   5.830   3.240  1.00 77.87           C  
ANISOU 4420  C   TYR B 108     7802   9158  12628   -885   -512    814       C  
ATOM   4421  O   TYR B 108      51.974   6.829   3.617  1.00 77.04           O  
ANISOU 4421  O   TYR B 108     7604   9140  12528   -802   -450    874       O  
ATOM   4422  CB  TYR B 108      53.872   7.383   1.658  1.00 72.41           C  
ANISOU 4422  CB  TYR B 108     7308   8532  11674   -763   -673    657       C  
ATOM   4423  CG  TYR B 108      55.096   7.560   0.770  1.00 72.78           C  
ANISOU 4423  CG  TYR B 108     7531   8556  11566   -732   -750    555       C  
ATOM   4424  CD1 TYR B 108      56.364   7.747   1.320  1.00 73.11           C  
ANISOU 4424  CD1 TYR B 108     7717   8574  11488   -662   -658    531       C  
ATOM   4425  CD2 TYR B 108      54.988   7.530  -0.615  1.00 73.89           C  
ANISOU 4425  CD2 TYR B 108     7690   8707  11677   -767   -913    483       C  
ATOM   4426  CE1 TYR B 108      57.495   7.881   0.512  1.00 73.12           C  
ANISOU 4426  CE1 TYR B 108     7864   8553  11366   -634   -713    449       C  
ATOM   4427  CE2 TYR B 108      56.110   7.681  -1.434  1.00 73.74           C  
ANISOU 4427  CE2 TYR B 108     7835   8672  11511   -727   -962    401       C  
ATOM   4428  CZ  TYR B 108      57.362   7.860  -0.866  1.00 79.75           C  
ANISOU 4428  CZ  TYR B 108     8725   9401  12176   -663   -854    391       C  
ATOM   4429  OH  TYR B 108      58.473   8.030  -1.665  1.00 80.94           O  
ANISOU 4429  OH  TYR B 108     9019   9537  12198   -622   -887    323       O  
ATOM   4430  N   ASP B 109      52.356   4.584   3.720  1.00 76.14           N  
ANISOU 4430  N   ASP B 109     7543   8851  12534   -982   -462    863       N  
ATOM   4431  CA  ASP B 109      51.375   4.282   4.758  1.00 77.58           C  
ANISOU 4431  CA  ASP B 109     7566   9043  12867   -999   -321   1004       C  
ATOM   4432  C   ASP B 109      52.115   3.855   6.012  1.00 83.17           C  
ANISOU 4432  C   ASP B 109     8382   9718  13502   -941   -146   1074       C  
ATOM   4433  O   ASP B 109      52.574   2.709   6.111  1.00 83.44           O  
ANISOU 4433  O   ASP B 109     8488   9643  13572  -1010   -138   1074       O  
ATOM   4434  CB  ASP B 109      50.367   3.211   4.305  1.00 81.29           C  
ANISOU 4434  CB  ASP B 109     7871   9437  13576  -1163   -396   1028       C  
ATOM   4435  CG  ASP B 109      49.124   3.072   5.181  1.00 90.33           C  
ANISOU 4435  CG  ASP B 109     8801  10609  14913  -1185   -259   1186       C  
ATOM   4436  OD1 ASP B 109      48.847   4.004   5.980  1.00 89.16           O  
ANISOU 4436  OD1 ASP B 109     8609  10564  14703  -1059   -128   1268       O  
ATOM   4437  OD2 ASP B 109      48.360   2.100   4.976  1.00 98.98           O  
ANISOU 4437  OD2 ASP B 109     9757  11622  16230  -1328   -293   1220       O  
ATOM   4438  N   TRP B 110      52.304   4.805   6.934  1.00 80.07           N  
ANISOU 4438  N   TRP B 110     8014   9418  12991   -803    -14   1124       N  
ATOM   4439  CA  TRP B 110      53.008   4.578   8.186  1.00 80.01           C  
ANISOU 4439  CA  TRP B 110     8112   9413  12875   -718    143   1186       C  
ATOM   4440  C   TRP B 110      52.158   3.659   9.083  1.00 87.76           C  
ANISOU 4440  C   TRP B 110     8974  10360  14012   -765    288   1346       C  
ATOM   4441  O   TRP B 110      51.095   4.058   9.557  1.00 88.29           O  
ANISOU 4441  O   TRP B 110     8886  10492  14169   -740    383   1445       O  
ATOM   4442  CB  TRP B 110      53.328   5.922   8.866  1.00 77.51           C  
ANISOU 4442  CB  TRP B 110     7850   9210  12391   -558    225   1170       C  
ATOM   4443  CG  TRP B 110      54.223   5.789  10.054  1.00 77.73           C  
ANISOU 4443  CG  TRP B 110     8010   9259  12264   -459    348   1198       C  
ATOM   4444  CD1 TRP B 110      53.845   5.637  11.354  1.00 81.61           C  
ANISOU 4444  CD1 TRP B 110     8471   9803  12733   -382    525   1321       C  
ATOM   4445  CD2 TRP B 110      55.652   5.720  10.040  1.00 76.03           C  
ANISOU 4445  CD2 TRP B 110     7972   9019  11895   -423    299   1108       C  
ATOM   4446  NE1 TRP B 110      54.951   5.520  12.157  1.00 80.41           N  
ANISOU 4446  NE1 TRP B 110     8474   9672  12405   -293    576   1305       N  
ATOM   4447  CE2 TRP B 110      56.076   5.559  11.376  1.00 80.33           C  
ANISOU 4447  CE2 TRP B 110     8585   9613  12323   -321    436   1175       C  
ATOM   4448  CE3 TRP B 110      56.621   5.778   9.025  1.00 75.76           C  
ANISOU 4448  CE3 TRP B 110     8043   8935  11809   -460    156    982       C  
ATOM   4449  CZ2 TRP B 110      57.425   5.456  11.725  1.00 78.66           C  
ANISOU 4449  CZ2 TRP B 110     8530   9403  11954   -261    418   1115       C  
ATOM   4450  CZ3 TRP B 110      57.955   5.692   9.372  1.00 76.24           C  
ANISOU 4450  CZ3 TRP B 110     8252   8990  11727   -402    156    929       C  
ATOM   4451  CH2 TRP B 110      58.347   5.538  10.708  1.00 77.32           C  
ANISOU 4451  CH2 TRP B 110     8442   9177  11759   -307    277    992       C  
ATOM   4452  N   LEU B 111      52.611   2.408   9.253  1.00 87.17           N  
ANISOU 4452  N   LEU B 111     8962  10172  13985   -835    308   1379       N  
ATOM   4453  CA  LEU B 111      51.919   1.372  10.034  1.00 90.01           C  
ANISOU 4453  CA  LEU B 111     9221  10466  14512   -893    451   1544       C  
ATOM   4454  C   LEU B 111      52.682   1.052  11.346  1.00 95.75           C  
ANISOU 4454  C   LEU B 111    10078  11212  15091   -773    622   1644       C  
ATOM   4455  O   LEU B 111      52.712  -0.109  11.778  1.00 96.73           O  
ANISOU 4455  O   LEU B 111    10220  11230  15302   -822    697   1742       O  
ATOM   4456  CB  LEU B 111      51.779   0.086   9.170  1.00 91.08           C  
ANISOU 4456  CB  LEU B 111     9325  10433  14847  -1072    340   1509       C  
ATOM   4457  CG  LEU B 111      50.976   0.182   7.865  1.00 96.42           C  
ANISOU 4457  CG  LEU B 111     9873  11087  15674  -1202    148   1403       C  
ATOM   4458  CD1 LEU B 111      51.194  -1.037   6.998  1.00 97.04           C  
ANISOU 4458  CD1 LEU B 111     9990  10999  15884  -1354     21   1318       C  
ATOM   4459  CD2 LEU B 111      49.488   0.398   8.132  1.00101.32           C  
ANISOU 4459  CD2 LEU B 111    10246  11758  16494  -1247    208   1517       C  
ATOM   4460  N   PHE B 112      53.282   2.086  11.984  1.00 91.58           N  
ANISOU 4460  N   PHE B 112     9639  10817  14340   -612    680   1619       N  
ATOM   4461  CA  PHE B 112      54.075   1.915  13.204  1.00 91.26           C  
ANISOU 4461  CA  PHE B 112     9730  10827  14118   -478    815   1690       C  
ATOM   4462  C   PHE B 112      53.614   2.861  14.346  1.00 96.17           C  
ANISOU 4462  C   PHE B 112    10321  11603  14617   -323    969   1758       C  
ATOM   4463  O   PHE B 112      54.239   2.884  15.409  1.00 96.03           O  
ANISOU 4463  O   PHE B 112    10416  11659  14413   -190   1072   1801       O  
ATOM   4464  CB  PHE B 112      55.562   2.170  12.898  1.00 91.14           C  
ANISOU 4464  CB  PHE B 112     9904  10814  13912   -425    698   1543       C  
ATOM   4465  CG  PHE B 112      56.187   1.233  11.890  1.00 92.34           C  
ANISOU 4465  CG  PHE B 112    10116  10821  14146   -544    567   1472       C  
ATOM   4466  CD1 PHE B 112      56.779   0.040  12.297  1.00 96.56           C  
ANISOU 4466  CD1 PHE B 112    10727  11262  14700   -553    623   1553       C  
ATOM   4467  CD2 PHE B 112      56.235   1.567  10.542  1.00 93.26           C  
ANISOU 4467  CD2 PHE B 112    10229  10901  14307   -628    392   1322       C  
ATOM   4468  CE1 PHE B 112      57.378  -0.818  11.367  1.00 96.96           C  
ANISOU 4468  CE1 PHE B 112    10842  11170  14827   -651    510   1476       C  
ATOM   4469  CE2 PHE B 112      56.829   0.709   9.614  1.00 95.77           C  
ANISOU 4469  CE2 PHE B 112    10615  11090  14682   -723    278   1245       C  
ATOM   4470  CZ  PHE B 112      57.399  -0.478  10.032  1.00 94.61           C  
ANISOU 4470  CZ  PHE B 112    10541  10841  14567   -735    339   1316       C  
ATOM   4471  N   GLY B 113      52.538   3.613  14.121  1.00 93.34           N  
ANISOU 4471  N   GLY B 113     9813  11296  14357   -334    980   1763       N  
ATOM   4472  CA  GLY B 113      52.008   4.550  15.107  1.00 94.06           C  
ANISOU 4472  CA  GLY B 113     9866  11523  14348   -186   1129   1816       C  
ATOM   4473  C   GLY B 113      52.660   5.918  15.036  1.00 97.23           C  
ANISOU 4473  C   GLY B 113    10380  12011  14553    -73   1054   1649       C  
ATOM   4474  O   GLY B 113      53.824   6.023  14.643  1.00 95.35           O  
ANISOU 4474  O   GLY B 113    10290  11748  14190    -69    936   1524       O  
ATOM   4475  N   PRO B 114      51.957   7.001  15.454  1.00 94.86           N  
ANISOU 4475  N   PRO B 114    10010  11806  14226     28   1132   1645       N  
ATOM   4476  CA  PRO B 114      52.544   8.354  15.333  1.00 93.33           C  
ANISOU 4476  CA  PRO B 114     9918  11669  13874    127   1061   1478       C  
ATOM   4477  C   PRO B 114      53.693   8.621  16.310  1.00 95.22           C  
ANISOU 4477  C   PRO B 114    10345  11974  13861    260   1101   1411       C  
ATOM   4478  O   PRO B 114      54.430   9.593  16.111  1.00 93.59           O  
ANISOU 4478  O   PRO B 114    10236  11785  13539    315   1014   1253       O  
ATOM   4479  CB  PRO B 114      51.368   9.286  15.655  1.00 96.58           C  
ANISOU 4479  CB  PRO B 114    10199  12156  14342    212   1171   1520       C  
ATOM   4480  CG  PRO B 114      50.138   8.432  15.484  1.00102.64           C  
ANISOU 4480  CG  PRO B 114    10762  12890  15345    109   1232   1684       C  
ATOM   4481  CD  PRO B 114      50.560   7.069  15.926  1.00 98.42           C  
ANISOU 4481  CD  PRO B 114    10273  12303  14820     46   1283   1789       C  
ATOM   4482  N   VAL B 115      53.855   7.772  17.346  1.00 91.74           N  
ANISOU 4482  N   VAL B 115     9951  11568  13340    313   1228   1532       N  
ATOM   4483  CA  VAL B 115      54.924   7.922  18.339  1.00 90.89           C  
ANISOU 4483  CA  VAL B 115    10015  11540  12979    448   1257   1479       C  
ATOM   4484  C   VAL B 115      56.266   7.564  17.664  1.00 91.97           C  
ANISOU 4484  C   VAL B 115    10270  11606  13069    378   1079   1364       C  
ATOM   4485  O   VAL B 115      57.213   8.343  17.769  1.00 91.14           O  
ANISOU 4485  O   VAL B 115    10280  11544  12807    449   1000   1213       O  
ATOM   4486  CB  VAL B 115      54.665   7.082  19.624  1.00 96.39           C  
ANISOU 4486  CB  VAL B 115    10724  12304  13596    538   1451   1668       C  
ATOM   4487  CG1 VAL B 115      55.830   7.188  20.603  1.00 96.02           C  
ANISOU 4487  CG1 VAL B 115    10859  12354  13269    683   1453   1610       C  
ATOM   4488  CG2 VAL B 115      53.365   7.513  20.303  1.00 98.06           C  
ANISOU 4488  CG2 VAL B 115    10818  12596  13845    624   1644   1781       C  
ATOM   4489  N   MET B 116      56.316   6.449  16.906  1.00 87.21           N  
ANISOU 4489  N   MET B 116     9629  10888  12619    235   1014   1424       N  
ATOM   4490  CA  MET B 116      57.534   6.018  16.219  1.00 85.60           C  
ANISOU 4490  CA  MET B 116     9528  10609  12386    172    863   1329       C  
ATOM   4491  C   MET B 116      57.836   6.909  15.001  1.00 83.30           C  
ANISOU 4491  C   MET B 116     9237  10274  12140    107    701   1159       C  
ATOM   4492  O   MET B 116      58.961   6.881  14.500  1.00 82.49           O  
ANISOU 4492  O   MET B 116     9229  10133  11980     86    584   1055       O  
ATOM   4493  CB  MET B 116      57.451   4.555  15.787  1.00 89.53           C  
ANISOU 4493  CB  MET B 116     9994  10987  13036     52    861   1443       C  
ATOM   4494  CG  MET B 116      57.367   3.618  16.954  1.00 96.77           C  
ANISOU 4494  CG  MET B 116    10932  11932  13903    123   1022   1622       C  
ATOM   4495  SD  MET B 116      57.485   1.879  16.503  1.00103.69           S  
ANISOU 4495  SD  MET B 116    11793  12639  14966     -9   1029   1754       S  
ATOM   4496  CE  MET B 116      57.022   1.134  18.126  1.00103.08           C  
ANISOU 4496  CE  MET B 116    11729  12638  14798    128   1272   1997       C  
ATOM   4497  N   CYS B 117      56.862   7.726  14.555  1.00 75.60           N  
ANISOU 4497  N   CYS B 117     8155   9309  11261     90    702   1141       N  
ATOM   4498  CA  CYS B 117      57.068   8.706  13.483  1.00 71.88           C  
ANISOU 4498  CA  CYS B 117     7683   8808  10819     56    571   1002       C  
ATOM   4499  C   CYS B 117      58.010   9.804  14.002  1.00 74.42           C  
ANISOU 4499  C   CYS B 117     8119   9191  10968    171    557    868       C  
ATOM   4500  O   CYS B 117      58.948  10.182  13.297  1.00 72.61           O  
ANISOU 4500  O   CYS B 117     7952   8919  10719    144    439    747       O  
ATOM   4501  CB  CYS B 117      55.734   9.267  12.995  1.00 71.30           C  
ANISOU 4501  CB  CYS B 117     7459   8740  10893     27    589   1042       C  
ATOM   4502  SG  CYS B 117      55.867  10.607  11.774  1.00 73.06           S  
ANISOU 4502  SG  CYS B 117     7678   8937  11145     16    451    903       S  
ATOM   4503  N   LYS B 118      57.811  10.240  15.269  1.00 71.38           N  
ANISOU 4503  N   LYS B 118     7763   8902  10457    301    679    888       N  
ATOM   4504  CA  LYS B 118      58.680  11.212  15.930  1.00 70.67           C  
ANISOU 4504  CA  LYS B 118     7782   8873  10196    414    665    749       C  
ATOM   4505  C   LYS B 118      59.990  10.592  16.363  1.00 74.84           C  
ANISOU 4505  C   LYS B 118     8429   9419  10589    434    609    712       C  
ATOM   4506  O   LYS B 118      61.032  11.208  16.169  1.00 73.18           O  
ANISOU 4506  O   LYS B 118     8293   9204  10308    452    512    566       O  
ATOM   4507  CB  LYS B 118      58.015  11.841  17.164  1.00 74.15           C  
ANISOU 4507  CB  LYS B 118     8220   9421  10533    559    814    770       C  
ATOM   4508  CG  LYS B 118      56.892  12.782  16.858  1.00 84.46           C  
ANISOU 4508  CG  LYS B 118     9423  10720  11946    581    870    768       C  
ATOM   4509  CD  LYS B 118      56.433  13.511  18.101  1.00 91.04           C  
ANISOU 4509  CD  LYS B 118    10281  11659  12651    745   1019    758       C  
ATOM   4510  CE  LYS B 118      55.383  14.545  17.789  1.00 95.49           C  
ANISOU 4510  CE  LYS B 118    10747  12210  13323    785   1077    744       C  
ATOM   4511  NZ  LYS B 118      55.892  15.604  16.881  1.00 98.96           N  
ANISOU 4511  NZ  LYS B 118    11221  12571  13810    759    951    583       N  
ATOM   4512  N   VAL B 119      59.936   9.397  17.003  1.00 73.00           N  
ANISOU 4512  N   VAL B 119     8205   9206  10325    440    678    852       N  
ATOM   4513  CA  VAL B 119      61.102   8.730  17.586  1.00 73.12           C  
ANISOU 4513  CA  VAL B 119     8328   9254  10203    484    642    847       C  
ATOM   4514  C   VAL B 119      62.096   8.329  16.468  1.00 77.92           C  
ANISOU 4514  C   VAL B 119     8962   9757  10886    376    493    777       C  
ATOM   4515  O   VAL B 119      63.228   8.807  16.506  1.00 77.25           O  
ANISOU 4515  O   VAL B 119     8948   9693  10709    409    400    648       O  
ATOM   4516  CB  VAL B 119      60.714   7.507  18.459  1.00 77.52           C  
ANISOU 4516  CB  VAL B 119     8884   9844  10726    525    770   1043       C  
ATOM   4517  CG1 VAL B 119      61.952   6.757  18.946  1.00 77.23           C  
ANISOU 4517  CG1 VAL B 119     8954   9835  10556    576    720   1049       C  
ATOM   4518  CG2 VAL B 119      59.862   7.939  19.645  1.00 78.72           C  
ANISOU 4518  CG2 VAL B 119     9022  10116  10772    656    933   1115       C  
ATOM   4519  N   PHE B 120      61.690   7.485  15.489  1.00 76.02           N  
ANISOU 4519  N   PHE B 120     8663   9409  10813    250    471    853       N  
ATOM   4520  CA  PHE B 120      62.612   7.050  14.428  1.00 75.71           C  
ANISOU 4520  CA  PHE B 120     8659   9273  10833    160    346    790       C  
ATOM   4521  C   PHE B 120      62.935   8.196  13.463  1.00 77.29           C  
ANISOU 4521  C   PHE B 120     8855   9446  11066    126    245    641       C  
ATOM   4522  O   PHE B 120      64.029   8.204  12.898  1.00 76.83           O  
ANISOU 4522  O   PHE B 120     8850   9348  10994    101    151    558       O  
ATOM   4523  CB  PHE B 120      62.088   5.849  13.642  1.00 78.51           C  
ANISOU 4523  CB  PHE B 120     8964   9516  11351     41    345    889       C  
ATOM   4524  CG  PHE B 120      62.063   4.591  14.476  1.00 82.47           C  
ANISOU 4524  CG  PHE B 120     9481  10009  11843     65    442   1041       C  
ATOM   4525  CD1 PHE B 120      63.238   3.918  14.785  1.00 86.08           C  
ANISOU 4525  CD1 PHE B 120    10032  10461  12214    111    418   1051       C  
ATOM   4526  CD2 PHE B 120      60.862   4.044  14.902  1.00 87.04           C  
ANISOU 4526  CD2 PHE B 120     9973  10577  12519     41    561   1188       C  
ATOM   4527  CE1 PHE B 120      63.219   2.765  15.571  1.00 88.70           C  
ANISOU 4527  CE1 PHE B 120    10383  10779  12539    147    517   1210       C  
ATOM   4528  CE2 PHE B 120      60.842   2.876  15.672  1.00 91.57           C  
ANISOU 4528  CE2 PHE B 120    10562  11130  13100     65    667   1348       C  
ATOM   4529  CZ  PHE B 120      62.023   2.242  15.998  1.00 89.55           C  
ANISOU 4529  CZ  PHE B 120    10412  10868  12745    122    645   1361       C  
ATOM   4530  N   GLY B 121      62.032   9.166  13.336  1.00 71.83           N  
ANISOU 4530  N   GLY B 121     8100   8775  10416    136    274    618       N  
ATOM   4531  CA  GLY B 121      62.271  10.360  12.535  1.00 69.99           C  
ANISOU 4531  CA  GLY B 121     7864   8515  10215    121    199    495       C  
ATOM   4532  C   GLY B 121      63.440  11.148  13.098  1.00 72.44           C  
ANISOU 4532  C   GLY B 121     8254   8863  10405    196    160    366       C  
ATOM   4533  O   GLY B 121      64.325  11.576  12.353  1.00 70.97           O  
ANISOU 4533  O   GLY B 121     8096   8626  10244    160     73    274       O  
ATOM   4534  N   SER B 122      63.472  11.285  14.439  1.00 69.49           N  
ANISOU 4534  N   SER B 122     7916   8585   9900    302    226    361       N  
ATOM   4535  CA  SER B 122      64.527  11.961  15.190  1.00 69.18           C  
ANISOU 4535  CA  SER B 122     7950   8603   9733    381    181    228       C  
ATOM   4536  C   SER B 122      65.792  11.132  15.241  1.00 73.79           C  
ANISOU 4536  C   SER B 122     8588   9190  10258    372    108    224       C  
ATOM   4537  O   SER B 122      66.883  11.689  15.142  1.00 73.05           O  
ANISOU 4537  O   SER B 122     8525   9091  10138    376     20    100       O  
ATOM   4538  CB  SER B 122      64.061  12.248  16.609  1.00 73.41           C  
ANISOU 4538  CB  SER B 122     8513   9254  10127    509    274    228       C  
ATOM   4539  OG  SER B 122      62.893  13.045  16.590  1.00 80.81           O  
ANISOU 4539  OG  SER B 122     9393  10186  11125    530    355    238       O  
ATOM   4540  N   PHE B 123      65.649   9.799  15.431  1.00 71.06           N  
ANISOU 4540  N   PHE B 123     8247   8848   9904    362    150    365       N  
ATOM   4541  CA  PHE B 123      66.758   8.848  15.521  1.00 70.71           C  
ANISOU 4541  CA  PHE B 123     8252   8803   9813    367     97    391       C  
ATOM   4542  C   PHE B 123      67.550   8.844  14.208  1.00 72.16           C  
ANISOU 4542  C   PHE B 123     8429   8881  10108    270      1    329       C  
ATOM   4543  O   PHE B 123      68.777   8.729  14.231  1.00 72.12           O  
ANISOU 4543  O   PHE B 123     8457   8882  10063    286    -70    277       O  
ATOM   4544  CB  PHE B 123      66.232   7.447  15.855  1.00 73.49           C  
ANISOU 4544  CB  PHE B 123     8603   9148  10170    370    184    571       C  
ATOM   4545  CG  PHE B 123      67.283   6.391  16.108  1.00 75.78           C  
ANISOU 4545  CG  PHE B 123     8948   9437  10410    398    150    622       C  
ATOM   4546  CD1 PHE B 123      67.860   6.249  17.365  1.00 80.30           C  
ANISOU 4546  CD1 PHE B 123     9574  10130  10805    527    156    637       C  
ATOM   4547  CD2 PHE B 123      67.623   5.476  15.119  1.00 77.79           C  
ANISOU 4547  CD2 PHE B 123     9199   9571  10787    308    117    665       C  
ATOM   4548  CE1 PHE B 123      68.801   5.248  17.612  1.00 81.77           C  
ANISOU 4548  CE1 PHE B 123     9803  10317  10948    567    128    704       C  
ATOM   4549  CE2 PHE B 123      68.555   4.466  15.370  1.00 81.29           C  
ANISOU 4549  CE2 PHE B 123     9690  10003  11194    346    100    724       C  
ATOM   4550  CZ  PHE B 123      69.142   4.361  16.614  1.00 80.42           C  
ANISOU 4550  CZ  PHE B 123     9624  10013  10917    477    105    750       C  
ATOM   4551  N   LEU B 124      66.843   9.010  13.073  1.00 66.07           N  
ANISOU 4551  N   LEU B 124     7610   8023   9469    178     -1    337       N  
ATOM   4552  CA  LEU B 124      67.424   9.114  11.739  1.00 64.01           C  
ANISOU 4552  CA  LEU B 124     7348   7671   9303     96    -77    282       C  
ATOM   4553  C   LEU B 124      68.303  10.353  11.631  1.00 68.53           C  
ANISOU 4553  C   LEU B 124     7928   8252   9859    117   -136    144       C  
ATOM   4554  O   LEU B 124      69.458  10.246  11.221  1.00 69.97           O  
ANISOU 4554  O   LEU B 124     8131   8408  10046    105   -195     94       O  
ATOM   4555  CB  LEU B 124      66.297   9.166  10.686  1.00 63.21           C  
ANISOU 4555  CB  LEU B 124     7194   7503   9322     13    -67    323       C  
ATOM   4556  CG  LEU B 124      66.669   9.583   9.261  1.00 66.14           C  
ANISOU 4556  CG  LEU B 124     7566   7796   9769    -54   -138    264       C  
ATOM   4557  CD1 LEU B 124      67.517   8.526   8.564  1.00 65.41           C  
ANISOU 4557  CD1 LEU B 124     7518   7641   9695    -97   -178    281       C  
ATOM   4558  CD2 LEU B 124      65.430   9.870   8.464  1.00 68.35           C  
ANISOU 4558  CD2 LEU B 124     7787   8049  10136   -104   -135    296       C  
ATOM   4559  N   THR B 125      67.755  11.521  12.011  1.00 63.35           N  
ANISOU 4559  N   THR B 125     7249   7623   9196    150   -111     84       N  
ATOM   4560  CA  THR B 125      68.406  12.822  11.917  1.00 62.05           C  
ANISOU 4560  CA  THR B 125     7083   7442   9049    161   -155    -50       C  
ATOM   4561  C   THR B 125      69.564  12.904  12.927  1.00 67.45           C  
ANISOU 4561  C   THR B 125     7802   8195   9632    223   -205   -140       C  
ATOM   4562  O   THR B 125      70.615  13.455  12.600  1.00 68.29           O  
ANISOU 4562  O   THR B 125     7902   8267   9781    201   -270   -236       O  
ATOM   4563  CB  THR B 125      67.364  13.913  12.150  1.00 62.04           C  
ANISOU 4563  CB  THR B 125     7055   7446   9072    192   -101    -78       C  
ATOM   4564  OG1 THR B 125      66.251  13.661  11.297  1.00 57.06           O  
ANISOU 4564  OG1 THR B 125     6380   6775   8528    142    -65     22       O  
ATOM   4565  CG2 THR B 125      67.898  15.299  11.879  1.00 59.35           C  
ANISOU 4565  CG2 THR B 125     6710   7050   8791    191   -135   -207       C  
ATOM   4566  N   LEU B 126      69.387  12.322  14.125  1.00 64.01           N  
ANISOU 4566  N   LEU B 126     7396   7860   9066    302   -175    -99       N  
ATOM   4567  CA  LEU B 126      70.391  12.295  15.196  1.00 63.75           C  
ANISOU 4567  CA  LEU B 126     7396   7920   8905    379   -234   -175       C  
ATOM   4568  C   LEU B 126      71.672  11.618  14.701  1.00 67.98           C  
ANISOU 4568  C   LEU B 126     7927   8427   9475    344   -311   -172       C  
ATOM   4569  O   LEU B 126      72.737  12.233  14.740  1.00 68.20           O  
ANISOU 4569  O   LEU B 126     7936   8453   9522    339   -393   -293       O  
ATOM   4570  CB  LEU B 126      69.815  11.554  16.434  1.00 64.15           C  
ANISOU 4570  CB  LEU B 126     7487   8088   8800    479   -168    -81       C  
ATOM   4571  CG  LEU B 126      70.574  11.603  17.768  1.00 69.04           C  
ANISOU 4571  CG  LEU B 126     8153   8844   9236    595   -220   -154       C  
ATOM   4572  CD1 LEU B 126      69.719  11.095  18.877  1.00 70.43           C  
ANISOU 4572  CD1 LEU B 126     8371   9129   9260    701   -120    -42       C  
ATOM   4573  CD2 LEU B 126      71.840  10.807  17.737  1.00 71.05           C  
ANISOU 4573  CD2 LEU B 126     8409   9116   9472    597   -313   -151       C  
ATOM   4574  N   ASN B 127      71.559  10.363  14.223  1.00 64.11           N  
ANISOU 4574  N   ASN B 127     7447   7904   9007    318   -281    -37       N  
ATOM   4575  CA  ASN B 127      72.692   9.569  13.752  1.00 63.39           C  
ANISOU 4575  CA  ASN B 127     7356   7782   8947    300   -333    -15       C  
ATOM   4576  C   ASN B 127      73.201  10.070  12.390  1.00 66.87           C  
ANISOU 4576  C   ASN B 127     7765   8116   9529    211   -366    -73       C  
ATOM   4577  O   ASN B 127      74.374   9.853  12.092  1.00 66.90           O  
ANISOU 4577  O   ASN B 127     7753   8107   9560    209   -419   -105       O  
ATOM   4578  CB  ASN B 127      72.314   8.099  13.666  1.00 61.43           C  
ANISOU 4578  CB  ASN B 127     7136   7507   8696    301   -277    141       C  
ATOM   4579  CG  ASN B 127      72.027   7.503  15.022  1.00 67.98           C  
ANISOU 4579  CG  ASN B 127     8000   8443   9386    402   -234    225       C  
ATOM   4580  OD1 ASN B 127      72.873   7.486  15.922  1.00 53.80           O  
ANISOU 4580  OD1 ASN B 127     6221   6750   7472    493   -285    190       O  
ATOM   4581  ND2 ASN B 127      70.840   6.967  15.185  1.00 58.95           N  
ANISOU 4581  ND2 ASN B 127     6864   7278   8256    392   -139    348       N  
ATOM   4582  N   MET B 128      72.354  10.755  11.581  1.00 62.84           N  
ANISOU 4582  N   MET B 128     7239   7535   9103    149   -330    -79       N  
ATOM   4583  CA  MET B 128      72.808  11.337  10.311  1.00 62.02           C  
ANISOU 4583  CA  MET B 128     7111   7339   9114     81   -350   -122       C  
ATOM   4584  C   MET B 128      73.807  12.455  10.585  1.00 67.65           C  
ANISOU 4584  C   MET B 128     7790   8060   9854     91   -402   -250       C  
ATOM   4585  O   MET B 128      74.886  12.468   9.994  1.00 68.05           O  
ANISOU 4585  O   MET B 128     7815   8074   9966     67   -435   -275       O  
ATOM   4586  CB  MET B 128      71.646  11.865   9.461  1.00 63.80           C  
ANISOU 4586  CB  MET B 128     7326   7506   9408     33   -307    -95       C  
ATOM   4587  CG  MET B 128      72.121  12.472   8.149  1.00 66.75           C  
ANISOU 4587  CG  MET B 128     7685   7794   9882    -21   -319   -122       C  
ATOM   4588  SD  MET B 128      70.902  13.458   7.264  1.00 70.18           S  
ANISOU 4588  SD  MET B 128     8100   8176  10390    -52   -284   -104       S  
ATOM   4589  CE  MET B 128      70.699  14.816   8.380  1.00 67.42           C  
ANISOU 4589  CE  MET B 128     7727   7855  10036     -3   -272   -201       C  
ATOM   4590  N   PHE B 129      73.443  13.389  11.495  1.00 64.55           N  
ANISOU 4590  N   PHE B 129     7391   7712   9423    127   -407   -334       N  
ATOM   4591  CA  PHE B 129      74.313  14.491  11.879  1.00 64.61           C  
ANISOU 4591  CA  PHE B 129     7364   7718   9466    131   -466   -478       C  
ATOM   4592  C   PHE B 129      75.493  13.981  12.698  1.00 70.80           C  
ANISOU 4592  C   PHE B 129     8136   8589  10175    177   -547   -522       C  
ATOM   4593  O   PHE B 129      76.593  14.491  12.513  1.00 71.76           O  
ANISOU 4593  O   PHE B 129     8203   8684  10377    149   -607   -607       O  
ATOM   4594  CB  PHE B 129      73.567  15.584  12.650  1.00 66.44           C  
ANISOU 4594  CB  PHE B 129     7607   7969   9669    167   -450   -570       C  
ATOM   4595  CG  PHE B 129      72.749  16.482  11.757  1.00 66.89           C  
ANISOU 4595  CG  PHE B 129     7651   7922   9842    123   -389   -561       C  
ATOM   4596  CD1 PHE B 129      73.369  17.400  10.910  1.00 69.73           C  
ANISOU 4596  CD1 PHE B 129     7971   8175  10348     66   -400   -618       C  
ATOM   4597  CD2 PHE B 129      71.368  16.497  11.841  1.00 67.65           C  
ANISOU 4597  CD2 PHE B 129     7766   8030   9907    149   -318   -493       C  
ATOM   4598  CE1 PHE B 129      72.617  18.240  10.093  1.00 70.06           C  
ANISOU 4598  CE1 PHE B 129     8005   8123  10491     41   -340   -594       C  
ATOM   4599  CE2 PHE B 129      70.618  17.362  11.047  1.00 70.31           C  
ANISOU 4599  CE2 PHE B 129     8084   8281  10350    123   -269   -479       C  
ATOM   4600  CZ  PHE B 129      71.247  18.224  10.176  1.00 68.54           C  
ANISOU 4600  CZ  PHE B 129     7833   7951  10258     74   -281   -526       C  
ATOM   4601  N   ALA B 130      75.298  12.945  13.545  1.00 66.77           N  
ANISOU 4601  N   ALA B 130     7667   8179   9523    249   -545   -450       N  
ATOM   4602  CA  ALA B 130      76.404  12.377  14.313  1.00 66.62           C  
ANISOU 4602  CA  ALA B 130     7636   8254   9420    310   -626   -471       C  
ATOM   4603  C   ALA B 130      77.460  11.800  13.365  1.00 69.87           C  
ANISOU 4603  C   ALA B 130     8005   8606   9935    267   -648   -427       C  
ATOM   4604  O   ALA B 130      78.648  11.947  13.625  1.00 71.33           O  
ANISOU 4604  O   ALA B 130     8136   8833  10135    285   -732   -495       O  
ATOM   4605  CB  ALA B 130      75.903  11.319  15.269  1.00 67.75           C  
ANISOU 4605  CB  ALA B 130     7839   8502   9400    402   -596   -365       C  
ATOM   4606  N   SER B 131      77.028  11.241  12.216  1.00 64.35           N  
ANISOU 4606  N   SER B 131     7324   7810   9318    210   -575   -328       N  
ATOM   4607  CA  SER B 131      77.929  10.719  11.183  1.00 63.28           C  
ANISOU 4607  CA  SER B 131     7159   7607   9276    176   -574   -289       C  
ATOM   4608  C   SER B 131      78.714  11.861  10.535  1.00 67.44           C  
ANISOU 4608  C   SER B 131     7614   8073   9938    118   -598   -388       C  
ATOM   4609  O   SER B 131      79.943  11.835  10.546  1.00 68.08           O  
ANISOU 4609  O   SER B 131     7629   8172  10068    126   -651   -428       O  
ATOM   4610  CB  SER B 131      77.147   9.941  10.124  1.00 63.92           C  
ANISOU 4610  CB  SER B 131     7292   7602   9391    136   -495   -177       C  
ATOM   4611  OG  SER B 131      77.998   9.473   9.091  1.00 67.82           O  
ANISOU 4611  OG  SER B 131     7773   8033   9963    115   -484   -149       O  
ATOM   4612  N   ILE B 132      77.997  12.883  10.025  1.00 62.98           N  
ANISOU 4612  N   ILE B 132     7052   7438   9441     64   -558   -422       N  
ATOM   4613  CA  ILE B 132      78.561  14.050   9.334  1.00 62.62           C  
ANISOU 4613  CA  ILE B 132     6944   7308   9541      5   -555   -494       C  
ATOM   4614  C   ILE B 132      79.507  14.850  10.286  1.00 67.30           C  
ANISOU 4614  C   ILE B 132     7462   7944  10166     12   -647   -638       C  
ATOM   4615  O   ILE B 132      80.569  15.292   9.841  1.00 67.63           O  
ANISOU 4615  O   ILE B 132     7422   7935  10341    -30   -665   -681       O  
ATOM   4616  CB  ILE B 132      77.413  14.956   8.786  1.00 64.80           C  
ANISOU 4616  CB  ILE B 132     7250   7509   9864    -32   -492   -489       C  
ATOM   4617  CG1 ILE B 132      76.519  14.165   7.792  1.00 64.11           C  
ANISOU 4617  CG1 ILE B 132     7222   7389   9747    -44   -426   -361       C  
ATOM   4618  CG2 ILE B 132      77.979  16.217   8.121  1.00 64.72           C  
ANISOU 4618  CG2 ILE B 132     7177   7397  10015    -87   -475   -548       C  
ATOM   4619  CD1 ILE B 132      75.260  14.876   7.296  1.00 68.82           C  
ANISOU 4619  CD1 ILE B 132     7843   7936  10370    -64   -375   -336       C  
ATOM   4620  N   PHE B 133      79.142  15.015  11.573  1.00 63.64           N  
ANISOU 4620  N   PHE B 133     7025   7575   9582     67   -705   -712       N  
ATOM   4621  CA  PHE B 133      79.972  15.787  12.492  1.00 64.36           C  
ANISOU 4621  CA  PHE B 133     7053   7714   9686     76   -811   -872       C  
ATOM   4622  C   PHE B 133      81.217  15.007  12.882  1.00 68.68           C  
ANISOU 4622  C   PHE B 133     7537   8346  10211    111   -899   -871       C  
ATOM   4623  O   PHE B 133      82.259  15.631  13.055  1.00 69.82           O  
ANISOU 4623  O   PHE B 133     7582   8482  10465     76   -978   -981       O  
ATOM   4624  CB  PHE B 133      79.216  16.222  13.754  1.00 67.04           C  
ANISOU 4624  CB  PHE B 133     7452   8141   9880    140   -847   -964       C  
ATOM   4625  CG  PHE B 133      77.974  17.064  13.541  1.00 68.16           C  
ANISOU 4625  CG  PHE B 133     7645   8208  10047    122   -764   -979       C  
ATOM   4626  CD1 PHE B 133      77.938  18.044  12.554  1.00 70.65           C  
ANISOU 4626  CD1 PHE B 133     7922   8377  10546     42   -717  -1005       C  
ATOM   4627  CD2 PHE B 133      76.921  17.013  14.443  1.00 71.62           C  
ANISOU 4627  CD2 PHE B 133     8159   8725  10328    197   -736   -978       C  
ATOM   4628  CE1 PHE B 133      76.806  18.837  12.370  1.00 72.01           C  
ANISOU 4628  CE1 PHE B 133     8135   8480  10746     39   -642  -1011       C  
ATOM   4629  CE2 PHE B 133      75.806  17.839  14.286  1.00 74.98           C  
ANISOU 4629  CE2 PHE B 133     8618   9084  10787    191   -659   -996       C  
ATOM   4630  CZ  PHE B 133      75.751  18.739  13.240  1.00 72.49           C  
ANISOU 4630  CZ  PHE B 133     8266   8621  10657    114   -616  -1011       C  
ATOM   4631  N   PHE B 134      81.148  13.659  12.984  1.00 64.66           N  
ANISOU 4631  N   PHE B 134     7074   7910   9585    177   -883   -744       N  
ATOM   4632  CA  PHE B 134      82.353  12.879  13.297  1.00 64.72           C  
ANISOU 4632  CA  PHE B 134     7017   7993   9580    224   -959   -725       C  
ATOM   4633  C   PHE B 134      83.266  12.782  12.039  1.00 68.91           C  
ANISOU 4633  C   PHE B 134     7469   8422  10293    161   -913   -676       C  
ATOM   4634  O   PHE B 134      84.480  12.685  12.204  1.00 69.95           O  
ANISOU 4634  O   PHE B 134     7499   8593  10487    174   -984   -706       O  
ATOM   4635  CB  PHE B 134      82.045  11.486  13.864  1.00 65.90           C  
ANISOU 4635  CB  PHE B 134     7241   8238   9560    324   -948   -597       C  
ATOM   4636  CG  PHE B 134      81.637  11.513  15.323  1.00 67.80           C  
ANISOU 4636  CG  PHE B 134     7533   8619   9608    414  -1012   -644       C  
ATOM   4637  CD1 PHE B 134      82.565  11.803  16.317  1.00 72.52           C  
ANISOU 4637  CD1 PHE B 134     8071   9341  10142    472  -1155   -759       C  
ATOM   4638  CD2 PHE B 134      80.368  11.116  15.713  1.00 68.68           C  
ANISOU 4638  CD2 PHE B 134     7751   8751   9593    454   -931   -562       C  
ATOM   4639  CE1 PHE B 134      82.193  11.816  17.668  1.00 74.49           C  
ANISOU 4639  CE1 PHE B 134     8383   9738  10183    573  -1214   -804       C  
ATOM   4640  CE2 PHE B 134      80.000  11.113  17.065  1.00 72.66           C  
ANISOU 4640  CE2 PHE B 134     8309   9395   9904    554   -971   -592       C  
ATOM   4641  CZ  PHE B 134      80.913  11.468  18.033  1.00 72.63           C  
ANISOU 4641  CZ  PHE B 134     8262   9519   9816    619  -1112   -714       C  
ATOM   4642  N   ILE B 135      82.700  12.894  10.807  1.00 64.60           N  
ANISOU 4642  N   ILE B 135     6961   7753   9830     99   -798   -607       N  
ATOM   4643  CA  ILE B 135      83.463  12.985   9.543  1.00 64.06           C  
ANISOU 4643  CA  ILE B 135     6831   7586   9923     46   -734   -563       C  
ATOM   4644  C   ILE B 135      84.277  14.288   9.577  1.00 70.23           C  
ANISOU 4644  C   ILE B 135     7490   8325  10870    -20   -780   -686       C  
ATOM   4645  O   ILE B 135      85.458  14.296   9.215  1.00 71.12           O  
ANISOU 4645  O   ILE B 135     7492   8421  11110    -37   -789   -686       O  
ATOM   4646  CB  ILE B 135      82.518  12.906   8.286  1.00 65.53           C  
ANISOU 4646  CB  ILE B 135     7104   7669  10126      8   -610   -467       C  
ATOM   4647  CG1 ILE B 135      81.896  11.501   8.144  1.00 65.13           C  
ANISOU 4647  CG1 ILE B 135     7156   7643   9948     59   -572   -354       C  
ATOM   4648  CG2 ILE B 135      83.255  13.304   6.988  1.00 65.28           C  
ANISOU 4648  CG2 ILE B 135     7013   7539  10250    -39   -534   -432       C  
ATOM   4649  CD1 ILE B 135      80.810  11.361   7.071  1.00 70.14           C  
ANISOU 4649  CD1 ILE B 135     7879   8197  10575     23   -481   -280       C  
ATOM   4650  N   THR B 136      83.634  15.377  10.051  1.00 67.71           N  
ANISOU 4650  N   THR B 136     7187   7982  10559    -54   -806   -792       N  
ATOM   4651  CA  THR B 136      84.216  16.709  10.197  1.00 69.33           C  
ANISOU 4651  CA  THR B 136     7289   8123  10930   -124   -853   -930       C  
ATOM   4652  C   THR B 136      85.343  16.668  11.245  1.00 76.96           C  
ANISOU 4652  C   THR B 136     8148   9195  11898   -102  -1005  -1047       C  
ATOM   4653  O   THR B 136      86.396  17.255  11.001  1.00 78.08           O  
ANISOU 4653  O   THR B 136     8153   9286  12228   -164  -1038  -1111       O  
ATOM   4654  CB  THR B 136      83.124  17.713  10.569  1.00 74.56           C  
