HEADER    MEMBRANE PROTEIN/INHIBITOR/IMMUNE SYSTEM18-JUL-22   7YIT              
TITLE     MOLECULAR MECHANISM OF BIASED SIGNALING AT THE KAPPA OPIOID RECEPTOR  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: KAPPA-TYPE OPIOID RECEPTOR;                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: K-OR-1,KOR-1;                                               
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: NANOBODY39;                                                
COMPND   9 CHAIN: D;                                                            
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: SOLUBLE CYTOCHROME B562;                                   
COMPND  13 CHAIN: E;                                                            
COMPND  14 SYNONYM: CYTOCHROME B-562;                                           
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: OPRK1, OPRK;                                                   
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: LAMA GLAMA;                                     
SOURCE  10 ORGANISM_TAXID: 9844;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  15 ORGANISM_TAXID: 562;                                                 
SOURCE  16 GENE: CYBC;                                                          
SOURCE  17 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    KAPPA OPIOID RECEPTOR, MEMBRANE PROTEIN, NALFURAFINE, OPIOIDS,        
KEYWDS   2 MEMBRANE PROTEIN-INHIBITOR-IMMUNE SYSTEM COMPLEX                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.KIM,T.CHE                                                           
REVDAT   1   12-APR-23 7YIT    0                                                
JRNL        AUTH   A.EL DAIBANI,J.M.PAGGI,K.KIM,Y.D.LALOUDAKIS,P.POPOV,         
JRNL        AUTH 2 S.M.BERNHARD,B.E.KRUMM,R.H.J.OLSEN,J.DIBERTO,F.I.CARROLL,    
JRNL        AUTH 3 V.KATRITCH,B.WUNSCH,R.O.DROR,T.CHE                           
JRNL        TITL   MOLECULAR MECHANISM OF BIASED SIGNALING AT THE KAPPA OPIOID  
JRNL        TITL 2 RECEPTOR.                                                    
JRNL        REF    NAT COMMUN                    V.  14  1338 2023              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   36906681                                                     
JRNL        DOI    10.1038/S41467-023-37041-7                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.19.2_4158                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.14                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 12420                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.290                           
REMARK   3   R VALUE            (WORKING SET) : 0.285                           
REMARK   3   FREE R VALUE                     : 0.335                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.020                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1244                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 37.1400 -  6.8500    0.98     1385   159  0.2452 0.2764        
REMARK   3     2  6.8500 -  5.4400    0.98     1303   145  0.3415 0.3832        
REMARK   3     3  5.4400 -  4.7600    0.98     1297   146  0.2676 0.3072        
REMARK   3     4  4.7600 -  4.3200    0.97     1270   145  0.2571 0.3471        
REMARK   3     5  4.3200 -  4.0100    0.97     1275   130  0.2777 0.3411        
REMARK   3     6  4.0100 -  3.7800    0.93     1219   143  0.3177 0.3939        
REMARK   3     7  3.7800 -  3.5900    0.91     1171   123  0.3516 0.4368        
REMARK   3     8  3.5900 -  3.4300    0.89     1153   132  0.3982 0.4491        
REMARK   3     9  3.4300 -  3.3000    0.86     1103   121  0.4287 0.4849        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.720            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 43.377           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 125.3                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 130.8                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           3456                                  
REMARK   3   ANGLE     :  0.820           4754                                  
REMARK   3   CHIRALITY :  0.045            601                                  
REMARK   3   PLANARITY :  0.005            582                                  
REMARK   3   DIHEDRAL  :  7.609            498                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  17.0018  16.9771   5.5068              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2127 T22:   1.0167                                     
REMARK   3      T33:   1.0228 T12:  -0.0213                                     
REMARK   3      T13:   0.0479 T23:   0.0396                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4681 L22:   0.7973                                     
REMARK   3      L33:   0.3541 L12:   0.0729                                     
REMARK   3      L13:  -0.0686 L23:   0.3144                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0554 S12:  -0.0086 S13:  -0.0352                       
REMARK   3      S21:   0.0202 S22:  -0.0051 S23:  -0.0538                       
REMARK   3      S31:   0.0824 S32:  -0.1890 S33:   0.0813                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 7YIT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-JUL-22.                  
REMARK 100 THE DEPOSITION ID IS D_1300030960.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-AUG-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 83                                 
REMARK 200  PH                             : 6.5-7.0                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0330                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40881                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.380                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.56                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: 6B73                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.75                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 40-200 MM MAGNESIUM SULFATE HYDRATE,     
REMARK 280  100 MM SODIUM CITRATE TRIBASIC DEHYDRATE, 10 MM MANGANESE (II)      
REMARK 280  CHLORIDE TETRAHYDRATE 28-30% PEG400, PH 6.7, LIPIDIC CUBIC PHASE,   
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   X,-Y,-Z                                                 
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-Y+1/2,Z+1/2                                         
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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.26500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       77.23000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.26500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       77.23000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, E                               
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     ILE A    54                                                      
REMARK 465     MET A    90                                                      
REMARK 465     ASP A   204                                                      
REMARK 465     VAL A   205                                                      
REMARK 465     LEU A   258                                                      
REMARK 465     LEU A   259                                                      
REMARK 465     SER A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     THR A   302                                                      
REMARK 465     SER A   303                                                      
REMARK 465     HIS A   304                                                      
REMARK 465     LEU A   348                                                      
REMARK 465     LYS A   349                                                      
REMARK 465     MET A   350                                                      
REMARK 465     ARG A   351                                                      
REMARK 465     MET A   352                                                      
REMARK 465     GLU A   353                                                      
REMARK 465     ARG A   354                                                      
REMARK 465     GLN A   355                                                      
REMARK 465     SER A   356                                                      
REMARK 465     THR A   357                                                      
REMARK 465     SER A   358                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     GLN D     3                                                      
REMARK 465     ARG D    39                                                      
REMARK 465     ALA D    40                                                      
REMARK 465     PRO D    41                                                      
REMARK 465     GLY D    42                                                      
REMARK 465     GLY D   103                                                      
REMARK 465     GLN D   104                                                      
REMARK 465     SER D   105                                                      
REMARK 465     SER D   106                                                      
REMARK 465     SER D   107                                                      
REMARK 465     PRO D   108                                                      
REMARK 465     TYR D   109                                                      
REMARK 465     MET E  1000                                                      
REMARK 465     ALA E  1001                                                      
REMARK 465     ALA E  1020                                                      
REMARK 465     ASP E  1021                                                      
REMARK 465     ASN E  1022                                                      
REMARK 465     ALA E  1023                                                      
REMARK 465     ALA E  1024                                                      
REMARK 465     GLN E  1041                                                      
REMARK 465     LYS E  1042                                                      
REMARK 465     ALA E  1043                                                      
REMARK 465     THR E  1044                                                      
REMARK 465     PRO E  1045                                                      
REMARK 465     PRO E  1046                                                      
REMARK 465     LYS E  1047                                                      
REMARK 465     LEU E  1048                                                      
REMARK 465     GLU E  1049                                                      
REMARK 465     ASP E  1050                                                      
REMARK 465     LYS E  1051                                                      
REMARK 465     SER E  1052                                                      
REMARK 465     PRO E  1053                                                      
REMARK 465     ASP E  1054                                                      
REMARK 465     SER E  1055                                                      
REMARK 465     PRO E  1056                                                      
REMARK 465     GLU E  1057                                                      
REMARK 465     GLY E  1082                                                      
REMARK 465     LYS E  1083                                                      
REMARK 465     GLU E  1084                                                      
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     SER A  55    OG                                                  
REMARK 470     SER A  67    OG                                                  
REMARK 470     ARG A  86    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR A  87    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A  89    CG   CD   CE   NZ                                   
REMARK 470     LYS A  91    CG   CD   CE   NZ                                   
REMARK 470     LYS A 132    CG   CD   CE   NZ                                   
REMARK 470     LEU A 173    CG   CD1  CD2                                       
REMARK 470     LYS A 174    CG   CD   CE   NZ                                   
REMARK 470     LYS A 176    CG   CD   CE   NZ                                   
REMARK 470     LEU A 185    CG   CD1  CD2                                       
REMARK 470     LYS A 200    CG   CD   CE   NZ                                   
REMARK 470     ARG A 202    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 203    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 216    CG   OD1  OD2                                       
REMARK 470     LYS A 254    CG   CD   CE   NZ                                   
REMARK 470     ARG A 257    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 262    OG                                                  
REMARK 470     ARG A 263    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 265    CG   CD   CE   NZ                                   
REMARK 470     ARG A 267    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 269    CG   CD1  CD2                                       
REMARK 470     ARG A 270    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 271    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 297    CG   CD   OE1  OE2                                  
REMARK 470     THR A 306    OG1  CG2                                            
REMARK 470     ASN A 336    CG   OD1  ND2                                       
REMARK 470     LYS A 338    CG   CD   CE   NZ                                   
REMARK 470     ARG A 339    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 342    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL D   4    CG1  CG2                                            
REMARK 470     GLN D   5    CG   CD   OE1  NE2                                  
REMARK 470     VAL D   7    CG1  CG2                                            
REMARK 470     GLU D   8    CG   CD   OE1  OE2                                  
REMARK 470     LEU D  13    CG   CD1  CD2                                       
REMARK 470     ARG D  15    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D  21    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D  28    CG   CD   OE1  OE2                                  
REMARK 470     ARG D  29    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D  38    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D  43    CG   CD   CE   NZ                                   
REMARK 470     GLU D  44    CG   CD   OE1  OE2                                  
REMARK 470     PHE D  47    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     TYR D  60    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP D  62    CG   OD1  OD2                                       
REMARK 470     ARG D  67    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU D  81    CG   CD1  CD2                                       
REMARK 470     LEU D  86    CG   CD1  CD2                                       
REMARK 470     LYS D  87    CG   CD   CE   NZ                                   
REMARK 470     HIS D  88    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU D  89    CG   CD   OE1  OE2                                  
REMARK 470     ASP D  90    CG   OD1  OD2                                       
REMARK 470     VAL D  93    CG1  CG2                                            
REMARK 470     TYR D  95    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG D  99    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN D 116    CG   CD   OE1  NE2                                  
REMARK 470     GLN D 119    CG   CD   OE1  NE2                                  
REMARK 470     ASP E1002    CG   OD1  OD2                                       
REMARK 470     LEU E1003    CG   CD1  CD2                                       
REMARK 470     ASP E1005    CG   OD1  OD2                                       
REMARK 470     ASN E1006    CG   OD1  ND2                                       
REMARK 470     GLU E1008    CG   CD   OE1  OE2                                  
REMARK 470     ASP E1012    CG   OD1  OD2                                       
REMARK 470     ASN E1013    CG   OD1  ND2                                       
REMARK 470     LEU E1014    CG   CD1  CD2                                       
REMARK 470     LYS E1015    CG   CD   CE   NZ                                   
REMARK 470     ILE E1017    CG1  CG2  CD1                                       
REMARK 470     GLU E1018    CG   CD   OE1  OE2                                  
REMARK 470     LYS E1019    CG   CD   CE   NZ                                   
REMARK 470     GLN E1025    CG   CD   OE1  NE2                                  
REMARK 470     VAL E1026    CG1  CG2                                            
REMARK 470     LYS E1027    CG   CD   CE   NZ                                   
REMARK 470     ASP E1028    CG   OD1  OD2                                       
REMARK 470     LYS E1032    CG   CD   CE   NZ                                   
REMARK 470     ARG E1034    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU E1038    CG   CD1  CD2                                       
REMARK 470     ASP E1039    OD1  OD2                                            
REMARK 470     MET E1058    CG   SD   CE                                        
REMARK 470     LYS E1059    CG   CD   CE   NZ                                   
REMARK 470     ASP E1060    CG   OD1  OD2                                       
REMARK 470     PHE E1061    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG E1062    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS E1063    CG   ND1  CD2  CE1  NE2                             
REMARK 470     PHE E1065    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP E1066    CG   OD1  OD2                                       
REMARK 470     LEU E1068    CG   CD1  CD2                                       
REMARK 470     ILE E1072    CG1  CG2  CD1                                       
REMARK 470     LYS E1077    CG   CD   CE   NZ                                   
REMARK 470     LEU E1078    CG   CD1  CD2                                       
REMARK 470     ASN E1080    CG   OD1  ND2                                       
REMARK 470     GLU E1081    CG   CD   OE1  OE2                                  
REMARK 470     LYS E1085    CG   CD   CE   NZ                                   
REMARK 470     GLU E1086    CG   CD   OE1  OE2                                  
REMARK 470     GLN E1088    CG   CD   OE1  NE2                                  
REMARK 470     GLU E1092    CG   CD   OE1  OE2                                  
REMARK 470     GLN E1093    CG   CD   OE1  NE2                                  
REMARK 470     ARG E1098    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE E1102    CG1  CG2  CD1                                       
REMARK 470     GLN E1103    CG   CD   OE1  NE2                                  
REMARK 470     LYS E1104    CG   CD   CE   NZ                                   
REMARK 470     TYR E1105    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU E1106    CG   CD1  CD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH2  ARG A   170     O    ILE D    56              2.10            
REMARK 500   OG1  THR D    52     OD1  ASP D    57              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A  56       44.44    -79.84                                   
REMARK 500    HIS A 162       64.36   -119.77                                   
REMARK 500    SER A 211     -168.64   -161.36                                   
REMARK 500    TYR A 219       29.85     48.94                                   
REMARK 500    ALA D  49      156.38    -49.10                                   
REMARK 500    LYS D  87     -169.44   -126.51                                   
REMARK 500    LEU E1003     -138.81     46.98                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  7YIT A   54   358  UNP    P41145   OPRK_HUMAN      54    358             
DBREF  7YIT D    1   123  PDB    7YIT     7YIT             1    123             
DBREF  7YIT E 1001  1106  UNP    P0ABE7   C562_ECOLX      23    128             
SEQADV 7YIT LEU A  135  UNP  P41145    ILE   135 ENGINEERED MUTATION            
SEQADV 7YIT CYS A  324  UNP  P41145    SER   324 ENGINEERED MUTATION            
SEQADV 7YIT MET E 1000  UNP  P0ABE7              INITIATING METHIONINE          
SEQADV 7YIT TRP E 1007  UNP  P0ABE7    MET    29 ENGINEERED MUTATION            
SEQADV 7YIT GLU E 1084  UNP  P0ABE7    VAL   106 ENGINEERED MUTATION            
SEQADV 7YIT ILE E 1102  UNP  P0ABE7    HIS   124 ENGINEERED MUTATION            
SEQADV 7YIT LEU E 1106  UNP  P0ABE7    ARG   128 VARIANT                        
SEQADV 7YIT GLY E 1107  UNP  P0ABE7              LINKER                         
SEQADV 7YIT SER E 1108  UNP  P0ABE7              LINKER                         
SEQRES   1 A  305  ILE SER PRO ALA ILE PRO VAL ILE ILE THR ALA VAL TYR          
SEQRES   2 A  305  SER VAL VAL PHE VAL VAL GLY LEU VAL GLY ASN SER LEU          
SEQRES   3 A  305  VAL MET PHE VAL ILE ILE ARG TYR THR LYS MET LYS THR          
SEQRES   4 A  305  ALA THR ASN ILE TYR ILE PHE ASN LEU ALA LEU ALA ASP          
SEQRES   5 A  305  ALA LEU VAL THR THR THR MET PRO PHE GLN SER THR VAL          
SEQRES   6 A  305  TYR LEU MET ASN SER TRP PRO PHE GLY ASP VAL LEU CYS          
SEQRES   7 A  305  LYS ILE VAL LEU SER ILE ASP TYR TYR ASN MET PHE THR          
SEQRES   8 A  305  SER ILE PHE THR LEU THR MET MET SER VAL ASP ARG TYR          
SEQRES   9 A  305  ILE ALA VAL CYS HIS PRO VAL LYS ALA LEU ASP PHE ARG          
SEQRES  10 A  305  THR PRO LEU LYS ALA LYS ILE ILE ASN ILE CYS ILE TRP          
SEQRES  11 A  305  LEU LEU SER SER SER VAL GLY ILE SER ALA ILE VAL LEU          
SEQRES  12 A  305  GLY GLY THR LYS VAL ARG GLU ASP VAL ASP VAL ILE GLU          
SEQRES  13 A  305  CYS SER LEU GLN PHE PRO ASP ASP ASP TYR SER TRP TRP          
SEQRES  14 A  305  ASP LEU PHE MET LYS ILE CYS VAL PHE ILE PHE ALA PHE          
SEQRES  15 A  305  VAL ILE PRO VAL LEU ILE ILE ILE VAL CYS TYR THR LEU          
SEQRES  16 A  305  MET ILE LEU ARG LEU LYS SER VAL ARG LEU LEU SER GLY          
SEQRES  17 A  305  SER ARG GLU LYS ASP ARG ASN LEU ARG ARG ILE THR ARG          
SEQRES  18 A  305  LEU VAL LEU VAL VAL VAL ALA VAL PHE VAL VAL CYS TRP          
SEQRES  19 A  305  THR PRO ILE HIS ILE PHE ILE LEU VAL GLU ALA LEU GLY          
SEQRES  20 A  305  SER THR SER HIS SER THR ALA ALA LEU SER SER TYR TYR          
SEQRES  21 A  305  PHE CYS ILE ALA LEU GLY TYR THR ASN SER CYS LEU ASN          
SEQRES  22 A  305  PRO ILE LEU TYR ALA PHE LEU ASP GLU ASN PHE LYS ARG          
SEQRES  23 A  305  CYS PHE ARG ASP PHE CYS PHE PRO LEU LYS MET ARG MET          
SEQRES  24 A  305  GLU ARG GLN SER THR SER                                      
SEQRES   1 D  123  MET ALA GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU          
SEQRES   2 D  123  VAL ARG PRO GLY GLY SER LEU ARG LEU SER CYS VAL ASP          
SEQRES   3 D  123  SER GLU ARG THR SER TYR PRO MET GLY TRP PHE ARG ARG          
SEQRES   4 D  123  ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA SER ILE THR          
SEQRES   5 D  123  TRP SER GLY ILE ASP PRO THR TYR ALA ASP SER VAL ALA          
SEQRES   6 D  123  ASP ARG PHE THR THR SER ARG ASP VAL ALA ASN ASN THR          
SEQRES   7 D  123  LEU TYR LEU GLN MET ASN SER LEU LYS HIS GLU ASP THR          
SEQRES   8 D  123  ALA VAL TYR TYR CYS ALA ALA ARG ALA PRO VAL GLY GLN          
SEQRES   9 D  123  SER SER SER PRO TYR ASP TYR ASP TYR TRP GLY GLN GLY          
SEQRES  10 D  123  THR GLN VAL THR VAL SER                                      
SEQRES   1 E  109  MET ALA ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP          
SEQRES   2 E  109  ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN          
SEQRES   3 E  109  VAL LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU          
SEQRES   4 E  109  ASP ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS          
SEQRES   5 E  109  SER PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY          
SEQRES   6 E  109  PHE ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS          
SEQRES   7 E  109  LEU ALA ASN GLU GLY LYS GLU LYS GLU ALA GLN ALA ALA          
SEQRES   8 E  109  ALA GLU GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN          
SEQRES   9 E  109  LYS TYR LEU GLY SER                                          
HET    IVB  A 401      35                                                       
HETNAM     IVB ~{N}-[(4~{R},4~{A}~{S},7~{R},7~{A}~{R},12~{B}~{S})-3-            
HETNAM   2 IVB  (CYCLOPROPYLMETHYL)-4~{A},9-BIS(OXIDANYL)-1,2,4,5,6,7,          
HETNAM   3 IVB  7~{A},13-OCTAHYDRO-4,12-METHANOBENZOFURO[3,2-                   
HETNAM   4 IVB  E]ISOQUINOLIN-7-YL]-3-(FURAN-3-YL)-~{N}-METHYL-                 
HETNAM   5 IVB  PROPANAMIDE                                                     
HETSYN     IVB NALFURANFINE                                                     
FORMUL   4  IVB    C28 H32 N2 O5                                                
HELIX    1 AA1 PRO A   56  TYR A   87  1                                  32    
HELIX    2 AA2 THR A   92  VAL A  108  1                                  17    
HELIX    3 AA3 THR A  111  ASN A  122  1                                  12    
HELIX    4 AA4 ASP A  128  HIS A  162  1                                  35    
HELIX    5 AA5 LYS A  165  ARG A  170  1                                   6    
HELIX    6 AA6 THR A  171  LEU A  196  1                                  26    
HELIX    7 AA7 TRP A  221  PHE A  235  1                                  15    
HELIX    8 AA8 PHE A  235  VAL A  256  1                                  22    
HELIX    9 AA9 ARG A  263  GLY A  300  1                                  38    
HELIX   10 AB1 THR A  306  ALA A  331  1                                  26    
HELIX   11 AB2 ASP A  334  PHE A  346  1                                  13    
HELIX   12 AB3 LYS D   87  THR D   91  5                                   5    
HELIX   13 AB4 LEU E 1003  LYS E 1019  1                                  17    
HELIX   14 AB5 VAL E 1026  LEU E 1038  1                                  13    
HELIX   15 AB6 LYS E 1059  GLU E 1081  1                                  23    
HELIX   16 AB7 ALA E 1087  LEU E 1106  1                                  20    
SHEET    1 AA1 2 GLY A 197  VAL A 201  0                                        
SHEET    2 AA1 2 ILE A 208  LEU A 212 -1  O  SER A 211   N  GLY A 198           
SHEET    1 AA2 4 VAL D   7  GLU D   8  0                                        
SHEET    2 AA2 4 SER D  19  VAL D  25 -1  O  VAL D  25   N  VAL D   7           
SHEET    3 AA2 4 THR D  78  ASN D  84 -1  O  LEU D  81   N  LEU D  22           
SHEET    4 AA2 4 PHE D  68  ASP D  73 -1  N  SER D  71   O  TYR D  80           
SHEET    1 AA3 3 GLY D  35  PHE D  37  0                                        
SHEET    2 AA3 3 ALA D  92  ALA D  97 -1  O  ALA D  97   N  GLY D  35           
SHEET    3 AA3 3 THR D 118  VAL D 120 -1  O  THR D 118   N  TYR D  94           
SHEET    1 AA4 2 SER D  50  ILE D  51  0                                        
SHEET    2 AA4 2 PRO D  58  THR D  59 -1  O  THR D  59   N  SER D  50           
SSBOND   1 CYS A  131    CYS A  210                          1555   1555  2.03  
SSBOND   2 CYS D   24    CYS D   96                          1555   1555  2.03  
CRYST1   70.750   76.530  154.460  90.00  90.00  90.00 P 2 21 21     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      0.014134  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013067  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006474        0.00000                         
ATOM      1  N   SER A  55      31.051  -2.818 -16.912  1.00174.09           N  
ANISOU    1  N   SER A  55    23647  20286  22211  -1066   1720   -385       N  
ATOM      2  CA  SER A  55      30.987  -2.541 -15.483  1.00170.26           C  
ANISOU    2  CA  SER A  55    23132  19794  21765  -1010   1644   -323       C  
ATOM      3  C   SER A  55      29.864  -1.562 -15.163  1.00166.72           C  
ANISOU    3  C   SER A  55    22699  19443  21204   -993   1577   -270       C  
ATOM      4  O   SER A  55      30.121  -0.385 -14.905  1.00163.53           O  
ANISOU    4  O   SER A  55    22291  19058  20786   -953   1550   -235       O  
ATOM      5  CB  SER A  55      32.322  -1.987 -14.979  1.00169.50           C  
ANISOU    5  CB  SER A  55    23004  19628  21772   -959   1647   -314       C  
ATOM      6  N   PRO A  56      28.614  -2.040 -15.174  1.00160.50           N  
ANISOU    6  N   PRO A  56    21925  18715  20341  -1023   1552   -266       N  
ATOM      7  CA  PRO A  56      27.503  -1.172 -14.772  1.00155.43           C  
ANISOU    7  CA  PRO A  56    21289  18163  19603  -1005   1485   -219       C  
ATOM      8  C   PRO A  56      27.395  -1.080 -13.259  1.00150.03           C  
ANISOU    8  C   PRO A  56    20577  17467  18960   -957   1421   -164       C  
ATOM      9  O   PRO A  56      26.298  -1.172 -12.699  1.00147.43           O  
ANISOU    9  O   PRO A  56    20246  17192  18577   -960   1376   -138       O  
ATOM     10  CB  PRO A  56      26.293  -1.877 -15.391  1.00154.92           C  
ANISOU   10  CB  PRO A  56    21244  18158  19460  -1061   1490   -249       C  
ATOM     11  CG  PRO A  56      26.649  -3.314 -15.195  1.00159.35           C  
ANISOU   11  CG  PRO A  56    21794  18646  20107  -1088   1527   -282       C  
ATOM     12  CD  PRO A  56      28.123  -3.371 -15.577  1.00162.61           C  
ANISOU   12  CD  PRO A  56    22202  18973  20611  -1078   1584   -310       C  
ATOM     13  N   ALA A  57      28.540  -0.906 -12.592  1.00103.48           N  
ANISOU   13  N   ALA A  57    14660  11500  13160   -913   1418   -148       N  
ATOM     14  CA  ALA A  57      28.542  -0.741 -11.144  1.00 98.50           C  
ANISOU   14  CA  ALA A  57    14007  10855  12564   -864   1355    -96       C  
ATOM     15  C   ALA A  57      27.974   0.613 -10.752  1.00 99.87           C  
ANISOU   15  C   ALA A  57    14180  11102  12664   -829   1301    -50       C  
ATOM     16  O   ALA A  57      27.181   0.709  -9.809  1.00 96.12           O  
ANISOU   16  O   ALA A  57    13700  10666  12156   -812   1247    -12       O  
ATOM     17  CB  ALA A  57      29.959  -0.904 -10.595  1.00 95.79           C  
ANISOU   17  CB  ALA A  57    13638  10415  12344   -825   1362    -97       C  
ATOM     18  N   ILE A  58      28.355   1.664 -11.488  1.00140.36           N  
ANISOU   18  N   ILE A  58    19316  16249  17765   -819   1317    -56       N  
ATOM     19  CA  ILE A  58      27.901   3.015 -11.156  1.00135.29           C  
ANISOU   19  CA  ILE A  58    18674  15670  17062   -783   1267    -14       C  
ATOM     20  C   ILE A  58      26.380   3.120 -11.113  1.00133.66           C  
ANISOU   20  C   ILE A  58    18478  15554  16751   -799   1228      2       C  
ATOM     21  O   ILE A  58      25.851   3.662 -10.131  1.00132.39           O  
ANISOU   21  O   ILE A  58    18303  15429  16569   -765   1171     43       O  
ATOM     22  CB  ILE A  58      28.539   4.037 -12.116  1.00137.60           C  
ANISOU   22  CB  ILE A  58    18981  15962  17339   -778   1302    -27       C  
ATOM     23  CG1 ILE A  58      30.025   4.221 -11.799  1.00139.87           C  
ANISOU   23  CG1 ILE A  58    19243  16163  17737   -747   1325    -34       C  
ATOM     24  CG2 ILE A  58      27.797   5.364 -12.055  1.00137.64           C  
ANISOU   24  CG2 ILE A  58    18996  16044  17259   -752   1255     11       C  
ATOM     25  CD1 ILE A  58      30.365   4.129 -10.331  1.00132.32           C  
ANISOU   25  CD1 ILE A  58    18253  15170  16852   -699   1270     -1       C  
ATOM     26  N   PRO A  59      25.626   2.634 -12.109  1.00100.53           N  
ANISOU   26  N   PRO A  59    14304  11402  12492   -850   1254    -31       N  
ATOM     27  CA  PRO A  59      24.168   2.570 -11.921  1.00100.51           C  
ANISOU   27  CA  PRO A  59    14301  11480  12407   -866   1213    -21       C  
ATOM     28  C   PRO A  59      23.763   1.737 -10.717  1.00101.86           C  
ANISOU   28  C   PRO A  59    14451  11635  12614   -865   1187     -2       C  
ATOM     29  O   PRO A  59      22.752   2.047 -10.075  1.00101.38           O  
ANISOU   29  O   PRO A  59    14381  11635  12504   -855   1141     23       O  
ATOM     30  CB  PRO A  59      23.685   1.947 -13.239  1.00100.67           C  
ANISOU   30  CB  PRO A  59    14347  11529  12375   -925   1254    -71       C  
ATOM     31  CG  PRO A  59      24.690   2.443 -14.226  1.00104.94           C  
ANISOU   31  CG  PRO A  59    14911  12037  12925   -926   1301    -91       C  
ATOM     32  CD  PRO A  59      25.980   2.215 -13.479  1.00102.90           C  
ANISOU   32  CD  PRO A  59    14630  11686  12781   -896   1319    -82       C  
ATOM     33  N   VAL A  60      24.527   0.691 -10.391  1.00150.26           N  
ANISOU   33  N   VAL A  60    20577  17684  18829   -874   1218    -15       N  
ATOM     34  CA  VAL A  60      24.184  -0.170  -9.260  1.00150.76           C  
ANISOU   34  CA  VAL A  60    20631  17724  18925   -875   1197      5       C  
ATOM     35  C   VAL A  60      24.432   0.545  -7.935  1.00148.31           C  
ANISOU   35  C   VAL A  60    20307  17407  18637   -816   1143     59       C  
ATOM     36  O   VAL A  60      23.572   0.542  -7.046  1.00146.77           O  
ANISOU   36  O   VAL A  60    20108  17251  18408   -811   1106     88       O  
ATOM     37  CB  VAL A  60      24.954  -1.502  -9.336  1.00150.74           C  
ANISOU   37  CB  VAL A  60    20633  17632  19010   -899   1243    -24       C  
ATOM     38  CG1 VAL A  60      24.917  -2.214  -7.993  1.00149.58           C  
ANISOU   38  CG1 VAL A  60    20481  17441  18910   -883   1215     11       C  
ATOM     39  CG2 VAL A  60      24.358  -2.389 -10.413  1.00148.39           C  
ANISOU   39  CG2 VAL A  60    20349  17353  18681   -965   1289    -76       C  
ATOM     40  N   ILE A  61      25.611   1.158  -7.771  1.00110.11           N  
ANISOU   40  N   ILE A  61    15461  12519  13857   -773   1140     69       N  
ATOM     41  CA  ILE A  61      25.894   1.856  -6.517  1.00109.20           C  
ANISOU   41  CA  ILE A  61    15332  12397  13763   -716   1086    116       C  
ATOM     42  C   ILE A  61      24.849   2.926  -6.248  1.00105.73           C  
ANISOU   42  C   ILE A  61    14890  12048  13236   -701   1043    143       C  
ATOM     43  O   ILE A  61      24.337   3.042  -5.129  1.00101.21           O  
ANISOU   43  O   ILE A  61    14311  11496  12647   -681   1000    177       O  
ATOM     44  CB  ILE A  61      27.315   2.458  -6.502  1.00109.08           C  
ANISOU   44  CB  ILE A  61    15303  12319  13824   -674   1090    116       C  
ATOM     45  CG1 ILE A  61      28.320   1.563  -7.228  1.00110.23           C  
ANISOU   45  CG1 ILE A  61    15448  12385  14050   -697   1147     72       C  
ATOM     46  CG2 ILE A  61      27.754   2.762  -5.067  1.00102.78           C  
ANISOU   46  CG2 ILE A  61    14492  11491  13069   -620   1034    157       C  
ATOM     47  CD1 ILE A  61      29.700   2.164  -7.338  1.00105.10           C  
ANISOU   47  CD1 ILE A  61    14779  11675  13479   -661   1159     62       C  
ATOM     48  N   ILE A  62      24.507   3.717  -7.266  1.00108.59           N  
ANISOU   48  N   ILE A  62    15257  12464  13540   -710   1053    128       N  
ATOM     49  CA  ILE A  62      23.649   4.874  -7.030  1.00110.16           C  
ANISOU   49  CA  ILE A  62    15449  12741  13666   -686   1008    153       C  
ATOM     50  C   ILE A  62      22.237   4.427  -6.675  1.00108.95           C  
ANISOU   50  C   ILE A  62    15292  12652  13453   -713    988    155       C  
ATOM     51  O   ILE A  62      21.638   4.935  -5.719  1.00108.55           O  
ANISOU   51  O   ILE A  62    15228  12639  13376   -688    945    185       O  
ATOM     52  CB  ILE A  62      23.650   5.826  -8.242  1.00105.98           C  
ANISOU   52  CB  ILE A  62    14932  12248  13088   -687   1022    139       C  
ATOM     53  CG1 ILE A  62      24.878   6.752  -8.252  1.00103.99           C  
ANISOU   53  CG1 ILE A  62    14677  11948  12886   -646   1027    150       C  
ATOM     54  CG2 ILE A  62      22.401   6.689  -8.227  1.00 99.32           C  
ANISOU   54  CG2 ILE A  62    14084  11495  12157   -677    978    155       C  
ATOM     55  CD1 ILE A  62      26.219   6.101  -7.952  1.00103.38           C  
ANISOU   55  CD1 ILE A  62    14591  11775  12912   -638   1056    139       C  
ATOM     56  N   THR A  63      21.679   3.469  -7.426  1.00112.59           N  
ANISOU   56  N   THR A  63    15762  13126  13892   -768   1021    120       N  
ATOM     57  CA  THR A  63      20.325   3.026  -7.114  1.00112.95           C  
ANISOU   57  CA  THR A  63    15799  13231  13886   -798   1006    116       C  
ATOM     58  C   THR A  63      20.287   2.375  -5.739  1.00114.65           C  
ANISOU   58  C   THR A  63    16010  13413  14140   -792    993    144       C  
ATOM     59  O   THR A  63      19.247   2.396  -5.069  1.00112.92           O  
ANISOU   59  O   THR A  63    15779  13244  13880   -799    971    156       O  
ATOM     60  CB  THR A  63      19.803   2.065  -8.188  1.00114.71           C  
ANISOU   60  CB  THR A  63    16031  13469  14085   -860   1045     68       C  
ATOM     61  OG1 THR A  63      18.455   1.682  -7.878  1.00116.07           O  
ANISOU   61  OG1 THR A  63    16189  13702  14212   -891   1030     60       O  
ATOM     62  CG2 THR A  63      20.666   0.803  -8.244  1.00114.91           C  
ANISOU   62  CG2 THR A  63    16069  13406  14185   -887   1092     49       C  
ATOM     63  N   ALA A  64      21.416   1.802  -5.304  1.00140.71           N  
ANISOU   63  N   ALA A  64    19320  16626  17516   -778   1008    154       N  
ATOM     64  CA  ALA A  64      21.536   1.338  -3.926  1.00139.27           C  
ANISOU   64  CA  ALA A  64    19142  16405  17369   -761    988    189       C  
ATOM     65  C   ALA A  64      21.371   2.494  -2.951  1.00139.51           C  
ANISOU   65  C   ALA A  64    19162  16473  17374   -710    936    228       C  
ATOM     66  O   ALA A  64      20.554   2.426  -2.029  1.00137.37           O  
ANISOU   66  O   ALA A  64    18890  16235  17070   -713    916    249       O  
ATOM     67  CB  ALA A  64      22.882   0.644  -3.713  1.00135.85           C  
ANISOU   67  CB  ALA A  64    18720  15870  17028   -746   1004    192       C  
ATOM     68  N   VAL A  65      22.126   3.580  -3.156  1.00111.16           N  
ANISOU   68  N   VAL A  65    15563  12878  13796   -666    919    236       N  
ATOM     69  CA  VAL A  65      22.004   4.751  -2.288  1.00107.60           C  
ANISOU   69  CA  VAL A  65    15100  12461  13322   -617    871    268       C  
ATOM     70  C   VAL A  65      20.564   5.237  -2.258  1.00105.87           C  
ANISOU   70  C   VAL A  65    14868  12334  13022   -631    853    267       C  
ATOM     71  O   VAL A  65      20.006   5.517  -1.192  1.00105.19           O  
ANISOU   71  O   VAL A  65    14777  12278  12913   -614    824    291       O  
ATOM     72  CB  VAL A  65      22.961   5.867  -2.742  1.00108.44           C  
ANISOU   72  CB  VAL A  65    15198  12550  13454   -576    863    269       C  
ATOM     73  CG1 VAL A  65      23.084   6.920  -1.658  1.00108.00           C  
ANISOU   73  CG1 VAL A  65    15131  12509  13396   -522    813    302       C  
ATOM     74  CG2 VAL A  65      24.330   5.292  -3.052  1.00109.71           C  
ANISOU   74  CG2 VAL A  65    15364  12621  13699   -573    891    255       C  
ATOM     75  N   TYR A  66      19.939   5.334  -3.433  1.00 97.37           N  
ANISOU   75  N   TYR A  66    13788  11307  11903   -661    871    237       N  
ATOM     76  CA  TYR A  66      18.524   5.681  -3.482  1.00 99.11           C  
ANISOU   76  CA  TYR A  66    13990  11614  12052   -676    853    229       C  
ATOM     77  C   TYR A  66      17.682   4.628  -2.779  1.00 95.35           C  
ANISOU   77  C   TYR A  66    13513  11147  11568   -716    865    226       C  
ATOM     78  O   TYR A  66      16.604   4.936  -2.264  1.00 89.91           O  
ANISOU   78  O   TYR A  66    12806  10521  10836   -719    845    228       O  
ATOM     79  CB  TYR A  66      18.061   5.848  -4.933  1.00101.85           C  
ANISOU   79  CB  TYR A  66    14336  12005  12356   -703    866    194       C  
ATOM     80  CG  TYR A  66      18.490   7.146  -5.584  1.00 98.27           C  
ANISOU   80  CG  TYR A  66    13886  11566  11886   -663    848    202       C  
ATOM     81  CD1 TYR A  66      19.836   7.472  -5.705  1.00 98.22           C  
ANISOU   81  CD1 TYR A  66    13893  11494  11931   -635    861    213       C  
ATOM     82  CD2 TYR A  66      17.552   8.047  -6.073  1.00 96.05           C  
ANISOU   82  CD2 TYR A  66    13592  11361  11540   -653    817    197       C  
ATOM     83  CE1 TYR A  66      20.239   8.654  -6.296  1.00 97.77           C  
ANISOU   83  CE1 TYR A  66    13842  11446  11860   -603    850    220       C  
ATOM     84  CE2 TYR A  66      17.950   9.240  -6.668  1.00 99.85           C  
ANISOU   84  CE2 TYR A  66    14083  11851  12006   -617    801    208       C  
ATOM     85  CZ  TYR A  66      19.296   9.535  -6.773  1.00 96.47           C  
ANISOU   85  CZ  TYR A  66    13672  11354  11628   -594    821    220       C  
ATOM     86  OH  TYR A  66      19.709  10.708  -7.358  1.00 92.44           O  
ANISOU   86  OH  TYR A  66    13174  10847  11104   -562    812    231       O  
ATOM     87  N   SER A  67      18.161   3.384  -2.744  1.00 98.87           N  
ANISOU   87  N   SER A  67    13978  11529  12059   -748    899    219       N  
ATOM     88  CA  SER A  67      17.430   2.314  -2.074  1.00 98.67           C  
ANISOU   88  CA  SER A  67    13959  11502  12030   -789    917    218       C  
ATOM     89  C   SER A  67      17.675   2.323  -0.568  1.00 94.26           C  
ANISOU   89  C   SER A  67    13414  10913  11489   -760    896    262       C  
ATOM     90  O   SER A  67      16.731   2.158   0.214  1.00 89.45           O  
ANISOU   90  O   SER A  67    12801  10340  10846   -777    893    270       O  
ATOM     91  CB  SER A  67      17.819   0.964  -2.677  1.00 95.18           C  
ANISOU   91  CB  SER A  67    13535  10999  11629   -836    964    193       C  
ATOM     92  N   VAL A  68      18.932   2.499  -0.144  1.00 97.41           N  
ANISOU   92  N   VAL A  68    13828  11245  11939   -716    880    288       N  
ATOM     93  CA  VAL A  68      19.219   2.642   1.283  1.00 96.97           C  
ANISOU   93  CA  VAL A  68    13787  11163  11892   -682    850    331       C  
ATOM     94  C   VAL A  68      18.513   3.866   1.848  1.00101.13           C  
ANISOU   94  C   VAL A  68    14295  11766  12366   -652    815    343       C  
ATOM     95  O   VAL A  68      17.858   3.797   2.894  1.00102.38           O  
ANISOU   95  O   VAL A  68    14460  11946  12494   -657    806    362       O  
ATOM     96  CB  VAL A  68      20.736   2.717   1.537  1.00 99.65           C  
ANISOU   96  CB  VAL A  68    14140  11422  12302   -636    832    350       C  
ATOM     97  CG1 VAL A  68      21.027   2.428   2.989  1.00102.13           C  
ANISOU   97  CG1 VAL A  68    14481  11696  12628   -612    804    391       C  
ATOM     98  CG2 VAL A  68      21.480   1.723   0.682  1.00103.79           C  
ANISOU   98  CG2 VAL A  68    14674  11878  12885   -661    869    326       C  
ATOM     99  N   VAL A  69      18.640   5.008   1.164  1.00 91.98           N  
ANISOU   99  N   VAL A  69    13112  10643  11195   -623    796    332       N  
ATOM    100  CA  VAL A  69      18.099   6.259   1.688  1.00 87.77           C  
ANISOU  100  CA  VAL A  69    12557  10171  10619   -587    760    343       C  
ATOM    101  C   VAL A  69      16.576   6.226   1.686  1.00 87.41           C  
ANISOU  101  C   VAL A  69    12491  10206  10515   -622    768    325       C  
ATOM    102  O   VAL A  69      15.930   6.741   2.608  1.00 89.72           O  
ANISOU  102  O   VAL A  69    12774  10539  10776   -608    749    336       O  
ATOM    103  CB  VAL A  69      18.655   7.452   0.886  1.00 87.11           C  
ANISOU  103  CB  VAL A  69    12458  10098  10543   -548    742    337       C  
ATOM    104  CG1 VAL A  69      17.841   8.718   1.135  1.00 86.74           C  
ANISOU  104  CG1 VAL A  69    12385  10125  10447   -519    709    340       C  
ATOM    105  CG2 VAL A  69      20.127   7.674   1.220  1.00 86.96           C  
ANISOU  105  CG2 VAL A  69    12451  10004  10585   -506    728    356       C  
ATOM    106  N   PHE A  70      15.982   5.599   0.666  1.00 87.64           N  
ANISOU  106  N   PHE A  70    12512  10256  10530   -670    797    291       N  
ATOM    107  CA  PHE A  70      14.528   5.523   0.553  1.00 87.87           C  
ANISOU  107  CA  PHE A  70    12514  10362  10511   -706    804    265       C  
ATOM    108  C   PHE A  70      13.903   5.006   1.840  1.00 88.09           C  
ANISOU  108  C   PHE A  70    12549  10395  10528   -726    814    279       C  
ATOM    109  O   PHE A  70      13.003   5.634   2.409  1.00 88.11           O  
ANISOU  109  O   PHE A  70    12527  10458  10494   -718    800    276       O  
ATOM    110  CB  PHE A  70      14.167   4.603  -0.623  1.00 88.18           C  
ANISOU  110  CB  PHE A  70    12551  10405  10549   -761    837    225       C  
ATOM    111  CG  PHE A  70      12.693   4.525  -0.945  1.00 88.48           C  
ANISOU  111  CG  PHE A  70    12554  10523  10542   -799    841    188       C  
ATOM    112  CD1 PHE A  70      11.757   4.098  -0.009  1.00 88.74           C  
ANISOU  112  CD1 PHE A  70    12576  10582  10561   -828    855    186       C  
ATOM    113  CD2 PHE A  70      12.250   4.840  -2.208  1.00 88.58           C  
ANISOU  113  CD2 PHE A  70    12546  10582  10527   -809    832    153       C  
ATOM    114  CE1 PHE A  70      10.418   4.026  -0.322  1.00 89.07           C  
ANISOU  114  CE1 PHE A  70    12578  10695  10570   -864    860    146       C  
ATOM    115  CE2 PHE A  70      10.913   4.758  -2.518  1.00 88.91           C  
ANISOU  115  CE2 PHE A  70    12552  10697  10533   -842    829    115       C  
ATOM    116  CZ  PHE A  70       9.997   4.355  -1.577  1.00 89.15           C  
ANISOU  116  CZ  PHE A  70    12563  10753  10558   -870    843    109       C  
ATOM    117  N   VAL A  71      14.378   3.858   2.318  1.00119.86           N  
ANISOU  117  N   VAL A  71    16608  14352  14582   -751    842    295       N  
ATOM    118  CA  VAL A  71      13.691   3.170   3.402  1.00121.11           C  
ANISOU  118  CA  VAL A  71    16781  14510  14723   -784    863    306       C  
ATOM    119  C   VAL A  71      13.965   3.837   4.743  1.00119.84           C  
ANISOU  119  C   VAL A  71    16637  14346  14552   -740    834    345       C  
ATOM    120  O   VAL A  71      13.043   4.036   5.541  1.00119.05           O  
ANISOU  120  O   VAL A  71    16528  14292  14413   -752    839    345       O  
ATOM    121  CB  VAL A  71      14.092   1.689   3.406  1.00122.01           C  
ANISOU  121  CB  VAL A  71    16933  14550  14874   -827    902    311       C  
ATOM    122  CG1 VAL A  71      13.271   0.928   2.382  1.00121.82           C  
ANISOU  122  CG1 VAL A  71    16889  14554  14845   -889    940    264       C  
ATOM    123  CG2 VAL A  71      15.560   1.568   3.091  1.00120.03           C  
ANISOU  123  CG2 VAL A  71    16707  14222  14678   -793    890    329       C  
ATOM    124  N   VAL A  72      15.225   4.192   5.014  1.00103.50           N  
ANISOU  124  N   VAL A  72    14590  12221  12516   -689    804    375       N  
ATOM    125  CA  VAL A  72      15.559   4.830   6.287  1.00106.43           C  
ANISOU  125  CA  VAL A  72    14978  12584  12874   -645    771    410       C  
ATOM    126  C   VAL A  72      14.707   6.076   6.489  1.00107.59           C  
ANISOU  126  C   VAL A  72    15086  12815  12977   -624    751    397       C  
ATOM    127  O   VAL A  72      14.159   6.310   7.573  1.00108.43           O  
ANISOU  127  O   VAL A  72    15200  12949  13049   -622    748    408       O  
ATOM    128  CB  VAL A  72      17.063   5.154   6.356  1.00104.70           C  
ANISOU  128  CB  VAL A  72    14777  12298  12705   -592    736    434       C  
ATOM    129  CG1 VAL A  72      17.437   5.641   7.750  1.00105.73           C  
ANISOU  129  CG1 VAL A  72    14932  12416  12824   -550    700    469       C  
ATOM    130  CG2 VAL A  72      17.881   3.928   5.994  1.00101.58           C  
ANISOU  130  CG2 VAL A  72    14411  11820  12363   -612    758    440       C  
ATOM    131  N   GLY A  73      14.580   6.893   5.443  1.00110.88           N  
ANISOU  131  N   GLY A  73    15464  13272  13393   -607    737    372       N  
ATOM    132  CA  GLY A  73      13.668   8.022   5.514  1.00111.65           C  
ANISOU  132  CA  GLY A  73    15522  13449  13453   -588    718    355       C  
ATOM    133  C   GLY A  73      12.217   7.595   5.592  1.00112.20           C  
ANISOU  133  C   GLY A  73    15566  13580  13486   -639    747    326       C  
ATOM    134  O   GLY A  73      11.447   8.119   6.400  1.00115.23           O  
ANISOU  134  O   GLY A  73    15932  14011  13839   -633    744    322       O  
ATOM    135  N   LEU A  74      11.823   6.633   4.760  1.00 98.87           N  
ANISOU  135  N   LEU A  74    13873  11890  11803   -691    780    301       N  
ATOM    136  CA  LEU A  74      10.426   6.217   4.743  1.00100.72           C  
ANISOU  136  CA  LEU A  74    14077  12183  12010   -742    809    266       C  
ATOM    137  C   LEU A  74      10.059   5.502   6.038  1.00103.67           C  
ANISOU  137  C   LEU A  74    14479  12541  12371   -775    842    282       C  
ATOM    138  O   LEU A  74       9.030   5.807   6.652  1.00102.23           O  
ANISOU  138  O   LEU A  74    14269  12413  12158   -788    853    265       O  
ATOM    139  CB  LEU A  74      10.159   5.333   3.522  1.00 96.90           C  
ANISOU  139  CB  LEU A  74    13584  11698  11538   -791    834    232       C  
ATOM    140  CG  LEU A  74       8.719   5.233   3.015  1.00 96.60           C  
ANISOU  140  CG  LEU A  74    13493  11736  11474   -834    848    180       C  
ATOM    141  CD1 LEU A  74       7.794   4.472   3.947  1.00100.20           C  
ANISOU  141  CD1 LEU A  74    13947  12205  11920   -886    892    170       C  
ATOM    142  CD2 LEU A  74       8.199   6.647   2.813  1.00 98.63           C  
ANISOU  142  CD2 LEU A  74    13705  12063  11709   -786    803    167       C  
ATOM    143  N   VAL A  75      10.894   4.554   6.476  1.00120.25           N  
ANISOU  143  N   VAL A  75    16634  14562  14493   -787    860    315       N  
ATOM    144  CA  VAL A  75      10.601   3.825   7.710  1.00121.66           C  
ANISOU  144  CA  VAL A  75    16853  14719  14655   -819    892    337       C  
ATOM    145  C   VAL A  75      10.584   4.784   8.890  1.00120.38           C  
ANISOU  145  C   VAL A  75    16696  14580  14461   -777    866    360       C  
ATOM    146  O   VAL A  75       9.599   4.869   9.632  1.00119.12           O  
ANISOU  146  O   VAL A  75    16527  14466  14267   -802    891    348       O  
ATOM    147  CB  VAL A  75      11.616   2.686   7.930  1.00119.66           C  
ANISOU  147  CB  VAL A  75    16662  14369  14435   -830    905    373       C  
ATOM    148  CG1 VAL A  75      11.776   2.376   9.420  1.00117.35           C  
ANISOU  148  CG1 VAL A  75    16427  14041  14120   -828    911    417       C  
ATOM    149  CG2 VAL A  75      11.192   1.443   7.169  1.00114.53           C  
ANISOU  149  CG2 VAL A  75    16012  13701  13804   -896    953    347       C  
ATOM    150  N   GLY A  76      11.662   5.553   9.050  1.00 98.29           N  
ANISOU  150  N   GLY A  76    13913  11754  11679   -713    819    387       N  
ATOM    151  CA  GLY A  76      11.745   6.453  10.186  1.00 96.47           C  
ANISOU  151  CA  GLY A  76    13692  11541  11421   -672    792    407       C  
ATOM    152  C   GLY A  76      10.595   7.436  10.218  1.00 98.04           C  
ANISOU  152  C   GLY A  76    13834  11828  11588   -669    792    371       C  
ATOM    153  O   GLY A  76       9.880   7.538  11.216  1.00 99.35           O  
ANISOU  153  O   GLY A  76    14005  12026  11718   -684    812    369       O  
ATOM    154  N   ASN A  77      10.374   8.135   9.102  1.00102.11           N  
ANISOU  154  N   ASN A  77    14296  12384  12116   -650    771    341       N  
ATOM    155  CA  ASN A  77       9.349   9.171   9.060  1.00102.27           C  
ANISOU  155  CA  ASN A  77    14258  12484  12114   -636    761    307       C  
ATOM    156  C   ASN A  77       7.966   8.577   9.245  1.00105.85           C  
ANISOU  156  C   ASN A  77    14685  12988  12546   -698    809    271       C  
ATOM    157  O   ASN A  77       7.114   9.176   9.907  1.00105.10           O  
ANISOU  157  O   ASN A  77    14560  12946  12426   -696    815    251       O  
ATOM    158  CB  ASN A  77       9.426   9.932   7.745  1.00100.31           C  
ANISOU  158  CB  ASN A  77    13967  12261  11884   -606    727    286       C  
ATOM    159  CG  ASN A  77      10.652  10.793   7.662  1.00100.42           C  
ANISOU  159  CG  ASN A  77    13998  12237  11919   -543    682    315       C  
ATOM    160  OD1 ASN A  77      11.667  10.489   8.272  1.00 98.51           O  
ANISOU  160  OD1 ASN A  77    13803  11934  11692   -529    677    350       O  
ATOM    161  ND2 ASN A  77      10.566  11.881   6.923  1.00100.69           N  
ANISOU  161  ND2 ASN A  77    13995  12304  11957   -504    649    300       N  
ATOM    162  N   SER A  78       7.713   7.409   8.651  1.00112.12           N  
ANISOU  162  N   SER A  78    15485  13764  13351   -754    845    259       N  
ATOM    163  CA  SER A  78       6.466   6.710   8.936  1.00112.55           C  
ANISOU  163  CA  SER A  78    15518  13856  13389   -819    898    225       C  
ATOM    164  C   SER A  78       6.414   6.292  10.398  1.00111.42           C  
ANISOU  164  C   SER A  78    15425  13688  13220   -840    933    253       C  
ATOM    165  O   SER A  78       5.444   6.583  11.105  1.00111.77           O  
ANISOU  165  O   SER A  78    15445  13783  13239   -859    960    229       O  
ATOM    166  CB  SER A  78       6.307   5.498   8.017  1.00110.61           C  
ANISOU  166  CB  SER A  78    15274  13587  13165   -877    930    206       C  
ATOM    167  OG  SER A  78       6.598   5.832   6.670  1.00110.13           O  
ANISOU  167  OG  SER A  78    15184  13536  13123   -854    894    189       O  
ATOM    168  N   LEU A  79       7.478   5.647  10.883  1.00122.59           N  
ANISOU  168  N   LEU A  79    16913  15025  14639   -835    933    303       N  
ATOM    169  CA  LEU A  79       7.501   5.195  12.272  1.00124.48           C  
ANISOU  169  CA  LEU A  79    17213  15235  14847   -854    962    336       C  
ATOM    170  C   LEU A  79       7.447   6.370  13.243  1.00124.99           C  
ANISOU  170  C   LEU A  79    17274  15337  14879   -808    937    342       C  
ATOM    171  O   LEU A  79       6.735   6.314  14.252  1.00125.70           O  
ANISOU  171  O   LEU A  79    17378  15451  14931   -837    975    337       O  
ATOM    172  CB  LEU A  79       8.740   4.335  12.523  1.00122.84           C  
ANISOU  172  CB  LEU A  79    17083  14933  14656   -848    953    390       C  
ATOM    173  CG  LEU A  79       9.067   3.924  13.956  1.00120.45           C  
ANISOU  173  CG  LEU A  79    16860  14587  14318   -852    965    437       C  
ATOM    174  CD1 LEU A  79       8.455   2.575  14.274  1.00116.54           C  
ANISOU  174  CD1 LEU A  79    16405  14063  13811   -929   1034    441       C  
ATOM    175  CD2 LEU A  79      10.573   3.892  14.152  1.00120.56           C  
ANISOU  175  CD2 LEU A  79    16928  14525  14355   -798    912    487       C  
ATOM    176  N   VAL A  80       8.189   7.445  12.954  1.00116.90           N  
ANISOU  176  N   VAL A  80    16232  14315  13869   -739    876    350       N  
ATOM    177  CA  VAL A  80       8.169   8.618  13.828  1.00115.80           C  
ANISOU  177  CA  VAL A  80    16085  14209  13703   -693    850    351       C  
ATOM    178  C   VAL A  80       6.772   9.225  13.871  1.00117.07           C  
ANISOU  178  C   VAL A  80    16180  14455  13847   -712    876    299       C  
ATOM    179  O   VAL A  80       6.267   9.580  14.943  1.00119.94           O  
ANISOU  179  O   VAL A  80    16551  14847  14174   -716    896    292       O  
ATOM    180  CB  VAL A  80       9.222   9.650  13.377  1.00113.59           C  
ANISOU  180  CB  VAL A  80    15794  13914  13451   -619    783    365       C  
ATOM    181  CG1 VAL A  80       8.811  11.060  13.780  1.00115.24           C  
ANISOU  181  CG1 VAL A  80    15961  14181  13645   -575    758    342       C  
ATOM    182  CG2 VAL A  80      10.590   9.300  13.943  1.00115.30           C  
ANISOU  182  CG2 VAL A  80    16082  14052  13677   -591    754    417       C  
ATOM    183  N   MET A  81       6.122   9.353  12.711  1.00121.09           N  
ANISOU  183  N   MET A  81    16622  15006  14381   -722    874    257       N  
ATOM    184  CA  MET A  81       4.755   9.868  12.686  1.00122.27           C  
ANISOU  184  CA  MET A  81    16699  15234  14522   -739    895    202       C  
ATOM    185  C   MET A  81       3.807   8.959  13.459  1.00124.34           C  
ANISOU  185  C   MET A  81    16974  15510  14760   -812    969    185       C  
ATOM    186  O   MET A  81       2.999   9.431  14.266  1.00123.73           O  
ANISOU  186  O   MET A  81    16873  15479  14660   -821    995    158       O  
ATOM    187  CB  MET A  81       4.270  10.025  11.246  1.00123.36           C  
ANISOU  187  CB  MET A  81    16770  15409  14691   -739    874    163       C  
ATOM    188  CG  MET A  81       4.888  11.167  10.474  1.00119.34           C  
ANISOU  188  CG  MET A  81    16237  14905  14201   -668    807    169       C  
ATOM    189  SD  MET A  81       4.710  10.834   8.715  1.00121.83           S  
ANISOU  189  SD  MET A  81    16514  15232  14543   -681    788    143       S  
ATOM    190  CE  MET A  81       2.937  10.593   8.603  1.00119.56           C  
ANISOU  190  CE  MET A  81    16150  15026  14253   -735    825     74       C  
ATOM    191  N   PHE A  82       3.885   7.646  13.225  1.00169.50           N  
ANISOU  191  N   PHE A  82    22730  21187  20487   -869   1007    197       N  
ATOM    192  CA  PHE A  82       2.943   6.746  13.883  1.00171.99           C  
ANISOU  192  CA  PHE A  82    23056  21511  20782   -945   1084    179       C  
ATOM    193  C   PHE A  82       3.250   6.554  15.362  1.00172.91           C  
ANISOU  193  C   PHE A  82    23251  21594  20852   -952   1112    220       C  
ATOM    194  O   PHE A  82       2.362   6.134  16.112  1.00175.96           O  
ANISOU  194  O   PHE A  82    23643  22000  21212  -1009   1179    201       O  
ATOM    195  CB  PHE A  82       2.870   5.396  13.160  1.00167.95           C  
ANISOU  195  CB  PHE A  82    22557  20962  20294  -1005   1119    176       C  
ATOM    196  CG  PHE A  82       2.756   5.512  11.662  1.00170.53           C  
ANISOU  196  CG  PHE A  82    22821  21313  20660   -996   1085    141       C  
ATOM    197  CD1 PHE A  82       1.980   6.507  11.088  1.00171.62           C  
ANISOU  197  CD1 PHE A  82    22873  21527  20808   -970   1056     90       C  
ATOM    198  CD2 PHE A  82       3.378   4.597  10.829  1.00171.95           C  
ANISOU  198  CD2 PHE A  82    23029  21439  20866  -1014   1083    156       C  
ATOM    199  CE1 PHE A  82       1.864   6.619   9.718  1.00170.06           C  
ANISOU  199  CE1 PHE A  82    22625  21351  20638   -960   1020     60       C  
ATOM    200  CE2 PHE A  82       3.263   4.704   9.453  1.00171.18           C  
ANISOU  200  CE2 PHE A  82    22878  21365  20796  -1008   1053    122       C  
ATOM    201  CZ  PHE A  82       2.504   5.716   8.899  1.00170.01           C  
ANISOU  201  CZ  PHE A  82    22651  21294  20650   -981   1020     76       C  
ATOM    202  N   VAL A  83       4.475   6.849  15.803  1.00117.64           N  
ANISOU  202  N   VAL A  83    16312  14544  13841   -899   1065    274       N  
ATOM    203  CA  VAL A  83       4.736   6.929  17.237  1.00116.91           C  
ANISOU  203  CA  VAL A  83    16290  14432  13698   -894   1078    309       C  
ATOM    204  C   VAL A  83       4.077   8.175  17.821  1.00116.24           C  
ANISOU  204  C   VAL A  83    16158  14418  13590   -867   1075    272       C  
ATOM    205  O   VAL A  83       3.429   8.123  18.872  1.00115.75           O  
ANISOU  205  O   VAL A  83    16119  14377  13484   -901   1127    263       O  
ATOM    206  CB  VAL A  83       6.251   6.912  17.516  1.00113.72           C  
ANISOU  206  CB  VAL A  83    15960  13956  13293   -841   1020    372       C  
ATOM    207  CG1 VAL A  83       6.552   7.622  18.829  1.00113.53           C  
ANISOU  207  CG1 VAL A  83    15981  13935  13219   -807   1003    394       C  
ATOM    208  CG2 VAL A  83       6.781   5.487  17.536  1.00116.25           C  
ANISOU  208  CG2 VAL A  83    16354  14198  13619   -881   1043    415       C  
ATOM    209  N   ILE A  84       4.227   9.314  17.140  1.00132.76           N  
ANISOU  209  N   ILE A  84    18186  16545  15712   -806   1017    250       N  
ATOM    210  CA  ILE A  84       3.649  10.562  17.637  1.00133.77           C  
ANISOU  210  CA  ILE A  84    18265  16735  15826   -774   1009    214       C  
ATOM    211  C   ILE A  84       2.128  10.470  17.677  1.00133.74           C  
ANISOU  211  C   ILE A  84    18196  16798  15822   -829   1073    151       C  
ATOM    212  O   ILE A  84       1.499  10.818  18.680  1.00135.54           O  
ANISOU  212  O   ILE A  84    18424  17059  16016   -843   1112    129       O  
ATOM    213  CB  ILE A  84       4.123  11.766  16.795  1.00130.47           C  
ANISOU  213  CB  ILE A  84    17792  16334  15446   -698    934    204       C  
ATOM    214  CG1 ILE A  84       5.479  12.310  17.269  1.00128.53           C  
ANISOU  214  CG1 ILE A  84    17603  16040  15192   -636    877    253       C  
ATOM    215  CG2 ILE A  84       3.100  12.894  16.833  1.00125.87           C  
ANISOU  215  CG2 ILE A  84    17127  15828  14869   -679    935    147       C  
ATOM    216  CD1 ILE A  84       6.531  11.289  17.563  1.00130.28           C  
ANISOU  216  CD1 ILE A  84    17912  16184  15404   -648    873    311       C  
ATOM    217  N   ILE A  85       1.510   9.985  16.597  1.00138.01           N  
ANISOU  217  N   ILE A  85    18679  17357  16400   -861   1085    117       N  
ATOM    218  CA  ILE A  85       0.055  10.079  16.525  1.00139.59           C  
ANISOU  218  CA  ILE A  85    18799  17627  16611   -903   1134     48       C  
ATOM    219  C   ILE A  85      -0.603   9.166  17.552  1.00142.85           C  
ANISOU  219  C   ILE A  85    19252  18034  16989   -982   1225     42       C  
ATOM    220  O   ILE A  85      -1.699   9.463  18.042  1.00144.84           O  
ANISOU  220  O   ILE A  85    19455  18342  17236  -1011   1274    -12       O  
ATOM    221  CB  ILE A  85      -0.463   9.783  15.105  1.00140.72           C  
ANISOU  221  CB  ILE A  85    18870  17794  16803   -919   1119      9       C  
ATOM    222  CG1 ILE A  85      -0.060   8.382  14.656  1.00143.32           C  
ANISOU  222  CG1 ILE A  85    19250  18066  17138   -971   1145     38       C  
ATOM    223  CG2 ILE A  85       0.059  10.814  14.121  1.00135.88           C  
ANISOU  223  CG2 ILE A  85    18216  17193  16218   -842   1034     11       C  
ATOM    224  CD1 ILE A  85      -0.264   8.141  13.170  1.00146.13           C  
ANISOU  224  CD1 ILE A  85    19549  18436  17537   -975   1116      8       C  
ATOM    225  N   ARG A  86       0.039   8.051  17.901  1.00152.11           N  
ANISOU  225  N   ARG A  86    20517  19139  18138  -1018   1251     95       N  
ATOM    226  CA  ARG A  86      -0.536   7.099  18.847  1.00153.59           C  
ANISOU  226  CA  ARG A  86    20755  19312  18289  -1097   1341     97       C  
ATOM    227  C   ARG A  86      -0.014   7.307  20.266  1.00154.85           C  
ANISOU  227  C   ARG A  86    21006  19445  18384  -1083   1352    142       C  
ATOM    228  O   ARG A  86      -0.802   7.484  21.199  1.00154.38           O  
ANISOU  228  O   ARG A  86    20948  19421  18290  -1118   1413    114       O  
ATOM    229  CB  ARG A  86      -0.263   5.664  18.382  1.00149.29           C  
ANISOU  229  CB  ARG A  86    20259  18706  17758  -1151   1370    126       C  
ATOM    230  N   TYR A  87       1.309   7.289  20.446  1.00146.62           N  
ANISOU  230  N   TYR A  87    20042  18343  17326  -1035   1293    209       N  
ATOM    231  CA  TYR A  87       1.875   7.355  21.790  1.00145.79           C  
ANISOU  231  CA  TYR A  87    20033  18206  17155  -1024   1297    256       C  
ATOM    232  C   TYR A  87       1.654   8.727  22.424  1.00148.30           C  
ANISOU  232  C   TYR A  87    20317  18581  17451   -977   1277    226       C  
ATOM    233  O   TYR A  87       0.969   8.846  23.447  1.00150.33           O  
ANISOU  233  O   TYR A  87    20592  18866  17659  -1011   1337    206       O  
ATOM    234  CB  TYR A  87       3.364   7.004  21.748  1.00144.22           C  
ANISOU  234  CB  TYR A  87    19914  17927  16955   -979   1230    330       C  
ATOM    235  N   THR A  88       2.216   9.779  21.825  1.00130.61           N  
ANISOU  235  N   THR A  88    18027  16356  15246   -900   1197    220       N  
ATOM    236  CA  THR A  88       2.138  11.144  22.357  1.00126.65           C  
ANISOU  236  CA  THR A  88    17492  15900  14730   -847   1168    193       C  
ATOM    237  C   THR A  88       1.239  11.978  21.445  1.00126.97           C  
ANISOU  237  C   THR A  88    17409  16009  14826   -830   1160    124       C  
ATOM    238  O   THR A  88       1.723  12.683  20.557  1.00126.46           O  
ANISOU  238  O   THR A  88    17298  15946  14805   -770   1090    124       O  
ATOM    239  CB  THR A  88       3.528  11.785  22.468  1.00121.93           C  
ANISOU  239  CB  THR A  88    16937  15261  14131   -769   1081    240       C  
ATOM    240  OG1 THR A  88       3.855  12.437  21.235  1.00119.63           O  
ANISOU  240  OG1 THR A  88    16573  14979  13904   -716   1018    227       O  
ATOM    241  CG2 THR A  88       4.582  10.746  22.761  1.00125.33           C  
ANISOU  241  CG2 THR A  88    17471  15612  14539   -778   1066    311       C  
ATOM    242  N   LYS A  89      -0.070  11.918  21.692  1.00134.35           N  
ANISOU  242  N   LYS A  89    18291  16997  15758   -882   1231     66       N  
ATOM    243  CA  LYS A  89      -1.059  12.634  20.880  1.00135.35           C  
ANISOU  243  CA  LYS A  89    18296  17191  15940   -870   1225     -5       C  
ATOM    244  C   LYS A  89      -0.741  14.120  20.736  1.00136.29           C  
ANISOU  244  C   LYS A  89    18368  17336  16079   -784   1154    -19       C  
ATOM    245  O   LYS A  89       0.030  14.676  21.516  1.00136.10           O  
ANISOU  245  O   LYS A  89    18399  17291  16021   -744   1126     12       O  
ATOM    246  CB  LYS A  89      -2.458  12.470  21.478  1.00132.82           C  
ANISOU  246  CB  LYS A  89    17932  16924  15610   -935   1316    -69       C  
ATOM    247  N   LYS A  91      -0.885  18.706  22.549  1.00158.24           N  
ANISOU  247  N   LYS A  91    21042  20222  18858   -593   1065   -116       N  
ATOM    248  CA  LYS A  91       0.469  18.183  22.414  1.00159.16           C  
ANISOU  248  CA  LYS A  91    21247  20272  18955   -576   1019    -40       C  
ATOM    249  C   LYS A  91       1.500  19.266  22.681  1.00156.07           C  
ANISOU  249  C   LYS A  91    20877  19858  18563   -500    949    -17       C  
ATOM    250  O   LYS A  91       1.218  20.454  22.528  1.00153.79           O  
ANISOU  250  O   LYS A  91    20524  19602  18308   -450    921    -56       O  
ATOM    251  CB  LYS A  91       0.686  17.597  21.018  1.00156.87           C  
ANISOU  251  CB  LYS A  91    20931  19960  18711   -578    986    -19       C  
ATOM    252  N   THR A  92       2.701  18.848  23.074  1.00128.97           N  
ANISOU  252  N   THR A  92    17537  16368  15099   -490    920     45       N  
ATOM    253  CA  THR A  92       3.787  19.796  23.266  1.00129.05           C  
ANISOU  253  CA  THR A  92    17568  16350  15115   -419    849     67       C  
ATOM    254  C   THR A  92       4.160  20.426  21.926  1.00125.82           C  
ANISOU  254  C   THR A  92    17097  15932  14776   -365    785     68       C  
ATOM    255  O   THR A  92       3.902  19.866  20.856  1.00126.04           O  
ANISOU  255  O   THR A  92    17094  15959  14837   -384    787     72       O  
ATOM    256  CB  THR A  92       4.996  19.103  23.910  1.00127.74           C  
ANISOU  256  CB  THR A  92    17509  16121  14904   -421    828    131       C  
ATOM    257  OG1 THR A  92       5.778  20.060  24.635  1.00132.52           O  
ANISOU  257  OG1 THR A  92    18141  16714  15495   -366    780    135       O  
ATOM    258  CG2 THR A  92       5.879  18.459  22.865  1.00125.28           C  
ANISOU  258  CG2 THR A  92    17212  15755  14632   -411    785    179       C  
ATOM    259  N   ALA A  93       4.734  21.628  21.987  1.00128.73           N  
ANISOU  259  N   ALA A  93    17450  16295  15166   -300    732     64       N  
ATOM    260  CA  ALA A  93       5.071  22.340  20.758  1.00127.20           C  
ANISOU  260  CA  ALA A  93    17203  16092  15036   -248    674     65       C  
ATOM    261  C   ALA A  93       6.074  21.553  19.927  1.00124.70           C  
ANISOU  261  C   ALA A  93    16927  15719  14736   -249    644    120       C  
ATOM    262  O   ALA A  93       5.915  21.413  18.709  1.00124.49           O  
ANISOU  262  O   ALA A  93    16860  15692  14748   -248    630    120       O  
ATOM    263  CB  ALA A  93       5.619  23.729  21.084  1.00126.51           C  
ANISOU  263  CB  ALA A  93    17102  15998  14967   -180    627     54       C  
ATOM    264  N   THR A  94       7.112  21.018  20.575  1.00147.11           N  
ANISOU  264  N   THR A  94    19844  18506  17545   -252    632    164       N  
ATOM    265  CA  THR A  94       8.116  20.252  19.845  1.00149.76           C  
ANISOU  265  CA  THR A  94    20216  18782  17902   -253    604    213       C  
ATOM    266  C   THR A  94       7.486  19.079  19.102  1.00148.72           C  
ANISOU  266  C   THR A  94    20076  18657  17772   -310    645    216       C  
ATOM    267  O   THR A  94       7.920  18.744  17.996  1.00146.49           O  
ANISOU  267  O   THR A  94    19784  18347  17527   -306    624    234       O  
ATOM    268  CB  THR A  94       9.203  19.762  20.801  1.00149.67           C  
ANISOU  268  CB  THR A  94    20292  18718  17857   -250    587    256       C  
ATOM    269  OG1 THR A  94       9.483  20.778  21.774  1.00149.94           O  
ANISOU  269  OG1 THR A  94    20336  18762  17874   -211    563    241       O  
ATOM    270  CG2 THR A  94      10.476  19.440  20.034  1.00145.74           C  
ANISOU  270  CG2 THR A  94    19816  18155  17401   -226    540    298       C  
ATOM    271  N   ASN A  95       6.443  18.471  19.678  1.00121.02           N  
ANISOU  271  N   ASN A  95    16570  15186  14228   -366    707    193       N  
ATOM    272  CA  ASN A  95       5.776  17.342  19.035  1.00117.96           C  
ANISOU  272  CA  ASN A  95    16170  14804  13843   -426    751    190       C  
ATOM    273  C   ASN A  95       5.139  17.754  17.713  1.00116.07           C  
ANISOU  273  C   ASN A  95    15846  14601  13653   -414    736    156       C  
