HEADER    SIGNARING PROTEIN/INHIBITOR             28-APR-22   7XN9              
TITLE     CRYSTAL STRUCTURE OF SSTR2 AND L-054,522 COMPLEX                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SOMATOSTATIN RECEPTOR TYPE 2,ENDO-1,4-BETA-XYLANASE;       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: SS-2-R,SS2-R,SS2R,SRIF-1,XYLANASE,1,4-BETA-D-XYLAN          
COMPND   5 XYLANOHYDROLASE;                                                     
COMPND   6 EC: 3.2.1.8;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 OTHER_DETAILS: FUSION PROTEIN OF SSTR2 AND ENDO-1,4-BETA-XYLANASE    
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, NIALLIA CIRCULANS;                
SOURCE   3 ORGANISM_COMMON: HUMAN, BACILLUS CIRCULANS;                          
SOURCE   4 ORGANISM_TAXID: 9606, 1397;                                          
SOURCE   5 GENE: SSTR2, XLNA;                                                   
SOURCE   6 EXPRESSION_SYSTEM: INSECTA ENVIRONMENTAL SAMPLE;                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 2588572                                     
KEYWDS    G PROTEIN-COUPLED RECEPTOR, SOMATOSTATIN RECEPTOR 2, STRUCTURAL       
KEYWDS   2 PROTEIN, SIGNALING PROTEIN, SIGNARING PROTEIN-INHIBITOR COMPLEX      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.ZHAO,S.HAN,N.QIU,W.FENG,M.LU,D.YANG,M.-W.WANG,B.WU,Q.ZHAO           
REVDAT   2   17-AUG-22 7XN9    1       JRNL                                     
REVDAT   1   03-AUG-22 7XN9    0                                                
JRNL        AUTH   W.ZHAO,S.HAN,N.QIU,W.FENG,M.LU,W.ZHANG,M.WANG,Q.ZHOU,S.CHEN, 
JRNL        AUTH 2 W.XU,J.DU,X.CHU,C.YI,A.DAI,L.HU,M.Y.SHEN,Y.SUN,Q.ZHANG,Y.MA, 
JRNL        AUTH 3 W.ZHONG,D.YANG,M.W.WANG,B.WU,Q.ZHAO                          
JRNL        TITL   STRUCTURAL INSIGHTS INTO LIGAND RECOGNITION AND SELECTIVITY  
JRNL        TITL 2 OF SOMATOSTATIN RECEPTORS.                                   
JRNL        REF    CELL RES.                     V.  32   761 2022              
JRNL        REFN                   ISSN 1001-0602                               
JRNL        PMID   35739238                                                     
JRNL        DOI    10.1038/S41422-022-00679-X                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.15.2_3472                                   
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.26                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.370                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 19449                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.215                           
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.265                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 987                             
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 37.2600 -  4.9700    0.99     2772   136  0.1999 0.2343        
REMARK   3     2  4.9700 -  3.9500    1.00     2675   131  0.2078 0.2547        
REMARK   3     3  3.9500 -  3.4500    1.00     2642   139  0.2165 0.2634        
REMARK   3     4  3.4500 -  3.1300    1.00     2641   129  0.2248 0.3124        
REMARK   3     5  3.1300 -  2.9100    1.00     2608   146  0.2183 0.3119        
REMARK   3     6  2.9100 -  2.7400    0.99     2606   149  0.2353 0.3062        
REMARK   3     7  2.7400 -  2.6000    0.97     2518   157  0.2513 0.3109        
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)     : 0.351            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.225           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 64.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 64.25                          
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      :  0.013           3899                                  
REMARK   3   ANGLE     :  1.108           5330                                  
REMARK   3   CHIRALITY :  0.062            598                                  
REMARK   3   PLANARITY :  0.006            643                                  
REMARK   3   DIHEDRAL  : 15.762           1318                                  
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):  10.2653  35.3039  25.1864              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4027 T22:   0.4319                                     
REMARK   3      T33:   0.4102 T12:   0.0118                                     
REMARK   3      T13:   0.0018 T23:   0.0242                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2330 L22:   1.4107                                     
REMARK   3      L33:   0.0624 L12:   0.3143                                     
REMARK   3      L13:  -0.0315 L23:   0.5017                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0690 S12:  -0.0301 S13:   0.0214                       
REMARK   3      S21:  -0.2686 S22:   0.0074 S23:   0.1077                       
REMARK   3      S31:  -0.0539 S32:  -0.0279 S33:   0.0633                       
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 7XN9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-MAY-22.                  
REMARK 100 THE DEPOSITION ID IS D_1300029146.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 80                                 
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19455                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.260                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.9100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
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: 4N6H                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.77                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100-400 MM LITHIUM NITRATE, 6-10%        
REMARK 280  PEG2000, 100 MM L-054,522, AND 0.1 M HEPES, PH 7.0, LIPIDIC         
REMARK 280  CUBIC PHASE, TEMPERATURE 293K                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       85.24950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       85.24950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       37.26000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       48.97850            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       37.26000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       48.97850            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       85.24950            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       37.26000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       48.97850            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       85.24950            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       37.26000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       48.97850            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -24                                                      
REMARK 465     LYS A   -23                                                      
REMARK 465     THR A   -22                                                      
REMARK 465     ILE A   -21                                                      
REMARK 465     ILE A   -20                                                      
REMARK 465     ALA A   -19                                                      
REMARK 465     LEU A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     TYR A   -16                                                      
REMARK 465     ILE A   -15                                                      
REMARK 465     PHE A   -14                                                      
REMARK 465     CYS A   -13                                                      
REMARK 465     LEU A   -12                                                      
REMARK 465     VAL A   -11                                                      
REMARK 465     PHE A   -10                                                      
REMARK 465     ALA A    -9                                                      
REMARK 465     ASP A    -8                                                      
REMARK 465     TYR A    -7                                                      
REMARK 465     LYS A    -6                                                      
REMARK 465     ASP A    -5                                                      
REMARK 465     ASP A    -4                                                      
REMARK 465     ASP A    -3                                                      
REMARK 465     ASP A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     PRO A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     MET A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     ASP A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     PRO A     7                                                      
REMARK 465     LEU A     8                                                      
REMARK 465     ASN A     9                                                      
REMARK 465     GLY A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     HIS A    12                                                      
REMARK 465     THR A    13                                                      
REMARK 465     TRP A    14                                                      
REMARK 465     LEU A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     ILE A    17                                                      
REMARK 465     PRO A    18                                                      
REMARK 465     PHE A    19                                                      
REMARK 465     ASP A    20                                                      
REMARK 465     LEU A    21                                                      
REMARK 465     ASN A    22                                                      
REMARK 465     GLY A    23                                                      
REMARK 465     SER A    24                                                      
REMARK 465     VAL A    25                                                      
REMARK 465     VAL A    26                                                      
REMARK 465     SER A    27                                                      
REMARK 465     THR A    28                                                      
REMARK 465     ASN A    29                                                      
REMARK 465     THR A    30                                                      
REMARK 465     SER A    31                                                      
REMARK 465     ASN A    32                                                      
REMARK 465     GLN A    33                                                      
REMARK 465     THR A    34                                                      
REMARK 465     GLU A    35                                                      
REMARK 465     PRO A    36                                                      
REMARK 465     GLY A  1160                                                      
REMARK 465     VAL A   332                                                      
REMARK 465     SER A   333                                                      
REMARK 465     GLY A   334                                                      
REMARK 465     THR A   335                                                      
REMARK 465     ASP A   336                                                      
REMARK 465     ASP A   337                                                      
REMARK 465     GLY A   338                                                      
REMARK 465     GLU A   339                                                      
REMARK 465     ARG A   340                                                      
REMARK 465     SER A   341                                                      
REMARK 465     ASP A   342                                                      
REMARK 465     SER A   343                                                      
REMARK 465     LYS A   344                                                      
REMARK 465     GLN A   345                                                      
REMARK 465     ASP A   346                                                      
REMARK 465     LYS A   347                                                      
REMARK 465     SER A   348                                                      
REMARK 465     ARG A   349                                                      
REMARK 465     LEU A   350                                                      
REMARK 465     ASN A   351                                                      
REMARK 465     GLU A   352                                                      
REMARK 465     THR A   353                                                      
REMARK 465     THR A   354                                                      
REMARK 465     GLU A   355                                                      
REMARK 465     THR A   356                                                      
REMARK 465     GLN A   357                                                      
REMARK 465     ARG A   358                                                      
REMARK 465     THR A   359                                                      
REMARK 465     GLU A   360                                                      
REMARK 465     PHE A   361                                                      
REMARK 465     LEU A   362                                                      
REMARK 465     GLU A   363                                                      
REMARK 465     VAL A   364                                                      
REMARK 465     LEU A   365                                                      
REMARK 465     PHE A   366                                                      
REMARK 465     GLN A   367                                                      
REMARK 465     GLY A   368                                                      
REMARK 465     PRO A   369                                                      
REMARK 465     HIS A   370                                                      
REMARK 465     HIS A   371                                                      
REMARK 465     HIS A   372                                                      
REMARK 465     HIS A   373                                                      
REMARK 465     HIS A   374                                                      
REMARK 465     HIS A   375                                                      
REMARK 465     HIS A   376                                                      
REMARK 465     HIS A   377                                                      
REMARK 465     HIS A   378                                                      
REMARK 465     HIS A   379                                                      
REMARK 465     GLU A   380                                                      
REMARK 465     PRO A   381                                                      
REMARK 465     GLU A   382                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  73    CG   CD   CE   NZ                                   
REMARK 470     GLU A 200    CG   CD   OE1  OE2                                  
REMARK 470     ARG A1111    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR A1112    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A1153    CG   CD   CE   NZ                                   
REMARK 470     ASN A1158    CG   OD1  ND2                                       
REMARK 470     MET A 282    CG   SD   CE                                        
REMARK 470     LYS A 331    CG   CD   CE   NZ                                   
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    SER A 150       34.82    -94.88                                   
REMARK 500    PHE A 217      -57.82   -150.44                                   
REMARK 500    SER A1116     -164.05   -127.80                                   
REMARK 500    VAL A 330     -161.28   -116.55                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  7XN9 A    2   239  UNP    P30874   SSR2_HUMAN       2    239             
DBREF  7XN9 A 1000  1184  UNP    P09850   XYNA_NIACI      29    213             
DBREF  7XN9 A  243   359  UNP    P30874   SSR2_HUMAN     243    359             
SEQADV 7XN9 MET A  -24  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 LYS A  -23  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 THR A  -22  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 ILE A  -21  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 ILE A  -20  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 ALA A  -19  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 LEU A  -18  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 SER A  -17  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 TYR A  -16  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 ILE A  -15  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 PHE A  -14  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 CYS A  -13  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 LEU A  -12  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 VAL A  -11  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 PHE A  -10  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 ALA A   -9  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 ASP A   -8  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 TYR A   -7  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 LYS A   -6  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 ASP A   -5  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 ASP A   -4  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 ASP A   -3  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 ASP A   -2  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 GLY A   -1  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 ALA A    0  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 PRO A    1  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 GLU A  106  UNP  P30874    VAL   106 CONFLICT                       
SEQADV 7XN9 PHE A 1010  UNP  P09850    ASP    39 CONFLICT                       
SEQADV 7XN9 ASP A 1121  UNP  P09850    ARG   150 CONFLICT                       
SEQADV 7XN9 ASP A  316  UNP  P30874    SER   316 CONFLICT                       
SEQADV 7XN9 GLU A  360  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 PHE A  361  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 LEU A  362  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 GLU A  363  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 VAL A  364  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 LEU A  365  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 PHE A  366  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 GLN A  367  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 GLY A  368  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 PRO A  369  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 HIS A  370  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 HIS A  371  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 HIS A  372  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 HIS A  373  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 HIS A  374  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 HIS A  375  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 HIS A  376  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 HIS A  377  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 HIS A  378  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 HIS A  379  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 GLU A  380  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 PRO A  381  UNP  P30874              EXPRESSION TAG                 
SEQADV 7XN9 GLU A  382  UNP  P30874              EXPRESSION TAG                 
SEQRES   1 A  589  MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU          
SEQRES   2 A  589  VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO          
SEQRES   3 A  589  ASP MET ALA ASP GLU PRO LEU ASN GLY SER HIS THR TRP          
SEQRES   4 A  589  LEU SER ILE PRO PHE ASP LEU ASN GLY SER VAL VAL SER          
SEQRES   5 A  589  THR ASN THR SER ASN GLN THR GLU PRO TYR TYR ASP LEU          
SEQRES   6 A  589  THR SER ASN ALA VAL LEU THR PHE ILE TYR PHE VAL VAL          
SEQRES   7 A  589  CYS ILE ILE GLY LEU CYS GLY ASN THR LEU VAL ILE TYR          
SEQRES   8 A  589  VAL ILE LEU ARG TYR ALA LYS MET LYS THR ILE THR ASN          
SEQRES   9 A  589  ILE TYR ILE LEU ASN LEU ALA ILE ALA ASP GLU LEU PHE          
SEQRES  10 A  589  MET LEU GLY LEU PRO PHE LEU ALA MET GLN VAL ALA LEU          
SEQRES  11 A  589  GLU HIS TRP PRO PHE GLY LYS ALA ILE CYS ARG VAL VAL          
SEQRES  12 A  589  MET THR VAL ASP GLY ILE ASN GLN PHE THR SER ILE PHE          
SEQRES  13 A  589  CYS LEU THR VAL MET SER ILE ASP ARG TYR LEU ALA VAL          
SEQRES  14 A  589  VAL HIS PRO ILE LYS SER ALA LYS TRP ARG ARG PRO ARG          
SEQRES  15 A  589  THR ALA LYS MET ILE THR MET ALA VAL TRP GLY VAL SER          
SEQRES  16 A  589  LEU LEU VAL ILE LEU PRO ILE MET ILE TYR ALA GLY LEU          
SEQRES  17 A  589  ARG SER ASN GLN TRP GLY ARG SER SER CYS THR ILE ASN          
SEQRES  18 A  589  TRP PRO GLY GLU SER GLY ALA TRP TYR THR GLY PHE ILE          
SEQRES  19 A  589  ILE TYR THR PHE ILE LEU GLY PHE LEU VAL PRO LEU THR          
SEQRES  20 A  589  ILE ILE CYS LEU CYS TYR LEU PHE ILE ILE ILE LYS VAL          
SEQRES  21 A  589  LYS SER SER GLY ALA SER THR ASP TYR TRP GLN ASN TRP          
SEQRES  22 A  589  THR PHE GLY GLY GLY ILE VAL ASN ALA VAL ASN GLY SER          
SEQRES  23 A  589  GLY GLY ASN TYR SER VAL ASN TRP SER ASN THR GLY ASN          
SEQRES  24 A  589  PHE VAL VAL GLY LYS GLY TRP THR THR GLY SER PRO PHE          
SEQRES  25 A  589  ARG THR ILE ASN TYR ASN ALA GLY VAL TRP ALA PRO ASN          
SEQRES  26 A  589  GLY ASN GLY TYR LEU THR LEU TYR GLY TRP THR ARG SER          
SEQRES  27 A  589  PRO LEU ILE GLU TYR TYR VAL VAL ASP SER TRP GLY THR          
SEQRES  28 A  589  TYR ARG PRO THR GLY THR TYR LYS GLY THR VAL LYS SER          
SEQRES  29 A  589  ASP GLY GLY THR TYR ASP ILE TYR THR THR THR ARG TYR          
SEQRES  30 A  589  ASN ALA PRO SER ILE ASP GLY ASP ASP THR THR PHE THR          
SEQRES  31 A  589  GLN TYR TRP SER VAL ARG GLN SER LYS ARG PRO THR GLY          
SEQRES  32 A  589  SER ASN ALA THR ILE THR PHE THR ASN HIS VAL ASN ALA          
SEQRES  33 A  589  TRP LYS SER HIS GLY MET ASN LEU GLY SER ASN TRP ALA          
SEQRES  34 A  589  TYR GLN VAL MET ALA THR GLU GLY TYR GLN SER SER GLY          
SEQRES  35 A  589  SER SER ASN VAL THR VAL TRP GLY SER SER LYS ARG LYS          
SEQRES  36 A  589  LYS SER GLU LYS LYS VAL THR ARG MET VAL SER ILE VAL          
SEQRES  37 A  589  VAL ALA VAL PHE ILE PHE CYS TRP LEU PRO PHE TYR ILE          
SEQRES  38 A  589  PHE ASN VAL SER SER VAL SER MET ALA ILE SER PRO THR          
SEQRES  39 A  589  PRO ALA LEU LYS GLY MET PHE ASP PHE VAL VAL VAL LEU          
SEQRES  40 A  589  THR TYR ALA ASN SER CYS ALA ASN PRO ILE LEU TYR ALA          
SEQRES  41 A  589  PHE LEU ASP ASP ASN PHE LYS LYS SER PHE GLN ASN VAL          
SEQRES  42 A  589  LEU CYS LEU VAL LYS VAL SER GLY THR ASP ASP GLY GLU          
SEQRES  43 A  589  ARG SER ASP SER LYS GLN ASP LYS SER ARG LEU ASN GLU          
SEQRES  44 A  589  THR THR GLU THR GLN ARG THR GLU PHE LEU GLU VAL LEU          
SEQRES  45 A  589  PHE GLN GLY PRO HIS HIS HIS HIS HIS HIS HIS HIS HIS          
SEQRES  46 A  589  HIS GLU PRO GLU                                              
HET    EPE  A1201      15                                                       
HET    GI9  A1202      94                                                       
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID              
HETNAM     GI9 TERT-BUTYL (2S)-6-AZANYL-2-[[(2R,3S)-3-(1H-INDOL-3-YL)-          
HETNAM   2 GI9  2-[[4-(2-OXIDANYLIDENE-3H-BENZIMIDAZOL-1-YL)PIPERIDIN-          
HETNAM   3 GI9  1-YL]CARBONYLAMINO]BUTANOYL]AMINO]HEXANOATE                     
HETSYN     EPE HEPES                                                            
HETSYN     GI9 L-054,52                                                         
FORMUL   2  EPE    C8 H18 N2 O4 S                                               
FORMUL   3  GI9    C35 H47 N7 O5                                                
HELIX    1 AA1 ASP A   39  TYR A   71  1                                  33    
HELIX    2 AA2 ALA A   72  LYS A   75  5                                   4    
HELIX    3 AA3 THR A   76  GLU A  106  1                                  31    
HELIX    4 AA4 PHE A  110  HIS A  146  1                                  37    
HELIX    5 AA5 ILE A  148  LYS A  152  5                                   5    
HELIX    6 AA6 ARG A  155  ILE A  174  1                                  20    
HELIX    7 AA7 ILE A  174  TYR A  180  1                                   7    
HELIX    8 AA8 TRP A  197  GLU A  200  5                                   4    
HELIX    9 AA9 SER A  201  PHE A  217  1                                  17    
HELIX   10 AB1 PHE A  217  SER A  238  1                                  22    
HELIX   11 AB2 PHE A 1145  HIS A 1155  1                                  11    
HELIX   12 AB3 LYS A  248  SER A  281  1                                  34    
HELIX   13 AB4 THR A  287  ASP A  316  1                                  30    
HELIX   14 AB5 ASP A  316  CYS A  328  1                                  13    
SHEET    1 AA1 2 ALA A 181  SER A 185  0                                        
SHEET    2 AA1 2 SER A 191  ILE A 195 -1  O  SER A 192   N  ARG A 184           
SHEET    1 AA2 8 TYR A1004  THR A1009  0                                        
SHEET    2 AA2 8 PHE A1035  TRP A1041 -1  O  GLY A1038   N  GLN A1006           
SHEET    3 AA2 8 ASN A1162  GLY A1172 -1  O  THR A1170   N  VAL A1037           
SHEET    4 AA2 8 GLY A1063  ARG A1072 -1  N  TYR A1068   O  VAL A1167           
SHEET    5 AA2 8 ILE A1076  TRP A1084 -1  O  TYR A1078   N  GLY A1069           
SHEET    6 AA2 8 THR A1122  ARG A1131  1  O  SER A1129   N  VAL A1081           
SHEET    7 AA2 8 GLY A1102  ALA A1114 -1  N  ASP A1105   O  VAL A1130           
SHEET    8 AA2 8 GLY A1095  SER A1099 -1  N  VAL A1097   O  TYR A1104           
SHEET    1 AA3 5 ILE A1014  VAL A1018  0                                        
SHEET    2 AA3 5 ASN A1024  SER A1030 -1  O  ASN A1028   N  ASN A1016           
SHEET    3 AA3 5 SER A1176  TRP A1184 -1  O  GLY A1177   N  TRP A1029           
SHEET    4 AA3 5 THR A1049  ASN A1060 -1  N  ASN A1060   O  SER A1176           
SHEET    5 AA3 5 ALA A1141  THR A1144 -1  O  ILE A1143   N  ILE A1050           
SSBOND   1 CYS A  115    CYS A  193                          1555   1555  2.05  
CISPEP   1 SER A 1073    PRO A 1074          0        -2.03                     
CRYST1   74.520   97.957  170.499  90.00  90.00  90.00 C 2 2 21      8          
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      0.013419  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010209  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005865        0.00000                         
ATOM      1  N   TYR A  37      28.278  32.299  67.179  1.00 88.08           N  
ANISOU    1  N   TYR A  37    12838  10883   9747    -16  -1733    594       N  
ATOM      2  CA  TYR A  37      27.336  33.369  66.865  1.00 96.18           C  
ANISOU    2  CA  TYR A  37    13784  12005  10754    -58  -1539    553       C  
ATOM      3  C   TYR A  37      27.900  34.370  65.838  1.00 99.15           C  
ANISOU    3  C   TYR A  37    13920  12448  11306     10  -1512    501       C  
ATOM      4  O   TYR A  37      27.231  35.342  65.465  1.00 97.11           O  
ANISOU    4  O   TYR A  37    13573  12269  11056    -13  -1364    464       O  
ATOM      5  CB  TYR A  37      26.909  34.099  68.144  1.00 93.27           C  
ANISOU    5  CB  TYR A  37    13588  11631  10221   -137  -1519    544       C  
ATOM      6  CG  TYR A  37      28.012  34.850  68.863  1.00102.40           C  
ANISOU    6  CG  TYR A  37    14768  12754  11387   -107  -1681    524       C  
ATOM      7  CD1 TYR A  37      29.164  34.201  69.296  1.00105.19           C  
ANISOU    7  CD1 TYR A  37    15187  13014  11766    -57  -1902    550       C  
ATOM      8  CD2 TYR A  37      27.888  36.206  69.135  1.00107.81           C  
ANISOU    8  CD2 TYR A  37    15409  13495  12059   -130  -1616    476       C  
ATOM      9  CE1 TYR A  37      30.165  34.886  69.964  1.00105.07           C  
ANISOU    9  CE1 TYR A  37    15192  12963  11767    -28  -2058    526       C  
ATOM     10  CE2 TYR A  37      28.884  36.900  69.806  1.00108.94           C  
ANISOU   10  CE2 TYR A  37    15574  13607  12211   -103  -1763    454       C  
ATOM     11  CZ  TYR A  37      30.017  36.236  70.218  1.00105.70           C  
ANISOU   11  CZ  TYR A  37    15229  13104  11830    -52  -1985    479       C  
ATOM     12  OH  TYR A  37      31.006  36.926  70.883  1.00108.12           O  
ANISOU   12  OH  TYR A  37    15552  13375  12153    -24  -2138    452       O  
ATOM     13  N   TYR A  38      29.124  34.118  65.376  1.00 88.97           N  
ANISOU   13  N   TYR A  38    12526  11119  10159     92  -1652    494       N  
ATOM     14  CA  TYR A  38      29.703  34.888  64.283  1.00 82.01           C  
ANISOU   14  CA  TYR A  38    11417  10288   9454    156  -1620    444       C  
ATOM     15  C   TYR A  38      30.743  34.025  63.588  1.00 83.05           C  
ANISOU   15  C   TYR A  38    11453  10364   9740    231  -1737    448       C  
ATOM     16  O   TYR A  38      31.620  33.464  64.249  1.00 91.06           O  
ANISOU   16  O   TYR A  38    12546  11290  10762    258  -1918    463       O  
ATOM     17  CB  TYR A  38      30.342  36.196  64.773  1.00 88.81           C  
ANISOU   17  CB  TYR A  38    12242  11164  10336    169  -1671    397       C  
ATOM     18  CG  TYR A  38      31.263  36.819  63.739  1.00 98.47           C  
ANISOU   18  CG  TYR A  38    13246  12410  11756    245  -1681    345       C  
ATOM     19  CD1 TYR A  38      30.748  37.418  62.588  1.00 98.49           C  
ANISOU   19  CD1 TYR A  38    13092  12494  11834    250  -1517    316       C  
ATOM     20  CD2 TYR A  38      32.652  36.782  63.892  1.00100.89           C  
ANISOU   20  CD2 TYR A  38    13505  12648  12180    309  -1857    320       C  
ATOM     21  CE1 TYR A  38      31.593  37.978  61.622  1.00 97.32           C  
ANISOU   21  CE1 TYR A  38    12758  12361  11860    313  -1516    267       C  
ATOM     22  CE2 TYR A  38      33.503  37.340  62.933  1.00 94.69           C  
ANISOU   22  CE2 TYR A  38    12519  11876  11582    373  -1852    265       C  
ATOM     23  CZ  TYR A  38      32.968  37.937  61.803  1.00 94.94           C  
ANISOU   23  CZ  TYR A  38    12410  11990  11673    372  -1677    239       C  
ATOM     24  OH  TYR A  38      33.806  38.485  60.852  1.00 96.34           O  
ANISOU   24  OH  TYR A  38    12404  12174  12027    428  -1664    183       O  
ATOM     25  N   ASP A  39      30.655  33.940  62.262  1.00 80.21           N  
ANISOU   25  N   ASP A  39    10924  10047   9504    264  -1637    430       N  
ATOM     26  CA  ASP A  39      31.519  33.103  61.427  1.00 81.87           C  
ANISOU   26  CA  ASP A  39    11026  10208   9871    327  -1712    427       C  
ATOM     27  C   ASP A  39      32.364  34.032  60.554  1.00 79.19           C  
ANISOU   27  C   ASP A  39    10489   9895   9705    382  -1697    361       C  
ATOM     28  O   ASP A  39      31.917  34.475  59.494  1.00 84.32           O  
ANISOU   28  O   ASP A  39    11016  10612  10408    382  -1550    339       O  
ATOM     29  CB  ASP A  39      30.659  32.125  60.586  1.00 92.76           C  
ANISOU   29  CB  ASP A  39    12391  11612  11243    310  -1596    460       C  
ATOM     30  CG  ASP A  39      31.480  31.048  59.880  1.00 98.76           C  
ANISOU   30  CG  ASP A  39    13072  12308  12144    364  -1679    465       C  
ATOM     31  OD1 ASP A  39      32.729  31.054  59.983  1.00 97.18           O  
ANISOU   31  OD1 ASP A  39    12816  12044  12064    418  -1823    437       O  
ATOM     32  OD2 ASP A  39      30.856  30.188  59.212  1.00 99.20           O  
ANISOU   32  OD2 ASP A  39    13118  12378  12198    352  -1596    492       O  
ATOM     33  N   LEU A  40      33.587  34.325  61.006  1.00 76.43           N  
ANISOU   33  N   LEU A  40    10112   9484   9442    428  -1851    329       N  
ATOM     34  CA  LEU A  40      34.454  35.256  60.287  1.00 79.22           C  
ANISOU   34  CA  LEU A  40    10286   9853   9962    477  -1839    259       C  
ATOM     35  C   LEU A  40      34.728  34.790  58.861  1.00 83.62           C  
ANISOU   35  C   LEU A  40    10686  10412  10676    512  -1766    237       C  
ATOM     36  O   LEU A  40      34.803  35.608  57.938  1.00 86.65           O  
ANISOU   36  O   LEU A  40    10932  10845  11147    524  -1655    191       O  
ATOM     37  CB  LEU A  40      35.763  35.433  61.052  1.00 77.70           C  
ANISOU   37  CB  LEU A  40    10096   9576   9849    522  -2036    226       C  
ATOM     38  CG  LEU A  40      36.702  36.524  60.552  1.00 79.21           C  
ANISOU   38  CG  LEU A  40    10119   9776  10203    568  -2033    146       C  
ATOM     39  CD1 LEU A  40      37.302  37.229  61.738  1.00 74.91           C  
ANISOU   39  CD1 LEU A  40     9642   9196   9624    575  -2171    124       C  
ATOM     40  CD2 LEU A  40      37.792  35.940  59.678  1.00 79.29           C  
ANISOU   40  CD2 LEU A  40     9983   9716  10428    629  -2090    103       C  
ATOM     41  N   THR A  41      34.884  33.479  58.664  1.00 76.35           N  
ANISOU   41  N   THR A  41     9789   9431   9788    525  -1825    269       N  
ATOM     42  CA  THR A  41      35.129  32.945  57.326  1.00 84.12           C  
ANISOU   42  CA  THR A  41    10634  10412  10917    552  -1754    248       C  
ATOM     43  C   THR A  41      33.906  33.121  56.428  1.00 88.88           C  
ANISOU   43  C   THR A  41    11211  11108  11452    512  -1554    266       C  
ATOM     44  O   THR A  41      34.018  33.621  55.300  1.00 83.08           O  
ANISOU   44  O   THR A  41    10340  10408  10816    526  -1447    225       O  
ATOM     45  CB  THR A  41      35.517  31.465  57.413  1.00 80.03           C  
ANISOU   45  CB  THR A  41    10158   9807  10442    571  -1867    282       C  
ATOM     46  OG1 THR A  41      34.380  30.700  57.845  1.00 88.15           O  
ANISOU   46  OG1 THR A  41    11337  10858  11300    522  -1829    354       O  
ATOM     47  CG2 THR A  41      36.655  31.269  58.404  1.00 79.07           C  
ANISOU   47  CG2 THR A  41    10081   9585  10379    610  -2085    268       C  
ATOM     48  N   SER A  42      32.730  32.685  56.904  1.00 88.58           N  
ANISOU   48  N   SER A  42    11305  11103  11247    462  -1504    324       N  
ATOM     49  CA  SER A  42      31.492  32.889  56.158  1.00 82.79           C  
ANISOU   49  CA  SER A  42    10553  10454  10449    423  -1324    338       C  
ATOM     50  C   SER A  42      31.227  34.367  55.919  1.00 79.23           C  
ANISOU   50  C   SER A  42    10034  10075   9994    413  -1226    297       C  
ATOM     51  O   SER A  42      30.550  34.734  54.952  1.00 90.27           O  
ANISOU   51  O   SER A  42    11361  11534  11403    400  -1087    287       O  
ATOM     52  CB  SER A  42      30.317  32.256  56.903  1.00 86.56           C  
ANISOU   52  CB  SER A  42    11192  10945  10753    367  -1294    397       C  
ATOM     53  OG  SER A  42      29.119  32.983  56.691  1.00 89.54           O  
ANISOU   53  OG  SER A  42    11571  11405  11044    322  -1142    396       O  
ATOM     54  N   ASN A  43      31.746  35.228  56.787  1.00 72.81           N  
ANISOU   54  N   ASN A  43     9246   9254   9166    419  -1301    273       N  
ATOM     55  CA  ASN A  43      31.642  36.656  56.542  1.00 76.12           C  
ANISOU   55  CA  ASN A  43     9589   9735   9600    415  -1217    230       C  
ATOM     56  C   ASN A  43      32.606  37.089  55.446  1.00 73.40           C  
ANISOU   56  C   ASN A  43     9078   9379   9432    464  -1198    173       C  
ATOM     57  O   ASN A  43      32.254  37.915  54.593  1.00 74.81           O  
ANISOU   57  O   ASN A  43     9171   9613   9638    458  -1074    146       O  
ATOM     58  CB  ASN A  43      31.923  37.412  57.833  1.00 86.17           C  
ANISOU   58  CB  ASN A  43    10942  10998  10801    405  -1303    220       C  
ATOM     59  CG  ASN A  43      31.031  38.605  58.007  1.00 82.58           C  
ANISOU   59  CG  ASN A  43    10496  10623  10260    363  -1186    208       C  
ATOM     60  OD1 ASN A  43      29.848  38.465  58.297  1.00 78.07           O  
ANISOU   60  OD1 ASN A  43    10012  10089   9564    310  -1104    241       O  
ATOM     61  ND2 ASN A  43      31.593  39.798  57.830  1.00 84.80           N  
ANISOU   61  ND2 ASN A  43    10680  10925  10615    386  -1174    156       N  
ATOM     62  N   ALA A  44      33.824  36.537  55.455  1.00 68.43           N  
ANISOU   62  N   ALA A  44     8405   8670   8926    510  -1321    150       N  
ATOM     63  CA  ALA A  44      34.851  36.957  54.509  1.00 65.87           C  
ANISOU   63  CA  ALA A  44     7926   8321   8782    552  -1305     84       C  
ATOM     64  C   ALA A  44      34.512  36.523  53.092  1.00 58.76           C  
ANISOU   64  C   ALA A  44     6945   7439   7940    548  -1178     82       C  
ATOM     65  O   ALA A  44      34.733  37.276  52.131  1.00 53.35           O  
ANISOU   65  O   ALA A  44     6154   6778   7339    555  -1081     36       O  
ATOM     66  CB  ALA A  44      36.204  36.388  54.925  1.00 73.49           C  
ANISOU   66  CB  ALA A  44     8863   9184   9876    600  -1472     54       C  
ATOM     67  N   VAL A  45      33.984  35.308  52.940  1.00 56.71           N  
ANISOU   67  N   VAL A  45     6742   7167   7636    534  -1177    132       N  
ATOM     68  CA  VAL A  45      33.636  34.835  51.607  1.00 57.42           C  
ANISOU   68  CA  VAL A  45     6766   7274   7777    527  -1061    132       C  
ATOM     69  C   VAL A  45      32.515  35.687  51.020  1.00 61.51           C  
ANISOU   69  C   VAL A  45     7280   7882   8211    492   -909    139       C  
ATOM     70  O   VAL A  45      32.498  35.953  49.808  1.00 60.84           O  
ANISOU   70  O   VAL A  45     7111   7815   8193    492   -806    112       O  
ATOM     71  CB  VAL A  45      33.284  33.332  51.651  1.00 61.15           C  
ANISOU   71  CB  VAL A  45     7305   7714   8216    519  -1097    185       C  
ATOM     72  CG1 VAL A  45      32.167  33.064  52.647  1.00 66.85           C  
ANISOU   72  CG1 VAL A  45     8173   8470   8755    480  -1106    249       C  
ATOM     73  CG2 VAL A  45      32.894  32.822  50.279  1.00 57.53           C  
ANISOU   73  CG2 VAL A  45     6783   7274   7804    509   -978    185       C  
ATOM     74  N   LEU A  46      31.589  36.157  51.867  1.00 63.90           N  
ANISOU   74  N   LEU A  46     7674   8236   8370    460   -895    171       N  
ATOM     75  CA  LEU A  46      30.515  37.026  51.395  1.00 56.03           C  
ANISOU   75  CA  LEU A  46     6669   7317   7304    428   -763    172       C  
ATOM     76  C   LEU A  46      31.033  38.413  51.051  1.00 52.30           C  
ANISOU   76  C   LEU A  46     6108   6866   6899    443   -725    117       C  
ATOM     77  O   LEU A  46      30.559  39.033  50.097  1.00 50.46           O  
ANISOU   77  O   LEU A  46     5821   6673   6677    433   -614    102       O  
ATOM     78  CB  LEU A  46      29.402  37.118  52.433  1.00 67.08           C  
ANISOU   78  CB  LEU A  46     8186   8755   8546    385   -754    212       C  
ATOM     79  CG  LEU A  46      28.208  36.243  52.031  1.00 82.38           C  
ANISOU   79  CG  LEU A  46    10173  10717  10412    352   -677    255       C  
ATOM     80  CD1 LEU A  46      28.653  34.772  51.919  1.00 81.58           C  
ANISOU   80  CD1 LEU A  46    10094  10556  10348    369   -746    283       C  
ATOM     81  CD2 LEU A  46      27.021  36.392  52.984  1.00 83.56           C  
ANISOU   81  CD2 LEU A  46    10431  10901  10415    302   -643    284       C  
ATOM     82  N   THR A  47      32.000  38.925  51.805  1.00 56.07           N  
ANISOU   82  N   THR A  47     6572   7311   7421    468   -817     84       N  
ATOM     83  CA  THR A  47      32.611  40.190  51.408  1.00 58.81           C  
ANISOU   83  CA  THR A  47     6826   7670   7851    486   -779     26       C  
ATOM     84  C   THR A  47      33.312  40.040  50.063  1.00 62.96           C  
ANISOU   84  C   THR A  47     7242   8162   8516    508   -724    -15       C  
ATOM     85  O   THR A  47      33.265  40.948  49.223  1.00 57.71           O  
ANISOU   85  O   THR A  47     6514   7525   7888    504   -625    -48       O  
ATOM     86  CB  THR A  47      33.575  40.671  52.496  1.00 58.43           C  
ANISOU   86  CB  THR A  47     6781   7585   7834    510   -899     -5       C  
ATOM     87  OG1 THR A  47      32.929  40.551  53.768  1.00 67.86           O  
ANISOU   87  OG1 THR A  47     8100   8797   8886    482   -957     39       O  
ATOM     88  CG2 THR A  47      33.970  42.139  52.280  1.00 54.40           C  
ANISOU   88  CG2 THR A  47     6191   7102   7378    520   -848    -62       C  
ATOM     89  N   PHE A  48      33.917  38.874  49.824  1.00 59.08           N  
ANISOU   89  N   PHE A  48     6738   7608   8103    526   -781    -13       N  
ATOM     90  CA  PHE A  48      34.568  38.606  48.547  1.00 55.62           C  
ANISOU   90  CA  PHE A  48     6204   7130   7800    540   -721    -55       C  
ATOM     91  C   PHE A  48      33.557  38.582  47.402  1.00 54.08           C  
ANISOU   91  C   PHE A  48     6012   6985   7551    508   -583    -31       C  
ATOM     92  O   PHE A  48      33.809  39.133  46.322  1.00 48.19           O  
ANISOU   92  O   PHE A  48     5200   6238   6874    505   -490    -72       O  
ATOM     93  CB  PHE A  48      35.322  37.272  48.636  1.00 66.56           C  
ANISOU   93  CB  PHE A  48     7580   8436   9274    562   -816    -54       C  
ATOM     94  CG  PHE A  48      36.007  36.871  47.360  1.00 70.34           C  
ANISOU   94  CG  PHE A  48     7963   8865   9898    570   -752   -101       C  
ATOM     95  CD1 PHE A  48      37.038  37.640  46.837  1.00 64.82           C  
ANISOU   95  CD1 PHE A  48     7162   8127   9339    587   -719   -181       C  
ATOM     96  CD2 PHE A  48      35.595  35.738  46.660  1.00 74.00           C  
ANISOU   96  CD2 PHE A  48     8442   9319  10357    555   -712    -69       C  
ATOM     97  CE1 PHE A  48      37.657  37.277  45.650  1.00 67.14           C  
ANISOU   97  CE1 PHE A  48     7376   8369   9765    584   -645   -230       C  
ATOM     98  CE2 PHE A  48      36.219  35.359  45.468  1.00 64.56           C  
ANISOU   98  CE2 PHE A  48     7164   8074   9293    555   -644   -116       C  
ATOM     99  CZ  PHE A  48      37.246  36.132  44.959  1.00 61.92           C  
ANISOU   99  CZ  PHE A  48     6734   7698   9096    567   -607   -197       C  
ATOM    100  N   ILE A  49      32.408  37.944  47.621  1.00 49.57           N  
ANISOU  100  N   ILE A  49     5524   6452   6858    482   -570     32       N  
ATOM    101  CA  ILE A  49      31.388  37.853  46.582  1.00 48.34           C  
ANISOU  101  CA  ILE A  49     5376   6340   6652    454   -454     55       C  
ATOM    102  C   ILE A  49      30.843  39.235  46.219  1.00 51.82           C  
ANISOU  102  C   ILE A  49     5799   6836   7053    439   -367     38       C  
ATOM    103  O   ILE A  49      30.639  39.541  45.037  1.00 55.84           O  
ANISOU  103  O   ILE A  49     6274   7354   7589    428   -274     22       O  
ATOM    104  CB  ILE A  49      30.267  36.904  47.031  1.00 49.07           C  
ANISOU  104  CB  ILE A  49     5559   6458   6628    430   -465    120       C  
ATOM    105  CG1 ILE A  49      30.704  35.437  46.847  1.00 47.96           C  
ANISOU  105  CG1 ILE A  49     5422   6261   6541    442   -515    136       C  
ATOM    106  CG2 ILE A  49      28.959  37.249  46.316  1.00 43.12           C  
ANISOU  106  CG2 ILE A  49     4823   5765   5796    399   -355    140       C  
ATOM    107  CD1 ILE A  49      30.016  34.452  47.818  1.00 43.27           C  
ANISOU  107  CD1 ILE A  49     4930   5669   5844    428   -576    195       C  
ATOM    108  N   TYR A  50      30.597  40.088  47.220  1.00 50.68           N  
ANISOU  108  N   TYR A  50     5685   6727   6846    435   -397     39       N  
ATOM    109  CA  TYR A  50      30.237  41.476  46.937  1.00 55.41           C  
ANISOU  109  CA  TYR A  50     6257   7371   7426    425   -323     16       C  
ATOM    110  C   TYR A  50      31.219  42.111  45.959  1.00 51.41           C  
ANISOU  110  C   TYR A  50     5664   6832   7038    442   -277    -42       C  
ATOM    111  O   TYR A  50      30.814  42.731  44.965  1.00 49.35           O  
ANISOU  111  O   TYR A  50     5383   6591   6776    428   -183    -52       O  
ATOM    112  CB  TYR A  50      30.166  42.294  48.236  1.00 54.72           C  
ANISOU  112  CB  TYR A  50     6200   7310   7280    423   -374     13       C  
ATOM    113  CG  TYR A  50      28.815  42.194  48.895  1.00 52.92           C  
ANISOU  113  CG  TYR A  50     6055   7132   6921    387   -357     59       C  
ATOM    114  CD1 TYR A  50      28.417  41.009  49.500  1.00 54.92           C  
ANISOU  114  CD1 TYR A  50     6385   7372   7111    375   -406    103       C  
ATOM    115  CD2 TYR A  50      27.919  43.253  48.874  1.00 53.63           C  
ANISOU  115  CD2 TYR A  50     6146   7276   6956    364   -286     55       C  
ATOM    116  CE1 TYR A  50      27.180  40.879  50.087  1.00 55.68           C  
ANISOU  116  CE1 TYR A  50     6557   7505   7093    337   -378    137       C  
ATOM    117  CE2 TYR A  50      26.661  43.132  49.452  1.00 53.55           C  
ANISOU  117  CE2 TYR A  50     6203   7302   6840    327   -261     88       C  
ATOM    118  CZ  TYR A  50      26.297  41.934  50.055  1.00 56.88           C  
ANISOU  118  CZ  TYR A  50     6702   7708   7201    312   -303    127       C  
ATOM    119  OH  TYR A  50      25.062  41.771  50.637  1.00 54.77           O  
ANISOU  119  OH  TYR A  50     6505   7470   6836    271   -268    152       O  
ATOM    120  N   PHE A  51      32.518  41.914  46.185  1.00 54.19           N  
ANISOU  120  N   PHE A  51     5966   7125   7498    472   -341    -83       N  
ATOM    121  CA  PHE A  51      33.491  42.602  45.341  1.00 61.52           C  