ANISOU 4654  CB  THR B 136     8020   8738  11572   -144   -841  -1013       C  
ATOM   4655  OG1 THR B 136      82.095  17.656   9.585  1.00 67.95           O  
ANISOU 4655  OG1 THR B 136     7267   7818  10734   -156   -712   -892       O  
ATOM   4656  CG2 THR B 136      83.646  19.132  10.695  1.00 74.58           C  
ANISOU 4656  CG2 THR B 136     7929   8647  11762   -220   -883  -1167       C  
ATOM   4657  N   CYS B 137      85.140  15.947  12.382  1.00 75.01           N  
ANISOU 4657  N   CYS B 137     7956   9099  11447     -9  -1095  -1064       N  
ATOM   4658  CA  CYS B 137      86.163  15.788  13.426  1.00 77.30           C  
ANISOU 4658  CA  CYS B 137     8154   9520  11698     36  -1256  -1165       C  
ATOM   4659  C   CYS B 137      87.397  15.116  12.849  1.00 82.06           C  
ANISOU 4659  C   CYS B 137     8634  10129  12416     37  -1259  -1083       C  
ATOM   4660  O   CYS B 137      88.496  15.586  13.109  1.00 83.51           O  
ANISOU 4660  O   CYS B 137     8668  10335  12728      4  -1365  -1186       O  
ATOM   4661  CB  CYS B 137      85.633  15.006  14.621  1.00 78.32           C  
ANISOU 4661  CB  CYS B 137     8385   9812  11562    156  -1322  -1151       C  
ATOM   4662  SG  CYS B 137      84.456  15.920  15.639  1.00 83.07           S  
ANISOU 4662  SG  CYS B 137     9101  10445  12017    179  -1347  -1288       S  
ATOM   4663  N   MET B 138      87.218  14.040  12.051  1.00 77.79           N  
ANISOU 4663  N   MET B 138     8153   9564  11840     74  -1143   -907       N  
ATOM   4664  CA  MET B 138      88.307  13.293  11.415  1.00 78.50           C  
ANISOU 4664  CA  MET B 138     8147   9653  12029     95  -1116   -812       C  
ATOM   4665  C   MET B 138      89.190  14.188  10.533  1.00 82.38           C  
ANISOU 4665  C   MET B 138     8490  10030  12778     -5  -1073   -846       C  
ATOM   4666  O   MET B 138      90.409  14.039  10.573  1.00 82.77           O  
ANISOU 4666  O   MET B 138     8387  10118  12943      0  -1130   -858       O  
ATOM   4667  CB  MET B 138      87.775  12.129  10.558  1.00 79.82           C  
ANISOU 4667  CB  MET B 138     8430   9777  12120    141   -978   -636       C  
ATOM   4668  CG  MET B 138      87.249  10.937  11.361  1.00 83.88           C  
ANISOU 4668  CG  MET B 138     9055  10395  12420    250  -1007   -562       C  
ATOM   4669  SD  MET B 138      88.471  10.198  12.480  1.00 91.00           S  
ANISOU 4669  SD  MET B 138     9854  11463  13257    365  -1154   -567       S  
ATOM   4670  CE  MET B 138      89.834   9.827  11.324  1.00 87.87           C  
ANISOU 4670  CE  MET B 138     9322  10998  13067    357  -1085   -488       C  
ATOM   4671  N   SER B 139      88.586  15.099   9.742  1.00 78.27           N  
ANISOU 4671  N   SER B 139     8009   9373  12356    -90   -968   -849       N  
ATOM   4672  CA  SER B 139      89.341  15.999   8.863  1.00 78.65           C  
ANISOU 4672  CA  SER B 139     7928   9299  12658   -184   -899   -857       C  
ATOM   4673  C   SER B 139      90.138  17.030   9.688  1.00 83.81           C  
ANISOU 4673  C   SER B 139     8422   9959  13466   -252  -1039  -1034       C  
ATOM   4674  O   SER B 139      91.282  17.324   9.341  1.00 83.93           O  
ANISOU 4674  O   SER B 139     8264   9933  13692   -303  -1037  -1039       O  
ATOM   4675  CB  SER B 139      88.411  16.706   7.884  1.00 81.25           C  
ANISOU 4675  CB  SER B 139     8352   9488  13033   -240   -757   -806       C  
ATOM   4676  OG  SER B 139      87.782  15.766   7.030  1.00 89.51           O  
ANISOU 4676  OG  SER B 139     9528  10527  13954   -186   -642   -656       O  
ATOM   4677  N   VAL B 140      89.548  17.537  10.793  1.00 80.95           N  
ANISOU 4677  N   VAL B 140     8112   9650  12996   -248  -1162  -1183       N  
ATOM   4678  CA  VAL B 140      90.182  18.493  11.713  1.00 82.68           C  
ANISOU 4678  CA  VAL B 140     8201   9882  13330   -308  -1323  -1388       C  
ATOM   4679  C   VAL B 140      91.329  17.780  12.460  1.00 88.71           C  
ANISOU 4679  C   VAL B 140     8835  10807  14062   -248  -1481  -1423       C  
ATOM   4680  O   VAL B 140      92.387  18.382  12.657  1.00 90.10           O  
ANISOU 4680  O   VAL B 140     8823  10972  14439   -316  -1579  -1531       O  
ATOM   4681  CB  VAL B 140      89.144  19.115  12.695  1.00 86.39           C  
ANISOU 4681  CB  VAL B 140     8794  10372  13657   -298  -1397  -1538       C  
ATOM   4682  CG1 VAL B 140      89.817  19.961  13.775  1.00 88.59           C  
ANISOU 4682  CG1 VAL B 140     8959  10690  14013   -341  -1591  -1777       C  
ATOM   4683  CG2 VAL B 140      88.101  19.935  11.944  1.00 84.87           C  
ANISOU 4683  CG2 VAL B 140     8700  10012  13537   -357  -1246  -1506       C  
ATOM   4684  N   ASP B 141      91.129  16.487  12.828  1.00 84.88           N  
ANISOU 4684  N   ASP B 141     8443  10466  13343   -120  -1500  -1320       N  
ATOM   4685  CA  ASP B 141      92.116  15.664  13.538  1.00 85.84           C  
ANISOU 4685  CA  ASP B 141     8459  10751  13404    -34  -1640  -1320       C  
ATOM   4686  C   ASP B 141      93.297  15.331  12.618  1.00 90.01           C  
ANISOU 4686  C   ASP B 141     8817  11234  14148    -56  -1574  -1214       C  
ATOM   4687  O   ASP B 141      94.445  15.507  13.034  1.00 91.97           O  
ANISOU 4687  O   ASP B 141     8873  11553  14518    -66  -1708  -1291       O  
ATOM   4688  CB  ASP B 141      91.479  14.374  14.080  1.00 86.71           C  
ANISOU 4688  CB  ASP B 141     8726  10995  13223    112  -1641  -1206       C  
ATOM   4689  CG  ASP B 141      92.420  13.548  14.933  1.00 99.49           C  
ANISOU 4689  CG  ASP B 141    10249  12791  14762    222  -1789  -1193       C  
ATOM   4690  OD1 ASP B 141      92.686  13.954  16.092  1.00102.45           O  
ANISOU 4690  OD1 ASP B 141    10576  13296  15055    250  -1981  -1348       O  
ATOM   4691  OD2 ASP B 141      92.865  12.477  14.459  1.00103.78           O  
ANISOU 4691  OD2 ASP B 141    10770  13346  15316    289  -1715  -1031       O  
ATOM   4692  N   ARG B 142      93.020  14.864  11.372  1.00 84.30           N  
ANISOU 4692  N   ARG B 142     8159  10402  13470    -59  -1370  -1043       N  
ATOM   4693  CA  ARG B 142      94.060  14.556  10.386  1.00 84.31           C  
ANISOU 4693  CA  ARG B 142     8018  10351  13665    -69  -1270   -931       C  
ATOM   4694  C   ARG B 142      94.855  15.810  10.029  1.00 92.07           C  
ANISOU 4694  C   ARG B 142     8802  11230  14952   -203  -1275  -1023       C  
ATOM   4695  O   ARG B 142      96.065  15.707   9.862  1.00 94.16           O  
ANISOU 4695  O   ARG B 142     8865  11520  15393   -210  -1303  -1008       O  
ATOM   4696  CB  ARG B 142      93.490  13.923   9.109  1.00 80.37           C  
ANISOU 4696  CB  ARG B 142     7655   9753  13128    -42  -1050   -751       C  
ATOM   4697  CG  ARG B 142      93.095  12.458   9.243  1.00 83.62           C  
ANISOU 4697  CG  ARG B 142     8211  10246  13313     90  -1026   -632       C  
ATOM   4698  CD  ARG B 142      92.648  11.910   7.900  1.00 88.90           C  
ANISOU 4698  CD  ARG B 142     8992  10808  13976    105   -822   -483       C  
ATOM   4699  NE  ARG B 142      92.477  10.456   7.923  1.00 96.14           N  
ANISOU 4699  NE  ARG B 142    10026  11778  14723    225   -792   -373       N  
ATOM   4700  CZ  ARG B 142      92.111   9.727   6.871  1.00106.81           C  
ANISOU 4700  CZ  ARG B 142    11492  13053  16040    260   -637   -256       C  
ATOM   4701  NH1 ARG B 142      91.862  10.308   5.703  1.00 87.55           N  
ANISOU 4701  NH1 ARG B 142     9068  10498  13697    196   -498   -224       N  
ATOM   4702  NH2 ARG B 142      91.984   8.411   6.981  1.00 95.05           N  
ANISOU 4702  NH2 ARG B 142    10103  11597  14415    364   -620   -171       N  
ATOM   4703  N   TYR B 143      94.195  16.990   9.948  1.00 89.81           N  
ANISOU 4703  N   TYR B 143     8562  10820  14740   -309  -1247  -1117       N  
ATOM   4704  CA  TYR B 143      94.866  18.262   9.656  1.00 92.09           C  
ANISOU 4704  CA  TYR B 143     8673  10980  15336   -448  -1244  -1209       C  
ATOM   4705  C   TYR B 143      95.807  18.640  10.800  1.00100.48           C  
ANISOU 4705  C   TYR B 143     9543  12139  16495   -482  -1480  -1398       C  
ATOM   4706  O   TYR B 143      96.961  18.975  10.542  1.00101.96           O  
ANISOU 4706  O   TYR B 143     9502  12291  16949   -550  -1493  -1409       O  
ATOM   4707  CB  TYR B 143      93.850  19.395   9.397  1.00 93.06           C  
ANISOU 4707  CB  TYR B 143     8914  10952  15495   -534  -1173  -1272       C  
ATOM   4708  CG  TYR B 143      94.480  20.770   9.323  1.00 97.46           C  
ANISOU 4708  CG  TYR B 143     9297  11362  16372   -680  -1191  -1393       C  
ATOM   4709  CD1 TYR B 143      95.209  21.165   8.205  1.00 99.92           C  
ANISOU 4709  CD1 TYR B 143     9478  11530  16957   -754  -1023  -1276       C  
ATOM   4710  CD2 TYR B 143      94.304  21.696  10.347  1.00100.04           C  
ANISOU 4710  CD2 TYR B 143     9598  11681  16730   -742  -1363  -1624       C  
ATOM   4711  CE1 TYR B 143      95.814  22.419   8.144  1.00102.79           C  
ANISOU 4711  CE1 TYR B 143     9670  11740  17644   -896  -1028  -1376       C  
ATOM   4712  CE2 TYR B 143      94.892  22.959  10.291  1.00103.14           C  
ANISOU 4712  CE2 TYR B 143     9830  11916  17444   -887  -1382  -1748       C  
ATOM   4713  CZ  TYR B 143      95.646  23.317   9.185  1.00111.56           C  
ANISOU 4713  CZ  TYR B 143    10752  12830  18803   -969  -1210  -1616       C  
ATOM   4714  OH  TYR B 143      96.227  24.561   9.120  1.00115.09           O  
ANISOU 4714  OH  TYR B 143    11032  13102  19594  -1119  -1214  -1724       O  
ATOM   4715  N   GLN B 144      95.326  18.541  12.056  1.00 98.50           N  
ANISOU 4715  N   GLN B 144     9382  12020  16022   -426  -1664  -1540       N  
ATOM   4716  CA  GLN B 144      96.082  18.864  13.267  1.00101.15           C  
ANISOU 4716  CA  GLN B 144     9570  12477  16385   -438  -1920  -1744       C  
ATOM   4717  C   GLN B 144      97.276  17.880  13.434  1.00108.38           C  
ANISOU 4717  C   GLN B 144    10315  13547  17319   -355  -2008  -1669       C  
ATOM   4718  O   GLN B 144      98.270  18.236  14.065  1.00110.21           O  
ANISOU 4718  O   GLN B 144    10342  13854  17678   -392  -2201  -1812       O  
ATOM   4719  CB  GLN B 144      95.136  18.819  14.482  1.00102.08           C  
ANISOU 4719  CB  GLN B 144     9872  12716  16197   -361  -2060  -1877       C  
ATOM   4720  CG  GLN B 144      95.695  19.418  15.769  1.00119.66           C  
ANISOU 4720  CG  GLN B 144    11986  15052  18428   -383  -2331  -2136       C  
ATOM   4721  CD  GLN B 144      94.679  19.498  16.891  1.00134.95           C  
ANISOU 4721  CD  GLN B 144    14123  17093  20058   -303  -2436  -2268       C  
ATOM   4722  OE1 GLN B 144      94.904  20.170  17.903  1.00135.07           O  
ANISOU 4722  OE1 GLN B 144    14096  17158  20066   -333  -2632  -2511       O  
ATOM   4723  NE2 GLN B 144      93.524  18.862  16.730  1.00117.33           N  
ANISOU 4723  NE2 GLN B 144    12114  14887  17577   -204  -2302  -2121       N  
ATOM   4724  N   SER B 145      97.186  16.673  12.827  1.00105.17           N  
ANISOU 4724  N   SER B 145     9983  13177  16800   -246  -1866  -1449       N  
ATOM   4725  CA  SER B 145      98.246  15.658  12.840  1.00106.86           C  
ANISOU 4725  CA  SER B 145    10050  13516  17036   -149  -1909  -1345       C  
ATOM   4726  C   SER B 145      99.324  15.964  11.799  1.00114.96           C  
ANISOU 4726  C   SER B 145    10846  14430  18405   -234  -1791  -1269       C  
ATOM   4727  O   SER B 145     100.480  15.584  11.984  1.00116.50           O  
ANISOU 4727  O   SER B 145    10822  14717  18724   -203  -1882  -1258       O  
ATOM   4728  CB  SER B 145      97.665  14.273  12.581  1.00107.94           C  
ANISOU 4728  CB  SER B 145    10375  13712  16924      3  -1793  -1149       C  
ATOM   4729  OG  SER B 145      96.730  13.910  13.579  1.00115.94           O  
ANISOU 4729  OG  SER B 145    11583  14837  17632     90  -1891  -1195       O  
ATOM   4730  N   VAL B 146      98.941  16.633  10.697  1.00113.17           N  
ANISOU 4730  N   VAL B 146    10664  14007  18326   -333  -1582  -1206       N  
ATOM   4731  CA  VAL B 146      99.850  16.992   9.608  1.00115.15           C  
ANISOU 4731  CA  VAL B 146    10722  14134  18896   -411  -1424  -1109       C  
ATOM   4732  C   VAL B 146     100.619  18.285   9.983  1.00125.26           C  
ANISOU 4732  C   VAL B 146    11756  15348  20490   -572  -1553  -1289       C  
ATOM   4733  O   VAL B 146     101.848  18.252  10.021  1.00126.74           O  
ANISOU 4733  O   VAL B 146    11679  15581  20896   -592  -1617  -1292       O  
ATOM   4734  CB  VAL B 146      99.090  17.146   8.255  1.00116.84           C  
ANISOU 4734  CB  VAL B 146    11101  14176  19118   -437  -1148   -959       C  
ATOM   4735  CG1 VAL B 146      99.974  17.755   7.178  1.00117.87           C  
ANISOU 4735  CG1 VAL B 146    11036  14165  19585   -528   -974   -868       C  
ATOM   4736  CG2 VAL B 146      98.517  15.815   7.785  1.00114.39           C  
ANISOU 4736  CG2 VAL B 146    10997  13922  18543   -288  -1025   -788       C  
ATOM   4737  N   ILE B 147      99.899  19.405  10.257  1.00125.10           N  
ANISOU 4737  N   ILE B 147    11816  15214  20504   -683  -1588  -1440       N  
ATOM   4738  CA  ILE B 147     100.490  20.714  10.573  1.00129.21           C  
ANISOU 4738  CA  ILE B 147    12130  15628  21335   -851  -1697  -1627       C  
ATOM   4739  C   ILE B 147     101.304  20.613  11.917  1.00139.73           C  
ANISOU 4739  C   ILE B 147    13287  17145  22658   -839  -2016  -1828       C  
ATOM   4740  O   ILE B 147     102.401  21.177  11.984  1.00142.40           O  
ANISOU 4740  O   ILE B 147    13342  17451  23311   -945  -2102  -1909       O  
ATOM   4741  CB  ILE B 147      99.408  21.857  10.619  1.00131.99           C  
ANISOU 4741  CB  ILE B 147    12650  15817  21685   -946  -1663  -1747       C  
ATOM   4742  CG1 ILE B 147     100.024  23.271  10.815  1.00135.55           C  
ANISOU 4742  CG1 ILE B 147    12891  16107  22506  -1133  -1742  -1933       C  
ATOM   4743  CG2 ILE B 147      98.289  21.611  11.624  1.00131.75           C  
ANISOU 4743  CG2 ILE B 147    12863  15905  21292   -857  -1800  -1866       C  
ATOM   4744  CD1 ILE B 147     100.900  23.808   9.648  1.00146.48           C  
ANISOU 4744  CD1 ILE B 147    14067  17302  24287  -1247  -1529  -1786       C  
ATOM   4745  N   TYR B 148     100.810  19.862  12.932  1.00138.40           N  
ANISOU 4745  N   TYR B 148    13276  17174  22137   -704  -2182  -1890       N  
ATOM   4746  CA  TYR B 148     101.538  19.665  14.198  1.00141.87           C  
ANISOU 4746  CA  TYR B 148    13573  17818  22512   -661  -2488  -2063       C  
ATOM   4747  C   TYR B 148     101.838  18.158  14.389  1.00146.83           C  
ANISOU 4747  C   TYR B 148    14225  18655  22909   -467  -2510  -1894       C  
ATOM   4748  O   TYR B 148     100.979  17.423  14.886  1.00144.90           O  
ANISOU 4748  O   TYR B 148    14214  18526  22316   -332  -2533  -1857       O  
ATOM   4749  CB  TYR B 148     100.765  20.238  15.412  1.00144.04           C  
ANISOU 4749  CB  TYR B 148    14003  18155  22572   -662  -2692  -2311       C  
ATOM   4750  CG  TYR B 148     100.416  21.705  15.290  1.00147.24           C  
ANISOU 4750  CG  TYR B 148    14410  18342  23192   -837  -2668  -2485       C  
ATOM   4751  CD1 TYR B 148     101.346  22.692  15.600  1.00152.44           C  
ANISOU 4751  CD1 TYR B 148    14811  18923  24187   -995  -2815  -2684       C  
ATOM   4752  CD2 TYR B 148      99.130  22.107  14.943  1.00146.14           C  
ANISOU 4752  CD2 TYR B 148    14530  18079  22918   -841  -2514  -2465       C  
ATOM   4753  CE1 TYR B 148     101.027  24.045  15.494  1.00154.62           C  
ANISOU 4753  CE1 TYR B 148    15093  18975  24680  -1156  -2785  -2845       C  
ATOM   4754  CE2 TYR B 148      98.799  23.455  14.828  1.00148.01           C  
ANISOU 4754  CE2 TYR B 148    14774  18105  23357   -988  -2484  -2617       C  
ATOM   4755  CZ  TYR B 148      99.750  24.423  15.109  1.00159.47           C  
ANISOU 4755  CZ  TYR B 148    15976  19460  25153  -1146  -2616  -2807       C  
ATOM   4756  OH  TYR B 148      99.421  25.754  15.017  1.00162.10           O  
ANISOU 4756  OH  TYR B 148    16322  19566  25702  -1290  -2581  -2960       O  
ATOM   4757  N   PRO B 149     103.046  17.673  13.996  1.00146.02           N  
ANISOU 4757  N   PRO B 149    13877  18596  23007   -446  -2492  -1780       N  
ATOM   4758  CA  PRO B 149     103.335  16.227  14.113  1.00145.61           C  
ANISOU 4758  CA  PRO B 149    13851  18719  22756   -252  -2489  -1604       C  
ATOM   4759  C   PRO B 149     103.387  15.724  15.568  1.00150.98           C  
ANISOU 4759  C   PRO B 149    14550  19651  23167   -123  -2780  -1720       C  
ATOM   4760  O   PRO B 149     103.128  14.541  15.801  1.00149.57           O  
ANISOU 4760  O   PRO B 149    14495  19602  22733     55  -2762  -1574       O  
ATOM   4761  CB  PRO B 149     104.716  16.092  13.465  1.00149.18           C  
ANISOU 4761  CB  PRO B 149    13991  19152  23539   -279  -2429  -1500       C  
ATOM   4762  CG  PRO B 149     104.870  17.315  12.607  1.00153.91           C  
ANISOU 4762  CG  PRO B 149    14481  19518  24479   -478  -2281  -1534       C  
ATOM   4763  CD  PRO B 149     104.168  18.392  13.358  1.00149.78           C  
ANISOU 4763  CD  PRO B 149    14048  18947  23915   -592  -2439  -1782       C  
ATOM   4764  N   PHE B 150     103.741  16.616  16.534  1.00149.87           N  
ANISOU 4764  N   PHE B 150    14286  19573  23084   -209  -3044  -1981       N  
ATOM   4765  CA  PHE B 150     103.870  16.384  17.985  1.00176.64           C  
ANISOU 4765  CA  PHE B 150    17676  23211  26229   -101  -3356  -2138       C  
ATOM   4766  C   PHE B 150     105.095  15.502  18.277  1.00203.01           C  
ANISOU 4766  C   PHE B 150    20774  26741  29618     17  -3489  -2048       C  
ATOM   4767  O   PHE B 150     105.282  14.431  17.701  1.00161.95           O  
ANISOU 4767  O   PHE B 150    15613  21581  24341    156  -3343  -1807       O  
ATOM   4768  CB  PHE B 150     102.600  15.763  18.610  1.00176.40           C  
ANISOU 4768  CB  PHE B 150    17988  23280  25758     50  -3342  -2098       C  
ATOM   4769  N   TRP B 158      92.448  14.312  26.760  1.00145.59           N  
ANISOU 4769  N   TRP B 158    16435  20357  18525   1154  -3413  -2292       N  
ATOM   4770  CA  TRP B 158      91.275  14.981  27.316  1.00145.69           C  
ANISOU 4770  CA  TRP B 158    16630  20369  18359   1165  -3382  -2445       C  
ATOM   4771  C   TRP B 158      90.373  15.596  26.235  1.00145.32           C  
ANISOU 4771  C   TRP B 158    16646  20046  18524   1004  -3149  -2428       C  
ATOM   4772  O   TRP B 158      89.177  15.741  26.485  1.00144.18           O  
ANISOU 4772  O   TRP B 158    16687  19887  18208   1052  -3021  -2412       O  
ATOM   4773  CB  TRP B 158      91.690  16.085  28.289  1.00148.03           C  
ANISOU 4773  CB  TRP B 158    16861  20768  18616   1144  -3652  -2797       C  
ATOM   4774  CG  TRP B 158      92.211  15.571  29.593  1.00152.44           C  
ANISOU 4774  CG  TRP B 158    17438  21641  18840   1347  -3882  -2847       C  
ATOM   4775  CD1 TRP B 158      93.460  15.088  29.842  1.00157.30           C  
ANISOU 4775  CD1 TRP B 158    17881  22420  19467   1410  -4086  -2828       C  
ATOM   4776  CD2 TRP B 158      91.525  15.582  30.855  1.00154.13           C  
ANISOU 4776  CD2 TRP B 158    17855  22058  18651   1526  -3937  -2929       C  
ATOM   4777  NE1 TRP B 158      93.583  14.753  31.173  1.00159.58           N  
ANISOU 4777  NE1 TRP B 158    18254  23005  19374   1620  -4275  -2888       N  
ATOM   4778  CE2 TRP B 158      92.414  15.056  31.820  1.00161.04           C  
ANISOU 4778  CE2 TRP B 158    18675  23221  19291   1696  -4183  -2952       C  
ATOM   4779  CE3 TRP B 158      90.233  15.961  31.260  1.00154.89           C  
ANISOU 4779  CE3 TRP B 158    18172  22124  18553   1570  -3792  -2972       C  
ATOM   4780  CZ2 TRP B 158      92.047  14.881  33.160  1.00162.75           C  
ANISOU 4780  CZ2 TRP B 158    19065  23703  19072   1914  -4284  -3011       C  
ATOM   4781  CZ3 TRP B 158      89.878  15.807  32.592  1.00158.77           C  
ANISOU 4781  CZ3 TRP B 158    18829  22872  18626   1781  -3883  -3037       C  
ATOM   4782  CH2 TRP B 158      90.779  15.277  33.527  1.00162.32           C  
ANISOU 4782  CH2 TRP B 158    19233  23611  18832   1952  -4126  -3056       C  
ATOM   4783  N   GLN B 159      90.926  15.964  25.051  1.00138.98           N  
ANISOU 4783  N   GLN B 159    15688  19033  18087    823  -3091  -2427       N  
ATOM   4784  CA  GLN B 159      90.132  16.591  23.981  1.00135.37           C  
ANISOU 4784  CA  GLN B 159    15282  18319  17834    677  -2879  -2405       C  
ATOM   4785  C   GLN B 159      88.965  15.677  23.505  1.00133.17           C  
ANISOU 4785  C   GLN B 159    15176  17993  17432    741  -2630  -2133       C  
ATOM   4786  O   GLN B 159      87.890  16.197  23.248  1.00131.37           O  
ANISOU 4786  O   GLN B 159    15065  17645  17207    696  -2488  -2144       O  
ATOM   4787  CB  GLN B 159      91.005  16.978  22.766  1.00136.17           C  
ANISOU 4787  CB  GLN B 159    15187  18223  18330    497  -2843  -2401       C  
ATOM   4788  CG  GLN B 159      91.746  15.823  22.065  1.00154.00           C  
ANISOU 4788  CG  GLN B 159    17342  20486  20685    521  -2775  -2158       C  
ATOM   4789  CD  GLN B 159      92.563  16.275  20.871  1.00174.42           C  
ANISOU 4789  CD  GLN B 159    19744  22879  23648    355  -2713  -2150       C  
ATOM   4790  OE1 GLN B 159      93.049  17.411  20.796  1.00171.19           O  
ANISOU 4790  OE1 GLN B 159    19206  22381  23456    225  -2806  -2351       O  
ATOM   4791  NE2 GLN B 159      92.812  15.359  19.947  1.00165.70           N  
ANISOU 4791  NE2 GLN B 159    18616  21709  22632    362  -2557  -1915       N  
ATOM   4792  N   ALA B 160      89.164  14.348  23.413  1.00126.71           N  
ANISOU 4792  N   ALA B 160    14365  17262  16515    847  -2583  -1898       N  
ATOM   4793  CA  ALA B 160      88.129  13.418  22.940  1.00123.02           C  
ANISOU 4793  CA  ALA B 160    14042  16737  15962    897  -2359  -1643       C  
ATOM   4794  C   ALA B 160      87.007  13.214  23.972  1.00124.08           C  
ANISOU 4794  C   ALA B 160    14369  16999  15778   1034  -2316  -1618       C  
ATOM   4795  O   ALA B 160      85.856  13.063  23.574  1.00121.55           O  
ANISOU 4795  O   ALA B 160    14167  16578  15437   1018  -2125  -1497       O  
ATOM   4796  CB  ALA B 160      88.748  12.074  22.606  1.00123.42           C  
ANISOU 4796  CB  ALA B 160    14041  16835  16020    973  -2332  -1418       C  
ATOM   4797  N   SER B 161      87.334  13.210  25.283  1.00121.15           N  
ANISOU 4797  N   SER B 161    14023  16851  15156   1172  -2491  -1727       N  
ATOM   4798  CA  SER B 161      86.364  12.987  26.361  1.00120.62           C  
ANISOU 4798  CA  SER B 161    14140  16932  14760   1328  -2448  -1695       C  
ATOM   4799  C   SER B 161      85.363  14.166  26.492  1.00121.91           C  
ANISOU 4799  C   SER B 161    14397  17011  14912   1267  -2389  -1877       C  
ATOM   4800  O   SER B 161      84.365  14.031  27.206  1.00121.90           O  
ANISOU 4800  O   SER B 161    14550  17103  14663   1385  -2308  -1840       O  
ATOM   4801  CB  SER B 161      87.078  12.768  27.691  1.00126.87           C  
ANISOU 4801  CB  SER B 161    14931  17998  15276   1502  -2664  -1772       C  
ATOM   4802  OG  SER B 161      87.837  13.904  28.066  1.00137.77           O  
ANISOU 4802  OG  SER B 161    16210  19424  16711   1444  -2893  -2080       O  
ATOM   4803  N   TYR B 162      85.603  15.293  25.777  1.00115.99           N  
ANISOU 4803  N   TYR B 162    13554  16077  14439   1090  -2409  -2053       N  
ATOM   4804  CA  TYR B 162      84.698  16.446  25.778  1.00114.59           C  
ANISOU 4804  CA  TYR B 162    13456  15789  14295   1027  -2342  -2219       C  
ATOM   4805  C   TYR B 162      84.112  16.686  24.361  1.00112.31           C  
ANISOU 4805  C   TYR B 162    13143  15238  14290    868  -2145  -2114       C  
ATOM   4806  O   TYR B 162      82.941  17.060  24.266  1.00110.86           O  
ANISOU 4806  O   TYR B 162    13067  14976  14080    863  -2003  -2107       O  
ATOM   4807  CB  TYR B 162      85.393  17.720  26.298  1.00118.53           C  
ANISOU 4807  CB  TYR B 162    13884  16301  14853    973  -2554  -2557       C  
ATOM   4808  CG  TYR B 162      85.805  17.614  27.753  1.00124.14           C  
ANISOU 4808  CG  TYR B 162    14640  17282  15247   1141  -2759  -2693       C  
ATOM   4809  CD1 TYR B 162      84.904  17.897  28.778  1.00127.57           C  
ANISOU 4809  CD1 TYR B 162    15253  17845  15373   1285  -2732  -2766       C  
ATOM   4810  CD2 TYR B 162      87.089  17.215  28.107  1.00126.81           C  
ANISOU 4810  CD2 TYR B 162    14842  17759  15583   1167  -2979  -2745       C  
ATOM   4811  CE1 TYR B 162      85.267  17.763  30.118  1.00131.40           C  
ANISOU 4811  CE1 TYR B 162    15796  18599  15533   1460  -2917  -2881       C  
ATOM   4812  CE2 TYR B 162      87.462  17.075  29.443  1.00130.78           C  
ANISOU 4812  CE2 TYR B 162    15389  18531  15772   1337  -3180  -2861       C  
ATOM   4813  CZ  TYR B 162      86.549  17.353  30.446  1.00140.21           C  
ANISOU 4813  CZ  TYR B 162    16777  19857  16640   1485  -3150  -2931       C  
ATOM   4814  OH  TYR B 162      86.925  17.222  31.763  1.00145.08           O  
ANISOU 4814  OH  TYR B 162    17450  20754  16922   1667  -3349  -3046       O  
ATOM   4815  N   ILE B 163      84.890  16.420  23.273  1.00104.86           N  
ANISOU 4815  N   ILE B 163    12066  14175  13601    755  -2129  -2019       N  
ATOM   4816  CA  ILE B 163      84.424  16.608  21.886  1.00100.75           C  
ANISOU 4816  CA  ILE B 163    11526  13426  13331    618  -1950  -1911       C  
ATOM   4817  C   ILE B 163      83.370  15.533  21.546  1.00 99.40           C  
ANISOU 4817  C   ILE B 163    11472  13248  13047    679  -1759  -1651       C  
ATOM   4818  O   ILE B 163      82.327  15.895  21.013  1.00 98.07           O  
ANISOU 4818  O   ILE B 163    11375  12964  12922    635  -1616  -1615       O  
ATOM   4819  CB  ILE B 163      85.587  16.609  20.839  1.00103.20           C  
ANISOU 4819  CB  ILE B 163    11663  13622  13927    496  -1980  -1884       C  
ATOM   4820  CG1 ILE B 163      86.446  17.896  20.988  1.00105.35           C  
ANISOU 4820  CG1 ILE B 163    11804  13841  14382    395  -2138  -2148       C  
ATOM   4821  CG2 ILE B 163      85.043  16.515  19.399  1.00101.43           C  
ANISOU 4821  CG2 ILE B 163    11447  13194  13898    392  -1779  -1724       C  
ATOM   4822  CD1 ILE B 163      87.702  17.996  20.067  1.00112.36           C  
ANISOU 4822  CD1 ILE B 163    12494  14636  15563    280  -2179  -2134       C  
ATOM   4823  N   VAL B 164      83.620  14.243  21.866  1.00 93.20           N  
ANISOU 4823  N   VAL B 164    10702  12583  12128    781  -1760  -1473       N  
ATOM   4824  CA  VAL B 164      82.683  13.145  21.568  1.00 90.36           C  
ANISOU 4824  CA  VAL B 164    10442  12206  11684    832  -1586  -1226       C  
ATOM   4825  C   VAL B 164      81.286  13.437  22.233  1.00 93.07           C  
ANISOU 4825  C   VAL B 164    10926  12589  11847    898  -1487  -1228       C  
ATOM   4826  O   VAL B 164      80.308  13.415  21.481  1.00 91.01           O  
ANISOU 4826  O   VAL B 164    10708  12200  11671    837  -1329  -1125       O  
ATOM   4827  CB  VAL B 164      83.221  11.751  21.978  1.00 94.38           C  
ANISOU 4827  CB  VAL B 164    10953  12845  12061    953  -1616  -1054       C  
ATOM   4828  CG1 VAL B 164      82.146  10.677  21.836  1.00 92.97           C  
ANISOU 4828  CG1 VAL B 164    10888  12645  11790   1008  -1437   -816       C  
ATOM   4829  CG2 VAL B 164      84.458  11.380  21.163  1.00 93.77           C  
ANISOU 4829  CG2 VAL B 164    10738  12706  12183    890  -1669  -1018       C  
ATOM   4830  N   PRO B 165      81.138  13.768  23.562  1.00 90.45           N  
ANISOU 4830  N   PRO B 165    10663  12426  11277   1020  -1571  -1348       N  
ATOM   4831  CA  PRO B 165      79.788  14.069  24.091  1.00 89.56           C  
ANISOU 4831  CA  PRO B 165    10677  12338  11013   1085  -1447  -1338       C  
ATOM   4832  C   PRO B 165      79.163  15.301  23.431  1.00 90.80           C  
ANISOU 4832  C   PRO B 165    10828  12325  11347    968  -1383  -1472       C  
ATOM   4833  O   PRO B 165      77.958  15.313  23.200  1.00 89.13           O  
ANISOU 4833  O   PRO B 165    10685  12056  11125    971  -1224  -1381       O  
ATOM   4834  CB  PRO B 165      80.037  14.325  25.584  1.00 93.98           C  
ANISOU 4834  CB  PRO B 165    11301  13119  11287   1242  -1577  -1477       C  
ATOM   4835  CG  PRO B 165      81.328  13.673  25.881  1.00 99.54           C  
ANISOU 4835  CG  PRO B 165    11926  13940  11954   1287  -1745  -1470       C  
ATOM   4836  CD  PRO B 165      82.145  13.847  24.642  1.00 94.02           C  
ANISOU 4836  CD  PRO B 165    11084  13065  11573   1117  -1777  -1492       C  
ATOM   4837  N   LEU B 166      79.991  16.311  23.093  1.00 87.46           N  
ANISOU 4837  N   LEU B 166    10313  11816  11104    864  -1503  -1675       N  
ATOM   4838  CA  LEU B 166      79.579  17.559  22.448  1.00 86.98           C  
ANISOU 4838  CA  LEU B 166    10236  11576  11237    752  -1452  -1806       C  
ATOM   4839  C   LEU B 166      79.055  17.312  21.017  1.00 88.70           C  
ANISOU 4839  C   LEU B 166    10422  11610  11670    639  -1295  -1626       C  
ATOM   4840  O   LEU B 166      78.107  17.977  20.605  1.00 88.50           O  
ANISOU 4840  O   LEU B 166    10429  11467  11730    596  -1186  -1638       O  
ATOM   4841  CB  LEU B 166      80.768  18.530  22.409  1.00 88.64           C  
ANISOU 4841  CB  LEU B 166    10338  11732  11608    664  -1623  -2047       C  
ATOM   4842  CG  LEU B 166      80.517  19.954  21.922  1.00 94.00           C  
ANISOU 4842  CG  LEU B 166    10997  12222  12496    556  -1594  -2217       C  
ATOM   4843  CD1 LEU B 166      79.680  20.743  22.937  1.00 96.00           C  
ANISOU 4843  CD1 LEU B 166    11372  12529  12574    653  -1581  -2375       C  
ATOM   4844  CD2 LEU B 166      81.833  20.677  21.702  1.00 97.78           C  
ANISOU 4844  CD2 LEU B 166    11339  12627  13186    447  -1753  -2408       C  
ATOM   4845  N   VAL B 167      79.672  16.374  20.264  1.00 83.38           N  
ANISOU 4845  N   VAL B 167     9687  10916  11076    600  -1286  -1464       N  
ATOM   4846  CA  VAL B 167      79.261  16.038  18.889  1.00 80.71           C  
ANISOU 4846  CA  VAL B 167     9328  10424  10916    504  -1153  -1298       C  
ATOM   4847  C   VAL B 167      77.874  15.355  18.938  1.00 82.90           C  
ANISOU 4847  C   VAL B 167     9705  10718  11076    560  -1002  -1126       C  
ATOM   4848  O   VAL B 167      77.015  15.671  18.112  1.00 81.07           O  
ANISOU 4848  O   VAL B 167     9483  10362  10958    494   -891  -1071       O  
ATOM   4849  CB  VAL B 167      80.313  15.166  18.153  1.00 83.96           C  
ANISOU 4849  CB  VAL B 167     9657  10817  11425    466  -1185  -1190       C  
ATOM   4850  CG1 VAL B 167      79.789  14.686  16.809  1.00 82.05           C  
ANISOU 4850  CG1 VAL B 167     9421  10439  11317    391  -1046  -1019       C  
ATOM   4851  CG2 VAL B 167      81.613  15.933  17.955  1.00 84.54           C  
ANISOU 4851  CG2 VAL B 167     9607  10852  11664    393  -1312  -1347       C  
ATOM   4852  N   TRP B 168      77.647  14.469  19.932  1.00 80.22           N  
ANISOU 4852  N   TRP B 168     9432  10533  10514    683   -999  -1041       N  
ATOM   4853  CA  TRP B 168      76.348  13.820  20.145  1.00 79.59           C  
ANISOU 4853  CA  TRP B 168     9434  10478  10329    740   -853   -878       C  
ATOM   4854  C   TRP B 168      75.322  14.828  20.695  1.00 87.65           C  
ANISOU 4854  C   TRP B 168    10509  11506  11289    776   -794   -982       C  
ATOM   4855  O   TRP B 168      74.118  14.642  20.514  1.00 86.25           O  
ANISOU 4855  O   TRP B 168    10367  11295  11110    782   -656   -865       O  
ATOM   4856  CB  TRP B 168      76.461  12.614  21.090  1.00 78.31           C  
ANISOU 4856  CB  TRP B 168     9324  10474   9955    870   -853   -745       C  
ATOM   4857  CG  TRP B 168      77.149  11.425  20.489  1.00 77.72           C  
ANISOU 4857  CG  TRP B 168     9210  10372   9948    848   -865   -598       C  
ATOM   4858  CD1 TRP B 168      78.440  11.034  20.686  1.00 81.19           C  
ANISOU 4858  CD1 TRP B 168     9600  10879  10371    880   -993   -629       C  
ATOM   4859  CD2 TRP B 168      76.590  10.503  19.547  1.00 75.67           C  
ANISOU 4859  CD2 TRP B 168     8954  10001   9794    790   -747   -408       C  
ATOM   4860  NE1 TRP B 168      78.704   9.894  19.968  1.00 79.48           N  
ANISOU 4860  NE1 TRP B 168     9364  10600  10236    858   -947   -460       N  
ATOM   4861  CE2 TRP B 168      77.590   9.556  19.243  1.00 79.43           C  
ANISOU 4861  CE2 TRP B 168     9396  10479  10307    798   -800   -332       C  
ATOM   4862  CE3 TRP B 168      75.335  10.388  18.922  1.00 75.44           C  
ANISOU 4862  CE3 TRP B 168     8950   9872   9841    731   -609   -302       C  
ATOM   4863  CZ2 TRP B 168      77.375   8.501  18.345  1.00 77.44           C  
ANISOU 4863  CZ2 TRP B 168     9147  10119  10157    752   -713   -165       C  
ATOM   4864  CZ3 TRP B 168      75.119   9.334  18.048  1.00 75.56           C  
ANISOU 4864  CZ3 TRP B 168     8961   9790   9956    678   -539   -141       C  
ATOM   4865  CH2 TRP B 168      76.134   8.415  17.755  1.00 76.11           C  
ANISOU 4865  CH2 TRP B 168     9011   9852  10056    688   -588    -80       C  
ATOM   4866  N   CYS B 169      75.803  15.896  21.350  1.00 88.45           N  
ANISOU 4866  N   CYS B 169    10610  11643  11355    798   -901  -1208       N  
ATOM   4867  CA  CYS B 169      74.944  16.941  21.886  1.00 90.39           C  
ANISOU 4867  CA  CYS B 169    10910  11881  11552    839   -853  -1339       C  
ATOM   4868  C   CYS B 169      74.427  17.825  20.741  1.00 93.94           C  
ANISOU 4868  C   CYS B 169    11315  12130  12248    717   -779  -1358       C  
ATOM   4869  O   CYS B 169      73.229  18.096  20.693  1.00 93.13           O  
ANISOU 4869  O   CYS B 169    11249  11991  12146    740   -652  -1305       O  
ATOM   4870  CB  CYS B 169      75.680  17.765  22.936  1.00 93.43           C  
ANISOU 4870  CB  CYS B 169    11315  12360  11825    901  -1005  -1593       C  
ATOM   4871  SG  CYS B 169      74.690  19.099  23.649  1.00 99.25           S  
ANISOU 4871  SG  CYS B 169    12134  13075  12503    963   -948  -1789       S  
ATOM   4872  N   MET B 170      75.321  18.259  19.818  1.00 90.49           N  
ANISOU 4872  N   MET B 170    10792  11567  12022    596   -851  -1418       N  
ATOM   4873  CA  MET B 170      74.964  19.103  18.668  1.00 89.01           C  
ANISOU 4873  CA  MET B 170    10560  11189  12071    485   -783  -1419       C  
ATOM   4874  C   MET B 170      74.077  18.351  17.678  1.00 88.86           C  
ANISOU 4874  C   MET B 170    10541  11114  12108    450   -653  -1191       C  
ATOM   4875  O   MET B 170      73.239  18.975  17.034  1.00 87.42           O  
ANISOU 4875  O   MET B 170    10353  10820  12043    410   -566  -1165       O  
ATOM   4876  CB  MET B 170      76.212  19.618  17.941  1.00 91.61           C  
ANISOU 4876  CB  MET B 170    10794  11410  12601    374   -877  -1507       C  
ATOM   4877  CG  MET B 170      77.043  20.583  18.763  1.00 97.83           C  
ANISOU 4877  CG  MET B 170    11560  12210  13402    376  -1011  -1760       C  
ATOM   4878  SD  MET B 170      78.494  21.208  17.859  1.00102.81           S  
ANISOU 4878  SD  MET B 170    12049  12698  14315    230  -1105  -1845       S  
ATOM   4879  CE  MET B 170      79.467  19.703  17.681  1.00 98.95           C  
ANISOU 4879  CE  MET B 170    11510  12345  13744    250  -1176  -1706       C  
ATOM   4880  N   ALA B 171      74.276  17.024  17.533  1.00 83.81           N  
ANISOU 4880  N   ALA B 171     9905  10546  11392    466   -646  -1033       N  
ATOM   4881  CA  ALA B 171      73.458  16.187  16.648  1.00 81.99           C  
ANISOU 4881  CA  ALA B 171     9676  10268  11208    430   -540   -831       C  
ATOM   4882  C   ALA B 171      72.033  16.037  17.209  1.00 86.56           C  
ANISOU 4882  C   ALA B 171    10307  10903  11680    503   -429   -750       C  
ATOM   4883  O   ALA B 171      71.059  15.986  16.450  1.00 85.48           O  
ANISOU 4883  O   ALA B 171    10155  10697  11626    461   -338   -635       O  
ATOM   4884  CB  ALA B 171      74.106  14.823  16.467  1.00 82.07           C  
ANISOU 4884  CB  ALA B 171     9680  10325  11178    430   -569   -707       C  
ATOM   4885  N   CYS B 172      71.927  16.013  18.546  1.00 84.36           N  
ANISOU 4885  N   CYS B 172    10082  10756  11214    617   -438   -814       N  
ATOM   4886  CA  CYS B 172      70.689  15.898  19.301  1.00 84.73           C  
ANISOU 4886  CA  CYS B 172    10178  10879  11136    710   -322   -745       C  
ATOM   4887  C   CYS B 172      69.869  17.195  19.184  1.00 87.56           C  
ANISOU 4887  C   CYS B 172    10533  11158  11578    707   -261   -842       C  
ATOM   4888  O   CYS B 172      68.651  17.123  19.044  1.00 87.76           O  
ANISOU 4888  O   CYS B 172    10551  11167  11628    722   -139   -730       O  