ATOM    274  O   ASN A  95       5.182  17.003  16.732  1.00117.06           O  
ANISOU  274  O   ASN A  95    15967  14711  13800   -438    737    166       O  
ATOM    275  CB  ASN A  95       4.719  16.756  19.970  1.00122.07           C  
ANISOU  275  CB  ASN A  95    16703  15361  14318   -488    825    165       C  
ATOM    276  CG  ASN A  95       5.237  15.578  20.771  1.00125.37           C  
ANISOU  276  CG  ASN A  95    17217  15728  14689   -531    853    212       C  
ATOM    277  OD1 ASN A  95       4.459  14.804  21.327  1.00129.33           O  
ANISOU  277  OD1 ASN A  95    17740  16245  15155   -594    920    202       O  
ATOM    278  ND2 ASN A  95       6.559  15.447  20.853  1.00123.38           N  
ANISOU  278  ND2 ASN A  95    17026  15415  14438   -497    803    263       N  
ATOM    279  N   ILE A  96       4.525  18.938  17.675  1.00 96.58           N  
ANISOU  279  N   ILE A  96    13313  12180  11202   -378    721    113       N  
ATOM    280  CA  ILE A  96       3.933  19.430  16.432  1.00 97.19           C  
ANISOU  280  CA  ILE A  96    13312  12290  11323   -358    696     83       C  
ATOM    281  C   ILE A  96       5.011  19.627  15.371  1.00 95.38           C  
ANISOU  281  C   ILE A  96    13098  12015  11127   -317    640    121       C  
ATOM    282  O   ILE A  96       4.807  19.309  14.193  1.00 94.97           O  
ANISOU  282  O   ILE A  96    13018  11968  11098   -327    629    118       O  
ATOM    283  CB  ILE A  96       3.136  20.726  16.686  1.00 94.15           C  
ANISOU  283  CB  ILE A  96    12859  11959  10954   -319    686     33       C  
ATOM    284  CG1 ILE A  96       2.271  20.618  17.946  1.00 96.36           C  
ANISOU  284  CG1 ILE A  96    13137  12278  11199   -357    747     -3       C  
ATOM    285  CG2 ILE A  96       2.233  21.032  15.508  1.00 93.06           C  
ANISOU  285  CG2 ILE A  96    12640  11863  10856   -311    669     -5       C  
ATOM    286  CD1 ILE A  96       1.448  19.345  18.031  1.00101.91           C  
ANISOU  286  CD1 ILE A  96    13841  12997  11882   -436    814    -18       C  
ATOM    287  N   TYR A  97       6.176  20.145  15.769  1.00126.94           N  
ANISOU  287  N   TYR A  97    17138  15967  15125   -273    603    154       N  
ATOM    288  CA  TYR A  97       7.250  20.373  14.805  1.00126.91           C  
ANISOU  288  CA  TYR A  97    17148  15917  15156   -236    556    187       C  
ATOM    289  C   TYR A  97       7.798  19.065  14.245  1.00125.67           C  
ANISOU  289  C   TYR A  97    17034  15716  14999   -277    569    220       C  
ATOM    290  O   TYR A  97       7.929  18.912  13.026  1.00127.40           O  
ANISOU  290  O   TYR A  97    17236  15927  15244   -275    554    224       O  
ATOM    291  CB  TYR A  97       8.374  21.191  15.440  1.00128.10           C  
ANISOU  291  CB  TYR A  97    17331  16027  15312   -184    518    210       C  
ATOM    292  CG  TYR A  97       8.084  22.665  15.563  1.00127.47           C  
ANISOU  292  CG  TYR A  97    17205  15977  15251   -131    490    180       C  
ATOM    293  CD1 TYR A  97       6.935  23.220  15.012  1.00128.12           C  
ANISOU  293  CD1 TYR A  97    17218  16114  15347   -124    493    140       C  
ATOM    294  CD2 TYR A  97       8.977  23.509  16.203  1.00125.96           C  
ANISOU  294  CD2 TYR A  97    17035  15755  15067    -84    458    191       C  
ATOM    295  CE1 TYR A  97       6.671  24.577  15.121  1.00129.15           C  
ANISOU  295  CE1 TYR A  97    17306  16266  15499    -72    466    114       C  
ATOM    296  CE2 TYR A  97       8.726  24.864  16.312  1.00131.25           C  
ANISOU  296  CE2 TYR A  97    17663  16447  15758    -36    434    163       C  
ATOM    297  CZ  TYR A  97       7.573  25.394  15.771  1.00129.12           C  
ANISOU  297  CZ  TYR A  97    17328  16229  15503    -29    439    125       C  
ATOM    298  OH  TYR A  97       7.327  26.744  15.884  1.00124.31           O  
ANISOU  298  OH  TYR A  97    16678  15637  14919     22    414     98       O  
ATOM    299  N   ILE A  98       8.144  18.111  15.116  1.00 99.88           N  
ANISOU  299  N   ILE A  98    13827  12420  11704   -312    597    245       N  
ATOM    300  CA  ILE A  98       8.744  16.871  14.626  1.00100.13           C  
ANISOU  300  CA  ILE A  98    13901  12402  11742   -346    608    277       C  
ATOM    301  C   ILE A  98       7.763  16.135  13.727  1.00 97.78           C  
ANISOU  301  C   ILE A  98    13567  12137  11449   -396    642    252       C  
ATOM    302  O   ILE A  98       8.137  15.632  12.661  1.00 94.40           O  
ANISOU  302  O   ILE A  98    13140  11684  11045   -405    634    262       O  
ATOM    303  CB  ILE A  98       9.224  15.978  15.790  1.00 99.99           C  
ANISOU  303  CB  ILE A  98    13958  12345  11690   -374    630    309       C  
ATOM    304  CG1 ILE A  98       8.242  16.001  16.957  1.00101.31           C  
ANISOU  304  CG1 ILE A  98    14127  12557  11809   -402    672    286       C  
ATOM    305  CG2 ILE A  98      10.590  16.403  16.273  1.00 95.09           C  
ANISOU  305  CG2 ILE A  98    13381  11670  11080   -324    582    343       C  
ATOM    306  CD1 ILE A  98       8.610  15.058  18.077  1.00105.25           C  
ANISOU  306  CD1 ILE A  98    14707  13017  12264   -435    697    320       C  
ATOM    307  N   PHE A  99       6.492  16.076  14.133  1.00109.97           N  
ANISOU  307  N   PHE A  99    15074  13737  12970   -430    681    213       N  
ATOM    308  CA  PHE A  99       5.492  15.377  13.333  1.00111.54           C  
ANISOU  308  CA  PHE A  99    15233  13971  13177   -479    713    182       C  
ATOM    309  C   PHE A  99       5.383  15.979  11.940  1.00108.05           C  
ANISOU  309  C   PHE A  99    14738  13549  12768   -448    672    165       C  
ATOM    310  O   PHE A  99       5.483  15.271  10.933  1.00104.77           O  
ANISOU  310  O   PHE A  99    14323  13118  12366   -473    673    168       O  
ATOM    311  CB  PHE A  99       4.128  15.419  14.020  1.00114.71           C  
ANISOU  311  CB  PHE A  99    15592  14434  13558   -514    759    135       C  
ATOM    312  CG  PHE A  99       2.979  15.239  13.066  1.00116.08           C  
ANISOU  312  CG  PHE A  99    15693  14660  13752   -543    772     86       C  
ATOM    313  CD1 PHE A  99       2.675  13.988  12.551  1.00112.71           C  
ANISOU  313  CD1 PHE A  99    15273  14223  13328   -605    808     82       C  
ATOM    314  CD2 PHE A  99       2.222  16.327  12.660  1.00118.19           C  
ANISOU  314  CD2 PHE A  99    15885  14983  14040   -506    742     44       C  
ATOM    315  CE1 PHE A  99       1.626  13.822  11.663  1.00110.45           C  
ANISOU  315  CE1 PHE A  99    14918  13986  13061   -631    814     33       C  
ATOM    316  CE2 PHE A  99       1.175  16.169  11.768  1.00117.55           C  
ANISOU  316  CE2 PHE A  99    15735  14949  13978   -528    745     -3       C  
ATOM    317  CZ  PHE A  99       0.876  14.912  11.270  1.00111.52           C  
ANISOU  317  CZ  PHE A  99    14978  14180  13216   -592    780    -10       C  
ATOM    318  N   ASN A 100       5.172  17.291  11.864  1.00149.26           N  
ANISOU  318  N   ASN A 100    19913  18799  17999   -394    635    146       N  
ATOM    319  CA  ASN A 100       4.965  17.912  10.565  1.00149.53           C  
ANISOU  319  CA  ASN A 100    19901  18854  18059   -363    594    131       C  
ATOM    320  C   ASN A 100       6.225  17.844   9.718  1.00143.28           C  
ANISOU  320  C   ASN A 100    19151  18005  17284   -340    562    173       C  
ATOM    321  O   ASN A 100       6.149  17.587   8.512  1.00142.45           O  
ANISOU  321  O   ASN A 100    19033  17902  17189   -349    550    168       O  
ATOM    322  CB  ASN A 100       4.499  19.350  10.738  1.00147.41           C  
ANISOU  322  CB  ASN A 100    19583  18626  17802   -308    561    106       C  
ATOM    323  CG  ASN A 100       2.988  19.481  10.659  1.00156.44           C  
ANISOU  323  CG  ASN A 100    20651  19839  18948   -326    576     48       C  
ATOM    324  OD1 ASN A 100       2.431  19.743   9.594  1.00160.10           O  
ANISOU  324  OD1 ASN A 100    21068  20333  19429   -315    546     26       O  
ATOM    325  ND2 ASN A 100       2.320  19.334  11.799  1.00157.82           N  
ANISOU  325  ND2 ASN A 100    20814  20042  19107   -354    620     22       N  
ATOM    326  N   LEU A 101       7.391  18.077  10.325  1.00 89.65           N  
ANISOU  326  N   LEU A 101    12409  11160  10496   -312    550    210       N  
ATOM    327  CA  LEU A 101       8.637  17.864   9.599  1.00 87.51           C  
ANISOU  327  CA  LEU A 101    12176  10828  10245   -297    529    246       C  
ATOM    328  C   LEU A 101       8.710  16.434   9.097  1.00 91.56           C  
ANISOU  328  C   LEU A 101    12716  11317  10756   -354    562    254       C  
ATOM    329  O   LEU A 101       8.978  16.196   7.914  1.00 94.58           O  
ANISOU  329  O   LEU A 101    13098  11686  11154   -359    553    256       O  
ATOM    330  CB  LEU A 101       9.847  18.187  10.477  1.00 87.29           C  
ANISOU  330  CB  LEU A 101    12195  10747  10226   -264    513    279       C  
ATOM    331  CG  LEU A 101      11.148  17.440  10.147  1.00 88.20           C  
ANISOU  331  CG  LEU A 101    12361  10789  10363   -269    511    316       C  
ATOM    332  CD1 LEU A 101      11.760  17.949   8.858  1.00 88.38           C  
ANISOU  332  CD1 LEU A 101    12374  10790  10417   -241    485    322       C  
ATOM    333  CD2 LEU A 101      12.171  17.542  11.272  1.00 88.59           C  
ANISOU  333  CD2 LEU A 101    12453  10790  10415   -245    497    343       C  
ATOM    334  N   ALA A 102       8.434  15.469   9.980  1.00 99.49           N  
ANISOU  334  N   ALA A 102    13745  12316  11740   -400    602    256       N  
ATOM    335  CA  ALA A 102       8.420  14.070   9.567  1.00 99.91           C  
ANISOU  335  CA  ALA A 102    13822  12345  11793   -458    638    260       C  
ATOM    336  C   ALA A 102       7.400  13.842   8.459  1.00100.15           C  
ANISOU  336  C   ALA A 102    13803  12424  11825   -488    647    221       C  
ATOM    337  O   ALA A 102       7.741  13.320   7.393  1.00 98.46           O  
ANISOU  337  O   ALA A 102    13596  12188  11625   -503    644    224       O  
ATOM    338  CB  ALA A 102       8.135  13.165  10.764  1.00 99.93           C  
ANISOU  338  CB  ALA A 102    13861  12338  11770   -503    682    268       C  
ATOM    339  N   LEU A 103       6.152  14.273   8.677  1.00 93.10           N  
ANISOU  339  N   LEU A 103    12856  11599  10920   -495    654    181       N  
ATOM    340  CA  LEU A 103       5.114  14.099   7.662  1.00 90.64           C  
ANISOU  340  CA  LEU A 103    12489  11338  10611   -521    655    138       C  
ATOM    341  C   LEU A 103       5.543  14.723   6.343  1.00 90.26           C  
ANISOU  341  C   LEU A 103    12431  11286  10577   -481    606    143       C  
ATOM    342  O   LEU A 103       5.438  14.098   5.281  1.00 88.59           O  
ANISOU  342  O   LEU A 103    12216  11075  10368   -510    608    131       O  
ATOM    343  CB  LEU A 103       3.793  14.711   8.141  1.00 91.32           C  
ANISOU  343  CB  LEU A 103    12511  11496  10691   -520    660     92       C  
ATOM    344  CG  LEU A 103       2.799  15.218   7.082  1.00 89.46           C  
ANISOU  344  CG  LEU A 103    12204  11321  10466   -510    628     46       C  
ATOM    345  CD1 LEU A 103       2.290  14.075   6.215  1.00 90.99           C  
ANISOU  345  CD1 LEU A 103    12386  11526  10662   -570    651     21       C  
ATOM    346  CD2 LEU A 103       1.631  15.999   7.694  1.00 89.86           C  
ANISOU  346  CD2 LEU A 103    12188  11435  10520   -496    628      1       C  
ATOM    347  N   ALA A 104       6.038  15.962   6.398  1.00141.40           N  
ANISOU  347  N   ALA A 104    18906  17759  17062   -417    564    159       N  
ATOM    348  CA  ALA A 104       6.530  16.625   5.196  1.00141.84           C  
ANISOU  348  CA  ALA A 104    18962  17803  17127   -379    522    170       C  
ATOM    349  C   ALA A 104       7.701  15.860   4.596  1.00135.81           C  
ANISOU  349  C   ALA A 104    18254  16976  16374   -395    533    201       C  
ATOM    350  O   ALA A 104       7.613  15.336   3.480  1.00133.09           O  
ANISOU  350  O   ALA A 104    17910  16633  16026   -420    534    190       O  
ATOM    351  CB  ALA A 104       6.932  18.065   5.514  1.00133.73           C  
ANISOU  351  CB  ALA A 104    17929  16773  16110   -310    483    184       C  
ATOM    352  N   ASP A 105       8.800  15.752   5.339  1.00116.09           N  
ANISOU  352  N   ASP A 105    15801  14419  13888   -382    541    236       N  
ATOM    353  CA  ASP A 105       9.982  15.149   4.747  1.00113.90           C  
ANISOU  353  CA  ASP A 105    15570  14077  13630   -390    548    263       C  
ATOM    354  C   ASP A 105       9.879  13.634   4.676  1.00116.81           C  
ANISOU  354  C   ASP A 105    15959  14426  13997   -453    591    258       C  
ATOM    355  O   ASP A 105      10.867  12.969   4.343  1.00115.09           O  
ANISOU  355  O   ASP A 105    15781  14149  13800   -464    604    278       O  
ATOM    356  CB  ASP A 105      11.253  15.600   5.487  1.00116.47           C  
ANISOU  356  CB  ASP A 105    15931  14344  13978   -349    535    299       C  
ATOM    357  CG  ASP A 105      11.534  14.820   6.754  1.00120.44           C  
ANISOU  357  CG  ASP A 105    16466  14817  14480   -371    559    316       C  
ATOM    358  OD1 ASP A 105      10.596  14.320   7.402  1.00122.39           O  
ANISOU  358  OD1 ASP A 105    16703  15099  14702   -406    584    300       O  
ATOM    359  OD2 ASP A 105      12.718  14.768   7.142  1.00119.01           O  
ANISOU  359  OD2 ASP A 105    16321  14575  14322   -350    550    344       O  
ATOM    360  N   ALA A 106       8.713  13.080   5.014  1.00105.18           N  
ANISOU  360  N   ALA A 106    14460  13000  12505   -496    617    230       N  
ATOM    361  CA  ALA A 106       8.367  11.747   4.536  1.00104.08           C  
ANISOU  361  CA  ALA A 106    14328  12854  12364   -560    654    213       C  
ATOM    362  C   ALA A 106       7.988  11.792   3.063  1.00102.38           C  
ANISOU  362  C   ALA A 106    14086  12668  12145   -568    639    185       C  
ATOM    363  O   ALA A 106       8.463  10.978   2.263  1.00101.07           O  
ANISOU  363  O   ALA A 106    13946  12468  11988   -597    655    185       O  
ATOM    364  CB  ALA A 106       7.216  11.161   5.356  1.00103.00           C  
ANISOU  364  CB  ALA A 106    14168  12756  12211   -607    691    187       C  
ATOM    365  N   LEU A 107       7.146  12.761   2.684  1.00 92.43           N  
ANISOU  365  N   LEU A 107    12779  11471  10871   -541    604    160       N  
ATOM    366  CA  LEU A 107       6.602  12.794   1.331  1.00 90.73           C  
ANISOU  366  CA  LEU A 107    12537  11292  10643   -550    584    130       C  
ATOM    367  C   LEU A 107       7.661  13.105   0.284  1.00 89.92           C  
ANISOU  367  C   LEU A 107    12473  11149  10545   -523    563    154       C  
ATOM    368  O   LEU A 107       7.442  12.821  -0.897  1.00 89.93           O  
ANISOU  368  O   LEU A 107    12472  11164  10531   -542    556    133       O  
ATOM    369  CB  LEU A 107       5.457  13.810   1.232  1.00 88.68           C  
ANISOU  369  CB  LEU A 107    12217  11106  10372   -520    544     99       C  
ATOM    370  CG  LEU A 107       4.189  13.595   2.070  1.00 89.11           C  
ANISOU  370  CG  LEU A 107    12219  11214  10424   -548    565     60       C  
ATOM    371  CD1 LEU A 107       2.960  14.206   1.402  1.00 89.53           C  
ANISOU  371  CD1 LEU A 107    12205  11342  10470   -535    525     14       C  
ATOM    372  CD2 LEU A 107       3.955  12.126   2.362  1.00 97.26           C  
ANISOU  372  CD2 LEU A 107    13264  12232  11460   -622    622     46       C  
ATOM    373  N   VAL A 108       8.792  13.693   0.675  1.00102.12           N  
ANISOU  373  N   VAL A 108    14051  12643  12107   -481    555    193       N  
ATOM    374  CA  VAL A 108       9.868  13.895  -0.288  1.00100.43           C  
ANISOU  374  CA  VAL A 108    13875  12383  11902   -463    548    214       C  
ATOM    375  C   VAL A 108      10.503  12.561  -0.654  1.00100.16           C  
ANISOU  375  C   VAL A 108    13876  12299  11882   -513    590    214       C  
ATOM    376  O   VAL A 108      10.826  12.315  -1.822  1.00100.57           O  
ANISOU  376  O   VAL A 108    13946  12338  11928   -526    594    206       O  
ATOM    377  CB  VAL A 108      10.903  14.893   0.257  1.00102.20           C  
ANISOU  377  CB  VAL A 108    14119  12564  12147   -407    530    250       C  
ATOM    378  CG1 VAL A 108      11.243  14.543   1.653  1.00103.55           C  
ANISOU  378  CG1 VAL A 108    14299  12707  12337   -409    548    267       C  
ATOM    379  CG2 VAL A 108      12.159  14.891  -0.595  1.00 99.31           C  
ANISOU  379  CG2 VAL A 108    13794  12138  11800   -398    538    270       C  
ATOM    380  N   THR A 109      10.678  11.672   0.332  1.00 87.50           N  
ANISOU  380  N   THR A 109    12286  10664  10296   -541    622    223       N  
ATOM    381  CA  THR A 109      11.198  10.331   0.069  1.00 87.60           C  
ANISOU  381  CA  THR A 109    12330  10626  10328   -589    663    221       C  
ATOM    382  C   THR A 109      10.229   9.466  -0.735  1.00 88.02           C  
ANISOU  382  C   THR A 109    12365  10718  10362   -646    682    180       C  
ATOM    383  O   THR A 109      10.639   8.426  -1.258  1.00 88.14           O  
ANISOU  383  O   THR A 109    12405  10694  10392   -685    714    172       O  
ATOM    384  CB  THR A 109      11.568   9.651   1.392  1.00 87.58           C  
ANISOU  384  CB  THR A 109    12350  10579  10346   -600    687    245       C  
ATOM    385  OG1 THR A 109      10.461   9.728   2.300  1.00 89.48           O  
ANISOU  385  OG1 THR A 109    12563  10871  10564   -612    690    233       O  
ATOM    386  CG2 THR A 109      12.798  10.306   2.016  1.00 87.19           C  
ANISOU  386  CG2 THR A 109    12328  10477  10324   -548    668    284       C  
ATOM    387  N   THR A 110       8.966   9.880  -0.853  1.00 88.29           N  
ANISOU  387  N   THR A 110    12353  10827  10367   -649    662    149       N  
ATOM    388  CA  THR A 110       8.034   9.252  -1.782  1.00 88.73           C  
ANISOU  388  CA  THR A 110    12384  10927  10404   -696    668    103       C  
ATOM    389  C   THR A 110       8.453   9.470  -3.233  1.00 88.73           C  
ANISOU  389  C   THR A 110    12402  10924  10389   -688    650     96       C  
ATOM    390  O   THR A 110       8.162   8.637  -4.098  1.00 89.06           O  
ANISOU  390  O   THR A 110    12445  10973  10420   -735    666     63       O  
ATOM    391  CB  THR A 110       6.633   9.816  -1.535  1.00 89.04           C  
ANISOU  391  CB  THR A 110    12363  11047  10422   -692    643     71       C  
ATOM    392  OG1 THR A 110       6.151   9.340  -0.274  1.00 89.17           O  
ANISOU  392  OG1 THR A 110    12366  11067  10450   -717    675     69       O  
ATOM    393  CG2 THR A 110       5.655   9.414  -2.632  1.00 89.53           C  
ANISOU  393  CG2 THR A 110    12392  11163  10464   -728    632     19       C  
ATOM    394  N   THR A 111       9.141  10.572  -3.514  1.00103.15           N  
ANISOU  394  N   THR A 111    14245  12737  12210   -633    619    124       N  
ATOM    395  CA  THR A 111       9.539  10.945  -4.866  1.00101.42           C  
ANISOU  395  CA  THR A 111    14050  12516  11970   -622    602    121       C  
ATOM    396  C   THR A 111      10.835  10.276  -5.316  1.00103.50           C  
ANISOU  396  C   THR A 111    14364  12704  12258   -639    641    135       C  
ATOM    397  O   THR A 111      11.343  10.613  -6.390  1.00105.89           O  
ANISOU  397  O   THR A 111    14694  12994  12544   -630    636    137       O  
ATOM    398  CB  THR A 111       9.686  12.465  -4.962  1.00 97.98           C  
ANISOU  398  CB  THR A 111    13611  12095  11520   -555    555    146       C  
ATOM    399  OG1 THR A 111      10.841  12.881  -4.225  1.00 95.55           O  
ANISOU  399  OG1 THR A 111    13330  11727  11248   -521    566    187       O  
ATOM    400  CG2 THR A 111       8.461  13.145  -4.385  1.00100.37           C  
ANISOU  400  CG2 THR A 111    13860  12466  11809   -533    517    131       C  
ATOM    401  N   MET A 112      11.383   9.356  -4.528  1.00 94.63           N  
ANISOU  401  N   MET A 112    13254  11527  11174   -664    681    146       N  
ATOM    402  CA  MET A 112      12.627   8.682  -4.880  1.00 94.66           C  
ANISOU  402  CA  MET A 112    13300  11454  11212   -678    718    156       C  
ATOM    403  C   MET A 112      12.494   7.622  -5.978  1.00 98.59           C  
ANISOU  403  C   MET A 112    13811  11949  11700   -735    749    118       C  
ATOM    404  O   MET A 112      13.437   7.461  -6.764  1.00 96.65           O  
ANISOU  404  O   MET A 112    13599  11657  11468   -738    771    118       O  
ATOM    405  CB  MET A 112      13.247   8.066  -3.628  1.00 92.12           C  
ANISOU  405  CB  MET A 112    12990  11075  10938   -680    742    181       C  
ATOM    406  CG  MET A 112      13.360   9.042  -2.481  1.00 87.68           C  
ANISOU  406  CG  MET A 112    12417  10517  10382   -628    712    215       C  
ATOM    407  SD  MET A 112      14.825   8.753  -1.475  1.00 87.26           S  
ANISOU  407  SD  MET A 112    12396  10371  10388   -604    726    254       S  
ATOM    408  CE  MET A 112      16.091   8.569  -2.738  1.00 87.21           C  
ANISOU  408  CE  MET A 112    12420  10304  10413   -606    749    248       C  
ATOM    409  N   PRO A 113      11.388   6.864  -6.070  1.00117.10           N  
ANISOU  409  N   PRO A 113    16130  14337  14025   -782    756     81       N  
ATOM    410  CA  PRO A 113      11.269   5.925  -7.203  1.00119.77           C  
ANISOU  410  CA  PRO A 113    16481  14674  14352   -835    783     40       C  
ATOM    411  C   PRO A 113      11.241   6.628  -8.544  1.00119.23           C  
ANISOU  411  C   PRO A 113    16426  14640  14237   -821    756     26       C  
ATOM    412  O   PRO A 113      11.991   6.264  -9.460  1.00119.48           O  
ANISOU  412  O   PRO A 113    16494  14634  14269   -839    783     16       O  
ATOM    413  CB  PRO A 113       9.942   5.206  -6.925  1.00118.88           C  
ANISOU  413  CB  PRO A 113    16329  14613  14228   -882    787      2       C  
ATOM    414  CG  PRO A 113       9.713   5.367  -5.502  1.00117.30           C  
ANISOU  414  CG  PRO A 113    16110  14410  14048   -865    786     30       C  
ATOM    415  CD  PRO A 113      10.241   6.721  -5.161  1.00114.81           C  
ANISOU  415  CD  PRO A 113    15799  14095  13729   -796    748     70       C  
ATOM    416  N   PHE A 114      10.383   7.641  -8.674  1.00104.52           N  
ANISOU  416  N   PHE A 114    14535  12845  12332   -790    704     24       N  
ATOM    417  CA  PHE A 114      10.243   8.351  -9.938  1.00106.34           C  
ANISOU  417  CA  PHE A 114    14783  13112  12510   -774    670     14       C  
ATOM    418  C   PHE A 114      11.562   8.988 -10.352  1.00104.87           C  
ANISOU  418  C   PHE A 114    14645  12868  12330   -740    682     50       C  
ATOM    419  O   PHE A 114      11.943   8.943 -11.527  1.00105.83           O  
ANISOU  419  O   PHE A 114    14805  12982  12422   -754    693     37       O  
ATOM    420  CB  PHE A 114       9.156   9.424  -9.838  1.00108.63           C  
ANISOU  420  CB  PHE A 114    15033  13477  12763   -734    606     14       C  
ATOM    421  CG  PHE A 114       7.875   8.968  -9.177  1.00111.46           C  
ANISOU  421  CG  PHE A 114    15333  13890  13128   -760    595    -20       C  
ATOM    422  CD1 PHE A 114       7.812   8.729  -7.808  1.00109.79           C  
ANISOU  422  CD1 PHE A 114    15097  13661  12958   -761    618     -5       C  
ATOM    423  CD2 PHE A 114       6.731   8.775  -9.932  1.00112.58           C  
ANISOU  423  CD2 PHE A 114    15445  14100  13232   -785    564    -68       C  
ATOM    424  CE1 PHE A 114       6.635   8.320  -7.213  1.00109.54           C  
ANISOU  424  CE1 PHE A 114    15012  13678  12930   -789    616    -37       C  
ATOM    425  CE2 PHE A 114       5.548   8.365  -9.340  1.00111.06           C  
ANISOU  425  CE2 PHE A 114    15192  13956  13050   -811    559   -104       C  
ATOM    426  CZ  PHE A 114       5.502   8.136  -7.980  1.00109.44           C  
ANISOU  426  CZ  PHE A 114    14964  13732  12888   -815    589    -89       C  
ATOM    427  N   GLN A 115      12.270   9.592  -9.398  1.00102.32           N  
ANISOU  427  N   GLN A 115    14323  12506  12047   -698    683     91       N  
ATOM    428  CA  GLN A 115      13.559  10.193  -9.712  1.00104.13           C  
ANISOU  428  CA  GLN A 115    14593  12678  12294   -668    699    122       C  
ATOM    429  C   GLN A 115      14.617   9.132  -9.988  1.00105.05           C  
ANISOU  429  C   GLN A 115    14741  12722  12453   -705    760    111       C  
ATOM    430  O   GLN A 115      15.535   9.367 -10.784  1.00102.74           O  
ANISOU  430  O   GLN A 115    14486  12391  12161   -702    784    115       O  
ATOM    431  CB  GLN A 115      13.996  11.119  -8.574  1.00101.86           C  
ANISOU  431  CB  GLN A 115    14292  12368  12041   -612    680    164       C  
ATOM    432  CG  GLN A 115      13.556  12.570  -8.765  1.00104.68           C  
ANISOU  432  CG  GLN A 115    14643  12770  12362   -561    628    182       C  
ATOM    433  CD  GLN A 115      14.682  13.464  -9.246  1.00101.59           C  
ANISOU  433  CD  GLN A 115    14290  12330  11978   -527    636    211       C  
ATOM    434  OE1 GLN A 115      15.632  13.726  -8.512  1.00 99.14           O  
ANISOU  434  OE1 GLN A 115    13983  11966  11720   -502    651    236       O  
ATOM    435  NE2 GLN A 115      14.588  13.923 -10.490  1.00 99.08           N  
ANISOU  435  NE2 GLN A 115    14006  12032  11610   -527    626    207       N  
ATOM    436  N   SER A 116      14.507   7.965  -9.347  1.00132.29           N  
ANISOU  436  N   SER A 116    18175  16150  15939   -742    788     96       N  
ATOM    437  CA  SER A 116      15.457   6.888  -9.608  1.00130.72           C  
ANISOU  437  CA  SER A 116    18002  15881  15785   -778    844     83       C  
ATOM    438  C   SER A 116      15.179   6.215 -10.944  1.00131.50           C  
ANISOU  438  C   SER A 116    18120  15996  15846   -828    867     37       C  
ATOM    439  O   SER A 116      16.112   5.776 -11.626  1.00130.57           O  
ANISOU  439  O   SER A 116    18035  15826  15751   -847    911     24       O  
ATOM    440  CB  SER A 116      15.417   5.861  -8.483  1.00129.12           C  
ANISOU  440  CB  SER A 116    17782  15644  15632   -799    864     86       C  
ATOM    441  OG  SER A 116      15.998   4.643  -8.908  1.00138.21           O  
ANISOU  441  OG  SER A 116    18954  16739  16819   -843    916     61       O  
ATOM    442  N   THR A 117      13.900   6.107 -11.321  1.00 89.55           N  
ANISOU  442  N   THR A 117    12786  10758  10480   -851    839      8       N  
ATOM    443  CA  THR A 117      13.545   5.522 -12.612  1.00 90.06           C  
ANISOU  443  CA  THR A 117    12870  10848  10502   -898    853    -39       C  
ATOM    444  C   THR A 117      14.292   6.223 -13.734  1.00 90.15           C  
ANISOU  444  C   THR A 117    12928  10846  10479   -882    858    -34       C  
ATOM    445  O   THR A 117      14.990   5.585 -14.530  1.00 90.38           O  
ANISOU  445  O   THR A 117    12991  10834  10514   -916    907    -58       O  
ATOM    446  CB  THR A 117      12.035   5.634 -12.852  1.00 90.43           C  
ANISOU  446  CB  THR A 117    12882  10985  10492   -911    804    -69       C  
ATOM    447  OG1 THR A 117      11.336   4.688 -12.036  1.00 90.52           O  
ANISOU  447  OG1 THR A 117    12854  11004  10535   -947    817    -89       O  
ATOM    448  CG2 THR A 117      11.715   5.346 -14.309  1.00 91.00           C  
ANISOU  448  CG2 THR A 117    12980  11091  10505   -948    803   -114       C  
ATOM    449  N   VAL A 118      14.196   7.554 -13.770  1.00111.07           N  
ANISOU  449  N   VAL A 118    15582  13525  13094   -830    814      0       N  
ATOM    450  CA  VAL A 118      14.780   8.332 -14.856  1.00113.11           C  
ANISOU  450  CA  VAL A 118    15891  13776  13310   -815    816      9       C  
ATOM    451  C   VAL A 118      16.289   8.145 -14.907  1.00112.62           C  
ANISOU  451  C   VAL A 118    15860  13626  13304   -817    879     20       C  
ATOM    452  O   VAL A 118      16.891   8.212 -15.984  1.00113.37           O  
ANISOU  452  O   VAL A 118    16003  13701  13373   -833    912      8       O  
ATOM    453  CB  VAL A 118      14.381   9.817 -14.709  1.00112.72           C  
ANISOU  453  CB  VAL A 118    15837  13768  13224   -755    755     48       C  
ATOM    454  CG1 VAL A 118      15.417  10.734 -15.323  1.00112.99           C  
ANISOU  454  CG1 VAL A 118    15923  13761  13248   -727    773     77       C  
ATOM    455  CG2 VAL A 118      13.048  10.067 -15.356  1.00114.13           C  
ANISOU  455  CG2 VAL A 118    16006  14032  13327   -758    697     25       C  
ATOM    456  N   TYR A 119      16.927   7.887 -13.766  1.00112.57           N  
ANISOU  456  N   TYR A 119    15830  13566  13377   -801    898     41       N  
ATOM    457  CA  TYR A 119      18.374   7.709 -13.772  1.00111.77           C  
ANISOU  457  CA  TYR A 119    15750  13380  13339   -799    953     48       C  
ATOM    458  C   TYR A 119      18.752   6.514 -14.636  1.00115.43           C  
ANISOU  458  C   TYR A 119    16237  13810  13812   -858   1012      1       C  
ATOM    459  O   TYR A 119      19.417   6.655 -15.669  1.00116.04           O  
ANISOU  459  O   TYR A 119    16355  13864  13872   -872   1050    -14       O  
ATOM    460  CB  TYR A 119      18.914   7.481 -12.363  1.00108.98           C  
ANISOU  460  CB  TYR A 119    15364  12975  13068   -775    954     73       C  
ATOM    461  CG  TYR A 119      20.393   7.154 -12.348  1.00108.24           C  
ANISOU  461  CG  TYR A 119    15284  12790  13050   -774   1008     72       C  
ATOM    462  CD1 TYR A 119      21.258   7.720 -13.279  1.00109.38           C  
ANISOU  462  CD1 TYR A 119    15464  12906  13191   -770   1041     68       C  
ATOM    463  CD2 TYR A 119      20.916   6.245 -11.445  1.00108.79           C  
ANISOU  463  CD2 TYR A 119    15335  12801  13198   -779   1027     73       C  
ATOM    464  CE1 TYR A 119      22.602   7.422 -13.282  1.00110.45           C  
ANISOU  464  CE1 TYR A 119    15604  12958  13403   -771   1092     61       C  
ATOM    465  CE2 TYR A 119      22.262   5.934 -11.451  1.00110.58           C  
ANISOU  465  CE2 TYR A 119    15569  12945  13502   -776   1071     68       C  
ATOM    466  CZ  TYR A 119      23.100   6.530 -12.365  1.00110.17           C  
ANISOU  466  CZ  TYR A 119    15543  12867  13450   -772   1105     59       C  
ATOM    467  OH  TYR A 119      24.441   6.228 -12.367  1.00109.79           O  
ANISOU  467  OH  TYR A 119    15495  12734  13486   -769   1151     48       O  
ATOM    468  N   LEU A 120      18.334   5.327 -14.199  1.00113.74           N  
ANISOU  468  N   LEU A 120    15999  13591  13626   -893   1024    -24       N  
ATOM    469  CA  LEU A 120      18.686   4.108 -14.914  1.00112.53           C  
ANISOU  469  CA  LEU A 120    15864  13400  13492   -949   1081    -71       C  
ATOM    470  C   LEU A 120      18.047   4.089 -16.295  1.00113.68           C  
ANISOU  470  C   LEU A 120    16040  13602  13551   -986   1081   -110       C  
ATOM    471  O   LEU A 120      18.694   3.727 -17.285  1.00117.12           O  
ANISOU  471  O   LEU A 120    16512  14006  13981  -1017   1131   -142       O  
ATOM    472  CB  LEU A 120      18.250   2.893 -14.095  1.00113.22           C  
ANISOU  472  CB  LEU A 120    15920  13473  13626   -979   1089    -86       C  
ATOM    473  CG  LEU A 120      18.770   2.847 -12.653  1.00109.50           C  
ANISOU  473  CG  LEU A 120    15424  12950  13232   -943   1082    -45       C  
ATOM    474  CD1 LEU A 120      17.767   2.171 -11.721  1.00104.16           C  
ANISOU  474  CD1 LEU A 120    14717  12300  12560   -961   1062    -44       C  
ATOM    475  CD2 LEU A 120      20.132   2.169 -12.568  1.00108.55           C  
ANISOU  475  CD2 LEU A 120    15315  12731  13197   -948   1136    -51       C  
ATOM    476  N   MET A 121      16.783   4.498 -16.381  1.00137.28           N  
ANISOU  476  N   MET A 121    19014  16675  16471   -982   1022   -111       N  
ATOM    477  CA  MET A 121      16.036   4.408 -17.625  1.00143.53           C  
ANISOU  477  CA  MET A 121    19831  17527  17178  -1016   1009   -151       C  
ATOM    478  C   MET A 121      16.410   5.504 -18.605  1.00142.69           C  
ANISOU  478  C   MET A 121    19775  17433  17007   -992   1001   -135       C  
ATOM    479  O   MET A 121      16.207   5.334 -19.812  1.00143.94           O  
ANISOU  479  O   MET A 121    19974  17619  17098  -1025   1009   -170       O  
ATOM    480  CB  MET A 121      14.547   4.493 -17.330  1.00144.63           C  
ANISOU  480  CB  MET A 121    19930  17750  17274  -1015    944   -160       C  
ATOM    481  CG  MET A 121      13.649   4.068 -18.445  1.00148.26           C  
ANISOU  481  CG  MET A 121    20402  18272  17660  -1059    927   -213       C  
ATOM    482  SD  MET A 121      12.064   3.874 -17.642  1.00157.32           S  
ANISOU  482  SD  MET A 121    21478  19494  18803  -1062    867   -227       S  
ATOM    483  CE  MET A 121      12.004   2.095 -17.511  1.00156.08           C  
ANISOU  483  CE  MET A 121    21303  19299  18700  -1137    928   -282       C  
ATOM    484  N   ASN A 122      16.936   6.620 -18.101  1.00107.40           N  
ANISOU  484  N   ASN A 122    15308  12944  12554   -937    984    -82       N  
ATOM    485  CA  ASN A 122      17.304   7.774 -18.916  1.00107.43           C  
ANISOU  485  CA  ASN A 122    15362  12954  12501   -910    976    -58       C  
ATOM    486  C   ASN A 122      16.128   8.261 -19.754  1.00105.90           C  
ANISOU  486  C   ASN A 122    15187  12846  12202   -909    914    -67       C  
ATOM    487  O   ASN A 122      16.288   8.609 -20.923  1.00102.33           O  
ANISOU  487  O   ASN A 122    14795  12405  11681   -921    923    -75       O  
ATOM    488  CB  ASN A 122      18.518   7.470 -19.794  1.00108.41           C  
ANISOU  488  CB  ASN A 122    15538  13015  12638   -940   1055    -78       C  
ATOM    489  CG  ASN A 122      19.506   8.619 -19.829  1.00111.26           C  
ANISOU  489  CG  ASN A 122    15928  13332  13012   -900   1073    -36       C  
ATOM    490  OD1 ASN A 122      20.159   8.918 -18.826  1.00112.31           O  
ANISOU  490  OD1 ASN A 122    16030  13419  13224   -865   1079     -6       O  
ATOM    491  ND2 ASN A 122      19.624   9.268 -20.983  1.00108.36           N  
ANISOU  491  ND2 ASN A 122    15624  12979  12567   -905   1082    -34       N  
ATOM    492  N   SER A 123      14.942   8.271 -19.148  1.00103.13           N  
ANISOU  492  N   SER A 123    14786  12558  11842   -896    851    -68       N  
ATOM    493  CA  SER A 123      13.710   8.803 -19.726  1.00104.55           C  
ANISOU  493  CA  SER A 123    14967  12823  11935   -885    777    -76       C  
ATOM    494  C   SER A 123      12.623   8.673 -18.663  1.00103.60           C  
ANISOU  494  C   SER A 123    14771  12749  11843   -871    726    -79       C  
ATOM    495  O   SER A 123      12.821   8.035 -17.625  1.00101.27           O  
ANISOU  495  O   SER A 123    14436  12421  11624   -881    756    -78       O  
ATOM    496  CB  SER A 123      13.300   8.084 -21.013  1.00107.04           C  
ANISOU  496  CB  SER A 123    15318  13171  12179   -939    783   -130       C  
ATOM    497  OG  SER A 123      11.927   8.287 -21.293  1.00108.01           O  
ANISOU  497  OG  SER A 123    15418  13381  12240   -933    704   -149       O  
ATOM    498  N   TRP A 124      11.459   9.264 -18.945  1.00104.20           N  
ANISOU  498  N   TRP A 124    14831  12902  11858   -850    650    -83       N  
ATOM    499  CA  TRP A 124      10.355   9.381 -17.988  1.00106.95           C  
ANISOU  499  CA  TRP A 124    15106  13301  12229   -830    598    -86       C  
ATOM    500  C   TRP A 124       9.118   8.639 -18.483  1.00108.59           C  
ANISOU  500  C   TRP A 124    15284  13578  12399   -871    564   -146       C  
ATOM    501  O   TRP A 124       8.253   9.226 -19.153  1.00106.84           O  
ANISOU  501  O   TRP A 124    15063  13421  12111   -852    494   -156       O  
ATOM    502  CB  TRP A 124      10.036  10.853 -17.729  1.00110.63           C  
ANISOU  502  CB  TRP A 124    15567  13795  12673   -760    533    -40       C  
ATOM    503  CG  TRP A 124       8.918  11.078 -16.756  1.00110.51           C  
ANISOU  503  CG  TRP A 124    15475  13832  12681   -736    481    -44       C  
ATOM    504  CD1 TRP A 124       7.618  11.361 -17.064  1.00109.94           C  
ANISOU  504  CD1 TRP A 124    15368  13839  12566   -725    409    -71       C  
ATOM    505  CD2 TRP A 124       8.992  11.053 -15.324  1.00109.03           C  
ANISOU  505  CD2 TRP A 124    15237  13622  12566   -720    498    -25       C  
ATOM    506  NE1 TRP A 124       6.879  11.508 -15.918  1.00108.99           N  
ANISOU  506  NE1 TRP A 124    15175  13746  12491   -705    385    -72       N  
ATOM    507  CE2 TRP A 124       7.698  11.324 -14.835  1.00109.39           C  
ANISOU  507  CE2 TRP A 124    15219  13736  12608   -703    440    -43       C  
ATOM    508  CE3 TRP A 124      10.022  10.827 -14.409  1.00104.33           C  
ANISOU  508  CE3 TRP A 124    14646  12958  12038   -718    554      4       C  
ATOM    509  CZ2 TRP A 124       7.410  11.373 -13.475  1.00107.56           C  
ANISOU  509  CZ2 TRP A 124    14931  13504  12432   -688    444    -32       C  
ATOM    510  CZ3 TRP A 124       9.734  10.875 -13.060  1.00104.84           C  
ANISOU  510  CZ3 TRP A 124    14658  13022  12154   -700    550     17       C  
ATOM    511  CH2 TRP A 124       8.440  11.148 -12.607  1.00107.13           C  
ANISOU  511  CH2 TRP A 124    14889  13381  12434   -687    499     -1       C  
ATOM    512  N   PRO A 125       8.961   7.363 -18.129  1.00136.45           N  
ANISOU  512  N   PRO A 125    18780  17095  15971   -926    606   -187       N  
ATOM    513  CA  PRO A 125       7.861   6.556 -18.669  1.00140.75           C  
ANISOU  513  CA  PRO A 125    19296  17699  16485   -974    582   -252       C  
ATOM    514  C   PRO A 125       6.514   6.771 -17.995  1.00141.27           C  
ANISOU  514  C   PRO A 125    19284  17833  16559   -959    522   -268       C  
ATOM    515  O   PRO A 125       5.577   6.021 -18.286  1.00138.64           O  
ANISOU  515  O   PRO A 125    18915  17546  16215  -1002    507   -327       O  
ATOM    516  CB  PRO A 125       8.362   5.130 -18.406  1.00138.86           C  
ANISOU  516  CB  PRO A 125    19054  17405  16304  -1036    662   -283       C  
ATOM    517  CG  PRO A 125       9.019   5.277 -17.078  1.00135.80           C  
ANISOU  517  CG  PRO A 125    18647  16960  15992  -1008    695   -234       C  
ATOM    518  CD  PRO A 125       9.807   6.566 -17.222  1.00135.59           C  
ANISOU  518  CD  PRO A 125    18661  16911  15944   -948    678   -177       C  
ATOM    519  N   PHE A 126       6.386   7.748 -17.098  1.00130.43           N  
ANISOU  519  N   PHE A 126    17882  16466  15209   -901    491   -223       N  
ATOM    520  CA  PHE A 126       5.173   7.905 -16.307  1.00130.49           C  
ANISOU  520  CA  PHE A 126    17811  16531  15238   -889    447   -241       C  
ATOM    521  C   PHE A 126       4.213   8.955 -16.850  1.00131.74           C  
ANISOU  521  C   PHE A 126    17951  16764  15340   -843    354   -246       C  
ATOM    522  O   PHE A 126       3.115   9.105 -16.301  1.00131.20           O  
ANISOU  522  O   PHE A 126    17811  16749  15290   -833    313   -270       O  
ATOM    523  CB  PHE A 126       5.530   8.237 -14.851  1.00127.75           C  
ANISOU  523  CB  PHE A 126    17436  16146  14956   -858    472   -196       C  
ATOM    524  CG  PHE A 126       6.551   7.312 -14.250  1.00127.61           C  
ANISOU  524  CG  PHE A 126    17441  16050  14996   -893    554   -182       C  
ATOM    525  CD1 PHE A 126       6.217   6.003 -13.930  1.00126.47           C  
ANISOU  525  CD1 PHE A 126    17270  15898  14887   -956    599   -224       C  
ATOM    526  CD2 PHE A 126       7.840   7.747 -14.002  1.00125.15           C  
ANISOU  526  CD2 PHE A 126    17175  15670  14706   -862    586   -130       C  
ATOM    527  CE1 PHE A 126       7.152   5.146 -13.377  1.00121.27           C  
ANISOU  527  CE1 PHE A 126    16633  15161  14281   -984    669   -210       C  
ATOM    528  CE2 PHE A 126       8.778   6.894 -13.448  1.00125.20           C  
ANISOU  528  CE2 PHE A 126    17199  15602  14768   -890    655   -119       C  
ATOM    529  CZ  PHE A 126       8.434   5.591 -13.136  1.00119.67           C  
ANISOU  529  CZ  PHE A 126    16475  14892  14101   -949    695   -157       C  
ATOM    530  N   GLY A 127       4.584   9.676 -17.905  1.00137.95           N  
ANISOU  530  N   GLY A 127    18800  17553  16062   -815    320   -225       N  
ATOM    531  CA  GLY A 127       3.664  10.600 -18.537  1.00141.06           C  
ANISOU  531  CA  GLY A 127    19185  18015  16397   -771    226   -230       C  
ATOM    532  C   GLY A 127       3.656  11.985 -17.920  1.00136.51           C  
ANISOU  532  C   GLY A 127    18597  17439  15833   -694    183   -175       C  
ATOM    533  O   GLY A 127       4.437  12.328 -17.028  1.00134.35           O  
ANISOU  533  O   GLY A 127    18328  17112  15608   -671    225   -129       O  
ATOM    534  N   ASP A 128       2.726  12.800 -18.421  1.00118.98           N  
ANISOU  534  N   ASP A 128    16360  15280  13568   -651     92   -182       N  
ATOM    535  CA  ASP A 128       2.657  14.208 -18.042  1.00119.84           C  
ANISOU  535  CA  ASP A 128    16464  15391  13679   -573     41   -132       C  
ATOM    536  C   ASP A 128       2.012  14.392 -16.673  1.00120.05           C  
ANISOU  536  C   ASP A 128    16400  15435  13778   -553     36   -139       C  
ATOM    537  O   ASP A 128       2.617  14.968 -15.762  1.00119.29           O  
ANISOU  537  O   ASP A 128    16303  15296  13725   -520     65    -93       O  
ATOM    538  CB  ASP A 128       1.881  14.996 -19.101  1.00121.02           C  
ANISOU  538  CB  ASP A 128    16631  15596  13755   -532    -60   -137       C  
ATOM    539  CG  ASP A 128       2.598  16.259 -19.528  1.00116.81           C  
ANISOU  539  CG  ASP A 128    16175  15027  13182   -472    -82    -68       C  
ATOM    540  OD1 ASP A 128       3.807  16.382 -19.245  1.00114.83           O  
ANISOU  540  OD1 ASP A 128    15974  14706  12951   -474    -12    -23       O  
ATOM    541  OD2 ASP A 128       1.949  17.134 -20.134  1.00118.01           O  
ANISOU  541  OD2 ASP A 128    16336  15217  13284   -422   -171    -59       O  
ATOM    542  N   VAL A 129       0.780  13.901 -16.514  1.00112.07           N  
ANISOU  542  N   VAL A 129    15311  14488  12784   -574      3   -200       N  
ATOM    543  CA  VAL A 129       0.033  14.131 -15.279  1.00110.15           C  
ANISOU  543  CA  VAL A 129    14979  14270  12605   -556     -4   -213       C  
ATOM    544  C   VAL A 129       0.791  13.579 -14.074  1.00110.03           C  
ANISOU  544  C   VAL A 129    14958  14196  12651   -584     88   -192       C  
ATOM    545  O   VAL A 129       0.820  14.202 -13.007  1.00109.56           O  
ANISOU  545  O   VAL A 129    14868  14125  12634   -548     95   -166       O  
ATOM    546  CB  VAL A 129      -1.389  13.545 -15.399  1.00108.57           C  
ANISOU  546  CB  VAL A 129    14694  14145  12413   -586    -45   -292       C  
ATOM    547  CG1 VAL A 129      -1.340  12.079 -15.786  1.00118.20           C  
ANISOU  547  CG1 VAL A 129    15920  15362  13630   -670      9   -340       C  
ATOM    548  CG2 VAL A 129      -2.151  13.717 -14.093  1.00105.82           C  
ANISOU  548  CG2 VAL A 129    14252  13820  12134   -574    -39   -311       C  
ATOM    549  N   LEU A 130       1.436  12.419 -14.226  1.00122.02           N  
ANISOU  549  N   LEU A 130    16511  15676  14174   -648    158   -203       N  
ATOM    550  CA  LEU A 130       2.253  11.898 -13.135  1.00121.09           C  
ANISOU  550  CA  LEU A 130    16399  15496  14112   -670    240   -177       C  
ATOM    551  C   LEU A 130       3.569  12.652 -12.980  1.00120.00           C  
ANISOU  551  C   LEU A 130    16326  15292  13976   -628    262   -109       C  
ATOM    552  O   LEU A 130       4.204  12.548 -11.925  1.00119.87           O  
ANISOU  552  O   LEU A 130    16309  15228  14008   -627    311    -80       O  
ATOM    553  CB  LEU A 130       2.535  10.409 -13.331  1.00121.79           C  
ANISOU  553  CB  LEU A 130    16502  15559  14212   -749    306   -212       C  
ATOM    554  CG  LEU A 130       2.581   9.622 -12.018  1.00117.20           C  
ANISOU  554  CG  LEU A 130    15887  14948  13697   -784    371   -215       C  
ATOM    555  CD1 LEU A 130       1.193   9.538 -11.399  1.00117.72           C  
ANISOU  555  CD1 LEU A 130    15865  15078  13786   -795    347   -262       C  
ATOM    556  CD2 LEU A 130       3.169   8.236 -12.214  1.00118.82           C  
ANISOU  556  CD2 LEU A 130    16124  15106  13918   -853    442   -233       C  
ATOM    557  N   CYS A 131       4.009  13.383 -14.006  1.00112.49           N  
ANISOU  557  N   CYS A 131    15434  14334  12972   -596    228    -82       N  
ATOM    558  CA  CYS A 131       5.160  14.259 -13.825  1.00111.52           C  
ANISOU  558  CA  CYS A 131    15364  14151  12856   -552    246    -19       C  
ATOM    559  C   CYS A 131       4.775  15.538 -13.096  1.00113.39           C  
ANISOU  559  C   CYS A 131    15566  14405  13111   -483    197     10       C  
ATOM    560  O   CYS A 131       5.586  16.088 -12.343  1.00115.78           O  
ANISOU  560  O   CYS A 131    15882  14658  13449   -453    224     53       O  
ATOM    561  CB  CYS A 131       5.798  14.594 -15.174  1.00111.99           C  
ANISOU  561  CB  CYS A 131    15505  14192  12853   -546    236      0       C  
ATOM    562  SG  CYS A 131       6.819  16.091 -15.182  1.00108.39           S  
ANISOU  562  SG  CYS A 131    15108  13683  12392   -477    229     73       S  
ATOM    563  N   LYS A 132       3.549  16.020 -13.306  1.00145.73           N  
ANISOU  563  N   LYS A 132    19614  18570  17188   -457    125    -18       N  
ATOM    564  CA  LYS A 132       3.108  17.244 -12.648  1.00145.31           C  
ANISOU  564  CA  LYS A 132    19522  18534  17155   -390     76      4       C  
ATOM    565  C   LYS A 132       3.003  17.055 -11.139  1.00143.97           C  
ANISOU  565  C   LYS A 132    19294  18356  17051   -395    116      0       C  
ATOM    566  O   LYS A 132       3.538  17.857 -10.365  1.00143.38           O  
ANISOU  566  O   LYS A 132    19225  18248  17006   -352    125     39       O  
ATOM    567  CB  LYS A 132       1.768  17.697 -13.229  1.00143.79           C  
ANISOU  567  CB  LYS A 132    19283  18416  16932   -363    -12    -32       C  
ATOM    568  N   ILE A 133       2.324  15.992 -10.701  1.00106.87           N  
ANISOU  568  N   ILE A 133    14544  13687  12376   -448    143    -49       N  
ATOM    569  CA  ILE A 133       2.098  15.792  -9.272  1.00107.35           C  
ANISOU  569  CA  ILE A 133    14552  13745  12492   -456    181    -56       C  
ATOM    570  C   ILE A 133       3.404  15.464  -8.555  1.00105.73           C  
ANISOU  570  C   ILE A 133    14394  13464  12315   -469    250    -13       C  
ATOM    571  O   ILE A 133       3.631  15.907  -7.424  1.00104.61           O  
ANISOU  571  O   ILE A 133    14236  13303  12208   -444    267     10       O  
ATOM    572  CB  ILE A 133       1.033  14.704  -9.040  1.00108.85           C  
ANISOU  572  CB  ILE A 133    14678  13983  12698   -516    197   -120       C  
ATOM    573  CG1 ILE A 133      -0.139  14.874 -10.013  1.00108.76           C  
ANISOU  573  CG1 ILE A 133    14625  14042  12655   -509    125   -169       C  
ATOM    574  CG2 ILE A 133       0.545  14.741  -7.598  1.00108.74           C  
ANISOU  574  CG2 ILE A 133    14603  13979  12733   -516    225   -130       C  
ATOM    575  CD1 ILE A 133      -1.212  15.840  -9.542  1.00109.11           C  
ANISOU  575  CD1 ILE A 133    14595  14142  12721   -458     66   -189       C  
ATOM    576  N   VAL A 134       4.275  14.673  -9.185  1.00115.50           N  
ANISOU  576  N   VAL A 134    15689  14657  13539   -508    291     -4       N  
ATOM    577  CA  VAL A 134       5.575  14.386  -8.582  1.00115.67           C  
ANISOU  577  CA  VAL A 134    15755  14603  13591   -516    351     35       C  
ATOM    578  C   VAL A 134       6.399  15.663  -8.474  1.00114.09           C  
ANISOU  578  C   VAL A 134    15588  14367  13394   -452    332     87       C  
ATOM    579  O   VAL A 134       7.043  15.923  -7.450  1.00111.46           O  
ANISOU  579  O   VAL A 134    15257  13994  13100   -432    357    116       O  
ATOM    580  CB  VAL A 134       6.307  13.293  -9.383  1.00117.65           C  
ANISOU  580  CB  VAL A 134    16056  14815  13832   -570    397     27       C  
ATOM    581  CG1 VAL A 134       7.818  13.437  -9.254  1.00117.37           C  
ANISOU  581  CG1 VAL A 134    16078  14698  13818   -556    438     74       C  
ATOM    582  CG2 VAL A 134       5.860  11.925  -8.916  1.00114.81           C  
ANISOU  582  CG2 VAL A 134    15667  14460  13497   -635    441    -11       C  
ATOM    583  N   LEU A 135       6.383  16.484  -9.525  1.00107.17           N  
ANISOU  583  N   LEU A 135    14740  13504  12476   -418    287     99       N  
ATOM    584  CA  LEU A 135       7.010  17.797  -9.437  1.00107.77           C  
ANISOU  584  CA  LEU A 135    14843  13548  12555   -356    265    146       C  
ATOM    585  C   LEU A 135       6.338  18.662  -8.377  1.00106.12           C  
ANISOU  585  C   LEU A 135    14578  13369  12376   -309    232    147       C  
ATOM    586  O   LEU A 135       7.011  19.454  -7.707  1.00106.96           O  
ANISOU  586  O   LEU A 135    14694  13436  12509   -270    238    182       O  
ATOM    587  CB  LEU A 135       6.977  18.484 -10.801  1.00106.60           C  
ANISOU  587  CB  LEU A 135    14741  13412  12351   -331    221    157       C  
ATOM    588  CG  LEU A 135       8.160  18.214 -11.733  1.00106.09           C  
ANISOU  588  CG  LEU A 135    14755  13291  12264   -354    262    179       C  
ATOM    589  CD1 LEU A 135       8.236  19.309 -12.764  1.00105.73           C  
ANISOU  589  CD1 LEU A 135    14759  13246  12167   -312    218    207       C  
ATOM    590  CD2 LEU A 135       9.468  18.128 -10.962  1.00104.92           C  
ANISOU  590  CD2 LEU A 135    14628  13068  12169   -356    324    209       C  
ATOM    591  N   SER A 136       5.021  18.528  -8.206  1.00 91.72           N  
ANISOU  591  N   SER A 136    12690  11612  10548   -314    198    106       N  
ATOM    592  CA  SER A 136       4.349  19.222  -7.113  1.00 90.56           C  
ANISOU  592  CA  SER A 136    12482  11493  10433   -277    177     99       C  
ATOM    593  C   SER A 136       4.801  18.679  -5.763  1.00 91.19           C  
ANISOU  593  C   SER A 136    12551  11541  10556   -301    236    104       C  
ATOM    594  O   SER A 136       5.220  19.440  -4.889  1.00 90.18           O  
ANISOU  594  O   SER A 136    12421  11388  10455   -262    239    131       O  
ATOM    595  CB  SER A 136       2.830  19.103  -7.260  1.00 90.70           C  
ANISOU  595  CB  SER A 136    12429  11589  10443   -283    133     45       C  
ATOM    596  OG  SER A 136       2.178  19.175  -6.000  1.00 90.77           O  
ANISOU  596  OG  SER A 136    12373  11623  10492   -280    145     23       O  
ATOM    597  N   ILE A 137       4.762  17.357  -5.589  1.00108.67           N  
ANISOU  597  N   ILE A 137    14762  13752  12776   -365    284     81       N  
ATOM    598  CA  ILE A 137       5.056  16.761  -4.288  1.00107.49           C  
ANISOU  598  CA  ILE A 137    14603  13576  12662   -390    336     85       C  
ATOM    599  C   ILE A 137       6.489  17.064  -3.868  1.00106.55           C  
ANISOU  599  C   ILE A 137    14539  13384  12563   -367    362    135       C  
ATOM    600  O   ILE A 137       6.752  17.438  -2.719  1.00106.83           O  
ANISOU  600  O   ILE A 137    14564  13401  12624   -346    373    152       O  
ATOM    601  CB  ILE A 137       4.794  15.244  -4.327  1.00107.83           C  
ANISOU  601  CB  ILE A 137    14643  13622  12707   -465    383     54       C  
ATOM    602  CG1 ILE A 137       3.296  14.967  -4.427  1.00107.83           C  
ANISOU  602  CG1 ILE A 137    14575  13696  12699   -489    363     -3       C  
ATOM    603  CG2 ILE A 137       5.393  14.559  -3.105  1.00102.65           C  
ANISOU  603  CG2 ILE A 137    14002  12919  12082   -490    440     72       C  
ATOM    604  CD1 ILE A 137       2.937  13.526  -4.228  1.00102.39           C  
ANISOU  604  CD1 ILE A 137    13874  13009  12019   -564    414    -37       C  
ATOM    605  N   ASP A 138       7.436  16.908  -4.795  1.00122.72           N  
ANISOU  605  N   ASP A 138    16642  15388  14600   -373    373    156       N  
ATOM    606  CA  ASP A 138       8.846  16.965  -4.424  1.00122.00           C  
ANISOU  606  CA  ASP A 138    16597  15222  14536   -362    405    196       C  
ATOM    607  C   ASP A 138       9.275  18.397  -4.111  1.00124.09           C  
ANISOU  607  C   ASP A 138    16866  15470  14813   -296    374    228       C  
ATOM    608  O   ASP A 138       9.907  18.652  -3.079  1.00126.59           O  
ANISOU  608  O   ASP A 138    17185  15751  15162   -277    389    248       O  
ATOM    609  CB  ASP A 138       9.693  16.347  -5.540  1.00121.04           C  
ANISOU  609  CB  ASP A 138    16528  15059  14403   -392    432    201       C  
ATOM    610  CG  ASP A 138      11.169  16.651  -5.402  1.00123.27           C  
ANISOU  610  CG  ASP A 138    16854  15265  14716   -371    457    239       C  
ATOM    611  OD1 ASP A 138      11.651  16.839  -4.261  1.00119.99           O  
ANISOU  611  OD1 ASP A 138    16432  14820  14338   -352    467    257       O  
ATOM    612  OD2 ASP A 138      11.856  16.675  -6.443  1.00124.86           O  
ANISOU  612  OD2 ASP A 138    17099  15436  14905   -377    469    247       O  
ATOM    613  N   TYR A 139       8.946  19.346  -4.991  1.00114.29           N  
ANISOU  613  N   TYR A 139    15629  14253  13544   -260    330    232       N  
ATOM    614  CA  TYR A 139       9.116  20.762  -4.673  1.00114.95           C  
ANISOU  614  CA  TYR A 139    15709  14327  13640   -196    297    257       C  
ATOM    615  C   TYR A 139       8.395  21.153  -3.384  1.00114.81           C  
ANISOU  615  C   TYR A 139    15636  14343  13645   -175    284    243       C  
ATOM    616  O   TYR A 139       9.014  21.652  -2.439  1.00112.84           O  
ANISOU  616  O   TYR A 139    15389  14060  13427   -148    294    263       O  
ATOM    617  CB  TYR A 139       8.622  21.612  -5.848  1.00116.86           C  
ANISOU  617  CB  TYR A 139    15962  14596  13842   -165    246    261       C  
ATOM    618  CG  TYR A 139       9.653  21.915  -6.912  1.00118.30           C  
ANISOU  618  CG  TYR A 139    16212  14728  14007   -159    257    292       C  
ATOM    619  CD1 TYR A 139      10.990  21.610  -6.722  1.00117.74           C  
ANISOU  619  CD1 TYR A 139    16181  14588  13967   -175    308    314       C  
ATOM    620  CD2 TYR A 139       9.280  22.467  -8.128  1.00118.98           C  
ANISOU  620  CD2 TYR A 139    16325  14834  14046   -142    217    298       C  
ATOM    621  CE1 TYR A 139      11.928  21.901  -7.693  1.00117.13           C  
ANISOU  621  CE1 TYR A 139    16164  14464  13878   -173    326    338       C  
ATOM    622  CE2 TYR A 139      10.214  22.738  -9.111  1.00117.09           C  
ANISOU  622  CE2 TYR A 139    16154  14547  13786   -141    234    326       C  
ATOM    623  CZ  TYR A 139      11.540  22.448  -8.887  1.00116.24           C  
ANISOU  623  CZ  TYR A 139    16081  14372  13713   -159    292    344       C  
ATOM    624  OH  TYR A 139      12.482  22.716  -9.854  1.00116.20           O  
ANISOU  624  OH  TYR A 139    16142  14318  13691   -163    317    368       O  
ATOM    625  N   TYR A 140       7.083  20.907  -3.327  1.00109.84           N  
ANISOU  625  N   TYR A 140    14954  13778  13001   -187    263    205       N  
ATOM    626  CA  TYR A 140       6.252  21.396  -2.229  1.00109.27           C  
ANISOU  626  CA  TYR A 140    14824  13745  12948   -165    250    185       C  
ATOM    627  C   TYR A 140       6.775  20.955  -0.869  1.00109.08           C  
ANISOU  627  C   TYR A 140    14803  13692  12952   -182    295    193       C  
ATOM    628  O   TYR A 140       6.873  21.763   0.060  1.00110.11           O  
ANISOU  628  O   TYR A 140    14919  13816  13103   -144    288    201       O  
ATOM    629  CB  TYR A 140       4.814  20.929  -2.450  1.00110.23           C  
ANISOU  629  CB  TYR A 140    14889  13939  13055   -190    232    136       C  
ATOM    630  CG  TYR A 140       3.817  21.309  -1.392  1.00110.69           C  
ANISOU  630  CG  TYR A 140    14880  14043  13134   -176    225    105       C  
ATOM    631  CD1 TYR A 140       3.851  22.542  -0.778  1.00113.51           C  
ANISOU  631  CD1 TYR A 140    15221  14396  13511   -117    200    116       C  
ATOM    632  CD2 TYR A 140       2.792  20.440  -1.052  1.00116.35           C  
ANISOU  632  CD2 TYR A 140    15547  14808  13852   -223    245     58       C  
ATOM    633  CE1 TYR A 140       2.924  22.880   0.187  1.00115.58           C  
ANISOU  633  CE1 TYR A 140    15422  14701  13794   -106    198     82       C  
ATOM    634  CE2 TYR A 140       1.858  20.772  -0.098  1.00118.33           C  
ANISOU  634  CE2 TYR A 140    15735  15101  14123   -214    246     24       C  
ATOM    635  CZ  TYR A 140       1.924  21.996   0.517  1.00117.62           C  
ANISOU  635  CZ  TYR A 140    15631  15007  14053   -154    222     36       C  
ATOM    636  OH  TYR A 140       0.989  22.332   1.470  1.00120.45           O  
ANISOU  636  OH  TYR A 140    15925  15407  14432   -147    227     -2       O  
ATOM    637  N   ASN A 141       7.115  19.681  -0.728  1.00 94.20           N  
ANISOU  637  N   ASN A 141    12939  11786  11067   -238    340    190       N  
ATOM    638  CA  ASN A 141       7.567  19.171   0.555  1.00 92.11           C  
ANISOU  638  CA  ASN A 141    12682  11493  10823   -256    380    199       C  
ATOM    639  C   ASN A 141       9.082  19.157   0.680  1.00 90.71           C  
ANISOU  639  C   ASN A 141    12559  11239  10666   -245    398    240       C  
ATOM    640  O   ASN A 141       9.607  18.628   1.663  1.00 90.58           O  
ANISOU  640  O   ASN A 141    12559  11190  10666   -260    426    251       O  
ATOM    641  CB  ASN A 141       6.977  17.788   0.807  1.00 88.84           C  
ANISOU  641  CB  ASN A 141    12256  11098  10402   -322    420    173       C  
ATOM    642  CG  ASN A 141       5.464  17.812   0.829  1.00 92.10           C  
ANISOU  642  CG  ASN A 141    12605  11585  10802   -334    406    126       C  
ATOM    643  OD1 ASN A 141       4.838  18.568   0.096  1.00 94.72           O  
ANISOU  643  OD1 ASN A 141    12908  11957  11126   -304    361    111       O  
ATOM    644  ND2 ASN A 141       4.870  17.025   1.714  1.00 95.12           N  
ANISOU  644  ND2 ASN A 141    12966  11987  11189   -377    444    104       N  
ATOM    645  N   MET A 142       9.798  19.718  -0.292  1.00 97.11           N  
ANISOU  645  N   MET A 142    13400  12019  11477   -220    381    260       N  
ATOM    646  CA  MET A 142      11.144  20.178   0.013  1.00 99.33           C  
ANISOU  646  CA  MET A 142    13718  12234  11788   -192    389    294       C  
ATOM    647  C   MET A 142      11.074  21.476   0.804  1.00100.64           C  
ANISOU  647  C   MET A 142    13862  12407  11969   -136    360    301       C  
ATOM    648  O   MET A 142      11.690  21.607   1.866  1.00 99.56           O  
ANISOU  648  O   MET A 142    13731  12239  11856   -123    369    312       O  
ATOM    649  CB  MET A 142      11.957  20.390  -1.263  1.00 99.65           C  
ANISOU  649  CB  MET A 142    13799  12236  11826   -186    389    312       C  
ATOM    650  CG  MET A 142      13.100  21.380  -1.064  1.00 97.59           C  
ANISOU  650  CG  MET A 142    13561  11920  11598   -142    384    340       C  
ATOM    651  SD  MET A 142      13.877  21.943  -2.584  1.00 94.64           S  
ANISOU  651  SD  MET A 142    13233  11507  11217   -130    386    360       S  
ATOM    652  CE  MET A 142      12.426  22.322  -3.564  1.00 96.41           C  
ANISOU  652  CE  MET A 142    13440  11806  11385   -124    343    344       C  
ATOM    653  N   PHE A 143      10.302  22.439   0.301  1.00129.91           N  
ANISOU  653  N   PHE A 143    17544  16154  15661   -102    321    292       N  
ATOM    654  CA  PHE A 143      10.132  23.708   0.999  1.00129.19           C  
ANISOU  654  CA  PHE A 143    17429  16070  15586    -48    293    294       C  
ATOM    655  C   PHE A 143       9.511  23.508   2.375  1.00129.21           C  
ANISOU  655  C   PHE A 143    17396  16106  15595    -55    304    272       C  
ATOM    656  O   PHE A 143       9.971  24.095   3.360  1.00128.78           O  
ANISOU  656  O   PHE A 143    17340  16029  15560    -27    303    280       O  
ATOM    657  CB  PHE A 143       9.286  24.643   0.138  1.00128.67           C  
ANISOU  657  CB  PHE A 143    17341  16043  15503    -12    248    287       C  
ATOM    658  CG  PHE A 143      10.092  25.456  -0.825  1.00127.72           C  
ANISOU  658  CG  PHE A 143    17264  15879  15386     19    232    318       C  
ATOM    659  CD1 PHE A 143      11.122  26.259  -0.372  1.00128.54           C  
ANISOU  659  CD1 PHE A 143    17390  15928  15524     53    237    343       C  
ATOM    660  CD2 PHE A 143       9.888  25.346  -2.187  1.00129.72           C  
ANISOU  660  CD2 PHE A 143    17540  16141  15606     10    218    323       C  
ATOM    661  CE1 PHE A 143      11.880  27.003  -1.255  1.00128.60           C  
ANISOU  661  CE1 PHE A 143    17438  15890  15535     78    231    371       C  
ATOM    662  CE2 PHE A 143      10.660  26.072  -3.082  1.00131.32           C  
ANISOU  662  CE2 PHE A 143    17791  16299  15806     35    211    354       C  
ATOM    663  CZ  PHE A 143      11.658  26.903  -2.614  1.00129.11           C  
ANISOU  663  CZ  PHE A 143    17530  15963  15563     68    220    379       C  
ATOM    664  N   THR A 144       8.487  22.658   2.469  1.00106.74           N  
ANISOU  664  N   THR A 144    14520  13309  12729    -96    317    242       N  
ATOM    665  CA  THR A 144       7.837  22.438   3.756  1.00108.17           C  
ANISOU  665  CA  THR A 144    14669  13521  12910   -109    335    220       C  
ATOM    666  C   THR A 144       8.799  21.817   4.763  1.00105.79           C  
ANISOU  666  C   THR A 144    14406  13172  12619   -128    368    241       C  
ATOM    667  O   THR A 144       8.765  22.152   5.953  1.00103.00           O  
ANISOU  667  O   THR A 144    14044  12822  12269   -115    374    237       O  
ATOM    668  CB  THR A 144       6.604  21.552   3.583  1.00111.10           C  
ANISOU  668  CB  THR A 144    15002  13949  13261   -157    350    182       C  
ATOM    669  OG1 THR A 144       5.688  22.184   2.683  1.00111.62           O  
ANISOU  669  OG1 THR A 144    15028  14062  13321   -133    309    159       O  
ATOM    670  CG2 THR A 144       5.907  21.382   4.907  1.00111.95           C  
ANISOU  670  CG2 THR A 144    15078  14088  13368   -173    375    156       C  
ATOM    671  N   SER A 145       9.663  20.906   4.308  1.00 94.81           N  
ANISOU  671  N   SER A 145    13058  11735  11231   -159    390    262       N  
ATOM    672  CA  SER A 145      10.624  20.300   5.225  1.00 95.10           C  
ANISOU  672  CA  SER A 145    13133  11721  11280   -173    415    284       C  
ATOM    673  C   SER A 145      11.732  21.282   5.597  1.00 92.72           C  
ANISOU  673  C   SER A 145    12850  11372  11007   -122    393    307       C  
ATOM    674  O   SER A 145      12.086  21.397   6.775  1.00 90.06           O  
ANISOU  674  O   SER A 145    12522  11020  10676   -111    395    313       O  
ATOM    675  CB  SER A 145      11.196  19.009   4.630  1.00 94.80           C  
ANISOU  675  CB  SER A 145    13130  11645  11244   -219    444    295       C  
ATOM    676  OG  SER A 145      12.323  19.238   3.805  1.00 92.95           O  
ANISOU  676  OG  SER A 145    12926  11357  11033   -201    437    317       O  
ATOM    677  N   ILE A 146      12.279  22.013   4.615  1.00 91.50           N  
ANISOU  677  N   ILE A 146    12704  11193  10868    -92    374    320       N  
ATOM    678  CA  ILE A 146      13.305  23.017   4.920  1.00 92.21           C  
ANISOU  678  CA  ILE A 146    12808  11237  10990    -45    356    338       C  
ATOM    679  C   ILE A 146      12.740  24.114   5.809  1.00 90.41           C  
ANISOU  679  C   ILE A 146    12548  11041  10763     -5    332    324       C  
ATOM    680  O   ILE A 146      13.401  24.576   6.747  1.00 85.75           O  
ANISOU  680  O   ILE A 146    11965  10423  10193     20    325    330       O  
ATOM    681  CB  ILE A 146      13.916  23.614   3.635  1.00 91.52           C  
ANISOU  681  CB  ILE A 146    12737  11117  10917    -25    346    354       C  
ATOM    682  CG1 ILE A 146      14.440  22.533   2.690  1.00 87.05           C  
ANISOU  682  CG1 ILE A 146    12203  10522  10350    -67    374    362       C  
ATOM    683  CG2 ILE A 146      15.045  24.575   3.991  1.00 86.99           C  
ANISOU  683  CG2 ILE A 146    12177  10489  10385     17    335    370       C  
ATOM    684  CD1 ILE A 146      15.107  21.383   3.405  1.00 93.54           C  
ANISOU  684  CD1 ILE A 146    13045  11308  11188    -99    401    367       C  
ATOM    685  N   PHE A 147      11.519  24.560   5.524  1.00 97.90           N  
ANISOU  685  N   PHE A 147    13457  12048  11691      4    318    302       N  
ATOM    686  CA  PHE A 147      10.930  25.609   6.342  1.00 98.49           C  
ANISOU  686  CA  PHE A 147    13498  12153  11771     42    298    283       C  
ATOM    687  C   PHE A 147      10.581  25.104   7.743  1.00 98.04           C  
ANISOU  687  C   PHE A 147    13432  12118  11699     20    319    266       C  
ATOM    688  O   PHE A 147      10.780  25.824   8.730  1.00 96.43           O  
ANISOU  688  O   PHE A 147    13224  11909  11506     50    311    261       O  
ATOM    689  CB  PHE A 147       9.724  26.208   5.625  1.00 99.85           C  
ANISOU  689  CB  PHE A 147    13627  12379  11932     60    273    261       C  
ATOM    690  CG  PHE A 147      10.099  27.160   4.530  1.00102.72           C  
ANISOU  690  CG  PHE A 147    14002  12717  12310    100    242    281       C  
ATOM    691  CD1 PHE A 147      11.419  27.558   4.377  1.00101.13           C  
ANISOU  691  CD1 PHE A 147    13841  12450  12134    118    244    310       C  
ATOM    692  CD2 PHE A 147       9.145  27.666   3.663  1.00104.14           C  
ANISOU  692  CD2 PHE A 147    14155  12936  12478    118    212    269       C  
ATOM    693  CE1 PHE A 147      11.787  28.438   3.379  1.00101.45           C  
ANISOU  693  CE1 PHE A 147    13899  12462  12186    151    224    330       C  
ATOM    694  CE2 PHE A 147       9.504  28.548   2.659  1.00103.78           C  
ANISOU  694  CE2 PHE A 147    14129  12862  12439    155    184    292       C  
ATOM    695  CZ  PHE A 147      10.830  28.934   2.518  1.00103.72           C  
ANISOU  695  CZ  PHE A 147    14167  12788  12455    170    194    323       C  
ATOM    696  N   THR A 148      10.050  23.879   7.859  1.00 89.71           N  
ANISOU  696  N   THR A 148    12380  11087  10620    -33    349    258       N  
ATOM    697  CA  THR A 148       9.761  23.330   9.185  1.00 86.70           C  
ANISOU  697  CA  THR A 148    12002  10720  10219    -59    376    246       C  
ATOM    698  C   THR A 148      11.051  23.041   9.940  1.00 86.44           C  
ANISOU  698  C   THR A 148    12020  10628  10196    -56    379    276       C  
ATOM    699  O   THR A 148      11.142  23.273  11.151  1.00 86.52           O  
ANISOU  699  O   THR A 148    12038  10639  10196    -46    381    271       O  
ATOM    700  CB  THR A 148       8.911  22.064   9.068  1.00 86.97           C  
ANISOU  700  CB  THR A 148    12030  10788  10227   -120    412    232       C  
ATOM    701  OG1 THR A 148       7.639  22.389   8.490  1.00 87.29           O  
ANISOU  701  OG1 THR A 148    12015  10889  10263   -120    404    197       O  
ATOM    702  CG2 THR A 148       8.664  21.479  10.438  1.00 87.18           C  
ANISOU  702  CG2 THR A 148    12071  10824  10230   -150    444    225       C  
ATOM    703  N   LEU A 149      12.064  22.553   9.227  1.00 86.18           N  
ANISOU  703  N   LEU A 149    12020  10542  10182    -62    378    303       N  
ATOM    704  CA  LEU A 149      13.395  22.411   9.801  1.00 85.96           C  
ANISOU  704  CA  LEU A 149    12033  10452  10176    -50    372    328       C  
ATOM    705  C   LEU A 149      13.972  23.760  10.220  1.00 85.82           C  
ANISOU  705  C   LEU A 149    12008  10417  10184      6    340    327       C  
ATOM    706  O   LEU A 149      14.690  23.847  11.223  1.00 85.79           O  
ANISOU  706  O   LEU A 149    12025  10384  10187     20    330    334       O  
ATOM    707  CB  LEU A 149      14.294  21.709   8.786  1.00 85.76           C  
ANISOU  707  CB  LEU A 149    12035  10375  10174    -67    380    350       C  
ATOM    708  CG  LEU A 149      15.803  21.896   8.677  1.00 85.49           C  
ANISOU  708  CG  LEU A 149    12029  10270  10185    -43    366    371       C  
ATOM    709  CD1 LEU A 149      16.531  21.419   9.910  1.00 85.52           C  
ANISOU  709  CD1 LEU A 149    12061  10238  10194    -42    361    383       C  
ATOM    710  CD2 LEU A 149      16.259  21.134   7.459  1.00 85.41           C  
ANISOU  710  CD2 LEU A 149    12034  10227  10190    -70    385    382       C  
ATOM    711  N   THR A 150      13.679  24.826   9.460  1.00135.00           N  
ANISOU  711  N   THR A 150    18207  16660  16428     39    322    318       N  
ATOM    712  CA  THR A 150      14.144  26.157   9.855  1.00138.61           C  
ANISOU  712  CA  THR A 150    18654  17099  16913     91    294    314       C  
ATOM    713  C   THR A 150      13.312  26.711  10.999  1.00137.06           C  
ANISOU  713  C   THR A 150    18432  16949  16696    105    290    287       C  
ATOM    714  O   THR A 150      13.802  27.525  11.786  1.00133.90           O  
ANISOU  714  O   THR A 150    18033  16531  16312    139    273    281       O  
ATOM    715  CB  THR A 150      14.054  27.167   8.710  1.00138.06           C  
ANISOU  715  CB  THR A 150    18566  17026  16864    123    277    316       C  
ATOM    716  OG1 THR A 150      12.814  27.000   8.036  1.00141.62           O  
ANISOU  716  OG1 THR A 150    18989  17532  17287    108    280    302       O  
ATOM    717  CG2 THR A 150      15.141  26.940   7.689  1.00136.48           C  
ANISOU  717  CG2 THR A 150    18396  16769  16692    119    281    342       C  
ATOM    718  N   MET A 151      12.035  26.342  11.068  1.00131.42           N  
ANISOU  718  N   MET A 151    17690  16294  15948     80    308    265       N  
ATOM    719  CA  MET A 151      11.185  26.942  12.085  1.00131.71           C  
ANISOU  719  CA  MET A 151    17697  16376  15969     93    309    233       C  
ATOM    720  C   MET A 151      11.443  26.340  13.455  1.00131.48           C  
ANISOU  720  C   MET A 151    17700  16343  15912     70    327    233       C  
ATOM    721  O   MET A 151      11.250  27.013  14.474  1.00130.15           O  