ANISOU  121  CA  PHE A  51     6812   8016   8547    484   -287   -150       C  
ATOM    122  C   PHE A  51      33.526  42.004  43.937  1.00 57.20           C  
ANISOU  122  C   PHE A  51     6244   7439   8051    470   -203   -157       C  
ATOM    123  O   PHE A  51      33.599  42.743  42.947  1.00 53.66           O  
ANISOU  123  O   PHE A  51     5768   6989   7632    457   -107   -189       O  
ATOM    124  CB  PHE A  51      34.869  42.606  46.017  1.00 48.80           C  
ANISOU  124  CB  PHE A  51     5145   6344   7052    519   -380   -202       C  
ATOM    125  CG  PHE A  51      35.039  43.729  47.018  1.00 49.74           C  
ANISOU  125  CG  PHE A  51     5262   6490   7147    530   -424   -221       C  
ATOM    126  CD1 PHE A  51      34.780  45.040  46.654  1.00 51.51           C  
ANISOU  126  CD1 PHE A  51     5464   6755   7354    519   -338   -244       C  
ATOM    127  CD2 PHE A  51      35.415  43.470  48.328  1.00 59.49           C  
ANISOU  127  CD2 PHE A  51     6526   7708   8369    549   -554   -213       C  
ATOM    128  CE1 PHE A  51      34.914  46.079  47.566  1.00 56.86           C  
ANISOU  128  CE1 PHE A  51     6136   7458   8009    527   -374   -263       C  
ATOM    129  CE2 PHE A  51      35.553  44.514  49.255  1.00 62.85           C  
ANISOU  129  CE2 PHE A  51     6955   8159   8767    556   -593   -232       C  
ATOM    130  CZ  PHE A  51      35.299  45.818  48.869  1.00 49.72           C  
ANISOU  130  CZ  PHE A  51     5259   6540   7092    545   -499   -258       C  
ATOM    131  N   VAL A  52      33.404  40.684  43.819  1.00 45.07           N  
ANISOU  131  N   VAL A  52     4731   5880   6515    468   -233   -126       N  
ATOM    132  CA  VAL A  52      33.341  40.095  42.487  1.00 48.83           C  
ANISOU  132  CA  VAL A  52     5195   6330   7027    450   -149   -131       C  
ATOM    133  C   VAL A  52      32.166  40.662  41.706  1.00 60.47           C  
ANISOU  133  C   VAL A  52     6713   7861   8403    419    -54   -102       C  
ATOM    134  O   VAL A  52      32.288  41.012  40.525  1.00 76.21           O  
ANISOU  134  O   VAL A  52     8692   9836  10430    402     36   -130       O  
ATOM    135  CB  VAL A  52      33.254  38.569  42.568  1.00 47.17           C  
ANISOU  135  CB  VAL A  52     5008   6092   6821    451   -199    -96       C  
ATOM    136  CG1 VAL A  52      32.989  38.017  41.175  1.00 44.54           C  
ANISOU  136  CG1 VAL A  52     4675   5744   6504    425   -103    -96       C  
ATOM    137  CG2 VAL A  52      34.541  38.009  43.176  1.00 48.98           C  
ANISOU  137  CG2 VAL A  52     5187   6250   7175    483   -296   -134       C  
ATOM    138  N   VAL A  53      31.002  40.741  42.341  1.00 50.11           N  
ANISOU  138  N   VAL A  53     5459   6610   6970    410    -75    -49       N  
ATOM    139  CA  VAL A  53      29.821  41.211  41.630  1.00 43.98           C  
ANISOU  139  CA  VAL A  53     4720   5880   6110    384      0    -23       C  
ATOM    140  C   VAL A  53      30.053  42.626  41.119  1.00 49.33           C  
ANISOU  140  C   VAL A  53     5369   6563   6811    380     62    -63       C  
ATOM    141  O   VAL A  53      29.826  42.929  39.943  1.00 52.85           O  
ANISOU  141  O   VAL A  53     5823   7000   7258    362    140    -71       O  
ATOM    142  CB  VAL A  53      28.595  41.120  42.549  1.00 41.79           C  
ANISOU  142  CB  VAL A  53     4500   5660   5719    373    -33     29       C  
ATOM    143  CG1 VAL A  53      27.394  41.884  41.946  1.00 41.55           C  
ANISOU  143  CG1 VAL A  53     4493   5674   5619    350     35     44       C  
ATOM    144  CG2 VAL A  53      28.292  39.680  42.825  1.00 38.46           C  
ANISOU  144  CG2 VAL A  53     4115   5227   5271    371    -75     68       C  
ATOM    145  N   CYS A  54      30.559  43.499  41.990  1.00 55.64           N  
ANISOU  145  N   CYS A  54     6140   7371   7629    397     26    -89       N  
ATOM    146  CA  CYS A  54      30.848  44.878  41.611  1.00 54.90           C  
ANISOU  146  CA  CYS A  54     6017   7282   7563    396     81   -130       C  
ATOM    147  C   CYS A  54      31.716  44.953  40.351  1.00 54.65           C  
ANISOU  147  C   CYS A  54     5953   7190   7623    389    156   -178       C  
ATOM    148  O   CYS A  54      31.457  45.767  39.449  1.00 44.87           O  
ANISOU  148  O   CYS A  54     4728   5953   6370    371    235   -191       O  
ATOM    149  CB  CYS A  54      31.530  45.579  42.786  1.00 59.23           C  
ANISOU  149  CB  CYS A  54     6529   7835   8141    419     21   -159       C  
ATOM    150  SG  CYS A  54      31.985  47.302  42.462  1.00 64.44           S  
ANISOU  150  SG  CYS A  54     7145   8498   8842    421     86   -215       S  
ATOM    151  N   ILE A  55      32.726  44.081  40.259  1.00 56.34           N  
ANISOU  151  N   ILE A  55     6129   7344   7932    400    135   -208       N  
ATOM    152  CA  ILE A  55      33.656  44.123  39.137  1.00 59.75           C  
ANISOU  152  CA  ILE A  55     6526   7709   8467    388    214   -267       C  
ATOM    153  C   ILE A  55      32.979  43.637  37.867  1.00 55.56           C  
ANISOU  153  C   ILE A  55     6050   7173   7889    354    291   -241       C  
ATOM    154  O   ILE A  55      33.032  44.296  36.822  1.00 61.73           O  
ANISOU  154  O   ILE A  55     6849   7932   8673    329    382   -266       O  
ATOM    155  CB  ILE A  55      34.914  43.287  39.440  1.00 67.20           C  
ANISOU  155  CB  ILE A  55     7406   8584   9543    409    166   -312       C  
ATOM    156  CG1 ILE A  55      35.588  43.756  40.736  1.00 69.09           C  
ANISOU  156  CG1 ILE A  55     7597   8823   9829    445     73   -338       C  
ATOM    157  CG2 ILE A  55      35.863  43.301  38.227  1.00 61.34           C  
ANISOU  157  CG2 ILE A  55     6626   7763   8917    388    266   -383       C  
ATOM    158  CD1 ILE A  55      35.925  45.246  40.784  1.00 61.53           C  
ANISOU  158  CD1 ILE A  55     6611   7876   8892    448    116   -384       C  
ATOM    159  N   ILE A  56      32.345  42.471  37.935  1.00 50.25           N  
ANISOU  159  N   ILE A  56     5410   6515   7169    351    254   -191       N  
ATOM    160  CA  ILE A  56      31.712  41.909  36.750  1.00 47.67           C  
ANISOU  160  CA  ILE A  56     5134   6179   6799    320    319   -167       C  
ATOM    161  C   ILE A  56      30.651  42.855  36.224  1.00 42.14           C  
ANISOU  161  C   ILE A  56     4490   5522   6001    300    363   -140       C  
ATOM    162  O   ILE A  56      30.512  43.053  35.011  1.00 45.99           O  
ANISOU  162  O   ILE A  56     5017   5982   6475    271    439   -150       O  
ATOM    163  CB  ILE A  56      31.136  40.521  37.073  1.00 50.12           C  
ANISOU  163  CB  ILE A  56     5466   6504   7072    323    264   -116       C  
ATOM    164  CG1 ILE A  56      32.282  39.529  37.291  1.00 45.02           C  
ANISOU  164  CG1 ILE A  56     4766   5797   6542    337    229   -149       C  
ATOM    165  CG2 ILE A  56      30.223  40.063  35.959  1.00 57.86           C  
ANISOU  165  CG2 ILE A  56     6506   7491   7988    292    320    -84       C  
ATOM    166  CD1 ILE A  56      31.826  38.180  37.706  1.00 54.47           C  
ANISOU  166  CD1 ILE A  56     5983   7003   7709    344    169   -100       C  
ATOM    167  N   GLY A  57      29.916  43.494  37.132  1.00 50.31           N  
ANISOU  167  N   GLY A  57     5532   6616   6968    315    315   -111       N  
ATOM    168  CA  GLY A  57      28.862  44.394  36.708  1.00 49.86           C  
ANISOU  168  CA  GLY A  57     5520   6596   6828    299    345    -87       C  
ATOM    169  C   GLY A  57      29.360  45.699  36.134  1.00 54.35           C  
ANISOU  169  C   GLY A  57     6083   7142   7425    291    407   -130       C  
ATOM    170  O   GLY A  57      28.749  46.232  35.199  1.00 55.39           O  
ANISOU  170  O   GLY A  57     6267   7270   7510    269    454   -120       O  
ATOM    171  N   LEU A  58      30.454  46.244  36.685  1.00 46.55           N  
ANISOU  171  N   LEU A  58     5038   6136   6516    309    403   -179       N  
ATOM    172  CA  LEU A  58      31.006  47.468  36.107  1.00 49.79           C  
ANISOU  172  CA  LEU A  58     5441   6516   6959    299    472   -226       C  
ATOM    173  C   LEU A  58      31.689  47.221  34.758  1.00 52.35           C  
ANISOU  173  C   LEU A  58     5790   6767   7335    268    563   -265       C  
ATOM    174  O   LEU A  58      31.655  48.104  33.898  1.00 49.85           O  
ANISOU  174  O   LEU A  58     5515   6427   7000    245    633   -282       O  
ATOM    175  CB  LEU A  58      31.973  48.135  37.079  1.00 44.43           C  
ANISOU  175  CB  LEU A  58     4690   5836   6355    326    445   -273       C  
ATOM    176  CG  LEU A  58      31.286  48.954  38.167  1.00 53.21           C  
ANISOU  176  CG  LEU A  58     5794   7016   7406    344    390   -247       C  
ATOM    177  CD1 LEU A  58      32.253  49.264  39.268  1.00 56.01           C  
ANISOU  177  CD1 LEU A  58     6080   7368   7832    373    341   -288       C  
ATOM    178  CD2 LEU A  58      30.678  50.236  37.620  1.00 51.66           C  
ANISOU  178  CD2 LEU A  58     5630   6837   7161    329    443   -245       C  
ATOM    179  N   CYS A  59      32.298  46.046  34.540  1.00 49.48           N  
ANISOU  179  N   CYS A  59     5406   6360   7033    264    566   -280       N  
ATOM    180  CA  CYS A  59      32.842  45.739  33.213  1.00 54.55           C  
ANISOU  180  CA  CYS A  59     6081   6930   7717    226    662   -317       C  
ATOM    181  C   CYS A  59      31.743  45.688  32.165  1.00 60.21           C  
ANISOU  181  C   CYS A  59     6897   7655   8326    193    696   -270       C  
ATOM    182  O   CYS A  59      31.784  46.406  31.153  1.00 64.99           O  
ANISOU  182  O   CYS A  59     7562   8222   8908    160    775   -290       O  
ATOM    183  CB  CYS A  59      33.602  44.401  33.212  1.00 58.06           C  
ANISOU  183  CB  CYS A  59     6480   7327   8251    227    653   -341       C  
ATOM    184  SG  CYS A  59      35.216  44.390  34.011  1.00 61.62           S  
ANISOU  184  SG  CYS A  59     6816   7725   8873    256    632   -423       S  
ATOM    185  N   GLY A  60      30.772  44.801  32.370  1.00 43.47           N  
ANISOU  185  N   GLY A  60     4800   5578   6139    199    637   -210       N  
ATOM    186  CA  GLY A  60      29.776  44.566  31.347  1.00 44.21           C  
ANISOU  186  CA  GLY A  60     4983   5670   6143    169    660   -170       C  
ATOM    187  C   GLY A  60      28.927  45.783  31.079  1.00 49.29           C  
ANISOU  187  C   GLY A  60     5681   6340   6708    164    661   -149       C  
ATOM    188  O   GLY A  60      28.630  46.102  29.924  1.00 55.13           O  
ANISOU  188  O   GLY A  60     6504   7042   7401    130    712   -147       O  
ATOM    189  N   ASN A  61      28.532  46.492  32.134  1.00 40.22           N  
ANISOU  189  N   ASN A  61     4492   5248   5543    195    604   -134       N  
ATOM    190  CA  ASN A  61      27.722  47.676  31.913  1.00 42.51           C  
ANISOU  190  CA  ASN A  61     4824   5558   5770    191    601   -117       C  
ATOM    191  C   ASN A  61      28.542  48.791  31.276  1.00 51.71           C  
ANISOU  191  C   ASN A  61     6009   6673   6965    173    677   -165       C  
ATOM    192  O   ASN A  61      28.008  49.563  30.472  1.00 53.94           O  
ANISOU  192  O   ASN A  61     6366   6937   7193    152    700   -154       O  
ATOM    193  CB  ASN A  61      27.075  48.144  33.220  1.00 48.74           C  
ANISOU  193  CB  ASN A  61     5562   6418   6538    223    529    -94       C  
ATOM    194  CG  ASN A  61      25.940  47.227  33.677  1.00 49.63           C  
ANISOU  194  CG  ASN A  61     5681   6577   6599    231    465    -42       C  
ATOM    195  OD1 ASN A  61      24.912  47.096  33.018  1.00 62.78           O  
ANISOU  195  OD1 ASN A  61     7401   8243   8208    217    456    -11       O  
ATOM    196  ND2 ASN A  61      26.137  46.584  34.797  1.00 51.28           N  
ANISOU  196  ND2 ASN A  61     5836   6817   6829    252    420    -37       N  
ATOM    197  N   THR A  62      29.840  48.888  31.586  1.00 48.33           N  
ANISOU  197  N   THR A  62     5520   6214   6629    179    716   -222       N  
ATOM    198  CA  THR A  62      30.640  49.899  30.898  1.00 50.84           C  
ANISOU  198  CA  THR A  62     5862   6475   6981    156    803   -274       C  
ATOM    199  C   THR A  62      30.748  49.558  29.425  1.00 49.73           C  
ANISOU  199  C   THR A  62     5818   6262   6816    106    884   -284       C  
ATOM    200  O   THR A  62      30.654  50.441  28.557  1.00 48.15           O  
ANISOU  200  O   THR A  62     5698   6022   6574     76    940   -293       O  
ATOM    201  CB  THR A  62      32.031  50.019  31.528  1.00 43.62           C  
ANISOU  201  CB  THR A  62     4854   5534   6186    172    829   -342       C  
ATOM    202  OG1 THR A  62      31.894  50.454  32.885  1.00 46.51           O  
ANISOU  202  OG1 THR A  62     5145   5965   6561    215    751   -332       O  
ATOM    203  CG2 THR A  62      32.895  51.022  30.778  1.00 39.55           C  
ANISOU  203  CG2 THR A  62     4361   4951   5714    144    934   -406       C  
ATOM    204  N   LEU A  63      30.898  48.265  29.143  1.00 46.42           N  
ANISOU  204  N   LEU A  63     5398   5823   6417     94    888   -281       N  
ATOM    205  CA  LEU A  63      30.930  47.764  27.778  1.00 42.56           C  
ANISOU  205  CA  LEU A  63     5005   5268   5898     42    961   -287       C  
ATOM    206  C   LEU A  63      29.633  48.067  27.036  1.00 42.43           C  
ANISOU  206  C   LEU A  63     5100   5263   5757     25    932   -229       C  
ATOM    207  O   LEU A  63      29.661  48.431  25.856  1.00 46.42           O  
ANISOU  207  O   LEU A  63     5714   5706   6218    -21    999   -240       O  
ATOM    208  CB  LEU A  63      31.203  46.259  27.815  1.00 43.26           C  
ANISOU  208  CB  LEU A  63     5057   5347   6033     41    953   -288       C  
ATOM    209  CG  LEU A  63      31.258  45.603  26.450  1.00 49.03           C  
ANISOU  209  CG  LEU A  63     5881   6010   6738    -16   1031   -297       C  
ATOM    210  CD1 LEU A  63      32.313  46.303  25.646  1.00 44.63           C  
ANISOU  210  CD1 LEU A  63     5361   5366   6229    -61   1154   -369       C  
ATOM    211  CD2 LEU A  63      31.566  44.130  26.590  1.00 50.37           C  
ANISOU  211  CD2 LEU A  63     5999   6172   6966    -14   1020   -300       C  
ATOM    212  N   VAL A  64      28.489  47.946  27.720  1.00 42.34           N  
ANISOU  212  N   VAL A  64     5069   5326   5693     60    832   -170       N  
ATOM    213  CA  VAL A  64      27.192  48.172  27.083  1.00 48.57           C  
ANISOU  213  CA  VAL A  64     5950   6124   6381     49    788   -118       C  
ATOM    214  C   VAL A  64      26.966  49.662  26.801  1.00 51.10           C  
ANISOU  214  C   VAL A  64     6322   6430   6665     43    797   -122       C  
ATOM    215  O   VAL A  64      26.416  50.036  25.758  1.00 48.87           O  
ANISOU  215  O   VAL A  64     6152   6104   6310     13    803   -104       O  
ATOM    216  CB  VAL A  64      26.063  47.577  27.949  1.00 46.20           C  
ANISOU  216  CB  VAL A  64     5600   5899   6052     85    687    -66       C  
ATOM    217  CG1 VAL A  64      24.716  48.170  27.546  1.00 49.16           C  
ANISOU  217  CG1 VAL A  64     6044   6287   6348     85    630    -24       C  
ATOM    218  CG2 VAL A  64      26.035  46.054  27.836  1.00 39.11           C  
ANISOU  218  CG2 VAL A  64     4694   5001   5164     80    680    -52       C  
ATOM    219  N   ILE A  65      27.393  50.535  27.717  1.00 53.21           N  
ANISOU  219  N   ILE A  65     6511   6728   6979     72    793   -145       N  
ATOM    220  CA  ILE A  65      27.280  51.975  27.495  1.00 53.21           C  
ANISOU  220  CA  ILE A  65     6550   6712   6954     67    808   -153       C  
ATOM    221  C   ILE A  65      28.184  52.428  26.347  1.00 54.10           C  
ANISOU  221  C   ILE A  65     6753   6734   7069     19    917   -198       C  
ATOM    222  O   ILE A  65      27.784  53.247  25.505  1.00 53.39           O  
ANISOU  222  O   ILE A  65     6770   6602   6914     -7    930   -186       O  
ATOM    223  CB  ILE A  65      27.606  52.725  28.799  1.00 52.91           C  
ANISOU  223  CB  ILE A  65     6400   6729   6973    108    784   -173       C  
ATOM    224  CG1 ILE A  65      26.637  52.307  29.933  1.00 39.12           C  
ANISOU  224  CG1 ILE A  65     4582   5067   5214    147    684   -130       C  
ATOM    225  CG2 ILE A  65      27.686  54.244  28.545  1.00 41.22           C  
ANISOU  225  CG2 ILE A  65     4955   5226   5481    101    815   -190       C  
ATOM    226  CD1 ILE A  65      27.215  52.514  31.355  1.00 38.74           C  
ANISOU  226  CD1 ILE A  65     4418   5070   5230    182    663   -154       C  
ATOM    227  N   TYR A  66      29.417  51.911  26.299  1.00 50.97           N  
ANISOU  227  N   TYR A  66     6316   6299   6750      3    997   -253       N  
ATOM    228  CA  TYR A  66      30.353  52.293  25.247  1.00 45.30           C  
ANISOU  228  CA  TYR A  66     5678   5486   6046    -50   1119   -307       C  
ATOM    229  C   TYR A  66      29.828  51.935  23.852  1.00 47.83           C  
ANISOU  229  C   TYR A  66     6156   5746   6272   -104   1146   -281       C  
ATOM    230  O   TYR A  66      29.881  52.760  22.925  1.00 45.41           O  
ANISOU  230  O   TYR A  66     5969   5374   5911   -146   1203   -292       O  
ATOM    231  CB  TYR A  66      31.718  51.633  25.487  1.00 46.09           C  
ANISOU  231  CB  TYR A  66     5693   5553   6266    -58   1196   -377       C  
ATOM    232  CG  TYR A  66      32.679  51.879  24.336  1.00 44.25           C  
ANISOU  232  CG  TYR A  66     5545   5212   6054   -122   1338   -442       C  
ATOM    233  CD1 TYR A  66      33.255  53.148  24.147  1.00 44.78           C  
ANISOU  233  CD1 TYR A  66     5638   5237   6139   -139   1412   -488       C  
ATOM    234  CD2 TYR A  66      32.985  50.869  23.416  1.00 40.17           C  
ANISOU  234  CD2 TYR A  66     5091   4633   5539   -173   1406   -460       C  
ATOM    235  CE1 TYR A  66      34.136  53.399  23.096  1.00 44.30           C  
ANISOU  235  CE1 TYR A  66     5664   5070   6098   -205   1556   -553       C  
ATOM    236  CE2 TYR A  66      33.842  51.113  22.345  1.00 42.97           C  
ANISOU  236  CE2 TYR A  66     5534   4882   5910   -241   1548   -525       C  
ATOM    237  CZ  TYR A  66      34.417  52.392  22.191  1.00 44.50           C  
ANISOU  237  CZ  TYR A  66     5756   5032   6122   -259   1626   -573       C  
ATOM    238  OH  TYR A  66      35.281  52.671  21.150  1.00 50.59           O  
ANISOU  238  OH  TYR A  66     6620   5691   6910   -332   1779   -643       O  
ATOM    239  N   VAL A  67      29.361  50.698  23.665  1.00 40.81           N  
ANISOU  239  N   VAL A  67     5275   4871   5361   -107   1109   -250       N  
ATOM    240  CA  VAL A  67      28.999  50.284  22.305  1.00 46.64           C  
ANISOU  240  CA  VAL A  67     6164   5543   6015   -163   1142   -234       C  
ATOM    241  C   VAL A  67      27.727  51.005  21.850  1.00 49.01           C  
ANISOU  241  C   VAL A  67     6569   5848   6203   -161   1059   -174       C  
ATOM    242  O   VAL A  67      27.595  51.376  20.672  1.00 49.55           O  
ANISOU  242  O   VAL A  67     6793   5841   6194   -212   1097   -171       O  
ATOM    243  CB  VAL A  67      28.871  48.732  22.176  1.00 49.56           C  
ANISOU  243  CB  VAL A  67     6513   5923   6396   -170   1129   -220       C  
ATOM    244  CG1 VAL A  67      30.172  48.006  22.588  1.00 42.18           C  
ANISOU  244  CG1 VAL A  67     5472   4970   5584   -172   1206   -283       C  
ATOM    245  CG2 VAL A  67      27.666  48.159  22.991  1.00 42.10           C  
ANISOU  245  CG2 VAL A  67     5502   5069   5424   -115    995   -154       C  
ATOM    246  N   ILE A  68      26.784  51.242  22.763  1.00 44.44           N  
ANISOU  246  N   ILE A  68     5915   5350   5619   -105    946   -130       N  
ATOM    247  CA  ILE A  68      25.609  52.003  22.374  1.00 46.86           C  
ANISOU  247  CA  ILE A  68     6308   5655   5843   -100    863    -83       C  
ATOM    248  C   ILE A  68      25.996  53.441  22.017  1.00 46.21           C  
ANISOU  248  C   ILE A  68     6293   5523   5743   -118    910   -106       C  
ATOM    249  O   ILE A  68      25.570  53.973  20.989  1.00 43.09           O  
ANISOU  249  O   ILE A  68     6045   5062   5265   -153    903    -87       O  
ATOM    250  CB  ILE A  68      24.543  51.940  23.482  1.00 47.48           C  
ANISOU  250  CB  ILE A  68     6279   5825   5935    -40    744    -42       C  
ATOM    251  CG1 ILE A  68      24.074  50.501  23.653  1.00 42.33           C  
ANISOU  251  CG1 ILE A  68     5589   5209   5286    -31    702    -17       C  
ATOM    252  CG2 ILE A  68      23.373  52.875  23.159  1.00 48.04           C  
ANISOU  252  CG2 ILE A  68     6420   5888   5945    -32    656     -4       C  
ATOM    253  CD1 ILE A  68      23.122  50.285  24.792  1.00 41.34           C  
ANISOU  253  CD1 ILE A  68     5356   5169   5181     21    604     14       C  
ATOM    254  N   LEU A  69      26.843  54.074  22.830  1.00 48.81           N  
ANISOU  254  N   LEU A  69     6521   5875   6148    -98    958   -147       N  
ATOM    255  CA  LEU A  69      27.183  55.471  22.597  1.00 42.72           C  
ANISOU  255  CA  LEU A  69     5801   5064   5369   -111   1002   -170       C  
ATOM    256  C   LEU A  69      28.138  55.660  21.422  1.00 43.85           C  
ANISOU  256  C   LEU A  69     6072   5099   5489   -179   1133   -215       C  
ATOM    257  O   LEU A  69      28.012  56.650  20.693  1.00 50.42           O  
ANISOU  257  O   LEU A  69     7029   5870   6259   -209   1153   -212       O  
ATOM    258  CB  LEU A  69      27.769  56.078  23.864  1.00 40.91           C  
ANISOU  258  CB  LEU A  69     5419   4893   5230    -67   1011   -203       C  
ATOM    259  CG  LEU A  69      26.857  56.489  25.020  1.00 43.62           C  
ANISOU  259  CG  LEU A  69     5658   5328   5587     -8    899   -167       C  
ATOM    260  CD1 LEU A  69      27.708  57.085  26.098  1.00 38.84           C  
ANISOU  260  CD1 LEU A  69     4927   4762   5069     22    934   -212       C  
ATOM    261  CD2 LEU A  69      25.745  57.492  24.614  1.00 41.76           C  
ANISOU  261  CD2 LEU A  69     5506   5080   5282     -5    826   -125       C  
ATOM    262  N   ARG A  70      29.130  54.810  21.284  1.00 44.82           N  
ANISOU  262  N   ARG A  70     6166   5195   5670   -206   1227   -264       N  
ATOM    263  CA  ARG A  70      30.047  54.891  20.161  1.00 46.31           C  
ANISOU  263  CA  ARG A  70     6476   5274   5845   -280   1367   -316       C  
ATOM    264  C   ARG A  70      29.611  54.502  18.753  1.00 52.25           C  
ANISOU  264  C   ARG A  70     7423   5946   6484   -345   1386   -291       C  
ATOM    265  O   ARG A  70      29.907  55.191  17.815  1.00 58.41           O  
ANISOU  265  O   ARG A  70     8351   6636   7206   -402   1464   -311       O  
ATOM    266  CB  ARG A  70      31.329  54.158  20.486  1.00 49.79           C  
ANISOU  266  CB  ARG A  70     6812   5702   6406   -290   1470   -389       C  
ATOM    267  CG  ARG A  70      32.399  54.330  19.441  1.00 44.95           C  
ANISOU  267  CG  ARG A  70     6304   4971   5804   -370   1635   -461       C  
ATOM    268  CD  ARG A  70      33.152  55.618  19.639  1.00 44.91           C  
ANISOU  268  CD  ARG A  70     6283   4933   5846   -373   1712   -515       C  
ATOM    269  NE  ARG A  70      34.369  55.678  18.859  1.00 44.58           N  
ANISOU  269  NE  ARG A  70     6303   4782   5855   -446   1888   -603       N  
ATOM    270  CZ  ARG A  70      34.582  56.563  17.912  1.00 54.86           C  
ANISOU  270  CZ  ARG A  70     7764   5991   7088   -509   1983   -626       C  
ATOM    271  NH1 ARG A  70      33.670  57.452  17.652  1.00 48.65           N  
ANISOU  271  NH1 ARG A  70     7087   5212   6188   -501   1907   -562       N  
ATOM    272  NH2 ARG A  70      35.700  56.566  17.241  1.00 50.75           N  
ANISOU  272  NH2 ARG A  70     7295   5367   6621   -580   2154   -714       N  
ATOM    273  N   TYR A  71      28.881  53.411  18.619  1.00 53.35           N  
ANISOU  273  N   TYR A  71     7568   6115   6588   -337   1313   -248       N  
ATOM    274  CA  TYR A  71      28.501  52.895  17.311  1.00 50.96           C  
ANISOU  274  CA  TYR A  71     7444   5737   6182   -399   1329   -227       C  
ATOM    275  C   TYR A  71      27.144  53.275  16.796  1.00 48.06           C  
ANISOU  275  C   TYR A  71     7199   5366   5697   -392   1201   -155       C  
ATOM    276  O   TYR A  71      26.187  53.223  17.500  1.00 51.14           O  
ANISOU  276  O   TYR A  71     7505   5834   6093   -332   1073   -107       O  
ATOM    277  CB  TYR A  71      28.588  51.376  17.285  1.00 49.94           C  
ANISOU  277  CB  TYR A  71     7264   5626   6084   -406   1338   -230       C  
ATOM    278  CG  TYR A  71      29.861  50.768  17.774  1.00 46.19           C  
ANISOU  278  CG  TYR A  71     6661   5151   5738   -411   1446   -300       C  
ATOM    279  CD1 TYR A  71      31.028  51.458  17.760  1.00 53.66           C  
ANISOU  279  CD1 TYR A  71     7594   6043   6751   -438   1569   -373       C  
ATOM    280  CD2 TYR A  71      29.889  49.483  18.215  1.00 48.37           C  
ANISOU  280  CD2 TYR A  71     6833   5472   6072   -390   1422   -297       C  
ATOM    281  CE1 TYR A  71      32.191  50.889  18.198  1.00 45.22           C  
ANISOU  281  CE1 TYR A  71     6401   4966   5816   -441   1659   -444       C  
ATOM    282  CE2 TYR A  71      31.047  48.908  18.649  1.00 54.46           C  
ANISOU  282  CE2 TYR A  71     7487   6235   6970   -392   1508   -363       C  
ATOM    283  CZ  TYR A  71      32.193  49.619  18.632  1.00 54.15           C  
ANISOU  283  CZ  TYR A  71     7430   6140   7004   -417   1624   -438       C  
ATOM    284  OH  TYR A  71      33.343  49.048  19.065  1.00 56.10           O  
ANISOU  284  OH  TYR A  71     7553   6370   7392   -418   1701   -509       O  
ATOM    285  N   ALA A  72      27.091  53.632  15.529  1.00 50.83           N  
ANISOU  285  N   ALA A  72     7755   5615   5944   -459   1240   -152       N  
ATOM    286  CA  ALA A  72      25.881  54.050  14.841  1.00 49.42           C  
ANISOU  286  CA  ALA A  72     7725   5406   5648   -462   1118    -88       C  
ATOM    287  C   ALA A  72      24.831  52.986  14.748  1.00 57.74           C  
ANISOU  287  C   ALA A  72     8772   6498   6670   -440   1002    -38       C  
ATOM    288  O   ALA A  72      23.664  53.253  14.804  1.00 56.78           O  
ANISOU  288  O   ALA A  72     8667   6398   6508   -403    860     14       O  
ATOM    289  CB  ALA A  72      26.214  54.569  13.473  1.00 52.04           C  
ANISOU  289  CB  ALA A  72     8294   5607   5872   -548   1199   -102       C  
ATOM    290  N   LYS A  73      25.269  51.753  14.615  1.00 58.49           N  
ANISOU  290  N   LYS A  73     8835   6598   6792   -464   1066    -60       N  
ATOM    291  CA  LYS A  73      24.411  50.592  14.507  1.00 55.58           C  
ANISOU  291  CA  LYS A  73     8454   6263   6401   -448    978    -20       C  
ATOM    292  C   LYS A  73      23.527  50.394  15.725  1.00 59.30           C  
ANISOU  292  C   LYS A  73     8747   6848   6936   -361    849     16       C  
ATOM    293  O   LYS A  73      22.417  49.949  15.616  1.00 57.05           O  
ANISOU  293  O   LYS A  73     8476   6585   6615   -338    733     61       O  
ATOM    294  CB  LYS A  73      25.250  49.343  14.245  1.00 59.59           C  
ANISOU  294  CB  LYS A  73     8939   6755   6947   -491   1093    -61       C  
ATOM    295  N   MET A  74      24.038  50.719  16.890  1.00 49.65           N  
ANISOU  295  N   MET A  74     7360   5694   5811   -316    873     -7       N  
ATOM    296  CA  MET A  74      23.333  50.574  18.128  1.00 47.75           C  
ANISOU  296  CA  MET A  74     6954   5558   5633   -241    771     19       C  
ATOM    297  C   MET A  74      22.328  51.661  18.445  1.00 49.81           C  
ANISOU  297  C   MET A  74     7213   5838   5872   -200    656     54       C  
ATOM    298  O   MET A  74      21.644  51.582  19.423  1.00 57.29           O  
ANISOU  298  O   MET A  74     8035   6865   6868   -145    573     73       O  
ATOM    299  CB  MET A  74      24.334  50.435  19.247  1.00 52.56           C  
ANISOU  299  CB  MET A  74     7396   6224   6350   -213    842    -22       C  
ATOM    300  CG  MET A  74      25.369  49.377  18.979  1.00 50.61           C  
ANISOU  300  CG  MET A  74     7135   5951   6145   -250    952    -63       C  
ATOM    301  SD  MET A  74      24.690  47.773  18.608  1.00 49.51           S  
ANISOU  301  SD  MET A  74     7008   5826   5978   -257    906    -31       S  
ATOM    302  CE  MET A  74      24.487  47.096  20.217  1.00 44.69           C  
ANISOU  302  CE  MET A  74     6187   5331   5463   -182    840    -19       C  
ATOM    303  N   LYS A  75      22.192  52.666  17.611  1.00 56.79           N  
ANISOU  303  N   LYS A  75     8243   6647   6686   -230    647     61       N  
ATOM    304  CA  LYS A  75      21.247  53.714  17.898  1.00 51.84           C  
ANISOU  304  CA  LYS A  75     7612   6033   6052   -192    534     91       C  
ATOM    305  C   LYS A  75      19.850  53.319  17.516  1.00 60.41           C  
ANISOU  305  C   LYS A  75     8745   7113   7095   -175    392    137       C  
ATOM    306  O   LYS A  75      19.346  53.738  16.513  1.00 81.01           O  
ANISOU  306  O   LYS A  75    11513   9643   9624   -202    335    159       O  
ATOM    307  CB  LYS A  75      21.600  54.969  17.123  1.00 49.49           C  
ANISOU  307  CB  LYS A  75     7462   5648   5695   -229    569     83       C  
ATOM    308  CG  LYS A  75      23.025  55.432  17.310  1.00 64.74           C  
ANISOU  308  CG  LYS A  75     9369   7564   7665   -256    721     29       C  
ATOM    309  CD  LYS A  75      23.180  56.324  18.519  1.00 77.01           C  
ANISOU  309  CD  LYS A  75    10769   9188   9303   -202    713     14       C  
ATOM    310  CE  LYS A  75      24.532  56.148  19.179  1.00 75.90           C  
ANISOU  310  CE  LYS A  75    10514   9076   9247   -205    844    -43       C  
ATOM    311  NZ  LYS A  75      25.662  56.412  18.267  1.00 72.73           N  
ANISOU  311  NZ  LYS A  75    10235   8580   8820   -273    986    -90       N  
ATOM    312  N   THR A  76      19.211  52.532  18.356  1.00 61.13           N  
ANISOU  312  N   THR A  76     8697   7286   7244   -129    331    149       N  
ATOM    313  CA  THR A  76      17.853  52.111  18.143  1.00 58.73           C  
ANISOU  313  CA  THR A  76     8409   6984   6924   -107    197    184       C  
ATOM    314  C   THR A  76      17.038  52.561  19.329  1.00 63.99           C  
ANISOU  314  C   THR A  76     8921   7724   7669    -46    113    189       C  
ATOM    315  O   THR A  76      17.562  52.861  20.369  1.00 57.69           O  
ANISOU  315  O   THR A  76     7997   6988   6933    -22    165    169       O  
ATOM    316  CB  THR A  76      17.718  50.597  17.974  1.00 53.92           C  
ANISOU  316  CB  THR A  76     7783   6394   6310   -117    206    190       C  
ATOM    317  OG1 THR A  76      17.935  49.950  19.215  1.00 59.05           O  
ANISOU  317  OG1 THR A  76     8253   7139   7043    -79    237    177       O  
ATOM    318  CG2 THR A  76      18.694  50.092  17.004  1.00 50.81           C  
ANISOU  318  CG2 THR A  76     7511   5938   5858   -180    315    174       C  
ATOM    319  N   ILE A  77      15.740  52.655  19.159  1.00 61.21           N  
ANISOU  319  N   ILE A  77     8582   7358   7317    -22    -18    213       N  
ATOM    320  CA  ILE A  77      14.907  53.112  20.266  1.00 52.55           C  
ANISOU  320  CA  ILE A  77     7339   6322   6304     30    -91    210       C  
ATOM    321  C   ILE A  77      15.101  52.213  21.478  1.00 54.08           C  
ANISOU  321  C   ILE A  77     7369   6614   6565     55    -41    196       C  
ATOM    322  O   ILE A  77      15.298  52.690  22.605  1.00 56.24           O  
ANISOU  322  O   ILE A  77     7520   6950   6900     82    -15    180       O  
ATOM    323  CB  ILE A  77      13.427  53.163  19.842  1.00 55.46           C  
ANISOU  323  CB  ILE A  77     7740   6652   6679     49   -243    229       C  
ATOM    324  CG1 ILE A  77      13.238  54.082  18.644  1.00 64.26           C  
ANISOU  324  CG1 ILE A  77     9031   7661   7724     25   -308    245       C  
ATOM    325  CG2 ILE A  77      12.550  53.599  20.991  1.00 66.49           C  
ANISOU  325  CG2 ILE A  77     8981   8107   8176     98   -307    216       C  
ATOM    326  CD1 ILE A  77      13.103  53.303  17.352  1.00 75.75           C  
ANISOU  326  CD1 ILE A  77    10649   9042   9089    -14   -336    265       C  
ATOM    327  N   THR A  78      15.033  50.892  21.266  1.00 49.40           N  
ANISOU  327  N   THR A  78     6778   6034   5958     45    -28    203       N  
ATOM    328  CA  THR A  78      15.129  49.980  22.394  1.00 46.37           C  
ANISOU  328  CA  THR A  78     6250   5736   5633     69      8    194       C  
ATOM    329  C   THR A  78      16.426  50.211  23.146  1.00 48.75           C  
ANISOU  329  C   THR A  78     6484   6077   5960     68    116    172       C  
ATOM    330  O   THR A  78      16.446  50.163  24.383  1.00 46.24           O  
ANISOU  330  O   THR A  78     6037   5831   5700     97    126    162       O  
ATOM    331  CB  THR A  78      15.001  48.530  21.923  1.00 54.74           C  
ANISOU  331  CB  THR A  78     7337   6792   6669     53     15    205       C  
ATOM    332  OG1 THR A  78      13.682  48.326  21.410  1.00 70.30           O  
ANISOU  332  OG1 THR A  78     9346   8731   8632     62    -97    220       O  
ATOM    333  CG2 THR A  78      15.239  47.532  23.068  1.00 52.02           C  
ANISOU  333  CG2 THR A  78     6858   6530   6378     73     61    197       C  
ATOM    334  N   ASN A  79      17.493  50.553  22.418  1.00 54.10           N  
ANISOU  334  N   ASN A  79     7253   6704   6597     33    194    161       N  
ATOM    335  CA  ASN A  79      18.798  50.784  23.027  1.00 63.37           C  
ANISOU  335  CA  ASN A  79     8367   7905   7806     30    297    131       C  
ATOM    336  C   ASN A  79      18.882  52.097  23.790  1.00 59.15           C  
ANISOU  336  C   ASN A  79     7770   7396   7309     55    291    118       C  
ATOM    337  O   ASN A  79      19.784  52.238  24.633  1.00 56.98           O  
ANISOU  337  O   ASN A  79     7406   7161   7080     66    356     92       O  
ATOM    338  CB  ASN A  79      19.901  50.739  21.974  1.00 58.38           C  
ANISOU  338  CB  ASN A  79     7850   7201   7130    -21    394    113       C  
ATOM    339  CG  ASN A  79      20.232  49.333  21.559  1.00 42.85           C  
ANISOU  339  CG  ASN A  79     5902   5226   5153    -45    437    112       C  
ATOM    340  OD1 ASN A  79      19.850  48.389  22.228  1.00 47.09           O  
ANISOU  340  OD1 ASN A  79     6347   5820   5724    -20    407    122       O  
ATOM    341  ND2 ASN A  79      20.920  49.185  20.447  1.00 44.21           N  
ANISOU  341  ND2 ASN A  79     6197   5323   5277    -98    511     98       N  
ATOM    342  N   ILE A  80      17.962  53.040  23.539  1.00 48.01           N  
ANISOU  342  N   ILE A  80     6398   5959   5884     65    209    132       N  
ATOM    343  CA  ILE A  80      17.846  54.205  24.415  1.00 44.30           C  
ANISOU  343  CA  ILE A  80     5847   5524   5462     93    193    120       C  
ATOM    344  C   ILE A  80      17.430  53.771  25.824  1.00 46.27           C  
ANISOU  344  C   ILE A  80     5942   5863   5777    129    172    115       C  
ATOM    345  O   ILE A  80      18.000  54.229  26.827  1.00 50.07           O  
ANISOU  345  O   ILE A  80     6330   6393   6301    145    214     94       O  
ATOM    346  CB  ILE A  80      16.872  55.236  23.817  1.00 48.29           C  
ANISOU  346  CB  ILE A  80     6424   5975   5948     97    100    136       C  
ATOM    347  CG1 ILE A  80      17.446  55.789  22.510  1.00 47.33           C  
ANISOU  347  CG1 ILE A  80     6470   5761   5752     56    133    140       C  
ATOM    348  CG2 ILE A  80      16.565  56.340  24.843  1.00 46.61           C  
ANISOU  348  CG2 ILE A  80     6106   5806   5798    129     75    122       C  
ATOM    349  CD1 ILE A  80      16.645  56.917  21.899  1.00 46.90           C  
ANISOU  349  CD1 ILE A  80     6503   5642   5676     58     41    156       C  
ATOM    350  N   TYR A  81      16.468  52.852  25.926  1.00 43.28           N  
ANISOU  350  N   TYR A  81     5537   5503   5404    140    112    131       N  
ATOM    351  CA  TYR A  81      16.101  52.328  27.239  1.00 44.29           C  
ANISOU  351  CA  TYR A  81     5534   5708   5585    166    104    125       C  
ATOM    352  C   TYR A  81      17.224  51.488  27.836  1.00 47.56           C  
ANISOU  352  C   TYR A  81     5899   6164   6008    163    185    115       C  
ATOM    353  O   TYR A  81      17.481  51.553  29.045  1.00 48.45           O  
ANISOU  353  O   TYR A  81     5914   6336   6160    181    204    101       O  
ATOM    354  CB  TYR A  81      14.812  51.500  27.152  1.00 49.50           C  
ANISOU  354  CB  TYR A  81     6184   6371   6254    173     29    140       C  
ATOM    355  CG  TYR A  81      13.662  52.300  26.633  1.00 55.91           C  
ANISOU  355  CG  TYR A  81     7031   7136   7077    180    -64    143       C  
ATOM    356  CD1 TYR A  81      13.274  53.467  27.285  1.00 64.36           C  
ANISOU  356  CD1 TYR A  81     8039   8219   8195    198    -91    127       C  
ATOM    357  CD2 TYR A  81      12.984  51.926  25.475  1.00 51.93           C  
ANISOU  357  CD2 TYR A  81     6623   6569   6538    169   -131    161       C  
ATOM    358  CE1 TYR A  81      12.243  54.231  26.818  1.00 66.08           C  
ANISOU  358  CE1 TYR A  81     8283   8387   8436    206   -182    126       C  
ATOM    359  CE2 TYR A  81      11.937  52.693  24.994  1.00 54.54           C  
ANISOU  359  CE2 TYR A  81     6987   6848   6887    179   -232    162       C  
ATOM    360  CZ  TYR A  81      11.575  53.842  25.677  1.00 58.70           C  
ANISOU  360  CZ  TYR A  81     7444   7387   7472    198   -258    144       C  
ATOM    361  OH  TYR A  81      10.550  54.625  25.234  1.00 63.56           O  
ANISOU  361  OH  TYR A  81     8084   7946   8121    209   -363    141       O  
ATOM    362  N   ILE A  82      17.897  50.681  27.021  1.00 46.35           N  
ANISOU  362  N   ILE A  82     5813   5976   5820    139    229    119       N  
ATOM    363  CA  ILE A  82      18.913  49.797  27.586  1.00 50.90           C  
ANISOU  363  CA  ILE A  82     6336   6585   6419    138    294    107       C  
ATOM    364  C   ILE A  82      20.073  50.612  28.127  1.00 42.21           C  
ANISOU  364  C   ILE A  82     5193   5494   5350    142    356     77       C  
ATOM    365  O   ILE A  82      20.600  50.334  29.213  1.00 42.18           O  
ANISOU  365  O   ILE A  82     5099   5539   5387    160    374     64       O  
ATOM    366  CB  ILE A  82      19.365  48.771  26.539  1.00 47.73           C  
ANISOU  366  CB  ILE A  82     6013   6137   5984    108    333    112       C  
ATOM    367  CG1 ILE A  82      18.153  47.960  26.096  1.00 53.68           C  
ANISOU  367  CG1 ILE A  82     6800   6886   6712    108    265    140       C  
ATOM    368  CG2 ILE A  82      20.422  47.911  27.118  1.00 56.32           C  
ANISOU  368  CG2 ILE A  82     7039   7250   7110    110    393     96       C  
ATOM    369  CD1 ILE A  82      18.474  46.689  25.419  1.00 57.77           C  
ANISOU  369  CD1 ILE A  82     7362   7380   7208     84    298    146       C  
ATOM    370  N   LEU A  83      20.467  51.645  27.386  1.00 41.97           N  
ANISOU  370  N   LEU A  83     5233   5413   5302    126    384     65       N  
ATOM    371  CA  LEU A  83      21.456  52.600  27.867  1.00 46.37           C  
ANISOU  371  CA  LEU A  83     5750   5976   5894    130    439     32       C  
ATOM    372  C   LEU A  83      21.118  53.112  29.274  1.00 52.72           C  
ANISOU  372  C   LEU A  83     6440   6850   6740    165    403     28       C  
ATOM    373  O   LEU A  83      21.976  53.148  30.170  1.00 53.56           O  
ANISOU  373  O   LEU A  83     6470   6991   6890    178    439      3       O  
ATOM    374  CB  LEU A  83      21.539  53.754  26.870  1.00 51.85           C  
ANISOU  374  CB  LEU A  83     6545   6603   6553    108    457     27       C  
ATOM    375  CG  LEU A  83      22.545  54.879  27.090  1.00 43.42           C  
ANISOU  375  CG  LEU A  83     5459   5523   5515    106    523    -10       C  
ATOM    376  CD1 LEU A  83      23.933  54.324  27.342  1.00 40.01           C  
ANISOU  376  CD1 LEU A  83     4983   5090   5130     98    611    -48       C  
ATOM    377  CD2 LEU A  83      22.531  55.735  25.854  1.00 36.96           C  
ANISOU  377  CD2 LEU A  83     4775   4623   4644     74    541     -8       C  
ATOM    378  N   ASN A  84      19.859  53.496  29.490  1.00 39.06           N  
ANISOU  378  N   ASN A  84     4699   5139   5004    178    330     47       N  
ATOM    379  CA  ASN A  84      19.481  54.015  30.793  1.00 38.23           C  
ANISOU  379  CA  ASN A  84     4493   5095   4938    203    305     38       C  
ATOM    380  C   ASN A  84      19.522  52.927  31.856  1.00 45.74           C  
ANISOU  380  C   ASN A  84     5369   6104   5908    215    302     41       C  
ATOM    381  O   ASN A  84      20.046  53.149  32.955  1.00 45.07           O  
ANISOU  381  O   ASN A  84     5211   6061   5852    228    320     23       O  
ATOM    382  CB  ASN A  84      18.110  54.681  30.694  1.00 45.98           C  
ANISOU  382  CB  ASN A  84     5479   6070   5921    210    233     50       C  
ATOM    383  CG  ASN A  84      18.216  56.145  30.201  1.00 59.64           C  
ANISOU  383  CG  ASN A  84     7249   7760   7651    207    234     40       C  
ATOM    384  OD1 ASN A  84      18.045  57.083  30.977  1.00 68.07           O  
ANISOU  384  OD1 ASN A  84     8251   8857   8754    221    227     24       O  
ATOM    385  ND2 ASN A  84      18.553  56.327  28.922  1.00 56.25           N  
ANISOU  385  ND2 ASN A  84     6932   7262   7179    186    249     48       N  
ATOM    386  N   LEU A  85      19.020  51.733  31.537  1.00 47.15           N  
ANISOU  386  N   LEU A  85     5570   6278   6066    209    280     62       N  
ATOM    387  CA  LEU A  85      19.207  50.607  32.436  1.00 40.58           C  
ANISOU  387  CA  LEU A  85     4683   5490   5245    217    284     67       C  
ATOM    388  C   LEU A  85      20.684  50.395  32.743  1.00 46.69           C  
ANISOU  388  C   LEU A  85     5433   6264   6042    219    338     46       C  
ATOM    389  O   LEU A  85      21.070  50.166  33.901  1.00 40.76           O  
ANISOU  389  O   LEU A  85     4617   5554   5314    233    336     38       O  
ATOM    390  CB  LEU A  85      18.605  49.360  31.807  1.00 42.25           C  
ANISOU  390  CB  LEU A  85     4936   5686   5432    208    263     91       C  
ATOM    391  CG  LEU A  85      18.503  48.114  32.668  1.00 48.35           C  
ANISOU  391  CG  LEU A  85     5662   6499   6212    214    257    101       C  
ATOM    392  CD1 LEU A  85      18.112  48.437  34.111  1.00 54.17           C  
ANISOU  392  CD1 LEU A  85     6326   7290   6967    227    240     93       C  
ATOM    393  CD2 LEU A  85      17.490  47.203  32.023  1.00 55.45           C  
ANISOU  393  CD2 LEU A  85     6598   7382   7089    206    225    123       C  
ATOM    394  N   ALA A  86      21.531  50.493  31.707  1.00 43.25           N  
ANISOU  394  N   ALA A  86     5055   5776   5604    203    386     34       N  
ATOM    395  CA  ALA A  86      22.971  50.302  31.875  1.00 38.44           C  
ANISOU  395  CA  ALA A  86     4419   5152   5034    202    442      3       C  
ATOM    396  C   ALA A  86      23.602  51.393  32.743  1.00 47.07           C  
ANISOU  396  C   ALA A  86     5450   6268   6165    219    455    -27       C  
ATOM    397  O   ALA A  86      24.422  51.083  33.609  1.00 46.06           O  
ANISOU  397  O   ALA A  86     5261   6162   6080    233    461    -47       O  
ATOM    398  CB  ALA A  86      23.638  50.234  30.503  1.00 38.26           C  
ANISOU  398  CB  ALA A  86     4477   5059   5002    172    502    -11       C  
ATOM    399  N   ILE A  87      23.245  52.673  32.525  1.00 44.24           N  
ANISOU  399  N   ILE A  87     5110   5903   5796    217    455    -33       N  
ATOM    400  CA  ILE A  87      23.713  53.748  33.411  1.00 41.86           C  
ANISOU  400  CA  ILE A  87     4746   5630   5530    234    465    -61       C  
ATOM    401  C   ILE A  87      23.221  53.544  34.847  1.00 40.12           C  
ANISOU  401  C   ILE A  87     4450   5476   5316    254    415    -52       C  
ATOM    402  O   ILE A  87      23.969  53.739  35.812  1.00 47.37           O  
ANISOU  402  O   ILE A  87     5308   6420   6269    268    421    -76       O  
ATOM    403  CB  ILE A  87      23.282  55.123  32.880  1.00 39.14           C  
ANISOU  403  CB  ILE A  87     4438   5263   5171    227    469    -64       C  
ATOM    404  CG1 ILE A  87      23.994  55.443  31.573  1.00 39.34           C  
ANISOU  404  CG1 ILE A  87     4547   5214   5186    202    531    -80       C  
ATOM    405  CG2 ILE A  87      23.539  56.180  33.944  1.00 39.27           C  
ANISOU  405  CG2 ILE A  87     4379   5319   5223    246    470    -90       C  
ATOM    406  CD1 ILE A  87      23.658  56.836  31.023  1.00 39.96           C  
ANISOU  406  CD1 ILE A  87     4675   5262   5247    195    535    -83       C  
ATOM    407  N   ALA A  88      21.955  53.182  35.017  1.00 36.31           N  
ANISOU  407  N   ALA A  88     3974   5019   4805    253    368    -22       N  
ATOM    408  CA  ALA A  88      21.468  52.863  36.359  1.00 44.87           C  
ANISOU  408  CA  ALA A  88     5000   6159   5890    263    334    -17       C  
ATOM    409  C   ALA A  88      22.219  51.683  36.975  1.00 43.30           C  
ANISOU  409  C   ALA A  88     4782   5973   5699    269    331    -15       C  
ATOM    410  O   ALA A  88      22.559  51.718  38.162  1.00 45.31           O  
ANISOU  410  O   ALA A  88     4990   6262   5965    279    317    -26       O  