ATOM   4889  CB  CYS B 172      71.004  15.571  20.755  1.00 87.36           C  
ANISOU 4889  CB  CYS B 172    10580  11389  11224    848   -355   -790       C  
ATOM   4890  SG  CYS B 172      69.552  15.414  21.815  1.00 92.97           S  
ANISOU 4890  SG  CYS B 172    11354  12214  11755    986   -188   -685       S  
ATOM   4891  N   LEU B 173      70.529  18.366  19.245  1.00 83.24           N  
ANISOU 4891  N   LEU B 173     9983  10554  11089    689   -343  -1046       N  
ATOM   4892  CA  LEU B 173      69.883  19.682  19.138  1.00 82.97           C  
ANISOU 4892  CA  LEU B 173     9950  10421  11153    691   -293  -1159       C  
ATOM   4893  C   LEU B 173      69.438  19.971  17.699  1.00 83.85           C  
ANISOU 4893  C   LEU B 173     9998  10375  11488    586   -238  -1059       C  
ATOM   4894  O   LEU B 173      68.433  20.654  17.499  1.00 83.71           O  
ANISOU 4894  O   LEU B 173     9975  10298  11535    608   -145  -1042       O  
ATOM   4895  CB  LEU B 173      70.826  20.806  19.619  1.00 84.28           C  
ANISOU 4895  CB  LEU B 173    10128  10550  11346    687   -409  -1413       C  
ATOM   4896  CG  LEU B 173      71.323  20.742  21.067  1.00 91.11           C  
ANISOU 4896  CG  LEU B 173    11061  11575  11982    798   -496  -1563       C  
ATOM   4897  CD1 LEU B 173      72.338  21.826  21.336  1.00 92.65           C  
ANISOU 4897  CD1 LEU B 173    11242  11706  12254    757   -636  -1821       C  
ATOM   4898  CD2 LEU B 173      70.176  20.823  22.068  1.00 95.27           C  
ANISOU 4898  CD2 LEU B 173    11671  12205  12321    943   -385  -1566       C  
ATOM   4899  N   SER B 174      70.195  19.466  16.702  1.00 77.81           N  
ANISOU 4899  N   SER B 174     9184   9548  10832    483   -295   -991       N  
ATOM   4900  CA  SER B 174      69.905  19.654  15.277  1.00 75.54           C  
ANISOU 4900  CA  SER B 174     8844   9127  10731    390   -256   -893       C  
ATOM   4901  C   SER B 174      68.731  18.785  14.828  1.00 77.44           C  
ANISOU 4901  C   SER B 174     9073   9395  10956    391   -166   -698       C  
ATOM   4902  O   SER B 174      68.127  19.060  13.787  1.00 74.97           O  
ANISOU 4902  O   SER B 174     8721   8993  10770    342   -124   -620       O  
ATOM   4903  CB  SER B 174      71.134  19.323  14.440  1.00 77.82           C  
ANISOU 4903  CB  SER B 174     9094   9361  11113    298   -337   -886       C  
ATOM   4904  OG  SER B 174      72.232  20.152  14.780  1.00 86.84           O  
ANISOU 4904  OG  SER B 174    10222  10465  12307    281   -423  -1064       O  
ATOM   4905  N   SER B 175      68.419  17.732  15.613  1.00 75.29           N  
ANISOU 4905  N   SER B 175     8828   9246  10533    449   -140   -615       N  
ATOM   4906  CA  SER B 175      67.350  16.779  15.329  1.00 75.16           C  
ANISOU 4906  CA  SER B 175     8790   9257  10510    444    -58   -432       C  
ATOM   4907  C   SER B 175      66.056  17.114  16.111  1.00 80.50           C  
ANISOU 4907  C   SER B 175     9472   9998  11115    538     54   -403       C  
ATOM   4908  O   SER B 175      65.068  16.388  15.963  1.00 80.67           O  
ANISOU 4908  O   SER B 175     9462  10050  11137    539    132   -249       O  
ATOM   4909  CB  SER B 175      67.801  15.359  15.663  1.00 79.21           C  
ANISOU 4909  CB  SER B 175     9323   9841  10932    442    -82   -334       C  
ATOM   4910  OG  SER B 175      68.100  15.221  17.041  1.00 92.59           O  
ANISOU 4910  OG  SER B 175    11072  11658  12451    541    -98   -392       O  
ATOM   4911  N   LEU B 176      66.049  18.217  16.917  1.00 77.44           N  
ANISOU 4911  N   LEU B 176     9118   9622  10682    617     67   -553       N  
ATOM   4912  CA  LEU B 176      64.865  18.663  17.684  1.00 77.49           C  
ANISOU 4912  CA  LEU B 176     9134   9686  10621    724    187   -542       C  
ATOM   4913  C   LEU B 176      63.728  19.153  16.739  1.00 79.08           C  
ANISOU 4913  C   LEU B 176     9260   9799  10989    692    265   -452       C  
ATOM   4914  O   LEU B 176      62.588  18.745  16.979  1.00 78.61           O  
ANISOU 4914  O   LEU B 176     9162   9797  10911    735    371   -323       O  
ATOM   4915  CB  LEU B 176      65.198  19.767  18.705  1.00 78.80           C  
ANISOU 4915  CB  LEU B 176     9370   9880  10691    822    173   -750       C  
ATOM   4916  CG  LEU B 176      66.002  19.339  19.931  1.00 84.35           C  
ANISOU 4916  CG  LEU B 176    10152  10719  11179    900    110   -840       C  
ATOM   4917  CD1 LEU B 176      66.437  20.536  20.737  1.00 85.87           C  
ANISOU 4917  CD1 LEU B 176    10408  10910  11308    972     62  -1085       C  
ATOM   4918  CD2 LEU B 176      65.208  18.369  20.808  1.00 87.86           C  
ANISOU 4918  CD2 LEU B 176    10623  11313  11448   1003    220   -691       C  
ATOM   4919  N   PRO B 177      63.974  19.949  15.648  1.00 73.95           N  
ANISOU 4919  N   PRO B 177     8578   9017  10505    620    219   -497       N  
ATOM   4920  CA  PRO B 177      62.852  20.336  14.762  1.00 73.12           C  
ANISOU 4920  CA  PRO B 177     8396   8846  10540    606    285   -393       C  
ATOM   4921  C   PRO B 177      62.139  19.114  14.149  1.00 75.30           C  
ANISOU 4921  C   PRO B 177     8605   9160  10846    545    303   -201       C  
ATOM   4922  O   PRO B 177      60.944  19.188  13.886  1.00 75.15           O  
ANISOU 4922  O   PRO B 177     8513   9148  10893    564    376    -99       O  
ATOM   4923  CB  PRO B 177      63.531  21.175  13.675  1.00 74.12           C  
ANISOU 4923  CB  PRO B 177     8514   8834  10814    534    216   -456       C  
ATOM   4924  CG  PRO B 177      64.787  21.671  14.307  1.00 79.06           C  
ANISOU 4924  CG  PRO B 177     9208   9440  11393    540    148   -638       C  
ATOM   4925  CD  PRO B 177      65.244  20.549  15.180  1.00 74.83           C  
ANISOU 4925  CD  PRO B 177     8711   9033  10688    557    114   -630       C  
ATOM   4926  N   THR B 178      62.862  17.983  13.966  1.00 70.08           N  
ANISOU 4926  N   THR B 178     7963   8521  10142    475    235   -157       N  
ATOM   4927  CA  THR B 178      62.301  16.730  13.454  1.00 68.51           C  
ANISOU 4927  CA  THR B 178     7713   8342   9975    409    242      4       C  
ATOM   4928  C   THR B 178      61.342  16.148  14.478  1.00 73.46           C  
ANISOU 4928  C   THR B 178     8315   9068  10528    478    354    103       C  
ATOM   4929  O   THR B 178      60.225  15.793  14.129  1.00 73.87           O  
ANISOU 4929  O   THR B 178     8280   9120  10666    453    408    226       O  
ATOM   4930  CB  THR B 178      63.412  15.734  13.111  1.00 74.51           C  
ANISOU 4930  CB  THR B 178     8516   9093  10701    338    154      7       C  
ATOM   4931  OG1 THR B 178      64.381  16.350  12.272  1.00 76.06           O  
ANISOU 4931  OG1 THR B 178     8734   9206  10961    288     69    -86       O  
ATOM   4932  CG2 THR B 178      62.886  14.484  12.469  1.00 70.90           C  
ANISOU 4932  CG2 THR B 178     8015   8626  10299    260    151    150       C  
ATOM   4933  N   PHE B 179      61.768  16.073  15.750  1.00 70.78           N  
ANISOU 4933  N   PHE B 179     8047   8816  10030    570    390     50       N  
ATOM   4934  CA  PHE B 179      60.950  15.541  16.839  1.00 71.77           C  
ANISOU 4934  CA  PHE B 179     8164   9047  10059    657    516    151       C  
ATOM   4935  C   PHE B 179      59.712  16.393  17.075  1.00 77.31           C  
ANISOU 4935  C   PHE B 179     8808   9763  10804    736    633    165       C  
ATOM   4936  O   PHE B 179      58.674  15.869  17.480  1.00 77.76           O  
ANISOU 4936  O   PHE B 179     8803   9880  10862    775    754    302       O  
ATOM   4937  CB  PHE B 179      61.780  15.470  18.133  1.00 74.14           C  
ANISOU 4937  CB  PHE B 179     8571   9449  10149    759    514     70       C  
ATOM   4938  CG  PHE B 179      61.036  14.911  19.322  1.00 76.91           C  
ANISOU 4938  CG  PHE B 179     8932   9923  10369    871    657    183       C  
ATOM   4939  CD1 PHE B 179      60.875  13.538  19.480  1.00 79.71           C  
ANISOU 4939  CD1 PHE B 179     9263  10308  10717    842    706    363       C  
ATOM   4940  CD2 PHE B 179      60.539  15.753  20.310  1.00 80.29           C  
ANISOU 4940  CD2 PHE B 179     9401  10431  10676   1013    750    108       C  
ATOM   4941  CE1 PHE B 179      60.189  13.020  20.581  1.00 82.07           C  
ANISOU 4941  CE1 PHE B 179     9568  10715  10900    950    858    490       C  
ATOM   4942  CE2 PHE B 179      59.848  15.234  21.409  1.00 84.79           C  
ANISOU 4942  CE2 PHE B 179     9983  11123  11111   1130    901    226       C  
ATOM   4943  CZ  PHE B 179      59.684  13.871  21.539  1.00 82.87           C  
ANISOU 4943  CZ  PHE B 179     9707  10910  10870   1097    958    426       C  
ATOM   4944  N   TYR B 180      59.837  17.706  16.836  1.00 74.62           N  
ANISOU 4944  N   TYR B 180     8481   9360  10510    762    605     28       N  
ATOM   4945  CA  TYR B 180      58.804  18.691  17.098  1.00 75.80           C  
ANISOU 4945  CA  TYR B 180     8589   9509  10701    856    712     14       C  
ATOM   4946  C   TYR B 180      57.742  18.699  15.989  1.00 79.04           C  
ANISOU 4946  C   TYR B 180     8866   9860  11305    791    729    143       C  
ATOM   4947  O   TYR B 180      56.556  18.820  16.307  1.00 80.32           O  
ANISOU 4947  O   TYR B 180     8946  10065  11505    857    849    235       O  
ATOM   4948  CB  TYR B 180      59.450  20.086  17.230  1.00 77.83           C  
ANISOU 4948  CB  TYR B 180     8924   9702  10947    908    669   -192       C  
ATOM   4949  CG  TYR B 180      58.577  21.109  17.918  1.00 82.44           C  
ANISOU 4949  CG  TYR B 180     9506  10298  11519   1045    795   -246       C  
ATOM   4950  CD1 TYR B 180      58.544  21.205  19.308  1.00 86.11           C  
ANISOU 4950  CD1 TYR B 180    10051  10872  11796   1182    882   -316       C  
ATOM   4951  CD2 TYR B 180      57.822  22.019  17.184  1.00 84.03           C  
ANISOU 4951  CD2 TYR B 180     9636  10404  11888   1052    828   -234       C  
ATOM   4952  CE1 TYR B 180      57.739  22.147  19.951  1.00 88.89           C  
ANISOU 4952  CE1 TYR B 180    10411  11234  12131   1321   1009   -375       C  
ATOM   4953  CE2 TYR B 180      57.009  22.965  17.816  1.00 86.89           C  
ANISOU 4953  CE2 TYR B 180     9997  10768  12249   1190    953   -283       C  
ATOM   4954  CZ  TYR B 180      56.974  23.028  19.201  1.00 96.30           C  
ANISOU 4954  CZ  TYR B 180    11270  12064  13255   1324   1047   -360       C  
ATOM   4955  OH  TYR B 180      56.176  23.956  19.833  1.00 99.16           O  
ANISOU 4955  OH  TYR B 180    11640  12427  13608   1472   1181   -418       O  
ATOM   4956  N   PHE B 181      58.136  18.551  14.704  1.00 73.58           N  
ANISOU 4956  N   PHE B 181     8148   9081  10730    670    610    155       N  
ATOM   4957  CA  PHE B 181      57.147  18.652  13.630  1.00 73.04           C  
ANISOU 4957  CA  PHE B 181     7958   8967  10826    619    602    261       C  
ATOM   4958  C   PHE B 181      56.811  17.274  12.967  1.00 75.57           C  
ANISOU 4958  C   PHE B 181     8203   9303  11206    504    558    405       C  
ATOM   4959  O   PHE B 181      55.709  17.175  12.413  1.00 75.93           O  
ANISOU 4959  O   PHE B 181     8124   9353  11372    481    578    512       O  
ATOM   4960  CB  PHE B 181      57.608  19.636  12.538  1.00 73.97           C  
ANISOU 4960  CB  PHE B 181     8092   8975  11037    583    510    186       C  
ATOM   4961  CG  PHE B 181      57.774  21.054  13.049  1.00 76.02           C  
ANISOU 4961  CG  PHE B 181     8407   9185  11292    685    557     52       C  
ATOM   4962  CD1 PHE B 181      56.666  21.854  13.303  1.00 79.95           C  
ANISOU 4962  CD1 PHE B 181     8839   9677  11862    782    657     81       C  
ATOM   4963  CD2 PHE B 181      59.037  21.603  13.229  1.00 77.65           C  
ANISOU 4963  CD2 PHE B 181     8723   9341  11439    683    501   -107       C  
ATOM   4964  CE1 PHE B 181      56.819  23.153  13.792  1.00 81.65           C  
ANISOU 4964  CE1 PHE B 181     9114   9828  12081    882    707    -53       C  
ATOM   4965  CE2 PHE B 181      59.189  22.906  13.707  1.00 81.39           C  
ANISOU 4965  CE2 PHE B 181     9247   9750  11927    769    541   -247       C  
ATOM   4966  CZ  PHE B 181      58.079  23.675  13.980  1.00 80.65           C  
ANISOU 4966  CZ  PHE B 181     9104   9641  11900    869    646   -223       C  
ATOM   4967  N   ARG B 182      57.689  16.225  13.036  1.00 69.63           N  
ANISOU 4967  N   ARG B 182     7516   8557  10384    434    498    406       N  
ATOM   4968  CA  ARG B 182      57.327  14.909  12.451  1.00 68.81           C  
ANISOU 4968  CA  ARG B 182     7346   8447  10350    325    463    531       C  
ATOM   4969  C   ARG B 182      56.119  14.303  13.169  1.00 73.66           C  
ANISOU 4969  C   ARG B 182     7858   9127  11000    352    589    669       C  
ATOM   4970  O   ARG B 182      56.145  14.153  14.391  1.00 74.76           O  
ANISOU 4970  O   ARG B 182     8040   9337  11028    439    697    686       O  
ATOM   4971  CB  ARG B 182      58.488  13.889  12.470  1.00 67.00           C  
ANISOU 4971  CB  ARG B 182     7210   8204  10043    264    396    511       C  
ATOM   4972  CG  ARG B 182      59.494  14.026  11.330  1.00 68.84           C  
ANISOU 4972  CG  ARG B 182     7498   8359  10299    189    262    430       C  
ATOM   4973  CD  ARG B 182      58.895  13.623   9.999  1.00 63.36           C  
ANISOU 4973  CD  ARG B 182     6726   7615   9733     90    190    494       C  
ATOM   4974  NE  ARG B 182      59.822  13.838   8.896  1.00 59.15           N  
ANISOU 4974  NE  ARG B 182     6251   7015   9207     38     80    422       N  
ATOM   4975  CZ  ARG B 182      59.487  13.710   7.619  1.00 78.33           C  
ANISOU 4975  CZ  ARG B 182     8639   9407  11715    -30      1    450       C  
ATOM   4976  NH1 ARG B 182      58.245  13.398   7.280  1.00 69.33           N  
ANISOU 4976  NH1 ARG B 182     7387   8287  10667    -63      1    536       N  
ATOM   4977  NH2 ARG B 182      60.379  13.936   6.669  1.00 69.78           N  
ANISOU 4977  NH2 ARG B 182     7621   8274  10621    -60    -80    392       N  
ATOM   4978  N   ASP B 183      55.040  14.005  12.414  1.00 69.05           N  
ANISOU 4978  N   ASP B 183     7135   8528  10573    284    577    771       N  
ATOM   4979  CA  ASP B 183      53.822  13.422  12.983  1.00 69.66           C  
ANISOU 4979  CA  ASP B 183     7084   8658  10727    292    698    917       C  
ATOM   4980  C   ASP B 183      52.993  12.756  11.881  1.00 72.77           C  
ANISOU 4980  C   ASP B 183     7332   9012  11307    163    618   1004       C  
ATOM   4981  O   ASP B 183      53.123  13.125  10.709  1.00 71.41           O  
ANISOU 4981  O   ASP B 183     7145   8796  11191    113    488    950       O  
ATOM   4982  CB  ASP B 183      52.996  14.503  13.713  1.00 72.65           C  
ANISOU 4982  CB  ASP B 183     7409   9099  11096    433    836    926       C  
ATOM   4983  CG  ASP B 183      51.887  13.974  14.602  1.00 80.87           C  
ANISOU 4983  CG  ASP B 183     8337  10212  12179    477   1006   1078       C  
ATOM   4984  OD1 ASP B 183      52.102  12.926  15.263  1.00 79.75           O  
ANISOU 4984  OD1 ASP B 183     8223  10087  11991    448   1059   1156       O  
ATOM   4985  OD2 ASP B 183      50.861  14.675  14.745  1.00 88.50           O  
ANISOU 4985  OD2 ASP B 183     9199  11218  13211    561   1104   1121       O  
ATOM   4986  N   VAL B 184      52.165  11.757  12.252  1.00 70.01           N  
ANISOU 4986  N   VAL B 184     6874   8676  11051    110    693   1140       N  
ATOM   4987  CA  VAL B 184      51.295  11.037  11.318  1.00 69.85           C  
ANISOU 4987  CA  VAL B 184     6697   8617  11225    -23    614   1217       C  
ATOM   4988  C   VAL B 184      50.044  11.878  11.070  1.00 75.32           C  
ANISOU 4988  C   VAL B 184     7217   9359  12042     23    647   1270       C  
ATOM   4989  O   VAL B 184      49.365  12.273  12.017  1.00 75.95           O  
ANISOU 4989  O   VAL B 184     7231   9503  12122    127    811   1343       O  
ATOM   4990  CB  VAL B 184      50.947   9.611  11.827  1.00 74.07           C  
ANISOU 4990  CB  VAL B 184     7173   9127  11842   -107    688   1343       C  
ATOM   4991  CG1 VAL B 184      49.819   8.981  11.028  1.00 74.80           C  
ANISOU 4991  CG1 VAL B 184     7066   9187  12169   -238    629   1426       C  
ATOM   4992  CG2 VAL B 184      52.169   8.715  11.796  1.00 72.87           C  
ANISOU 4992  CG2 VAL B 184     7179   8908  11600   -166    622   1292       C  
ATOM   4993  N   ARG B 185      49.770  12.178   9.790  1.00 72.49           N  
ANISOU 4993  N   ARG B 185     6791   8977  11775    -40    491   1233       N  
ATOM   4994  CA  ARG B 185      48.596  12.935   9.355  1.00 73.88           C  
ANISOU 4994  CA  ARG B 185     6791   9199  12081      0    487   1287       C  
ATOM   4995  C   ARG B 185      47.954  12.235   8.157  1.00 81.92           C  
ANISOU 4995  C   ARG B 185     7670  10196  13259   -144    317   1313       C  
ATOM   4996  O   ARG B 185      48.662  11.720   7.283  1.00 80.12           O  
ANISOU 4996  O   ARG B 185     7537   9915  12989   -232    159   1229       O  
ATOM   4997  CB  ARG B 185      48.940  14.400   9.022  1.00 70.31           C  
ANISOU 4997  CB  ARG B 185     6415   8754  11545    122    466   1200       C  
ATOM   4998  CG  ARG B 185      49.474  15.220  10.207  1.00 74.43           C  
ANISOU 4998  CG  ARG B 185     7068   9293  11920    268    619   1146       C  
ATOM   4999  CD  ARG B 185      48.452  15.435  11.318  1.00 71.00           C  
ANISOU 4999  CD  ARG B 185     6523   8929  11524    375    818   1243       C  
ATOM   5000  NE  ARG B 185      49.053  16.063  12.498  1.00 75.58           N  
ANISOU 5000  NE  ARG B 185     7254   9530  11932    512    950   1168       N  
ATOM   5001  CZ  ARG B 185      49.172  17.377  12.677  1.00 96.18           C  
ANISOU 5001  CZ  ARG B 185     9925  12132  14488    640    988   1080       C  
ATOM   5002  NH1 ARG B 185      49.734  17.854  13.779  1.00 87.65           N  
ANISOU 5002  NH1 ARG B 185     8986  11070  13248    754   1093    992       N  
ATOM   5003  NH2 ARG B 185      48.737  18.223  11.750  1.00 85.37           N  
ANISOU 5003  NH2 ARG B 185     8480  10733  13224    658    917   1076       N  
ATOM   5004  N   THR B 186      46.608  12.191   8.137  1.00 82.94           N  
ANISOU 5004  N   THR B 186     7571  10371  13573   -165    350   1426       N  
ATOM   5005  CA  THR B 186      45.859  11.528   7.081  1.00 84.67           C  
ANISOU 5005  CA  THR B 186     7625  10582  13964   -304    184   1450       C  
ATOM   5006  C   THR B 186      45.851  12.421   5.835  1.00 89.46           C  
ANISOU 5006  C   THR B 186     8232  11215  14543   -270     10   1381       C  
ATOM   5007  O   THR B 186      45.444  13.586   5.900  1.00 89.12           O  
ANISOU 5007  O   THR B 186     8147  11225  14491   -136     63   1405       O  
ATOM   5008  CB  THR B 186      44.434  11.182   7.556  1.00100.27           C  
ANISOU 5008  CB  THR B 186     9335  12605  16159   -329    283   1598       C  
ATOM   5009  OG1 THR B 186      43.714  12.383   7.829  1.00106.95           O  
ANISOU 5009  OG1 THR B 186    10081  13532  17024   -176    378   1651       O  
ATOM   5010  CG2 THR B 186      44.425  10.284   8.788  1.00 98.74           C  
ANISOU 5010  CG2 THR B 186     9137  12383  15996   -355    476   1693       C  
ATOM   5011  N   ILE B 187      46.356  11.880   4.715  1.00 86.90           N  
ANISOU 5011  N   ILE B 187     7972  10852  14196   -379   -189   1296       N  
ATOM   5012  CA  ILE B 187      46.380  12.565   3.422  1.00 87.01           C  
ANISOU 5012  CA  ILE B 187     7997  10897  14166   -351   -365   1240       C  
ATOM   5013  C   ILE B 187      45.088  12.164   2.719  1.00 94.85           C  
ANISOU 5013  C   ILE B 187     8745  11947  15348   -431   -500   1296       C  
ATOM   5014  O   ILE B 187      45.018  11.083   2.132  1.00 94.98           O  
ANISOU 5014  O   ILE B 187     8730  11930  15427   -579   -644   1250       O  
ATOM   5015  CB  ILE B 187      47.676  12.234   2.620  1.00 88.23           C  
ANISOU 5015  CB  ILE B 187     8372  10989  14161   -401   -493   1114       C  
ATOM   5016  CG1 ILE B 187      48.985  12.397   3.494  1.00 86.72           C  
ANISOU 5016  CG1 ILE B 187     8400  10739  13811   -343   -356   1062       C  
ATOM   5017  CG2 ILE B 187      47.738  13.014   1.302  1.00 88.88           C  
ANISOU 5017  CG2 ILE B 187     8481  11113  14177   -351   -655   1074       C  
ATOM   5018  CD1 ILE B 187      49.303  13.827   4.147  1.00 93.36           C  
ANISOU 5018  CD1 ILE B 187     9312  11600  14561   -175   -223   1063       C  
ATOM   5019  N   GLU B 188      44.038  13.002   2.872  1.00 93.99           N  
ANISOU 5019  N   GLU B 188     8453  11917  15341   -333   -445   1392       N  
ATOM   5020  CA  GLU B 188      42.656  12.774   2.430  1.00 96.68           C  
ANISOU 5020  CA  GLU B 188     8513  12331  15888   -382   -543   1470       C  
ATOM   5021  C   GLU B 188      42.540  12.322   0.960  1.00101.98           C  
ANISOU 5021  C   GLU B 188     9156  13025  16567   -487   -827   1390       C  
ATOM   5022  O   GLU B 188      41.763  11.404   0.690  1.00102.96           O  
ANISOU 5022  O   GLU B 188     9105  13153  16861   -630   -933   1398       O  
ATOM   5023  CB  GLU B 188      41.825  14.050   2.602  1.00 99.12           C  
ANISOU 5023  CB  GLU B 188     8691  12727  16245   -211   -465   1564       C  
ATOM   5024  N   TYR B 189      43.284  12.951   0.022  1.00 98.44           N  
ANISOU 5024  N   TYR B 189     8877  12589  15938   -418   -948   1313       N  
ATOM   5025  CA  TYR B 189      43.172  12.614  -1.403  1.00 99.63           C  
ANISOU 5025  CA  TYR B 189     9018  12782  16057   -488  -1216   1237       C  
ATOM   5026  C   TYR B 189      43.913  11.294  -1.748  1.00102.08           C  
ANISOU 5026  C   TYR B 189     9468  13001  16316   -651  -1313   1111       C  
ATOM   5027  O   TYR B 189      43.769  10.803  -2.872  1.00102.98           O  
ANISOU 5027  O   TYR B 189     9598  13142  16387   -716  -1536   1023       O  
ATOM   5028  CB  TYR B 189      43.696  13.751  -2.301  1.00101.01           C  
ANISOU 5028  CB  TYR B 189     9328  13004  16049   -342  -1290   1219       C  
ATOM   5029  CG  TYR B 189      45.141  14.150  -2.089  1.00101.44           C  
ANISOU 5029  CG  TYR B 189     9664  12973  15904   -278  -1179   1159       C  
ATOM   5030  CD1 TYR B 189      45.481  15.157  -1.190  1.00102.93           C  
ANISOU 5030  CD1 TYR B 189     9917  13132  16061   -146   -972   1210       C  
ATOM   5031  CD2 TYR B 189      46.157  13.604  -2.869  1.00101.19           C  
ANISOU 5031  CD2 TYR B 189     9830  12896  15721   -341  -1288   1045       C  
ATOM   5032  CE1 TYR B 189      46.805  15.565  -1.025  1.00102.25           C  
ANISOU 5032  CE1 TYR B 189    10070  12968  15812    -95   -885   1147       C  
ATOM   5033  CE2 TYR B 189      47.485  14.004  -2.713  1.00100.28           C  
ANISOU 5033  CE2 TYR B 189     9951  12708  15443   -283  -1187    997       C  
ATOM   5034  CZ  TYR B 189      47.804  14.984  -1.786  1.00107.84           C  
ANISOU 5034  CZ  TYR B 189    10954  13634  16386   -167   -992   1047       C  
ATOM   5035  OH  TYR B 189      49.108  15.386  -1.622  1.00107.82           O  
ANISOU 5035  OH  TYR B 189    11166  13558  16244   -119   -904    992       O  
ATOM   5036  N   LEU B 190      44.661  10.709  -0.790  1.00 95.85           N  
ANISOU 5036  N   LEU B 190     8778  12111  15531   -708  -1151   1103       N  
ATOM   5037  CA  LEU B 190      45.358   9.431  -0.992  1.00 94.01           C  
ANISOU 5037  CA  LEU B 190     8671  11776  15272   -852  -1216    998       C  
ATOM   5038  C   LEU B 190      44.790   8.337  -0.075  1.00 98.11           C  
ANISOU 5038  C   LEU B 190     9053  12225  15999   -983  -1117   1054       C  
ATOM   5039  O   LEU B 190      45.020   7.146  -0.326  1.00 98.30           O  
ANISOU 5039  O   LEU B 190     9110  12160  16080  -1129  -1200    980       O  
ATOM   5040  CB  LEU B 190      46.871   9.567  -0.754  1.00 91.02           C  
ANISOU 5040  CB  LEU B 190     8577  11326  14681   -794  -1123    932       C  
ATOM   5041  CG  LEU B 190      47.673  10.383  -1.758  1.00 93.50           C  
ANISOU 5041  CG  LEU B 190     9061  11676  14789   -691  -1213    866       C  
ATOM   5042  CD1 LEU B 190      49.080  10.600  -1.260  1.00 91.32           C  
ANISOU 5042  CD1 LEU B 190     9022  11325  14351   -640  -1088    820       C  
ATOM   5043  CD2 LEU B 190      47.683   9.728  -3.135  1.00 95.04           C  
ANISOU 5043  CD2 LEU B 190     9281  11892  14939   -767  -1457    763       C  
ATOM   5044  N   GLY B 191      44.051   8.755   0.961  1.00 94.09           N  
ANISOU 5044  N   GLY B 191     8395  11751  15605   -922   -932   1190       N  
ATOM   5045  CA  GLY B 191      43.450   7.873   1.962  1.00 94.10           C  
ANISOU 5045  CA  GLY B 191     8254  11695  15804  -1017   -789   1284       C  
ATOM   5046  C   GLY B 191      44.495   7.048   2.683  1.00 93.73           C  
ANISOU 5046  C   GLY B 191     8407  11532  15674  -1058   -667   1258       C  
ATOM   5047  O   GLY B 191      44.288   5.857   2.936  1.00 94.25           O  
ANISOU 5047  O   GLY B 191     8421  11503  15888  -1200   -657   1271       O  
ATOM   5048  N   VAL B 192      45.640   7.684   2.997  1.00 85.64           N  
ANISOU 5048  N   VAL B 192     7610  10507  14422   -931   -577   1222       N  
ATOM   5049  CA  VAL B 192      46.786   7.020   3.584  1.00 82.67           C  
ANISOU 5049  CA  VAL B 192     7440  10037  13933   -946   -483   1187       C  
ATOM   5050  C   VAL B 192      47.305   7.850   4.795  1.00 83.84           C  
ANISOU 5050  C   VAL B 192     7689  10224  13943   -786   -266   1246       C  
ATOM   5051  O   VAL B 192      47.204   9.077   4.791  1.00 83.11           O  
ANISOU 5051  O   VAL B 192     7590  10210  13777   -657   -239   1252       O  
ATOM   5052  CB  VAL B 192      47.866   6.837   2.464  1.00 84.72           C  
ANISOU 5052  CB  VAL B 192     7905  10252  14034   -974   -657   1031       C  
ATOM   5053  CG1 VAL B 192      48.613   8.128   2.147  1.00 82.79           C  
ANISOU 5053  CG1 VAL B 192     7791  10074  13589   -827   -672    983       C  
ATOM   5054  CG2 VAL B 192      48.846   5.761   2.812  1.00 83.63           C  
ANISOU 5054  CG2 VAL B 192     7938  10001  13839  -1030   -603    991       C  
ATOM   5055  N   ASN B 193      47.810   7.172   5.837  1.00 79.38           N  
ANISOU 5055  N   ASN B 193     7212   9602  13348   -790   -115   1290       N  
ATOM   5056  CA  ASN B 193      48.371   7.849   7.003  1.00 78.21           C  
ANISOU 5056  CA  ASN B 193     7178   9494  13045   -642     70   1323       C  
ATOM   5057  C   ASN B 193      49.862   7.982   6.812  1.00 80.18           C  
ANISOU 5057  C   ASN B 193     7673   9703  13089   -607     19   1204       C  
ATOM   5058  O   ASN B 193      50.593   6.999   6.961  1.00 80.21           O  
ANISOU 5058  O   ASN B 193     7780   9628  13068   -673     17   1184       O  
ATOM   5059  CB  ASN B 193      48.034   7.122   8.315  1.00 80.39           C  
ANISOU 5059  CB  ASN B 193     7397   9758  13389   -639    275   1460       C  
ATOM   5060  CG  ASN B 193      46.578   7.181   8.718  1.00103.82           C  
ANISOU 5060  CG  ASN B 193    10114  12779  16554   -642    375   1598       C  
ATOM   5061  OD1 ASN B 193      45.688   7.466   7.921  1.00 94.64           O  
ANISOU 5061  OD1 ASN B 193     8777  11638  15545   -707    254   1598       O  
ATOM   5062  ND2 ASN B 193      46.299   6.880   9.974  1.00 98.31           N  
ANISOU 5062  ND2 ASN B 193     9386  12111  15858   -569    599   1726       N  
ATOM   5063  N   ALA B 194      50.316   9.188   6.432  1.00 74.15           N  
ANISOU 5063  N   ALA B 194     6993   8985  12196   -505    -24   1127       N  
ATOM   5064  CA  ALA B 194      51.722   9.445   6.150  1.00 71.11           C  
ANISOU 5064  CA  ALA B 194     6819   8566  11636   -472    -79   1013       C  
ATOM   5065  C   ALA B 194      52.418  10.142   7.319  1.00 73.55           C  
ANISOU 5065  C   ALA B 194     7242   8905  11800   -342     66   1004       C  
ATOM   5066  O   ALA B 194      51.826  11.001   7.976  1.00 72.98           O  
ANISOU 5066  O   ALA B 194     7107   8893  11727   -239    168   1043       O  
ATOM   5067  CB  ALA B 194      51.848  10.293   4.900  1.00 70.98           C  
ANISOU 5067  CB  ALA B 194     6822   8566  11581   -455   -226    937       C  
ATOM   5068  N   CYS B 195      53.686   9.751   7.566  1.00 69.29           N  
ANISOU 5068  N   CYS B 195     6868   8322  11139   -342     67    944       N  
ATOM   5069  CA  CYS B 195      54.579  10.324   8.576  1.00 68.48           C  
ANISOU 5069  CA  CYS B 195     6891   8246  10883   -229    165    904       C  
ATOM   5070  C   CYS B 195      55.207  11.575   7.971  1.00 72.48           C  
ANISOU 5070  C   CYS B 195     7471   8755  11312   -167     99    800       C  
ATOM   5071  O   CYS B 195      56.287  11.506   7.379  1.00 72.46           O  
ANISOU 5071  O   CYS B 195     7580   8707  11244   -195     10    719       O  
ATOM   5072  CB  CYS B 195      55.616   9.286   9.017  1.00 68.22           C  
ANISOU 5072  CB  CYS B 195     6980   8168  10770   -260    174    892       C  
ATOM   5073  SG  CYS B 195      56.879   9.895  10.170  1.00 71.32           S  
ANISOU 5073  SG  CYS B 195     7530   8605  10964   -129    251    823       S  
ATOM   5074  N   ILE B 196      54.463  12.697   8.008  1.00 68.66           N  
ANISOU 5074  N   ILE B 196     6912   8316  10861    -85    144    814       N  
ATOM   5075  CA  ILE B 196      54.877  13.947   7.367  1.00 67.41           C  
ANISOU 5075  CA  ILE B 196     6804   8142  10666    -26     92    737       C  
ATOM   5076  C   ILE B 196      55.510  14.913   8.374  1.00 70.86           C  
ANISOU 5076  C   ILE B 196     7329   8589  11004     91    191    669       C  
ATOM   5077  O   ILE B 196      55.591  14.630   9.569  1.00 71.37           O  
ANISOU 5077  O   ILE B 196     7417   8692  11007    139    297    681       O  
ATOM   5078  CB  ILE B 196      53.682  14.658   6.648  1.00 71.19           C  
ANISOU 5078  CB  ILE B 196     7141   8649  11260     -6     57    793       C  
ATOM   5079  CG1 ILE B 196      52.621  15.174   7.656  1.00 72.75           C  
ANISOU 5079  CG1 ILE B 196     7222   8904  11515     87    199    867       C  
ATOM   5080  CG2 ILE B 196      53.069  13.760   5.557  1.00 72.17           C  
ANISOU 5080  CG2 ILE B 196     7174   8769  11477   -125    -75    836       C  
ATOM   5081  CD1 ILE B 196      51.630  16.149   7.081  1.00 82.57           C  
ANISOU 5081  CD1 ILE B 196     8340  10174  12859    146    180    914       C  
ATOM   5082  N   MET B 197      55.923  16.077   7.860  1.00 66.20           N  
ANISOU 5082  N   MET B 197     6789   7964  10402    140    156    599       N  
ATOM   5083  CA  MET B 197      56.478  17.182   8.617  1.00 65.48           C  
ANISOU 5083  CA  MET B 197     6775   7858  10248    242    228    511       C  
ATOM   5084  C   MET B 197      55.322  18.131   8.883  1.00 70.62           C  
ANISOU 5084  C   MET B 197     7326   8533  10972    339    314    555       C  
ATOM   5085  O   MET B 197      55.023  19.000   8.056  1.00 70.38           O  
ANISOU 5085  O   MET B 197     7259   8468  11014    367    279    565       O  
ATOM   5086  CB  MET B 197      57.646  17.810   7.819  1.00 66.66           C  
ANISOU 5086  CB  MET B 197     7023   7931  10374    227    147    420       C  
ATOM   5087  CG  MET B 197      58.682  18.485   8.668  1.00 69.61           C  
ANISOU 5087  CG  MET B 197     7503   8277  10669    283    188    299       C  
ATOM   5088  SD  MET B 197      59.685  17.337   9.636  1.00 72.59           S  
ANISOU 5088  SD  MET B 197     7967   8696  10918    247    182    257       S  
ATOM   5089  CE  MET B 197      60.690  18.489  10.515  1.00 69.57           C  
ANISOU 5089  CE  MET B 197     7681   8287  10465    326    208     97       C  
ATOM   5090  N   ALA B 198      54.563  17.853   9.957  1.00 68.27           N  
ANISOU 5090  N   ALA B 198     6973   8303  10664    393    432    606       N  
ATOM   5091  CA  ALA B 198      53.336  18.573  10.318  1.00 69.16           C  
ANISOU 5091  CA  ALA B 198     6974   8453  10852    493    539    666       C  
ATOM   5092  C   ALA B 198      53.638  20.019  10.838  1.00 72.48           C  
ANISOU 5092  C   ALA B 198     7473   8833  11234    621    609    557       C  
ATOM   5093  O   ALA B 198      53.466  20.305  12.028  1.00 71.98           O  
ANISOU 5093  O   ALA B 198     7444   8808  11098    720    732    518       O  
ATOM   5094  CB  ALA B 198      52.565  17.781  11.374  1.00 71.02           C  
ANISOU 5094  CB  ALA B 198     7139   8771  11075    516    663    756       C  
ATOM   5095  N   PHE B 199      54.057  20.927   9.919  1.00 69.76           N  
ANISOU 5095  N   PHE B 199     7159   8405  10943    623    535    510       N  
ATOM   5096  CA  PHE B 199      54.359  22.340  10.222  1.00 70.58           C  
ANISOU 5096  CA  PHE B 199     7332   8434  11052    729    591    406       C  
ATOM   5097  C   PHE B 199      53.109  23.163  10.512  1.00 77.48           C  
ANISOU 5097  C   PHE B 199     8103   9323  12014    856    706    464       C  
ATOM   5098  O   PHE B 199      52.025  22.763  10.066  1.00 77.66           O  
ANISOU 5098  O   PHE B 199     7978   9406  12123    844    705    601       O  
ATOM   5099  CB  PHE B 199      55.093  23.017   9.054  1.00 71.58           C  
ANISOU 5099  CB  PHE B 199     7508   8456  11234    689    491    373       C  
ATOM   5100  CG  PHE B 199      56.433  22.478   8.658  1.00 72.23           C  
ANISOU 5100  CG  PHE B 199     7694   8503  11248    584    390    305       C  
ATOM   5101  CD1 PHE B 199      57.520  22.582   9.519  1.00 75.84           C  
ANISOU 5101  CD1 PHE B 199     8266   8936  11615    588    404    169       C  
ATOM   5102  CD2 PHE B 199      56.672  22.070   7.352  1.00 73.86           C  
ANISOU 5102  CD2 PHE B 199     7887   8689  11486    499    279    366       C  
ATOM   5103  CE1 PHE B 199      58.788  22.159   9.123  1.00 75.91           C  
ANISOU 5103  CE1 PHE B 199     8355   8910  11579    499    314    111       C  
ATOM   5104  CE2 PHE B 199      57.945  21.664   6.949  1.00 75.84           C  
ANISOU 5104  CE2 PHE B 199     8233   8901  11681    417    203    305       C  
ATOM   5105  CZ  PHE B 199      58.998  21.726   7.832  1.00 73.94           C  
ANISOU 5105  CZ  PHE B 199     8088   8637  11368    417    224    183       C  
ATOM   5106  N   PRO B 200      53.227  24.370  11.144  1.00 75.81           N  
ANISOU 5106  N   PRO B 200     7956   9047  11800    976    796    360       N  
ATOM   5107  CA  PRO B 200      52.029  25.207  11.340  1.00 77.89           C  
ANISOU 5107  CA  PRO B 200     8121   9314  12160   1111    913    419       C  
ATOM   5108  C   PRO B 200      51.377  25.517   9.990  1.00 84.22           C  
ANISOU 5108  C   PRO B 200     8803  10089  13108   1097    840    547       C  
ATOM   5109  O   PRO B 200      52.080  25.958   9.079  1.00 83.46           O  
ANISOU 5109  O   PRO B 200     8765   9903  13041   1052    746    522       O  
ATOM   5110  CB  PRO B 200      52.575  26.463  12.033  1.00 79.99           C  
ANISOU 5110  CB  PRO B 200     8513   9477  12404   1219    988    252       C  
ATOM   5111  CG  PRO B 200      53.845  26.029  12.659  1.00 83.05           C  
ANISOU 5111  CG  PRO B 200     9045   9864  12647   1152    937    108       C  
ATOM   5112  CD  PRO B 200      54.424  25.023  11.711  1.00 76.94           C  
ANISOU 5112  CD  PRO B 200     8257   9107  11868    996    794    178       C  
ATOM   5113  N   PRO B 201      50.078  25.178   9.792  1.00 82.64           N  
ANISOU 5113  N   PRO B 201     8428   9975  12996   1126    872    696       N  
ATOM   5114  CA  PRO B 201      49.466  25.356   8.461  1.00 82.88           C  
ANISOU 5114  CA  PRO B 201     8337  10005  13148   1110    773    820       C  
ATOM   5115  C   PRO B 201      49.446  26.814   7.995  1.00 88.82           C  
ANISOU 5115  C   PRO B 201     9117  10645  13986   1228    802    808       C  
ATOM   5116  O   PRO B 201      49.585  27.053   6.791  1.00 88.67           O  
ANISOU 5116  O   PRO B 201     9082  10591  14016   1200    692    870       O  
ATOM   5117  CB  PRO B 201      48.038  24.842   8.653  1.00 85.96           C  
ANISOU 5117  CB  PRO B 201     8524  10512  13626   1139    827    961       C  
ATOM   5118  CG  PRO B 201      47.804  24.870  10.127  1.00 91.41           C  
ANISOU 5118  CG  PRO B 201     9238  11236  14259   1229   1007    914       C  
ATOM   5119  CD  PRO B 201      49.125  24.576  10.745  1.00 85.52           C  
ANISOU 5119  CD  PRO B 201     8689  10450  13354   1173    995    765       C  
ATOM   5120  N   GLU B 202      49.316  27.783   8.938  1.00 86.69           N  
ANISOU 5120  N   GLU B 202     8900  10312  13727   1364    952    725       N  
ATOM   5121  CA  GLU B 202      49.262  29.216   8.628  1.00 87.67           C  
ANISOU 5121  CA  GLU B 202     9056  10303  13951   1487   1004    706       C  
ATOM   5122  C   GLU B 202      50.611  29.714   8.039  1.00 90.76           C  
ANISOU 5122  C   GLU B 202     9604  10555  14324   1418    922    609       C  
ATOM   5123  O   GLU B 202      50.590  30.709   7.318  1.00 91.70           O  