ANISOU  721  O   MET A 151    17523  16192  15736     91    323    211       O  
ATOM    722  CB  MET A 151       9.712  26.808  11.713  1.00133.55           C  
ANISOU  722  CB  MET A 151    17885  16675  16184     74    323    203       C  
ATOM    723  CG  MET A 151       8.929  27.987  12.213  1.00134.33           C  
ANISOU  723  CG  MET A 151    17936  16812  16291    112    310    167       C  
ATOM    724  SD  MET A 151       9.708  29.479  11.565  1.00145.31           S  
ANISOU  724  SD  MET A 151    19324  18159  17730    180    265    182       S  
ATOM    725  CE  MET A 151       8.652  30.778  12.199  1.00138.98           C  
ANISOU  725  CE  MET A 151    18462  17401  16941    223    252    134       C  
ATOM    726  N   MET A 152      11.865  25.078  13.496  1.00131.03           N  
ANISOU  726  N   MET A 152    17684  16263  15839     29    346    256       N  
ATOM    727  CA  MET A 152      12.461  24.555  14.715  1.00132.11           C  
ANISOU  727  CA  MET A 152    17865  16376  15953     16    352    268       C  
ATOM    728  C   MET A 152      13.689  25.362  15.100  1.00130.42           C  
ANISOU  728  C   MET A 152    17669  16114  15772     63    314    278       C  
ATOM    729  O   MET A 152      13.993  25.508  16.287  1.00132.31           O  
ANISOU  729  O   MET A 152    17931  16349  15992     72    306    274       O  
ATOM    730  CB  MET A 152      12.830  23.081  14.538  1.00131.26           C  
ANISOU  730  CB  MET A 152    17800  16240  15832    -30    373    296       C  
ATOM    731  CG  MET A 152      11.649  22.170  14.260  1.00131.87           C  
ANISOU  731  CG  MET A 152    17864  16363  15880    -83    414    284       C  
ATOM    732  SD  MET A 152      12.146  20.631  13.472  1.00128.61           S  
ANISOU  732  SD  MET A 152    17487  15907  15472   -130    434    315       S  
ATOM    733  CE  MET A 152      11.264  19.436  14.461  1.00125.93           C  
ANISOU  733  CE  MET A 152    17174  15596  15079   -192    483    310       C  
ATOM    734  N   SER A 153      14.395  25.908  14.110  1.00135.62           N  
ANISOU  734  N   SER A 153    18316  16735  16476     91    293    290       N  
ATOM    735  CA  SER A 153      15.637  26.617  14.386  1.00135.69           C  
ANISOU  735  CA  SER A 153    18338  16691  16525    131    261    297       C  
ATOM    736  C   SER A 153      15.387  27.896  15.170  1.00134.46           C  
ANISOU  736  C   SER A 153    18159  16557  16372    170    243    268       C  
ATOM    737  O   SER A 153      16.087  28.183  16.147  1.00135.20           O  
ANISOU  737  O   SER A 153    18272  16628  16469    189    222    264       O  
ATOM    738  CB  SER A 153      16.364  26.923  13.081  1.00136.30           C  
ANISOU  738  CB  SER A 153    18409  16725  16651    146    252    313       C  
ATOM    739  OG  SER A 153      16.765  25.722  12.439  1.00135.83           O  
ANISOU  739  OG  SER A 153    18376  16639  16594    111    270    337       O  
ATOM    740  N   VAL A 154      14.396  28.681  14.753  1.00134.91           N  
ANISOU  740  N   VAL A 154    18174  16656  16430    185    247    246       N  
ATOM    741  CA  VAL A 154      14.095  29.912  15.475  1.00135.91           C  
ANISOU  741  CA  VAL A 154    18274  16801  16564    223    232    214       C  
ATOM    742  C   VAL A 154      13.384  29.601  16.790  1.00136.04           C  
ANISOU  742  C   VAL A 154    18297  16863  16529    203    251    190       C  
ATOM    743  O   VAL A 154      13.485  30.372  17.753  1.00134.89           O  
ANISOU  743  O   VAL A 154    18149  16722  16381    228    239    166       O  
ATOM    744  CB  VAL A 154      13.280  30.865  14.579  1.00130.46           C  
ANISOU  744  CB  VAL A 154    17536  16136  15896    250    227    199       C  
ATOM    745  CG1 VAL A 154      12.077  30.155  13.992  1.00131.71           C  
ANISOU  745  CG1 VAL A 154    17672  16345  16025    216    251    194       C  
ATOM    746  CG2 VAL A 154      12.866  32.122  15.329  1.00131.34           C  
ANISOU  746  CG2 VAL A 154    17616  16267  16019    290    215    162       C  
ATOM    747  N   ASP A 155      12.680  28.467  16.866  1.00104.74           N  
ANISOU  747  N   ASP A 155    14344  12931  12522    154    284    195       N  
ATOM    748  CA  ASP A 155      11.964  28.119  18.090  1.00104.65           C  
ANISOU  748  CA  ASP A 155    14343  12961  12457    128    311    173       C  
ATOM    749  C   ASP A 155      12.926  27.906  19.251  1.00103.60           C  
ANISOU  749  C   ASP A 155    14265  12796  12303    131    295    184       C  
ATOM    750  O   ASP A 155      12.709  28.418  20.355  1.00103.40           O  
ANISOU  750  O   ASP A 155    14245  12793  12251    141    296    157       O  
ATOM    751  CB  ASP A 155      11.117  26.868  17.873  1.00104.89           C  
ANISOU  751  CB  ASP A 155    14379  13024  12451     71    352    178       C  
ATOM    752  CG  ASP A 155      10.074  26.688  18.954  1.00105.77           C  
ANISOU  752  CG  ASP A 155    14487  13189  12513     42    392    146       C  
ATOM    753  OD1 ASP A 155       9.672  27.703  19.552  1.00107.32           O  
ANISOU  753  OD1 ASP A 155    14655  13411  12710     70    388    110       O  
ATOM    754  OD2 ASP A 155       9.686  25.537  19.234  1.00107.12           O  
ANISOU  754  OD2 ASP A 155    14686  13372  12644    -10    428    156       O  
ATOM    755  N   ARG A 156      13.991  27.134  19.024  1.00131.02           N  
ANISOU  755  N   ARG A 156    17780  16217  15786    122    279    222       N  
ATOM    756  CA  ARG A 156      14.985  26.931  20.073  1.00131.77           C  
ANISOU  756  CA  ARG A 156    17925  16276  15865    131    253    235       C  
ATOM    757  C   ARG A 156      15.768  28.204  20.362  1.00129.57           C  
ANISOU  757  C   ARG A 156    17632  15972  15627    184    212    216       C  
ATOM    758  O   ARG A 156      16.189  28.425  21.503  1.00130.84           O  
ANISOU  758  O   ARG A 156    17822  16128  15763    196    191    205       O  
ATOM    759  CB  ARG A 156      15.926  25.781  19.701  1.00131.96           C  
ANISOU  759  CB  ARG A 156    17992  16247  15901    112    244    277       C  
ATOM    760  CG  ARG A 156      15.244  24.609  18.994  1.00135.48           C  
ANISOU  760  CG  ARG A 156    18441  16707  16328     62    284    295       C  
ATOM    761  CD  ARG A 156      16.012  23.308  19.215  1.00136.47           C  
ANISOU  761  CD  ARG A 156    18624  16785  16442     36    281    333       C  
ATOM    762  NE  ARG A 156      15.230  22.129  18.859  1.00134.84           N  
ANISOU  762  NE  ARG A 156    18428  16597  16206    -18    326    346       N  
ATOM    763  CZ  ARG A 156      15.750  20.973  18.469  1.00137.30           C  
ANISOU  763  CZ  ARG A 156    18774  16867  16528    -43    331    378       C  
ATOM    764  NH1 ARG A 156      17.059  20.795  18.387  1.00134.29           N  
ANISOU  764  NH1 ARG A 156    18417  16422  16186    -20    293    400       N  
ATOM    765  NH2 ARG A 156      14.936  19.963  18.173  1.00138.52           N  
ANISOU  765  NH2 ARG A 156    18935  17041  16655    -95    375    383       N  
ATOM    766  N   TYR A 157      15.971  29.050  19.352  1.00 99.98           N  
ANISOU  766  N   TYR A 157    13842  12207  11938    215    199    212       N  
ATOM    767  CA  TYR A 157      16.635  30.330  19.577  1.00 99.82           C  
ANISOU  767  CA  TYR A 157    13803  12161  11961    263    165    190       C  
ATOM    768  C   TYR A 157      15.790  31.265  20.432  1.00 98.40           C  
ANISOU  768  C   TYR A 157    13600  12030  11758    280    172    147       C  
ATOM    769  O   TYR A 157      16.318  31.956  21.310  1.00 97.14           O  
ANISOU  769  O   TYR A 157    13449  11858  11603    306    146    125       O  
ATOM    770  CB  TYR A 157      16.954  30.983  18.238  1.00 98.35           C  
ANISOU  770  CB  TYR A 157    13583  11944  11840    287    158    199       C  
ATOM    771  CG  TYR A 157      17.142  32.476  18.307  1.00 95.87           C  
ANISOU  771  CG  TYR A 157    13237  11618  11569    334    137    170       C  
ATOM    772  CD1 TYR A 157      16.058  33.341  18.178  1.00 97.90           C  
ANISOU  772  CD1 TYR A 157    13454  11918  11826    351    149    143       C  
ATOM    773  CD2 TYR A 157      18.398  33.026  18.505  1.00 96.40           C  
ANISOU  773  CD2 TYR A 157    13313  11631  11686    363    105    168       C  
ATOM    774  CE1 TYR A 157      16.223  34.709  18.252  1.00101.19           C  
ANISOU  774  CE1 TYR A 157    13843  12320  12286    395    130    117       C  
ATOM    775  CE2 TYR A 157      18.576  34.391  18.571  1.00 97.87           C  
ANISOU  775  CE2 TYR A 157    13469  11802  11914    404     89    141       C  
ATOM    776  CZ  TYR A 157      17.485  35.230  18.446  1.00100.49           C  
ANISOU  776  CZ  TYR A 157    13766  12174  12243    420    102    116       C  
ATOM    777  OH  TYR A 157      17.650  36.593  18.514  1.00 96.63           O  
ANISOU  777  OH  TYR A 157    13249  11666  11800    461     87     89       O  
ATOM    778  N   ILE A 158      14.484  31.325  20.161  1.00 99.50           N  
ANISOU  778  N   ILE A 158    13707  12223  11877    265    205    129       N  
ATOM    779  CA  ILE A 158      13.602  32.257  20.857  1.00 98.46           C  
ANISOU  779  CA  ILE A 158    13543  12136  11733    282    216     82       C  
ATOM    780  C   ILE A 158      13.552  31.935  22.345  1.00100.80           C  
ANISOU  780  C   ILE A 158    13879  12454  11966    263    225     65       C  
ATOM    781  O   ILE A 158      13.479  32.837  23.189  1.00102.78           O  
ANISOU  781  O   ILE A 158    14122  12718  12213    288    217     27       O  
ATOM    782  CB  ILE A 158      12.201  32.231  20.215  1.00 99.08           C  
ANISOU  782  CB  ILE A 158    13574  12267  11806    267    249     66       C  
ATOM    783  CG1 ILE A 158      12.170  33.121  18.968  1.00100.42           C  
ANISOU  783  CG1 ILE A 158    13698  12418  12037    305    229     69       C  
ATOM    784  CG2 ILE A 158      11.120  32.626  21.213  1.00 98.04           C  
ANISOU  784  CG2 ILE A 158    13420  12193  11639    262    278     17       C  
ATOM    785  CD1 ILE A 158      11.881  34.584  19.248  1.00101.88           C  
ANISOU  785  CD1 ILE A 158    13843  12610  12256    352    215     29       C  
ATOM    786  N   ALA A 159      13.601  30.648  22.693  1.00 90.43           N  
ANISOU  786  N   ALA A 159    12614  11142  10601    220    242     93       N  
ATOM    787  CA  ALA A 159      13.550  30.259  24.098  1.00 88.68           C  
ANISOU  787  CA  ALA A 159    12444  10940  10311    199    252     83       C  
ATOM    788  C   ALA A 159      14.734  30.822  24.878  1.00 90.18           C  
ANISOU  788  C   ALA A 159    12664  11091  10509    234    202     78       C  
ATOM    789  O   ALA A 159      14.561  31.401  25.955  1.00 93.71           O  
ANISOU  789  O   ALA A 159    13122  11562  10922    243    201     42       O  
ATOM    790  CB  ALA A 159      13.506  28.738  24.213  1.00 92.99           C  
ANISOU  790  CB  ALA A 159    13043  11483  10807    147    275    122       C  
ATOM    791  N   VAL A 160      15.947  30.668  24.347  1.00120.74           N  
ANISOU  791  N   VAL A 160    16547  14902  14426    253    160    109       N  
ATOM    792  CA  VAL A 160      17.134  31.075  25.093  1.00123.46           C  
ANISOU  792  CA  VAL A 160    16919  15207  14781    284    108    103       C  
ATOM    793  C   VAL A 160      17.236  32.594  25.181  1.00125.66           C  
ANISOU  793  C   VAL A 160    17152  15486  15107    329     89     58       C  
ATOM    794  O   VAL A 160      17.453  33.149  26.265  1.00129.79           O  
ANISOU  794  O   VAL A 160    17692  16016  15606    345     69     26       O  
ATOM    795  CB  VAL A 160      18.399  30.469  24.465  1.00126.79           C  
ANISOU  795  CB  VAL A 160    17358  15564  15250    291     72    144       C  
ATOM    796  CG1 VAL A 160      19.578  30.626  25.410  1.00127.75           C  
ANISOU  796  CG1 VAL A 160    17516  15649  15373    316     16    138       C  
ATOM    797  CG2 VAL A 160      18.163  29.008  24.139  1.00127.58           C  
ANISOU  797  CG2 VAL A 160    17495  15664  15317    246     98    187       C  
ATOM    798  N   CYS A 161      17.084  33.290  24.048  1.00 89.90           N  
ANISOU  798  N   CYS A 161    12568  10944  10644    350     95     56       N  
ATOM    799  CA  CYS A 161      17.410  34.715  23.991  1.00 90.61           C  
ANISOU  799  CA  CYS A 161    12619  11016  10793    396     73     20       C  
ATOM    800  C   CYS A 161      16.258  35.634  24.378  1.00 88.31           C  
ANISOU  800  C   CYS A 161    12290  10775  10488    407     99    -27       C  
ATOM    801  O   CYS A 161      16.506  36.698  24.956  1.00 88.51           O  
ANISOU  801  O   CYS A 161    12301  10794  10535    439     80    -67       O  
ATOM    802  CB  CYS A 161      17.905  35.103  22.592  1.00 90.30           C  
ANISOU  802  CB  CYS A 161    12546  10932  10834    416     65     42       C  
ATOM    803  SG  CYS A 161      19.248  34.086  21.927  1.00 90.13           S  
ANISOU  803  SG  CYS A 161    12555  10845  10844    403     42     92       S  
ATOM    804  N   HIS A 162      15.014  35.269  24.078  1.00100.93           N  
ANISOU  804  N   HIS A 162    13869  12424  12058    382    142    -29       N  
ATOM    805  CA  HIS A 162      13.842  36.064  24.448  1.00102.32           C  
ANISOU  805  CA  HIS A 162    14003  12649  12224    390    170    -78       C  
ATOM    806  C   HIS A 162      12.927  35.241  25.349  1.00101.66           C  
ANISOU  806  C   HIS A 162    13945  12622  12057    345    213    -91       C  
ATOM    807  O   HIS A 162      11.781  34.953  24.986  1.00101.17           O  
ANISOU  807  O   HIS A 162    13853  12603  11983    323    254    -99       O  
ATOM    808  CB  HIS A 162      13.091  36.551  23.208  1.00102.84           C  
ANISOU  808  CB  HIS A 162    14011  12724  12342    406    183    -77       C  
ATOM    809  CG  HIS A 162      13.901  37.435  22.307  1.00104.98           C  
ANISOU  809  CG  HIS A 162    14260  12937  12690    449    148    -64       C  
ATOM    810  ND1 HIS A 162      15.054  37.011  21.681  1.00103.50           N  
ANISOU  810  ND1 HIS A 162    14099  12694  12530    448    124    -21       N  
ATOM    811  CD2 HIS A 162      13.716  38.721  21.919  1.00104.96           C  
ANISOU  811  CD2 HIS A 162    14213  12921  12745    492    138    -89       C  
ATOM    812  CE1 HIS A 162      15.547  37.997  20.952  1.00104.41           C  
ANISOU  812  CE1 HIS A 162    14190  12767  12715    486    104    -20       C  
ATOM    813  NE2 HIS A 162      14.754  39.046  21.080  1.00105.07           N  
ANISOU  813  NE2 HIS A 162    14233  12873  12818    514    110    -59       N  
ATOM    814  N   PRO A 163      13.395  34.873  26.552  1.00105.68           N  
ANISOU  814  N   PRO A 163    14512  13133  12508    330    206    -95       N  
ATOM    815  CA  PRO A 163      12.726  33.792  27.302  1.00106.82           C  
ANISOU  815  CA  PRO A 163    14701  13319  12567    278    248    -90       C  
ATOM    816  C   PRO A 163      11.256  34.035  27.600  1.00108.04           C  
ANISOU  816  C   PRO A 163    14817  13538  12696    258    306   -136       C  
ATOM    817  O   PRO A 163      10.461  33.091  27.516  1.00108.83           O  
ANISOU  817  O   PRO A 163    14925  13670  12757    212    351   -124       O  
ATOM    818  CB  PRO A 163      13.560  33.713  28.587  1.00106.16           C  
ANISOU  818  CB  PRO A 163    14684  13222  12431    280    218    -94       C  
ATOM    819  CG  PRO A 163      14.911  34.177  28.161  1.00104.01           C  
ANISOU  819  CG  PRO A 163    14410  12888  12224    322    155    -77       C  
ATOM    820  CD  PRO A 163      14.614  35.326  27.243  1.00106.76           C  
ANISOU  820  CD  PRO A 163    14682  13230  12653    358    156   -102       C  
ATOM    821  N   VAL A 164      10.853  35.262  27.937  1.00 90.54           N  
ANISOU  821  N   VAL A 164    12556  11340  10506    291    309   -192       N  
ATOM    822  CA  VAL A 164       9.432  35.491  28.182  1.00 91.00           C  
ANISOU  822  CA  VAL A 164    12569  11457  10548    273    366   -241       C  
ATOM    823  C   VAL A 164       8.656  35.589  26.875  1.00 90.72           C  
ANISOU  823  C   VAL A 164    12463  11433  10574    281    377   -237       C  
ATOM    824  O   VAL A 164       7.439  35.358  26.864  1.00 91.06           O  
ANISOU  824  O   VAL A 164    12469  11525  10604    254    426   -266       O  
ATOM    825  CB  VAL A 164       9.210  36.742  29.049  1.00 91.44           C  
ANISOU  825  CB  VAL A 164    12601  11531  10611    304    369   -308       C  
ATOM    826  CG1 VAL A 164       7.839  36.702  29.719  1.00 92.09           C  
ANISOU  826  CG1 VAL A 164    12659  11678  10652    271    438   -362       C  
ATOM    827  CG2 VAL A 164      10.320  36.874  30.080  1.00 91.58           C  
ANISOU  827  CG2 VAL A 164    12685  11522  10590    313    332   -308       C  
ATOM    828  N   LYS A 165       9.325  35.920  25.767  1.00123.38           N  
ANISOU  828  N   LYS A 165    16580  15524  14776    316    332   -203       N  
ATOM    829  CA  LYS A 165       8.691  35.807  24.459  1.00124.95           C  
ANISOU  829  CA  LYS A 165    16727  15729  15019    319    336   -188       C  
ATOM    830  C   LYS A 165       8.482  34.357  24.050  1.00127.71           C  
ANISOU  830  C   LYS A 165    17104  16090  15330    266    360   -147       C  
ATOM    831  O   LYS A 165       7.604  34.079  23.226  1.00130.72           O  
ANISOU  831  O   LYS A 165    17442  16498  15729    253    379   -148       O  
ATOM    832  CB  LYS A 165       9.522  36.522  23.395  1.00125.16           C  
ANISOU  832  CB  LYS A 165    16737  15701  15119    367    285   -160       C  
ATOM    833  CG  LYS A 165       9.000  37.891  23.015  1.00132.56           C  
ANISOU  833  CG  LYS A 165    17609  16640  16119    418    273   -199       C  
ATOM    834  CD  LYS A 165      10.029  38.643  22.196  1.00133.22           C  
ANISOU  834  CD  LYS A 165    17693  16659  16266    462    225   -170       C  
ATOM    835  CE  LYS A 165       9.364  39.488  21.131  1.00128.39           C  
ANISOU  835  CE  LYS A 165    17022  16045  15714    501    213   -177       C  
ATOM    836  NZ  LYS A 165      10.346  39.857  20.096  1.00117.31           N  
ANISOU  836  NZ  LYS A 165    15633  14579  14362    529    176   -133       N  
ATOM    837  N   ALA A 166       9.274  33.431  24.600  1.00110.72           N  
ANISOU  837  N   ALA A 166    15024  13916  13127    236    357   -111       N  
ATOM    838  CA  ALA A 166       9.032  32.010  24.388  1.00106.24           C  
ANISOU  838  CA  ALA A 166    14489  13359  12518    181    387    -76       C  
ATOM    839  C   ALA A 166       7.736  31.548  25.034  1.00106.74           C  
ANISOU  839  C   ALA A 166    14542  13484  12532    134    452   -112       C  
ATOM    840  O   ALA A 166       7.180  30.529  24.620  1.00110.49           O  
ANISOU  840  O   ALA A 166    15018  13975  12989     89    485    -95       O  
ATOM    841  CB  ALA A 166      10.200  31.192  24.933  1.00100.89           C  
ANISOU  841  CB  ALA A 166    13894  12640  11802    165    365    -31       C  
ATOM    842  N   LEU A 167       7.232  32.286  26.024  1.00104.50           N  
ANISOU  842  N   LEU A 167    14245  13232  12228    142    474   -165       N  
ATOM    843  CA  LEU A 167       6.016  31.872  26.713  1.00106.75           C  
ANISOU  843  CA  LEU A 167    14520  13575  12466     94    543   -205       C  
ATOM    844  C   LEU A 167       4.827  31.791  25.765  1.00107.03           C  
ANISOU  844  C   LEU A 167    14476  13646  12543     83    571   -228       C  
ATOM    845  O   LEU A 167       3.915  30.988  25.987  1.00106.41           O  
ANISOU  845  O   LEU A 167    14394  13607  12431     29    630   -243       O  
ATOM    846  CB  LEU A 167       5.722  32.837  27.859  1.00110.06           C  
ANISOU  846  CB  LEU A 167    14932  14020  12866    111    561   -265       C  
ATOM    847  CG  LEU A 167       6.182  32.414  29.255  1.00109.41           C  
ANISOU  847  CG  LEU A 167    14938  13938  12696     82    578   -262       C  
ATOM    848  CD1 LEU A 167       5.333  33.104  30.302  1.00116.59           C  
ANISOU  848  CD1 LEU A 167    15827  14895  13577     75    627   -335       C  
ATOM    849  CD2 LEU A 167       6.124  30.909  29.442  1.00110.17           C  
ANISOU  849  CD2 LEU A 167    15099  14034  12725     18    613   -217       C  
ATOM    850  N   ASP A 168       4.810  32.613  24.713  1.00116.16           N  
ANISOU  850  N   ASP A 168    15570  14790  13774    133    530   -232       N  
ATOM    851  CA  ASP A 168       3.762  32.539  23.701  1.00116.45           C  
ANISOU  851  CA  ASP A 168    15534  14858  13853    129    542   -249       C  
ATOM    852  C   ASP A 168       4.184  31.766  22.462  1.00116.75           C  
ANISOU  852  C   ASP A 168    15583  14868  13908    120    514   -192       C  
ATOM    853  O   ASP A 168       3.346  31.094  21.853  1.00116.95           O  
ANISOU  853  O   ASP A 168    15575  14922  13937     87    539   -198       O  
ATOM    854  CB  ASP A 168       3.316  33.944  23.275  1.00114.83           C  
ANISOU  854  CB  ASP A 168    15251  14661  13718    191    513   -292       C  
ATOM    855  CG  ASP A 168       4.486  34.874  22.998  1.00120.32           C  
ANISOU  855  CG  ASP A 168    15966  15300  14451    250    451   -265       C  
ATOM    856  OD1 ASP A 168       5.177  35.270  23.962  1.00124.16           O  
ANISOU  856  OD1 ASP A 168    16493  15768  14914    261    445   -272       O  
ATOM    857  OD2 ASP A 168       4.710  35.219  21.816  1.00119.45           O  
ANISOU  857  OD2 ASP A 168    15830  15163  14391    284    408   -238       O  
ATOM    858  N   PHE A 169       5.461  31.847  22.079  1.00108.12           N  
ANISOU  858  N   PHE A 169    14535  13718  12828    147    465   -142       N  
ATOM    859  CA  PHE A 169       5.930  31.164  20.878  1.00106.87           C  
ANISOU  859  CA  PHE A 169    14389  13529  12688    139    440    -91       C  
ATOM    860  C   PHE A 169       5.818  29.653  21.044  1.00111.39           C  
ANISOU  860  C   PHE A 169    15005  14108  13208     73    480    -65       C  
ATOM    861  O   PHE A 169       5.457  28.939  20.099  1.00110.98           O  
ANISOU  861  O   PHE A 169    14937  14064  13167     48    487    -49       O  
ATOM    862  CB  PHE A 169       7.373  31.592  20.583  1.00104.91           C  
ANISOU  862  CB  PHE A 169    14179  13216  12465    180    387    -49       C  
ATOM    863  CG  PHE A 169       7.865  31.245  19.194  1.00109.49           C  
ANISOU  863  CG  PHE A 169    14761  13762  13078    185    359     -5       C  
ATOM    864  CD1 PHE A 169       7.774  29.962  18.681  1.00113.58           C  
ANISOU  864  CD1 PHE A 169    15301  14282  13574    137    379     25       C  
ATOM    865  CD2 PHE A 169       8.419  32.228  18.396  1.00107.48           C  
ANISOU  865  CD2 PHE A 169    14488  13472  12878    237    316      6       C  
ATOM    866  CE1 PHE A 169       8.230  29.667  17.410  1.00112.79           C  
ANISOU  866  CE1 PHE A 169    15202  14151  13501    141    356     61       C  
ATOM    867  CE2 PHE A 169       8.874  31.938  17.124  1.00106.43           C  
ANISOU  867  CE2 PHE A 169    14360  13308  12770    240    294     46       C  
ATOM    868  CZ  PHE A 169       8.780  30.657  16.631  1.00104.96           C  
ANISOU  868  CZ  PHE A 169    14196  13127  12559    192    314     71       C  
ATOM    869  N   ARG A 170       6.092  29.155  22.251  1.00103.24           N  
ANISOU  869  N   ARG A 170    14031  13075  12119     43    507    -62       N  
ATOM    870  CA  ARG A 170       6.115  27.728  22.546  1.00 99.25           C  
ANISOU  870  CA  ARG A 170    13583  12567  11562    -19    544    -31       C  
ATOM    871  C   ARG A 170       4.733  27.132  22.780  1.00101.71           C  
ANISOU  871  C   ARG A 170    13864  12935  11848    -74    611    -69       C  
ATOM    872  O   ARG A 170       4.635  25.921  23.003  1.00105.19           O  
ANISOU  872  O   ARG A 170    14349  13372  12245   -130    649    -46       O  
ATOM    873  CB  ARG A 170       6.988  27.459  23.771  1.00 97.39           C  
ANISOU  873  CB  ARG A 170    13430  12303  11271    -27    540    -10       C  
ATOM    874  CG  ARG A 170       8.438  27.857  23.599  1.00 96.20           C  
ANISOU  874  CG  ARG A 170    13312  12092  11146     20    475     27       C  
ATOM    875  CD  ARG A 170       9.059  27.081  22.468  1.00 98.81           C  
ANISOU  875  CD  ARG A 170    13655  12382  11507     13    453     76       C  
ATOM    876  NE  ARG A 170      10.490  26.872  22.653  1.00101.10           N  
ANISOU  876  NE  ARG A 170    14002  12611  11799     32    409    118       N  
ATOM    877  CZ  ARG A 170      11.035  25.718  23.015  1.00102.95           C  
ANISOU  877  CZ  ARG A 170    14303  12815  11997      0    413    158       C  
ATOM    878  NH1 ARG A 170      10.297  24.642  23.242  1.00104.41           N  
ANISOU  878  NH1 ARG A 170    14511  13022  12136    -57    464    164       N  
ATOM    879  NH2 ARG A 170      12.356  25.638  23.143  1.00 99.50           N  
ANISOU  879  NH2 ARG A 170    13910  12322  11575     25    365    190       N  
ATOM    880  N   THR A 171       3.671  27.932  22.760  1.00121.48           N  
ANISOU  880  N   THR A 171    16293  15487  14379    -60    628   -127       N  
ATOM    881  CA  THR A 171       2.337  27.372  22.907  1.00124.87           C  
ANISOU  881  CA  THR A 171    16682  15969  14794   -113    694   -169       C  
ATOM    882  C   THR A 171       1.995  26.510  21.694  1.00127.44           C  
ANISOU  882  C   THR A 171    16981  16295  15144   -141    694   -150       C  
ATOM    883  O   THR A 171       2.448  26.786  20.581  1.00127.37           O  
ANISOU  883  O   THR A 171    16954  16263  15179   -104    640   -125       O  
ATOM    884  CB  THR A 171       1.296  28.474  23.065  1.00126.70           C  
ANISOU  884  CB  THR A 171    16829  16250  15063    -85    706   -241       C  
ATOM    885  OG1 THR A 171       1.332  29.335  21.921  1.00125.83           O  
ANISOU  885  OG1 THR A 171    16657  16131  15021    -26    647   -242       O  
ATOM    886  CG2 THR A 171       1.580  29.282  24.311  1.00132.18           C  
ANISOU  886  CG2 THR A 171    17549  16944  15729    -64    714   -266       C  
ATOM    887  N   PRO A 172       1.217  25.443  21.888  1.00140.35           N  
ANISOU  887  N   PRO A 172    18619  17957  16750   -209    756   -162       N  
ATOM    888  CA  PRO A 172       0.824  24.611  20.737  1.00139.23           C  
ANISOU  888  CA  PRO A 172    18449  17820  16634   -238    757   -152       C  
ATOM    889  C   PRO A 172       0.163  25.403  19.620  1.00139.48           C  
ANISOU  889  C   PRO A 172    18386  17880  16730   -197    718   -187       C  
ATOM    890  O   PRO A 172       0.504  25.222  18.443  1.00139.70           O  
ANISOU  890  O   PRO A 172    18406  17887  16784   -182    675   -157       O  
ATOM    891  CB  PRO A 172      -0.144  23.591  21.363  1.00140.87           C  
ANISOU  891  CB  PRO A 172    18659  18061  16804   -318    841   -180       C  
ATOM    892  CG  PRO A 172      -0.420  24.097  22.775  1.00144.08           C  
ANISOU  892  CG  PRO A 172    19083  18490  17173   -323    884   -215       C  
ATOM    893  CD  PRO A 172       0.805  24.840  23.164  1.00143.69           C  
ANISOU  893  CD  PRO A 172    19086  18399  17111   -266    828   -179       C  
ATOM    894  N   LEU A 173      -0.771  26.293  19.966  1.00107.13           N  
ANISOU  894  N   LEU A 173    14219  13828  12658   -176    731   -250       N  
ATOM    895  CA  LEU A 173      -1.458  27.094  18.957  1.00104.18           C  
ANISOU  895  CA  LEU A 173    13755  13482  12348   -131    689   -284       C  
ATOM    896  C   LEU A 173      -0.474  27.929  18.148  1.00103.38           C  
ANISOU  896  C   LEU A 173    13667  13336  12276    -61    610   -242       C  
ATOM    897  O   LEU A 173      -0.580  28.010  16.920  1.00102.46           O  
ANISOU  897  O   LEU A 173    13519  13218  12194    -40    566   -231       O  
ATOM    898  CB  LEU A 173      -2.500  27.996  19.615  1.00108.74           C  
ANISOU  898  CB  LEU A 173    14259  14108  12951   -114    715   -359       C  
ATOM    899  N   LYS A 174       0.484  28.568  18.827  1.00106.82           N  
ANISOU  899  N   LYS A 174    14152  13736  12698    -27    591   -219       N  
ATOM    900  CA  LYS A 174       1.525  29.313  18.125  1.00107.22           C  
ANISOU  900  CA  LYS A 174    14223  13738  12778     33    524   -177       C  
ATOM    901  C   LYS A 174       2.294  28.412  17.171  1.00107.70           C  
ANISOU  901  C   LYS A 174    14329  13761  12830     14    503   -118       C  
ATOM    902  O   LYS A 174       2.479  28.752  15.999  1.00107.72           O  
ANISOU  902  O   LYS A 174    14314  13748  12867     47    457   -100       O  
ATOM    903  CB  LYS A 174       2.483  29.959  19.120  1.00106.54           C  
ANISOU  903  CB  LYS A 174    14187  13619  12675     62    514   -164       C  
ATOM    904  N   ALA A 175       2.775  27.268  17.663  1.00133.37           N  
ANISOU  904  N   ALA A 175    17645  16994  16037    -38    537    -88       N  
ATOM    905  CA  ALA A 175       3.421  26.308  16.775  1.00129.75           C  
ANISOU  905  CA  ALA A 175    17226  16500  15573    -61    524    -38       C  
ATOM    906  C   ALA A 175       2.483  25.914  15.641  1.00126.50           C  
ANISOU  906  C   ALA A 175    16759  16122  15184    -80    524    -58       C  
ATOM    907  O   ALA A 175       2.827  26.049  14.466  1.00126.05           O  
ANISOU  907  O   ALA A 175    16696  16046  15152    -56    482    -34       O  
ATOM    908  CB  ALA A 175       3.874  25.078  17.557  1.00127.80           C  
ANISOU  908  CB  ALA A 175    17051  16231  15276   -118    566     -9       C  
ATOM    909  N   LYS A 176       1.265  25.485  15.985  1.00 90.31           N  
ANISOU  909  N   LYS A 176    12130  11591  10592   -123    572   -105       N  
ATOM    910  CA  LYS A 176       0.284  25.083  14.977  1.00 90.57           C  
ANISOU  910  CA  LYS A 176    12102  11662  10647   -144    571   -133       C  
ATOM    911  C   LYS A 176      -0.031  26.214  14.001  1.00 90.54           C  
ANISOU  911  C   LYS A 176    12038  11672  10690    -80    509   -150       C  
ATOM    912  O   LYS A 176      -0.146  25.984  12.790  1.00 90.44           O  
ANISOU  912  O   LYS A 176    12010  11661  10693    -77    476   -140       O  
ATOM    913  CB  LYS A 176      -0.996  24.604  15.663  1.00 91.26           C  
ANISOU  913  CB  LYS A 176    12144  11805  10727   -197    635   -192       C  
ATOM    914  N   ILE A 177      -0.198  27.437  14.513  1.00114.22           N  
ANISOU  914  N   ILE A 177    15006  14681  13713    -28    492   -176       N  
ATOM    915  CA  ILE A 177      -0.422  28.589  13.642  1.00114.41           C  
ANISOU  915  CA  ILE A 177    14981  14709  13782     39    429   -185       C  
ATOM    916  C   ILE A 177       0.770  28.784  12.719  1.00113.47           C  
ANISOU  916  C   ILE A 177    14916  14533  13665     72    379   -123       C  
ATOM    917  O   ILE A 177       0.623  28.904  11.497  1.00115.45           O  
ANISOU  917  O   ILE A 177    15149  14784  13934     92    336   -112       O  
ATOM    918  CB  ILE A 177      -0.680  29.849  14.484  1.00111.68           C  
ANISOU  918  CB  ILE A 177    14599  14372  13460     88    425   -222       C  
ATOM    919  CG1 ILE A 177      -2.137  29.906  14.938  1.00113.22           C  
ANISOU  919  CG1 ILE A 177    14712  14632  13675     70    460   -298       C  
ATOM    920  CG2 ILE A 177      -0.326  31.094  13.702  1.00112.37           C  
ANISOU  920  CG2 ILE A 177    14673  14433  13588    164    356   -206       C  
ATOM    921  CD1 ILE A 177      -2.531  31.239  15.547  1.00122.11           C  
ANISOU  921  CD1 ILE A 177    15789  15771  14838    125    449   -342       C  
ATOM    922  N   ILE A 178       1.973  28.817  13.295  1.00 98.53           N  
ANISOU  922  N   ILE A 178    13091  12591  11755     77    383    -82       N  
ATOM    923  CA  ILE A 178       3.189  28.882  12.495  1.00 98.88           C  
ANISOU  923  CA  ILE A 178    13190  12578  11804     99    347    -25       C  
ATOM    924  C   ILE A 178       3.304  27.658  11.602  1.00101.26           C  
ANISOU  924  C   ILE A 178    13516  12874  12087     52    355      0       C  
ATOM    925  O   ILE A 178       3.853  27.730  10.496  1.00102.90           O  
ANISOU  925  O   ILE A 178    13743  13051  12303     70    321     33       O  
ATOM    926  CB  ILE A 178       4.413  29.040  13.420  1.00 98.43           C  
ANISOU  926  CB  ILE A 178    13194  12472  11735    108    354      4       C  
ATOM    927  CG1 ILE A 178       4.359  30.394  14.140  1.00100.58           C  
ANISOU  927  CG1 ILE A 178    13440  12745  12030    162    337    -23       C  
ATOM    928  CG2 ILE A 178       5.693  28.882  12.649  1.00 99.18           C  
ANISOU  928  CG2 ILE A 178    13343  12505  11835    119    327     59       C  
ATOM    929  CD1 ILE A 178       5.360  30.550  15.275  1.00102.01           C  
ANISOU  929  CD1 ILE A 178    13673  12890  12195    166    347     -8       C  
ATOM    930  N   ASN A 179       2.750  26.536  12.037  1.00149.33           N  
ANISOU  930  N   ASN A 179    19602  18990  18148    -10    403    -17       N  
ATOM    931  CA  ASN A 179       2.925  25.286  11.326  1.00150.76           C  
ANISOU  931  CA  ASN A 179    19812  19160  18312    -60    418      6       C  
ATOM    932  C   ASN A 179       1.856  25.059  10.264  1.00152.57           C  
ANISOU  932  C   ASN A 179    19983  19433  18552    -72    404    -25       C  
ATOM    933  O   ASN A 179       1.952  24.088   9.505  1.00155.15           O  
ANISOU  933  O   ASN A 179    20329  19754  18867   -111    412    -11       O  
ATOM    934  CB  ASN A 179       2.944  24.139  12.329  1.00150.51           C  
ANISOU  934  CB  ASN A 179    19815  19126  18245   -122    478      7       C  
ATOM    935  CG  ASN A 179       3.877  23.049  11.929  1.00154.04           C  
ANISOU  935  CG  ASN A 179    20326  19525  18676   -157    487     54       C  
ATOM    936  OD1 ASN A 179       3.447  21.952  11.646  1.00157.14           O  
ANISOU  936  OD1 ASN A 179    20720  19930  19056   -211    518     47       O  
ATOM    937  ND2 ASN A 179       5.172  23.344  11.899  1.00150.44           N  
ANISOU  937  ND2 ASN A 179    19922  19012  18226   -126    461     97       N  
ATOM    938  N   ILE A 180       0.844  25.918  10.197  1.00108.60           N  
ANISOU  938  N   ILE A 180    14345  13911  13009    -39    383    -70       N  
ATOM    939  CA  ILE A 180      -0.083  25.933   9.068  1.00108.30           C  
ANISOU  939  CA  ILE A 180    14250  13911  12987    -34    350    -98       C  
ATOM    940  C   ILE A 180       0.390  26.897   7.993  1.00108.75           C  
ANISOU  940  C   ILE A 180    14316  13943  13061     29    282    -68       C  
ATOM    941  O   ILE A 180       0.426  26.558   6.808  1.00109.83           O  
ANISOU  941  O   ILE A 180    14463  14077  13190     24    254    -52       O  
ATOM    942  CB  ILE A 180      -1.505  26.298   9.545  1.00110.20           C  
ANISOU  942  CB  ILE A 180    14403  14216  13252    -33    361   -167       C  
ATOM    943  CG1 ILE A 180      -2.196  25.093  10.173  1.00109.44           C  
ANISOU  943  CG1 ILE A 180    14292  14152  13139   -111    430   -202       C  
ATOM    944  CG2 ILE A 180      -2.336  26.842   8.388  1.00113.18           C  
ANISOU  944  CG2 ILE A 180    14718  14627  13659      4    300   -194       C  
ATOM    945  CD1 ILE A 180      -3.606  25.393  10.635  1.00112.68           C  
ANISOU  945  CD1 ILE A 180    14611  14625  13578   -116    448   -276       C  
ATOM    946  N   CYS A 181       0.768  28.105   8.415  1.00128.28           N  
ANISOU  946  N   CYS A 181    16791  16395  15554     87    259    -60       N  
ATOM    947  CA  CYS A 181       1.262  29.120   7.493  1.00129.48           C  
ANISOU  947  CA  CYS A 181    16958  16515  15724    149    200    -29       C  
ATOM    948  C   CYS A 181       2.392  28.572   6.639  1.00128.64           C  
ANISOU  948  C   CYS A 181    16923  16358  15595    133    195     27       C  
ATOM    949  O   CYS A 181       2.492  28.871   5.442  1.00129.91           O  
ANISOU  949  O   CYS A 181    17096  16509  15756    158    152     48       O  
ATOM    950  CB  CYS A 181       1.742  30.332   8.291  1.00128.01           C  
ANISOU  950  CB  CYS A 181    16776  16300  15561    202    190    -24       C  
ATOM    951  SG  CYS A 181       0.421  31.399   8.888  1.00125.24           S  
ANISOU  951  SG  CYS A 181    16335  16000  15249    246    176    -90       S  
ATOM    952  N   ILE A 182       3.241  27.742   7.242  1.00111.57           N  
ANISOU  952  N   ILE A 182    14812  14165  13414     92    238     51       N  
ATOM    953  CA  ILE A 182       4.470  27.294   6.606  1.00111.88           C  
ANISOU  953  CA  ILE A 182    14920  14148  13442     81    239    101       C  
ATOM    954  C   ILE A 182       4.164  26.377   5.428  1.00111.23           C  
ANISOU  954  C   ILE A 182    14841  14080  13339     43    235    103       C  
ATOM    955  O   ILE A 182       4.918  26.330   4.448  1.00109.09           O  
ANISOU  955  O   ILE A 182    14614  13773  13063     49    219    138       O  
ATOM    956  CB  ILE A 182       5.324  26.614   7.684  1.00109.15           C  
ANISOU  956  CB  ILE A 182    14619  13769  13085     48    283    119       C  
ATOM    957  CG1 ILE A 182       6.564  25.963   7.126  1.00106.96           C  
ANISOU  957  CG1 ILE A 182    14404  13433  12801     29    290    164       C  
ATOM    958  CG2 ILE A 182       4.556  25.525   8.344  1.00109.02           C  
ANISOU  958  CG2 ILE A 182    14584  13792  13048    -11    328     90       C  
ATOM    959  CD1 ILE A 182       7.553  25.863   8.207  1.00103.77           C  
ANISOU  959  CD1 ILE A 182    14040  12987  12400     28    311    183       C  
ATOM    960  N   TRP A 183       3.059  25.634   5.506  1.00139.83           N  
ANISOU  960  N   TRP A 183    18419  17757  16952      2    253     63       N  
ATOM    961  CA  TRP A 183       2.602  24.826   4.382  1.00141.69           C  
ANISOU  961  CA  TRP A 183    18648  18014  17171    -32    245     54       C  
ATOM    962  C   TRP A 183       1.950  25.694   3.316  1.00141.84           C  
ANISOU  962  C   TRP A 183    18633  18061  17197     15    182     42       C  
ATOM    963  O   TRP A 183       2.131  25.452   2.118  1.00142.43           O  
ANISOU  963  O   TRP A 183    18734  18128  17254     11    158     59       O  
ATOM    964  CB  TRP A 183       1.625  23.752   4.866  1.00142.01           C  
ANISOU  964  CB  TRP A 183    18649  18102  17204    -93    287     10       C  
ATOM    965  CG  TRP A 183       2.285  22.653   5.638  1.00141.22           C  
ANISOU  965  CG  TRP A 183    18598  17971  17090   -148    347     28       C  
ATOM    966  CD1 TRP A 183       2.937  22.773   6.830  1.00140.20           C  
ANISOU  966  CD1 TRP A 183    18500  17811  16961   -144    375     47       C  
ATOM    967  CD2 TRP A 183       2.358  21.268   5.279  1.00145.87           C  
ANISOU  967  CD2 TRP A 183    19210  18552  17661   -213    382     31       C  
ATOM    968  NE1 TRP A 183       3.413  21.553   7.235  1.00145.07           N  
ANISOU  968  NE1 TRP A 183    19160  18400  17560   -200    422     64       N  
ATOM    969  CE2 TRP A 183       3.066  20.610   6.303  1.00146.51           C  
ANISOU  969  CE2 TRP A 183    19338  18594  17734   -243    429     54       C  
ATOM    970  CE3 TRP A 183       1.890  20.519   4.194  1.00147.81           C  
ANISOU  970  CE3 TRP A 183    19444  18818  17898   -247    375     13       C  
ATOM    971  CZ2 TRP A 183       3.329  19.239   6.269  1.00140.59           C  
ANISOU  971  CZ2 TRP A 183    18624  17822  16971   -305    472     64       C  
ATOM    972  CZ3 TRP A 183       2.147  19.156   4.165  1.00143.06           C  
ANISOU  972  CZ3 TRP A 183    18876  18197  17284   -312    421     19       C  
ATOM    973  CH2 TRP A 183       2.860  18.533   5.196  1.00142.50           C  
ANISOU  973  CH2 TRP A 183    18852  18084  17209   -340    469     45       C  
ATOM    974  N   LEU A 184       1.190  26.710   3.738  1.00119.67           N  
ANISOU  974  N   LEU A 184    15771  15284  14415     61    155     13       N  
ATOM    975  CA  LEU A 184       0.587  27.634   2.781  1.00121.21           C  
ANISOU  975  CA  LEU A 184    15935  15499  14620    115     88      5       C  
ATOM    976  C   LEU A 184       1.657  28.380   1.996  1.00122.14           C  
ANISOU  976  C   LEU A 184    16117  15559  14730    158     56     62       C  
ATOM    977  O   LEU A 184       1.503  28.620   0.793  1.00121.01           O  
ANISOU  977  O   LEU A 184    15987  15420  14573    178      8     74       O  
ATOM    978  CB  LEU A 184      -0.333  28.625   3.498  1.00124.36           C  
ANISOU  978  CB  LEU A 184    16262  15932  15055    160     69    -37       C  
ATOM    979  CG  LEU A 184      -1.247  28.109   4.613  1.00126.10           C  
ANISOU  979  CG  LEU A 184    16421  16202  15290    121    116    -94       C  
ATOM    980  CD1 LEU A 184      -2.100  29.237   5.172  1.00124.18           C  
ANISOU  980  CD1 LEU A 184    16107  15987  15087    174     92   -136       C  
ATOM    981  CD2 LEU A 184      -2.123  26.968   4.125  1.00127.65           C  
ANISOU  981  CD2 LEU A 184    16582  16446  15475     64    128   -131       C  
ATOM    982  N   LEU A 185       2.744  28.772   2.667  1.00135.02           N  
ANISOU  982  N   LEU A 185    17792  17137  16372    172     80     95       N  
ATOM    983  CA  LEU A 185       3.871  29.377   1.965  1.00132.82           C  
ANISOU  983  CA  LEU A 185    17578  16798  16091    203     62    147       C  
ATOM    984  C   LEU A 185       4.449  28.413   0.938  1.00130.05           C  
ANISOU  984  C   LEU A 185    17279  16427  15706    160     74    174       C  
ATOM    985  O   LEU A 185       4.654  28.776  -0.226  1.00129.28           O  
ANISOU  985  O   LEU A 185    17215  16314  15593    180     41    198       O  
ATOM    986  CB  LEU A 185       4.944  29.804   2.966  1.00130.66           C  
ANISOU  986  CB  LEU A 185    17334  16472  15838    216     91    170       C  
ATOM    987  N   SER A 186       4.716  27.171   1.352  1.00131.30           N  
ANISOU  987  N   SER A 186    17450  16584  15852     99    124    168       N  
ATOM    988  CA  SER A 186       5.191  26.162   0.411  1.00131.95           C  
ANISOU  988  CA  SER A 186    17578  16651  15907     54    140    185       C  
ATOM    989  C   SER A 186       4.148  25.851  -0.656  1.00131.74           C  
ANISOU  989  C   SER A 186    17524  16675  15855     43    106    159       C  
ATOM    990  O   SER A 186       4.504  25.441  -1.767  1.00128.94           O  
ANISOU  990  O   SER A 186    17211  16307  15472     25    100    176       O  
ATOM    991  CB  SER A 186       5.574  24.882   1.154  1.00129.09           C  
ANISOU  991  CB  SER A 186    17228  16276  15542     -6    199    181       C  
ATOM    992  OG  SER A 186       6.478  25.137   2.211  1.00126.29           O  
ANISOU  992  OG  SER A 186    16896  15878  15209      5    224    201       O  
ATOM    993  N   SER A 187       2.861  26.034  -0.335  1.00135.47           N  
ANISOU  993  N   SER A 187    17925  17208  16337     52     83    114       N  
ATOM    994  CA  SER A 187       1.793  25.708  -1.278  1.00136.14           C  
ANISOU  994  CA  SER A 187    17975  17348  16403     41     45     81       C  
ATOM    995  C   SER A 187       1.934  26.502  -2.567  1.00136.02           C  
ANISOU  995  C   SER A 187    17994  17320  16366     87    -16    109       C  
ATOM    996  O   SER A 187       1.657  25.986  -3.655  1.00133.63           O  
ANISOU  996  O   SER A 187    17706  17038  16031     66    -38    103       O  
ATOM    997  CB  SER A 187       0.427  25.962  -0.639  1.00136.45           C  
ANISOU  997  CB  SER A 187    17925  17450  16469     53     28     25       C  
ATOM    998  OG  SER A 187      -0.517  26.388  -1.608  1.00133.81           O  
ANISOU  998  OG  SER A 187    17554  17158  16129     83    -40      1       O  
ATOM    999  N   SER A 188       2.357  27.763  -2.461  1.00107.65           N  
ANISOU  999  N   SER A 188    14418  13694  12790    148    -42    139       N  
ATOM   1000  CA  SER A 188       2.632  28.562  -3.649  1.00105.00           C  
ANISOU 1000  CA  SER A 188    14130  13334  12431    191    -93    176       C  
ATOM   1001  C   SER A 188       3.589  27.839  -4.586  1.00102.68           C  
ANISOU 1001  C   SER A 188    13913  13002  12097    151    -66    209       C  
ATOM   1002  O   SER A 188       3.388  27.822  -5.805  1.00102.04           O  
ANISOU 1002  O   SER A 188    13862  12933  11977    154   -104    217       O  
ATOM   1003  CB  SER A 188       3.211  29.913  -3.237  1.00103.04           C  
ANISOU 1003  CB  SER A 188    13899  13038  12212    253   -106    208       C  
ATOM   1004  OG  SER A 188       4.597  29.795  -2.969  1.00103.55           O  
ANISOU 1004  OG  SER A 188    14024  13038  12281    236    -54    247       O  
ATOM   1005  N   VAL A 189       4.637  27.234  -4.032  1.00128.38           N  
ANISOU 1005  N   VAL A 189    17202  16213  15362    114     -3    226       N  
ATOM   1006  CA  VAL A 189       5.552  26.454  -4.854  1.00131.89           C  
ANISOU 1006  CA  VAL A 189    17713  16622  15777     72     30    251       C  
ATOM   1007  C   VAL A 189       4.869  25.189  -5.362  1.00132.27           C  
ANISOU 1007  C   VAL A 189    17743  16716  15796     14     36    215       C  
ATOM   1008  O   VAL A 189       5.096  24.758  -6.500  1.00131.33           O  
ANISOU 1008  O   VAL A 189    17669  16591  15637     -8     33    223       O  
ATOM   1009  CB  VAL A 189       6.834  26.150  -4.062  1.00132.06           C  
ANISOU 1009  CB  VAL A 189    17767  16582  15827     51     92    274       C  
ATOM   1010  CG1 VAL A 189       7.490  24.869  -4.559  1.00131.82           C  
ANISOU 1010  CG1 VAL A 189    17778  16530  15777    -11    139    277       C  
ATOM   1011  CG2 VAL A 189       7.778  27.334  -4.170  1.00129.85           C  
ANISOU 1011  CG2 VAL A 189    17530  16243  15563    100     85    317       C  
ATOM   1012  N   GLY A 190       4.020  24.579  -4.536  1.00136.93           N  
ANISOU 1012  N   GLY A 190    18270  17352  16405    -12     50    172       N  
ATOM   1013  CA  GLY A 190       3.268  23.423  -4.995  1.00136.30           C  
ANISOU 1013  CA  GLY A 190    18166  17319  16303    -67     54    131       C  
ATOM   1014  C   GLY A 190       2.341  23.755  -6.148  1.00136.10           C  
ANISOU 1014  C   GLY A 190    18125  17340  16245    -45    -15    112       C  
ATOM   1015  O   GLY A 190       2.206  22.976  -7.095  1.00136.16           O  
ANISOU 1015  O   GLY A 190    18153  17364  16216    -84    -19     98       O  
ATOM   1016  N   ILE A 191       1.695  24.921  -6.088  1.00101.63           N  
ANISOU 1016  N   ILE A 191    13724  12997  11892     18    -73    110       N  
ATOM   1017  CA  ILE A 191       0.776  25.316  -7.152  1.00101.59           C  
ANISOU 1017  CA  ILE A 191    13704  13038  11859     47   -151     92       C  
ATOM   1018  C   ILE A 191       1.543  25.636  -8.433  1.00 99.33           C  
ANISOU 1018  C   ILE A 191    13507  12713  11521     61   -173    140       C  
ATOM   1019  O   ILE A 191       1.101  25.296  -9.537  1.00 97.48           O  
ANISOU 1019  O   ILE A 191    13288  12509  11241     48   -213    126       O  
ATOM   1020  CB  ILE A 191      -0.100  26.502  -6.701  1.00101.26           C  
ANISOU 1020  CB  ILE A 191    13600  13024  11852    115   -208     77       C  
ATOM   1021  CG1 ILE A 191      -0.816  26.215  -5.372  1.00100.45           C  
ANISOU 1021  CG1 ILE A 191    13411  12957  11800     98   -176     28       C  
ATOM   1022  CG2 ILE A 191      -1.133  26.834  -7.765  1.00101.21           C  
ANISOU 1022  CG2 ILE A 191    13569  13066  11818    147   -296     55       C  
ATOM   1023  CD1 ILE A 191      -1.301  24.789  -5.187  1.00102.83           C  
ANISOU 1023  CD1 ILE A 191    13677  13296  12099     22   -132    -19       C  
ATOM   1024  N   SER A 192       2.699  26.297  -8.315  1.00106.84           N  
ANISOU 1024  N   SER A 192    14519  13598  12478     85   -147    193       N  
ATOM   1025  CA  SER A 192       3.476  26.627  -9.507  1.00106.36           C  
ANISOU 1025  CA  SER A 192    14547  13497  12369     95   -158    238       C  
ATOM   1026  C   SER A 192       3.955  25.368 -10.217  1.00104.20           C  
ANISOU 1026  C   SER A 192    14318  13216  12056     26   -115    231       C  
ATOM   1027  O   SER A 192       3.895  25.285 -11.448  1.00106.63           O  
ANISOU 1027  O   SER A 192    14674  13533  12307     20   -144    238       O  
ATOM   1028  CB  SER A 192       4.665  27.521  -9.143  1.00108.02           C  
ANISOU 1028  CB  SER A 192    14808  13634  12603    127   -128    291       C  
ATOM   1029  OG  SER A 192       5.809  26.756  -8.795  1.00104.45           O  
ANISOU 1029  OG  SER A 192    14389  13133  12163     78    -50    303       O  
ATOM   1030  N   ALA A 193       4.411  24.366  -9.457  1.00 90.93           N  
ANISOU 1030  N   ALA A 193    12623  11522  10405    -27    -45    216       N  
ATOM   1031  CA  ALA A 193       4.988  23.163 -10.058  1.00 90.83           C  
ANISOU 1031  CA  ALA A 193    12653  11493  10364    -92      4    210       C  
ATOM   1032  C   ALA A 193       3.945  22.323 -10.786  1.00 91.42           C  
ANISOU 1032  C   ALA A 193    12701  11631  10403   -129    -27    161       C  
ATOM   1033  O   ALA A 193       4.288  21.586 -11.716  1.00 91.57           O  
ANISOU 1033  O   ALA A 193    12768  11643  10381   -171     -8    157       O  
ATOM   1034  CB  ALA A 193       5.683  22.323  -8.989  1.00 91.12           C  
ANISOU 1034  CB  ALA A 193    12680  11496  10447   -134     79    206       C  
ATOM   1035  N   ILE A 194       2.680  22.407 -10.373  1.00 91.79           N  
ANISOU 1035  N   ILE A 194    12668  11740  10467   -115    -71    120       N  
ATOM   1036  CA  ILE A 194       1.617  21.698 -11.078  1.00 92.44           C  
ANISOU 1036  CA  ILE A 194    12716  11887  10520   -146   -108     68       C  
ATOM   1037  C   ILE A 194       1.467  22.245 -12.496  1.00 93.06           C  
ANISOU 1037  C   ILE A 194    12847  11978  10533   -116   -176     83       C  
ATOM   1038  O   ILE A 194       1.710  21.537 -13.481  1.00 93.29           O  
ANISOU 1038  O   ILE A 194    12926  12007  10513   -158   -168     76       O  
ATOM   1039  CB  ILE A 194       0.299  21.782 -10.284  1.00 92.76           C  
ANISOU 1039  CB  ILE A 194    12653  11988  10601   -134   -140     17       C  
ATOM   1040  CG1 ILE A 194       0.308  20.769  -9.140  1.00 92.34           C  
ANISOU 1040  CG1 ILE A 194    12558  11933  10593   -190    -65    -11       C  
ATOM   1041  CG2 ILE A 194      -0.907  21.536 -11.179  1.00 93.61           C  
ANISOU 1041  CG2 ILE A 194    12723  12166  10680   -138   -210    -34       C  
ATOM   1042  CD1 ILE A 194      -1.050  20.523  -8.524  1.00 92.77           C  
ANISOU 1042  CD1 ILE A 194    12513  12054  10683   -200    -82    -74       C  
ATOM   1043  N   VAL A 195       1.105  23.527 -12.620  1.00117.17           N  
ANISOU 1043  N   VAL A 195    15897  15038  13585    -44   -244    106       N  
ATOM   1044  CA  VAL A 195       0.877  24.112 -13.942  1.00119.57           C  
ANISOU 1044  CA  VAL A 195    16254  15354  13822    -11   -318    124       C  
ATOM   1045  C   VAL A 195       2.171  24.143 -14.753  1.00121.44           C  
ANISOU 1045  C   VAL A 195    16603  15528  14010    -26   -276    176       C  
ATOM   1046  O   VAL A 195       2.211  23.698 -15.907  1.00125.72           O  
ANISOU 1046  O   VAL A 195    17201  16081  14487    -53   -290    172       O  
ATOM   1047  CB  VAL A 195       0.238  25.511 -13.813  1.00119.88           C  
ANISOU 1047  CB  VAL A 195    16265  15405  13877     74   -398    140       C  
ATOM   1048  CG1 VAL A 195       1.062  26.423 -12.919  1.00117.41           C  
ANISOU 1048  CG1 VAL A 195    15967  15032  13612    112   -360    188       C  
ATOM   1049  CG2 VAL A 195       0.080  26.148 -15.183  1.00120.93           C  
ANISOU 1049  CG2 VAL A 195    16467  15543  13938    112   -476    168       C  
ATOM   1050  N   LEU A 196       3.253  24.638 -14.150  1.00 93.19           N  
ANISOU 1050  N   LEU A 196    13058  11883  10465    -12   -221    222       N  
ATOM   1051  CA  LEU A 196       4.523  24.798 -14.848  1.00 93.00           C  
ANISOU 1051  CA  LEU A 196    13136  11795  10406    -23   -177    271       C  
ATOM   1052  C   LEU A 196       5.209  23.458 -15.103  1.00 92.71           C  
ANISOU 1052  C   LEU A 196    13128  11741  10358   -101   -101    252       C  
ATOM   1053  O   LEU A 196       6.147  23.393 -15.908  1.00 92.72           O  
ANISOU 1053  O   LEU A 196    13213  11697  10321   -121    -64    280       O  
ATOM   1054  CB  LEU A 196       5.418  25.721 -14.013  1.00 92.58           C  
ANISOU 1054  CB  LEU A 196    13095  11678  10405     14   -142    317       C  
ATOM   1055  CG  LEU A 196       4.955  27.179 -13.859  1.00 92.70           C  
ANISOU 1055  CG  LEU A 196    13098  11693  10432     94   -209    344       C  
ATOM   1056  CD1 LEU A 196       6.110  28.125 -13.678  1.00 92.33           C  
ANISOU 1056  CD1 LEU A 196    13108  11568  10405    124   -173    400       C  
ATOM   1057  CD2 LEU A 196       4.106  27.627 -15.041  1.00 93.62           C  
ANISOU 1057  CD2 LEU A 196    13243  11849  10481    127   -298    347       C  
ATOM   1058  N   GLY A 197       4.774  22.397 -14.424  1.00 95.68           N  
ANISOU 1058  N   GLY A 197    13438  12148  10770   -146    -73    204       N  
ATOM   1059  CA  GLY A 197       5.383  21.090 -14.596  1.00100.23           C  
ANISOU 1059  CA  GLY A 197    14036  12704  11343   -218     -2    184       C  
ATOM   1060  C   GLY A 197       4.794  20.350 -15.781  1.00104.08           C  
ANISOU 1060  C   GLY A 197    14543  13237  11766   -256    -30    146       C  
ATOM   1061  O   GLY A 197       3.570  20.273 -15.942  1.00103.99           O  
ANISOU 1061  O   GLY A 197    14478  13293  11741   -249    -94    107       O  
ATOM   1062  N   GLY A 198       5.670  19.800 -16.611  1.00126.36           N  
ANISOU 1062  N   GLY A 198    17439  16023  14551   -298     18    155       N  
ATOM   1063  CA  GLY A 198       5.262  19.044 -17.769  1.00126.26           C  
ANISOU 1063  CA  GLY A 198    17455  16046  14472   -340      1    118       C  
ATOM   1064  C   GLY A 198       6.421  18.217 -18.276  1.00130.75           C  
ANISOU 1064  C   GLY A 198    18090  16561  15028   -397     85    120       C  
ATOM   1065  O   GLY A 198       7.473  18.132 -17.639  1.00129.07           O  
ANISOU 1065  O   GLY A 198    17890  16286  14867   -405    155    146       O  
ATOM   1066  N   THR A 199       6.217  17.611 -19.444  1.00117.14           N  
ANISOU 1066  N   THR A 199    16409  14863  13237   -436     75     91       N  
ATOM   1067  CA  THR A 199       7.199  16.719 -20.046  1.00114.08           C  
ANISOU 1067  CA  THR A 199    16081  14431  12833   -496    154     81       C  
ATOM   1068  C   THR A 199       7.538  17.189 -21.453  1.00113.79           C  
ANISOU 1068  C   THR A 199    16144  14388  12703   -492    139    101       C  
ATOM   1069  O   THR A 199       6.640  17.434 -22.264  1.00113.75           O  
ANISOU 1069  O   THR A 199    16153  14440  12628   -478     61     86       O  
ATOM   1070  CB  THR A 199       6.675  15.282 -20.082  1.00112.72           C  
ANISOU 1070  CB  THR A 199    15867  14292  12671   -562    175     14       C  
ATOM   1071  OG1 THR A 199       5.354  15.276 -20.637  1.00115.13           O  
ANISOU 1071  OG1 THR A 199    16141  14677  12926   -557     90    -25       O  
ATOM   1072  CG2 THR A 199       6.633  14.695 -18.683  1.00110.74           C  
ANISOU 1072  CG2 THR A 199    15536  14027  12512   -576    216      1       C  
ATOM   1073  N   LYS A 200       8.833  17.308 -21.737  1.00127.22           N  
ANISOU 1073  N   LYS A 200    17915  16018  14403   -505    212    134       N  
ATOM   1074  CA  LYS A 200       9.327  17.686 -23.054  1.00130.74           C  
ANISOU 1074  CA  LYS A 200    18467  16447  14762   -512    218    154       C  
ATOM   1075  C   LYS A 200      10.281  16.617 -23.568  1.00133.17           C  
ANISOU 1075  C   LYS A 200    18819  16713  15068   -582    313    126       C  
ATOM   1076  O   LYS A 200      11.085  16.072 -22.806  1.00132.29           O  
ANISOU 1076  O   LYS A 200    18678  16550  15038   -605    388    122       O  
ATOM   1077  CB  LYS A 200      10.038  19.046 -23.017  1.00126.51           C  
ANISOU 1077  CB  LYS A 200    17983  15860  14225   -458    221    223       C  
ATOM   1078  N   VAL A 201      10.183  16.314 -24.863  1.00154.57           N  
ANISOU 1078  N   VAL A 201    21599  19444  17685   -615    308    104       N  
ATOM   1079  CA  VAL A 201      11.107  15.372 -25.486  1.00156.38           C  
ANISOU 1079  CA  VAL A 201    21880  19632  17906   -682    400     75       C  
ATOM   1080  C   VAL A 201      12.482  16.017 -25.611  1.00161.13           C  
ANISOU 1080  C   VAL A 201    22549  20152  18522   -674    476    123       C  
ATOM   1081  O   VAL A 201      12.620  17.131 -26.134  1.00165.16           O  
ANISOU 1081  O   VAL A 201    23125  20653  18976   -636    450    171       O  
ATOM   1082  CB  VAL A 201      10.567  14.918 -26.851  1.00157.91           C  
ANISOU 1082  CB  VAL A 201    22134  19876  17989   -719    370     36       C  
ATOM   1083  CG1 VAL A 201      10.079  16.114 -27.664  1.00154.35           C  
ANISOU 1083  CG1 VAL A 201    21752  19457  17439   -669    287     77       C  
ATOM   1084  CG2 VAL A 201      11.634  14.149 -27.615  1.00161.18           C  
ANISOU 1084  CG2 VAL A 201    22616  20240  18384   -783    472     11       C  
ATOM   1085  N   ARG A 202      13.512  15.317 -25.123  1.00215.51           N  
ANISOU 1085  N   ARG A 202    29418  26977  25489   -710    570    109       N  
ATOM   1086  CA  ARG A 202      14.858  15.887 -25.111  1.00218.71           C  
ANISOU 1086  CA  ARG A 202    29872  27301  25928   -703    647    147       C  
ATOM   1087  C   ARG A 202      15.395  16.099 -26.523  1.00223.18           C  
ANISOU 1087  C   ARG A 202    30549  27849  26399   -732    686    151       C  
ATOM   1088  O   ARG A 202      15.989  17.142 -26.815  1.00225.72           O  
ANISOU 1088  O   ARG A 202    30932  28132  26699   -705    702    200       O  
ATOM   1089  CB  ARG A 202      15.804  14.992 -24.310  1.00215.58           C  
ANISOU 1089  CB  ARG A 202    29426  26844  25640   -735    733    124       C  
ATOM   1090  N   GLU A 203      15.198  15.129 -27.409  1.00181.06           N  
ANISOU 1090  N   GLU A 203    25246  22541  21008   -789    705     99       N  
ATOM   1091  CA  GLU A 203      15.715  15.239 -28.767  1.00183.74           C  
ANISOU 1091  CA  GLU A 203    25697  22865  21252   -823    750     96       C  
ATOM   1092  C   GLU A 203      14.586  15.464 -29.764  1.00184.01           C  
ANISOU 1092  C   GLU A 203    25782  22976  21156   -817    658     91       C  
ATOM   1093  O   GLU A 203      14.830  15.790 -30.924  1.00181.63           O  
ANISOU 1093  O   GLU A 203    25586  22672  20754   -834    673    100       O  
ATOM   1094  CB  GLU A 203      16.513  13.996 -29.135  1.00182.35           C  
ANISOU 1094  CB  GLU A 203    25531  22651  21104   -896    852     38       C  
ATOM   1095  N   ASP A 206      14.367  11.477 -28.656  1.00134.98           N  
ANISOU 1095  N   ASP A 206    19380  16777  15128   -960    764    -93       N  
ATOM   1096  CA  ASP A 206      14.618  10.066 -28.372  1.00137.55           C  
ANISOU 1096  CA  ASP A 206    19659  17081  15523  -1017    827   -154       C  
ATOM   1097  C   ASP A 206      14.302   9.741 -26.919  1.00137.58           C  
ANISOU 1097  C   ASP A 206    19556  17081  15638   -995    809   -149       C  
ATOM   1098  O   ASP A 206      13.964   8.606 -26.578  1.00133.75           O  
ANISOU 1098  O   ASP A 206    19016  16604  15198  -1033    822   -199       O  
ATOM   1099  CB  ASP A 206      16.071   9.702 -28.681  1.00136.80           C  
ANISOU 1099  CB  ASP A 206    19609  16902  15469  -1055    946   -163       C  
ATOM   1100  CG  ASP A 206      16.213   8.920 -29.971  1.00139.60           C  
ANISOU 1100  CG  ASP A 206    20032  17264  15747  -1121    993   -222       C  
ATOM   1101  OD1 ASP A 206      15.180   8.649 -30.621  1.00140.47           O  
ANISOU 1101  OD1 ASP A 206    20155  17446  15771  -1137    929   -255       O  
ATOM   1102  OD2 ASP A 206      17.357   8.567 -30.332  1.00136.42           O  
ANISOU 1102  OD2 ASP A 206    19667  16795  15372  -1157   1094   -239       O  
ATOM   1103  N   VAL A 207      14.417  10.761 -26.071  1.00209.64           N  
ANISOU 1103  N   VAL A 207    28656  26192  24805   -934    779    -90       N  
ATOM   1104  CA  VAL A 207      14.274  10.634 -24.625  1.00202.32           C  
ANISOU 1104  CA  VAL A 207    27638  25252  23980   -907    768    -76       C  
ATOM   1105  C   VAL A 207      13.265  11.662 -24.136  1.00198.22           C  
ANISOU 1105  C   VAL A 207    27085  24791  23440   -846    669    -38       C  
ATOM   1106  O   VAL A 207      13.459  12.868 -24.332  1.00201.37           O  
ANISOU 1106  O   VAL A 207    27525  25183  23804   -799    643     12       O  
ATOM   1107  CB  VAL A 207      15.617  10.824 -23.905  1.00202.94           C  
ANISOU 1107  CB  VAL A 207    27712  25243  24152   -894    842    -44       C  
ATOM   1108  CG1 VAL A 207      15.389  11.012 -22.426  1.00202.12           C  
ANISOU 1108  CG1 VAL A 207    27527  25136  24135   -853    812    -17       C  
ATOM   1109  CG2 VAL A 207      16.523   9.626 -24.155  1.00204.80           C  
ANISOU 1109  CG2 VAL A 207    27958  25422  24436   -954    937    -89       C  
ATOM   1110  N   ILE A 208      12.197  11.193 -23.497  1.00107.24           N  
ANISOU 1110  N   ILE A 208    15487  13320  11940   -846    618    -64       N  
ATOM   1111  CA  ILE A 208      11.258  12.088 -22.831  1.00106.27           C  
ANISOU 1111  CA  ILE A 208    15315  13246  11818   -787    532    -35       C  
ATOM   1112  C   ILE A 208      11.845  12.515 -21.489  1.00107.27           C  
ANISOU 1112  C   ILE A 208    15396  13323  12039   -750    556      7       C  
ATOM   1113  O   ILE A 208      12.490  11.724 -20.787  1.00105.54           O  
ANISOU 1113  O   ILE A 208    15149  13055  11898   -776    619     -4       O  
ATOM   1114  CB  ILE A 208       9.877  11.420 -22.671  1.00105.44           C  
ANISOU 1114  CB  ILE A 208    15142  13216  11704   -805    473    -86       C  
ATOM   1115  CG1 ILE A 208       8.752  12.447 -22.804  1.00107.69           C  
ANISOU 1115  CG1 ILE A 208    15410  13570  11936   -751    367    -69       C  
ATOM   1116  CG2 ILE A 208       9.741  10.740 -21.339  1.00105.16           C  
ANISOU 1116  CG2 ILE A 208    15023  13166  11766   -816    498    -98       C  
ATOM   1117  CD1 ILE A 208       7.361  11.854 -22.630  1.00104.99           C  
ANISOU 1117  CD1 ILE A 208    14994  13304  11594   -767    307   -124       C  
ATOM   1118  N   GLU A 209      11.659  13.788 -21.148  1.00126.88           N  
ANISOU 1118  N   GLU A 209    17877  15816  14515   -686    504     56       N  
ATOM   1119  CA  GLU A 209      12.165  14.352 -19.905  1.00122.76           C  
ANISOU 1119  CA  GLU A 209    17316  15252  14074   -645    518     96       C  
ATOM   1120  C   GLU A 209      11.024  15.033 -19.167  1.00121.15           C  
ANISOU 1120  C   GLU A 209    17050  15106  13876   -596    436    107       C  
ATOM   1121  O   GLU A 209      10.121  15.598 -19.790  1.00120.43           O  
ANISOU 1121  O   GLU A 209    16968  15072  13719   -572    363    106       O  
ATOM   1122  CB  GLU A 209      13.307  15.354 -20.160  1.00120.20           C  
ANISOU 1122  CB  GLU A 209    17054  14866  13750   -615    551    146       C  
ATOM   1123  CG  GLU A 209      12.863  16.797 -20.317  1.00121.78           C  
ANISOU 1123  CG  GLU A 209    17274  15090  13907   -552    482    191       C  
ATOM   1124  CD  GLU A 209      13.962  17.782 -19.994  1.00123.71           C  
ANISOU 1124  CD  GLU A 209    17548  15266  14190   -517    518    242       C  
ATOM   1125  OE1 GLU A 209      15.027  17.345 -19.510  1.00120.12           O  
ANISOU 1125  OE1 GLU A 209    17087  14749  13805   -538    591    240       O  
ATOM   1126  OE2 GLU A 209      13.761  18.995 -20.219  1.00122.92           O  
ANISOU 1126  OE2 GLU A 209    17477  15173  14055   -468    472    282       O  
ATOM   1127  N   CYS A 210      11.051  14.952 -17.839  1.00122.25           N  
ANISOU 1127  N   CYS A 210    17125  15230  14094   -581    446    115       N  
ATOM   1128  CA  CYS A 210      10.073  15.626 -16.995  1.00121.27           C  
ANISOU 1128  CA  CYS A 210    16937  15152  13986   -534    380    124       C  
ATOM   1129  C   CYS A 210      10.796  16.653 -16.141  1.00121.62           C  
ANISOU 1129  C   CYS A 210    16981  15150  14080   -482    388    175       C  
ATOM   1130  O   CYS A 210      11.727  16.309 -15.403  1.00122.33           O  
ANISOU 1130  O   CYS A 210    17064  15182  14233   -492    446    186       O  
ATOM   1131  CB  CYS A 210       9.316  14.645 -16.103  1.00120.79           C  
ANISOU 1131  CB  CYS A 210    16800  15124  13970   -564    382     84       C  
ATOM   1132  SG  CYS A 210       8.651  15.419 -14.611  1.00113.26           S  
ANISOU 1132  SG  CYS A 210    15769  14194  13071   -510    341    102       S  
ATOM   1133  N   SER A 211      10.360  17.901 -16.237  1.00119.19           N  
ANISOU 1133  N   SER A 211    16677  14864  13745   -425    327    205       N  
ATOM   1134  CA  SER A 211      10.920  19.002 -15.472  1.00115.91           C  
ANISOU 1134  CA  SER A 211    16258  14409  13373   -371    326    251       C  
ATOM   1135  C   SER A 211       9.896  20.127 -15.490  1.00119.00           C  
ANISOU 1135  C   SER A 211    16628  14851  13734   -312    241    265       C  
ATOM   1136  O   SER A 211       8.742  19.930 -15.886  1.00119.33           O  
ANISOU 1136  O   SER A 211    16645  14960  13737   -315    185    235       O  
ATOM   1137  CB  SER A 211      12.280  19.430 -16.033  1.00115.15           C  
ANISOU 1137  CB  SER A 211    16237  14240  13275   -371    380    285       C  
ATOM   1138  OG  SER A 211      12.145  19.936 -17.348  1.00122.71           O  
ANISOU 1138  OG  SER A 211    17263  15210  14151   -366    354    297       O  
ATOM   1139  N   LEU A 212      10.308  21.308 -15.046  1.00120.63           N  
ANISOU 1139  N   LEU A 212    16844  15025  13967   -259    230    307       N  
ATOM   1140  CA  LEU A 212       9.416  22.456 -14.998  1.00118.41           C  
ANISOU 1140  CA  LEU A 212    16541  14781  13667   -197    151    323       C  
ATOM   1141  C   LEU A 212       9.460  23.123 -16.371  1.00119.95           C  
ANISOU 1141  C   LEU A 212    16818  14974  13785   -181    120    350       C  
ATOM   1142  O   LEU A 212      10.508  23.635 -16.780  1.00120.85           O  
ANISOU 1142  O   LEU A 212    16999  15026  13891   -176    160    387       O  
ATOM   1143  CB  LEU A 212       9.859  23.425 -13.906  1.00119.12           C  
ANISOU 1143  CB  LEU A 212    16607  14833  13821   -148    156    356       C  
ATOM   1144  CG  LEU A 212       8.787  24.136 -13.091  1.00116.26           C  
ANISOU 1144  CG  LEU A 212    16174  14517  13482    -97     92    349       C  
ATOM   1145  CD1 LEU A 212       7.627  23.196 -12.839  1.00111.44           C  
ANISOU 1145  CD1 LEU A 212    15497  13978  12870   -127     68    296       C  
ATOM   1146  CD2 LEU A 212       9.364  24.674 -11.798  1.00113.71           C  
ANISOU 1146  CD2 LEU A 212    15820  14154  13232    -69    118    367       C  
ATOM   1147  N   GLN A 213       8.336  23.111 -17.084  1.00119.29           N  
ANISOU 1147  N   GLN A 213    16729  14954  13641   -173     48    329       N  
ATOM   1148  CA  GLN A 213       8.328  23.470 -18.501  1.00122.42           C  
ANISOU 1148  CA  GLN A 213    17211  15354  13949   -169     18    348       C  
ATOM   1149  C   GLN A 213       8.276  24.985 -18.676  1.00122.92           C  
ANISOU 1149  C   GLN A 213    17310  15398  13996    -98    -34    400       C  
ATOM   1150  O   GLN A 213       7.321  25.632 -18.232  1.00122.89           O  
ANISOU 1150  O   GLN A 213    17252  15434  14009    -47   -107    398       O  
ATOM   1151  CB  GLN A 213       7.142  22.817 -19.205  1.00124.65           C  
ANISOU 1151  CB  GLN A 213    17473  15713  14173   -189    -44    302       C  
ATOM   1152  CG  GLN A 213       7.339  21.350 -19.545  1.00123.12           C  
ANISOU 1152  CG  GLN A 213    17282  15529  13968   -266     11    254       C  
ATOM   1153  CD  GLN A 213       8.755  21.030 -19.978  1.00125.10           C  
ANISOU 1153  CD  GLN A 213    17611  15709  14213   -307    104    275       C  
ATOM   1154  OE1 GLN A 213       9.202  21.471 -21.037  1.00131.66           O  
ANISOU 1154  OE1 GLN A 213    18531  16518  14977   -305    106    302       O  
ATOM   1155  NE2 GLN A 213       9.465  20.250 -19.170  1.00121.51           N  
ANISOU 1155  NE2 GLN A 213    17123  15217  13829   -344    180    261       N  
ATOM   1156  N   PHE A 214       9.275  25.545 -19.370  1.00132.06           N  
ANISOU 1156  N   PHE A 214    18560  16495  15121    -97      4    445       N  
ATOM   1157  CA  PHE A 214       9.442  26.987 -19.493  1.00132.09           C  
ANISOU 1157  CA  PHE A 214    18608  16463  15118    -35    -28    501       C  
ATOM   1158  C   PHE A 214       9.613  27.407 -20.946  1.00137.21           C  
ANISOU 1158  C   PHE A 214    19369  17097  15666    -35    -44    534       C  
ATOM   1159  O   PHE A 214      10.345  26.756 -21.702  1.00137.15           O  
ANISOU 1159  O   PHE A 214    19427  17067  15618    -90     19    529       O  
ATOM   1160  CB  PHE A 214      10.659  27.456 -18.687  1.00130.07           C  
ANISOU 1160  CB  PHE A 214    18355  16130  14938    -29     47    530       C  
ATOM   1161  CG  PHE A 214      10.331  27.839 -17.284  1.00130.79           C  
ANISOU 1161  CG  PHE A 214    18354  16228  15114     10     28    523       C  
ATOM   1162  CD1 PHE A 214       9.092  27.548 -16.756  1.00132.25           C  
ANISOU 1162  CD1 PHE A 214    18454  16484  15311     25    -34    485       C  
ATOM   1163  CD2 PHE A 214      11.256  28.472 -16.489  1.00127.77           C  
ANISOU 1163  CD2 PHE A 214    17966  15781  14799     28     75    549       C  
ATOM   1164  CE1 PHE A 214       8.784  27.885 -15.472  1.00127.44           C  
ANISOU 1164  CE1 PHE A 214    17764  15882  14776     57    -46    476       C  
ATOM   1165  CE2 PHE A 214      10.949  28.812 -15.197  1.00128.06           C  
ANISOU 1165  CE2 PHE A 214    17921  15827  14908     62     57    539       C  
ATOM   1166  CZ  PHE A 214       9.707  28.519 -14.688  1.00129.70           C  
ANISOU 1166  CZ  PHE A 214    18051  16106  15123     76     -1    503       C  
ATOM   1167  N   PRO A 215       8.959  28.495 -21.362  1.00131.39           N  
ANISOU 1167  N   PRO A 215    18661  16373  14889     27   -128    568       N  
ATOM   1168  CA  PRO A 215       9.126  28.982 -22.737  1.00130.63           C  
ANISOU 1168  CA  PRO A 215    18684  16259  14690     31   -147    608       C  
ATOM   1169  C   PRO A 215      10.564  29.404 -23.000  1.00130.28           C  