ATOM    411  CB  ALA A  88      19.961  52.574  36.337  1.00 43.37           C  
ANISOU  411  CB  ALA A  88     4822   5981   5675    256    293      8       C  
ATOM    412  N   ASP A  89      22.457  50.616  36.210  1.00 41.76           N  
ANISOU  412  N   ASP A  89     4623   5747   5497    262    340     -1       N  
ATOM    413  CA  ASP A  89      23.180  49.480  36.789  1.00 52.81           C  
ANISOU  413  CA  ASP A  89     6000   7152   6913    270    331      0       C  
ATOM    414  C   ASP A  89      24.625  49.858  37.111  1.00 47.01           C  
ANISOU  414  C   ASP A  89     5228   6401   6232    282    354    -38       C  
ATOM    415  O   ASP A  89      25.157  49.477  38.157  1.00 52.82           O  
ANISOU  415  O   ASP A  89     5925   7157   6988    296    325    -45       O  
ATOM    416  CB  ASP A  89      23.135  48.267  35.853  1.00 65.49           C  
ANISOU  416  CB  ASP A  89     7649   8724   8508    258    340     19       C  
ATOM    417  CG  ASP A  89      21.773  47.536  35.875  1.00 68.77           C  
ANISOU  417  CG  ASP A  89     8088   9162   8880    251    306     55       C  
ATOM    418  OD1 ASP A  89      21.049  47.649  36.905  1.00 58.72           O  
ANISOU  418  OD1 ASP A  89     6788   7931   7593    256    276     63       O  
ATOM    419  OD2 ASP A  89      21.440  46.850  34.855  1.00 59.93           O  
ANISOU  419  OD2 ASP A  89     7014   8012   7743    238    313     71       O  
ATOM    420  N   GLU A  90      25.259  50.638  36.235  1.00 50.32           N  
ANISOU  420  N   GLU A  90     5661   6781   6677    275    404    -66       N  
ATOM    421  CA  GLU A  90      26.605  51.141  36.488  1.00 41.30           C  
ANISOU  421  CA  GLU A  90     4476   5617   5598    286    433   -112       C  
ATOM    422  C   GLU A  90      26.691  51.920  37.797  1.00 43.25           C  
ANISOU  422  C   GLU A  90     4667   5910   5856    305    401   -126       C  
ATOM    423  O   GLU A  90      27.597  51.680  38.606  1.00 57.34           O  
ANISOU  423  O   GLU A  90     6405   7695   7686    322    380   -150       O  
ATOM    424  CB  GLU A  90      27.053  52.022  35.321  1.00 52.88           C  
ANISOU  424  CB  GLU A  90     5980   7033   7080    269    502   -140       C  
ATOM    425  CG  GLU A  90      28.532  52.384  35.346  1.00 57.56           C  
ANISOU  425  CG  GLU A  90     6530   7586   7753    274    550   -199       C  
ATOM    426  CD  GLU A  90      29.408  51.364  34.604  1.00 70.84           C  
ANISOU  426  CD  GLU A  90     8224   9209   9482    259    591   -221       C  
ATOM    427  OE1 GLU A  90      30.498  51.753  34.100  1.00 59.59           O  
ANISOU  427  OE1 GLU A  90     6789   7728   8123    249    660   -276       O  
ATOM    428  OE2 GLU A  90      29.012  50.174  34.538  1.00 71.74           O  
ANISOU  428  OE2 GLU A  90     8354   9328   9574    257    561   -189       O  
ATOM    429  N   LEU A  91      25.800  52.899  38.004  1.00 39.30           N  
ANISOU  429  N   LEU A  91     4170   5442   5322    302    394   -116       N  
ATOM    430  CA  LEU A  91      25.867  53.686  39.234  1.00 37.71           C  
ANISOU  430  CA  LEU A  91     3917   5282   5129    315    371   -133       C  
ATOM    431  C   LEU A  91      25.557  52.833  40.457  1.00 47.94           C  
ANISOU  431  C   LEU A  91     5199   6616   6400    320    315   -113       C  
ATOM    432  O   LEU A  91      26.142  53.041  41.531  1.00 50.49           O  
ANISOU  432  O   LEU A  91     5485   6958   6741    332    289   -132       O  
ATOM    433  CB  LEU A  91      24.923  54.881  39.160  1.00 38.82           C  
ANISOU  433  CB  LEU A  91     4062   5443   5245    307    379   -129       C  
ATOM    434  CG  LEU A  91      25.212  55.982  38.114  1.00 49.55           C  
ANISOU  434  CG  LEU A  91     5442   6763   6623    301    430   -150       C  
ATOM    435  CD1 LEU A  91      24.213  57.128  38.180  1.00 39.49           C  
ANISOU  435  CD1 LEU A  91     4166   5509   5330    297    423   -144       C  
ATOM    436  CD2 LEU A  91      26.628  56.538  38.255  1.00 54.74           C  
ANISOU  436  CD2 LEU A  91     6060   7398   7339    312    468   -199       C  
ATOM    437  N   PHE A  92      24.657  51.862  40.291  1.00 48.89           N  
ANISOU  437  N   PHE A  92     5354   6744   6477    309    295    -75       N  
ATOM    438  CA  PHE A  92      24.338  50.893  41.328  1.00 47.47           C  
ANISOU  438  CA  PHE A  92     5178   6592   6268    309    250    -52       C  
ATOM    439  C   PHE A  92      25.599  50.208  41.851  1.00 55.12           C  
ANISOU  439  C   PHE A  92     6127   7541   7274    326    221    -67       C  
ATOM    440  O   PHE A  92      25.787  50.051  43.065  1.00 57.27           O  
ANISOU  440  O   PHE A  92     6391   7835   7534    332    176    -68       O  
ATOM    441  CB  PHE A  92      23.365  49.867  40.739  1.00 46.28           C  
ANISOU  441  CB  PHE A  92     5068   6436   6080    295    246    -16       C  
ATOM    442  CG  PHE A  92      22.414  49.279  41.724  1.00 43.59           C  
ANISOU  442  CG  PHE A  92     4740   6130   5693    283    216      8       C  
ATOM    443  CD1 PHE A  92      21.907  50.047  42.775  1.00 44.18           C  
ANISOU  443  CD1 PHE A  92     4798   6239   5748    274    210     -3       C  
ATOM    444  CD2 PHE A  92      22.001  47.967  41.584  1.00 48.55           C  
ANISOU  444  CD2 PHE A  92     5399   6750   6297    276    202     37       C  
ATOM    445  CE1 PHE A  92      21.016  49.517  43.684  1.00 38.03           C  
ANISOU  445  CE1 PHE A  92     4039   5486   4926    255    196     12       C  
ATOM    446  CE2 PHE A  92      21.104  47.408  42.489  1.00 52.48           C  
ANISOU  446  CE2 PHE A  92     5914   7274   6751    261    185     54       C  
ATOM    447  CZ  PHE A  92      20.604  48.187  43.544  1.00 52.78           C  
ANISOU  447  CZ  PHE A  92     5942   7343   6769    248    185     41       C  
ATOM    448  N   MET A  93      26.468  49.774  40.935  1.00 45.20           N  
ANISOU  448  N   MET A  93     4869   6239   6067    332    244    -81       N  
ATOM    449  CA  MET A  93      27.683  49.074  41.329  1.00 50.21           C  
ANISOU  449  CA  MET A  93     5476   6843   6757    350    214   -102       C  
ATOM    450  C   MET A  93      28.606  49.967  42.159  1.00 63.11           C  
ANISOU  450  C   MET A  93     7062   8479   8438    368    195   -144       C  
ATOM    451  O   MET A  93      29.323  49.471  43.039  1.00 57.96           O  
ANISOU  451  O   MET A  93     6391   7818   7815    385    136   -154       O  
ATOM    452  CB  MET A  93      28.396  48.551  40.077  1.00 47.22           C  
ANISOU  452  CB  MET A  93     5100   6407   6434    346    259   -119       C  
ATOM    453  CG  MET A  93      27.579  47.526  39.227  1.00 41.06           C  
ANISOU  453  CG  MET A  93     4370   5620   5611    328    273    -79       C  
ATOM    454  SD  MET A  93      27.049  46.149  40.274  1.00 65.32           S  
ANISOU  454  SD  MET A  93     7459   8720   8640    333    200    -35       S  
ATOM    455  CE  MET A  93      26.579  44.921  39.081  1.00 70.98           C  
ANISOU  455  CE  MET A  93     8217   9410   9343    316    228     -6       C  
ATOM    456  N   LEU A  94      28.577  51.284  41.924  1.00 65.56           N  
ANISOU  456  N   LEU A  94     7354   8799   8757    366    238   -169       N  
ATOM    457  CA  LEU A  94      29.473  52.192  42.633  1.00 59.41           C  
ANISOU  457  CA  LEU A  94     6525   8020   8028    383    227   -214       C  
ATOM    458  C   LEU A  94      29.191  52.258  44.123  1.00 57.47           C  
ANISOU  458  C   LEU A  94     6278   7818   7740    388    160   -202       C  
ATOM    459  O   LEU A  94      30.076  52.661  44.884  1.00 66.21           O  
ANISOU  459  O   LEU A  94     7347   8918   8890    406    126   -238       O  
ATOM    460  CB  LEU A  94      29.375  53.603  42.069  1.00 55.85           C  
ANISOU  460  CB  LEU A  94     6061   7572   7587    377    290   -239       C  
ATOM    461  CG  LEU A  94      29.947  53.839  40.689  1.00 47.13           C  
ANISOU  461  CG  LEU A  94     4963   6414   6532    369    364   -266       C  
ATOM    462  CD1 LEU A  94      29.676  55.285  40.327  1.00 58.17           C  
ANISOU  462  CD1 LEU A  94     6360   7820   7923    362    415   -283       C  
ATOM    463  CD2 LEU A  94      31.439  53.556  40.671  1.00 49.74           C  
ANISOU  463  CD2 LEU A  94     5245   6690   6963    385    370   -321       C  
ATOM    464  N   GLY A  95      27.988  51.904  44.561  1.00 48.91           N  
ANISOU  464  N   GLY A  95     5236   6773   6573    369    143   -158       N  
ATOM    465  CA  GLY A  95      27.752  51.879  45.993  1.00 50.01           C  
ANISOU  465  CA  GLY A  95     5390   6946   6667    365     87   -150       C  
ATOM    466  C   GLY A  95      28.187  50.603  46.673  1.00 57.03           C  
ANISOU  466  C   GLY A  95     6306   7815   7547    373     15   -132       C  
ATOM    467  O   GLY A  95      28.302  50.559  47.907  1.00 50.72           O  
ANISOU  467  O   GLY A  95     5528   7029   6716    372    -43   -130       O  
ATOM    468  N   LEU A  96      28.445  49.565  45.880  1.00 48.83           N  
ANISOU  468  N   LEU A  96     5275   6741   6537    380     16   -118       N  
ATOM    469  CA  LEU A  96      28.784  48.267  46.447  1.00 50.50           C  
ANISOU  469  CA  LEU A  96     5515   6930   6743    387    -54    -97       C  
ATOM    470  C   LEU A  96      30.010  48.294  47.355  1.00 62.98           C  
ANISOU  470  C   LEU A  96     7072   8482   8377    413   -133   -129       C  
ATOM    471  O   LEU A  96      29.982  47.611  48.397  1.00 54.37           O  
ANISOU  471  O   LEU A  96     6028   7390   7242    412   -209   -106       O  
ATOM    472  CB  LEU A  96      28.971  47.268  45.308  1.00 60.14           C  
ANISOU  472  CB  LEU A  96     6735   8112   8004    391    -31    -86       C  
ATOM    473  CG  LEU A  96      28.456  45.871  45.593  1.00 57.01           C  
ANISOU  473  CG  LEU A  96     6391   7713   7558    382    -70    -40       C  
ATOM    474  CD1 LEU A  96      27.274  45.960  46.530  1.00 54.24           C  
ANISOU  474  CD1 LEU A  96     6095   7410   7104    357    -80     -7       C  
ATOM    475  CD2 LEU A  96      28.065  45.234  44.288  1.00 45.95           C  
ANISOU  475  CD2 LEU A  96     4996   6297   6167    372    -14    -24       C  
ATOM    476  N   PRO A  97      31.098  49.024  47.044  1.00 74.51           N  
ANISOU  476  N   PRO A  97     8466   9913   9931    436   -122   -183       N  
ATOM    477  CA  PRO A  97      32.252  49.004  47.964  1.00 71.02           C  
ANISOU  477  CA  PRO A  97     7998   9438   9550    463   -210   -217       C  
ATOM    478  C   PRO A  97      31.884  49.430  49.367  1.00 66.08           C  
ANISOU  478  C   PRO A  97     7414   8849   8843    454   -269   -204       C  
ATOM    479  O   PRO A  97      32.130  48.675  50.319  1.00 72.86           O  
ANISOU  479  O   PRO A  97     8317   9689   9676    460   -365   -187       O  
ATOM    480  CB  PRO A  97      33.240  49.972  47.302  1.00 65.17           C  
ANISOU  480  CB  PRO A  97     7175   8667   8919    481   -160   -284       C  
ATOM    481  CG  PRO A  97      32.913  49.873  45.836  1.00 57.67           C  
ANISOU  481  CG  PRO A  97     6220   7707   7985    466    -61   -279       C  
ATOM    482  CD  PRO A  97      31.412  49.782  45.813  1.00 66.47           C  
ANISOU  482  CD  PRO A  97     7399   8879   8979    437    -33   -219       C  
ATOM    483  N   PHE A  98      31.272  50.609  49.509  1.00 55.64           N  
ANISOU  483  N   PHE A  98     6087   7575   7478    437   -214   -212       N  
ATOM    484  CA  PHE A  98      30.773  51.064  50.808  1.00 56.41           C  
ANISOU  484  CA  PHE A  98     6232   7712   7491    418   -252   -200       C  
ATOM    485  C   PHE A  98      29.990  49.977  51.541  1.00 56.45           C  
ANISOU  485  C   PHE A  98     6330   7724   7396    393   -297   -147       C  
ATOM    486  O   PHE A  98      30.237  49.705  52.720  1.00 55.28           O  
ANISOU  486  O   PHE A  98     6235   7566   7204    389   -380   -140       O  
ATOM    487  CB  PHE A  98      29.906  52.309  50.625  1.00 52.95           C  
ANISOU  487  CB  PHE A  98     5776   7324   7016    394   -165   -208       C  
ATOM    488  CG  PHE A  98      30.580  53.404  49.848  1.00 51.95           C  
ANISOU  488  CG  PHE A  98     5570   7189   6979    414   -111   -257       C  
ATOM    489  CD1 PHE A  98      30.678  53.338  48.473  1.00 51.01           C  
ANISOU  489  CD1 PHE A  98     5419   7047   6914    421    -45   -262       C  
ATOM    490  CD2 PHE A  98      31.108  54.501  50.497  1.00 54.97           C  
ANISOU  490  CD2 PHE A  98     5916   7583   7388    423   -121   -299       C  
ATOM    491  CE1 PHE A  98      31.286  54.323  47.765  1.00 55.20           C  
ANISOU  491  CE1 PHE A  98     5890   7563   7520    434     12   -308       C  
ATOM    492  CE2 PHE A  98      31.727  55.500  49.786  1.00 51.82           C  
ANISOU  492  CE2 PHE A  98     5446   7173   7072    440    -65   -346       C  
ATOM    493  CZ  PHE A  98      31.815  55.413  48.420  1.00 59.46           C  
ANISOU  493  CZ  PHE A  98     6389   8114   8089    444      4   -351       C  
ATOM    494  N   LEU A  99      29.056  49.320  50.856  1.00 59.42           N  
ANISOU  494  N   LEU A  99     6733   8113   7733    374   -245   -109       N  
ATOM    495  CA  LEU A  99      28.202  48.367  51.562  1.00 52.30           C  
ANISOU  495  CA  LEU A  99     5921   7219   6733    344   -272    -62       C  
ATOM    496  C   LEU A  99      28.957  47.098  51.932  1.00 50.76           C  
ANISOU  496  C   LEU A  99     5763   6974   6552    363   -368    -44       C  
ATOM    497  O   LEU A  99      28.619  46.449  52.927  1.00 55.45           O  
ANISOU  497  O   LEU A  99     6444   7563   7063    342   -421    -14       O  
ATOM    498  CB  LEU A  99      26.956  48.046  50.724  1.00 47.36           C  
ANISOU  498  CB  LEU A  99     5306   6617   6070    319   -189    -32       C  
ATOM    499  CG  LEU A  99      26.145  49.312  50.363  1.00 49.68           C  
ANISOU  499  CG  LEU A  99     5564   6954   6358    301   -105    -50       C  
ATOM    500  CD1 LEU A  99      25.057  49.059  49.329  1.00 50.40           C  
ANISOU  500  CD1 LEU A  99     5653   7057   6439    285    -36    -29       C  
ATOM    501  CD2 LEU A  99      25.573  49.981  51.586  1.00 40.61           C  
ANISOU  501  CD2 LEU A  99     4452   5837   5140    268   -104    -57       C  
ATOM    502  N   ALA A 100      29.986  46.738  51.161  1.00 53.55           N  
ANISOU  502  N   ALA A 100     6054   7282   7010    400   -389    -66       N  
ATOM    503  CA  ALA A 100      30.765  45.547  51.490  1.00 51.59           C  
ANISOU  503  CA  ALA A 100     5831   6978   6795    422   -488    -54       C  
ATOM    504  C   ALA A 100      31.530  45.718  52.793  1.00 56.56           C  
ANISOU  504  C   ALA A 100     6492   7582   7418    435   -602    -70       C  
ATOM    505  O   ALA A 100      31.730  44.737  53.522  1.00 64.23           O  
ANISOU  505  O   ALA A 100     7532   8516   8355    437   -698    -42       O  
ATOM    506  CB  ALA A 100      31.731  45.209  50.362  1.00 53.88           C  
ANISOU  506  CB  ALA A 100     6037   7220   7216    455   -477    -86       C  
ATOM    507  N   MET A 101      31.957  46.945  53.106  1.00 51.68           N  
ANISOU  507  N   MET A 101     5830   6979   6828    443   -598   -113       N  
ATOM    508  CA  MET A 101      32.623  47.185  54.380  1.00 55.40           C  
ANISOU  508  CA  MET A 101     6337   7428   7285    453   -709   -129       C  
ATOM    509  C   MET A 101      31.708  46.894  55.547  1.00 62.01           C  
ANISOU  509  C   MET A 101     7301   8288   7970    409   -738    -83       C  
ATOM    510  O   MET A 101      32.170  46.453  56.606  1.00 65.17           O  
ANISOU  510  O   MET A 101     7777   8650   8336    412   -856    -74       O  
ATOM    511  CB  MET A 101      33.113  48.628  54.461  1.00 60.74           C  
ANISOU  511  CB  MET A 101     6940   8123   8013    465   -683   -185       C  
ATOM    512  CG  MET A 101      34.287  48.902  53.532  1.00 76.19           C  
ANISOU  512  CG  MET A 101     8780  10038  10132    508   -673   -244       C  
ATOM    513  SD  MET A 101      35.694  47.833  53.882  1.00 81.95           S  
ANISOU  513  SD  MET A 101     9493  10672  10972    554   -825   -267       S  
ATOM    514  CE  MET A 101      36.048  47.230  52.234  1.00 82.34           C  
ANISOU  514  CE  MET A 101     9455  10686  11146    570   -741   -285       C  
ATOM    515  N   GLN A 102      30.414  47.171  55.374  1.00 66.55           N  
ANISOU  515  N   GLN A 102     7907   8920   8460    366   -632    -58       N  
ATOM    516  CA  GLN A 102      29.429  46.901  56.410  1.00 62.72           C  
ANISOU  516  CA  GLN A 102     7543   8454   7834    315   -633    -22       C  
ATOM    517  C   GLN A 102      29.123  45.407  56.512  1.00 60.68           C  
ANISOU  517  C   GLN A 102     7368   8161   7524    304   -674     29       C  
ATOM    518  O   GLN A 102      28.819  44.910  57.599  1.00 57.01           O  
ANISOU  518  O   GLN A 102     7025   7681   6956    272   -727     57       O  
ATOM    519  CB  GLN A 102      28.164  47.714  56.122  1.00 51.93           C  
ANISOU  519  CB  GLN A 102     6162   7150   6417    274   -502    -24       C  
ATOM    520  CG  GLN A 102      27.006  47.360  57.017  1.00 54.81           C  
ANISOU  520  CG  GLN A 102     6645   7532   6651    213   -474      8       C  
ATOM    521  CD  GLN A 102      26.102  48.526  57.294  1.00 56.56           C  
ANISOU  521  CD  GLN A 102     6855   7803   6832    171   -379    -16       C  
ATOM    522  OE1 GLN A 102      26.574  49.630  57.556  1.00 64.11           O  
ANISOU  522  OE1 GLN A 102     7766   8776   7818    181   -383    -53       O  
ATOM    523  NE2 GLN A 102      24.787  48.293  57.233  1.00 57.38           N  
ANISOU  523  NE2 GLN A 102     6996   7929   6875    124   -292      0       N  
ATOM    524  N   VAL A 103      29.217  44.677  55.398  1.00 54.20           N  
ANISOU  524  N   VAL A 103     6492   7326   6774    328   -649     40       N  
ATOM    525  CA  VAL A 103      29.105  43.226  55.446  1.00 54.43           C  
ANISOU  525  CA  VAL A 103     6589   7317   6774    326   -697     84       C  
ATOM    526  C   VAL A 103      30.292  42.619  56.182  1.00 57.41           C  
ANISOU  526  C   VAL A 103     7003   7626   7184    358   -848     83       C  
ATOM    527  O   VAL A 103      30.132  41.694  56.987  1.00 62.00           O  
ANISOU  527  O   VAL A 103     7697   8173   7685    340   -921    122       O  
ATOM    528  CB  VAL A 103      28.982  42.673  54.018  1.00 60.97           C  
ANISOU  528  CB  VAL A 103     7341   8146   7680    345   -630     89       C  
ATOM    529  CG1 VAL A 103      29.036  41.122  54.015  1.00 62.59           C  
ANISOU  529  CG1 VAL A 103     7603   8304   7874    349   -687    131       C  
ATOM    530  CG2 VAL A 103      27.725  43.215  53.379  1.00 60.03           C  
ANISOU  530  CG2 VAL A 103     7203   8086   7520    312   -498     93       C  
ATOM    531  N   ALA A 104      31.500  43.131  55.921  1.00 56.61           N  
ANISOU  531  N   ALA A 104     6808   7497   7206    405   -901     35       N  
ATOM    532  CA  ALA A 104      32.703  42.536  56.496  1.00 61.34           C  
ANISOU  532  CA  ALA A 104     7422   8020   7867    442  -1055     26       C  
ATOM    533  C   ALA A 104      32.856  42.911  57.960  1.00 69.63           C  
ANISOU  533  C   ALA A 104     8573   9056   8826    426  -1155     28       C  
ATOM    534  O   ALA A 104      33.307  42.093  58.778  1.00 64.19           O  
ANISOU  534  O   ALA A 104     7974   8306   8110    433  -1289     51       O  
ATOM    535  CB  ALA A 104      33.946  42.972  55.712  1.00 55.68           C  
ANISOU  535  CB  ALA A 104     6562   7269   7326    495  -1072    -38       C  
ATOM    536  N   LEU A 105      32.483  44.142  58.308  1.00 68.07           N  
ANISOU  536  N   LEU A 105     8369   8911   8581    403  -1094      5       N  
ATOM    537  CA  LEU A 105      32.722  44.664  59.644  1.00 67.89           C  
ANISOU  537  CA  LEU A 105     8434   8878   8484    387  -1182     -3       C  
ATOM    538  C   LEU A 105      31.488  44.722  60.525  1.00 59.34           C  
ANISOU  538  C   LEU A 105     7490   7833   7224    316  -1128     35       C  
ATOM    539  O   LEU A 105      31.637  44.836  61.744  1.00 61.27           O  
ANISOU  539  O   LEU A 105     7847   8053   7381    293  -1214     40       O  
ATOM    540  CB  LEU A 105      33.301  46.075  59.561  1.00 64.42           C  
ANISOU  540  CB  LEU A 105     7892   8464   8122    408  -1159    -65       C  
ATOM    541  CG  LEU A 105      34.592  46.102  58.780  1.00 61.12           C  
ANISOU  541  CG  LEU A 105     7338   8000   7886    473  -1208   -116       C  
ATOM    542  CD1 LEU A 105      35.068  47.523  58.627  1.00 53.06           C  
ANISOU  542  CD1 LEU A 105     6215   7007   6940    490  -1164   -178       C  
ATOM    543  CD2 LEU A 105      35.586  45.247  59.538  1.00 56.05           C  
ANISOU  543  CD2 LEU A 105     6749   7270   7278    505  -1392   -114       C  
ATOM    544  N   GLU A 106      30.289  44.664  59.944  1.00 58.55           N  
ANISOU  544  N   GLU A 106     7387   7785   7075    279   -988     56       N  
ATOM    545  CA  GLU A 106      29.058  45.051  60.641  1.00 60.82           C  
ANISOU  545  CA  GLU A 106     7770   8116   7224    208   -900     71       C  
ATOM    546  C   GLU A 106      29.220  46.430  61.281  1.00 57.58           C  
ANISOU  546  C   GLU A 106     7345   7736   6799    195   -890     28       C  
ATOM    547  O   GLU A 106      28.742  46.684  62.394  1.00 58.47           O  
ANISOU  547  O   GLU A 106     7574   7852   6792    140   -891     33       O  
ATOM    548  CB  GLU A 106      28.632  43.994  61.671  1.00 64.65           C  
ANISOU  548  CB  GLU A 106     8433   8558   7572    163   -958    119       C  
ATOM    549  CG  GLU A 106      27.932  42.729  61.085  1.00 79.84           C  
ANISOU  549  CG  GLU A 106    10387  10472   9476    152   -912    164       C  
ATOM    550  CD  GLU A 106      26.843  43.011  60.014  1.00 89.71           C  
ANISOU  550  CD  GLU A 106    11547  11785  10753    135   -749    158       C  
ATOM    551  OE1 GLU A 106      27.180  43.184  58.816  1.00 87.98           O  
ANISOU  551  OE1 GLU A 106    11193  11582  10653    182   -717    141       O  
ATOM    552  OE2 GLU A 106      25.639  43.034  60.368  1.00 92.17           O  
ANISOU  552  OE2 GLU A 106    11928  12122  10969     73   -653    167       O  
ATOM    553  N   HIS A 107      29.920  47.322  60.564  1.00 55.30           N  
ANISOU  553  N   HIS A 107     6912   7464   6634    242   -876    -17       N  
ATOM    554  CA  HIS A 107      30.157  48.703  60.976  1.00 55.36           C  
ANISOU  554  CA  HIS A 107     6878   7504   6654    238   -858    -64       C  
ATOM    555  C   HIS A 107      30.206  49.605  59.743  1.00 54.69           C  
ANISOU  555  C   HIS A 107     6633   7460   6685    269   -756   -100       C  
ATOM    556  O   HIS A 107      30.734  49.212  58.697  1.00 50.59           O  
ANISOU  556  O   HIS A 107     6027   6922   6272    314   -757   -105       O  
ATOM    557  CB  HIS A 107      31.460  48.842  61.784  1.00 57.95           C  
ANISOU  557  CB  HIS A 107     7224   7779   7016    274  -1012    -89       C  
ATOM    558  CG  HIS A 107      31.758  50.252  62.207  1.00 70.10           C  
ANISOU  558  CG  HIS A 107     8714   9348   8572    272   -996   -140       C  
ATOM    559  ND1 HIS A 107      31.156  50.848  63.299  1.00 69.56           N  
ANISOU  559  ND1 HIS A 107     8745   9304   8380    213   -975   -142       N  
ATOM    560  CD2 HIS A 107      32.582  51.189  61.675  1.00 66.53           C  
ANISOU  560  CD2 HIS A 107     8127   8905   8247    319   -990   -194       C  
ATOM    561  CE1 HIS A 107      31.593  52.090  63.415  1.00 65.76           C  
ANISOU  561  CE1 HIS A 107     8186   8848   7951    226   -961   -192       C  
ATOM    562  NE2 HIS A 107      32.457  52.323  62.442  1.00 65.77           N  
ANISOU  562  NE2 HIS A 107     8045   8841   8103    291   -970   -225       N  
ATOM    563  N   TRP A 108      29.630  50.816  59.874  1.00 55.24           N  
ANISOU  563  N   TRP A 108     6673   7583   6732    240   -665   -127       N  
ATOM    564  CA  TRP A 108      29.663  51.827  58.823  1.00 54.53           C  
ANISOU  564  CA  TRP A 108     6446   7530   6741    264   -572   -163       C  
ATOM    565  C   TRP A 108      30.753  52.843  59.143  1.00 54.56           C  
ANISOU  565  C   TRP A 108     6386   7527   6817    297   -624   -217       C  
ATOM    566  O   TRP A 108      30.613  53.600  60.109  1.00 67.59           O  
ANISOU  566  O   TRP A 108     8077   9197   8407    268   -629   -234       O  
ATOM    567  CB  TRP A 108      28.302  52.525  58.675  1.00 58.36           C  
ANISOU  567  CB  TRP A 108     6928   8073   7171    214   -440   -162       C  
ATOM    568  CG  TRP A 108      28.308  53.627  57.627  1.00 52.59           C  
ANISOU  568  CG  TRP A 108     6070   7375   6536    237   -352   -196       C  
ATOM    569  CD1 TRP A 108      28.466  54.969  57.847  1.00 48.87           C  
ANISOU  569  CD1 TRP A 108     5544   6933   6093    236   -318   -239       C  
ATOM    570  CD2 TRP A 108      28.179  53.465  56.209  1.00 45.32           C  
ANISOU  570  CD2 TRP A 108     5072   6456   5690    264   -293   -190       C  
ATOM    571  NE1 TRP A 108      28.448  55.653  56.653  1.00 55.47           N  
ANISOU  571  NE1 TRP A 108     6274   7785   7015    260   -242   -259       N  
ATOM    572  CE2 TRP A 108      28.269  54.756  55.631  1.00 48.30           C  
ANISOU  572  CE2 TRP A 108     5356   6861   6135    276   -226   -229       C  
ATOM    573  CE3 TRP A 108      28.011  52.355  55.369  1.00 45.43           C  
ANISOU  573  CE3 TRP A 108     5092   6450   5720    276   -290   -156       C  
ATOM    574  CZ2 TRP A 108      28.192  54.971  54.254  1.00 43.13           C  
ANISOU  574  CZ2 TRP A 108     4626   6208   5554    298   -159   -233       C  
ATOM    575  CZ3 TRP A 108      27.926  52.567  53.994  1.00 46.77           C  
ANISOU  575  CZ3 TRP A 108     5183   6624   5965    297   -221   -162       C  
ATOM    576  CH2 TRP A 108      28.018  53.871  53.453  1.00 52.28           C  
ANISOU  576  CH2 TRP A 108     5799   7345   6720    307   -158   -199       C  
ATOM    577  N   PRO A 109      31.839  52.896  58.393  1.00 61.45           N  
ANISOU  577  N   PRO A 109     7160   8370   7820    354   -657   -248       N  
ATOM    578  CA  PRO A 109      32.968  53.743  58.806  1.00 58.37           C  
ANISOU  578  CA  PRO A 109     6712   7962   7506    388   -720   -304       C  
ATOM    579  C   PRO A 109      32.942  55.182  58.317  1.00 64.59           C  
ANISOU  579  C   PRO A 109     7398   8792   8351    392   -620   -350       C  
ATOM    580  O   PRO A 109      33.714  55.992  58.836  1.00 81.55           O  
ANISOU  580  O   PRO A 109     9509  10932  10542    410   -663   -397       O  
ATOM    581  CB  PRO A 109      34.175  53.022  58.205  1.00 52.34           C  
ANISOU  581  CB  PRO A 109     5885   7131   6869    446   -799   -323       C  
ATOM    582  CG  PRO A 109      33.633  52.315  57.022  1.00 57.83           C  
ANISOU  582  CG  PRO A 109     6557   7832   7582    445   -719   -291       C  
ATOM    583  CD  PRO A 109      32.214  51.943  57.333  1.00 53.99           C  
ANISOU  583  CD  PRO A 109     6170   7389   6955    389   -663   -234       C  
ATOM    584  N   PHE A 110      32.119  55.527  57.323  1.00 60.77           N  
ANISOU  584  N   PHE A 110     6869   8347   7874    378   -495   -340       N  
ATOM    585  CA  PHE A 110      32.313  56.782  56.604  1.00 51.93           C  
ANISOU  585  CA  PHE A 110     5644   7252   6836    393   -410   -384       C  
ATOM    586  C   PHE A 110      31.418  57.909  57.098  1.00 51.68           C  
ANISOU  586  C   PHE A 110     5621   7278   6739    351   -336   -392       C  
ATOM    587  O   PHE A 110      31.131  58.828  56.332  1.00 50.38           O  
ANISOU  587  O   PHE A 110     5384   7139   6618    352   -242   -412       O  
ATOM    588  CB  PHE A 110      32.074  56.601  55.106  1.00 49.05           C  
ANISOU  588  CB  PHE A 110     5220   6884   6531    406   -323   -375       C  
ATOM    589  CG  PHE A 110      32.500  55.281  54.567  1.00 45.67           C  
ANISOU  589  CG  PHE A 110     4805   6409   6139    429   -371   -352       C  
ATOM    590  CD1 PHE A 110      31.647  54.184  54.612  1.00 53.36           C  
ANISOU  590  CD1 PHE A 110     5859   7387   7030    404   -377   -295       C  
ATOM    591  CD2 PHE A 110      33.732  55.138  53.959  1.00 46.20           C  
ANISOU  591  CD2 PHE A 110     4798   6423   6331    474   -399   -393       C  
ATOM    592  CE1 PHE A 110      32.024  52.957  54.064  1.00 46.57           C  
ANISOU  592  CE1 PHE A 110     5006   6482   6206    424   -416   -274       C  
ATOM    593  CE2 PHE A 110      34.122  53.926  53.442  1.00 55.27           C  
ANISOU  593  CE2 PHE A 110     5953   7524   7523    492   -437   -377       C  
ATOM    594  CZ  PHE A 110      33.258  52.826  53.488  1.00 51.68           C  
ANISOU  594  CZ  PHE A 110     5580   7078   6980    468   -448   -315       C  
ATOM    595  N   GLY A 111      30.947  57.850  58.335  1.00 54.21           N  
ANISOU  595  N   GLY A 111     6032   7613   6954    310   -372   -378       N  
ATOM    596  CA  GLY A 111      30.107  58.911  58.851  1.00 47.40           C  
ANISOU  596  CA  GLY A 111     5174   6799   6036    266   -297   -392       C  
ATOM    597  C   GLY A 111      28.679  58.997  58.341  1.00 51.93           C  
ANISOU  597  C   GLY A 111     5754   7410   6568    224   -186   -366       C  
ATOM    598  O   GLY A 111      28.309  58.372  57.346  1.00 62.30           O  
ANISOU  598  O   GLY A 111     7051   8715   7904    236   -153   -338       O  
ATOM    599  N   LYS A 112      27.887  59.841  59.012  1.00 61.52           N  
ANISOU  599  N   LYS A 112     6984   8661   7730    176   -127   -382       N  
ATOM    600  CA  LYS A 112      26.452  59.957  58.765  1.00 59.96           C  
ANISOU  600  CA  LYS A 112     6796   8491   7495    129    -29   -366       C  
ATOM    601  C   LYS A 112      26.145  60.554  57.400  1.00 57.10           C  
ANISOU  601  C   LYS A 112     6333   8142   7220    155     47   -373       C  
ATOM    602  O   LYS A 112      25.126  60.203  56.788  1.00 44.68           O  
ANISOU  602  O   LYS A 112     4764   6574   5638    136    102   -349       O  
ATOM    603  CB  LYS A 112      25.805  60.807  59.870  1.00 59.25           C  
ANISOU  603  CB  LYS A 112     6738   8429   7344     70     16   -394       C  
ATOM    604  CG  LYS A 112      24.316  61.065  59.710  1.00 68.96           C  
ANISOU  604  CG  LYS A 112     7966   9682   8555     18    122   -393       C  
ATOM    605  CD  LYS A 112      23.632  61.167  61.065  1.00 77.82           C  
ANISOU  605  CD  LYS A 112     9178  10810   9579    -58    150   -408       C  
ATOM    606  CE  LYS A 112      23.307  59.785  61.644  1.00 81.22           C  
ANISOU  606  CE  LYS A 112     9737  11211   9910    -92    114   -369       C  
ATOM    607  NZ  LYS A 112      23.465  59.748  63.137  1.00 80.22           N  
ANISOU  607  NZ  LYS A 112     9729  11074   9678   -145     79   -380       N  
ATOM    608  N   ALA A 113      26.982  61.475  56.918  1.00 60.22           N  
ANISOU  608  N   ALA A 113     6643   8539   7700    195     52   -407       N  
ATOM    609  CA  ALA A 113      26.631  62.184  55.694  1.00 52.27           C  
ANISOU  609  CA  ALA A 113     5557   7541   6764    211    127   -415       C  
ATOM    610  C   ALA A 113      26.770  61.281  54.479  1.00 61.42           C  
ANISOU  610  C   ALA A 113     6710   8670   7956    243    122   -383       C  
ATOM    611  O   ALA A 113      25.887  61.258  53.616  1.00 74.32           O  
ANISOU  611  O   ALA A 113     8333  10308   9597    234    176   -364       O  
ATOM    612  CB  ALA A 113      27.478  63.437  55.537  1.00 43.41           C  
ANISOU  612  CB  ALA A 113     4353   6424   5717    240    143   -462       C  
ATOM    613  N   ILE A 114      27.862  60.522  54.392  1.00 59.38           N  
ANISOU  613  N   ILE A 114     6459   8378   7723    278     53   -380       N  
ATOM    614  CA  ILE A 114      28.001  59.631  53.249  1.00 54.64           C  
ANISOU  614  CA  ILE A 114     5857   7748   7157    303     54   -354       C  
ATOM    615  C   ILE A 114      26.963  58.508  53.305  1.00 61.07           C  
ANISOU  615  C   ILE A 114     6742   8565   7896    273     52   -304       C  
ATOM    616  O   ILE A 114      26.583  57.965  52.260  1.00 69.19           O  
ANISOU  616  O   ILE A 114     7768   9581   8940    280     79   -279       O  
ATOM    617  CB  ILE A 114      29.434  59.084  53.165  1.00 45.75           C  
ANISOU  617  CB  ILE A 114     4713   6578   6091    346    -16   -371       C  
ATOM    618  CG1 ILE A 114      30.435  60.231  53.251  1.00 61.56           C  
ANISOU  618  CG1 ILE A 114     6642   8575   8171    372    -12   -428       C  
ATOM    619  CG2 ILE A 114      29.632  58.388  51.868  1.00 51.72           C  
ANISOU  619  CG2 ILE A 114     5452   7301   6896    368      5   -355       C  
ATOM    620  CD1 ILE A 114      30.305  61.198  52.135  1.00 63.27           C  
ANISOU  620  CD1 ILE A 114     6798   8797   8446    379     79   -448       C  
ATOM    621  N   CYS A 115      26.491  58.135  54.506  1.00 51.24           N  
ANISOU  621  N   CYS A 115     5568   7333   6568    237     22   -292       N  
ATOM    622  CA  CYS A 115      25.463  57.096  54.606  1.00 55.39           C  
ANISOU  622  CA  CYS A 115     6163   7858   7024    204     31   -251       C  
ATOM    623  C   CYS A 115      24.198  57.536  53.886  1.00 55.56           C  
ANISOU  623  C   CYS A 115     6156   7901   7055    180    118   -247       C  
ATOM    624  O   CYS A 115      23.650  56.792  53.063  1.00 57.55           O  
ANISOU  624  O   CYS A 115     6416   8141   7309    182    134   -218       O  
ATOM    625  CB  CYS A 115      25.163  56.751  56.076  1.00 50.56           C  
ANISOU  625  CB  CYS A 115     5642   7251   6316    160     -2   -245       C  
ATOM    626  SG  CYS A 115      23.636  55.754  56.438  1.00 66.30           S  
ANISOU  626  SG  CYS A 115     7727   9247   8217     99     41   -209       S  
ATOM    627  N   ARG A 116      23.737  58.759  54.180  1.00 52.70           N  
ANISOU  627  N   ARG A 116     5755   7565   6704    159    168   -279       N  
ATOM    628  CA  ARG A 116      22.592  59.342  53.501  1.00 46.59           C  
ANISOU  628  CA  ARG A 116     4942   6804   5958    141    241   -284       C  
ATOM    629  C   ARG A 116      22.810  59.412  51.994  1.00 50.90           C  
ANISOU  629  C   ARG A 116     5438   7331   6569    181    252   -273       C  
ATOM    630  O   ARG A 116      21.883  59.154  51.216  1.00 54.92           O  
ANISOU  630  O   ARG A 116     5947   7833   7087    173    282   -255       O  
ATOM    631  CB  ARG A 116      22.323  60.733  54.075  1.00 51.87           C  
ANISOU  631  CB  ARG A 116     5568   7498   6643    118    284   -326       C  
ATOM    632  CG  ARG A 116      21.029  61.347  53.565  1.00 65.59           C  
ANISOU  632  CG  ARG A 116     7265   9242   8413     94    351   -336       C  
ATOM    633  CD  ARG A 116      20.838  62.791  54.008  1.00 75.59           C  
ANISOU  633  CD  ARG A 116     8476  10531   9714     76    395   -380       C  
ATOM    634  NE  ARG A 116      20.892  62.953  55.462  1.00 81.43           N  
ANISOU  634  NE  ARG A 116     9255  11288  10396     34    397   -403       N  
ATOM    635  CZ  ARG A 116      19.937  62.569  56.308  1.00 75.11           C  
ANISOU  635  CZ  ARG A 116     8507  10490   9543    -24    428   -409       C  
ATOM    636  NH1 ARG A 116      18.827  61.983  55.864  1.00 64.16           N  
ANISOU  636  NH1 ARG A 116     7128   9088   8161    -45    460   -396       N  
ATOM    637  NH2 ARG A 116      20.102  62.770  57.610  1.00 82.57           N  
ANISOU  637  NH2 ARG A 116     9499  11446  10429    -64    430   -432       N  
ATOM    638  N   VAL A 117      24.022  59.768  51.556  1.00 49.72           N  
ANISOU  638  N   VAL A 117     5253   7169   6470    222    232   -288       N  
ATOM    639  CA  VAL A 117      24.259  59.885  50.120  1.00 51.26           C  
ANISOU  639  CA  VAL A 117     5415   7340   6722    252    254   -282       C  
ATOM    640  C   VAL A 117      24.147  58.522  49.456  1.00 52.57           C  
ANISOU  640  C   VAL A 117     5622   7480   6870    260    232   -243       C  
ATOM    641  O   VAL A 117      23.413  58.354  48.471  1.00 64.14           O  
ANISOU  641  O   VAL A 117     7092   8936   8344    257    259   -223       O  
ATOM    642  CB  VAL A 117      25.617  60.551  49.830  1.00 47.43           C  
ANISOU  642  CB  VAL A 117     4882   6838   6299    288    249   -315       C  
ATOM    643  CG1 VAL A 117      26.058  60.233  48.417  1.00 41.34           C  
ANISOU  643  CG1 VAL A 117     4104   6029   5573    314    266   -306       C  
ATOM    644  CG2 VAL A 117      25.503  62.042  49.979  1.00 45.92           C  
ANISOU  644  CG2 VAL A 117     4641   6668   6139    283    292   -350       C  
ATOM    645  N   VAL A 118      24.834  57.520  50.011  1.00 42.86           N  
ANISOU  645  N   VAL A 118     4428   6239   5618    268    177   -231       N  
ATOM    646  CA  VAL A 118      24.868  56.200  49.380  1.00 47.93           C  
ANISOU  646  CA  VAL A 118     5104   6854   6252    278    155   -196       C  
ATOM    647  C   VAL A 118      23.471  55.578  49.347  1.00 48.11           C  
ANISOU  647  C   VAL A 118     5169   6889   6223    246    176   -165       C  
ATOM    648  O   VAL A 118      23.051  55.025  48.323  1.00 49.51           O  
ANISOU  648  O   VAL A 118     5352   7049   6409    250    191   -142       O  
ATOM    649  CB  VAL A 118      25.890  55.291  50.096  1.00 44.73           C  
ANISOU  649  CB  VAL A 118     4727   6429   5839    294     83   -193       C  
ATOM    650  CG1 VAL A 118      25.681  53.821  49.736  1.00 41.09           C  
ANISOU  650  CG1 VAL A 118     4312   5946   5353    294     58   -153       C  
ATOM    651  CG2 VAL A 118      27.322  55.735  49.798  1.00 38.19           C  
ANISOU  651  CG2 VAL A 118     3846   5574   5090    332     65   -230       C  
ATOM    652  N   MET A 119      22.728  55.667  50.459  1.00 50.18           N  
ANISOU  652  N   MET A 119     5460   7175   6431    209    180   -168       N  
ATOM    653  CA  MET A 119      21.350  55.179  50.497  1.00 39.72           C  
ANISOU  653  CA  MET A 119     4166   5857   5069    173    211   -150       C  
ATOM    654  C   MET A 119      20.457  55.913  49.500  1.00 43.82           C  
ANISOU  654  C   MET A 119     4639   6377   5634    171    260   -159       C  
ATOM    655  O   MET A 119      19.553  55.312  48.918  1.00 54.25           O  
ANISOU  655  O   MET A 119     5974   7686   6952    161    274   -140       O  
ATOM    656  CB  MET A 119      20.771  55.318  51.907  1.00 40.82           C  
ANISOU  656  CB  MET A 119     4344   6015   5150    127    222   -164       C  
ATOM    657  CG  MET A 119      21.253  54.299  52.951  1.00 53.52           C  
ANISOU  657  CG  MET A 119     6033   7614   6689    115    170   -145       C  
ATOM    658  SD  MET A 119      21.291  52.566  52.388  1.00 71.50           S  
ANISOU  658  SD  MET A 119     8361   9862   8945    130    133    -97       S  
ATOM    659  CE  MET A 119      21.221  51.632  53.932  1.00 75.85           C  
ANISOU  659  CE  MET A 119     9024  10402   9394     89     95    -80       C  
ATOM    660  N   THR A 120      20.699  57.192  49.267  1.00 50.20           N  
ANISOU  660  N   THR A 120     5395   7193   6487    182    281   -187       N  
ATOM    661  CA  THR A 120      19.867  57.906  48.308  1.00 57.46           C  
ANISOU  661  CA  THR A 120     6277   8104   7450    182    315   -193       C  
ATOM    662  C   THR A 120      20.211  57.551  46.863  1.00 37.81           C  
ANISOU  662  C   THR A 120     3794   5585   4989    213    306   -171       C  
ATOM    663  O   THR A 120      19.313  57.337  46.055  1.00 40.62           O  
ANISOU  663  O   THR A 120     4156   5923   5355    208    313   -156       O  
ATOM    664  CB  THR A 120      19.982  59.417  48.539  1.00 60.30           C  
ANISOU  664  CB  THR A 120     6585   8479   7849    182    341   -230       C  
ATOM    665  OG1 THR A 120      19.326  59.742  49.764  1.00 62.87           O  
ANISOU  665  OG1 THR A 120     6908   8828   8150    142    362   -253       O  
ATOM    666  CG2 THR A 120      19.316  60.194  47.420  1.00 48.92           C  
ANISOU  666  CG2 THR A 120     5110   7018   6458    189    362   -234       C  
ATOM    667  N   VAL A 121      21.493  57.520  46.509  1.00 41.44           N  
ANISOU  667  N   VAL A 121     4250   6030   5465    243    292   -172       N  
ATOM    668  CA  VAL A 121      21.881  57.121  45.157  1.00 48.11           C  
ANISOU  668  CA  VAL A 121     5109   6840   6333    264    294   -156       C  
ATOM    669  C   VAL A 121      21.464  55.679  44.883  1.00 55.25           C  
ANISOU  669  C   VAL A 121     6057   7732   7205    258    274   -120       C  
ATOM    670  O   VAL A 121      20.888  55.364  43.827  1.00 55.45           O  
ANISOU  670  O   VAL A 121     6101   7735   7233    258    281   -102       O  
ATOM    671  CB  VAL A 121      23.397  57.331  44.976  1.00 45.80           C  
ANISOU  671  CB  VAL A 121     4798   6528   6074    291    293   -176       C  
ATOM    672  CG1 VAL A 121      23.870  56.850  43.614  1.00 32.47           C  
ANISOU  672  CG1 VAL A 121     3132   4798   4409    305    307   -165       C  
ATOM    673  CG2 VAL A 121      23.736  58.811  45.183  1.00 40.59           C  
ANISOU  673  CG2 VAL A 121     4093   5880   5450    296    319   -213       C  
ATOM    674  N   ASP A 122      21.743  54.786  45.832  1.00 51.12           N  
ANISOU  674  N   ASP A 122     5556   7220   6647    253    245   -111       N  
ATOM    675  CA  ASP A 122      21.315  53.404  45.719  1.00 41.21           C  
ANISOU  675  CA  ASP A 122     4343   5956   5360    246    228    -78       C  
ATOM    676  C   ASP A 122      19.829  53.298  45.397  1.00 46.07           C  
ANISOU  676  C   ASP A 122     4967   6574   5962    222    248    -68       C  
ATOM    677  O   ASP A 122      19.427  52.483  44.558  1.00 54.23           O  
ANISOU  677  O   ASP A 122     6023   7587   6993    224    245    -44       O  
ATOM    678  CB  ASP A 122      21.637  52.677  47.025  1.00 44.65           C  
ANISOU  678  CB  ASP A 122     4809   6404   5752    236    193    -72       C  
ATOM    679  CG  ASP A 122      21.299  51.186  46.969  1.00 61.49           C  
ANISOU  679  CG  ASP A 122     6990   8523   7850    229    173    -37       C  
ATOM    680  OD1 ASP A 122      22.173  50.388  46.534  1.00 72.07           O  
ANISOU  680  OD1 ASP A 122     8339   9838   9207    251    146    -24       O  
ATOM    681  OD2 ASP A 122      20.165  50.814  47.361  1.00 62.32           O  
ANISOU  681  OD2 ASP A 122     7121   8638   7918    199    189    -28       O  
ATOM    682  N   GLY A 123      18.995  54.110  46.061  1.00 45.98           N  
ANISOU  682  N   GLY A 123     4936   6584   5952    198    269    -89       N  
ATOM    683  CA  GLY A 123      17.553  54.004  45.874  1.00 36.89           C  
ANISOU  683  CA  GLY A 123     3783   5429   4804    174    287    -90       C  
ATOM    684  C   GLY A 123      17.106  54.468  44.497  1.00 52.60           C  
ANISOU  684  C   GLY A 123     5757   7392   6838    189    287    -87       C  
ATOM    685  O   GLY A 123      16.330  53.779  43.813  1.00 49.90           O  
ANISOU  685  O   GLY A 123     5432   7030   6498    186    280    -71       O  
ATOM    686  N   ILE A 124      17.589  55.644  44.077  1.00 45.74           N  
ANISOU  686  N   ILE A 124     4859   6518   6001    205    294   -103       N  
ATOM    687  CA  ILE A 124      17.241  56.174  42.763  1.00 49.94           C  
ANISOU  687  CA  ILE A 124     5391   7018   6566    217    289    -99       C  
ATOM    688  C   ILE A 124      17.559  55.163  41.679  1.00 50.66           C  
ANISOU  688  C   ILE A 124     5529   7080   6640    230    274    -68       C  
ATOM    689  O   ILE A 124      16.792  54.990  40.727  1.00 50.44           O  
ANISOU  689  O   ILE A 124     5521   7022   6621    230    258    -56       O  
ATOM    690  CB  ILE A 124      17.971  57.497  42.490  1.00 59.58           C  
ANISOU  690  CB  ILE A 124     6589   8235   7816    232    302   -119       C  
ATOM    691  CG1 ILE A 124      17.843  58.456  43.668  1.00 70.06           C  
ANISOU  691  CG1 ILE A 124     7867   9594   9157    218    321   -152       C  
ATOM    692  CG2 ILE A 124      17.429  58.129  41.223  1.00 60.18           C  
ANISOU  692  CG2 ILE A 124     6676   8269   7919    239    292   -114       C  
ATOM    693  CD1 ILE A 124      18.495  59.831  43.415  1.00 61.35           C  
ANISOU  693  CD1 ILE A 124     6735   8487   8088    233    337   -174       C  
ATOM    694  N   ASN A 125      18.707  54.500  41.788  1.00 50.65           N  
ANISOU  694  N   ASN A 125     5546   7081   6620    242    274    -58       N  
ATOM    695  CA  ASN A 125      19.093  53.555  40.751  1.00 41.85           C  
ANISOU  695  CA  ASN A 125     4472   5934   5494    252    268    -34       C  
ATOM    696  C   ASN A 125      18.243  52.296  40.815  1.00 46.86           C  
ANISOU  696  C   ASN A 125     5130   6570   6104    240    252    -10       C  
ATOM    697  O   ASN A 125      17.830  51.786  39.772  1.00 46.28           O  
ANISOU  697  O   ASN A 125     5088   6468   6028    240    244      8       O  
ATOM    698  CB  ASN A 125      20.583  53.252  40.865  1.00 46.02           C  
ANISOU  698  CB  ASN A 125     5001   6457   6029    267    276    -39       C  
ATOM    699  CG  ASN A 125      21.422  54.420  40.396  1.00 51.13           C  
ANISOU  699  CG  ASN A 125     5632   7086   6708    278    302    -65       C  
ATOM    700  OD1 ASN A 125      21.349  54.818  39.232  1.00 48.95           O  