ANISOU 5123  O   GLU B 202     9730  10564  14549   1484    925    648       O  
ATOM   5124  CB  GLU B 202      48.865  30.085   9.850  1.00 90.63           C  
ANISOU 5124  CB  GLU B 202     9464  10632  14340   1648   1189    615       C  
ATOM   5125  CG  GLU B 202      49.723  29.975  11.107  1.00100.36           C  
ANISOU 5125  CG  GLU B 202    10855  11850  15429   1639   1249    423       C  
ATOM   5126  CD  GLU B 202      49.580  28.736  11.974  1.00115.87           C  
ANISOU 5126  CD  GLU B 202    12796  13970  17259   1589   1277    433       C  
ATOM   5127  OE1 GLU B 202      48.721  27.873  11.675  1.00110.30           O  
ANISOU 5127  OE1 GLU B 202    11935  13384  16592   1551   1261    592       O  
ATOM   5128  OE2 GLU B 202      50.281  28.670  13.008  1.00108.15           O  
ANISOU 5128  OE2 GLU B 202    11951  12995  16147   1599   1321    282       O  
ATOM   5129  N   LYS B 203      51.746  29.023   8.282  1.00 85.13           N  
ANISOU 5129  N   LYS B 203     9006   9848  13494   1292    854    503       N  
ATOM   5130  CA  LYS B 203      53.042  29.390   7.680  1.00 83.56           C  
ANISOU 5130  CA  LYS B 203     8931   9528  13290   1216    777    425       C  
ATOM   5131  C   LYS B 203      53.775  28.132   7.192  1.00 84.40           C  
ANISOU 5131  C   LYS B 203     9064   9711  13293   1056    645    436       C  
ATOM   5132  O   LYS B 203      54.971  27.986   7.436  1.00 82.80           O  
ANISOU 5132  O   LYS B 203     8976   9461  13023    982    613    316       O  
ATOM   5133  CB  LYS B 203      53.934  30.189   8.653  1.00 86.65           C  
ANISOU 5133  CB  LYS B 203     9462   9795  13666   1250    850    227       C  
ATOM   5134  CG  LYS B 203      53.473  31.616   8.902  1.00107.42           C  
ANISOU 5134  CG  LYS B 203    12100  12289  16424   1400    970    193       C  
ATOM   5135  CD  LYS B 203      54.517  32.385   9.680  1.00122.57           C  
ANISOU 5135  CD  LYS B 203    14164  14068  18338   1405   1009    -25       C  
ATOM   5136  CE  LYS B 203      54.147  33.835   9.842  1.00141.42           C  
ANISOU 5136  CE  LYS B 203    16573  16289  20873   1546   1126    -74       C  
ATOM   5137  NZ  LYS B 203      55.221  34.597  10.536  1.00154.74           N  
ANISOU 5137  NZ  LYS B 203    18399  17823  22572   1534   1146   -309       N  
ATOM   5138  N   TYR B 204      53.063  27.253   6.453  1.00 80.22           N  
ANISOU 5138  N   TYR B 204     8423   9293  12763   1005    563    577       N  
ATOM   5139  CA  TYR B 204      53.574  25.948   6.019  1.00 78.24           C  
ANISOU 5139  CA  TYR B 204     8187   9118  12422    862    445    590       C  
ATOM   5140  C   TYR B 204      54.677  26.098   4.934  1.00 80.52           C  
ANISOU 5140  C   TYR B 204     8569   9328  12697    793    352    576       C  
ATOM   5141  O   TYR B 204      55.703  25.416   5.041  1.00 79.19           O  
ANISOU 5141  O   TYR B 204     8486   9158  12444    697    304    500       O  
ATOM   5142  CB  TYR B 204      52.428  25.058   5.493  1.00 79.69           C  
ANISOU 5142  CB  TYR B 204     8218   9429  12632    828    380    731       C  
ATOM   5143  CG  TYR B 204      52.797  23.588   5.419  1.00 80.50           C  
ANISOU 5143  CG  TYR B 204     8330   9605  12649    688    290    724       C  
ATOM   5144  CD1 TYR B 204      53.419  23.059   4.292  1.00 81.84           C  
ANISOU 5144  CD1 TYR B 204     8544   9772  12782    592    157    738       C  
ATOM   5145  CD2 TYR B 204      52.528  22.727   6.480  1.00 81.24           C  
ANISOU 5145  CD2 TYR B 204     8399   9768  12701    660    350    708       C  
ATOM   5146  CE1 TYR B 204      53.796  21.716   4.235  1.00 82.28           C  
ANISOU 5146  CE1 TYR B 204     8619   9876  12768    469     82    722       C  
ATOM   5147  CE2 TYR B 204      52.903  21.383   6.436  1.00 81.52           C  
ANISOU 5147  CE2 TYR B 204     8449   9850  12673    536    279    708       C  
ATOM   5148  CZ  TYR B 204      53.533  20.879   5.309  1.00 89.51           C  
ANISOU 5148  CZ  TYR B 204     9504  10845  13659    439    142    710       C  
ATOM   5149  OH  TYR B 204      53.896  19.551   5.243  1.00 91.49           O  
ANISOU 5149  OH  TYR B 204     9775  11127  13859    323     76    704       O  
ATOM   5150  N   ALA B 205      54.484  26.979   3.918  1.00 76.58           N  
ANISOU 5150  N   ALA B 205     8051   8766  12278    852    337    659       N  
ATOM   5151  CA  ALA B 205      55.482  27.185   2.850  1.00 74.97           C  
ANISOU 5151  CA  ALA B 205     7932   8490  12063    804    272    670       C  
ATOM   5152  C   ALA B 205      56.767  27.792   3.408  1.00 76.62           C  
ANISOU 5152  C   ALA B 205     8265   8563  12286    788    333    533       C  
ATOM   5153  O   ALA B 205      57.861  27.352   3.046  1.00 75.85           O  
ANISOU 5153  O   ALA B 205     8242   8436  12140    702    281    494       O  
ATOM   5154  CB  ALA B 205      54.921  28.081   1.754  1.00 76.70           C  
ANISOU 5154  CB  ALA B 205     8103   8678  12363    896    262    808       C  
ATOM   5155  N   GLN B 206      56.625  28.770   4.319  1.00 71.94           N  
ANISOU 5155  N   GLN B 206     7685   7886  11762    872    441    451       N  
ATOM   5156  CA  GLN B 206      57.716  29.480   4.990  1.00 71.10           C  
ANISOU 5156  CA  GLN B 206     7681   7642  11692    865    497    295       C  
ATOM   5157  C   GLN B 206      58.577  28.494   5.758  1.00 73.21           C  
ANISOU 5157  C   GLN B 206     8008   7971  11837    766    451    168       C  
ATOM   5158  O   GLN B 206      59.793  28.533   5.630  1.00 72.17           O  
ANISOU 5158  O   GLN B 206     7949   7765  11707    696    422     85       O  
ATOM   5159  CB  GLN B 206      57.192  30.586   5.940  1.00 73.84           C  
ANISOU 5159  CB  GLN B 206     8027   7902  12126    989    618    221       C  
ATOM   5160  CG  GLN B 206      56.242  31.622   5.334  1.00 86.34           C  
ANISOU 5160  CG  GLN B 206     9545   9417  13842   1113    680    351       C  
ATOM   5161  CD  GLN B 206      54.778  31.223   5.223  1.00109.55           C  
ANISOU 5161  CD  GLN B 206    12353  12501  16771   1183    680    493       C  
ATOM   5162  OE1 GLN B 206      54.395  30.195   4.679  1.00105.82           O  
ANISOU 5162  OE1 GLN B 206    11815  12167  16226   1119    585    591       O  
ATOM   5163  NE2 GLN B 206      53.914  32.166   5.543  1.00107.53           N  
ANISOU 5163  NE2 GLN B 206    12047  12194  16616   1323    783    521       N  
ATOM   5164  N   TRP B 207      57.950  27.571   6.511  1.00 69.59           N  
ANISOU 5164  N   TRP B 207     7510   7652  11281    761    447    168       N  
ATOM   5165  CA  TRP B 207      58.638  26.530   7.271  1.00 68.38           C  
ANISOU 5165  CA  TRP B 207     7407   7575  11001    682    407     76       C  
ATOM   5166  C   TRP B 207      59.284  25.491   6.368  1.00 70.47           C  
ANISOU 5166  C   TRP B 207     7682   7883  11209    567    301    133       C  
ATOM   5167  O   TRP B 207      60.392  25.051   6.662  1.00 69.77           O  
ANISOU 5167  O   TRP B 207     7662   7791  11058    499    261     44       O  
ATOM   5168  CB  TRP B 207      57.680  25.828   8.220  1.00 67.64           C  
ANISOU 5168  CB  TRP B 207     7261   7610  10829    721    454     95       C  
ATOM   5169  CG  TRP B 207      57.587  26.482   9.554  1.00 69.80           C  
ANISOU 5169  CG  TRP B 207     7578   7867  11077    817    553    -33       C  
ATOM   5170  CD1 TRP B 207      56.629  27.349   9.984  1.00 74.10           C  
ANISOU 5170  CD1 TRP B 207     8083   8388  11684    942    660    -27       C  
ATOM   5171  CD2 TRP B 207      58.547  26.385  10.609  1.00 69.80           C  
ANISOU 5171  CD2 TRP B 207     7676   7871  10972    806    550   -197       C  
ATOM   5172  NE1 TRP B 207      56.904  27.758  11.267  1.00 74.63           N  
ANISOU 5172  NE1 TRP B 207     8227   8446  11682   1011    729   -186       N  
ATOM   5173  CE2 TRP B 207      58.083  27.189  11.673  1.00 75.37           C  
ANISOU 5173  CE2 TRP B 207     8407   8562  11668    928    655   -294       C  
ATOM   5174  CE3 TRP B 207      59.766  25.696  10.760  1.00 70.10           C  
ANISOU 5174  CE3 TRP B 207     7782   7930  10922    713    465   -272       C  
ATOM   5175  CZ2 TRP B 207      58.777  27.300  12.884  1.00 75.41           C  
ANISOU 5175  CZ2 TRP B 207     8509   8583  11560    958    665   -473       C  
ATOM   5176  CZ3 TRP B 207      60.460  25.818  11.952  1.00 72.12           C  
ANISOU 5176  CZ3 TRP B 207     8120   8203  11078    742    471   -438       C  
ATOM   5177  CH2 TRP B 207      59.966  26.608  12.999  1.00 74.43           C  
ANISOU 5177  CH2 TRP B 207     8443   8489  11347    862    564   -542       C  
ATOM   5178  N   SER B 208      58.598  25.085   5.289  1.00 66.16           N  
ANISOU 5178  N   SER B 208     7070   7383  10683    551    250    275       N  
ATOM   5179  CA  SER B 208      59.123  24.109   4.336  1.00 64.43           C  
ANISOU 5179  CA  SER B 208     6869   7205  10407    454    149    324       C  
ATOM   5180  C   SER B 208      60.391  24.642   3.660  1.00 67.93           C  
ANISOU 5180  C   SER B 208     7393   7542  10876    421    133    288       C  
ATOM   5181  O   SER B 208      61.345  23.892   3.483  1.00 66.46           O  
ANISOU 5181  O   SER B 208     7256   7369  10625    341     79    256       O  
ATOM   5182  CB  SER B 208      58.068  23.769   3.292  1.00 67.61           C  
ANISOU 5182  CB  SER B 208     7184   7677  10826    459     90    466       C  
ATOM   5183  OG  SER B 208      56.895  23.242   3.888  1.00 77.55           O  
ANISOU 5183  OG  SER B 208     8348   9034  12086    473    104    509       O  
ATOM   5184  N   ALA B 209      60.408  25.946   3.318  1.00 65.88           N  
ANISOU 5184  N   ALA B 209     7141   7168  10722    487    191    298       N  
ATOM   5185  CA  ALA B 209      61.556  26.605   2.694  1.00 65.24           C  
ANISOU 5185  CA  ALA B 209     7122   6968  10698    461    201    280       C  
ATOM   5186  C   ALA B 209      62.668  26.817   3.711  1.00 68.27           C  
ANISOU 5186  C   ALA B 209     7562   7283  11096    420    224    114       C  
ATOM   5187  O   ALA B 209      63.824  26.578   3.393  1.00 67.70           O  
ANISOU 5187  O   ALA B 209     7530   7171  11023    351    197     79       O  
ATOM   5188  CB  ALA B 209      61.134  27.934   2.083  1.00 66.97           C  
ANISOU 5188  CB  ALA B 209     7325   7076  11043    549    265    362       C  
ATOM   5189  N   GLY B 210      62.299  27.204   4.932  1.00 64.97           N  
ANISOU 5189  N   GLY B 210     7140   6861  10684    469    271     12       N  
ATOM   5190  CA  GLY B 210      63.226  27.459   6.030  1.00 64.69           C  
ANISOU 5190  CA  GLY B 210     7156   6776  10647    445    279   -166       C  
ATOM   5191  C   GLY B 210      63.994  26.243   6.504  1.00 67.37           C  
ANISOU 5191  C   GLY B 210     7522   7218  10858    367    206   -224       C  
ATOM   5192  O   GLY B 210      65.219  26.312   6.653  1.00 66.89           O  
ANISOU 5192  O   GLY B 210     7494   7104  10817    309    174   -316       O  
ATOM   5193  N   ILE B 211      63.277  25.119   6.747  1.00 63.23           N  
ANISOU 5193  N   ILE B 211     6973   6835  10217    367    181   -162       N  
ATOM   5194  CA  ILE B 211      63.875  23.864   7.220  1.00 62.56           C  
ANISOU 5194  CA  ILE B 211     6912   6848  10009    306    122   -193       C  
ATOM   5195  C   ILE B 211      64.738  23.263   6.089  1.00 67.03           C  
ANISOU 5195  C   ILE B 211     7491   7399  10578    223     60   -133       C  
ATOM   5196  O   ILE B 211      65.772  22.679   6.399  1.00 66.47           O  
ANISOU 5196  O   ILE B 211     7452   7346  10456    173     17   -197       O  
ATOM   5197  CB  ILE B 211      62.801  22.859   7.738  1.00 65.42           C  
ANISOU 5197  CB  ILE B 211     7237   7343  10276    327    132   -121       C  
ATOM   5198  CG1 ILE B 211      62.063  23.419   8.993  1.00 67.18           C  
ANISOU 5198  CG1 ILE B 211     7454   7593  10478    424    214   -185       C  
ATOM   5199  CG2 ILE B 211      63.387  21.484   8.048  1.00 65.10           C  
ANISOU 5199  CG2 ILE B 211     7222   7388  10124    266     77   -121       C  
ATOM   5200  CD1 ILE B 211      62.927  23.733  10.301  1.00 75.57           C  
ANISOU 5200  CD1 ILE B 211     8588   8656  11469    454    219   -362       C  
ATOM   5201  N   ALA B 212      64.371  23.476   4.799  1.00 64.31           N  
ANISOU 5201  N   ALA B 212     7126   7020  10290    222     58    -16       N  
ATOM   5202  CA  ALA B 212      65.162  22.991   3.656  1.00 63.72           C  
ANISOU 5202  CA  ALA B 212     7075   6931  10205    163     14     41       C  
ATOM   5203  C   ALA B 212      66.529  23.687   3.605  1.00 69.14           C  
ANISOU 5203  C   ALA B 212     7791   7509  10970    134     33    -35       C  
ATOM   5204  O   ALA B 212      67.531  23.026   3.336  1.00 67.76           O  
ANISOU 5204  O   ALA B 212     7639   7347  10761     78     -2    -48       O  
ATOM   5205  CB  ALA B 212      64.413  23.211   2.357  1.00 64.60           C  
ANISOU 5205  CB  ALA B 212     7164   7039  10343    191     11    177       C  
ATOM   5206  N   LEU B 213      66.573  25.010   3.907  1.00 67.90           N  
ANISOU 5206  N   LEU B 213     7627   7240  10932    171     91    -90       N  
ATOM   5207  CA  LEU B 213      67.814  25.784   3.974  1.00 68.82           C  
ANISOU 5207  CA  LEU B 213     7754   7235  11161    135    112   -176       C  
ATOM   5208  C   LEU B 213      68.689  25.310   5.146  1.00 73.17           C  
ANISOU 5208  C   LEU B 213     8315   7829  11658     93     60   -329       C  
ATOM   5209  O   LEU B 213      69.909  25.283   5.005  1.00 72.77           O  
ANISOU 5209  O   LEU B 213     8260   7737  11653     35     38   -375       O  
ATOM   5210  CB  LEU B 213      67.542  27.300   4.098  1.00 70.64           C  
ANISOU 5210  CB  LEU B 213     7975   7316  11548    183    187   -206       C  
ATOM   5211  CG  LEU B 213      67.454  28.173   2.803  1.00 76.99           C  
ANISOU 5211  CG  LEU B 213     8772   8006  12476    208    254    -66       C  
ATOM   5212  CD1 LEU B 213      68.784  28.202   2.044  1.00 77.83           C  
ANISOU 5212  CD1 LEU B 213     8880   8034  12657    139    266    -49       C  
ATOM   5213  CD2 LEU B 213      66.354  27.754   1.892  1.00 79.11           C  
ANISOU 5213  CD2 LEU B 213     9033   8366  12658    259    244    102       C  
ATOM   5214  N   MET B 214      68.070  24.914   6.284  1.00 70.00           N  
ANISOU 5214  N   MET B 214     7922   7521  11153    131     41   -397       N  
ATOM   5215  CA  MET B 214      68.778  24.382   7.457  1.00 69.70           C  
ANISOU 5215  CA  MET B 214     7902   7556  11026    114    -14   -527       C  
ATOM   5216  C   MET B 214      69.505  23.076   7.094  1.00 72.99           C  
ANISOU 5216  C   MET B 214     8323   8056  11356     59    -72   -472       C  
ATOM   5217  O   MET B 214      70.631  22.871   7.539  1.00 73.87           O  
ANISOU 5217  O   MET B 214     8432   8177  11457     25   -122   -561       O  
ATOM   5218  CB  MET B 214      67.803  24.155   8.624  1.00 72.35           C  
ANISOU 5218  CB  MET B 214     8253   7988  11248    186      1   -568       C  
ATOM   5219  CG  MET B 214      68.445  23.559   9.864  1.00 75.98           C  
ANISOU 5219  CG  MET B 214     8741   8550  11580    190    -55   -680       C  
ATOM   5220  SD  MET B 214      67.227  23.301  11.157  1.00 80.92           S  
ANISOU 5220  SD  MET B 214     9390   9289  12066    294     -6   -703       S  
ATOM   5221  CE  MET B 214      68.212  22.551  12.381  1.00 77.81           C  
ANISOU 5221  CE  MET B 214     9035   9023  11505    299    -82   -795       C  
ATOM   5222  N   LYS B 215      68.868  22.212   6.274  1.00 67.64           N  
ANISOU 5222  N   LYS B 215     7645   7432  10623     53    -70   -333       N  
ATOM   5223  CA  LYS B 215      69.449  20.954   5.786  1.00 66.09           C  
ANISOU 5223  CA  LYS B 215     7461   7296  10353      7   -116   -276       C  
ATOM   5224  C   LYS B 215      70.741  21.221   4.995  1.00 70.54           C  
ANISOU 5224  C   LYS B 215     8020   7781  11001    -40   -118   -281       C  
ATOM   5225  O   LYS B 215      71.740  20.545   5.225  1.00 71.05           O  
ANISOU 5225  O   LYS B 215     8086   7878  11033    -70   -157   -317       O  
ATOM   5226  CB  LYS B 215      68.445  20.185   4.903  1.00 67.05           C  
ANISOU 5226  CB  LYS B 215     7585   7467  10425      7   -116   -143       C  
ATOM   5227  CG  LYS B 215      67.133  19.823   5.586  1.00 71.13           C  
ANISOU 5227  CG  LYS B 215     8084   8062  10879     43   -106   -115       C  
ATOM   5228  CD  LYS B 215      66.171  19.141   4.626  1.00 69.33           C  
ANISOU 5228  CD  LYS B 215     7838   7871  10634     29   -122      5       C  
ATOM   5229  CE  LYS B 215      64.878  18.775   5.291  1.00 67.08           C  
ANISOU 5229  CE  LYS B 215     7513   7659  10317     55   -105     44       C  
ATOM   5230  NZ  LYS B 215      63.984  18.039   4.369  1.00 78.98           N  
ANISOU 5230  NZ  LYS B 215     8985   9200  11823     27   -140    148       N  
ATOM   5231  N   ASN B 216      70.716  22.218   4.072  1.00 66.42           N  
ANISOU 5231  N   ASN B 216     7486   7155  10595    -37    -66   -234       N  
ATOM   5232  CA  ASN B 216      71.848  22.596   3.225  1.00 66.01           C  
ANISOU 5232  CA  ASN B 216     7420   7019  10641    -75    -40   -213       C  
ATOM   5233  C   ASN B 216      72.999  23.165   4.041  1.00 71.14           C  
ANISOU 5233  C   ASN B 216     8033   7609  11389   -111    -55   -350       C  
ATOM   5234  O   ASN B 216      74.113  22.653   3.951  1.00 70.69           O  
ANISOU 5234  O   ASN B 216     7954   7564  11339   -150    -80   -368       O  
ATOM   5235  CB  ASN B 216      71.431  23.634   2.163  1.00 64.91           C  
ANISOU 5235  CB  ASN B 216     7279   6781  10602    -50     34   -112       C  
ATOM   5236  CG  ASN B 216      70.474  23.166   1.095  1.00 75.94           C  
ANISOU 5236  CG  ASN B 216     8707   8238  11910    -15     35     28       C  
ATOM   5237  OD1 ASN B 216      69.729  23.962   0.521  1.00 67.97           O  
ANISOU 5237  OD1 ASN B 216     7695   7183  10946     31     77    110       O  
ATOM   5238  ND2 ASN B 216      70.464  21.878   0.793  1.00 65.64           N  
ANISOU 5238  ND2 ASN B 216     7429   7034  10478    -32    -17     55       N  
ATOM   5239  N   ILE B 217      72.728  24.224   4.831  1.00 68.69           N  
ANISOU 5239  N   ILE B 217     7709   7232  11157    -95    -45   -453       N  
ATOM   5240  CA  ILE B 217      73.728  24.953   5.615  1.00 69.63           C  
ANISOU 5240  CA  ILE B 217     7788   7277  11390   -133    -72   -608       C  
ATOM   5241  C   ILE B 217      74.379  24.035   6.677  1.00 73.82           C  
ANISOU 5241  C   ILE B 217     8315   7932  11801   -143   -169   -714       C  
ATOM   5242  O   ILE B 217      75.598  23.876   6.673  1.00 73.91           O  
ANISOU 5242  O   ILE B 217     8278   7934  11869   -192   -207   -757       O  
ATOM   5243  CB  ILE B 217      73.097  26.209   6.291  1.00 73.71           C  
ANISOU 5243  CB  ILE B 217     8312   7699  11996   -100    -43   -711       C  
ATOM   5244  CG1 ILE B 217      72.475  27.150   5.228  1.00 74.50           C  
ANISOU 5244  CG1 ILE B 217     8412   7666  12227    -77     59   -588       C  
ATOM   5245  CG2 ILE B 217      74.141  26.953   7.144  1.00 75.31           C  
ANISOU 5245  CG2 ILE B 217     8474   7822  12318   -147    -92   -903       C  
ATOM   5246  CD1 ILE B 217      71.655  28.322   5.781  1.00 83.44           C  
ANISOU 5246  CD1 ILE B 217     9559   8699  13445    -24    106   -660       C  
ATOM   5247  N   LEU B 218      73.569  23.443   7.560  1.00 70.20           N  
ANISOU 5247  N   LEU B 218     7899   7589  11184    -90   -202   -742       N  
ATOM   5248  CA  LEU B 218      74.018  22.658   8.707  1.00 69.87           C  
ANISOU 5248  CA  LEU B 218     7865   7672  11009    -75   -286   -832       C  
ATOM   5249  C   LEU B 218      74.512  21.239   8.312  1.00 71.40           C  
ANISOU 5249  C   LEU B 218     8060   7958  11110    -90   -315   -732       C  
ATOM   5250  O   LEU B 218      75.422  20.723   8.955  1.00 72.02           O  
ANISOU 5250  O   LEU B 218     8120   8106  11137    -92   -386   -798       O  
ATOM   5251  CB  LEU B 218      72.836  22.544   9.690  1.00 70.26           C  
ANISOU 5251  CB  LEU B 218     7965   7809  10920      1   -277   -859       C  
ATOM   5252  CG  LEU B 218      73.098  22.027  11.092  1.00 76.22           C  
ANISOU 5252  CG  LEU B 218     8744   8694  11522     47   -348   -963       C  
ATOM   5253  CD1 LEU B 218      74.106  22.912  11.840  1.00 78.26           C  
ANISOU 5253  CD1 LEU B 218     8976   8913  11847     30   -423  -1162       C  
ATOM   5254  CD2 LEU B 218      71.821  21.988  11.872  1.00 78.46           C  
ANISOU 5254  CD2 LEU B 218     9076   9050  11683    129   -301   -955       C  
ATOM   5255  N   GLY B 219      73.924  20.638   7.283  1.00 65.37           N  
ANISOU 5255  N   GLY B 219     7319   7193  10325    -94   -266   -584       N  
ATOM   5256  CA  GLY B 219      74.264  19.284   6.857  1.00 63.42           C  
ANISOU 5256  CA  GLY B 219     7087   7014   9995   -103   -284   -494       C  
ATOM   5257  C   GLY B 219      75.197  19.131   5.669  1.00 65.35           C  
ANISOU 5257  C   GLY B 219     7309   7199  10323   -144   -259   -431       C  
ATOM   5258  O   GLY B 219      75.637  18.010   5.380  1.00 64.28           O  
ANISOU 5258  O   GLY B 219     7188   7113  10123   -145   -274   -377       O  
ATOM   5259  N   PHE B 220      75.509  20.229   4.955  1.00 61.03           N  
ANISOU 5259  N   PHE B 220     6728   6541   9921   -170   -209   -430       N  
ATOM   5260  CA  PHE B 220      76.409  20.118   3.807  1.00 60.07           C  
ANISOU 5260  CA  PHE B 220     6584   6366   9875   -198   -164   -355       C  
ATOM   5261  C   PHE B 220      77.384  21.313   3.747  1.00 65.88           C  
ANISOU 5261  C   PHE B 220     7242   6987  10802   -241   -135   -414       C  
ATOM   5262  O   PHE B 220      78.586  21.085   3.801  1.00 66.00           O  
ANISOU 5262  O   PHE B 220     7196   7001  10879   -270   -152   -444       O  
ATOM   5263  CB  PHE B 220      75.618  20.007   2.486  1.00 60.51           C  
ANISOU 5263  CB  PHE B 220     6692   6403   9896   -178   -101   -217       C  
ATOM   5264  CG  PHE B 220      76.466  19.736   1.260  1.00 60.77           C  
ANISOU 5264  CG  PHE B 220     6725   6406   9959   -186    -45   -129       C  
ATOM   5265  CD1 PHE B 220      76.906  18.449   0.967  1.00 62.32           C  
ANISOU 5265  CD1 PHE B 220     6950   6671  10056   -177    -66    -99       C  
ATOM   5266  CD2 PHE B 220      76.770  20.755   0.365  1.00 61.98           C  
ANISOU 5266  CD2 PHE B 220     6855   6458  10235   -190     41    -65       C  
ATOM   5267  CE1 PHE B 220      77.673  18.196  -0.169  1.00 62.60           C  
ANISOU 5267  CE1 PHE B 220     6993   6684  10107   -169     -2    -22       C  
ATOM   5268  CE2 PHE B 220      77.538  20.499  -0.773  1.00 64.41           C  
ANISOU 5268  CE2 PHE B 220     7169   6750  10554   -182    111     27       C  
ATOM   5269  CZ  PHE B 220      77.981  19.221  -1.033  1.00 61.83           C  
ANISOU 5269  CZ  PHE B 220     6874   6501  10119   -169     88     43       C  
ATOM   5270  N   ILE B 221      76.875  22.567   3.642  1.00 63.21           N  
ANISOU 5270  N   ILE B 221     6899   6545  10573   -243    -87   -426       N  
ATOM   5271  CA  ILE B 221      77.681  23.785   3.479  1.00 64.35           C  
ANISOU 5271  CA  ILE B 221     6971   6546  10934   -291    -41   -468       C  
ATOM   5272  C   ILE B 221      78.741  23.884   4.598  1.00 69.54           C  
ANISOU 5272  C   ILE B 221     7551   7210  11661   -337   -130   -636       C  
ATOM   5273  O   ILE B 221      79.929  23.836   4.277  1.00 69.86           O  
ANISOU 5273  O   ILE B 221     7511   7216  11816   -384   -121   -631       O  
ATOM   5274  CB  ILE B 221      76.805  25.078   3.433  1.00 68.48           C  
ANISOU 5274  CB  ILE B 221     7512   6951  11555   -274     16   -471       C  
ATOM   5275  CG1 ILE B 221      75.694  25.021   2.323  1.00 68.73           C  
ANISOU 5275  CG1 ILE B 221     7610   6990  11512   -216     89   -300       C  
ATOM   5276  CG2 ILE B 221      77.654  26.354   3.324  1.00 70.32           C  
ANISOU 5276  CG2 ILE B 221     7668   7009  12041   -332     69   -520       C  
ATOM   5277  CD1 ILE B 221      76.160  24.798   0.831  1.00 81.05           C  
ANISOU 5277  CD1 ILE B 221     9177   8529  13090   -213    171   -134       C  
ATOM   5278  N   ILE B 222      78.325  24.010   5.886  1.00 66.71           N  
ANISOU 5278  N   ILE B 222     7211   6906  11230   -318   -215   -780       N  
ATOM   5279  CA  ILE B 222      79.245  24.157   7.032  1.00 67.63           C  
ANISOU 5279  CA  ILE B 222     7261   7046  11388   -351   -323   -959       C  
ATOM   5280  C   ILE B 222      80.210  22.920   7.114  1.00 71.04           C  
ANISOU 5280  C   ILE B 222     7653   7601  11739   -352   -386   -932       C  
ATOM   5281  O   ILE B 222      81.420  23.146   7.072  1.00 70.69           O  
ANISOU 5281  O   ILE B 222     7505   7515  11840   -408   -412   -979       O  
ATOM   5282  CB  ILE B 222      78.495  24.378   8.381  1.00 71.01           C  
ANISOU 5282  CB  ILE B 222     7743   7539  11700   -303   -399  -1110       C  
ATOM   5283  CG1 ILE B 222      77.750  25.734   8.370  1.00 71.88           C  
ANISOU 5283  CG1 ILE B 222     7880   7508  11925   -299   -334  -1158       C  
ATOM   5284  CG2 ILE B 222      79.464  24.307   9.573  1.00 73.20           C  
ANISOU 5284  CG2 ILE B 222     7960   7878  11974   -323   -533  -1295       C  
ATOM   5285  CD1 ILE B 222      76.882  26.005   9.597  1.00 79.54           C  
ANISOU 5285  CD1 ILE B 222     8915   8537  12768   -233   -382  -1299       C  
ATOM   5286  N   PRO B 223      79.754  21.636   7.180  1.00 66.84           N  
ANISOU 5286  N   PRO B 223     7189   7205  11003   -295   -404   -851       N  
ATOM   5287  CA  PRO B 223      80.732  20.533   7.264  1.00 66.40           C  
ANISOU 5287  CA  PRO B 223     7092   7244  10894   -288   -456   -828       C  
ATOM   5288  C   PRO B 223      81.684  20.483   6.060  1.00 71.37           C  
ANISOU 5288  C   PRO B 223     7655   7801  11662   -328   -380   -726       C  
ATOM   5289  O   PRO B 223      82.857  20.179   6.255  1.00 72.05           O  
ANISOU 5289  O   PRO B 223     7651   7918  11808   -345   -425   -758       O  
ATOM   5290  CB  PRO B 223      79.863  19.275   7.311  1.00 66.58           C  
ANISOU 5290  CB  PRO B 223     7213   7379  10704   -224   -455   -734       C  
ATOM   5291  CG  PRO B 223      78.526  19.699   6.884  1.00 70.51           C  
ANISOU 5291  CG  PRO B 223     7787   7832  11173   -211   -385   -675       C  
ATOM   5292  CD  PRO B 223      78.373  21.122   7.259  1.00 67.11           C  
ANISOU 5292  CD  PRO B 223     7327   7306  10865   -235   -380   -783       C  
ATOM   5293  N   LEU B 224      81.206  20.821   4.838  1.00 67.54           N  
ANISOU 5293  N   LEU B 224     7208   7228  11227   -334   -262   -604       N  
ATOM   5294  CA  LEU B 224      82.044  20.801   3.636  1.00 67.28           C  
ANISOU 5294  CA  LEU B 224     7126   7132  11308   -355   -167   -495       C  
ATOM   5295  C   LEU B 224      83.106  21.916   3.735  1.00 72.80           C  
ANISOU 5295  C   LEU B 224     7688   7722  12252   -428   -160   -569       C  
ATOM   5296  O   LEU B 224      84.229  21.689   3.288  1.00 74.08           O  
ANISOU 5296  O   LEU B 224     7759   7879  12510   -448   -133   -533       O  
ATOM   5297  CB  LEU B 224      81.193  20.932   2.342  1.00 66.59           C  
ANISOU 5297  CB  LEU B 224     7122   6987  11192   -330    -50   -348       C  
ATOM   5298  CG  LEU B 224      81.859  20.701   0.956  1.00 71.59           C  
ANISOU 5298  CG  LEU B 224     7742   7579  11881   -322     69   -207       C  
ATOM   5299  CD1 LEU B 224      82.518  21.942   0.394  1.00 73.29           C  
ANISOU 5299  CD1 LEU B 224     7863   7652  12332   -372    163   -182       C  
ATOM   5300  CD2 LEU B 224      82.730  19.450   0.917  1.00 73.54           C  
ANISOU 5300  CD2 LEU B 224     7974   7916  12052   -296     51   -184       C  
ATOM   5301  N   ILE B 225      82.785  23.079   4.368  1.00 68.79           N  
ANISOU 5301  N   ILE B 225     7160   7123  11854   -467   -184   -681       N  
ATOM   5302  CA  ILE B 225      83.765  24.164   4.573  1.00 69.82           C  
ANISOU 5302  CA  ILE B 225     7155   7130  12242   -551   -191   -777       C  
ATOM   5303  C   ILE B 225      84.955  23.591   5.350  1.00 74.57           C  
ANISOU 5303  C   ILE B 225     7646   7827  12859   -573   -315   -884       C  
ATOM   5304  O   ILE B 225      86.081  23.723   4.887  1.00 75.46           O  
ANISOU 5304  O   ILE B 225     7631   7891  13151   -623   -281   -855       O  
ATOM   5305  CB  ILE B 225      83.162  25.422   5.278  1.00 73.51           C  
ANISOU 5305  CB  ILE B 225     7637   7488  12805   -580   -218   -914       C  
ATOM   5306  CG1 ILE B 225      82.123  26.123   4.361  1.00 73.46           C  
ANISOU 5306  CG1 ILE B 225     7712   7364  12836   -556    -78   -781       C  
ATOM   5307  CG2 ILE B 225      84.271  26.403   5.689  1.00 75.45           C  
ANISOU 5307  CG2 ILE B 225     7734   7613  13321   -679   -264  -1059       C  
ATOM   5308  CD1 ILE B 225      81.361  27.338   4.970  1.00 79.00           C  
ANISOU 5308  CD1 ILE B 225     8447   7947  13624   -562    -81   -894       C  
ATOM   5309  N   PHE B 226      84.692  22.882   6.473  1.00 71.08           N  
ANISOU 5309  N   PHE B 226     7253   7532  12223   -524   -449   -984       N  
ATOM   5310  CA  PHE B 226      85.706  22.223   7.307  1.00 71.41           C  
ANISOU 5310  CA  PHE B 226     7202   7693  12235   -520   -584  -1077       C  
ATOM   5311  C   PHE B 226      86.499  21.165   6.534  1.00 74.26           C  
ANISOU 5311  C   PHE B 226     7515   8113  12587   -494   -533   -936       C  
ATOM   5312  O   PHE B 226      87.729  21.198   6.564  1.00 75.13           O  
ANISOU 5312  O   PHE B 226     7474   8220  12851   -534   -569   -968       O  
ATOM   5313  CB  PHE B 226      85.063  21.559   8.528  1.00 72.70           C  
ANISOU 5313  CB  PHE B 226     7461   8013  12150   -444   -705  -1163       C  
ATOM   5314  CG  PHE B 226      84.631  22.506   9.619  1.00 75.80           C  
ANISOU 5314  CG  PHE B 226     7872   8385  12542   -458   -796  -1355       C  
ATOM   5315  CD1 PHE B 226      83.413  23.173   9.544  1.00 78.57           C  
ANISOU 5315  CD1 PHE B 226     8324   8652  12875   -449   -723  -1357       C  
ATOM   5316  CD2 PHE B 226      85.408  22.680  10.755  1.00 79.82           C  
ANISOU 5316  CD2 PHE B 226     8307   8976  13045   -463   -961  -1537       C  
ATOM   5317  CE1 PHE B 226      83.011  24.045  10.559  1.00 80.57           C  
ANISOU 5317  CE1 PHE B 226     8605   8884  13125   -448   -797  -1543       C  
ATOM   5318  CE2 PHE B 226      84.999  23.544  11.774  1.00 84.12           C  
ANISOU 5318  CE2 PHE B 226     8886   9508  13568   -464  -1048  -1734       C  
ATOM   5319  CZ  PHE B 226      83.802  24.220  11.668  1.00 81.67           C  
ANISOU 5319  CZ  PHE B 226     8681   9099  13252   -455   -958  -1737       C  
ATOM   5320  N   ILE B 227      85.805  20.239   5.845  1.00 68.63           N  
ANISOU 5320  N   ILE B 227     6922   7448  11707   -427   -451   -787       N  
ATOM   5321  CA  ILE B 227      86.421  19.135   5.097  1.00 68.13           C  
ANISOU 5321  CA  ILE B 227     6843   7437  11606   -385   -394   -658       C  
ATOM   5322  C   ILE B 227      87.335  19.703   3.970  1.00 72.39           C  
ANISOU 5322  C   ILE B 227     7274   7860  12369   -435   -265   -572       C  
ATOM   5323  O   ILE B 227      88.469  19.231   3.827  1.00 73.54           O  
ANISOU 5323  O   ILE B 227     7305   8037  12600   -431   -263   -548       O  
ATOM   5324  CB  ILE B 227      85.330  18.173   4.527  1.00 69.72           C  
ANISOU 5324  CB  ILE B 227     7212   7687  11592   -313   -333   -539       C  
ATOM   5325  CG1 ILE B 227      84.490  17.559   5.678  1.00 69.95           C  
ANISOU 5325  CG1 ILE B 227     7330   7827  11421   -265   -444   -606       C  
ATOM   5326  CG2 ILE B 227      85.962  17.061   3.684  1.00 69.78           C  
ANISOU 5326  CG2 ILE B 227     7220   7731  11564   -264   -266   -420       C  
ATOM   5327  CD1 ILE B 227      83.266  16.716   5.266  1.00 77.44           C  
ANISOU 5327  CD1 ILE B 227     8429   8807  12188   -215   -396   -509       C  
ATOM   5328  N   ALA B 228      86.860  20.719   3.210  1.00 67.10           N  
ANISOU 5328  N   ALA B 228     6635   7060  11801   -472   -152   -518       N  
ATOM   5329  CA  ALA B 228      87.630  21.320   2.115  1.00 67.00           C  
ANISOU 5329  CA  ALA B 228     6531   6929  11996   -511     -4   -412       C  
ATOM   5330  C   ALA B 228      88.845  22.091   2.640  1.00 72.47           C  
ANISOU 5330  C   ALA B 228     7021   7555  12958   -602    -51   -514       C  
ATOM   5331  O   ALA B 228      89.937  21.912   2.105  1.00 73.74           O  
ANISOU 5331  O   ALA B 228     7058   7700  13262   -615     22   -440       O  
ATOM   5332  CB  ALA B 228      86.750  22.245   1.293  1.00 67.26           C  
ANISOU 5332  CB  ALA B 228     6650   6843  12064   -520    116   -329       C  
ATOM   5333  N   THR B 229      88.666  22.918   3.698  1.00 68.84           N  
ANISOU 5333  N   THR B 229     6525   7060  12571   -662   -176   -690       N  
ATOM   5334  CA  THR B 229      89.740  23.723   4.289  1.00 70.39           C  
ANISOU 5334  CA  THR B 229     6528   7188  13031   -761   -252   -823       C  
ATOM   5335  C   THR B 229      90.829  22.803   4.865  1.00 75.08           C  
ANISOU 5335  C   THR B 229     6999   7925  13604   -742   -370   -871       C  
ATOM   5336  O   THR B 229      92.015  23.099   4.700  1.00 76.35           O  
ANISOU 5336  O   THR B 229     6968   8039  14003   -805   -359   -874       O  
ATOM   5337  CB  THR B 229      89.182  24.667   5.363  1.00 76.41           C  
ANISOU 5337  CB  THR B 229     7313   7896  13824   -811   -375  -1025       C  
ATOM   5338  OG1 THR B 229      88.148  25.459   4.781  1.00 72.44           O  
ANISOU 5338  OG1 THR B 229     6920   7257  13345   -813   -252   -960       O  
ATOM   5339  CG2 THR B 229      90.247  25.587   5.956  1.00 77.98           C  
ANISOU 5339  CG2 THR B 229     7312   8006  14309   -926   -470  -1191       C  
ATOM   5340  N   CYS B 230      90.435  21.679   5.502  1.00 70.67           N  
ANISOU 5340  N   CYS B 230     6542   7536  12774   -650   -473   -891       N  
ATOM   5341  CA  CYS B 230      91.401  20.732   6.061  1.00 71.00           C  
ANISOU 5341  CA  CYS B 230     6481   7722  12774   -607   -584   -916       C  
ATOM   5342  C   CYS B 230      92.135  20.000   4.936  1.00 73.47           C  
ANISOU 5342  C   CYS B 230     6743   8039  13133   -565   -438   -732       C  
ATOM   5343  O   CYS B 230      93.289  19.645   5.133  1.00 74.58           O  
ANISOU 5343  O   CYS B 230     6726   8243  13368   -559   -489   -739       O  
ATOM   5344  CB  CYS B 230      90.732  19.747   7.009  1.00 70.48           C  
ANISOU 5344  CB  CYS B 230     6548   7821  12411   -512   -712   -965       C  
ATOM   5345  SG  CYS B 230      90.122  20.500   8.537  1.00 75.34           S  
ANISOU 5345  SG  CYS B 230     7200   8474  12953   -537   -902  -1202       S  
ATOM   5346  N   TYR B 231      91.499  19.801   3.760  1.00 67.87           N  
ANISOU 5346  N   TYR B 231     6161   7266  12359   -530   -259   -573       N  
ATOM   5347  CA  TYR B 231      92.169  19.150   2.637  1.00 67.48           C  
ANISOU 5347  CA  TYR B 231     6083   7217  12339   -479   -105   -406       C  
ATOM   5348  C   TYR B 231      93.271  20.039   2.073  1.00 74.40           C  
ANISOU 5348  C   TYR B 231     6755   7981  13531   -559     -4   -366       C  
ATOM   5349  O   TYR B 231      94.410  19.587   1.952  1.00 75.31           O  
ANISOU 5349  O   TYR B 231     6717   8143  13754   -543      6   -332       O  
ATOM   5350  CB  TYR B 231      91.191  18.760   1.513  1.00 66.99           C  
ANISOU 5350  CB  TYR B 231     6221   7127  12104   -415     45   -263       C  
ATOM   5351  CG  TYR B 231      91.910  18.356   0.242  1.00 68.99           C  
ANISOU 5351  CG  TYR B 231     6445   7354  12415   -368    231    -99       C  
ATOM   5352  CD1 TYR B 231      92.638  17.172   0.175  1.00 70.88           C  
ANISOU 5352  CD1 TYR B 231     6660   7687  12585   -285    241    -49       C  
ATOM   5353  CD2 TYR B 231      91.851  19.152  -0.897  1.00 70.15           C  
ANISOU 5353  CD2 TYR B 231     6593   7380  12679   -394    407     14       C  
ATOM   5354  CE1 TYR B 231      93.329  16.813  -0.978  1.00 71.62           C  
ANISOU 5354  CE1 TYR B 231     6726   7757  12728   -230    423     94       C  
ATOM   5355  CE2 TYR B 231      92.523  18.794  -2.063  1.00 71.63           C  
ANISOU 5355  CE2 TYR B 231     6760   7553  12904   -336    591    170       C  
ATOM   5356  CZ  TYR B 231      93.256  17.618  -2.100  1.00 78.66           C  
ANISOU 5356  CZ  TYR B 231     7625   8540  13721   -254    599    203       C  
ATOM   5357  OH  TYR B 231      93.919  17.249  -3.244  1.00 80.55           O  