ANISOU 1169  C   PRO A 215    18726  16126  14650     10    -51    652       C  
ATOM   1170  O   PRO A 215      11.145  30.193 -22.251  1.00128.43           O  
ANISOU 1170  O   PRO A 215    18476  15837  14485     40    -21    681       O  
ATOM   1171  CB  PRO A 215       8.168  30.176 -22.788  1.00126.71           C  
ANISOU 1171  CB  PRO A 215    18183  15784  14178    112   -256    639       C  
ATOM   1172  CG  PRO A 215       7.069  29.735 -21.876  1.00129.13           C  
ANISOU 1172  CG  PRO A 215    18362  16159  14542    128   -312    586       C  
ATOM   1173  CD  PRO A 215       7.859  29.210 -20.693  1.00129.00           C  
ANISOU 1173  CD  PRO A 215    18282  16111  14621     94   -219    566       C  
ATOM   1174  N   ASP A 216      11.138  28.866 -24.076  1.00143.59           N  
ANISOU 1174  N   ASP A 216    20501  17796  16261    -44      0    651       N  
ATOM   1175  CA  ASP A 216      12.531  29.103 -24.425  1.00142.55           C  
ANISOU 1175  CA  ASP A 216    20451  17582  16131    -76    104    682       C  
ATOM   1176  C   ASP A 216      12.696  30.126 -25.542  1.00142.05           C  
ANISOU 1176  C   ASP A 216    20514  17483  15976    -53     86    742       C  
ATOM   1177  O   ASP A 216      13.792  30.247 -26.095  1.00141.89           O  
ANISOU 1177  O   ASP A 216    20577  17398  15936    -90    175    765       O  
ATOM   1178  CB  ASP A 216      13.208  27.788 -24.819  1.00138.77           C  
ANISOU 1178  CB  ASP A 216    19987  17099  15640   -158    192    638       C  
ATOM   1179  N   ASP A 217      11.643  30.861 -25.883  1.00148.45           N  
ANISOU 1179  N   ASP A 217    21340  18332  16733      6    -24    768       N  
ATOM   1180  CA  ASP A 217      11.710  31.858 -26.942  1.00148.67           C  
ANISOU 1180  CA  ASP A 217    21494  18326  16668     34    -52    830       C  
ATOM   1181  C   ASP A 217      12.051  33.245 -26.390  1.00149.85           C  
ANISOU 1181  C   ASP A 217    21651  18409  16875     93    -54    888       C  
ATOM   1182  O   ASP A 217      11.869  33.533 -25.206  1.00149.75           O  
ANISOU 1182  O   ASP A 217    21538  18397  16964    129    -69    876       O  
ATOM   1183  CB  ASP A 217      10.393  31.896 -27.726  1.00150.97           C  
ANISOU 1183  CB  ASP A 217    21809  18692  16862     68   -179    828       C  
ATOM   1184  CG  ASP A 217       9.229  32.447 -26.912  1.00153.31           C  
ANISOU 1184  CG  ASP A 217    22005  19032  17213    144   -291    823       C  
ATOM   1185  OD1 ASP A 217       9.354  32.590 -25.681  1.00155.46           O  
ANISOU 1185  OD1 ASP A 217    22178  19291  17598    161   -268    810       O  
ATOM   1186  OD2 ASP A 217       8.178  32.753 -27.516  1.00157.10           O  
ANISOU 1186  OD2 ASP A 217    22505  19561  17624    187   -404    831       O  
ATOM   1187  N   ASP A 218      12.555  34.102 -27.279  1.00153.91           N  
ANISOU 1187  N   ASP A 218    22292  18864  17321    101    -34    948       N  
ATOM   1188  CA  ASP A 218      12.855  35.507 -26.982  1.00149.03           C  
ANISOU 1188  CA  ASP A 218    21705  18177  16741    157    -39   1009       C  
ATOM   1189  C   ASP A 218      13.812  35.646 -25.797  1.00145.12           C  
ANISOU 1189  C   ASP A 218    21136  17626  16378    147     50    998       C  
ATOM   1190  O   ASP A 218      13.496  36.265 -24.779  1.00143.47           O  
ANISOU 1190  O   ASP A 218    20846  17413  16255    200     11   1000       O  
ATOM   1191  CB  ASP A 218      11.578  36.301 -26.713  1.00146.57           C  
ANISOU 1191  CB  ASP A 218    21353  17907  16432    244   -175   1028       C  
ATOM   1192  CG  ASP A 218      11.801  37.797 -26.787  1.00150.16           C  
ANISOU 1192  CG  ASP A 218    21875  18286  16892    302   -191   1100       C  
ATOM   1193  OD1 ASP A 218      12.963  38.246 -26.700  1.00148.33           O  
ANISOU 1193  OD1 ASP A 218    21691  17972  16697    278    -90   1128       O  
ATOM   1194  OD2 ASP A 218      10.803  38.531 -26.858  1.00152.43           O  
ANISOU 1194  OD2 ASP A 218    22158  18597  17160    374   -304   1124       O  
ATOM   1195  N   TYR A 219      15.000  35.060 -25.956  1.00112.86           N  
ANISOU 1195  N   TYR A 219    17080  13496  12308     77    170    982       N  
ATOM   1196  CA  TYR A 219      16.086  35.178 -24.978  1.00110.44           C  
ANISOU 1196  CA  TYR A 219    16716  13125  12120     61    262    971       C  
ATOM   1197  C   TYR A 219      15.615  34.892 -23.553  1.00111.70           C  
ANISOU 1197  C   TYR A 219    16731  13325  12385     90    224    930       C  
ATOM   1198  O   TYR A 219      16.158  35.437 -22.588  1.00109.66           O  
ANISOU 1198  O   TYR A 219    16420  13020  12224    110    256    934       O  
ATOM   1199  CB  TYR A 219      16.743  36.556 -25.044  1.00110.30           C  
ANISOU 1199  CB  TYR A 219    16766  13019  12123     92    294   1032       C  
ATOM   1200  CG  TYR A 219      17.105  37.028 -26.436  1.00111.12           C  
ANISOU 1200  CG  TYR A 219    17025  13080  12117     72    325   1083       C  
ATOM   1201  CD1 TYR A 219      16.151  37.591 -27.277  1.00109.18           C  
ANISOU 1201  CD1 TYR A 219    16856  12861  11764    115    227   1127       C  
ATOM   1202  CD2 TYR A 219      18.405  36.911 -26.907  1.00112.39           C  
ANISOU 1202  CD2 TYR A 219    17254  13170  12279      8    452   1087       C  
ATOM   1203  CE1 TYR A 219      16.487  38.026 -28.546  1.00110.54           C  
ANISOU 1203  CE1 TYR A 219    17179  12992  11828     96    255   1178       C  
ATOM   1204  CE2 TYR A 219      18.749  37.342 -28.172  1.00111.37           C  
ANISOU 1204  CE2 TYR A 219    17271  12999  12045    -15    488   1133       C  
ATOM   1205  CZ  TYR A 219      17.788  37.897 -28.987  1.00111.40           C  
ANISOU 1205  CZ  TYR A 219    17359  13032  11937     29    390   1181       C  
ATOM   1206  OH  TYR A 219      18.140  38.321 -30.243  1.00113.81           O  
ANISOU 1206  OH  TYR A 219    17819  13293  12130      4    427   1230       O  
ATOM   1207  N   SER A 220      14.601  34.038 -23.410  1.00104.72           N  
ANISOU 1207  N   SER A 220    15782  12527  11481     90    157    888       N  
ATOM   1208  CA  SER A 220      14.010  33.773 -22.106  1.00100.77           C  
ANISOU 1208  CA  SER A 220    15150  12070  11068    117    116    849       C  
ATOM   1209  C   SER A 220      14.947  32.882 -21.308  1.00 94.73           C  
ANISOU 1209  C   SER A 220    14323  11282  10386     64    209    807       C  
ATOM   1210  O   SER A 220      15.253  31.762 -21.721  1.00100.87           O  
ANISOU 1210  O   SER A 220    15111  12076  11138      4    258    774       O  
ATOM   1211  CB  SER A 220      12.635  33.122 -22.246  1.00101.73           C  
ANISOU 1211  CB  SER A 220    15222  12287  11142    128     22    814       C  
ATOM   1212  OG  SER A 220      11.660  34.065 -22.661  1.00103.42           O  
ANISOU 1212  OG  SER A 220    15463  12523  11306    194    -82    848       O  
ATOM   1213  N   TRP A 221      15.412  33.389 -20.175  1.00110.12           N  
ANISOU 1213  N   TRP A 221    16211  13193  12435     89    232    809       N  
ATOM   1214  CA  TRP A 221      16.216  32.622 -19.239  1.00110.53           C  
ANISOU 1214  CA  TRP A 221    16194  13226  12576     52    304    770       C  
ATOM   1215  C   TRP A 221      15.440  32.337 -17.959  1.00109.27           C  
ANISOU 1215  C   TRP A 221    15919  13120  12479     80    252    736       C  
ATOM   1216  O   TRP A 221      16.030  32.161 -16.891  1.00107.52           O  
ANISOU 1216  O   TRP A 221    15635  12874  12345     74    291    717       O  
ATOM   1217  CB  TRP A 221      17.519  33.353 -18.923  1.00112.01           C  
ANISOU 1217  CB  TRP A 221    16405  13322  12832     50    381    793       C  
ATOM   1218  CG  TRP A 221      17.322  34.708 -18.290  1.00115.28           C  
ANISOU 1218  CG  TRP A 221    16802  13709  13292    117    339    826       C  
ATOM   1219  CD1 TRP A 221      16.631  35.769 -18.806  1.00113.72           C  
ANISOU 1219  CD1 TRP A 221    16652  13512  13043    169    272    869       C  
ATOM   1220  CD2 TRP A 221      17.789  35.124 -17.003  1.00115.92           C  
ANISOU 1220  CD2 TRP A 221    16809  13758  13479    140    355    815       C  
ATOM   1221  NE1 TRP A 221      16.660  36.823 -17.929  1.00111.17           N  
ANISOU 1221  NE1 TRP A 221    16290  13156  12792    222    252    885       N  
ATOM   1222  CE2 TRP A 221      17.364  36.453 -16.813  1.00114.75           C  
ANISOU 1222  CE2 TRP A 221    16668  13591  13341    204    302    850       C  
ATOM   1223  CE3 TRP A 221      18.531  34.503 -15.993  1.00115.82           C  
ANISOU 1223  CE3 TRP A 221    16725  13728  13551    114    407    778       C  
ATOM   1224  CZ2 TRP A 221      17.658  37.170 -15.658  1.00116.54           C  
ANISOU 1224  CZ2 TRP A 221    16835  13786  13660    239    304    847       C  
ATOM   1225  CZ3 TRP A 221      18.822  35.216 -14.847  1.00113.30           C  
ANISOU 1225  CZ3 TRP A 221    16350  13380  13320    151    404    776       C  
ATOM   1226  CH2 TRP A 221      18.388  36.535 -14.689  1.00114.70           C  
ANISOU 1226  CH2 TRP A 221    16535  13540  13505    211    354    808       C  
ATOM   1227  N   TRP A 222      14.110  32.283 -18.061  1.00100.03           N  
ANISOU 1227  N   TRP A 222    14719  12023  11265    109    162    726       N  
ATOM   1228  CA  TRP A 222      13.281  32.153 -16.870  1.00101.67           C  
ANISOU 1228  CA  TRP A 222    14819  12281  11530    138    112    695       C  
ATOM   1229  C   TRP A 222      13.551  30.862 -16.113  1.00103.40           C  
ANISOU 1229  C   TRP A 222    14972  12519  11796     88    160    646       C  
ATOM   1230  O   TRP A 222      13.228  30.775 -14.923  1.00102.82           O  
ANISOU 1230  O   TRP A 222    14814  12467  11786    105    145    623       O  
ATOM   1231  CB  TRP A 222      11.803  32.276 -17.247  1.00103.56           C  
ANISOU 1231  CB  TRP A 222    15039  12595  11713    174     10    687       C  
ATOM   1232  CG  TRP A 222      11.267  33.674 -17.038  1.00109.91           C  
ANISOU 1232  CG  TRP A 222    15840  13389  12531    250    -58    721       C  
ATOM   1233  CD1 TRP A 222      10.124  34.021 -16.374  1.00110.47           C  
ANISOU 1233  CD1 TRP A 222    15832  13511  12629    301   -136    702       C  
ATOM   1234  CD2 TRP A 222      11.863  34.908 -17.474  1.00113.45           C  
ANISOU 1234  CD2 TRP A 222    16366  13766  12972    284    -49    777       C  
ATOM   1235  NE1 TRP A 222       9.969  35.385 -16.371  1.00106.67           N  
ANISOU 1235  NE1 TRP A 222    15372  12996  12160    366   -179    742       N  
ATOM   1236  CE2 TRP A 222      11.022  35.953 -17.042  1.00113.96           C  
ANISOU 1236  CE2 TRP A 222    16394  13844  13062    357   -128    790       C  
ATOM   1237  CE3 TRP A 222      13.022  35.232 -18.193  1.00111.44           C  
ANISOU 1237  CE3 TRP A 222    16209  13438  12696    258     21    816       C  
ATOM   1238  CZ2 TRP A 222      11.305  37.294 -17.302  1.00118.05           C  
ANISOU 1238  CZ2 TRP A 222    16971  14299  13583    406   -141    843       C  
ATOM   1239  CZ3 TRP A 222      13.298  36.562 -18.450  1.00103.39           C  
ANISOU 1239  CZ3 TRP A 222    15249  12358  11678    304     12    868       C  
ATOM   1240  CH2 TRP A 222      12.445  37.575 -18.009  1.00111.69           C  
ANISOU 1240  CH2 TRP A 222    16264  13420  12753    377    -70    883       C  
ATOM   1241  N   ASP A 223      14.153  29.868 -16.763  1.00101.80           N  
ANISOU 1241  N   ASP A 223    14808  12306  11564     26    219    631       N  
ATOM   1242  CA  ASP A 223      14.578  28.676 -16.040  1.00101.21           C  
ANISOU 1242  CA  ASP A 223    14678  12234  11542    -21    272    590       C  
ATOM   1243  C   ASP A 223      15.715  29.004 -15.081  1.00 97.93           C  
ANISOU 1243  C   ASP A 223    14240  11752  11217    -16    330    598       C  
ATOM   1244  O   ASP A 223      15.706  28.567 -13.925  1.00 98.32           O  
ANISOU 1244  O   ASP A 223    14216  11812  11329    -16    334    573       O  
ATOM   1245  CB  ASP A 223      14.980  27.584 -17.037  1.00100.61           C  
ANISOU 1245  CB  ASP A 223    14653  12158  11416    -86    322    570       C  
ATOM   1246  CG  ASP A 223      15.752  26.450 -16.392  1.00 97.74           C  
ANISOU 1246  CG  ASP A 223    14250  11772  11116   -135    392    536       C  
ATOM   1247  OD1 ASP A 223      16.989  26.557 -16.230  1.00 94.79           O  
ANISOU 1247  OD1 ASP A 223    13895  11329  10792   -149    462    545       O  
ATOM   1248  OD2 ASP A 223      15.104  25.446 -16.037  1.00 96.74           O  
ANISOU 1248  OD2 ASP A 223    14071  11696  10991   -158    377    499       O  
ATOM   1249  N   LEU A 224      16.694  29.785 -15.541  1.00 90.64           N  
ANISOU 1249  N   LEU A 224    13379  10759  10300    -11    374    631       N  
ATOM   1250  CA  LEU A 224      17.793  30.178 -14.671  1.00 90.13           C  
ANISOU 1250  CA  LEU A 224    13292  10629  10326     -4    425    635       C  
ATOM   1251  C   LEU A 224      17.302  31.100 -13.565  1.00 89.88           C  
ANISOU 1251  C   LEU A 224    13201  10607  10342     56    371    643       C  
ATOM   1252  O   LEU A 224      17.843  31.085 -12.453  1.00 89.33           O  
ANISOU 1252  O   LEU A 224    13078  10512  10350     61    393    629       O  
ATOM   1253  CB  LEU A 224      18.892  30.847 -15.499  1.00 90.48           C  
ANISOU 1253  CB  LEU A 224    13417  10596  10364    -16    486    666       C  
ATOM   1254  CG  LEU A 224      20.111  31.480 -14.823  1.00 90.14           C  
ANISOU 1254  CG  LEU A 224    13362  10475  10411     -7    541    673       C  
ATOM   1255  CD1 LEU A 224      20.667  30.573 -13.744  1.00 89.45           C  
ANISOU 1255  CD1 LEU A 224    13201  10381  10403    -29    572    634       C  
ATOM   1256  CD2 LEU A 224      21.188  31.811 -15.847  1.00 90.57           C  
ANISOU 1256  CD2 LEU A 224    13501  10459  10453    -38    617    693       C  
ATOM   1257  N   PHE A 225      16.276  31.903 -13.849  1.00108.55           N  
ANISOU 1257  N   PHE A 225    15573  13006  12663    102    299    664       N  
ATOM   1258  CA  PHE A 225      15.702  32.758 -12.818  1.00107.44           C  
ANISOU 1258  CA  PHE A 225    15374  12880  12569    159    247    665       C  
ATOM   1259  C   PHE A 225      15.048  31.934 -11.715  1.00103.20           C  
ANISOU 1259  C   PHE A 225    14746  12402  12064    153    225    623       C  
ATOM   1260  O   PHE A 225      15.351  32.115 -10.531  1.00102.91           O  
ANISOU 1260  O   PHE A 225    14655  12349  12095    168    235    611       O  
ATOM   1261  CB  PHE A 225      14.694  33.724 -13.434  1.00108.85           C  
ANISOU 1261  CB  PHE A 225    15580  13085  12695    210    171    693       C  
ATOM   1262  CG  PHE A 225      14.317  34.846 -12.524  1.00112.01           C  
ANISOU 1262  CG  PHE A 225    15934  13479  13148    273    128    701       C  
ATOM   1263  CD1 PHE A 225      15.286  35.697 -12.018  1.00110.32           C  
ANISOU 1263  CD1 PHE A 225    15727  13192  12996    290    168    719       C  
ATOM   1264  CD2 PHE A 225      12.996  35.038 -12.151  1.00112.38           C  
ANISOU 1264  CD2 PHE A 225    15923  13590  13187    314     50    685       C  
ATOM   1265  CE1 PHE A 225      14.945  36.731 -11.168  1.00107.49           C  
ANISOU 1265  CE1 PHE A 225    15326  12826  12688    347    130    722       C  
ATOM   1266  CE2 PHE A 225      12.648  36.072 -11.300  1.00112.45           C  
ANISOU 1266  CE2 PHE A 225    15887  13592  13248    371     14    688       C  
ATOM   1267  CZ  PHE A 225      13.624  36.919 -10.809  1.00108.02           C  
ANISOU 1267  CZ  PHE A 225    15338  12958  12745    388     53    707       C  
ATOM   1268  N   MET A 226      14.155  31.012 -12.081  1.00113.18           N  
ANISOU 1268  N   MET A 226    15994  13732  13278    129    197    598       N  
ATOM   1269  CA  MET A 226      13.486  30.208 -11.063  1.00116.97           C  
ANISOU 1269  CA  MET A 226    16392  14265  13786    118    181    558       C  
ATOM   1270  C   MET A 226      14.455  29.270 -10.355  1.00116.64           C  
ANISOU 1270  C   MET A 226    16330  14191  13795     74    249    538       C  
ATOM   1271  O   MET A 226      14.205  28.878  -9.210  1.00114.76           O  
ANISOU 1271  O   MET A 226    16029  13976  13598     74    245    514       O  
ATOM   1272  CB  MET A 226      12.331  29.420 -11.677  1.00119.57           C  
ANISOU 1272  CB  MET A 226    16708  14669  14053     98    140    532       C  
ATOM   1273  CG  MET A 226      11.198  30.292 -12.189  1.00122.24           C  
ANISOU 1273  CG  MET A 226    17047  15048  14349    149     58    544       C  
ATOM   1274  SD  MET A 226      10.929  31.810 -11.259  1.00131.56           S  
ANISOU 1274  SD  MET A 226    18189  16212  15585    226     15    562       S  
ATOM   1275  CE  MET A 226       9.197  31.645 -10.833  1.00130.05           C  
ANISOU 1275  CE  MET A 226    17911  16115  15388    252    -64    520       C  
ATOM   1276  N   LYS A 227      15.551  28.885 -11.013  1.00105.05           N  
ANISOU 1276  N   LYS A 227    14918  12672  12326     36    310    548       N  
ATOM   1277  CA  LYS A 227      16.610  28.179 -10.301  1.00101.37           C  
ANISOU 1277  CA  LYS A 227    14432  12162  11921      5    370    532       C  
ATOM   1278  C   LYS A 227      17.430  29.123  -9.429  1.00 99.34           C  
ANISOU 1278  C   LYS A 227    14160  11849  11734     40    383    547       C  
ATOM   1279  O   LYS A 227      17.945  28.704  -8.389  1.00102.42           O  
ANISOU 1279  O   LYS A 227    14510  12223  12183     32    404    530       O  
ATOM   1280  CB  LYS A 227      17.510  27.428 -11.281  1.00 99.37           C  
ANISOU 1280  CB  LYS A 227    14235  11871  11652    -48    433    530       C  
ATOM   1281  CG  LYS A 227      16.820  26.258 -11.958  1.00102.17           C  
ANISOU 1281  CG  LYS A 227    14594  12277  11947    -92    429    505       C  
ATOM   1282  CD  LYS A 227      17.753  25.544 -12.922  1.00107.28           C  
ANISOU 1282  CD  LYS A 227    15298  12883  12581   -144    496    499       C  
ATOM   1283  CE  LYS A 227      17.023  24.468 -13.716  1.00104.12           C  
ANISOU 1283  CE  LYS A 227    14910  12535  12116   -187    489    472       C  
ATOM   1284  NZ  LYS A 227      17.868  23.263 -13.940  1.00102.23           N  
ANISOU 1284  NZ  LYS A 227    14682  12262  11900   -244    559    446       N  
ATOM   1285  N   ILE A 228      17.573  30.386  -9.832  1.00 88.26           N  
ANISOU 1285  N   ILE A 228    12792  10416  10327     77    370    578       N  
ATOM   1286  CA  ILE A 228      18.087  31.394  -8.911  1.00 88.02           C  
ANISOU 1286  CA  ILE A 228    12738  10344  10363    117    369    587       C  
ATOM   1287  C   ILE A 228      17.078  31.644  -7.795  1.00 87.84           C  
ANISOU 1287  C   ILE A 228    12647  10374  10355    155    312    571       C  
ATOM   1288  O   ILE A 228      17.430  31.678  -6.609  1.00 87.43           O  
ANISOU 1288  O   ILE A 228    12550  10310  10361    165    318    556       O  
ATOM   1289  CB  ILE A 228      18.429  32.690  -9.672  1.00 88.45           C  
ANISOU 1289  CB  ILE A 228    12851  10349  10408    147    372    624       C  
ATOM   1290  CG1 ILE A 228      19.805  32.572 -10.334  1.00 88.51           C  
ANISOU 1290  CG1 ILE A 228    12912  10283  10435    109    448    633       C  
ATOM   1291  CG2 ILE A 228      18.360  33.906  -8.751  1.00 88.36           C  
ANISOU 1291  CG2 ILE A 228    12805  10319  10448    202    341    632       C  
ATOM   1292  CD1 ILE A 228      20.961  32.958  -9.427  1.00 88.14           C  
ANISOU 1292  CD1 ILE A 228    12836  10172  10480    116    487    625       C  
ATOM   1293  N   CYS A 229      15.802  31.788  -8.163  1.00 89.74           N  
ANISOU 1293  N   CYS A 229    12878  10676  10543    174    256    571       N  
ATOM   1294  CA  CYS A 229      14.757  32.086  -7.190  1.00 88.13           C  
ANISOU 1294  CA  CYS A 229    12608  10525  10353    210    204    552       C  
ATOM   1295  C   CYS A 229      14.646  30.991  -6.142  1.00 87.68           C  
ANISOU 1295  C   CYS A 229    12496  10499  10319    179    220    517       C  
ATOM   1296  O   CYS A 229      14.519  31.271  -4.947  1.00 87.80           O  
ANISOU 1296  O   CYS A 229    12463  10522  10376    201    209    503       O  
ATOM   1297  CB  CYS A 229      13.421  32.264  -7.908  1.00 90.64           C  
ANISOU 1297  CB  CYS A 229    12924  10904  10611    230    143    552       C  
ATOM   1298  SG  CYS A 229      12.998  33.977  -8.292  1.00106.79           S  
ANISOU 1298  SG  CYS A 229    14992  12930  12653    302     88    586       S  
ATOM   1299  N   VAL A 230      14.673  29.731  -6.577  1.00 90.30           N  
ANISOU 1299  N   VAL A 230    12838  10848  10623    127    246    503       N  
ATOM   1300  CA  VAL A 230      14.542  28.619  -5.639  1.00 90.77           C  
ANISOU 1300  CA  VAL A 230    12852  10934  10701     95    262    473       C  
ATOM   1301  C   VAL A 230      15.771  28.527  -4.743  1.00 88.88           C  
ANISOU 1301  C   VAL A 230    12610  10636  10524     89    303    475       C  
ATOM   1302  O   VAL A 230      15.659  28.308  -3.531  1.00 86.54           O  
ANISOU 1302  O   VAL A 230    12270  10352  10257     94    300    458       O  
ATOM   1303  CB  VAL A 230      14.294  27.303  -6.399  1.00 87.40           C  
ANISOU 1303  CB  VAL A 230    12441  10534  10232     40    282    458       C  
ATOM   1304  CG1 VAL A 230      14.790  26.127  -5.589  1.00 87.00           C  
ANISOU 1304  CG1 VAL A 230    12369  10471  10214     -1    322    439       C  
ATOM   1305  CG2 VAL A 230      12.817  27.145  -6.723  1.00 87.79           C  
ANISOU 1305  CG2 VAL A 230    12461  10660  10233     43    232    439       C  
ATOM   1306  N   PHE A 231      16.959  28.709  -5.320  1.00 97.64           N  
ANISOU 1306  N   PHE A 231    13765  11680  11654     80    343    493       N  
ATOM   1307  CA  PHE A 231      18.191  28.516  -4.563  1.00 94.87           C  
ANISOU 1307  CA  PHE A 231    13409  11272  11367     72    380    490       C  
ATOM   1308  C   PHE A 231      18.277  29.460  -3.373  1.00 95.31           C  
ANISOU 1308  C   PHE A 231    13428  11316  11468    117    356    488       C  
ATOM   1309  O   PHE A 231      18.792  29.083  -2.316  1.00 94.39           O  
ANISOU 1309  O   PHE A 231    13286  11185  11394    113    366    475       O  
ATOM   1310  CB  PHE A 231      19.397  28.681  -5.486  1.00 95.62           C  
ANISOU 1310  CB  PHE A 231    13554  11297  11479     56    428    505       C  
ATOM   1311  CG  PHE A 231      20.662  29.061  -4.779  1.00 93.43           C  
ANISOU 1311  CG  PHE A 231    13268  10953  11278     67    455    504       C  
ATOM   1312  CD1 PHE A 231      21.482  28.091  -4.239  1.00 91.96           C  
ANISOU 1312  CD1 PHE A 231    13068  10739  11136     39    486    486       C  
ATOM   1313  CD2 PHE A 231      21.071  30.379  -4.724  1.00 92.29           C  
ANISOU 1313  CD2 PHE A 231    13132  10770  11164    105    450    519       C  
ATOM   1314  CE1 PHE A 231      22.658  28.432  -3.602  1.00 89.51           C  
ANISOU 1314  CE1 PHE A 231    12744  10366  10897     51    504    481       C  
ATOM   1315  CE2 PHE A 231      22.251  30.726  -4.097  1.00 90.52           C  
ANISOU 1315  CE2 PHE A 231    12896  10484  11013    113    474    512       C  
ATOM   1316  CZ  PHE A 231      23.045  29.749  -3.534  1.00 89.14           C  
ANISOU 1316  CZ  PHE A 231    12702  10285  10882     87    499    492       C  
ATOM   1317  N   ILE A 232      17.779  30.688  -3.516  1.00108.92           N  
ANISOU 1317  N   ILE A 232    15152  13048  13184    161    323    501       N  
ATOM   1318  CA  ILE A 232      17.856  31.619  -2.394  1.00109.39           C  
ANISOU 1318  CA  ILE A 232    15178  13097  13289    204    302    496       C  
ATOM   1319  C   ILE A 232      16.671  31.441  -1.447  1.00109.88           C  
ANISOU 1319  C   ILE A 232    15187  13228  13334    216    264    473       C  
ATOM   1320  O   ILE A 232      16.821  31.596  -0.231  1.00108.48           O  
ANISOU 1320  O   ILE A 232    14977  13049  13191    231    259    457       O  
ATOM   1321  CB  ILE A 232      17.997  33.068  -2.902  1.00110.02           C  
ANISOU 1321  CB  ILE A 232    15281  13141  13379    246    289    519       C  
ATOM   1322  CG1 ILE A 232      16.788  33.500  -3.735  1.00110.03           C  
ANISOU 1322  CG1 ILE A 232    15294  13189  13324    267    247    531       C  
ATOM   1323  CG2 ILE A 232      19.273  33.229  -3.713  1.00109.87           C  
ANISOU 1323  CG2 ILE A 232    15313  13048  13384    228    337    538       C  
ATOM   1324  CD1 ILE A 232      15.784  34.286  -2.957  1.00109.86           C  
ANISOU 1324  CD1 ILE A 232    15225  13208  13310    314    198    518       C  
ATOM   1325  N   PHE A 233      15.494  31.088  -1.966  1.00129.44           N  
ANISOU 1325  N   PHE A 233    17655  15766  15759    209    240    467       N  
ATOM   1326  CA  PHE A 233      14.353  30.805  -1.097  1.00132.86           C  
ANISOU 1326  CA  PHE A 233    18036  16266  16180    213    213    440       C  
ATOM   1327  C   PHE A 233      14.529  29.496  -0.332  1.00132.44           C  
ANISOU 1327  C   PHE A 233    17968  16224  16130    168    241    421       C  
ATOM   1328  O   PHE A 233      14.135  29.395   0.837  1.00128.66           O  
ANISOU 1328  O   PHE A 233    17452  15773  15662    173    235    401       O  
ATOM   1329  CB  PHE A 233      13.066  30.771  -1.918  1.00135.99           C  
ANISOU 1329  CB  PHE A 233    18423  16722  16527    216    178    434       C  
ATOM   1330  CG  PHE A 233      12.238  32.014  -1.798  1.00139.63           C  
ANISOU 1330  CG  PHE A 233    18856  17204  16992    272    130    432       C  
ATOM   1331  CD1 PHE A 233      12.808  33.264  -1.948  1.00134.83           C  
ANISOU 1331  CD1 PHE A 233    18272  16545  16412    316    122    456       C  
ATOM   1332  CD2 PHE A 233      10.881  31.928  -1.540  1.00145.15           C  
ANISOU 1332  CD2 PHE A 233    19504  17972  17673    282     95    403       C  
ATOM   1333  CE1 PHE A 233      12.042  34.410  -1.837  1.00141.59           C  
ANISOU 1333  CE1 PHE A 233    19104  17417  17278    369     77    453       C  
ATOM   1334  CE2 PHE A 233      10.107  33.067  -1.429  1.00145.81           C  
ANISOU 1334  CE2 PHE A 233    19559  18075  17768    336     50    398       C  
ATOM   1335  CZ  PHE A 233      10.689  34.312  -1.579  1.00142.03           C  
ANISOU 1335  CZ  PHE A 233    19106  17542  17316    382     39    424       C  
ATOM   1336  N   ALA A 234      15.106  28.478  -0.975  1.00107.53           N  
ANISOU 1336  N   ALA A 234    14844  13048  12964    124    274    428       N  
ATOM   1337  CA  ALA A 234      15.205  27.151  -0.380  1.00101.75           C  
ANISOU 1337  CA  ALA A 234    14102  12324  12232     80    300    413       C  
ATOM   1338  C   ALA A 234      16.496  26.911   0.382  1.00100.11           C  
ANISOU 1338  C   ALA A 234    13906  12058  12073     76    326    418       C  
ATOM   1339  O   ALA A 234      16.523  26.041   1.259  1.00100.55           O  
ANISOU 1339  O   ALA A 234    13950  12121  12135     53    337    407       O  
ATOM   1340  CB  ALA A 234      15.076  26.072  -1.458  1.00105.82           C  
ANISOU 1340  CB  ALA A 234    14644  12851  12713     33    321    411       C  
ATOM   1341  N   PHE A 235      17.573  27.623   0.060  1.00 87.68           N  
ANISOU 1341  N   PHE A 235    12357  10423  10536     95    337    434       N  
ATOM   1342  CA  PHE A 235      18.851  27.358   0.709  1.00 86.99           C  
ANISOU 1342  CA  PHE A 235    12275  10277  10501     90    359    434       C  
ATOM   1343  C   PHE A 235      19.397  28.554   1.477  1.00 91.21           C  
ANISOU 1343  C   PHE A 235    12796  10780  11080    135    342    435       C  
ATOM   1344  O   PHE A 235      19.650  28.435   2.681  1.00 89.55           O  
ANISOU 1344  O   PHE A 235    12567  10566  10893    144    332    424       O  
ATOM   1345  CB  PHE A 235      19.859  26.876  -0.337  1.00 85.32           C  
ANISOU 1345  CB  PHE A 235    12101  10012  10306     62    399    443       C  
ATOM   1346  CG  PHE A 235      21.204  26.550   0.229  1.00 85.74           C  
ANISOU 1346  CG  PHE A 235    12155  10001  10422     57    421    439       C  
ATOM   1347  CD1 PHE A 235      22.183  27.523   0.346  1.00 85.11           C  
ANISOU 1347  CD1 PHE A 235    12076   9866  10395     85    424    443       C  
ATOM   1348  CD2 PHE A 235      21.480  25.268   0.674  1.00 88.66           C  
ANISOU 1348  CD2 PHE A 235    12523  10364  10801     25    435    431       C  
ATOM   1349  CE1 PHE A 235      23.422  27.218   0.872  1.00 85.76           C  
ANISOU 1349  CE1 PHE A 235    12154   9890  10540     83    440    434       C  
ATOM   1350  CE2 PHE A 235      22.715  24.954   1.204  1.00 90.17           C  
ANISOU 1350  CE2 PHE A 235    12713  10495  11053     25    447    426       C  
ATOM   1351  CZ  PHE A 235      23.689  25.929   1.304  1.00 90.36           C  
ANISOU 1351  CZ  PHE A 235    12733  10467  11131     54    448    426       C  
ATOM   1352  N   VAL A 236      19.570  29.712   0.836  1.00 98.06           N  
ANISOU 1352  N   VAL A 236    13676  11623  11958    164    338    447       N  
ATOM   1353  CA  VAL A 236      20.418  30.752   1.418  1.00 95.00           C  
ANISOU 1353  CA  VAL A 236    13282  11187  11627    199    333    446       C  
ATOM   1354  C   VAL A 236      19.754  31.366   2.642  1.00 93.43           C  
ANISOU 1354  C   VAL A 236    13046  11025  11430    233    296    430       C  
ATOM   1355  O   VAL A 236      20.279  31.278   3.758  1.00 93.36           O  
ANISOU 1355  O   VAL A 236    13020  11000  11451    239    291    416       O  
ATOM   1356  CB  VAL A 236      20.771  31.823   0.372  1.00 93.25           C  
ANISOU 1356  CB  VAL A 236    13089  10925  11417    217    344    465       C  
ATOM   1357  CG1 VAL A 236      22.008  32.581   0.809  1.00 96.10           C  
ANISOU 1357  CG1 VAL A 236    13447  11217  11849    236    356    460       C  
ATOM   1358  CG2 VAL A 236      21.021  31.177  -0.960  1.00 91.47           C  
ANISOU 1358  CG2 VAL A 236    12904  10684  11166    180    378    479       C  
ATOM   1359  N   ILE A 237      18.595  31.990   2.458  1.00 91.48           N  
ANISOU 1359  N   ILE A 237    12785  10825  11148    256    270    430       N  
ATOM   1360  CA  ILE A 237      17.956  32.665   3.585  1.00 91.12           C  
ANISOU 1360  CA  ILE A 237    12702  10812  11107    289    240    410       C  
ATOM   1361  C   ILE A 237      17.506  31.631   4.618  1.00 90.39           C  
ANISOU 1361  C   ILE A 237    12590  10764  10992    264    240    391       C  
ATOM   1362  O   ILE A 237      17.480  31.969   5.809  1.00 87.67           O  
ANISOU 1362  O   ILE A 237    12222  10427  10660    283    226    373       O  
ATOM   1363  CB  ILE A 237      16.809  33.600   3.143  1.00 89.61           C  
ANISOU 1363  CB  ILE A 237    12497  10659  10893    323    211    411       C  
ATOM   1364  CG1 ILE A 237      15.506  32.867   2.819  1.00 89.16           C  
ANISOU 1364  CG1 ILE A 237    12423  10673  10781    303    199    403       C  
ATOM   1365  CG2 ILE A 237      17.234  34.412   1.927  1.00 90.97           C  
ANISOU 1365  CG2 ILE A 237    12704  10784  11075    339    215    439       C  
ATOM   1366  CD1 ILE A 237      14.342  33.788   2.518  1.00 86.36           C  
ANISOU 1366  CD1 ILE A 237    12045  10357  10411    342    162    398       C  
ATOM   1367  N   PRO A 238      17.179  30.373   4.262  1.00 85.37           N  
ANISOU 1367  N   PRO A 238    11962  10154  10321    221    256    394       N  
ATOM   1368  CA  PRO A 238      16.998  29.383   5.338  1.00 85.27           C  
ANISOU 1368  CA  PRO A 238    11939  10167  10294    196    262    380       C  
ATOM   1369  C   PRO A 238      18.283  29.081   6.084  1.00 85.07           C  
ANISOU 1369  C   PRO A 238    11928  10087  10309    193    270    382       C  
ATOM   1370  O   PRO A 238      18.264  29.010   7.318  1.00 85.06           O  
ANISOU 1370  O   PRO A 238    11916  10097  10307    199    258    368       O  
ATOM   1371  CB  PRO A 238      16.460  28.154   4.600  1.00 85.32           C  
ANISOU 1371  CB  PRO A 238    11955  10202  10262    149    280    383       C  
ATOM   1372  CG  PRO A 238      15.762  28.717   3.446  1.00 85.53           C  
ANISOU 1372  CG  PRO A 238    11980  10252  10267    161    269    388       C  
ATOM   1373  CD  PRO A 238      16.668  29.826   2.990  1.00 85.50           C  
ANISOU 1373  CD  PRO A 238    11995  10191  10301    195    265    405       C  
ATOM   1374  N   VAL A 239      19.406  28.918   5.374  1.00 85.55           N  
ANISOU 1374  N   VAL A 239    12014  10088  10405    184    288    396       N  
ATOM   1375  CA  VAL A 239      20.681  28.677   6.051  1.00 85.18           C  
ANISOU 1375  CA  VAL A 239    11974   9986  10405    185    291    394       C  
ATOM   1376  C   VAL A 239      21.012  29.840   6.968  1.00 84.86           C  
ANISOU 1376  C   VAL A 239    11915   9930  10397    228    265    380       C  
ATOM   1377  O   VAL A 239      21.401  29.652   8.125  1.00 84.83           O  
ANISOU 1377  O   VAL A 239    11907   9920  10406    234    249    369       O  
ATOM   1378  CB  VAL A 239      21.813  28.448   5.033  1.00 85.36           C  
ANISOU 1378  CB  VAL A 239    12019   9945  10469    170    319    405       C  
ATOM   1379  CG1 VAL A 239      23.167  28.763   5.671  1.00 84.73           C  
ANISOU 1379  CG1 VAL A 239    11935   9802  10457    188    314    396       C  
ATOM   1380  CG2 VAL A 239      21.786  27.028   4.518  1.00 87.65           C  
ANISOU 1380  CG2 VAL A 239    12327  10238  10738    124    345    411       C  
ATOM   1381  N   LEU A 240      20.856  31.062   6.462  1.00 90.36           N  
ANISOU 1381  N   LEU A 240    12605  10620  11108    258    259    381       N  
ATOM   1382  CA  LEU A 240      21.234  32.229   7.246  1.00 91.66           C  
ANISOU 1382  CA  LEU A 240    12752  10764  11310    298    238    366       C  
ATOM   1383  C   LEU A 240      20.343  32.392   8.469  1.00 91.88           C  
ANISOU 1383  C   LEU A 240    12758  10847  11307    312    213    345       C  
ATOM   1384  O   LEU A 240      20.833  32.755   9.542  1.00 93.08           O  
ANISOU 1384  O   LEU A 240    12901  10985  11482    331    195    327       O  
ATOM   1385  CB  LEU A 240      21.228  33.485   6.378  1.00 94.90           C  
ANISOU 1385  CB  LEU A 240    13164  11150  11742    325    240    374       C  
ATOM   1386  CG  LEU A 240      22.574  33.787   5.703  1.00 98.78           C  
ANISOU 1386  CG  LEU A 240    13674  11564  12292    323    264    382       C  
ATOM   1387  CD1 LEU A 240      23.523  34.404   6.716  1.00100.54           C  
ANISOU 1387  CD1 LEU A 240    13879  11746  12576    347    250    360       C  
ATOM   1388  CD2 LEU A 240      23.219  32.566   5.054  1.00 95.74           C  
ANISOU 1388  CD2 LEU A 240    13312  11156  11910    281    295    394       C  
ATOM   1389  N   ILE A 241      19.041  32.125   8.343  1.00 85.17           N  
ANISOU 1389  N   ILE A 241    11896  10059  10403    303    212    344       N  
ATOM   1390  CA  ILE A 241      18.202  32.090   9.541  1.00 85.28           C  
ANISOU 1390  CA  ILE A 241    11890  10127  10386    307    198    321       C  
ATOM   1391  C   ILE A 241      18.774  31.103  10.545  1.00 85.20           C  
ANISOU 1391  C   ILE A 241    11897  10108  10368    284    200    319       C  
ATOM   1392  O   ILE A 241      19.161  31.473  11.658  1.00 85.26           O  
ANISOU 1392  O   ILE A 241    11901  10108  10387    302    182    302       O  
ATOM   1393  CB  ILE A 241      16.748  31.737   9.194  1.00 85.43           C  
ANISOU 1393  CB  ILE A 241    11892  10214  10354    292    203    317       C  
ATOM   1394  CG1 ILE A 241      16.135  32.809   8.302  1.00 85.59           C  
ANISOU 1394  CG1 ILE A 241    11896  10244  10382    323    191    318       C  
ATOM   1395  CG2 ILE A 241      15.938  31.545  10.465  1.00 85.59           C  
ANISOU 1395  CG2 ILE A 241    11893  10286  10341    287    200    291       C  
ATOM   1396  CD1 ILE A 241      14.627  32.859   8.368  1.00 85.85           C  
ANISOU 1396  CD1 ILE A 241    11895  10347  10378    325    183    299       C  
ATOM   1397  N   ILE A 242      18.872  29.833  10.148  1.00 89.57           N  
ANISOU 1397  N   ILE A 242    12470  10660  10902    244    219    335       N  
ATOM   1398  CA  ILE A 242      19.253  28.796  11.101  1.00 90.21           C  
ANISOU 1398  CA  ILE A 242    12572  10735  10969    221    218    337       C  
ATOM   1399  C   ILE A 242      20.702  28.971  11.539  1.00 90.23           C  
ANISOU 1399  C   ILE A 242    12586  10673  11024    240    201    337       C  
ATOM   1400  O   ILE A 242      21.038  28.719  12.699  1.00 94.42           O  
ANISOU 1400  O   ILE A 242    13127  11200  11548    243    182    330       O  
ATOM   1401  CB  ILE A 242      18.957  27.395  10.521  1.00 92.73           C  
ANISOU 1401  CB  ILE A 242    12909  11065  11260    174    244    354       C  
ATOM   1402  CG1 ILE A 242      19.971  26.930   9.466  1.00 90.75           C  
ANISOU 1402  CG1 ILE A 242    12676  10758  11048    161    259    371       C  
ATOM   1403  CG2 ILE A 242      17.598  27.388   9.902  1.00 94.73           C  
ANISOU 1403  CG2 ILE A 242    13143  11378  11472    160    258    348       C  
ATOM   1404  CD1 ILE A 242      21.203  26.241  10.021  1.00 89.93           C  
ANISOU 1404  CD1 ILE A 242    12593  10598  10979    156    253    378       C  
ATOM   1405  N   ILE A 243      21.583  29.421  10.643  1.00 88.61           N  
ANISOU 1405  N   ILE A 243    12379  10415  10872    251    207    344       N  
ATOM   1406  CA  ILE A 243      22.950  29.632  11.104  1.00 90.73           C  
ANISOU 1406  CA  ILE A 243    12650  10623  11199    268    190    337       C  
ATOM   1407  C   ILE A 243      23.019  30.826  12.049  1.00 91.88           C  
ANISOU 1407  C   ILE A 243    12778  10772  11360    308    161    312       C  
ATOM   1408  O   ILE A 243      23.900  30.886  12.911  1.00 94.65           O  
ANISOU 1408  O   ILE A 243    13130  11091  11741    322    135    299       O  
ATOM   1409  CB  ILE A 243      23.941  29.780   9.935  1.00 92.10           C  
ANISOU 1409  CB  ILE A 243    12827  10736  11433    266    212    345       C  
ATOM   1410  CG1 ILE A 243      25.362  29.535  10.438  1.00 91.98           C  
ANISOU 1410  CG1 ILE A 243    12812  10658  11479    273    196    336       C  
ATOM   1411  CG2 ILE A 243      23.892  31.186   9.367  1.00 95.16           C  
ANISOU 1411  CG2 ILE A 243    13199  11112  11846    294    215    339       C  
ATOM   1412  CD1 ILE A 243      25.540  28.217  11.165  1.00 94.20           C  
ANISOU 1412  CD1 ILE A 243    13112  10941  11740    253    184    342       C  
ATOM   1413  N   VAL A 244      22.095  31.780  11.934  1.00100.71           N  
ANISOU 1413  N   VAL A 244    13878  11928  12460    326    161    303       N  
ATOM   1414  CA  VAL A 244      22.099  32.899  12.870  1.00105.18           C  
ANISOU 1414  CA  VAL A 244    14425  12497  13040    362    136    275       C  
ATOM   1415  C   VAL A 244      21.485  32.489  14.203  1.00104.13           C  
ANISOU 1415  C   VAL A 244    14297  12413  12852    357    120    260       C  
ATOM   1416  O   VAL A 244      22.110  32.643  15.257  1.00104.80           O  
ANISOU 1416  O   VAL A 244    14388  12484  12949    372     94    243       O  
ATOM   1417  CB  VAL A 244      21.387  34.128  12.269  1.00109.29           C  
ANISOU 1417  CB  VAL A 244    14924  13033  13568    388    140    269       C  
ATOM   1418  CG1 VAL A 244      20.795  35.009  13.367  1.00103.78           C  
ANISOU 1418  CG1 VAL A 244    14205  12368  12857    417    120    237       C  
ATOM   1419  CG2 VAL A 244      22.363  34.936  11.428  1.00106.58           C  
ANISOU 1419  CG2 VAL A 244    14580  12624  13292    405    148    275       C  
ATOM   1420  N   CYS A 245      20.265  31.943  14.181  1.00 85.46           N  
ANISOU 1420  N   CYS A 245    11934  10108  10428    335    137    265       N  
ATOM   1421  CA  CYS A 245      19.564  31.670  15.434  1.00 85.68           C  
ANISOU 1421  CA  CYS A 245    11967  10186  10402    327    132    248       C  
ATOM   1422  C   CYS A 245      20.355  30.743  16.347  1.00 85.76           C  
ANISOU 1422  C   CYS A 245    12012  10173  10398    313    116    256       C  
ATOM   1423  O   CYS A 245      20.333  30.904  17.572  1.00 85.99           O  
ANISOU 1423  O   CYS A 245    12053  10220  10402    322     97    237       O  
ATOM   1424  CB  CYS A 245      18.179  31.096  15.160  1.00 85.76           C  
ANISOU 1424  CB  CYS A 245    11969  10257  10356    299    159    251       C  
ATOM   1425  SG  CYS A 245      17.247  31.959  13.926  1.00 85.73           S  
ANISOU 1425  SG  CYS A 245    11928  10278  10367    315    170    248       S  
ATOM   1426  N   TYR A 246      21.056  29.763  15.788  1.00 85.60           N  
ANISOU 1426  N   TYR A 246    12013  10116  10397    291    122    282       N  
ATOM   1427  CA  TYR A 246      21.906  28.954  16.651  1.00 89.06           C  
ANISOU 1427  CA  TYR A 246    12483  10524  10830    284     98    289       C  
ATOM   1428  C   TYR A 246      23.139  29.729  17.095  1.00 87.36           C  
ANISOU 1428  C   TYR A 246    12261  10259  10675    321     60    271       C  
ATOM   1429  O   TYR A 246      23.439  29.786  18.292  1.00 86.12           O  
ANISOU 1429  O   TYR A 246    12120  10104  10500    334     27    257       O  
ATOM   1430  CB  TYR A 246      22.281  27.628  15.976  1.00 94.00           C  
ANISOU 1430  CB  TYR A 246    13132  11122  11463    251    115    320       C  
ATOM   1431  CG  TYR A 246      21.095  26.701  15.793  1.00 93.91           C  
ANISOU 1431  CG  TYR A 246    13133  11160  11388    210    149    334       C  
ATOM   1432  CD1 TYR A 246      19.984  27.091  15.071  1.00 95.09           C  
ANISOU 1432  CD1 TYR A 246    13256  11356  11518    202    177    328       C  
ATOM   1433  CD2 TYR A 246      21.064  25.457  16.404  1.00 93.78           C  
ANISOU 1433  CD2 TYR A 246    13155  11144  11333    181    152    352       C  
ATOM   1434  CE1 TYR A 246      18.907  26.269  14.927  1.00 94.57           C  
ANISOU 1434  CE1 TYR A 246    13195  11335  11401    164    207    334       C  
ATOM   1435  CE2 TYR A 246      19.972  24.620  16.265  1.00 99.13           C  
ANISOU 1435  CE2 TYR A 246    13843  11864  11957    140    188    362       C  
ATOM   1436  CZ  TYR A 246      18.890  25.036  15.520  1.00 97.59           C  
ANISOU 1436  CZ  TYR A 246    13615  11717  11749    131    216    350       C  
ATOM   1437  OH  TYR A 246      17.788  24.222  15.362  1.00 95.61           O  
ANISOU 1437  OH  TYR A 246    13367  11510  11450     89    251    353       O  
ATOM   1438  N   THR A 247      23.843  30.377  16.161  1.00109.68           N  
ANISOU 1438  N   THR A 247    15062  13040  13570    337     64    269       N  
ATOM   1439  CA  THR A 247      25.095  31.013  16.557  1.00110.73           C  
ANISOU 1439  CA  THR A 247    15185  13120  13768    367     30    248       C  
ATOM   1440  C   THR A 247      24.854  32.149  17.534  1.00107.82           C  
ANISOU 1440  C   THR A 247    14803  12774  13391    398      5    214       C  
ATOM   1441  O   THR A 247      25.781  32.551  18.239  1.00107.54           O  
ANISOU 1441  O   THR A 247    14764  12706  13392    421    -32    191       O  
ATOM   1442  CB  THR A 247      25.860  31.551  15.349  1.00110.80           C  
ANISOU 1442  CB  THR A 247    15170  13075  13854    375     49    249       C  
ATOM   1443  OG1 THR A 247      27.174  31.934  15.767  1.00110.93           O  
ANISOU 1443  OG1 THR A 247    15175  13035  13940    398     18    227       O  
ATOM   1444  CG2 THR A 247      25.187  32.807  14.826  1.00111.84           C  
ANISOU 1444  CG2 THR A 247    15278  13225  13991    392     67    239       C  
ATOM   1445  N   LEU A 248      23.632  32.664  17.590  1.00 85.91           N  
ANISOU 1445  N   LEU A 248    12018  10055  10571    399     24    207       N  
ATOM   1446  CA  LEU A 248      23.281  33.737  18.504  1.00 87.65           C  
ANISOU 1446  CA  LEU A 248    12224  10300  10780    426      6    171       C  
ATOM   1447  C   LEU A 248      22.727  33.192  19.811  1.00 87.91           C  
ANISOU 1447  C   LEU A 248    12285  10381  10736    415     -7    162       C  
ATOM   1448  O   LEU A 248      22.977  33.772  20.875  1.00 86.71           O  
ANISOU 1448  O   LEU A 248    12136  10232  10578    436    -36    131       O  
ATOM   1449  CB  LEU A 248      22.272  34.668  17.816  1.00 89.16           C  
ANISOU 1449  CB  LEU A 248    12384  10520  10972    437     33    164       C  
ATOM   1450  CG  LEU A 248      21.867  36.073  18.274  1.00 88.03           C  
ANISOU 1450  CG  LEU A 248    12213  10392  10844    472     24    126       C  
ATOM   1451  CD1 LEU A 248      20.835  36.595  17.294  1.00 86.19           C  
ANISOU 1451  CD1 LEU A 248    11956  10182  10610    476     52    134       C  
ATOM   1452  CD2 LEU A 248      21.327  36.147  19.701  1.00 93.50           C  
ANISOU 1452  CD2 LEU A 248    12914  11131  11480    474     10     95       C  
ATOM   1453  N   MET A 249      21.999  32.074  19.743  1.00107.73           N  
ANISOU 1453  N   MET A 249    14820  12926  13188    379     17    188       N  
ATOM   1454  CA  MET A 249      21.490  31.421  20.946  1.00109.09           C  
ANISOU 1454  CA  MET A 249    15028  13138  13282    361     13    186       C  
ATOM   1455  C   MET A 249      22.625  30.983  21.865  1.00108.17           C  
ANISOU 1455  C   MET A 249    14948  12985  13168    370    -34    187       C  
ATOM   1456  O   MET A 249      22.527  31.116  23.091  1.00107.62           O  
ANISOU 1456  O   MET A 249    14902  12937  13050    376    -56    168       O  
ATOM   1457  CB  MET A 249      20.626  30.224  20.548  1.00104.16           C  
ANISOU 1457  CB  MET A 249    14423  12546  12608    317     52    216       C  
ATOM   1458  CG  MET A 249      20.670  29.061  21.516  1.00109.38           C  
ANISOU 1458  CG  MET A 249    15139  13214  13206    290     45    234       C  
ATOM   1459  SD  MET A 249      19.629  27.684  20.983  1.00119.04           S  
ANISOU 1459  SD  MET A 249    16382  14471  14378    235     97    266       S  
ATOM   1460  CE  MET A 249      20.883  26.534  20.424  1.00107.70           C  
ANISOU 1460  CE  MET A 249    14974  12964  12984    226     78    305       C  
ATOM   1461  N   ILE A 250      23.709  30.454  21.292  1.00 86.80           N  
ANISOU 1461  N   ILE A 250    12244  10220  10516    371    -51    208       N  
ATOM   1462  CA  ILE A 250      24.821  29.982  22.108  1.00 87.07           C  
ANISOU 1462  CA  ILE A 250    12308  10214  10559    383   -102    210       C  
ATOM   1463  C   ILE A 250      25.677  31.118  22.644  1.00 87.23           C  
ANISOU 1463  C   ILE A 250    12306  10208  10630    423   -146    170       C  
ATOM   1464  O   ILE A 250      26.459  30.898  23.577  1.00 87.57           O  
ANISOU 1464  O   ILE A 250    12374  10231  10669    438   -198    161       O  
ATOM   1465  CB  ILE A 250      25.718  29.000  21.334  1.00 86.90           C  
ANISOU 1465  CB  ILE A 250    12293  10136  10588    372   -106    240       C  
ATOM   1466  CG1 ILE A 250      26.775  29.759  20.531  1.00 86.69           C  
ANISOU 1466  CG1 ILE A 250    12222  10054  10663    397   -115    223       C  
ATOM   1467  CG2 ILE A 250      24.876  28.084  20.450  1.00 86.65           C  
ANISOU 1467  CG2 ILE A 250    12271  10127  10526    332    -53    273       C  
ATOM   1468  CD1 ILE A 250      27.978  28.930  20.159  1.00 86.70           C  
ANISOU 1468  CD1 ILE A 250    12227   9990  10725    396   -135    237       C  
ATOM   1469  N   LEU A 251      25.573  32.323  22.076  1.00 92.51           N  
ANISOU 1469  N   LEU A 251    12928  10873  11347    442   -130    144       N  
ATOM   1470  CA  LEU A 251      26.309  33.453  22.637  1.00 92.40           C  
ANISOU 1470  CA  LEU A 251    12892  10836  11382    478   -169    101       C  
ATOM   1471  C   LEU A 251      25.688  33.911  23.948  1.00 93.85           C  
ANISOU 1471  C   LEU A 251    13094  11069  11496    487   -186     71       C  
ATOM   1472  O   LEU A 251      26.406  34.266  24.889  1.00 94.40           O  
ANISOU 1472  O   LEU A 251    13171  11123  11572    509   -236     41       O  
ATOM   1473  CB  LEU A 251      26.367  34.605  21.642  1.00 90.66           C  
ANISOU 1473  CB  LEU A 251    12621  10591  11234    495   -143     86       C  
ATOM   1474  CG  LEU A 251      27.138  34.346  20.355  1.00 86.72           C  
ANISOU 1474  CG  LEU A 251    12104  10036  10811    488   -124    108       C  
ATOM   1475  CD1 LEU A 251      26.651  35.305  19.295  1.00 88.39           C  
ANISOU 1475  CD1 LEU A 251    12284  10245  11056    493    -82    107       C  
ATOM   1476  CD2 LEU A 251      28.634  34.489  20.578  1.00 86.85           C  
ANISOU 1476  CD2 LEU A 251    12107   9988  10906    507   -166     86       C  
ATOM   1477  N   ARG A 252      24.355  33.921  24.020  1.00116.43           N  
ANISOU 1477  N   ARG A 252    15959  13988  14290    469   -145     74       N  
ATOM   1478  CA  ARG A 252      23.677  34.146  25.291  1.00118.41           C  
ANISOU 1478  CA  ARG A 252    16235  14291  14464    468   -151     47       C  
ATOM   1479  C   ARG A 252      24.070  33.086  26.307  1.00119.94           C  
ANISOU 1479  C   ARG A 252    16490  14486  14594    455   -186     64       C  
ATOM   1480  O   ARG A 252      24.201  33.376  27.502  1.00122.48           O  
ANISOU 1480  O   ARG A 252    16840  14825  14873    466   -220     36       O  
ATOM   1481  CB  ARG A 252      22.165  34.138  25.077  1.00119.26           C  
ANISOU 1481  CB  ARG A 252    16334  14460  14517    446    -94     50       C  
ATOM   1482  CG  ARG A 252      21.640  35.285  24.233  1.00124.87           C  
ANISOU 1482  CG  ARG A 252    16988  15176  15281    464    -67     29       C  
ATOM   1483  CD  ARG A 252      21.304  36.485  25.082  1.00119.99           C  
ANISOU 1483  CD  ARG A 252    16351  14581  14657    490    -74    -24       C  
ATOM   1484  NE  ARG A 252      19.920  36.400  25.528  1.00115.89           N  
ANISOU 1484  NE  ARG A 252    15835  14130  14067    470    -34    -38       N  
ATOM   1485  CZ  ARG A 252      19.561  35.996  26.738  1.00123.61           C  
ANISOU 1485  CZ  ARG A 252    16854  15147  14965    453    -34    -53       C  
ATOM   1486  NH1 ARG A 252      20.460  35.663  27.650  1.00125.80           N  
ANISOU 1486  NH1 ARG A 252    17177  15405  15217    456    -78    -54       N  
ATOM   1487  NH2 ARG A 252      18.268  35.914  27.036  1.00122.81           N  
ANISOU 1487  NH2 ARG A 252    16750  15106  14807    431     12    -67       N  
ATOM   1488  N   LEU A 253      24.256  31.846  25.845  1.00106.22           N  
ANISOU 1488  N   LEU A 253    14780  12731  12850    431   -180    111       N  
ATOM   1489  CA  LEU A 253      24.642  30.759  26.738  1.00107.86           C  
ANISOU 1489  CA  LEU A 253    15051  12931  12998    419   -214    134       C  
ATOM   1490  C   LEU A 253      26.009  31.017  27.359  1.00109.22           C  
ANISOU 1490  C   LEU A 253    15230  13056  13213    454   -289    115       C  
ATOM   1491  O   LEU A 253      26.168  30.957  28.583  1.00114.35           O  
ANISOU 1491  O   LEU A 253    15924  13720  13804    462   -331    102       O  
ATOM   1492  CB  LEU A 253      24.636  29.433  25.976  1.00107.61           C  
ANISOU 1492  CB  LEU A 253    15039  12880  12968    388   -191    186       C  
ATOM   1493  CG  LEU A 253      23.308  28.671  25.930  1.00108.53           C  
ANISOU 1493  CG  LEU A 253    15183  13048  13006    344   -132    211       C  
ATOM   1494  CD1 LEU A 253      23.540  27.186  25.675  1.00107.39           C  
ANISOU 1494  CD1 LEU A 253    15081  12876  12846    316   -128    261       C  
ATOM   1495  CD2 LEU A 253      22.502  28.895  27.201  1.00109.24           C  
ANISOU 1495  CD2 LEU A 253    15309  13193  13002    335   -125    190       C  
ATOM   1496  N   LYS A 254      27.014  31.311  26.531  1.00111.04           N  
ANISOU 1496  N   LYS A 254    15415  13230  13546    474   -307    110       N  
ATOM   1497  CA  LYS A 254      28.323  31.654  27.075  1.00114.82           C  
ANISOU 1497  CA  LYS A 254    15886  13662  14078    509   -379     82       C  
ATOM   1498  C   LYS A 254      28.257  32.926  27.915  1.00119.91           C  
ANISOU 1498  C   LYS A 254    16516  14330  14714    534   -402     27       C  
ATOM   1499  O   LYS A 254      29.003  33.068  28.892  1.00124.17           O  
ANISOU 1499  O   LYS A 254    17076  14857  15248    556   -467      1       O  
ATOM   1500  CB  LYS A 254      29.340  31.804  25.943  1.00111.85           C  
ANISOU 1500  CB  LYS A 254    15457  13221  13820    521   -380     81       C  
ATOM   1501  N   SER A 255      27.358  33.849  27.561  1.00112.09           N  
ANISOU 1501  N   SER A 255    15492  13374  13722    531   -351      6       N  
ATOM   1502  CA  SER A 255      27.211  35.104  28.290  1.00110.77           C  
ANISOU 1502  CA  SER A 255    15308  13229  13553    554   -365    -50       C  
ATOM   1503  C   SER A 255      26.671  34.915  29.702  1.00116.87           C  
ANISOU 1503  C   SER A 255    16137  14052  14215    547   -383    -64       C  
ATOM   1504  O   SER A 255      26.741  35.854  30.502  1.00120.47           O  
ANISOU 1504  O   SER A 255    16586  14522  14663    567   -408   -115       O  
ATOM   1505  CB  SER A 255      26.285  36.046  27.524  1.00109.18           C  
ANISOU 1505  CB  SER A 255    15059  13050  13376    553   -304    -63       C  
ATOM   1506  OG  SER A 255      24.932  35.828  27.894  1.00106.93           O  
ANISOU 1506  OG  SER A 255    14798  12830  13000    529   -260    -57       O  
ATOM   1507  N   VAL A 256      26.125  33.739  30.021  1.00114.95           N  
ANISOU 1507  N   VAL A 256    15952  13837  13886    517   -369    -22       N  
ATOM   1508  CA  VAL A 256      25.438  33.562  31.298  1.00114.42           C  
ANISOU 1508  CA  VAL A 256    15945  13824  13705    503   -370    -32       C  
ATOM   1509  C   VAL A 256      26.387  33.787  32.470  1.00115.94           C  
ANISOU 1509  C   VAL A 256    16171  14001  13879    530   -451    -63       C  
ATOM   1510  O   VAL A 256      26.006  34.392  33.481  1.00118.52           O  
ANISOU 1510  O   VAL A 256    16520  14367  14144    533   -457   -104       O  
ATOM   1511  CB  VAL A 256      24.756  32.182  31.362  1.00111.72           C  
ANISOU 1511  CB  VAL A 256    15663  13506  13281    462   -337     23       C  
ATOM   1512  CG1 VAL A 256      25.753  31.075  31.640  1.00113.62           C  
ANISOU 1512  CG1 VAL A 256    15955  13702  13515    465   -396     62       C  
ATOM   1513  CG2 VAL A 256      23.748  32.191  32.462  1.00113.46           C  
ANISOU 1513  CG2 VAL A 256    15933  13788  13387    439   -309      7       C  
ATOM   1514  N   ARG A 257      27.635  33.335  32.345  1.00130.88           N  
ANISOU 1514  N   ARG A 257    18065  15836  15827    550   -514    -49       N  
ATOM   1515  CA  ARG A 257      28.625  33.408  33.422  1.00138.11           C  
ANISOU 1515  CA  ARG A 257    19014  16733  16729    577   -603    -75       C  
ATOM   1516  C   ARG A 257      28.083  32.861  34.747  1.00140.68           C  
ANISOU 1516  C   ARG A 257    19430  17105  16915    561   -618    -66       C  
ATOM   1517  O   ARG A 257      27.561  33.607  35.580  1.00138.10           O  
ANISOU 1517  O   ARG A 257    19118  16823  16529    561   -611   -109       O  
ATOM   1518  CB  ARG A 257      29.110  34.848  33.604  1.00142.23           C  
ANISOU 1518  CB  ARG A 257    19479  17246  17318    610   -629   -145       C  
ATOM   1519  N   SER A 262      31.748  26.220  39.216  1.00 99.37           N  
ANISOU 1519  N   SER A 262    14709  11712  11335    612  -1066    188       N  
ATOM   1520  CA  SER A 262      30.925  25.237  38.517  1.00102.97           C  
ANISOU 1520  CA  SER A 262    15186  12168  11770    567   -978    250       C  
ATOM   1521  C   SER A 262      31.323  25.118  37.048  1.00108.19           C  
ANISOU 1521  C   SER A 262    15750  12783  12576    571   -946    255       C  
ATOM   1522  O   SER A 262      31.871  26.058  36.469  1.00110.47           O  
ANISOU 1522  O   SER A 262    15945  13058  12971    596   -957    204       O  
ATOM   1523  CB  SER A 262      29.443  25.603  38.629  1.00101.77           C  
ANISOU 1523  CB  SER A 262    15050  12089  11530    517   -869    243       C  
ATOM   1524  N   ARG A 263      31.043  23.951  36.449  1.00155.13           N  
ANISOU 1524  N   ARG A 263    21719  18703  18520    544   -905    316       N  
ATOM   1525  CA  ARG A 263      31.374  23.687  35.052  1.00156.31           C  
ANISOU 1525  CA  ARG A 263    21788  18809  18794    542   -870    326       C  
ATOM   1526  C   ARG A 263      30.158  23.244  34.243  1.00156.35           C  
ANISOU 1526  C   ARG A 263    21789  18843  18774    488   -755    358       C  
ATOM   1527  O   ARG A 263      30.319  22.601  33.201  1.00158.00           O  
ANISOU 1527  O   ARG A 263    21963  19014  19055    477   -724    385       O  
ATOM   1528  CB  ARG A 263      32.482  22.636  34.941  1.00154.28           C  
ANISOU 1528  CB  ARG A 263    21549  18475  18595    570   -945    362       C  
ATOM   1529  N   GLU A 264      28.945  23.567  34.702  1.00137.18           N  
ANISOU 1529  N   GLU A 264    19393  16482  16245    452   -690    353       N  
ATOM   1530  CA  GLU A 264      27.755  23.252  33.917  1.00136.59           C  
ANISOU 1530  CA  GLU A 264    19303  16441  16154    402   -582    373       C  
ATOM   1531  C   GLU A 264      27.722  24.021  32.603  1.00135.49           C  
ANISOU 1531  C   GLU A 264    19055  16301  16126    406   -536    342       C  
ATOM   1532  O   GLU A 264      27.182  23.522  31.611  1.00131.63           O  
ANISOU 1532  O   GLU A 264    18539  15810  15663    374   -469    366       O  
ATOM   1533  CB  GLU A 264      26.493  23.534  34.729  1.00135.31           C  
ANISOU 1533  CB  GLU A 264    19191  16352  15870    366   -524    364       C  
ATOM   1534  CG  GLU A 264      26.537  22.961  36.128  1.00136.56           C  
ANISOU 1534  CG  GLU A 264    19464  16514  15908    362   -569    389       C  
ATOM   1535  CD  GLU A 264      25.421  21.963  36.378  1.00141.85           C  
ANISOU 1535  CD  GLU A 264    20211  17210  16476    304   -493    436       C  
ATOM   1536  OE1 GLU A 264      24.429  21.983  35.622  1.00145.24           O  
ANISOU 1536  OE1 GLU A 264    20595  17672  16917    265   -400    433       O  
ATOM   1537  OE2 GLU A 264      25.547  21.138  37.308  1.00143.67           O  
ANISOU 1537  OE2 GLU A 264    20546  17425  16616    296   -526    478       O  
ATOM   1538  N   LYS A 265      28.272  25.236  32.575  1.00180.81           N  
ANISOU 1538  N   LYS A 265    24731  22039  21928    442   -570    287       N  
ATOM   1539  CA  LYS A 265      28.354  25.971  31.318  1.00179.11           C  
ANISOU 1539  CA  LYS A 265    24419  21814  21820    448   -530    261       C  
ATOM   1540  C   LYS A 265      29.331  25.307  30.356  1.00179.46           C  
ANISOU 1540  C   LYS A 265    24430  21790  21968    460   -551    284       C  
ATOM   1541  O   LYS A 265      28.983  25.017  29.207  1.00178.68           O  
ANISOU 1541  O   LYS A 265    24293  21683  21913    436   -490    301       O  
ATOM   1542  CB  LYS A 265      28.754  27.423  31.580  1.00175.52           C  
ANISOU 1542  CB  LYS A 265    23911  21369  21409    483   -562    197       C  
ATOM   1543  N   ASP A 266      30.552  25.028  30.821  1.00161.13           N  
ANISOU 1543  N   ASP A 266    22122  19416  19685    496   -639    282       N  
ATOM   1544  CA  ASP A 266      31.594  24.527  29.927  1.00159.45           C  
ANISOU 1544  CA  ASP A 266    21866  19133  19585    512   -661    291       C  
ATOM   1545  C   ASP A 266      31.225  23.169  29.343  1.00156.20           C  
ANISOU 1545  C   ASP A 266    21489  18703  19158    478   -618    349       C  
ATOM   1546  O   ASP A 266      31.452  22.911  28.154  1.00154.85           O  
ANISOU 1546  O   ASP A 266    21267  18499  19069    469   -580    355       O  
ATOM   1547  CB  ASP A 266      32.925  24.450  30.672  1.00162.17           C  
ANISOU 1547  CB  ASP A 266    22220  19428  19969    559   -770    275       C  
ATOM   1548  CG  ASP A 266      33.204  25.696  31.488  1.00167.28           C  
ANISOU 1548  CG  ASP A 266    22850  20100  20610    590   -819    218       C  
ATOM   1549  OD1 ASP A 266      32.486  26.702  31.300  1.00165.33           O  
ANISOU 1549  OD1 ASP A 266    22569  19899  20351    577   -764    188       O  
ATOM   1550  OD2 ASP A 266      34.139  25.673  32.314  1.00171.23           O  
ANISOU 1550  OD2 ASP A 266    23368  20572  21119    627   -914    202       O  
ATOM   1551  N   ARG A 267      30.662  22.284  30.166  1.00178.93           N  
ANISOU 1551  N   ARG A 267    24456  21599  21930    457   -621    391       N  
ATOM   1552  CA  ARG A 267      30.230  20.983  29.670  1.00180.48           C  
ANISOU 1552  CA  ARG A 267    24688  21777  22107    421   -576    445       C  
ATOM   1553  C   ARG A 267      29.059  21.124  28.705  1.00176.93           C  
ANISOU 1553  C   ARG A 267    24204  21373  21650    376   -471    446       C  
ATOM   1554  O   ARG A 267      29.079  20.562  27.603  1.00176.13           O  
ANISOU 1554  O   ARG A 267    24071  21244  21607    357   -430    462       O  
ATOM   1555  CB  ARG A 267      29.859  20.074  30.842  1.00179.55           C  
ANISOU 1555  CB  ARG A 267    24680  21669  21873    407   -600    488       C  
ATOM   1556  N   ASN A 268      28.029  21.878  29.101  1.00120.04           N  
ANISOU 1556  N   ASN A 268    17001  14235  14372    358   -430    425       N  
ATOM   1557  CA  ASN A 268      26.845  22.023  28.258  1.00117.48           C  
ANISOU 1557  CA  ASN A 268    16643  13958  14036    317   -337    424       C  
ATOM   1558  C   ASN A 268      27.147  22.838  27.004  1.00116.68           C  
ANISOU 1558  C   ASN A 268    16450  13844  14040    331   -314    394       C  
ATOM   1559  O   ASN A 268      26.560  22.580  25.946  1.00114.77           O  
ANISOU 1559  O   ASN A 268    16177  13611  13818    302   -251    404       O  
ATOM   1560  CB  ASN A 268      25.704  22.653  29.068  1.00115.05           C  
ANISOU 1560  CB  ASN A 268    16359  13725  13631    298   -302    404       C  
ATOM   1561  CG  ASN A 268      24.340  22.547  28.384  1.00113.37           C  
ANISOU 1561  CG  ASN A 268    16125  13562  13390    251   -208    408       C  
ATOM   1562  OD1 ASN A 268      23.308  22.574  29.052  1.00113.24           O  
ANISOU 1562  OD1 ASN A 268    16143  13599  13285    223   -168    404       O  
ATOM   1563  ND2 ASN A 268      24.327  22.441  27.059  1.00113.33           N  
ANISOU 1563  ND2 ASN A 268    16062  13540  13458    242   -172    412       N  
ATOM   1564  N   LEU A 269      28.033  23.831  27.100  1.00135.06           N  
ANISOU 1564  N   LEU A 269    18734  16151  16431    374   -364    354       N  
ATOM   1565  CA  LEU A 269      28.413  24.581  25.907  1.00131.90           C  
ANISOU 1565  CA  LEU A 269    18253  15731  16133    386   -342    329       C  
ATOM   1566  C   LEU A 269      29.029  23.655  24.868  1.00131.47           C  
ANISOU 1566  C   LEU A 269    18183  15620  16151    377   -331    355       C  
ATOM   1567  O   LEU A 269      28.607  23.638  23.707  1.00129.63           O  
ANISOU 1567  O   LEU A 269    17914  15391  15949    354   -270    360       O  
ATOM   1568  CB  LEU A 269      29.380  25.707  26.270  1.00129.05           C  
ANISOU 1568  CB  LEU A 269    17853  15348  15834    432   -400    282       C  
ATOM   1569  N   ARG A 270      30.012  22.850  25.280  1.00114.80           N  
ANISOU 1569  N   ARG A 270    16101  13454  14065    395   -390    371       N  
ATOM   1570  CA  ARG A 270      30.608  21.883  24.365  1.00112.91           C  
ANISOU 1570  CA  ARG A 270    15849  13158  13895    386   -379    394       C  
ATOM   1571  C   ARG A 270      29.577  20.886  23.853  1.00112.37           C  
ANISOU 1571  C   ARG A 270    15812  13111  13771    336   -310    434       C  
ATOM   1572  O   ARG A 270      29.688  20.405  22.719  1.00110.68           O  
ANISOU 1572  O   ARG A 270    15570  12870  13613    318   -270    443       O  
ATOM   1573  CB  ARG A 270      31.761  21.149  25.055  1.00113.44           C  
ANISOU 1573  CB  ARG A 270    15947  13164  13991    417   -461    405       C  
ATOM   1574  N   ARG A 271      28.568  20.569  24.669  1.00141.23           N  
ANISOU 1574  N   ARG A 271    19526  16815  17318    312   -294    455       N  
ATOM   1575  CA  ARG A 271      27.552  19.604  24.261  1.00140.99           C  
ANISOU 1575  CA  ARG A 271    19526  16806  17236    262   -229    490       C  
ATOM   1576  C   ARG A 271      26.595  20.198  23.236  1.00141.50           C  
ANISOU 1576  C   ARG A 271    19538  16918  17306    235   -155    472       C  
ATOM   1577  O   ARG A 271      26.224  19.526  22.268  1.00143.18           O  
ANISOU 1577  O   ARG A 271    19741  17127  17536    203   -104    488       O  
ATOM   1578  CB  ARG A 271      26.782  19.102  25.482  1.00138.97           C  
ANISOU 1578  CB  ARG A 271    19351  16586  16866    241   -230    515       C  
ATOM   1579  N   ILE A 272      26.173  21.449  23.432  1.00103.95           N  
ANISOU 1579  N   ILE A 272    14751  12211  12537    249   -150    438       N  
ATOM   1580  CA  ILE A 272      25.236  22.060  22.492  1.00100.26           C  
ANISOU 1580  CA  ILE A 272    14235  11788  12073    229    -87    422       C  
ATOM   1581  C   ILE A 272      25.955  22.555  21.243  1.00100.45           C  
ANISOU 1581  C   ILE A 272    14197  11774  12196    246    -81    406       C  
ATOM   1582  O   ILE A 272      25.407  22.491  20.137  1.00 99.45           O  
ANISOU 1582  O   ILE A 272    14042  11661  12084    222    -29    409       O  
ATOM   1583  CB  ILE A 272      24.434  23.177  23.182  1.00 99.53           C  
ANISOU 1583  CB  ILE A 272    14132  11758  11927    238    -81    391       C  
ATOM   1584  CG1 ILE A 272      23.196  22.593  23.854  1.00 98.65           C  
ANISOU 1584  CG1 ILE A 272    14067  11700  11716    198    -42    406       C  
ATOM   1585  CG2 ILE A 272      24.010  24.243  22.186  1.00106.90           C  
ANISOU 1585  CG2 ILE A 272    14998  12715  12904    244    -46    364       C  
ATOM   1586  CD1 ILE A 272      22.086  22.260  22.864  1.00 98.45           C  
ANISOU 1586  CD1 ILE A 272    14016  11710  11680    157     29    412       C  
ATOM   1587  N   THR A 273      27.183  23.054  21.387  1.00128.33           N  
ANISOU 1587  N   THR A 273    17707  15257  15796    286   -133    387       N  
ATOM   1588  CA  THR A 273      28.009  23.305  20.212  1.00129.28           C  
ANISOU 1588  CA  THR A 273    17777  15329  16014    296   -123    376       C  
ATOM   1589  C   THR A 273      28.137  22.037  19.381  1.00128.48           C  
ANISOU 1589  C   THR A 273    17688  15194  15934    266    -93    405       C  
ATOM   1590  O   THR A 273      27.952  22.055  18.159  1.00125.33           O  
ANISOU 1590  O   THR A 273    17259  14793  15569    247    -44    404       O  
ATOM   1591  CB  THR A 273      29.389  23.813  20.633  1.00131.52           C  
ANISOU 1591  CB  THR A 273    18039  15559  16372    340   -186    350       C  
ATOM   1592  OG1 THR A 273      29.314  25.209  20.943  1.00129.37           O  
ANISOU 1592  OG1 THR A 273    17737  15312  16106    365   -198    314       O  
ATOM   1593  CG2 THR A 273      30.402  23.603  19.513  1.00128.12           C  
ANISOU 1593  CG2 THR A 273    17570  15065  16045    343   -174    345       C  
ATOM   1594  N   ARG A 274      28.441  20.919  20.043  1.00113.55           N  
ANISOU 1594  N   ARG A 274    15845  13276  14022    261   -122    431       N  
ATOM   1595  CA  ARG A 274      28.447  19.615  19.393  1.00114.68           C  
ANISOU 1595  CA  ARG A 274    16008  13389  14178    230    -92    460       C  
ATOM   1596  C   ARG A 274      27.162  19.395  18.603  1.00114.49           C  
ANISOU 1596  C   ARG A 274    15980  13415  14104    184    -20    470       C  
ATOM   1597  O   ARG A 274      27.189  19.183  17.386  1.00112.76           O  
ANISOU 1597  O   ARG A 274    15733  13182  13928    166     22    468       O  
ATOM   1598  CB  ARG A 274      28.621  18.530  20.456  1.00118.22           C  
ANISOU 1598  CB  ARG A 274    16522  13815  14583    229   -132    491       C  
ATOM   1599  CG  ARG A 274      29.427  17.313  20.050  1.00120.08           C  
ANISOU 1599  CG  ARG A 274    16770  13980  14876    225   -142    512       C  
ATOM   1600  CD  ARG A 274      28.817  16.068  20.675  1.00119.08           C  
ANISOU 1600  CD  ARG A 274    16715  13855  14674    196   -135    554       C  
ATOM   1601  NE  ARG A 274      28.966  16.063  22.128  1.00119.26           N  
ANISOU 1601  NE  ARG A 274    16794  13881  14639    219   -197    568       N  
ATOM   1602  CZ  ARG A 274      30.119  15.950  22.777  1.00122.22           C  
ANISOU 1602  CZ  ARG A 274    17182  14202  15055    263   -275    568       C  
ATOM   1603  NH1 ARG A 274      31.266  15.803  22.135  1.00121.53           N  
ANISOU 1603  NH1 ARG A 274    17051  14051  15075    288   -300    553       N  
ATOM   1604  NH2 ARG A 274      30.119  15.984  24.107  1.00125.68           N  
ANISOU 1604  NH2 ARG A 274    17677  14651  15424    281   -330    581       N  
ATOM   1605  N   LEU A 275      26.018  19.473  19.291  1.00102.91           N  
ANISOU 1605  N   LEU A 275    14542  12011  12550    166     -4    476       N  
ATOM   1606  CA  LEU A 275      24.732  19.189  18.657  1.00103.66           C  
ANISOU 1606  CA  LEU A 275    14633  12157  12597    121     61    482       C  
ATOM   1607  C   LEU A 275      24.438  20.183  17.540  1.00100.10           C  
ANISOU 1607  C   LEU A 275    14124  11731  12181    126     92    457       C  
ATOM   1608  O   LEU A 275      23.899  19.813  16.489  1.00 95.90           O  
ANISOU 1608  O   LEU A 275    13576  11211  11652     95    138    461       O  
ATOM   1609  CB  LEU A 275      23.628  19.211  19.720  1.00102.93           C  
ANISOU 1609  CB  LEU A 275    14576  12124  12409    104     71    487       C  
ATOM   1610  CG  LEU A 275      22.203  18.665  19.536  1.00106.09           C  
ANISOU 1610  CG  LEU A 275    14987  12579  12744     53    132    494       C  
ATOM   1611  CD1 LEU A 275      21.411  18.947  20.807  1.00107.14           C  
ANISOU 1611  CD1 LEU A 275    15151  12763  12793     47    132    489       C  
ATOM   1612  CD2 LEU A 275      21.443  19.205  18.321  1.00106.03           C  
ANISOU 1612  CD2 LEU A 275    14923  12611  12754     39    177    473       C  
ATOM   1613  N   VAL A 276      24.776  21.453  17.754  1.00148.23           N  
ANISOU 1613  N   VAL A 276    20188  17832  18300    163     65    432       N  
ATOM   1614  CA  VAL A 276      24.476  22.475  16.758  1.00149.08           C  
ANISOU 1614  CA  VAL A 276    20246  17960  18437    170     91    411       C  
ATOM   1615  C   VAL A 276      25.219  22.182  15.461  1.00148.07           C  
ANISOU 1615  C   VAL A 276    20098  17782  18381    164    111    414       C  
ATOM   1616  O   VAL A 276      24.627  22.172  14.375  1.00146.66           O  
ANISOU 1616  O   VAL A 276    19902  17623  18199    141    154    416       O  
ATOM   1617  CB  VAL A 276      24.825  23.870  17.305  1.00146.49           C  