ANISOU  700  OD1 ASN A 125     5384   6776   6440    278    318    -63       O  
ATOM    701  ND2 ASN A 125      22.167  55.021  41.311  1.00 56.40           N  
ANISOU  701  ND2 ASN A 125     6261   7776   7393    286    306    -91       N  
ATOM    702  N   GLN A 126      17.916  51.820  42.031  1.00 39.71           N  
ANISOU  702  N   GLN A 126     4215   5694   5178    226    249    -12       N  
ATOM    703  CA  GLN A 126      16.996  50.697  42.171  1.00 46.10           C  
ANISOU  703  CA  GLN A 126     5046   6503   5965    210    242      6       C  
ATOM    704  C   GLN A 126      15.672  50.940  41.439  1.00 46.72           C  
ANISOU  704  C   GLN A 126     5118   6563   6070    201    239      1       C  
ATOM    705  O   GLN A 126      15.176  50.064  40.722  1.00 61.46           O  
ANISOU  705  O   GLN A 126     7011   8410   7933    201    228     19       O  
ATOM    706  CB  GLN A 126      16.732  50.408  43.644  1.00 49.31           C  
ANISOU  706  CB  GLN A 126     5452   6939   6343    188    249     -3       C  
ATOM    707  CG  GLN A 126      15.637  49.368  43.855  1.00 50.33           C  
ANISOU  707  CG  GLN A 126     5604   7065   6456    165    255      7       C  
ATOM    708  CD  GLN A 126      15.579  48.814  45.271  1.00 49.13           C  
ANISOU  708  CD  GLN A 126     5478   6931   6258    139    265      5       C  
ATOM    709  OE1 GLN A 126      16.463  49.078  46.092  1.00 48.83           O  
ANISOU  709  OE1 GLN A 126     5448   6909   6197    141    255      2       O  
ATOM    710  NE2 GLN A 126      14.527  48.031  45.559  1.00 46.51           N  
ANISOU  710  NE2 GLN A 126     5165   6593   5914    112    284      5       N  
ATOM    711  N   PHE A 127      15.085  52.116  41.607  1.00 39.83           N  
ANISOU  711  N   PHE A 127     4210   5693   5230    194    245    -26       N  
ATOM    712  CA  PHE A 127      13.761  52.346  41.057  1.00 38.50           C  
ANISOU  712  CA  PHE A 127     4028   5501   5101    186    232    -38       C  
ATOM    713  C   PHE A 127      13.782  52.777  39.600  1.00 44.11           C  
ANISOU  713  C   PHE A 127     4760   6171   5828    205    202    -26       C  
ATOM    714  O   PHE A 127      12.833  52.464  38.863  1.00 44.60           O  
ANISOU  714  O   PHE A 127     4833   6201   5910    204    174    -23       O  
ATOM    715  CB  PHE A 127      13.014  53.373  41.912  1.00 45.24           C  
ANISOU  715  CB  PHE A 127     4829   6367   5994    167    249    -77       C  
ATOM    716  CG  PHE A 127      12.581  52.824  43.218  1.00 41.87           C  
ANISOU  716  CG  PHE A 127     4396   5965   5550    137    281    -92       C  
ATOM    717  CD1 PHE A 127      11.479  51.987  43.300  1.00 40.88           C  
ANISOU  717  CD1 PHE A 127     4272   5825   5437    116    288   -100       C  
ATOM    718  CD2 PHE A 127      13.309  53.075  44.361  1.00 48.60           C  
ANISOU  718  CD2 PHE A 127     5247   6850   6367    126    305   -100       C  
ATOM    719  CE1 PHE A 127      11.091  51.436  44.512  1.00 46.36           C  
ANISOU  719  CE1 PHE A 127     4973   6535   6107     81    328   -116       C  
ATOM    720  CE2 PHE A 127      12.924  52.529  45.586  1.00 43.84           C  
ANISOU  720  CE2 PHE A 127     4659   6264   5735     91    336   -113       C  
ATOM    721  CZ  PHE A 127      11.824  51.702  45.661  1.00 43.12           C  
ANISOU  721  CZ  PHE A 127     4576   6156   5652     67    352   -120       C  
ATOM    722  N   THR A 128      14.846  53.468  39.163  1.00 50.20           N  
ANISOU  722  N   THR A 128     5545   6936   6592    220    208    -22       N  
ATOM    723  CA  THR A 128      15.040  53.732  37.731  1.00 47.73           C  
ANISOU  723  CA  THR A 128     5279   6579   6279    232    189     -7       C  
ATOM    724  C   THR A 128      15.302  52.448  36.947  1.00 48.59           C  
ANISOU  724  C   THR A 128     5441   6668   6354    233    183     22       C  
ATOM    725  O   THR A 128      14.815  52.299  35.819  1.00 45.35           O  
ANISOU  725  O   THR A 128     5074   6216   5941    234    155     35       O  
ATOM    726  CB  THR A 128      16.172  54.731  37.533  1.00 41.22           C  
ANISOU  726  CB  THR A 128     4458   5750   5454    242    212    -16       C  
ATOM    727  OG1 THR A 128      15.852  55.932  38.225  1.00 49.00           O  
ANISOU  727  OG1 THR A 128     5393   6753   6473    241    217    -43       O  
ATOM    728  CG2 THR A 128      16.415  55.046  36.079  1.00 47.22           C  
ANISOU  728  CG2 THR A 128     5282   6456   6204    247    202     -3       C  
ATOM    729  N   SER A 129      16.035  51.501  37.546  1.00 50.92           N  
ANISOU  729  N   SER A 129     5735   6988   6624    233    205     31       N  
ATOM    730  CA  SER A 129      16.231  50.177  36.956  1.00 47.76           C  
ANISOU  730  CA  SER A 129     5375   6572   6199    232    203     56       C  
ATOM    731  C   SER A 129      14.904  49.517  36.581  1.00 47.59           C  
ANISOU  731  C   SER A 129     5364   6537   6181    224    174     65       C  
ATOM    732  O   SER A 129      14.674  49.176  35.414  1.00 50.30           O  
ANISOU  732  O   SER A 129     5754   6842   6516    224    155     79       O  
ATOM    733  CB  SER A 129      17.023  49.282  37.918  1.00 52.55           C  
ANISOU  733  CB  SER A 129     5968   7209   6789    234    220     62       C  
ATOM    734  OG  SER A 129      16.817  47.896  37.638  1.00 82.37           O  
ANISOU  734  OG  SER A 129     9772  10978  10548    229    213     84       O  
ATOM    735  N   ILE A 130      14.001  49.339  37.547  1.00 45.19           N  
ANISOU  735  N   ILE A 130     5021   6257   5891    214    173     52       N  
ATOM    736  CA  ILE A 130      12.772  48.619  37.196  1.00 40.60           C  
ANISOU  736  CA  ILE A 130     4444   5657   5324    206    150     53       C  
ATOM    737  C   ILE A 130      11.789  49.481  36.371  1.00 42.70           C  
ANISOU  737  C   ILE A 130     4707   5884   5633    209    108     38       C  
ATOM    738  O   ILE A 130      11.102  48.964  35.483  1.00 48.66           O  
ANISOU  738  O   ILE A 130     5488   6604   6395    210     73     46       O  
ATOM    739  CB  ILE A 130      12.126  48.052  38.467  1.00 50.60           C  
ANISOU  739  CB  ILE A 130     5676   6953   6595    188    172     38       C  
ATOM    740  CG1 ILE A 130      11.065  47.002  38.092  1.00 60.23           C  
ANISOU  740  CG1 ILE A 130     6903   8153   7828    180    159     40       C  
ATOM    741  CG2 ILE A 130      11.544  49.182  39.312  1.00 52.35           C  
ANISOU  741  CG2 ILE A 130     5847   7188   6856    176    183      2       C  
ATOM    742  CD1 ILE A 130      11.516  46.025  36.976  1.00 56.01           C  
ANISOU  742  CD1 ILE A 130     6421   7597   7263    191    143     74       C  
ATOM    743  N   PHE A 131      11.722  50.794  36.607  1.00 40.09           N  
ANISOU  743  N   PHE A 131     4346   5554   5333    212    104     16       N  
ATOM    744  CA  PHE A 131      10.842  51.631  35.794  1.00 41.52           C  
ANISOU  744  CA  PHE A 131     4528   5689   5559    217     52      3       C  
ATOM    745  C   PHE A 131      11.288  51.644  34.329  1.00 47.64           C  
ANISOU  745  C   PHE A 131     5382   6418   6300    227     20     31       C  
ATOM    746  O   PHE A 131      10.456  51.740  33.408  1.00 43.87           O  
ANISOU  746  O   PHE A 131     4934   5892   5844    230    -39     32       O  
ATOM    747  CB  PHE A 131      10.805  53.047  36.358  1.00 45.96           C  
ANISOU  747  CB  PHE A 131     5042   6259   6160    217     58    -25       C  
ATOM    748  CG  PHE A 131      10.188  53.150  37.734  1.00 50.38           C  
ANISOU  748  CG  PHE A 131     5530   6854   6758    200     91    -60       C  
ATOM    749  CD1 PHE A 131       9.429  52.122  38.256  1.00 38.38           C  
ANISOU  749  CD1 PHE A 131     3992   5342   5249    184    104    -70       C  
ATOM    750  CD2 PHE A 131      10.372  54.301  38.510  1.00 58.11           C  
ANISOU  750  CD2 PHE A 131     6463   7854   7763    195    115    -86       C  
ATOM    751  CE1 PHE A 131       8.879  52.230  39.515  1.00 39.97           C  
ANISOU  751  CE1 PHE A 131     4140   5568   5480    159    146   -106       C  
ATOM    752  CE2 PHE A 131       9.811  54.414  39.777  1.00 50.21           C  
ANISOU  752  CE2 PHE A 131     5404   6880   6793    171    153   -121       C  
ATOM    753  CZ  PHE A 131       9.073  53.376  40.280  1.00 37.68           C  
ANISOU  753  CZ  PHE A 131     3809   5297   5211    151    171   -132       C  
ATOM    754  N   CYS A 132      12.603  51.554  34.100  1.00 47.73           N  
ANISOU  754  N   CYS A 132     5433   6439   6262    229     58     50       N  
ATOM    755  CA  CYS A 132      13.117  51.407  32.739  1.00 52.21           C  
ANISOU  755  CA  CYS A 132     6088   6960   6790    228     46     73       C  
ATOM    756  C   CYS A 132      12.619  50.136  32.104  1.00 54.31           C  
ANISOU  756  C   CYS A 132     6392   7207   7038    223     23     91       C  
ATOM    757  O   CYS A 132      12.188  50.132  30.947  1.00 49.17           O  
ANISOU  757  O   CYS A 132     5806   6503   6375    221    -22    102       O  
ATOM    758  CB  CYS A 132      14.639  51.391  32.735  1.00 52.73           C  
ANISOU  758  CB  CYS A 132     6177   7038   6822    227    105     80       C  
ATOM    759  SG  CYS A 132      15.309  52.977  32.321  1.00 73.97           S  
ANISOU  759  SG  CYS A 132     8892   9701   9514    229    118     67       S  
ATOM    760  N   LEU A 133      12.755  49.028  32.830  1.00 54.82           N  
ANISOU  760  N   LEU A 133     6423   7310   7095    220     55     95       N  
ATOM    761  CA  LEU A 133      12.260  47.756  32.353  1.00 47.56           C  
ANISOU  761  CA  LEU A 133     5530   6378   6164    215     40    110       C  
ATOM    762  C   LEU A 133      10.781  47.854  32.017  1.00 50.06           C  
ANISOU  762  C   LEU A 133     5835   6663   6521    217    -23     96       C  
ATOM    763  O   LEU A 133      10.336  47.403  30.955  1.00 48.32           O  
ANISOU  763  O   LEU A 133     5669   6400   6291    215    -65    108       O  
ATOM    764  CB  LEU A 133      12.523  46.708  33.421  1.00 54.10           C  
ANISOU  764  CB  LEU A 133     6316   7254   6986    212     81    113       C  
ATOM    765  CG  LEU A 133      12.288  45.282  33.010  1.00 53.77           C  
ANISOU  765  CG  LEU A 133     6300   7204   6926    206     80    131       C  
ATOM    766  CD1 LEU A 133      12.885  45.101  31.638  1.00 41.53           C  
ANISOU  766  CD1 LEU A 133     4826   5611   5341    202     75    149       C  
ATOM    767  CD2 LEU A 133      13.004  44.427  34.038  1.00 46.48           C  
ANISOU  767  CD2 LEU A 133     5350   6322   5987    204    124    138       C  
ATOM    768  N   THR A 134      10.016  48.504  32.887  1.00 47.19           N  
ANISOU  768  N   THR A 134     5403   6316   6213    219    -32     67       N  
ATOM    769  CA  THR A 134       8.595  48.674  32.628  1.00 47.37           C  
ANISOU  769  CA  THR A 134     5400   6302   6298    221    -93     43       C  
ATOM    770  C   THR A 134       8.363  49.424  31.325  1.00 46.10           C  
ANISOU  770  C   THR A 134     5302   6077   6138    230   -166     51       C  
ATOM    771  O   THR A 134       7.668  48.936  30.428  1.00 54.37           O  
ANISOU  771  O   THR A 134     6388   7078   7191    232   -225     55       O  
ATOM    772  CB  THR A 134       7.948  49.397  33.807  1.00 46.23           C  
ANISOU  772  CB  THR A 134     5167   6179   6219    216    -78      3       C  
ATOM    773  OG1 THR A 134       8.194  48.647  35.007  1.00 53.15           O  
ANISOU  773  OG1 THR A 134     6007   7109   7080    203    -11     -1       O  
ATOM    774  CG2 THR A 134       6.467  49.549  33.582  1.00 38.46           C  
ANISOU  774  CG2 THR A 134     4142   5149   5320    218   -138    -33       C  
ATOM    775  N   VAL A 135       8.948  50.612  31.191  1.00 50.67           N  
ANISOU  775  N   VAL A 135     5899   6647   6707    234   -166     53       N  
ATOM    776  CA  VAL A 135       8.767  51.373  29.957  1.00 51.27           C  
ANISOU  776  CA  VAL A 135     6051   6655   6774    239   -236     63       C  
ATOM    777  C   VAL A 135       9.217  50.551  28.746  1.00 45.53           C  
ANISOU  777  C   VAL A 135     5431   5893   5974    230   -246     96       C  
ATOM    778  O   VAL A 135       8.560  50.543  27.702  1.00 50.26           O  
ANISOU  778  O   VAL A 135     6096   6430   6571    231   -324    103       O  
ATOM    779  CB  VAL A 135       9.505  52.720  30.048  1.00 47.00           C  
ANISOU  779  CB  VAL A 135     5519   6113   6224    241   -217     62       C  
ATOM    780  CG1 VAL A 135       9.555  53.356  28.730  1.00 48.74           C  
ANISOU  780  CG1 VAL A 135     5845   6262   6413    240   -276     80       C  
ATOM    781  CG2 VAL A 135       8.784  53.639  31.007  1.00 52.18           C  
ANISOU  781  CG2 VAL A 135     6077   6785   6963    248   -230     25       C  
ATOM    782  N   MET A 136      10.311  49.809  28.887  1.00 46.27           N  
ANISOU  782  N   MET A 136     5543   6023   6013    220   -169    114       N  
ATOM    783  CA  MET A 136      10.799  48.987  27.783  1.00 49.48           C  
ANISOU  783  CA  MET A 136     6048   6397   6356    205   -162    140       C  
ATOM    784  C   MET A 136       9.764  47.954  27.345  1.00 51.53           C  
ANISOU  784  C   MET A 136     6315   6635   6628    206   -216    142       C  
ATOM    785  O   MET A 136       9.601  47.699  26.146  1.00 50.15           O  
ANISOU  785  O   MET A 136     6236   6405   6415    196   -261    158       O  
ATOM    786  CB  MET A 136      12.092  48.296  28.208  1.00 51.67           C  
ANISOU  786  CB  MET A 136     6317   6718   6597    196    -69    149       C  
ATOM    787  CG  MET A 136      12.969  47.808  27.085  1.00 55.25           C  
ANISOU  787  CG  MET A 136     6872   7133   6988    175    -37    168       C  
ATOM    788  SD  MET A 136      14.603  47.601  27.785  1.00 70.56           S  
ANISOU  788  SD  MET A 136     8776   9115   8918    169     68    162       S  
ATOM    789  CE  MET A 136      14.410  46.136  28.765  1.00 67.17           C  
ANISOU  789  CE  MET A 136     8266   8743   8511    178     86    167       C  
ATOM    790  N   SER A 137       9.094  47.309  28.305  1.00 45.49           N  
ANISOU  790  N   SER A 137     5458   5912   5914    213   -208    125       N  
ATOM    791  CA  SER A 137       8.048  46.352  27.961  1.00 50.90           C  
ANISOU  791  CA  SER A 137     6139   6577   6625    215   -255    119       C  
ATOM    792  C   SER A 137       6.841  47.056  27.362  1.00 54.97           C  
ANISOU  792  C   SER A 137     6662   7029   7194    226   -361    100       C  
ATOM    793  O   SER A 137       6.215  46.545  26.426  1.00 64.58           O  
ANISOU  793  O   SER A 137     7932   8196   8408    226   -427    104       O  
ATOM    794  CB  SER A 137       7.630  45.540  29.191  1.00 57.44           C  
ANISOU  794  CB  SER A 137     6869   7459   7496    216   -210    101       C  
ATOM    795  OG  SER A 137       8.712  44.853  29.803  1.00 51.35           O  
ANISOU  795  OG  SER A 137     6091   6740   6679    208   -126    119       O  
ATOM    796  N   ILE A 138       6.494  48.233  27.876  1.00 47.76           N  
ANISOU  796  N   ILE A 138     5698   6113   6337    236   -384     76       N  
ATOM    797  CA  ILE A 138       5.405  48.974  27.255  1.00 47.14           C  
ANISOU  797  CA  ILE A 138     5628   5964   6320    248   -495     57       C  
ATOM    798  C   ILE A 138       5.740  49.258  25.795  1.00 48.98           C  
ANISOU  798  C   ILE A 138     6002   6129   6480    244   -558     89       C  
ATOM    799  O   ILE A 138       4.885  49.138  24.905  1.00 45.38           O  
ANISOU  799  O   ILE A 138     5595   5606   6043    249   -660     86       O  
ATOM    800  CB  ILE A 138       5.101  50.259  28.049  1.00 51.72           C  
ANISOU  800  CB  ILE A 138     6130   6550   6973    258   -503     26       C  
ATOM    801  CG1 ILE A 138       4.614  49.911  29.458  1.00 49.50           C  
ANISOU  801  CG1 ILE A 138     5721   6325   6763    255   -441    -13       C  
ATOM    802  CG2 ILE A 138       4.055  51.101  27.336  1.00 46.38           C  
ANISOU  802  CG2 ILE A 138     5466   5790   6365    273   -628      6       C  
ATOM    803  CD1 ILE A 138       4.476  51.125  30.363  1.00 46.49           C  
ANISOU  803  CD1 ILE A 138     5261   5958   6444    257   -425    -45       C  
ATOM    804  N   ASP A 139       7.008  49.578  25.519  1.00 57.44           N  
ANISOU  804  N   ASP A 139     7146   7213   7468    229   -496    118       N  
ATOM    805  CA  ASP A 139       7.433  49.808  24.142  1.00 45.87           C  
ANISOU  805  CA  ASP A 139     5829   5678   5920    214   -534    148       C  
ATOM    806  C   ASP A 139       7.298  48.547  23.298  1.00 47.96           C  
ANISOU  806  C   ASP A 139     6165   5920   6137    200   -549    164       C  
ATOM    807  O   ASP A 139       6.864  48.615  22.139  1.00 51.43           O  
ANISOU  807  O   ASP A 139     6713   6283   6544    194   -637    176       O  
ATOM    808  CB  ASP A 139       8.865  50.320  24.113  1.00 46.66           C  
ANISOU  808  CB  ASP A 139     5981   5797   5950    197   -442    165       C  
ATOM    809  CG  ASP A 139       9.291  50.768  22.722  1.00 71.50           C  
ANISOU  809  CG  ASP A 139     9292   8862   9012    174   -473    190       C  
ATOM    810  OD1 ASP A 139       8.819  51.854  22.289  1.00 81.39           O  
ANISOU  810  OD1 ASP A 139    10592  10057  10277    181   -555    189       O  
ATOM    811  OD2 ASP A 139      10.099  50.051  22.068  1.00 67.55           O  
ANISOU  811  OD2 ASP A 139     8878   8353   8436    146   -413    208       O  
ATOM    812  N   ARG A 140       7.653  47.383  23.857  1.00 46.68           N  
ANISOU  812  N   ARG A 140     5949   5819   5970    195   -469    166       N  
ATOM    813  CA  ARG A 140       7.476  46.130  23.120  1.00 49.19           C  
ANISOU  813  CA  ARG A 140     6322   6118   6251    182   -479    178       C  
ATOM    814  C   ARG A 140       6.003  45.853  22.850  1.00 50.34           C  
ANISOU  814  C   ARG A 140     6442   6223   6463    199   -590    158       C  
ATOM    815  O   ARG A 140       5.639  45.404  21.756  1.00 51.74           O  
ANISOU  815  O   ARG A 140     6713   6342   6605    190   -656    169       O  
ATOM    816  CB  ARG A 140       8.093  44.956  23.888  1.00 57.51           C  
ANISOU  816  CB  ARG A 140     7308   7244   7298    176   -375    182       C  
ATOM    817  CG  ARG A 140       9.595  45.074  24.158  1.00 57.17           C  
ANISOU  817  CG  ARG A 140     7282   7237   7204    161   -268    196       C  
ATOM    818  CD  ARG A 140      10.382  44.731  22.922  1.00 52.79           C  
ANISOU  818  CD  ARG A 140     6857   6634   6566    129   -243    216       C  
ATOM    819  NE  ARG A 140      10.535  45.905  22.085  1.00 62.73           N  
ANISOU  819  NE  ARG A 140     8220   7830   7785    118   -282    222       N  
ATOM    820  CZ  ARG A 140      10.494  45.891  20.758  1.00 63.36           C  
ANISOU  820  CZ  ARG A 140     8441   7835   7799     92   -322    237       C  
ATOM    821  NH1 ARG A 140      10.285  44.755  20.102  1.00 49.73           N  
ANISOU  821  NH1 ARG A 140     6762   6090   6041     76   -328    245       N  
ATOM    822  NH2 ARG A 140      10.662  47.027  20.091  1.00 65.16           N  
ANISOU  822  NH2 ARG A 140     8768   8002   7988     80   -354    243       N  
ATOM    823  N   TYR A 141       5.142  46.114  23.838  1.00 52.83           N  
ANISOU  823  N   TYR A 141     6631   6562   6878    222   -611    124       N  
ATOM    824  CA  TYR A 141       3.711  45.917  23.636  1.00 59.78           C  
ANISOU  824  CA  TYR A 141     7472   7396   7844    239   -715     92       C  
ATOM    825  C   TYR A 141       3.175  46.796  22.501  1.00 51.84           C  
ANISOU  825  C   TYR A 141     6563   6295   6838    246   -850     95       C  
ATOM    826  O   TYR A 141       2.391  46.330  21.666  1.00 58.31           O  
ANISOU  826  O   TYR A 141     7430   7055   7670    250   -946     90       O  
ATOM    827  CB  TYR A 141       2.961  46.183  24.944  1.00 50.14           C  
ANISOU  827  CB  TYR A 141     6100   6212   6738    255   -697     46       C  
ATOM    828  CG  TYR A 141       1.509  46.461  24.716  1.00 46.81           C  
ANISOU  828  CG  TYR A 141     5631   5724   6430    274   -815      2       C  
ATOM    829  CD1 TYR A 141       0.613  45.424  24.520  1.00 48.53           C  
ANISOU  829  CD1 TYR A 141     5819   5922   6698    278   -851    -22       C  
ATOM    830  CD2 TYR A 141       1.032  47.762  24.674  1.00 48.28           C  
ANISOU  830  CD2 TYR A 141     5801   5862   6681    288   -895    -19       C  
ATOM    831  CE1 TYR A 141      -0.725  45.669  24.295  1.00 47.74           C  
ANISOU  831  CE1 TYR A 141     5668   5753   6717    297   -965    -71       C  
ATOM    832  CE2 TYR A 141      -0.307  48.023  24.448  1.00 51.13           C  
ANISOU  832  CE2 TYR A 141     6113   6152   7163    308  -1014    -66       C  
ATOM    833  CZ  TYR A 141      -1.182  46.969  24.258  1.00 51.42           C  
ANISOU  833  CZ  TYR A 141     6116   6167   7255    312  -1049    -94       C  
ATOM    834  OH  TYR A 141      -2.521  47.224  24.035  1.00 63.29           O  
ANISOU  834  OH  TYR A 141     7561   7593   8895    333  -1170   -149       O  
ATOM    835  N   LEU A 142       3.584  48.067  22.459  1.00 47.02           N  
ANISOU  835  N   LEU A 142     5986   5666   6214    247   -863    104       N  
ATOM    836  CA  LEU A 142       3.124  48.968  21.406  1.00 50.90           C  
ANISOU  836  CA  LEU A 142     6580   6060   6698    253   -996    110       C  
ATOM    837  C   LEU A 142       3.578  48.503  20.035  1.00 56.43           C  
ANISOU  837  C   LEU A 142     7456   6706   7280    227  -1024    150       C  
ATOM    838  O   LEU A 142       2.801  48.547  19.077  1.00 59.61           O  
ANISOU  838  O   LEU A 142     7941   7024   7686    232  -1156    150       O  
ATOM    839  CB  LEU A 142       3.625  50.389  21.654  1.00 48.88           C  
ANISOU  839  CB  LEU A 142     6333   5800   6439    255   -986    115       C  
ATOM    840  CG  LEU A 142       2.948  51.122  22.798  1.00 48.89           C  
ANISOU  840  CG  LEU A 142     6180   5827   6569    279   -994     71       C  
ATOM    841  CD1 LEU A 142       3.576  52.490  23.035  1.00 50.61           C  
ANISOU  841  CD1 LEU A 142     6410   6045   6774    279   -972     79       C  
ATOM    842  CD2 LEU A 142       1.478  51.237  22.516  1.00 49.30           C  
ANISOU  842  CD2 LEU A 142     6190   5804   6736    303  -1138     33       C  
ATOM    843  N   ALA A 143       4.840  48.068  19.925  1.00 59.55           N  
ANISOU  843  N   ALA A 143     7912   7143   7573    198   -903    180       N  
ATOM    844  CA  ALA A 143       5.400  47.611  18.651  1.00 55.33           C  
ANISOU  844  CA  ALA A 143     7548   6557   6919    164   -904    213       C  
ATOM    845  C   ALA A 143       4.659  46.393  18.088  1.00 56.55           C  
ANISOU  845  C   ALA A 143     7721   6688   7077    162   -960    209       C  
ATOM    846  O   ALA A 143       4.430  46.306  16.874  1.00 57.69           O  
ANISOU  846  O   ALA A 143     8011   6752   7158    145  -1045    225       O  
ATOM    847  CB  ALA A 143       6.889  47.285  18.840  1.00 50.67           C  
ANISOU  847  CB  ALA A 143     6982   6022   6249    133   -745    232       C  
ATOM    848  N   VAL A 144       4.305  45.427  18.942  1.00 51.22           N  
ANISOU  848  N   VAL A 144     6911   6080   6471    177   -912    188       N  
ATOM    849  CA  VAL A 144       3.697  44.203  18.434  1.00 49.43           C  
ANISOU  849  CA  VAL A 144     6698   5837   6246    174   -949    183       C  
ATOM    850  C   VAL A 144       2.224  44.429  18.137  1.00 52.63           C  
ANISOU  850  C   VAL A 144     7078   6174   6743    204  -1108    152       C  
ATOM    851  O   VAL A 144       1.724  44.017  17.084  1.00 60.75           O  
ANISOU  851  O   VAL A 144     8206   7133   7741    197  -1204    157       O  
ATOM    852  CB  VAL A 144       3.891  43.029  19.422  1.00 50.25           C  
ANISOU  852  CB  VAL A 144     6676   6032   6384    177   -835    172       C  
ATOM    853  CG1 VAL A 144       3.097  41.842  18.986  1.00 48.01           C  
ANISOU  853  CG1 VAL A 144     6389   5729   6122    179   -880    160       C  
ATOM    854  CG2 VAL A 144       5.341  42.647  19.560  1.00 48.54           C  
ANISOU  854  CG2 VAL A 144     6493   5868   6082    148   -694    200       C  
ATOM    855  N   VAL A 145       1.505  45.089  19.050  1.00 61.60           N  
ANISOU  855  N   VAL A 145     8083   7324   8000    235  -1141    115       N  
ATOM    856  CA  VAL A 145       0.045  45.017  19.048  1.00 60.17           C  
ANISOU  856  CA  VAL A 145     7826   7091   7944    264  -1267     69       C  
ATOM    857  C   VAL A 145      -0.537  46.253  18.371  1.00 54.56           C  
ANISOU  857  C   VAL A 145     7184   6283   7265    280  -1423     64       C  
ATOM    858  O   VAL A 145      -1.599  46.181  17.755  1.00 56.49           O  
ANISOU  858  O   VAL A 145     7443   6447   7573    298  -1568     39       O  
ATOM    859  CB  VAL A 145      -0.517  44.834  20.480  1.00 62.76           C  
ANISOU  859  CB  VAL A 145     7960   7485   8403    284  -1202     20       C  
ATOM    860  CG1 VAL A 145      -2.047  44.768  20.477  1.00 52.16           C  
ANISOU  860  CG1 VAL A 145     6530   6079   7208    311  -1324    -40       C  
ATOM    861  CG2 VAL A 145       0.065  43.577  21.155  1.00 63.86           C  
ANISOU  861  CG2 VAL A 145     8045   7714   8504    267  -1055     29       C  
ATOM    862  N   HIS A 146       0.160  47.391  18.441  1.00 62.10           N  
ANISOU  862  N   HIS A 146     8185   7237   8175    274  -1401     87       N  
ATOM    863  CA  HIS A 146      -0.319  48.637  17.820  1.00 58.32           C  
ANISOU  863  CA  HIS A 146     7777   6661   7719    288  -1548     86       C  
ATOM    864  C   HIS A 146       0.778  49.307  16.999  1.00 65.41           C  
ANISOU  864  C   HIS A 146     8857   7528   8467    257  -1527    140       C  
ATOM    865  O   HIS A 146       1.073  50.493  17.187  1.00 72.53           O  
ANISOU  865  O   HIS A 146     9769   8416   9372    261  -1533    146       O  
ATOM    866  CB  HIS A 146      -0.850  49.605  18.879  1.00 61.01           C  
ANISOU  866  CB  HIS A 146     7965   7018   8200    316  -1558     43       C  
ATOM    867  CG  HIS A 146      -1.857  49.009  19.820  1.00 72.40           C  
ANISOU  867  CG  HIS A 146     9223   8492   9794    338  -1549    -19       C  
ATOM    868  ND1 HIS A 146      -3.151  48.716  19.443  1.00 73.07           N  
ANISOU  868  ND1 HIS A 146     9270   8502   9993    361  -1687    -64       N  
ATOM    869  CD2 HIS A 146      -1.764  48.672  21.129  1.00 68.60           C  
ANISOU  869  CD2 HIS A 146     8590   8103   9372    337  -1417    -48       C  
ATOM    870  CE1 HIS A 146      -3.808  48.214  20.474  1.00 67.45           C  
ANISOU  870  CE1 HIS A 146     8387   7834   9407    371  -1629   -120       C  
ATOM    871  NE2 HIS A 146      -2.992  48.183  21.512  1.00 72.99           N  
ANISOU  871  NE2 HIS A 146     9024   8637  10073    355  -1465   -110       N  
ATOM    872  N   PRO A 147       1.405  48.597  16.058  1.00 67.88           N  
ANISOU  872  N   PRO A 147     9320   7823   8648    222  -1498    177       N  
ATOM    873  CA  PRO A 147       2.551  49.205  15.368  1.00 68.42           C  
ANISOU  873  CA  PRO A 147     9556   7864   8574    184  -1446    221       C  
ATOM    874  C   PRO A 147       2.182  50.417  14.523  1.00 76.36           C  
ANISOU  874  C   PRO A 147    10698   8757   9558    187  -1595    234       C  
ATOM    875  O   PRO A 147       2.895  51.428  14.567  1.00 84.24           O  
ANISOU  875  O   PRO A 147    11749   9750  10511    175  -1551    252       O  
ATOM    876  CB  PRO A 147       3.103  48.048  14.525  1.00 67.26           C  
ANISOU  876  CB  PRO A 147     9533   7714   8309    144  -1390    247       C  
ATOM    877  CG  PRO A 147       1.967  47.125  14.346  1.00 61.44           C  
ANISOU  877  CG  PRO A 147     8745   6956   7642    165  -1490    223       C  
ATOM    878  CD  PRO A 147       1.149  47.221  15.582  1.00 63.05           C  
ANISOU  878  CD  PRO A 147     8734   7214   8009    211  -1499    177       C  
ATOM    879  N   ILE A 148       1.073  50.359  13.778  1.00 83.51           N  
ANISOU  879  N   ILE A 148    11660   9569  10502    204  -1775    225       N  
ATOM    880  CA  ILE A 148       0.721  51.446  12.863  1.00 80.30           C  
ANISOU  880  CA  ILE A 148    11406   9040  10063    205  -1935    242       C  
ATOM    881  C   ILE A 148       0.463  52.743  13.622  1.00 82.20           C  
ANISOU  881  C   ILE A 148    11541   9280  10410    238  -1968    222       C  
ATOM    882  O   ILE A 148       0.878  53.826  13.192  1.00 86.50           O  
ANISOU  882  O   ILE A 148    12206   9768  10892    225  -1999    248       O  
ATOM    883  CB  ILE A 148      -0.509  51.061  12.019  1.00 81.85           C  
ANISOU  883  CB  ILE A 148    11661   9134  10302    224  -2137    228       C  
ATOM    884  CG1 ILE A 148      -0.276  49.773  11.237  1.00 83.90           C  
ANISOU  884  CG1 ILE A 148    12030   9393  10455    189  -2106    247       C  
ATOM    885  CG2 ILE A 148      -0.891  52.198  11.086  1.00 86.55           C  
ANISOU  885  CG2 ILE A 148    12424   9595  10867    226  -2319    248       C  
ATOM    886  CD1 ILE A 148      -1.548  49.227  10.613  1.00 86.24           C  
ANISOU  886  CD1 ILE A 148    12341   9607  10819    213  -2294    223       C  
ATOM    887  N   LYS A 149      -0.242  52.659  14.745  1.00 83.78           N  
ANISOU  887  N   LYS A 149    11520   9539  10773    278  -1961    173       N  
ATOM    888  CA  LYS A 149      -0.777  53.861  15.372  1.00 90.15           C  
ANISOU  888  CA  LYS A 149    12222  10325  11706    311  -2027    143       C  
ATOM    889  C   LYS A 149       0.296  54.601  16.159  1.00 91.74           C  
ANISOU  889  C   LYS A 149    12380  10605  11871    298  -1870    156       C  
ATOM    890  O   LYS A 149       0.293  55.837  16.205  1.00101.03           O  
ANISOU  890  O   LYS A 149    13571  11740  13074    308  -1920    158       O  
ATOM    891  CB  LYS A 149      -1.962  53.504  16.277  1.00 93.24           C  
ANISOU  891  CB  LYS A 149    12394  10740  12291    351  -2069     76       C  
ATOM    892  CG  LYS A 149      -3.284  53.140  15.558  1.00 90.87           C  
ANISOU  892  CG  LYS A 149    12110  10336  12083    377  -2268     45       C  
ATOM    893  CD  LYS A 149      -3.212  51.815  14.778  1.00 74.97           C  
ANISOU  893  CD  LYS A 149    10195   8318   9971    356  -2267     66       C  
ATOM    894  CE  LYS A 149      -2.708  50.649  15.631  1.00 70.71           C  
ANISOU  894  CE  LYS A 149     9539   7908   9419    342  -2074     59       C  
ATOM    895  NZ  LYS A 149      -2.240  49.492  14.789  1.00 64.43           N  
ANISOU  895  NZ  LYS A 149     8876   7117   8487    309  -2038     95       N  
ATOM    896  N   SER A 150       1.221  53.870  16.775  1.00 88.11           N  
ANISOU  896  N   SER A 150    11868  10255  11355    277  -1687    165       N  
ATOM    897  CA  SER A 150       2.295  54.490  17.550  1.00 92.42           C  
ANISOU  897  CA  SER A 150    12369  10878  11869    265  -1536    174       C  
ATOM    898  C   SER A 150       3.571  54.676  16.735  1.00101.28           C  
ANISOU  898  C   SER A 150    13679  11981  12822    221  -1458    223       C  
ATOM    899  O   SER A 150       4.679  54.553  17.269  1.00105.10           O  
ANISOU  899  O   SER A 150    14133  12545  13255    202  -1296    230       O  
ATOM    900  CB  SER A 150       2.560  53.672  18.812  1.00 85.78           C  
ANISOU  900  CB  SER A 150    11352  10161  11080    269  -1388    149       C  
ATOM    901  OG  SER A 150       3.007  52.363  18.499  1.00 83.84           O  
ANISOU  901  OG  SER A 150    11151   9950  10753    246  -1316    167       O  
ATOM    902  N   ALA A 151       3.449  54.967  15.433  1.00 99.56           N  
ANISOU  902  N   ALA A 151    13660  11651  12516    202  -1570    252       N  
ATOM    903  CA  ALA A 151       4.609  55.428  14.676  1.00 91.55           C  
ANISOU  903  CA  ALA A 151    12832  10602  11351    156  -1496    291       C  
ATOM    904  C   ALA A 151       5.138  56.737  15.240  1.00 94.70           C  
ANISOU  904  C   ALA A 151    13193  11016  11771    163  -1444    288       C  
ATOM    905  O   ALA A 151       6.330  57.038  15.106  1.00104.71           O  
ANISOU  905  O   ALA A 151    14542  12299  12943    127  -1316    306       O  
ATOM    906  CB  ALA A 151       4.254  55.595  13.197  1.00 82.20           C  
ANISOU  906  CB  ALA A 151    11881   9283  10070    133  -1641    321       C  
ATOM    907  N   LYS A 152       4.270  57.512  15.892  1.00 86.50           N  
ANISOU  907  N   LYS A 152    12026   9972  10867    206  -1537    261       N  
ATOM    908  CA  LYS A 152       4.652  58.808  16.433  1.00 89.89           C  
ANISOU  908  CA  LYS A 152    12414  10412  11330    215  -1502    256       C  
ATOM    909  C   LYS A 152       5.209  58.679  17.843  1.00 91.03           C  
ANISOU  909  C   LYS A 152    12362  10688  11538    226  -1342    228       C  
ATOM    910  O   LYS A 152       6.062  59.480  18.250  1.00 92.78           O  
ANISOU  910  O   LYS A 152    12574  10941  11738    217  -1245    231       O  
ATOM    911  CB  LYS A 152       3.454  59.772  16.410  1.00 92.61           C  
ANISOU  911  CB  LYS A 152    12719  10675  11792    254  -1683    236       C  
ATOM    912  CG  LYS A 152       2.829  60.037  15.012  1.00 94.55           C  
ANISOU  912  CG  LYS A 152    13168  10775  11983    248  -1874    264       C  
ATOM    913  CD  LYS A 152       2.091  58.824  14.415  1.00 89.95           C  
ANISOU  913  CD  LYS A 152    12621  10161  11397    250  -1965    262       C  
ATOM    914  CE  LYS A 152       2.068  58.849  12.888  1.00 88.46           C  
ANISOU  914  CE  LYS A 152    12697   9842  11072    220  -2086    304       C  
ATOM    915  NZ  LYS A 152       1.130  57.835  12.318  1.00 84.24           N  
ANISOU  915  NZ  LYS A 152    12186   9262  10561    230  -2214    296       N  
ATOM    916  N   TRP A 153       4.760  57.670  18.587  1.00 91.20           N  
ANISOU  916  N   TRP A 153    12236  10782  11633    242  -1311    202       N  
ATOM    917  CA  TRP A 153       5.219  57.474  19.956  1.00 92.04           C  
ANISOU  917  CA  TRP A 153    12167  11009  11797    250  -1170    176       C  
ATOM    918  C   TRP A 153       6.600  56.835  20.031  1.00 87.85           C  
ANISOU  918  C   TRP A 153    11676  10545  11158    218  -1005    197       C  
ATOM    919  O   TRP A 153       7.233  56.897  21.091  1.00 86.48           O  
ANISOU  919  O   TRP A 153    11386  10459  11012    221   -886    182       O  
ATOM    920  CB  TRP A 153       4.205  56.619  20.732  1.00 93.12           C  
ANISOU  920  CB  TRP A 153    12140  11190  12050    276  -1196    139       C  
ATOM    921  CG  TRP A 153       3.395  57.393  21.747  1.00 90.77           C  
ANISOU  921  CG  TRP A 153    11678  10909  11903    305  -1231     92       C  
ATOM    922  CD1 TRP A 153       3.515  57.328  23.105  1.00 90.16           C  
ANISOU  922  CD1 TRP A 153    11436  10925  11894    311  -1124     61       C  
ATOM    923  CD2 TRP A 153       2.346  58.344  21.482  1.00 96.15           C  
ANISOU  923  CD2 TRP A 153    12346  11502  12686    330  -1383     70       C  
ATOM    924  NE1 TRP A 153       2.615  58.179  23.703  1.00 99.90           N  
ANISOU  924  NE1 TRP A 153    12554  12138  13264    334  -1188     17       N  
ATOM    925  CE2 TRP A 153       1.885  58.814  22.731  1.00 98.67           C  
ANISOU  925  CE2 TRP A 153    12482  11871  13139    347  -1348     20       C  
ATOM    926  CE3 TRP A 153       1.756  58.845  20.315  1.00101.07           C  
ANISOU  926  CE3 TRP A 153    13099  12003  13300    338  -1550     86       C  
ATOM    927  CZ2 TRP A 153       0.860  59.757  22.845  1.00 95.51           C  
ANISOU  927  CZ2 TRP A 153    12012  11403  12876    372  -1467    -18       C  
ATOM    928  CZ3 TRP A 153       0.735  59.785  20.432  1.00 99.34           C  
ANISOU  928  CZ3 TRP A 153    12812  11715  13218    367  -1681     50       C  
ATOM    929  CH2 TRP A 153       0.300  60.228  21.687  1.00 97.92           C  
ANISOU  929  CH2 TRP A 153    12436  11588  13182    384  -1636     -3       C  
ATOM    930  N   ARG A 154       7.084  56.231  18.940  1.00 88.42           N  
ANISOU  930  N   ARG A 154    11910  10571  11114    185   -995    228       N  
ATOM    931  CA  ARG A 154       8.358  55.516  18.924  1.00 71.65           C  
ANISOU  931  CA  ARG A 154     9824   8499   8901    151   -842    240       C  
ATOM    932  C   ARG A 154       9.419  56.278  18.138  1.00 79.03           C  
ANISOU  932  C   ARG A 154    10921   9379   9730    113   -784    261       C  
ATOM    933  O   ARG A 154      10.258  55.687  17.457  1.00 84.27           O  
ANISOU  933  O   ARG A 154    11698  10025  10295     72   -703    275       O  
ATOM    934  CB  ARG A 154       8.182  54.104  18.375  1.00 65.41           C  
ANISOU  934  CB  ARG A 154     9080   7706   8068    136   -845    250       C  
ATOM    935  CG  ARG A 154       7.110  53.302  19.121  1.00 76.96           C  
ANISOU  935  CG  ARG A 154    10388   9217   9637    170   -896    226       C  
ATOM    936  CD  ARG A 154       7.363  51.793  19.111  1.00 79.15           C  
ANISOU  936  CD  ARG A 154    10650   9541   9882    155   -826    230       C  
ATOM    937  NE  ARG A 154       8.726  51.460  19.514  1.00 76.85           N  
ANISOU  937  NE  ARG A 154    10346   9315   9540    132   -667    236       N  
ATOM    938  CZ  ARG A 154       9.587  50.779  18.765  1.00 76.06           C  
ANISOU  938  CZ  ARG A 154    10356   9198   9345     93   -594    253       C  
ATOM    939  NH1 ARG A 154       9.223  50.345  17.569  1.00 76.38           N  
ANISOU  939  NH1 ARG A 154    10538   9163   9321     70   -662    270       N  
ATOM    940  NH2 ARG A 154      10.815  50.531  19.216  1.00 76.77           N  
ANISOU  940  NH2 ARG A 154    10414   9342   9412     76   -453    249       N  
ATOM    941  N   ARG A 155       9.386  57.607  18.226  1.00 80.68           N  
ANISOU  941  N   ARG A 155    11140   9554   9960    124   -819    259       N  
ATOM    942  CA  ARG A 155      10.476  58.427  17.719  1.00 64.76           C  
ANISOU  942  CA  ARG A 155     9251   7497   7857     89   -739    271       C  
ATOM    943  C   ARG A 155      11.566  58.544  18.777  1.00 68.45           C  
ANISOU  943  C   ARG A 155     9594   8061   8354     90   -580    248       C  
ATOM    944  O   ARG A 155      11.266  58.586  19.976  1.00 71.89           O  
ANISOU  944  O   ARG A 155     9849   8578   8888    126   -569    226       O  
ATOM    945  CB  ARG A 155       9.980  59.816  17.336  1.00 78.63           C  
ANISOU  945  CB  ARG A 155    11079   9171   9624    100   -848    279       C  
ATOM    946  CG  ARG A 155       9.643  59.951  15.863  1.00 89.56           C  
ANISOU  946  CG  ARG A 155    12693  10426  10909     70   -958    311       C  
ATOM    947  CD  ARG A 155       8.595  61.030  15.624  1.00 96.44           C  
ANISOU  947  CD  ARG A 155    13591  11216  11835    100  -1132    316       C  
ATOM    948  NE  ARG A 155       7.502  60.545  14.780  1.00 99.72           N  
ANISOU  948  NE  ARG A 155    14096  11550  12243    107  -1302    331       N  
ATOM    949  CZ  ARG A 155       7.595  60.324  13.471  1.00 96.15           C  
ANISOU  949  CZ  ARG A 155    13872  10998  11664     66  -1354    362       C  
ATOM    950  NH1 ARG A 155       8.734  60.552  12.825  1.00 93.64           N  
ANISOU  950  NH1 ARG A 155    13721  10644  11214     10  -1239    381       N  
ATOM    951  NH2 ARG A 155       6.541  59.876  12.807  1.00 98.88           N  
ANISOU  951  NH2 ARG A 155    14280  11272  12017     78  -1520    371       N  
ATOM    952  N   PRO A 156      12.828  58.566  18.350  1.00 72.89           N  
ANISOU  952  N   PRO A 156    10252   8609   8834     48   -454    250       N  
ATOM    953  CA  PRO A 156      13.931  58.630  19.326  1.00 66.29           C  
ANISOU  953  CA  PRO A 156     9298   7858   8033     50   -307    223       C  
ATOM    954  C   PRO A 156      13.803  59.766  20.331  1.00 65.04           C  
ANISOU  954  C   PRO A 156     9013   7742   7958     85   -315    205       C  
ATOM    955  O   PRO A 156      14.115  59.571  21.514  1.00 67.00           O  
ANISOU  955  O   PRO A 156     9101   8083   8272    107   -248    182       O  
ATOM    956  CB  PRO A 156      15.163  58.799  18.430  1.00 59.25           C  
ANISOU  956  CB  PRO A 156     8563   6905   7043     -5   -195    223       C  
ATOM    957  CG  PRO A 156      14.766  58.167  17.128  1.00 55.09           C  
ANISOU  957  CG  PRO A 156     8214   6292   6424    -40   -256    250       C  
ATOM    958  CD  PRO A 156      13.310  58.434  16.962  1.00 60.08           C  
ANISOU  958  CD  PRO A 156     8850   6890   7088     -6   -436    270       C  
ATOM    959  N   ARG A 157      13.328  60.942  19.897  1.00 57.77           N  
ANISOU  959  N   ARG A 157     8164   6751   7035     90   -399    215       N  
ATOM    960  CA  ARG A 157      13.326  62.115  20.768  1.00 57.53           C  
ANISOU  960  CA  ARG A 157     8026   6753   7079    117   -393    195       C  
ATOM    961  C   ARG A 157      12.332  61.979  21.921  1.00 61.97           C  
ANISOU  961  C   ARG A 157     8399   7388   7758    162   -456    177       C  
ATOM    962  O   ARG A 157      12.559  62.531  23.004  1.00 68.40           O  
ANISOU  962  O   ARG A 157     9079   8269   8641    182   -404    152       O  
ATOM    963  CB  ARG A 157      13.038  63.372  19.942  1.00 65.39           C  
ANISOU  963  CB  ARG A 157     9156   7646   8042    110   -474    211       C  
ATOM    964  CG  ARG A 157      12.574  64.568  20.763  1.00 76.94           C  
ANISOU  964  CG  ARG A 157    10502   9130   9603    145   -518    194       C  
ATOM    965  CD  ARG A 157      11.080  64.841  20.564  1.00 83.04           C  
ANISOU  965  CD  ARG A 157    11262   9848  10440    175   -698    202       C  
ATOM    966  NE  ARG A 157      10.587  65.961  21.369  1.00 86.49           N  
ANISOU  966  NE  ARG A 157    11577  10302  10985    207   -738    179       N  
ATOM    967  CZ  ARG A 157      10.981  67.226  21.238  1.00 89.53           C  
ANISOU  967  CZ  ARG A 157    12010  10647  11362    203   -726    179       C  
ATOM    968  NH1 ARG A 157      11.892  67.562  20.326  1.00 94.42           N  
ANISOU  968  NH1 ARG A 157    12804  11203  11868    165   -668    200       N  
ATOM    969  NH2 ARG A 157      10.456  68.158  22.027  1.00 83.92           N  
ANISOU  969  NH2 ARG A 157    11171   9955  10760    232   -764    155       N  
ATOM    970  N   THR A 158      11.243  61.237  21.730  1.00 60.95           N  
ANISOU  970  N   THR A 158     8257   7245   7657    176   -560    184       N  
ATOM    971  CA  THR A 158      10.294  61.101  22.824  1.00 60.20           C  
ANISOU  971  CA  THR A 158     7984   7211   7678    212   -606    158       C  
ATOM    972  C   THR A 158      10.667  59.967  23.780  1.00 62.55           C  
ANISOU  972  C   THR A 158     8162   7610   7994    214   -509    144       C  
ATOM    973  O   THR A 158      10.337  60.039  24.969  1.00 69.00           O  
ANISOU  973  O   THR A 158     8826   8496   8896    235   -490    117       O  
ATOM    974  CB  THR A 158       8.881  60.937  22.263  1.00 64.45           C  
ANISOU  974  CB  THR A 158     8546   7681   8261    229   -766    162       C  
ATOM    975  OG1 THR A 158       8.594  59.560  22.026  1.00 57.79           O  
ANISOU  975  OG1 THR A 158     7710   6851   7395    223   -774    169       O  
ATOM    976  CG2 THR A 158       8.765  61.701  20.952  1.00 71.77           C  
ANISOU  976  CG2 THR A 158     9658   8489   9122    215   -861    190       C  
ATOM    977  N   ALA A 159      11.375  58.934  23.303  1.00 63.98           N  
ANISOU  977  N   ALA A 159     8414   7799   8098    190   -444    160       N  
ATOM    978  CA  ALA A 159      11.965  57.957  24.219  1.00 51.24           C  
ANISOU  978  CA  ALA A 159     6696   6277   6495    191   -342    148       C  
ATOM    979  C   ALA A 159      13.029  58.599  25.105  1.00 58.54           C  
ANISOU  979  C   ALA A 159     7549   7259   7434    192   -235    129       C  
ATOM    980  O   ALA A 159      13.238  58.162  26.247  1.00 60.08           O  
ANISOU  980  O   ALA A 159     7620   7536   7673    204   -180    112       O  
ATOM    981  CB  ALA A 159      12.569  56.785  23.440  1.00 53.77           C  
ANISOU  981  CB  ALA A 159     7113   6583   6735    163   -295    167       C  
ATOM    982  N   LYS A 160      13.712  59.633  24.600  1.00 53.49           N  
ANISOU  982  N   LYS A 160     6991   6575   6759    178   -206    131       N  
ATOM    983  CA  LYS A 160      14.639  60.383  25.442  1.00 54.76           C  
ANISOU  983  CA  LYS A 160     7077   6784   6946    183   -114    107       C  
ATOM    984  C   LYS A 160      13.896  61.246  26.452  1.00 65.83           C  
ANISOU  984  C   LYS A 160     8353   8224   8436    212   -159     87       C  
ATOM    985  O   LYS A 160      14.373  61.430  27.581  1.00 65.36           O  
ANISOU  985  O   LYS A 160     8180   8235   8417    222    -92     63       O  
ATOM    986  CB  LYS A 160      15.569  61.250  24.589  1.00 51.48           C  
ANISOU  986  CB  LYS A 160     6786   6304   6471    157    -62    110       C  
ATOM    987  CG  LYS A 160      16.628  60.462  23.843  1.00 52.74           C  
ANISOU  987  CG  LYS A 160     7046   6438   6556    121     28    113       C  
ATOM    988  CD  LYS A 160      17.420  61.349  22.911  1.00 56.53           C  
ANISOU  988  CD  LYS A 160     7665   6838   6976     88     81    111       C  
ATOM    989  CE  LYS A 160      18.224  60.515  21.931  1.00 65.09           C  
ANISOU  989  CE  LYS A 160     8875   7873   7982     42    156    114       C  
ATOM    990  NZ  LYS A 160      19.629  61.024  21.826  1.00 72.87           N  