ANISOU 5357  OH  TYR B 231     7850   8768  13987   -184    791    350       O  
ATOM   5358  N   PHE B 232      92.933  21.289   1.705  1.00 71.85           N  
ANISOU 5358  N   PHE B 232     6424   7505  13370   -641     80   -360       N  
ATOM   5359  CA  PHE B 232      93.896  22.225   1.132  1.00 73.13           C  
ANISOU 5359  CA  PHE B 232     6392   7533  13860   -727    199   -305       C  
ATOM   5360  C   PHE B 232      94.907  22.682   2.207  1.00 78.56           C  
ANISOU 5360  C   PHE B 232     6851   8222  14775   -826     30   -479       C  
ATOM   5361  O   PHE B 232      96.026  23.067   1.860  1.00 79.35           O  
ANISOU 5361  O   PHE B 232     6739   8255  15155   -889     99   -438       O  
ATOM   5362  CB  PHE B 232      93.187  23.426   0.491  1.00 74.66           C  
ANISOU 5362  CB  PHE B 232     6651   7552  14163   -781    334   -246       C  
ATOM   5363  CG  PHE B 232      92.349  23.037  -0.708  1.00 74.26           C  
ANISOU 5363  CG  PHE B 232     6800   7507  13910   -681    502    -63       C  
ATOM   5364  CD1 PHE B 232      92.946  22.739  -1.930  1.00 77.51           C  
ANISOU 5364  CD1 PHE B 232     7187   7901  14364   -629    705    129       C  
ATOM   5365  CD2 PHE B 232      90.962  23.017  -0.630  1.00 74.63           C  
ANISOU 5365  CD2 PHE B 232     7053   7576  13727   -638    459    -84       C  
ATOM   5366  CE1 PHE B 232      92.172  22.377  -3.037  1.00 77.26           C  
ANISOU 5366  CE1 PHE B 232     7346   7885  14123   -530    845    282       C  
ATOM   5367  CE2 PHE B 232      90.187  22.662  -1.741  1.00 76.33           C  
ANISOU 5367  CE2 PHE B 232     7442   7804  13757   -549    593     73       C  
ATOM   5368  CZ  PHE B 232      90.798  22.355  -2.941  1.00 74.89           C  
ANISOU 5368  CZ  PHE B 232     7244   7611  13600   -495    778    249       C  
ATOM   5369  N   GLY B 233      94.527  22.558   3.483  1.00 75.32           N  
ANISOU 5369  N   GLY B 233     6481   7903  14233   -828   -190   -666       N  
ATOM   5370  CA  GLY B 233      95.395  22.834   4.622  1.00 77.20           C  
ANISOU 5370  CA  GLY B 233     6527   8184  14621   -900   -394   -856       C  
ATOM   5371  C   GLY B 233      96.488  21.783   4.727  1.00 82.19           C  
ANISOU 5371  C   GLY B 233     7018   8962  15248   -839   -445   -813       C  
ATOM   5372  O   GLY B 233      97.656  22.117   4.960  1.00 83.90           O  
ANISOU 5372  O   GLY B 233     6990   9172  15716   -911   -516   -878       O  
ATOM   5373  N   ILE B 234      96.111  20.494   4.515  1.00 77.20           N  
ANISOU 5373  N   ILE B 234     6533   8456  14342   -703   -405   -699       N  
ATOM   5374  CA  ILE B 234      97.026  19.347   4.480  1.00 77.44           C  
ANISOU 5374  CA  ILE B 234     6466   8618  14340   -614   -420   -626       C  
ATOM   5375  C   ILE B 234      97.861  19.442   3.201  1.00 83.69           C  
ANISOU 5375  C   ILE B 234     7134   9320  15342   -621   -193   -450       C  
ATOM   5376  O   ILE B 234      99.082  19.376   3.271  1.00 84.97           O  
ANISOU 5376  O   ILE B 234     7063   9510  15711   -639   -208   -440       O  
ATOM   5377  CB  ILE B 234      96.256  17.994   4.586  1.00 78.20           C  
ANISOU 5377  CB  ILE B 234     6780   8847  14086   -470   -438   -566       C  
ATOM   5378  CG1 ILE B 234      95.617  17.838   5.984  1.00 77.96           C  
ANISOU 5378  CG1 ILE B 234     6834   8927  13859   -452   -665   -731       C  
ATOM   5379  CG2 ILE B 234      97.186  16.804   4.298  1.00 79.49           C  
ANISOU 5379  CG2 ILE B 234     6858   9110  14235   -365   -398   -454       C  
ATOM   5380  CD1 ILE B 234      94.674  16.615   6.169  1.00 79.14           C  
ANISOU 5380  CD1 ILE B 234     7211   9182  13675   -327   -677   -673       C  
ATOM   5381  N   ARG B 235      97.198  19.656   2.044  1.00 80.70           N  
ANISOU 5381  N   ARG B 235     6908   8840  14916   -604     17   -309       N  
ATOM   5382  CA  ARG B 235      97.815  19.781   0.719  1.00 81.59           C  
ANISOU 5382  CA  ARG B 235     6950   8869  15183   -590    265   -121       C  
ATOM   5383  C   ARG B 235      98.916  20.847   0.738  1.00 89.41           C  
ANISOU 5383  C   ARG B 235     7653   9749  16567   -719    293   -141       C  
ATOM   5384  O   ARG B 235      99.946  20.649   0.100  1.00 90.30           O  
ANISOU 5384  O   ARG B 235     7597   9866  16847   -697    418    -25       O  
ATOM   5385  CB  ARG B 235      96.746  20.119  -0.341  1.00 80.05           C  
ANISOU 5385  CB  ARG B 235     6973   8578  14866   -565    447     -1       C  
ATOM   5386  CG  ARG B 235      97.262  20.102  -1.769  1.00 91.70           C  
ANISOU 5386  CG  ARG B 235     8417   9993  16434   -517    715    208       C  
ATOM   5387  CD  ARG B 235      96.161  20.323  -2.778  1.00105.95           C  
ANISOU 5387  CD  ARG B 235    10444  11727  18084   -474    873    326       C  
ATOM   5388  NE  ARG B 235      96.669  20.252  -4.150  1.00123.67           N  
ANISOU 5388  NE  ARG B 235    12675  13937  20378   -405   1132    529       N  
ATOM   5389  CZ  ARG B 235      96.756  19.132  -4.866  1.00141.70           C  
ANISOU 5389  CZ  ARG B 235    15076  16313  22451   -267   1228    626       C  
ATOM   5390  NH1 ARG B 235      96.378  17.971  -4.343  1.00127.87           N  
ANISOU 5390  NH1 ARG B 235    13456  14680  20449   -194   1089    544       N  
ATOM   5391  NH2 ARG B 235      97.235  19.162  -6.101  1.00132.33           N  
ANISOU 5391  NH2 ARG B 235    13877  15094  21307   -198   1473    805       N  
ATOM   5392  N   LYS B 236      98.719  21.943   1.509  1.00 88.89           N  
ANISOU 5392  N   LYS B 236     7527   9588  16660   -852    173   -296       N  
ATOM   5393  CA  LYS B 236      99.684  23.042   1.659  1.00 92.89           C  
ANISOU 5393  CA  LYS B 236     7761   9963  17569  -1000    176   -347       C  
ATOM   5394  C   LYS B 236     100.982  22.569   2.364  1.00102.25           C  
ANISOU 5394  C   LYS B 236     8678  11262  18912  -1015     31   -422       C  
ATOM   5395  O   LYS B 236     102.079  22.822   1.859  1.00103.66           O  
ANISOU 5395  O   LYS B 236     8617  11381  19388  -1064    148   -329       O  
ATOM   5396  CB  LYS B 236      99.053  24.201   2.460  1.00 95.57           C  
ANISOU 5396  CB  LYS B 236     8126  10190  17995  -1124     34   -543       C  
ATOM   5397  CG  LYS B 236      99.959  25.427   2.629  1.00109.11           C  
ANISOU 5397  CG  LYS B 236     9573  11735  20151  -1296     32   -617       C  
ATOM   5398  CD  LYS B 236      99.395  26.470   3.605  1.00121.31           C  
ANISOU 5398  CD  LYS B 236    11136  13188  21769  -1411   -162   -868       C  
ATOM   5399  CE  LYS B 236      99.349  25.985   5.041  1.00135.29           C  
ANISOU 5399  CE  LYS B 236    12902  15142  23359  -1389   -474  -1105       C  
ATOM   5400  NZ  LYS B 236      98.824  27.023   5.965  1.00146.68           N  
ANISOU 5400  NZ  LYS B 236    14381  16494  24857  -1487   -646  -1355       N  
ATOM   5401  N   HIS B 237     100.839  21.904   3.535  1.00101.14           N  
ANISOU 5401  N   HIS B 237     8572  11285  18571   -968   -220   -581       N  
ATOM   5402  CA  HIS B 237     101.947  21.434   4.375  1.00103.97           C  
ANISOU 5402  CA  HIS B 237     8696  11779  19028   -966   -410   -676       C  
ATOM   5403  C   HIS B 237     102.787  20.343   3.676  1.00108.86           C  
ANISOU 5403  C   HIS B 237     9217  12490  19654   -849   -272   -485       C  
ATOM   5404  O   HIS B 237     103.991  20.265   3.933  1.00111.35           O  
ANISOU 5404  O   HIS B 237     9246  12839  20222   -885   -320   -494       O  
ATOM   5405  CB  HIS B 237     101.414  20.886   5.710  1.00104.42           C  
ANISOU 5405  CB  HIS B 237     8877  12005  18792   -903   -683   -852       C  
ATOM   5406  CG  HIS B 237     102.488  20.567   6.707  1.00110.50           C  
ANISOU 5406  CG  HIS B 237     9412  12926  19648   -900   -916   -973       C  
ATOM   5407  ND1 HIS B 237     103.078  19.315   6.759  1.00112.61           N  
ANISOU 5407  ND1 HIS B 237     9618  13352  19817   -763   -922   -865       N  
ATOM   5408  CD2 HIS B 237     103.054  21.358   7.650  1.00114.98           C  
ANISOU 5408  CD2 HIS B 237     9796  13505  20386  -1011  -1154  -1195       C  
ATOM   5409  CE1 HIS B 237     103.981  19.382   7.728  1.00114.46           C  
ANISOU 5409  CE1 HIS B 237     9627  13699  20162   -791  -1163  -1010       C  
ATOM   5410  NE2 HIS B 237     104.002  20.590   8.295  1.00116.27           N  
ANISOU 5410  NE2 HIS B 237     9777  13852  20549   -942  -1318  -1219       N  
ATOM   5411  N   LEU B 238     102.175  19.515   2.816  1.00103.46           N  
ANISOU 5411  N   LEU B 238     8762  11846  18703   -707   -108   -324       N  
ATOM   5412  CA  LEU B 238     102.906  18.453   2.128  1.00104.03           C  
ANISOU 5412  CA  LEU B 238     8777  11999  18752   -576     34   -153       C  
ATOM   5413  C   LEU B 238     103.746  19.028   0.981  1.00112.22           C  
ANISOU 5413  C   LEU B 238     9630  12911  20099   -622    295     12       C  
ATOM   5414  O   LEU B 238     104.807  18.476   0.675  1.00113.29           O  
ANISOU 5414  O   LEU B 238     9576  13106  20362   -559    368    109       O  
ATOM   5415  CB  LEU B 238     101.968  17.354   1.610  1.00101.25           C  
ANISOU 5415  CB  LEU B 238     8734  11704  18031   -421    131    -52       C  
ATOM   5416  CG  LEU B 238     101.604  16.237   2.611  1.00104.21           C  
ANISOU 5416  CG  LEU B 238     9223  12248  18126   -311    -72   -132       C  
ATOM   5417  CD1 LEU B 238     100.918  16.759   3.824  1.00103.84           C  
ANISOU 5417  CD1 LEU B 238     9232  12237  17985   -384   -323   -332       C  
ATOM   5418  CD2 LEU B 238     100.753  15.219   1.970  1.00104.33           C  
ANISOU 5418  CD2 LEU B 238     9519  12284  17836   -177     49    -24       C  
ATOM   5419  N   LEU B 239     103.356  20.197   0.437  1.00110.84           N  
ANISOU 5419  N   LEU B 239     9491  12561  20062   -728    434     48       N  
ATOM   5420  CA  LEU B 239     104.133  20.908  -0.592  1.00113.63           C  
ANISOU 5420  CA  LEU B 239     9665  12776  20732   -784    690    212       C  
ATOM   5421  C   LEU B 239     105.090  21.939   0.060  1.00122.28           C  
ANISOU 5421  C   LEU B 239    10419  13791  22252   -963    578     99       C  
ATOM   5422  O   LEU B 239     105.591  22.836  -0.620  1.00123.52           O  
ANISOU 5422  O   LEU B 239    10405  13796  22730  -1053    770    209       O  
ATOM   5423  CB  LEU B 239     103.186  21.611  -1.605  1.00112.83           C  
ANISOU 5423  CB  LEU B 239     9778  12523  20568   -798    903    327       C  
ATOM   5424  CG  LEU B 239     102.595  20.796  -2.792  1.00116.14           C  
ANISOU 5424  CG  LEU B 239    10468  12983  20676   -630   1120    510       C  
ATOM   5425  CD1 LEU B 239     103.673  20.413  -3.807  1.00118.32           C  
ANISOU 5425  CD1 LEU B 239    10613  13258  21084   -547   1391    724       C  
ATOM   5426  CD2 LEU B 239     101.762  19.588  -2.347  1.00115.97           C  
ANISOU 5426  CD2 LEU B 239    10688  13117  20259   -506    966    431       C  
ATOM   5427  N   LYS B 240     105.360  21.773   1.366  1.00121.35           N  
ANISOU 5427  N   LYS B 240    10222  13773  22115  -1008    269   -121       N  
ATOM   5428  CA  LYS B 240     106.159  22.686   2.181  1.00125.21           C  
ANISOU 5428  CA  LYS B 240    10401  14213  22961  -1174     93   -282       C  
ATOM   5429  C   LYS B 240     107.159  21.895   3.071  1.00134.69           C  
ANISOU 5429  C   LYS B 240    11369  15603  24205  -1127   -113   -358       C  
ATOM   5430  O   LYS B 240     107.745  22.455   4.002  1.00136.42           O  
ANISOU 5430  O   LYS B 240    11362  15834  24638  -1248   -345   -546       O  
ATOM   5431  CB  LYS B 240     105.175  23.516   3.038  1.00126.87           C  
ANISOU 5431  CB  LYS B 240    10732  14355  23119  -1286   -116   -515       C  
ATOM   5432  CG  LYS B 240     105.745  24.708   3.796  1.00139.60           C  
ANISOU 5432  CG  LYS B 240    12062  15909  25071  -1466   -340   -737       C  
ATOM   5433  CD  LYS B 240     104.679  25.395   4.677  1.00145.13           C  
ANISOU 5433  CD  LYS B 240    12929  16603  25609  -1523   -586   -995       C  
ATOM   5434  CE  LYS B 240     103.516  25.988   3.909  1.00149.96           C  
ANISOU 5434  CE  LYS B 240    13769  17015  26193  -1569   -416   -952       C  
ATOM   5435  N   THR B 241     107.375  20.601   2.759  1.00133.52           N  
ANISOU 5435  N   THR B 241    11276  15604  23851   -948    -42   -223       N  
ATOM   5436  CA  THR B 241     108.252  19.746   3.553  1.00136.26           C  
ANISOU 5436  CA  THR B 241    11404  16137  24233   -883   -236   -278       C  
ATOM   5437  C   THR B 241     109.481  19.324   2.707  1.00146.38           C  
ANISOU 5437  C   THR B 241    12401  17432  25783   -838    -49    -93       C  
ATOM   5438  O   THR B 241     110.587  19.820   2.960  1.00149.25           O  
ANISOU 5438  O   THR B 241    12417  17775  26514   -954   -125   -144       O  
ATOM   5439  CB  THR B 241     107.461  18.519   4.079  1.00140.57           C  
ANISOU 5439  CB  THR B 241    12194  16869  24346   -700   -364   -298       C  
ATOM   5440  OG1 THR B 241     106.273  18.965   4.739  1.00137.24           O  
ANISOU 5440  OG1 THR B 241    12000  16452  23694   -742   -553   -477       O  
ATOM   5441  CG2 THR B 241     108.284  17.641   5.028  1.00140.54           C  
ANISOU 5441  CG2 THR B 241    11959  17058  24381   -623   -573   -347       C  
ATOM   5442  N   ASN B 242     109.300  18.401   1.734  1.00144.34           N  
ANISOU 5442  N   ASN B 242    12285  17215  25345   -665    185    111       N  
ATOM   5443  CA  ASN B 242     110.410  17.883   0.916  1.00147.25           C  
ANISOU 5443  CA  ASN B 242    12411  17599  25936   -592    398    302       C  
ATOM   5444  C   ASN B 242     109.890  17.333  -0.428  1.00151.58           C  
ANISOU 5444  C   ASN B 242    13229  18108  26257   -439    725    516       C  
ATOM   5445  O   ASN B 242     108.745  16.867  -0.507  1.00148.59           O  
ANISOU 5445  O   ASN B 242    13185  17773  25500   -336    700    497       O  
ATOM   5446  CB  ASN B 242     111.135  16.784   1.712  1.00149.27           C  
ANISOU 5446  CB  ASN B 242    12473  18057  26186   -489    187    252       C  
ATOM   5447  CG  ASN B 242     112.331  16.163   1.048  1.00171.35           C  
ANISOU 5447  CG  ASN B 242    15224  20926  28953   -295    411    465       C  
ATOM   5448  OD1 ASN B 242     113.025  16.774   0.226  1.00165.72           O  
ANISOU 5448  OD1 ASN B 242    14458  20113  28394   -280    723    648       O  
ATOM   5449  ND2 ASN B 242     112.642  14.951   1.467  1.00162.78           N  
ANISOU 5449  ND2 ASN B 242    14166  20014  27668   -136    261    445       N  
ATOM   5450  N   SER B 243     110.733  17.384  -1.486  1.00150.84           N  
ANISOU 5450  N   SER B 243    12994  17936  26382   -417   1030    717       N  
ATOM   5451  CA  SER B 243     110.317  16.937  -2.816  1.00149.51           C  
ANISOU 5451  CA  SER B 243    13086  17736  25985   -264   1341    910       C  
ATOM   5452  C   SER B 243     111.298  15.859  -3.420  1.00154.54           C  
ANISOU 5452  C   SER B 243    13689  18489  26540    -51   1492   1054       C  
ATOM   5453  O   SER B 243     111.430  15.781  -4.647  1.00153.90           O  
ANISOU 5453  O   SER B 243    13751  18373  26352     71   1788   1228       O  
ATOM   5454  CB  SER B 243     110.212  18.138  -3.759  1.00153.53           C  
ANISOU 5454  CB  SER B 243    13580  18066  26691   -353   1627   1054       C  
ATOM   5455  OG  SER B 243     109.519  17.791  -4.949  1.00158.24           O  
ANISOU 5455  OG  SER B 243    14554  18607  26962   -299   1734   1091       O  
ATOM   5456  N   TYR B 244     111.916  14.988  -2.560  1.00152.12           N  
ANISOU 5456  N   TYR B 244    13208  18324  26267      5   1285    979       N  
ATOM   5457  CA  TYR B 244     112.748  13.864  -3.046  1.00152.80           C  
ANISOU 5457  CA  TYR B 244    13235  18518  26303    211   1409   1107       C  
ATOM   5458  C   TYR B 244     111.857  12.804  -3.722  1.00154.17           C  
ANISOU 5458  C   TYR B 244    13803  18711  26064    399   1538   1167       C  
ATOM   5459  O   TYR B 244     110.664  12.739  -3.431  1.00151.35           O  
ANISOU 5459  O   TYR B 244    13740  18355  25412    389   1394   1056       O  
ATOM   5460  CB  TYR B 244     113.606  13.201  -1.933  1.00155.08           C  
ANISOU 5460  CB  TYR B 244    13322  18964  26638    246   1110    994       C  
ATOM   5461  CG  TYR B 244     114.905  13.912  -1.588  1.00160.61           C  
ANISOU 5461  CG  TYR B 244    13557  19692  27775    172   1087   1024       C  
ATOM   5462  CD1 TYR B 244     115.967  13.938  -2.487  1.00164.84           C  
ANISOU 5462  CD1 TYR B 244    13893  20156  28582    190   1405   1216       C  
ATOM   5463  CD2 TYR B 244     115.149  14.367  -0.296  1.00162.81           C  
ANISOU 5463  CD2 TYR B 244    13591  20076  28194     89    747    861       C  
ATOM   5464  CE1 TYR B 244     117.177  14.557  -2.166  1.00169.45           C  
ANISOU 5464  CE1 TYR B 244    14027  20763  29594    114   1390   1250       C  
ATOM   5465  CE2 TYR B 244     116.360  14.977   0.044  1.00167.23           C  
ANISOU 5465  CE2 TYR B 244    13705  20665  29170     14    707    879       C  
ATOM   5466  CZ  TYR B 244     117.372  15.072  -0.896  1.00177.63           C  
ANISOU 5466  CZ  TYR B 244    14813  21900  30779     21   1032   1077       C  
ATOM   5467  OH  TYR B 244     118.569  15.671  -0.576  1.00183.06           O  
ANISOU 5467  OH  TYR B 244    15032  22613  31908    -61   1000   1102       O  
ATOM   5468  N   GLY B 245     112.456  11.994  -4.601  1.00151.45           N  
ANISOU 5468  N   GLY B 245    13455  18380  25709    572   1813   1339       N  
ATOM   5469  CA  GLY B 245     111.775  10.925  -5.334  1.00149.16           C  
ANISOU 5469  CA  GLY B 245    13524  18099  25052    758   1957   1393       C  
ATOM   5470  C   GLY B 245     111.184   9.835  -4.460  1.00150.56           C  
ANISOU 5470  C   GLY B 245    13868  18377  24962    861   1721   1281       C  
ATOM   5471  O   GLY B 245     110.065   9.382  -4.716  1.00147.77           O  
ANISOU 5471  O   GLY B 245    13862  18006  24280    916   1704   1236       O  
ATOM   5472  N   LYS B 246     111.936   9.401  -3.425  1.00147.57           N  
ANISOU 5472  N   LYS B 246    13236  18106  24725    895   1543   1246       N  
ATOM   5473  CA  LYS B 246     111.487   8.371  -2.478  1.00145.40           C  
ANISOU 5473  CA  LYS B 246    13104  17929  24211    996   1317   1156       C  
ATOM   5474  C   LYS B 246     110.366   8.912  -1.574  1.00144.96           C  
ANISOU 5474  C   LYS B 246    13222  17861  23996    846   1065    989       C  
ATOM   5475  O   LYS B 246     109.449   8.166  -1.219  1.00142.81           O  
ANISOU 5475  O   LYS B 246    13233  17605  23422    906    968    929       O  
ATOM   5476  CB  LYS B 246     112.659   7.864  -1.621  1.00150.18           C  
ANISOU 5476  CB  LYS B 246    13378  18667  25018   1058   1153   1156       C  
ATOM   5477  N   ASN B 247     110.437  10.210  -1.219  1.00139.65           N  
ANISOU 5477  N   ASN B 247    12367  17150  23545    648    971    916       N  
ATOM   5478  CA  ASN B 247     109.446  10.862  -0.361  1.00136.50           C  
ANISOU 5478  CA  ASN B 247    12082  16737  23044    493    727    743       C  
ATOM   5479  C   ASN B 247     108.297  11.472  -1.195  1.00134.34           C  
ANISOU 5479  C   ASN B 247    12096  16328  22617    421    875    753       C  
ATOM   5480  O   ASN B 247     107.353  12.005  -0.614  1.00132.66           O  
ANISOU 5480  O   ASN B 247    12019  16090  22296    307    710    623       O  
ATOM   5481  CB  ASN B 247     110.115  11.944   0.491  1.00140.12           C  
ANISOU 5481  CB  ASN B 247    12201  17209  23831    314    542    639       C  
ATOM   5482  N   ARG B 248     108.364  11.352  -2.545  1.00127.66           N  
ANISOU 5482  N   ARG B 248    11345  15406  21752    501   1187    909       N  
ATOM   5483  CA  ARG B 248     107.350  11.848  -3.492  1.00124.39           C  
ANISOU 5483  CA  ARG B 248    11196  14878  21187    465   1356    949       C  
ATOM   5484  C   ARG B 248     106.149  10.887  -3.538  1.00121.84           C  
ANISOU 5484  C   ARG B 248    11248  14577  20468    572   1315    908       C  
ATOM   5485  O   ARG B 248     105.004  11.333  -3.453  1.00119.25           O  
ANISOU 5485  O   ARG B 248    11132  14197  19979    492   1255    839       O  
ATOM   5486  CB  ARG B 248     107.981  12.010  -4.889  1.00126.38           C  
ANISOU 5486  CB  ARG B 248    11386  15064  21568    531   1703   1138       C  
ATOM   5487  CG  ARG B 248     107.086  12.577  -5.978  1.00135.84           C  
ANISOU 5487  CG  ARG B 248    12834  16155  22623    510   1897   1206       C  
ATOM   5488  CD  ARG B 248     107.881  12.697  -7.262  1.00149.70           C  
ANISOU 5488  CD  ARG B 248    14518  17869  24494    601   2246   1405       C  
ATOM   5489  NE  ARG B 248     107.075  13.217  -8.364  1.00159.72           N  
ANISOU 5489  NE  ARG B 248    16035  19053  25601    604   2433   1483       N  
ATOM   5490  CZ  ARG B 248     107.540  13.444  -9.590  1.00176.02           C  
ANISOU 5490  CZ  ARG B 248    18103  21077  27700    690   2752   1664       C  
ATOM   5491  NH1 ARG B 248     108.815  13.207  -9.879  1.00162.42           N  
ANISOU 5491  NH1 ARG B 248    16146  19384  26183    777   2935   1787       N  
ATOM   5492  NH2 ARG B 248     106.738  13.918 -10.533  1.00164.83           N  
ANISOU 5492  NH2 ARG B 248    16923  19598  26109    699   2894   1730       N  
ATOM   5493  N   ILE B 249     106.425   9.571  -3.683  1.00115.93           N  
ANISOU 5493  N   ILE B 249    10571  13896  19581    751   1356    953       N  
ATOM   5494  CA  ILE B 249     105.437   8.487  -3.699  1.00112.60           C  
ANISOU 5494  CA  ILE B 249    10480  13486  18818    859   1321    917       C  
ATOM   5495  C   ILE B 249     104.610   8.539  -2.389  1.00112.69           C  
ANISOU 5495  C   ILE B 249    10571  13544  18704    774   1019    766       C  
ATOM   5496  O   ILE B 249     103.376   8.554  -2.442  1.00109.88           O  
ANISOU 5496  O   ILE B 249    10479  13149  18121    744    979    711       O  
ATOM   5497  CB  ILE B 249     106.160   7.101  -3.890  1.00116.53           C  
ANISOU 5497  CB  ILE B 249    10981  14034  19261   1068   1416    994       C  
ATOM   5498  CG1 ILE B 249     106.930   7.000  -5.243  1.00118.63           C  
ANISOU 5498  CG1 ILE B 249    11203  14257  19615   1176   1742   1144       C  
ATOM   5499  CG2 ILE B 249     105.212   5.916  -3.711  1.00115.17           C  
ANISOU 5499  CG2 ILE B 249    11122  13863  18775   1168   1346    942       C  
ATOM   5500  CD1 ILE B 249     106.070   7.067  -6.584  1.00125.32           C  
ANISOU 5500  CD1 ILE B 249    12351  15018  20248   1206   1956   1188       C  
ATOM   5501  N   THR B 250     105.312   8.625  -1.232  1.00108.84           N  
ANISOU 5501  N   THR B 250     9843  13145  18366    738    812    702       N  
ATOM   5502  CA  THR B 250     104.750   8.676   0.123  1.00106.86           C  
ANISOU 5502  CA  THR B 250     9631  12965  18007    678    522    563       C  
ATOM   5503  C   THR B 250     103.873   9.931   0.299  1.00108.35           C  
ANISOU 5503  C   THR B 250     9887  13086  18194    497    444    460       C  
ATOM   5504  O   THR B 250     102.831   9.853   0.946  1.00106.06           O  
ANISOU 5504  O   THR B 250     9779  12816  17703    468    291    365       O  
ATOM   5505  CB  THR B 250     105.893   8.651   1.169  1.00115.46           C  
ANISOU 5505  CB  THR B 250    10412  14175  19283    687    333    524       C  
ATOM   5506  OG1 THR B 250     106.765   7.550   0.905  1.00116.16           O  
ANISOU 5506  OG1 THR B 250    10419  14316  19402    864    433    638       O  
ATOM   5507  CG2 THR B 250     105.383   8.562   2.601  1.00112.86           C  
ANISOU 5507  CG2 THR B 250    10135  13944  18803    664     37    390       C  
ATOM   5508  N   ARG B 251     104.282  11.071  -0.298  1.00105.20           N  
ANISOU 5508  N   ARG B 251     9344  12600  18025    384    566    490       N  
ATOM   5509  CA  ARG B 251     103.553  12.344  -0.217  1.00103.91           C  
ANISOU 5509  CA  ARG B 251     9225  12350  17905    217    522    408       C  
ATOM   5510  C   ARG B 251     102.204  12.273  -0.962  1.00103.90           C  
ANISOU 5510  C   ARG B 251     9555  12274  17648    235    634    437       C  
ATOM   5511  O   ARG B 251     101.181  12.678  -0.411  1.00101.69           O  
ANISOU 5511  O   ARG B 251     9417  11980  17240    160    500    334       O  
ATOM   5512  CB  ARG B 251     104.405  13.489  -0.802  1.00106.39           C  
ANISOU 5512  CB  ARG B 251     9290  12573  18560    106    658    465       C  
ATOM   5513  CG  ARG B 251     103.794  14.880  -0.616  1.00114.89           C  
ANISOU 5513  CG  ARG B 251    10375  13543  19737    -72    602    374       C  
ATOM   5514  CD  ARG B 251     104.467  15.918  -1.483  1.00124.61           C  
ANISOU 5514  CD  ARG B 251    11418  14647  21279   -163    808    477       C  
ATOM   5515  NE  ARG B 251     104.184  15.690  -2.899  1.00133.23           N  
ANISOU 5515  NE  ARG B 251    12679  15679  22264    -67   1103    656       N  
ATOM   5516  CZ  ARG B 251     104.684  16.420  -3.889  1.00152.31           C  
ANISOU 5516  CZ  ARG B 251    14989  17990  24893   -103   1344    796       C  
ATOM   5517  NH1 ARG B 251     105.520  17.420  -3.629  1.00144.35           N  
ANISOU 5517  NH1 ARG B 251    13691  16907  24250   -246   1335    781       N  
ATOM   5518  NH2 ARG B 251     104.373  16.141  -5.148  1.00138.81           N  
ANISOU 5518  NH2 ARG B 251    13460  16248  23034      7   1599    952       N  
ATOM   5519  N   ASP B 252     102.223  11.794  -2.224  1.00 99.54           N  
ANISOU 5519  N   ASP B 252     9117  11679  17025    337    877    574       N  
ATOM   5520  CA  ASP B 252     101.045  11.713  -3.083  1.00 96.93           C  
ANISOU 5520  CA  ASP B 252     9083  11285  16460    363    992    609       C  
ATOM   5521  C   ASP B 252     100.024  10.694  -2.556  1.00 97.24           C  
ANISOU 5521  C   ASP B 252     9368  11376  16201    427    854    535       C  
ATOM   5522  O   ASP B 252      98.832  10.945  -2.699  1.00 95.69           O  
ANISOU 5522  O   ASP B 252     9377  11139  15841    384    832    498       O  
ATOM   5523  CB  ASP B 252     101.435  11.354  -4.525  1.00 99.52           C  
ANISOU 5523  CB  ASP B 252     9467  11576  16769    477   1276    762       C  
ATOM   5524  CG  ASP B 252     102.237  12.424  -5.257  1.00111.27           C  
ANISOU 5524  CG  ASP B 252    10750  12996  18532    418   1464    870       C  
ATOM   5525  OD1 ASP B 252     102.654  13.416  -4.604  1.00112.75           O  
ANISOU 5525  OD1 ASP B 252    10707  13160  18974    283   1366    820       O  
ATOM   5526  OD2 ASP B 252     102.441  12.277  -6.479  1.00117.83           O  
ANISOU 5526  OD2 ASP B 252    11650  13795  19327    510   1712   1003       O  
ATOM   5527  N   GLN B 253     100.464   9.580  -1.926  1.00 92.50           N  
ANISOU 5527  N   GLN B 253     8739  10860  15546    529    763    521       N  
ATOM   5528  CA  GLN B 253      99.524   8.588  -1.383  1.00 89.94           C  
ANISOU 5528  CA  GLN B 253     8638  10572  14965    589    644    466       C  
ATOM   5529  C   GLN B 253      98.760   9.174  -0.177  1.00 90.77           C  
ANISOU 5529  C   GLN B 253     8761  10709  15020    476    418    341       C  
ATOM   5530  O   GLN B 253      97.596   8.830   0.011  1.00 88.69           O  
ANISOU 5530  O   GLN B 253     8713  10435  14548    475    361    301       O  
ATOM   5531  CB  GLN B 253     100.212   7.268  -0.990  1.00 92.11           C  
ANISOU 5531  CB  GLN B 253     8875  10917  15207    735    616    500       C  
ATOM   5532  CG  GLN B 253     100.746   6.490  -2.196  1.00111.94           C  
ANISOU 5532  CG  GLN B 253    11426  13390  17715    873    848    612       C  
ATOM   5533  CD  GLN B 253     101.220   5.095  -1.876  1.00134.38           C  
ANISOU 5533  CD  GLN B 253    14297  16273  20486   1031    832    642       C  
ATOM   5534  OE1 GLN B 253     100.597   4.361  -1.100  1.00128.63           O  
ANISOU 5534  OE1 GLN B 253    13719  15561  19594   1059    705    596       O  
ATOM   5535  NE2 GLN B 253     102.206   4.627  -2.631  1.00129.97           N  
ANISOU 5535  NE2 GLN B 253    13644  15712  20028   1153   1003    735       N  
ATOM   5536  N   VAL B 254      99.389  10.085   0.598  1.00 87.20           N  
ANISOU 5536  N   VAL B 254     8080  10288  14763    380    296    273       N  
ATOM   5537  CA  VAL B 254      98.743  10.779   1.724  1.00 85.77           C  
ANISOU 5537  CA  VAL B 254     7907  10135  14546    275     89    138       C  
ATOM   5538  C   VAL B 254      97.682  11.745   1.141  1.00 87.68           C  
ANISOU 5538  C   VAL B 254     8286  10271  14758    172    162    121       C  
ATOM   5539  O   VAL B 254      96.573  11.832   1.672  1.00 85.91           O  
ANISOU 5539  O   VAL B 254     8215  10051  14375    137     58     46       O  
ATOM   5540  CB  VAL B 254      99.778  11.505   2.638  1.00 91.38           C  
ANISOU 5540  CB  VAL B 254     8333  10906  15483    203    -68     52       C  
ATOM   5541  CG1 VAL B 254      99.093  12.337   3.714  1.00 90.64           C  
ANISOU 5541  CG1 VAL B 254     8263  10830  15345     97   -268   -104       C  
ATOM   5542  CG2 VAL B 254     100.735  10.505   3.279  1.00 92.47           C  
ANISOU 5542  CG2 VAL B 254     8342  11167  15626    321   -161     75       C  
ATOM   5543  N   LEU B 255      98.016  12.414   0.016  1.00 84.24           N  
ANISOU 5543  N   LEU B 255     7800   9742  14466    140    354    208       N  
ATOM   5544  CA  LEU B 255      97.120  13.331  -0.692  1.00 82.90           C  
ANISOU 5544  CA  LEU B 255     7753   9469  14276     64    450    225       C  
ATOM   5545  C   LEU B 255      95.956  12.572  -1.330  1.00 85.04           C  
ANISOU 5545  C   LEU B 255     8309   9734  14267    138    507    263       C  
ATOM   5546  O   LEU B 255      94.849  13.111  -1.375  1.00 83.94           O  
ANISOU 5546  O   LEU B 255     8307   9554  14033     81    476    225       O  
ATOM   5547  CB  LEU B 255      97.870  14.137  -1.767  1.00 84.29           C  
ANISOU 5547  CB  LEU B 255     7803   9555  14669     35    662    338       C  
ATOM   5548  CG  LEU B 255      98.909  15.156  -1.268  1.00 91.11           C  
ANISOU 5548  CG  LEU B 255     8369  10386  15863    -74    628    305       C  
ATOM   5549  CD1 LEU B 255      99.732  15.718  -2.414  1.00 92.81           C  
ANISOU 5549  CD1 LEU B 255     8467  10513  16284    -78    878    455       C  
ATOM   5550  CD2 LEU B 255      98.258  16.274  -0.486  1.00 93.34           C  
ANISOU 5550  CD2 LEU B 255     8631  10614  16219   -215    477    169       C  
ATOM   5551  N   LYS B 256      96.196  11.325  -1.811  1.00 80.91           N  
ANISOU 5551  N   LYS B 256     7871   9248  13623    266    586    330       N  
ATOM   5552  CA  LYS B 256      95.149  10.469  -2.393  1.00 79.03           C  
ANISOU 5552  CA  LYS B 256     7895   9000  13132    336    627    351       C  
ATOM   5553  C   LYS B 256      94.126  10.089  -1.321  1.00 81.43           C  
ANISOU 5553  C   LYS B 256     8313   9349  13279    313    436    254       C  
ATOM   5554  O   LYS B 256      92.925  10.122  -1.590  1.00 80.36           O  
ANISOU 5554  O   LYS B 256     8362   9185  12986    295    429    239       O  
ATOM   5555  CB  LYS B 256      95.730   9.203  -3.050  1.00 82.09           C  
ANISOU 5555  CB  LYS B 256     8335   9404  13450    479    746    425       C  
ATOM   5556  CG  LYS B 256      96.530   9.454  -4.324  1.00102.76           C  
ANISOU 5556  CG  LYS B 256    10896  11981  16166    529    974    536       C  
ATOM   5557  CD  LYS B 256      97.073   8.145  -4.915  1.00114.45           C  
ANISOU 5557  CD  LYS B 256    12443  13477  17564    685   1090    592       C  
ATOM   5558  CE  LYS B 256      97.895   8.334  -6.174  1.00125.70           C  
ANISOU 5558  CE  LYS B 256    13814  14874  19072    757   1333    708       C  
ATOM   5559  NZ  LYS B 256      99.142   9.111  -5.930  1.00135.41           N  
ANISOU 5559  NZ  LYS B 256    14746  16114  20591    712   1376    759       N  
ATOM   5560  N   MET B 257      94.603   9.766  -0.096  1.00 77.58           N  
ANISOU 5560  N   MET B 257     7708   8937  12833    318    283    195       N  
ATOM   5561  CA  MET B 257      93.754   9.437   1.056  1.00 76.30           C  
ANISOU 5561  CA  MET B 257     7634   8831  12527    307    109    115       C  
ATOM   5562  C   MET B 257      92.981  10.674   1.536  1.00 79.10           C  
ANISOU 5562  C   MET B 257     7989   9165  12902    187     22     27       C  
ATOM   5563  O   MET B 257      91.863  10.544   2.048  1.00 77.49           O  
ANISOU 5563  O   MET B 257     7915   8981  12547    174    -67    -21       O  
ATOM   5564  CB  MET B 257      94.589   8.861   2.210  1.00 79.67           C  
ANISOU 5564  CB  MET B 257     7925   9357  12988    364    -23     88       C  
ATOM   5565  CG  MET B 257      95.232   7.534   1.892  1.00 84.23           C  
ANISOU 5565  CG  MET B 257     8517   9953  13535    499     52    174       C  
ATOM   5566  SD  MET B 257      96.263   6.953   3.260  1.00 90.30           S  
ANISOU 5566  SD  MET B 257     9104  10851  14355    578   -113    158       S  
ATOM   5567  CE  MET B 257      96.875   5.472   2.593  1.00 87.61           C  
ANISOU 5567  CE  MET B 257     8815  10490  13984    741     23    275       C  
ATOM   5568  N   ALA B 258      93.592  11.869   1.368  1.00 75.22           N  
ANISOU 5568  N   ALA B 258     7344   8625  12610    103     57     11       N  
ATOM   5569  CA  ALA B 258      93.034  13.163   1.757  1.00 73.81           C  
ANISOU 5569  CA  ALA B 258     7147   8402  12497    -10     -7    -74       C  
ATOM   5570  C   ALA B 258      91.946  13.620   0.765  1.00 74.88           C  
ANISOU 5570  C   ALA B 258     7445   8448  12558    -36    113    -20       C  
ATOM   5571  O   ALA B 258      90.914  14.143   1.186  1.00 72.84           O  
ANISOU 5571  O   ALA B 258     7270   8172  12235    -88     46    -83       O  
ATOM   5572  CB  ALA B 258      94.151  14.202   1.835  1.00 75.96           C  
ANISOU 5572  CB  ALA B 258     7182   8637  13043    -91     -7   -106       C  
ATOM   5573  N   ALA B 259      92.182  13.430  -0.544  1.00 71.41           N  
ANISOU 5573  N   ALA B 259     7048   7961  12122     11    289     96       N  
ATOM   5574  CA  ALA B 259      91.242  13.824  -1.593  1.00 70.63           C  
ANISOU 5574  CA  ALA B 259     7103   7796  11939      6    401    159       C  
ATOM   5575  C   ALA B 259      90.045  12.886  -1.644  1.00 74.22           C  
ANISOU 5575  C   ALA B 259     7769   8286  12144     59    357    152       C  
ATOM   5576  O   ALA B 259      89.003  13.253  -2.180  1.00 73.29           O  
ANISOU 5576  O   ALA B 259     7780   8134  11934     42    386    170       O  
ATOM   5577  CB  ALA B 259      91.945  13.834  -2.940  1.00 72.41           C  
ANISOU 5577  CB  ALA B 259     7306   7977  12230     56    602    285       C  
ATOM   5578  N   ALA B 260      90.197  11.666  -1.107  1.00 71.31           N  
ANISOU 5578  N   ALA B 260     7432   7983  11678    123    289    131       N  
ATOM   5579  CA  ALA B 260      89.147  10.658  -1.116  1.00 70.05           C  
ANISOU 5579  CA  ALA B 260     7458   7844  11313    167    250    126       C  
ATOM   5580  C   ALA B 260      88.056  10.967  -0.084  1.00 74.62           C  
ANISOU 5580  C   ALA B 260     8083   8449  11818    109    111     48       C  
ATOM   5581  O   ALA B 260      86.905  10.601  -0.319  1.00 73.75           O  
ANISOU 5581  O   ALA B 260     8121   8332  11567    113     97     51       O  
ATOM   5582  CB  ALA B 260      89.742   9.287  -0.844  1.00 70.94           C  
ANISOU 5582  CB  ALA B 260     7579   7999  11377    258    239    142       C  
ATOM   5583  N   VAL B 261      88.395  11.634   1.046  1.00 72.30           N  
ANISOU 5583  N   VAL B 261     7663   8187  11619     59      7    -26       N  
ATOM   5584  CA  VAL B 261      87.391  11.917   2.084  1.00 71.97           C  
ANISOU 5584  CA  VAL B 261     7670   8180  11497     21   -114   -104       C  
ATOM   5585  C   VAL B 261      86.497  13.112   1.643  1.00 76.22           C  
ANISOU 5585  C   VAL B 261     8250   8649  12060    -49    -78   -115       C  
ATOM   5586  O   VAL B 261      85.314  13.117   1.989  1.00 76.14           O  
ANISOU 5586  O   VAL B 261     8341   8650  11939    -59   -124   -137       O  
ATOM   5587  CB  VAL B 261      87.974  12.168   3.509  1.00 76.66           C  
ANISOU 5587  CB  VAL B 261     8136   8846  12145      8   -253   -197       C  
ATOM   5588  CG1 VAL B 261      88.701  10.934   4.036  1.00 76.61           C  
ANISOU 5588  CG1 VAL B 261     8100   8920  12088     94   -300   -172       C  
ATOM   5589  CG2 VAL B 261      88.878  13.394   3.560  1.00 77.84           C  
ANISOU 5589  CG2 VAL B 261     8114   8957  12503    -61   -256   -250       C  
ATOM   5590  N   VAL B 262      87.039  14.084   0.865  1.00 72.38           N  
ANISOU 5590  N   VAL B 262     7684   8089  11726    -88     13    -86       N  
ATOM   5591  CA  VAL B 262      86.273  15.254   0.410  1.00 71.18           C  
ANISOU 5591  CA  VAL B 262     7567   7862  11617   -142     58    -80       C  