ANISOU 1617  CB  VAL A 276    19893  17636  18129    213     57    383       C  
ATOM   1618  CG1 VAL A 276      25.134  24.837  16.169  1.00144.39           C  
ANISOU 1618  CG1 VAL A 276    19580  17354  17926    229     74    366       C  
ATOM   1619  CG2 VAL A 276      23.710  24.384  18.203  1.00146.01           C  
ANISOU 1619  CG2 VAL A 276    19840  17642  17994    212     60    371       C  
ATOM   1620  N   LEU A 277      26.524  21.907  15.561  1.00102.57           N  
ANISOU 1620  N   LEU A 277    14336  11954  12683    184     80    414       N  
ATOM   1621  CA  LEU A 277      27.340  21.729  14.362  1.00100.61           C  
ANISOU 1621  CA  LEU A 277    14064  11653  12510    179    102    410       C  
ATOM   1622  C   LEU A 277      26.825  20.604  13.482  1.00 99.59           C  
ANISOU 1622  C   LEU A 277    13949  11527  12362    135    149    429       C  
ATOM   1623  O   LEU A 277      26.996  20.648  12.260  1.00 98.11           O  
ANISOU 1623  O   LEU A 277    13742  11324  12211    121    186    423       O  
ATOM   1624  CB  LEU A 277      28.801  21.466  14.728  1.00 98.63           C  
ANISOU 1624  CB  LEU A 277    13809  11330  12335    206     60    402       C  
ATOM   1625  CG  LEU A 277      29.584  22.511  15.517  1.00100.24           C  
ANISOU 1625  CG  LEU A 277    13993  11517  12577    250      8    376       C  
ATOM   1626  CD1 LEU A 277      31.040  22.478  15.095  1.00100.34           C  
ANISOU 1626  CD1 LEU A 277    13975  11453  12695    269     -6    357       C  
ATOM   1627  CD2 LEU A 277      29.004  23.890  15.282  1.00100.23           C  
ANISOU 1627  CD2 LEU A 277    13964  11558  12562    261     25    358       C  
ATOM   1628  N   VAL A 278      26.196  19.592  14.072  1.00 99.25           N  
ANISOU 1628  N   VAL A 278    13945  11504  12262    110    152    450       N  
ATOM   1629  CA  VAL A 278      25.775  18.442  13.284  1.00101.42           C  
ANISOU 1629  CA  VAL A 278    14234  11776  12525     66    195    465       C  
ATOM   1630  C   VAL A 278      24.696  18.846  12.286  1.00 99.57           C  
ANISOU 1630  C   VAL A 278    13978  11596  12257     41    241    457       C  
ATOM   1631  O   VAL A 278      24.793  18.543  11.091  1.00 98.57           O  
ANISOU 1631  O   VAL A 278    13840  11455  12157     20    276    454       O  
ATOM   1632  CB  VAL A 278      25.312  17.299  14.207  1.00 97.97           C  
ANISOU 1632  CB  VAL A 278    13846  11345  12034     43    189    490       C  
ATOM   1633  CG1 VAL A 278      24.307  16.415  13.500  1.00 97.06           C  
ANISOU 1633  CG1 VAL A 278    13740  11258  11880     -9    243    499       C  
ATOM   1634  CG2 VAL A 278      26.507  16.487  14.669  1.00 88.37           C  
ANISOU 1634  CG2 VAL A 278    12653  10055  10868     59    153    502       C  
ATOM   1635  N   VAL A 279      23.671  19.564  12.747  1.00104.29           N  
ANISOU 1635  N   VAL A 279    14570  12259  12798     44    240    451       N  
ATOM   1636  CA  VAL A 279      22.550  19.882  11.866  1.00105.73           C  
ANISOU 1636  CA  VAL A 279    14730  12496  12945     22    277    443       C  
ATOM   1637  C   VAL A 279      23.012  20.739  10.697  1.00103.34           C  
ANISOU 1637  C   VAL A 279    14398  12176  12691     39    286    431       C  
ATOM   1638  O   VAL A 279      22.639  20.498   9.543  1.00100.50           O  
ANISOU 1638  O   VAL A 279    14031  11826  12327     14    320    430       O  
ATOM   1639  CB  VAL A 279      21.418  20.570  12.643  1.00104.81           C  
ANISOU 1639  CB  VAL A 279    14606  12448  12769     28    271    434       C  
ATOM   1640  CG1 VAL A 279      20.205  20.650  11.754  1.00100.11           C  
ANISOU 1640  CG1 VAL A 279    13989  11907  12139      2    306    425       C  
ATOM   1641  CG2 VAL A 279      21.109  19.810  13.918  1.00106.11           C  
ANISOU 1641  CG2 VAL A 279    14808  12623  12885     14    263    446       C  
ATOM   1642  N   VAL A 280      23.817  21.765  10.978  1.00114.44           N  
ANISOU 1642  N   VAL A 280    15787  13554  14139     80    258    420       N  
ATOM   1643  CA  VAL A 280      24.327  22.581   9.884  1.00117.06           C  
ANISOU 1643  CA  VAL A 280    16097  13862  14520     93    272    411       C  
ATOM   1644  C   VAL A 280      25.311  21.777   9.042  1.00114.63           C  
ANISOU 1644  C   VAL A 280    15795  13493  14266     75    295    414       C  
ATOM   1645  O   VAL A 280      25.374  21.952   7.820  1.00115.44           O  
ANISOU 1645  O   VAL A 280    15891  13586  14384     62    328    411       O  
ATOM   1646  CB  VAL A 280      24.933  23.898  10.414  1.00113.21           C  
ANISOU 1646  CB  VAL A 280    15589  13358  14069    138    241    395       C  
ATOM   1647  CG1 VAL A 280      24.044  24.484  11.493  1.00110.48           C  
ANISOU 1647  CG1 VAL A 280    15240  13068  13670    155    216    389       C  
ATOM   1648  CG2 VAL A 280      26.348  23.700  10.935  1.00112.74           C  
ANISOU 1648  CG2 VAL A 280    15529  13231  14076    158    214    389       C  
ATOM   1649  N   ALA A 281      26.081  20.878   9.660  1.00 85.11           N  
ANISOU 1649  N   ALA A 281    12072   9710  10556     74    278    419       N  
ATOM   1650  CA  ALA A 281      26.922  19.992   8.867  1.00 85.16           C  
ANISOU 1650  CA  ALA A 281    12082   9659  10615     54    304    418       C  
ATOM   1651  C   ALA A 281      26.068  19.091   7.988  1.00 85.46           C  
ANISOU 1651  C   ALA A 281    12135   9724  10610      8    347    427       C  
ATOM   1652  O   ALA A 281      26.383  18.874   6.812  1.00 85.09           O  
ANISOU 1652  O   ALA A 281    12085   9655  10591    -12    384    420       O  
ATOM   1653  CB  ALA A 281      27.828  19.161   9.773  1.00 85.40           C  
ANISOU 1653  CB  ALA A 281    12126   9637  10685     65    270    423       C  
ATOM   1654  N   VAL A 282      24.975  18.565   8.543  1.00 92.39           N  
ANISOU 1654  N   VAL A 282    13030  10653  11421    -12    345    439       N  
ATOM   1655  CA  VAL A 282      24.035  17.776   7.751  1.00 90.23           C  
ANISOU 1655  CA  VAL A 282    12766  10413  11104    -58    385    442       C  
ATOM   1656  C   VAL A 282      23.469  18.622   6.621  1.00 87.22           C  
ANISOU 1656  C   VAL A 282    12366  10069  10705    -61    406    431       C  
ATOM   1657  O   VAL A 282      23.614  18.292   5.440  1.00 85.48           O  
ANISOU 1657  O   VAL A 282    12148   9834  10497    -84    440    426       O  
ATOM   1658  CB  VAL A 282      22.915  17.218   8.647  1.00 91.36           C  
ANISOU 1658  CB  VAL A 282    12925  10606  11180    -78    380    452       C  
ATOM   1659  CG1 VAL A 282      21.642  16.973   7.841  1.00 91.82           C  
ANISOU 1659  CG1 VAL A 282    12977  10724  11187   -116    415    446       C  
ATOM   1660  CG2 VAL A 282      23.375  15.949   9.335  1.00 87.19           C  
ANISOU 1660  CG2 VAL A 282    12430  10035  10665    -93    376    468       C  
ATOM   1661  N   PHE A 283      22.857  19.752   6.971  1.00 97.61           N  
ANISOU 1661  N   PHE A 283    13666  11431  11992    -35    386    428       N  
ATOM   1662  CA  PHE A 283      22.147  20.546   5.976  1.00101.28           C  
ANISOU 1662  CA  PHE A 283    14115  11936  12431    -35    399    422       C  
ATOM   1663  C   PHE A 283      23.089  21.075   4.903  1.00 99.01           C  
ANISOU 1663  C   PHE A 283    13827  11601  12192    -25    416    418       C  
ATOM   1664  O   PHE A 283      22.733  21.112   3.718  1.00 96.46           O  
ANISOU 1664  O   PHE A 283    13509  11292  11851    -44    442    416       O  
ATOM   1665  CB  PHE A 283      21.404  21.692   6.658  1.00100.86           C  
ANISOU 1665  CB  PHE A 283    14042  11931  12348     -3    371    417       C  
ATOM   1666  CG  PHE A 283      20.401  22.356   5.773  1.00 97.74           C  
ANISOU 1666  CG  PHE A 283    13634  11587  11917     -3    378    412       C  
ATOM   1667  CD1 PHE A 283      20.791  23.319   4.859  1.00 93.85           C  
ANISOU 1667  CD1 PHE A 283    13137  11075  11447     18    380    413       C  
ATOM   1668  CD2 PHE A 283      19.070  21.987   5.826  1.00 97.65           C  
ANISOU 1668  CD2 PHE A 283    13613  11640  11850    -26    382    406       C  
ATOM   1669  CE1 PHE A 283      19.865  23.921   4.035  1.00 99.21           C  
ANISOU 1669  CE1 PHE A 283    13808  11798  12090     21    380    411       C  
ATOM   1670  CE2 PHE A 283      18.138  22.584   5.003  1.00 96.72           C  
ANISOU 1670  CE2 PHE A 283    13479  11569  11702    -23    380    399       C  
ATOM   1671  CZ  PHE A 283      18.535  23.552   4.106  1.00100.27           C  
ANISOU 1671  CZ  PHE A 283    13929  11998  12171      3    376    404       C  
ATOM   1672  N   VAL A 284      24.288  21.508   5.296  1.00 96.33           N  
ANISOU 1672  N   VAL A 284    13481  11204  11914      3    403    415       N  
ATOM   1673  CA  VAL A 284      25.247  21.998   4.311  1.00 94.27           C  
ANISOU 1673  CA  VAL A 284    13219  10893  11706      8    427    408       C  
ATOM   1674  C   VAL A 284      25.611  20.884   3.340  1.00 94.90           C  
ANISOU 1674  C   VAL A 284    13316  10944  11800    -32    469    406       C  
ATOM   1675  O   VAL A 284      25.334  20.970   2.139  1.00 93.47           O  
ANISOU 1675  O   VAL A 284    13145  10772  11597    -53    501    404       O  
ATOM   1676  CB  VAL A 284      26.494  22.579   5.000  1.00 92.95           C  
ANISOU 1676  CB  VAL A 284    13036  10669  11611     43    406    399       C  
ATOM   1677  CG1 VAL A 284      27.689  22.568   4.058  1.00 89.08           C  
ANISOU 1677  CG1 VAL A 284    12545  10112  11190     35    442    388       C  
ATOM   1678  CG2 VAL A 284      26.207  23.990   5.466  1.00 99.25           C  
ANISOU 1678  CG2 VAL A 284    13818  11490  12401     81    378    397       C  
ATOM   1679  N   VAL A 285      26.193  19.797   3.856  1.00 86.44           N  
ANISOU 1679  N   VAL A 285    12249   9835  10760    -44    468    404       N  
ATOM   1680  CA  VAL A 285      26.688  18.751   2.972  1.00 85.06           C  
ANISOU 1680  CA  VAL A 285    12086   9621  10612    -80    509    396       C  
ATOM   1681  C   VAL A 285      25.550  18.053   2.240  1.00 85.10           C  
ANISOU 1681  C   VAL A 285    12107   9676  10550   -121    534    399       C  
ATOM   1682  O   VAL A 285      25.769  17.475   1.171  1.00 85.20           O  
ANISOU 1682  O   VAL A 285    12132   9670  10571   -153    575    389       O  
ATOM   1683  CB  VAL A 285      27.538  17.737   3.755  1.00 85.19           C  
ANISOU 1683  CB  VAL A 285    12104   9583  10683    -78    495    395       C  
ATOM   1684  CG1 VAL A 285      28.582  18.453   4.601  1.00 85.21           C  
ANISOU 1684  CG1 VAL A 285    12085   9542  10748    -34    459    389       C  
ATOM   1685  CG2 VAL A 285      26.651  16.853   4.598  1.00 85.24           C  
ANISOU 1685  CG2 VAL A 285    12126   9626  10637    -93    476    410       C  
ATOM   1686  N   CYS A 286      24.329  18.104   2.774  1.00109.11           N  
ANISOU 1686  N   CYS A 286    15148  12783  13527   -123    512    408       N  
ATOM   1687  CA  CYS A 286      23.216  17.458   2.090  1.00110.53           C  
ANISOU 1687  CA  CYS A 286    15336  13012  13646   -163    534    406       C  
ATOM   1688  C   CYS A 286      22.789  18.249   0.856  1.00111.54           C  
ANISOU 1688  C   CYS A 286    15466  13170  13744   -166    548    401       C  
ATOM   1689  O   CYS A 286      22.568  17.668  -0.213  1.00112.83           O  
ANISOU 1689  O   CYS A 286    15644  13339  13887   -201    580    392       O  
ATOM   1690  CB  CYS A 286      22.046  17.266   3.053  1.00113.18           C  
ANISOU 1690  CB  CYS A 286    15668  13408  13930   -167    510    412       C  
ATOM   1691  SG  CYS A 286      22.019  15.630   3.844  1.00123.13           S  
ANISOU 1691  SG  CYS A 286    16946  14646  15192   -201    519    418       S  
ATOM   1692  N   TRP A 287      22.686  19.581   0.972  1.00 86.03           N  
ANISOU 1692  N   TRP A 287    12225   9956  10508   -128    525    407       N  
ATOM   1693  CA  TRP A 287      22.164  20.387  -0.126  1.00 85.12           C  
ANISOU 1693  CA  TRP A 287    12116   9872  10356   -125    531    407       C  
ATOM   1694  C   TRP A 287      23.178  21.276  -0.830  1.00 85.14           C  
ANISOU 1694  C   TRP A 287    12128   9823  10398   -107    548    410       C  
ATOM   1695  O   TRP A 287      22.896  21.715  -1.945  1.00 85.28           O  
ANISOU 1695  O   TRP A 287    12165   9854  10384   -114    563    412       O  
ATOM   1696  CB  TRP A 287      21.007  21.283   0.338  1.00 85.11           C  
ANISOU 1696  CB  TRP A 287    12094   9934  10308    -98    492    412       C  
ATOM   1697  CG  TRP A 287      19.935  20.581   1.083  1.00 85.14           C  
ANISOU 1697  CG  TRP A 287    12084   9992  10273   -115    478    407       C  
ATOM   1698  CD1 TRP A 287      19.976  20.143   2.371  1.00 85.33           C  
ANISOU 1698  CD1 TRP A 287    12100  10013  10308   -112    466    408       C  
ATOM   1699  CD2 TRP A 287      18.659  20.193   0.564  1.00 85.78           C  
ANISOU 1699  CD2 TRP A 287    12160  10136  10297   -142    478    397       C  
ATOM   1700  NE1 TRP A 287      18.791  19.531   2.699  1.00 86.60           N  
ANISOU 1700  NE1 TRP A 287    12252  10231  10423   -137    464    401       N  
ATOM   1701  CE2 TRP A 287      17.967  19.542   1.604  1.00 88.04           C  
ANISOU 1701  CE2 TRP A 287    12431  10455  10566   -156    471    392       C  
ATOM   1702  CE3 TRP A 287      18.032  20.339  -0.678  1.00 85.51           C  
ANISOU 1702  CE3 TRP A 287    12132  10134  10223   -155    482    392       C  
ATOM   1703  CZ2 TRP A 287      16.676  19.034   1.442  1.00 89.75           C  
ANISOU 1703  CZ2 TRP A 287    12632  10733  10735   -185    472    377       C  
ATOM   1704  CZ3 TRP A 287      16.748  19.842  -0.838  1.00 85.71           C  
ANISOU 1704  CZ3 TRP A 287    12141  10223  10200   -180    475    376       C  
ATOM   1705  CH2 TRP A 287      16.084  19.198   0.217  1.00 87.77           C  
ANISOU 1705  CH2 TRP A 287    12381  10514  10452   -196    472    367       C  
ATOM   1706  N   THR A 288      24.319  21.584  -0.225  1.00105.02           N  
ANISOU 1706  N   THR A 288    14636  12283  12982    -84    547    408       N  
ATOM   1707  CA  THR A 288      25.261  22.463  -0.918  1.00107.35           C  
ANISOU 1707  CA  THR A 288    14941  12530  13320    -71    570    407       C  
ATOM   1708  C   THR A 288      25.756  21.873  -2.234  1.00106.57           C  
ANISOU 1708  C   THR A 288    14868  12398  13225   -110    624    398       C  
ATOM   1709  O   THR A 288      25.760  22.601  -3.243  1.00108.25           O  
ANISOU 1709  O   THR A 288    15104  12609  13418   -111    646    404       O  
ATOM   1710  CB  THR A 288      26.431  22.836   0.000  1.00109.82           C  
ANISOU 1710  CB  THR A 288    15230  12784  13711    -41    558    399       C  
ATOM   1711  OG1 THR A 288      26.025  23.889   0.885  1.00108.31           O  
ANISOU 1711  OG1 THR A 288    15021  12620  13511     -1    515    406       O  
ATOM   1712  CG2 THR A 288      27.627  23.315  -0.820  1.00104.38           C  
ANISOU 1712  CG2 THR A 288    14549  12030  13082    -44    600    390       C  
ATOM   1713  N   PRO A 289      26.181  20.604  -2.314  1.00114.99           N  
ANISOU 1713  N   PRO A 289    15936  13438  14315   -142    650    385       N  
ATOM   1714  CA  PRO A 289      26.695  20.101  -3.600  1.00117.40           C  
ANISOU 1714  CA  PRO A 289    16268  13712  14628   -180    706    371       C  
ATOM   1715  C   PRO A 289      25.656  20.026  -4.714  1.00115.94           C  
ANISOU 1715  C   PRO A 289    16112  13580  14358   -207    718    376       C  
ATOM   1716  O   PRO A 289      26.021  20.226  -5.880  1.00117.36           O  
ANISOU 1716  O   PRO A 289    16323  13740  14529   -227    760    371       O  
ATOM   1717  CB  PRO A 289      27.247  18.714  -3.243  1.00117.23           C  
ANISOU 1717  CB  PRO A 289    16236  13652  14652   -204    722    355       C  
ATOM   1718  CG  PRO A 289      26.521  18.319  -2.012  1.00117.39           C  
ANISOU 1718  CG  PRO A 289    16240  13711  14652   -190    673    366       C  
ATOM   1719  CD  PRO A 289      26.299  19.586  -1.252  1.00116.24           C  
ANISOU 1719  CD  PRO A 289    16078  13587  14500   -145    630    381       C  
ATOM   1720  N   ILE A 290      24.387  19.733  -4.415  1.00 85.70           N  
ANISOU 1720  N   ILE A 290    12277   9819  10467   -211    683    382       N  
ATOM   1721  CA  ILE A 290      23.383  19.684  -5.478  1.00 85.92           C  
ANISOU 1721  CA  ILE A 290    12330   9900  10416   -234    687    382       C  
ATOM   1722  C   ILE A 290      23.061  21.085  -5.977  1.00 86.01           C  
ANISOU 1722  C   ILE A 290    12357   9932  10393   -204    668    400       C  
ATOM   1723  O   ILE A 290      23.044  21.342  -7.187  1.00 86.30           O  
ANISOU 1723  O   ILE A 290    12430   9968  10392   -219    692    402       O  
ATOM   1724  CB  ILE A 290      22.109  18.956  -5.014  1.00 85.89           C  
ANISOU 1724  CB  ILE A 290    12309   9962  10364   -249    656    378       C  
ATOM   1725  CG1 ILE A 290      20.986  19.199  -6.025  1.00 86.15           C  
ANISOU 1725  CG1 ILE A 290    12359  10057  10317   -261    644    377       C  
ATOM   1726  CG2 ILE A 290      21.687  19.419  -3.637  1.00 85.65           C  
ANISOU 1726  CG2 ILE A 290    12245   9956  10342   -212    610    389       C  
ATOM   1727  CD1 ILE A 290      19.723  18.436  -5.754  1.00 86.21           C  
ANISOU 1727  CD1 ILE A 290    12348  10130  10280   -283    621    365       C  
ATOM   1728  N   HIS A 291      22.812  22.017  -5.050  1.00 90.00           N  
ANISOU 1728  N   HIS A 291    12837  10451  10909   -160    626    414       N  
ATOM   1729  CA  HIS A 291      22.434  23.370  -5.441  1.00 85.94           C  
ANISOU 1729  CA  HIS A 291    12335   9954  10366   -126    604    433       C  
ATOM   1730  C   HIS A 291      23.522  24.011  -6.283  1.00 86.12           C  
ANISOU 1730  C   HIS A 291    12391   9914  10417   -127    647    439       C  
ATOM   1731  O   HIS A 291      23.227  24.679  -7.279  1.00 86.41           O  
ANISOU 1731  O   HIS A 291    12465   9960  10407   -125    651    453       O  
ATOM   1732  CB  HIS A 291      22.130  24.218  -4.206  1.00 85.72           C  
ANISOU 1732  CB  HIS A 291    12271   9942  10357    -79    558    441       C  
ATOM   1733  CG  HIS A 291      20.720  24.084  -3.726  1.00 85.71           C  
ANISOU 1733  CG  HIS A 291    12245  10016  10304    -72    514    439       C  
ATOM   1734  ND1 HIS A 291      20.399  23.821  -2.412  1.00 85.49           N  
ANISOU 1734  ND1 HIS A 291    12181  10010  10292    -61    488    432       N  
ATOM   1735  CD2 HIS A 291      19.544  24.136  -4.397  1.00 85.94           C  
ANISOU 1735  CD2 HIS A 291    12281  10106  10268    -78    492    439       C  
ATOM   1736  CE1 HIS A 291      19.085  23.742  -2.290  1.00 85.59           C  
ANISOU 1736  CE1 HIS A 291    12176  10091  10253    -61    459    426       C  
ATOM   1737  NE2 HIS A 291      18.543  23.927  -3.480  1.00 85.86           N  
ANISOU 1737  NE2 HIS A 291    12232  10150  10241    -70    458    430       N  
ATOM   1738  N   ILE A 292      24.788  23.800  -5.915  1.00 86.99           N  
ANISOU 1738  N   ILE A 292    12491   9958  10604   -131    680    427       N  
ATOM   1739  CA  ILE A 292      25.884  24.255  -6.764  1.00 89.51           C  
ANISOU 1739  CA  ILE A 292    12839  10213  10957   -141    734    426       C  
ATOM   1740  C   ILE A 292      25.820  23.565  -8.119  1.00 94.91           C  
ANISOU 1740  C   ILE A 292    13568  10900  11594   -188    779    418       C  
ATOM   1741  O   ILE A 292      25.999  24.200  -9.166  1.00 95.25           O  
ANISOU 1741  O   ILE A 292    13656  10927  11608   -196    809    429       O  
ATOM   1742  CB  ILE A 292      27.241  24.019  -6.077  1.00 87.79           C  
ANISOU 1742  CB  ILE A 292    12591   9925  10839   -139    759    406       C  
ATOM   1743  CG1 ILE A 292      27.540  25.146  -5.092  1.00 91.65           C  
ANISOU 1743  CG1 ILE A 292    13052  10397  11375    -91    725    414       C  
ATOM   1744  CG2 ILE A 292      28.355  23.944  -7.111  1.00 86.51           C  
ANISOU 1744  CG2 ILE A 292    12457   9698  10714   -170    831    392       C  
ATOM   1745  CD1 ILE A 292      28.987  25.190  -4.639  1.00 96.19           C  
ANISOU 1745  CD1 ILE A 292    13600  10895  12051    -86    751    392       C  
ATOM   1746  N   PHE A 293      25.552  22.257  -8.125  1.00115.97           N  
ANISOU 1746  N   PHE A 293    16227  13586  14249   -222    786    400       N  
ATOM   1747  CA  PHE A 293      25.595  21.508  -9.374  1.00114.30           C  
ANISOU 1747  CA  PHE A 293    16056  13373  14000   -270    834    385       C  
ATOM   1748  C   PHE A 293      24.483  21.933 -10.325  1.00116.81           C  
ANISOU 1748  C   PHE A 293    16415  13751  14218   -273    812    401       C  
ATOM   1749  O   PHE A 293      24.740  22.221 -11.499  1.00120.81           O  
ANISOU 1749  O   PHE A 293    16972  14241  14688   -293    850    405       O  
ATOM   1750  CB  PHE A 293      25.518  20.009  -9.096  1.00117.26           C  
ANISOU 1750  CB  PHE A 293    16412  13754  14390   -303    844    360       C  
ATOM   1751  CG  PHE A 293      26.184  19.174 -10.150  1.00126.55           C  
ANISOU 1751  CG  PHE A 293    17617  14892  15573   -352    911    334       C  
ATOM   1752  CD1 PHE A 293      27.554  18.955 -10.120  1.00129.00           C  
ANISOU 1752  CD1 PHE A 293    17919  15126  15971   -361    963    314       C  
ATOM   1753  CD2 PHE A 293      25.447  18.639 -11.193  1.00122.23           C  
ANISOU 1753  CD2 PHE A 293    17107  14388  14949   -389    923    325       C  
ATOM   1754  CE1 PHE A 293      28.170  18.196 -11.098  1.00126.09           C  
ANISOU 1754  CE1 PHE A 293    17576  14722  15612   -407   1030    286       C  
ATOM   1755  CE2 PHE A 293      26.059  17.889 -12.176  1.00120.61           C  
ANISOU 1755  CE2 PHE A 293    16931  14148  14747   -436    988    297       C  
ATOM   1756  CZ  PHE A 293      27.420  17.662 -12.127  1.00122.95           C  
ANISOU 1756  CZ  PHE A 293    17218  14367  15132   -445   1044    277       C  
ATOM   1757  N   ILE A 294      23.236  21.982  -9.844  1.00 87.03           N  
ANISOU 1757  N   ILE A 294    12621  10048  10399   -254    750    410       N  
ATOM   1758  CA  ILE A 294      22.125  22.193 -10.771  1.00 87.38           C  
ANISOU 1758  CA  ILE A 294    12698  10152  10350   -260    723    419       C  
ATOM   1759  C   ILE A 294      22.039  23.634 -11.271  1.00 88.79           C  
ANISOU 1759  C   ILE A 294    12911  10326  10498   -224    706    450       C  
ATOM   1760  O   ILE A 294      21.390  23.893 -12.294  1.00 90.02           O  
ANISOU 1760  O   ILE A 294    13110  10515  10577   -230    692    460       O  
ATOM   1761  CB  ILE A 294      20.782  21.747 -10.160  1.00 87.26           C  
ANISOU 1761  CB  ILE A 294    12643  10212  10299   -254    666    412       C  
ATOM   1762  CG1 ILE A 294      20.121  22.862  -9.361  1.00 87.11           C  
ANISOU 1762  CG1 ILE A 294    12595  10223  10279   -199    607    433       C  
ATOM   1763  CG2 ILE A 294      20.955  20.507  -9.315  1.00 86.97           C  
ANISOU 1763  CG2 ILE A 294    12568  10168  10308   -278    680    389       C  
ATOM   1764  CD1 ILE A 294      18.758  22.469  -8.889  1.00 87.09           C  
ANISOU 1764  CD1 ILE A 294    12555  10296  10239   -197    556    422       C  
ATOM   1765  N   LEU A 295      22.674  24.585 -10.585  1.00104.29           N  
ANISOU 1765  N   LEU A 295    14857  12248  12519   -187    704    465       N  
ATOM   1766  CA  LEU A 295      22.795  25.923 -11.153  1.00105.25           C  
ANISOU 1766  CA  LEU A 295    15020  12349  12621   -159    702    495       C  
ATOM   1767  C   LEU A 295      23.758  25.928 -12.335  1.00109.06           C  
ANISOU 1767  C   LEU A 295    15564  12776  13098   -195    774    495       C  
ATOM   1768  O   LEU A 295      23.448  26.489 -13.394  1.00109.34           O  
ANISOU 1768  O   LEU A 295    15661  12820  13065   -197    775    516       O  
ATOM   1769  CB  LEU A 295      23.243  26.916 -10.080  1.00102.76           C  
ANISOU 1769  CB  LEU A 295    14669  12001  12375   -114    684    506       C  
ATOM   1770  CG  LEU A 295      22.208  27.287  -9.012  1.00105.24           C  
ANISOU 1770  CG  LEU A 295    14933  12370  12684    -71    612    511       C  
ATOM   1771  CD1 LEU A 295      22.422  28.709  -8.519  1.00 94.15           C  
ANISOU 1771  CD1 LEU A 295    13521  10937  11314    -22    592    531       C  
ATOM   1772  CD2 LEU A 295      20.785  27.108  -9.540  1.00103.04           C  
ANISOU 1772  CD2 LEU A 295    14663  12168  12319    -70    565    515       C  
ATOM   1773  N   VAL A 296      24.917  25.279 -12.186  1.00117.89           N  
ANISOU 1773  N   VAL A 296    16670  13838  14286   -224    834    470       N  
ATOM   1774  CA  VAL A 296      25.904  25.254 -13.262  1.00118.42           C  
ANISOU 1774  CA  VAL A 296    16789  13847  14356   -262    913    464       C  
ATOM   1775  C   VAL A 296      25.350  24.546 -14.491  1.00120.09           C  
ANISOU 1775  C   VAL A 296    17055  14096  14478   -304    929    456       C  
ATOM   1776  O   VAL A 296      25.667  24.921 -15.626  1.00123.65           O  
ANISOU 1776  O   VAL A 296    17574  14524  14884   -325    973    466       O  
ATOM   1777  CB  VAL A 296      27.214  24.606 -12.771  1.00114.37           C  
ANISOU 1777  CB  VAL A 296    16239  13269  13946   -282    970    431       C  
ATOM   1778  CG1 VAL A 296      28.251  24.580 -13.881  1.00116.64           C  
ANISOU 1778  CG1 VAL A 296    16577  13496  14245   -324   1059    417       C  
ATOM   1779  CG2 VAL A 296      27.753  25.361 -11.571  1.00113.75           C  
ANISOU 1779  CG2 VAL A 296    16110  13157  13954   -239    947    436       C  
ATOM   1780  N   GLU A 297      24.514  23.522 -14.295  1.00136.12           N  
ANISOU 1780  N   GLU A 297    19059  16184  16478   -318    895    438       N  
ATOM   1781  CA  GLU A 297      23.847  22.863 -15.413  1.00141.18           C  
ANISOU 1781  CA  GLU A 297    19746  16867  17028   -356    899    428       C  
ATOM   1782  C   GLU A 297      22.857  23.774 -16.128  1.00142.59           C  
ANISOU 1782  C   GLU A 297    19972  17093  17111   -332    847    461       C  
ATOM   1783  O   GLU A 297      22.435  23.447 -17.243  1.00141.32           O  
ANISOU 1783  O   GLU A 297    19867  16961  16868   -361    853    456       O  
ATOM   1784  CB  GLU A 297      23.125  21.601 -14.930  1.00138.76           C  
ANISOU 1784  CB  GLU A 297    19393  16611  16720   -375    870    399       C  
ATOM   1785  N   ALA A 298      22.477  24.898 -15.515  1.00116.50           N  
ANISOU 1785  N   ALA A 298    16650  13797  13816   -278    794    492       N  
ATOM   1786  CA  ALA A 298      21.577  25.857 -16.145  1.00114.46           C  
ANISOU 1786  CA  ALA A 298    16438  13577  13476   -247    740    526       C  
ATOM   1787  C   ALA A 298      22.314  26.936 -16.929  1.00111.42           C  
ANISOU 1787  C   ALA A 298    16125  13134  13077   -241    781    558       C  
ATOM   1788  O   ALA A 298      21.754  27.484 -17.884  1.00105.74           O  
ANISOU 1788  O   ALA A 298    15472  12435  12271   -234    756    585       O  
ATOM   1789  CB  ALA A 298      20.678  26.509 -15.091  1.00105.97           C  
ANISOU 1789  CB  ALA A 298    15303  12542  12417   -190    660    540       C  
ATOM   1790  N   LEU A 299      23.550  27.264 -16.546  1.00112.59           N  
ANISOU 1790  N   LEU A 299    16263  13207  13307   -244    842    557       N  
ATOM   1791  CA  LEU A 299      24.345  28.182 -17.356  1.00113.70           C  
ANISOU 1791  CA  LEU A 299    16476  13285  13438   -250    897    582       C  
ATOM   1792  C   LEU A 299      25.082  27.452 -18.472  1.00119.77           C  
ANISOU 1792  C   LEU A 299    17304  14024  14180   -314    983    561       C  
ATOM   1793  O   LEU A 299      25.166  27.955 -19.600  1.00119.42           O  
ANISOU 1793  O   LEU A 299    17348  13963  14064   -329   1012    584       O  
ATOM   1794  CB  LEU A 299      25.319  28.967 -16.470  1.00114.74           C  
ANISOU 1794  CB  LEU A 299    16570  13350  13675   -225    924    586       C  
ATOM   1795  CG  LEU A 299      26.609  28.393 -15.868  1.00116.33           C  
ANISOU 1795  CG  LEU A 299    16722  13492  13986   -251    992    549       C  
ATOM   1796  CD1 LEU A 299      27.798  28.454 -16.822  1.00114.57           C  
ANISOU 1796  CD1 LEU A 299    16556  13197  13778   -296   1093    540       C  
ATOM   1797  CD2 LEU A 299      26.940  29.146 -14.584  1.00120.23           C  
ANISOU 1797  CD2 LEU A 299    17153  13959  14571   -205    964    553       C  
ATOM   1798  N   GLY A 300      25.619  26.275 -18.180  1.00176.15           N  
ANISOU 1798  N   GLY A 300    24401  21154  21374   -350   1025    516       N  
ATOM   1799  CA  GLY A 300      26.346  25.546 -19.187  1.00177.42           C  
ANISOU 1799  CA  GLY A 300    24610  21283  21518   -411   1110    489       C  
ATOM   1800  C   GLY A 300      26.434  24.081 -18.840  1.00178.57           C  
ANISOU 1800  C   GLY A 300    24703  21444  21702   -444   1125    440       C  
ATOM   1801  O   GLY A 300      25.766  23.596 -17.924  1.00175.70           O  
ANISOU 1801  O   GLY A 300    24274  21124  21359   -423   1063    433       O  
ATOM   1802  N   SER A 301      27.270  23.385 -19.598  1.00164.55           N  
ANISOU 1802  N   SER A 301    22958  19629  19936   -498   1211    407       N  
ATOM   1803  CA  SER A 301      27.548  21.970 -19.397  1.00163.43           C  
ANISOU 1803  CA  SER A 301    22772  19484  19839   -535   1241    358       C  
ATOM   1804  C   SER A 301      26.276  21.142 -19.259  1.00162.01           C  
ANISOU 1804  C   SER A 301    22571  19385  19600   -536   1170    350       C  
ATOM   1805  O   SER A 301      25.950  20.652 -18.172  1.00160.36           O  
ANISOU 1805  O   SER A 301    22290  19196  19442   -515   1125    341       O  
ATOM   1806  CB  SER A 301      28.438  21.770 -18.169  1.00162.78           C  
ANISOU 1806  CB  SER A 301    22607  19350  19890   -517   1254    340       C  
ATOM   1807  OG  SER A 301      28.809  20.400 -18.046  1.00164.42           O  
ANISOU 1807  OG  SER A 301    22779  19545  20147   -553   1288    293       O  
ATOM   1808  N   SER A 305      27.046  14.564 -20.307  1.00 94.84           N  
ANISOU 1808  N   SER A 305    13996  10854  11186   -758   1356    118       N  
ATOM   1809  CA  SER A 305      27.774  13.317 -20.511  1.00 94.69           C  
ANISOU 1809  CA  SER A 305    13961  10788  11229   -803   1426     64       C  
ATOM   1810  C   SER A 305      27.269  12.207 -19.581  1.00103.35           C  
ANISOU 1810  C   SER A 305    14995  11902  12372   -801   1385     48       C  
ATOM   1811  O   SER A 305      26.267  12.380 -18.882  1.00101.59           O  
ANISOU 1811  O   SER A 305    14745  11734  12120   -771   1306     76       O  
ATOM   1812  CB  SER A 305      29.279  13.545 -20.324  1.00 91.81           C  
ANISOU 1812  CB  SER A 305    13578  10332  10972   -801   1500     51       C  
ATOM   1813  OG  SER A 305      29.607  13.814 -18.971  1.00 90.65           O  
ANISOU 1813  OG  SER A 305    13363  10159  10921   -752   1459     72       O  
ATOM   1814  N   THR A 306      27.959  11.063 -19.589  1.00164.34           N  
ANISOU 1814  N   THR A 306    22697  19575  20170   -835   1442      2       N  
ATOM   1815  CA  THR A 306      27.463   9.893 -18.871  1.00159.15           C  
ANISOU 1815  CA  THR A 306    21992  18929  19547   -842   1412    -15       C  
ATOM   1816  C   THR A 306      27.890   9.907 -17.406  1.00157.24           C  
ANISOU 1816  C   THR A 306    21685  18650  19409   -797   1378      7       C  
ATOM   1817  O   THR A 306      27.069   9.677 -16.511  1.00158.93           O  
ANISOU 1817  O   THR A 306    21866  18902  19618   -776   1313     27       O  
ATOM   1818  CB  THR A 306      27.941   8.612 -19.557  1.00159.28           C  
ANISOU 1818  CB  THR A 306    22018  18908  19594   -898   1485    -75       C  
ATOM   1819  N   ALA A 307      29.175  10.158 -17.144  1.00135.52           N  
ANISOU 1819  N   ALA A 307    18914  15823  16753   -782   1421      1       N  
ATOM   1820  CA  ALA A 307      29.652  10.183 -15.765  1.00138.37           C  
ANISOU 1820  CA  ALA A 307    19216  16146  17213   -737   1385     19       C  
ATOM   1821  C   ALA A 307      29.181  11.430 -15.023  1.00134.69           C  
ANISOU 1821  C   ALA A 307    18740  15718  16718   -685   1316     72       C  
ATOM   1822  O   ALA A 307      29.022  11.396 -13.797  1.00131.88           O  
ANISOU 1822  O   ALA A 307    18340  15363  16403   -648   1261     94       O  
ATOM   1823  CB  ALA A 307      31.177  10.086 -15.734  1.00137.27           C  
ANISOU 1823  CB  ALA A 307    19054  15914  17189   -736   1448     -9       C  
ATOM   1824  N   ALA A 308      28.966  12.537 -15.737  1.00130.05           N  
ANISOU 1824  N   ALA A 308    18194  15159  16059   -680   1318     92       N  
ATOM   1825  CA  ALA A 308      28.465  13.744 -15.087  1.00128.06           C  
ANISOU 1825  CA  ALA A 308    17935  14943  15779   -629   1252    140       C  
ATOM   1826  C   ALA A 308      27.018  13.569 -14.645  1.00127.32           C  
ANISOU 1826  C   ALA A 308    17831  14930  15614   -619   1177    160       C  
ATOM   1827  O   ALA A 308      26.640  14.011 -13.554  1.00126.53           O  
ANISOU 1827  O   ALA A 308    17695  14850  15530   -577   1117    190       O  
ATOM   1828  CB  ALA A 308      28.604  14.947 -16.020  1.00132.03           C  
ANISOU 1828  CB  ALA A 308    18491  15450  16225   -628   1276    158       C  
ATOM   1829  N   LEU A 309      26.195  12.925 -15.476  1.00118.10           N  
ANISOU 1829  N   LEU A 309    16694  13810  14369   -658   1181    141       N  
ATOM   1830  CA  LEU A 309      24.810  12.658 -15.101  1.00120.29           C  
ANISOU 1830  CA  LEU A 309    16956  14164  14586   -654   1115    152       C  
ATOM   1831  C   LEU A 309      24.717  11.725 -13.897  1.00117.88           C  
ANISOU 1831  C   LEU A 309    16598  13846  14346   -650   1094    146       C  
ATOM   1832  O   LEU A 309      23.682  11.699 -13.220  1.00112.88           O  
ANISOU 1832  O   LEU A 309    15939  13266  13682   -635   1036    162       O  
ATOM   1833  CB  LEU A 309      24.051  12.081 -16.303  1.00118.19           C  
ANISOU 1833  CB  LEU A 309    16732  13946  14231   -702   1127    124       C  
ATOM   1834  CG  LEU A 309      22.544  11.834 -16.181  1.00116.44           C  
ANISOU 1834  CG  LEU A 309    16497  13808  13938   -705   1062    125       C  
ATOM   1835  CD1 LEU A 309      21.766  13.130 -16.312  1.00111.07           C  
ANISOU 1835  CD1 LEU A 309    15832  13184  13185   -666   1002    162       C  
ATOM   1836  CD2 LEU A 309      22.082  10.837 -17.225  1.00118.81           C  
ANISOU 1836  CD2 LEU A 309    16826  14135  14183   -763   1088     81       C  
ATOM   1837  N   SER A 310      25.778  10.969 -13.610  1.00153.90           N  
ANISOU 1837  N   SER A 310    21142  18335  18998   -661   1139    124       N  
ATOM   1838  CA  SER A 310      25.805  10.129 -12.418  1.00153.62           C  
ANISOU 1838  CA  SER A 310    21063  18278  19028   -652   1118    125       C  
ATOM   1839  C   SER A 310      26.193  10.933 -11.180  1.00154.18           C  
ANISOU 1839  C   SER A 310    21100  18329  19151   -596   1075    161       C  
ATOM   1840  O   SER A 310      25.553  10.809 -10.129  1.00153.98           O  
ANISOU 1840  O   SER A 310    21049  18333  19124   -576   1024    181       O  
ATOM   1841  CB  SER A 310      26.766   8.959 -12.627  1.00157.29           C  
ANISOU 1841  CB  SER A 310    21523  18670  19571   -684   1178     87       C  
ATOM   1842  OG  SER A 310      26.079   7.823 -13.119  1.00155.85           O  
ANISOU 1842  OG  SER A 310    21351  18511  19353   -732   1194     57       O  
ATOM   1843  N   SER A 311      27.247  11.756 -11.285  1.00126.68           N  
ANISOU 1843  N   SER A 311    17620  14799  15716   -573   1098    166       N  
ATOM   1844  CA  SER A 311      27.620  12.643 -10.183  1.00123.32           C  
ANISOU 1844  CA  SER A 311    17164  14357  15336   -519   1056    196       C  
ATOM   1845  C   SER A 311      26.449  13.525  -9.778  1.00119.01           C  
ANISOU 1845  C   SER A 311    16617  13887  14715   -491    993    230       C  
ATOM   1846  O   SER A 311      26.241  13.797  -8.591  1.00118.62           O  
ANISOU 1846  O   SER A 311    16537  13847  14685   -455    944    252       O  
ATOM   1847  CB  SER A 311      28.815  13.519 -10.577  1.00121.49           C  
ANISOU 1847  CB  SER A 311    16937  14069  15155   -505   1096    191       C  
ATOM   1848  OG  SER A 311      29.900  12.755 -11.069  1.00126.57           O  
ANISOU 1848  OG  SER A 311    17579  14643  15870   -534   1161    153       O  
ATOM   1849  N   TYR A 312      25.678  13.983 -10.764  1.00 98.14           N  
ANISOU 1849  N   TYR A 312    14008  11296  11985   -506    993    233       N  
ATOM   1850  CA  TYR A 312      24.509  14.810 -10.491  1.00100.25           C  
ANISOU 1850  CA  TYR A 312    14273  11636  12182   -478    932    260       C  
ATOM   1851  C   TYR A 312      23.457  14.032  -9.708  1.00 98.09           C  
ANISOU 1851  C   TYR A 312    13971  11410  11888   -485    891    259       C  
ATOM   1852  O   TYR A 312      22.859  14.559  -8.760  1.00 95.93           O  
ANISOU 1852  O   TYR A 312    13672  11172  11607   -451    840    282       O  
ATOM   1853  CB  TYR A 312      23.967  15.345 -11.821  1.00 98.60           C  
ANISOU 1853  CB  TYR A 312    14111  11467  11886   -494    939    261       C  
ATOM   1854  CG  TYR A 312      22.525  15.793 -11.859  1.00 93.77           C  
ANISOU 1854  CG  TYR A 312    13499  10940  11191   -481    878    276       C  
ATOM   1855  CD1 TYR A 312      21.495  14.881 -12.030  1.00 94.07           C  
ANISOU 1855  CD1 TYR A 312    13530  11030  11182   -512    862    256       C  
ATOM   1856  CD2 TYR A 312      22.198  17.136 -11.754  1.00 93.02           C  
ANISOU 1856  CD2 TYR A 312    13408  10867  11067   -437    838    307       C  
ATOM   1857  CE1 TYR A 312      20.184  15.290 -12.084  1.00 93.92           C  
ANISOU 1857  CE1 TYR A 312    13504  11088  11094   -500    805    264       C  
ATOM   1858  CE2 TYR A 312      20.885  17.555 -11.803  1.00 94.99           C  
ANISOU 1858  CE2 TYR A 312    13653  11192  11246   -421    780    318       C  
ATOM   1859  CZ  TYR A 312      19.881  16.625 -11.967  1.00 93.39           C  
ANISOU 1859  CZ  TYR A 312    13438  11043  11001   -452    763    295       C  
ATOM   1860  OH  TYR A 312      18.566  17.029 -12.019  1.00 93.39           O  
ANISOU 1860  OH  TYR A 312    13427  11118  10940   -437    704    299       O  
ATOM   1861  N   TYR A 313      23.227  12.770 -10.078  1.00 87.40           N  
ANISOU 1861  N   TYR A 313    12622  10058  10527   -531    918    231       N  
ATOM   1862  CA  TYR A 313      22.223  11.976  -9.377  1.00 87.33           C  
ANISOU 1862  CA  TYR A 313    12588  10091  10500   -544    887    228       C  
ATOM   1863  C   TYR A 313      22.719  11.529  -8.009  1.00 87.05           C  
ANISOU 1863  C   TYR A 313    12523  10013  10537   -525    877    240       C  
ATOM   1864  O   TYR A 313      21.911  11.266  -7.110  1.00 86.92           O  
ANISOU 1864  O   TYR A 313    12486  10033  10507   -521    842    250       O  
ATOM   1865  CB  TYR A 313      21.813  10.779 -10.231  1.00 87.69           C  
ANISOU 1865  CB  TYR A 313    12651  10149  10518   -602    920    192       C  
ATOM   1866  CG  TYR A 313      20.595  11.087 -11.056  1.00 87.94           C  
ANISOU 1866  CG  TYR A 313    12697  10261  10458   -616    894    184       C  
ATOM   1867  CD1 TYR A 313      19.319  10.952 -10.526  1.00 87.92           C  
ANISOU 1867  CD1 TYR A 313    12666  10323  10416   -617    849    185       C  
ATOM   1868  CD2 TYR A 313      20.723  11.555 -12.356  1.00 88.27           C  
ANISOU 1868  CD2 TYR A 313    12778  10310  10448   -628    913    175       C  
ATOM   1869  CE1 TYR A 313      18.206  11.257 -11.274  1.00 88.21           C  
ANISOU 1869  CE1 TYR A 313    12709  10432  10374   -626    819    174       C  
ATOM   1870  CE2 TYR A 313      19.619  11.862 -13.112  1.00 88.56           C  
ANISOU 1870  CE2 TYR A 313    12831  10420  10399   -636    880    169       C  
ATOM   1871  CZ  TYR A 313      18.362  11.712 -12.567  1.00 88.53           C  
ANISOU 1871  CZ  TYR A 313    12792  10481  10365   -634    830    167       C  
ATOM   1872  OH  TYR A 313      17.259  12.024 -13.319  1.00 88.88           O  
ANISOU 1872  OH  TYR A 313    12846  10597  10329   -639    792    157       O  
ATOM   1873  N   PHE A 314      24.038  11.426  -7.836  1.00120.09           N  
ANISOU 1873  N   PHE A 314    16707  14122  14800   -514    906    237       N  
ATOM   1874  CA  PHE A 314      24.592  11.249  -6.501  1.00117.31           C  
ANISOU 1874  CA  PHE A 314    16329  13728  14514   -485    883    254       C  
ATOM   1875  C   PHE A 314      24.249  12.445  -5.621  1.00122.01           C  
ANISOU 1875  C   PHE A 314    16907  14357  15092   -435    830    284       C  
ATOM   1876  O   PHE A 314      23.845  12.284  -4.462  1.00121.14           O  
ANISOU 1876  O   PHE A 314    16780  14263  14986   -419    794    300       O  
ATOM   1877  CB  PHE A 314      26.107  11.060  -6.598  1.00115.65           C  
ANISOU 1877  CB  PHE A 314    16116  13430  14394   -478    920    240       C  
ATOM   1878  CG  PHE A 314      26.800  10.947  -5.271  1.00119.97           C  
ANISOU 1878  CG  PHE A 314    16638  13930  15014   -442    890    256       C  
ATOM   1879  CD1 PHE A 314      26.200  10.291  -4.204  1.00120.63           C  
ANISOU 1879  CD1 PHE A 314    16714  14030  15089   -440    855    271       C  
ATOM   1880  CD2 PHE A 314      28.051  11.516  -5.083  1.00122.86           C  
ANISOU 1880  CD2 PHE A 314    16990  14236  15455   -411    896    253       C  
ATOM   1881  CE1 PHE A 314      26.843  10.189  -2.981  1.00120.94           C  
ANISOU 1881  CE1 PHE A 314    16738  14026  15187   -405    823    287       C  
ATOM   1882  CE2 PHE A 314      28.700  11.423  -3.861  1.00124.47           C  
ANISOU 1882  CE2 PHE A 314    17171  14398  15724   -375    860    265       C  
ATOM   1883  CZ  PHE A 314      28.094  10.759  -2.807  1.00123.66           C  
ANISOU 1883  CZ  PHE A 314    17068  14313  15606   -371    822    284       C  
ATOM   1884  N   CYS A 315      24.383  13.657  -6.171  1.00107.90           N  
ANISOU 1884  N   CYS A 315    15129  12583  13286   -413    827    292       N  
ATOM   1885  CA  CYS A 315      24.108  14.873  -5.413  1.00105.81           C  
ANISOU 1885  CA  CYS A 315    14848  12345  13010   -365    779    318       C  
ATOM   1886  C   CYS A 315      22.622  15.035  -5.120  1.00105.74           C  
ANISOU 1886  C   CYS A 315    14831  12418  12928   -364    738    328       C  
ATOM   1887  O   CYS A 315      22.255  15.612  -4.088  1.00104.94           O  
ANISOU 1887  O   CYS A 315    14708  12341  12825   -330    697    345       O  
ATOM   1888  CB  CYS A 315      24.637  16.087  -6.174  1.00104.29           C  
ANISOU 1888  CB  CYS A 315    14672  12138  12817   -345    792    324       C  
ATOM   1889  SG  CYS A 315      26.436  16.162  -6.250  1.00102.73           S  
ANISOU 1889  SG  CYS A 315    14471  11841  12720   -338    837    311       S  
ATOM   1890  N   ILE A 316      21.758  14.549  -6.017  1.00 99.98           N  
ANISOU 1890  N   ILE A 316    14115  11733  12139   -401    749    312       N  
ATOM   1891  CA  ILE A 316      20.322  14.572  -5.756  1.00100.08           C  
ANISOU 1891  CA  ILE A 316    14112  11824  12091   -404    712    313       C  
ATOM   1892  C   ILE A 316      20.006  13.737  -4.524  1.00101.55           C  
ANISOU 1892  C   ILE A 316    14276  12012  12297   -412    702    314       C  
ATOM   1893  O   ILE A 316      19.222  14.144  -3.656  1.00102.14           O  
ANISOU 1893  O   ILE A 316    14328  12131  12351   -391    666    325       O  
ATOM   1894  CB  ILE A 316      19.547  14.062  -6.983  1.00 98.59           C  
ANISOU 1894  CB  ILE A 316    13941  11678  11842   -447    727    289       C  
ATOM   1895  CG1 ILE A 316      19.503  15.125  -8.076  1.00 98.67           C  
ANISOU 1895  CG1 ILE A 316    13976  11705  11808   -431    720    296       C  
ATOM   1896  CG2 ILE A 316      18.127  13.696  -6.584  1.00 96.36           C  
ANISOU 1896  CG2 ILE A 316    13632  11466  11514   -461    696    280       C  
ATOM   1897  CD1 ILE A 316      18.520  14.815  -9.177  1.00 98.69           C  
ANISOU 1897  CD1 ILE A 316    13995  11765  11738   -463    714    275       C  
ATOM   1898  N   ALA A 317      20.622  12.555  -4.427  1.00 97.38           N  
ANISOU 1898  N   ALA A 317    13756  11433  11812   -442    735    303       N  
ATOM   1899  CA  ALA A 317      20.421  11.689  -3.271  1.00 94.65           C  
ANISOU 1899  CA  ALA A 317    13399  11078  11486   -451    728    309       C  
ATOM   1900  C   ALA A 317      20.866  12.369  -1.986  1.00 95.96           C  
ANISOU 1900  C   ALA A 317    13551  11225  11682   -403    695    335       C  
ATOM   1901  O   ALA A 317      20.217  12.225  -0.944  1.00 97.52           O  
ANISOU 1901  O   ALA A 317    13739  11451  11864   -399    672    346       O  
ATOM   1902  CB  ALA A 317      21.177  10.379  -3.464  1.00 97.75           C  
ANISOU 1902  CB  ALA A 317    13806  11406  11927   -485    769    295       C  
ATOM   1903  N   LEU A 318      21.977  13.107  -2.038  1.00 87.10           N  
ANISOU 1903  N   LEU A 318    12431  10056  10606   -369    693    343       N  
ATOM   1904  CA  LEU A 318      22.446  13.812  -0.849  1.00 85.72           C  
ANISOU 1904  CA  LEU A 318    12244   9864  10462   -322    658    363       C  
ATOM   1905  C   LEU A 318      21.382  14.771  -0.330  1.00 86.77           C  
ANISOU 1905  C   LEU A 318    12361  10067  10542   -298    620    373       C  
ATOM   1906  O   LEU A 318      21.149  14.849   0.882  1.00 85.53           O  
ANISOU 1906  O   LEU A 318    12194   9921  10384   -279    592    386       O  
ATOM   1907  CB  LEU A 318      23.748  14.553  -1.154  1.00 85.64           C  
ANISOU 1907  CB  LEU A 318    12233   9796  10510   -293    665    363       C  
ATOM   1908  CG  LEU A 318      24.943  13.720  -1.626  1.00 85.79           C  
ANISOU 1908  CG  LEU A 318    12261   9739  10596   -311    704    348       C  
ATOM   1909  CD1 LEU A 318      26.240  14.363  -1.189  1.00 85.75           C  
ANISOU 1909  CD1 LEU A 318    12243   9673  10666   -272    695    349       C  
ATOM   1910  CD2 LEU A 318      24.866  12.315  -1.069  1.00 87.53           C  
ANISOU 1910  CD2 LEU A 318    12487   9938  10832   -337    709    346       C  
ATOM   1911  N   GLY A 319      20.710  15.493  -1.231  1.00104.50           N  
ANISOU 1911  N   GLY A 319    14604  12360  12743   -298    618    368       N  
ATOM   1912  CA  GLY A 319      19.567  16.288  -0.811  1.00104.83           C  
ANISOU 1912  CA  GLY A 319    14625  12470  12735   -277    582    372       C  
ATOM   1913  C   GLY A 319      18.461  15.434  -0.222  1.00105.85           C  
ANISOU 1913  C   GLY A 319    14743  12646  12830   -308    580    364       C  
ATOM   1914  O   GLY A 319      17.814  15.821   0.755  1.00106.69           O  
ANISOU 1914  O   GLY A 319    14831  12789  12919   -290    554    369       O  
ATOM   1915  N   TYR A 320      18.227  14.261  -0.815  1.00 90.46           N  
ANISOU 1915  N   TYR A 320    12805  10695  10872   -356    610    348       N  
ATOM   1916  CA  TYR A 320      17.236  13.326  -0.289  1.00 88.35           C  
ANISOU 1916  CA  TYR A 320    12528  10463  10578   -393    617    338       C  
ATOM   1917  C   TYR A 320      17.633  12.811   1.086  1.00 89.41           C  
ANISOU 1917  C   TYR A 320    12669  10562  10740   -388    615    356       C  
ATOM   1918  O   TYR A 320      16.766  12.468   1.899  1.00 90.36           O  
ANISOU 1918  O   TYR A 320    12781  10718  10834   -403    612    355       O  
ATOM   1919  CB  TYR A 320      17.072  12.154  -1.252  1.00 86.38           C  
ANISOU 1919  CB  TYR A 320    12292  10207  10321   -447    653    316       C  
ATOM   1920  CG  TYR A 320      16.019  12.336  -2.315  1.00 86.60           C  
ANISOU 1920  CG  TYR A 320    12308  10300  10297   -467    648    292       C  
ATOM   1921  CD1 TYR A 320      14.673  12.314  -1.989  1.00 86.78           C  
ANISOU 1921  CD1 TYR A 320    12302  10392  10280   -481    632    277       C  
ATOM   1922  CD2 TYR A 320      16.369  12.495  -3.652  1.00 86.70           C  
ANISOU 1922  CD2 TYR A 320    12338  10304  10299   -475    660    281       C  
ATOM   1923  CE1 TYR A 320      13.704  12.461  -2.954  1.00 87.05           C  
ANISOU 1923  CE1 TYR A 320    12320  10485  10270   -497    621    251       C  
ATOM   1924  CE2 TYR A 320      15.403  12.643  -4.625  1.00 86.97           C  
ANISOU 1924  CE2 TYR A 320    12366  10398  10281   -492    649    259       C  
ATOM   1925  CZ  TYR A 320      14.071  12.623  -4.265  1.00 87.15           C  
ANISOU 1925  CZ  TYR A 320    12354  10489  10268   -501    626    244       C  
ATOM   1926  OH  TYR A 320      13.089  12.768  -5.213  1.00 90.57           O  
ANISOU 1926  OH  TYR A 320    12776  10983  10653   -514    606    219       O  
ATOM   1927  N   THR A 321      18.939  12.728   1.350  1.00100.11           N  
ANISOU 1927  N   THR A 321    14041  11846  12148   -368    617    370       N  
ATOM   1928  CA  THR A 321      19.419  12.215   2.627  1.00100.94           C  
ANISOU 1928  CA  THR A 321    14160  11912  12281   -359    608    389       C  
ATOM   1929  C   THR A 321      18.967  13.091   3.788  1.00104.37           C  
ANISOU 1929  C   THR A 321    14581  12383  12690   -325    573    402       C  
ATOM   1930  O   THR A 321      18.594  12.578   4.850  1.00105.06           O  
ANISOU 1930  O   THR A 321    14679  12477  12762   -335    569    412       O  
ATOM   1931  CB  THR A 321      20.940  12.108   2.602  1.00100.09           C  
ANISOU 1931  CB  THR A 321    14066  11723  12242   -337    609    397       C  
ATOM   1932  OG1 THR A 321      21.346  11.450   1.399  1.00 97.91           O  
ANISOU 1932  OG1 THR A 321    13798  11415  11987   -368    646    380       O  
ATOM   1933  CG2 THR A 321      21.434  11.315   3.793  1.00103.43           C  
ANISOU 1933  CG2 THR A 321    14508  12099  12692   -334    598    416       C  
ATOM   1934  N   ASN A 322      19.004  14.413   3.612  1.00100.94           N  
ANISOU 1934  N   ASN A 322    14128  11971  12252   -285    549    401       N  
ATOM   1935  CA  ASN A 322      18.611  15.305   4.696  1.00102.50           C  
ANISOU 1935  CA  ASN A 322    14312  12202  12430   -250    516    408       C  
ATOM   1936  C   ASN A 322      17.219  14.954   5.203  1.00105.09           C  
ANISOU 1936  C   ASN A 322    14630  12595  12706   -279    523    399       C  
ATOM   1937  O   ASN A 322      16.965  14.967   6.412  1.00105.07           O  
ANISOU 1937  O   ASN A 322    14631  12603  12687   -271    512    407       O  
ATOM   1938  CB  ASN A 322      18.699  16.761   4.224  1.00103.12           C  
ANISOU 1938  CB  ASN A 322    14371  12299  12512   -209    495    404       C  
ATOM   1939  CG  ASN A 322      18.075  17.747   5.201  1.00103.93           C  
ANISOU 1939  CG  ASN A 322    14453  12446  12591   -176    464    404       C  
ATOM   1940  OD1 ASN A 322      16.861  17.958   5.205  1.00101.84           O  
ANISOU 1940  OD1 ASN A 322    14168  12244  12283   -185    463    392       O  
ATOM   1941  ND2 ASN A 322      18.909  18.338   6.055  1.00100.55           N  
ANISOU 1941  ND2 ASN A 322    14029  11984  12193   -138    440    414       N  
ATOM   1942  N   SER A 323      16.319  14.575   4.297  1.00121.61           N  
ANISOU 1942  N   SER A 323    16708  14728  14769   -314    543    380       N  
ATOM   1943  CA  SER A 323      14.982  14.186   4.717  1.00120.09           C  
ANISOU 1943  CA  SER A 323    16499  14595  14534   -346    554    365       C  
ATOM   1944  C   SER A 323      14.945  12.814   5.377  1.00122.66           C  
ANISOU 1944  C   SER A 323    16851  14894  14859   -390    583    372       C  
ATOM   1945  O   SER A 323      14.018  12.540   6.146  1.00126.23           O  
ANISOU 1945  O   SER A 323    17297  15385  15280   -412    594    365       O  
ATOM   1946  CB  SER A 323      14.039  14.221   3.524  1.00120.53           C  
ANISOU 1946  CB  SER A 323    16529  14704  14564   -369    560    338       C  
ATOM   1947  OG  SER A 323      13.939  15.538   3.008  1.00126.48           O  
ANISOU 1947  OG  SER A 323    17262  15484  15312   -326    530    335       O  
ATOM   1948  N   CYS A 324      15.917  11.944   5.103  1.00144.75           N  
ANISOU 1948  N   CYS A 324    19680  17626  17693   -404    599    384       N  
ATOM   1949  CA  CYS A 324      15.966  10.657   5.789  1.00147.38           C  
ANISOU 1949  CA  CYS A 324    20044  17924  18029   -441    623    396       C  
ATOM   1950  C   CYS A 324      16.740  10.733   7.094  1.00146.25           C  
ANISOU 1950  C   CYS A 324    19930  17737  17899   -409    600    426       C  
ATOM   1951  O   CYS A 324      16.418  10.012   8.048  1.00148.00           O  
ANISOU 1951  O   CYS A 324    20178  17953  18101   -432    612    439       O  
ATOM   1952  CB  CYS A 324      16.602   9.584   4.898  1.00149.18           C  
ANISOU 1952  CB  CYS A 324    20292  18098  18293   -472    651    392       C  
ATOM   1953  SG  CYS A 324      18.407   9.505   4.935  1.00152.60           S  
ANISOU 1953  SG  CYS A 324    20751  18435  18795   -434    635    414       S  
ATOM   1954  N   LEU A 325      17.765  11.586   7.144  1.00 90.48           N  
ANISOU 1954  N   LEU A 325    12865  10643  10869   -358    567    436       N  
ATOM   1955  CA  LEU A 325      18.562  11.755   8.350  1.00 88.52           C  
ANISOU 1955  CA  LEU A 325    12643  10356  10637   -323    537    461       C  
ATOM   1956  C   LEU A 325      17.844  12.586   9.398  1.00 90.22           C  
ANISOU 1956  C   LEU A 325    12848  10624  10805   -304    517    461       C  
ATOM   1957  O   LEU A 325      18.186  12.501  10.582  1.00 91.24           O  
ANISOU 1957  O   LEU A 325    13007  10732  10927   -288    498    481       O  
ATOM   1958  CB  LEU A 325      19.892  12.421   8.002  1.00 88.78           C  
ANISOU 1958  CB  LEU A 325    12668  10337  10726   -277    510    464       C  
ATOM   1959  CG  LEU A 325      21.009  11.482   7.561  1.00 86.86           C  
ANISOU 1959  CG  LEU A 325    12444  10016  10542   -285    520    470       C  
ATOM   1960  CD1 LEU A 325      22.381  12.096   7.811  1.00 86.76           C  
ANISOU 1960  CD1 LEU A 325    12428   9947  10589   -235    485    476       C  
ATOM   1961  CD2 LEU A 325      20.875  10.123   8.231  1.00 92.72           C  
ANISOU 1961  CD2 LEU A 325    13225  10728  11277   -318    533    488       C  
ATOM   1962  N   ASN A 326      16.871  13.396   8.984  1.00114.89           N  
ANISOU 1962  N   ASN A 326    15935  13817  13901   -303    521    439       N  
ATOM   1963  CA  ASN A 326      16.217  14.310   9.917  1.00118.72           C  
ANISOU 1963  CA  ASN A 326    16406  14352  14349   -281    504    433       C  
ATOM   1964  C   ASN A 326      15.554  13.602  11.089  1.00116.85           C  
ANISOU 1964  C   ASN A 326    16197  14132  14070   -312    523    441       C  
ATOM   1965  O   ASN A 326      15.771  14.031  12.235  1.00118.91           O  
ANISOU 1965  O   ASN A 326    16476  14390  14314   -286    501    452       O  
ATOM   1966  CB  ASN A 326      15.215  15.195   9.168  1.00120.31           C  
ANISOU 1966  CB  ASN A 326    16559  14622  14533   -276    505    405       C  
ATOM   1967  CG  ASN A 326      15.819  16.520   8.730  1.00118.07           C  
ANISOU 1967  CG  ASN A 326    16254  14332  14277   -223    472    403       C  
ATOM   1968  OD1 ASN A 326      15.104  17.421   8.298  1.00117.19           O  
ANISOU 1968  OD1 ASN A 326    16106  14268  14151   -207    463    385       O  
ATOM   1969  ND2 ASN A 326      17.140  16.639   8.834  1.00117.63           N  
ANISOU 1969  ND2 ASN A 326    16219  14213  14264   -194    453    420       N  
ATOM   1970  N   PRO A 327      14.752  12.547  10.904  1.00 91.43           N  
ANISOU 1970  N   PRO A 327    12983  10926  10828   -368    564    435       N  
ATOM   1971  CA  PRO A 327      14.136  11.909  12.080  1.00 92.94           C  
ANISOU 1971  CA  PRO A 327    13207  11129  10977   -400    588    444       C  
ATOM   1972  C   PRO A 327      15.156  11.436  13.088  1.00 91.78           C  
ANISOU 1972  C   PRO A 327    13119  10917  10834   -384    568    481       C  
ATOM   1973  O   PRO A 327      14.906  11.515  14.295  1.00 91.37           O  
ANISOU 1973  O   PRO A 327    13097  10877  10742   -383    566    492       O  
ATOM   1974  CB  PRO A 327      13.358  10.727  11.485  1.00 92.97           C  
ANISOU 1974  CB  PRO A 327    13210  11141  10974   -464    637    432       C  
ATOM   1975  CG  PRO A 327      13.930  10.532  10.132  1.00 95.68           C  
ANISOU 1975  CG  PRO A 327    13537  11456  11360   -462    633    425       C  
ATOM   1976  CD  PRO A 327      14.331  11.887   9.659  1.00 93.38           C  
ANISOU 1976  CD  PRO A 327    13212  11182  11087   -407    593    417       C  
ATOM   1977  N   ILE A 328      16.311  10.956  12.628  1.00101.75           N  
ANISOU 1977  N   ILE A 328    14402  12112  12147   -370    551    500       N  
ATOM   1978  CA  ILE A 328      17.349  10.522  13.555  1.00104.08           C  
ANISOU 1978  CA  ILE A 328    14751  12342  12454   -348    521    534       C  
ATOM   1979  C   ILE A 328      17.832  11.700  14.383  1.00102.92           C  
ANISOU 1979  C   ILE A 328    14601  12204  12300   -293    473    537       C  
ATOM   1980  O   ILE A 328      18.018  11.592  15.600  1.00105.54           O  
ANISOU 1980  O   ILE A 328    14977  12522  12600   -283    454    558       O  
ATOM   1981  CB  ILE A 328      18.506   9.855  12.791  1.00104.25           C  
ANISOU 1981  CB  ILE A 328    14782  12287  12541   -341    512    545       C  
ATOM   1982  CG1 ILE A 328      17.985   8.685  11.946  1.00102.70           C  
ANISOU 1982  CG1 ILE A 328    14587  12083  12351   -399    562    538       C  
ATOM   1983  CG2 ILE A 328      19.577   9.393  13.765  1.00105.35           C  
ANISOU 1983  CG2 ILE A 328    14973  12357  12698   -314    474    580       C  
ATOM   1984  CD1 ILE A 328      19.072   7.753  11.443  1.00 99.34           C  
ANISOU 1984  CD1 ILE A 328    14184  11575  11987   -399    560    551       C  
ATOM   1985  N   LEU A 329      18.024  12.849  13.736  1.00110.06           N  
ANISOU 1985  N   LEU A 329    15457  13130  13231   -257    454    515       N  
ATOM   1986  CA  LEU A 329      18.532  14.030  14.424  1.00109.54           C  
ANISOU 1986  CA  LEU A 329    15383  13070  13168   -204    408    512       C  
ATOM   1987  C   LEU A 329      17.461  14.680  15.292  1.00108.94           C  
ANISOU 1987  C   LEU A 329    15300  13061  13030   -207    416    498       C  
ATOM   1988  O   LEU A 329      17.707  15.012  16.457  1.00111.39           O  
ANISOU 1988  O   LEU A 329    15639  13370  13314   -184    390    507       O  
ATOM   1989  CB  LEU A 329      19.051  15.034  13.399  1.00110.88           C  
ANISOU 1989  CB  LEU A 329    15505  13237  13389   -169    392    493       C  
ATOM   1990  CG  LEU A 329      20.423  14.736  12.810  1.00114.18           C  
ANISOU 1990  CG  LEU A 329    15927  13580  13876   -150    373    503       C  
ATOM   1991  CD1 LEU A 329      21.034  16.022  12.273  1.00110.08           C  
ANISOU 1991  CD1 LEU A 329    15369  13057  13399   -105    350    486       C  
ATOM   1992  CD2 LEU A 329      21.318  14.073  13.853  1.00109.39           C  
ANISOU 1992  CD2 LEU A 329    15368  12915  13280   -136    341    529       C  
ATOM   1993  N   TYR A 330      16.272  14.891  14.734  1.00 97.44           N  
ANISOU 1993  N   TYR A 330    13806  11667  11551   -234    452    473       N  
ATOM   1994  CA  TYR A 330      15.247  15.679  15.407  1.00 98.49           C  
ANISOU 1994  CA  TYR A 330    13918  11867  11638   -232    461    450       C  
ATOM   1995  C   TYR A 330      14.247  14.860  16.204  1.00 98.39           C  
ANISOU 1995  C   TYR A 330    13933  11883  11568   -283    504    451       C  
ATOM   1996  O   TYR A 330      13.391  15.446  16.877  1.00 93.66           O  
ANISOU 1996  O   TYR A 330    13320  11339  10929   -286    518    429       O  
ATOM   1997  CB  TYR A 330      14.498  16.557  14.403  1.00 99.60           C  
ANISOU 1997  CB  TYR A 330    13992  12060  11791   -224    467    417       C  
ATOM   1998  CG  TYR A 330      15.309  17.742  13.943  1.00101.96           C  
ANISOU 1998  CG  TYR A 330    14265  12342  12134   -167    426    413       C  
ATOM   1999  CD1 TYR A 330      16.495  17.586  13.237  1.00101.52           C  
ANISOU 1999  CD1 TYR A 330    14218  12225  12129   -150    406    429       C  
ATOM   2000  CD2 TYR A 330      14.925  19.021  14.306  1.00 99.91           C  
ANISOU 2000  CD2 TYR A 330    13972  12122  11866   -132    408    390       C  
ATOM   2001  CE1 TYR A 330      17.236  18.679  12.853  1.00 99.94           C  
ANISOU 2001  CE1 TYR A 330    13995  12006  11970   -102    375    424       C  
ATOM   2002  CE2 TYR A 330      15.650  20.107  13.937  1.00 98.84           C  
ANISOU 2002  CE2 TYR A 330    13817  11968  11772    -82    373    387       C  
ATOM   2003  CZ  TYR A 330      16.805  19.938  13.213  1.00 99.13           C  
ANISOU 2003  CZ  TYR A 330    13863  11944  11857    -69    358    404       C  
ATOM   2004  OH  TYR A 330      17.515  21.055  12.857  1.00 99.93           O  
ANISOU 2004  OH  TYR A 330    13943  12024  12000    -23    329    398       O  
ATOM   2005  N   ALA A 331      14.309  13.535  16.131  1.00138.28           N  
ANISOU 2005  N   ALA A 331    19024  16899  16616   -326    531    473       N  
ATOM   2006  CA  ALA A 331      13.511  12.701  17.016  1.00141.29           C  
ANISOU 2006  CA  ALA A 331    19446  17296  16942   -377    575    480       C  
ATOM   2007  C   ALA A 331      14.379  11.795  17.877  1.00140.90           C  
ANISOU 2007  C   ALA A 331    19476  17178  16880   -379    560    525       C  
ATOM   2008  O   ALA A 331      14.284  11.854  19.107  1.00142.97           O  
ANISOU 2008  O   ALA A 331    19785  17447  17092   -378    558    537       O  
ATOM   2009  CB  ALA A 331      12.498  11.897  16.192  1.00141.92           C  
ANISOU 2009  CB  ALA A 331    19499  17402  17022   -436    630    460       C  
ATOM   2010  N   PHE A 332      15.250  10.986  17.274  1.00141.76           N  
ANISOU 2010  N   PHE A 332    19605  17222  17034   -379    548    548       N  
ATOM   2011  CA  PHE A 332      16.007  10.014  18.053  1.00143.94           C  
ANISOU 2011  CA  PHE A 332    19958  17430  17302   -383    534    592       C  
ATOM   2012  C   PHE A 332      17.018  10.678  18.980  1.00142.70           C  
ANISOU 2012  C   PHE A 332    19831  17247  17143   -324    469    610       C  
ATOM   2013  O   PHE A 332      17.476  10.040  19.937  1.00144.40           O  
ANISOU 2013  O   PHE A 332    20117  17418  17331   -323    451    645       O  
ATOM   2014  CB  PHE A 332      16.706   9.012  17.126  1.00146.38           C  
ANISOU 2014  CB  PHE A 332    20274  17674  17671   -394    536    607       C  
ATOM   2015  CG  PHE A 332      15.777   7.970  16.535  1.00145.07           C  
ANISOU 2015  CG  PHE A 332    20105  17518  17497   -462    601    598       C  
ATOM   2016  CD1 PHE A 332      14.403   8.173  16.514  1.00142.19           C  
ANISOU 2016  CD1 PHE A 332    19708  17226  17090   -503    649    568       C  
ATOM   2017  CD2 PHE A 332      16.281   6.809  15.968  1.00148.41           C  
ANISOU 2017  CD2 PHE A 332    20551  17876  17961   -484    613    615       C  
ATOM   2018  CE1 PHE A 332      13.553   7.236  15.967  1.00144.46           C  
ANISOU 2018  CE1 PHE A 332    19989  17524  17376   -566    707    554       C  
ATOM   2019  CE2 PHE A 332      15.432   5.863  15.412  1.00150.89           C  
ANISOU 2019  CE2 PHE A 332    20861  18198  18271   -547    672    603       C  
ATOM   2020  CZ  PHE A 332      14.063   6.082  15.413  1.00150.92           C  
ANISOU 2020  CZ  PHE A 332    20834  18278  18232   -589    719    572       C  
ATOM   2021  N   LEU A 333      17.375  11.936  18.723  1.00 98.62           N  
ANISOU 2021  N   LEU A 333    14198  11687  11587   -276    433    586       N  
ATOM   2022  CA  LEU A 333      18.206  12.704  19.640  1.00 98.23           C  
ANISOU 2022  CA  LEU A 333    14169  11622  11533   -222    373    593       C  
ATOM   2023  C   LEU A 333      17.396  13.571  20.594  1.00 98.23           C  
ANISOU 2023  C   LEU A 333    14169  11687  11468   -220    380    573       C  
ATOM   2024  O   LEU A 333      17.991  14.263  21.425  1.00102.62           O  
ANISOU 2024  O   LEU A 333    14742  12237  12012   -177    332    574       O  
ATOM   2025  CB  LEU A 333      19.202  13.580  18.868  1.00 95.62           C  
ANISOU 2025  CB  LEU A 333    13786  11268  11276   -170    329    577       C  
ATOM   2026  CG  LEU A 333      20.528  12.985  18.362  1.00 98.38           C  
ANISOU 2026  CG  LEU A 333    14145  11536  11697   -148    295    596       C  
ATOM   2027  CD1 LEU A 333      21.536  12.902  19.491  1.00103.19           C  
ANISOU 2027  CD1 LEU A 333    14806  12098  12305   -110    234    620       C  
ATOM   2028  CD2 LEU A 333      20.352  11.612  17.726  1.00 99.60           C  
ANISOU 2028  CD2 LEU A 333    14320  11658  11866   -195    336    613       C  
ATOM   2029  N   ASP A 334      16.067  13.551  20.513  1.00191.16           N  
ANISOU 2029  N   ASP A 334    25918  23518  23197   -264    439    552       N  
ATOM   2030  CA  ASP A 334      15.228  14.257  21.474  1.00195.75           C  
ANISOU 2030  CA  ASP A 334    26501  24160  23716   -268    456    530       C  
ATOM   2031  C   ASP A 334      14.716  13.265  22.507  1.00197.35           C  
ANISOU 2031  C   ASP A 334    26780  24358  23847   -316    494    555       C  
ATOM   2032  O   ASP A 334      13.971  12.338  22.170  1.00199.05           O  
ANISOU 2032  O   ASP A 334    27001  24578  24051   -372    551    558       O  
ATOM   2033  CB  ASP A 334      14.055  14.967  20.803  1.00195.82           C  
ANISOU 2033  CB  ASP A 334    26433  24240  23729   -282    496    484       C  
ATOM   2034  CG  ASP A 334      14.489  16.167  20.009  1.00196.47           C  
ANISOU 2034  CG  ASP A 334    26450  24331  23869   -230    456    460       C  
ATOM   2035  OD1 ASP A 334      15.643  16.607  20.192  1.00195.35           O  
ANISOU 2035  OD1 ASP A 334    26321  24147  23756   -182    402    473       O  
ATOM   2036  OD2 ASP A 334      13.663  16.707  19.248  1.00200.78           O  
ANISOU 2036  OD2 ASP A 334    26932  24925  24430   -235    479    427       O  
ATOM   2037  N   GLU A 335      15.101  13.477  23.764  1.00199.37           N  
ANISOU 2037  N   GLU A 335    27095  24605  24051   -296    464    570       N  
ATOM   2038  CA  GLU A 335      14.745  12.533  24.815  1.00202.21           C  
ANISOU 2038  CA  GLU A 335    27543  24953  24336   -340    496    601       C  
ATOM   2039  C   GLU A 335      13.249  12.541  25.105  1.00201.72           C  
ANISOU 2039  C   GLU A 335    27466  24958  24219   -396    578    571       C  
ATOM   2040  O   GLU A 335      12.685  11.495  25.440  1.00202.60           O  
ANISOU 2040  O   GLU A 335    27630  25059  24289   -454    632    591       O  
ATOM   2041  CB  GLU A 335      15.540  12.840  26.080  1.00201.26           C  
ANISOU 2041  CB  GLU A 335    27492  24810  24169   -301    438    623       C  
ATOM   2042  CG  GLU A 335      17.033  12.590  25.939  1.00202.89           C  
ANISOU 2042  CG  GLU A 335    27722  24940  24428   -251    359    657       C  
ATOM   2043  CD  GLU A 335      17.795  12.973  27.185  1.00207.70           C  
ANISOU 2043  CD  GLU A 335    28395  25532  24992   -209    293    672       C  
ATOM   2044  OE1 GLU A 335      17.191  13.606  28.077  1.00207.46           O  
ANISOU 2044  OE1 GLU A 335    28382  25553  24892   -216    310    652       O  
ATOM   2045  OE2 GLU A 335      18.997  12.644  27.273  1.00212.33           O  
ANISOU 2045  OE2 GLU A 335    29010  26052  25612   -170    225    701       O  
ATOM   2046  N   ASN A 336      12.589  13.696  24.977  1.00141.18           N  
ANISOU 2046  N   ASN A 336    19728  17357  16556   -382    589    520       N  
ATOM   2047  CA  ASN A 336      11.143  13.743  25.170  1.00143.27           C  
ANISOU 2047  CA  ASN A 336    19966  17687  16782   -434    667    483       C  
ATOM   2048  C   ASN A 336      10.408  12.878  24.157  1.00140.58           C  
ANISOU 2048  C   ASN A 336    19588  17351  16474   -487    722    476       C  
ATOM   2049  O   ASN A 336       9.255  12.499  24.394  1.00138.60           O  
ANISOU 2049  O   ASN A 336    19332  17140  16189   -545    794    454       O  
ATOM   2050  CB  ASN A 336      10.643  15.188  25.093  1.00145.59           C  
ANISOU 2050  CB  ASN A 336    20181  18046  17090   -401    660    428       C  
ATOM   2051  N   PHE A 337      11.049  12.565  23.033  1.00160.07           N  
ANISOU 2051  N   PHE A 337    22030  19782  19009   -470    690    490       N  
ATOM   2052  CA  PHE A 337      10.573  11.561  22.092  1.00162.96           C  
ANISOU 2052  CA  PHE A 337    22376  20137  19404   -520    734    490       C  
ATOM   2053  C   PHE A 337      11.269  10.218  22.284  1.00164.81           C  
ANISOU 2053  C   PHE A 337    22692  20294  19633   -544    734    544       C  
ATOM   2054  O   PHE A 337      10.605   9.178  22.358  1.00164.53           O  
ANISOU 2054  O   PHE A 337    22686  20252  19576   -607    795    552       O  
ATOM   2055  CB  PHE A 337      10.789  12.039  20.652  1.00160.64           C  
ANISOU 2055  CB  PHE A 337    22002  19850  19185   -491    705    468       C  
ATOM   2056  CG  PHE A 337      10.659  10.944  19.635  1.00158.87           C  
ANISOU 2056  CG  PHE A 337    21768  19598  18995   -532    734    474       C  
ATOM   2057  CD1 PHE A 337       9.419  10.489  19.239  1.00160.37           C  
ANISOU 2057  CD1 PHE A 337    21922  19833  19180   -591    797    442       C  
ATOM   2058  CD2 PHE A 337      11.784  10.318  19.130  1.00158.03           C  
ANISOU 2058  CD2 PHE A 337    21693  19422  18931   -516    700    510       C  
ATOM   2059  CE1 PHE A 337       9.311   9.469  18.313  1.00162.74           C  
ANISOU 2059  CE1 PHE A 337    22215  20107  19512   -632    823    445       C  
ATOM   2060  CE2 PHE A 337      11.681   9.294  18.214  1.00158.63           C  
ANISOU 2060  CE2 PHE A 337    21763  19470  19039   -555    728    513       C  
ATOM   2061  CZ  PHE A 337      10.442   8.869  17.802  1.00160.37           C  
ANISOU 2061  CZ  PHE A 337    21948  19736  19250   -614    790    481       C  
ATOM   2062  N   LYS A 338      12.607  10.225  22.354  1.00110.89           N  
ANISOU 2062  N   LYS A 338    15900  13405  12830   -493    666    580       N  
ATOM   2063  CA  LYS A 338      13.366   8.980  22.432  1.00108.57           C  
ANISOU 2063  CA  LYS A 338    15677  13031  12544   -506    656    631       C  
ATOM   2064  C   LYS A 338      12.946   8.138  23.626  1.00109.85           C  
ANISOU 2064  C   LYS A 338    15932  13178  12630   -552    696    663       C  