ANISOU  990  NZ  LYS A 160     9892   8839   8956     14    292     82       N  
ATOM    991  N   MET A 161      12.732  61.786  26.084  1.00 65.34           N  
ANISOU  991  N   MET A 161     8308   8109   8410    224   -272     92       N  
ATOM    992  CA  MET A 161      11.939  62.471  27.099  1.00 63.64           C  
ANISOU  992  CA  MET A 161     7958   7928   8293    248   -310     65       C  
ATOM    993  C   MET A 161      11.390  61.473  28.115  1.00 56.85           C  
ANISOU  993  C   MET A 161     6973   7140   7486    258   -300     48       C  
ATOM    994  O   MET A 161      11.411  61.736  29.323  1.00 46.34           O  
ANISOU  994  O   MET A 161     5520   5876   6212    266   -255     20       O  
ATOM    995  CB  MET A 161      10.824  63.291  26.445  1.00 69.29           C  
ANISOU  995  CB  MET A 161     8716   8560   9051    259   -440     69       C  
ATOM    996  CG  MET A 161      11.325  64.570  25.748  1.00 80.83           C  
ANISOU  996  CG  MET A 161    10280   9956  10476    251   -446     80       C  
ATOM    997  SD  MET A 161      10.080  65.862  25.459  1.00 97.26           S  
ANISOU  997  SD  MET A 161    12359  11953  12642    272   -592     73       S  
ATOM    998  CE  MET A 161       8.826  64.971  24.515  1.00 84.61           C  
ANISOU  998  CE  MET A 161    10828  10276  11044    278   -742     91       C  
ATOM    999  N   ILE A 162      10.949  60.297  27.653  1.00 51.08           N  
ANISOU  999  N   ILE A 162     6278   6398   6732    254   -335     63       N  
ATOM   1000  CA  ILE A 162      10.411  59.299  28.576  1.00 52.77           C  
ANISOU 1000  CA  ILE A 162     6384   6674   6991    260   -322     47       C  
ATOM   1001  C   ILE A 162      11.456  58.903  29.623  1.00 51.75           C  
ANISOU 1001  C   ILE A 162     6187   6630   6843    255   -206     38       C  
ATOM   1002  O   ILE A 162      11.154  58.839  30.823  1.00 48.17           O  
ANISOU 1002  O   ILE A 162     5621   6236   6444    260   -180     13       O  
ATOM   1003  CB  ILE A 162       9.871  58.078  27.809  1.00 57.54           C  
ANISOU 1003  CB  ILE A 162     7048   7247   7566    256   -372     66       C  
ATOM   1004  CG1 ILE A 162       8.524  58.403  27.161  1.00 51.60           C  
ANISOU 1004  CG1 ILE A 162     6316   6420   6870    268   -504     60       C  
ATOM   1005  CG2 ILE A 162       9.668  56.909  28.749  1.00 59.57           C  
ANISOU 1005  CG2 ILE A 162     7212   7575   7848    256   -327     53       C  
ATOM   1006  CD1 ILE A 162       8.062  57.346  26.186  1.00 48.94           C  
ANISOU 1006  CD1 ILE A 162     6063   6038   6495    262   -566     81       C  
ATOM   1007  N   THR A 163      12.710  58.671  29.199  1.00 48.25           N  
ANISOU 1007  N   THR A 163     5815   6190   6328    242   -137     55       N  
ATOM   1008  CA  THR A 163      13.722  58.255  30.173  1.00 44.89           C  
ANISOU 1008  CA  THR A 163     5325   5837   5894    240    -42     44       C  
ATOM   1009  C   THR A 163      14.072  59.375  31.150  1.00 51.62           C  
ANISOU 1009  C   THR A 163     6097   6728   6789    248     -4     18       C  
ATOM   1010  O   THR A 163      14.332  59.099  32.325  1.00 54.94           O  
ANISOU 1010  O   THR A 163     6429   7215   7232    252     41      1       O  
ATOM   1011  CB  THR A 163      14.994  57.723  29.489  1.00 53.02           C  
ANISOU 1011  CB  THR A 163     6439   6852   6856    224     25     59       C  
ATOM   1012  OG1 THR A 163      15.388  58.565  28.397  1.00 58.91           O  
ANISOU 1012  OG1 THR A 163     7293   7528   7563    211     24     67       O  
ATOM   1013  CG2 THR A 163      14.784  56.273  28.982  1.00 52.13           C  
ANISOU 1013  CG2 THR A 163     6368   6732   6708    215     13     80       C  
ATOM   1014  N   MET A 164      14.059  60.640  30.718  1.00 60.34           N  
ANISOU 1014  N   MET A 164     7232   7790   7905    251    -25     13       N  
ATOM   1015  CA  MET A 164      14.298  61.719  31.680  1.00 57.87           C  
ANISOU 1015  CA  MET A 164     6834   7515   7638    258      9    -15       C  
ATOM   1016  C   MET A 164      13.212  61.747  32.743  1.00 56.78           C  
ANISOU 1016  C   MET A 164     6584   7416   7574    265    -22    -39       C  
ATOM   1017  O   MET A 164      13.494  61.979  33.925  1.00 55.63           O  
ANISOU 1017  O   MET A 164     6350   7330   7455    265     28    -63       O  
ATOM   1018  CB  MET A 164      14.376  63.069  30.978  1.00 67.97           C  
ANISOU 1018  CB  MET A 164     8170   8735   8921    259    -13    -15       C  
ATOM   1019  CG  MET A 164      15.752  63.429  30.457  1.00 80.21           C  
ANISOU 1019  CG  MET A 164     9794  10267  10417    248     63    -12       C  
ATOM   1020  SD  MET A 164      15.648  64.824  29.319  1.00102.17           S  
ANISOU 1020  SD  MET A 164    12684  12954  13182    242     23     -3       S  
ATOM   1021  CE  MET A 164      14.762  66.032  30.310  1.00 88.32           C  
ANISOU 1021  CE  MET A 164    10806  11226  11526    262    -21    -30       C  
ATOM   1022  N   ALA A 165      11.961  61.508  32.336  1.00 57.83           N  
ANISOU 1022  N   ALA A 165     6721   7510   7743    268   -104    -37       N  
ATOM   1023  CA  ALA A 165      10.874  61.350  33.291  1.00 56.94           C  
ANISOU 1023  CA  ALA A 165     6503   7425   7707    269   -124    -67       C  
ATOM   1024  C   ALA A 165      11.190  60.252  34.300  1.00 55.76           C  
ANISOU 1024  C   ALA A 165     6303   7347   7536    260    -59    -72       C  
ATOM   1025  O   ALA A 165      11.019  60.443  35.507  1.00 61.86           O  
ANISOU 1025  O   ALA A 165     6988   8168   8348    253    -21   -101       O  
ATOM   1026  CB  ALA A 165       9.568  61.045  32.553  1.00 51.71           C  
ANISOU 1026  CB  ALA A 165     5860   6700   7087    274   -223    -66       C  
ATOM   1027  N   VAL A 166      11.683  59.106  33.820  1.00 53.44           N  
ANISOU 1027  N   VAL A 166     6070   7056   7179    257    -45    -43       N  
ATOM   1028  CA  VAL A 166      11.936  57.964  34.699  1.00 52.91           C  
ANISOU 1028  CA  VAL A 166     5966   7048   7090    249      4    -43       C  
ATOM   1029  C   VAL A 166      12.882  58.350  35.834  1.00 51.04           C  
ANISOU 1029  C   VAL A 166     5678   6870   6845    247     74    -58       C  
ATOM   1030  O   VAL A 166      12.626  58.046  37.003  1.00 56.93           O  
ANISOU 1030  O   VAL A 166     6360   7662   7608    237    102    -77       O  
ATOM   1031  CB  VAL A 166      12.467  56.767  33.888  1.00 54.76           C  
ANISOU 1031  CB  VAL A 166     6279   7269   7259    248      9     -9       C  
ATOM   1032  CG1 VAL A 166      13.084  55.722  34.800  1.00 55.32           C  
ANISOU 1032  CG1 VAL A 166     6319   7398   7302    242     65     -6       C  
ATOM   1033  CG2 VAL A 166      11.332  56.134  33.080  1.00 51.89           C  
ANISOU 1033  CG2 VAL A 166     5947   6858   6909    248    -61      0       C  
ATOM   1034  N   TRP A 167      13.977  59.042  35.515  1.00 49.76           N  
ANISOU 1034  N   TRP A 167     5547   6703   6657    253    104    -54       N  
ATOM   1035  CA  TRP A 167      14.862  59.534  36.569  1.00 47.81           C  
ANISOU 1035  CA  TRP A 167     5247   6506   6411    253    161    -73       C  
ATOM   1036  C   TRP A 167      14.144  60.515  37.500  1.00 57.90           C  
ANISOU 1036  C   TRP A 167     6446   7805   7749    248    160   -107       C  
ATOM   1037  O   TRP A 167      14.375  60.506  38.714  1.00 65.01           O  
ANISOU 1037  O   TRP A 167     7290   8756   8653    240    198   -127       O  
ATOM   1038  CB  TRP A 167      16.098  60.196  35.964  1.00 41.00           C  
ANISOU 1038  CB  TRP A 167     4429   5624   5525    260    195    -70       C  
ATOM   1039  CG  TRP A 167      16.976  59.246  35.245  1.00 45.01           C  
ANISOU 1039  CG  TRP A 167     5004   6114   5984    258    217    -49       C  
ATOM   1040  CD1 TRP A 167      16.949  58.962  33.910  1.00 39.93           C  
ANISOU 1040  CD1 TRP A 167     4450   5412   5308    253    199    -26       C  
ATOM   1041  CD2 TRP A 167      18.025  58.446  35.812  1.00 42.38           C  
ANISOU 1041  CD2 TRP A 167     4654   5815   5632    260    261    -51       C  
ATOM   1042  NE1 TRP A 167      17.900  58.027  33.610  1.00 47.97           N  
ANISOU 1042  NE1 TRP A 167     5505   6429   6292    248    238    -17       N  
ATOM   1043  CE2 TRP A 167      18.589  57.697  34.753  1.00 49.01           C  
ANISOU 1043  CE2 TRP A 167     5568   6615   6437    254    274    -33       C  
ATOM   1044  CE3 TRP A 167      18.540  58.284  37.109  1.00 36.59           C  
ANISOU 1044  CE3 TRP A 167     3856   5137   4909    263    286    -68       C  
ATOM   1045  CZ2 TRP A 167      19.655  56.792  34.950  1.00 39.97           C  
ANISOU 1045  CZ2 TRP A 167     4423   5483   5282    255    312    -34       C  
ATOM   1046  CZ3 TRP A 167      19.576  57.385  37.305  1.00 35.67           C  
ANISOU 1046  CZ3 TRP A 167     3746   5032   4777    267    312    -66       C  
ATOM   1047  CH2 TRP A 167      20.127  56.651  36.226  1.00 37.35           C  
ANISOU 1047  CH2 TRP A 167     4022   5203   4968    264    325    -50       C  
ATOM   1048  N   GLY A 168      13.280  61.377  36.956  1.00 47.27           N  
ANISOU 1048  N   GLY A 168     5095   6415   6450    251    113   -116       N  
ATOM   1049  CA  GLY A 168      12.565  62.307  37.811  1.00 52.23           C  
ANISOU 1049  CA  GLY A 168     5641   7056   7147    244    114   -154       C  
ATOM   1050  C   GLY A 168      11.648  61.606  38.800  1.00 63.87           C  
ANISOU 1050  C   GLY A 168     7054   8559   8652    225    124   -177       C  
ATOM   1051  O   GLY A 168      11.701  61.860  40.012  1.00 68.03           O  
ANISOU 1051  O   GLY A 168     7522   9131   9194    209    170   -206       O  
ATOM   1052  N   VAL A 169      10.801  60.704  38.286  1.00 58.50           N  
ANISOU 1052  N   VAL A 169     6395   7850   7981    223     82   -167       N  
ATOM   1053  CA  VAL A 169       9.868  59.932  39.104  1.00 48.88           C  
ANISOU 1053  CA  VAL A 169     5128   6648   6794    202     95   -192       C  
ATOM   1054  C   VAL A 169      10.600  59.160  40.210  1.00 59.34           C  
ANISOU 1054  C   VAL A 169     6452   8036   8060    187    161   -187       C  
ATOM   1055  O   VAL A 169      10.131  59.108  41.355  1.00 66.01           O  
ANISOU 1055  O   VAL A 169     7246   8908   8927    161    201   -220       O  
ATOM   1056  CB  VAL A 169       9.041  58.999  38.200  1.00 48.23           C  
ANISOU 1056  CB  VAL A 169     5082   6522   6723    208     39   -177       C  
ATOM   1057  CG1 VAL A 169       8.259  57.998  39.030  1.00 52.66           C  
ANISOU 1057  CG1 VAL A 169     5604   7101   7304    185     67   -200       C  
ATOM   1058  CG2 VAL A 169       8.104  59.804  37.303  1.00 40.57           C  
ANISOU 1058  CG2 VAL A 169     4105   5482   5830    220    -40   -191       C  
ATOM   1059  N   SER A 170      11.753  58.549  39.891  1.00 52.60           N  
ANISOU 1059  N   SER A 170     5656   7200   7131    200    173   -150       N  
ATOM   1060  CA  SER A 170      12.531  57.844  40.915  1.00 56.08           C  
ANISOU 1060  CA  SER A 170     6098   7691   7517    190    220   -144       C  
ATOM   1061  C   SER A 170      12.935  58.761  42.055  1.00 52.61           C  
ANISOU 1061  C   SER A 170     5613   7290   7087    179    260   -174       C  
ATOM   1062  O   SER A 170      12.849  58.377  43.230  1.00 60.32           O  
ANISOU 1062  O   SER A 170     6573   8300   8046    155    293   -190       O  
ATOM   1063  CB  SER A 170      13.790  57.215  40.316  1.00 61.46           C  
ANISOU 1063  CB  SER A 170     6839   8375   8137    209    221   -107       C  
ATOM   1064  OG  SER A 170      13.478  56.269  39.322  1.00 71.72           O  
ANISOU 1064  OG  SER A 170     8187   9642   9420    215    190    -80       O  
ATOM   1065  N   LEU A 171      13.409  59.963  41.720  1.00 58.08           N  
ANISOU 1065  N   LEU A 171     6292   7974   7801    193    258   -182       N  
ATOM   1066  CA  LEU A 171      13.820  60.947  42.719  1.00 60.20           C  
ANISOU 1066  CA  LEU A 171     6514   8277   8084    184    295   -213       C  
ATOM   1067  C   LEU A 171      12.694  61.286  43.688  1.00 59.05           C  
ANISOU 1067  C   LEU A 171     6310   8141   7988    151    316   -254       C  
ATOM   1068  O   LEU A 171      12.936  61.473  44.885  1.00 69.43           O  
ANISOU 1068  O   LEU A 171     7601   9493   9288    129    357   -277       O  
ATOM   1069  CB  LEU A 171      14.303  62.208  42.018  1.00 59.08           C  
ANISOU 1069  CB  LEU A 171     6366   8113   7968    204    288   -216       C  
ATOM   1070  CG  LEU A 171      15.348  63.054  42.741  1.00 66.30           C  
ANISOU 1070  CG  LEU A 171     7253   9063   8875    207    327   -235       C  
ATOM   1071  CD1 LEU A 171      16.264  62.227  43.652  1.00 66.46           C  
ANISOU 1071  CD1 LEU A 171     7287   9126   8839    203    349   -230       C  
ATOM   1072  CD2 LEU A 171      16.176  63.801  41.692  1.00 61.86           C  
ANISOU 1072  CD2 LEU A 171     6720   8470   8314    232    323   -224       C  
ATOM   1073  N   LEU A 172      11.460  61.378  43.191  1.00 43.04           N  
ANISOU 1073  N   LEU A 172     4258   6072   6023    145    288   -269       N  
ATOM   1074  CA  LEU A 172      10.326  61.609  44.077  1.00 53.73           C  
ANISOU 1074  CA  LEU A 172     5552   7425   7440    110    316   -318       C  
ATOM   1075  C   LEU A 172      10.062  60.397  44.961  1.00 61.17           C  
ANISOU 1075  C   LEU A 172     6512   8389   8339     79    354   -322       C  
ATOM   1076  O   LEU A 172       9.912  60.529  46.179  1.00 61.71           O  
ANISOU 1076  O   LEU A 172     6559   8484   8403     42    408   -355       O  
ATOM   1077  CB  LEU A 172       9.081  61.951  43.259  1.00 66.12           C  
ANISOU 1077  CB  LEU A 172     7086   8933   9102    114    268   -339       C  
ATOM   1078  CG  LEU A 172       9.222  63.136  42.304  1.00 65.96           C  
ANISOU 1078  CG  LEU A 172     7060   8877   9124    144    220   -333       C  
ATOM   1079  CD1 LEU A 172       7.863  63.528  41.769  1.00 61.39           C  
ANISOU 1079  CD1 LEU A 172     6436   8235   8654    143    166   -364       C  
ATOM   1080  CD2 LEU A 172       9.916  64.328  42.993  1.00 65.17           C  
ANISOU 1080  CD2 LEU A 172     6924   8810   9028    139    262   -353       C  
ATOM   1081  N   VAL A 173      10.021  59.202  44.357  1.00 64.56           N  
ANISOU 1081  N   VAL A 173     6991   8807   8732     91    327   -287       N  
ATOM   1082  CA  VAL A 173       9.681  57.972  45.075  1.00 55.78           C  
ANISOU 1082  CA  VAL A 173     5904   7708   7582     62    359   -288       C  
ATOM   1083  C   VAL A 173      10.689  57.662  46.191  1.00 64.20           C  
ANISOU 1083  C   VAL A 173     7006   8823   8564     47    397   -276       C  
ATOM   1084  O   VAL A 173      10.329  57.032  47.195  1.00 74.70           O  
ANISOU 1084  O   VAL A 173     8352  10163   9865      9    439   -292       O  
ATOM   1085  CB  VAL A 173       9.546  56.799  44.071  1.00 45.86           C  
ANISOU 1085  CB  VAL A 173     4693   6427   6303     83    317   -249       C  
ATOM   1086  CG1 VAL A 173       9.689  55.431  44.752  1.00 46.72           C  
ANISOU 1086  CG1 VAL A 173     4849   6558   6345     63    347   -232       C  
ATOM   1087  CG2 VAL A 173       8.218  56.859  43.347  1.00 39.85           C  
ANISOU 1087  CG2 VAL A 173     3896   5614   5630     83    284   -275       C  
ATOM   1088  N   ILE A 174      11.946  58.101  46.070  1.00 51.56           N  
ANISOU 1088  N   ILE A 174     5422   7244   6923     75    384   -253       N  
ATOM   1089  CA  ILE A 174      12.919  57.786  47.116  1.00 57.02           C  
ANISOU 1089  CA  ILE A 174     6147   7975   7543     65    404   -244       C  
ATOM   1090  C   ILE A 174      13.116  58.943  48.092  1.00 62.16           C  
ANISOU 1090  C   ILE A 174     6762   8650   8206     44    438   -282       C  
ATOM   1091  O   ILE A 174      14.030  58.888  48.931  1.00 67.60           O  
ANISOU 1091  O   ILE A 174     7477   9367   8839     40    445   -278       O  
ATOM   1092  CB  ILE A 174      14.279  57.319  46.547  1.00 53.73           C  
ANISOU 1092  CB  ILE A 174     5771   7565   7078    105    370   -201       C  
ATOM   1093  CG1 ILE A 174      14.927  58.375  45.647  1.00 62.00           C  
ANISOU 1093  CG1 ILE A 174     6795   8603   8160    139    353   -199       C  
ATOM   1094  CG2 ILE A 174      14.155  55.996  45.862  1.00 39.90           C  
ANISOU 1094  CG2 ILE A 174     4064   5795   5301    115    346   -165       C  
ATOM   1095  CD1 ILE A 174      15.920  59.275  46.382  1.00 61.98           C  
ANISOU 1095  CD1 ILE A 174     6772   8628   8149    143    369   -218       C  
ATOM   1096  N   LEU A 175      12.281  59.980  48.023  1.00 53.60           N  
ANISOU 1096  N   LEU A 175     5617   7551   7198     31    456   -321       N  
ATOM   1097  CA  LEU A 175      12.360  61.031  49.035  1.00 58.86           C  
ANISOU 1097  CA  LEU A 175     6247   8240   7879      4    497   -362       C  
ATOM   1098  C   LEU A 175      12.353  60.480  50.459  1.00 62.02           C  
ANISOU 1098  C   LEU A 175     6686   8663   8215    -44    541   -378       C  
ATOM   1099  O   LEU A 175      13.173  60.950  51.268  1.00 66.35           O  
ANISOU 1099  O   LEU A 175     7246   9241   8723    -50    552   -386       O  
ATOM   1100  CB  LEU A 175      11.241  62.066  48.829  1.00 55.49           C  
ANISOU 1100  CB  LEU A 175     5744   7785   7554    -11    514   -409       C  
ATOM   1101  CG  LEU A 175      11.499  63.123  47.732  1.00 60.84           C  
ANISOU 1101  CG  LEU A 175     6385   8444   8288     32    474   -401       C  
ATOM   1102  CD1 LEU A 175      10.358  64.107  47.665  1.00 61.11           C  
ANISOU 1102  CD1 LEU A 175     6344   8445   8430     14    483   -451       C  
ATOM   1103  CD2 LEU A 175      12.820  63.874  47.880  1.00 58.70           C  
ANISOU 1103  CD2 LEU A 175     6117   8204   7982     55    475   -391       C  
ATOM   1104  N   PRO A 176      11.518  59.489  50.825  1.00 54.13           N  
ANISOU 1104  N   PRO A 176     5719   7648   7200    -80    566   -384       N  
ATOM   1105  CA  PRO A 176      11.613  58.924  52.184  1.00 44.32           C  
ANISOU 1105  CA  PRO A 176     4538   6423   5880   -129    607   -394       C  
ATOM   1106  C   PRO A 176      13.006  58.453  52.578  1.00 57.01           C  
ANISOU 1106  C   PRO A 176     6212   8057   7393   -106    567   -352       C  
ATOM   1107  O   PRO A 176      13.440  58.734  53.705  1.00 53.25           O  
ANISOU 1107  O   PRO A 176     5767   7600   6865   -136    586   -368       O  
ATOM   1108  CB  PRO A 176      10.620  57.755  52.140  1.00 47.44           C  
ANISOU 1108  CB  PRO A 176     4964   6789   6274   -157    629   -395       C  
ATOM   1109  CG  PRO A 176       9.653  58.107  51.103  1.00 48.73           C  
ANISOU 1109  CG  PRO A 176     5054   6920   6543   -141    620   -415       C  
ATOM   1110  CD  PRO A 176      10.391  58.902  50.076  1.00 50.92           C  
ANISOU 1110  CD  PRO A 176     5295   7204   6848    -81    561   -388       C  
ATOM   1111  N   ILE A 177      13.707  57.715  51.703  1.00 55.50           N  
ANISOU 1111  N   ILE A 177     6043   7863   7181    -57    510   -303       N  
ATOM   1112  CA  ILE A 177      15.062  57.269  52.033  1.00 57.35           C  
ANISOU 1112  CA  ILE A 177     6329   8114   7346    -32    466   -269       C  
ATOM   1113  C   ILE A 177      15.949  58.474  52.297  1.00 60.93           C  
ANISOU 1113  C   ILE A 177     6746   8590   7814    -15    458   -288       C  
ATOM   1114  O   ILE A 177      16.696  58.520  53.282  1.00 68.29           O  
ANISOU 1114  O   ILE A 177     7715   9539   8694    -25    447   -292       O  
ATOM   1115  CB  ILE A 177      15.656  56.403  50.908  1.00 61.21           C  
ANISOU 1115  CB  ILE A 177     6834   8590   7833     18    414   -222       C  
ATOM   1116  CG1 ILE A 177      14.789  55.183  50.612  1.00 61.43           C  
ANISOU 1116  CG1 ILE A 177     6896   8597   7848      3    420   -204       C  
ATOM   1117  CG2 ILE A 177      17.083  55.988  51.276  1.00 53.39           C  
ANISOU 1117  CG2 ILE A 177     5884   7610   6792     44    366   -198       C  
ATOM   1118  CD1 ILE A 177      15.096  54.565  49.272  1.00 50.73           C  
ANISOU 1118  CD1 ILE A 177     5539   7225   6512     48    380   -167       C  
ATOM   1119  N   MET A 178      15.882  59.460  51.403  1.00 64.74           N  
ANISOU 1119  N   MET A 178     7160   9069   8370     13    461   -300       N  
ATOM   1120  CA  MET A 178      16.613  60.707  51.587  1.00 62.21           C  
ANISOU 1120  CA  MET A 178     6795   8766   8074     28    463   -323       C  
ATOM   1121  C   MET A 178      16.466  61.226  53.011  1.00 58.04           C  
ANISOU 1121  C   MET A 178     6276   8260   7518    -20    500   -361       C  
ATOM   1122  O   MET A 178      17.459  61.425  53.717  1.00 70.00           O  
ANISOU 1122  O   MET A 178     7811   9793   8992    -15    481   -364       O  
ATOM   1123  CB  MET A 178      16.111  61.734  50.580  1.00 53.22           C  
ANISOU 1123  CB  MET A 178     5588   7613   7019     46    475   -338       C  
ATOM   1124  CG  MET A 178      17.126  62.750  50.204  1.00 67.14           C  
ANISOU 1124  CG  MET A 178     7316   9385   8810     82    464   -344       C  
ATOM   1125  SD  MET A 178      16.560  63.629  48.747  1.00 88.25           S  
ANISOU 1125  SD  MET A 178     9939  12025  11566    108    462   -345       S  
ATOM   1126  CE  MET A 178      16.302  65.252  49.472  1.00 78.70           C  
ANISOU 1126  CE  MET A 178     8660  10833  10411     86    504   -398       C  
ATOM   1127  N   ILE A 179      15.221  61.377  53.471  1.00 45.97           N  
ANISOU 1127  N   ILE A 179     4735   6723   6008    -72    554   -394       N  
ATOM   1128  CA  ILE A 179      14.962  61.988  54.768  1.00 60.10           C  
ANISOU 1128  CA  ILE A 179     6530   8527   7777   -127    605   -438       C  
ATOM   1129  C   ILE A 179      15.452  61.108  55.914  1.00 59.47           C  
ANISOU 1129  C   ILE A 179     6550   8454   7590   -157    594   -424       C  
ATOM   1130  O   ILE A 179      16.057  61.601  56.872  1.00 60.53           O  
ANISOU 1130  O   ILE A 179     6708   8607   7682   -176    594   -442       O  
ATOM   1131  CB  ILE A 179      13.464  62.313  54.901  1.00 59.02           C  
ANISOU 1131  CB  ILE A 179     6352   8370   7704   -178    673   -484       C  
ATOM   1132  CG1 ILE A 179      13.061  63.340  53.837  1.00 63.73           C  
ANISOU 1132  CG1 ILE A 179     6852   8953   8410   -145    669   -499       C  
ATOM   1133  CG2 ILE A 179      13.145  62.811  56.301  1.00 45.86           C  
ANISOU 1133  CG2 ILE A 179     4704   6712   6010   -247    739   -534       C  
ATOM   1134  CD1 ILE A 179      14.066  64.488  53.695  1.00 67.37           C  
ANISOU 1134  CD1 ILE A 179     7272   9438   8889   -109    649   -502       C  
ATOM   1135  N   TYR A 180      15.219  59.802  55.841  1.00 63.76           N  
ANISOU 1135  N   TYR A 180     7158   8981   8086   -163    578   -392       N  
ATOM   1136  CA  TYR A 180      15.331  58.967  57.025  1.00 57.81           C  
ANISOU 1136  CA  TYR A 180     6510   8222   7231   -209    580   -385       C  
ATOM   1137  C   TYR A 180      16.522  58.026  57.026  1.00 64.27           C  
ANISOU 1137  C   TYR A 180     7396   9041   7983   -168    496   -334       C  
ATOM   1138  O   TYR A 180      16.678  57.271  57.998  1.00 71.35           O  
ANISOU 1138  O   TYR A 180     8393   9927   8789   -203    482   -322       O  
ATOM   1139  CB  TYR A 180      14.037  58.167  57.225  1.00 62.75           C  
ANISOU 1139  CB  TYR A 180     7174   8822   7848   -264    640   -397       C  
ATOM   1140  CG  TYR A 180      12.879  59.051  57.642  1.00 67.07           C  
ANISOU 1140  CG  TYR A 180     7670   9361   8454   -323    732   -462       C  
ATOM   1141  CD1 TYR A 180      12.847  59.636  58.904  1.00 61.97           C  
ANISOU 1141  CD1 TYR A 180     7061   8720   7764   -384    783   -503       C  
ATOM   1142  CD2 TYR A 180      11.832  59.327  56.764  1.00 68.49           C  
ANISOU 1142  CD2 TYR A 180     7762   9520   8739   -318    764   -486       C  
ATOM   1143  CE1 TYR A 180      11.799  60.462  59.286  1.00 55.33           C  
ANISOU 1143  CE1 TYR A 180     6168   7867   6988   -442    874   -570       C  
ATOM   1144  CE2 TYR A 180      10.776  60.149  57.141  1.00 64.71           C  
ANISOU 1144  CE2 TYR A 180     7227   9027   8334   -371    845   -553       C  
ATOM   1145  CZ  TYR A 180      10.766  60.711  58.406  1.00 65.23           C  
ANISOU 1145  CZ  TYR A 180     7326   9100   8359   -434    905   -596       C  
ATOM   1146  OH  TYR A 180       9.726  61.533  58.785  1.00 72.69           O  
ANISOU 1146  OH  TYR A 180     8209  10025   9386   -492    993   -669       O  
ATOM   1147  N   ALA A 181      17.363  58.042  55.986  1.00 57.25           N  
ANISOU 1147  N   ALA A 181     6459   8156   7138    -99    439   -306       N  
ATOM   1148  CA  ALA A 181      18.618  57.287  56.025  1.00 55.36           C  
ANISOU 1148  CA  ALA A 181     6267   7910   6855    -59    358   -269       C  
ATOM   1149  C   ALA A 181      19.545  57.816  57.124  1.00 55.49           C  
ANISOU 1149  C   ALA A 181     6316   7938   6829    -66    323   -287       C  
ATOM   1150  O   ALA A 181      19.705  59.030  57.286  1.00 53.39           O  
ANISOU 1150  O   ALA A 181     5993   7692   6601    -66    347   -322       O  
ATOM   1151  CB  ALA A 181      19.323  57.348  54.669  1.00 42.95           C  
ANISOU 1151  CB  ALA A 181     4630   6335   5353      9    321   -249       C  
ATOM   1152  N   GLY A 182      20.145  56.904  57.882  1.00 51.39           N  
ANISOU 1152  N   GLY A 182     5890   7403   6233    -72    263   -262       N  
ATOM   1153  CA  GLY A 182      21.005  57.304  58.980  1.00 50.37           C  
ANISOU 1153  CA  GLY A 182     5805   7276   6055    -80    215   -278       C  
ATOM   1154  C   GLY A 182      21.724  56.127  59.617  1.00 65.27           C  
ANISOU 1154  C   GLY A 182     7800   9135   7866    -76    125   -243       C  
ATOM   1155  O   GLY A 182      21.747  55.015  59.080  1.00 63.25           O  
ANISOU 1155  O   GLY A 182     7568   8858   7607    -54     95   -205       O  
ATOM   1156  N   LEU A 183      22.301  56.390  60.792  1.00 69.75           N  
ANISOU 1156  N   LEU A 183     8434   9696   8371    -97     79   -257       N  
ATOM   1157  CA  LEU A 183      23.082  55.412  61.540  1.00 55.17           C  
ANISOU 1157  CA  LEU A 183     6698   7814   6450    -92    -26   -228       C  
ATOM   1158  C   LEU A 183      22.283  54.833  62.698  1.00 54.75           C  
ANISOU 1158  C   LEU A 183     6791   7742   6272   -173      1   -219       C  
ATOM   1159  O   LEU A 183      21.474  55.527  63.315  1.00 67.88           O  
ANISOU 1159  O   LEU A 183     8472   9419   7900   -236     87   -253       O  
ATOM   1160  CB  LEU A 183      24.361  56.053  62.066  1.00 63.97           C  
ANISOU 1160  CB  LEU A 183     7801   8925   7581    -59   -114   -249       C  
ATOM   1161  CG  LEU A 183      25.170  56.605  60.900  1.00 57.70           C  
ANISOU 1161  CG  LEU A 183     6866   8143   6915     17   -128   -263       C  
ATOM   1162  CD1 LEU A 183      26.224  57.521  61.386  1.00 50.31           C  
ANISOU 1162  CD1 LEU A 183     5895   7210   6012     42   -183   -301       C  
ATOM   1163  CD2 LEU A 183      25.756  55.438  60.133  1.00 51.20           C  
ANISOU 1163  CD2 LEU A 183     6039   7286   6128     68   -195   -226       C  
ATOM   1164  N   ARG A 184      22.509  53.550  62.979  1.00 55.98           N  
ANISOU 1164  N   ARG A 184     7050   7857   6361   -173    -68   -177       N  
ATOM   1165  CA  ARG A 184      21.871  52.865  64.096  1.00 57.66           C  
ANISOU 1165  CA  ARG A 184     7424   8040   6444   -250    -52   -165       C  
ATOM   1166  C   ARG A 184      22.903  51.994  64.804  1.00 63.35           C  
ANISOU 1166  C   ARG A 184     8264   8713   7093   -232   -194   -129       C  
ATOM   1167  O   ARG A 184      23.713  51.330  64.154  1.00 71.81           O  
ANISOU 1167  O   ARG A 184     9297   9766   8220   -165   -284   -100       O  
ATOM   1168  CB  ARG A 184      20.686  52.009  63.633  1.00 56.96           C  
ANISOU 1168  CB  ARG A 184     7355   7944   6343   -284     35   -146       C  
ATOM   1169  CG  ARG A 184      19.790  51.501  64.756  1.00 61.51           C  
ANISOU 1169  CG  ARG A 184     8088   8490   6793   -379     94   -149       C  
ATOM   1170  CD  ARG A 184      18.934  50.287  64.331  1.00 73.74           C  
ANISOU 1170  CD  ARG A 184     9677  10016   8326   -398    142   -120       C  
ATOM   1171  NE  ARG A 184      18.283  50.470  63.027  1.00 90.29           N  
ANISOU 1171  NE  ARG A 184    11624  12142  10538   -364    213   -131       N  
ATOM   1172  CZ  ARG A 184      17.040  50.924  62.845  1.00 86.56           C  
ANISOU 1172  CZ  ARG A 184    11104  11683  10103   -412    340   -171       C  
ATOM   1173  NH1 ARG A 184      16.270  51.243  63.884  1.00 87.31           N  
ANISOU 1173  NH1 ARG A 184    11279  11764  10131   -501    426   -210       N  
ATOM   1174  NH2 ARG A 184      16.563  51.058  61.612  1.00 76.14           N  
ANISOU 1174  NH2 ARG A 184     9654  10384   8891   -372    378   -176       N  
ATOM   1175  N   SER A 185      22.878  52.013  66.134  1.00 57.72           N  
ANISOU 1175  N   SER A 185     7698   7974   6260   -295   -217   -135       N  
ATOM   1176  CA  SER A 185      23.717  51.122  66.916  1.00 58.99           C  
ANISOU 1176  CA  SER A 185     7999   8078   6337   -288   -358    -99       C  
ATOM   1177  C   SER A 185      23.292  49.669  66.722  1.00 63.28           C  
ANISOU 1177  C   SER A 185     8628   8584   6833   -298   -366    -49       C  
ATOM   1178  O   SER A 185      22.152  49.375  66.364  1.00 80.98           O  
ANISOU 1178  O   SER A 185    10863  10838   9067   -339   -245    -49       O  
ATOM   1179  CB  SER A 185      23.641  51.493  68.393  1.00 66.87           C  
ANISOU 1179  CB  SER A 185     9155   9053   7201   -365   -369   -116       C  
ATOM   1180  OG  SER A 185      24.384  52.673  68.640  1.00 87.49           O  
ANISOU 1180  OG  SER A 185    11699  11688   9857   -340   -409   -155       O  
ATOM   1181  N   ASN A 186      24.224  48.749  66.959  1.00 58.36           N  
ANISOU 1181  N   ASN A 186     8080   7910   6185   -260   -513    -10       N  
ATOM   1182  CA  ASN A 186      23.923  47.320  66.888  1.00 59.21           C  
ANISOU 1182  CA  ASN A 186     8283   7974   6240   -270   -535     40       C  
ATOM   1183  C   ASN A 186      24.454  46.612  68.139  1.00 63.50           C  
ANISOU 1183  C   ASN A 186     9029   8446   6651   -300   -664     71       C  
ATOM   1184  O   ASN A 186      25.062  47.225  69.033  1.00 60.94           O  
ANISOU 1184  O   ASN A 186     8770   8105   6279   -311   -740     53       O  
ATOM   1185  CB  ASN A 186      24.457  46.678  65.587  1.00 59.01           C  
ANISOU 1185  CB  ASN A 186     8128   7952   6343   -183   -581     64       C  
ATOM   1186  CG  ASN A 186      25.995  46.748  65.433  1.00 60.87           C  
ANISOU 1186  CG  ASN A 186     8302   8162   6663    -99   -741     63       C  
ATOM   1187  OD1 ASN A 186      26.759  46.403  66.342  1.00 59.65           O  
ANISOU 1187  OD1 ASN A 186     8262   7953   6450    -97   -876     78       O  
ATOM   1188  ND2 ASN A 186      26.441  47.162  64.253  1.00 58.23           N  
ANISOU 1188  ND2 ASN A 186     7790   7860   6474    -32   -725     44       N  
ATOM   1189  N   GLN A 187      24.185  45.302  68.198  1.00 70.50           N  
ANISOU 1189  N   GLN A 187    10023   9286   7478   -315   -688    118       N  
ATOM   1190  CA  GLN A 187      24.549  44.466  69.338  1.00 72.08           C  
ANISOU 1190  CA  GLN A 187    10437   9408   7541   -349   -806    156       C  
ATOM   1191  C   GLN A 187      26.049  44.258  69.470  1.00 75.96           C  
ANISOU 1191  C   GLN A 187    10924   9854   8083   -271  -1014    172       C  
ATOM   1192  O   GLN A 187      26.514  43.877  70.551  1.00 89.39           O  
ANISOU 1192  O   GLN A 187    12801  11487   9674   -296  -1138    193       O  
ATOM   1193  CB  GLN A 187      23.888  43.100  69.213  1.00 76.83           C  
ANISOU 1193  CB  GLN A 187    11136   9973   8084   -377   -774    201       C  
ATOM   1194  CG  GLN A 187      24.453  42.259  68.082  1.00 78.91           C  
ANISOU 1194  CG  GLN A 187    11280  10232   8471   -288   -843    232       C  
ATOM   1195  CD  GLN A 187      23.415  41.336  67.495  1.00 86.63           C  
ANISOU 1195  CD  GLN A 187    12261  11214   9439   -315   -729    256       C  
ATOM   1196  OE1 GLN A 187      22.405  41.799  66.972  1.00 96.28           O  
ANISOU 1196  OE1 GLN A 187    13399  12490  10693   -345   -571    226       O  
ATOM   1197  NE2 GLN A 187      23.652  40.024  67.577  1.00 81.98           N  
ANISOU 1197  NE2 GLN A 187    11769  10565   8813   -304   -813    306       N  
ATOM   1198  N   TRP A 188      26.809  44.458  68.399  1.00 68.75           N  
ANISOU 1198  N   TRP A 188     9819   8967   7335   -179  -1057    159       N  
ATOM   1199  CA  TRP A 188      28.253  44.337  68.479  1.00 70.17           C  
ANISOU 1199  CA  TRP A 188     9971   9099   7590   -103  -1247    160       C  
ATOM   1200  C   TRP A 188      28.922  45.604  69.001  1.00 70.09           C  
ANISOU 1200  C   TRP A 188     9925   9105   7603    -92  -1295    112       C  
ATOM   1201  O   TRP A 188      30.147  45.610  69.164  1.00 67.99           O  
ANISOU 1201  O   TRP A 188     9635   8794   7405    -30  -1458    102       O  
ATOM   1202  CB  TRP A 188      28.838  43.980  67.106  1.00 67.23           C  
ANISOU 1202  CB  TRP A 188     9412   8739   7395    -14  -1265    159       C  
ATOM   1203  CG  TRP A 188      28.046  42.982  66.281  1.00 72.79           C  
ANISOU 1203  CG  TRP A 188    10098   9452   8106    -20  -1174    195       C  
ATOM   1204  CD1 TRP A 188      27.257  43.261  65.206  1.00 74.26           C  
ANISOU 1204  CD1 TRP A 188    10153   9704   8358    -20  -1019    181       C  
ATOM   1205  CD2 TRP A 188      28.017  41.552  66.433  1.00 77.04           C  
ANISOU 1205  CD2 TRP A 188    10749   9929   8593    -24  -1243    248       C  
ATOM   1206  NE1 TRP A 188      26.718  42.106  64.695  1.00 77.19           N  
ANISOU 1206  NE1 TRP A 188    10548  10061   8720    -25   -984    221       N  
ATOM   1207  CE2 TRP A 188      27.172  41.042  65.429  1.00 76.97           C  
ANISOU 1207  CE2 TRP A 188    10667   9957   8621    -28  -1115    262       C  
ATOM   1208  CE3 TRP A 188      28.616  40.658  67.324  1.00 91.16           C  
ANISOU 1208  CE3 TRP A 188    12698  11630  10307    -25  -1406    285       C  
ATOM   1209  CZ2 TRP A 188      26.910  39.672  65.289  1.00 84.38           C  
ANISOU 1209  CZ2 TRP A 188    11681  10853   9527    -33  -1135    310       C  
ATOM   1210  CZ3 TRP A 188      28.356  39.296  67.187  1.00 90.69           C  
ANISOU 1210  CZ3 TRP A 188    12718  11526  10214    -30  -1428    336       C  
ATOM   1211  CH2 TRP A 188      27.509  38.819  66.177  1.00 85.96           C  
ANISOU 1211  CH2 TRP A 188    12037  10971   9656    -34  -1289    347       C  
ATOM   1212  N   GLY A 189      28.163  46.670  69.261  1.00 63.64           N  
ANISOU 1212  N   GLY A 189     9095   8344   6739   -148  -1160     77       N  
ATOM   1213  CA  GLY A 189      28.744  47.941  69.652  1.00 61.01           C  
ANISOU 1213  CA  GLY A 189     8707   8034   6438   -137  -1189     27       C  
ATOM   1214  C   GLY A 189      29.165  48.852  68.516  1.00 62.01           C  
ANISOU 1214  C   GLY A 189     8600   8220   6740    -67  -1138    -16       C  
ATOM   1215  O   GLY A 189      29.957  49.775  68.745  1.00 66.03           O  
ANISOU 1215  O   GLY A 189     9047   8735   7305    -36  -1197    -57       O  
ATOM   1216  N   ARG A 190      28.659  48.632  67.304  1.00 59.83           N  
ANISOU 1216  N   ARG A 190     8198   7983   6550    -43  -1032    -10       N  
ATOM   1217  CA  ARG A 190      29.058  49.347  66.098  1.00 58.69           C  
ANISOU 1217  CA  ARG A 190     7845   7884   6569     22   -984    -44       C  
ATOM   1218  C   ARG A 190      27.846  50.088  65.534  1.00 58.92           C  
ANISOU 1218  C   ARG A 190     7800   7986   6602    -19   -795    -62       C  
ATOM   1219  O   ARG A 190      26.748  50.028  66.084  1.00 59.49           O  
ANISOU 1219  O   ARG A 190     7972   8070   6564    -95   -705    -54       O  
ATOM   1220  CB  ARG A 190      29.673  48.373  65.078  1.00 59.76           C  
ANISOU 1220  CB  ARG A 190     7901   7990   6816     92  -1044    -22       C  
ATOM   1221  CG  ARG A 190      30.887  47.616  65.636  1.00 57.75           C  
ANISOU 1221  CG  ARG A 190     7712   7654   6577    136  -1241     -9       C  
ATOM   1222  CD  ARG A 190      31.240  46.302  64.920  1.00 59.74           C  
ANISOU 1222  CD  ARG A 190     7944   7860   6894    180  -1301     27       C  
ATOM   1223  NE  ARG A 190      32.404  45.652  65.555  1.00 61.46           N  
ANISOU 1223  NE  ARG A 190     8226   7992   7135    220  -1501     34       N  
ATOM   1224  CZ  ARG A 190      33.544  45.320  64.939  1.00 59.60           C  
ANISOU 1224  CZ  ARG A 190     7879   7710   7054    297  -1601     13       C  
ATOM   1225  NH1 ARG A 190      33.715  45.542  63.645  1.00 61.19           N  
ANISOU 1225  NH1 ARG A 190     7907   7944   7397    339  -1514    -14       N  
ATOM   1226  NH2 ARG A 190      34.529  44.762  65.621  1.00 61.27           N  
ANISOU 1226  NH2 ARG A 190     8158   7838   7285    329  -1790     16       N  
ATOM   1227  N   SER A 191      28.050  50.792  64.427  1.00 57.80           N  
ANISOU 1227  N   SER A 191     7484   7885   6592     31   -737    -92       N  
ATOM   1228  CA  SER A 191      27.010  51.596  63.796  1.00 64.15           C  
ANISOU 1228  CA  SER A 191     8201   8751   7420      3   -576   -112       C  
ATOM   1229  C   SER A 191      26.681  51.024  62.423  1.00 61.18           C  
ANISOU 1229  C   SER A 191     7731   8386   7126     38   -519    -92       C  
ATOM   1230  O   SER A 191      27.580  50.827  61.601  1.00 69.90           O  
ANISOU 1230  O   SER A 191     8746   9477   8337    105   -574    -94       O  
ATOM   1231  CB  SER A 191      27.458  53.056  63.663  1.00 58.68           C  
ANISOU 1231  CB  SER A 191     7394   8096   6805     26   -549   -166       C  
ATOM   1232  OG  SER A 191      27.561  53.674  64.935  1.00 68.07           O  
ANISOU 1232  OG  SER A 191     8671   9282   7910    -18   -580   -188       O  
ATOM   1233  N   SER A 192      25.399  50.757  62.178  1.00 59.25           N  
ANISOU 1233  N   SER A 192     7511   8165   6838    -10   -407    -77       N  
ATOM   1234  CA  SER A 192      24.927  50.364  60.854  1.00 58.85           C  
ANISOU 1234  CA  SER A 192     7369   8130   6861     17   -341    -63       C  
ATOM   1235  C   SER A 192      24.259  51.538  60.162  1.00 63.67           C  
ANISOU 1235  C   SER A 192     7867   8792   7534     11   -226    -98       C  
ATOM   1236  O   SER A 192      23.551  52.333  60.793  1.00 65.66           O  
ANISOU 1236  O   SER A 192     8138   9067   7741    -41   -157   -124       O  
ATOM   1237  CB  SER A 192      23.943  49.200  60.900  1.00 54.03           C  
ANISOU 1237  CB  SER A 192     6849   7504   6178    -25   -301    -24       C  
ATOM   1238  OG  SER A 192      24.350  48.240  61.841  1.00 71.07           O  
ANISOU 1238  OG  SER A 192     9144   9612   8247    -40   -398      7       O  
ATOM   1239  N   CYS A 193      24.533  51.649  58.865  1.00 57.75           N  
ANISOU 1239  N   CYS A 193     7002   8053   6889     64   -208   -100       N  
ATOM   1240  CA  CYS A 193      23.773  52.495  57.967  1.00 52.40           C  
ANISOU 1240  CA  CYS A 193     6227   7413   6271     62   -104   -121       C  
ATOM   1241  C   CYS A 193      22.505  51.744  57.572  1.00 62.21           C  
ANISOU 1241  C   CYS A 193     7499   8656   7484     27    -34    -97       C  
ATOM   1242  O   CYS A 193      22.584  50.606  57.097  1.00 62.43           O  
ANISOU 1242  O   CYS A 193     7550   8660   7511     45    -64    -62       O  
ATOM   1243  CB  CYS A 193      24.629  52.841  56.758  1.00 47.73           C  
ANISOU 1243  CB  CYS A 193     5522   6820   5792    127   -119   -131       C  
ATOM   1244  SG  CYS A 193      23.875  53.917  55.569  1.00 57.43           S  
ANISOU 1244  SG  CYS A 193     6642   8084   7096    132    -12   -154       S  
ATOM   1245  N   THR A 194      21.346  52.348  57.812  1.00 59.52           N  
ANISOU 1245  N   THR A 194     7155   8338   7122    -24     58   -120       N  
ATOM   1246  CA  THR A 194      20.063  51.745  57.425  1.00 71.23           C  
ANISOU 1246  CA  THR A 194     8652   9819   8594    -58    131   -109       C  
ATOM   1247  C   THR A 194      19.061  52.876  57.210  1.00 65.14           C  
ANISOU 1247  C   THR A 194     7808   9074   7867    -87    226   -150       C  
ATOM   1248  O   THR A 194      19.446  54.040  57.050  1.00 66.38           O  
ANISOU 1248  O   THR A 194     7893   9253   8076    -67    232   -178       O  
ATOM   1249  CB  THR A 194      19.597  50.703  58.468  1.00 76.32           C  
ANISOU 1249  CB  THR A 194     9432  10437   9131   -113    129    -89       C  
ATOM   1250  OG1 THR A 194      18.394  50.048  58.007  1.00 75.51           O  
ANISOU 1250  OG1 THR A 194     9332  10326   9030   -142    201    -82       O  
ATOM   1251  CG2 THR A 194      19.367  51.355  59.860  1.00 59.21           C  
ANISOU 1251  CG2 THR A 194     7339   8271   6886   -177    156   -120       C  
ATOM   1252  N   ILE A 195      17.776  52.556  57.192  1.00 61.64           N  
ANISOU 1252  N   ILE A 195     7382   8626   7415   -133    301   -158       N  
ATOM   1253  CA  ILE A 195      16.742  53.583  57.235  1.00 62.06           C  
ANISOU 1253  CA  ILE A 195     7376   8693   7510   -171    390   -206       C  
ATOM   1254  C   ILE A 195      16.200  53.636  58.652  1.00 55.15           C  
ANISOU 1254  C   ILE A 195     6592   7808   6554   -250    440   -233       C  
ATOM   1255  O   ILE A 195      15.731  52.626  59.191  1.00 57.76           O  
ANISOU 1255  O   ILE A 195     7018   8113   6815   -293    458   -220       O  
ATOM   1256  CB  ILE A 195      15.629  53.334  56.210  1.00 66.49           C  
ANISOU 1256  CB  ILE A 195     7879   9246   8138   -170    441   -210       C  
ATOM   1257  CG1 ILE A 195      16.252  53.007  54.857  1.00 62.49           C  
ANISOU 1257  CG1 ILE A 195     7317   8740   7685    -98    385   -174       C  
ATOM   1258  CG2 ILE A 195      14.806  54.596  56.054  1.00 61.61           C  
ANISOU 1258  CG2 ILE A 195     7175   8640   7595   -191    509   -261       C  
ATOM   1259  CD1 ILE A 195      17.170  54.103  54.354  1.00 46.16           C  
ANISOU 1259  CD1 ILE A 195     5175   6691   5673    -50    354   -183       C  
ATOM   1260  N   ASN A 196      16.319  54.799  59.277  1.00 60.22           N  
ANISOU 1260  N   ASN A 196     7211   8468   7201   -273    465   -273       N  
ATOM   1261  CA  ASN A 196      15.821  54.940  60.633  1.00 69.36           C  
ANISOU 1261  CA  ASN A 196     8460   9615   8280   -356    521   -305       C  
ATOM   1262  C   ASN A 196      14.302  54.920  60.616  1.00 70.93           C  
ANISOU 1262  C   ASN A 196     8640   9796   8512   -417    635   -345       C  
ATOM   1263  O   ASN A 196      13.670  55.369  59.657  1.00 80.48           O  
ANISOU 1263  O   ASN A 196     9739  11013   9827   -394    669   -364       O  
ATOM   1264  CB  ASN A 196      16.351  56.226  61.267  1.00 63.58           C  
ANISOU 1264  CB  ASN A 196     7702   8905   7550   -364    521   -340       C  
ATOM   1265  CG  ASN A 196      17.829  56.118  61.643  1.00 67.37           C  
ANISOU 1265  CG  ASN A 196     8228   9389   7979   -320    407   -310       C  
ATOM   1266  OD1 ASN A 196      18.301  55.055  62.054  1.00 68.91           O  
ANISOU 1266  OD1 ASN A 196     8528   9558   8095   -318    342   -271       O  
ATOM   1267  ND2 ASN A 196      18.567  57.215  61.489  1.00 73.47           N  
ANISOU 1267  ND2 ASN A 196     8921  10188   8805   -281    381   -330       N  
ATOM   1268  N   TRP A 197      13.716  54.354  61.656  1.00 78.43           N  
ANISOU 1268  N   TRP A 197     9706  10717   9377   -496    691   -360       N  
ATOM   1269  CA  TRP A 197      12.267  54.356  61.755  1.00 82.76           C  
ANISOU 1269  CA  TRP A 197    10237  11241   9966   -563    811   -411       C  
ATOM   1270  C   TRP A 197      11.773  55.794  61.902  1.00 83.23           C  
ANISOU 1270  C   TRP A 197    10202  11316  10106   -591    882   -477       C  
ATOM   1271  O   TRP A 197      12.238  56.522  62.797  1.00 82.09           O  
ANISOU 1271  O   TRP A 197    10095  11184   9913   -621    886   -497       O  
ATOM   1272  CB  TRP A 197      11.799  53.510  62.936  1.00 81.05           C  
ANISOU 1272  CB  TRP A 197    10177  10984   9634   -651    868   -420       C  
ATOM   1273  CG  TRP A 197      11.997  52.053  62.733  1.00 71.85           C  
ANISOU 1273  CG  TRP A 197     9097   9796   8405   -632    817   -362       C  
ATOM   1274  CD1 TRP A 197      12.685  51.455  61.723  1.00 74.01           C  
ANISOU 1274  CD1 TRP A 197     9328  10085   8708   -546    720   -304       C  
ATOM   1275  CD2 TRP A 197      11.506  50.997  63.568  1.00 75.43           C  
ANISOU 1275  CD2 TRP A 197     9699  10204   8757   -704    866   -359       C  
ATOM   1276  NE1 TRP A 197      12.652  50.088  61.871  1.00 72.22           N  
ANISOU 1276  NE1 TRP A 197     9205   9827   8408   -557    701   -264       N  
ATOM   1277  CE2 TRP A 197      11.931  49.781  62.995  1.00 77.48           C  
ANISOU 1277  CE2 TRP A 197     9992  10454   8990   -652    787   -295       C  
ATOM   1278  CE3 TRP A 197      10.746  50.961  64.744  1.00 81.05           C  
ANISOU 1278  CE3 TRP A 197    10524  10877   9395   -813    974   -407       C  
ATOM   1279  CZ2 TRP A 197      11.623  48.539  63.560  1.00 77.08           C  
ANISOU 1279  CZ2 TRP A 197    10084  10360   8845   -701    808   -274       C  