ATOM   5592  C   VAL B 262      85.403  14.836  -0.815  1.00 73.39           C  
ANISOU 5592  C   VAL B 262     8001   8123  11761    -99    150     16       C  
ATOM   5593  O   VAL B 262      84.207  15.131  -0.812  1.00 72.83           O  
ANISOU 5593  O   VAL B 262     8019   8043  11608   -114    122      8       O  
ATOM   5594  CB  VAL B 262      87.166  16.509   0.106  1.00 76.16           C  
ANISOU 5594  CB  VAL B 262     8051   8406  12481   -202    127    -74       C  
ATOM   5595  CG1 VAL B 262      88.306  16.208  -0.860  1.00 77.26           C  
ANISOU 5595  CG1 VAL B 262     8119   8526  12709   -167    257     25       C  
ATOM   5596  CG2 VAL B 262      86.339  17.694  -0.373  1.00 75.65           C  
ANISOU 5596  CG2 VAL B 262     8030   8248  12464   -245    185    -51       C  
ATOM   5597  N   LEU B 263      85.978  14.122  -1.811  1.00 69.32           N  
ANISOU 5597  N   LEU B 263     7518   7609  11213    -40    250     98       N  
ATOM   5598  CA  LEU B 263      85.256  13.672  -3.012  1.00 68.91           C  
ANISOU 5598  CA  LEU B 263     7616   7549  11017      9    324    171       C  
ATOM   5599  C   LEU B 263      84.089  12.718  -2.675  1.00 70.55           C  
ANISOU 5599  C   LEU B 263     7954   7802  11048     23    229    132       C  
ATOM   5600  O   LEU B 263      83.014  12.879  -3.251  1.00 69.47           O  
ANISOU 5600  O   LEU B 263     7918   7658  10819     21    230    154       O  
ATOM   5601  CB  LEU B 263      86.197  12.974  -4.009  1.00 70.23           C  
ANISOU 5601  CB  LEU B 263     7797   7717  11171     83    446    244       C  
ATOM   5602  CG  LEU B 263      86.814  13.817  -5.145  1.00 77.09           C  
ANISOU 5602  CG  LEU B 263     8624   8533  12134     99    607    344       C  
ATOM   5603  CD1 LEU B 263      87.607  15.022  -4.628  1.00 78.84           C  
ANISOU 5603  CD1 LEU B 263     8658   8703  12596     28    626    338       C  
ATOM   5604  CD2 LEU B 263      87.695  12.957  -6.027  1.00 80.71           C  
ANISOU 5604  CD2 LEU B 263     9116   9008  12543    192    729    409       C  
ATOM   5605  N   ALA B 264      84.290  11.749  -1.749  1.00 66.24           N  
ANISOU 5605  N   ALA B 264     7398   7303  10467     38    147     84       N  
ATOM   5606  CA  ALA B 264      83.245  10.796  -1.348  1.00 65.02           C  
ANISOU 5606  CA  ALA B 264     7353   7179  10174     46     69     59       C  
ATOM   5607  C   ALA B 264      82.055  11.513  -0.699  1.00 68.44           C  
ANISOU 5607  C   ALA B 264     7799   7621  10584     -9     -4     22       C  
ATOM   5608  O   ALA B 264      80.907  11.185  -1.002  1.00 68.30           O  
ANISOU 5608  O   ALA B 264     7878   7605  10467    -14    -28     32       O  
ATOM   5609  CB  ALA B 264      83.806   9.761  -0.389  1.00 65.95           C  
ANISOU 5609  CB  ALA B 264     7440   7338  10279     80     10     34       C  
ATOM   5610  N   PHE B 265      82.326  12.514   0.160  1.00 64.06           N  
ANISOU 5610  N   PHE B 265     7143   7067  10131    -49    -39    -25       N  
ATOM   5611  CA  PHE B 265      81.286  13.285   0.836  1.00 62.52           C  
ANISOU 5611  CA  PHE B 265     6955   6876   9926    -89    -96    -68       C  
ATOM   5612  C   PHE B 265      80.465  14.086  -0.188  1.00 65.25           C  
ANISOU 5612  C   PHE B 265     7351   7170  10272   -103    -35    -17       C  
ATOM   5613  O   PHE B 265      79.239  14.124  -0.076  1.00 64.45           O  
ANISOU 5613  O   PHE B 265     7308   7081  10098   -111    -70    -17       O  
ATOM   5614  CB  PHE B 265      81.912  14.219   1.890  1.00 64.59           C  
ANISOU 5614  CB  PHE B 265     7099   7140  10301   -122   -145   -150       C  
ATOM   5615  CG  PHE B 265      80.928  14.957   2.771  1.00 65.55           C  
ANISOU 5615  CG  PHE B 265     7230   7273  10404   -147   -206   -216       C  
ATOM   5616  CD1 PHE B 265      80.433  14.371   3.929  1.00 67.30           C  
ANISOU 5616  CD1 PHE B 265     7477   7571  10521   -125   -288   -261       C  
ATOM   5617  CD2 PHE B 265      80.555  16.266   2.482  1.00 67.90           C  
ANISOU 5617  CD2 PHE B 265     7506   7499  10794   -183   -171   -229       C  
ATOM   5618  CE1 PHE B 265      79.544  15.062   4.753  1.00 68.14           C  
ANISOU 5618  CE1 PHE B 265     7594   7694  10603   -135   -329   -322       C  
ATOM   5619  CE2 PHE B 265      79.671  16.957   3.311  1.00 70.28           C  
ANISOU 5619  CE2 PHE B 265     7817   7805  11082   -194   -218   -297       C  
ATOM   5620  CZ  PHE B 265      79.172  16.350   4.442  1.00 67.67           C  
ANISOU 5620  CZ  PHE B 265     7516   7561  10636   -169   -295   -346       C  
ATOM   5621  N   ILE B 266      81.133  14.691  -1.195  1.00 61.89           N  
ANISOU 5621  N   ILE B 266     6899   6692   9926    -97     60     38       N  
ATOM   5622  CA  ILE B 266      80.470  15.493  -2.236  1.00 61.77           C  
ANISOU 5622  CA  ILE B 266     6930   6632   9907    -92    128    108       C  
ATOM   5623  C   ILE B 266      79.626  14.557  -3.141  1.00 66.08           C  
ANISOU 5623  C   ILE B 266     7605   7215  10287    -51    125    154       C  
ATOM   5624  O   ILE B 266      78.439  14.825  -3.323  1.00 66.62           O  
ANISOU 5624  O   ILE B 266     7726   7291  10297    -55     96    171       O  
ATOM   5625  CB  ILE B 266      81.487  16.344  -3.070  1.00 65.29           C  
ANISOU 5625  CB  ILE B 266     7310   7011  10485    -88    249    174       C  
ATOM   5626  CG1 ILE B 266      82.226  17.359  -2.160  1.00 65.72           C  
ANISOU 5626  CG1 ILE B 266     7227   7012  10733   -148    235    111       C  
ATOM   5627  CG2 ILE B 266      80.786  17.073  -4.229  1.00 65.78           C  
ANISOU 5627  CG2 ILE B 266     7440   7038  10515    -59    330    274       C  
ATOM   5628  CD1 ILE B 266      83.360  18.149  -2.802  1.00 68.28           C  
ANISOU 5628  CD1 ILE B 266     7450   7256  11236   -162    354    171       C  
ATOM   5629  N   ILE B 267      80.208  13.459  -3.661  1.00 61.50           N  
ANISOU 5629  N   ILE B 267     7072   6657   9638    -12    148    165       N  
ATOM   5630  CA  ILE B 267      79.488  12.531  -4.546  1.00 60.86           C  
ANISOU 5630  CA  ILE B 267     7117   6600   9406     24    136    184       C  
ATOM   5631  C   ILE B 267      78.220  11.981  -3.841  1.00 64.52           C  
ANISOU 5631  C   ILE B 267     7620   7094   9799    -11     25    138       C  
ATOM   5632  O   ILE B 267      77.165  11.930  -4.473  1.00 64.87           O  
ANISOU 5632  O   ILE B 267     7737   7153   9759     -9     -5    154       O  
ATOM   5633  CB  ILE B 267      80.407  11.359  -5.022  1.00 64.05           C  
ANISOU 5633  CB  ILE B 267     7563   7009   9766     75    182    183       C  
ATOM   5634  CG1 ILE B 267      81.553  11.897  -5.921  1.00 64.84           C  
ANISOU 5634  CG1 ILE B 267     7628   7084   9923    122    316    250       C  
ATOM   5635  CG2 ILE B 267      79.591  10.284  -5.783  1.00 65.08           C  
ANISOU 5635  CG2 ILE B 267     7831   7154   9744    102    145    166       C  
ATOM   5636  CD1 ILE B 267      82.603  10.895  -6.314  1.00 72.72           C  
ANISOU 5636  CD1 ILE B 267     8644   8084  10902    186    383    254       C  
ATOM   5637  N   CYS B 268      78.312  11.628  -2.541  1.00 60.68           N  
ANISOU 5637  N   CYS B 268     7080   6623   9351    -40    -34     88       N  
ATOM   5638  CA  CYS B 268      77.212  11.000  -1.798  1.00 59.68           C  
ANISOU 5638  CA  CYS B 268     6983   6524   9168    -67   -116     60       C  
ATOM   5639  C   CYS B 268      76.162  12.016  -1.316  1.00 64.44           C  
ANISOU 5639  C   CYS B 268     7550   7137   9796    -98   -148     57       C  
ATOM   5640  O   CYS B 268      74.988  11.642  -1.265  1.00 65.55           O  
ANISOU 5640  O   CYS B 268     7726   7297   9883   -115   -195     63       O  
ATOM   5641  CB  CYS B 268      77.755  10.221  -0.613  1.00 59.27           C  
ANISOU 5641  CB  CYS B 268     6900   6493   9129    -62   -151     27       C  
ATOM   5642  SG  CYS B 268      78.698   8.750  -1.073  1.00 63.25           S  
ANISOU 5642  SG  CYS B 268     7457   6976   9598    -14   -119     36       S  
ATOM   5643  N   TRP B 269      76.545  13.245  -0.922  1.00 61.03           N  
ANISOU 5643  N   TRP B 269     7044   6687   9456   -107   -124     43       N  
ATOM   5644  CA  TRP B 269      75.545  14.169  -0.368  1.00 60.92           C  
ANISOU 5644  CA  TRP B 269     7001   6676   9470   -125   -148     30       C  
ATOM   5645  C   TRP B 269      75.161  15.353  -1.302  1.00 64.09           C  
ANISOU 5645  C   TRP B 269     7402   7034   9915   -116    -98     83       C  
ATOM   5646  O   TRP B 269      74.084  15.901  -1.096  1.00 63.14           O  
ANISOU 5646  O   TRP B 269     7278   6920   9792   -117   -119     92       O  
ATOM   5647  CB  TRP B 269      76.028  14.768   0.956  1.00 60.05           C  
ANISOU 5647  CB  TRP B 269     6816   6569   9432   -137   -168    -42       C  
ATOM   5648  CG  TRP B 269      75.977  13.792   2.095  1.00 60.82           C  
ANISOU 5648  CG  TRP B 269     6918   6728   9464   -132   -226    -80       C  
ATOM   5649  CD1 TRP B 269      77.018  13.088   2.621  1.00 63.67           C  
ANISOU 5649  CD1 TRP B 269     7260   7115   9819   -117   -245   -104       C  
ATOM   5650  CD2 TRP B 269      74.793  13.321   2.763  1.00 60.49           C  
ANISOU 5650  CD2 TRP B 269     6903   6730   9352   -131   -261    -74       C  
ATOM   5651  NE1 TRP B 269      76.569  12.265   3.631  1.00 62.80           N  
ANISOU 5651  NE1 TRP B 269     7170   7061   9632   -102   -290   -111       N  
ATOM   5652  CE2 TRP B 269      75.204  12.379   3.728  1.00 64.29           C  
ANISOU 5652  CE2 TRP B 269     7385   7259   9782   -114   -294    -91       C  
ATOM   5653  CE3 TRP B 269      73.422  13.622   2.653  1.00 61.75           C  
ANISOU 5653  CE3 TRP B 269     7074   6895   9493   -139   -263    -47       C  
ATOM   5654  CZ2 TRP B 269      74.297  11.743   4.584  1.00 63.92           C  
ANISOU 5654  CZ2 TRP B 269     7358   7259   9668   -105   -314    -74       C  
ATOM   5655  CZ3 TRP B 269      72.525  12.989   3.499  1.00 63.27           C  
ANISOU 5655  CZ3 TRP B 269     7274   7137   9630   -136   -287    -38       C  
ATOM   5656  CH2 TRP B 269      72.963  12.066   4.453  1.00 64.02           C  
ANISOU 5656  CH2 TRP B 269     7376   7273   9676   -121   -306    -48       C  
ATOM   5657  N   LEU B 270      75.993  15.751  -2.293  1.00 61.15           N  
ANISOU 5657  N   LEU B 270     7032   6621   9583    -97    -24    130       N  
ATOM   5658  CA  LEU B 270      75.647  16.893  -3.158  1.00 61.18           C  
ANISOU 5658  CA  LEU B 270     7039   6581   9627    -76     36    202       C  
ATOM   5659  C   LEU B 270      74.309  16.644  -3.930  1.00 65.07           C  
ANISOU 5659  C   LEU B 270     7602   7120  10004    -49     -4    255       C  
ATOM   5660  O   LEU B 270      73.488  17.568  -3.928  1.00 65.19           O  
ANISOU 5660  O   LEU B 270     7598   7118  10055    -39     -2    287       O  
ATOM   5661  CB  LEU B 270      76.765  17.235  -4.158  1.00 61.84           C  
ANISOU 5661  CB  LEU B 270     7119   6620   9757    -50    139    268       C  
ATOM   5662  CG  LEU B 270      76.551  18.463  -5.062  1.00 67.46           C  
ANISOU 5662  CG  LEU B 270     7833   7276  10522    -18    225    368       C  
ATOM   5663  CD1 LEU B 270      76.329  19.741  -4.243  1.00 67.61           C  
ANISOU 5663  CD1 LEU B 270     7776   7219  10695    -50    233    341       C  
ATOM   5664  CD2 LEU B 270      77.728  18.647  -5.999  1.00 71.01           C  
ANISOU 5664  CD2 LEU B 270     8277   7689  11016     11    345    444       C  
ATOM   5665  N   PRO B 271      74.020  15.446  -4.541  1.00 60.56           N  
ANISOU 5665  N   PRO B 271     7104   6601   9304    -39    -49    256       N  
ATOM   5666  CA  PRO B 271      72.730  15.282  -5.248  1.00 59.97           C  
ANISOU 5666  CA  PRO B 271     7078   6573   9134    -21   -108    291       C  
ATOM   5667  C   PRO B 271      71.512  15.584  -4.351  1.00 64.09           C  
ANISOU 5667  C   PRO B 271     7546   7114   9690    -50   -171    272       C  
ATOM   5668  O   PRO B 271      70.606  16.291  -4.800  1.00 64.96           O  
ANISOU 5668  O   PRO B 271     7648   7238   9795    -23   -184    325       O  
ATOM   5669  CB  PRO B 271      72.741  13.813  -5.667  1.00 61.27           C  
ANISOU 5669  CB  PRO B 271     7318   6774   9189    -26   -159    254       C  
ATOM   5670  CG  PRO B 271      74.169  13.474  -5.780  1.00 65.92           C  
ANISOU 5670  CG  PRO B 271     7919   7331   9795    -10    -85    242       C  
ATOM   5671  CD  PRO B 271      74.849  14.229  -4.681  1.00 61.51           C  
ANISOU 5671  CD  PRO B 271     7265   6734   9370    -38    -49    221       C  
ATOM   5672  N   PHE B 272      71.511  15.107  -3.083  1.00 59.37           N  
ANISOU 5672  N   PHE B 272     6911   6522   9127    -90   -200    206       N  
ATOM   5673  CA  PHE B 272      70.415  15.344  -2.149  1.00 58.64           C  
ANISOU 5673  CA  PHE B 272     6767   6452   9062   -107   -238    192       C  
ATOM   5674  C   PHE B 272      70.220  16.845  -1.854  1.00 64.27           C  
ANISOU 5674  C   PHE B 272     7428   7125   9866    -82   -191    208       C  
ATOM   5675  O   PHE B 272      69.079  17.314  -1.859  1.00 65.87           O  
ANISOU 5675  O   PHE B 272     7604   7346  10077    -64   -209    242       O  
ATOM   5676  CB  PHE B 272      70.628  14.598  -0.824  1.00 59.88           C  
ANISOU 5676  CB  PHE B 272     6903   6626   9223   -137   -258    130       C  
ATOM   5677  CG  PHE B 272      69.555  14.900   0.203  1.00 61.72           C  
ANISOU 5677  CG  PHE B 272     7085   6888   9478   -140   -274    121       C  
ATOM   5678  CD1 PHE B 272      68.342  14.214   0.192  1.00 65.01           C  
ANISOU 5678  CD1 PHE B 272     7493   7347   9863   -159   -320    151       C  
ATOM   5679  CD2 PHE B 272      69.742  15.899   1.156  1.00 64.40           C  
ANISOU 5679  CD2 PHE B 272     7380   7209   9878   -123   -240     80       C  
ATOM   5680  CE1 PHE B 272      67.338  14.521   1.112  1.00 66.42           C  
ANISOU 5680  CE1 PHE B 272     7613   7555  10069   -153   -315    158       C  
ATOM   5681  CE2 PHE B 272      68.736  16.207   2.076  1.00 67.34           C  
ANISOU 5681  CE2 PHE B 272     7713   7613  10260   -109   -239     73       C  
ATOM   5682  CZ  PHE B 272      67.539  15.519   2.043  1.00 65.79           C  
ANISOU 5682  CZ  PHE B 272     7502   7464  10031   -121   -269    120       C  
ATOM   5683  N   HIS B 273      71.307  17.580  -1.553  1.00 59.33           N  
ANISOU 5683  N   HIS B 273     6779   6439   9324    -81   -133    179       N  
ATOM   5684  CA  HIS B 273      71.219  18.991  -1.178  1.00 58.55           C  
ANISOU 5684  CA  HIS B 273     6634   6276   9337    -65    -85    173       C  
ATOM   5685  C   HIS B 273      70.924  19.879  -2.402  1.00 63.20           C  
ANISOU 5685  C   HIS B 273     7237   6823   9954    -21    -34    276       C  
ATOM   5686  O   HIS B 273      70.346  20.955  -2.223  1.00 63.81           O  
ANISOU 5686  O   HIS B 273     7283   6851  10112      5     -3    295       O  
ATOM   5687  CB  HIS B 273      72.494  19.444  -0.476  1.00 59.08           C  
ANISOU 5687  CB  HIS B 273     6663   6284   9501    -91    -53     96       C  
ATOM   5688  CG  HIS B 273      72.645  18.784   0.857  1.00 61.84           C  
ANISOU 5688  CG  HIS B 273     6996   6686   9815   -113   -108      0       C  
ATOM   5689  ND1 HIS B 273      72.022  19.290   1.982  1.00 63.50           N  
ANISOU 5689  ND1 HIS B 273     7181   6907  10040   -104   -125    -63       N  
ATOM   5690  CD2 HIS B 273      73.252  17.622   1.181  1.00 63.46           C  
ANISOU 5690  CD2 HIS B 273     7214   6940   9957   -130   -144    -29       C  
ATOM   5691  CE1 HIS B 273      72.295  18.441   2.955  1.00 62.93           C  
ANISOU 5691  CE1 HIS B 273     7109   6898   9903   -113   -170   -124       C  
ATOM   5692  NE2 HIS B 273      73.035  17.421   2.521  1.00 63.15           N  
ANISOU 5692  NE2 HIS B 273     7157   6947   9889   -130   -185   -102       N  
ATOM   5693  N   VAL B 274      71.223  19.409  -3.632  1.00 60.21           N  
ANISOU 5693  N   VAL B 274     6912   6467   9498     -1    -24    346       N  
ATOM   5694  CA  VAL B 274      70.862  20.158  -4.846  1.00 61.02           C  
ANISOU 5694  CA  VAL B 274     7040   6553   9591     60     20    461       C  
ATOM   5695  C   VAL B 274      69.332  20.154  -4.958  1.00 64.12           C  
ANISOU 5695  C   VAL B 274     7424   7007   9929     89    -50    497       C  
ATOM   5696  O   VAL B 274      68.728  21.222  -5.075  1.00 65.14           O  
ANISOU 5696  O   VAL B 274     7523   7099  10128    134    -17    556       O  
ATOM   5697  CB  VAL B 274      71.551  19.617  -6.140  1.00 65.26           C  
ANISOU 5697  CB  VAL B 274     7649   7118  10028     91     50    524       C  
ATOM   5698  CG1 VAL B 274      70.896  20.182  -7.409  1.00 65.93           C  
ANISOU 5698  CG1 VAL B 274     7777   7229  10046    171     66    649       C  
ATOM   5699  CG2 VAL B 274      73.054  19.899  -6.129  1.00 64.91           C  
ANISOU 5699  CG2 VAL B 274     7588   6999  10075     76    149    522       C  
ATOM   5700  N   LEU B 275      68.716  18.960  -4.827  1.00 58.73           N  
ANISOU 5700  N   LEU B 275     6756   6411   9145     61   -145    458       N  
ATOM   5701  CA  LEU B 275      67.257  18.762  -4.897  1.00 58.10           C  
ANISOU 5701  CA  LEU B 275     6649   6402   9024     73   -227    483       C  
ATOM   5702  C   LEU B 275      66.537  19.472  -3.746  1.00 61.96           C  
ANISOU 5702  C   LEU B 275     7059   6868   9614     73   -211    461       C  
ATOM   5703  O   LEU B 275      65.433  19.971  -3.958  1.00 63.01           O  
ANISOU 5703  O   LEU B 275     7150   7028   9762    116   -233    520       O  
ATOM   5704  CB  LEU B 275      66.904  17.265  -4.875  1.00 57.10           C  
ANISOU 5704  CB  LEU B 275     6544   6346   8804     21   -321    430       C  
ATOM   5705  CG  LEU B 275      67.490  16.396  -5.997  1.00 60.91           C  
ANISOU 5705  CG  LEU B 275     7117   6855   9170     25   -348    428       C  
ATOM   5706  CD1 LEU B 275      67.221  14.952  -5.742  1.00 60.91           C  
ANISOU 5706  CD1 LEU B 275     7136   6890   9120    -37   -429    356       C  
ATOM   5707  CD2 LEU B 275      66.956  16.798  -7.366  1.00 63.06           C  
ANISOU 5707  CD2 LEU B 275     7427   7178   9356     94   -380    511       C  
ATOM   5708  N   THR B 276      67.163  19.519  -2.538  1.00 56.98           N  
ANISOU 5708  N   THR B 276     6409   6195   9046     36   -175    374       N  
ATOM   5709  CA  THR B 276      66.634  20.176  -1.332  1.00 56.62           C  
ANISOU 5709  CA  THR B 276     6305   6129   9078     45   -150    329       C  
ATOM   5710  C   THR B 276      66.622  21.707  -1.539  1.00 63.56           C  
ANISOU 5710  C   THR B 276     7166   6918  10068    101    -75    368       C  
ATOM   5711  O   THR B 276      65.666  22.370  -1.124  1.00 64.55           O  
ANISOU 5711  O   THR B 276     7245   7037  10243    143    -60    382       O  
ATOM   5712  CB  THR B 276      67.460  19.773  -0.102  1.00 59.11           C  
ANISOU 5712  CB  THR B 276     6622   6435   9402      1   -142    221       C  
ATOM   5713  OG1 THR B 276      67.389  18.361   0.049  1.00 60.44           O  
ANISOU 5713  OG1 THR B 276     6811   6675   9480    -41   -200    206       O  
ATOM   5714  CG2 THR B 276      66.975  20.420   1.175  1.00 55.99           C  
ANISOU 5714  CG2 THR B 276     6183   6031   9057     22   -116    160       C  
ATOM   5715  N   PHE B 277      67.674  22.265  -2.181  1.00 60.52           N  
ANISOU 5715  N   PHE B 277     6810   6454   9729    105    -18    395       N  
ATOM   5716  CA  PHE B 277      67.742  23.698  -2.453  1.00 60.85           C  
ANISOU 5716  CA  PHE B 277     6838   6388   9897    155     66    447       C  
ATOM   5717  C   PHE B 277      66.703  24.070  -3.532  1.00 66.03           C  
ANISOU 5717  C   PHE B 277     7496   7078  10514    232     59    587       C  
ATOM   5718  O   PHE B 277      66.048  25.109  -3.404  1.00 67.59           O  
ANISOU 5718  O   PHE B 277     7661   7216  10804    292    104    633       O  
ATOM   5719  CB  PHE B 277      69.160  24.127  -2.870  1.00 62.65           C  
ANISOU 5719  CB  PHE B 277     7083   6516  10203    130    140    450       C  
ATOM   5720  CG  PHE B 277      69.281  25.603  -3.192  1.00 64.96           C  
ANISOU 5720  CG  PHE B 277     7360   6672  10652    173    240    514       C  
ATOM   5721  CD1 PHE B 277      69.315  26.555  -2.178  1.00 68.41           C  
ANISOU 5721  CD1 PHE B 277     7757   7001  11235    164    277    423       C  
ATOM   5722  CD2 PHE B 277      69.397  26.038  -4.506  1.00 67.84           C  
ANISOU 5722  CD2 PHE B 277     7753   7006  11015    229    303    666       C  
ATOM   5723  CE1 PHE B 277      69.398  27.923  -2.478  1.00 70.68           C  
ANISOU 5723  CE1 PHE B 277     8030   7135  11689    202    376    480       C  
ATOM   5724  CE2 PHE B 277      69.504  27.405  -4.803  1.00 72.05           C  
ANISOU 5724  CE2 PHE B 277     8271   7396  11709    272    409    744       C  
ATOM   5725  CZ  PHE B 277      69.501  28.337  -3.787  1.00 70.38           C  
ANISOU 5725  CZ  PHE B 277     8015   7060  11665    254    446    649       C  
ATOM   5726  N   LEU B 278      66.529  23.209  -4.565  1.00 61.39           N  
ANISOU 5726  N   LEU B 278     6947   6589   9789    238     -5    649       N  
ATOM   5727  CA  LEU B 278      65.526  23.414  -5.619  1.00 61.55           C  
ANISOU 5727  CA  LEU B 278     6969   6674   9742    315    -44    771       C  
ATOM   5728  C   LEU B 278      64.113  23.319  -5.032  1.00 66.88           C  
ANISOU 5728  C   LEU B 278     7570   7414  10426    329   -110    762       C  
ATOM   5729  O   LEU B 278      63.237  24.082  -5.440  1.00 67.74           O  
ANISOU 5729  O   LEU B 278     7642   7528  10567    410   -106    857       O  
ATOM   5730  CB  LEU B 278      65.698  22.408  -6.763  1.00 61.16           C  
ANISOU 5730  CB  LEU B 278     6986   6722   9530    314   -113    804       C  
ATOM   5731  CG  LEU B 278      66.969  22.492  -7.601  1.00 65.27           C  
ANISOU 5731  CG  LEU B 278     7582   7200  10019    327    -36    845       C  
ATOM   5732  CD1 LEU B 278      67.053  21.339  -8.560  1.00 65.37           C  
ANISOU 5732  CD1 LEU B 278     7667   7317   9852    328   -112    844       C  
ATOM   5733  CD2 LEU B 278      67.047  23.794  -8.365  1.00 68.53           C  
ANISOU 5733  CD2 LEU B 278     8004   7543  10493    418     64    987       C  
ATOM   5734  N   ASP B 279      63.909  22.400  -4.044  1.00 62.98           N  
ANISOU 5734  N   ASP B 279     7048   6967   9913    258   -160    658       N  
ATOM   5735  CA  ASP B 279      62.651  22.230  -3.302  1.00 63.40           C  
ANISOU 5735  CA  ASP B 279     7020   7079   9990    262   -201    645       C  
ATOM   5736  C   ASP B 279      62.308  23.506  -2.530  1.00 69.54           C  
ANISOU 5736  C   ASP B 279     7752   7774  10895    322   -111    645       C  
ATOM   5737  O   ASP B 279      61.159  23.946  -2.557  1.00 71.30           O  
ANISOU 5737  O   ASP B 279     7905   8029  11155    383   -119    705       O  
ATOM   5738  CB  ASP B 279      62.736  21.037  -2.334  1.00 64.31           C  
ANISOU 5738  CB  ASP B 279     7128   7240  10066    177   -239    545       C  
ATOM   5739  CG  ASP B 279      61.505  20.831  -1.455  1.00 74.07           C  
ANISOU 5739  CG  ASP B 279     8274   8533  11335    179   -255    540       C  
ATOM   5740  OD1 ASP B 279      60.372  20.963  -1.972  1.00 74.96           O  
ANISOU 5740  OD1 ASP B 279     8319   8701  11460    220   -298    619       O  
ATOM   5741  OD2 ASP B 279      61.674  20.451  -0.280  1.00 79.56           O  
ANISOU 5741  OD2 ASP B 279     8963   9229  12036    141   -228    464       O  
ATOM   5742  N   ALA B 280      63.309  24.099  -1.846  1.00 65.08           N  
ANISOU 5742  N   ALA B 280     7222   7100  10406    306    -30    570       N  
ATOM   5743  CA  ALA B 280      63.150  25.338  -1.087  1.00 65.29           C  
ANISOU 5743  CA  ALA B 280     7223   7023  10563    358     58    540       C  
ATOM   5744  C   ALA B 280      62.695  26.475  -1.996  1.00 71.45           C  
ANISOU 5744  C   ALA B 280     7990   7741  11417    453    106    671       C  
ATOM   5745  O   ALA B 280      61.805  27.237  -1.601  1.00 72.70           O  
ANISOU 5745  O   ALA B 280     8097   7872  11652    526    144    694       O  
ATOM   5746  CB  ALA B 280      64.451  25.706  -0.401  1.00 65.53           C  
ANISOU 5746  CB  ALA B 280     7292   6945  10660    309    113    426       C  
ATOM   5747  N   LEU B 281      63.269  26.564  -3.234  1.00 67.67           N  
ANISOU 5747  N   LEU B 281     7559   7247  10906    465    109    768       N  
ATOM   5748  CA  LEU B 281      62.912  27.596  -4.224  1.00 68.34           C  
ANISOU 5748  CA  LEU B 281     7643   7281  11042    567    158    921       C  
ATOM   5749  C   LEU B 281      61.463  27.413  -4.697  1.00 72.73           C  
ANISOU 5749  C   LEU B 281     8139   7962  11531    641     77   1019       C  
ATOM   5750  O   LEU B 281      60.794  28.403  -4.977  1.00 73.44           O  
ANISOU 5750  O   LEU B 281     8198   8012  11693    746    120   1129       O  
ATOM   5751  CB  LEU B 281      63.871  27.584  -5.434  1.00 68.07           C  
ANISOU 5751  CB  LEU B 281     7679   7225  10957    570    185   1011       C  
ATOM   5752  CG  LEU B 281      65.341  27.958  -5.166  1.00 70.62           C  
ANISOU 5752  CG  LEU B 281     8039   7408  11384    508    281    948       C  
ATOM   5753  CD1 LEU B 281      66.189  27.705  -6.377  1.00 69.68           C  
ANISOU 5753  CD1 LEU B 281     7982   7303  11189    511    307   1042       C  
ATOM   5754  CD2 LEU B 281      65.477  29.400  -4.722  1.00 72.43           C  
ANISOU 5754  CD2 LEU B 281     8247   7455  11819    546    398    955       C  
ATOM   5755  N   ALA B 282      60.973  26.154  -4.747  1.00 68.35           N  
ANISOU 5755  N   ALA B 282     7558   7552  10858    586    -39    978       N  
ATOM   5756  CA  ALA B 282      59.590  25.851  -5.112  1.00 68.56           C  
ANISOU 5756  CA  ALA B 282     7504   7705  10840    634   -133   1051       C  
ATOM   5757  C   ALA B 282      58.621  26.386  -4.043  1.00 74.72           C  
ANISOU 5757  C   ALA B 282     8190   8462  11739    680    -84   1033       C  
ATOM   5758  O   ALA B 282      57.597  26.972  -4.400  1.00 76.08           O  
ANISOU 5758  O   ALA B 282     8290   8664  11952    779    -92   1140       O  
ATOM   5759  CB  ALA B 282      59.409  24.359  -5.299  1.00 68.37           C  
ANISOU 5759  CB  ALA B 282     7474   7812  10691    544   -260    994       C  
ATOM   5760  N   TRP B 283      58.971  26.239  -2.739  1.00 71.17           N  
ANISOU 5760  N   TRP B 283     7744   7961  11339    622    -27    901       N  
ATOM   5761  CA  TRP B 283      58.162  26.758  -1.629  1.00 71.74           C  
ANISOU 5761  CA  TRP B 283     7743   8009  11505    672     39    866       C  
ATOM   5762  C   TRP B 283      58.231  28.286  -1.559  1.00 78.01           C  
ANISOU 5762  C   TRP B 283     8552   8653  12436    773    156    897       C  
ATOM   5763  O   TRP B 283      57.261  28.909  -1.128  1.00 80.35           O  
ANISOU 5763  O   TRP B 283     8778   8936  12814    860    207    921       O  
ATOM   5764  CB  TRP B 283      58.581  26.164  -0.276  1.00 69.53           C  
ANISOU 5764  CB  TRP B 283     7480   7729  11207    594     65    715       C  
ATOM   5765  CG  TRP B 283      58.253  24.710  -0.120  1.00 69.73           C  
ANISOU 5765  CG  TRP B 283     7475   7887  11131    508    -28    695       C  
ATOM   5766  CD1 TRP B 283      59.121  23.660  -0.178  1.00 71.56           C  
ANISOU 5766  CD1 TRP B 283     7771   8145  11273    409    -82    635       C  
ATOM   5767  CD2 TRP B 283      56.944  24.141   0.031  1.00 69.93           C  
ANISOU 5767  CD2 TRP B 283     7389   8027  11155    516    -75    748       C  
ATOM   5768  NE1 TRP B 283      58.440  22.474  -0.025  1.00 70.77           N  
ANISOU 5768  NE1 TRP B 283     7617   8154  11119    351   -156    641       N  
ATOM   5769  CE2 TRP B 283      57.100  22.741   0.096  1.00 72.86           C  
ANISOU 5769  CE2 TRP B 283     7768   8475  11441    409   -154    709       C  
ATOM   5770  CE3 TRP B 283      55.650  24.683   0.131  1.00 72.22           C  
ANISOU 5770  CE3 TRP B 283     7563   8355  11522    604    -52    827       C  
ATOM   5771  CZ2 TRP B 283      56.018  21.878   0.267  1.00 72.54           C  
ANISOU 5771  CZ2 TRP B 283     7621   8537  11402    375   -209    746       C  
ATOM   5772  CZ3 TRP B 283      54.577  23.825   0.290  1.00 73.83           C  
ANISOU 5772  CZ3 TRP B 283     7653   8678  11724    573   -110    867       C  
ATOM   5773  CH2 TRP B 283      54.765  22.444   0.365  1.00 73.71           C  
ANISOU 5773  CH2 TRP B 283     7645   8726  11634    454   -188    825       C  
ATOM   5774  N   MET B 284      59.355  28.889  -1.994  1.00 73.92           N  
ANISOU 5774  N   MET B 284     8117   8013  11956    764    207    903       N  
ATOM   5775  CA  MET B 284      59.530  30.348  -2.028  1.00 75.15           C  
ANISOU 5775  CA  MET B 284     8291   7996  12266    849    324    941       C  
ATOM   5776  C   MET B 284      58.765  30.984  -3.210  1.00 78.37           C  
ANISOU 5776  C   MET B 284     8666   8419  12692    971    323   1141       C  
ATOM   5777  O   MET B 284      58.639  32.209  -3.275  1.00 79.47           O  
ANISOU 5777  O   MET B 284     8803   8423  12971   1069    423   1203       O  
ATOM   5778  CB  MET B 284      61.016  30.714  -2.119  1.00 77.78           C  
ANISOU 5778  CB  MET B 284     8709   8187  12655    782    383    882       C  
ATOM   5779  CG  MET B 284      61.784  30.406  -0.861  1.00 81.54           C  
ANISOU 5779  CG  MET B 284     9212   8631  13138    684    388    683       C  
ATOM   5780  SD  MET B 284      63.549  30.730  -1.036  1.00 86.65           S  
ANISOU 5780  SD  MET B 284     9928   9127  13868    596    440    619       S  
ATOM   5781  CE  MET B 284      64.095  30.324   0.583  1.00 82.87           C  
ANISOU 5781  CE  MET B 284     9458   8665  13363    505    407    385       C  
ATOM   5782  N   GLY B 285      58.274  30.148  -4.123  1.00 72.91           N  
ANISOU 5782  N   GLY B 285     7953   7889  11861    970    206   1234       N  
ATOM   5783  CA  GLY B 285      57.531  30.583  -5.297  1.00 73.21           C  
ANISOU 5783  CA  GLY B 285     7959   7983  11876   1089    173   1422       C  
ATOM   5784  C   GLY B 285      58.408  30.904  -6.484  1.00 76.22           C  
ANISOU 5784  C   GLY B 285     8431   8319  12209   1112    197   1532       C  
ATOM   5785  O   GLY B 285      57.924  31.457  -7.472  1.00 77.72           O  
ANISOU 5785  O   GLY B 285     8614   8535  12381   1232    192   1704       O  
ATOM   5786  N   VAL B 286      59.703  30.556  -6.397  1.00 70.73           N  
ANISOU 5786  N   VAL B 286     7821   7563  11493   1007    230   1441       N  
ATOM   5787  CA  VAL B 286      60.696  30.789  -7.445  1.00 70.76           C  
ANISOU 5787  CA  VAL B 286     7911   7519  11456   1020    277   1539       C  
ATOM   5788  C   VAL B 286      60.462  29.766  -8.561  1.00 76.08           C  
ANISOU 5788  C   VAL B 286     8609   8389  11910   1025    141   1602       C  
ATOM   5789  O   VAL B 286      60.394  30.147  -9.729  1.00 76.98           O  
ANISOU 5789  O   VAL B 286     8759   8539  11951   1127    144   1765       O  
ATOM   5790  CB  VAL B 286      62.147  30.730  -6.879  1.00 73.42           C  
ANISOU 5790  CB  VAL B 286     8307   7726  11865    905    360   1415       C  
ATOM   5791  CG1 VAL B 286      63.183  30.959  -7.971  1.00 73.79           C  
ANISOU 5791  CG1 VAL B 286     8429   7718  11889    925    434   1534       C  
ATOM   5792  CG2 VAL B 286      62.338  31.737  -5.747  1.00 73.48           C  
ANISOU 5792  CG2 VAL B 286     8290   7545  12085    895    470   1321       C  
ATOM   5793  N   ILE B 287      60.316  28.474  -8.196  1.00 73.11           N  
ANISOU 5793  N   ILE B 287     8215   8138  11426    924     22   1474       N  
ATOM   5794  CA  ILE B 287      60.054  27.399  -9.156  1.00 73.47           C  
ANISOU 5794  CA  ILE B 287     8284   8360  11273    918   -122   1501       C  
ATOM   5795  C   ILE B 287      58.533  27.107  -9.164  1.00 80.21           C  
ANISOU 5795  C   ILE B 287     9026   9349  12102    960   -250   1529       C  
ATOM   5796  O   ILE B 287      57.999  26.657  -8.157  1.00 79.08           O  
ANISOU 5796  O   ILE B 287     8802   9219  12026    897   -275   1430       O  
ATOM   5797  CB  ILE B 287      60.893  26.109  -8.867  1.00 74.49           C  
ANISOU 5797  CB  ILE B 287     8468   8531  11305    782   -174   1354       C  
ATOM   5798  CG1 ILE B 287      62.419  26.428  -8.686  1.00 73.78           C  
ANISOU 5798  CG1 ILE B 287     8458   8301  11273    732    -42   1314       C  
ATOM   5799  CG2 ILE B 287      60.625  25.029  -9.937  1.00 75.24           C  
ANISOU 5799  CG2 ILE B 287     8602   8791  11193    787   -321   1375       C  
ATOM   5800  CD1 ILE B 287      63.439  25.183  -8.759  1.00 81.19           C  
ANISOU 5800  CD1 ILE B 287     9457   9283  12107    623    -85   1196       C  
ATOM   5801  N   ASN B 288      57.837  27.378 -10.278  1.00 80.13           N  
ANISOU 5801  N   ASN B 288     9004   9447  11995   1073   -330   1671       N  
ATOM   5802  CA  ASN B 288      56.394  27.108 -10.359  1.00 81.80           C  
ANISOU 5802  CA  ASN B 288     9091   9800  12189   1119   -468   1710       C  
ATOM   5803  C   ASN B 288      56.078  26.157 -11.539  1.00 87.69           C  
ANISOU 5803  C   ASN B 288     9862  10731  12726   1122   -653   1724       C  
ATOM   5804  O   ASN B 288      54.953  26.153 -12.052  1.00 89.10           O  
ANISOU 5804  O   ASN B 288     9950  11041  12862   1198   -782   1802       O  
ATOM   5805  CB  ASN B 288      55.598  28.415 -10.485  1.00 84.91           C  
ANISOU 5805  CB  ASN B 288     9418  10152  12693   1279   -403   1873       C  
ATOM   5806  CG  ASN B 288      55.580  29.237  -9.218  1.00108.35           C  
ANISOU 5806  CG  ASN B 288    12341  12954  15873   1281   -249   1832       C  
ATOM   5807  OD1 ASN B 288      55.505  28.711  -8.098  1.00 98.06           O  
ANISOU 5807  OD1 ASN B 288    10976  11645  14637   1189   -249   1699       O  
ATOM   5808  ND2 ASN B 288      55.508  30.549  -9.371  1.00104.82           N  
ANISOU 5808  ND2 ASN B 288    11916  12377  15535   1401   -118   1956       N  
ATOM   5809  N   SER B 289      57.057  25.315 -11.913  1.00 83.88           N  
ANISOU 5809  N   SER B 289     9497  10259  12116   1040   -672   1638       N  
ATOM   5810  CA  SER B 289      56.934  24.326 -12.976  1.00 85.07           C  
ANISOU 5810  CA  SER B 289     9698  10566  12058   1030   -839   1611       C  
ATOM   5811  C   SER B 289      56.773  22.939 -12.372  1.00 90.03           C  
ANISOU 5811  C   SER B 289    10288  11235  12684    869   -945   1431       C  
ATOM   5812  O   SER B 289      57.669  22.480 -11.672  1.00 88.28           O  
ANISOU 5812  O   SER B 289    10116  10914  12514    765   -857   1326       O  
ATOM   5813  CB  SER B 289      58.151  24.388 -13.894  1.00 89.28           C  
ANISOU 5813  CB  SER B 289    10398  11077  12447   1073   -767   1652       C  
ATOM   5814  OG  SER B 289      58.094  23.410 -14.919  1.00100.30           O  
ANISOU 5814  OG  SER B 289    11863  12622  13624   1070   -924   1604       O  
ATOM   5815  N   CYS B 290      55.629  22.275 -12.624  1.00 89.77           N  
ANISOU 5815  N   CYS B 290    10157  11341  12608    847  -1132   1401       N  
ATOM   5816  CA  CYS B 290      55.348  20.934 -12.101  1.00 90.02           C  
ANISOU 5816  CA  CYS B 290    10141  11401  12661    690  -1234   1243       C  
ATOM   5817  C   CYS B 290      56.235  19.884 -12.794  1.00 88.91           C  
ANISOU 5817  C   CYS B 290    10150  11280  12351    627  -1291   1136       C  
ATOM   5818  O   CYS B 290      56.457  18.825 -12.207  1.00 86.35           O  
ANISOU 5818  O   CYS B 290     9828  10921  12061    493  -1312   1003       O  
ATOM   5819  CB  CYS B 290      53.872  20.585 -12.253  1.00 93.90           C  
ANISOU 5819  CB  CYS B 290    10466  12022  13188    679  -1413   1246       C  
ATOM   5820  SG  CYS B 290      52.773  21.551 -11.189  1.00 99.52           S  
ANISOU 5820  SG  CYS B 290    10981  12705  14130    730  -1331   1342       S  
ATOM   5821  N   GLU B 291      56.741  20.169 -14.022  1.00 84.44           N  
ANISOU 5821  N   GLU B 291     9711  10768  11605    732  -1303   1200       N  
ATOM   5822  CA  GLU B 291      57.653  19.266 -14.734  1.00 83.53           C  
ANISOU 5822  CA  GLU B 291     9752  10671  11316    697  -1334   1104       C  
ATOM   5823  C   GLU B 291      58.927  19.075 -13.919  1.00 84.57           C  
ANISOU 5823  C   GLU B 291     9959  10651  11523    619  -1160   1041       C  
ATOM   5824  O   GLU B 291      59.323  17.943 -13.655  1.00 84.15           O  
ANISOU 5824  O   GLU B 291     9951  10576  11447    511  -1194    905       O  
ATOM   5825  CB  GLU B 291      58.006  19.751 -16.158  1.00 86.57           C  
ANISOU 5825  CB  GLU B 291    10263  11145  11483    851  -1349   1207       C  
ATOM   5826  CG  GLU B 291      56.885  19.827 -17.188  1.00100.04           C  