ATOM   2065  O   LYS A 338      12.963   6.905  23.552  1.00111.44           O  
ANISOU 2065  O   LYS A 338    16182  13328  12831   -593    725    695       O  
ATOM   2066  CB  LYS A 338      14.865   9.278  22.499  1.00104.82           C  
ANISOU 2066  CB  LYS A 338    15221  12497  12107   -438    570    658       C  
ATOM   2067  N   ARG A 339      12.571   8.782  24.732  1.00148.10           N  
ANISOU 2067  N   ARG A 339    20804  18063  17406   -548    701    655       N  
ATOM   2068  CA  ARG A 339      12.045   8.041  25.871  1.00150.69           C  
ANISOU 2068  CA  ARG A 339    21223  18383  17651   -598    750    682       C  
ATOM   2069  C   ARG A 339      10.752   7.328  25.505  1.00153.76           C  
ANISOU 2069  C   ARG A 339    21589  18801  18031   -678    847    659       C  
ATOM   2070  O   ARG A 339      10.546   6.168  25.880  1.00158.37           O  
ANISOU 2070  O   ARG A 339    22246  19344  18584   -731    891    694       O  
ATOM   2071  CB  ARG A 339      11.819   8.979  27.053  1.00145.96           C  
ANISOU 2071  CB  ARG A 339    20649  17830  16979   -581    743    668       C  
ATOM   2072  N   CYS A 340       9.868   8.003  24.770  1.00142.02           N  
ANISOU 2072  N   CYS A 340    20002  17383  16575   -689    879    600       N  
ATOM   2073  CA  CYS A 340       8.580   7.400  24.443  1.00144.86           C  
ANISOU 2073  CA  CYS A 340    20330  17777  16931   -765    968    569       C  
ATOM   2074  C   CYS A 340       8.729   6.270  23.433  1.00148.80           C  
ANISOU 2074  C   CYS A 340    20825  18228  17486   -796    983    584       C  
ATOM   2075  O   CYS A 340       8.245   5.155  23.661  1.00152.54           O  
ANISOU 2075  O   CYS A 340    21347  18674  17937   -862   1046    601       O  
ATOM   2076  CB  CYS A 340       7.610   8.448  23.912  1.00142.63           C  
ANISOU 2076  CB  CYS A 340    19939  17582  16673   -762    989    499       C  
ATOM   2077  SG  CYS A 340       5.911   7.857  23.977  1.00142.10           S  
ANISOU 2077  SG  CYS A 340    19840  17567  16583   -857   1104    452       S  
ATOM   2078  N   PHE A 341       9.358   6.558  22.286  1.00145.03           N  
ANISOU 2078  N   PHE A 341    20287  17738  17079   -754    931    575       N  
ATOM   2079  CA  PHE A 341       9.524   5.549  21.239  1.00145.58           C  
ANISOU 2079  CA  PHE A 341    20346  17764  17204   -781    944    583       C  
ATOM   2080  C   PHE A 341      10.134   4.265  21.782  1.00146.75           C  
ANISOU 2080  C   PHE A 341    20596  17825  17336   -805    951    643       C  
ATOM   2081  O   PHE A 341       9.772   3.164  21.347  1.00148.02           O  
ANISOU 2081  O   PHE A 341    20769  17956  17514   -861   1001    647       O  
ATOM   2082  CB  PHE A 341      10.392   6.091  20.105  1.00139.98           C  
ANISOU 2082  CB  PHE A 341    19578  17042  16565   -723    879    575       C  
ATOM   2083  CG  PHE A 341      11.170   5.024  19.377  1.00139.35           C  
ANISOU 2083  CG  PHE A 341    19524  16886  16536   -730    868    604       C  
ATOM   2084  CD1 PHE A 341      10.576   4.269  18.379  1.00140.85           C  
ANISOU 2084  CD1 PHE A 341    19676  17078  16760   -781    915    579       C  
ATOM   2085  CD2 PHE A 341      12.497   4.779  19.695  1.00135.04           C  
ANISOU 2085  CD2 PHE A 341    19036  16266  16007   -684    809    652       C  
ATOM   2086  CE1 PHE A 341      11.292   3.294  17.710  1.00139.81           C  
ANISOU 2086  CE1 PHE A 341    19568  16876  16677   -788    908    601       C  
ATOM   2087  CE2 PHE A 341      13.213   3.805  19.034  1.00133.96           C  
ANISOU 2087  CE2 PHE A 341    18919  16057  15923   -689    801    674       C  
ATOM   2088  CZ  PHE A 341      12.611   3.063  18.040  1.00136.78           C  
ANISOU 2088  CZ  PHE A 341    19242  16417  16313   -742    853    649       C  
ATOM   2089  N   ARG A 342      11.095   4.394  22.702  1.00163.72           N  
ANISOU 2089  N   ARG A 342    22820  19931  19454   -760    896    690       N  
ATOM   2090  CA  ARG A 342      11.776   3.231  23.257  1.00165.36           C  
ANISOU 2090  CA  ARG A 342    23130  20051  19648   -771    889    752       C  
ATOM   2091  C   ARG A 342      10.778   2.214  23.798  1.00170.92           C  
ANISOU 2091  C   ARG A 342    23891  20748  20301   -855    978    763       C  
ATOM   2092  O   ARG A 342      10.856   1.027  23.474  1.00172.38           O  
ANISOU 2092  O   ARG A 342    24112  20873  20511   -893   1007    787       O  
ATOM   2093  CB  ARG A 342      12.758   3.665  24.345  1.00161.24           C  
ANISOU 2093  CB  ARG A 342    22680  19498  19086   -711    816    794       C  
ATOM   2094  N   ASP A 343       9.809   2.668  24.597  1.00200.82           N  
ANISOU 2094  N   ASP A 343    27684  24598  24022   -887   1029    740       N  
ATOM   2095  CA  ASP A 343       8.844   1.747  25.193  1.00203.45           C  
ANISOU 2095  CA  ASP A 343    28074  24925  24302   -971   1122    748       C  
ATOM   2096  C   ASP A 343       8.067   0.978  24.127  1.00203.53           C  
ANISOU 2096  C   ASP A 343    28024  24940  24368  -1034   1188    714       C  
ATOM   2097  O   ASP A 343       7.947  -0.251  24.197  1.00208.21           O  
ANISOU 2097  O   ASP A 343    28678  25474  24960  -1088   1235    743       O  
ATOM   2098  CB  ASP A 343       7.883   2.506  26.104  1.00209.29           C  
ANISOU 2098  CB  ASP A 343    28810  25741  24970   -995   1171    716       C  
ATOM   2099  CG  ASP A 343       6.636   1.701  26.414  1.00214.46           C  
ANISOU 2099  CG  ASP A 343    29487  26409  25591  -1091   1284    700       C  
ATOM   2100  OD1 ASP A 343       6.712   0.790  27.270  1.00212.98           O  
ANISOU 2100  OD1 ASP A 343    29412  26164  25347  -1129   1319    753       O  
ATOM   2101  OD2 ASP A 343       5.591   1.957  25.780  1.00214.63           O  
ANISOU 2101  OD2 ASP A 343    29411  26494  25644  -1128   1339    635       O  
ATOM   2102  N   PHE A 344       7.492   1.695  23.152  1.00170.31           N  
ANISOU 2102  N   PHE A 344    23700  20802  20208  -1029   1192    649       N  
ATOM   2103  CA  PHE A 344       6.695   1.046  22.108  1.00172.28           C  
ANISOU 2103  CA  PHE A 344    23885  21065  20509  -1088   1249    607       C  
ATOM   2104  C   PHE A 344       7.471  -0.067  21.419  1.00174.15           C  
ANISOU 2104  C   PHE A 344    24155  21216  20798  -1092   1233    642       C  
ATOM   2105  O   PHE A 344       6.898  -1.088  21.017  1.00173.47           O  
ANISOU 2105  O   PHE A 344    24070  21108  20732  -1160   1296    632       O  
ATOM   2106  CB  PHE A 344       6.244   2.078  21.070  1.00169.65           C  
ANISOU 2106  CB  PHE A 344    23426  20811  20223  -1061   1228    540       C  
ATOM   2107  CG  PHE A 344       4.766   2.370  21.089  1.00171.17           C  
ANISOU 2107  CG  PHE A 344    23550  21085  20402  -1116   1300    475       C  
ATOM   2108  CD1 PHE A 344       4.218   3.224  22.037  1.00171.60           C  
ANISOU 2108  CD1 PHE A 344    23602  21196  20404  -1110   1318    456       C  
ATOM   2109  CD2 PHE A 344       3.924   1.797  20.148  1.00170.24           C  
ANISOU 2109  CD2 PHE A 344    23366  20988  20328  -1172   1349    428       C  
ATOM   2110  CE1 PHE A 344       2.859   3.497  22.039  1.00171.66           C  
ANISOU 2110  CE1 PHE A 344    23539  21277  20408  -1159   1386    390       C  
ATOM   2111  CE2 PHE A 344       2.567   2.063  20.149  1.00168.07           C  
ANISOU 2111  CE2 PHE A 344    23021  20787  20050  -1220   1412    363       C  
ATOM   2112  CZ  PHE A 344       2.034   2.913  21.095  1.00167.80           C  
ANISOU 2112  CZ  PHE A 344    22981  20808  19968  -1214   1431    344       C  
ATOM   2113  N   CYS A 345       8.778   0.117  21.272  1.00159.51           N  
ANISOU 2113  N   CYS A 345    22324  19311  18970  -1022   1150    680       N  
ATOM   2114  CA  CYS A 345       9.622  -0.808  20.541  1.00157.63           C  
ANISOU 2114  CA  CYS A 345    22107  18994  18792  -1016   1126    708       C  
ATOM   2115  C   CYS A 345      10.645  -1.520  21.416  1.00158.58           C  
ANISOU 2115  C   CYS A 345    22342  19019  18892   -993   1091    783       C  
ATOM   2116  O   CYS A 345      11.420  -2.331  20.899  1.00161.08           O  
ANISOU 2116  O   CYS A 345    22681  19260  19262   -984   1069    808       O  
ATOM   2117  CB  CYS A 345      10.313  -0.059  19.404  1.00153.55           C  
ANISOU 2117  CB  CYS A 345    21509  18492  18341   -954   1060    681       C  
ATOM   2118  SG  CYS A 345       9.167   0.441  18.104  1.00153.46           S  
ANISOU 2118  SG  CYS A 345    21370  18572  18364   -986   1098    598       S  
ATOM   2119  N   PHE A 346      10.672  -1.247  22.719  1.00184.69           N  
ANISOU 2119  N   PHE A 346    25722  22327  22123   -983   1084    817       N  
ATOM   2120  CA  PHE A 346      11.467  -2.013  23.681  1.00188.04           C  
ANISOU 2120  CA  PHE A 346    26270  22664  22514   -970   1056    891       C  
ATOM   2121  C   PHE A 346      10.574  -2.342  24.874  1.00191.35           C  
ANISOU 2121  C   PHE A 346    26769  23096  22841  -1031   1127    911       C  
ATOM   2122  O   PHE A 346      10.790  -1.842  25.985  1.00191.32           O  
ANISOU 2122  O   PHE A 346    26828  23100  22765  -1004   1099    939       O  
ATOM   2123  CB  PHE A 346      12.707  -1.234  24.127  1.00183.62           C  
ANISOU 2123  CB  PHE A 346    25731  22086  21952   -879    951    920       C  
ATOM   2124  CG  PHE A 346      13.895  -1.389  23.216  1.00181.10           C  
ANISOU 2124  CG  PHE A 346    25378  21708  21722   -824    882    927       C  
ATOM   2125  CD1 PHE A 346      13.919  -0.775  21.972  1.00179.73           C  
ANISOU 2125  CD1 PHE A 346    25095  21578  21618   -805    871    874       C  
ATOM   2126  CD2 PHE A 346      14.997  -2.130  23.611  1.00181.71           C  
ANISOU 2126  CD2 PHE A 346    25536  21689  21817   -789    827    986       C  
ATOM   2127  CE1 PHE A 346      15.013  -0.910  21.134  1.00179.10           C  
ANISOU 2127  CE1 PHE A 346    24986  21444  21620   -758    816    876       C  
ATOM   2128  CE2 PHE A 346      16.095  -2.267  22.779  1.00180.70           C  
ANISOU 2128  CE2 PHE A 346    25373  21508  21779   -740    768    987       C  
ATOM   2129  CZ  PHE A 346      16.102  -1.657  21.539  1.00178.74           C  
ANISOU 2129  CZ  PHE A 346    25014  21303  21596   -726    766    931       C  
ATOM   2130  N   PRO A 347       9.545  -3.186  24.676  1.00145.93           N  
ANISOU 2130  N   PRO A 347    21016  17343  17086  -1117   1224    893       N  
ATOM   2131  CA  PRO A 347       8.567  -3.411  25.745  1.00144.27           C  
ANISOU 2131  CA  PRO A 347    20871  17154  16790  -1183   1306    901       C  
ATOM   2132  C   PRO A 347       9.047  -4.402  26.802  1.00145.15           C  
ANISOU 2132  C   PRO A 347    21133  17174  16845  -1197   1309    983       C  
ATOM   2133  O   PRO A 347       9.458  -3.981  27.884  1.00142.40           O  
ANISOU 2133  O   PRO A 347    20862  16822  16423  -1162   1269   1022       O  
ATOM   2134  CB  PRO A 347       7.362  -3.965  24.988  1.00142.50           C  
ANISOU 2134  CB  PRO A 347    20581  16962  16602  -1268   1405    846       C  
ATOM   2135  CG  PRO A 347       7.978  -4.733  23.864  1.00143.81           C  
ANISOU 2135  CG  PRO A 347    20720  17064  16856  -1259   1378    850       C  
ATOM   2136  CD  PRO A 347       9.229  -3.977  23.471  1.00142.20           C  
ANISOU 2136  CD  PRO A 347    20487  16852  16691  -1160   1265    863       C  
TER    2137      PRO A 347                                                      
ATOM   2138  N   VAL D   4      20.314  28.730  48.149  1.00155.62           N  
ANISOU 2138  N   VAL D   4    22475  19520  17132    182   -336    -23       N  
ATOM   2139  CA  VAL D   4      19.993  29.057  49.531  1.00162.36           C  
ANISOU 2139  CA  VAL D   4    23428  20422  17841    161   -326    -62       C  
ATOM   2140  C   VAL D   4      18.503  29.346  49.670  1.00165.20           C  
ANISOU 2140  C   VAL D   4    23772  20844  18152    101   -181   -104       C  
ATOM   2141  O   VAL D   4      17.734  28.488  50.101  1.00166.82           O  
ANISOU 2141  O   VAL D   4    24065  21067  18251     42   -104    -66       O  
ATOM   2142  CB  VAL D   4      20.830  30.249  50.032  1.00164.36           C  
ANISOU 2142  CB  VAL D   4    23651  20680  18119    216   -418   -136       C  
ATOM   2143  N   GLN D   5      18.097  30.558  49.301  1.00176.90           N  
ANISOU 2143  N   GLN D   5    25139  22357  19716    115   -142   -184       N  
ATOM   2144  CA  GLN D   5      16.709  30.987  49.401  1.00177.03           C  
ANISOU 2144  CA  GLN D   5    25122  22434  19706     66    -10   -237       C  
ATOM   2145  C   GLN D   5      16.181  31.314  48.013  1.00175.47           C  
ANISOU 2145  C   GLN D   5    24779  22233  19658     72     45   -248       C  
ATOM   2146  O   GLN D   5      16.808  32.077  47.268  1.00170.47           O  
ANISOU 2146  O   GLN D   5    24046  21573  19150    126    -13   -272       O  
ATOM   2147  CB  GLN D   5      16.572  32.201  50.325  1.00178.94           C  
ANISOU 2147  CB  GLN D   5    25364  22722  19903     77     -7   -332       C  
ATOM   2148  N   LEU D   6      15.031  30.738  47.671  1.00142.75           N  
ANISOU 2148  N   LEU D   6    20626  18114  15500     17    156   -232       N  
ATOM   2149  CA  LEU D   6      14.394  30.940  46.377  1.00138.54           C  
ANISOU 2149  CA  LEU D   6    19964  17582  15094     16    214   -240       C  
ATOM   2150  C   LEU D   6      13.116  31.743  46.566  1.00140.81           C  
ANISOU 2150  C   LEU D   6    20192  17931  15378    -13    322   -320       C  
ATOM   2151  O   LEU D   6      12.232  31.338  47.330  1.00141.75           O  
ANISOU 2151  O   LEU D   6    20378  18090  15390    -72    408   -331       O  
ATOM   2152  CB  LEU D   6      14.076  29.605  45.707  1.00136.45           C  
ANISOU 2152  CB  LEU D   6    19720  17293  14830    -23    253   -160       C  
ATOM   2153  CG  LEU D   6      15.207  28.579  45.705  1.00135.32           C  
ANISOU 2153  CG  LEU D   6    19659  17089  14666     -6    161    -74       C  
ATOM   2154  CD1 LEU D   6      14.845  27.412  44.809  1.00129.02           C  
ANISOU 2154  CD1 LEU D   6    18855  16266  13903    -40    205     -6       C  
ATOM   2155  CD2 LEU D   6      16.516  29.210  45.267  1.00132.45           C  
ANISOU 2155  CD2 LEU D   6    19242  16681  14402     68     41    -80       C  
ATOM   2156  N   VAL D   7      13.016  32.863  45.858  1.00163.96           N  
ANISOU 2156  N   VAL D   7    22999  20868  18430     27    318   -377       N  
ATOM   2157  CA  VAL D   7      11.917  33.808  46.016  1.00162.29           C  
ANISOU 2157  CA  VAL D   7    22718  20710  18235     13    405   -463       C  
ATOM   2158  C   VAL D   7      10.901  33.519  44.916  1.00159.39           C  
ANISOU 2158  C   VAL D   7    22260  20354  17948    -11    486   -454       C  
ATOM   2159  O   VAL D   7      11.031  34.004  43.789  1.00156.46           O  
ANISOU 2159  O   VAL D   7    21784  19960  17704     28    460   -456       O  
ATOM   2160  CB  VAL D   7      12.407  35.257  45.968  1.00159.30           C  
ANISOU 2160  CB  VAL D   7    22263  20327  17938     74    351   -534       C  
ATOM   2161  N   GLU D   8       9.877  32.737  45.247  1.00135.81           N  
ANISOU 2161  N   GLU D   8    19315  17401  14885    -78    584   -446       N  
ATOM   2162  CA  GLU D   8       8.819  32.418  44.294  1.00133.13           C  
ANISOU 2162  CA  GLU D   8    18891  17078  14613   -107    664   -445       C  
ATOM   2163  C   GLU D   8       7.923  33.636  44.111  1.00132.35           C  
ANISOU 2163  C   GLU D   8    18679  17021  14587    -93    719   -538       C  
ATOM   2164  O   GLU D   8       7.203  34.032  45.033  1.00134.46           O  
ANISOU 2164  O   GLU D   8    18965  17333  14789   -123    789   -603       O  
ATOM   2165  CB  GLU D   8       8.015  31.216  44.780  1.00135.97           C  
ANISOU 2165  CB  GLU D   8    19332  17460  14870   -187    756   -413       C  
ATOM   2166  N   SER D   9       7.967  34.236  42.925  1.00145.66           N  
ANISOU 2166  N   SER D   9    20249  18688  16408    -46    688   -545       N  
ATOM   2167  CA  SER D   9       7.163  35.407  42.617  1.00144.99           C  
ANISOU 2167  CA  SER D   9    20050  18633  16406    -23    729   -627       C  
ATOM   2168  C   SER D   9       5.819  34.962  42.043  1.00145.64           C  
ANISOU 2168  C   SER D   9    20068  18750  16519    -68    825   -640       C  
ATOM   2169  O   SER D   9       5.457  33.785  42.095  1.00149.79           O  
ANISOU 2169  O   SER D   9    20647  19281  16984   -124    872   -594       O  
ATOM   2170  CB  SER D   9       7.917  36.322  41.659  1.00147.61           C  
ANISOU 2170  CB  SER D   9    20298  18924  16865     51    644   -627       C  
ATOM   2171  OG  SER D   9       9.088  36.834  42.270  1.00148.08           O  
ANISOU 2171  OG  SER D   9    20408  18955  16902     89    561   -631       O  
ATOM   2172  N   GLY D  10       5.063  35.906  41.487  1.00143.51           N  
ANISOU 2172  N   GLY D  10    19681  18500  16346    -42    854   -704       N  
ATOM   2173  CA  GLY D  10       3.772  35.565  40.910  1.00144.70           C  
ANISOU 2173  CA  GLY D  10    19758  18685  16537    -78    938   -724       C  
ATOM   2174  C   GLY D  10       2.774  35.137  41.969  1.00149.97           C  
ANISOU 2174  C   GLY D  10    20471  19405  17107   -150   1048   -769       C  
ATOM   2175  O   GLY D  10       2.692  35.719  43.057  1.00157.72           O  
ANISOU 2175  O   GLY D  10    21488  20410  18026   -156   1076   -828       O  
ATOM   2176  N   GLY D  11       2.004  34.102  41.647  1.00134.83           N  
ANISOU 2176  N   GLY D  11    18553  17503  15175   -208   1116   -744       N  
ATOM   2177  CA  GLY D  11       0.988  33.611  42.552  1.00140.49           C  
ANISOU 2177  CA  GLY D  11    19308  18267  15805   -284   1232   -785       C  
ATOM   2178  C   GLY D  11      -0.228  34.521  42.593  1.00144.70           C  
ANISOU 2178  C   GLY D  11    19730  18849  16402   -284   1308   -890       C  
ATOM   2179  O   GLY D  11      -0.491  35.312  41.682  1.00143.34           O  
ANISOU 2179  O   GLY D  11    19438  18674  16352   -231   1278   -922       O  
ATOM   2180  N   GLY D  12      -0.982  34.395  43.677  1.00190.83           N  
ANISOU 2180  N   GLY D  12    25614  24733  22160   -344   1410   -946       N  
ATOM   2181  CA  GLY D  12      -2.151  35.219  43.886  1.00194.89           C  
ANISOU 2181  CA  GLY D  12    26029  25295  22725   -350   1493  -1054       C  
ATOM   2182  C   GLY D  12      -3.400  34.642  43.243  1.00195.71           C  
ANISOU 2182  C   GLY D  12    26047  25427  22887   -396   1578  -1077       C  
ATOM   2183  O   GLY D  12      -3.352  33.757  42.389  1.00193.84           O  
ANISOU 2183  O   GLY D  12    25804  25170  22676   -410   1558  -1010       O  
ATOM   2184  N   LEU D  13      -4.541  35.167  43.677  1.00140.69           N  
ANISOU 2184  N   LEU D  13    19008  18506  15942   -421   1674  -1178       N  
ATOM   2185  CA  LEU D  13      -5.832  34.712  43.194  1.00138.94           C  
ANISOU 2185  CA  LEU D  13    18694  18317  15779   -468   1764  -1219       C  
ATOM   2186  C   LEU D  13      -6.109  35.253  41.796  1.00135.78           C  
ANISOU 2186  C   LEU D  13    18149  17906  15533   -402   1700  -1228       C  
ATOM   2187  O   LEU D  13      -5.472  36.198  41.324  1.00137.40           O  
ANISOU 2187  O   LEU D  13    18314  18086  15807   -321   1605  -1224       O  
ATOM   2188  CB  LEU D  13      -6.945  35.139  44.151  1.00140.76           C  
ANISOU 2188  CB  LEU D  13    18893  18601  15989   -514   1889  -1332       C  
ATOM   2189  N   VAL D  14      -7.078  34.628  41.129  1.00162.76           N  
ANISOU 2189  N   VAL D  14    21490  21344  19006   -440   1754  -1241       N  
ATOM   2190  CA  VAL D  14      -7.447  34.996  39.767  1.00164.34           C  
ANISOU 2190  CA  VAL D  14    21558  21539  19346   -386   1697  -1247       C  
ATOM   2191  C   VAL D  14      -8.847  34.460  39.512  1.00168.51           C  
ANISOU 2191  C   VAL D  14    21996  22109  19920   -445   1795  -1305       C  
ATOM   2192  O   VAL D  14      -9.354  33.624  40.261  1.00172.00           O  
ANISOU 2192  O   VAL D  14    22494  22575  20282   -531   1900  -1319       O  
ATOM   2193  CB  VAL D  14      -6.416  34.455  38.741  1.00165.25           C  
ANISOU 2193  CB  VAL D  14    21710  21604  19474   -352   1587  -1135       C  
ATOM   2194  CG1 VAL D  14      -6.588  32.959  38.535  1.00165.54           C  
ANISOU 2194  CG1 VAL D  14    21801  21639  19458   -427   1631  -1075       C  
ATOM   2195  CG2 VAL D  14      -6.506  35.212  37.421  1.00160.45           C  
ANISOU 2195  CG2 VAL D  14    20979  20982  19003   -273   1504  -1140       C  
ATOM   2196  N   ARG D  15      -9.496  34.980  38.474  1.00213.47           N  
ANISOU 2196  N   ARG D  15    27552  27813  25746   -398   1763  -1345       N  
ATOM   2197  CA  ARG D  15     -10.805  34.509  38.059  1.00216.07           C  
ANISOU 2197  CA  ARG D  15    27780  28181  26138   -444   1840  -1402       C  
ATOM   2198  C   ARG D  15     -10.673  33.267  37.181  1.00215.81           C  
ANISOU 2198  C   ARG D  15    27769  28130  26099   -479   1817  -1320       C  
ATOM   2199  O   ARG D  15      -9.623  33.031  36.578  1.00215.01           O  
ANISOU 2199  O   ARG D  15    27725  27986  25983   -443   1721  -1226       O  
ATOM   2200  CB  ARG D  15     -11.539  35.615  37.307  1.00215.36           C  
ANISOU 2200  CB  ARG D  15    27530  28106  26192   -373   1804  -1479       C  
ATOM   2201  N   PRO D  16     -11.722  32.444  37.104  1.00188.98           N  
ANISOU 2201  N   PRO D  16    24325  24764  22714   -552   1908  -1358       N  
ATOM   2202  CA  PRO D  16     -11.664  31.260  36.236  1.00188.58           C  
ANISOU 2202  CA  PRO D  16    24289  24698  22666   -588   1890  -1288       C  
ATOM   2203  C   PRO D  16     -11.519  31.634  34.767  1.00189.49           C  
ANISOU 2203  C   PRO D  16    24311  24795  22889   -511   1775  -1261       C  
ATOM   2204  O   PRO D  16     -12.047  32.647  34.302  1.00190.14           O  
ANISOU 2204  O   PRO D  16    24276  24895  23074   -449   1742  -1325       O  
ATOM   2205  CB  PRO D  16     -12.999  30.557  36.507  1.00189.39           C  
ANISOU 2205  CB  PRO D  16    24335  24845  22781   -677   2020  -1361       C  
ATOM   2206  CG  PRO D  16     -13.896  31.641  37.020  1.00189.97           C  
ANISOU 2206  CG  PRO D  16    24307  24959  22915   -658   2074  -1481       C  
ATOM   2207  CD  PRO D  16     -12.997  32.518  37.837  1.00188.57           C  
ANISOU 2207  CD  PRO D  16    24210  24763  22675   -611   2038  -1468       C  
ATOM   2208  N   GLY D  17     -10.791  30.794  34.034  1.00162.73           N  
ANISOU 2208  N   GLY D  17    20981  21371  19477   -514   1715  -1165       N  
ATOM   2209  CA  GLY D  17     -10.490  31.062  32.645  1.00160.25           C  
ANISOU 2209  CA  GLY D  17    20604  21035  19249   -446   1604  -1127       C  
ATOM   2210  C   GLY D  17      -9.400  32.085  32.419  1.00156.29           C  
ANISOU 2210  C   GLY D  17    20127  20495  18760   -354   1496  -1085       C  
ATOM   2211  O   GLY D  17      -9.115  32.415  31.260  1.00154.07           O  
ANISOU 2211  O   GLY D  17    19796  20193  18548   -293   1403  -1053       O  
ATOM   2212  N   GLY D  18      -8.782  32.593  33.482  1.00166.90           N  
ANISOU 2212  N   GLY D  18    21547  21828  20038   -344   1506  -1086       N  
ATOM   2213  CA  GLY D  18      -7.777  33.631  33.386  1.00165.34           C  
ANISOU 2213  CA  GLY D  18    21371  21595  19856   -261   1412  -1058       C  
ATOM   2214  C   GLY D  18      -6.369  33.084  33.276  1.00162.16           C  
ANISOU 2214  C   GLY D  18    21088  21141  19386   -254   1344   -951       C  
ATOM   2215  O   GLY D  18      -6.140  31.961  32.819  1.00162.99           O  
ANISOU 2215  O   GLY D  18    21237  21230  19462   -294   1342   -888       O  
ATOM   2216  N   SER D  19      -5.409  33.899  33.713  1.00146.41           N  
ANISOU 2216  N   SER D  19    19141  19117  17370   -202   1289   -935       N  
ATOM   2217  CA  SER D  19      -3.999  33.585  33.535  1.00142.59           C  
ANISOU 2217  CA  SER D  19    18754  18580  16842   -180   1211   -841       C  
ATOM   2218  C   SER D  19      -3.187  34.219  34.657  1.00140.43           C  
ANISOU 2218  C   SER D  19    18559  18292  16506   -160   1198   -847       C  
ATOM   2219  O   SER D  19      -3.646  35.148  35.329  1.00143.86           O  
ANISOU 2219  O   SER D  19    18956  18752  16953   -144   1230   -924       O  
ATOM   2220  CB  SER D  19      -3.497  34.083  32.176  1.00143.92           C  
ANISOU 2220  CB  SER D  19    18867  18713  17101   -108   1110   -801       C  
ATOM   2221  OG  SER D  19      -3.635  33.084  31.185  1.00146.34           O  
ANISOU 2221  OG  SER D  19    19164  19013  17424   -135   1100   -752       O  
ATOM   2222  N   LEU D  20      -1.972  33.701  34.856  1.00124.99           N  
ANISOU 2222  N   LEU D  20    16711  16295  14484   -161   1148   -768       N  
ATOM   2223  CA  LEU D  20      -1.001  34.330  35.745  1.00124.04           C  
ANISOU 2223  CA  LEU D  20    16664  16153  14314   -131   1110   -764       C  
ATOM   2224  C   LEU D  20       0.345  33.641  35.554  1.00121.04           C  
ANISOU 2224  C   LEU D  20    16380  15720  13891   -124   1038   -668       C  
ATOM   2225  O   LEU D  20       0.412  32.411  35.519  1.00122.28           O  
ANISOU 2225  O   LEU D  20    16597  15870  13994   -176   1060   -614       O  
ATOM   2226  CB  LEU D  20      -1.444  34.240  37.214  1.00126.69           C  
ANISOU 2226  CB  LEU D  20    17059  16525  14552   -185   1197   -816       C  
ATOM   2227  CG  LEU D  20      -0.481  34.661  38.337  1.00129.77           C  
ANISOU 2227  CG  LEU D  20    17547  16899  14861   -170   1167   -812       C  
ATOM   2228  CD1 LEU D  20       0.301  35.952  38.084  1.00127.66           C  
ANISOU 2228  CD1 LEU D  20    17242  16602  14661    -85   1079   -826       C  
ATOM   2229  CD2 LEU D  20      -1.253  34.757  39.647  1.00130.65           C  
ANISOU 2229  CD2 LEU D  20    17690  17058  14895   -222   1267   -885       C  
ATOM   2230  N   ARG D  21       1.409  34.436  35.454  1.00122.40           N  
ANISOU 2230  N   ARG D  21    16564  15854  14089    -60    953   -650       N  
ATOM   2231  CA  ARG D  21       2.760  33.926  35.242  1.00120.54           C  
ANISOU 2231  CA  ARG D  21    16408  15565  13828    -44    877   -566       C  
ATOM   2232  C   ARG D  21       3.506  33.880  36.569  1.00121.74           C  
ANISOU 2232  C   ARG D  21    16667  15709  13879    -56    869   -561       C  
ATOM   2233  O   ARG D  21       3.644  34.905  37.244  1.00126.90           O  
ANISOU 2233  O   ARG D  21    17315  16371  14531    -25    860   -615       O  
ATOM   2234  CB  ARG D  21       3.523  34.791  34.237  1.00117.39           C  
ANISOU 2234  CB  ARG D  21    15954  15123  13526     31    787   -548       C  
ATOM   2235  N   LEU D  22       4.000  32.698  36.929  1.00113.92           N  
ANISOU 2235  N   LEU D  22    15777  14701  12806    -99    870   -498       N  
ATOM   2236  CA  LEU D  22       4.781  32.508  38.144  1.00115.45           C  
ANISOU 2236  CA  LEU D  22    16085  14882  12897   -109    852   -481       C  
ATOM   2237  C   LEU D  22       6.259  32.457  37.785  1.00114.26           C  
ANISOU 2237  C   LEU D  22    15976  14672  12766    -62    745   -417       C  
ATOM   2238  O   LEU D  22       6.640  31.861  36.773  1.00112.74           O  
ANISOU 2238  O   LEU D  22    15769  14446  12623    -54    710   -359       O  
ATOM   2239  CB  LEU D  22       4.380  31.220  38.864  1.00118.06           C  
ANISOU 2239  CB  LEU D  22    16511  15229  13119   -187    921   -451       C  
ATOM   2240  CG  LEU D  22       2.907  30.802  38.823  1.00121.46           C  
ANISOU 2240  CG  LEU D  22    16896  15709  13546   -249   1033   -492       C  
ATOM   2241  CD1 LEU D  22       2.721  29.477  39.547  1.00124.76           C  
ANISOU 2241  CD1 LEU D  22    17424  16128  13851   -326   1094   -450       C  
ATOM   2242  CD2 LEU D  22       1.981  31.861  39.390  1.00122.73           C  
ANISOU 2242  CD2 LEU D  22    16993  15921  13720   -247   1093   -592       C  
ATOM   2243  N   SER D  23       7.094  33.073  38.624  1.00122.59           N  
ANISOU 2243  N   SER D  23    17081  15713  13783    -31    694   -432       N  
ATOM   2244  CA  SER D  23       8.517  33.238  38.309  1.00120.92           C  
ANISOU 2244  CA  SER D  23    16892  15445  13606     22    590   -386       C  
ATOM   2245  C   SER D  23       9.356  33.043  39.571  1.00121.49           C  
ANISOU 2245  C   SER D  23    17079  15507  13576     17    552   -375       C  
ATOM   2246  O   SER D  23       9.588  33.989  40.330  1.00123.02           O  
ANISOU 2246  O   SER D  23    17277  15712  13752     43    533   -428       O  
ATOM   2247  CB  SER D  23       8.765  34.601  37.675  1.00122.14           C  
ANISOU 2247  CB  SER D  23    16951  15586  13870     87    545   -429       C  
ATOM   2248  OG  SER D  23       8.567  35.646  38.613  1.00125.96           O  
ANISOU 2248  OG  SER D  23    17430  16097  14332    102    558   -503       O  
ATOM   2249  N   CYS D  24       9.826  31.815  39.778  1.00138.57           N  
ANISOU 2249  N   CYS D  24    19333  17645  15672    -13    537   -304       N  
ATOM   2250  CA  CYS D  24      10.813  31.555  40.815  1.00141.42           C  
ANISOU 2250  CA  CYS D  24    19804  17984  15944     -7    478   -280       C  
ATOM   2251  C   CYS D  24      12.204  31.889  40.298  1.00137.69           C  
ANISOU 2251  C   CYS D  24    19316  17455  15546     56    366   -251       C  
ATOM   2252  O   CYS D  24      12.529  31.635  39.134  1.00135.51           O  
ANISOU 2252  O   CYS D  24    18987  17144  15358     74    340   -212       O  
ATOM   2253  CB  CYS D  24      10.764  30.098  41.269  1.00144.21           C  
ANISOU 2253  CB  CYS D  24    20266  18329  16197    -63    504   -214       C  
ATOM   2254  SG  CYS D  24      12.168  29.639  42.306  1.00155.66           S  
ANISOU 2254  SG  CYS D  24    21852  19738  17554    -44    405   -166       S  
ATOM   2255  N   VAL D  25      13.029  32.456  41.174  1.00116.79           N  
ANISOU 2255  N   VAL D  25    16715  14799  12861     87    303   -274       N  
ATOM   2256  CA  VAL D  25      14.335  32.979  40.801  1.00113.47           C  
ANISOU 2256  CA  VAL D  25    16270  14327  12517    148    200   -266       C  
ATOM   2257  C   VAL D  25      15.294  32.731  41.955  1.00116.04           C  
ANISOU 2257  C   VAL D  25    16703  14637  12752    157    129   -253       C  
ATOM   2258  O   VAL D  25      14.887  32.657  43.118  1.00122.65           O  
ANISOU 2258  O   VAL D  25    17616  15511  13475    126    160   -276       O  
ATOM   2259  CB  VAL D  25      14.249  34.486  40.460  1.00113.25           C  
ANISOU 2259  CB  VAL D  25    16140  14307  12582    193    194   -338       C  
ATOM   2260  CG1 VAL D  25      13.560  35.250  41.594  1.00114.74           C  
ANISOU 2260  CG1 VAL D  25    16346  14550  12701    179    241   -415       C  
ATOM   2261  CG2 VAL D  25      15.623  35.074  40.152  1.00113.23           C  
ANISOU 2261  CG2 VAL D  25    16113  14250  12657    252     93   -335       C  
ATOM   2262  N   ASP D  26      16.576  32.575  41.630  1.00124.63           N  
ANISOU 2262  N   ASP D  26    17796  15668  13888    198     33   -216       N  
ATOM   2263  CA  ASP D  26      17.630  32.548  42.641  1.00129.11           C  
ANISOU 2263  CA  ASP D  26    18447  16215  14393    221    -55   -213       C  
ATOM   2264  C   ASP D  26      18.695  33.526  42.154  1.00128.16           C  
ANISOU 2264  C   ASP D  26    18251  16055  14387    284   -137   -244       C  
ATOM   2265  O   ASP D  26      19.659  33.125  41.496  1.00126.22           O  
ANISOU 2265  O   ASP D  26    17992  15755  14210    310   -202   -200       O  
ATOM   2266  CB  ASP D  26      18.177  31.134  42.837  1.00131.32           C  
ANISOU 2266  CB  ASP D  26    18824  16460  14610    203    -93   -131       C  
ATOM   2267  CG  ASP D  26      19.313  31.069  43.849  1.00133.78           C  
ANISOU 2267  CG  ASP D  26    19222  16748  14860    232   -196   -126       C  
ATOM   2268  OD1 ASP D  26      19.752  32.126  44.349  1.00137.57           O  
ANISOU 2268  OD1 ASP D  26    19682  17238  15352    267   -242   -188       O  
ATOM   2269  OD2 ASP D  26      19.767  29.944  44.150  1.00131.11           O  
ANISOU 2269  OD2 ASP D  26    18974  16381  14461    221   -234    -60       O  
ATOM   2270  N   SER D  27      18.519  34.808  42.487  1.00147.04           N  
ANISOU 2270  N   SER D  27    20595  18472  16802    305   -131   -322       N  
ATOM   2271  CA  SER D  27      19.491  35.824  42.100  1.00149.77           C  
ANISOU 2271  CA  SER D  27    20871  18780  17257    361   -203   -357       C  
ATOM   2272  C   SER D  27      20.826  35.632  42.803  1.00147.61           C  
ANISOU 2272  C   SER D  27    20659  18470  16955    390   -312   -348       C  
ATOM   2273  O   SER D  27      21.834  36.190  42.357  1.00147.83           O  
ANISOU 2273  O   SER D  27    20632  18452  17082    435   -382   -362       O  
ATOM   2274  CB  SER D  27      18.945  37.226  42.388  1.00147.14           C  
ANISOU 2274  CB  SER D  27    20478  18480  16950    375   -168   -446       C  
ATOM   2275  OG  SER D  27      18.888  37.486  43.780  1.00145.73           O  
ANISOU 2275  OG  SER D  27    20372  18337  16660    365   -178   -492       O  
ATOM   2276  N   GLU D  28      20.854  34.862  43.888  1.00118.99           N  
ANISOU 2276  N   GLU D  28    17148  14863  13199    366   -330   -325       N  
ATOM   2277  CA  GLU D  28      22.117  34.494  44.508  1.00121.04           C  
ANISOU 2277  CA  GLU D  28    17474  15086  13429    395   -442   -305       C  
ATOM   2278  C   GLU D  28      22.903  33.493  43.670  1.00119.09           C  
ANISOU 2278  C   GLU D  28    17224  14779  13244    407   -491   -229       C  
ATOM   2279  O   GLU D  28      24.001  33.103  44.075  1.00119.98           O  
ANISOU 2279  O   GLU D  28    17384  14854  13348    435   -589   -208       O  
ATOM   2280  CB  GLU D  28      21.869  33.927  45.909  1.00123.15           C  
ANISOU 2280  CB  GLU D  28    17875  15389  13529    365   -446   -298       C  
ATOM   2281  N   ARG D  29      22.351  33.045  42.541  1.00133.02           N  
ANISOU 2281  N   ARG D  29    18936  16534  15070    388   -425   -189       N  
ATOM   2282  CA  ARG D  29      23.024  32.139  41.608  1.00133.51           C  
ANISOU 2282  CA  ARG D  29    18984  16540  15203    397   -458   -122       C  
ATOM   2283  C   ARG D  29      23.615  30.912  42.305  1.00137.51           C  
ANISOU 2283  C   ARG D  29    19603  17021  15623    391   -520    -61       C  
ATOM   2284  O   ARG D  29      24.563  30.301  41.800  1.00139.51           O  
ANISOU 2284  O   ARG D  29    19851  17218  15939    415   -583    -18       O  
ATOM   2285  CB  ARG D  29      24.108  32.872  40.810  1.00128.31           C  
ANISOU 2285  CB  ARG D  29    18234  15830  14689    448   -522   -146       C  
ATOM   2286  N   THR D  30      23.075  30.542  43.471  1.00127.94           N  
ANISOU 2286  N   THR D  30    18495  15848  14268    360   -501    -57       N  
ATOM   2287  CA  THR D  30      23.496  29.310  44.131  1.00127.88           C  
ANISOU 2287  CA  THR D  30    18606  15817  14167    350   -551      9       C  
ATOM   2288  C   THR D  30      22.877  28.088  43.465  1.00124.38           C  
ANISOU 2288  C   THR D  30    18182  15360  13714    307   -482     82       C  
ATOM   2289  O   THR D  30      23.560  27.081  43.246  1.00121.60           O  
ANISOU 2289  O   THR D  30    17870  14956  13376    316   -534    144       O  
ATOM   2290  CB  THR D  30      23.123  29.346  45.616  1.00130.06           C  
ANISOU 2290  CB  THR D  30    18995  16138  14284    328   -551    -10       C  
ATOM   2291  OG1 THR D  30      21.699  29.280  45.755  1.00130.89           O  
ANISOU 2291  OG1 THR D  30    19115  16299  14317    270   -426    -18       O  
ATOM   2292  CG2 THR D  30      23.627  30.627  46.266  1.00130.98           C  
ANISOU 2292  CG2 THR D  30    19084  16273  14409    366   -610    -92       C  
ATOM   2293  N   SER D  31      21.592  28.168  43.126  1.00119.37           N  
ANISOU 2293  N   SER D  31    17519  14772  13066    260   -367     70       N  
ATOM   2294  CA  SER D  31      20.869  27.071  42.507  1.00117.62           C  
ANISOU 2294  CA  SER D  31    17312  14544  12834    214   -292    130       C  
ATOM   2295  C   SER D  31      20.146  27.569  41.265  1.00118.59           C  
ANISOU 2295  C   SER D  31    17312  14684  13062    204   -215    105       C  
ATOM   2296  O   SER D  31      19.707  28.720  41.199  1.00119.16           O  
ANISOU 2296  O   SER D  31    17315  14794  13168    215   -185     39       O  
ATOM   2297  CB  SER D  31      19.854  26.458  43.470  1.00118.33           C  
ANISOU 2297  CB  SER D  31    17505  14677  12776    154   -217    145       C  
ATOM   2298  OG  SER D  31      18.908  27.430  43.882  1.00118.93           O  
ANISOU 2298  OG  SER D  31    17552  14818  12819    134   -146     75       O  
ATOM   2299  N   TYR D  32      20.014  26.683  40.283  1.00123.65           N  
ANISOU 2299  N   TYR D  32    17932  15296  13754    186   -186    157       N  
ATOM   2300  CA  TYR D  32      19.307  27.005  39.055  1.00118.49           C  
ANISOU 2300  CA  TYR D  32    17172  14657  13193    175   -117    141       C  
ATOM   2301  C   TYR D  32      17.917  26.397  39.131  1.00118.49           C  
ANISOU 2301  C   TYR D  32    17196  14701  13122    109     -8    152       C  
ATOM   2302  O   TYR D  32      17.794  25.166  39.067  1.00115.66           O  
ANISOU 2302  O   TYR D  32    16899  14322  12725     74     12    211       O  
ATOM   2303  CB  TYR D  32      20.055  26.457  37.840  1.00115.49           C  
ANISOU 2303  CB  TYR D  32    16744  14217  12919    195   -152    186       C  
ATOM   2304  CG  TYR D  32      21.569  26.452  37.940  1.00115.14           C  
ANISOU 2304  CG  TYR D  32    16713  14114  12923    248   -264    199       C  
ATOM   2305  CD1 TYR D  32      22.265  27.504  38.532  1.00116.27           C  
ANISOU 2305  CD1 TYR D  32    16841  14257  13078    292   -331    148       C  
ATOM   2306  CD2 TYR D  32      22.301  25.380  37.447  1.00118.81           C  
ANISOU 2306  CD2 TYR D  32    17201  14519  13423    253   -303    259       C  
ATOM   2307  CE1 TYR D  32      23.645  27.486  38.618  1.00119.71           C  
ANISOU 2307  CE1 TYR D  32    17282  14638  13564    339   -435    156       C  
ATOM   2308  CE2 TYR D  32      23.677  25.353  37.528  1.00121.38           C  
ANISOU 2308  CE2 TYR D  32    17531  14789  13800    301   -406    268       C  
ATOM   2309  CZ  TYR D  32      24.346  26.406  38.114  1.00122.70           C  
ANISOU 2309  CZ  TYR D  32    17680  14959  13981    344   -472    215       C  
ATOM   2310  OH  TYR D  32      25.720  26.370  38.191  1.00124.55           O  
ANISOU 2310  OH  TYR D  32    17912  15137  14273    393   -575    218       O  
ATOM   2311  N   PRO D  33      16.848  27.187  39.272  1.00105.79           N  
ANISOU 2311  N   PRO D  33    15544  13152  11500     90     66     94       N  
ATOM   2312  CA  PRO D  33      15.506  26.589  39.231  1.00107.53           C  
ANISOU 2312  CA  PRO D  33    15773  13413  11669     26    174     99       C  
ATOM   2313  C   PRO D  33      15.191  26.038  37.847  1.00106.58           C  
ANISOU 2313  C   PRO D  33    15584  13275  11636     12    208    130       C  
ATOM   2314  O   PRO D  33      15.039  26.804  36.889  1.00105.62           O  
ANISOU 2314  O   PRO D  33    15358  13160  11613     37    213     99       O  
ATOM   2315  CB  PRO D  33      14.584  27.757  39.619  1.00106.39           C  
ANISOU 2315  CB  PRO D  33    15578  13332  11514     21    231     19       C  
ATOM   2316  CG  PRO D  33      15.495  28.759  40.294  1.00105.12           C  
ANISOU 2316  CG  PRO D  33    15425  13164  11353     74    150    -20       C  
ATOM   2317  CD  PRO D  33      16.797  28.628  39.570  1.00101.46           C  
ANISOU 2317  CD  PRO D  33    14938  12635  10976    123     56     19       C  
ATOM   2318  N   MET D  34      15.112  24.707  37.728  1.00129.14           N  
ANISOU 2318  N   MET D  34    18501  16107  14458    -27    229    192       N  
ATOM   2319  CA  MET D  34      14.930  24.040  36.444  1.00126.72           C  
ANISOU 2319  CA  MET D  34    18141  15777  14228    -42    254    225       C  
ATOM   2320  C   MET D  34      13.593  23.328  36.325  1.00126.92           C  
ANISOU 2320  C   MET D  34    18170  15840  14214   -111    360    228       C  
ATOM   2321  O   MET D  34      13.270  22.836  35.239  1.00126.49           O  
ANISOU 2321  O   MET D  34    18063  15776  14222   -127    389    246       O  
ATOM   2322  CB  MET D  34      16.029  22.995  36.209  1.00120.18           C  
ANISOU 2322  CB  MET D  34    17369  14879  13416    -29    188    295       C  
ATOM   2323  CG  MET D  34      17.431  23.469  36.480  1.00125.52           C  
ANISOU 2323  CG  MET D  34    18057  15513  14123     34     80    297       C  
ATOM   2324  SD  MET D  34      18.623  22.129  36.313  1.00131.12           S  
ANISOU 2324  SD  MET D  34    18836  16139  14846     46      8    377       S  
ATOM   2325  CE  MET D  34      19.954  22.950  35.487  1.00124.34           C  
ANISOU 2325  CE  MET D  34    17890  15235  14119    119    -84    358       C  
ATOM   2326  N   GLY D  35      12.828  23.233  37.406  1.00103.29           N  
ANISOU 2326  N   GLY D  35    15239  12888  11118   -153    419    210       N  
ATOM   2327  CA  GLY D  35      11.559  22.535  37.368  1.00104.37           C  
ANISOU 2327  CA  GLY D  35    15381  13058  11216   -224    525    208       C  
ATOM   2328  C   GLY D  35      10.572  23.131  38.346  1.00107.00           C  
ANISOU 2328  C   GLY D  35    15726  13455  11474   -255    597    149       C  
ATOM   2329  O   GLY D  35      10.947  23.784  39.327  1.00108.81           O  
ANISOU 2329  O   GLY D  35    16000  13695  11646   -232    564    124       O  
ATOM   2330  N   TRP D  36       9.296  22.888  38.071  1.00127.30           N  
ANISOU 2330  N   TRP D  36    18254  16067  14048   -310    697    122       N  
ATOM   2331  CA  TRP D  36       8.215  23.324  38.941  1.00134.23           C  
ANISOU 2331  CA  TRP D  36    19137  17006  14859   -350    784     61       C  
ATOM   2332  C   TRP D  36       7.431  22.124  39.451  1.00138.75           C  
ANISOU 2332  C   TRP D  36    19789  17584  15345   -433    876     89       C  
ATOM   2333  O   TRP D  36       7.254  21.132  38.738  1.00136.62           O  
ANISOU 2333  O   TRP D  36    19516  17288  15104   -465    900    131       O  
ATOM   2334  CB  TRP D  36       7.280  24.304  38.227  1.00131.49           C  
ANISOU 2334  CB  TRP D  36    18653  16708  14599   -339    827    -13       C  
ATOM   2335  CG  TRP D  36       7.897  25.642  37.992  1.00129.98           C  
ANISOU 2335  CG  TRP D  36    18394  16517  14475   -264    752    -51       C  
ATOM   2336  CD1 TRP D  36       8.781  25.976  37.011  1.00125.87           C  
ANISOU 2336  CD1 TRP D  36    17818  15956  14048   -206    669    -29       C  
ATOM   2337  CD2 TRP D  36       7.693  26.830  38.771  1.00135.79           C  
ANISOU 2337  CD2 TRP D  36    19112  17292  15190   -241    758   -121       C  
ATOM   2338  NE1 TRP D  36       9.128  27.300  37.120  1.00127.71           N  
ANISOU 2338  NE1 TRP D  36    18002  16200  14323   -149    623    -78       N  
ATOM   2339  CE2 TRP D  36       8.479  27.847  38.194  1.00132.88           C  
ANISOU 2339  CE2 TRP D  36    18677  16902  14910   -168    674   -136       C  
ATOM   2340  CE3 TRP D  36       6.919  27.134  39.896  1.00134.61           C  
ANISOU 2340  CE3 TRP D  36    18997  17190  14957   -278    830   -174       C  
ATOM   2341  CZ2 TRP D  36       8.514  29.144  38.700  1.00130.02           C  
ANISOU 2341  CZ2 TRP D  36    18280  16563  14557   -130    658   -201       C  
ATOM   2342  CZ3 TRP D  36       6.956  28.425  40.398  1.00130.12           C  
ANISOU 2342  CZ3 TRP D  36    18394  16649  14398   -239    813   -242       C  
ATOM   2343  CH2 TRP D  36       7.746  29.413  39.799  1.00129.18           C  
ANISOU 2343  CH2 TRP D  36    18207  16506  14370   -165    726   -254       C  
ATOM   2344  N   PHE D  37       6.966  22.228  40.695  1.00168.75           N  
ANISOU 2344  N   PHE D  37    23664  21417  19038   -470    932     62       N  
ATOM   2345  CA  PHE D  37       6.223  21.177  41.374  1.00166.69           C  
ANISOU 2345  CA  PHE D  37    23493  21162  18679   -553   1028     84       C  
ATOM   2346  C   PHE D  37       4.970  21.780  41.988  1.00169.09           C  
ANISOU 2346  C   PHE D  37    23763  21535  18947   -597   1137      1       C  
ATOM   2347  O   PHE D  37       5.006  22.892  42.523  1.00170.76           O  
ANISOU 2347  O   PHE D  37    23952  21780  19148   -564   1121    -56       O  
ATOM   2348  CB  PHE D  37       7.075  20.521  42.465  1.00166.55           C  
ANISOU 2348  CB  PHE D  37    23636  21103  18541   -558    985    149       C  
ATOM   2349  CG  PHE D  37       7.875  19.349  41.987  1.00167.47           C  
ANISOU 2349  CG  PHE D  37    23812  21150  18670   -555    929    240       C  
ATOM   2350  CD1 PHE D  37       7.316  18.086  41.918  1.00171.31           C  
ANISOU 2350  CD1 PHE D  37    24352  21615  19122   -625   1005    284       C  
ATOM   2351  CD2 PHE D  37       9.187  19.519  41.580  1.00165.71           C  
ANISOU 2351  CD2 PHE D  37    23584  20878  18500   -481    804    277       C  
ATOM   2352  CE1 PHE D  37       8.060  17.008  41.477  1.00173.13           C  
ANISOU 2352  CE1 PHE D  37    24636  21776  19369   -620    954    365       C  
ATOM   2353  CE2 PHE D  37       9.932  18.450  41.133  1.00166.87           C  
ANISOU 2353  CE2 PHE D  37    23780  20958  18666   -476    754    355       C  
ATOM   2354  CZ  PHE D  37       9.369  17.192  41.079  1.00171.45           C  
ANISOU 2354  CZ  PHE D  37    24417  21517  19210   -544    828    400       C  
ATOM   2355  N   ARG D  38       3.865  21.047  41.912  1.00158.33           N  
ANISOU 2355  N   ARG D  38    22394  20193  17572   -673   1248     -8       N  
ATOM   2356  CA  ARG D  38       2.602  21.523  42.468  1.00163.55           C  
ANISOU 2356  CA  ARG D  38    23018  20919  18206   -723   1363    -91       C  
ATOM   2357  C   ARG D  38       2.218  20.756  43.732  1.00166.18           C  
ANISOU 2357  C   ARG D  38    23491  21255  18395   -801   1450    -73       C  
ATOM   2358  O   ARG D  38       1.101  20.888  44.238  1.00165.67           O  
ANISOU 2358  O   ARG D  38    23411  21240  18298   -860   1566   -136       O  
ATOM   2359  CB  ARG D  38       1.488  21.413  41.428  1.00163.04           C  
ANISOU 2359  CB  ARG D  38    22822  20884  18244   -754   1434   -135       C  
ATOM   2360  N   LYS D  43      -4.011  16.378  48.111  1.00134.75           N  
ANISOU 2360  N   LYS D  43    19909  17377  13914  -1430   2346   -170       N  
ATOM   2361  CA  LYS D  43      -3.399  15.125  47.684  1.00139.91           C  
ANISOU 2361  CA  LYS D  43    20644  17957  14558  -1441   2302    -62       C  
ATOM   2362  C   LYS D  43      -1.876  15.212  47.719  1.00140.32           C  
ANISOU 2362  C   LYS D  43    20777  17959  14578  -1351   2137     23       C  
ATOM   2363  O   LYS D  43      -1.311  16.178  48.234  1.00137.69           O  
ANISOU 2363  O   LYS D  43    20459  17648  14210  -1291   2066      1       O  
ATOM   2364  CB  LYS D  43      -3.872  14.752  46.279  1.00141.20           C  
ANISOU 2364  CB  LYS D  43    20661  18116  14874  -1444   2308    -76       C  
ATOM   2365  N   GLU D  44      -1.218  14.201  47.156  1.00203.02           N  
ANISOU 2365  N   GLU D  44    28768  25832  22538  -1343   2076    115       N  
ATOM   2366  CA  GLU D  44       0.234  14.121  47.189  1.00204.96           C  
ANISOU 2366  CA  GLU D  44    29096  26022  22757  -1264   1924    200       C  
ATOM   2367  C   GLU D  44       0.859  15.247  46.364  1.00207.47           C  
ANISOU 2367  C   GLU D  44    29278  26360  23191  -1161   1801    164       C  
ATOM   2368  O   GLU D  44       0.170  16.042  45.717  1.00207.73           O  
ANISOU 2368  O   GLU D  44    29157  26445  23325  -1149   1831     80       O  
ATOM   2369  CB  GLU D  44       0.703  12.761  46.672  1.00204.70           C  
ANISOU 2369  CB  GLU D  44    29129  25911  22736  -1282   1896    298       C  
ATOM   2370  N   ARG D  45       2.191  15.314  46.404  1.00156.65           N  
ANISOU 2370  N   ARG D  45    22903  19879  16740  -1086   1662    228       N  
ATOM   2371  CA  ARG D  45       2.908  16.333  45.647  1.00150.60           C  
ANISOU 2371  CA  ARG D  45    22021  19121  16079   -988   1542    201       C  
ATOM   2372  C   ARG D  45       2.655  16.146  44.157  1.00151.16           C  
ANISOU 2372  C   ARG D  45    21949  19185  16299   -976   1535    194       C  
ATOM   2373  O   ARG D  45       2.764  15.034  43.629  1.00152.35           O  
ANISOU 2373  O   ARG D  45    22129  19286  16471  -1004   1540    255       O  
ATOM   2374  CB  ARG D  45       4.412  16.269  45.930  1.00146.46           C  
ANISOU 2374  CB  ARG D  45    21591  18541  15516   -916   1397    276       C  
ATOM   2375  CG  ARG D  45       5.270  16.610  44.709  1.00140.99           C  
ANISOU 2375  CG  ARG D  45    20789  17820  14959   -833   1278    289       C  
ATOM   2376  CD  ARG D  45       6.603  15.875  44.667  1.00138.92           C  
ANISOU 2376  CD  ARG D  45    20620  17480  14682   -789   1161    384       C  
ATOM   2377  NE  ARG D  45       7.436  16.149  45.832  1.00143.17           N  
ANISOU 2377  NE  ARG D  45    21282  18007  15110   -756   1088    408       N  
ATOM   2378  CZ  ARG D  45       8.652  15.651  46.016  1.00144.18           C  
ANISOU 2378  CZ  ARG D  45    21499  18070  15212   -710    976    484       C  
ATOM   2379  NH1 ARG D  45       9.231  14.887  45.103  1.00140.87           N  
ANISOU 2379  NH1 ARG D  45    21059  17591  14874   -689    923    542       N  
ATOM   2380  NH2 ARG D  45       9.305  15.928  47.142  1.00142.31           N  
ANISOU 2380  NH2 ARG D  45    21375  17830  14867   -684    914    498       N  
ATOM   2381  N   GLU D  46       2.311  17.238  43.482  1.00152.89           N  
ANISOU 2381  N   GLU D  46    22017  19452  16621   -935   1523    117       N  
ATOM   2382  CA  GLU D  46       2.085  17.230  42.046  1.00150.97           C  
ANISOU 2382  CA  GLU D  46    21635  19209  16519   -915   1506    103       C  
ATOM   2383  C   GLU D  46       3.321  17.761  41.331  1.00147.68           C  
ANISOU 2383  C   GLU D  46    21176  18758  16176   -818   1362    132       C  
ATOM   2384  O   GLU D  46       4.041  18.618  41.849  1.00146.68           O  
ANISOU 2384  O   GLU D  46    21071  18636  16024   -760   1288    122       O  
ATOM   2385  CB  GLU D  46       0.857  18.070  41.687  1.00148.31           C  
ANISOU 2385  CB  GLU D  46    21154  18943  16252   -931   1585      0       C  
ATOM   2386  CG  GLU D  46       0.368  17.906  40.255  1.00150.77           C  
ANISOU 2386  CG  GLU D  46    21330  19260  16697   -928   1589    -18       C  
ATOM   2387  CD  GLU D  46      -1.053  18.410  40.066  1.00149.94           C  
ANISOU 2387  CD  GLU D  46    21104  19222  16643   -967   1692   -116       C  
ATOM   2388  OE1 GLU D  46      -1.924  18.050  40.886  1.00148.38           O  
ANISOU 2388  OE1 GLU D  46    20951  19049  16376  -1044   1808   -146       O  
ATOM   2389  OE2 GLU D  46      -1.299  19.163  39.098  1.00153.43           O  
ANISOU 2389  OE2 GLU D  46    21408  19690  17197   -921   1656   -164       O  
ATOM   2390  N   PHE D  47       3.564  17.238  40.133  1.00152.76           N  
ANISOU 2390  N   PHE D  47    21760  19369  16914   -803   1325    166       N  
ATOM   2391  CA  PHE D  47       4.774  17.536  39.372  1.00149.15           C  
ANISOU 2391  CA  PHE D  47    21271  18870  16529   -721   1197    203       C  
ATOM   2392  C   PHE D  47       4.372  18.151  38.037  1.00147.22           C  
ANISOU 2392  C   PHE D  47    20867  18653  16418   -691   1187    154       C  
ATOM   2393  O   PHE D  47       4.064  17.429  37.083  1.00145.28           O  
ANISOU 2393  O   PHE D  47    20576  18391  16233   -716   1209    171       O  
ATOM   2394  CB  PHE D  47       5.609  16.276  39.168  1.00150.25           C  
ANISOU 2394  CB  PHE D  47    21501  18933  16653   -727   1152    296       C  
ATOM   2395  N   VAL D  48       4.378  19.482  37.971  1.00180.30           N  
ANISOU 2395  N   VAL D  48    24975  22881  20650   -636   1153     94       N  
ATOM   2396  CA  VAL D  48       4.158  20.194  36.717  1.00178.24           C  
ANISOU 2396  CA  VAL D  48    24571  22639  20512   -594   1125     54       C  
ATOM   2397  C   VAL D  48       5.464  20.202  35.930  1.00177.09           C  
ANISOU 2397  C   VAL D  48    24421  22437  20427   -527   1010    109       C  
ATOM   2398  O   VAL D  48       6.508  19.771  36.434  1.00180.07           O  
ANISOU 2398  O   VAL D  48    24898  22765  20754   -510    950    167       O  
ATOM   2399  CB  VAL D  48       3.629  21.623  36.949  1.00171.97           C  
ANISOU 2399  CB  VAL D  48    23692  21902  19744   -562   1136    -31       C  
ATOM   2400  CG1 VAL D  48       2.134  21.598  37.222  1.00171.15           C  
ANISOU 2400  CG1 VAL D  48    23543  21858  19629   -627   1257    -97       C  
ATOM   2401  CG2 VAL D  48       4.348  22.272  38.105  1.00170.77           C  
ANISOU 2401  CG2 VAL D  48    23619  21749  19517   -529   1093    -34       C  
ATOM   2402  N   ALA D  49       5.399  20.662  34.680  1.00119.57           N  
ANISOU 2402  N   ALA D  49    17024  15158  13250   -492    980     88       N  
ATOM   2403  CA  ALA D  49       6.498  20.625  33.720  1.00117.30           C  
ANISOU 2403  CA  ALA D  49    16716  14818  13033   -436    886    134       C  
ATOM   2404  C   ALA D  49       7.824  21.154  34.258  1.00110.73           C  
ANISOU 2404  C   ALA D  49    15939  13950  12183   -374    792    159       C  
ATOM   2405  O   ALA D  49       7.856  21.933  35.213  1.00111.82           O  
ANISOU 2405  O   ALA D  49    16101  14113  12272   -358    787    126       O  
ATOM   2406  CB  ALA D  49       6.108  21.425  32.478  1.00119.48           C  
ANISOU 2406  CB  ALA D  49    16858  15119  13417   -402    872     91       C  
ATOM   2407  N   SER D  50       8.927  20.720  33.654  1.00116.65           N  
ANISOU 2407  N   SER D  50    16707  14640  12973   -341    717    214       N  
ATOM   2408  CA  SER D  50      10.260  21.241  33.929  1.00111.80           C  
ANISOU 2408  CA  SER D  50    16124  13987  12367   -277    619    234       C  
ATOM   2409  C   SER D  50      10.937  21.578  32.600  1.00109.64           C  
ANISOU 2409  C   SER D  50    15770  13683  12206   -227    558    243       C  
ATOM   2410  O   SER D  50      10.400  21.314  31.520  1.00110.54           O  
ANISOU 2410  O   SER D  50    15818  13804  12380   -244    589    239       O  
ATOM   2411  CB  SER D  50      11.088  20.246  34.758  1.00114.53           C  
ANISOU 2411  CB  SER D  50    16598  14282  12637   -288    585    299       C  
ATOM   2412  OG  SER D  50      11.710  19.270  33.943  1.00115.43           O  
ANISOU 2412  OG  SER D  50    16723  14338  12797   -288    554    356       O  
ATOM   2413  N   ILE D  51      12.131  22.171  32.678  1.00 95.70           N  
ANISOU 2413  N   ILE D  51    14011  11882  10470   -166    471    252       N  
ATOM   2414  CA  ILE D  51      12.873  22.589  31.495  1.00 95.63           C  
ANISOU 2414  CA  ILE D  51    13931  11840  10564   -117    414    257       C  
ATOM   2415  C   ILE D  51      14.353  22.287  31.701  1.00 92.77           C  
ANISOU 2415  C   ILE D  51    13624  11412  10211    -78    327    301       C  
ATOM   2416  O   ILE D  51      14.818  22.073  32.822  1.00 95.04           O  
ANISOU 2416  O   ILE D  51    13997  11687  10428    -76    298    317       O  
ATOM   2417  CB  ILE D  51      12.651  24.093  31.180  1.00 97.59           C  
ANISOU 2417  CB  ILE D  51    14088  12123  10869    -73    402    196       C  
ATOM   2418  CG1 ILE D  51      12.826  24.374  29.682  1.00 97.23           C  
ANISOU 2418  CG1 ILE D  51    13956  12060  10928    -47    384    198       C  
ATOM   2419  CG2 ILE D  51      13.583  24.965  32.014  1.00 94.81           C  
ANISOU 2419  CG2 ILE D  51    13762  11756  10505    -23    335    180       C  
ATOM   2420  CD1 ILE D  51      12.716  25.843  29.304  1.00 94.55           C  
ANISOU 2420  CD1 ILE D  51    13533  11742  10649      0    366    147       C  
ATOM   2421  N   THR D  52      15.092  22.255  30.593  1.00 97.45           N  
ANISOU 2421  N   THR D  52    14171  11963  10894    -48    286    320       N  
ATOM   2422  CA  THR D  52      16.526  22.006  30.642  1.00 99.74           C  
ANISOU 2422  CA  THR D  52    14497  12187  11212     -9    203    355       C  
ATOM   2423  C   THR D  52      17.238  23.253  31.170  1.00 99.17           C  
ANISOU 2423  C   THR D  52    14408  12116  11157     47    141    319       C  
ATOM   2424  O   THR D  52      16.647  24.329  31.276  1.00 98.38           O  
ANISOU 2424  O   THR D  52    14257  12062  11060     58    163    268       O  
ATOM   2425  CB  THR D  52      17.045  21.639  29.251  1.00100.30           C  
ANISOU 2425  CB  THR D  52    14517  12215  11377      3    189    378       C  
ATOM   2426  OG1 THR D  52      16.187  20.649  28.678  1.00101.44           O  
ANISOU 2426  OG1 THR D  52    14662  12370  11511    -52    255    398       O  
ATOM   2427  CG2 THR D  52      18.447  21.034  29.324  1.00101.61           C  
ANISOU 2427  CG2 THR D  52    14729  12308  11571     32    116    420       C  
ATOM   2428  N   TRP D  53      18.524  23.109  31.507  1.00150.87           N  
ANISOU 2428  N   TRP D  53    20994  18610  17718     84     62    342       N  
ATOM   2429  CA  TRP D  53      19.248  24.220  32.115  1.00154.67           C  
ANISOU 2429  CA  TRP D  53    21465  19090  18212    134     -1    305       C  
ATOM   2430  C   TRP D  53      19.280  25.418  31.177  1.00155.46           C  
ANISOU 2430  C   TRP D  53    21463  19198  18407    168     -1    262       C  
ATOM   2431  O   TRP D  53      18.882  26.531  31.541  1.00156.72           O  
ANISOU 2431  O   TRP D  53    21589  19397  18561    183      8    213       O  
ATOM   2432  CB  TRP D  53      20.684  23.815  32.447  1.00156.37           C  
ANISOU 2432  CB  TRP D  53    21726  19241  18446    170    -91    335       C  
ATOM   2433  CG  TRP D  53      21.531  25.018  32.713  1.00158.45           C  
ANISOU 2433  CG  TRP D  53    21952  19495  18756    225   -157    291       C  
ATOM   2434  CD1 TRP D  53      21.267  26.003  33.622  1.00157.64           C  
ANISOU 2434  CD1 TRP D  53    21854  19434  18607    238   -163    244       C  
ATOM   2435  CD2 TRP D  53      22.734  25.407  32.042  1.00161.38           C  
ANISOU 2435  CD2 TRP D  53    22272  19813  19233    271   -219    286       C  
ATOM   2436  NE1 TRP D  53      22.241  26.966  33.576  1.00158.61           N  
ANISOU 2436  NE1 TRP D  53    21933  19531  18800    289   -229    209       N  
ATOM   2437  CE2 TRP D  53      23.153  26.626  32.613  1.00161.49           C  
ANISOU 2437  CE2 TRP D  53    22262  19838  19260    310   -263    234       C  
ATOM   2438  CE3 TRP D  53      23.504  24.842  31.024  1.00161.74           C  
ANISOU 2438  CE3 TRP D  53    22288  19801  19364    282   -239    315       C  
ATOM   2439  CZ2 TRP D  53      24.307  27.287  32.199  1.00162.57           C  
ANISOU 2439  CZ2 TRP D  53    22345  19928  19494    357   -324    213       C  
ATOM   2440  CZ3 TRP D  53      24.652  25.504  30.615  1.00165.49           C  
ANISOU 2440  CZ3 TRP D  53    22711  20232  19936    328   -297    293       C  
ATOM   2441  CH2 TRP D  53      25.039  26.711  31.201  1.00163.48           C  
ANISOU 2441  CH2 TRP D  53    22433  19989  19694    364   -338    243       C  
ATOM   2442  N   SER D  54      19.750  25.195  29.956  1.00146.65           N  
ANISOU 2442  N   SER D  54    20298  18042  17378    178     -9    282       N  
ATOM   2443  CA  SER D  54      19.897  26.236  28.956  1.00145.68           C  
ANISOU 2443  CA  SER D  54    20087  17916  17347    209    -12    252       C  
ATOM   2444  C   SER D  54      18.576  26.632  28.314  1.00145.81           C  
ANISOU 2444  C   SER D  54    20048  17986  17366    185     60    228       C  
ATOM   2445  O   SER D  54      18.566  27.517  27.448  1.00147.92           O  
ANISOU 2445  O   SER D  54    20245  18253  17704    210     62    205       O  
ATOM   2446  CB  SER D  54      20.919  25.779  27.915  1.00144.58           C  
ANISOU 2446  CB  SER D  54    19927  17714  17294    225    -43    282       C  
ATOM   2447  OG  SER D  54      20.797  24.385  27.669  1.00142.59           O  
ANISOU 2447  OG  SER D  54    19718  17443  17018    188    -21    330       O  
ATOM   2448  N   GLY D  55      17.473  26.000  28.708  1.00 90.55           N  
ANISOU 2448  N   GLY D  55    13079  11031  10294    138    118    234       N  
ATOM   2449  CA  GLY D  55      16.151  26.495  28.379  1.00 90.08           C  
ANISOU 2449  CA  GLY D  55    12966  11030  10229    118    182    199       C  
ATOM   2450  C   GLY D  55      15.644  26.226  26.982  1.00 89.57           C  
ANISOU 2450  C   GLY D  55    12845  10968  10220    103    216    210       C  
ATOM   2451  O   GLY D  55      14.710  26.908  26.544  1.00 89.47           O  
ANISOU 2451  O   GLY D  55    12771  10998  10226    103    251    176       O  
ATOM   2452  N   ILE D  56      16.215  25.251  26.268  1.00 96.37           N  
ANISOU 2452  N   ILE D  56    13723  11786  11109     91    206    255       N  
ATOM   2453  CA  ILE D  56      15.734  24.925  24.925  1.00 92.56           C  
ANISOU 2453  CA  ILE D  56    13191  11305  10672     73    238    264       C  
ATOM   2454  C   ILE D  56      14.484  24.064  24.987  1.00 90.73           C  
ANISOU 2454  C   ILE D  56    12970  11117  10386     15    305    266       C  
ATOM   2455  O   ILE D  56      13.406  24.472  24.542  1.00 90.00           O  
ANISOU 2455  O   ILE D  56    12823  11073  10301      3    346    235       O  
ATOM   2456  CB  ILE D  56      16.821  24.227  24.084  1.00 89.84           C  
ANISOU 2456  CB  ILE D  56    12857  10896  10381     80    207    305       C  
ATOM   2457  CG1 ILE D  56      18.187  24.905  24.184  1.00 89.85           C  
ANISOU 2457  CG1 ILE D  56    12856  10847  10435    132    141    303       C  
ATOM   2458  CG2 ILE D  56      16.362  24.072  22.655  1.00 92.83           C  
ANISOU 2458  CG2 ILE D  56    13183  11280  10807     66    237    308       C  
ATOM   2459  CD1 ILE D  56      19.018  24.430  25.303  1.00 90.26           C  
ANISOU 2459  CD1 ILE D  56    12976  10867  10450    140     97    321       C  
ATOM   2460  N   ASP D  57      14.609  22.855  25.530  1.00118.48           N  
ANISOU 2460  N   ASP D  57    16555  14613  13850    -22    317    302       N  
ATOM   2461  CA  ASP D  57      13.527  21.881  25.466  1.00122.00           C  
ANISOU 2461  CA  ASP D  57    17013  15088  14253    -83    384    309       C  
ATOM   2462  C   ASP D  57      12.834  21.723  26.810  1.00119.38           C  
ANISOU 2462  C   ASP D  57    16732  14793  13832   -115    422    296       C  
ATOM   2463  O   ASP D  57      13.487  21.376  27.806  1.00118.84           O  
ANISOU 2463  O   ASP D  57    16742  14698  13715   -112    395    320       O  
ATOM   2464  CB  ASP D  57      14.045  20.537  24.959  1.00122.67           C  
ANISOU 2464  CB  ASP D  57    17138  15122  14349   -109    383    359       C  
ATOM   2465  CG  ASP D  57      15.396  20.173  25.543  1.00124.11           C  
ANISOU 2465  CG  ASP D  57    17387  15242  14528    -82    322    396       C  
ATOM   2466  OD1 ASP D  57      15.782  20.772  26.560  1.00127.08           O  
ANISOU 2466  OD1 ASP D  57    17793  15620  14871    -55    288    386       O  
ATOM   2467  OD2 ASP D  57      16.075  19.285  24.977  1.00125.84           O  
ANISOU 2467  OD2 ASP D  57    17626  15408  14780    -88    306    433       O  
ATOM   2468  N   PRO D  58      11.532  22.002  26.887  1.00 90.74           N  
ANISOU 2468  N   PRO D  58    13065  11227  10184   -144    483    255       N  
ATOM   2469  CA  PRO D  58      10.760  21.746  28.104  1.00 91.48           C  
ANISOU 2469  CA  PRO D  58    13208  11358  10192   -186    536    240       C  
ATOM   2470  C   PRO D  58      10.045  20.404  28.068  1.00 91.84           C  
ANISOU 2470  C   PRO D  58    13289  11406  10200   -256    601    264       C  
ATOM   2471  O   PRO D  58       9.585  19.931  27.024  1.00 91.56           O  
ANISOU 2471  O   PRO D  58    13206  11374  10208   -278    626    265       O  
ATOM   2472  CB  PRO D  58       9.756  22.904  28.092  1.00 91.54           C  
ANISOU 2472  CB  PRO D  58    13136  11428  10215   -175    566    175       C  
ATOM   2473  CG  PRO D  58       9.446  23.082  26.625  1.00 90.96           C  
ANISOU 2473  CG  PRO D  58    12977  11360  10223   -164    564    166       C  
ATOM   2474  CD  PRO D  58      10.683  22.604  25.842  1.00 90.40           C  
ANISOU 2474  CD  PRO D  58    12928  11224  10198   -140    507    218       C  
ATOM   2475  N   THR D  59       9.944  19.785  29.239  1.00131.63           N  
ANISOU 2475  N   THR D  59    18416  16444  15155   -291    629    281       N  
ATOM   2476  CA  THR D  59       9.225  18.524  29.402  1.00138.74           C  
ANISOU 2476  CA  THR D  59    19362  17345  16010   -363    700    302       C  
ATOM   2477  C   THR D  59       7.861  18.847  29.994  1.00137.41           C  
ANISOU 2477  C   THR D  59    19168  17244  15798   -406    782    248       C  
ATOM   2478  O   THR D  59       7.721  18.990  31.209  1.00133.67           O  
ANISOU 2478  O   THR D  59    18756  16786  15247   -420    804    239       O  
ATOM   2479  CB  THR D  59      10.005  17.561  30.285  1.00137.26           C  
ANISOU 2479  CB  THR D  59    19294  17104  15755   -378    680    362       C  
ATOM   2480  OG1 THR D  59      11.395  17.624  29.938  1.00137.13           O  
ANISOU 2480  OG1 THR D  59    19292  17029  15784   -321    589    399       O  
ATOM   2481  CG2 THR D  59       9.503  16.151  30.076  1.00135.24           C  
ANISOU 2481  CG2 THR D  59    19078  16827  15479   -445    741    395       C  
ATOM   2482  N   TYR D  60       6.858  18.956  29.125  1.00157.62           N  
ANISOU 2482  N   TYR D  60    21637  19844  18408   -427    827    208       N  
ATOM   2483  CA  TYR D  60       5.547  19.452  29.511  1.00157.51           C  
ANISOU 2483  CA  TYR D  60    21573  19898  18377   -458    899    143       C  
ATOM   2484  C   TYR D  60       4.892  18.544  30.556  1.00161.55           C  
ANISOU 2484  C   TYR D  60    22162  20419  18801   -533    983    149       C  
ATOM   2485  O   TYR D  60       5.335  17.425  30.827  1.00162.80           O  
ANISOU 2485  O   TYR D  60    22409  20530  18916   -566    989    206       O  
ATOM   2486  CB  TYR D  60       4.645  19.576  28.283  1.00155.65           C  
ANISOU 2486  CB  TYR D  60    21226  19696  18217   -467    924    104       C  
ATOM   2487  N   ALA D  61       3.818  19.057  31.151  1.00152.23           N  
ANISOU 2487  N   ALA D  61    20948  19297  17595   -560   1051     88       N  
ATOM   2488  CA  ALA D  61       3.025  18.324  32.129  1.00158.43           C  
ANISOU 2488  CA  ALA D  61    21797  20100  18300   -637   1146     81       C  
ATOM   2489  C   ALA D  61       1.788  17.776  31.432  1.00161.32           C  
ANISOU 2489  C   ALA D  61    22087  20498  18707   -696   1224     44       C  
ATOM   2490  O   ALA D  61       1.010  18.540  30.850  1.00163.45           O  
ANISOU 2490  O   ALA D  61    22245  20817  19041   -681   1236    -20       O  
ATOM   2491  CB  ALA D  61       2.634  19.222  33.302  1.00157.01           C  
ANISOU 2491  CB  ALA D  61    21630  19965  18062   -634   1178     30       C  
ATOM   2492  N   ASP D  62       1.608  16.456  31.497  1.00123.58           N  
ANISOU 2492  N   ASP D  62    17370  15689  13895   -762   1277     82       N  
ATOM   2493  CA  ASP D  62       0.565  15.812  30.707  1.00124.95           C  
ANISOU 2493  CA  ASP D  62    17472  15884  14117   -819   1342     52       C  
ATOM   2494  C   ASP D  62      -0.834  16.194  31.175  1.00125.85           C  
ANISOU 2494  C   ASP D  62    17525  16067  14225   -865   1438    -30       C  
ATOM   2495  O   ASP D  62      -1.758  16.245  30.355  1.00125.84           O  
ANISOU 2495  O   ASP D  62    17418  16103  14293   -883   1468    -82       O  
ATOM   2496  CB  ASP D  62       0.742  14.294  30.747  1.00128.27           C  
ANISOU 2496  CB  ASP D  62    17981  16251  14502   -881   1379    112       C  
ATOM   2497  N   SER D  63      -1.010  16.462  32.474  1.00166.35           N  
ANISOU 2497  N   SER D  63    22719  21213  19273   -886   1486    -44       N  
ATOM   2498  CA  SER D  63      -2.342  16.676  33.034  1.00168.91           C  
ANISOU 2498  CA  SER D  63    22997  21597  19584   -942   1592   -122       C  
ATOM   2499  C   SER D  63      -3.116  17.716  32.238  1.00166.09           C  
ANISOU 2499  C   SER D  63    22485  21297  19324   -905   1581   -203       C  
ATOM   2500  O   SER D  63      -4.154  17.415  31.640  1.00165.45           O  
ANISOU 2500  O   SER D  63    22318  21248  19298   -947   1636   -252       O  
ATOM   2501  CB  SER D  63      -2.233  17.094  34.501  1.00171.15           C  
ANISOU 2501  CB  SER D  63    23368  21892  19769   -950   1626   -129       C  
ATOM   2502  OG  SER D  63      -1.380  16.215  35.211  1.00172.58           O  
ANISOU 2502  OG  SER D  63    23699  22016  19860   -971   1615    -46       O  
ATOM   2503  N   VAL D  64      -2.621  18.948  32.207  1.00177.77           N  
ANISOU 2503  N   VAL D  64    23928  22789  20827   -825   1506   -220       N  
ATOM   2504  CA  VAL D  64      -3.145  19.975  31.310  1.00178.60           C  
ANISOU 2504  CA  VAL D  64    23894  22935  21030   -774   1471   -282       C  
ATOM   2505  C   VAL D  64      -1.936  20.559  30.581  1.00177.74           C  
ANISOU 2505  C   VAL D  64    23783  22789  20960   -687   1349   -235       C  
ATOM   2506  O   VAL D  64      -1.317  21.522  31.042  1.00177.01           O  
ANISOU 2506  O   VAL D  64    23706  22694  20855   -629   1299   -237       O  
ATOM   2507  CB  VAL D  64      -3.934  21.064  32.046  1.00174.41           C  
ANISOU 2507  CB  VAL D  64    23306  22461  20499   -765   1516   -367       C  
ATOM   2508  CG1 VAL D  64      -4.868  21.771  31.084  1.00173.76           C  
ANISOU 2508  CG1 VAL D  64    23072  22425  20523   -738   1510   -440       C  
ATOM   2509  CG2 VAL D  64      -4.701  20.484  33.225  1.00178.13           C  
ANISOU 2509  CG2 VAL D  64    23835  22954  20892   -851   1637   -395       C  
ATOM   2510  N   ALA D  65      -1.588  19.971  29.436  1.00158.94           N  
ANISOU 2510  N   ALA D  65    21383  20378  18628   -679   1304   -194       N  
ATOM   2511  CA  ALA D  65      -0.578  20.527  28.546  1.00154.54           C  
ANISOU 2511  CA  ALA D  65    20806  19789  18122   -602   1198   -158       C  
ATOM   2512  C   ALA D  65      -1.189  21.459  27.515  1.00157.59           C  
ANISOU 2512  C   ALA D  65    21063  20213  18600   -557   1167   -213       C  
ATOM   2513  O   ALA D  65      -0.456  22.091  26.748  1.00154.36           O  