ATOM   1280  CZ3 TRP A 197      10.436  49.725  65.303  1.00 81.31           C  
ANISOU 1280  CZ3 TRP A 197    10705  10863   9328   -865   1000   -387       C  
ATOM   1281  CH2 TRP A 197      10.872  48.533  64.708  1.00 80.78           C  
ANISOU 1281  CH2 TRP A 197    10665  10789   9237   -807    914   -320       C  
ATOM   1282  N   PRO A 198      10.854  56.244  61.052  1.00 72.06           N  
ANISOU 1282  N   PRO A 198     8664   9897   8816   -581    932   -512       N  
ATOM   1283  CA  PRO A 198      10.383  57.633  61.149  1.00 73.23           C  
ANISOU 1283  CA  PRO A 198     8714  10054   9054   -604    993   -575       C  
ATOM   1284  C   PRO A 198       9.526  57.809  62.396  1.00 78.72           C  
ANISOU 1284  C   PRO A 198     9473  10719   9717   -714   1113   -643       C  
ATOM   1285  O   PRO A 198       8.621  57.012  62.661  1.00 88.13           O  
ANISOU 1285  O   PRO A 198    10716  11870  10898   -771   1185   -665       O  
ATOM   1286  CB  PRO A 198       9.570  57.826  59.861  1.00 69.67           C  
ANISOU 1286  CB  PRO A 198     8132   9594   8745   -563   1000   -590       C  
ATOM   1287  CG  PRO A 198       9.795  56.521  59.031  1.00 62.76           C  
ANISOU 1287  CG  PRO A 198     7291   8713   7843   -511    933   -525       C  
ATOM   1288  CD  PRO A 198      10.138  55.475  60.021  1.00 63.80           C  
ANISOU 1288  CD  PRO A 198     7571   8832   7838   -554    934   -499       C  
ATOM   1289  N   GLY A 199       9.838  58.840  63.180  1.00 79.04           N  
ANISOU 1289  N   GLY A 199     9515  10776   9740   -748   1140   -678       N  
ATOM   1290  CA  GLY A 199       9.210  59.019  64.479  1.00 80.12           C  
ANISOU 1290  CA  GLY A 199     9736  10883   9825   -859   1253   -740       C  
ATOM   1291  C   GLY A 199       9.455  57.886  65.463  1.00 82.35           C  
ANISOU 1291  C   GLY A 199    10207  11138   9945   -914   1255   -712       C  
ATOM   1292  O   GLY A 199       8.782  57.802  66.497  1.00 94.06           O  
ANISOU 1292  O   GLY A 199    11782  12582  11375  -1018   1363   -764       O  
ATOM   1293  N   GLU A 200      10.409  57.004  65.151  1.00 80.03           N  
ANISOU 1293  N   GLU A 200     9976  10858   9574   -849   1137   -631       N  
ATOM   1294  CA  GLU A 200      10.766  55.853  65.989  1.00 86.41           C  
ANISOU 1294  CA  GLU A 200    10968  11636  10227   -888   1112   -591       C  
ATOM   1295  C   GLU A 200       9.620  54.841  66.123  1.00 80.64           C  
ANISOU 1295  C   GLU A 200    10301  10854   9485   -954   1209   -613       C  
ATOM   1296  O   GLU A 200       9.547  54.094  67.102  1.00 85.54           O  
ANISOU 1296  O   GLU A 200    11089  11436   9977  -1026   1241   -608       O  
ATOM   1297  CB  GLU A 200      11.253  56.305  67.374  1.00 84.57           C  
ANISOU 1297  CB  GLU A 200    10863  11396   9872   -956   1122   -610       C  
ATOM   1298  N   SER A 201       8.741  54.771  65.131  1.00 74.34           N  
ANISOU 1298  N   SER A 201     9376  10051   8818   -930   1251   -636       N  
ATOM   1299  CA  SER A 201       7.538  53.946  65.191  1.00 86.23           C  
ANISOU 1299  CA  SER A 201    10915  11506  10344   -993   1356   -672       C  
ATOM   1300  C   SER A 201       7.637  52.806  64.175  1.00 81.68           C  
ANISOU 1300  C   SER A 201    10321  10930   9783   -921   1282   -610       C  
ATOM   1301  O   SER A 201       7.838  53.051  62.979  1.00 81.63           O  
ANISOU 1301  O   SER A 201    10184  10955   9877   -832   1211   -585       O  
ATOM   1302  CB  SER A 201       6.292  54.805  64.943  1.00 90.54           C  
ANISOU 1302  CB  SER A 201    11323  12031  11046  -1034   1474   -766       C  
ATOM   1303  OG  SER A 201       5.230  54.048  64.387  1.00 83.27           O  
ANISOU 1303  OG  SER A 201    10363  11071  10206  -1046   1533   -791       O  
ATOM   1304  N   GLY A 202       7.502  51.565  64.656  1.00 72.15           N  
ANISOU 1304  N   GLY A 202     9255   9686   8474   -962   1300   -585       N  
ATOM   1305  CA  GLY A 202       7.493  50.397  63.790  1.00 60.82           C  
ANISOU 1305  CA  GLY A 202     7813   8245   7050   -906   1246   -532       C  
ATOM   1306  C   GLY A 202       6.371  50.389  62.774  1.00 65.48           C  
ANISOU 1306  C   GLY A 202     8262   8822   7794   -890   1302   -575       C  
ATOM   1307  O   GLY A 202       6.434  49.609  61.813  1.00 54.71           O  
ANISOU 1307  O   GLY A 202     6860   7464   6462   -826   1242   -530       O  
ATOM   1308  N   ALA A 203       5.357  51.245  62.960  1.00 71.36           N  
ANISOU 1308  N   ALA A 203     8926   9546   8641   -947   1413   -664       N  
ATOM   1309  CA  ALA A 203       4.279  51.353  61.985  1.00 69.43           C  
ANISOU 1309  CA  ALA A 203     8536   9283   8562   -928   1453   -713       C  
ATOM   1310  C   ALA A 203       4.769  52.000  60.700  1.00 65.63           C  
ANISOU 1310  C   ALA A 203     7911   8848   8177   -821   1340   -676       C  
ATOM   1311  O   ALA A 203       4.458  51.527  59.597  1.00 57.82           O  
ANISOU 1311  O   ALA A 203     6848   7855   7265   -764   1298   -657       O  
ATOM   1312  CB  ALA A 203       3.103  52.145  62.563  1.00 60.72           C  
ANISOU 1312  CB  ALA A 203     7379   8137   7557  -1018   1597   -824       C  
ATOM   1313  N   TRP A 204       5.536  53.090  60.820  1.00 60.94           N  
ANISOU 1313  N   TRP A 204     7283   8295   7578   -794   1294   -667       N  
ATOM   1314  CA  TRP A 204       5.972  53.804  59.625  1.00 54.67           C  
ANISOU 1314  CA  TRP A 204     6360   7538   6876   -700   1200   -639       C  
ATOM   1315  C   TRP A 204       7.050  53.030  58.876  1.00 54.42           C  
ANISOU 1315  C   TRP A 204     6360   7537   6779   -615   1077   -546       C  
ATOM   1316  O   TRP A 204       7.123  53.110  57.644  1.00 53.14           O  
ANISOU 1316  O   TRP A 204     6108   7388   6696   -542   1012   -521       O  
ATOM   1317  CB  TRP A 204       6.441  55.216  59.998  1.00 61.47           C  
ANISOU 1317  CB  TRP A 204     7172   8429   7755   -700   1197   -664       C  
ATOM   1318  CG  TRP A 204       5.287  56.136  60.304  1.00 63.90           C  
ANISOU 1318  CG  TRP A 204     7395   8705   8181   -764   1305   -761       C  
ATOM   1319  CD1 TRP A 204       4.961  56.666  61.519  1.00 74.18           C  
ANISOU 1319  CD1 TRP A 204     8741   9988   9455   -855   1407   -824       C  
ATOM   1320  CD2 TRP A 204       4.286  56.595  59.386  1.00 63.84           C  
ANISOU 1320  CD2 TRP A 204     7244   8670   8342   -744   1320   -810       C  
ATOM   1321  NE1 TRP A 204       3.825  57.432  61.412  1.00 80.09           N  
ANISOU 1321  NE1 TRP A 204     9374  10701  10354   -893   1492   -913       N  
ATOM   1322  CE2 TRP A 204       3.390  57.400  60.113  1.00 71.51           C  
ANISOU 1322  CE2 TRP A 204     8170   9607   9393   -824   1434   -906       C  
ATOM   1323  CE3 TRP A 204       4.056  56.392  58.021  1.00 67.36           C  
ANISOU 1323  CE3 TRP A 204     7601   9112   8880   -668   1245   -784       C  
ATOM   1324  CZ2 TRP A 204       2.292  58.014  59.521  1.00 73.93           C  
ANISOU 1324  CZ2 TRP A 204     8337   9874   9879   -826   1468   -977       C  
ATOM   1325  CZ3 TRP A 204       2.969  57.005  57.433  1.00 65.66           C  
ANISOU 1325  CZ3 TRP A 204     7258   8858   8832   -670   1272   -850       C  
ATOM   1326  CH2 TRP A 204       2.100  57.809  58.183  1.00 72.03           C  
ANISOU 1326  CH2 TRP A 204     8013   9629   9727   -746   1379   -947       C  
ATOM   1327  N   TYR A 205       7.886  52.267  59.584  1.00 56.42           N  
ANISOU 1327  N   TYR A 205     6746   7798   6894   -624   1043   -496       N  
ATOM   1328  CA  TYR A 205       8.792  51.379  58.870  1.00 54.44           C  
ANISOU 1328  CA  TYR A 205     6523   7565   6598   -550    936   -416       C  
ATOM   1329  C   TYR A 205       8.002  50.344  58.086  1.00 51.71           C  
ANISOU 1329  C   TYR A 205     6157   7191   6298   -540    951   -409       C  
ATOM   1330  O   TYR A 205       8.329  50.041  56.928  1.00 55.84           O  
ANISOU 1330  O   TYR A 205     6624   7729   6865   -467    877   -367       O  
ATOM   1331  CB  TYR A 205       9.787  50.695  59.822  1.00 56.10           C  
ANISOU 1331  CB  TYR A 205     6880   7776   6659   -564    889   -367       C  
ATOM   1332  CG  TYR A 205      10.659  49.654  59.122  1.00 54.46           C  
ANISOU 1332  CG  TYR A 205     6700   7577   6417   -493    785   -291       C  
ATOM   1333  CD1 TYR A 205      11.723  50.037  58.295  1.00 57.57           C  
ANISOU 1333  CD1 TYR A 205     7025   8004   6844   -409    686   -251       C  
ATOM   1334  CD2 TYR A 205      10.405  48.298  59.267  1.00 54.63           C  
ANISOU 1334  CD2 TYR A 205     6812   7567   6378   -513    792   -263       C  
ATOM   1335  CE1 TYR A 205      12.519  49.089  57.641  1.00 65.47           C  
ANISOU 1335  CE1 TYR A 205     8045   9007   7824   -349    599   -189       C  
ATOM   1336  CE2 TYR A 205      11.185  47.343  58.625  1.00 72.85           C  
ANISOU 1336  CE2 TYR A 205     9138   9879   8661   -450    700   -197       C  
ATOM   1337  CZ  TYR A 205      12.241  47.740  57.808  1.00 78.27           C  
ANISOU 1337  CZ  TYR A 205     9753  10599   9389   -369    604   -162       C  
ATOM   1338  OH  TYR A 205      13.003  46.772  57.173  1.00 84.87           O  
ANISOU 1338  OH  TYR A 205    10603  11432  10210   -312    522   -104       O  
ATOM   1339  N   THR A 206       6.938  49.816  58.689  1.00 51.01           N  
ANISOU 1339  N   THR A 206     6116   7060   6205   -616   1052   -456       N  
ATOM   1340  CA  THR A 206       6.155  48.786  58.019  1.00 51.73           C  
ANISOU 1340  CA  THR A 206     6192   7121   6341   -610   1072   -455       C  
ATOM   1341  C   THR A 206       5.487  49.336  56.768  1.00 47.68           C  
ANISOU 1341  C   THR A 206     5527   6608   5981   -563   1057   -483       C  
ATOM   1342  O   THR A 206       5.555  48.725  55.698  1.00 47.52           O  
ANISOU 1342  O   THR A 206     5471   6591   5993   -504    995   -444       O  
ATOM   1343  CB  THR A 206       5.135  48.192  58.985  1.00 51.37           C  
ANISOU 1343  CB  THR A 206     6227   7024   6267   -708   1196   -510       C  
ATOM   1344  OG1 THR A 206       5.840  47.428  59.965  1.00 62.97           O  
ANISOU 1344  OG1 THR A 206     7859   8487   7578   -741   1185   -466       O  
ATOM   1345  CG2 THR A 206       4.204  47.258  58.253  1.00 59.74           C  
ANISOU 1345  CG2 THR A 206     7250   8051   7399   -703   1226   -524       C  
ATOM   1346  N   GLY A 207       4.883  50.519  56.873  1.00 51.86           N  
ANISOU 1346  N   GLY A 207     5968   7130   6605   -587   1106   -550       N  
ATOM   1347  CA  GLY A 207       4.328  51.173  55.699  1.00 46.69           C  
ANISOU 1347  CA  GLY A 207     5174   6470   6095   -539   1074   -574       C  
ATOM   1348  C   GLY A 207       5.343  51.395  54.596  1.00 45.79           C  
ANISOU 1348  C   GLY A 207     5023   6398   5979   -445    952   -504       C  
ATOM   1349  O   GLY A 207       4.993  51.352  53.416  1.00 44.74           O  
ANISOU 1349  O   GLY A 207     4816   6254   5930   -396    905   -497       O  
ATOM   1350  N   PHE A 208       6.612  51.623  54.962  1.00 53.59           N  
ANISOU 1350  N   PHE A 208     6066   7426   6871   -421    902   -454       N  
ATOM   1351  CA  PHE A 208       7.654  51.871  53.965  1.00 48.87           C  
ANISOU 1351  CA  PHE A 208     5435   6862   6272   -338    799   -394       C  
ATOM   1352  C   PHE A 208       8.058  50.588  53.267  1.00 44.66           C  
ANISOU 1352  C   PHE A 208     4946   6327   5694   -297    742   -333       C  
ATOM   1353  O   PHE A 208       8.348  50.590  52.067  1.00 47.63           O  
ANISOU 1353  O   PHE A 208     5275   6710   6114   -235    678   -301       O  
ATOM   1354  CB  PHE A 208       8.867  52.522  54.620  1.00 54.80           C  
ANISOU 1354  CB  PHE A 208     6222   7649   6949   -329    767   -372       C  
ATOM   1355  CG  PHE A 208      10.121  52.458  53.782  1.00 58.44           C  
ANISOU 1355  CG  PHE A 208     6678   8139   7389   -252    670   -309       C  
ATOM   1356  CD1 PHE A 208      10.377  53.427  52.820  1.00 57.79           C  
ANISOU 1356  CD1 PHE A 208     6508   8068   7381   -201    631   -309       C  
ATOM   1357  CD2 PHE A 208      11.050  51.436  53.968  1.00 57.82           C  
ANISOU 1357  CD2 PHE A 208     6684   8068   7218   -232    620   -254       C  
ATOM   1358  CE1 PHE A 208      11.536  53.375  52.059  1.00 56.09           C  
ANISOU 1358  CE1 PHE A 208     6292   7871   7148   -138    556   -259       C  
ATOM   1359  CE2 PHE A 208      12.199  51.369  53.207  1.00 54.46           C  
ANISOU 1359  CE2 PHE A 208     6247   7660   6787   -166    540   -206       C  
ATOM   1360  CZ  PHE A 208      12.449  52.347  52.251  1.00 56.71           C  
ANISOU 1360  CZ  PHE A 208     6446   7956   7146   -121    513   -210       C  
ATOM   1361  N   ILE A 209       8.076  49.480  53.999  1.00 53.26           N  
ANISOU 1361  N   ILE A 209     6134   7405   6698   -332    768   -316       N  
ATOM   1362  CA  ILE A 209       8.222  48.175  53.358  1.00 54.95           C  
ANISOU 1362  CA  ILE A 209     6384   7610   6884   -302    729   -267       C  
ATOM   1363  C   ILE A 209       7.110  47.948  52.333  1.00 50.38           C  
ANISOU 1363  C   ILE A 209     5728   7003   6409   -290    744   -293       C  
ATOM   1364  O   ILE A 209       7.368  47.516  51.207  1.00 59.08           O  
ANISOU 1364  O   ILE A 209     6805   8109   7534   -235    682   -254       O  
ATOM   1365  CB  ILE A 209       8.268  47.060  54.419  1.00 58.72           C  
ANISOU 1365  CB  ILE A 209     6985   8071   7255   -352    763   -252       C  
ATOM   1366  CG1 ILE A 209       9.695  46.909  54.962  1.00 59.15           C  
ANISOU 1366  CG1 ILE A 209     7119   8149   7207   -330    693   -198       C  
ATOM   1367  CG2 ILE A 209       7.756  45.728  53.857  1.00 65.59           C  
ANISOU 1367  CG2 ILE A 209     7875   8915   8129   -346    768   -232       C  
ATOM   1368  CD1 ILE A 209      10.693  46.486  53.915  1.00 55.62           C  
ANISOU 1368  CD1 ILE A 209     6648   7720   6766   -251    598   -138       C  
ATOM   1369  N   ILE A 210       5.856  48.228  52.702  1.00 52.47           N  
ANISOU 1369  N   ILE A 210     5957   7236   6744   -344    825   -364       N  
ATOM   1370  CA  ILE A 210       4.735  47.967  51.794  1.00 53.48           C  
ANISOU 1370  CA  ILE A 210     6011   7329   6982   -335    834   -397       C  
ATOM   1371  C   ILE A 210       4.842  48.858  50.555  1.00 61.81           C  
ANISOU 1371  C   ILE A 210     6971   8392   8123   -272    758   -390       C  
ATOM   1372  O   ILE A 210       4.723  48.393  49.409  1.00 59.55           O  
ANISOU 1372  O   ILE A 210     6658   8095   7873   -226    701   -364       O  
ATOM   1373  CB  ILE A 210       3.388  48.157  52.527  1.00 45.80           C  
ANISOU 1373  CB  ILE A 210     5010   6311   6082   -410    942   -487       C  
ATOM   1374  CG1 ILE A 210       3.224  47.130  53.650  1.00 54.55           C  
ANISOU 1374  CG1 ILE A 210     6230   7402   7097   -477   1023   -492       C  
ATOM   1375  CG2 ILE A 210       2.207  48.027  51.558  1.00 54.81           C  
ANISOU 1375  CG2 ILE A 210     6057   7409   7360   -396    940   -531       C  
ATOM   1376  CD1 ILE A 210       1.863  47.199  54.427  1.00 52.20           C  
ANISOU 1376  CD1 ILE A 210     5914   7048   6870   -563   1152   -590       C  
ATOM   1377  N   TYR A 211       5.080  50.150  50.781  1.00 47.73           N  
ANISOU 1377  N   TYR A 211     5143   6623   6369   -271    756   -412       N  
ATOM   1378  CA  TYR A 211       5.386  51.115  49.734  1.00 43.28           C  
ANISOU 1378  CA  TYR A 211     4508   6068   5866   -214    683   -399       C  
ATOM   1379  C   TYR A 211       6.461  50.612  48.770  1.00 47.34           C  
ANISOU 1379  C   TYR A 211     5058   6606   6323   -150    599   -322       C  
ATOM   1380  O   TYR A 211       6.256  50.591  47.550  1.00 57.99           O  
ANISOU 1380  O   TYR A 211     6371   7938   7724   -108    544   -308       O  
ATOM   1381  CB  TYR A 211       5.810  52.403  50.434  1.00 51.64           C  
ANISOU 1381  CB  TYR A 211     5545   7150   6925   -229    703   -422       C  
ATOM   1382  CG  TYR A 211       6.274  53.570  49.611  1.00 47.11           C  
ANISOU 1382  CG  TYR A 211     4911   6589   6401   -179    641   -411       C  
ATOM   1383  CD1 TYR A 211       5.361  54.450  49.050  1.00 48.79           C  
ANISOU 1383  CD1 TYR A 211     5034   6767   6737   -174    633   -459       C  
ATOM   1384  CD2 TYR A 211       7.637  53.851  49.487  1.00 45.80           C  
ANISOU 1384  CD2 TYR A 211     4778   6462   6162   -140    594   -359       C  
ATOM   1385  CE1 TYR A 211       5.787  55.575  48.341  1.00 46.83           C  
ANISOU 1385  CE1 TYR A 211     4740   6525   6530   -132    577   -448       C  
ATOM   1386  CE2 TYR A 211       8.074  54.944  48.784  1.00 54.44           C  
ANISOU 1386  CE2 TYR A 211     5824   7564   7299    -99    549   -352       C  
ATOM   1387  CZ  TYR A 211       7.145  55.808  48.209  1.00 55.52           C  
ANISOU 1387  CZ  TYR A 211     5881   7667   7548    -96    541   -394       C  
ATOM   1388  OH  TYR A 211       7.587  56.895  47.510  1.00 50.90           O  
ANISOU 1388  OH  TYR A 211     5258   7083   6997    -58    495   -385       O  
ATOM   1389  N   THR A 212       7.629  50.221  49.289  1.00 52.83           N  
ANISOU 1389  N   THR A 212     5824   7336   6913   -143    586   -275       N  
ATOM   1390  CA  THR A 212       8.696  49.810  48.375  1.00 54.80           C  
ANISOU 1390  CA  THR A 212     6097   7602   7122    -86    514   -211       C  
ATOM   1391  C   THR A 212       8.348  48.530  47.637  1.00 49.81           C  
ANISOU 1391  C   THR A 212     5489   6950   6488    -72    496   -185       C  
ATOM   1392  O   THR A 212       8.811  48.335  46.509  1.00 60.14           O  
ANISOU 1392  O   THR A 212     6791   8255   7802    -26    440   -149       O  
ATOM   1393  CB  THR A 212      10.027  49.609  49.095  1.00 58.50           C  
ANISOU 1393  CB  THR A 212     6630   8102   7496    -79    497   -173       C  
ATOM   1394  OG1 THR A 212       9.856  48.662  50.154  1.00 54.81           O  
ANISOU 1394  OG1 THR A 212     6236   7630   6961   -123    536   -172       O  
ATOM   1395  CG2 THR A 212      10.581  50.940  49.635  1.00 49.15           C  
ANISOU 1395  CG2 THR A 212     5419   6942   6316    -81    500   -194       C  
ATOM   1396  N   PHE A 213       7.535  47.657  48.240  1.00 48.84           N  
ANISOU 1396  N   PHE A 213     5394   6808   6356   -114    548   -206       N  
ATOM   1397  CA  PHE A 213       7.193  46.393  47.584  1.00 50.68           C  
ANISOU 1397  CA  PHE A 213     5648   7021   6587   -103    536   -183       C  
ATOM   1398  C   PHE A 213       6.203  46.614  46.448  1.00 61.18           C  
ANISOU 1398  C   PHE A 213     6908   8318   8019    -84    513   -210       C  
ATOM   1399  O   PHE A 213       6.257  45.926  45.421  1.00 56.97           O  
ANISOU 1399  O   PHE A 213     6381   7776   7491    -51    469   -178       O  
ATOM   1400  CB  PHE A 213       6.623  45.418  48.604  1.00 47.63           C  
ANISOU 1400  CB  PHE A 213     5318   6620   6160   -157    604   -200       C  
ATOM   1401  CG  PHE A 213       6.032  44.184  48.003  1.00 58.26           C  
ANISOU 1401  CG  PHE A 213     6674   7941   7520   -153    605   -191       C  
ATOM   1402  CD1 PHE A 213       6.843  43.192  47.493  1.00 44.31           C  
ANISOU 1402  CD1 PHE A 213     4955   6186   5695   -118    558   -129       C  
ATOM   1403  CD2 PHE A 213       4.660  43.996  47.972  1.00 63.82           C  
ANISOU 1403  CD2 PHE A 213     7338   8607   8304   -185    657   -249       C  
ATOM   1404  CE1 PHE A 213       6.305  42.049  46.960  1.00 43.61           C  
ANISOU 1404  CE1 PHE A 213     4876   6076   5619   -116    563   -121       C  
ATOM   1405  CE2 PHE A 213       4.112  42.838  47.409  1.00 54.54           C  
ANISOU 1405  CE2 PHE A 213     6170   7408   7146   -180    658   -243       C  
ATOM   1406  CZ  PHE A 213       4.943  41.867  46.907  1.00 51.99           C  
ANISOU 1406  CZ  PHE A 213     5898   7101   6755   -146    611   -176       C  
ATOM   1407  N   ILE A 214       5.304  47.587  46.615  1.00 65.73           N  
ANISOU 1407  N   ILE A 214     7419   8875   8683   -105    539   -270       N  
ATOM   1408  CA  ILE A 214       4.270  47.877  45.622  1.00 51.43           C  
ANISOU 1408  CA  ILE A 214     5537   7021   6983    -89    507   -305       C  
ATOM   1409  C   ILE A 214       4.843  48.676  44.459  1.00 54.97           C  
ANISOU 1409  C   ILE A 214     5965   7474   7449    -35    424   -273       C  
ATOM   1410  O   ILE A 214       4.634  48.327  43.291  1.00 56.52           O  
ANISOU 1410  O   ILE A 214     6158   7646   7672     -2    366   -254       O  
ATOM   1411  CB  ILE A 214       3.093  48.618  46.291  1.00 55.60           C  
ANISOU 1411  CB  ILE A 214     5998   7517   7612   -135    566   -389       C  
ATOM   1412  CG1 ILE A 214       2.320  47.680  47.223  1.00 60.31           C  
ANISOU 1412  CG1 ILE A 214     6618   8093   8204   -193    656   -429       C  
ATOM   1413  CG2 ILE A 214       2.158  49.202  45.261  1.00 61.59           C  
ANISOU 1413  CG2 ILE A 214     6674   8228   8499   -110    512   -427       C  
ATOM   1414  CD1 ILE A 214       1.292  48.390  48.078  1.00 53.75           C  
ANISOU 1414  CD1 ILE A 214     5730   7228   7464   -250    736   -519       C  
ATOM   1415  N   LEU A 215       5.566  49.763  44.756  1.00 46.86           N  
ANISOU 1415  N   LEU A 215     4929   6472   6405    -28    419   -268       N  
ATOM   1416  CA  LEU A 215       6.118  50.594  43.692  1.00 46.67           C  
ANISOU 1416  CA  LEU A 215     4892   6446   6395     18    350   -242       C  
ATOM   1417  C   LEU A 215       7.374  49.979  43.079  1.00 51.03           C  
ANISOU 1417  C   LEU A 215     5508   7022   6859     53    314   -174       C  
ATOM   1418  O   LEU A 215       7.631  50.137  41.878  1.00 50.37           O  
ANISOU 1418  O   LEU A 215     5433   6920   6783     88    258   -148       O  
ATOM   1419  CB  LEU A 215       6.431  51.991  44.215  1.00 52.88           C  
ANISOU 1419  CB  LEU A 215     5642   7248   7202     13    362   -265       C  
ATOM   1420  CG  LEU A 215       5.289  52.832  44.782  1.00 56.24           C  
ANISOU 1420  CG  LEU A 215     5994   7647   7728    -21    398   -338       C  
ATOM   1421  CD1 LEU A 215       5.844  54.198  45.134  1.00 51.14           C  
ANISOU 1421  CD1 LEU A 215     5320   7022   7089    -18    402   -348       C  
ATOM   1422  CD2 LEU A 215       4.093  52.939  43.822  1.00 49.22           C  
ANISOU 1422  CD2 LEU A 215     5051   6699   6952     -8    350   -370       C  
ATOM   1423  N   GLY A 216       8.171  49.284  43.868  1.00 45.81           N  
ANISOU 1423  N   GLY A 216     4895   6394   6117     42    345   -148       N  
ATOM   1424  CA  GLY A 216       9.377  48.768  43.269  1.00 42.17           C  
ANISOU 1424  CA  GLY A 216     4482   5948   5594     74    311    -94       C  
ATOM   1425  C   GLY A 216       9.265  47.413  42.628  1.00 41.77           C  
ANISOU 1425  C   GLY A 216     4467   5882   5520     83    296    -64       C  
ATOM   1426  O   GLY A 216      10.226  46.957  42.016  1.00 46.25           O  
ANISOU 1426  O   GLY A 216     5070   6455   6046    109    270    -23       O  
ATOM   1427  N   PHE A 217       8.125  46.743  42.732  1.00 46.55           N  
ANISOU 1427  N   PHE A 217     5062   6466   6158     61    316    -88       N  
ATOM   1428  CA  PHE A 217       8.131  45.336  42.365  1.00 54.41           C  
ANISOU 1428  CA  PHE A 217     6097   7455   7121     65    312    -58       C  
ATOM   1429  C   PHE A 217       6.778  44.872  41.835  1.00 58.69           C  
ANISOU 1429  C   PHE A 217     6611   7959   7730     57    310    -88       C  
ATOM   1430  O   PHE A 217       6.687  44.400  40.694  1.00 58.48           O  
ANISOU 1430  O   PHE A 217     6594   7911   7713     81    266    -68       O  
ATOM   1431  CB  PHE A 217       8.576  44.496  43.574  1.00 50.28           C  
ANISOU 1431  CB  PHE A 217     5620   6955   6529     40    355    -44       C  
ATOM   1432  CG  PHE A 217       8.721  43.044  43.273  1.00 41.87           C  
ANISOU 1432  CG  PHE A 217     4598   5883   5426     45    351    -10       C  
ATOM   1433  CD1 PHE A 217       9.908  42.551  42.750  1.00 39.90           C  
ANISOU 1433  CD1 PHE A 217     4383   5644   5133     74    316     38       C  
ATOM   1434  CD2 PHE A 217       7.667  42.165  43.504  1.00 48.84           C  
ANISOU 1434  CD2 PHE A 217     5484   6745   6327     18    386    -31       C  
ATOM   1435  CE1 PHE A 217      10.058  41.208  42.449  1.00 41.82           C  
ANISOU 1435  CE1 PHE A 217     4662   5880   5349     79    313     68       C  
ATOM   1436  CE2 PHE A 217       7.803  40.813  43.218  1.00 55.56           C  
ANISOU 1436  CE2 PHE A 217     6375   7591   7145     23    384      1       C  
ATOM   1437  CZ  PHE A 217       9.014  40.326  42.681  1.00 53.14           C  
ANISOU 1437  CZ  PHE A 217     6101   7296   6792     54    345     53       C  
ATOM   1438  N   LEU A 218       5.719  45.024  42.640  1.00 51.26           N  
ANISOU 1438  N   LEU A 218     5634   7004   6839     20    357   -142       N  
ATOM   1439  CA  LEU A 218       4.428  44.434  42.292  1.00 50.45           C  
ANISOU 1439  CA  LEU A 218     5500   6859   6807      8    363   -179       C  
ATOM   1440  C   LEU A 218       3.751  45.165  41.135  1.00 53.76           C  
ANISOU 1440  C   LEU A 218     5870   7240   7318     35    296   -201       C  
ATOM   1441  O   LEU A 218       3.225  44.534  40.212  1.00 46.64           O  
ANISOU 1441  O   LEU A 218     4966   6307   6446     51    256   -199       O  
ATOM   1442  CB  LEU A 218       3.530  44.410  43.523  1.00 47.44           C  
ANISOU 1442  CB  LEU A 218     5096   6467   6462    -44    444   -239       C  
ATOM   1443  CG  LEU A 218       2.068  43.978  43.380  1.00 65.08           C  
ANISOU 1443  CG  LEU A 218     7281   8651   8796    -66    469   -300       C  
ATOM   1444  CD1 LEU A 218       1.746  42.905  44.409  1.00 72.86           C  
ANISOU 1444  CD1 LEU A 218     8306   9635   9743   -114    557   -316       C  
ATOM   1445  CD2 LEU A 218       1.150  45.205  43.586  1.00 57.41           C  
ANISOU 1445  CD2 LEU A 218     6227   7647   7941    -83    478   -374       C  
ATOM   1446  N   VAL A 219       3.725  46.490  41.179  1.00 54.56           N  
ANISOU 1446  N   VAL A 219     5932   7338   7462     40    278   -224       N  
ATOM   1447  CA  VAL A 219       3.055  47.289  40.152  1.00 48.70           C  
ANISOU 1447  CA  VAL A 219     5145   6548   6808     64    206   -247       C  
ATOM   1448  C   VAL A 219       3.830  47.247  38.830  1.00 44.54           C  
ANISOU 1448  C   VAL A 219     4672   6019   6231    105    130   -189       C  
ATOM   1449  O   VAL A 219       3.220  47.002  37.785  1.00 56.01           O  
ANISOU 1449  O   VAL A 219     6126   7428   7726    123     68   -191       O  
ATOM   1450  CB  VAL A 219       2.839  48.730  40.653  1.00 50.59           C  
ANISOU 1450  CB  VAL A 219     5329   6784   7110     54    212   -289       C  
ATOM   1451  CG1 VAL A 219       2.454  49.642  39.517  1.00 43.04           C  
ANISOU 1451  CG1 VAL A 219     4347   5781   6226     86    121   -297       C  
ATOM   1452  CG2 VAL A 219       1.787  48.757  41.791  1.00 41.93           C  
ANISOU 1452  CG2 VAL A 219     4172   5670   6090      6    288   -364       C  
ATOM   1453  N   PRO A 220       5.151  47.456  38.798  1.00 45.29           N  
ANISOU 1453  N   PRO A 220     4816   6153   6240    119    134   -140       N  
ATOM   1454  CA  PRO A 220       5.868  47.255  37.518  1.00 58.50           C  
ANISOU 1454  CA  PRO A 220     6549   7815   7865    150     79    -90       C  
ATOM   1455  C   PRO A 220       5.656  45.884  36.899  1.00 52.17           C  
ANISOU 1455  C   PRO A 220     5782   7000   7041    153     68    -69       C  
ATOM   1456  O   PRO A 220       5.343  45.781  35.702  1.00 55.62           O  
ANISOU 1456  O   PRO A 220     6243   7396   7492    170      6    -59       O  
ATOM   1457  CB  PRO A 220       7.339  47.465  37.902  1.00 58.56           C  
ANISOU 1457  CB  PRO A 220     6592   7868   7791    155    111    -53       C  
ATOM   1458  CG  PRO A 220       7.301  48.297  39.127  1.00 52.65           C  
ANISOU 1458  CG  PRO A 220     5797   7145   7062    136    154    -85       C  
ATOM   1459  CD  PRO A 220       6.064  47.902  39.871  1.00 48.35           C  
ANISOU 1459  CD  PRO A 220     5208   6588   6574    106    187   -132       C  
ATOM   1460  N   LEU A 221       5.824  44.822  37.688  1.00 49.57           N  
ANISOU 1460  N   LEU A 221     5461   6700   6673    135    125    -61       N  
ATOM   1461  CA  LEU A 221       5.698  43.471  37.159  1.00 40.90           C  
ANISOU 1461  CA  LEU A 221     4396   5592   5552    138    121    -39       C  
ATOM   1462  C   LEU A 221       4.299  43.195  36.659  1.00 42.01           C  
ANISOU 1462  C   LEU A 221     4502   5686   5774    135     89    -79       C  
ATOM   1463  O   LEU A 221       4.125  42.507  35.649  1.00 58.20           O  
ANISOU 1463  O   LEU A 221     6582   7712   7821    149     48    -62       O  
ATOM   1464  CB  LEU A 221       6.085  42.454  38.222  1.00 47.97           C  
ANISOU 1464  CB  LEU A 221     5308   6523   6395    117    187    -26       C  
ATOM   1465  CG  LEU A 221       7.602  42.351  38.257  1.00 45.17           C  
ANISOU 1465  CG  LEU A 221     5000   6202   5961    130    192     23       C  
ATOM   1466  CD1 LEU A 221       8.046  41.547  39.443  1.00 47.65           C  
ANISOU 1466  CD1 LEU A 221     5334   6546   6225    111    244     35       C  
ATOM   1467  CD2 LEU A 221       8.087  41.759  36.953  1.00 42.21           C  
ANISOU 1467  CD2 LEU A 221     4667   5809   5561    151    156     59       C  
ATOM   1468  N   THR A 222       3.282  43.705  37.352  1.00 42.88           N  
ANISOU 1468  N   THR A 222     4548   5779   5966    117    108   -137       N  
ATOM   1469  CA  THR A 222       1.922  43.543  36.845  1.00 48.52           C  
ANISOU 1469  CA  THR A 222     5216   6438   6781    117     70   -185       C  
ATOM   1470  C   THR A 222       1.779  44.217  35.484  1.00 52.01           C  
ANISOU 1470  C   THR A 222     5674   6836   7253    149    -34   -176       C  
ATOM   1471  O   THR A 222       1.148  43.667  34.574  1.00 51.92           O  
ANISOU 1471  O   THR A 222     5671   6782   7275    162    -90   -181       O  
ATOM   1472  CB  THR A 222       0.890  44.108  37.836  1.00 49.33           C  
ANISOU 1472  CB  THR A 222     5240   6522   6983     89    113   -260       C  
ATOM   1473  OG1 THR A 222       1.064  43.520  39.122  1.00 50.02           O  
ANISOU 1473  OG1 THR A 222     5333   6645   7027     52    213   -267       O  
ATOM   1474  CG2 THR A 222      -0.484  43.784  37.387  1.00 43.33           C  
ANISOU 1474  CG2 THR A 222     4426   5700   6338     88     81   -317       C  
ATOM   1475  N   ILE A 223       2.369  45.408  35.327  1.00 47.46           N  
ANISOU 1475  N   ILE A 223     5107   6264   6661    162    -62   -161       N  
ATOM   1476  CA  ILE A 223       2.316  46.103  34.045  1.00 44.53           C  
ANISOU 1476  CA  ILE A 223     4770   5846   6304    188   -160   -147       C  
ATOM   1477  C   ILE A 223       3.097  45.330  32.988  1.00 44.11           C  
ANISOU 1477  C   ILE A 223     4808   5794   6158    201   -185    -89       C  
ATOM   1478  O   ILE A 223       2.644  45.173  31.847  1.00 45.15           O  
ANISOU 1478  O   ILE A 223     4976   5875   6305    215   -263    -84       O  
ATOM   1479  CB  ILE A 223       2.851  47.539  34.200  1.00 48.06           C  
ANISOU 1479  CB  ILE A 223     5212   6300   6748    194   -170   -144       C  
ATOM   1480  CG1 ILE A 223       2.119  48.289  35.298  1.00 46.71           C  
ANISOU 1480  CG1 ILE A 223     4950   6130   6670    177   -135   -205       C  
ATOM   1481  CG2 ILE A 223       2.718  48.327  32.904  1.00 48.92           C  
ANISOU 1481  CG2 ILE A 223     5365   6351   6873    219   -275   -132       C  
ATOM   1482  CD1 ILE A 223       2.451  49.802  35.275  1.00 41.23           C  
ANISOU 1482  CD1 ILE A 223     4244   5429   5993    186   -163   -208       C  
ATOM   1483  N   ILE A 224       4.282  44.840  33.341  1.00 43.67           N  
ANISOU 1483  N   ILE A 224     4792   5792   6011    195   -121    -47       N  
ATOM   1484  CA  ILE A 224       5.107  44.147  32.353  1.00 54.03           C  
ANISOU 1484  CA  ILE A 224     6186   7101   7242    202   -133      3       C  
ATOM   1485  C   ILE A 224       4.417  42.860  31.890  1.00 63.73           C  
ANISOU 1485  C   ILE A 224     7422   8309   8483    200   -147      0       C  
ATOM   1486  O   ILE A 224       4.314  42.596  30.679  1.00 56.61           O  
ANISOU 1486  O   ILE A 224     6577   7367   7564    209   -206     17       O  
ATOM   1487  CB  ILE A 224       6.532  43.920  32.925  1.00 46.78           C  
ANISOU 1487  CB  ILE A 224     5293   6238   6244    197    -62     39       C  
ATOM   1488  CG1 ILE A 224       7.290  45.260  32.948  1.00 39.09           C  
ANISOU 1488  CG1 ILE A 224     4328   5270   5254    203    -65     44       C  
ATOM   1489  CG2 ILE A 224       7.335  42.902  32.144  1.00 42.45           C  
ANISOU 1489  CG2 ILE A 224     4812   5689   5627    197    -52     80       C  
ATOM   1490  CD1 ILE A 224       8.274  45.393  34.017  1.00 35.91           C  
ANISOU 1490  CD1 ILE A 224     3907   4919   4816    198      1     52       C  
ATOM   1491  N   CYS A 225       3.863  42.079  32.840  1.00 57.76           N  
ANISOU 1491  N   CYS A 225     6612   7575   7759    186    -94    -25       N  
ATOM   1492  CA  CYS A 225       3.295  40.773  32.498  1.00 48.81           C  
ANISOU 1492  CA  CYS A 225     5484   6428   6635    182    -94    -28       C  
ATOM   1493  C   CYS A 225       1.983  40.895  31.738  1.00 48.30           C  
ANISOU 1493  C   CYS A 225     5394   6299   6659    192   -174    -69       C  
ATOM   1494  O   CYS A 225       1.687  40.061  30.876  1.00 45.55           O  
ANISOU 1494  O   CYS A 225     5078   5924   6305    198   -210    -60       O  
ATOM   1495  CB  CYS A 225       3.077  39.929  33.750  1.00 53.40           C  
ANISOU 1495  CB  CYS A 225     6023   7043   7222    161     -9    -46       C  
ATOM   1496  SG  CYS A 225       4.577  39.566  34.695  1.00 59.93           S  
ANISOU 1496  SG  CYS A 225     6885   7936   7948    151     69      2       S  
ATOM   1497  N   LEU A 226       1.173  41.903  32.040  1.00 46.89           N  
ANISOU 1497  N   LEU A 226     5156   6092   6570    194   -206   -117       N  
ATOM   1498  CA  LEU A 226       0.001  42.120  31.205  1.00 49.59           C  
ANISOU 1498  CA  LEU A 226     5476   6361   7004    209   -303   -156       C  
ATOM   1499  C   LEU A 226       0.413  42.498  29.793  1.00 51.35           C  
ANISOU 1499  C   LEU A 226     5789   6547   7175    228   -398   -115       C  
ATOM   1500  O   LEU A 226      -0.164  42.005  28.813  1.00 56.05           O  
ANISOU 1500  O   LEU A 226     6415   7092   7789    238   -472   -119       O  
ATOM   1501  CB  LEU A 226      -0.886  43.183  31.823  1.00 50.47           C  
ANISOU 1501  CB  LEU A 226     5500   6443   7232    207   -320   -220       C  
ATOM   1502  CG  LEU A 226      -1.520  42.582  33.078  1.00 50.73           C  
ANISOU 1502  CG  LEU A 226     5453   6496   7326    179   -223   -272       C  
ATOM   1503  CD1 LEU A 226      -2.449  43.570  33.710  1.00 55.89           C  
ANISOU 1503  CD1 LEU A 226     6014   7115   8108    170   -227   -345       C  
ATOM   1504  CD2 LEU A 226      -2.243  41.289  32.744  1.00 46.59           C  
ANISOU 1504  CD2 LEU A 226     4921   5948   6834    177   -224   -291       C  
ATOM   1505  N   CYS A 227       1.434  43.345  29.680  1.00 47.22           N  
ANISOU 1505  N   CYS A 227     5316   6044   6582    230   -392    -77       N  
ATOM   1506  CA  CYS A 227       1.978  43.710  28.381  1.00 50.79           C  
ANISOU 1506  CA  CYS A 227     5871   6459   6966    240   -462    -36       C  
ATOM   1507  C   CYS A 227       2.408  42.484  27.590  1.00 50.78           C  
ANISOU 1507  C   CYS A 227     5946   6460   6888    234   -452      1       C  
ATOM   1508  O   CYS A 227       2.178  42.402  26.382  1.00 52.72           O  
ANISOU 1508  O   CYS A 227     6267   6650   7115    239   -533     14       O  
ATOM   1509  CB  CYS A 227       3.155  44.667  28.573  1.00 50.40           C  
ANISOU 1509  CB  CYS A 227     5858   6440   6850    238   -424     -4       C  
ATOM   1510  SG  CYS A 227       2.599  46.380  28.646  1.00 57.74           S  
ANISOU 1510  SG  CYS A 227     6753   7328   7860    251   -496    -36       S  
ATOM   1511  N   TYR A 228       3.047  41.529  28.251  1.00 54.69           N  
ANISOU 1511  N   TYR A 228     6426   7014   7338    221   -356     19       N  
ATOM   1512  CA  TYR A 228       3.556  40.369  27.540  1.00 51.78           C  
ANISOU 1512  CA  TYR A 228     6124   6649   6900    213   -338     54       C  
ATOM   1513  C   TYR A 228       2.482  39.317  27.316  1.00 55.68           C  
ANISOU 1513  C   TYR A 228     6590   7119   7447    215   -365     27       C  
ATOM   1514  O   TYR A 228       2.572  38.552  26.351  1.00 56.70           O  
ANISOU 1514  O   TYR A 228     6784   7225   7534    211   -390     48       O  
ATOM   1515  CB  TYR A 228       4.746  39.795  28.304  1.00 53.82           C  
ANISOU 1515  CB  TYR A 228     6380   6973   7094    201   -233     84       C  
ATOM   1516  CG  TYR A 228       6.022  40.319  27.720  1.00 57.02           C  
ANISOU 1516  CG  TYR A 228     6864   7379   7422    197   -219    121       C  
ATOM   1517  CD1 TYR A 228       6.520  39.784  26.542  1.00 56.14           C  
ANISOU 1517  CD1 TYR A 228     6843   7238   7249    186   -230    148       C  
ATOM   1518  CD2 TYR A 228       6.701  41.389  28.302  1.00 51.88           C  
ANISOU 1518  CD2 TYR A 228     6199   6752   6763    199   -193    123       C  
ATOM   1519  CE1 TYR A 228       7.675  40.282  25.964  1.00 49.32           C  
ANISOU 1519  CE1 TYR A 228     6055   6365   6320    176   -207    174       C  
ATOM   1520  CE2 TYR A 228       7.853  41.887  27.740  1.00 44.82           C  
ANISOU 1520  CE2 TYR A 228     5374   5851   5806    193   -174    149       C  
ATOM   1521  CZ  TYR A 228       8.330  41.328  26.563  1.00 54.55           C  
ANISOU 1521  CZ  TYR A 228     6697   7050   6981    180   -179    173       C  
ATOM   1522  OH  TYR A 228       9.480  41.790  25.971  1.00 66.35           O  
ANISOU 1522  OH  TYR A 228     8264   8529   8416    167   -148    192       O  
ATOM   1523  N   LEU A 229       1.472  39.263  28.186  1.00 50.34           N  
ANISOU 1523  N   LEU A 229     5817   6444   6864    217   -355    -22       N  
ATOM   1524  CA  LEU A 229       0.299  38.440  27.909  1.00 47.00           C  
ANISOU 1524  CA  LEU A 229     5360   5985   6515    220   -391    -60       C  
ATOM   1525  C   LEU A 229      -0.431  38.939  26.673  1.00 48.69           C  
ANISOU 1525  C   LEU A 229     5612   6119   6767    237   -523    -74       C  
ATOM   1526  O   LEU A 229      -0.857  38.144  25.830  1.00 57.07           O  
ANISOU 1526  O   LEU A 229     6708   7147   7830    240   -571    -75       O  
ATOM   1527  CB  LEU A 229      -0.636  38.423  29.119  1.00 46.67           C  
ANISOU 1527  CB  LEU A 229     5206   5950   6577    213   -345   -121       C  
ATOM   1528  CG  LEU A 229      -2.070  37.902  28.954  1.00 52.19           C  
ANISOU 1528  CG  LEU A 229     5842   6596   7392    218   -388   -184       C  
ATOM   1529  CD1 LEU A 229      -2.114  36.391  28.666  1.00 48.99           C  
ANISOU 1529  CD1 LEU A 229     5457   6201   6956    211   -353   -171       C  
ATOM   1530  CD2 LEU A 229      -2.933  38.252  30.185  1.00 48.98           C  
ANISOU 1530  CD2 LEU A 229     5326   6186   7098    205   -335   -254       C  
ATOM   1531  N   PHE A 230      -0.575  40.257  26.536  1.00 57.28           N  
ANISOU 1531  N   PHE A 230     6702   7175   7888    248   -588    -85       N  
ATOM   1532  CA  PHE A 230      -1.216  40.786  25.339  1.00 53.81           C  
ANISOU 1532  CA  PHE A 230     6315   6653   7479    264   -727    -94       C  
ATOM   1533  C   PHE A 230      -0.366  40.521  24.106  1.00 54.50           C  
ANISOU 1533  C   PHE A 230     6543   6724   7441    257   -756    -35       C  
ATOM   1534  O   PHE A 230      -0.910  40.293  23.018  1.00 52.05           O  
ANISOU 1534  O   PHE A 230     6294   6348   7133    263   -857    -37       O  
ATOM   1535  CB  PHE A 230      -1.496  42.287  25.492  1.00 47.88           C  
ANISOU 1535  CB  PHE A 230     5537   5866   6787    277   -790   -116       C  
ATOM   1536  CG  PHE A 230      -2.332  42.624  26.691  1.00 54.13           C  
ANISOU 1536  CG  PHE A 230     6191   6666   7708    278   -755   -181       C  
ATOM   1537  CD1 PHE A 230      -3.296  41.723  27.165  1.00 59.82           C  
ANISOU 1537  CD1 PHE A 230     6825   7381   8524    274   -728   -235       C  
ATOM   1538  CD2 PHE A 230      -2.157  43.835  27.365  1.00 51.23           C  
ANISOU 1538  CD2 PHE A 230     5782   6311   7372    278   -738   -194       C  
ATOM   1539  CE1 PHE A 230      -4.082  42.019  28.296  1.00 50.62           C  
ANISOU 1539  CE1 PHE A 230     5535   6216   7480    266   -680   -304       C  
ATOM   1540  CE2 PHE A 230      -2.929  44.139  28.493  1.00 52.30           C  
ANISOU 1540  CE2 PHE A 230     5793   6452   7628    272   -695   -259       C  
ATOM   1541  CZ  PHE A 230      -3.898  43.229  28.956  1.00 57.97           C  
ANISOU 1541  CZ  PHE A 230     6428   7158   8439    264   -663   -316       C  
ATOM   1542  N   ILE A 231       0.963  40.540  24.259  1.00 49.87           N  
ANISOU 1542  N   ILE A 231     6009   6191   6748    241   -668     14       N  
ATOM   1543  CA  ILE A 231       1.856  40.265  23.135  1.00 53.73           C  
ANISOU 1543  CA  ILE A 231     6631   6663   7121    225   -673     63       C  
ATOM   1544  C   ILE A 231       1.698  38.820  22.666  1.00 62.91           C  
ANISOU 1544  C   ILE A 231     7815   7827   8262    216   -657     69       C  
ATOM   1545  O   ILE A 231       1.591  38.545  21.463  1.00 63.25           O  
ANISOU 1545  O   ILE A 231     7958   7817   8259    209   -724     84       O  
ATOM   1546  CB  ILE A 231       3.314  40.571  23.513  1.00 47.49           C  
ANISOU 1546  CB  ILE A 231     5872   5927   6245    210   -571    102       C  
ATOM   1547  CG1 ILE A 231       3.603  42.068  23.402  1.00 47.15           C  
ANISOU 1547  CG1 ILE A 231     5862   5859   6194    215   -609    106       C  
ATOM   1548  CG2 ILE A 231       4.256  39.770  22.632  1.00 47.71           C  
ANISOU 1548  CG2 ILE A 231     6005   5952   6170    186   -529    141       C  
ATOM   1549  CD1 ILE A 231       4.811  42.507  24.218  1.00 44.40           C  
ANISOU 1549  CD1 ILE A 231     5492   5573   5805    207   -504    124       C  
ATOM   1550  N   ILE A 232       1.684  37.873  23.605  1.00 58.41           N  
ANISOU 1550  N   ILE A 232     7159   7315   7718    213   -568     58       N  
ATOM   1551  CA  ILE A 232       1.635  36.484  23.174  1.00 64.09           C  
ANISOU 1551  CA  ILE A 232     7900   8039   8413    203   -543     67       C  
ATOM   1552  C   ILE A 232       0.232  36.099  22.700  1.00 74.57           C  
ANISOU 1552  C   ILE A 232     9199   9310   9825    217   -638     24       C  
ATOM   1553  O   ILE A 232       0.097  35.328  21.743  1.00 78.79           O  
ANISOU 1553  O   ILE A 232     9797   9812  10326    210   -674     34       O  
ATOM   1554  CB  ILE A 232       2.173  35.557  24.279  1.00 59.58           C  
ANISOU 1554  CB  ILE A 232     7262   7543   7834    194   -419     74       C  
ATOM   1555  CG1 ILE A 232       1.327  35.620  25.541  1.00 68.03           C  
ANISOU 1555  CG1 ILE A 232     8212   8636   9002    204   -392     29       C  
ATOM   1556  CG2 ILE A 232       3.554  35.979  24.649  1.00 56.09           C  
ANISOU 1556  CG2 ILE A 232     6849   7145   7319    184   -344    112       C  
ATOM   1557  CD1 ILE A 232       2.069  35.061  26.782  1.00 66.21           C  
ANISOU 1557  CD1 ILE A 232     7936   8478   8744    193   -272     44       C  
ATOM   1558  N   ILE A 233      -0.830  36.641  23.306  1.00 73.46           N  
ANISOU 1558  N   ILE A 233     8963   9148   9799    236   -682    -28       N  
ATOM   1559  CA  ILE A 233      -2.162  36.454  22.730  1.00 65.51           C  
ANISOU 1559  CA  ILE A 233     7931   8071   8888    252   -792    -76       C  
ATOM   1560  C   ILE A 233      -2.180  36.937  21.280  1.00 64.66           C  
ANISOU 1560  C   ILE A 233     7949   7889   8729    255   -922    -54       C  
ATOM   1561  O   ILE A 233      -2.630  36.231  20.370  1.00 63.59           O  
ANISOU 1561  O   ILE A 233     7865   7709   8588    255   -987    -58       O  
ATOM   1562  CB  ILE A 233      -3.230  37.176  23.573  1.00 61.44           C  
ANISOU 1562  CB  ILE A 233     7294   7533   8517    269   -822   -143       C  
ATOM   1563  CG1 ILE A 233      -3.315  36.609  25.000  1.00 60.12           C  
ANISOU 1563  CG1 ILE A 233     7016   7431   8396    257   -690   -171       C  
ATOM   1564  CG2 ILE A 233      -4.573  37.067  22.899  1.00 57.09           C  
ANISOU 1564  CG2 ILE A 233     6716   6898   8078    288   -950   -198       C  
ATOM   1565  CD1 ILE A 233      -3.502  35.114  25.076  1.00 59.41           C  
ANISOU 1565  CD1 ILE A 233     6909   7363   8303    247   -627   -176       C  
ATOM   1566  N   LYS A 234      -1.648  38.135  21.046  1.00 64.74           N  
ANISOU 1566  N   LYS A 234     8022   7883   8694    255   -956    -29       N  
ATOM   1567  CA  LYS A 234      -1.674  38.746  19.720  1.00 62.46           C  
ANISOU 1567  CA  LYS A 234     7867   7513   8351    255  -1083     -7       C  
ATOM   1568  C   LYS A 234      -0.940  37.895  18.692  1.00 65.85           C  
ANISOU 1568  C   LYS A 234     8429   7938   8653    228  -1061     39       C  
ATOM   1569  O   LYS A 234      -1.416  37.709  17.566  1.00 69.07           O  