ANISOU 5826  CG  GLU B 291    11925  13032  13052    947  -1550   1260       C  
ATOM   5827  CD  GLU B 291      56.001  21.062 -17.187  1.00129.92           C  
ANISOU 5827  CD  GLU B 291    15590  16850  16926   1069  -1538   1437       C  
ATOM   5828  OE1 GLU B 291      55.794  21.619 -18.289  1.00131.94           O  
ANISOU 5828  OE1 GLU B 291    15909  17187  17033   1233  -1543   1581       O  
ATOM   5829  OE2 GLU B 291      55.613  21.543 -16.101  1.00128.64           O  
ANISOU 5829  OE2 GLU B 291    15280  16623  16976   1014  -1503   1443       O  
ATOM   5830  N   VAL B 292      59.521  20.208 -13.473  1.00 78.98           N  
ANISOU 5830  N   VAL B 292     9254   9834  10923    673   -978   1141       N  
ATOM   5831  CA  VAL B 292      60.737  20.313 -12.659  1.00 76.42           C  
ANISOU 5831  CA  VAL B 292     8977   9364  10694    612   -808   1098       C  
ATOM   5832  C   VAL B 292      60.491  19.662 -11.289  1.00 78.41           C  
ANISOU 5832  C   VAL B 292     9142   9565  11087    479   -819    976       C  
ATOM   5833  O   VAL B 292      61.281  18.814 -10.867  1.00 77.17           O  
ANISOU 5833  O   VAL B 292     9037   9362  10923    389   -797    869       O  
ATOM   5834  CB  VAL B 292      61.171  21.807 -12.514  1.00 80.12           C  
ANISOU 5834  CB  VAL B 292     9444   9727  11272    703   -635   1233       C  
ATOM   5835  CG1 VAL B 292      62.392  21.958 -11.610  1.00 78.25           C  
ANISOU 5835  CG1 VAL B 292     9238   9343  11152    631   -480   1173       C  
ATOM   5836  CG2 VAL B 292      61.431  22.445 -13.876  1.00 81.56           C  
ANISOU 5836  CG2 VAL B 292     9714   9958  11316    845   -606   1381       C  
ATOM   5837  N   ILE B 293      59.376  20.033 -10.620  1.00 74.43           N  
ANISOU 5837  N   ILE B 293     8503   9074  10705    480   -848   1004       N  
ATOM   5838  CA  ILE B 293      58.989  19.526  -9.298  1.00 73.06           C  
ANISOU 5838  CA  ILE B 293     8234   8864  10662    377   -843    919       C  
ATOM   5839  C   ILE B 293      58.827  17.977  -9.365  1.00 77.68           C  
ANISOU 5839  C   ILE B 293     8823   9506  11185    265   -973    802       C  
ATOM   5840  O   ILE B 293      59.271  17.288  -8.442  1.00 76.97           O  
ANISOU 5840  O   ILE B 293     8734   9357  11155    171   -932    715       O  
ATOM   5841  CB  ILE B 293      57.700  20.240  -8.805  1.00 76.45           C  
ANISOU 5841  CB  ILE B 293     8515   9321  11212    427   -852    993       C  
ATOM   5842  CG1 ILE B 293      57.984  21.760  -8.619  1.00 76.62           C  
ANISOU 5842  CG1 ILE B 293     8545   9244  11322    529   -698   1088       C  
ATOM   5843  CG2 ILE B 293      57.184  19.624  -7.488  1.00 75.73           C  
ANISOU 5843  CG2 ILE B 293     8319   9218  11238    330   -851    916       C  
ATOM   5844  CD1 ILE B 293      56.766  22.637  -8.374  1.00 86.57           C  
ANISOU 5844  CD1 ILE B 293     9678  10520  12696    614   -686   1179       C  
ATOM   5845  N   ALA B 294      58.281  17.440 -10.477  1.00 74.78           N  
ANISOU 5845  N   ALA B 294     8472   9246  10696    281  -1128    797       N  
ATOM   5846  CA  ALA B 294      58.140  15.991 -10.668  1.00 74.12           C  
ANISOU 5846  CA  ALA B 294     8401   9197  10562    173  -1258    673       C  
ATOM   5847  C   ALA B 294      59.515  15.306 -10.763  1.00 75.29           C  
ANISOU 5847  C   ALA B 294     8700   9275  10633    130  -1193    586       C  
ATOM   5848  O   ALA B 294      59.691  14.204 -10.226  1.00 74.11           O  
ANISOU 5848  O   ALA B 294     8552   9082  10524     22  -1216    484       O  
ATOM   5849  CB  ALA B 294      57.329  15.706 -11.921  1.00 76.78           C  
ANISOU 5849  CB  ALA B 294     8732   9666  10775    212  -1447    673       C  
ATOM   5850  N   VAL B 295      60.493  15.964 -11.435  1.00 70.69           N  
ANISOU 5850  N   VAL B 295     8236   8673   9950    220  -1102    638       N  
ATOM   5851  CA  VAL B 295      61.853  15.428 -11.573  1.00 69.09           C  
ANISOU 5851  CA  VAL B 295     8165   8406   9678    198  -1023    572       C  
ATOM   5852  C   VAL B 295      62.441  15.275 -10.162  1.00 71.59           C  
ANISOU 5852  C   VAL B 295     8444   8614  10142    118   -909    530       C  
ATOM   5853  O   VAL B 295      62.864  14.174  -9.805  1.00 70.66           O  
ANISOU 5853  O   VAL B 295     8362   8459  10026     37   -921    432       O  
ATOM   5854  CB  VAL B 295      62.749  16.297 -12.503  1.00 72.63           C  
ANISOU 5854  CB  VAL B 295     8724   8856  10015    317   -923    663       C  
ATOM   5855  CG1 VAL B 295      64.181  15.778 -12.541  1.00 71.42           C  
ANISOU 5855  CG1 VAL B 295     8683   8634   9819    297   -822    604       C  
ATOM   5856  CG2 VAL B 295      62.174  16.371 -13.916  1.00 74.16           C  
ANISOU 5856  CG2 VAL B 295     8972   9178  10028    413  -1042    707       C  
ATOM   5857  N   ILE B 296      62.353  16.355  -9.338  1.00 67.39           N  
ANISOU 5857  N   ILE B 296     7837   8034   9733    145   -809    600       N  
ATOM   5858  CA  ILE B 296      62.841  16.389  -7.956  1.00 66.00           C  
ANISOU 5858  CA  ILE B 296     7621   7771   9684     88   -708    560       C  
ATOM   5859  C   ILE B 296      62.201  15.243  -7.143  1.00 72.40           C  
ANISOU 5859  C   ILE B 296     8370   8592  10545    -13   -779    482       C  
ATOM   5860  O   ILE B 296      62.926  14.557  -6.437  1.00 72.21           O  
ANISOU 5860  O   ILE B 296     8378   8515  10542    -71   -734    417       O  
ATOM   5861  CB  ILE B 296      62.577  17.766  -7.276  1.00 68.49           C  
ANISOU 5861  CB  ILE B 296     7861   8046  10117    143   -617    635       C  
ATOM   5862  CG1 ILE B 296      63.099  18.954  -8.145  1.00 68.84           C  
ANISOU 5862  CG1 ILE B 296     7958   8061  10135    244   -539    734       C  
ATOM   5863  CG2 ILE B 296      63.194  17.793  -5.866  1.00 67.58           C  
ANISOU 5863  CG2 ILE B 296     7719   7850  10107     92   -524    574       C  
ATOM   5864  CD1 ILE B 296      62.697  20.402  -7.657  1.00 66.45           C  
ANISOU 5864  CD1 ILE B 296     7585   7704   9959    312   -455    816       C  
ATOM   5865  N   ASP B 297      60.872  15.016  -7.271  1.00 71.48           N  
ANISOU 5865  N   ASP B 297     8161   8545  10453    -32   -887    497       N  
ATOM   5866  CA  ASP B 297      60.140  13.976  -6.540  1.00 72.38           C  
ANISOU 5866  CA  ASP B 297     8195   8664  10640   -130   -946    444       C  
ATOM   5867  C   ASP B 297      60.623  12.551  -6.867  1.00 78.30           C  
ANISOU 5867  C   ASP B 297     9027   9392  11331   -208  -1010    348       C  
ATOM   5868  O   ASP B 297      60.719  11.733  -5.950  1.00 77.32           O  
ANISOU 5868  O   ASP B 297     8880   9220  11278   -287   -986    306       O  
ATOM   5869  CB  ASP B 297      58.637  14.045  -6.827  1.00 76.01           C  
ANISOU 5869  CB  ASP B 297     8527   9208  11147   -131  -1059    487       C  
ATOM   5870  CG  ASP B 297      57.895  15.202  -6.177  1.00 95.28           C  
ANISOU 5870  CG  ASP B 297    10853  11665  13686    -65   -993    578       C  
ATOM   5871  OD1 ASP B 297      58.540  15.992  -5.439  1.00 95.83           O  
ANISOU 5871  OD1 ASP B 297    10949  11670  13792    -23   -857    597       O  
ATOM   5872  OD2 ASP B 297      56.654  15.275  -6.341  1.00106.70           O  
ANISOU 5872  OD2 ASP B 297    12175  13182  15183    -58  -1078    623       O  
ATOM   5873  N   LEU B 298      60.886  12.233  -8.145  1.00 76.99           N  
ANISOU 5873  N   LEU B 298     8960   9257  11034   -181  -1085    315       N  
ATOM   5874  CA  LEU B 298      61.299  10.869  -8.480  1.00 77.56           C  
ANISOU 5874  CA  LEU B 298     9119   9297  11053   -248  -1145    209       C  
ATOM   5875  C   LEU B 298      62.813  10.696  -8.247  1.00 78.82           C  
ANISOU 5875  C   LEU B 298     9395   9381  11171   -228  -1022    183       C  
ATOM   5876  O   LEU B 298      63.248   9.575  -8.000  1.00 79.08           O  
ANISOU 5876  O   LEU B 298     9480   9356  11212   -288  -1026    106       O  
ATOM   5877  CB  LEU B 298      60.913  10.476  -9.932  1.00 79.98           C  
ANISOU 5877  CB  LEU B 298     9485   9679  11226   -226  -1297    161       C  
ATOM   5878  CG  LEU B 298      61.418  11.304 -11.137  1.00 86.61           C  
ANISOU 5878  CG  LEU B 298    10423  10585  11901    -99  -1288    212       C  
ATOM   5879  CD1 LEU B 298      62.862  10.929 -11.524  1.00 86.47           C  
ANISOU 5879  CD1 LEU B 298    10562  10514  11777    -62  -1193    170       C  
ATOM   5880  CD2 LEU B 298      60.563  11.011 -12.366  1.00 91.71           C  
ANISOU 5880  CD2 LEU B 298    11080  11338  12428    -78  -1472    172       C  
ATOM   5881  N   ALA B 299      63.597  11.785  -8.291  1.00 72.78           N  
ANISOU 5881  N   ALA B 299     8661   8608  10384   -146   -911    249       N  
ATOM   5882  CA  ALA B 299      65.041  11.718  -8.080  1.00 70.60           C  
ANISOU 5882  CA  ALA B 299     8469   8267  10090   -127   -796    231       C  
ATOM   5883  C   ALA B 299      65.392  11.638  -6.598  1.00 72.05           C  
ANISOU 5883  C   ALA B 299     8593   8389  10393   -176   -716    222       C  
ATOM   5884  O   ALA B 299      66.432  11.078  -6.248  1.00 70.89           O  
ANISOU 5884  O   ALA B 299     8500   8191  10245   -189   -660    181       O  
ATOM   5885  CB  ALA B 299      65.712  12.933  -8.694  1.00 71.22           C  
ANISOU 5885  CB  ALA B 299     8585   8352  10122    -31   -708    309       C  
ATOM   5886  N   LEU B 300      64.525  12.189  -5.731  1.00 67.88           N  
ANISOU 5886  N   LEU B 300     7957   7875   9959   -190   -710    262       N  
ATOM   5887  CA  LEU B 300      64.755  12.306  -4.291  1.00 66.62           C  
ANISOU 5887  CA  LEU B 300     7743   7678   9891   -214   -633    258       C  
ATOM   5888  C   LEU B 300      64.943  10.913  -3.605  1.00 68.04           C  
ANISOU 5888  C   LEU B 300     7938   7825  10090   -284   -646    205       C  
ATOM   5889  O   LEU B 300      65.903  10.806  -2.850  1.00 66.40           O  
ANISOU 5889  O   LEU B 300     7756   7580   9894   -279   -575    186       O  
ATOM   5890  CB  LEU B 300      63.603  13.065  -3.621  1.00 67.26           C  
ANISOU 5890  CB  LEU B 300     7711   7792  10053   -205   -631    308       C  
ATOM   5891  CG  LEU B 300      63.862  13.664  -2.240  1.00 71.89           C  
ANISOU 5891  CG  LEU B 300     8251   8354  10711   -194   -538    308       C  
ATOM   5892  CD1 LEU B 300      65.025  14.672  -2.266  1.00 71.47           C  
ANISOU 5892  CD1 LEU B 300     8242   8255  10660   -143   -456    301       C  
ATOM   5893  CD2 LEU B 300      62.628  14.360  -1.742  1.00 76.44           C  
ANISOU 5893  CD2 LEU B 300     8722   8967  11356   -173   -535    356       C  
ATOM   5894  N   PRO B 301      64.130   9.836  -3.840  1.00 64.50           N  
ANISOU 5894  N   PRO B 301     7475   7380   9652   -349   -732    180       N  
ATOM   5895  CA  PRO B 301      64.406   8.553  -3.152  1.00 63.80           C  
ANISOU 5895  CA  PRO B 301     7407   7235   9599   -409   -722    144       C  
ATOM   5896  C   PRO B 301      65.798   7.993  -3.485  1.00 66.83           C  
ANISOU 5896  C   PRO B 301     7906   7568   9919   -386   -686     96       C  
ATOM   5897  O   PRO B 301      66.404   7.348  -2.636  1.00 66.09           O  
ANISOU 5897  O   PRO B 301     7828   7428   9855   -401   -637     88       O  
ATOM   5898  CB  PRO B 301      63.305   7.618  -3.679  1.00 66.45           C  
ANISOU 5898  CB  PRO B 301     7711   7570   9967   -484   -833    117       C  
ATOM   5899  CG  PRO B 301      62.231   8.512  -4.141  1.00 71.27           C  
ANISOU 5899  CG  PRO B 301     8233   8256  10589   -466   -890    159       C  
ATOM   5900  CD  PRO B 301      62.926   9.721  -4.688  1.00 66.61           C  
ANISOU 5900  CD  PRO B 301     7697   7698   9916   -372   -846    184       C  
ATOM   5901  N   PHE B 302      66.312   8.267  -4.701  1.00 63.71           N  
ANISOU 5901  N   PHE B 302     7588   7186   9434   -339   -701     75       N  
ATOM   5902  CA  PHE B 302      67.640   7.832  -5.136  1.00 63.34           C  
ANISOU 5902  CA  PHE B 302     7644   7098   9326   -302   -651     38       C  
ATOM   5903  C   PHE B 302      68.743   8.674  -4.474  1.00 67.05           C  
ANISOU 5903  C   PHE B 302     8095   7562   9820   -252   -545     73       C  
ATOM   5904  O   PHE B 302      69.750   8.116  -4.039  1.00 66.55           O  
ANISOU 5904  O   PHE B 302     8061   7457   9766   -244   -495     53       O  
ATOM   5905  CB  PHE B 302      67.771   7.908  -6.660  1.00 65.56           C  
ANISOU 5905  CB  PHE B 302     8013   7406   9490   -256   -692     12       C  
ATOM   5906  CG  PHE B 302      66.877   6.957  -7.418  1.00 67.94           C  
ANISOU 5906  CG  PHE B 302     8350   7710   9755   -304   -814    -56       C  
ATOM   5907  CD1 PHE B 302      67.319   5.686  -7.760  1.00 71.16           C  
ANISOU 5907  CD1 PHE B 302     8848   8051  10139   -327   -832   -140       C  
ATOM   5908  CD2 PHE B 302      65.612   7.351  -7.839  1.00 70.15           C  
ANISOU 5908  CD2 PHE B 302     8571   8055  10029   -323   -917    -43       C  
ATOM   5909  CE1 PHE B 302      66.504   4.819  -8.496  1.00 73.10           C  
ANISOU 5909  CE1 PHE B 302     9128   8286  10363   -379   -957   -225       C  
ATOM   5910  CE2 PHE B 302      64.799   6.483  -8.571  1.00 73.65           C  
ANISOU 5910  CE2 PHE B 302     9035   8503  10446   -375  -1051   -122       C  
ATOM   5911  CZ  PHE B 302      65.252   5.226  -8.899  1.00 72.24           C  
ANISOU 5911  CZ  PHE B 302     8951   8248  10248   -408  -1072   -220       C  
ATOM   5912  N   ALA B 303      68.551  10.013  -4.394  1.00 63.16           N  
ANISOU 5912  N   ALA B 303     7547   7103   9347   -220   -516    122       N  
ATOM   5913  CA  ALA B 303      69.508  10.944  -3.781  1.00 62.02           C  
ANISOU 5913  CA  ALA B 303     7373   6943   9248   -184   -428    141       C  
ATOM   5914  C   ALA B 303      69.653  10.682  -2.284  1.00 67.20           C  
ANISOU 5914  C   ALA B 303     7978   7589   9967   -211   -406    123       C  
ATOM   5915  O   ALA B 303      70.740  10.891  -1.737  1.00 67.62           O  
ANISOU 5915  O   ALA B 303     8024   7624  10043   -191   -354    108       O  
ATOM   5916  CB  ALA B 303      69.073  12.371  -4.012  1.00 62.50           C  
ANISOU 5916  CB  ALA B 303     7388   7024   9337   -151   -408    192       C  
ATOM   5917  N   ILE B 304      68.557  10.218  -1.630  1.00 64.01           N  
ANISOU 5917  N   ILE B 304     7531   7203   9588   -252   -447    130       N  
ATOM   5918  CA  ILE B 304      68.499   9.846  -0.211  1.00 63.84           C  
ANISOU 5918  CA  ILE B 304     7468   7185   9603   -266   -424    130       C  
ATOM   5919  C   ILE B 304      69.343   8.572   0.002  1.00 68.58           C  
ANISOU 5919  C   ILE B 304     8124   7747  10185   -275   -417    109       C  
ATOM   5920  O   ILE B 304      70.034   8.470   1.014  1.00 68.68           O  
ANISOU 5920  O   ILE B 304     8126   7765  10205   -254   -382    106       O  
ATOM   5921  CB  ILE B 304      67.013   9.660   0.267  1.00 67.05           C  
ANISOU 5921  CB  ILE B 304     7809   7621  10048   -302   -451    164       C  
ATOM   5922  CG1 ILE B 304      66.279  11.031   0.296  1.00 67.25           C  
ANISOU 5922  CG1 ILE B 304     7769   7682  10100   -273   -442    190       C  
ATOM   5923  CG2 ILE B 304      66.941   8.987   1.654  1.00 67.36           C  
ANISOU 5923  CG2 ILE B 304     7821   7666  10107   -309   -414    180       C  
ATOM   5924  CD1 ILE B 304      64.759  10.990   0.620  1.00 73.56           C  
ANISOU 5924  CD1 ILE B 304     8482   8518  10949   -298   -463    234       C  
ATOM   5925  N   LEU B 305      69.317   7.633  -0.964  1.00 65.27           N  
ANISOU 5925  N   LEU B 305     7769   7291   9738   -297   -455     89       N  
ATOM   5926  CA  LEU B 305      70.081   6.386  -0.887  1.00 64.99           C  
ANISOU 5926  CA  LEU B 305     7795   7202   9696   -298   -443     69       C  
ATOM   5927  C   LEU B 305      71.608   6.666  -0.894  1.00 68.40           C  
ANISOU 5927  C   LEU B 305     8254   7629  10108   -238   -387     55       C  
ATOM   5928  O   LEU B 305      72.323   6.033  -0.120  1.00 68.86           O  
ANISOU 5928  O   LEU B 305     8316   7669  10179   -218   -360     60       O  
ATOM   5929  CB  LEU B 305      69.706   5.450  -2.045  1.00 65.37           C  
ANISOU 5929  CB  LEU B 305     7913   7204   9720   -331   -498     29       C  
ATOM   5930  CG  LEU B 305      70.304   4.046  -2.023  1.00 69.53           C  
ANISOU 5930  CG  LEU B 305     8512   7651  10257   -334   -486      1       C  
ATOM   5931  CD1 LEU B 305      69.802   3.254  -0.823  1.00 69.60           C  
ANISOU 5931  CD1 LEU B 305     8478   7627  10341   -372   -473     45       C  
ATOM   5932  CD2 LEU B 305      69.956   3.311  -3.284  1.00 71.97           C  
ANISOU 5932  CD2 LEU B 305     8898   7913  10533   -363   -549    -66       C  
ATOM   5933  N   LEU B 306      72.092   7.623  -1.732  1.00 63.61           N  
ANISOU 5933  N   LEU B 306     7653   7038   9477   -205   -365     50       N  
ATOM   5934  CA  LEU B 306      73.514   8.001  -1.796  1.00 63.36           C  
ANISOU 5934  CA  LEU B 306     7621   7000   9451   -155   -304     45       C  
ATOM   5935  C   LEU B 306      74.009   8.565  -0.454  1.00 67.30           C  
ANISOU 5935  C   LEU B 306     8043   7526  10004   -146   -286     47       C  
ATOM   5936  O   LEU B 306      75.183   8.403  -0.127  1.00 68.52           O  
ANISOU 5936  O   LEU B 306     8182   7676  10176   -114   -257     37       O  
ATOM   5937  CB  LEU B 306      73.796   9.022  -2.905  1.00 63.86           C  
ANISOU 5937  CB  LEU B 306     7694   7071   9497   -127   -271     61       C  
ATOM   5938  CG  LEU B 306      73.695   8.543  -4.354  1.00 69.40           C  
ANISOU 5938  CG  LEU B 306     8489   7764  10115   -106   -278     54       C  
ATOM   5939  CD1 LEU B 306      73.841   9.711  -5.312  1.00 69.76           C  
ANISOU 5939  CD1 LEU B 306     8538   7831  10137    -66   -236     96       C  
ATOM   5940  CD2 LEU B 306      74.752   7.485  -4.668  1.00 72.43           C  
ANISOU 5940  CD2 LEU B 306     8939   8110  10472    -69   -239     26       C  
ATOM   5941  N   GLY B 307      73.114   9.196   0.305  1.00 62.09           N  
ANISOU 5941  N   GLY B 307     7331   6898   9362   -168   -307     54       N  
ATOM   5942  CA  GLY B 307      73.407   9.708   1.637  1.00 60.94           C  
ANISOU 5942  CA  GLY B 307     7123   6787   9243   -154   -302     38       C  
ATOM   5943  C   GLY B 307      73.752   8.575   2.580  1.00 63.30           C  
ANISOU 5943  C   GLY B 307     7433   7100   9520   -139   -310     45       C  
ATOM   5944  O   GLY B 307      74.755   8.651   3.293  1.00 63.54           O  
ANISOU 5944  O   GLY B 307     7433   7152   9555   -104   -307     25       O  
ATOM   5945  N   PHE B 308      72.944   7.484   2.549  1.00 58.53           N  
ANISOU 5945  N   PHE B 308     6865   6474   8898   -163   -323     79       N  
ATOM   5946  CA  PHE B 308      73.185   6.263   3.331  1.00 58.33           C  
ANISOU 5946  CA  PHE B 308     6861   6441   8861   -145   -317    109       C  
ATOM   5947  C   PHE B 308      74.405   5.501   2.807  1.00 61.91           C  
ANISOU 5947  C   PHE B 308     7358   6851   9315   -110   -302    100       C  
ATOM   5948  O   PHE B 308      75.059   4.805   3.577  1.00 62.03           O  
ANISOU 5948  O   PHE B 308     7371   6875   9322    -66   -293    123       O  
ATOM   5949  CB  PHE B 308      71.962   5.323   3.325  1.00 60.24           C  
ANISOU 5949  CB  PHE B 308     7125   6646   9118   -193   -325    152       C  
ATOM   5950  CG  PHE B 308      70.744   5.793   4.078  1.00 61.63           C  
ANISOU 5950  CG  PHE B 308     7245   6869   9302   -216   -322    184       C  
ATOM   5951  CD1 PHE B 308      70.645   5.614   5.451  1.00 65.03           C  
ANISOU 5951  CD1 PHE B 308     7651   7348   9709   -180   -292    228       C  
ATOM   5952  CD2 PHE B 308      69.641   6.297   3.402  1.00 63.61           C  
ANISOU 5952  CD2 PHE B 308     7470   7120   9579   -263   -346    180       C  
ATOM   5953  CE1 PHE B 308      69.499   6.012   6.146  1.00 66.31           C  
ANISOU 5953  CE1 PHE B 308     7764   7557   9876   -189   -271    264       C  
ATOM   5954  CE2 PHE B 308      68.485   6.673   4.096  1.00 66.66           C  
ANISOU 5954  CE2 PHE B 308     7795   7549   9985   -277   -333    218       C  
ATOM   5955  CZ  PHE B 308      68.426   6.536   5.463  1.00 65.18           C  
ANISOU 5955  CZ  PHE B 308     7584   7406   9776   -239   -288    259       C  
ATOM   5956  N   THR B 309      74.694   5.621   1.492  1.00 58.02           N  
ANISOU 5956  N   THR B 309     6905   6316   8823   -118   -294     73       N  
ATOM   5957  CA  THR B 309      75.813   4.954   0.826  1.00 58.31           C  
ANISOU 5957  CA  THR B 309     6988   6309   8858    -75   -263     61       C  
ATOM   5958  C   THR B 309      77.136   5.538   1.358  1.00 63.72           C  
ANISOU 5958  C   THR B 309     7606   7037   9567    -24   -241     57       C  
ATOM   5959  O   THR B 309      78.132   4.816   1.392  1.00 64.37           O  
ANISOU 5959  O   THR B 309     7697   7101   9660     27   -217     66       O  
ATOM   5960  CB  THR B 309      75.682   5.092  -0.702  1.00 63.54           C  
ANISOU 5960  CB  THR B 309     7710   6937   9493    -85   -254     33       C  
ATOM   5961  OG1 THR B 309      74.414   4.569  -1.086  1.00 65.38           O  
ANISOU 5961  OG1 THR B 309     7989   7140   9710   -139   -299     24       O  
ATOM   5962  CG2 THR B 309      76.764   4.347  -1.467  1.00 59.92           C  
ANISOU 5962  CG2 THR B 309     7310   6433   9023    -29   -206     19       C  
ATOM   5963  N   ASN B 310      77.134   6.809   1.838  1.00 59.96           N  
ANISOU 5963  N   ASN B 310     7058   6614   9112    -36   -253     39       N  
ATOM   5964  CA  ASN B 310      78.326   7.435   2.431  1.00 59.66           C  
ANISOU 5964  CA  ASN B 310     6939   6615   9115     -3   -252     17       C  
ATOM   5965  C   ASN B 310      78.753   6.664   3.692  1.00 64.47           C  
ANISOU 5965  C   ASN B 310     7526   7268   9702     42   -283     31       C  
ATOM   5966  O   ASN B 310      79.943   6.607   3.991  1.00 66.21           O  
ANISOU 5966  O   ASN B 310     7692   7513   9952     86   -287     23       O  
ATOM   5967  CB  ASN B 310      78.073   8.912   2.756  1.00 57.34           C  
ANISOU 5967  CB  ASN B 310     6580   6350   8857    -34   -266    -20       C  
ATOM   5968  CG  ASN B 310      79.285   9.687   3.240  1.00 77.18           C  
ANISOU 5968  CG  ASN B 310     9000   8887  11440    -19   -273    -62       C  
ATOM   5969  OD1 ASN B 310      79.261  10.318   4.301  1.00 72.46           O  
ANISOU 5969  OD1 ASN B 310     8347   8334  10851    -22   -319   -110       O  
ATOM   5970  ND2 ASN B 310      80.384   9.629   2.503  1.00 69.23           N  
ANISOU 5970  ND2 ASN B 310     7967   7851  10487      1   -229    -50       N  
ATOM   5971  N   SER B 311      77.786   6.023   4.391  1.00 59.63           N  
ANISOU 5971  N   SER B 311     6952   6666   9041     37   -300     65       N  
ATOM   5972  CA  SER B 311      78.032   5.222   5.595  1.00 59.39           C  
ANISOU 5972  CA  SER B 311     6916   6678   8971     92   -319    104       C  
ATOM   5973  C   SER B 311      78.670   3.865   5.230  1.00 63.78           C  
ANISOU 5973  C   SER B 311     7519   7174   9540    138   -289    151       C  
ATOM   5974  O   SER B 311      79.176   3.169   6.117  1.00 64.10           O  
ANISOU 5974  O   SER B 311     7551   7248   9558    204   -298    197       O  
ATOM   5975  CB  SER B 311      76.736   5.009   6.370  1.00 61.67           C  
ANISOU 5975  CB  SER B 311     7230   6988   9214     72   -321    144       C  
ATOM   5976  OG  SER B 311      76.174   6.245   6.777  1.00 69.68           O  
ANISOU 5976  OG  SER B 311     8203   8057  10217     46   -339     99       O  
ATOM   5977  N   CYS B 312      78.645   3.498   3.924  1.00 59.84           N  
ANISOU 5977  N   CYS B 312     7076   6589   9070    114   -251    140       N  
ATOM   5978  CA  CYS B 312      79.270   2.277   3.391  1.00 60.01           C  
ANISOU 5978  CA  CYS B 312     7154   6536   9111    161   -212    165       C  
ATOM   5979  C   CYS B 312      80.707   2.574   3.002  1.00 61.55           C  
ANISOU 5979  C   CYS B 312     7295   6750   9340    217   -188    146       C  
ATOM   5980  O   CYS B 312      81.548   1.676   3.001  1.00 62.13           O  
ANISOU 5980  O   CYS B 312     7377   6797   9434    289   -160    176       O  
ATOM   5981  CB  CYS B 312      78.484   1.728   2.202  1.00 60.93           C  
ANISOU 5981  CB  CYS B 312     7367   6555   9230    112   -190    144       C  
ATOM   5982  SG  CYS B 312      76.729   1.432   2.530  1.00 65.16           S  
ANISOU 5982  SG  CYS B 312     7935   7063   9759     26   -222    164       S  
ATOM   5983  N   VAL B 313      80.972   3.840   2.641  1.00 56.01           N  
ANISOU 5983  N   VAL B 313     6534   6088   8661    186   -190    103       N  
ATOM   5984  CA  VAL B 313      82.265   4.336   2.187  1.00 56.10           C  
ANISOU 5984  CA  VAL B 313     6473   6114   8730    220   -156     88       C  
ATOM   5985  C   VAL B 313      83.178   4.615   3.401  1.00 61.68           C  
ANISOU 5985  C   VAL B 313     7061   6905   9470    260   -209     86       C  
ATOM   5986  O   VAL B 313      84.355   4.268   3.347  1.00 62.53           O  
ANISOU 5986  O   VAL B 313     7107   7022   9629    319   -188    100       O  
ATOM   5987  CB  VAL B 313      82.090   5.611   1.306  1.00 59.43           C  
ANISOU 5987  CB  VAL B 313     6876   6528   9176    165   -129     57       C  
ATOM   5988  CG1 VAL B 313      83.437   6.156   0.836  1.00 59.97           C  
ANISOU 5988  CG1 VAL B 313     6859   6602   9327    196    -73     58       C  
ATOM   5989  CG2 VAL B 313      81.195   5.333   0.103  1.00 58.61           C  
ANISOU 5989  CG2 VAL B 313     6889   6364   9017    138    -96     56       C  
ATOM   5990  N   ASN B 314      82.633   5.208   4.495  1.00 58.33           N  
ANISOU 5990  N   ASN B 314     6606   6548   9010    234   -280     64       N  
ATOM   5991  CA  ASN B 314      83.387   5.577   5.710  1.00 58.67           C  
ANISOU 5991  CA  ASN B 314     6545   6687   9059    271   -355     39       C  
ATOM   5992  C   ASN B 314      84.327   4.439   6.189  1.00 63.80           C  
ANISOU 5992  C   ASN B 314     7171   7365   9704    369   -365     95       C  
ATOM   5993  O   ASN B 314      85.497   4.750   6.404  1.00 63.92           O  
ANISOU 5993  O   ASN B 314     7073   7431   9781    403   -396     73       O  
ATOM   5994  CB  ASN B 314      82.458   5.977   6.847  1.00 57.15           C  
ANISOU 5994  CB  ASN B 314     6366   6561   8788    254   -417     17       C  
ATOM   5995  CG  ASN B 314      81.693   7.236   6.565  1.00 69.41           C  
ANISOU 5995  CG  ASN B 314     7913   8099  10359    174   -418    -44       C  
ATOM   5996  OD1 ASN B 314      81.938   7.941   5.579  1.00 63.21           O  
ANISOU 5996  OD1 ASN B 314     7096   7265   9656    130   -382    -73       O  
ATOM   5997  ND2 ASN B 314      80.787   7.577   7.448  1.00 61.24           N  
ANISOU 5997  ND2 ASN B 314     6905   7110   9254    164   -449    -58       N  
ATOM   5998  N   PRO B 315      83.916   3.137   6.290  1.00 61.27           N  
ANISOU 5998  N   PRO B 315     6945   7003   9332    418   -335    170       N  
ATOM   5999  CA  PRO B 315      84.883   2.097   6.698  1.00 62.01           C  
ANISOU 5999  CA  PRO B 315     7012   7114   9433    526   -336    233       C  
ATOM   6000  C   PRO B 315      86.159   2.086   5.842  1.00 66.90           C  
ANISOU 6000  C   PRO B 315     7560   7708  10149    564   -291    227       C  
ATOM   6001  O   PRO B 315      87.255   1.975   6.391  1.00 68.26           O  
ANISOU 6001  O   PRO B 315     7626   7953  10356    637   -333    242       O  
ATOM   6002  CB  PRO B 315      84.098   0.802   6.487  1.00 63.79           C  
ANISOU 6002  CB  PRO B 315     7370   7243   9627    544   -277    307       C  
ATOM   6003  CG  PRO B 315      82.699   1.181   6.731  1.00 67.64           C  
ANISOU 6003  CG  PRO B 315     7914   7726  10058    462   -291    293       C  
ATOM   6004  CD  PRO B 315      82.568   2.549   6.112  1.00 62.52           C  
ANISOU 6004  CD  PRO B 315     7223   7092   9439    378   -301    204       C  
ATOM   6005  N   PHE B 316      86.021   2.243   4.511  1.00 62.35           N  
ANISOU 6005  N   PHE B 316     7036   7040   9614    521   -206    207       N  
ATOM   6006  CA  PHE B 316      87.140   2.231   3.568  1.00 62.55           C  
ANISOU 6006  CA  PHE B 316     7007   7034   9724    562   -131    210       C  
ATOM   6007  C   PHE B 316      87.973   3.520   3.642  1.00 67.04           C  
ANISOU 6007  C   PHE B 316     7419   7671  10381    527   -159    164       C  
ATOM   6008  O   PHE B 316      89.168   3.462   3.374  1.00 67.86           O  
ANISOU 6008  O   PHE B 316     7423   7786  10576    580   -120    183       O  
ATOM   6009  CB  PHE B 316      86.635   2.032   2.131  1.00 64.01           C  
ANISOU 6009  CB  PHE B 316     7312   7112   9895    532    -32    198       C  
ATOM   6010  CG  PHE B 316      86.011   0.676   1.890  1.00 66.09           C  
ANISOU 6010  CG  PHE B 316     7722   7283  10105    565      1    225       C  
ATOM   6011  CD1 PHE B 316      84.653   0.466   2.115  1.00 69.00           C  
ANISOU 6011  CD1 PHE B 316     8186   7618  10410    498    -37    217       C  
ATOM   6012  CD2 PHE B 316      86.782  -0.394   1.448  1.00 69.62           C  
ANISOU 6012  CD2 PHE B 316     8205   7666  10583    663     76    257       C  
ATOM   6013  CE1 PHE B 316      84.084  -0.797   1.925  1.00 70.44           C  
ANISOU 6013  CE1 PHE B 316     8492   7698  10573    515     -8    238       C  
ATOM   6014  CE2 PHE B 316      86.213  -1.660   1.263  1.00 73.02           C  
ANISOU 6014  CE2 PHE B 316     8773   7988  10984    688    107    271       C  
ATOM   6015  CZ  PHE B 316      84.868  -1.852   1.498  1.00 70.67           C  
ANISOU 6015  CZ  PHE B 316     8565   7652  10637    607     62    260       C  
ATOM   6016  N   LEU B 317      87.367   4.664   4.007  1.00 63.38           N  
ANISOU 6016  N   LEU B 317     6928   7244   9910    438   -220    106       N  
ATOM   6017  CA  LEU B 317      88.076   5.947   4.075  1.00 63.39           C  
ANISOU 6017  CA  LEU B 317     6783   7284  10018    388   -246     52       C  
ATOM   6018  C   LEU B 317      88.875   6.144   5.350  1.00 68.69           C  
ANISOU 6018  C   LEU B 317     7315   8062  10719    419   -366     18       C  
ATOM   6019  O   LEU B 317      89.884   6.848   5.307  1.00 69.28           O  
ANISOU 6019  O   LEU B 317     7239   8162  10922    401   -381    -16       O  
ATOM   6020  CB  LEU B 317      87.101   7.128   3.979  1.00 62.59           C  
ANISOU 6020  CB  LEU B 317     6712   7162   9906    286   -260     -5       C  
ATOM   6021  CG  LEU B 317      86.378   7.381   2.682  1.00 66.96           C  
ANISOU 6021  CG  LEU B 317     7370   7628  10442    243   -162     15       C  
ATOM   6022  CD1 LEU B 317      85.472   8.583   2.822  1.00 66.80           C  
ANISOU 6022  CD1 LEU B 317     7360   7602  10417    159   -193    -34       C  
ATOM   6023  CD2 LEU B 317      87.355   7.630   1.543  1.00 70.31           C  
ANISOU 6023  CD2 LEU B 317     7741   8008  10967    258    -52     47       C  
ATOM   6024  N   TYR B 318      88.395   5.628   6.494  1.00 66.28           N  
ANISOU 6024  N   TYR B 318     7056   7827  10302    462   -454     23       N  
ATOM   6025  CA  TYR B 318      89.038   5.934   7.766  1.00 67.98           C  
ANISOU 6025  CA  TYR B 318     7151   8166  10514    495   -588    -24       C  
ATOM   6026  C   TYR B 318      89.629   4.688   8.457  1.00 74.02           C  
ANISOU 6026  C   TYR B 318     7907   8997  11219    625   -626     56       C  
ATOM   6027  O   TYR B 318      90.812   4.722   8.765  1.00 74.20           O  
ANISOU 6027  O   TYR B 318     7784   9090  11317    676   -685     51       O  
ATOM   6028  CB  TYR B 318      88.038   6.612   8.711  1.00 69.05           C  
ANISOU 6028  CB  TYR B 318     7333   8355  10549    447   -673    -97       C  
ATOM   6029  CG  TYR B 318      87.484   7.890   8.127  1.00 70.95           C  
ANISOU 6029  CG  TYR B 318     7570   8528  10860    331   -641   -174       C  
ATOM   6030  CD1 TYR B 318      88.257   9.044   8.069  1.00 73.94           C  
ANISOU 6030  CD1 TYR B 318     7805   8905  11385    272   -674   -256       C  
ATOM   6031  CD2 TYR B 318      86.198   7.940   7.600  1.00 70.84           C  
ANISOU 6031  CD2 TYR B 318     7687   8446  10783    281   -577   -159       C  
ATOM   6032  CE1 TYR B 318      87.778  10.207   7.472  1.00 74.51           C  
ANISOU 6032  CE1 TYR B 318     7876   8896  11539    173   -629   -309       C  
ATOM   6033  CE2 TYR B 318      85.697   9.107   7.022  1.00 71.48           C  
ANISOU 6033  CE2 TYR B 318     7764   8464  10932    190   -543   -214       C  
ATOM   6034  CZ  TYR B 318      86.494  10.239   6.959  1.00 81.78           C  
ANISOU 6034  CZ  TYR B 318     8937   9756  12381    139   -563   -284       C  
ATOM   6035  OH  TYR B 318      86.027  11.397   6.394  1.00 86.70           O  
ANISOU 6035  OH  TYR B 318     9556  10302  13084     56   -520   -326       O  
ATOM   6036  N   CYS B 319      88.835   3.625   8.729  1.00 72.09           N  
ANISOU 6036  N   CYS B 319     7805   8730  10855    678   -595    136       N  
ATOM   6037  CA  CYS B 319      89.334   2.432   9.435  1.00 73.66           C  
ANISOU 6037  CA  CYS B 319     8009   8981  10998    812   -620    232       C  
ATOM   6038  C   CYS B 319      90.287   1.638   8.549  1.00 78.34           C  
ANISOU 6038  C   CYS B 319     8563   9505  11696    881   -533    297       C  
ATOM   6039  O   CYS B 319      91.382   1.324   9.005  1.00 79.82           O  
ANISOU 6039  O   CYS B 319     8629   9773  11926    974   -587    327       O  
ATOM   6040  CB  CYS B 319      88.187   1.543   9.912  1.00 74.05           C  
ANISOU 6040  CB  CYS B 319     8219   8995  10921    839   -586    310       C  
ATOM   6041  SG  CYS B 319      88.718   0.075  10.844  1.00 79.52           S  
ANISOU 6041  SG  CYS B 319     8934   9731  11547   1012   -598    456       S  
ATOM   6042  N   PHE B 320      89.877   1.296   7.304  1.00 74.40           N  
ANISOU 6042  N   PHE B 320     8167   8867  11236    845   -401    315       N  
ATOM   6043  CA  PHE B 320      90.669   0.448   6.402  1.00 75.10           C  
ANISOU 6043  CA  PHE B 320     8255   8873  11405    922   -294    373       C  
ATOM   6044  C   PHE B 320      91.858   1.222   5.771  1.00 83.21           C  
ANISOU 6044  C   PHE B 320     9119   9926  12572    911   -268    336       C  
ATOM   6045  O   PHE B 320      92.532   0.685   4.887  1.00 84.62           O  
ANISOU 6045  O   PHE B 320     9291  10039  12823    972   -158    377       O  
ATOM   6046  CB  PHE B 320      89.787  -0.150   5.274  1.00 75.38           C  
ANISOU 6046  CB  PHE B 320     8468   8758  11417    883   -172    379       C  
ATOM   6047  CG  PHE B 320      88.553  -0.947   5.665  1.00 76.07           C  
ANISOU 6047  CG  PHE B 320     8712   8783  11406    874   -171    417       C  
ATOM   6048  CD1 PHE B 320      88.400  -1.448   6.955  1.00 79.62           C  
ANISOU 6048  CD1 PHE B 320     9160   9310  11784    920   -252    471       C  
ATOM   6049  CD2 PHE B 320      87.599  -1.286   4.717  1.00 77.24           C  
ANISOU 6049  CD2 PHE B 320     9008   8800  11541    822    -89    403       C  
ATOM   6050  CE1 PHE B 320      87.262  -2.179   7.311  1.00 80.08           C  
ANISOU 6050  CE1 PHE B 320     9351   9302  11772    908   -232    523       C  
ATOM   6051  CE2 PHE B 320      86.465  -2.028   5.070  1.00 79.60           C  
ANISOU 6051  CE2 PHE B 320     9431   9032  11781    800    -88    437       C  
ATOM   6052  CZ  PHE B 320      86.308  -2.475   6.364  1.00 78.05           C  
ANISOU 6052  CZ  PHE B 320     9223   8903  11531    841   -150    505       C  
ATOM   6053  N   VAL B 321      92.145   2.443   6.254  1.00 81.34           N  
ANISOU 6053  N   VAL B 321     8746   9778  12382    838   -363    260       N  
ATOM   6054  CA  VAL B 321      93.233   3.282   5.747  1.00 82.60           C  
ANISOU 6054  CA  VAL B 321     8731   9953  12702    808   -339    228       C  
ATOM   6055  C   VAL B 321      94.055   3.861   6.922  1.00 90.02           C  
ANISOU 6055  C   VAL B 321     9475  11033  13696    816   -501    178       C  
ATOM   6056  O   VAL B 321      95.263   3.994   6.787  1.00 91.14           O  
ANISOU 6056  O   VAL B 321     9440  11212  13979    853   -501    191       O  
ATOM   6057  CB  VAL B 321      92.667   4.406   4.841  1.00 85.39           C  
ANISOU 6057  CB  VAL B 321     9118  10231  13096    678   -269    169       C  
ATOM   6058  CG1 VAL B 321      93.550   5.645   4.821  1.00 85.99           C  
ANISOU 6058  CG1 VAL B 321     8995  10342  13337    608   -299    112       C  
ATOM   6059  CG2 VAL B 321      92.403   3.890   3.433  1.00 84.69           C  
ANISOU 6059  CG2 VAL B 321     9158  10024  12998    696   -101    219       C  
ATOM   6060  N   GLY B 322      93.400   4.164   8.042  1.00 88.25           N  