ANISOU 2513  O   ALA D  65    20629  19783  18237   -490   1083   -191       O  
ATOM   2514  CB  ALA D  65       0.202  19.407  27.847  1.00149.28           C  
ANISOU 2514  CB  ALA D  65    20194  19066  17459   -616   1165    -85       C  
ATOM   2515  N   ASP D  66      -2.514  21.561  27.501  1.00184.82           N  
ANISOU 2515  N   ASP D  66    24431  23717  22075   -592   1232   -284       N  
ATOM   2516  CA  ASP D  66      -3.249  22.481  26.652  1.00182.75           C  
ANISOU 2516  CA  ASP D  66    24043  23497  21898   -550   1206   -345       C  
ATOM   2517  C   ASP D  66      -3.451  23.839  27.298  1.00181.98           C  
ANISOU 2517  C   ASP D  66    23906  23429  21810   -501   1199   -398       C  
ATOM   2518  O   ASP D  66      -4.206  24.653  26.763  1.00185.37           O  
ANISOU 2518  O   ASP D  66    24229  23895  22308   -468   1187   -457       O  
ATOM   2519  CB  ASP D  66      -4.608  21.875  26.286  1.00184.22           C  
ANISOU 2519  CB  ASP D  66    24152  23726  22117   -613   1278   -401       C  
ATOM   2520  CG  ASP D  66      -5.359  21.346  27.501  1.00185.84           C  
ANISOU 2520  CG  ASP D  66    24393  23956  22264   -690   1390   -436       C  
ATOM   2521  OD1 ASP D  66      -4.872  20.378  28.123  1.00184.59           O  
ANISOU 2521  OD1 ASP D  66    24342  23762  22032   -740   1425   -383       O  
ATOM   2522  OD2 ASP D  66      -6.430  21.895  27.833  1.00187.29           O  
ANISOU 2522  OD2 ASP D  66    24498  24192  22474   -702   1442   -517       O  
ATOM   2523  N   ARG D  67      -2.812  24.099  28.439  1.00135.95           N  
ANISOU 2523  N   ARG D  67    18160  17583  15913   -495   1205   -381       N  
ATOM   2524  CA  ARG D  67      -3.074  25.314  29.203  1.00134.98           C  
ANISOU 2524  CA  ARG D  67    18005  17489  15791   -460   1212   -439       C  
ATOM   2525  C   ARG D  67      -1.843  26.043  29.721  1.00132.64           C  
ANISOU 2525  C   ARG D  67    17775  17157  15464   -401   1146   -403       C  
ATOM   2526  O   ARG D  67      -1.962  27.230  30.044  1.00134.38           O  
ANISOU 2526  O   ARG D  67    17952  17397  15709   -354   1130   -452       O  
ATOM   2527  CB  ARG D  67      -3.993  24.998  30.393  1.00136.55           C  
ANISOU 2527  CB  ARG D  67    18224  17727  15932   -530   1323   -491       C  
ATOM   2528  N   PHE D  68      -0.682  25.402  29.823  1.00163.56           N  
ANISOU 2528  N   PHE D  68    21791  21022  19334   -401   1105   -326       N  
ATOM   2529  CA  PHE D  68       0.467  26.033  30.458  1.00162.22           C  
ANISOU 2529  CA  PHE D  68    21688  20820  19130   -352   1046   -298       C  
ATOM   2530  C   PHE D  68       1.676  25.980  29.538  1.00159.41           C  
ANISOU 2530  C   PHE D  68    21348  20408  18811   -303    953   -232       C  
ATOM   2531  O   PHE D  68       1.824  25.059  28.730  1.00161.62           O  
ANISOU 2531  O   PHE D  68    21636  20664  19107   -325    945   -188       O  
ATOM   2532  CB  PHE D  68       0.841  25.368  31.794  1.00164.76           C  
ANISOU 2532  CB  PHE D  68    22130  21128  19343   -398   1085   -271       C  
ATOM   2533  CG  PHE D  68      -0.336  24.845  32.569  1.00169.48           C  
ANISOU 2533  CG  PHE D  68    22736  21770  19891   -474   1196   -315       C  
ATOM   2534  CD1 PHE D  68      -1.359  25.665  32.942  1.00172.57           C  
ANISOU 2534  CD1 PHE D  68    23052  22215  20302   -477   1250   -400       C  
ATOM   2535  CD2 PHE D  68      -0.380  23.527  32.971  1.00170.47           C  
ANISOU 2535  CD2 PHE D  68    22947  21878  19947   -545   1250   -272       C  
ATOM   2536  CE1 PHE D  68      -2.434  25.189  33.674  1.00173.78           C  
ANISOU 2536  CE1 PHE D  68    23211  22408  20411   -551   1359   -446       C  
ATOM   2537  CE2 PHE D  68      -1.447  23.058  33.700  1.00172.25           C  
ANISOU 2537  CE2 PHE D  68    23182  22141  20125   -620   1358   -314       C  
ATOM   2538  CZ  PHE D  68      -2.469  23.887  34.044  1.00170.91           C  
ANISOU 2538  CZ  PHE D  68    22934  22027  19978   -623   1415   -401       C  
ATOM   2539  N   THR D  69       2.542  26.983  29.688  1.00118.93           N  
ANISOU 2539  N   THR D  69    16228  15260  13701   -238    886   -228       N  
ATOM   2540  CA  THR D  69       3.821  27.072  28.996  1.00115.12           C  
ANISOU 2540  CA  THR D  69    15768  14722  13252   -188    799   -171       C  
ATOM   2541  C   THR D  69       4.876  27.571  29.972  1.00111.44           C  
ANISOU 2541  C   THR D  69    15372  14227  12743   -156    757   -158       C  
ATOM   2542  O   THR D  69       4.582  28.362  30.873  1.00112.52           O  
ANISOU 2542  O   THR D  69    15506  14393  12855   -146    776   -207       O  
ATOM   2543  CB  THR D  69       3.757  28.020  27.790  1.00113.30           C  
ANISOU 2543  CB  THR D  69    15441  14490  13116   -130    750   -189       C  
ATOM   2544  OG1 THR D  69       2.531  27.815  27.080  1.00113.72           O  
ANISOU 2544  OG1 THR D  69    15416  14585  13208   -156    793   -224       O  
ATOM   2545  CG2 THR D  69       4.941  27.788  26.852  1.00108.66           C  
ANISOU 2545  CG2 THR D  69    14877  13845  12565    -98    679   -125       C  
ATOM   2546  N   THR D  70       6.112  27.121  29.774  1.00140.25           N  
ANISOU 2546  N   THR D  70    19082  17821  16388   -138    697    -95       N  
ATOM   2547  CA  THR D  70       7.221  27.477  30.645  1.00140.97           C  
ANISOU 2547  CA  THR D  70    19242  17880  16442   -106    646    -78       C  
ATOM   2548  C   THR D  70       8.425  27.905  29.821  1.00141.12           C  
ANISOU 2548  C   THR D  70    19245  17845  16528    -48    561    -45       C  
ATOM   2549  O   THR D  70       8.588  27.500  28.666  1.00140.80           O  
ANISOU 2549  O   THR D  70    19175  17783  16541    -44    544    -14       O  
ATOM   2550  CB  THR D  70       7.612  26.311  31.561  1.00144.71           C  
ANISOU 2550  CB  THR D  70    19828  18334  16822   -152    662    -32       C  
ATOM   2551  OG1 THR D  70       8.794  26.653  32.295  1.00145.55           O  
ANISOU 2551  OG1 THR D  70    19998  18405  16900   -115    596    -14       O  
ATOM   2552  CG2 THR D  70       7.860  25.051  30.748  1.00143.36           C  
ANISOU 2552  CG2 THR D  70    19679  18126  16664   -182    660     28       C  
ATOM   2553  N   SER D  71       9.268  28.733  30.433  1.00132.55           N  
ANISOU 2553  N   SER D  71    18181  16741  15440     -3    510    -56       N  
ATOM   2554  CA  SER D  71      10.481  29.221  29.798  1.00130.30           C  
ANISOU 2554  CA  SER D  71    17885  16404  15221     52    432    -31       C  
ATOM   2555  C   SER D  71      11.467  29.598  30.889  1.00128.71           C  
ANISOU 2555  C   SER D  71    17745  16180  14980     78    384    -33       C  
ATOM   2556  O   SER D  71      11.068  29.990  31.987  1.00130.00           O  
ANISOU 2556  O   SER D  71    17932  16376  15084     69    408    -72       O  
ATOM   2557  CB  SER D  71      10.192  30.422  28.896  1.00129.48           C  
ANISOU 2557  CB  SER D  71    17684  16307  15203     97    418    -67       C  
ATOM   2558  OG  SER D  71       9.417  31.402  29.571  1.00126.70           O  
ANISOU 2558  OG  SER D  71    17297  16000  14842    107    447   -132       O  
ATOM   2559  N   ARG D  72      12.756  29.479  30.586  1.00 99.64           N  
ANISOU 2559  N   ARG D  72    14087  12441  11331    109    316      6       N  
ATOM   2560  CA  ARG D  72      13.794  29.791  31.561  1.00100.33           C  
ANISOU 2560  CA  ARG D  72    14230  12502  11388    136    259      4       C  
ATOM   2561  C   ARG D  72      14.760  30.797  30.962  1.00101.82           C  
ANISOU 2561  C   ARG D  72    14368  12650  11667    196    196     -6       C  
ATOM   2562  O   ARG D  72      15.340  30.553  29.899  1.00101.15           O  
ANISOU 2562  O   ARG D  72    14259  12524  11650    210    170     28       O  
ATOM   2563  CB  ARG D  72      14.546  28.537  32.012  1.00 94.78           C  
ANISOU 2563  CB  ARG D  72    13618  11762  10630    114    232     62       C  
ATOM   2564  CG  ARG D  72      15.901  28.837  32.615  1.00 96.70           C  
ANISOU 2564  CG  ARG D  72    13903  11962  10876    156    150     69       C  
ATOM   2565  CD  ARG D  72      16.491  27.631  33.312  1.00 99.14           C  
ANISOU 2565  CD  ARG D  72    14312  12243  11115    134    123    121       C  
ATOM   2566  NE  ARG D  72      17.251  28.030  34.492  1.00 99.27           N  
ANISOU 2566  NE  ARG D  72    14385  12251  11082    160     64    105       N  
ATOM   2567  CZ  ARG D  72      18.534  28.364  34.485  1.00100.92           C  
ANISOU 2567  CZ  ARG D  72    14593  12412  11341    208    -19    108       C  
ATOM   2568  NH1 ARG D  72      19.255  28.319  33.376  1.00103.12           N  
ANISOU 2568  NH1 ARG D  72    14820  12643  11717    233    -51    129       N  
ATOM   2569  NH2 ARG D  72      19.108  28.761  35.616  1.00101.12           N  
ANISOU 2569  NH2 ARG D  72    14668  12437  11315    229    -72     86       N  
ATOM   2570  N   ASP D  73      14.931  31.923  31.647  1.00 91.38           N  
ANISOU 2570  N   ASP D  73    13034  11338  10348    228    174    -56       N  
ATOM   2571  CA  ASP D  73      15.938  32.907  31.274  1.00 91.03           C  
ANISOU 2571  CA  ASP D  73    12951  11251  10384    282    113    -70       C  
ATOM   2572  C   ASP D  73      17.252  32.401  31.847  1.00 91.15           C  
ANISOU 2572  C   ASP D  73    13033  11221  10380    294     47    -41       C  
ATOM   2573  O   ASP D  73      17.485  32.468  33.054  1.00 91.73           O  
ANISOU 2573  O   ASP D  73    13160  11305  10386    294     25    -60       O  
ATOM   2574  CB  ASP D  73      15.553  34.287  31.802  1.00 91.38           C  
ANISOU 2574  CB  ASP D  73    12956  11324  10441    310    120   -139       C  
ATOM   2575  CG  ASP D  73      16.524  35.387  31.384  1.00 90.97           C  
ANISOU 2575  CG  ASP D  73    12860  11226  10480    364     64   -158       C  
ATOM   2576  OD1 ASP D  73      17.753  35.166  31.315  1.00 90.80           O  
ANISOU 2576  OD1 ASP D  73    12861  11153  10485    382      6   -132       O  
ATOM   2577  OD2 ASP D  73      16.027  36.491  31.087  1.00 90.92           O  
ANISOU 2577  OD2 ASP D  73    12790  11232  10523    389     81   -201       O  
ATOM   2578  N   VAL D  74      18.100  31.852  30.979  1.00108.88           N  
ANISOU 2578  N   VAL D  74    15273  13414  12682    303     14      4       N  
ATOM   2579  CA  VAL D  74      19.371  31.304  31.438  1.00110.86           C  
ANISOU 2579  CA  VAL D  74    15579  13616  12925    317    -54     33       C  
ATOM   2580  C   VAL D  74      20.258  32.411  31.999  1.00109.81           C  
ANISOU 2580  C   VAL D  74    15432  13464  12826    363   -114    -11       C  
ATOM   2581  O   VAL D  74      20.835  32.274  33.083  1.00112.62           O  
ANISOU 2581  O   VAL D  74    15847  13815  13129    370   -160    -18       O  
ATOM   2582  CB  VAL D  74      20.059  30.529  30.299  1.00115.85           C  
ANISOU 2582  CB  VAL D  74    16198  14196  13623    317    -70     83       C  
ATOM   2583  CG1 VAL D  74      20.049  31.338  29.011  1.00114.89           C  
ANISOU 2583  CG1 VAL D  74    15993  14059  13601    339    -57     71       C  
ATOM   2584  CG2 VAL D  74      21.476  30.150  30.691  1.00117.70           C  
ANISOU 2584  CG2 VAL D  74    16472  14375  13874    342   -147    103       C  
ATOM   2585  N   ALA D  75      20.336  33.545  31.292  1.00111.24           N  
ANISOU 2585  N   ALA D  75    15539  13634  13094    394   -113    -44       N  
ATOM   2586  CA  ALA D  75      21.236  34.630  31.682  1.00111.97           C  
ANISOU 2586  CA  ALA D  75    15609  13698  13235    437   -168    -88       C  
ATOM   2587  C   ALA D  75      20.867  35.232  33.035  1.00111.85           C  
ANISOU 2587  C   ALA D  75    15625  13727  13147    439   -172   -140       C  
ATOM   2588  O   ALA D  75      21.755  35.625  33.802  1.00109.17           O  
ANISOU 2588  O   ALA D  75    15306  13367  12806    464   -232   -166       O  
ATOM   2589  CB  ALA D  75      21.242  35.716  30.603  1.00106.12           C  
ANISOU 2589  CB  ALA D  75    14786  12937  12599    465   -155   -110       C  
ATOM   2590  N   ASN D  76      19.574  35.328  33.340  1.00172.74           N  
ANISOU 2590  N   ASN D  76    23336  21497  20800    413   -107   -159       N  
ATOM   2591  CA  ASN D  76      19.107  35.894  34.599  1.00171.33           C  
ANISOU 2591  CA  ASN D  76    23186  21362  20548    410    -98   -213       C  
ATOM   2592  C   ASN D  76      18.839  34.844  35.665  1.00173.57           C  
ANISOU 2592  C   ASN D  76    23564  21677  20708    371    -88   -190       C  
ATOM   2593  O   ASN D  76      18.439  35.205  36.776  1.00175.75           O  
ANISOU 2593  O   ASN D  76    23876  21992  20909    362    -76   -233       O  
ATOM   2594  CB  ASN D  76      17.843  36.726  34.374  1.00173.28           C  
ANISOU 2594  CB  ASN D  76    23373  21655  20809    405    -29   -258       C  
ATOM   2595  CG  ASN D  76      18.045  37.825  33.354  1.00181.27           C  
ANISOU 2595  CG  ASN D  76    24300  22636  21939    445    -38   -279       C  
ATOM   2596  OD1 ASN D  76      18.834  37.683  32.419  1.00183.87           O  
ANISOU 2596  OD1 ASN D  76    24606  22914  22341    462    -69   -243       O  
ATOM   2597  ND2 ASN D  76      17.331  38.932  33.526  1.00189.26           N  
ANISOU 2597  ND2 ASN D  76    25265  23675  22971    460     -7   -337       N  
ATOM   2598  N   ASN D  77      19.056  33.562  35.355  1.00119.03           N  
ANISOU 2598  N   ASN D  77    16700  14748  13777    347    -92   -125       N  
ATOM   2599  CA  ASN D  77      18.903  32.471  36.319  1.00114.69           C  
ANISOU 2599  CA  ASN D  77    16250  14216  13111    310    -88    -93       C  
ATOM   2600  C   ASN D  77      17.487  32.466  36.896  1.00114.25           C  
ANISOU 2600  C   ASN D  77    16210  14227  12972    267     -2   -120       C  
ATOM   2601  O   ASN D  77      17.278  32.420  38.110  1.00116.05           O  
ANISOU 2601  O   ASN D  77    16508  14486  13101    250      4   -140       O  
ATOM   2602  CB  ASN D  77      19.961  32.577  37.422  1.00119.17           C  
ANISOU 2602  CB  ASN D  77    16881  14764  13634    335   -170   -104       C  
ATOM   2603  CG  ASN D  77      20.054  31.330  38.270  1.00120.15           C  
ANISOU 2603  CG  ASN D  77    17116  14888  13647    304   -183    -55       C  
ATOM   2604  OD1 ASN D  77      19.235  30.420  38.153  1.00122.09           O  
ANISOU 2604  OD1 ASN D  77    17394  15153  13841    258   -120    -18       O  
ATOM   2605  ND2 ASN D  77      21.052  31.287  39.147  1.00119.86           N  
ANISOU 2605  ND2 ASN D  77    17139  14828  13573    329   -266    -56       N  
ATOM   2606  N   THR D  78      16.506  32.535  36.000  1.00 93.71           N  
ANISOU 2606  N   THR D  78    13543  11648  10414    249     65   -124       N  
ATOM   2607  CA  THR D  78      15.099  32.638  36.355  1.00 95.23           C  
ANISOU 2607  CA  THR D  78    13726  11903  10553    211    152   -159       C  
ATOM   2608  C   THR D  78      14.295  31.614  35.572  1.00 97.90           C  
ANISOU 2608  C   THR D  78    14055  12252  10891    167    213   -116       C  
ATOM   2609  O   THR D  78      14.541  31.399  34.382  1.00100.03           O  
ANISOU 2609  O   THR D  78    14276  12490  11240    179    200    -84       O  
ATOM   2610  CB  THR D  78      14.549  34.043  36.058  1.00 98.11           C  
ANISOU 2610  CB  THR D  78    14000  12292  10986    240    174   -227       C  
ATOM   2611  OG1 THR D  78      15.387  35.031  36.671  1.00 98.68           O  
ANISOU 2611  OG1 THR D  78    14074  12346  11073    283    115   -268       O  
ATOM   2612  CG2 THR D  78      13.115  34.195  36.566  1.00 96.35           C  
ANISOU 2612  CG2 THR D  78    13766  12134  10708    203    263   -273       C  
ATOM   2613  N   LEU D  79      13.324  30.996  36.239  1.00137.37           N  
ANISOU 2613  N   LEU D  79    19099  17294  15800    114    282   -120       N  
ATOM   2614  CA  LEU D  79      12.384  30.079  35.610  1.00136.63           C  
ANISOU 2614  CA  LEU D  79    18992  17218  15703     66    351    -92       C  
ATOM   2615  C   LEU D  79      10.977  30.649  35.715  1.00139.62           C  
ANISOU 2615  C   LEU D  79    19313  17658  16077     42    434   -154       C  
ATOM   2616  O   LEU D  79      10.576  31.126  36.781  1.00144.73           O  
ANISOU 2616  O   LEU D  79    19987  18342  16662     32    463   -202       O  
ATOM   2617  CB  LEU D  79      12.441  28.694  36.255  1.00138.93           C  
ANISOU 2617  CB  LEU D  79    19390  17500  15896     16    368    -38       C  
ATOM   2618  CG  LEU D  79      11.695  27.592  35.498  1.00144.14           C  
ANISOU 2618  CG  LEU D  79    20040  18164  16562    -34    429     -1       C  
ATOM   2619  CD1 LEU D  79      11.881  27.678  33.994  1.00144.41           C  
ANISOU 2619  CD1 LEU D  79    19988  18172  16708     -8    407     16       C  
ATOM   2620  CD2 LEU D  79      12.069  26.222  36.017  1.00139.28           C  
ANISOU 2620  CD2 LEU D  79    19533  17518  15867    -72    426     64       C  
ATOM   2621  N   TYR D  80      10.238  30.602  34.612  1.00123.03           N  
ANISOU 2621  N   TYR D  80    17133  15570  14044     35    471   -157       N  
ATOM   2622  CA  TYR D  80       8.877  31.111  34.548  1.00124.96           C  
ANISOU 2622  CA  TYR D  80    17308  15870  14302     16    545   -216       C  
ATOM   2623  C   TYR D  80       7.915  29.971  34.254  1.00123.53           C  
ANISOU 2623  C   TYR D  80    17131  15712  14092    -47    618   -196       C  
ATOM   2624  O   TYR D  80       8.312  28.859  33.902  1.00126.02           O  
ANISOU 2624  O   TYR D  80    17493  15996  14392    -71    608   -133       O  
ATOM   2625  CB  TYR D  80       8.708  32.204  33.473  1.00125.66           C  
ANISOU 2625  CB  TYR D  80    17286  15956  14504     67    523   -248       C  
ATOM   2626  CG  TYR D  80       9.780  33.279  33.423  1.00120.62           C  
ANISOU 2626  CG  TYR D  80    16632  15280  13919    132    446   -258       C  
ATOM   2627  CD1 TYR D  80      11.042  33.011  32.908  1.00119.78           C  
ANISOU 2627  CD1 TYR D  80    16551  15115  13846    159    375   -204       C  
ATOM   2628  CD2 TYR D  80       9.526  34.564  33.887  1.00117.36           C  
ANISOU 2628  CD2 TYR D  80    16176  14886  13527    164    448   -326       C  
ATOM   2629  CE1 TYR D  80      12.017  33.984  32.859  1.00119.78           C  
ANISOU 2629  CE1 TYR D  80    16533  15079  13900    214    310   -218       C  
ATOM   2630  CE2 TYR D  80      10.498  35.543  33.845  1.00116.79           C  
ANISOU 2630  CE2 TYR D  80    16090  14777  13508    220    382   -338       C  
ATOM   2631  CZ  TYR D  80      11.742  35.247  33.329  1.00118.95           C  
ANISOU 2631  CZ  TYR D  80    16388  14994  13814    244    313   -284       C  
ATOM   2632  OH  TYR D  80      12.719  36.213  33.279  1.00116.93           O  
ANISOU 2632  OH  TYR D  80    16115  14699  13616    296    250   -300       O  
ATOM   2633  N   LEU D  81       6.632  30.277  34.417  1.00 99.82           N  
ANISOU 2633  N   LEU D  81    14077  12764  11088    -74    694   -254       N  
ATOM   2634  CA  LEU D  81       5.540  29.417  33.985  1.00104.25           C  
ANISOU 2634  CA  LEU D  81    14611  13353  11645   -130    768   -252       C  
ATOM   2635  C   LEU D  81       4.268  30.238  34.090  1.00105.54           C  
ANISOU 2635  C   LEU D  81    14689  13574  11839   -134    831   -335       C  
ATOM   2636  O   LEU D  81       3.988  30.802  35.152  1.00108.46           O  
ANISOU 2636  O   LEU D  81    15077  13972  12160   -140    863   -386       O  
ATOM   2637  CB  LEU D  81       5.441  28.153  34.848  1.00105.95           C  
ANISOU 2637  CB  LEU D  81    14932  13570  11756   -198    818   -217       C  
ATOM   2638  N   GLN D  82       3.519  30.337  32.994  1.00138.37           N  
ANISOU 2638  N   GLN D  82    18750  17747  16076   -130    845   -352       N  
ATOM   2639  CA  GLN D  82       2.271  31.095  32.989  1.00143.15           C  
ANISOU 2639  CA  GLN D  82    19262  18404  16722   -130    900   -432       C  
ATOM   2640  C   GLN D  82       1.154  30.144  32.582  1.00144.67           C  
ANISOU 2640  C   GLN D  82    19423  18629  16917   -192    972   -439       C  
ATOM   2641  O   GLN D  82       1.091  29.696  31.431  1.00147.61           O  
ANISOU 2641  O   GLN D  82    19754  18988  17343   -189    950   -408       O  
ATOM   2642  CB  GLN D  82       2.345  32.324  32.069  1.00146.31           C  
ANISOU 2642  CB  GLN D  82    19567  18796  17229    -56    841   -458       C  
ATOM   2643  CG  GLN D  82       1.045  32.752  31.420  1.00149.10           C  
ANISOU 2643  CG  GLN D  82    19807  19191  17654    -53    879   -517       C  
ATOM   2644  CD  GLN D  82       1.234  33.862  30.397  1.00149.09           C  
ANISOU 2644  CD  GLN D  82    19724  19169  17753     22    811   -526       C  
ATOM   2645  OE1 GLN D  82       2.351  34.320  30.145  1.00147.24           O  
ANISOU 2645  OE1 GLN D  82    19518  18889  17538     69    740   -488       O  
ATOM   2646  NE2 GLN D  82       0.129  34.326  29.828  1.00152.11           N  
ANISOU 2646  NE2 GLN D  82    20006  19586  18202     34    832   -578       N  
ATOM   2647  N   MET D  83       0.303  29.816  33.546  1.00149.98           N  
ANISOU 2647  N   MET D  83    20117  19342  17527   -250   1062   -482       N  
ATOM   2648  CA  MET D  83      -0.900  29.039  33.303  1.00156.91           C  
ANISOU 2648  CA  MET D  83    20952  20256  18410   -314   1144   -506       C  
ATOM   2649  C   MET D  83      -1.978  29.886  32.633  1.00156.51           C  
ANISOU 2649  C   MET D  83    20766  20245  18456   -287   1159   -581       C  
ATOM   2650  O   MET D  83      -2.140  31.067  32.946  1.00158.25           O  
ANISOU 2650  O   MET D  83    20938  20482  18708   -242   1149   -638       O  
ATOM   2651  CB  MET D  83      -1.413  28.462  34.623  1.00164.48           C  
ANISOU 2651  CB  MET D  83    21985  21242  19268   -387   1240   -530       C  
ATOM   2652  CG  MET D  83      -0.332  27.781  35.490  1.00166.03           C  
ANISOU 2652  CG  MET D  83    22327  21399  19359   -406   1220   -460       C  
ATOM   2653  SD  MET D  83       0.750  28.818  36.491  1.00159.53           S  
ANISOU 2653  SD  MET D  83    21568  20558  18487   -348   1156   -465       S  
ATOM   2654  CE  MET D  83      -0.473  29.586  37.537  1.00156.80           C  
ANISOU 2654  CE  MET D  83    21184  20278  18114   -378   1257   -573       C  
ATOM   2655  N   ASN D  84      -2.719  29.277  31.705  1.00141.40           N  
ANISOU 2655  N   ASN D  84    18788  18345  16591   -314   1180   -583       N  
ATOM   2656  CA  ASN D  84      -3.746  29.979  30.940  1.00141.39           C  
ANISOU 2656  CA  ASN D  84    18655  18381  16688   -286   1183   -649       C  
ATOM   2657  C   ASN D  84      -5.023  29.147  30.918  1.00146.44           C  
ANISOU 2657  C   ASN D  84    19249  19063  17330   -360   1274   -692       C  
ATOM   2658  O   ASN D  84      -4.968  27.933  30.701  1.00149.56           O  
ANISOU 2658  O   ASN D  84    19691  19445  17689   -415   1299   -646       O  
ATOM   2659  CB  ASN D  84      -3.275  30.257  29.503  1.00142.48           C  
ANISOU 2659  CB  ASN D  84    18743  18488  16904   -226   1088   -608       C  
ATOM   2660  CG  ASN D  84      -2.047  31.154  29.450  1.00140.05           C  
ANISOU 2660  CG  ASN D  84    18470  18136  16606   -153   1001   -572       C  
ATOM   2661  OD1 ASN D  84      -1.905  32.083  30.243  1.00140.67           O  
ANISOU 2661  OD1 ASN D  84    18553  18220  16676   -123   1001   -610       O  
ATOM   2662  ND2 ASN D  84      -1.148  30.872  28.510  1.00139.51           N  
ANISOU 2662  ND2 ASN D  84    18425  18023  16558   -126    930   -502       N  
ATOM   2663  N   SER D  85      -6.168  29.801  31.138  1.00190.29           N  
ANISOU 2663  N   SER D  85    24708  24665  22930   -361   1326   -784       N  
ATOM   2664  CA  SER D  85      -7.481  29.147  31.074  1.00195.30           C  
ANISOU 2664  CA  SER D  85    25276  25343  23585   -427   1414   -840       C  
ATOM   2665  C   SER D  85      -7.532  27.895  31.948  1.00198.62           C  
ANISOU 2665  C   SER D  85    25796  25763  23907   -521   1505   -815       C  
ATOM   2666  O   SER D  85      -8.048  26.848  31.547  1.00200.52           O  
ANISOU 2666  O   SER D  85    26028  26010  24150   -581   1548   -806       O  
ATOM   2667  CB  SER D  85      -7.857  28.812  29.630  1.00196.84           C  
ANISOU 2667  CB  SER D  85    25389  25540  23861   -414   1368   -829       C  
ATOM   2668  OG  SER D  85      -7.340  27.544  29.257  1.00200.25           O  
ANISOU 2668  OG  SER D  85    25896  25941  24248   -460   1365   -752       O  
ATOM   2669  N   LEU D  86      -6.988  28.002  33.157  1.00183.63           N  
ANISOU 2669  N   LEU D  86    23998  23855  21919   -535   1532   -803       N  
ATOM   2670  CA  LEU D  86      -6.992  26.889  34.091  1.00184.00           C  
ANISOU 2670  CA  LEU D  86    24154  23897  21862   -621   1616   -776       C  
ATOM   2671  C   LEU D  86      -8.361  26.757  34.756  1.00186.72           C  
ANISOU 2671  C   LEU D  86    24449  24295  22203   -691   1744   -866       C  
ATOM   2672  O   LEU D  86      -9.235  27.619  34.630  1.00185.69           O  
ANISOU 2672  O   LEU D  86    24201  24204  22148   -667   1764   -954       O  
ATOM   2673  CB  LEU D  86      -5.900  27.072  35.143  1.00183.09           C  
ANISOU 2673  CB  LEU D  86    24167  23752  21646   -607   1592   -730       C  
ATOM   2674  N   LYS D  87      -8.541  25.650  35.475  1.00219.20           N  
ANISOU 2674  N   LYS D  87    28652  28404  26230   -779   1833   -844       N  
ATOM   2675  CA  LYS D  87      -9.796  25.384  36.166  1.00220.83           C  
ANISOU 2675  CA  LYS D  87    28825  28656  26424   -858   1968   -926       C  
ATOM   2676  C   LYS D  87      -9.541  25.094  37.638  1.00220.40           C  
ANISOU 2676  C   LYS D  87    28907  28598  26238   -913   2044   -914       C  
ATOM   2677  O   LYS D  87      -8.431  25.310  38.135  1.00219.15           O  
ANISOU 2677  O   LYS D  87    28853  28407  26007   -877   1982   -854       O  
ATOM   2678  CB  LYS D  87     -10.534  24.215  35.509  1.00220.89           C  
ANISOU 2678  CB  LYS D  87    28796  28668  26465   -928   2023   -923       C  
ATOM   2679  N   HIS D  88     -10.569  24.620  38.348  1.00199.12           N  
ANISOU 2679  N   HIS D  88    26211  25934  23510  -1001   2179   -972       N  
ATOM   2680  CA  HIS D  88     -10.396  24.266  39.753  1.00196.75           C  
ANISOU 2680  CA  HIS D  88    26050  25630  23075  -1062   2261   -960       C  
ATOM   2681  C   HIS D  88      -9.393  23.133  39.928  1.00194.91           C  
ANISOU 2681  C   HIS D  88    25973  25340  22742  -1090   2231   -841       C  
ATOM   2682  O   HIS D  88      -8.770  23.016  40.989  1.00196.52           O  
ANISOU 2682  O   HIS D  88    26314  25526  22827  -1105   2242   -802       O  
ATOM   2683  CB  HIS D  88     -11.741  23.882  40.370  1.00197.05           C  
ANISOU 2683  CB  HIS D  88    26055  25712  23104  -1158   2421  -1045       C  
ATOM   2684  N   GLU D  89      -9.227  22.291  38.904  1.00148.16           N  
ANISOU 2684  N   GLU D  89    20036  19390  16869  -1095   2190   -784       N  
ATOM   2685  CA  GLU D  89      -8.269  21.194  38.989  1.00148.97           C  
ANISOU 2685  CA  GLU D  89    20278  19433  16890  -1117   2157   -672       C  
ATOM   2686  C   GLU D  89      -6.854  21.709  39.217  1.00151.12           C  
ANISOU 2686  C   GLU D  89    20636  19668  17114  -1038   2036   -604       C  
ATOM   2687  O   GLU D  89      -6.064  21.082  39.933  1.00152.27           O  
ANISOU 2687  O   GLU D  89    20928  19774  17152  -1058   2027   -530       O  
ATOM   2688  CB  GLU D  89      -8.331  20.348  37.718  1.00149.17           C  
ANISOU 2688  CB  GLU D  89    20251  19435  16993  -1126   2125   -634       C  
ATOM   2689  N   ASP D  90      -6.515  22.851  38.616  1.00150.40           N  
ANISOU 2689  N   ASP D  90    20455  19587  17103   -947   1942   -630       N  
ATOM   2690  CA  ASP D  90      -5.171  23.402  38.736  1.00148.15           C  
ANISOU 2690  CA  ASP D  90    20234  19266  16789   -870   1825   -572       C  
ATOM   2691  C   ASP D  90      -4.916  24.072  40.082  1.00146.40           C  
ANISOU 2691  C   ASP D  90    20092  19059  16474   -865   1845   -599       C  
ATOM   2692  O   ASP D  90      -3.754  24.330  40.415  1.00144.90           O  
ANISOU 2692  O   ASP D  90    19984  18836  16234   -816   1758   -546       O  
ATOM   2693  CB  ASP D  90      -4.916  24.398  37.602  1.00146.87           C  
ANISOU 2693  CB  ASP D  90    19949  19106  16747   -778   1722   -591       C  
ATOM   2694  N   THR D  91      -5.961  24.349  40.862  1.00157.31           N  
ANISOU 2694  N   THR D  91    21450  20490  17830   -916   1958   -682       N  
ATOM   2695  CA  THR D  91      -5.799  25.046  42.135  1.00157.09           C  
ANISOU 2695  CA  THR D  91    21492  20482  17714   -914   1984   -718       C  
ATOM   2696  C   THR D  91      -5.015  24.182  43.119  1.00158.67           C  
ANISOU 2696  C   THR D  91    21877  20645  17766   -954   1988   -637       C  
ATOM   2697  O   THR D  91      -5.469  23.096  43.495  1.00164.93           O  
ANISOU 2697  O   THR D  91    22742  21431  18494  -1039   2079   -613       O  
ATOM   2698  CB  THR D  91      -7.166  25.404  42.717  1.00158.24           C  
ANISOU 2698  CB  THR D  91    21571  20686  17866   -970   2118   -828       C  
ATOM   2699  OG1 THR D  91      -8.078  25.713  41.656  1.00160.08           O  
ANISOU 2699  OG1 THR D  91    21637  20947  18238   -956   2130   -890       O  
ATOM   2700  CG2 THR D  91      -7.055  26.603  43.646  1.00161.15           C  
ANISOU 2700  CG2 THR D  91    21949  21083  18199   -935   2119   -892       C  
ATOM   2701  N   ALA D  92      -3.849  24.669  43.542  1.00146.02           N  
ANISOU 2701  N   ALA D  92    20352  19017  16114   -894   1890   -597       N  
ATOM   2702  CA  ALA D  92      -2.988  23.972  44.498  1.00148.08           C  
ANISOU 2702  CA  ALA D  92    20790  19241  16234   -918   1872   -519       C  
ATOM   2703  C   ALA D  92      -1.839  24.901  44.880  1.00149.69           C  
ANISOU 2703  C   ALA D  92    21031  19430  16413   -836   1757   -508       C  
ATOM   2704  O   ALA D  92      -1.721  26.019  44.370  1.00148.97           O  
ANISOU 2704  O   ALA D  92    20832  19353  16415   -766   1698   -556       O  
ATOM   2705  CB  ALA D  92      -2.454  22.653  43.932  1.00149.29           C  
ANISOU 2705  CB  ALA D  92    21009  19338  16378   -938   1838   -416       C  
ATOM   2706  N   VAL D  93      -0.987  24.421  45.785  1.00253.42           N  
ANISOU 2706  N   VAL D  93    34326  32537  29426   -845   1724   -444       N  
ATOM   2707  CA  VAL D  93       0.242  25.127  46.132  1.00252.55           C  
ANISOU 2707  CA  VAL D  93    34264  32404  29289   -769   1602   -422       C  
ATOM   2708  C   VAL D  93       1.294  24.835  45.072  1.00249.15           C  
ANISOU 2708  C   VAL D  93    33812  31919  28937   -707   1477   -344       C  
ATOM   2709  O   VAL D  93       1.373  23.721  44.541  1.00249.45           O  
ANISOU 2709  O   VAL D  93    33879  31920  28981   -736   1480   -276       O  
ATOM   2710  CB  VAL D  93       0.727  24.717  47.534  1.00254.99           C  
ANISOU 2710  CB  VAL D  93    34752  32704  29431   -802   1611   -387       C  
ATOM   2711  N   TYR D  94       2.107  25.841  44.754  1.00159.99           N  
ANISOU 2711  N   TYR D  94    22466  20616  17706   -622   1371   -357       N  
ATOM   2712  CA  TYR D  94       3.075  25.759  43.667  1.00156.57           C  
ANISOU 2712  CA  TYR D  94    21992  20133  17364   -559   1257   -298       C  
ATOM   2713  C   TYR D  94       4.434  26.196  44.186  1.00155.62           C  
ANISOU 2713  C   TYR D  94    21945  19980  17203   -497   1141   -267       C  
ATOM   2714  O   TYR D  94       4.548  27.255  44.807  1.00159.22           O  
ANISOU 2714  O   TYR D  94    22392  20463  17643   -466   1124   -327       O  
ATOM   2715  CB  TYR D  94       2.646  26.650  42.497  1.00157.45           C  
ANISOU 2715  CB  TYR D  94    21936  20264  17622   -513   1243   -352       C  
ATOM   2716  CG  TYR D  94       1.528  26.066  41.671  1.00159.01           C  
ANISOU 2716  CG  TYR D  94    22053  20481  17883   -561   1325   -365       C  
ATOM   2717  CD1 TYR D  94       1.722  24.926  40.907  1.00159.85           C  
ANISOU 2717  CD1 TYR D  94    22177  20549  18010   -584   1313   -293       C  
ATOM   2718  CD2 TYR D  94       0.262  26.637  41.686  1.00160.08           C  
ANISOU 2718  CD2 TYR D  94    22092  20672  18057   -587   1416   -455       C  
ATOM   2719  CE1 TYR D  94       0.694  24.387  40.156  1.00161.07           C  
ANISOU 2719  CE1 TYR D  94    22256  20723  18222   -630   1387   -310       C  
ATOM   2720  CE2 TYR D  94      -0.774  26.101  40.943  1.00160.32           C  
ANISOU 2720  CE2 TYR D  94    22044  20722  18149   -631   1488   -473       C  
ATOM   2721  CZ  TYR D  94      -0.551  24.973  40.181  1.00161.54           C  
ANISOU 2721  CZ  TYR D  94    22219  20840  18321   -654   1473   -400       C  
ATOM   2722  OH  TYR D  94      -1.571  24.425  39.436  1.00163.76           O  
ANISOU 2722  OH  TYR D  94    22420  21140  18662   -699   1541   -421       O  
ATOM   2723  N   TYR D  95       5.462  25.391  43.930  1.00129.36           N  
ANISOU 2723  N   TYR D  95    18689  16597  13865   -479   1060   -179       N  
ATOM   2724  CA  TYR D  95       6.809  25.714  44.384  1.00128.60           C  
ANISOU 2724  CA  TYR D  95    18660  16465  13737   -420    942   -148       C  
ATOM   2725  C   TYR D  95       7.811  25.316  43.314  1.00123.09           C  
ANISOU 2725  C   TYR D  95    17934  15708  13128   -371    843    -81       C  
ATOM   2726  O   TYR D  95       7.741  24.209  42.774  1.00119.83           O  
ANISOU 2726  O   TYR D  95    17542  15265  12724   -403    861    -21       O  
ATOM   2727  CB  TYR D  95       7.136  25.006  45.706  1.00129.54           C  
ANISOU 2727  CB  TYR D  95    18948  16573  13699   -458    947   -107       C  
ATOM   2728  N   CYS D  96       8.737  26.219  43.007  1.00159.55           N  
ANISOU 2728  N   CYS D  96    22502  20307  17813   -297    744    -94       N  
ATOM   2729  CA  CYS D  96       9.810  25.886  42.086  1.00156.71           C  
ANISOU 2729  CA  CYS D  96    22122  19887  17532   -249    648    -34       C  
ATOM   2730  C   CYS D  96      10.785  24.916  42.744  1.00155.49           C  
ANISOU 2730  C   CYS D  96    22104  19683  17292   -252    585     42       C  
ATOM   2731  O   CYS D  96      10.974  24.918  43.963  1.00156.54           O  
ANISOU 2731  O   CYS D  96    22340  19826  17311   -262    577     40       O  
ATOM   2732  CB  CYS D  96      10.547  27.149  41.637  1.00155.89           C  
ANISOU 2732  CB  CYS D  96    21932  19774  17524   -172    564    -73       C  
ATOM   2733  SG  CYS D  96      11.854  27.685  42.761  1.00161.16           S  
ANISOU 2733  SG  CYS D  96    22687  20420  18126   -122    457    -75       S  
ATOM   2734  N   ALA D  97      11.393  24.067  41.922  1.00104.15           N  
ANISOU 2734  N   ALA D  97    15602  13127  10843   -241    540    110       N  
ATOM   2735  CA  ALA D  97      12.408  23.126  42.375  1.00104.32           C  
ANISOU 2735  CA  ALA D  97    15740  13092  10805   -233    468    186       C  
ATOM   2736  C   ALA D  97      13.730  23.460  41.702  1.00100.81           C  
ANISOU 2736  C   ALA D  97    15249  12596  10457   -159    348    205       C  
ATOM   2737  O   ALA D  97      13.798  23.550  40.472  1.00 99.73           O  
ANISOU 2737  O   ALA D  97    15014  12444  10436   -139    341    207       O  
ATOM   2738  CB  ALA D  97      12.002  21.684  42.070  1.00109.12           C  
ANISOU 2738  CB  ALA D  97    16400  13672  11388   -291    523    252       C  
ATOM   2739  N   ALA D  98      14.773  23.637  42.505  1.00110.75           N  
ANISOU 2739  N   ALA D  98    16580  13830  11669   -119    255    217       N  
ATOM   2740  CA  ALA D  98      16.085  24.011  42.001  1.00107.82           C  
ANISOU 2740  CA  ALA D  98    16167  13411  11388    -48    140    226       C  
ATOM   2741  C   ALA D  98      16.883  22.753  41.669  1.00106.61           C  
ANISOU 2741  C   ALA D  98    16072  13190  11246    -44     86    310       C  
ATOM   2742  O   ALA D  98      16.343  21.647  41.628  1.00114.49           O  
ANISOU 2742  O   ALA D  98    17125  14178  12200    -96    145    358       O  
ATOM   2743  CB  ALA D  98      16.804  24.895  43.014  1.00111.96           C  
ANISOU 2743  CB  ALA D  98    16730  13945  11867     -5     63    188       C  
ATOM   2744  N   ARG D  99      18.184  22.905  41.423  1.00 98.05           N  
ANISOU 2744  N   ARG D  99    14973  12055  10227     17    -24    324       N  
ATOM   2745  CA  ARG D  99      19.033  21.766  41.106  1.00 98.02           C  
ANISOU 2745  CA  ARG D  99    15017  11981  10245     29    -83    398       C  
ATOM   2746  C   ARG D  99      20.419  21.961  41.704  1.00 98.36           C  
ANISOU 2746  C   ARG D  99    15103  11982  10287     90   -212    406       C  
ATOM   2747  O   ARG D  99      20.836  23.080  42.011  1.00 98.33           O  
ANISOU 2747  O   ARG D  99    15059  11998  10303    130   -261    350       O  
ATOM   2748  CB  ARG D  99      19.151  21.544  39.596  1.00 96.99           C  
ANISOU 2748  CB  ARG D  99    14783  11820  10248     37    -70    411       C  
ATOM   2749  N   ALA D 100      21.128  20.846  41.857  1.00190.76           N  
ANISOU 2749  N   ALA D 100    26885  23625  21970     97   -269    474       N  
ATOM   2750  CA  ALA D 100      22.469  20.881  42.419  1.00192.65           C  
ANISOU 2750  CA  ALA D 100    27168  23819  22210    156   -400    486       C  
ATOM   2751  C   ALA D 100      23.406  21.657  41.495  1.00190.00           C  
ANISOU 2751  C   ALA D 100    26710  23456  22024    215   -465    449       C  
ATOM   2752  O   ALA D 100      23.290  21.562  40.267  1.00189.14           O  
ANISOU 2752  O   ALA D 100    26511  23332  22021    211   -425    452       O  
ATOM   2753  CB  ALA D 100      22.999  19.463  42.634  1.00194.48           C  
ANISOU 2753  CB  ALA D 100    27502  23986  22406    153   -445    570       C  
ATOM   2754  N   PRO D 101      24.332  22.443  42.050  1.00151.80           N  
ANISOU 2754  N   PRO D 101    21866  18612  17199    269   -562    411       N  
ATOM   2755  CA  PRO D 101      25.208  23.258  41.194  1.00152.95           C  
ANISOU 2755  CA  PRO D 101    21893  18732  17490    321   -616    370       C  
ATOM   2756  C   PRO D 101      26.143  22.445  40.320  1.00152.88           C  
ANISOU 2756  C   PRO D 101    21856  18648  17584    347   -667    415       C  
ATOM   2757  O   PRO D 101      26.445  22.880  39.202  1.00156.27           O  
ANISOU 2757  O   PRO D 101    22176  19060  18140    365   -658    393       O  
ATOM   2758  CB  PRO D 101      25.986  24.109  42.207  1.00154.42           C  
ANISOU 2758  CB  PRO D 101    22102  18926  17645    367   -712    323       C  
ATOM   2759  CG  PRO D 101      25.106  24.140  43.414  1.00158.24           C  
ANISOU 2759  CG  PRO D 101    22686  19466  17971    329   -670    317       C  
ATOM   2760  CD  PRO D 101      24.507  22.767  43.473  1.00153.00           C  
ANISOU 2760  CD  PRO D 101    22113  18789  17232    280   -615    394       C  
ATOM   2761  N   VAL D 102      26.619  21.296  40.791  1.00108.11           N  
ANISOU 2761  N   VAL D 102    16281  12932  11865    350   -720    478       N  
ATOM   2762  CA  VAL D 102      27.512  20.445  40.002  1.00110.45           C  
ANISOU 2762  CA  VAL D 102    16553  13152  12260    374   -768    520       C  
ATOM   2763  C   VAL D 102      27.696  19.072  40.658  1.00116.65           C  
ANISOU 2763  C   VAL D 102    17464  13894  12962    365   -805    596       C  
ATOM   2764  O   VAL D 102      27.470  18.031  40.030  1.00112.95           O  
ANISOU 2764  O   VAL D 102    17009  13391  12517    338   -762    648       O  
ATOM   2765  CB  VAL D 102      28.886  21.131  39.773  1.00106.54           C  
ANISOU 2765  CB  VAL D 102    15982  12618  11881    442   -875    479       C  
ATOM   2766  CG1 VAL D 102      29.431  21.718  41.070  1.00101.77           C  
ANISOU 2766  CG1 VAL D 102    15435  12028  11204    478   -969    448       C  
ATOM   2767  CG2 VAL D 102      29.876  20.151  39.155  1.00109.62           C  
ANISOU 2767  CG2 VAL D 102    16362  12925  12362    470   -933    522       C  
ATOM   2768  N   ASP D 110      16.548  14.199  41.322  1.00196.28           N  
ANISOU 2768  N   ASP D 110    27911  24263  22401   -278    221    753       N  
ATOM   2769  CA  ASP D 110      16.959  14.473  42.696  1.00196.69           C  
ANISOU 2769  CA  ASP D 110    28075  24322  22336   -259    166    760       C  
ATOM   2770  C   ASP D 110      17.194  15.965  42.932  1.00193.81           C  
ANISOU 2770  C   ASP D 110    27639  24010  21989   -211    122    685       C  
ATOM   2771  O   ASP D 110      18.303  16.381  43.274  1.00192.18           O  
ANISOU 2771  O   ASP D 110    27448  23779  21794   -146      7    686       O  
ATOM   2772  CB  ASP D 110      18.222  13.680  43.039  1.00198.36           C  
ANISOU 2772  CB  ASP D 110    28380  24452  22535   -213     49    832       C  
ATOM   2773  CG  ASP D 110      19.344  13.916  42.048  1.00199.94           C  
ANISOU 2773  CG  ASP D 110    28481  24608  22880   -143    -48    827       C  
ATOM   2774  OD1 ASP D 110      19.114  14.623  41.044  1.00196.91           O  
ANISOU 2774  OD1 ASP D 110    27962  24254  22600   -134    -18    775       O  
ATOM   2775  OD2 ASP D 110      20.460  13.402  42.277  1.00200.91           O  
ANISOU 2775  OD2 ASP D 110    28661  24665  23011    -96   -153    874       O  
ATOM   2776  N   TYR D 111      16.143  16.763  42.745  1.00156.24           N  
ANISOU 2776  N   TYR D 111    22803  19323  17239   -242    213    619       N  
ATOM   2777  CA  TYR D 111      16.233  18.195  42.996  1.00149.69           C  
ANISOU 2777  CA  TYR D 111    21906  18544  16424   -203    185    544       C  
ATOM   2778  C   TYR D 111      16.614  18.449  44.448  1.00150.10           C  
ANISOU 2778  C   TYR D 111    22076  18606  16347   -190    135    544       C  
ATOM   2779  O   TYR D 111      15.989  17.919  45.370  1.00153.64           O  
ANISOU 2779  O   TYR D 111    22637  19071  16669   -245    195    565       O  
ATOM   2780  CB  TYR D 111      14.904  18.872  42.668  1.00146.70           C  
ANISOU 2780  CB  TYR D 111    21438  18238  16063   -246    301    476       C  
ATOM   2781  CG  TYR D 111      14.566  18.862  41.195  1.00146.49           C  
ANISOU 2781  CG  TYR D 111    21282  18210  16169   -248    337    465       C  
ATOM   2782  CD1 TYR D 111      15.546  19.087  40.236  1.00146.29           C  
ANISOU 2782  CD1 TYR D 111    21180  18142  16262   -188    253    473       C  
ATOM   2783  CD2 TYR D 111      13.268  18.634  40.763  1.00145.84           C  
ANISOU 2783  CD2 TYR D 111    21154  18167  16093   -310    455    443       C  
ATOM   2784  CE1 TYR D 111      15.243  19.084  38.888  1.00145.65           C  
ANISOU 2784  CE1 TYR D 111    20988  18059  16293   -190    285    462       C  
ATOM   2785  CE2 TYR D 111      12.953  18.630  39.417  1.00146.53           C  
ANISOU 2785  CE2 TYR D 111    21125  18253  16296   -310    482    431       C  
ATOM   2786  CZ  TYR D 111      13.945  18.855  38.483  1.00146.94           C  
ANISOU 2786  CZ  TYR D 111    21111  18265  16456   -250    396    442       C  
ATOM   2787  OH  TYR D 111      13.643  18.850  37.139  1.00143.16           O  
ANISOU 2787  OH  TYR D 111    20525  17786  16085   -251    422    432       O  
ATOM   2788  N   ASP D 112      17.640  19.272  44.648  1.00174.40           N  
ANISOU 2788  N   ASP D 112    25131  21676  19458   -121     25    517       N  
ATOM   2789  CA  ASP D 112      18.266  19.393  45.958  1.00178.51           C  
ANISOU 2789  CA  ASP D 112    25769  22193  19865    -98    -52    525       C  
ATOM   2790  C   ASP D 112      17.684  20.516  46.805  1.00179.69           C  
ANISOU 2790  C   ASP D 112    25919  22416  19941   -108    -13    449       C  
ATOM   2791  O   ASP D 112      17.626  20.384  48.034  1.00181.54           O  
ANISOU 2791  O   ASP D 112    26277  22664  20034   -127    -19    458       O  
ATOM   2792  CB  ASP D 112      19.774  19.594  45.790  1.00177.38           C  
ANISOU 2792  CB  ASP D 112    25605  21996  19795    -16   -201    537       C  
ATOM   2793  CG  ASP D 112      20.380  18.624  44.791  1.00182.33           C  
ANISOU 2793  CG  ASP D 112    26206  22552  20522      0   -237    599       C  
ATOM   2794  OD1 ASP D 112      19.955  18.647  43.616  1.00180.18           O  
ANISOU 2794  OD1 ASP D 112    25825  22282  20354    -14   -176    586       O  
ATOM   2795  OD2 ASP D 112      21.273  17.838  45.176  1.00187.43           O  
ANISOU 2795  OD2 ASP D 112    26939  23137  21140     27   -326    658       O  
ATOM   2796  N   TYR D 113      17.249  21.613  46.188  1.00120.26           N  
ANISOU 2796  N   TYR D 113    18259  14933  12502    -98     26    375       N  
ATOM   2797  CA  TYR D 113      16.714  22.762  46.906  1.00113.72           C  
ANISOU 2797  CA  TYR D 113    17415  14171  11622   -103     62    295       C  
ATOM   2798  C   TYR D 113      15.286  23.010  46.445  1.00114.62           C  
ANISOU 2798  C   TYR D 113    17453  14340  11759   -159    202    251       C  
ATOM   2799  O   TYR D 113      15.012  23.025  45.241  1.00116.20           O  
ANISOU 2799  O   TYR D 113    17540  14533  12076   -157    232    247       O  
ATOM   2800  CB  TYR D 113      17.570  24.019  46.694  1.00109.25           C  
ANISOU 2800  CB  TYR D 113    16757  13606  11146    -30    -30    236       C  
ATOM   2801  CG  TYR D 113      19.068  23.809  46.842  1.00111.46           C  
ANISOU 2801  CG  TYR D 113    17077  13826  11448     33   -176    273       C  
ATOM   2802  CD1 TYR D 113      19.801  23.122  45.877  1.00113.40           C  
ANISOU 2802  CD1 TYR D 113    17284  14008  11795     61   -229    327       C  
ATOM   2803  CD2 TYR D 113      19.746  24.281  47.960  1.00115.61           C  
ANISOU 2803  CD2 TYR D 113    17676  14358  11893     65   -260    250       C  
ATOM   2804  CE1 TYR D 113      21.166  22.924  46.017  1.00115.37           C  
ANISOU 2804  CE1 TYR D 113    17563  14201  12073    119   -361    356       C  
ATOM   2805  CE2 TYR D 113      21.112  24.088  48.110  1.00115.53           C  
ANISOU 2805  CE2 TYR D 113    17696  14292  11907    125   -398    279       C  
ATOM   2806  CZ  TYR D 113      21.817  23.408  47.135  1.00115.88           C  
ANISOU 2806  CZ  TYR D 113    17696  14273  12060    152   -448    332       C  
ATOM   2807  OH  TYR D 113      23.174  23.212  47.278  1.00113.04           O  
ANISOU 2807  OH  TYR D 113    17359  13857  11733    212   -584    356       O  
ATOM   2808  N   TRP D 114      14.381  23.201  47.399  1.00150.77           N  
ANISOU 2808  N   TRP D 114    22090  18971  16223   -209    286    215       N  
ATOM   2809  CA  TRP D 114      12.960  23.345  47.117  1.00153.81           C  
ANISOU 2809  CA  TRP D 114    22414  19409  16617   -269    425    171       C  
ATOM   2810  C   TRP D 114      12.462  24.656  47.704  1.00157.33           C  
ANISOU 2810  C   TRP D 114    22816  19919  17043   -263    460     75       C  
ATOM   2811  O   TRP D 114      12.686  24.937  48.886  1.00159.74           O  
ANISOU 2811  O   TRP D 114    23217  20242  17235   -264    438     57       O  
ATOM   2812  CB  TRP D 114      12.173  22.163  47.689  1.00157.82           C  
ANISOU 2812  CB  TRP D 114    23036  19918  17009   -350    520    218       C  
ATOM   2813  CG  TRP D 114      12.684  20.833  47.223  1.00158.23           C  
ANISOU 2813  CG  TRP D 114    23145  19903  17073   -356    485    314       C  
ATOM   2814  CD1 TRP D 114      13.790  20.176  47.679  1.00158.44           C  
ANISOU 2814  CD1 TRP D 114    23280  19871  17048   -325    381    384       C  
ATOM   2815  CD2 TRP D 114      12.108  19.994  46.214  1.00158.62           C  
ANISOU 2815  CD2 TRP D 114    23142  19932  17192   -395    552    346       C  
ATOM   2816  NE1 TRP D 114      13.941  18.983  47.014  1.00160.76           N  
ANISOU 2816  NE1 TRP D 114    23594  20109  17380   -341    382    458       N  
ATOM   2817  CE2 TRP D 114      12.921  18.847  46.110  1.00160.51           C  
ANISOU 2817  CE2 TRP D 114    23466  20100  17420   -386    488    437       C  
ATOM   2818  CE3 TRP D 114      10.985  20.101  45.388  1.00156.75           C  
ANISOU 2818  CE3 TRP D 114    22797  19733  17030   -435    658    306       C  
ATOM   2819  CZ2 TRP D 114      12.646  17.815  45.215  1.00162.15           C  
ANISOU 2819  CZ2 TRP D 114    23652  20271  17686   -418    529    486       C  
ATOM   2820  CZ3 TRP D 114      10.715  19.076  44.501  1.00157.64           C  
ANISOU 2820  CZ3 TRP D 114    22888  19812  17197   -467    695    354       C  
ATOM   2821  CH2 TRP D 114      11.542  17.949  44.420  1.00160.28           C  
ANISOU 2821  CH2 TRP D 114    23308  20074  17517   -460    633    443       C  
ATOM   2822  N   GLY D 115      11.783  25.453  46.877  1.00151.39           N  
ANISOU 2822  N   GLY D 115    21922  19199  16398   -257    513     13       N  
ATOM   2823  CA  GLY D 115      11.325  26.752  47.315  1.00155.61           C  
ANISOU 2823  CA  GLY D 115    22401  19789  16935   -246    543    -81       C  
ATOM   2824  C   GLY D 115      10.130  26.674  48.245  1.00156.43           C  
ANISOU 2824  C   GLY D 115    22561  19948  16926   -318    667   -122       C  
ATOM   2825  O   GLY D 115       9.416  25.673  48.300  1.00153.30           O  
ANISOU 2825  O   GLY D 115    22216  19554  16476   -384    752    -85       O  
ATOM   2826  N   GLN D 116       9.920  27.768  48.984  1.00160.32           N  
ANISOU 2826  N   GLN D 116    23043  20487  17386   -307    681   -203       N  
ATOM   2827  CA  GLN D 116       8.814  27.827  49.935  1.00163.05           C  
ANISOU 2827  CA  GLN D 116    23440  20888  17624   -374    802   -255       C  
ATOM   2828  C   GLN D 116       7.478  27.610  49.235  1.00164.49           C  
ANISOU 2828  C   GLN D 116    23530  21101  17869   -426    929   -281       C  
ATOM   2829  O   GLN D 116       6.652  26.804  49.679  1.00167.28           O  
ANISOU 2829  O   GLN D 116    23950  21471  18138   -502   1032   -268       O  
ATOM   2830  CB  GLN D 116       8.828  29.168  50.672  1.00159.57           C  
ANISOU 2830  CB  GLN D 116    22976  20489  17164   -346    792   -348       C  
ATOM   2831  N   GLY D 117       7.253  28.308  48.137  1.00185.21           N  
ANISOU 2831  N   GLY D 117    26001  23730  20640   -388    922   -320       N  
ATOM   2832  CA  GLY D 117       6.080  28.033  47.337  1.00185.72           C  
ANISOU 2832  CA  GLY D 117    25972  23818  20777   -430   1024   -338       C  
ATOM   2833  C   GLY D 117       4.961  29.034  47.559  1.00189.62           C  
ANISOU 2833  C   GLY D 117    26377  24372  21296   -446   1117   -445       C  
ATOM   2834  O   GLY D 117       4.850  29.670  48.614  1.00191.36           O  
ANISOU 2834  O   GLY D 117    26643  24625  21438   -453   1140   -503       O  
ATOM   2835  N   THR D 118       4.113  29.174  46.541  1.00220.62           N  
ANISOU 2835  N   THR D 118    30173  28315  25337   -451   1169   -475       N  
ATOM   2836  CA  THR D 118       2.945  30.042  46.574  1.00221.47           C  
ANISOU 2836  CA  THR D 118    30178  28478  25492   -465   1260   -576       C  
ATOM   2837  C   THR D 118       1.742  29.256  46.069  1.00223.53           C  
ANISOU 2837  C   THR D 118    30391  28760  25781   -531   1370   -579       C  
ATOM   2838  O   THR D 118       1.879  28.342  45.253  1.00223.17           O  
ANISOU 2838  O   THR D 118    30342  28681  25770   -542   1352   -510       O  
ATOM   2839  CB  THR D 118       3.160  31.302  45.717  1.00217.62           C  
ANISOU 2839  CB  THR D 118    29551  27987  25145   -385   1194   -624       C  
ATOM   2840  OG1 THR D 118       4.399  31.921  46.083  1.00217.26           O  
ANISOU 2840  OG1 THR D 118    29551  27914  25084   -324   1084   -612       O  
ATOM   2841  CG2 THR D 118       2.031  32.302  45.922  1.00219.43           C  
ANISOU 2841  CG2 THR D 118    29684  28272  25418   -392   1279   -734       C  
ATOM   2842  N   GLN D 119       0.559  29.608  46.569  1.00219.10           N  
ANISOU 2842  N   GLN D 119    29791  28252  25204   -578   1486   -664       N  
ATOM   2843  CA  GLN D 119      -0.679  28.924  46.213  1.00218.95           C  
ANISOU 2843  CA  GLN D 119    29722  28258  25210   -647   1601   -683       C  
ATOM   2844  C   GLN D 119      -1.520  29.840  45.331  1.00216.43           C  
ANISOU 2844  C   GLN D 119    29226  27970  25036   -614   1622   -764       C  
ATOM   2845  O   GLN D 119      -1.985  30.892  45.781  1.00218.87           O  
ANISOU 2845  O   GLN D 119    29480  28317  25364   -598   1656   -854       O  
ATOM   2846  CB  GLN D 119      -1.447  28.507  47.465  1.00220.39           C  
ANISOU 2846  CB  GLN D 119    29997  28476  25263   -733   1729   -718       C  
ATOM   2847  N   VAL D 120      -1.704  29.440  44.077  1.00143.18           N  
ANISOU 2847  N   VAL D 120    19864  18677  15862   -602   1599   -732       N  
ATOM   2848  CA  VAL D 120      -2.672  30.081  43.193  1.00143.13           C  
ANISOU 2848  CA  VAL D 120    19696  18701  15988   -583   1629   -803       C  
ATOM   2849  C   VAL D 120      -4.066  29.614  43.586  1.00145.17           C  
ANISOU 2849  C   VAL D 120    19928  19006  16225   -668   1774   -864       C  
ATOM   2850  O   VAL D 120      -4.323  28.409  43.688  1.00145.23           O  
ANISOU 2850  O   VAL D 120    20002  19005  16174   -739   1833   -818       O  
ATOM   2851  CB  VAL D 120      -2.371  29.752  41.722  1.00143.08           C  
ANISOU 2851  CB  VAL D 120    19616  18661  16087   -545   1553   -746       C  
ATOM   2852  CG1 VAL D 120      -3.631  29.875  40.875  1.00144.40           C  
ANISOU 2852  CG1 VAL D 120    19640  18863  16362   -558   1613   -807       C  
ATOM   2853  CG2 VAL D 120      -1.270  30.660  41.186  1.00140.35           C  
ANISOU 2853  CG2 VAL D 120    19243  18281  15804   -450   1424   -723       C  
ATOM   2854  N   THR D 121      -4.972  30.562  43.807  1.00226.41           N  
ANISOU 2854  N   THR D 121    30120  29340  26565   -663   1835   -969       N  
ATOM   2855  CA  THR D 121      -6.310  30.260  44.305  1.00229.87           C  
ANISOU 2855  CA  THR D 121    30528  29826  26986   -744   1980  -1044       C  
ATOM   2856  C   THR D 121      -7.336  30.856  43.350  1.00228.91           C  
ANISOU 2856  C   THR D 121    30227  29734  27016   -718   1999  -1121       C  
ATOM   2857  O   THR D 121      -7.550  32.072  43.342  1.00230.12           O  
ANISOU 2857  O   THR D 121    30292  29906  27238   -663   1981  -1196       O  
ATOM   2858  CB  THR D 121      -6.498  30.797  45.725  1.00233.27           C  
ANISOU 2858  CB  THR D 121    31026  30288  27318   -772   2053  -1110       C  
ATOM   2859  OG1 THR D 121      -5.266  30.675  46.450  1.00232.28           O  
ANISOU 2859  OG1 THR D 121    31049  30130  27076   -755   1982  -1041       O  
ATOM   2860  CG2 THR D 121      -7.581  30.016  46.452  1.00234.06           C  
ANISOU 2860  CG2 THR D 121    31163  30422  27348   -879   2210  -1150       C  
ATOM   2861  N   VAL D 122      -7.974  30.000  42.557  1.00161.54           N  
ANISOU 2861  N   VAL D 122    21641  21203  18534   -758   2035  -1105       N  
ATOM   2862  CA  VAL D 122      -8.972  30.406  41.577  1.00160.72           C  
ANISOU 2862  CA  VAL D 122    21368  21126  18572   -738   2047  -1172       C  
ATOM   2863  C   VAL D 122     -10.331  29.855  41.990  1.00163.56           C  
ANISOU 2863  C   VAL D 122    21689  21529  18926   -830   2196  -1245       C  
ATOM   2864  O   VAL D 122     -10.435  28.725  42.485  1.00166.97           O  
ANISOU 2864  O   VAL D 122    22219  21956  19267   -914   2272  -1207       O  
ATOM   2865  CB  VAL D 122      -8.582  29.949  40.154  1.00162.24           C  
ANISOU 2865  CB  VAL D 122    21514  21285  18844   -700   1952  -1099       C  
ATOM   2866  CG1 VAL D 122      -8.903  28.481  39.928  1.00163.76           C  
ANISOU 2866  CG1 VAL D 122    21752  21470  19001   -782   2011  -1049       C  
ATOM   2867  CG2 VAL D 122      -9.315  30.776  39.123  1.00162.49           C  
ANISOU 2867  CG2 VAL D 122    21375  21339  19025   -644   1921  -1165       C  
ATOM   2868  N   SER D 123     -11.365  30.678  41.826  1.00167.89           N  
ANISOU 2868  N   SER D 123    22096  22119  19575   -814   2241  -1354       N  
ATOM   2869  CA  SER D 123     -12.746  30.273  42.086  1.00170.66           C  
ANISOU 2869  CA  SER D 123    22378  22513  19950   -895   2381  -1440       C  
ATOM   2870  C   SER D 123     -13.704  31.362  41.607  1.00171.20           C  
ANISOU 2870  C   SER D 123    22268  22619  20162   -846   2386  -1553       C  
ATOM   2871  O   SER D 123     -14.910  31.138  41.484  1.00170.52           O  
ANISOU 2871  O   SER D 123    22083  22569  20139   -895   2478  -1632       O  
ATOM   2872  CB  SER D 123     -12.969  29.985  43.578  1.00169.26           C  
ANISOU 2872  CB  SER D 123    22315  22356  19641   -978   2508  -1471       C  
ATOM   2873  OG  SER D 123     -14.291  30.307  43.980  1.00166.56           O  
ANISOU 2873  OG  SER D 123    21874  22065  19348  -1024   2634  -1595       O  
TER    2874      SER D 123                                                      
ATOM   2875  N   ASP E1002      26.581 -11.473 -33.688  1.00166.47           N  
ANISOU 2875  N   ASP E1002    23240  19653  20357  -1997   2457  -1397       N  
ATOM   2876  CA  ASP E1002      27.782 -12.295 -33.592  1.00170.12           C  
ANISOU 2876  CA  ASP E1002    23670  20000  20966  -2008   2555  -1448       C  
ATOM   2877  C   ASP E1002      28.337 -12.277 -32.170  1.00170.73           C  
ANISOU 2877  C   ASP E1002    23676  20004  21192  -1942   2528  -1382       C  
ATOM   2878  O   ASP E1002      29.107 -13.158 -31.789  1.00173.97           O  
ANISOU 2878  O   ASP E1002    24042  20316  21744  -1943   2583  -1416       O  
ATOM   2879  CB  ASP E1002      28.845 -11.818 -34.583  1.00171.24           C  
ANISOU 2879  CB  ASP E1002    23864  20115  21083  -2029   2652  -1486       C  
ATOM   2880  N   LEU E1003      27.923 -11.271 -31.396  1.00132.51           N  
ANISOU 2880  N   LEU E1003    18822  15209  16315  -1885   2440  -1289       N  
ATOM   2881  CA  LEU E1003      28.310 -11.109 -29.996  1.00135.20           C  
ANISOU 2881  CA  LEU E1003    19100  15496  16774  -1818   2398  -1217       C  
ATOM   2882  C   LEU E1003      29.810 -11.284 -29.771  1.00138.37           C  
ANISOU 2882  C   LEU E1003    19472  15785  17319  -1797   2476  -1235       C  
ATOM   2883  O   LEU E1003      30.626 -10.796 -30.561  1.00137.66           O  
ANISOU 2883  O   LEU E1003    19414  15680  17212  -1810   2546  -1264       O  
ATOM   2884  CB  LEU E1003      27.530 -12.093 -29.120  1.00132.73           C  
ANISOU 2884  CB  LEU E1003    18741  15172  16519  -1820   2348  -1211       C  
ATOM   2885  N   GLU E1004      30.179 -11.971 -28.685  1.00191.99           N  
ANISOU 2885  N   GLU E1004    26201  22496  24251  -1765   2463  -1218       N  
ATOM   2886  CA  GLU E1004      31.583 -12.200 -28.364  1.00192.45           C  
ANISOU 2886  CA  GLU E1004    26220  22443  24459  -1738   2526  -1235       C  
ATOM   2887  C   GLU E1004      32.235 -13.251 -29.254  1.00192.83           C  
ANISOU 2887  C   GLU E1004    26274  22424  24570  -1794   2633  -1340       C  
ATOM   2888  O   GLU E1004      33.461 -13.397 -29.207  1.00193.45           O  
ANISOU 2888  O   GLU E1004    26322  22412  24768  -1778   2697  -1368       O  
ATOM   2889  CB  GLU E1004      31.734 -12.616 -26.898  1.00189.65           C  
ANISOU 2889  CB  GLU E1004    25802  22024  24231  -1682   2468  -1180       C  
ATOM   2890  CG  GLU E1004      31.893 -11.456 -25.929  1.00188.90           C  
ANISOU 2890  CG  GLU E1004    25687  21947  24139  -1610   2396  -1086       C  
ATOM   2891  CD  GLU E1004      31.261 -11.731 -24.578  1.00185.63           C  
ANISOU 2891  CD  GLU E1004    25238  21531  23763  -1569   2306  -1018       C  
ATOM   2892  OE1 GLU E1004      30.036 -11.965 -24.530  1.00183.77           O  
ANISOU 2892  OE1 GLU E1004    25018  21363  23442  -1594   2258  -1006       O  
ATOM   2893  OE2 GLU E1004      31.990 -11.714 -23.563  1.00184.18           O  
ANISOU 2893  OE2 GLU E1004    25012  21278  23693  -1514   2283   -979       O  
ATOM   2894  N   ASP E1005      31.453 -13.993 -30.044  1.00169.87           N  
ANISOU 2894  N   ASP E1005    23398  19556  21589  -1858   2653  -1401       N  
ATOM   2895  CA  ASP E1005      32.030 -15.013 -30.916  1.00169.27           C  
ANISOU 2895  CA  ASP E1005    23329  19418  21568  -1915   2757  -1506       C  
ATOM   2896  C   ASP E1005      32.957 -14.389 -31.950  1.00170.15           C  
ANISOU 2896  C   ASP E1005    23478  19522  21650  -1936   2848  -1552       C  
ATOM   2897  O   ASP E1005      34.057 -14.897 -32.201  1.00168.72           O  
ANISOU 2897  O   ASP E1005    23273  19249  21583  -1946   2938  -1614       O  
ATOM   2898  CB  ASP E1005      30.920 -15.810 -31.601  1.00169.85           C  
ANISOU 2898  CB  ASP E1005    23436  19549  21552  -1982   2754  -1563       C  
ATOM   2899  N   ASN E1006      32.525 -13.285 -32.566  1.00173.56           N  
ANISOU 2899  N   ASN E1006    23969  20047  21929  -1944   2827  -1521       N  
ATOM   2900  CA  ASN E1006      33.394 -12.583 -33.504  1.00172.68           C  
ANISOU 2900  CA  ASN E1006    23900  19929  21780  -1963   2913  -1554       C  
ATOM   2901  C   ASN E1006      34.631 -12.045 -32.798  1.00172.07           C  
ANISOU 2901  C   ASN E1006    23772  19772  21835  -1906   2937  -1520       C  
ATOM   2902  O   ASN E1006      35.721 -12.022 -33.378  1.00170.95           O  
ANISOU 2902  O   ASN E1006    23632  19571  21752  -1924   3039  -1577       O  
ATOM   2903  CB  ASN E1006      32.628 -11.453 -34.194  1.00171.25           C  
ANISOU 2903  CB  ASN E1006    23797  19863  21407  -1975   2873  -1514       C  
ATOM   2904  N   TRP E1007      34.478 -11.606 -31.544  1.00180.08           N  
ANISOU 2904  N   TRP E1007    24739  20784  22899  -1837   2844  -1430       N  
ATOM   2905  CA  TRP E1007      35.636 -11.245 -30.733  1.00179.94           C  
ANISOU 2905  CA  TRP E1007    24661  20682  23025  -1778   2855  -1402       C  
ATOM   2906  C   TRP E1007      36.580 -12.429 -30.588  1.00180.21           C  
ANISOU 2906  C   TRP E1007    24639  20600  23232  -1785   2925  -1474       C  
ATOM   2907  O   TRP E1007      37.798 -12.291 -30.748  1.00178.49           O  
ANISOU 2907  O   TRP E1007    24394  20309  23116  -1776   3001  -1512       O  
ATOM   2908  CB  TRP E1007      35.187 -10.760 -29.356  1.00180.95           C  
ANISOU 2908  CB  TRP E1007    24749  20828  23174  -1707   2736  -1299       C  
ATOM   2909  CG  TRP E1007      36.309 -10.687 -28.363  1.00182.81           C  
ANISOU 2909  CG  TRP E1007    24913  20969  23576  -1646   2733  -1276       C  
ATOM   2910  CD1 TRP E1007      37.554 -10.165 -28.566  1.00183.74           C  
ANISOU 2910  CD1 TRP E1007    25011  21028  23772  -1631   2802  -1299       C  
ATOM   2911  CD2 TRP E1007      36.303 -11.203 -27.027  1.00184.29           C  
ANISOU 2911  CD2 TRP E1007    25040  21106  23875  -1592   2660  -1230       C  
ATOM   2912  NE1 TRP E1007      38.313 -10.297 -27.429  1.00186.30           N  
ANISOU 2912  NE1 TRP E1007    25262  21272  24250  -1569   2768  -1272       N  
ATOM   2913  CE2 TRP E1007      37.569 -10.933 -26.470  1.00186.98           C  
ANISOU 2913  CE2 TRP E1007    25326  21362  24357  -1542   2680  -1227       C  
ATOM   2914  CE3 TRP E1007      35.346 -11.855 -26.243  1.00184.04           C  
ANISOU 2914  CE3 TRP E1007    24997  21092  23836  -1581   2581  -1192       C  
ATOM   2915  CZ2 TRP E1007      37.903 -11.294 -25.166  1.00188.35           C  
ANISOU 2915  CZ2 TRP E1007    25438  21469  24658  -1480   2616  -1184       C  
ATOM   2916  CZ3 TRP E1007      35.679 -12.212 -24.949  1.00186.63           C  
ANISOU 2916  CZ3 TRP E1007    25269  21353  24289  -1523   2525  -1147       C  
ATOM   2917  CH2 TRP E1007      36.946 -11.931 -24.423  1.00188.88           C  
ANISOU 2917  CH2 TRP E1007    25503  21554  24706  -1472   2539  -1143       C  
ATOM   2918  N   GLU E1008      36.029 -13.608 -30.288  1.00181.37           N  
ANISOU 2918  N   GLU E1008    24767  20726  23420  -1800   2902  -1498       N  
ATOM   2919  CA  GLU E1008      36.852 -14.802 -30.150  1.00179.98           C  
ANISOU 2919  CA  GLU E1008    24539  20435  23410  -1805   2964  -1567       C  
ATOM   2920  C   GLU E1008      37.623 -15.112 -31.423  1.00180.16           C  
ANISOU 2920  C   GLU E1008    24584  20422  23445  -1865   3096  -1674       C  
ATOM   2921  O   GLU E1008      38.659 -15.780 -31.354  1.00179.06           O  
ANISOU 2921  O   GLU E1008    24395  20179  23462  -1859   3163  -1733       O  
ATOM   2922  CB  GLU E1008      35.987 -16.002 -29.756  1.00177.48           C  
ANISOU 2922  CB  GLU E1008    24212  20111  23113  -1822   2922  -1575       C  
ATOM   2923  N   THR E1009      37.152 -14.635 -32.579  1.00172.13           N  
ANISOU 2923  N   THR E1009    23644  19490  22269  -1921   3135  -1703       N  
ATOM   2924  CA  THR E1009      37.929 -14.791 -33.804  1.00170.29           C  
ANISOU 2924  CA  THR E1009    23440  19228  22035  -1979   3267  -1802       C  
ATOM   2925  C   THR E1009      39.259 -14.056 -33.699  1.00169.12           C  
ANISOU 2925  C   THR E1009    23259  19017  21983  -1947   3326  -1802       C  
ATOM   2926  O   THR E1009      40.299 -14.583 -34.110  1.00167.80           O  
ANISOU 2926  O   THR E1009    23062  18764  21932  -1967   3431  -1887       O  
ATOM   2927  CB  THR E1009      37.139 -14.286 -35.013  1.00166.99           C  
ANISOU 2927  CB  THR E1009    23119  18918  21411  -2042   3285  -1820       C  
ATOM   2928  OG1 THR E1009      35.755 -14.624 -34.863  1.00167.34           O  
ANISOU 2928  OG1 THR E1009    23187  19040  21353  -2054   3194  -1790       O  
ATOM   2929  CG2 THR E1009      37.665 -14.925 -36.290  1.00165.53           C  
ANISOU 2929  CG2 THR E1009    22970  18702  21221  -2117   3419  -1940       C  
ATOM   2930  N   LEU E1010      39.247 -12.838 -33.150  1.00159.30           N  
ANISOU 2930  N   LEU E1010    22016  17812  20698  -1896   3262  -1712       N  
ATOM   2931  CA  LEU E1010      40.496 -12.109 -32.955  1.00159.73           C  
ANISOU 2931  CA  LEU E1010    22031  17805  20852  -1862   3311  -1709       C  
ATOM   2932  C   LEU E1010      41.421 -12.849 -31.995  1.00160.55           C  
ANISOU 2932  C   LEU E1010    22036  17792  21174  -1812   3309  -1727       C  
ATOM   2933  O   LEU E1010      42.509 -13.293 -32.377  1.00161.06           O  
ANISOU 2933  O   LEU E1010    22062  17770  21362  -1828   3411  -1811       O  
ATOM   2934  CB  LEU E1010      40.231 -10.688 -32.442  1.00160.98           C  
ANISOU 2934  CB  LEU E1010    22207  18027  20930  -1814   3232  -1605       C  
ATOM   2935  CG  LEU E1010      39.373  -9.628 -33.152  1.00160.83           C  
ANISOU 2935  CG  LEU E1010    22282  18124  20702  -1841   3208  -1559       C  
ATOM   2936  CD1 LEU E1010      39.792  -9.408 -34.595  1.00160.66           C  
ANISOU 2936  CD1 LEU E1010    22332  18113  20599  -1912   3333  -1633       C  
ATOM   2937  CD2 LEU E1010      37.895  -9.911 -33.074  1.00161.86           C  
ANISOU 2937  CD2 LEU E1010    22451  18344  20705  -1851   3113  -1520       C  
ATOM   2938  N   ASN E1011      40.991 -13.007 -30.739  1.00198.76           N  
ANISOU 2938  N   ASN E1011    26831  22625  26063  -1750   3194  -1650       N  
ATOM   2939  CA  ASN E1011      41.896 -13.497 -29.702  1.00199.89           C  
ANISOU 2939  CA  ASN E1011    26884  22660  26406  -1690   3173  -1649       C  
ATOM   2940  C   ASN E1011      42.334 -14.936 -29.952  1.00199.46           C  
ANISOU 2940  C   ASN E1011    26794  22513  26478  -1716   3240  -1742       C  
ATOM   2941  O   ASN E1011      43.455 -15.311 -29.588  1.00197.90           O  
ANISOU 2941  O   ASN E1011    26525  22211  26457  -1683   3275  -1782       O  
ATOM   2942  CB  ASN E1011      41.243 -13.364 -28.326  1.00198.92           C  
ANISOU 2942  CB  ASN E1011    26735  22557  26288  -1622   3033  -1544       C  
ATOM   2943  CG  ASN E1011      39.805 -13.826 -28.317  1.00201.14           C  
ANISOU 2943  CG  ASN E1011    27064  22914  26445  -1650   2970  -1512       C  
ATOM   2944  OD1 ASN E1011      38.882 -13.013 -28.311  1.00200.63           O  
ANISOU 2944  OD1 ASN E1011    27046  22950  26233  -1651   2908  -1448       O  
ATOM   2945  ND2 ASN E1011      39.605 -15.138 -28.302  1.00201.93           N  
ANISOU 2945  ND2 ASN E1011    27150  22965  26609  -1673   2984  -1560       N  
ATOM   2946  N   ASP E1012      41.474 -15.762 -30.553  1.00229.66           N  
ANISOU 2946  N   ASP E1012    30664  26372  30224  -1774   3256  -1782       N  
ATOM   2947  CA  ASP E1012      41.915 -17.095 -30.948  1.00230.65           C  
ANISOU 2947  CA  ASP E1012    30762  26410  30465  -1807   3334  -1881       C  
ATOM   2948  C   ASP E1012      42.961 -17.011 -32.051  1.00231.32           C  
ANISOU 2948  C   ASP E1012    30848  26454  30589  -1852   3476  -1984       C  
ATOM   2949  O   ASP E1012      44.035 -17.613 -31.946  1.00230.80           O  
ANISOU 2949  O   ASP E1012    30716  26279  30698  -1837   3536  -2049       O  
ATOM   2950  CB  ASP E1012      40.727 -17.948 -31.395  1.00230.49           C  
ANISOU 2950  CB  ASP E1012    30792  26441  30343  -1864   3322  -1905       C  
ATOM   2951  N   ASN E1013      42.674 -16.246 -33.110  1.00154.34           N  
ANISOU 2951  N   ASN E1013    21173  16789  20679  -1907   3530  -2000       N  
ATOM   2952  CA  ASN E1013      43.647 -16.071 -34.184  1.00152.41           C  
ANISOU 2952  CA  ASN E1013    20941  16512  20457  -1955   3671  -2094       C  
ATOM   2953  C   ASN E1013      44.904 -15.357 -33.706  1.00150.01           C  
ANISOU 2953  C   ASN E1013    20570  16140  20286  -1903   3696  -2085       C  
ATOM   2954  O   ASN E1013      45.952 -15.474 -34.350  1.00149.68           O  
ANISOU 2954  O   ASN E1013    20505  16034  20332  -1931   3818  -2175       O  
ATOM   2955  CB  ASN E1013      43.024 -15.307 -35.352  1.00148.98           C  
ANISOU 2955  CB  ASN E1013    20612  16186  19808  -2020   3713  -2098       C  
ATOM   2956  N   LEU E1014      44.822 -14.614 -32.600  1.00167.80           N  
ANISOU 2956  N   LEU E1014    22791  18407  22558  -1830   3587  -1982       N  
ATOM   2957  CA  LEU E1014      46.030 -14.057 -32.001  1.00169.83           C  
ANISOU 2957  CA  LEU E1014    22973  18591  22965  -1775   3598  -1976       C  
ATOM   2958  C   LEU E1014      46.927 -15.161 -31.456  1.00169.00           C  
ANISOU 2958  C   LEU E1014    22772  18358  23083  -1740   3616  -2036       C  
ATOM   2959  O   LEU E1014      48.146 -15.138 -31.660  1.00169.08           O  
ANISOU 2959  O   LEU E1014    22724  18288  23231  -1736   3702  -2106       O  
ATOM   2960  CB  LEU E1014      45.665 -13.063 -30.899  1.00170.51           C  
ANISOU 2960  CB  LEU E1014    23048  18724  23015  -1704   3469  -1852       C  
ATOM   2961  N   LYS E1015      46.340 -16.139 -30.764  1.00173.91           N  