ANISOU 1569  O   LYS A 234     8930   8273   9040    226  -1170     39       O  
ATOM   1570  CB  LYS A 234      -1.045  40.134  19.787  1.00 50.80           C  
ANISOU 1570  CB  LYS A 234     6435   6031   6836    254  -1092     16       C  
ATOM   1571  CG  LYS A 234      -1.041  40.835  18.490  1.00 50.71           C  
ANISOU 1571  CG  LYS A 234     6574   5932   6762    250  -1217     40       C  
ATOM   1572  CD  LYS A 234      -2.453  41.165  18.126  1.00 54.30           C  
ANISOU 1572  CD  LYS A 234     6995   6301   7335    280  -1380     -8       C  
ATOM   1573  CE  LYS A 234      -2.543  41.650  16.705  1.00 64.39           C  
ANISOU 1573  CE  LYS A 234     8444   7479   8542    274  -1525     18       C  
ATOM   1574  NZ  LYS A 234      -1.462  42.633  16.421  1.00 61.25           N  
ANISOU 1574  NZ  LYS A 234     8162   7079   8030    253  -1493     67       N  
ATOM   1575  N   VAL A 235       0.238  37.393  19.055  1.00 66.43           N  
ANISOU 1575  N   VAL A 235     8515   8082   8643    204   -923     75       N  
ATOM   1576  CA  VAL A 235       1.062  36.668  18.093  1.00 59.40           C  
ANISOU 1576  CA  VAL A 235     7750   7185   7634    172   -886    115       C  
ATOM   1577  C   VAL A 235       0.364  35.390  17.665  1.00 62.71           C  
ANISOU 1577  C   VAL A 235     8159   7590   8079    171   -911     98       C  
ATOM   1578  O   VAL A 235       0.174  35.136  16.472  1.00 77.13           O  
ANISOU 1578  O   VAL A 235    10101   9354   9853    157   -989    107       O  
ATOM   1579  CB  VAL A 235       2.454  36.393  18.685  1.00 57.41           C  
ANISOU 1579  CB  VAL A 235     7491   7009   7314    150   -733    148       C  
ATOM   1580  CG1 VAL A 235       3.082  35.209  18.008  1.00 62.93           C  
ANISOU 1580  CG1 VAL A 235     8262   7714   7936    119   -671    171       C  
ATOM   1581  CG2 VAL A 235       3.333  37.631  18.528  1.00 56.18           C  
ANISOU 1581  CG2 VAL A 235     7408   6841   7096    139   -722    172       C  
ATOM   1582  N   LYS A 236      -0.058  34.580  18.636  1.00 65.91           N  
ANISOU 1582  N   LYS A 236     8431   8048   8562    185   -847     70       N  
ATOM   1583  CA  LYS A 236      -0.846  33.399  18.321  1.00 62.65           C  
ANISOU 1583  CA  LYS A 236     7992   7620   8192    188   -871     45       C  
ATOM   1584  C   LYS A 236      -2.106  33.772  17.547  1.00 78.00           C  
ANISOU 1584  C   LYS A 236     9957   9475  10206    209  -1036      8       C  
ATOM   1585  O   LYS A 236      -2.590  32.981  16.729  1.00 81.54           O  
ANISOU 1585  O   LYS A 236    10449   9883  10649    205  -1092     -1       O  
ATOM   1586  CB  LYS A 236      -1.183  32.652  19.616  1.00 65.06           C  
ANISOU 1586  CB  LYS A 236     8147   7990   8581    199   -775     15       C  
ATOM   1587  CG  LYS A 236      -1.261  31.129  19.494  1.00 83.58           C  
ANISOU 1587  CG  LYS A 236    10478  10358  10921    188   -718     14       C  
ATOM   1588  CD  LYS A 236       0.095  30.479  19.195  1.00 85.49           C  
ANISOU 1588  CD  LYS A 236    10798  10641  11045    157   -618     68       C  
ATOM   1589  CE  LYS A 236       1.247  31.095  19.991  1.00 85.89           C  
ANISOU 1589  CE  LYS A 236    10838  10747  11050    150   -527     99       C  
ATOM   1590  NZ  LYS A 236       2.545  30.952  19.268  1.00 85.89           N  
ANISOU 1590  NZ  LYS A 236    10947  10749  10937    118   -474    145       N  
ATOM   1591  N   SER A 237      -2.635  34.981  17.766  1.00 77.56           N  
ANISOU 1591  N   SER A 237     9871   9381  10217    232  -1121    -16       N  
ATOM   1592  CA  SER A 237      -3.822  35.408  17.035  1.00 79.34           C  
ANISOU 1592  CA  SER A 237    10115   9511  10522    255  -1294    -54       C  
ATOM   1593  C   SER A 237      -3.531  35.617  15.556  1.00 76.18           C  
ANISOU 1593  C   SER A 237     9902   9038  10008    236  -1397    -16       C  
ATOM   1594  O   SER A 237      -4.454  35.543  14.739  1.00 69.48           O  
ANISOU 1594  O   SER A 237     9092   8106   9200    250  -1542    -42       O  
ATOM   1595  CB  SER A 237      -4.392  36.693  17.647  1.00 89.87           C  
ANISOU 1595  CB  SER A 237    11369  10817  11959    282  -1358    -89       C  
ATOM   1596  OG  SER A 237      -5.223  36.419  18.771  1.00 98.41           O  
ANISOU 1596  OG  SER A 237    12278  11926  13188    300  -1314   -152       O  
ATOM   1597  N   SER A 238      -2.279  35.888  15.197  1.00 70.26           N  
ANISOU 1597  N   SER A 238     9269   8309   9117    204  -1326     42       N  
ATOM   1598  CA  SER A 238      -1.907  35.966  13.801  1.00 65.55           C  
ANISOU 1598  CA  SER A 238     8866   7644   8396    174  -1396     78       C  
ATOM   1599  C   SER A 238      -1.732  34.556  13.267  1.00 77.21           C  
ANISOU 1599  C   SER A 238    10383   9135   9818    148  -1343     86       C  
ATOM   1600  O   SER A 238      -1.944  33.570  13.972  1.00 93.18           O  
ANISOU 1600  O   SER A 238    12282  11218  11905    158  -1262     65       O  
ATOM   1601  CB  SER A 238      -0.632  36.778  13.626  1.00 63.29           C  
ANISOU 1601  CB  SER A 238     8689   7369   7990    143  -1325    127       C  
ATOM   1602  OG  SER A 238       0.515  36.005  13.932  1.00 66.83           O  
ANISOU 1602  OG  SER A 238     9133   7894   8365    112  -1156    154       O  
ATOM   1603  N   GLY A 239      -1.334  34.441  12.015  1.00 77.81           N  
ANISOU 1603  N   GLY A 239    10638   9153   9773    112  -1384    117       N  
ATOM   1604  CA  GLY A 239      -1.131  33.101  11.518  1.00 74.46           C  
ANISOU 1604  CA  GLY A 239    10249   8744   9298     84  -1324    123       C  
ATOM   1605  C   GLY A 239       0.299  32.627  11.561  1.00 69.30           C  
ANISOU 1605  C   GLY A 239     9643   8151   8539     38  -1151    162       C  
ATOM   1606  O   GLY A 239       0.616  31.597  10.958  1.00 74.25           O  
ANISOU 1606  O   GLY A 239    10328   8777   9105      5  -1100    171       O  
ATOM   1607  N   ALA A1000       1.179  33.350  12.255  1.00 69.90           N  
ANISOU 1607  N   ALA A1000     9689   8273   8597     35  -1059    181       N  
ATOM   1608  CA  ALA A1000       2.599  33.030  12.190  1.00 68.04           C  
ANISOU 1608  CA  ALA A1000     9510   8078   8267    -10   -906    213       C  
ATOM   1609  C   ALA A1000       2.884  31.626  12.709  1.00 70.42           C  
ANISOU 1609  C   ALA A1000     9711   8450   8596    -14   -787    208       C  
ATOM   1610  O   ALA A1000       3.840  30.980  12.266  1.00 76.80           O  
ANISOU 1610  O   ALA A1000    10586   9266   9327    -58   -686    226       O  
ATOM   1611  CB  ALA A1000       3.401  34.071  12.964  1.00 59.14           C  
ANISOU 1611  CB  ALA A1000     8345   6987   7137     -4   -838    226       C  
ATOM   1612  N   SER A1001       2.058  31.125  13.619  1.00 66.84           N  
ANISOU 1612  N   SER A1001     9101   8041   8254     27   -796    180       N  
ATOM   1613  CA  SER A1001       2.293  29.832  14.229  1.00 73.11           C  
ANISOU 1613  CA  SER A1001     9797   8903   9079     25   -685    176       C  
ATOM   1614  C   SER A1001       1.088  28.929  14.008  1.00 70.30           C  
ANISOU 1614  C   SER A1001     9393   8527   8790     44   -756    143       C  
ATOM   1615  O   SER A1001      -0.050  29.403  13.886  1.00 66.56           O  
ANISOU 1615  O   SER A1001     8899   8006   8383     74   -884    113       O  
ATOM   1616  CB  SER A1001       2.591  29.973  15.731  1.00 70.53           C  
ANISOU 1616  CB  SER A1001     9322   8656   8819     51   -596    172       C  
ATOM   1617  OG  SER A1001       1.409  29.870  16.501  1.00 76.54           O  
ANISOU 1617  OG  SER A1001     9957   9430   9693     91   -645    134       O  
ATOM   1618  N   THR A1002       1.359  27.624  13.954  1.00 68.78           N  
ANISOU 1618  N   THR A1002     9181   8367   8587     26   -672    146       N  
ATOM   1619  CA  THR A1002       0.307  26.624  13.806  1.00 66.02           C  
ANISOU 1619  CA  THR A1002     8776   8006   8303     41   -718    114       C  
ATOM   1620  C   THR A1002      -0.461  26.456  15.110  1.00 61.51           C  
ANISOU 1620  C   THR A1002     8033   7481   7856     83   -699     80       C  
ATOM   1621  O   THR A1002       0.087  26.607  16.202  1.00 72.55           O  
ANISOU 1621  O   THR A1002     9352   8942   9273     90   -605     90       O  
ATOM   1622  CB  THR A1002       0.897  25.277  13.387  1.00 60.26           C  
ANISOU 1622  CB  THR A1002     8075   7298   7523      7   -622    128       C  
ATOM   1623  OG1 THR A1002       1.657  24.730  14.469  1.00 54.67           O  
ANISOU 1623  OG1 THR A1002     7266   6669   6836      8   -484    142       O  
ATOM   1624  CG2 THR A1002       1.808  25.449  12.188  1.00 66.65           C  
ANISOU 1624  CG2 THR A1002     9056   8062   8206    -45   -611    159       C  
ATOM   1625  N   ASP A1003      -1.740  26.110  14.987  1.00 60.08           N  
ANISOU 1625  N   ASP A1003     7798   7265   7764    108   -786     34       N  
ATOM   1626  CA  ASP A1003      -2.627  26.043  16.138  1.00 55.34           C  
ANISOU 1626  CA  ASP A1003     7042   6691   7294    143   -775    -11       C  
ATOM   1627  C   ASP A1003      -3.539  24.827  16.102  1.00 59.20           C  
ANISOU 1627  C   ASP A1003     7462   7172   7858    152   -777    -53       C  
ATOM   1628  O   ASP A1003      -4.612  24.850  16.710  1.00 57.70           O  
ANISOU 1628  O   ASP A1003     7161   6969   7792    180   -809   -108       O  
ATOM   1629  CB  ASP A1003      -3.492  27.292  16.227  1.00 62.99           C  
ANISOU 1629  CB  ASP A1003     7986   7607   8339    173   -899    -46       C  
ATOM   1630  CG  ASP A1003      -4.500  27.394  15.083  1.00 75.69           C  
ANISOU 1630  CG  ASP A1003     9656   9124   9980    184  -1064    -77       C  
ATOM   1631  OD1 ASP A1003      -4.146  27.065  13.928  1.00 74.98           O  
ANISOU 1631  OD1 ASP A1003     9698   8998   9792    159  -1102    -49       O  
ATOM   1632  OD2 ASP A1003      -5.656  27.796  15.345  1.00 79.05           O  
ANISOU 1632  OD2 ASP A1003     9997   9505  10532    217  -1156   -134       O  
ATOM   1633  N   TYR A1004      -3.144  23.759  15.402  1.00 69.50           N  
ANISOU 1633  N   TYR A1004     8826   8482   9099    126   -737    -32       N  
ATOM   1634  CA  TYR A1004      -3.975  22.558  15.315  1.00 67.05           C  
ANISOU 1634  CA  TYR A1004     8453   8164   8857    134   -735    -71       C  
ATOM   1635  C   TYR A1004      -3.103  21.305  15.254  1.00 62.34           C  
ANISOU 1635  C   TYR A1004     7875   7618   8193    103   -609    -37       C  
ATOM   1636  O   TYR A1004      -2.023  21.297  14.650  1.00 56.73           O  
ANISOU 1636  O   TYR A1004     7269   6914   7372     70   -570     10       O  
ATOM   1637  CB  TYR A1004      -4.907  22.611  14.098  1.00 69.15           C  
ANISOU 1637  CB  TYR A1004     8787   8344   9142    141   -890   -103       C  
ATOM   1638  CG  TYR A1004      -5.872  21.458  14.018  1.00 62.30           C  
ANISOU 1638  CG  TYR A1004     7845   7463   8364    152   -899   -153       C  
ATOM   1639  CD1 TYR A1004      -7.008  21.435  14.805  1.00 67.00           C  
ANISOU 1639  CD1 TYR A1004     8300   8047   9109    186   -919   -220       C  
ATOM   1640  CD2 TYR A1004      -5.652  20.395  13.153  1.00 63.92           C  
ANISOU 1640  CD2 TYR A1004     8118   7662   8508    127   -882   -140       C  
ATOM   1641  CE1 TYR A1004      -7.899  20.393  14.747  1.00 65.93           C  
ANISOU 1641  CE1 TYR A1004     8092   7894   9062    196   -920   -272       C  
ATOM   1642  CE2 TYR A1004      -6.553  19.340  13.083  1.00 68.92           C  
ANISOU 1642  CE2 TYR A1004     8678   8282   9227    139   -889   -189       C  
ATOM   1643  CZ  TYR A1004      -7.676  19.351  13.891  1.00 70.86           C  
ANISOU 1643  CZ  TYR A1004     8783   8517   9624    175   -908   -255       C  
ATOM   1644  OH  TYR A1004      -8.593  18.321  13.859  1.00 82.49           O  
ANISOU 1644  OH  TYR A1004    10176   9972  11192    186   -908   -312       O  
ATOM   1645  N   TRP A1005      -3.590  20.238  15.876  1.00 67.72           N  
ANISOU 1645  N   TRP A1005     8454   8329   8947    112   -542    -65       N  
ATOM   1646  CA  TRP A1005      -2.833  18.993  16.000  1.00 65.99           C  
ANISOU 1646  CA  TRP A1005     8230   8159   8683     88   -418    -36       C  
ATOM   1647  C   TRP A1005      -3.703  17.827  15.546  1.00 56.31           C  
ANISOU 1647  C   TRP A1005     6972   6910   7512     90   -434    -75       C  
ATOM   1648  O   TRP A1005      -4.755  17.561  16.137  1.00 53.35           O  
ANISOU 1648  O   TRP A1005     6494   6528   7248    116   -444   -128       O  
ATOM   1649  CB  TRP A1005      -2.338  18.796  17.438  1.00 59.82           C  
ANISOU 1649  CB  TRP A1005     7357   7448   7926     93   -295    -22       C  
ATOM   1650  CG  TRP A1005      -1.862  17.403  17.798  1.00 64.23           C  
ANISOU 1650  CG  TRP A1005     7881   8050   8475     78   -177     -5       C  
ATOM   1651  CD1 TRP A1005      -2.408  16.576  18.740  1.00 59.43           C  
ANISOU 1651  CD1 TRP A1005     7172   7468   7940     89   -109    -32       C  
ATOM   1652  CD2 TRP A1005      -0.733  16.694  17.250  1.00 53.82           C  
ANISOU 1652  CD2 TRP A1005     6628   6749   7072     45   -110     39       C  
ATOM   1653  NE1 TRP A1005      -1.708  15.401  18.796  1.00 54.65           N  
ANISOU 1653  NE1 TRP A1005     6570   6895   7300     69    -14     -2       N  
ATOM   1654  CE2 TRP A1005      -0.671  15.448  17.902  1.00 49.13           C  
ANISOU 1654  CE2 TRP A1005     5964   6192   6510     43    -13     40       C  
ATOM   1655  CE3 TRP A1005       0.211  16.984  16.251  1.00 53.13           C  
ANISOU 1655  CE3 TRP A1005     6653   6643   6890     15   -119     74       C  
ATOM   1656  CZ2 TRP A1005       0.306  14.494  17.610  1.00 47.97           C  
ANISOU 1656  CZ2 TRP A1005     5847   6065   6312     16     68     74       C  
ATOM   1657  CZ3 TRP A1005       1.198  16.039  15.969  1.00 58.73           C  
ANISOU 1657  CZ3 TRP A1005     7391   7372   7551    -17    -27    103       C  
ATOM   1658  CH2 TRP A1005       1.238  14.807  16.652  1.00 54.75           C  
ANISOU 1658  CH2 TRP A1005     6807   6907   7090    -14     62    103       C  
ATOM   1659  N   GLN A1006      -3.266  17.149  14.489  1.00 50.58           N  
ANISOU 1659  N   GLN A1006     6336   6169   6713     61   -432    -54       N  
ATOM   1660  CA  GLN A1006      -4.010  16.060  13.878  1.00 57.22           C  
ANISOU 1660  CA  GLN A1006     7164   6984   7592     59   -455    -88       C  
ATOM   1661  C   GLN A1006      -3.249  14.769  14.155  1.00 50.38           C  
ANISOU 1661  C   GLN A1006     6273   6172   6697     35   -314    -61       C  
ATOM   1662  O   GLN A1006      -2.057  14.673  13.851  1.00 60.25           O  
ANISOU 1662  O   GLN A1006     7595   7442   7854      2   -249    -13       O  
ATOM   1663  CB  GLN A1006      -4.181  16.326  12.376  1.00 63.87           C  
ANISOU 1663  CB  GLN A1006     8141   7756   8370     41   -576    -88       C  
ATOM   1664  CG  GLN A1006      -4.720  15.160  11.530  1.00 66.40           C  
ANISOU 1664  CG  GLN A1006     8479   8049   8703     30   -597   -115       C  
ATOM   1665  CD  GLN A1006      -6.243  15.128  11.467  1.00 75.35           C  
ANISOU 1665  CD  GLN A1006     9539   9130   9959     68   -714   -185       C  
ATOM   1666  OE1 GLN A1006      -6.926  15.852  12.202  1.00 84.71           O  
ANISOU 1666  OE1 GLN A1006    10641  10307  11240    104   -758   -220       O  
ATOM   1667  NE2 GLN A1006      -6.781  14.288  10.590  1.00 69.88           N  
ANISOU 1667  NE2 GLN A1006     8876   8400   9276     60   -762   -213       N  
ATOM   1668  N   ASN A1007      -3.912  13.798  14.781  1.00 53.66           N  
ANISOU 1668  N   ASN A1007     6583   6607   7198     51   -261    -95       N  
ATOM   1669  CA  ASN A1007      -3.269  12.502  15.089  1.00 49.57           C  
ANISOU 1669  CA  ASN A1007     6035   6135   6663     31   -131    -71       C  
ATOM   1670  C   ASN A1007      -4.359  11.432  15.000  1.00 49.92           C  
ANISOU 1670  C   ASN A1007     6010   6163   6795     42   -134   -124       C  
ATOM   1671  O   ASN A1007      -4.891  10.944  15.979  1.00 49.66           O  
ANISOU 1671  O   ASN A1007     5874   6152   6842     60    -74   -152       O  
ATOM   1672  CB  ASN A1007      -2.574  12.512  16.451  1.00 47.12           C  
ANISOU 1672  CB  ASN A1007     5661   5885   6357     35    -22    -42       C  
ATOM   1673  CG  ASN A1007      -1.819  11.223  16.739  1.00 60.60           C  
ANISOU 1673  CG  ASN A1007     7348   7633   8046     15     98    -12       C  
ATOM   1674  OD1 ASN A1007      -1.593  10.400  15.836  1.00 61.59           O  
ANISOU 1674  OD1 ASN A1007     7516   7745   8139     -9    112     -7       O  
ATOM   1675  ND2 ASN A1007      -1.445  11.025  18.011  1.00 55.99           N  
ANISOU 1675  ND2 ASN A1007     6701   7093   7481     23    185      5       N  
ATOM   1676  N   TRP A1008      -4.704  11.081  13.770  1.00 53.03           N  
ANISOU 1676  N   TRP A1008     6468   6513   7169     30   -205   -140       N  
ATOM   1677  CA  TRP A1008      -5.810  10.197  13.468  1.00 47.24           C  
ANISOU 1677  CA  TRP A1008     5679   5750   6519     42   -234   -197       C  
ATOM   1678  C   TRP A1008      -5.278   8.860  12.970  1.00 48.74           C  
ANISOU 1678  C   TRP A1008     5892   5961   6667     11   -148   -177       C  
ATOM   1679  O   TRP A1008      -4.518   8.803  11.996  1.00 56.22           O  
ANISOU 1679  O   TRP A1008     6948   6897   7518    -24   -156   -143       O  
ATOM   1680  CB  TRP A1008      -6.733  10.817  12.420  1.00 49.19           C  
ANISOU 1680  CB  TRP A1008     5981   5921   6787     55   -400   -239       C  
ATOM   1681  CG  TRP A1008      -7.889   9.948  12.154  1.00 53.75           C  
ANISOU 1681  CG  TRP A1008     6492   6466   7465     72   -435   -304       C  
ATOM   1682  CD1 TRP A1008      -9.049   9.903  12.858  1.00 50.53           C  
ANISOU 1682  CD1 TRP A1008     5962   6040   7198    107   -452   -373       C  
ATOM   1683  CD2 TRP A1008      -7.979   8.924  11.157  1.00 55.20           C  
ANISOU 1683  CD2 TRP A1008     6722   6630   7622     50   -442   -313       C  
ATOM   1684  NE1 TRP A1008      -9.864   8.938  12.349  1.00 56.02           N  
ANISOU 1684  NE1 TRP A1008     6621   6705   7961    112   -474   -425       N  
ATOM   1685  CE2 TRP A1008      -9.226   8.313  11.308  1.00 55.38           C  
ANISOU 1685  CE2 TRP A1008     6642   6624   7775     78   -471   -387       C  
ATOM   1686  CE3 TRP A1008      -7.119   8.460  10.157  1.00 56.56           C  
ANISOU 1686  CE3 TRP A1008     7010   6803   7676      6   -421   -269       C  
ATOM   1687  CZ2 TRP A1008      -9.647   7.270  10.485  1.00 53.14           C  
ANISOU 1687  CZ2 TRP A1008     6368   6315   7506     68   -487   -416       C  
ATOM   1688  CZ3 TRP A1008      -7.545   7.427   9.343  1.00 54.69           C  
ANISOU 1688  CZ3 TRP A1008     6787   6542   7450     -7   -435   -297       C  
ATOM   1689  CH2 TRP A1008      -8.799   6.858   9.503  1.00 52.73           C  
ANISOU 1689  CH2 TRP A1008     6437   6268   7331     26   -473   -369       C  
ATOM   1690  N   THR A1009      -5.700   7.791  13.627  1.00 46.78           N  
ANISOU 1690  N   THR A1009     5544   5737   6493     20    -65   -203       N  
ATOM   1691  CA  THR A1009      -5.414   6.437  13.191  1.00 49.64           C  
ANISOU 1691  CA  THR A1009     5909   6112   6839     -4     11   -195       C  
ATOM   1692  C   THR A1009      -6.708   5.643  13.101  1.00 56.05           C  
ANISOU 1692  C   THR A1009     6642   6896   7758     16    -13   -265       C  
ATOM   1693  O   THR A1009      -7.594   5.762  13.959  1.00 67.21           O  
ANISOU 1693  O   THR A1009     7959   8305   9274     46    -10   -312       O  
ATOM   1694  CB  THR A1009      -4.422   5.723  14.150  1.00 49.44           C  
ANISOU 1694  CB  THR A1009     5842   6149   6794    -18    161   -149       C  
ATOM   1695  OG1 THR A1009      -4.310   4.332  13.801  1.00 65.14           O  
ANISOU 1695  OG1 THR A1009     7814   8147   8789    -37    234   -151       O  
ATOM   1696  CG2 THR A1009      -4.846   5.889  15.606  1.00 42.19           C  
ANISOU 1696  CG2 THR A1009     4824   5256   5949     11    210   -164       C  
ATOM   1697  N   PHE A1010      -6.805   4.846  12.044  1.00 55.33           N  
ANISOU 1697  N   PHE A1010     6596   6783   7646     -4    -32   -275       N  
ATOM   1698  CA  PHE A1010      -7.995   4.051  11.862  1.00 54.70           C  
ANISOU 1698  CA  PHE A1010     6443   6672   7667     14    -57   -344       C  
ATOM   1699  C   PHE A1010      -7.934   2.866  12.818  1.00 59.85           C  
ANISOU 1699  C   PHE A1010     6997   7370   8373     14     92   -346       C  
ATOM   1700  O   PHE A1010      -8.911   2.546  13.509  1.00 51.15           O  
ANISOU 1700  O   PHE A1010     5793   6259   7384     39    114   -404       O  
ATOM   1701  CB  PHE A1010      -8.129   3.718  10.366  1.00 60.14           C  
ANISOU 1701  CB  PHE A1010     7226   7316   8308     -9   -142   -355       C  
ATOM   1702  CG  PHE A1010      -9.403   2.985  10.008  1.00 59.83           C  
ANISOU 1702  CG  PHE A1010     7121   7236   8376     11   -194   -433       C  
ATOM   1703  CD1 PHE A1010     -10.655   3.595  10.018  1.00 70.79           C  
ANISOU 1703  CD1 PHE A1010     8458   8567   9872     51   -318   -503       C  
ATOM   1704  CD2 PHE A1010      -9.311   1.660   9.524  1.00 68.74           C  
ANISOU 1704  CD2 PHE A1010     8244   8374   9498    -12   -125   -438       C  
ATOM   1705  CE1 PHE A1010     -11.776   2.890   9.728  1.00 73.64           C  
ANISOU 1705  CE1 PHE A1010     8750   8887  10342     70   -358   -579       C  
ATOM   1706  CE2 PHE A1010     -10.546   0.934   9.165  1.00 78.67           C  
ANISOU 1706  CE2 PHE A1010     9435   9590  10866      8   -174   -517       C  
ATOM   1707  CZ  PHE A1010     -11.746   1.578   9.309  1.00 76.32           C  
ANISOU 1707  CZ  PHE A1010     9079   9240  10680     50   -289   -587       C  
ATOM   1708  N   GLY A1011      -6.771   2.227  12.913  1.00 69.05           N  
ANISOU 1708  N   GLY A1011     8192   8581   9463    -17    199   -286       N  
ATOM   1709  CA  GLY A1011      -6.548   1.344  14.047  1.00 56.82           C  
ANISOU 1709  CA  GLY A1011     6561   7076   7953    -15    336   -274       C  
ATOM   1710  C   GLY A1011      -5.555   0.211  13.956  1.00 54.92           C  
ANISOU 1710  C   GLY A1011     6334   6869   7664    -46    446   -227       C  
ATOM   1711  O   GLY A1011      -5.142  -0.305  14.997  1.00 67.19           O  
ANISOU 1711  O   GLY A1011     7838   8459   9232    -44    549   -202       O  
ATOM   1712  N   GLY A1012      -5.191  -0.223  12.754  1.00 53.56           N  
ANISOU 1712  N   GLY A1012     6229   6682   7439    -76    427   -219       N  
ATOM   1713  CA  GLY A1012      -4.221  -1.295  12.625  1.00 50.75           C  
ANISOU 1713  CA  GLY A1012     5881   6353   7048   -109    534   -180       C  
ATOM   1714  C   GLY A1012      -2.782  -0.792  12.690  1.00 56.10           C  
ANISOU 1714  C   GLY A1012     6622   7052   7640   -134    571   -115       C  
ATOM   1715  O   GLY A1012      -2.452   0.292  12.200  1.00 51.58           O  
ANISOU 1715  O   GLY A1012     6129   6464   7006   -143    500   -101       O  
ATOM   1716  N   GLY A1013      -1.911  -1.619  13.300  1.00 53.24           N  
ANISOU 1716  N   GLY A1013     6225   6722   7281   -147    682    -78       N  
ATOM   1717  CA  GLY A1013      -0.491  -1.318  13.423  1.00 50.23           C  
ANISOU 1717  CA  GLY A1013     5886   6358   6840   -171    727    -23       C  
ATOM   1718  C   GLY A1013      -0.202  -0.304  14.518  1.00 45.92           C  
ANISOU 1718  C   GLY A1013     5327   5833   6287   -144    714      3       C  
ATOM   1719  O   GLY A1013      -1.028  -0.049  15.388  1.00 45.46           O  
ANISOU 1719  O   GLY A1013     5215   5783   6276   -110    697    -16       O  
ATOM   1720  N   ILE A1014       0.991   0.288  14.469  1.00 43.05           N  
ANISOU 1720  N   ILE A1014     5014   5475   5868   -164    727     44       N  
ATOM   1721  CA  ILE A1014       1.406   1.251  15.485  1.00 51.89           C  
ANISOU 1721  CA  ILE A1014     6124   6615   6977   -141    716     72       C  
ATOM   1722  C   ILE A1014       1.714   2.584  14.829  1.00 48.00           C  
ANISOU 1722  C   ILE A1014     5714   6103   6420   -152    643     77       C  
ATOM   1723  O   ILE A1014       2.521   2.653  13.900  1.00 58.00           O  
ANISOU 1723  O   ILE A1014     7050   7350   7635   -190    654     88       O  
ATOM   1724  CB  ILE A1014       2.607   0.765  16.324  1.00 66.86           C  
ANISOU 1724  CB  ILE A1014     7991   8535   8879   -147    800    116       C  
ATOM   1725  CG1 ILE A1014       3.116   1.907  17.214  1.00 73.11           C  
ANISOU 1725  CG1 ILE A1014     8789   9342   9647   -128    777    144       C  
ATOM   1726  CG2 ILE A1014       3.717   0.248  15.458  1.00 75.81           C  
ANISOU 1726  CG2 ILE A1014     9162   9653   9988   -190    849    131       C  
ATOM   1727  CD1 ILE A1014       3.831   1.442  18.483  1.00 81.83           C  
ANISOU 1727  CD1 ILE A1014     9846  10470  10776   -116    838    179       C  
ATOM   1728  N   VAL A1015       1.074   3.637  15.328  1.00 59.50           N  
ANISOU 1728  N   VAL A1015     7163   7561   7882   -121    575     66       N  
ATOM   1729  CA  VAL A1015       1.250   5.006  14.845  1.00 56.46           C  
ANISOU 1729  CA  VAL A1015     6853   7158   7443   -124    497     70       C  
ATOM   1730  C   VAL A1015       1.708   5.824  16.051  1.00 53.04           C  
ANISOU 1730  C   VAL A1015     6388   6753   7010   -101    508     97       C  
ATOM   1731  O   VAL A1015       0.898   6.353  16.817  1.00 47.71           O  
ANISOU 1731  O   VAL A1015     5669   6086   6373    -68    472     79       O  
ATOM   1732  CB  VAL A1015      -0.036   5.561  14.224  1.00 43.79           C  
ANISOU 1732  CB  VAL A1015     5270   5518   5851   -108    388     26       C  
ATOM   1733  CG1 VAL A1015       0.122   7.034  13.799  1.00 50.06           C  
ANISOU 1733  CG1 VAL A1015     6144   6288   6588   -109    300     34       C  
ATOM   1734  CG2 VAL A1015      -0.432   4.693  13.062  1.00 42.52           C  
ANISOU 1734  CG2 VAL A1015     5144   5327   5686   -132    375      1       C  
ATOM   1735  N   ASN A1016       3.025   5.929  16.239  1.00 46.31           N  
ANISOU 1735  N   ASN A1016     5557   5914   6125   -119    562    136       N  
ATOM   1736  CA  ASN A1016       3.596   6.590  17.418  1.00 49.20           C  
ANISOU 1736  CA  ASN A1016     5894   6308   6492    -99    577    163       C  
ATOM   1737  C   ASN A1016       3.978   8.033  17.074  1.00 44.35           C  
ANISOU 1737  C   ASN A1016     5345   5681   5826   -102    519    170       C  
ATOM   1738  O   ASN A1016       5.043   8.305  16.534  1.00 48.96           O  
ANISOU 1738  O   ASN A1016     5983   6252   6368   -131    541    188       O  
ATOM   1739  CB  ASN A1016       4.775   5.782  17.926  1.00 53.42           C  
ANISOU 1739  CB  ASN A1016     6401   6859   7038   -112    663    196       C  
ATOM   1740  CG  ASN A1016       5.387   6.361  19.162  1.00 53.93           C  
ANISOU 1740  CG  ASN A1016     6438   6948   7104    -90    673    224       C  
ATOM   1741  OD1 ASN A1016       4.743   7.090  19.922  1.00 58.48           O  
ANISOU 1741  OD1 ASN A1016     6995   7538   7686    -63    636    218       O  
ATOM   1742  ND2 ASN A1016       6.639   6.016  19.396  1.00 52.58           N  
ANISOU 1742  ND2 ASN A1016     6263   6779   6937   -104    724    252       N  
ATOM   1743  N   ALA A1017       3.100   8.970  17.404  1.00 47.42           N  
ANISOU 1743  N   ALA A1017     5725   6069   6225    -74    448    152       N  
ATOM   1744  CA  ALA A1017       3.226  10.353  16.965  1.00 47.71           C  
ANISOU 1744  CA  ALA A1017     5826   6086   6215    -76    378    154       C  
ATOM   1745  C   ALA A1017       3.473  11.264  18.157  1.00 53.26           C  
ANISOU 1745  C   ALA A1017     6493   6818   6927    -50    378    169       C  
ATOM   1746  O   ALA A1017       2.697  11.256  19.119  1.00 64.02           O  
ANISOU 1746  O   ALA A1017     7789   8198   8338    -22    374    154       O  
ATOM   1747  CB  ALA A1017       1.966  10.798  16.216  1.00 46.24           C  
ANISOU 1747  CB  ALA A1017     5668   5863   6037    -66    278    116       C  
ATOM   1748  N   VAL A1018       4.532  12.069  18.075  1.00 53.73           N  
ANISOU 1748  N   VAL A1018     6599   6877   6940    -63    384    195       N  
ATOM   1749  CA  VAL A1018       4.916  13.000  19.135  1.00 55.38           C  
ANISOU 1749  CA  VAL A1018     6780   7111   7150    -42    382    211       C  
ATOM   1750  C   VAL A1018       4.481  14.409  18.753  1.00 52.65           C  
ANISOU 1750  C   VAL A1018     6481   6745   6780    -33    298    198       C  
ATOM   1751  O   VAL A1018       4.840  14.904  17.678  1.00 51.44           O  
ANISOU 1751  O   VAL A1018     6411   6557   6575    -58    269    200       O  
ATOM   1752  CB  VAL A1018       6.434  12.949  19.381  1.00 54.70           C  
ANISOU 1752  CB  VAL A1018     6704   7037   7043    -59    447    243       C  
ATOM   1753  CG1 VAL A1018       6.819  13.849  20.526  1.00 41.47           C  
ANISOU 1753  CG1 VAL A1018     4998   5387   5371    -36    442    258       C  
ATOM   1754  CG2 VAL A1018       6.898  11.500  19.637  1.00 45.68           C  
ANISOU 1754  CG2 VAL A1018     5519   5904   5932    -69    522    254       C  
ATOM   1755  N   ASN A1019       3.725  15.065  19.635  1.00 56.80           N  
ANISOU 1755  N   ASN A1019     6956   7284   7341     -3    262    184       N  
ATOM   1756  CA  ASN A1019       3.347  16.476  19.454  1.00 54.66           C  
ANISOU 1756  CA  ASN A1019     6717   6994   7057      9    182    172       C  
ATOM   1757  C   ASN A1019       4.445  17.346  20.073  1.00 60.47           C  
ANISOU 1757  C   ASN A1019     7461   7753   7761      9    210    201       C  
ATOM   1758  O   ASN A1019       4.371  17.766  21.232  1.00 52.20           O  
ANISOU 1758  O   ASN A1019     6358   6734   6739     30    221    203       O  
ATOM   1759  CB  ASN A1019       1.974  16.753  20.059  1.00 48.25           C  
ANISOU 1759  CB  ASN A1019     5840   6180   6314     39    133    133       C  
ATOM   1760  CG  ASN A1019       1.588  18.232  20.020  1.00 54.95           C  
ANISOU 1760  CG  ASN A1019     6708   7008   7164     54     50    119       C  
ATOM   1761  OD1 ASN A1019       2.274  19.055  19.436  1.00 54.60           O  
ANISOU 1761  OD1 ASN A1019     6735   6949   7063     43     22    140       O  
ATOM   1762  ND2 ASN A1019       0.473  18.563  20.644  1.00 58.37           N  
ANISOU 1762  ND2 ASN A1019     7074   7435   7669     78     15     80       N  
ATOM   1763  N   GLY A1020       5.461  17.641  19.267  1.00 55.75           N  
ANISOU 1763  N   GLY A1020     6938   7136   7107    -18    222    220       N  
ATOM   1764  CA  GLY A1020       6.665  18.288  19.732  1.00 61.82           C  
ANISOU 1764  CA  GLY A1020     7714   7921   7851    -22    261    244       C  
ATOM   1765  C   GLY A1020       6.505  19.783  19.967  1.00 66.89           C  
ANISOU 1765  C   GLY A1020     8373   8560   8481     -6    203    241       C  
ATOM   1766  O   GLY A1020       5.406  20.338  19.987  1.00 55.81           O  
ANISOU 1766  O   GLY A1020     6959   7146   7100     13    133    220       O  
ATOM   1767  N   SER A1021       7.664  20.437  20.133  1.00 75.99           N  
ANISOU 1767  N   SER A1021     9548   9718   9606    -16    236    259       N  
ATOM   1768  CA  SER A1021       7.732  21.838  20.549  1.00 81.19           C  
ANISOU 1768  CA  SER A1021    10212  10381  10255      0    198    259       C  
ATOM   1769  C   SER A1021       7.332  22.763  19.405  1.00 80.01           C  
ANISOU 1769  C   SER A1021    10152  10183  10064    -12    126    249       C  
ATOM   1770  O   SER A1021       7.995  22.791  18.361  1.00 81.43           O  
ANISOU 1770  O   SER A1021    10420  10326  10193    -47    142    255       O  
ATOM   1771  CB  SER A1021       9.143  22.184  21.027  1.00 84.06           C  
ANISOU 1771  CB  SER A1021    10571  10760  10607     -8    258    278       C  
ATOM   1772  OG  SER A1021       9.550  21.401  22.139  1.00 89.93           O  
ANISOU 1772  OG  SER A1021    11240  11543  11387      5    309    289       O  
ATOM   1773  N   GLY A1022       6.266  23.537  19.612  1.00 74.49           N  
ANISOU 1773  N   GLY A1022     9435   9476   9389     13     46    232       N  
ATOM   1774  CA  GLY A1022       5.874  24.552  18.655  1.00 73.50           C  
ANISOU 1774  CA  GLY A1022     9396   9301   9230      7    -38    224       C  
ATOM   1775  C   GLY A1022       5.171  23.990  17.436  1.00 82.81           C  
ANISOU 1775  C   GLY A1022    10644  10431  10390     -9    -94    212       C  
ATOM   1776  O   GLY A1022       4.088  23.409  17.553  1.00 87.86           O  
ANISOU 1776  O   GLY A1022    11231  11069  11082     10   -133    189       O  
ATOM   1777  N   GLY A1023       5.764  24.166  16.258  1.00 81.31           N  
ANISOU 1777  N   GLY A1023    10574  10194  10124    -47    -96    223       N  
ATOM   1778  CA  GLY A1023       5.230  23.618  15.029  1.00 71.07           C  
ANISOU 1778  CA  GLY A1023     9364   8847   8795    -70   -145    214       C  
ATOM   1779  C   GLY A1023       5.836  22.297  14.601  1.00 72.03           C  
ANISOU 1779  C   GLY A1023     9498   8974   8896   -104    -57    219       C  
ATOM   1780  O   GLY A1023       5.538  21.829  13.497  1.00 70.34           O  
ANISOU 1780  O   GLY A1023     9370   8714   8642   -132    -88    212       O  
ATOM   1781  N   ASN A1024       6.665  21.674  15.439  1.00 71.81           N  
ANISOU 1781  N   ASN A1024     9391   8997   8898   -104     46    230       N  
ATOM   1782  CA  ASN A1024       7.325  20.413  15.120  1.00 64.48           C  
ANISOU 1782  CA  ASN A1024     8462   8073   7964   -135    135    234       C  
ATOM   1783  C   ASN A1024       6.475  19.215  15.555  1.00 68.73           C  
ANISOU 1783  C   ASN A1024     8911   8640   8562   -112    136    223       C  
ATOM   1784  O   ASN A1024       5.768  19.256  16.565  1.00 67.19           O  
ANISOU 1784  O   ASN A1024     8622   8480   8426    -71    112    217       O  
ATOM   1785  CB  ASN A1024       8.697  20.365  15.795  1.00 51.53           C  
ANISOU 1785  CB  ASN A1024     6780   6463   6335   -145    237    249       C  
ATOM   1786  CG  ASN A1024       9.428  19.058  15.560  1.00 60.73           C  
ANISOU 1786  CG  ASN A1024     7931   7630   7513   -175    330    249       C  
ATOM   1787  OD1 ASN A1024       9.582  18.256  16.476  1.00 68.24           O  
ANISOU 1787  OD1 ASN A1024     8785   8624   8521   -154    374    256       O  
ATOM   1788  ND2 ASN A1024       9.908  18.847  14.335  1.00 66.29           N  
ANISOU 1788  ND2 ASN A1024     8737   8284   8165   -228    362    241       N  
ATOM   1789  N   TYR A1025       6.519  18.154  14.756  1.00 68.68           N  
ANISOU 1789  N   TYR A1025     8939   8613   8541   -143    167    218       N  
ATOM   1790  CA  TYR A1025       5.960  16.872  15.160  1.00 55.75           C  
ANISOU 1790  CA  TYR A1025     7217   7004   6960   -128    194    209       C  
ATOM   1791  C   TYR A1025       6.813  15.769  14.559  1.00 47.44           C  
ANISOU 1791  C   TYR A1025     6191   5942   5891   -171    283    214       C  
ATOM   1792  O   TYR A1025       7.576  15.993  13.620  1.00 47.86           O  
ANISOU 1792  O   TYR A1025     6342   5957   5887   -216    310    216       O  
ATOM   1793  CB  TYR A1025       4.486  16.722  14.747  1.00 55.91           C  
ANISOU 1793  CB  TYR A1025     7238   7002   7004   -108     98    182       C  
ATOM   1794  CG  TYR A1025       4.230  16.569  13.263  1.00 54.71           C  
ANISOU 1794  CG  TYR A1025     7203   6790   6794   -144     50    171       C  
ATOM   1795  CD1 TYR A1025       4.473  15.365  12.615  1.00 54.53           C  
ANISOU 1795  CD1 TYR A1025     7201   6758   6758   -178    107    168       C  
ATOM   1796  CD2 TYR A1025       3.700  17.622  12.514  1.00 49.68           C  
ANISOU 1796  CD2 TYR A1025     6660   6101   6115   -145    -60    163       C  
ATOM   1797  CE1 TYR A1025       4.243  15.219  11.254  1.00 51.76           C  
ANISOU 1797  CE1 TYR A1025     6969   6351   6348   -216     63    157       C  
ATOM   1798  CE2 TYR A1025       3.450  17.479  11.161  1.00 51.75           C  
ANISOU 1798  CE2 TYR A1025     7045   6302   6314   -181   -114    154       C  
ATOM   1799  CZ  TYR A1025       3.725  16.274  10.540  1.00 50.78           C  
ANISOU 1799  CZ  TYR A1025     6947   6173   6174   -217    -50    151       C  
ATOM   1800  OH  TYR A1025       3.486  16.111   9.209  1.00 53.92           O  
ANISOU 1800  OH  TYR A1025     7474   6509   6504   -258   -100    141       O  
ATOM   1801  N   SER A1026       6.684  14.571  15.121  1.00 48.84           N  
ANISOU 1801  N   SER A1026     6282   6152   6122   -159    334    214       N  
ATOM   1802  CA  SER A1026       7.318  13.383  14.563  1.00 45.98           C  
ANISOU 1802  CA  SER A1026     5931   5780   5759   -197    414    214       C  
ATOM   1803  C   SER A1026       6.316  12.245  14.539  1.00 46.24           C  
ANISOU 1803  C   SER A1026     5914   5822   5833   -184    403    198       C  
ATOM   1804  O   SER A1026       5.409  12.172  15.376  1.00 49.98           O  
ANISOU 1804  O   SER A1026     6311   6323   6356   -142    369    191       O  
ATOM   1805  CB  SER A1026       8.541  12.951  15.365  1.00 45.38           C  
ANISOU 1805  CB  SER A1026     5792   5731   5720   -200    507    231       C  
ATOM   1806  OG  SER A1026       8.181  12.532  16.678  1.00 55.14           O  
ANISOU 1806  OG  SER A1026     6922   7014   7015   -156    512    241       O  
ATOM   1807  N   VAL A1027       6.491  11.334  13.597  1.00 43.99           N  
ANISOU 1807  N   VAL A1027     5671   5512   5532   -223    442    189       N  
ATOM   1808  CA  VAL A1027       5.710  10.106  13.627  1.00 54.48           C  
ANISOU 1808  CA  VAL A1027     6943   6852   6906   -213    451    175       C  
ATOM   1809  C   VAL A1027       6.623   8.923  13.334  1.00 43.94           C  
ANISOU 1809  C   VAL A1027     5597   5516   5584   -251    554    180       C  
ATOM   1810  O   VAL A1027       7.505   8.991  12.478  1.00 45.51           O  
ANISOU 1810  O   VAL A1027     5871   5680   5739   -300    597    179       O  
ATOM   1811  CB  VAL A1027       4.492  10.159  12.663  1.00 51.21           C  
ANISOU 1811  CB  VAL A1027     6586   6402   6472   -214    359    147       C  
ATOM   1812  CG1 VAL A1027       4.922  10.535  11.269  1.00 66.21           C  
ANISOU 1812  CG1 VAL A1027     8624   8245   8286   -268    343    143       C  
ATOM   1813  CG2 VAL A1027       3.739   8.819  12.663  1.00 41.80           C  
ANISOU 1813  CG2 VAL A1027     5330   5220   5333   -206    379    127       C  
ATOM   1814  N   ASN A1028       6.427   7.849  14.084  1.00 48.26           N  
ANISOU 1814  N   ASN A1028     6049   6094   6194   -230    598    183       N  
ATOM   1815  CA  ASN A1028       6.969   6.537  13.777  1.00 43.54           C  
ANISOU 1815  CA  ASN A1028     5428   5492   5623   -260    682    181       C  
ATOM   1816  C   ASN A1028       5.792   5.584  13.631  1.00 48.29           C  
ANISOU 1816  C   ASN A1028     5993   6099   6256   -245    664    161       C  
ATOM   1817  O   ASN A1028       4.965   5.460  14.546  1.00 44.96           O  
ANISOU 1817  O   ASN A1028     5498   5705   5878   -202    639    158       O  
ATOM   1818  CB  ASN A1028       7.939   6.069  14.858  1.00 42.23           C  
ANISOU 1818  CB  ASN A1028     5183   5354   5510   -247    754    206       C  
ATOM   1819  CG  ASN A1028       9.373   6.509  14.575  1.00 67.12           C  
ANISOU 1819  CG  ASN A1028     8372   8482   8648   -282    804    212       C  
ATOM   1820  OD1 ASN A1028      10.194   5.729  14.073  1.00 73.97           O  
ANISOU 1820  OD1 ASN A1028     9240   9326   9536   -322    879    205       O  
ATOM   1821  ND2 ASN A1028       9.681   7.765  14.894  1.00 72.98           N  
ANISOU 1821  ND2 ASN A1028     9141   9227   9362   -270    768    222       N  
ATOM   1822  N   TRP A1029       5.693   4.951  12.462  1.00 47.02           N  
ANISOU 1822  N   TRP A1029     5887   5908   6073   -286    677    142       N  
ATOM   1823  CA  TRP A1029       4.593   4.057  12.162  1.00 44.18           C  
ANISOU 1823  CA  TRP A1029     5498   5546   5741   -276    657    116       C  
ATOM   1824  C   TRP A1029       5.112   2.745  11.575  1.00 45.85           C  
ANISOU 1824  C   TRP A1029     5704   5747   5969   -318    744    111       C  
ATOM   1825  O   TRP A1029       6.208   2.689  11.003  1.00 49.20           O  
ANISOU 1825  O   TRP A1029     6179   6150   6366   -366    805    116       O  
ATOM   1826  CB  TRP A1029       3.586   4.765  11.232  1.00 44.45           C  
ANISOU 1826  CB  TRP A1029     5615   5545   5731   -277    548     90       C  
ATOM   1827  CG  TRP A1029       3.909   4.783   9.754  1.00 46.17           C  
ANISOU 1827  CG  TRP A1029     5958   5712   5874   -336    542     78       C  
ATOM   1828  CD1 TRP A1029       3.495   3.886   8.823  1.00 45.62           C  
ANISOU 1828  CD1 TRP A1029     5921   5618   5796   -366    546     54       C  
ATOM   1829  CD2 TRP A1029       4.662   5.769   9.047  1.00 48.10           C  
ANISOU 1829  CD2 TRP A1029     6320   5919   6036   -376    530     88       C  
ATOM   1830  NE1 TRP A1029       3.934   4.238   7.590  1.00 44.95           N  
ANISOU 1830  NE1 TRP A1029     5973   5482   5626   -424    537     49       N  
ATOM   1831  CE2 TRP A1029       4.673   5.385   7.692  1.00 54.77           C  
ANISOU 1831  CE2 TRP A1029     7273   6715   6822   -434    532     69       C  
ATOM   1832  CE3 TRP A1029       5.330   6.940   9.425  1.00 46.76           C  
ANISOU 1832  CE3 TRP A1029     6178   5751   5837   -372    522    109       C  
ATOM   1833  CZ2 TRP A1029       5.331   6.132   6.702  1.00 56.33           C  
ANISOU 1833  CZ2 TRP A1029     7617   6861   6926   -491    531     71       C  
ATOM   1834  CZ3 TRP A1029       5.975   7.672   8.455  1.00 50.20           C  
ANISOU 1834  CZ3 TRP A1029     6748   6138   6188   -424    521    110       C  
ATOM   1835  CH2 TRP A1029       5.971   7.269   7.106  1.00 50.95           C  
ANISOU 1835  CH2 TRP A1029     6959   6181   6220   -485    528     91       C  
ATOM   1836  N   SER A1030       4.333   1.671  11.751  1.00 51.42           N  
ANISOU 1836  N   SER A1030     6344   6467   6727   -301    758     95       N  
ATOM   1837  CA  SER A1030       4.698   0.389  11.143  1.00 63.91           C  
ANISOU 1837  CA  SER A1030     7918   8038   8328   -340    837     85       C  
ATOM   1838  C   SER A1030       3.486  -0.536  11.000  1.00 52.32           C  
ANISOU 1838  C   SER A1030     6405   6574   6901   -322    819     56       C  
ATOM   1839  O   SER A1030       2.641  -0.616  11.892  1.00 50.10           O  
ANISOU 1839  O   SER A1030     6051   6318   6669   -274    794     51       O  
ATOM   1840  CB  SER A1030       5.815  -0.306  11.935  1.00 62.53           C  
ANISOU 1840  CB  SER A1030     7672   7882   8204   -343    935    112       C  
ATOM   1841  OG  SER A1030       5.306  -0.959  13.072  1.00 61.46           O  
ANISOU 1841  OG  SER A1030     7439   7781   8132   -298    948    121       O  
ATOM   1842  N   ASN A1031       3.413  -1.203   9.847  1.00 50.73           N  
ANISOU 1842  N   ASN A1031     6254   6343   6678   -365    836     33       N  
ATOM   1843  CA  ASN A1031       2.372  -2.174   9.488  1.00 49.37           C  
ANISOU 1843  CA  ASN A1031     6048   6168   6543   -358    825      0       C  
ATOM   1844  C   ASN A1031       0.973  -1.669   9.813  1.00 53.04           C  
ANISOU 1844  C   ASN A1031     6486   6634   7033   -307    723    -26       C  
ATOM   1845  O   ASN A1031       0.170  -2.368  10.438  1.00 58.93           O  
ANISOU 1845  O   ASN A1031     7141   7399   7851   -273    736    -45       O  
ATOM   1846  CB  ASN A1031       2.630  -3.530  10.154  1.00 46.64           C  
ANISOU 1846  CB  ASN A1031     5599   5849   6272   -353    927      7       C  
ATOM   1847  CG  ASN A1031       2.468  -4.703   9.190  1.00 48.05           C  
ANISOU 1847  CG  ASN A1031     5787   6010   6462   -392    971    -20       C  
ATOM   1848  OD1 ASN A1031       3.142  -4.781   8.158  1.00 56.37           O  
ANISOU 1848  OD1 ASN A1031     6919   7033   7466   -449   1001    -25       O  
ATOM   1849  ND2 ASN A1031       1.585  -5.626   9.531  1.00 45.25           N  
ANISOU 1849  ND2 ASN A1031     5353   5669   6170   -364    984    -41       N  
ATOM   1850  N   THR A1032       0.667  -0.461   9.328  1.00 48.71           N  
ANISOU 1850  N   THR A1032     6018   6058   6429   -305    622    -33       N  
ATOM   1851  CA  THR A1032      -0.550   0.263   9.670  1.00 46.04           C  
ANISOU 1851  CA  THR A1032     5657   5715   6123   -256    515    -59       C  
ATOM   1852  C   THR A1032      -1.634   0.051   8.620  1.00 53.37           C  
ANISOU 1852  C   THR A1032     6627   6600   7052   -260    425   -106       C  
ATOM   1853  O   THR A1032      -1.396  -0.464   7.527  1.00 65.77           O  
ANISOU 1853  O   THR A1032     8271   8142   8575   -305    435   -114       O  
ATOM   1854  CB  THR A1032      -0.277   1.774   9.802  1.00 52.62           C  
ANISOU 1854  CB  THR A1032     6550   6538   6904   -246    444    -39       C  
ATOM   1855  OG1 THR A1032      -0.112   2.336   8.493  1.00 58.63           O  
ANISOU 1855  OG1 THR A1032     7448   7250   7579   -287    379    -43       O  
ATOM   1856  CG2 THR A1032       0.977   2.068  10.620  1.00 46.11           C  
ANISOU 1856  CG2 THR A1032     5707   5747   6064   -252    527      7       C  
ATOM   1857  N   GLY A1033      -2.844   0.474   8.970  1.00 59.03           N  
ANISOU 1857  N   GLY A1033     7295   7305   7828   -212    334   -143       N  
ATOM   1858  CA  GLY A1033      -3.866   0.775   7.986  1.00 53.14           C  
ANISOU 1858  CA  GLY A1033     6606   6504   7079   -208    204   -187       C  
ATOM   1859  C   GLY A1033      -3.796   2.264   7.702  1.00 49.47           C  