ANISOU 6060  N   GLY B 322     9282  10889  13359    789   -636    120       N  
ATOM   6061  CA  GLY B 322      94.005   4.750   9.239  1.00 90.16           C  
ANISOU 6061  CA  GLY B 322     9367  11274  13615    794   -815     45       C  
ATOM   6062  C   GLY B 322      95.309   4.138   9.712  1.00 97.14           C  
ANISOU 6062  C   GLY B 322    10098  12262  14551    920   -886    100       C  
ATOM   6063  O   GLY B 322      96.198   4.857  10.182  1.00 97.70           O  
ANISOU 6063  O   GLY B 322     9972  12429  14719    903  -1012     26       O  
ATOM   6064  N   ASN B 323      95.433   2.806   9.576  1.00 95.33           N  
ANISOU 6064  N   ASN B 323     9951  12005  14265   1049   -810    228       N  
ATOM   6065  CA  ASN B 323      96.620   2.033   9.963  1.00 97.60           C  
ANISOU 6065  CA  ASN B 323    10111  12377  14596   1197   -855    311       C  
ATOM   6066  C   ASN B 323      97.809   2.370   9.026  1.00103.42           C  
ANISOU 6066  C   ASN B 323    10656  13083  15556   1189   -780    316       C  
ATOM   6067  O   ASN B 323      98.959   2.422   9.478  1.00105.40           O  
ANISOU 6067  O   ASN B 323    10700  13445  15903   1255   -878    322       O  
ATOM   6068  CB  ASN B 323      96.269   0.526   9.910  1.00 98.24           C  
ANISOU 6068  CB  ASN B 323    10363  12391  14574   1327   -757    450       C  
ATOM   6069  CG  ASN B 323      97.270  -0.468  10.475  1.00122.11           C  
ANISOU 6069  CG  ASN B 323    13298  15495  17604   1510   -799    564       C  
ATOM   6070  OD1 ASN B 323      96.876  -1.495  11.039  1.00117.27           O  
ANISOU 6070  OD1 ASN B 323    12811  14879  16866   1617   -795    664       O  
ATOM   6071  ND2 ASN B 323      98.570  -0.203  10.372  1.00114.86           N  
ANISOU 6071  ND2 ASN B 323    12157  14648  16838   1555   -839    562       N  
ATOM   6072  N   ARG B 324      97.507   2.641   7.736  1.00 98.29           N  
ANISOU 6072  N   ARG B 324    10070  12292  14986   1110   -608    314       N  
ATOM   6073  CA  ARG B 324      98.473   2.917   6.672  1.00 98.27           C  
ANISOU 6073  CA  ARG B 324     9921  12237  15181   1104   -484    339       C  
ATOM   6074  C   ARG B 324      98.713   4.444   6.519  1.00101.36           C  
ANISOU 6074  C   ARG B 324    10161  12633  15719    947   -522    234       C  
ATOM   6075  O   ARG B 324      99.814   4.845   6.149  1.00102.96           O  
ANISOU 6075  O   ARG B 324    10164  12836  16119    937   -472    247       O  
ATOM   6076  CB  ARG B 324      97.946   2.301   5.363  1.00 96.76           C  
ANISOU 6076  CB  ARG B 324     9915  11891  14958   1128   -268    404       C  
ATOM   6077  CG  ARG B 324      98.946   2.249   4.222  1.00104.84           C  
ANISOU 6077  CG  ARG B 324    10830  12857  16147   1164    -99    457       C  
ATOM   6078  CD  ARG B 324      98.556   1.237   3.156  1.00107.88           C  
ANISOU 6078  CD  ARG B 324    11419  13114  16457   1243     89    521       C  
ATOM   6079  NE  ARG B 324      97.270   1.533   2.525  1.00110.16           N  
ANISOU 6079  NE  ARG B 324    11926  13310  16621   1143    140    472       N  
ATOM   6080  CZ  ARG B 324      97.132   2.232   1.405  1.00120.56           C  
ANISOU 6080  CZ  ARG B 324    13279  14557  17971   1070    264    454       C  
ATOM   6081  NH1 ARG B 324      98.199   2.720   0.783  1.00105.42           N  
ANISOU 6081  NH1 ARG B 324    11198  12643  16214   1081    370    487       N  
ATOM   6082  NH2 ARG B 324      95.926   2.457   0.902  1.00106.48           N  
ANISOU 6082  NH2 ARG B 324    11689  12704  16064    990    288    412       N  
ATOM   6083  N   PHE B 325      97.708   5.279   6.833  1.00 95.55           N  
ANISOU 6083  N   PHE B 325     9511  11894  14899    830   -604    134       N  
ATOM   6084  CA  PHE B 325      97.806   6.744   6.777  1.00 94.95           C  
ANISOU 6084  CA  PHE B 325     9314  11802  14960    678   -645     26       C  
ATOM   6085  C   PHE B 325      98.767   7.245   7.847  1.00101.47           C  
ANISOU 6085  C   PHE B 325     9904  12761  15888    669   -845    -59       C  
ATOM   6086  O   PHE B 325      99.478   8.222   7.623  1.00101.62           O  
ANISOU 6086  O   PHE B 325     9735  12762  16115    569   -858   -121       O  
ATOM   6087  CB  PHE B 325      96.406   7.383   6.962  1.00 94.51           C  
ANISOU 6087  CB  PHE B 325     9442  11698  14770    577   -667    -51       C  
ATOM   6088  CG  PHE B 325      96.340   8.896   6.879  1.00 95.41           C  
ANISOU 6088  CG  PHE B 325     9468  11764  15019    424   -689   -159       C  
ATOM   6089  CD1 PHE B 325      96.076   9.531   5.671  1.00 97.27           C  
ANISOU 6089  CD1 PHE B 325     9737  11869  15353    348   -519   -126       C  
ATOM   6090  CD2 PHE B 325      96.477   9.680   8.019  1.00 97.41           C  
ANISOU 6090  CD2 PHE B 325     9623  12099  15290    364   -879   -295       C  
ATOM   6091  CE1 PHE B 325      96.001  10.928   5.596  1.00 97.86           C  
ANISOU 6091  CE1 PHE B 325     9735  11881  15566    212   -528   -211       C  
ATOM   6092  CE2 PHE B 325      96.404  11.076   7.942  1.00 99.83           C  
ANISOU 6092  CE2 PHE B 325     9853  12337  15739    221   -894   -402       C  
ATOM   6093  CZ  PHE B 325      96.167  11.689   6.732  1.00 97.12           C  
ANISOU 6093  CZ  PHE B 325     9537  11850  15513    145   -714   -352       C  
ATOM   6094  N   GLN B 326      98.768   6.573   9.017  1.00100.14           N  
ANISOU 6094  N   GLN B 326     9747  12727  15575    773  -1002    -59       N  
ATOM   6095  CA  GLN B 326      99.583   6.918  10.183  1.00102.51           C  
ANISOU 6095  CA  GLN B 326     9843  13185  15922    787  -1228   -148       C  
ATOM   6096  C   GLN B 326     101.067   6.659   9.925  1.00108.50           C  
ANISOU 6096  C   GLN B 326    10341  13985  16900    843  -1219    -90       C  
ATOM   6097  O   GLN B 326     101.894   7.503  10.273  1.00109.50           O  
ANISOU 6097  O   GLN B 326    10233  14160  17210    762  -1335   -188       O  
ATOM   6098  CB  GLN B 326      99.124   6.121  11.416  1.00104.24           C  
ANISOU 6098  CB  GLN B 326    10170  13543  15894    914  -1375   -133       C  
ATOM   6099  N   GLN B 327     101.407   5.509   9.322  1.00105.61           N  
ANISOU 6099  N   GLN B 327    10008  13591  16527    980  -1080     65       N  
ATOM   6100  CA  GLN B 327     102.797   5.175   9.040  1.00107.87           C  
ANISOU 6100  CA  GLN B 327    10051  13914  17019   1056  -1045    140       C  
ATOM   6101  C   GLN B 327     103.355   6.017   7.888  1.00113.13           C  
ANISOU 6101  C   GLN B 327    10573  14468  17943    934   -894    131       C  
ATOM   6102  O   GLN B 327     104.556   6.285   7.887  1.00114.87           O  
ANISOU 6102  O   GLN B 327    10511  14744  18390    918   -945    121       O  
ATOM   6103  CB  GLN B 327     102.966   3.685   8.725  1.00109.23           C  
ANISOU 6103  CB  GLN B 327    10322  14062  17119   1241   -909    306       C  
ATOM   6104  CG  GLN B 327     103.072   2.816   9.985  1.00129.20           C  
ANISOU 6104  CG  GLN B 327    12867  16737  19488   1401  -1073    354       C  
ATOM   6105  CD  GLN B 327     104.342   3.062  10.802  1.00149.91           C  
ANISOU 6105  CD  GLN B 327    15184  19535  22239   1455  -1271    328       C  
ATOM   6106  OE1 GLN B 327     105.385   3.504  10.294  1.00144.82           O  
ANISOU 6106  OE1 GLN B 327    14289  18891  21845   1415  -1241    323       O  
ATOM   6107  NE2 GLN B 327     104.306   2.694  12.072  1.00143.75           N  
ANISOU 6107  NE2 GLN B 327    14414  18914  21292   1561  -1471    328       N  
ATOM   6108  N   LYS B 328     102.508   6.470   6.943  1.00108.47           N  
ANISOU 6108  N   LYS B 328    10162  13727  17325    849   -713    141       N  
ATOM   6109  CA  LYS B 328     103.001   7.289   5.829  1.00108.93           C  
ANISOU 6109  CA  LYS B 328    10106  13674  17609    745   -545    156       C  
ATOM   6110  C   LYS B 328     103.138   8.771   6.247  1.00115.40           C  
ANISOU 6110  C   LYS B 328    10764  14492  18592    566   -673     13       C  
ATOM   6111  O   LYS B 328     103.879   9.514   5.597  1.00115.98           O  
ANISOU 6111  O   LYS B 328    10645  14501  18921    482   -577     27       O  
ATOM   6112  CB  LYS B 328     102.096   7.165   4.591  1.00108.57           C  
ANISOU 6112  CB  LYS B 328    10313  13481  17459    729   -320    217       C  
ATOM   6113  CG  LYS B 328     102.215   5.799   3.911  1.00111.65           C  
ANISOU 6113  CG  LYS B 328    10809  13835  17779    890   -142    353       C  
ATOM   6114  CD  LYS B 328     101.331   5.673   2.689  1.00113.06           C  
ANISOU 6114  CD  LYS B 328    11230  13878  17849    873     60    393       C  
ATOM   6115  CE  LYS B 328     101.659   4.431   1.896  1.00116.32           C  
ANISOU 6115  CE  LYS B 328    11731  14244  18221   1028    248    507       C  
ATOM   6116  NZ  LYS B 328     101.504   3.176   2.673  1.00121.19           N  
ANISOU 6116  NZ  LYS B 328    12451  14906  18692   1166    170    538       N  
ATOM   6117  N   LEU B 329     102.465   9.188   7.338  1.00113.13           N  
ANISOU 6117  N   LEU B 329    10547  14268  18168    511   -879   -121       N  
ATOM   6118  CA  LEU B 329     102.560  10.561   7.841  1.00114.49           C  
ANISOU 6118  CA  LEU B 329    10581  14431  18491    347  -1013   -280       C  
ATOM   6119  C   LEU B 329     103.796  10.688   8.757  1.00122.05           C  
ANISOU 6119  C   LEU B 329    11238  15530  19605    356  -1227   -355       C  
ATOM   6120  O   LEU B 329     104.429  11.745   8.795  1.00123.25           O  
ANISOU 6120  O   LEU B 329    11167  15649  20014    222  -1284   -449       O  
ATOM   6121  CB  LEU B 329     101.264  10.969   8.578  1.00113.11           C  
ANISOU 6121  CB  LEU B 329    10622  14257  18099    288  -1126   -403       C  
ATOM   6122  CG  LEU B 329     101.138  12.441   9.018  1.00118.61           C  
ANISOU 6122  CG  LEU B 329    11230  14899  18938    113  -1230   -578       C  
ATOM   6123  CD1 LEU B 329     101.281  13.398   7.846  1.00118.69           C  
ANISOU 6123  CD1 LEU B 329    11187  14726  19183     -9  -1022   -531       C  
ATOM   6124  CD2 LEU B 329      99.828  12.690   9.712  1.00119.69           C  
ANISOU 6124  CD2 LEU B 329    11594  15047  18837     90  -1323   -684       C  
ATOM   6125  N   ARG B 330     104.158   9.595   9.457  1.00119.91           N  
ANISOU 6125  N   ARG B 330    10954  15411  19195    517  -1341   -305       N  
ATOM   6126  CA  ARG B 330     105.343   9.548  10.317  1.00122.71           C  
ANISOU 6126  CA  ARG B 330    11027  15927  19669    560  -1556   -357       C  
ATOM   6127  C   ARG B 330     106.620   9.380   9.467  1.00129.13           C  
ANISOU 6127  C   ARG B 330    11575  16713  20775    587  -1420   -237       C  
ATOM   6128  O   ARG B 330     107.712   9.720   9.933  1.00131.61           O  
ANISOU 6128  O   ARG B 330    11587  17125  21293    566  -1574   -293       O  
ATOM   6129  CB  ARG B 330     105.225   8.412  11.344  1.00123.05           C  
ANISOU 6129  CB  ARG B 330    11167  16143  19442    745  -1711   -319       C  
ATOM   6130  N   SER B 331     106.476   8.871   8.220  1.00124.73           N  
ANISOU 6130  N   SER B 331    11127  16028  20236    635  -1132    -78       N  
ATOM   6131  CA  SER B 331     107.586   8.677   7.280  1.00126.13           C  
ANISOU 6131  CA  SER B 331    11087  16166  20670    676   -950     54       C  
ATOM   6132  C   SER B 331     108.058  10.017   6.693  1.00130.91           C  
ANISOU 6132  C   SER B 331    11478  16664  21597    487   -880      2       C  
ATOM   6133  O   SER B 331     109.266  10.239   6.586  1.00132.70           O  
ANISOU 6133  O   SER B 331    11382  16931  22107    470   -899     23       O  
ATOM   6134  CB  SER B 331     107.184   7.730   6.153  1.00128.28           C  
ANISOU 6134  CB  SER B 331    11582  16336  20823    796   -666    220       C  
ATOM   6135  OG  SER B 331     106.916   6.423   6.630  1.00136.78           O  
ANISOU 6135  OG  SER B 331    12821  17490  21659    976   -710    286       O  
ATOM   6136  N   VAL B 332     107.109  10.904   6.315  1.00125.87           N  
ANISOU 6136  N   VAL B 332    11010  15887  20928    347   -796    -56       N  
ATOM   6137  CA  VAL B 332     107.420  12.225   5.750  1.00126.72           C  
ANISOU 6137  CA  VAL B 332    10948  15865  21334    164   -712    -96       C  
ATOM   6138  C   VAL B 332     107.916  13.168   6.877  1.00133.10           C  
ANISOU 6138  C   VAL B 332    11522  16737  22311     25  -1002   -297       C  
ATOM   6139  O   VAL B 332     108.705  14.077   6.603  1.00134.87           O  
ANISOU 6139  O   VAL B 332    11488  16884  22870   -115   -978   -329       O  
ATOM   6140  CB  VAL B 332     106.232  12.868   4.968  1.00128.07           C  
ANISOU 6140  CB  VAL B 332    11380  15865  21413     74   -532    -84       C  
ATOM   6141  CG1 VAL B 332     105.972  12.149   3.649  1.00126.56           C  
ANISOU 6141  CG1 VAL B 332    11355  15597  21134    186   -229    107       C  
ATOM   6142  CG2 VAL B 332     104.962  12.951   5.805  1.00125.76           C  
ANISOU 6142  CG2 VAL B 332    11357  15597  20830     54   -692   -213       C  
ATOM   6143  N   PHE B 333     107.470  12.937   8.131  1.00129.25           N  
ANISOU 6143  N   PHE B 333    11125  16389  21594     67  -1271   -432       N  
ATOM   6144  CA  PHE B 333     107.863  13.740   9.290  1.00130.94           C  
ANISOU 6144  CA  PHE B 333    11153  16689  21909    -40  -1575   -647       C  
ATOM   6145  C   PHE B 333     109.257  13.314   9.804  1.00136.92           C  
ANISOU 6145  C   PHE B 333    11580  17614  22829     33  -1742   -642       C  
ATOM   6146  O   PHE B 333     110.128  14.174   9.963  1.00138.75           O  
ANISOU 6146  O   PHE B 333    11506  17840  23372   -100  -1859   -748       O  
ATOM   6147  CB  PHE B 333     106.815  13.619  10.407  1.00131.37           C  
ANISOU 6147  CB  PHE B 333    11463  16832  21618     -6  -1776   -787       C  
ATOM   6148  N   ARG B 334     109.459  11.985  10.045  1.00132.91           N  
ANISOU 6148  N   ARG B 334    11128  17246  22125    244  -1750   -513       N  
ATOM   6149  CA  ARG B 334     110.701  11.348  10.523  1.00162.32           C  
ANISOU 6149  CA  ARG B 334    14574  21150  25953    365  -1896   -470       C  
ATOM   6150  C   ARG B 334     111.206  12.009  11.812  1.00190.06           C  
ANISOU 6150  C   ARG B 334    17888  24818  29510    294  -2268   -693       C  
ATOM   6151  O   ARG B 334     112.043  11.440  12.514  1.00149.95           O  
ANISOU 6151  O   ARG B 334    12679  19939  24355    432  -2472   -689       O  
ATOM   6152  CB  ARG B 334     111.805  11.395   9.452  1.00164.25           C  
ANISOU 6152  CB  ARG B 334    14522  21322  26565    345  -1695   -331       C  
TER    6153      ARG B 334                                                      
HETATM 6154  N1  8ES A1501      77.243  -2.606  37.295  1.00121.80           N  
ANISOU 6154  N1  8ES A1501    12799  21227  12251   1798     77   1388       N  
HETATM 6155  N3  8ES A1501      82.588  -2.298  32.946  1.00127.96           N  
ANISOU 6155  N3  8ES A1501    12916  22606  13095   1565   -314   1052       N  
HETATM 6156  C4  8ES A1501      74.145  -3.788  38.050  1.00119.07           C  
ANISOU 6156  C4  8ES A1501    12756  20307  12180   1902    435   1789       C  
HETATM 6157  C5  8ES A1501      78.551  -2.538  37.749  1.00122.73           C  
ANISOU 6157  C5  8ES A1501    12805  21677  12150   1891    -41   1288       C  
HETATM 6158  C6  8ES A1501      76.606  -1.408  36.747  1.00121.37           C  
ANISOU 6158  C6  8ES A1501    12734  21017  12365   1544     81   1269       C  
HETATM 6159  C7  8ES A1501      77.257  -0.983  35.418  1.00121.42           C  
ANISOU 6159  C7  8ES A1501    12639  21001  12494   1367     -2   1157       C  
HETATM 6160  C8  8ES A1501      77.275   0.301  35.115  1.00121.70           C  
ANISOU 6160  C8  8ES A1501    12630  21036  12574   1157    -41    984       C  
HETATM 6161  C10 8ES A1501      78.457  -0.076  32.962  1.00121.50           C  
ANISOU 6161  C10 8ES A1501    12486  20953  12724   1055   -113    959       C  
HETATM 6162  C13 8ES A1501      81.315  -0.654  32.217  1.00126.02           C  
ANISOU 6162  C13 8ES A1501    12758  22007  13119   1173   -262    897       C  
HETATM 6163  C15 8ES A1501      80.228   1.597  29.362  1.00122.03           C  
ANISOU 6163  C15 8ES A1501    12373  20900  13095    620   -168    682       C  
HETATM 6164  C17 8ES A1501      78.337   1.307  30.842  1.00121.97           C  
ANISOU 6164  C17 8ES A1501    12545  20731  13068    712   -108    792       C  
HETATM 6165  C20 8ES A1501      79.078  -6.159  38.667  1.00123.29           C  
ANISOU 6165  C20 8ES A1501    13103  21831  11909   2617    104   1757       C  
HETATM 6166  C21 8ES A1501      80.422  -6.124  39.085  1.00125.33           C  
ANISOU 6166  C21 8ES A1501    13232  22462  11926   2759    -26   1662       C  
HETATM 6167  C22 8ES A1501      81.168  -4.918  39.074  1.00126.86           C  
ANISOU 6167  C22 8ES A1501    13235  22887  12081   2587   -173   1438       C  
HETATM 6168  C24 8ES A1501      83.645  -5.232  38.601  1.00132.72           C  
ANISOU 6168  C24 8ES A1501    13646  24178  12603   2732   -396   1321       C  
HETATM 6169  C26 8ES A1501      82.504  -5.138  36.210  1.00130.97           C  
ANISOU 6169  C26 8ES A1501    13524  23352  12886   2373   -263   1398       C  
HETATM 6170  C28 8ES A1501      83.605  -6.832  34.857  1.00131.91           C  
ANISOU 6170  C28 8ES A1501    13662  23483  12976   2652   -242   1598       C  
HETATM 6171  O1  8ES A1501      84.765  -5.168  38.985  1.00134.76           O  
ANISOU 6171  O1  8ES A1501    13735  24785  12681   2832   -520   1236       O  
HETATM 6172  C25 8ES A1501      83.427  -5.697  37.155  1.00132.76           C  
ANISOU 6172  C25 8ES A1501    13692  23915  12836   2645   -323   1419       C  
HETATM 6173  S   8ES A1501      84.362  -6.917  36.396  1.00134.49           S  
ANISOU 6173  S   8ES A1501    13897  24216  12986   2883   -317   1559       S  
HETATM 6174  C27 8ES A1501      82.595  -5.817  34.853  1.00130.25           C  
ANISOU 6174  C27 8ES A1501    13477  23068  12943   2377   -222   1500       C  
HETATM 6175  N6  8ES A1501      82.553  -4.867  39.505  1.00130.67           N  
ANISOU 6175  N6  8ES A1501    13546  23769  12334   2711   -322   1331       N  
HETATM 6176  C29 8ES A1501      82.843  -4.417  40.863  1.00132.92           C  
ANISOU 6176  C29 8ES A1501    13816  24313  12376   2819   -403   1230       C  
HETATM 6177  C30 8ES A1501      82.316  -5.453  41.854  1.00134.13           C  
ANISOU 6177  C30 8ES A1501    14184  24416  12364   3138   -281   1418       C  
HETATM 6178  C35 8ES A1501      82.985  -6.827  41.930  1.00135.70           C  
ANISOU 6178  C35 8ES A1501    14424  24742  12393   3472   -257   1577       C  
HETATM 6179  C34 8ES A1501      82.536  -7.733  42.779  1.00136.92           C  
ANISOU 6179  C34 8ES A1501    14788  24834  12400   3753   -132   1746       C  
HETATM 6180  C33 8ES A1501      81.331  -7.418  43.673  1.00136.53           C  
ANISOU 6180  C33 8ES A1501    14921  24588  12365   3740     -3   1793       C  
HETATM 6181  C32 8ES A1501      80.752  -6.234  43.603  1.00135.16           C  
ANISOU 6181  C32 8ES A1501    14700  24316  12338   3460    -26   1660       C  
HETATM 6182  C31 8ES A1501      81.273  -5.181  42.616  1.00133.92           C  
ANISOU 6182  C31 8ES A1501    14321  24223  12341   3137   -177   1457       C  
HETATM 6183  C1  8ES A1501      78.480  -4.987  38.230  1.00122.68           C  
ANISOU 6183  C1  8ES A1501    12974  21622  12016   2333     89   1632       C  
HETATM 6184  C23 8ES A1501      80.529  -3.753  38.635  1.00125.13           C  
ANISOU 6184  C23 8ES A1501    12992  22498  12054   2287   -172   1317       C  
HETATM 6185  C   8ES A1501      79.222  -3.781  38.220  1.00123.50           C  
ANISOU 6185  C   8ES A1501    12920  21940  12065   2177    -44   1413       C  
HETATM 6186  O   8ES A1501      79.286  -1.339  37.719  1.00122.71           O  
ANISOU 6186  O   8ES A1501    12670  21857  12097   1718   -160   1070       O  
HETATM 6187  C2  8ES A1501      76.557  -3.870  37.350  1.00120.68           C  
ANISOU 6187  C2  8ES A1501    12783  20903  12167   1954    193   1607       C  
HETATM 6188  C3  8ES A1501      75.102  -4.009  36.881  1.00118.45           C  
ANISOU 6188  C3  8ES A1501    12596  20270  12142   1843    313   1721       C  
HETATM 6189  N   8ES A1501      77.147  -5.022  37.784  1.00121.64           N  
ANISOU 6189  N   8ES A1501    12947  21145  12126   2204    205   1726       N  
HETATM 6190  C19 8ES A1501      77.878  -1.998  34.434  1.00121.55           C  
ANISOU 6190  C19 8ES A1501    12630  20981  12572   1441    -25   1247       C  
HETATM 6191  C18 8ES A1501      78.425  -1.580  33.296  1.00121.49           C  
ANISOU 6191  C18 8ES A1501    12548  20948  12665   1303    -79   1157       C  
HETATM 6192  C9  8ES A1501      77.924   0.780  33.817  1.00121.02           C  
ANISOU 6192  C9  8ES A1501    12458  20918  12607    986    -97    878       C  
HETATM 6193  C11 8ES A1501      79.094   0.474  31.672  1.00122.46           C  
ANISOU 6193  C11 8ES A1501    12535  21039  12956    897   -148    858       C  
HETATM 6194  C16 8ES A1501      78.900   1.862  29.694  1.00121.64           C  
ANISOU 6194  C16 8ES A1501    12460  20643  13115    579   -121    701       C  
HETATM 6195  C14 8ES A1501      80.993   0.786  30.190  1.00123.20           C  
ANISOU 6195  C14 8ES A1501    12425  21313  13073    802   -217    746       C  
HETATM 6196  C12 8ES A1501      80.440   0.245  31.351  1.00123.83           C  
ANISOU 6196  C12 8ES A1501    12565  21436  13047    943   -212    827       C  
HETATM 6197  N5  8ES A1501      81.611  -0.478  33.592  1.00128.46           N  
ANISOU 6197  N5  8ES A1501    13009  22573  13226   1252   -315    846       N  
HETATM 6198  N4  8ES A1501      82.401  -1.492  34.034  1.00129.73           N  
ANISOU 6198  N4  8ES A1501    13113  22957  13223   1496   -351    939       N  
HETATM 6199  N2  8ES A1501      81.916  -1.787  31.823  1.00125.80           N  
ANISOU 6199  N2  8ES A1501    12717  22034  13048   1365   -264   1024       N  
HETATM 6200  N1  8ES B1201      67.348  11.891   4.696  1.00 61.37           N  
ANISOU 6200  N1  8ES B1201     6963   7012   9342   -169   -283    134       N  
HETATM 6201  N3  8ES B1201      62.793  15.036   8.809  1.00 69.16           N  
ANISOU 6201  N3  8ES B1201     7719   8211  10348     74     -6    184       N  
HETATM 6202  C4  8ES B1201      70.086   9.902   4.296  1.00 59.24           C  
ANISOU 6202  C4  8ES B1201     6812   6686   9011   -177   -316     97       C  
HETATM 6203  C5  8ES B1201      66.014  12.042   4.338  1.00 61.93           C  
ANISOU 6203  C5  8ES B1201     6985   7094   9451   -187   -287    183       C  
HETATM 6204  C6  8ES B1201      68.248  13.045   4.647  1.00 61.13           C  
ANISOU 6204  C6  8ES B1201     6940   6963   9326   -139   -274     71       C  
HETATM 6205  C7  8ES B1201      67.873  14.094   5.712  1.00 60.64           C  
ANISOU 6205  C7  8ES B1201     6841   6929   9269    -91   -238     32       C  
HETATM 6206  C8  8ES B1201      68.128  15.361   5.450  1.00 60.02           C  
ANISOU 6206  C8  8ES B1201     6750   6810   9243    -73   -225    -10       C  
HETATM 6207  C10 8ES B1201      67.200  16.135   7.629  1.00 62.64           C  
ANISOU 6207  C10 8ES B1201     7053   7221   9526     16   -164    -76       C  
HETATM 6208  C13 8ES B1201      64.413  16.542   8.696  1.00 68.47           C  
ANISOU 6208  C13 8ES B1201     7705   8050  10261    102    -47     18       C  
HETATM 6209  C15 8ES B1201      66.266  19.456  10.268  1.00 65.49           C  
ANISOU 6209  C15 8ES B1201     7403   7582   9897    211    -41   -326       C  
HETATM 6210  C17 8ES B1201      67.851  18.202   8.951  1.00 64.13           C  
ANISOU 6210  C17 8ES B1201     7248   7376   9745     93   -139   -272       C  
HETATM 6211  C20 8ES B1201      64.778   8.550   5.090  1.00 62.04           C  
ANISOU 6211  C20 8ES B1201     6983   7091   9497   -297   -284    321       C  
HETATM 6212  C21 8ES B1201      63.407   8.685   4.796  1.00 63.60           C  
ANISOU 6212  C21 8ES B1201     7098   7302   9764   -333   -295    365       C  
HETATM 6213  C22 8ES B1201      62.861   9.917   4.348  1.00 64.41           C  
ANISOU 6213  C22 8ES B1201     7154   7436   9883   -308   -309    352       C  
HETATM 6214  C24 8ES B1201      60.448  10.297   5.093  1.00 67.46           C  
ANISOU 6214  C24 8ES B1201     7348   7897  10388   -304   -247    467       C  
HETATM 6215  C26 8ES B1201      61.954  11.136   7.114  1.00 66.79           C  
ANISOU 6215  C26 8ES B1201     7370   7858  10150   -165   -121    400       C  
HETATM 6216  C28 8ES B1201      60.804  10.403   9.131  1.00 69.99           C  
ANISOU 6216  C28 8ES B1201     7707   8347  10540   -112     36    525       C  
HETATM 6217  O1  8ES B1201      59.297  10.401   4.811  1.00 70.63           O  
ANISOU 6217  O1  8ES B1201     7650   8321  10867   -325   -260    515       O  
HETATM 6218  C25 8ES B1201      60.816  10.436   6.575  1.00 68.34           C  
ANISOU 6218  C25 8ES B1201     7485   8043  10438   -235   -143    474       C  
HETATM 6219  S   8ES B1201      59.819   9.836   7.841  1.00 71.29           S  
ANISOU 6219  S   8ES B1201     7783   8461  10842   -221    -35    577       S  
HETATM 6220  C27 8ES B1201      61.950  11.109   8.633  1.00 67.89           C  
ANISOU 6220  C27 8ES B1201     7516   8055  10222    -96    -28    419       C  
HETATM 6221  N6  8ES B1201      61.441  10.060   4.041  1.00 64.45           N  
ANISOU 6221  N6  8ES B1201     7057   7466   9966   -335   -327    404       N  
HETATM 6222  C29 8ES B1201      61.020   9.960   2.652  1.00 64.07           C  
ANISOU 6222  C29 8ES B1201     6995   7402   9947   -383   -427    394       C  
HETATM 6223  C30 8ES B1201      61.236   8.533   2.155  1.00 63.37           C  
ANISOU 6223  C30 8ES B1201     6951   7257   9871   -464   -484    376       C  
HETATM 6224  C35 8ES B1201      60.347   7.416   2.716  1.00 64.34           C  
ANISOU 6224  C35 8ES B1201     7001   7355  10089   -536   -468    432       C  
HETATM 6225  C34 8ES B1201      60.525   6.176   2.299  1.00 64.40           C  
ANISOU 6225  C34 8ES B1201     7051   7291  10128   -609   -514    409       C  
HETATM 6226  C33 8ES B1201      61.624   5.867   1.272  1.00 61.91           C  
ANISOU 6226  C33 8ES B1201     6863   6929   9732   -608   -578    322       C  
HETATM 6227  C32 8ES B1201      62.389   6.838   0.792  1.00 59.35           C  
ANISOU 6227  C32 8ES B1201     6596   6638   9316   -540   -584    284       C  
HETATM 6228  C31 8ES B1201      62.197   8.274   1.277  1.00 59.65           C  
ANISOU 6228  C31 8ES B1201     6580   6747   9337   -468   -533    315       C  
HETATM 6229  C1  8ES B1201      65.613   9.647   4.944  1.00 61.46           C  
ANISOU 6229  C1  8ES B1201     6938   7031   9383   -249   -288    258       C  
HETATM 6230  C23 8ES B1201      63.736  11.001   4.205  1.00 64.18           C  
ANISOU 6230  C23 8ES B1201     7169   7408   9808   -253   -304    295       C  
HETATM 6231  C   8ES B1201      65.078  10.881   4.494  1.00 62.84           C  
ANISOU 6231  C   8ES B1201     7073   7221   9584   -231   -294    245       C  
HETATM 6232  O   8ES B1201      65.504  13.281   3.907  1.00 61.46           O  
ANISOU 6232  O   8ES B1201     6890   7032   9431   -162   -281    182       O  
HETATM 6233  C2  8ES B1201      67.808  10.598   5.135  1.00 61.18           C  
ANISOU 6233  C2  8ES B1201     6973   6990   9282   -181   -286    152       C  
HETATM 6234  C3  8ES B1201      69.280  10.364   5.511  1.00 60.32           C  
ANISOU 6234  C3  8ES B1201     6904   6879   9135   -152   -290    107       C  
HETATM 6235  N   8ES B1201      66.980   9.518   5.266  1.00 61.19           N  
ANISOU 6235  N   8ES B1201     6964   6989   9297   -216   -283    214       N  
HETATM 6236  C19 8ES B1201      67.232  13.718   7.068  1.00 61.50           C  
ANISOU 6236  C19 8ES B1201     6937   7106   9324    -55   -205     42       C  
HETATM 6237  C18 8ES B1201      66.928  14.657   7.960  1.00 61.78           C  
ANISOU 6237  C18 8ES B1201     6955   7169   9349     -1   -170     -7       C  
HETATM 6238  C9  8ES B1201      67.750  16.439   6.464  1.00 62.10           C  
ANISOU 6238  C9  8ES B1201     6989   7085   9520    -21   -187    -68       C  
HETATM 6239  C11 8ES B1201      66.855  17.286   8.598  1.00 64.30           C  
ANISOU 6239  C11 8ES B1201     7253   7441   9739     81   -122   -153       C  
HETATM 6240  C16 8ES B1201      67.560  19.278   9.785  1.00 65.53           C  
ANISOU 6240  C16 8ES B1201     7425   7544   9930    152   -105   -365       C  
HETATM 6241  C14 8ES B1201      65.257  18.575   9.901  1.00 65.00           C  
ANISOU 6241  C14 8ES B1201     7309   7569   9819    199    -16   -192       C  
HETATM 6242  C12 8ES B1201      65.543  17.507   9.052  1.00 66.36           C  
ANISOU 6242  C12 8ES B1201     7480   7740   9992    127    -63   -110       C  
HETATM 6243  N5  8ES B1201      63.964  16.198   7.395  1.00 69.87           N  
ANISOU 6243  N5  8ES B1201     7850   8194  10502     44    -83     99       N  
HETATM 6244  N4  8ES B1201      62.958  15.278   7.472  1.00 69.78           N  
ANISOU 6244  N4  8ES B1201     7793   8229  10493     23    -69    190       N  
HETATM 6245  N2  8ES B1201      63.690  15.814   9.564  1.00 68.08           N  
ANISOU 6245  N2  8ES B1201     7638   8074  10156    129      1     72       N  
CONECT 1370 1954                                                                
CONECT 1954 1370                                                                
CONECT 3876 5820                                                                
CONECT 4502 5073                                                                
CONECT 5073 4502                                                                
CONECT 5820 3876                                                                
CONECT 6154 6157 6158 6187                                                      
CONECT 6155 6198 6199                                                           
CONECT 6156 6188                                                                
CONECT 6157 6154 6185 6186                                                      
CONECT 6158 6154 6159                                                           
CONECT 6159 6158 6160 6190                                                      
CONECT 6160 6159 6192                                                           
CONECT 6161 6191 6192 6193                                                      
CONECT 6162 6196 6197 6199                                                      
CONECT 6163 6194 6195                                                           
CONECT 6164 6193 6194                                                           
CONECT 6165 6166 6183                                                           
CONECT 6166 6165 6167                                                           
CONECT 6167 6166 6175 6184                                                      
CONECT 6168 6171 6172 6175                                                      
CONECT 6169 6172 6174                                                           
CONECT 6170 6173 6174                                                           
CONECT 6171 6168                                                                
CONECT 6172 6168 6169 6173                                                      
CONECT 6173 6170 6172                                                           
CONECT 6174 6169 6170                                                           
CONECT 6175 6167 6168 6176                                                      
CONECT 6176 6175 6177                                                           
CONECT 6177 6176 6178 6182                                                      
CONECT 6178 6177 6179                                                           
CONECT 6179 6178 6180                                                           
CONECT 6180 6179 6181                                                           
CONECT 6181 6180 6182                                                           
CONECT 6182 6177 6181                                                           
CONECT 6183 6165 6185 6189                                                      
CONECT 6184 6167 6185                                                           
CONECT 6185 6157 6183 6184                                                      
CONECT 6186 6157                                                                
CONECT 6187 6154 6188 6189                                                      
CONECT 6188 6156 6187                                                           
CONECT 6189 6183 6187                                                           
CONECT 6190 6159 6191                                                           
CONECT 6191 6161 6190                                                           
CONECT 6192 6160 6161                                                           
CONECT 6193 6161 6164 6196                                                      
CONECT 6194 6163 6164                                                           
CONECT 6195 6163 6196                                                           
CONECT 6196 6162 6193 6195                                                      
CONECT 6197 6162 6198                                                           
CONECT 6198 6155 6197                                                           
CONECT 6199 6155 6162                                                           
CONECT 6200 6203 6204 6233                                                      
CONECT 6201 6244 6245                                                           
CONECT 6202 6234                                                                
CONECT 6203 6200 6231 6232                                                      
CONECT 6204 6200 6205                                                           
CONECT 6205 6204 6206 6236                                                      
CONECT 6206 6205 6238                                                           
CONECT 6207 6237 6238 6239                                                      
CONECT 6208 6242 6243 6245                                                      
CONECT 6209 6240 6241                                                           
CONECT 6210 6239 6240                                                           
CONECT 6211 6212 6229                                                           
CONECT 6212 6211 6213                                                           
CONECT 6213 6212 6221 6230                                                      
CONECT 6214 6217 6218 6221                                                      
CONECT 6215 6218 6220                                                           
CONECT 6216 6219 6220                                                           
CONECT 6217 6214                                                                
CONECT 6218 6214 6215 6219                                                      
CONECT 6219 6216 6218                                                           
CONECT 6220 6215 6216                                                           
CONECT 6221 6213 6214 6222                                                      
CONECT 6222 6221 6223                                                           
CONECT 6223 6222 6224 6228                                                      
CONECT 6224 6223 6225                                                           
CONECT 6225 6224 6226                                                           
CONECT 6226 6225 6227                                                           
CONECT 6227 6226 6228                                                           
CONECT 6228 6223 6227                                                           
CONECT 6229 6211 6231 6235                                                      
CONECT 6230 6213 6231                                                           
CONECT 6231 6203 6229 6230                                                      
CONECT 6232 6203                                                                
CONECT 6233 6200 6234 6235                                                      
CONECT 6234 6202 6233                                                           
CONECT 6235 6229 6233                                                           
CONECT 6236 6205 6237                                                           
CONECT 6237 6207 6236                                                           
CONECT 6238 6206 6207                                                           
CONECT 6239 6207 6210 6242                                                      
CONECT 6240 6209 6210                                                           
CONECT 6241 6209 6242                                                           
CONECT 6242 6208 6239 6241                                                      
CONECT 6243 6208 6244                                                           
CONECT 6244 6201 6243                                                           
CONECT 6245 6201 6208                                                           
MASTER      394    0    2   35    4    0    8    6 6243    2   98   64          
END