ANISOU 2961  N   LYS E1015    23375  18957  23745  -1716   3536  -2011       N  
ATOM   2962  CA  LYS E1015      47.129 -17.260 -30.265  1.00173.44           C  
ANISOU 2962  CA  LYS E1015    23232  18772  23894  -1682   3548  -2067       C  
ATOM   2963  C   LYS E1015      47.727 -18.061 -31.414  1.00174.08           C  
ANISOU 2963  C   LYS E1015    23310  18796  24035  -1749   3694  -2202       C  
ATOM   2964  O   LYS E1015      48.880 -18.505 -31.337  1.00173.64           O  
ANISOU 2964  O   LYS E1015    23177  18633  24165  -1727   3753  -2274       O  
ATOM   2965  CB  LYS E1015      46.268 -18.153 -29.371  1.00172.40           C  
ANISOU 2965  CB  LYS E1015    23098  18632  23773  -1651   3439  -2010       C  
ATOM   2966  N   VAL E1016      46.958 -18.260 -32.489  1.00145.74           N  
ANISOU 2966  N   VAL E1016    19804  15278  20292  -1829   3753  -2242       N  
ATOM   2967  CA  VAL E1016      47.495 -18.911 -33.684  1.00144.85           C  
ANISOU 2967  CA  VAL E1016    19700  15123  20213  -1901   3901  -2374       C  
ATOM   2968  C   VAL E1016      48.629 -18.079 -34.271  1.00145.25           C  
ANISOU 2968  C   VAL E1016    19733  15151  20306  -1915   4010  -2428       C  
ATOM   2969  O   VAL E1016      49.674 -18.610 -34.668  1.00144.10           O  
ANISOU 2969  O   VAL E1016    19531  14912  20308  -1929   4118  -2533       O  
ATOM   2970  CB  VAL E1016      46.381 -19.153 -34.719  1.00143.27           C  
ANISOU 2970  CB  VAL E1016    19602  15018  19817  -1985   3933  -2400       C  
ATOM   2971  CG1 VAL E1016      46.826 -20.189 -35.737  1.00142.57           C  
ANISOU 2971  CG1 VAL E1016    19512  14869  19788  -2052   4068  -2539       C  
ATOM   2972  CG2 VAL E1016      45.102 -19.603 -34.037  1.00141.26           C  
ANISOU 2972  CG2 VAL E1016    19372  14813  19488  -1967   3806  -2321       C  
ATOM   2973  N   ILE E1017      48.433 -16.760 -34.347  1.00164.31           N  
ANISOU 2973  N   ILE E1017    22192  17647  22591  -1913   3988  -2358       N  
ATOM   2974  CA  ILE E1017      49.504 -15.879 -34.797  1.00162.88           C  
ANISOU 2974  CA  ILE E1017    21993  17442  22452  -1923   4086  -2398       C  
ATOM   2975  C   ILE E1017      50.661 -15.888 -33.806  1.00163.83           C  
ANISOU 2975  C   ILE E1017    21993  17456  22800  -1845   4061  -2401       C  
ATOM   2976  O   ILE E1017      51.815 -15.658 -34.190  1.00163.41           O  
ANISOU 2976  O   ILE E1017    21892  17339  22859  -1855   4168  -2478       O  
ATOM   2977  CB  ILE E1017      48.971 -14.454 -35.026  1.00160.74           C  
ANISOU 2977  CB  ILE E1017    21802  17281  21992  -1934   4057  -2313       C  
ATOM   2978  N   GLU E1018      50.383 -16.146 -32.524  1.00205.76           N  
ANISOU 2978  N   GLU E1018    27253  22743  28181  -1766   3922  -2320       N  
ATOM   2979  CA  GLU E1018      51.456 -16.291 -31.546  1.00206.00           C  
ANISOU 2979  CA  GLU E1018    27170  22668  28433  -1688   3886  -2326       C  
ATOM   2980  C   GLU E1018      52.326 -17.506 -31.836  1.00204.18           C  
ANISOU 2980  C   GLU E1018    26869  22318  28392  -1698   3974  -2447       C  
ATOM   2981  O   GLU E1018      53.445 -17.594 -31.319  1.00205.49           O  
ANISOU 2981  O   GLU E1018    26935  22387  28754  -1645   3981  -2483       O  
ATOM   2982  CB  GLU E1018      50.878 -16.383 -30.132  1.00203.88           C  
ANISOU 2982  CB  GLU E1018    26877  22404  28183  -1606   3716  -2211       C  
ATOM   2983  N   LYS E1019      51.838 -18.436 -32.651  1.00126.46           N  
ANISOU 2983  N   LYS E1019    17073  12480  18496  -1763   4040  -2513       N  
ATOM   2984  CA  LYS E1019      52.625 -19.582 -33.087  1.00126.79           C  
ANISOU 2984  CA  LYS E1019    17056  12412  18704  -1782   4140  -2639       C  
ATOM   2985  C   LYS E1019      52.961 -19.466 -34.573  1.00127.76           C  
ANISOU 2985  C   LYS E1019    17226  12555  18763  -1878   4313  -2751       C  
ATOM   2986  O   LYS E1019      54.121 -19.288 -34.951  1.00124.92           O  
ANISOU 2986  O   LYS E1019    16807  12128  18527  -1886   4420  -2837       O  
ATOM   2987  CB  LYS E1019      51.872 -20.886 -32.816  1.00127.30           C  
ANISOU 2987  CB  LYS E1019    17132  12452  18783  -1781   4085  -2638       C  
ATOM   2988  N   GLN E1025      53.439 -18.521 -43.705  1.00166.91           N  
ANISOU 2988  N   GLN E1025    22705  17761  22952  -2516   5298  -3326       N  
ATOM   2989  CA  GLN E1025      52.437 -17.526 -44.068  1.00165.69           C  
ANISOU 2989  CA  GLN E1025    22678  17737  22538  -2543   5242  -3227       C  
ATOM   2990  C   GLN E1025      51.335 -17.459 -43.018  1.00168.77           C  
ANISOU 2990  C   GLN E1025    23069  18186  22870  -2473   5043  -3092       C  
ATOM   2991  O   GLN E1025      50.390 -18.250 -43.036  1.00169.20           O  
ANISOU 2991  O   GLN E1025    23155  18275  22857  -2485   4979  -3087       O  
ATOM   2992  CB  GLN E1025      51.839 -17.837 -45.440  1.00164.47           C  
ANISOU 2992  CB  GLN E1025    22649  17651  22190  -2646   5335  -3298       C  
ATOM   2993  N   VAL E1026      51.462 -16.497 -42.106  1.00167.77           N  
ANISOU 2993  N   VAL E1026    22906  18069  22770  -2403   4950  -2985       N  
ATOM   2994  CA  VAL E1026      50.474 -16.276 -41.057  1.00163.28           C  
ANISOU 2994  CA  VAL E1026    22337  17557  22145  -2334   4765  -2851       C  
ATOM   2995  C   VAL E1026      49.338 -15.433 -41.621  1.00163.93           C  
ANISOU 2995  C   VAL E1026    22553  17775  21959  -2372   4719  -2773       C  
ATOM   2996  O   VAL E1026      48.467 -14.965 -40.878  1.00162.62           O  
ANISOU 2996  O   VAL E1026    22402  17673  21711  -2322   4574  -2656       O  
ATOM   2997  CB  VAL E1026      51.106 -15.601 -39.826  1.00153.07           C  
ANISOU 2997  CB  VAL E1026    20948  16216  20995  -2242   4684  -2774       C  
ATOM   2998  N   LYS E1027      49.348 -15.226 -42.943  1.00150.25           N  
ANISOU 2998  N   LYS E1027    20918  16084  20088  -2460   4843  -2840       N  
ATOM   2999  CA  LYS E1027      48.342 -14.382 -43.579  1.00151.51           C  
ANISOU 2999  CA  LYS E1027    21210  16368  19988  -2497   4806  -2771       C  
ATOM   3000  C   LYS E1027      46.933 -14.931 -43.392  1.00151.92           C  
ANISOU 3000  C   LYS E1027    21305  16498  19921  -2492   4677  -2722       C  
ATOM   3001  O   LYS E1027      45.976 -14.153 -43.309  1.00150.86           O  
ANISOU 3001  O   LYS E1027    21241  16462  19615  -2480   4576  -2622       O  
ATOM   3002  CB  LYS E1027      48.656 -14.225 -45.068  1.00152.67           C  
ANISOU 3002  CB  LYS E1027    21457  16536  20015  -2596   4970  -2864       C  
ATOM   3003  N   ASP E1028      46.784 -16.257 -43.323  1.00196.52           N  
ANISOU 3003  N   ASP E1028    26909  22101  25660  -2503   4680  -2793       N  
ATOM   3004  CA  ASP E1028      45.454 -16.847 -43.196  1.00197.75           C  
ANISOU 3004  CA  ASP E1028    27102  22327  25708  -2507   4569  -2757       C  
ATOM   3005  C   ASP E1028      44.760 -16.383 -41.921  1.00197.59           C  
ANISOU 3005  C   ASP E1028    27046  22343  25688  -2422   4396  -2620       C  
ATOM   3006  O   ASP E1028      43.576 -16.024 -41.945  1.00196.86           O  
ANISOU 3006  O   ASP E1028    27020  22352  25424  -2424   4297  -2548       O  
ATOM   3007  CB  ASP E1028      45.551 -18.373 -43.231  1.00199.97           C  
ANISOU 3007  CB  ASP E1028    27328  22533  26118  -2527   4608  -2859       C  
ATOM   3008  N   ALA E1029      45.481 -16.380 -40.796  1.00200.47           N  
ANISOU 3008  N   ALA E1029    27302  22624  26243  -2347   4357  -2586       N  
ATOM   3009  CA  ALA E1029      44.896 -15.904 -39.546  1.00198.94           C  
ANISOU 3009  CA  ALA E1029    27074  22461  26054  -2266   4198  -2457       C  
ATOM   3010  C   ALA E1029      44.576 -14.417 -39.615  1.00196.98           C  
ANISOU 3010  C   ALA E1029    26891  22300  25651  -2254   4154  -2362       C  
ATOM   3011  O   ALA E1029      43.492 -13.990 -39.201  1.00195.33           O  
ANISOU 3011  O   ALA E1029    26719  22177  25320  -2228   4030  -2266       O  
ATOM   3012  CB  ALA E1029      45.837 -16.195 -38.377  1.00198.51           C  
ANISOU 3012  CB  ALA E1029    26895  22295  26237  -2189   4171  -2447       C  
ATOM   3013  N   LEU E1030      45.506 -13.618 -40.143  1.00213.72           N  
ANISOU 3013  N   LEU E1030    29026  24400  27779  -2273   4257  -2388       N  
ATOM   3014  CA  LEU E1030      45.303 -12.174 -40.214  1.00212.52           C  
ANISOU 3014  CA  LEU E1030    28936  24320  27493  -2260   4224  -2300       C  
ATOM   3015  C   LEU E1030      44.151 -11.814 -41.145  1.00213.39           C  
ANISOU 3015  C   LEU E1030    29177  24549  27353  -2315   4203  -2275       C  
ATOM   3016  O   LEU E1030      43.348 -10.927 -40.830  1.00215.01           O  
ANISOU 3016  O   LEU E1030    29425  24835  27432  -2284   4096  -2171       O  
ATOM   3017  CB  LEU E1030      46.592 -11.488 -40.666  1.00208.56           C  
ANISOU 3017  CB  LEU E1030    28425  23760  27059  -2279   4357  -2346       C  
ATOM   3018  CG  LEU E1030      47.860 -11.668 -39.827  1.00209.44           C  
ANISOU 3018  CG  LEU E1030    28405  23754  27419  -2226   4386  -2376       C  
ATOM   3019  CD1 LEU E1030      48.717 -10.427 -39.924  1.00205.74           C  
ANISOU 3019  CD1 LEU E1030    27938  23270  26964  -2220   4449  -2356       C  
ATOM   3020  CD2 LEU E1030      47.527 -11.948 -38.368  1.00212.89           C  
ANISOU 3020  CD2 LEU E1030    28755  24171  27963  -2136   4232  -2295       C  
ATOM   3021  N   THR E1031      44.060 -12.480 -42.300  1.00135.76           N  
ANISOU 3021  N   THR E1031    19407  14728  17448  -2396   4301  -2374       N  
ATOM   3022  CA  THR E1031      42.936 -12.244 -43.200  1.00134.46           C  
ANISOU 3022  CA  THR E1031    19366  14676  17046  -2448   4273  -2358       C  
ATOM   3023  C   THR E1031      41.621 -12.637 -42.545  1.00135.00           C  
ANISOU 3023  C   THR E1031    19426  14809  17058  -2414   4117  -2293       C  
ATOM   3024  O   THR E1031      40.618 -11.927 -42.674  1.00134.99           O  
ANISOU 3024  O   THR E1031    19498  14908  16882  -2409   4026  -2216       O  
ATOM   3025  CB  THR E1031      43.129 -13.012 -44.505  1.00136.90           C  
ANISOU 3025  CB  THR E1031    19736  14978  17302  -2540   4407  -2486       C  
ATOM   3026  OG1 THR E1031      43.460 -14.376 -44.210  1.00138.96           O  
ANISOU 3026  OG1 THR E1031    19910  15156  17733  -2542   4439  -2571       O  
ATOM   3027  CG2 THR E1031      44.234 -12.383 -45.342  1.00136.07           C  
ANISOU 3027  CG2 THR E1031    19671  14835  17193  -2586   4563  -2540       C  
ATOM   3028  N   LYS E1032      41.603 -13.775 -41.848  1.00155.39           N  
ANISOU 3028  N   LYS E1032    21921  17332  19787  -2391   4085  -2324       N  
ATOM   3029  CA  LYS E1032      40.438 -14.136 -41.052  1.00156.63           C  
ANISOU 3029  CA  LYS E1032    22056  17538  19916  -2353   3939  -2256       C  
ATOM   3030  C   LYS E1032      40.261 -13.212 -39.855  1.00155.33           C  
ANISOU 3030  C   LYS E1032    21851  17391  19778  -2268   3818  -2129       C  
ATOM   3031  O   LYS E1032      39.151 -13.108 -39.322  1.00155.53           O  
ANISOU 3031  O   LYS E1032    21885  17486  19725  -2240   3693  -2055       O  
ATOM   3032  CB  LYS E1032      40.549 -15.587 -40.582  1.00156.83           C  
ANISOU 3032  CB  LYS E1032    22001  17484  20103  -2350   3944  -2320       C  
ATOM   3033  N   MET E1033      41.328 -12.539 -39.424  1.00159.69           N  
ANISOU 3033  N   MET E1033    22356  17882  20439  -2228   3856  -2108       N  
ATOM   3034  CA  MET E1033      41.215 -11.619 -38.300  1.00159.92           C  
ANISOU 3034  CA  MET E1033    22345  17925  20492  -2149   3746  -1991       C  
ATOM   3035  C   MET E1033      40.773 -10.234 -38.759  1.00163.90           C  
ANISOU 3035  C   MET E1033    22939  18521  20814  -2154   3720  -1920       C  
ATOM   3036  O   MET E1033      39.876  -9.630 -38.158  1.00164.06           O  
ANISOU 3036  O   MET E1033    22972  18612  20753  -2111   3596  -1823       O  
ATOM   3037  CB  MET E1033      42.546 -11.536 -37.556  1.00158.89           C  
ANISOU 3037  CB  MET E1033    22117  17686  20569  -2100   3787  -2001       C  
ATOM   3038  CG  MET E1033      42.403 -10.958 -36.181  1.00157.92           C  
ANISOU 3038  CG  MET E1033    21933  17562  20506  -2013   3660  -1892       C  
ATOM   3039  SD  MET E1033      43.862 -11.091 -35.153  1.00158.17           S  
ANISOU 3039  SD  MET E1033    21837  17462  20797  -1947   3682  -1907       S  
ATOM   3040  CE  MET E1033      43.402  -9.926 -33.878  1.00159.63           C  
ANISOU 3040  CE  MET E1033    22002  17697  20954  -1862   3532  -1764       C  
ATOM   3041  N   ARG E1034      41.396  -9.715 -39.822  1.00205.57           N  
ANISOU 3041  N   ARG E1034    28282  23797  26029  -2206   3838  -1968       N  
ATOM   3042  CA  ARG E1034      41.040  -8.391 -40.324  1.00204.27           C  
ANISOU 3042  CA  ARG E1034    28211  23711  25691  -2213   3822  -1900       C  
ATOM   3043  C   ARG E1034      39.637  -8.370 -40.914  1.00205.21           C  
ANISOU 3043  C   ARG E1034    28425  23944  25602  -2243   3746  -1874       C  
ATOM   3044  O   ARG E1034      38.950  -7.344 -40.838  1.00206.08           O  
ANISOU 3044  O   ARG E1034    28588  24131  25582  -2217   3662  -1784       O  
ATOM   3045  CB  ARG E1034      42.060  -7.928 -41.365  1.00201.28           C  
ANISOU 3045  CB  ARG E1034    27885  23296  25294  -2269   3978  -1964       C  
ATOM   3046  N   ALA E1035      39.199  -9.480 -41.517  1.00165.15           N  
ANISOU 3046  N   ALA E1035    23371  18882  20497  -2296   3773  -1954       N  
ATOM   3047  CA  ALA E1035      37.823  -9.559 -41.995  1.00166.66           C  
ANISOU 3047  CA  ALA E1035    23638  19180  20504  -2321   3688  -1934       C  
ATOM   3048  C   ALA E1035      36.834  -9.665 -40.841  1.00165.62           C  
ANISOU 3048  C   ALA E1035    23448  19087  20393  -2259   3532  -1853       C  
ATOM   3049  O   ALA E1035      35.714  -9.152 -40.937  1.00165.99           O  
ANISOU 3049  O   ALA E1035    23550  19232  20289  -2251   3432  -1792       O  
ATOM   3050  CB  ALA E1035      37.657 -10.742 -42.949  1.00166.50           C  
ANISOU 3050  CB  ALA E1035    23651  19159  20452  -2398   3763  -2050       C  
ATOM   3051  N   ALA E1036      37.224 -10.330 -39.751  1.00188.72           N  
ANISOU 3051  N   ALA E1036    26264  21936  23504  -2214   3509  -1851       N  
ATOM   3052  CA  ALA E1036      36.353 -10.405 -38.583  1.00190.37           C  
ANISOU 3052  CA  ALA E1036    26418  22174  23738  -2154   3368  -1771       C  
ATOM   3053  C   ALA E1036      36.190  -9.045 -37.918  1.00191.17           C  
ANISOU 3053  C   ALA E1036    26522  22316  23796  -2090   3283  -1656       C  
ATOM   3054  O   ALA E1036      35.148  -8.775 -37.308  1.00191.98           O  
ANISOU 3054  O   ALA E1036    26621  22485  23837  -2054   3161  -1583       O  
ATOM   3055  CB  ALA E1036      36.900 -11.423 -37.582  1.00191.32           C  
ANISOU 3055  CB  ALA E1036    26430  22196  24067  -2121   3370  -1795       C  
ATOM   3056  N   ALA E1037      37.205  -8.185 -38.019  1.00166.60           N  
ANISOU 3056  N   ALA E1037    23416  19164  20721  -2078   3350  -1644       N  
ATOM   3057  CA  ALA E1037      37.126  -6.860 -37.413  1.00164.15           C  
ANISOU 3057  CA  ALA E1037    23108  18884  20376  -2019   3278  -1540       C  
ATOM   3058  C   ALA E1037      36.030  -6.015 -38.054  1.00166.28           C  
ANISOU 3058  C   ALA E1037    23479  19268  20431  -2032   3213  -1487       C  
ATOM   3059  O   ALA E1037      35.364  -5.229 -37.371  1.00168.06           O  
ANISOU 3059  O   ALA E1037    23698  19545  20610  -1979   3102  -1394       O  
ATOM   3060  CB  ALA E1037      38.479  -6.159 -37.518  1.00163.17           C  
ANISOU 3060  CB  ALA E1037    22972  18689  20336  -2013   3377  -1550       C  
ATOM   3061  N   LEU E1038      35.823  -6.167 -39.366  1.00159.12           N  
ANISOU 3061  N   LEU E1038    22664  18400  19392  -2102   3279  -1546       N  
ATOM   3062  CA  LEU E1038      34.841  -5.359 -40.082  1.00159.52           C  
ANISOU 3062  CA  LEU E1038    22820  18557  19234  -2116   3220  -1500       C  
ATOM   3063  C   LEU E1038      33.408  -5.643 -39.647  1.00159.55           C  
ANISOU 3063  C   LEU E1038    22811  18642  19166  -2095   3080  -1461       C  
ATOM   3064  O   LEU E1038      32.504  -4.882 -40.014  1.00156.83           O  
ANISOU 3064  O   LEU E1038    22537  18388  18663  -2089   3004  -1408       O  
ATOM   3065  CB  LEU E1038      34.981  -5.582 -41.591  1.00159.54           C  
ANISOU 3065  CB  LEU E1038    22926  18579  19114  -2200   3325  -1581       C  
ATOM   3066  N   ASP E1039      33.180  -6.712 -38.885  1.00185.03           N  
ANISOU 3066  N   ASP E1039    25954  21840  22509  -2083   3046  -1485       N  
ATOM   3067  CA  ASP E1039      31.869  -7.040 -38.342  1.00185.46           C  
ANISOU 3067  CA  ASP E1039    25983  21963  22520  -2062   2920  -1451       C  
ATOM   3068  C   ASP E1039      31.599  -6.373 -36.997  1.00184.90           C  
ANISOU 3068  C   ASP E1039    25848  21898  22509  -1981   2814  -1349       C  
ATOM   3069  O   ASP E1039      30.531  -6.593 -36.416  1.00186.72           O  
ANISOU 3069  O   ASP E1039    26049  22180  22714  -1960   2710  -1315       O  
ATOM   3070  CB  ASP E1039      31.726  -8.564 -38.218  1.00182.36           C  
ANISOU 3070  CB  ASP E1039    25538  21533  22218  -2096   2942  -1530       C  
ATOM   3071  CG  ASP E1039      32.002  -9.068 -36.815  1.00181.02           C  
ANISOU 3071  CG  ASP E1039    25260  21294  22228  -2042   2905  -1500       C  
ATOM   3072  N   ALA E1040      32.528  -5.560 -36.498  1.00167.69           N  
ANISOU 3072  N   ALA E1040    23644  19666  20406  -1938   2840  -1303       N  
ATOM   3073  CA  ALA E1040      32.324  -4.819 -35.254  1.00165.60           C  
ANISOU 3073  CA  ALA E1040    23324  19407  20190  -1862   2742  -1207       C  
ATOM   3074  C   ALA E1040      31.469  -3.574 -35.480  1.00166.39           C  
ANISOU 3074  C   ALA E1040    23489  19601  20132  -1839   2659  -1130       C  
ATOM   3075  O   ALA E1040      30.241  -3.647 -35.521  1.00165.44           O  
ANISOU 3075  O   ALA E1040    23385  19561  19911  -1839   2569  -1111       O  
ATOM   3076  CB  ALA E1040      33.665  -4.430 -34.640  1.00164.35           C  
ANISOU 3076  CB  ALA E1040    23111  19155  20178  -1825   2800  -1193       C  
ATOM   3077  N   MET E1058      30.321   6.901 -27.836  1.00196.37           N  
ANISOU 3077  N   MET E1058    27097  23528  23985  -1244   1995   -361       N  
ATOM   3078  CA  MET E1058      30.365   5.800 -28.791  1.00196.42           C  
ANISOU 3078  CA  MET E1058    27134  23532  23964  -1309   2062   -433       C  
ATOM   3079  C   MET E1058      31.469   6.018 -29.814  1.00197.33           C  
ANISOU 3079  C   MET E1058    27306  23593  24079  -1352   2182   -472       C  
ATOM   3080  O   MET E1058      31.668   5.196 -30.709  1.00197.44           O  
ANISOU 3080  O   MET E1058    27353  23596  24070  -1411   2254   -537       O  
ATOM   3081  CB  MET E1058      29.018   5.644 -29.500  1.00195.90           C  
ANISOU 3081  CB  MET E1058    27123  23560  23749  -1332   2001   -433       C  
ATOM   3082  N   LYS E1059      32.182   7.137 -29.681  1.00239.67           N  
ANISOU 3082  N   LYS E1059    32678  28919  29465  -1326   2206   -433       N  
ATOM   3083  CA  LYS E1059      33.228   7.455 -30.647  1.00240.13           C  
ANISOU 3083  CA  LYS E1059    32793  28925  29520  -1368   2326   -467       C  
ATOM   3084  C   LYS E1059      34.463   6.589 -30.430  1.00239.62           C  
ANISOU 3084  C   LYS E1059    32664  28770  29612  -1390   2421   -535       C  
ATOM   3085  O   LYS E1059      35.131   6.198 -31.396  1.00239.86           O  
ANISOU 3085  O   LYS E1059    32734  28764  29637  -1447   2530   -596       O  
ATOM   3086  CB  LYS E1059      33.585   8.939 -30.564  1.00239.04           C  
ANISOU 3086  CB  LYS E1059    32685  28774  29364  -1335   2325   -405       C  
ATOM   3087  N   ASP E1060      34.789   6.286 -29.170  1.00212.88           N  
ANISOU 3087  N   ASP E1060    29178  25343  26363  -1344   2380   -526       N  
ATOM   3088  CA  ASP E1060      35.956   5.461 -28.877  1.00212.49           C  
ANISOU 3088  CA  ASP E1060    29061  25204  26473  -1356   2457   -588       C  
ATOM   3089  C   ASP E1060      35.803   4.030 -29.384  1.00212.56           C  
ANISOU 3089  C   ASP E1060    29068  25208  26488  -1406   2498   -661       C  
ATOM   3090  O   ASP E1060      36.813   3.355 -29.612  1.00210.70           O  
ANISOU 3090  O   ASP E1060    28803  24898  26356  -1434   2591   -728       O  
ATOM   3091  CB  ASP E1060      36.232   5.462 -27.371  1.00211.00           C  
ANISOU 3091  CB  ASP E1060    28773  24979  26419  -1290   2388   -556       C  
ATOM   3092  N   PHE E1061      34.569   3.553 -29.566  1.00304.83           N  
ANISOU 3092  N   PHE E1061    40782  36969  38070  -1418   2431   -652       N  
ATOM   3093  CA  PHE E1061      34.352   2.193 -30.050  1.00304.94           C  
ANISOU 3093  CA  PHE E1061    40796  36981  38086  -1468   2466   -723       C  
ATOM   3094  C   PHE E1061      34.641   2.075 -31.543  1.00305.40           C  
ANISOU 3094  C   PHE E1061    40938  37041  38059  -1538   2571   -783       C  
ATOM   3095  O   PHE E1061      35.404   1.200 -31.967  1.00306.26           O  
ANISOU 3095  O   PHE E1061    41033  37090  38243  -1580   2665   -860       O  
ATOM   3096  CB  PHE E1061      32.919   1.753 -29.746  1.00305.39           C  
ANISOU 3096  CB  PHE E1061    40853  37119  38063  -1460   2360   -697       C  
ATOM   3097  N   ARG E1062      34.034   2.946 -32.357  1.00173.47           N  
ANISOU 3097  N   ARG E1062    24321  20399  21192  -1552   2555   -749       N  
ATOM   3098  CA  ARG E1062      34.275   2.906 -33.797  1.00171.10           C  
ANISOU 3098  CA  ARG E1062    24114  20104  20792  -1620   2652   -801       C  
ATOM   3099  C   ARG E1062      35.719   3.251 -34.133  1.00168.99           C  
ANISOU 3099  C   ARG E1062    23848  19750  20610  -1640   2779   -835       C  
ATOM   3100  O   ARG E1062      36.245   2.800 -35.158  1.00163.95           O  
ANISOU 3100  O   ARG E1062    23256  19086  19950  -1703   2889   -906       O  
ATOM   3101  CB  ARG E1062      33.320   3.858 -34.520  1.00168.92           C  
ANISOU 3101  CB  ARG E1062    23938  19915  20328  -1622   2597   -747       C  
ATOM   3102  N   HIS E1063      36.371   4.057 -33.292  1.00286.09           N  
ANISOU 3102  N   HIS E1063    38628  34537  35537  -1590   2768   -790       N  
ATOM   3103  CA  HIS E1063      37.791   4.333 -33.471  1.00285.38           C  
ANISOU 3103  CA  HIS E1063    38520  34358  35553  -1606   2887   -828       C  
ATOM   3104  C   HIS E1063      38.647   3.162 -33.005  1.00282.29           C  
ANISOU 3104  C   HIS E1063    38032  33887  35337  -1611   2940   -902       C  
ATOM   3105  O   HIS E1063      39.683   2.868 -33.611  1.00280.19           O  
ANISOU 3105  O   HIS E1063    37766  33555  35137  -1655   3064   -973       O  
ATOM   3106  CB  HIS E1063      38.180   5.607 -32.721  1.00286.40           C  
ANISOU 3106  CB  HIS E1063    38624  34468  35728  -1550   2853   -758       C  
ATOM   3107  N   GLY E1064      38.227   2.482 -31.935  1.00168.77           N  
ANISOU 3107  N   GLY E1064    23576  19512  21038  -1568   2849   -887       N  
ATOM   3108  CA  GLY E1064      38.996   1.377 -31.388  1.00166.30           C  
ANISOU 3108  CA  GLY E1064    23172  19120  20897  -1564   2884   -948       C  
ATOM   3109  C   GLY E1064      39.099   0.179 -32.308  1.00161.07           C  
ANISOU 3109  C   GLY E1064    22530  18439  20228  -1631   2970  -1039       C  
ATOM   3110  O   GLY E1064      39.970  -0.676 -32.106  1.00155.05           O  
ANISOU 3110  O   GLY E1064    21701  17596  19613  -1638   3031  -1104       O  
ATOM   3111  N   PHE E1065      38.219   0.086 -33.304  1.00208.48           N  
ANISOU 3111  N   PHE E1065    28626  24517  26069  -1679   2972  -1048       N  
ATOM   3112  CA  PHE E1065      38.317  -0.957 -34.314  1.00207.64           C  
ANISOU 3112  CA  PHE E1065    28553  24399  25941  -1749   3062  -1140       C  
ATOM   3113  C   PHE E1065      39.097  -0.506 -35.542  1.00203.94           C  
ANISOU 3113  C   PHE E1065    28159  23908  25421  -1808   3196  -1188       C  
ATOM   3114  O   PHE E1065      39.773  -1.328 -36.172  1.00197.16           O  
ANISOU 3114  O   PHE E1065    27295  22996  24619  -1859   3306  -1280       O  
ATOM   3115  CB  PHE E1065      36.919  -1.421 -34.732  1.00206.68           C  
ANISOU 3115  CB  PHE E1065    28487  24370  25672  -1773   2990  -1132       C  
ATOM   3116  N   ASP E1066      39.027   0.783 -35.888  1.00183.11           N  
ANISOU 3116  N   ASP E1066    25590  21304  22679  -1802   3194  -1130       N  
ATOM   3117  CA  ASP E1066      39.778   1.290 -37.034  1.00179.85           C  
ANISOU 3117  CA  ASP E1066    25256  20868  22213  -1860   3326  -1170       C  
ATOM   3118  C   ASP E1066      41.281   1.259 -36.771  1.00175.44           C  
ANISOU 3118  C   ASP E1066    24622  20201  21836  -1860   3435  -1222       C  
ATOM   3119  O   ASP E1066      42.072   0.999 -37.686  1.00171.97           O  
ANISOU 3119  O   ASP E1066    24214  19717  21411  -1922   3572  -1301       O  
ATOM   3120  CB  ASP E1066      39.319   2.708 -37.372  1.00180.13           C  
ANISOU 3120  CB  ASP E1066    25382  20960  22097  -1848   3289  -1086       C  
ATOM   3121  N   ILE E1067      41.690   1.530 -35.528  1.00202.29           N  
ANISOU 3121  N   ILE E1067    27923  23559  25379  -1793   3376  -1183       N  
ATOM   3122  CA  ILE E1067      43.101   1.449 -35.156  1.00199.50           C  
ANISOU 3122  CA  ILE E1067    27483  23102  25216  -1785   3463  -1235       C  
ATOM   3123  C   ILE E1067      43.617   0.022 -35.315  1.00197.41           C  
ANISOU 3123  C   ILE E1067    27161  22778  25069  -1816   3532  -1337       C  
ATOM   3124  O   ILE E1067      44.716  -0.204 -35.835  1.00194.57           O  
ANISOU 3124  O   ILE E1067    26782  22346  24801  -1855   3663  -1418       O  
ATOM   3125  CB  ILE E1067      43.296   1.966 -33.716  1.00201.87           C  
ANISOU 3125  CB  ILE E1067    27688  23377  25635  -1700   3363  -1169       C  
ATOM   3126  CG1 ILE E1067      44.739   1.780 -33.253  1.00197.98           C  
ANISOU 3126  CG1 ILE E1067    27093  22777  25353  -1687   3439  -1229       C  
ATOM   3127  CG2 ILE E1067      42.332   1.299 -32.750  1.00203.63           C  
ANISOU 3127  CG2 ILE E1067    27864  23641  25866  -1651   3224  -1127       C  
ATOM   3128  CD1 ILE E1067      45.181   2.829 -32.284  1.00190.69           C  
ANISOU 3128  CD1 ILE E1067    26115  21830  24508  -1624   3386  -1168       C  
ATOM   3129  N   LEU E1068      42.835  -0.962 -34.861  1.00189.18           N  
ANISOU 3129  N   LEU E1068    26088  21762  24030  -1799   3447  -1336       N  
ATOM   3130  CA  LEU E1068      43.275  -2.352 -34.922  1.00188.11           C  
ANISOU 3130  CA  LEU E1068    25895  21566  24014  -1823   3502  -1427       C  
ATOM   3131  C   LEU E1068      43.393  -2.837 -36.362  1.00186.65           C  
ANISOU 3131  C   LEU E1068    25789  21385  23745  -1911   3629  -1515       C  
ATOM   3132  O   LEU E1068      44.329  -3.573 -36.696  1.00184.97           O  
ANISOU 3132  O   LEU E1068    25534  21095  23652  -1943   3739  -1610       O  
ATOM   3133  CB  LEU E1068      42.317  -3.241 -34.130  1.00189.65           C  
ANISOU 3133  CB  LEU E1068    26050  21790  24217  -1789   3381  -1399       C  
ATOM   3134  N   VAL E1069      42.456  -2.438 -37.229  1.00117.65           N  
ANISOU 3134  N   VAL E1069    17164  12736  14802  -1950   3615  -1488       N  
ATOM   3135  CA  VAL E1069      42.547  -2.825 -38.635  1.00112.78           C  
ANISOU 3135  CA  VAL E1069    16635  12130  14088  -2036   3734  -1569       C  
ATOM   3136  C   VAL E1069      43.834  -2.288 -39.243  1.00112.65           C  
ANISOU 3136  C   VAL E1069    16630  12045  14126  -2072   3884  -1620       C  
ATOM   3137  O   VAL E1069      44.523  -2.989 -39.992  1.00112.55           O  
ANISOU 3137  O   VAL E1069    16619  11982  14163  -2131   4013  -1722       O  
ATOM   3138  CB  VAL E1069      41.310  -2.348 -39.420  1.00110.87           C  
ANISOU 3138  CB  VAL E1069    16518  11999  13608  -2064   3679  -1521       C  
ATOM   3139  CG1 VAL E1069      41.445  -2.728 -40.887  1.00108.51           C  
ANISOU 3139  CG1 VAL E1069    16317  11710  13202  -2154   3804  -1606       C  
ATOM   3140  CG2 VAL E1069      40.042  -2.939 -38.837  1.00115.83           C  
ANISOU 3140  CG2 VAL E1069    17127  12692  14191  -2032   3538  -1481       C  
ATOM   3141  N   GLY E1070      44.180  -1.037 -38.926  1.00164.58           N  
ANISOU 3141  N   GLY E1070    23213  18618  20702  -2040   3874  -1553       N  
ATOM   3142  CA  GLY E1070      45.434  -0.480 -39.407  1.00163.96           C  
ANISOU 3142  CA  GLY E1070    23136  18469  20691  -2073   4018  -1600       C  
ATOM   3143  C   GLY E1070      46.645  -1.242 -38.903  1.00163.45           C  
ANISOU 3143  C   GLY E1070    22944  18297  20863  -2062   4089  -1685       C  
ATOM   3144  O   GLY E1070      47.568  -1.530 -39.667  1.00162.35           O  
ANISOU 3144  O   GLY E1070    22808  18099  20780  -2120   4239  -1779       O  
ATOM   3145  N   GLN E1071      46.659  -1.579 -37.610  1.00134.44           N  
ANISOU 3145  N   GLN E1071    19157  14594  17330  -1988   3983  -1654       N  
ATOM   3146  CA  GLN E1071      47.749  -2.390 -37.075  1.00132.96           C  
ANISOU 3146  CA  GLN E1071    18845  14302  17370  -1970   4033  -1732       C  
ATOM   3147  C   GLN E1071      47.698  -3.817 -37.600  1.00130.66           C  
ANISOU 3147  C   GLN E1071    18546  13988  17110  -2014   4088  -1827       C  
ATOM   3148  O   GLN E1071      48.747  -4.444 -37.778  1.00129.27           O  
ANISOU 3148  O   GLN E1071    18304  13724  17087  -2035   4195  -1924       O  
ATOM   3149  CB  GLN E1071      47.715  -2.384 -35.552  1.00131.60           C  
ANISOU 3149  CB  GLN E1071    18566  14109  17328  -1877   3896  -1668       C  
ATOM   3150  CG  GLN E1071      48.170  -1.082 -34.943  1.00128.04           C  
ANISOU 3150  CG  GLN E1071    18091  13647  16912  -1831   3868  -1603       C  
ATOM   3151  CD  GLN E1071      47.672  -0.930 -33.536  1.00129.98           C  
ANISOU 3151  CD  GLN E1071    18272  13911  17205  -1744   3704  -1515       C  
ATOM   3152  OE1 GLN E1071      46.472  -0.816 -33.317  1.00131.74           O  
ANISOU 3152  OE1 GLN E1071    18545  14216  17294  -1726   3596  -1440       O  
ATOM   3153  NE2 GLN E1071      48.585  -0.923 -32.571  1.00129.75           N  
ANISOU 3153  NE2 GLN E1071    18130  13805  17366  -1689   3685  -1525       N  
ATOM   3154  N   ILE E1072      46.497  -4.354 -37.830  1.00126.85           N  
ANISOU 3154  N   ILE E1072    18124  13581  16492  -2028   4016  -1804       N  
ATOM   3155  CA  ILE E1072      46.386  -5.612 -38.563  1.00129.29           C  
ANISOU 3155  CA  ILE E1072    18449  13878  16798  -2086   4083  -1900       C  
ATOM   3156  C   ILE E1072      46.881  -5.427 -39.990  1.00129.47           C  
ANISOU 3156  C   ILE E1072    18558  13898  16736  -2174   4246  -1978       C  
ATOM   3157  O   ILE E1072      47.601  -6.276 -40.529  1.00127.47           O  
ANISOU 3157  O   ILE E1072    18278  13581  16575  -2220   4364  -2089       O  
ATOM   3158  CB  ILE E1072      44.937  -6.133 -38.530  1.00130.80           C  
ANISOU 3158  CB  ILE E1072    18690  14158  16852  -2085   3969  -1857       C  
ATOM   3159  N   ASP E1073      46.506  -4.309 -40.621  1.00146.33           N  
ANISOU 3159  N   ASP E1073    20803  16101  18696  -2199   4255  -1922       N  
ATOM   3160  CA  ASP E1073      46.997  -4.004 -41.961  1.00144.12           C  
ANISOU 3160  CA  ASP E1073    20618  15817  18323  -2283   4412  -1987       C  
ATOM   3161  C   ASP E1073      48.508  -3.821 -41.961  1.00143.76           C  
ANISOU 3161  C   ASP E1073    20500  15667  18455  -2294   4549  -2057       C  
ATOM   3162  O   ASP E1073      49.188  -4.210 -42.918  1.00144.07           O  
ANISOU 3162  O   ASP E1073    20567  15666  18509  -2366   4703  -2160       O  
ATOM   3163  CB  ASP E1073      46.306  -2.750 -42.499  1.00142.18           C  
ANISOU 3163  CB  ASP E1073    20502  15658  17860  -2297   4380  -1898       C  
ATOM   3164  CG  ASP E1073      44.979  -3.056 -43.163  1.00143.01           C  
ANISOU 3164  CG  ASP E1073    20714  15865  17757  -2328   4313  -1878       C  
ATOM   3165  OD1 ASP E1073      44.957  -3.888 -44.096  1.00145.33           O  
ANISOU 3165  OD1 ASP E1073    21055  16161  18001  -2396   4398  -1967       O  
ATOM   3166  OD2 ASP E1073      43.957  -2.469 -42.747  1.00143.31           O1-
ANISOU 3166  OD2 ASP E1073    20788  15981  17685  -2283   4175  -1776       O1-
ATOM   3167  N   ASP E1074      49.051  -3.226 -40.893  1.00176.23           N  
ANISOU 3167  N   ASP E1074    24519  19735  22706  -2225   4495  -2007       N  
ATOM   3168  CA  ASP E1074      50.499  -3.083 -40.775  1.00176.70           C  
ANISOU 3168  CA  ASP E1074    24491  19690  22955  -2228   4613  -2077       C  
ATOM   3169  C   ASP E1074      51.186  -4.444 -40.778  1.00174.91           C  
ANISOU 3169  C   ASP E1074    24171  19382  22905  -2242   4684  -2196       C  
ATOM   3170  O   ASP E1074      52.274  -4.601 -41.345  1.00172.39           O  
ANISOU 3170  O   ASP E1074    23823  18990  22687  -2289   4838  -2296       O  
ATOM   3171  CB  ASP E1074      50.852  -2.318 -39.497  1.00175.53           C  
ANISOU 3171  CB  ASP E1074    24249  19514  22931  -2143   4517  -2001       C  
ATOM   3172  CG  ASP E1074      50.445  -0.856 -39.551  1.00175.28           C  
ANISOU 3172  CG  ASP E1074    24302  19543  22754  -2134   4478  -1898       C  
ATOM   3173  OD1 ASP E1074      49.928  -0.417 -40.600  1.00175.97           O1-
ANISOU 3173  OD1 ASP E1074    24523  19691  22646  -2193   4528  -1883       O1-
ATOM   3174  OD2 ASP E1074      50.637  -0.145 -38.540  1.00173.03           O  
ANISOU 3174  OD2 ASP E1074    23951  19242  22549  -2066   4396  -1831       O  
ATOM   3175  N   ALA E1075      50.564  -5.440 -40.145  1.00167.60           N  
ANISOU 3175  N   ALA E1075    23196  18465  22022  -2202   4576  -2187       N  
ATOM   3176  CA  ALA E1075      51.184  -6.756 -40.045  1.00167.32           C  
ANISOU 3176  CA  ALA E1075    23066  18345  22163  -2206   4629  -2293       C  
ATOM   3177  C   ALA E1075      51.100  -7.532 -41.354  1.00166.19           C  
ANISOU 3177  C   ALA E1075    22998  18210  21935  -2298   4756  -2396       C  
ATOM   3178  O   ALA E1075      51.948  -8.395 -41.609  1.00166.11           O  
ANISOU 3178  O   ALA E1075    22922  18117  22074  -2324   4861  -2510       O  
ATOM   3179  CB  ALA E1075      50.543  -7.551 -38.908  1.00168.72           C  
ANISOU 3179  CB  ALA E1075    23170  18523  22412  -2134   4472  -2246       C  
ATOM   3180  N   LEU E1076      50.085  -7.258 -42.184  1.00116.45           N  
ANISOU 3180  N   LEU E1076    16835  12010  15401  -2348   4744  -2361       N  
ATOM   3181  CA  LEU E1076      49.961  -7.965 -43.458  1.00117.36           C  
ANISOU 3181  CA  LEU E1076    17031  12140  15420  -2438   4860  -2458       C  
ATOM   3182  C   LEU E1076      51.195  -7.767 -44.328  1.00118.60           C  
ANISOU 3182  C   LEU E1076    17195  12230  15639  -2503   5057  -2561       C  
ATOM   3183  O   LEU E1076      51.692  -8.722 -44.935  1.00119.56           O  
ANISOU 3183  O   LEU E1076    17297  12300  15832  -2554   5172  -2681       O  
ATOM   3184  CB  LEU E1076      48.709  -7.507 -44.210  1.00118.84           C  
ANISOU 3184  CB  LEU E1076    17370  12448  15336  -2476   4810  -2396       C  
ATOM   3185  CG  LEU E1076      47.378  -8.246 -44.014  1.00118.15           C  
ANISOU 3185  CG  LEU E1076    17307  12433  15150  -2462   4677  -2361       C  
ATOM   3186  CD1 LEU E1076      47.377  -9.555 -44.789  1.00117.69           C  
ANISOU 3186  CD1 LEU E1076    17260  12354  15103  -2527   4763  -2482       C  
ATOM   3187  CD2 LEU E1076      47.057  -8.488 -42.559  1.00118.32           C  
ANISOU 3187  CD2 LEU E1076    17220  12439  15296  -2369   4522  -2288       C  
ATOM   3188  N   LYS E1077      51.701  -6.535 -44.408  1.00130.78           N  
ANISOU 3188  N   LYS E1077    18764  13770  17156  -2504   5102  -2519       N  
ATOM   3189  CA  LYS E1077      52.911  -6.293 -45.185  1.00132.36           C  
ANISOU 3189  CA  LYS E1077    18966  13902  17424  -2568   5295  -2616       C  
ATOM   3190  C   LYS E1077      54.090  -7.084 -44.626  1.00129.13           C  
ANISOU 3190  C   LYS E1077    18396  13373  17294  -2541   5356  -2715       C  
ATOM   3191  O   LYS E1077      54.856  -7.692 -45.384  1.00125.19           O  
ANISOU 3191  O   LYS E1077    17883  12815  16867  -2604   5513  -2841       O  
ATOM   3192  CB  LYS E1077      53.225  -4.795 -45.215  1.00132.33           C  
ANISOU 3192  CB  LYS E1077    19010  13912  17358  -2566   5319  -2542       C  
ATOM   3193  N   LEU E1078      54.241  -7.104 -43.297  1.00157.87           N  
ANISOU 3193  N   LEU E1078    21913  16976  21094  -2448   5230  -2661       N  
ATOM   3194  CA  LEU E1078      55.355  -7.812 -42.674  1.00157.56           C  
ANISOU 3194  CA  LEU E1078    21718  16822  21327  -2411   5269  -2747       C  
ATOM   3195  C   LEU E1078      55.274  -9.320 -42.882  1.00158.50           C  
ANISOU 3195  C   LEU E1078    21799  16903  21521  -2428   5291  -2842       C  
ATOM   3196  O   LEU E1078      56.267 -10.022 -42.653  1.00157.02           O  
ANISOU 3196  O   LEU E1078    21494  16614  21552  -2415   5357  -2939       O  
ATOM   3197  CB  LEU E1078      55.408  -7.487 -41.179  1.00156.47           C  
ANISOU 3197  CB  LEU E1078    21470  16661  21319  -2303   5110  -2657       C  
ATOM   3198  N   ALA E1079      54.112  -9.833 -43.290  1.00116.77           N  
ANISOU 3198  N   ALA E1079    16607  11697  16065  -2455   5235  -2817       N  
ATOM   3199  CA  ALA E1079      53.986 -11.245 -43.630  1.00117.35           C  
ANISOU 3199  CA  ALA E1079    16659  11739  16190  -2483   5269  -2913       C  
ATOM   3200  C   ALA E1079      54.418 -11.516 -45.068  1.00118.81           C  
ANISOU 3200  C   ALA E1079    16918  11914  16311  -2590   5463  -3036       C  
ATOM   3201  O   ALA E1079      55.055 -12.539 -45.344  1.00119.67           O  
ANISOU 3201  O   ALA E1079    16963  11945  16562  -2615   5559  -3158       O  
ATOM   3202  CB  ALA E1079      52.547 -11.708 -43.411  1.00116.55           C  
ANISOU 3202  CB  ALA E1079    16619  11724  15942  -2467   5123  -2838       C  
ATOM   3203  N   ASN E1080      54.083 -10.605 -45.988  1.00129.90           N  
ANISOU 3203  N   ASN E1080    18459  13395  17502  -2652   5522  -3007       N  
ATOM   3204  CA  ASN E1080      54.375 -10.809 -47.404  1.00131.32           C  
ANISOU 3204  CA  ASN E1080    18731  13577  17586  -2759   5702  -3116       C  
ATOM   3205  C   ASN E1080      55.860 -11.063 -47.634  1.00132.40           C  
ANISOU 3205  C   ASN E1080    18773  13599  17935  -2786   5875  -3245       C  
ATOM   3206  O   ASN E1080      56.239 -11.976 -48.378  1.00133.50           O  
ANISOU 3206  O   ASN E1080    18909  13696  18120  -2846   6001  -3373       O  
ATOM   3207  CB  ASN E1080      53.903  -9.598 -48.209  1.00131.48           C  
ANISOU 3207  CB  ASN E1080    18909  13688  17358  -2810   5730  -3046       C  
ATOM   3208  N   GLU E1081      56.716 -10.271 -46.998  1.00161.59           N  
ANISOU 3208  N   GLU E1081    22387  17242  21769  -2742   5884  -3218       N  
ATOM   3209  CA  GLU E1081      58.154 -10.490 -47.084  1.00161.36           C  
ANISOU 3209  CA  GLU E1081    22247  17097  21964  -2758   6035  -3340       C  
ATOM   3210  C   GLU E1081      58.583 -11.617 -46.148  1.00159.98           C  
ANISOU 3210  C   GLU E1081    21910  16833  22044  -2687   5972  -3393       C  
ATOM   3211  O   GLU E1081      58.073 -11.742 -45.033  1.00160.16           O  
ANISOU 3211  O   GLU E1081    21875  16866  22113  -2599   5796  -3301       O  
ATOM   3212  CB  GLU E1081      58.917  -9.206 -46.752  1.00170.47           C  
ANISOU 3212  CB  GLU E1081    23370  18227  23175  -2738   6067  -3296       C  
ATOM   3213  N   LYS E1085      57.107 -13.786 -39.581  1.00167.92           N  
ANISOU 3213  N   LYS E1085    22456  17725  23622  -2188   5099  -3037       N  
ATOM   3214  CA  LYS E1085      58.357 -13.886 -38.837  1.00169.02           C  
ANISOU 3214  CA  LYS E1085    22445  17750  24023  -2127   5108  -3086       C  
ATOM   3215  C   LYS E1085      58.560 -12.643 -37.989  1.00171.21           C  
ANISOU 3215  C   LYS E1085    22694  18048  24311  -2066   5021  -2986       C  
ATOM   3216  O   LYS E1085      58.482 -12.695 -36.761  1.00170.75           O  
ANISOU 3216  O   LYS E1085    22563  17969  24346  -1976   4872  -2912       O  
ATOM   3217  CB  LYS E1085      59.539 -14.077 -39.789  1.00169.18           C  
ANISOU 3217  CB  LYS E1085    22426  17694  24160  -2193   5311  -3239       C  
ATOM   3218  N   GLU E1086      58.817 -11.521 -38.656  1.00154.09           N  
ANISOU 3218  N   GLU E1086    20584  15918  22043  -2118   5116  -2984       N  
ATOM   3219  CA  GLU E1086      58.911 -10.235 -37.981  1.00153.19           C  
ANISOU 3219  CA  GLU E1086    20461  15834  21909  -2072   5042  -2886       C  
ATOM   3220  C   GLU E1086      57.547  -9.614 -37.728  1.00152.48           C  
ANISOU 3220  C   GLU E1086    20482  15864  21590  -2057   4908  -2743       C  
ATOM   3221  O   GLU E1086      57.474  -8.541 -37.120  1.00153.21           O  
ANISOU 3221  O   GLU E1086    20576  15990  21649  -2015   4831  -2651       O  
ATOM   3222  CB  GLU E1086      59.777  -9.271 -38.795  1.00157.17           C  
ANISOU 3222  CB  GLU E1086    20984  16325  22410  -2135   5204  -2943       C  
ATOM   3223  N   ALA E1087      56.469 -10.258 -38.180  1.00144.72           N  
ANISOU 3223  N   ALA E1087    19589  14944  20452  -2091   4878  -2726       N  
ATOM   3224  CA  ALA E1087      55.122  -9.774 -37.911  1.00144.54           C  
ANISOU 3224  CA  ALA E1087    19663  15033  20221  -2074   4744  -2596       C  
ATOM   3225  C   ALA E1087      54.693 -10.012 -36.470  1.00149.24           C  
ANISOU 3225  C   ALA E1087    20188  15624  20893  -1975   4558  -2504       C  
ATOM   3226  O   ALA E1087      53.621  -9.540 -36.077  1.00150.76           O  
ANISOU 3226  O   ALA E1087    20444  15904  20933  -1951   4437  -2392       O  
ATOM   3227  CB  ALA E1087      54.124 -10.434 -38.865  1.00138.66           C  
ANISOU 3227  CB  ALA E1087    19031  14356  19297  -2144   4772  -2618       C  
ATOM   3228  N   GLN E1088      55.493 -10.738 -35.682  1.00150.28           N  
ANISOU 3228  N   GLN E1088    20191  15654  21253  -1918   4534  -2550       N  
ATOM   3229  CA  GLN E1088      55.143 -10.987 -34.287  1.00148.42           C  
ANISOU 3229  CA  GLN E1088    19892  15408  21092  -1823   4359  -2464       C  
ATOM   3230  C   GLN E1088      55.138  -9.702 -33.468  1.00151.36           C  
ANISOU 3230  C   GLN E1088    20253  15817  21438  -1767   4265  -2360       C  
ATOM   3231  O   GLN E1088      54.337  -9.566 -32.536  1.00151.13           O  
ANISOU 3231  O   GLN E1088    20234  15835  21355  -1709   4114  -2253       O  
ATOM   3232  CB  GLN E1088      56.111 -12.001 -33.677  1.00148.27           C  
ANISOU 3232  CB  GLN E1088    19741  15265  21330  -1773   4359  -2541       C  
ATOM   3233  N   ALA E1089      56.031  -8.759 -33.788  1.00183.58           N  
ANISOU 3233  N   ALA E1089    24314  19875  25562  -1784   4357  -2391       N  
ATOM   3234  CA  ALA E1089      56.062  -7.486 -33.073  1.00185.07           C  
ANISOU 3234  CA  ALA E1089    24494  20096  25727  -1736   4278  -2299       C  
ATOM   3235  C   ALA E1089      54.778  -6.693 -33.288  1.00186.67           C  
ANISOU 3235  C   ALA E1089    24825  20422  25680  -1756   4213  -2189       C  
ATOM   3236  O   ALA E1089      54.231  -6.118 -32.339  1.00187.34           O  
ANISOU 3236  O   ALA E1089    24908  20550  25722  -1694   4074  -2082       O  
ATOM   3237  CB  ALA E1089      57.275  -6.666 -33.512  1.00183.86           C  
ANISOU 3237  CB  ALA E1089    24300  19892  25668  -1764   4408  -2366       C  
ATOM   3238  N   ALA E1090      54.288  -6.642 -34.528  1.00266.69           N  
ANISOU 3238  N   ALA E1090    35072  30614  35645  -1840   4310  -2215       N  
ATOM   3239  CA  ALA E1090      53.029  -5.953 -34.796  1.00268.94           C  
ANISOU 3239  CA  ALA E1090    35481  31015  35691  -1858   4245  -2115       C  
ATOM   3240  C   ALA E1090      51.864  -6.648 -34.104  1.00268.77           C  
ANISOU 3240  C   ALA E1090    35470  31043  35608  -1816   4096  -2046       C  
ATOM   3241  O   ALA E1090      50.947  -5.985 -33.605  1.00268.75           O  
ANISOU 3241  O   ALA E1090    35514  31118  35482  -1783   3979  -1937       O  
ATOM   3242  CB  ALA E1090      52.787  -5.865 -36.302  1.00268.09           C  
ANISOU 3242  CB  ALA E1090    35491  30952  35420  -1957   4379  -2166       C  
ATOM   3243  N   ALA E1091      51.881  -7.983 -34.072  1.00185.08           N  
ANISOU 3243  N   ALA E1091    24830  20396  25098  -1819   4101  -2109       N  
ATOM   3244  CA  ALA E1091      50.847  -8.722 -33.356  1.00183.61           C  
ANISOU 3244  CA  ALA E1091    24645  20243  24874  -1780   3966  -2048       C  
ATOM   3245  C   ALA E1091      50.856  -8.378 -31.870  1.00185.13           C  
ANISOU 3245  C   ALA E1091    24764  20421  25156  -1684   3820  -1958       C  
ATOM   3246  O   ALA E1091      49.794  -8.269 -31.244  1.00183.84           O  
ANISOU 3246  O   ALA E1091    24634  20325  24891  -1651   3692  -1864       O  
ATOM   3247  CB  ALA E1091      51.036 -10.225 -33.565  1.00179.79           C  
ANISOU 3247  CB  ALA E1091    24121  19692  24497  -1799   4010  -2140       C  
ATOM   3248  N   GLU E1092      52.047  -8.213 -31.287  1.00180.49           N  
ANISOU 3248  N   GLU E1092    24074  19746  24759  -1639   3835  -1990       N  
ATOM   3249  CA  GLU E1092      52.136  -7.790 -29.892  1.00179.30           C  
ANISOU 3249  CA  GLU E1092    23855  19581  24689  -1549   3699  -1908       C  
ATOM   3250  C   GLU E1092      51.555  -6.394 -29.702  1.00176.09           C  
ANISOU 3250  C   GLU E1092    23508  19263  24134  -1537   3639  -1808       C  
ATOM   3251  O   GLU E1092      50.825  -6.143 -28.736  1.00176.03           O  
ANISOU 3251  O   GLU E1092    23504  19300  24079  -1481   3500  -1710       O  
ATOM   3252  CB  GLU E1092      53.589  -7.837 -29.421  1.00180.26           C  
ANISOU 3252  CB  GLU E1092    23855  19592  25044  -1508   3735  -1974       C  
ATOM   3253  N   GLN E1093      51.870  -5.472 -30.613  1.00222.51           N  
ANISOU 3253  N   GLN E1093    29439  25166  29938  -1590   3744  -1830       N  
ATOM   3254  CA  GLN E1093      51.251  -4.153 -30.591  1.00225.16           C  
ANISOU 3254  CA  GLN E1093    29846  25587  30117  -1586   3697  -1736       C  
ATOM   3255  C   GLN E1093      49.777  -4.199 -30.967  1.00223.49           C  
ANISOU 3255  C   GLN E1093    29744  25481  29689  -1613   3638  -1671       C  
ATOM   3256  O   GLN E1093      49.073  -3.200 -30.780  1.00221.50           O  
ANISOU 3256  O   GLN E1093    29549  25306  29306  -1597   3569  -1582       O  
ATOM   3257  CB  GLN E1093      51.996  -3.206 -31.534  1.00224.82           C  
ANISOU 3257  CB  GLN E1093    29836  25533  30051  -1641   3834  -1780       C  
ATOM   3258  N   LEU E1094      49.302  -5.326 -31.497  1.00152.40           N  
ANISOU 3258  N   LEU E1094    20769  16484  20651  -1653   3664  -1719       N  
ATOM   3259  CA  LEU E1094      47.910  -5.477 -31.892  1.00152.43           C  
ANISOU 3259  CA  LEU E1094    20870  16587  20460  -1682   3610  -1670       C  
ATOM   3260  C   LEU E1094      47.031  -5.965 -30.742  1.00153.60           C  
ANISOU 3260  C   LEU E1094    20989  16761  20611  -1621   3456  -1596       C  
ATOM   3261  O   LEU E1094      45.871  -5.548 -30.637  1.00154.74           O  
ANISOU 3261  O   LEU E1094    21198  16997  20599  -1616   3371  -1516       O  
ATOM   3262  CB  LEU E1094      47.820  -6.417 -33.101  1.00152.50           C  
ANISOU 3262  CB  LEU E1094    20930  16592  20422  -1762   3720  -1764       C  
ATOM   3263  CG  LEU E1094      46.477  -6.954 -33.590  1.00155.26           C  
ANISOU 3263  CG  LEU E1094    21364  17027  20601  -1799   3677  -1745       C  
ATOM   3264  CD1 LEU E1094      46.524  -7.211 -35.082  1.00150.24           C  
ANISOU 3264  CD1 LEU E1094    20809  16408  19868  -1890   3812  -1830       C  
ATOM   3265  CD2 LEU E1094      46.187  -8.249 -32.868  1.00155.06           C  
ANISOU 3265  CD2 LEU E1094    21277  16964  20675  -1770   3610  -1758       C  
ATOM   3266  N   LYS E1095      47.550  -6.845 -29.879  1.00147.60           N  
ANISOU 3266  N   LYS E1095    20135  15920  20026  -1574   3420  -1619       N  
ATOM   3267  CA  LYS E1095      46.762  -7.309 -28.738  1.00145.71           C  
ANISOU 3267  CA  LYS E1095    19871  15698  19793  -1517   3278  -1546       C  
ATOM   3268  C   LYS E1095      46.498  -6.164 -27.764  1.00145.52           C  
ANISOU 3268  C   LYS E1095    19839  15718  19735  -1454   3168  -1442       C  
ATOM   3269  O   LYS E1095      45.363  -5.976 -27.307  1.00146.69           O  
ANISOU 3269  O   LYS E1095    20027  15942  19766  -1435   3066  -1361       O  
ATOM   3270  CB  LYS E1095      47.477  -8.476 -28.044  1.00145.07           C  
ANISOU 3270  CB  LYS E1095    19696  15512  19912  -1479   3267  -1595       C  
ATOM   3271  CG  LYS E1095      47.021  -8.803 -26.606  1.00142.47           C  
ANISOU 3271  CG  LYS E1095    19323  15175  19633  -1404   3119  -1515       C  
ATOM   3272  CD  LYS E1095      45.499  -8.872 -26.442  1.00141.52           C  
ANISOU 3272  CD  LYS E1095    19274  15153  19343  -1412   3030  -1439       C  
ATOM   3273  CE  LYS E1095      45.100  -8.971 -24.973  1.00138.41           C  
ANISOU 3273  CE  LYS E1095    18842  14757  18991  -1337   2889  -1352       C  
ATOM   3274  NZ  LYS E1095      43.630  -9.146 -24.786  1.00134.99           N  
ANISOU 3274  NZ  LYS E1095    18470  14412  18409  -1348   2809  -1287       N  
ATOM   3275  N   THR E1096      47.533  -5.381 -27.437  1.00117.63           N  
ANISOU 3275  N   THR E1096    16252  12137  16305  -1422   3190  -1447       N  
ATOM   3276  CA  THR E1096      47.330  -4.246 -26.540  1.00118.01           C  
ANISOU 3276  CA  THR E1096    16293  12224  16323  -1364   3092  -1354       C  
ATOM   3277  C   THR E1096      46.277  -3.287 -27.082  1.00118.09           C  
ANISOU 3277  C   THR E1096    16403  12343  16121  -1394   3073  -1289       C  
ATOM   3278  O   THR E1096      45.509  -2.707 -26.305  1.00116.69           O  
ANISOU 3278  O   THR E1096    16238  12224  15872  -1350   2961  -1199       O  
ATOM   3279  CB  THR E1096      48.648  -3.505 -26.290  1.00116.51           C  
ANISOU 3279  CB  THR E1096    16032  11965  16271  -1337   3136  -1382       C  
ATOM   3280  OG1 THR E1096      48.380  -2.228 -25.691  1.00112.75           O  
ANISOU 3280  OG1 THR E1096    15568  11539  15732  -1297   3060  -1296       O  
ATOM   3281  CG2 THR E1096      49.421  -3.299 -27.578  1.00117.73           C  
ANISOU 3281  CG2 THR E1096    16209  12091  16431  -1407   3296  -1469       C  
ATOM   3282  N   THR E1097      46.213  -3.116 -28.406  1.00161.92           N  
ANISOU 3282  N   THR E1097    22029  17924  21571  -1466   3180  -1334       N  
ATOM   3283  CA  THR E1097      45.122  -2.347 -28.998  1.00162.35           C  
ANISOU 3283  CA  THR E1097    22186  18083  21416  -1495   3157  -1275       C  
ATOM   3284  C   THR E1097      43.778  -3.023 -28.760  1.00164.15           C  
ANISOU 3284  C   THR E1097    22448  18379  21542  -1493   3062  -1234       C  
ATOM   3285  O   THR E1097      42.792  -2.365 -28.409  1.00165.64           O  
ANISOU 3285  O   THR E1097    22677  18648  21612  -1470   2968  -1150       O  
ATOM   3286  CB  THR E1097      45.350  -2.154 -30.494  1.00161.22           C  
ANISOU 3286  CB  THR E1097    22120  17951  21183  -1576   3293  -1337       C  
ATOM   3287  OG1 THR E1097      46.747  -1.966 -30.754  1.00159.55           O  
ANISOU 3287  OG1 THR E1097    21860  17654  21108  -1589   3405  -1406       O  
ATOM   3288  CG2 THR E1097      44.554  -0.956 -30.982  1.00160.26           C  
ANISOU 3288  CG2 THR E1097    22097  17922  20871  -1590   3268  -1266       C  
ATOM   3289  N   ARG E1098      43.714  -4.340 -28.974  1.00203.69           N  
ANISOU 3289  N   ARG E1098    27440  23355  26598  -1520   3090  -1295       N  
ATOM   3290  CA  ARG E1098      42.480  -5.068 -28.700  1.00204.85           C  
ANISOU 3290  CA  ARG E1098    27611  23558  26665  -1520   3004  -1262       C  
ATOM   3291  C   ARG E1098      42.071  -4.910 -27.244  1.00206.64           C  
ANISOU 3291  C   ARG E1098    27788  23793  26934  -1444   2869  -1177       C  
ATOM   3292  O   ARG E1098      40.881  -4.780 -26.930  1.00207.08           O  
ANISOU 3292  O   ARG E1098    27880  23928  26875  -1434   2779  -1113       O  
ATOM   3293  CB  ARG E1098      42.648  -6.546 -29.058  1.00202.44           C  
ANISOU 3293  CB  ARG E1098    27284  23198  26435  -1556   3060  -1347       C  
ATOM   3294  N   ASN E1099      43.051  -4.905 -26.341  1.00190.43           N  
ANISOU 3294  N   ASN E1099    25652  21660  25044  -1390   2853  -1177       N  
ATOM   3295  CA  ASN E1099      42.765  -4.666 -24.934  1.00189.60           C  
ANISOU 3295  CA  ASN E1099    25502  21559  24977  -1316   2727  -1096       C  
ATOM   3296  C   ASN E1099      42.252  -3.250 -24.699  1.00191.06           C  
ANISOU 3296  C   ASN E1099    25724  21822  25049  -1292   2667  -1014       C  
ATOM   3297  O   ASN E1099      41.453  -3.029 -23.782  1.00193.72           O  
ANISOU 3297  O   ASN E1099    26058  22204  25341  -1249   2557   -939       O  
ATOM   3298  CB  ASN E1099      44.020  -4.948 -24.105  1.00187.81           C  
ANISOU 3298  CB  ASN E1099    25181  21227  24953  -1265   2726  -1122       C  
ATOM   3299  CG  ASN E1099      44.059  -4.163 -22.815  1.00189.62           C  
ANISOU 3299  CG  ASN E1099    25370  21462  25216  -1190   2617  -1042       C  
ATOM   3300  OD1 ASN E1099      44.483  -3.007 -22.790  1.00188.98           O  
ANISOU 3300  OD1 ASN E1099    25285  21391  25126  -1173   2624  -1021       O  
ATOM   3301  ND2 ASN E1099      43.607  -4.784 -21.733  1.00192.27           N  
ANISOU 3301  ND2 ASN E1099    25678  21789  25586  -1145   2517   -997       N  
ATOM   3302  N   ALA E1100      42.688  -2.284 -25.513  1.00223.91           N  
ANISOU 3302  N   ALA E1100    29919  25995  29162  -1319   2741  -1029       N  
ATOM   3303  CA  ALA E1100      42.236  -0.906 -25.336  1.00226.83           C  
ANISOU 3303  CA  ALA E1100    30326  26431  29427  -1295   2689   -952       C  
ATOM   3304  C   ALA E1100      40.737  -0.775 -25.576  1.00228.94           C  
ANISOU 3304  C   ALA E1100    30667  26804  29515  -1312   2623   -898       C  
ATOM   3305  O   ALA E1100      40.043  -0.068 -24.835  1.00228.69           O  
ANISOU 3305  O   ALA E1100    30640  26828  29426  -1268   2525   -820       O  
ATOM   3306  CB  ALA E1100      43.011   0.032 -26.262  1.00226.80           C  
ANISOU 3306  CB  ALA E1100    30355  26414  29407  -1329   2793   -983       C  
ATOM   3307  N   TYR E1101      40.216  -1.442 -26.610  1.00190.81           N  
ANISOU 3307  N   TYR E1101    25894  22006  24598  -1374   2675   -944       N  
ATOM   3308  CA  TYR E1101      38.774  -1.459 -26.824  1.00190.97           C  
ANISOU 3308  CA  TYR E1101    25976  22124  24459  -1389   2607   -902       C  
ATOM   3309  C   TYR E1101      38.060  -2.461 -25.924  1.00187.93           C  
ANISOU 3309  C   TYR E1101    25551  21744  24109  -1366   2523   -884       C  
ATOM   3310  O   TYR E1101      36.826  -2.444 -25.862  1.00186.68           O  
ANISOU 3310  O   TYR E1101    25429  21667  23836  -1370   2452   -843       O  
ATOM   3311  CB  TYR E1101      38.455  -1.698 -28.315  1.00189.99           C  
ANISOU 3311  CB  TYR E1101    25934  22038  24216  -1466   2690   -957       C  
ATOM   3312  CG  TYR E1101      38.507  -3.125 -28.846  1.00185.92           C  
ANISOU 3312  CG  TYR E1101    25413  21489  23740  -1516   2750  -1040       C  
ATOM   3313  CD1 TYR E1101      37.568  -4.081 -28.469  1.00186.67           C  
ANISOU 3313  CD1 TYR E1101    25498  21612  23817  -1518   2685  -1035       C  
ATOM   3314  CD2 TYR E1101      39.468  -3.494 -29.778  1.00183.86           C  
ANISOU 3314  CD2 TYR E1101    25161  21169  23530  -1565   2878  -1126       C  
ATOM   3315  CE1 TYR E1101      37.614  -5.370 -28.970  1.00189.48           C  
ANISOU 3315  CE1 TYR E1101    25849  21933  24210  -1565   2742  -1113       C  
ATOM   3316  CE2 TYR E1101      39.515  -4.778 -30.291  1.00184.72           C  
ANISOU 3316  CE2 TYR E1101    25266  21246  23675  -1611   2936  -1206       C  
ATOM   3317  CZ  TYR E1101      38.589  -5.714 -29.882  1.00188.01           C  
ANISOU 3317  CZ  TYR E1101    25671  21688  24077  -1610   2866  -1199       C  
ATOM   3318  OH  TYR E1101      38.635  -6.996 -30.388  1.00184.38           O  
ANISOU 3318  OH  TYR E1101    25207  21193  23657  -1658   2925  -1280       O  
ATOM   3319  N   ILE E1102      38.798  -3.332 -25.236  1.00150.17           N  
ANISOU 3319  N   ILE E1102    20698  16876  19484  -1344   2530   -914       N  
ATOM   3320  CA  ILE E1102      38.200  -4.117 -24.162  1.00151.38           C  
ANISOU 3320  CA  ILE E1102    20812  17026  19678  -1310   2441   -881       C  
ATOM   3321  C   ILE E1102      37.908  -3.228 -22.957  1.00152.83           C  
ANISOU 3321  C   ILE E1102    20973  17239  19858  -1243   2335   -792       C  
ATOM   3322  O   ILE E1102      36.820  -3.281 -22.373  1.00152.43           O  
ANISOU 3322  O   ILE E1102    20933  17248  19737  -1227   2249   -738       O  
ATOM   3323  CB  ILE E1102      39.112  -5.300 -23.788  1.00149.53           C  
ANISOU 3323  CB  ILE E1102    20515  16686  19614  -1302   2477   -937       C  
ATOM   3324  N   GLN E1103      38.876  -2.389 -22.573  1.00254.01           N  
ANISOU 3324  N   GLN E1103    33752  30012  32749  -1203   2343   -778       N  
ATOM   3325  CA  GLN E1103      38.680  -1.498 -21.432  1.00253.35           C  
ANISOU 3325  CA  GLN E1103    33644  29952  32665  -1139   2246   -699       C  
ATOM   3326  C   GLN E1103      37.565  -0.497 -21.699  1.00257.59           C  
ANISOU 3326  C   GLN E1103    34241  30594  33037  -1144   2200   -641       C  
ATOM   3327  O   GLN E1103      36.775  -0.183 -20.801  1.00259.65           O  
ANISOU 3327  O   GLN E1103    34496  30902  33257  -1105   2104   -576       O  
ATOM   3328  CB  GLN E1103      39.983  -0.770 -21.100  1.00253.72           C  
ANISOU 3328  CB  GLN E1103    33642  29933  32827  -1103   2272   -707       C  
ATOM   3329  N   LYS E1104      37.499   0.032 -22.922  1.00235.07           N  
ANISOU 3329  N   LYS E1104    31449  27777  30090  -1190   2266   -664       N  
ATOM   3330  CA  LYS E1104      36.387   0.902 -23.289  1.00233.78           C  
ANISOU 3330  CA  LYS E1104    31348  27712  29764  -1196   2220   -613       C  
ATOM   3331  C   LYS E1104      35.064   0.148 -23.240  1.00234.15           C  
ANISOU 3331  C   LYS E1104    31416  27824  29726  -1214   2162   -602       C  
ATOM   3332  O   LYS E1104      34.051   0.684 -22.775  1.00232.86           O  
ANISOU 3332  O   LYS E1104    31266  27733  29478  -1189   2077   -542       O  
ATOM   3333  CB  LYS E1104      36.620   1.496 -24.678  1.00234.16           C  
ANISOU 3333  CB  LYS E1104    31465  27778  29726  -1246   2308   -644       C  
ATOM   3334  N   TYR E1105      35.055  -1.103 -23.710  1.00172.37           N  
ANISOU 3334  N   TYR E1105    23591  19973  21927  -1259   2210   -664       N  
ATOM   3335  CA  TYR E1105      33.847  -1.917 -23.645  1.00170.17           C  
ANISOU 3335  CA  TYR E1105    23326  19748  21582  -1280   2160   -661       C  
ATOM   3336  C   TYR E1105      33.464  -2.271 -22.213  1.00170.43           C  
ANISOU 3336  C   TYR E1105    23306  19772  21677  -1232   2072   -612       C  
ATOM   3337  O   TYR E1105      32.316  -2.660 -21.973  1.00169.66           O  
ANISOU 3337  O   TYR E1105    23218  19731  21512  -1240   2015   -592       O  
ATOM   3338  CB  TYR E1105      34.023  -3.193 -24.469  1.00166.77           C  
ANISOU 3338  CB  TYR E1105    22905  19281  21177  -1340   2238   -744       C  
ATOM   3339  N   LEU E1106      34.393  -2.144 -21.261  1.00170.79           N  
ANISOU 3339  N   LEU E1106    23297  19748  21847  -1181   2058   -594       N  
ATOM   3340  CA  LEU E1106      34.102  -2.433 -19.862  1.00169.30           C  
ANISOU 3340  CA  LEU E1106    23065  19547  21714  -1133   1974   -544       C  
ATOM   3341  C   LEU E1106      33.139  -1.432 -19.237  1.00165.92           C  
ANISOU 3341  C   LEU E1106    22648  19202  21190  -1098   1884   -469       C  
ATOM   3342  O   LEU E1106      32.629  -1.694 -18.144  1.00163.34           O  
ANISOU 3342  O   LEU E1106    22298  18883  20881  -1067   1813   -427       O  
ATOM   3343  CB  LEU E1106      35.398  -2.471 -19.048  1.00167.04           C  
ANISOU 3343  CB  LEU E1106    22720  19165  21581  -1086   1978   -546       C  
ATOM   3344  N   GLY E1107      32.883  -0.299 -19.895  1.00210.02           N  
ANISOU 3344  N   GLY E1107    28273  24846  26677  -1102   1888   -452       N  
ATOM   3345  CA  GLY E1107      31.958   0.676 -19.339  1.00207.45           C  
ANISOU 3345  CA  GLY E1107    27957  24599  26265  -1068   1804   -384       C  
ATOM   3346  C   GLY E1107      30.535   0.157 -19.241  1.00206.20           C  
ANISOU 3346  C   GLY E1107    27814  24513  26019  -1088   1751   -372       C  
ATOM   3347  O   GLY E1107      29.816   0.472 -18.288  1.00206.33           O  
ANISOU 3347  O   GLY E1107    27813  24570  26014  -1053   1674   -319       O  
ATOM   3348  N   SER E1108      30.109  -0.640 -20.217  1.00136.38           N  
ANISOU 3348  N   SER E1108    19002  15689  17128  -1146   1794   -423       N  
ATOM   3349  CA  SER E1108      28.744  -1.166 -20.250  1.00135.61           C  
ANISOU 3349  CA  SER E1108    18916  15661  16947  -1173   1750   -422       C  
ATOM   3350  C   SER E1108      28.452  -2.100 -19.079  1.00131.04           C  
ANISOU 3350  C   SER E1108    18295  15054  16442  -1159   1710   -406       C  
ATOM   3351  O   SER E1108      27.428  -2.787 -19.064  1.00128.18           O  
ANISOU 3351  O   SER E1108    17936  14733  16034  -1189   1687   -416       O  
ATOM   3352  CB  SER E1108      28.487  -1.904 -21.568  1.00137.30           C  
ANISOU 3352  CB  SER E1108    19171  15892  17106  -1242   1810   -489       C  
ATOM   3353  OG  SER E1108      27.365  -2.767 -21.462  1.00134.29           O  
ANISOU 3353  OG  SER E1108    18786  15552  16686  -1271   1778   -503       O  
TER    3354      SER E1108                                                      
HETATM 3355  C10 IVB A 401      15.767  18.228  -5.592  1.00106.95           C  
ANISOU 3355  C10 IVB A 401    14908  12966  12763   -296    525    334       C  
HETATM 3356  C13 IVB A 401      15.506  20.794  -7.038  1.00112.01           C  
ANISOU 3356  C13 IVB A 401    15583  13628  13346   -219    466    368       C  
HETATM 3357  C15 IVB A 401      16.144  19.397  -9.994  1.00111.49           C  
ANISOU 3357  C15 IVB A 401    15621  13537  13204   -312    537    344       C  
HETATM 3358  C17 IVB A 401      13.574  19.115  -5.244  1.00106.11           C  
ANISOU 3358  C17 IVB A 401    14743  12977  12598   -264    448    319       C  
HETATM 3359  C20 IVB A 401      15.265  21.840  -7.961  1.00113.42           C  
ANISOU 3359  C20 IVB A 401    15789  13819  13486   -191    439    384       C  
HETATM 3360  C21 IVB A 401      14.651  17.858  -3.398  1.00108.01           C  
ANISOU 3360  C21 IVB A 401    14974  13150  12915   -289    499    324       C  
HETATM 3361  C22 IVB A 401      14.863  16.440  -2.932  1.00104.06           C  
ANISOU 3361  C22 IVB A 401    14477  12626  12434   -336    535    314       C  
HETATM 3362  C24 IVB A 401      15.371  16.189  -1.502  1.00105.11           C  
ANISOU 3362  C24 IVB A 401    14604  12725  12607   -326    542    328       C  
HETATM 3363  C26 IVB A 401      15.783  23.173  -7.659  1.00115.50           C  
ANISOU 3363  C26 IVB A 401    16060  14050  13776   -139    426    412       C  
HETATM 3364  C28 IVB A 401      16.950  20.013 -12.365  1.00110.77           C  
ANISOU 3364  C28 IVB A 401    15640  13409  13039   -329    573    359       C  
HETATM 3365  C08 IVB A 401      14.876  19.482  -7.550  1.00113.51           C  
ANISOU 3365  C08 IVB A 401    15771  13852  13504   -274    480    338       C  
HETATM 3366  C09 IVB A 401      15.577  18.180  -7.211  1.00111.62           C  
ANISOU 3366  C09 IVB A 401    15535  13572  13303   -319    531    324       C  
HETATM 3367  C11 IVB A 401      14.815  19.802  -9.069  1.00112.60           C  
ANISOU 3367  C11 IVB A 401    15703  13746  13334   -280    476    340       C  
HETATM 3368  C12 IVB A 401      13.485  19.283  -6.775  1.00110.76           C  
ANISOU 3368  C12 IVB A 401    15367  13576  13141   -272    442    317       C  
HETATM 3369  C14 IVB A 401      16.858  17.893  -7.990  1.00110.90           C  
ANISOU 3369  C14 IVB A 401    15490  13414  13232   -339    580    328       C  
HETATM 3370  C16 IVB A 401      16.364  19.590  -4.982  1.00105.90           C  
ANISOU 3370  C16 IVB A 401    14771  12804  12661   -238    505    361       C  
HETATM 3371  C18 IVB A 401      16.738  18.054  -9.519  1.00112.73           C  
ANISOU 3371  C18 IVB A 401    15766  13658  13406   -356    586    323       C  
HETATM 3372  C19 IVB A 401      16.228  20.898  -5.825  1.00111.20           C  
ANISOU 3372  C19 IVB A 401    15462  13486  13304   -202    478    377       C  
HETATM 3373  C23 IVB A 401      16.306  16.011  -2.681  1.00103.30           C  
ANISOU 3373  C23 IVB A 401    14408  12449  12391   -338    567    329       C  
HETATM 3374  C25 IVB A 401      16.713  22.207  -5.563  1.00109.84           C  
ANISOU 3374  C25 IVB A 401    15293  13285  13154   -152    462    401       C  
HETATM 3375  C27 IVB A 401      16.510  23.311  -6.437  1.00112.47           C  
ANISOU 3375  C27 IVB A 401    15651  13626  13456   -123    439    417       C  
HETATM 3376  C29 IVB A 401      14.727  18.885 -12.216  1.00114.23           C  
ANISOU 3376  C29 IVB A 401    16015  13971  13418   -357    506    312       C  
HETATM 3377  C30 IVB A 401      13.507  18.194 -11.612  1.00115.12           C  
ANISOU 3377  C30 IVB A 401    16068  14146  13524   -372    474    281       C  
HETATM 3378  C31 IVB A 401      13.411  16.836 -11.677  1.00121.88           C  
ANISOU 3378  C31 IVB A 401    16916  15006  14386   -427    507    248       C  
HETATM 3379  C32 IVB A 401      12.368  15.912 -11.189  1.00123.27           C  
ANISOU 3379  C32 IVB A 401    17041  15233  14562   -458    495    212       C  
HETATM 3380  C33 IVB A 401      11.817  15.808  -9.850  1.00122.29           C  
ANISOU 3380  C33 IVB A 401    16859  15129  14476   -447    482    209       C  
HETATM 3381  C34 IVB A 401      11.720  14.911 -11.908  1.00119.45           C  
ANISOU 3381  C34 IVB A 401    16556  14785  14043   -508    499    172       C  
HETATM 3382  C35 IVB A 401      10.876  14.790  -9.834  1.00121.62           C  
ANISOU 3382  C35 IVB A 401    16742  15089  14379   -491    482    169       C  
HETATM 3383  N06 IVB A 401      14.450  17.965  -4.892  1.00107.87           N  
ANISOU 3383  N06 IVB A 401    14980  13148  12857   -302    497    316       N  
HETATM 3384  N07 IVB A 401      15.896  19.399 -11.538  1.00110.85           N  
ANISOU 3384  N07 IVB A 401    15590  13475  13052   -333    538    338       N  
HETATM 3385  O01 IVB A 401      14.536  21.252  -9.016  1.00114.28           O  
ANISOU 3385  O01 IVB A 401    15915  13971  13536   -223    431    365       O  
HETATM 3386  O02 IVB A 401      14.625  17.214  -7.644  1.00110.53           O  
ANISOU 3386  O02 IVB A 401    15386  13483  13127   -362    529    294       O  
HETATM 3387  O03 IVB A 401      15.612  24.269  -8.483  1.00114.13           O  
ANISOU 3387  O03 IVB A 401    15919  13878  13569   -107    399    434       O  
HETATM 3388  O04 IVB A 401      14.683  18.965 -13.449  1.00116.96           O  
ANISOU 3388  O04 IVB A 401    16410  14325  13706   -372    506    310       O  
HETATM 3389  O05 IVB A 401      10.818  14.243 -11.095  1.00120.59           O  
ANISOU 3389  O05 IVB A 401    16645  14968  14207   -528    491    145       O  
CONECT  562 1132                                                                
CONECT 1132  562                                                                
CONECT 2254 2733                                                                
CONECT 2733 2254                                                                
CONECT 3355 3366 3370 3383                                                      
CONECT 3356 3359 3365 3372                                                      
CONECT 3357 3367 3371 3384                                                      
CONECT 3358 3368 3383                                                           
CONECT 3359 3356 3363 3385                                                      
CONECT 3360 3361 3383                                                           
CONECT 3361 3360 3362 3373                                                      
CONECT 3362 3361 3373                                                           
CONECT 3363 3359 3375 3387                                                      
CONECT 3364 3384                                                                
CONECT 3365 3356 3366 3367 3368                                                 
CONECT 3366 3355 3365 3369 3386                                                 
CONECT 3367 3357 3365 3385                                                      
CONECT 3368 3358 3365                                                           
CONECT 3369 3366 3371                                                           
CONECT 3370 3355 3372                                                           
CONECT 3371 3357 3369                                                           
CONECT 3372 3356 3370 3374                                                      
CONECT 3373 3361 3362                                                           
CONECT 3374 3372 3375                                                           
CONECT 3375 3363 3374                                                           
CONECT 3376 3377 3384 3388                                                      
CONECT 3377 3376 3378                                                           
CONECT 3378 3377 3379                                                           
CONECT 3379 3378 3380 3381                                                      
CONECT 3380 3379 3382                                                           
CONECT 3381 3379 3389                                                           
CONECT 3382 3380 3389                                                           
CONECT 3383 3355 3358 3360                                                      
CONECT 3384 3357 3364 3376                                                      
CONECT 3385 3359 3367                                                           
CONECT 3386 3366                                                                
CONECT 3387 3363                                                                
CONECT 3388 3376                                                                
CONECT 3389 3381 3382                                                           
MASTER      425    0    1   16   11    0    0    6 3386    3   39   43          
END