ANISOU 1859  C   GLY A1033     6234   6008   6553   -204     95   -174       C  
ATOM   1860  O   GLY A1033      -2.697   2.817   7.701  1.00 56.52           O  
ANISOU 1860  O   GLY A1033     7192   6913   7370   -232    137   -128       O  
ATOM   1861  N   ASN A1034      -4.925   2.941   7.519  1.00 49.09           N  
ANISOU 1861  N   ASN A1034     6188   5919   6545   -169    -42   -215       N  
ATOM   1862  CA  ASN A1034      -4.887   4.366   7.217  1.00 51.99           C  
ANISOU 1862  CA  ASN A1034     6647   6250   6856   -165   -154   -202       C  
ATOM   1863  C   ASN A1034      -4.599   5.201   8.464  1.00 50.08           C  
ANISOU 1863  C   ASN A1034     6335   6048   6643   -133   -122   -178       C  
ATOM   1864  O   ASN A1034      -5.200   4.991   9.521  1.00 52.32           O  
ANISOU 1864  O   ASN A1034     6492   6360   7028    -92    -92   -203       O  
ATOM   1865  CB  ASN A1034      -6.194   4.830   6.565  1.00 52.31           C  
ANISOU 1865  CB  ASN A1034     6714   6222   6938   -137   -327   -256       C  
ATOM   1866  CG  ASN A1034      -5.975   6.049   5.678  1.00 80.32           C  
ANISOU 1866  CG  ASN A1034    10420   9714  10385   -157   -449   -236       C  
ATOM   1867  OD1 ASN A1034      -6.216   7.195   6.081  1.00 86.91           O  
ANISOU 1867  OD1 ASN A1034    11251  10535  11237   -126   -528   -235       O  
ATOM   1868  ND2 ASN A1034      -5.459   5.808   4.475  1.00 86.40           N  
ANISOU 1868  ND2 ASN A1034    11336  10449  11045   -213   -458   -219       N  
ATOM   1869  N   PHE A1035      -3.686   6.162   8.331  1.00 47.84           N  
ANISOU 1869  N   PHE A1035     6142   5764   6271   -154   -126   -134       N  
ATOM   1870  CA  PHE A1035      -3.454   7.145   9.377  1.00 47.03           C  
ANISOU 1870  CA  PHE A1035     5992   5690   6188   -124   -119   -114       C  
ATOM   1871  C   PHE A1035      -3.045   8.466   8.735  1.00 49.40           C  
ANISOU 1871  C   PHE A1035     6422   5951   6397   -141   -206    -91       C  
ATOM   1872  O   PHE A1035      -2.488   8.505   7.629  1.00 51.21           O  
ANISOU 1872  O   PHE A1035     6785   6145   6528   -189   -219    -74       O  
ATOM   1873  CB  PHE A1035      -2.380   6.675  10.372  1.00 53.48           C  
ANISOU 1873  CB  PHE A1035     6744   6573   7003   -133     33    -73       C  
ATOM   1874  CG  PHE A1035      -0.975   6.896   9.884  1.00 54.91           C  
ANISOU 1874  CG  PHE A1035     7024   6757   7082   -182     94    -26       C  
ATOM   1875  CD1 PHE A1035      -0.360   5.954   9.060  1.00 48.00           C  
ANISOU 1875  CD1 PHE A1035     6202   5873   6162   -232    162    -19       C  
ATOM   1876  CD2 PHE A1035      -0.288   8.074  10.205  1.00 49.41           C  
ANISOU 1876  CD2 PHE A1035     6368   6065   6340   -182     84      5       C  
ATOM   1877  CE1 PHE A1035       0.915   6.169   8.585  1.00 47.23           C  
ANISOU 1877  CE1 PHE A1035     6194   5769   5984   -282    226     14       C  
ATOM   1878  CE2 PHE A1035       0.982   8.310   9.718  1.00 43.26           C  
ANISOU 1878  CE2 PHE A1035     5680   5281   5477   -229    143     39       C  
ATOM   1879  CZ  PHE A1035       1.592   7.362   8.913  1.00 48.15           C  
ANISOU 1879  CZ  PHE A1035     6349   5888   6058   -281    217     41       C  
ATOM   1880  N   VAL A1036      -3.320   9.554   9.452  1.00 48.56           N  
ANISOU 1880  N   VAL A1036     6279   5848   6324   -105   -260    -92       N  
ATOM   1881  CA  VAL A1036      -2.874  10.881   9.049  1.00 47.90           C  
ANISOU 1881  CA  VAL A1036     6305   5733   6161   -116   -330    -66       C  
ATOM   1882  C   VAL A1036      -2.461  11.647  10.299  1.00 52.79           C  
ANISOU 1882  C   VAL A1036     6848   6399   6809    -89   -282    -44       C  
ATOM   1883  O   VAL A1036      -3.172  11.643  11.309  1.00 48.18           O  
ANISOU 1883  O   VAL A1036     6142   5840   6324    -47   -280    -70       O  
ATOM   1884  CB  VAL A1036      -3.956  11.634   8.245  1.00 54.13           C  
ANISOU 1884  CB  VAL A1036     7162   6446   6960    -98   -510   -101       C  
ATOM   1885  CG1 VAL A1036      -5.273  11.711   9.008  1.00 57.43           C  
ANISOU 1885  CG1 VAL A1036     7443   6859   7520    -39   -578   -156       C  
ATOM   1886  CG2 VAL A1036      -3.457  13.028   7.781  1.00 50.31           C  
ANISOU 1886  CG2 VAL A1036     6808   5924   6385   -114   -585    -70       C  
ATOM   1887  N   VAL A1037      -1.287  12.274  10.239  1.00 59.59           N  
ANISOU 1887  N   VAL A1037     7784   7272   7585   -118   -234      1       N  
ATOM   1888  CA  VAL A1037      -0.687  12.969  11.376  1.00 53.65           C  
ANISOU 1888  CA  VAL A1037     6972   6567   6847    -99   -178     26       C  
ATOM   1889  C   VAL A1037      -0.043  14.256  10.868  1.00 51.82           C  
ANISOU 1889  C   VAL A1037     6858   6304   6529   -119   -226     52       C  
ATOM   1890  O   VAL A1037       0.714  14.231   9.890  1.00 51.74           O  
ANISOU 1890  O   VAL A1037     6970   6264   6426   -168   -206     71       O  
ATOM   1891  CB  VAL A1037       0.355  12.081  12.084  1.00 48.94           C  
ANISOU 1891  CB  VAL A1037     6314   6029   6251   -115    -26     55       C  
ATOM   1892  CG1 VAL A1037       1.086  12.846  13.183  1.00 48.98           C  
ANISOU 1892  CG1 VAL A1037     6275   6076   6259    -99     22     83       C  
ATOM   1893  CG2 VAL A1037      -0.304  10.868  12.642  1.00 48.57           C  
ANISOU 1893  CG2 VAL A1037     6157   6010   6287    -95     20     31       C  
ATOM   1894  N   GLY A1038      -0.340  15.378  11.521  1.00 50.72           N  
ANISOU 1894  N   GLY A1038     6685   6167   6418    -85   -282     50       N  
ATOM   1895  CA  GLY A1038       0.162  16.655  11.043  1.00 55.01           C  
ANISOU 1895  CA  GLY A1038     7340   6676   6886   -100   -336     72       C  
ATOM   1896  C   GLY A1038      -0.222  17.808  11.949  1.00 50.91           C  
ANISOU 1896  C   GLY A1038     6757   6169   6419    -58   -388     66       C  
ATOM   1897  O   GLY A1038      -0.970  17.658  12.918  1.00 49.94           O  
ANISOU 1897  O   GLY A1038     6507   6074   6394    -17   -389     40       O  
ATOM   1898  N   LYS A1039       0.310  18.977  11.599  1.00 59.53           N  
ANISOU 1898  N   LYS A1039     7944   7233   7442    -71   -426     89       N  
ATOM   1899  CA  LYS A1039       0.068  20.227  12.301  1.00 57.28           C  
ANISOU 1899  CA  LYS A1039     7620   6952   7193    -37   -480     87       C  
ATOM   1900  C   LYS A1039      -0.310  21.292  11.286  1.00 59.97           C  
ANISOU 1900  C   LYS A1039     8089   7213   7482    -43   -619     84       C  
ATOM   1901  O   LYS A1039       0.136  21.249  10.137  1.00 58.00           O  
ANISOU 1901  O   LYS A1039     7986   6917   7134    -87   -635    101       O  
ATOM   1902  CB  LYS A1039       1.307  20.684  13.074  1.00 56.93           C  
ANISOU 1902  CB  LYS A1039     7556   6958   7114    -47   -372    122       C  
ATOM   1903  CG  LYS A1039       1.145  20.693  14.558  1.00 56.05           C  
ANISOU 1903  CG  LYS A1039     7298   6909   7088     -9   -320    114       C  
ATOM   1904  CD  LYS A1039       2.502  20.670  15.193  1.00 63.90           C  
ANISOU 1904  CD  LYS A1039     8280   7955   8046    -26   -199    150       C  
ATOM   1905  CE  LYS A1039       2.418  20.358  16.668  1.00 58.59           C  
ANISOU 1905  CE  LYS A1039     7471   7343   7446      4   -134    146       C  
ATOM   1906  NZ  LYS A1039       3.771  20.431  17.278  1.00 54.13           N  
ANISOU 1906  NZ  LYS A1039     6899   6821   6848    -10    -35    180       N  
ATOM   1907  N   GLY A1040      -1.107  22.262  11.727  1.00 56.88           N  
ANISOU 1907  N   GLY A1040     7650   6803   7157     -2   -717     63       N  
ATOM   1908  CA  GLY A1040      -1.649  23.262  10.832  1.00 57.33           C  
ANISOU 1908  CA  GLY A1040     7819   6778   7186      0   -872     56       C  
ATOM   1909  C   GLY A1040      -2.637  24.191  11.507  1.00 63.46           C  
ANISOU 1909  C   GLY A1040     8502   7538   8072     52   -972     22       C  
ATOM   1910  O   GLY A1040      -2.325  24.749  12.559  1.00 67.66           O  
ANISOU 1910  O   GLY A1040     8948   8120   8639     69   -910     28       O  
ATOM   1911  N   TRP A1041      -3.835  24.346  10.932  1.00 58.71           N  
ANISOU 1911  N   TRP A1041     7912   6864   7531     76  -1127    -18       N  
ATOM   1912  CA  TRP A1041      -4.789  25.367  11.345  1.00 66.54           C  
ANISOU 1912  CA  TRP A1041     8837   7816   8629    120  -1247    -56       C  
ATOM   1913  C   TRP A1041      -6.182  24.776  11.480  1.00 74.36           C  
ANISOU 1913  C   TRP A1041     9714   8775   9764    157  -1326   -124       C  
ATOM   1914  O   TRP A1041      -6.588  23.941  10.673  1.00 76.53           O  
ANISOU 1914  O   TRP A1041    10033   9014  10030    148  -1374   -139       O  
ATOM   1915  CB  TRP A1041      -4.820  26.532  10.350  1.00 69.71           C  
ANISOU 1915  CB  TRP A1041     9395   8131   8962    113  -1395    -38       C  
ATOM   1916  CG  TRP A1041      -3.615  27.372  10.478  1.00 59.48           C  
ANISOU 1916  CG  TRP A1041     8176   6863   7561     87  -1319     15       C  
ATOM   1917  CD1 TRP A1041      -3.461  28.449  11.286  1.00 61.97           C  
ANISOU 1917  CD1 TRP A1041     8432   7199   7913    108  -1310     18       C  
ATOM   1918  CD2 TRP A1041      -2.366  27.187   9.812  1.00 63.33           C  
ANISOU 1918  CD2 TRP A1041     8806   7360   7896     32  -1230     66       C  
ATOM   1919  NE1 TRP A1041      -2.194  28.957  11.167  1.00 62.02           N  
ANISOU 1919  NE1 TRP A1041     8535   7228   7800     73  -1225     69       N  
ATOM   1920  CE2 TRP A1041      -1.500  28.202  10.264  1.00 59.79           C  
ANISOU 1920  CE2 TRP A1041     8377   6937   7405     24  -1172     97       C  
ATOM   1921  CE3 TRP A1041      -1.892  26.262   8.879  1.00 66.26           C  
ANISOU 1921  CE3 TRP A1041     9289   7717   8170    -16  -1187     84       C  
ATOM   1922  CZ2 TRP A1041      -0.196  28.327   9.810  1.00 58.60           C  
ANISOU 1922  CZ2 TRP A1041     8349   6793   7122    -27  -1074    140       C  
ATOM   1923  CZ3 TRP A1041      -0.590  26.390   8.431  1.00 66.37           C  
ANISOU 1923  CZ3 TRP A1041     9428   7738   8054    -70  -1085    127       C  
ATOM   1924  CH2 TRP A1041       0.240  27.415   8.898  1.00 60.08           C  
ANISOU 1924  CH2 TRP A1041     8642   6962   7222    -75  -1030    153       C  
ATOM   1925  N   THR A1042      -6.917  25.238  12.500  1.00 82.59           N  
ANISOU 1925  N   THR A1042    10609   9827  10944    196  -1336   -170       N  
ATOM   1926  CA  THR A1042      -8.272  24.747  12.745  1.00 77.27           C  
ANISOU 1926  CA  THR A1042     9810   9119  10432    230  -1399   -248       C  
ATOM   1927  C   THR A1042      -9.266  25.271  11.717  1.00 77.20           C  
ANISOU 1927  C   THR A1042     9864   8996  10474    252  -1614   -286       C  
ATOM   1928  O   THR A1042     -10.285  24.621  11.463  1.00 82.41           O  
ANISOU 1928  O   THR A1042    10463   9611  11238    272  -1684   -346       O  
ATOM   1929  CB  THR A1042      -8.720  25.125  14.156  1.00 73.36           C  
ANISOU 1929  CB  THR A1042     9146   8660  10069    256  -1334   -292       C  
ATOM   1930  OG1 THR A1042      -7.604  25.043  15.049  1.00 76.44           O  
ANISOU 1930  OG1 THR A1042     9517   9144  10382    235  -1164   -242       O  
ATOM   1931  CG2 THR A1042      -9.782  24.183  14.647  1.00 66.03           C  
ANISOU 1931  CG2 THR A1042     8075   7726   9287    275  -1309   -367       C  
ATOM   1932  N   THR A1043      -9.003  26.432  11.122  1.00 71.79           N  
ANISOU 1932  N   THR A1043     9298   8258   9720    249  -1723   -254       N  
ATOM   1933  CA  THR A1043      -9.792  26.922   9.998  1.00 73.90           C  
ANISOU 1933  CA  THR A1043     9664   8409  10006    264  -1940   -277       C  
ATOM   1934  C   THR A1043      -8.844  27.316   8.877  1.00 75.11           C  
ANISOU 1934  C   THR A1043    10043   8532   9963    222  -1977   -203       C  
ATOM   1935  O   THR A1043      -7.972  28.172   9.066  1.00 66.64           O  
ANISOU 1935  O   THR A1043     9032   7484   8803    205  -1927   -154       O  
ATOM   1936  CB  THR A1043     -10.682  28.105  10.390  1.00 79.38           C  
ANISOU 1936  CB  THR A1043    10277   9039  10843    308  -2072   -327       C  
ATOM   1937  OG1 THR A1043     -11.786  27.634  11.171  1.00 84.93           O  
ANISOU 1937  OG1 THR A1043    10785   9740  11743    343  -2065   -414       O  
ATOM   1938  CG2 THR A1043     -11.220  28.799   9.144  1.00 81.42           C  
ANISOU 1938  CG2 THR A1043    10680   9172  11083    319  -2306   -330       C  
ATOM   1939  N   GLY A1044      -9.004  26.680   7.717  1.00 74.03           N  
ANISOU 1939  N   GLY A1044    10032   8339   9756    201  -2058   -198       N  
ATOM   1940  CA  GLY A1044      -8.165  26.993   6.587  1.00 74.14           C  
ANISOU 1940  CA  GLY A1044    10276   8313   9582    152  -2090   -135       C  
ATOM   1941  C   GLY A1044      -8.717  28.114   5.733  1.00 83.01           C  
ANISOU 1941  C   GLY A1044    11532   9316  10694    165  -2313   -137       C  
ATOM   1942  O   GLY A1044      -9.915  28.387   5.739  1.00 82.32           O  
ANISOU 1942  O   GLY A1044    11369   9158  10752    213  -2475   -196       O  
ATOM   1943  N   SER A1045      -7.816  28.760   4.987  1.00 88.22           N  
ANISOU 1943  N   SER A1045    12395   9944  11181    120  -2318    -75       N  
ATOM   1944  CA  SER A1045      -8.173  29.876   4.121  1.00 94.44           C  
ANISOU 1944  CA  SER A1045    13344  10612  11926    123  -2522    -64       C  
ATOM   1945  C   SER A1045      -7.283  29.855   2.881  1.00 97.17           C  
ANISOU 1945  C   SER A1045    13957  10911  12051     51  -2516     -4       C  
ATOM   1946  O   SER A1045      -6.069  29.624   3.005  1.00 97.22           O  
ANISOU 1946  O   SER A1045    14010  10990  11941      1  -2326     41       O  
ATOM   1947  CB  SER A1045      -8.036  31.224   4.840  1.00 91.27           C  
ANISOU 1947  CB  SER A1045    12890  10216  11572    150  -2534    -55       C  
ATOM   1948  OG  SER A1045      -6.789  31.830   4.544  1.00 93.51           O  
ANISOU 1948  OG  SER A1045    13332  10515  11684     98  -2442     12       O  
ATOM   1949  N   PRO A1046      -7.837  30.124   1.702  1.00 91.24           N  
ANISOU 1949  N   PRO A1046    13387  10037  11244     42  -2718     -4       N  
ATOM   1950  CA  PRO A1046      -7.099  29.927   0.447  1.00 88.80           C  
ANISOU 1950  CA  PRO A1046    13344   9672  10722    -34  -2711     45       C  
ATOM   1951  C   PRO A1046      -6.002  30.938   0.159  1.00 92.42           C  
ANISOU 1951  C   PRO A1046    13979  10114  11022    -85  -2650    105       C  
ATOM   1952  O   PRO A1046      -5.455  30.910  -0.945  1.00 96.14           O  
ANISOU 1952  O   PRO A1046    14694  10520  11316   -154  -2658    141       O  
ATOM   1953  CB  PRO A1046      -8.208  30.043  -0.608  1.00 85.43           C  
ANISOU 1953  CB  PRO A1046    13045   9106  10307    -18  -2979     20       C  
ATOM   1954  CG  PRO A1046      -9.212  30.904   0.019  1.00 91.16           C  
ANISOU 1954  CG  PRO A1046    13626   9795  11216     60  -3135    -23       C  
ATOM   1955  CD  PRO A1046      -9.231  30.518   1.457  1.00 90.21           C  
ANISOU 1955  CD  PRO A1046    13221   9803  11252    101  -2967    -56       C  
ATOM   1956  N   PHE A1047      -5.651  31.836   1.071  1.00 82.90           N  
ANISOU 1956  N   PHE A1047    12671   8958   9868    -59  -2586    115       N  
ATOM   1957  CA  PHE A1047      -4.601  32.798   0.782  1.00 86.94           C  
ANISOU 1957  CA  PHE A1047    13350   9450  10233   -108  -2523    168       C  
ATOM   1958  C   PHE A1047      -3.330  32.544   1.561  1.00 94.95           C  
ANISOU 1958  C   PHE A1047    14281  10586  11211   -139  -2260    191       C  
ATOM   1959  O   PHE A1047      -2.346  33.267   1.360  1.00 89.16           O  
ANISOU 1959  O   PHE A1047    13675   9843  10358   -185  -2179    230       O  
ATOM   1960  CB  PHE A1047      -5.106  34.217   1.054  1.00 96.45           C  
ANISOU 1960  CB  PHE A1047    14543  10596  11507    -61  -2674    166       C  
ATOM   1961  CG  PHE A1047      -6.319  34.552   0.266  1.00100.85           C  
ANISOU 1961  CG  PHE A1047    15190  11021  12108    -29  -2949    143       C  
ATOM   1962  CD1 PHE A1047      -6.229  34.731  -1.105  1.00101.00           C  
ANISOU 1962  CD1 PHE A1047    15497  10920  11960    -82  -3070    175       C  
ATOM   1963  CD2 PHE A1047      -7.561  34.616   0.874  1.00103.57           C  
ANISOU 1963  CD2 PHE A1047    15335  11353  12662     51  -3086     84       C  
ATOM   1964  CE1 PHE A1047      -7.347  35.012  -1.852  1.00100.66           C  
ANISOU 1964  CE1 PHE A1047    15545  10746  11956    -52  -3340    154       C  
ATOM   1965  CE2 PHE A1047      -8.692  34.897   0.130  1.00103.89           C  
ANISOU 1965  CE2 PHE A1047    15453  11263  12759     83  -3352     56       C  
ATOM   1966  CZ  PHE A1047      -8.584  35.097  -1.237  1.00101.02           C  
ANISOU 1966  CZ  PHE A1047    15380  10780  12225     34  -3486     93       C  
ATOM   1967  N   ARG A1048      -3.315  31.509   2.399  1.00 98.42           N  
ANISOU 1967  N   ARG A1048    14518  11131  11745   -119  -2127    167       N  
ATOM   1968  CA  ARG A1048      -2.214  31.271   3.318  1.00 88.10           C  
ANISOU 1968  CA  ARG A1048    13098   9941  10434   -134  -1896    182       C  
ATOM   1969  C   ARG A1048      -1.078  30.512   2.650  1.00 76.97           C  
ANISOU 1969  C   ARG A1048    11825   8545   8876   -215  -1737    210       C  
ATOM   1970  O   ARG A1048      -1.285  29.503   1.974  1.00 72.13           O  
ANISOU 1970  O   ARG A1048    11268   7911   8226   -243  -1745    200       O  
ATOM   1971  CB  ARG A1048      -2.697  30.501   4.542  1.00 93.57           C  
ANISOU 1971  CB  ARG A1048    13525  10734  11293    -79  -1825    144       C  
ATOM   1972  CG  ARG A1048      -1.568  29.846   5.339  1.00 85.12           C  
ANISOU 1972  CG  ARG A1048    12355   9780  10208   -103  -1589    160       C  
ATOM   1973  CD  ARG A1048      -2.064  28.684   6.191  1.00 77.75           C  
ANISOU 1973  CD  ARG A1048    11214   8926   9401    -66  -1523    126       C  
ATOM   1974  NE  ARG A1048      -3.484  28.768   6.542  1.00 69.21           N  
ANISOU 1974  NE  ARG A1048    10010   7817   8469     -3  -1671     77       N  
ATOM   1975  CZ  ARG A1048      -3.961  29.539   7.515  1.00 64.63           C  
ANISOU 1975  CZ  ARG A1048     9290   7258   8008     48  -1704     55       C  
ATOM   1976  NH1 ARG A1048      -3.119  30.295   8.208  1.00 65.14           N  
ANISOU 1976  NH1 ARG A1048     9329   7374   8048     44  -1604     82       N  
ATOM   1977  NH2 ARG A1048      -5.266  29.562   7.797  1.00 64.27           N  
ANISOU 1977  NH2 ARG A1048     9129   7179   8112    101  -1831      0       N  
ATOM   1978  N   THR A1049       0.123  31.020   2.841  1.00 83.64           N  
ANISOU 1978  N   THR A1049    12717   9419   9642   -254  -1594    239       N  
ATOM   1979  CA  THR A1049       1.365  30.333   2.538  1.00 82.23           C  
ANISOU 1979  CA  THR A1049    12609   9273   9360   -327  -1400    256       C  
ATOM   1980  C   THR A1049       1.717  29.371   3.673  1.00 91.02           C  
ANISOU 1980  C   THR A1049    13495  10511  10578   -301  -1239    241       C  
ATOM   1981  O   THR A1049       1.445  29.643   4.850  1.00 90.87           O  
ANISOU 1981  O   THR A1049    13286  10561  10680   -240  -1230    230       O  
ATOM   1982  CB  THR A1049       2.466  31.385   2.355  1.00 84.92           C  
ANISOU 1982  CB  THR A1049    13081   9588   9597   -373  -1318    285       C  
ATOM   1983  OG1 THR A1049       2.237  32.122   1.150  1.00 92.29           O  
ANISOU 1983  OG1 THR A1049    14264  10396  10408   -413  -1453    302       O  
ATOM   1984  CG2 THR A1049       3.842  30.794   2.351  1.00 84.98           C  
ANISOU 1984  CG2 THR A1049    13107   9642   9540   -438  -1094    291       C  
ATOM   1985  N   ILE A1050       2.327  28.239   3.323  1.00 81.91           N  
ANISOU 1985  N   ILE A1050    12366   9381   9377   -351  -1111    240       N  
ATOM   1986  CA  ILE A1050       2.713  27.234   4.306  1.00 73.18           C  
ANISOU 1986  CA  ILE A1050    11063   8383   8360   -333   -961    229       C  
ATOM   1987  C   ILE A1050       4.185  26.914   4.133  1.00 75.41           C  
ANISOU 1987  C   ILE A1050    11404   8686   8562   -402   -767    243       C  
ATOM   1988  O   ILE A1050       4.627  26.540   3.038  1.00 80.04           O  
ANISOU 1988  O   ILE A1050    12160   9212   9038   -474   -730    246       O  
ATOM   1989  CB  ILE A1050       1.887  25.943   4.197  1.00 68.40           C  
ANISOU 1989  CB  ILE A1050    10381   7793   7814   -315   -995    204       C  
ATOM   1990  CG1 ILE A1050       0.469  26.160   4.713  1.00 65.61           C  
ANISOU 1990  CG1 ILE A1050     9904   7438   7587   -237  -1155    177       C  
ATOM   1991  CG2 ILE A1050       2.555  24.846   4.982  1.00 61.11           C  
ANISOU 1991  CG2 ILE A1050     9307   6966   6946   -318   -818    200       C  
ATOM   1992  CD1 ILE A1050      -0.500  26.517   3.652  1.00 67.25           C  
ANISOU 1992  CD1 ILE A1050    10255   7539   7758   -236  -1354    168       C  
ATOM   1993  N   ASN A1051       4.933  27.034   5.220  1.00 67.62           N  
ANISOU 1993  N   ASN A1051    10275   7780   7637   -381   -644    246       N  
ATOM   1994  CA  ASN A1051       6.334  26.664   5.247  1.00 68.76           C  
ANISOU 1994  CA  ASN A1051    10433   7951   7743   -437   -457    250       C  
ATOM   1995  C   ASN A1051       6.509  25.395   6.067  1.00 61.55           C  
ANISOU 1995  C   ASN A1051     9338   7126   6923   -415   -352    239       C  
ATOM   1996  O   ASN A1051       5.705  25.100   6.959  1.00 59.78           O  
ANISOU 1996  O   ASN A1051     8954   6959   6803   -349   -403    232       O  
ATOM   1997  CB  ASN A1051       7.186  27.794   5.828  1.00 74.61           C  
ANISOU 1997  CB  ASN A1051    11160   8708   8481   -434   -395    262       C  
ATOM   1998  CG  ASN A1051       6.862  29.146   5.222  1.00 78.19           C  
ANISOU 1998  CG  ASN A1051    11768   9081   8861   -440   -515    274       C  
ATOM   1999  OD1 ASN A1051       5.704  29.574   5.180  1.00 81.07           O  
ANISOU 1999  OD1 ASN A1051    12131   9419   9254   -393   -680    275       O  
ATOM   2000  ND2 ASN A1051       7.890  29.815   4.721  1.00 82.51           N  
ANISOU 2000  ND2 ASN A1051    12451   9581   9317   -499   -431    281       N  
ATOM   2001  N   TYR A1052       7.564  24.645   5.763  1.00 57.01           N  
ANISOU 2001  N   TYR A1052     8792   6555   6315   -474   -203    234       N  
ATOM   2002  CA  TYR A1052       7.796  23.387   6.460  1.00 58.60           C  
ANISOU 2002  CA  TYR A1052     8835   6830   6601   -458   -104    224       C  
ATOM   2003  C   TYR A1052       9.227  22.927   6.229  1.00 62.48           C  
ANISOU 2003  C   TYR A1052     9356   7318   7066   -524     70    217       C  
ATOM   2004  O   TYR A1052       9.930  23.420   5.347  1.00 62.09           O  
ANISOU 2004  O   TYR A1052     9466   7200   6925   -591    118    213       O  
ATOM   2005  CB  TYR A1052       6.789  22.295   6.045  1.00 55.09           C  
ANISOU 2005  CB  TYR A1052     8376   6380   6175   -449   -170    213       C  
ATOM   2006  CG  TYR A1052       7.062  21.649   4.704  1.00 56.38           C  
ANISOU 2006  CG  TYR A1052     8703   6477   6243   -528   -135    204       C  
ATOM   2007  CD1 TYR A1052       7.886  20.519   4.604  1.00 57.40           C  
ANISOU 2007  CD1 TYR A1052     8800   6627   6383   -572     13    192       C  
ATOM   2008  CD2 TYR A1052       6.483  22.146   3.544  1.00 56.74           C  
ANISOU 2008  CD2 TYR A1052     8937   6433   6188   -559   -252    205       C  
ATOM   2009  CE1 TYR A1052       8.141  19.922   3.393  1.00 55.41           C  
ANISOU 2009  CE1 TYR A1052     8696   6312   6046   -650     55    180       C  
ATOM   2010  CE2 TYR A1052       6.735  21.555   2.316  1.00 66.37           C  
ANISOU 2010  CE2 TYR A1052    10320   7587   7311   -637   -217    196       C  
ATOM   2011  CZ  TYR A1052       7.561  20.437   2.247  1.00 66.28           C  
ANISOU 2011  CZ  TYR A1052    10269   7602   7314   -684    -58    182       C  
ATOM   2012  OH  TYR A1052       7.823  19.846   1.030  1.00 58.83           O  
ANISOU 2012  OH  TYR A1052     9487   6590   6275   -768    -13    169       O  
ATOM   2013  N   ASN A1053       9.646  21.969   7.050  1.00 65.21           N  
ANISOU 2013  N   ASN A1053     9546   7732   7500   -505    166    211       N  
ATOM   2014  CA  ASN A1053      10.973  21.380   6.951  1.00 59.07           C  
ANISOU 2014  CA  ASN A1053     8763   6952   6728   -560    328    197       C  
ATOM   2015  C   ASN A1053      10.841  19.904   7.282  1.00 56.42           C  
ANISOU 2015  C   ASN A1053     8308   6663   6464   -548    378    190       C  
ATOM   2016  O   ASN A1053      10.466  19.558   8.402  1.00 69.75           O  
ANISOU 2016  O   ASN A1053     9836   8422   8241   -484    358    198       O  
ATOM   2017  CB  ASN A1053      11.944  22.066   7.915  1.00 57.68           C  
ANISOU 2017  CB  ASN A1053     8498   6813   6604   -540    401    199       C  
ATOM   2018  CG  ASN A1053      13.382  21.713   7.650  1.00 63.86           C  
ANISOU 2018  CG  ASN A1053     9300   7570   7394   -604    561    176       C  
ATOM   2019  OD1 ASN A1053      14.075  22.436   6.947  1.00 71.93           O  
ANISOU 2019  OD1 ASN A1053    10452   8529   8350   -661    612    163       O  
ATOM   2020  ND2 ASN A1053      13.849  20.607   8.216  1.00 77.02           N  
ANISOU 2020  ND2 ASN A1053    10837   9280   9146   -596    643    166       N  
ATOM   2021  N   ALA A1054      11.141  19.033   6.329  1.00 58.84           N  
ANISOU 2021  N   ALA A1054     8696   6928   6732   -613    444    172       N  
ATOM   2022  CA  ALA A1054      11.134  17.596   6.591  1.00 65.91           C  
ANISOU 2022  CA  ALA A1054     9482   7863   7698   -609    505    163       C  
ATOM   2023  C   ALA A1054      12.550  17.159   6.962  1.00 67.92           C  
ANISOU 2023  C   ALA A1054     9668   8129   8011   -640    660    148       C  
ATOM   2024  O   ALA A1054      13.314  16.628   6.148  1.00 64.96           O  
ANISOU 2024  O   ALA A1054     9365   7704   7612   -714    766    123       O  
ATOM   2025  CB  ALA A1054      10.601  16.825   5.390  1.00 60.22           C  
ANISOU 2025  CB  ALA A1054     8874   7092   6914   -658    486    150       C  
ATOM   2026  N   GLY A1055      12.902  17.400   8.227  1.00 55.40           N  
ANISOU 2026  N   GLY A1055     7939   6602   6507   -584    673    159       N  
ATOM   2027  CA  GLY A1055      14.172  16.912   8.724  1.00 46.37           C  
ANISOU 2027  CA  GLY A1055     6707   5470   5440   -601    800    144       C  
ATOM   2028  C   GLY A1055      14.337  15.430   8.482  1.00 61.47           C  
ANISOU 2028  C   GLY A1055     8572   7385   7400   -627    873    128       C  
ATOM   2029  O   GLY A1055      15.426  14.960   8.144  1.00 69.96           O  
ANISOU 2029  O   GLY A1055     9650   8426   8507   -682    993    100       O  
ATOM   2030  N   VAL A1056      13.256  14.668   8.631  1.00 63.60           N  
ANISOU 2030  N   VAL A1056     8793   7691   7682   -590    804    142       N  
ATOM   2031  CA  VAL A1056      13.242  13.261   8.246  1.00 56.20           C  
ANISOU 2031  CA  VAL A1056     7827   6750   6777   -618    863    128       C  
ATOM   2032  C   VAL A1056      12.020  13.020   7.379  1.00 48.59           C  
ANISOU 2032  C   VAL A1056     6953   5766   5742   -626    776    129       C  
ATOM   2033  O   VAL A1056      10.913  13.455   7.719  1.00 53.68           O  
ANISOU 2033  O   VAL A1056     7582   6437   6376   -570    657    147       O  
ATOM   2034  CB  VAL A1056      13.233  12.320   9.468  1.00 57.33           C  
ANISOU 2034  CB  VAL A1056     7793   6960   7029   -561    879    141       C  
ATOM   2035  CG1 VAL A1056      13.661  10.929   9.068  1.00 49.34           C  
ANISOU 2035  CG1 VAL A1056     6749   5934   6063   -602    972    121       C  
ATOM   2036  CG2 VAL A1056      14.135  12.861  10.582  1.00 62.07           C  
ANISOU 2036  CG2 VAL A1056     8301   7588   7694   -528    909    149       C  
ATOM   2037  N   TRP A1057      12.219  12.336   6.262  1.00 53.03           N  
ANISOU 2037  N   TRP A1057     7608   6277   6262   -697    835    106       N  
ATOM   2038  CA  TRP A1057      11.109  11.823   5.457  1.00 57.45           C  
ANISOU 2038  CA  TRP A1057     8239   6820   6770   -706    760    103       C  
ATOM   2039  C   TRP A1057      11.521  10.428   5.002  1.00 61.89           C  
ANISOU 2039  C   TRP A1057     8777   7371   7367   -755    866     79       C  
ATOM   2040  O   TRP A1057      12.087  10.262   3.920  1.00 69.92           O  
ANISOU 2040  O   TRP A1057     9917   8325   8326   -839    942     54       O  
ATOM   2041  CB  TRP A1057      10.789  12.715   4.278  1.00 63.22           C  
ANISOU 2041  CB  TRP A1057     9169   7478   7375   -754    695     98       C  
ATOM   2042  CG  TRP A1057       9.772  12.075   3.406  1.00 66.36           C  
ANISOU 2042  CG  TRP A1057     9641   7848   7724   -769    623     90       C  
ATOM   2043  CD1 TRP A1057       9.928  11.675   2.107  1.00 65.86           C  
ANISOU 2043  CD1 TRP A1057     9731   7716   7577   -853    662     68       C  
ATOM   2044  CD2 TRP A1057       8.438  11.714   3.779  1.00 66.68           C  
ANISOU 2044  CD2 TRP A1057     9604   7928   7804   -700    503     98       C  
ATOM   2045  NE1 TRP A1057       8.761  11.111   1.641  1.00 66.19           N  
ANISOU 2045  NE1 TRP A1057     9797   7753   7599   -838    562     65       N  
ATOM   2046  CE2 TRP A1057       7.833  11.122   2.648  1.00 65.11           C  
ANISOU 2046  CE2 TRP A1057     9515   7680   7542   -743    464     81       C  
ATOM   2047  CE3 TRP A1057       7.694  11.837   4.956  1.00 59.94           C  
ANISOU 2047  CE3 TRP A1057     8602   7140   7034   -611    429    113       C  
ATOM   2048  CZ2 TRP A1057       6.528  10.650   2.667  1.00 54.19           C  
ANISOU 2048  CZ2 TRP A1057     8087   6313   6188   -695    351     76       C  
ATOM   2049  CZ3 TRP A1057       6.391  11.375   4.968  1.00 49.72           C  
ANISOU 2049  CZ3 TRP A1057     7265   5858   5768   -567    326    106       C  
ATOM   2050  CH2 TRP A1057       5.825  10.788   3.834  1.00 53.19           C  
ANISOU 2050  CH2 TRP A1057     7807   6249   6154   -607    286     87       C  
ATOM   2051  N   ALA A1058      11.227   9.425   5.827  1.00 55.88           N  
ANISOU 2051  N   ALA A1058     7862   6669   6700   -706    876     86       N  
ATOM   2052  CA  ALA A1058      11.737   8.071   5.629  1.00 59.72           C  
ANISOU 2052  CA  ALA A1058     8294   7154   7244   -743    984     66       C  
ATOM   2053  C   ALA A1058      10.600   7.057   5.519  1.00 58.44           C  
ANISOU 2053  C   ALA A1058     8090   7017   7098   -717    931     67       C  
ATOM   2054  O   ALA A1058      10.468   6.171   6.371  1.00 71.68           O  
ANISOU 2054  O   ALA A1058     9625   8745   8866   -673    952     74       O  
ATOM   2055  CB  ALA A1058      12.678   7.701   6.774  1.00 47.33           C  
ANISOU 2055  CB  ALA A1058     6572   5625   5788   -713   1064     72       C  
ATOM   2056  N   PRO A1059       9.778   7.130   4.483  1.00 51.06           N  
ANISOU 2056  N   PRO A1059     7278   6043   6079   -744    861     56       N  
ATOM   2057  CA  PRO A1059       8.721   6.122   4.346  1.00 60.61           C  
ANISOU 2057  CA  PRO A1059     8444   7272   7313   -721    814     49       C  
ATOM   2058  C   PRO A1059       9.264   4.791   3.820  1.00 55.95           C  
ANISOU 2058  C   PRO A1059     7837   6668   6753   -779    934     25       C  
ATOM   2059  O   PRO A1059      10.212   4.736   3.031  1.00 54.73           O  
ANISOU 2059  O   PRO A1059     7771   6461   6561   -859   1032      5       O  
ATOM   2060  CB  PRO A1059       7.733   6.773   3.362  1.00 48.38           C  
ANISOU 2060  CB  PRO A1059     7045   5675   5662   -733    687     43       C  
ATOM   2061  CG  PRO A1059       8.565   7.620   2.510  1.00 49.32           C  
ANISOU 2061  CG  PRO A1059     7327   5729   5684   -806    724     38       C  
ATOM   2062  CD  PRO A1059       9.807   8.037   3.330  1.00 49.72           C  
ANISOU 2062  CD  PRO A1059     7302   5802   5787   -803    826     47       C  
ATOM   2063  N   ASN A1060       8.665   3.702   4.312  1.00 52.35           N  
ANISOU 2063  N   ASN A1060     7260   6256   6374   -738    933     25       N  
ATOM   2064  CA  ASN A1060       8.927   2.340   3.841  1.00 44.74           C  
ANISOU 2064  CA  ASN A1060     6269   5284   5447   -783   1029      3       C  
ATOM   2065  C   ASN A1060       7.612   1.776   3.304  1.00 49.80           C  
ANISOU 2065  C   ASN A1060     6933   5924   6066   -769    944    -10       C  
ATOM   2066  O   ASN A1060       6.911   1.028   3.984  1.00 58.95           O  
ANISOU 2066  O   ASN A1060     7970   7130   7300   -713    923     -7       O  
ATOM   2067  CB  ASN A1060       9.477   1.502   4.910  1.00 45.36           C  
ANISOU 2067  CB  ASN A1060     6182   5410   5642   -749   1109     13       C  
ATOM   2068  CG  ASN A1060      10.058   0.205   4.373  1.00 62.78           C  
ANISOU 2068  CG  ASN A1060     8365   7595   7892   -808   1228    -14       C  
ATOM   2069  OD1 ASN A1060      10.075  -0.018   3.161  1.00 68.97           O  
ANISOU 2069  OD1 ASN A1060     9265   8328   8611   -880   1258    -41       O  
ATOM   2070  ND2 ASN A1060      10.540  -0.650   5.262  1.00 69.70           N  
ANISOU 2070  ND2 ASN A1060     9099   8507   8878   -780   1295     -6       N  
ATOM   2071  N   GLY A1061       7.284   2.131   2.072  1.00 58.59           N  
ANISOU 2071  N   GLY A1061     8209   6977   7074   -822    895    -28       N  
ATOM   2072  CA  GLY A1061       5.992   1.855   1.495  1.00 60.00           C  
ANISOU 2072  CA  GLY A1061     8431   7143   7222   -806    785    -42       C  
ATOM   2073  C   GLY A1061       5.173   3.119   1.309  1.00 61.77           C  
ANISOU 2073  C   GLY A1061     8750   7342   7377   -774    628    -33       C  
ATOM   2074  O   GLY A1061       5.694   4.239   1.286  1.00 60.71           O  
ANISOU 2074  O   GLY A1061     8694   7185   7186   -787    614    -17       O  
ATOM   2075  N   ASN A1062       3.854   2.926   1.203  1.00 50.31           N  
ANISOU 2075  N   ASN A1062     7282   5893   5942   -729    506    -46       N  
ATOM   2076  CA  ASN A1062       2.915   3.996   0.869  1.00 47.26           C  
ANISOU 2076  CA  ASN A1062     6987   5468   5500   -699    337    -47       C  
ATOM   2077  C   ASN A1062       2.743   4.963   2.042  1.00 48.23           C  
ANISOU 2077  C   ASN A1062     7015   5632   5676   -625    284    -24       C  
ATOM   2078  O   ASN A1062       2.222   4.594   3.098  1.00 54.97           O  
ANISOU 2078  O   ASN A1062     7708   6544   6635   -558    280    -25       O  
ATOM   2079  CB  ASN A1062       1.570   3.400   0.459  1.00 47.56           C  
ANISOU 2079  CB  ASN A1062     7013   5492   5565   -670    226    -77       C  
ATOM   2080  CG  ASN A1062       0.620   4.436  -0.142  1.00 54.27           C  
ANISOU 2080  CG  ASN A1062     7984   6282   6355   -652     39    -85       C  
ATOM   2081  OD1 ASN A1062       1.030   5.551  -0.479  1.00 56.24           O  
ANISOU 2081  OD1 ASN A1062     8360   6491   6517   -676     -1    -65       O  
ATOM   2082  ND2 ASN A1062      -0.658   4.068  -0.276  1.00 50.63           N  
ANISOU 2082  ND2 ASN A1062     7483   5810   5946   -608    -79   -116       N  
ATOM   2083  N   GLY A1063       3.165   6.211   1.837  1.00 48.73           N  
ANISOU 2083  N   GLY A1063     7188   5663   5665   -641    245     -6       N  
ATOM   2084  CA  GLY A1063       2.989   7.321   2.751  1.00 46.53           C  
ANISOU 2084  CA  GLY A1063     6854   5410   5417   -580    180     14       C  
ATOM   2085  C   GLY A1063       3.173   8.642   2.019  1.00 54.01           C  
ANISOU 2085  C   GLY A1063     7977   6292   6254   -612    101     25       C  
ATOM   2086  O   GLY A1063       4.139   8.818   1.272  1.00 55.56           O  
ANISOU 2086  O   GLY A1063     8304   6447   6361   -687    178     30       O  
ATOM   2087  N   TYR A1064       2.248   9.575   2.190  1.00 54.02           N  
ANISOU 2087  N   TYR A1064     7988   6277   6261   -559    -50     25       N  
ATOM   2088  CA  TYR A1064       2.321  10.871   1.528  1.00 49.36           C  
ANISOU 2088  CA  TYR A1064     7565   5621   5569   -582   -142     38       C  
ATOM   2089  C   TYR A1064       2.811  11.925   2.512  1.00 49.21           C  
ANISOU 2089  C   TYR A1064     7482   5638   5577   -546   -124     62       C  
ATOM   2090  O   TYR A1064       2.244  12.063   3.603  1.00 49.15           O  
ANISOU 2090  O   TYR A1064     7322   5684   5670   -472   -160     62       O  
ATOM   2091  CB  TYR A1064       0.956  11.309   0.996  1.00 47.76           C  
ANISOU 2091  CB  TYR A1064     7426   5363   5358   -548   -341     20       C  
ATOM   2092  CG  TYR A1064       0.162  10.305   0.189  1.00 55.88           C  
ANISOU 2092  CG  TYR A1064     8487   6359   6386   -562   -396    -11       C  
ATOM   2093  CD1 TYR A1064       0.790   9.392  -0.665  1.00 50.39           C  
ANISOU 2093  CD1 TYR A1064     7881   5644   5622   -640   -292    -17       C  
ATOM   2094  CD2 TYR A1064      -1.247  10.301   0.254  1.00 61.44           C  
ANISOU 2094  CD2 TYR A1064     9134   7045   7164   -499   -557    -41       C  
ATOM   2095  CE1 TYR A1064       0.039   8.496  -1.409  1.00 48.85           C  
ANISOU 2095  CE1 TYR A1064     7717   5418   5425   -653   -348    -47       C  
ATOM   2096  CE2 TYR A1064      -1.997   9.409  -0.481  1.00 53.83           C  
ANISOU 2096  CE2 TYR A1064     8197   6050   6208   -509   -615    -73       C  
ATOM   2097  CZ  TYR A1064      -1.343   8.508  -1.313  1.00 52.14           C  
ANISOU 2097  CZ  TYR A1064     8075   5821   5915   -586   -511    -74       C  
ATOM   2098  OH  TYR A1064      -2.093   7.615  -2.051  1.00 55.84           O  
ANISOU 2098  OH  TYR A1064     8572   6257   6389   -597   -570   -107       O  
ATOM   2099  N   LEU A1065       3.845  12.676   2.123  1.00 51.15           N  
ANISOU 2099  N   LEU A1065     7850   5851   5735   -600    -66     80       N  
ATOM   2100  CA  LEU A1065       4.175  13.958   2.760  1.00 54.30           C  
ANISOU 2100  CA  LEU A1065     8239   6260   6132   -571    -88    102       C  
ATOM   2101  C   LEU A1065       3.495  15.070   1.970  1.00 51.73           C  
ANISOU 2101  C   LEU A1065     8074   5856   5724   -573   -251    104       C  
ATOM   2102  O   LEU A1065       3.943  15.399   0.868  1.00 60.45           O  
ANISOU 2102  O   LEU A1065     9374   6887   6708   -645   -248    108       O  
ATOM   2103  CB  LEU A1065       5.681  14.195   2.797  1.00 60.49           C  
ANISOU 2103  CB  LEU A1065     9061   7046   6876   -627     66    114       C  
ATOM   2104  CG  LEU A1065       6.103  15.569   3.339  1.00 63.15           C  
ANISOU 2104  CG  LEU A1065     9407   7385   7200   -605     48    134       C  
ATOM   2105  CD1 LEU A1065       5.603  15.745   4.768  1.00 54.29           C  
ANISOU 2105  CD1 LEU A1065     8090   6342   6195   -515     11    142       C  
ATOM   2106  CD2 LEU A1065       7.624  15.762   3.269  1.00 64.45           C  
ANISOU 2106  CD2 LEU A1065     9615   7541   7331   -667    205    137       C  
ATOM   2107  N   THR A1066       2.432  15.657   2.529  1.00 51.93           N  
ANISOU 2107  N   THR A1066     8024   5891   5816   -498   -391    101       N  
ATOM   2108  CA  THR A1066       1.514  16.490   1.748  1.00 61.04           C  
ANISOU 2108  CA  THR A1066     9312   6963   6916   -490   -577     96       C  
ATOM   2109  C   THR A1066       0.746  17.464   2.646  1.00 63.61           C  
ANISOU 2109  C   THR A1066     9532   7307   7330   -409   -692     95       C  
ATOM   2110  O   THR A1066       0.583  17.235   3.848  1.00 66.74           O  
ANISOU 2110  O   THR A1066     9738   7780   7841   -354   -645     89       O  
ATOM   2111  CB  THR A1066       0.507  15.614   0.987  1.00 57.08           C  
ANISOU 2111  CB  THR A1066     8843   6423   6422   -491   -673     67       C  
ATOM   2112  OG1 THR A1066      -0.579  16.421   0.501  1.00 59.67           O  
ANISOU 2112  OG1 THR A1066     9253   6677   6740   -459   -880     56       O  
ATOM   2113  CG2 THR A1066      -0.074  14.552   1.922  1.00 54.47           C  
ANISOU 2113  CG2 THR A1066     8294   6170   6234   -434   -633     43       C  
ATOM   2114  N   LEU A1067       0.216  18.524   2.027  1.00 60.82           N  
ANISOU 2114  N   LEU A1067     9310   6875   6922   -405   -849     98       N  
ATOM   2115  CA  LEU A1067      -0.759  19.390   2.682  1.00 60.55           C  
ANISOU 2115  CA  LEU A1067     9185   6838   6981   -329   -989     86       C  
ATOM   2116  C   LEU A1067      -2.162  18.846   2.467  1.00 58.46           C  
ANISOU 2116  C   LEU A1067     8866   6543   6802   -285  -1133     45       C  
ATOM   2117  O   LEU A1067      -2.496  18.386   1.379  1.00 64.17           O  
ANISOU 2117  O   LEU A1067     9717   7202   7462   -320  -1204     34       O  
ATOM   2118  CB  LEU A1067      -0.667  20.819   2.146  1.00 76.10           C  
ANISOU 2118  CB  LEU A1067    11317   8733   8866   -342  -1098    107       C  
ATOM   2119  CG  LEU A1067      -1.823  21.739   2.579  1.00 75.65           C  
ANISOU 2119  CG  LEU A1067    11190   8647   8905   -268  -1277     88       C  
ATOM   2120  CD1 LEU A1067      -1.514  22.514   3.875  1.00 67.39           C  
ANISOU 2120  CD1 LEU A1067     9998   7670   7937   -223  -1215     97       C  
ATOM   2121  CD2 LEU A1067      -2.230  22.686   1.447  1.00 65.23           C  
ANISOU 2121  CD2 LEU A1067    10084   7210   7492   -287  -1458     96       C  
ATOM   2122  N   TYR A1068      -2.994  18.914   3.507  1.00 64.31           N  
ANISOU 2122  N   TYR A1068     9418   7325   7691   -212  -1174     17       N  
ATOM   2123  CA  TYR A1068      -4.231  18.140   3.562  1.00 60.90           C  
ANISOU 2123  CA  TYR A1068     8882   6884   7374   -169  -1260    -33       C  
ATOM   2124  C   TYR A1068      -5.332  18.956   4.227  1.00 58.66           C  
ANISOU 2124  C   TYR A1068     8485   6581   7222    -96  -1396    -68       C  
ATOM   2125  O   TYR A1068      -5.111  19.529   5.293  1.00 59.83           O  
ANISOU 2125  O   TYR A1068     8522   6782   7428    -67  -1336    -61       O  
ATOM   2126  CB  TYR A1068      -3.983  16.822   4.326  1.00 55.32           C  
ANISOU 2126  CB  TYR A1068     8017   6268   6735   -165  -1093    -43       C  
ATOM   2127  CG  TYR A1068      -5.199  15.938   4.593  1.00 65.76           C  
ANISOU 2127  CG  TYR A1068     9201   7594   8192   -120  -1145    -98       C  
ATOM   2128  CD1 TYR A1068      -5.733  15.134   3.591  1.00 72.98           C  
ANISOU 2128  CD1 TYR A1068    10186   8458   9087   -139  -1213   -124       C  
ATOM   2129  CD2 TYR A1068      -5.793  15.881   5.868  1.00 61.73           C  
ANISOU 2129  CD2 TYR A1068     8491   7136   7829    -61  -1116   -129       C  
ATOM   2130  CE1 TYR A1068      -6.841  14.310   3.839  1.00 79.84           C  
ANISOU 2130  CE1 TYR A1068    10922   9327  10088    -97  -1255   -180       C  
ATOM   2131  CE2 TYR A1068      -6.898  15.066   6.124  1.00 60.83           C  
ANISOU 2131  CE2 TYR A1068     8250   7019   7843    -24  -1150   -187       C  
ATOM   2132  CZ  TYR A1068      -7.414  14.278   5.101  1.00 72.80           C  
ANISOU 2132  CZ  TYR A1068     9831   8484   9344    -40  -1220   -213       C  
ATOM   2133  OH  TYR A1068      -8.498  13.458   5.322  1.00 68.77           O  
ANISOU 2133  OH  TYR A1068     9195   7968   8968     -4  -1251   -275       O  
ATOM   2134  N   GLY A1069      -6.520  18.989   3.618  1.00 59.78           N  
ANISOU 2134  N   GLY A1069     8650   6643   7420    -69  -1577   -111       N  
ATOM   2135  CA  GLY A1069      -7.624  19.745   4.183  1.00 62.29           C  
ANISOU 2135  CA  GLY A1069     8856   6928   7882     -2  -1714   -155       C  
ATOM   2136  C   GLY A1069      -8.986  19.330   3.667  1.00 63.10           C  
ANISOU 2136  C   GLY A1069     8929   6957   8089     33  -1881   -219       C  
ATOM   2137  O   GLY A1069      -9.118  18.617   2.671  1.00 69.43           O  
ANISOU 2137  O   GLY A1069     9836   7716   8828      3  -1928   -224       O  
ATOM   2138  N   TRP A1070     -10.012  19.800   4.367  1.00 64.98           N  
ANISOU 2138  N   TRP A1070     9020   7176   8495     95  -1972   -274       N  
ATOM   2139  CA  TRP A1070     -11.400  19.534   4.012  1.00 78.58           C  
ANISOU 2139  CA  TRP A1070    10685   8819  10354    138  -2141   -349       C  
ATOM   2140  C   TRP A1070     -12.156  20.850   3.834  1.00 74.90           C  
ANISOU 2140  C   TRP A1070    10245   8257   9958    178  -2351   -375       C  
ATOM   2141  O   TRP A1070     -11.652  21.933   4.151  1.00 77.45           O  
ANISOU 2141  O   TRP A1070    10604   8586  10237    177  -2347   -337       O  
ATOM   2142  CB  TRP A1070     -12.098  18.679   5.080  1.00 77.93           C  
ANISOU 2142  CB  TRP A1070    10367   8793  10451    177  -2046   -414       C  
ATOM   2143  CG  TRP A1070     -11.790  17.195   5.057  1.00 71.87           C  
ANISOU 2143  CG  TRP A1070     9564   8088   9655    149  -1898   -412       C  
ATOM   2144  CD1 TRP A1070     -10.786  16.559   5.731  1.00 76.78           C  
ANISOU 2144  CD1 TRP A1070    10141   8816  10216    119  -1681   -368       C  
ATOM   2145  CD2 TRP A1070     -12.518  16.165   4.360  1.00 77.60           C  
ANISOU 2145  CD2 TRP A1070    10288   8773  10425    150  -1961   -459       C  
ATOM   2146  NE1 TRP A1070     -10.836  15.200   5.492  1.00 87.02           N  
ANISOU 2146  NE1 TRP A1070    11410  10138  11514    101  -1602   -383       N  
ATOM   2147  CE2 TRP A1070     -11.887  14.934   4.652  1.00 84.05           C  
ANISOU 2147  CE2 TRP A1070    11059   9676  11199    119  -1767   -439       C  
ATOM   2148  CE3 TRP A1070     -13.628  16.165   3.512  1.00 76.85           C  
ANISOU 2148  CE3 TRP A1070    10226   8572  10401    176  -2167   -518       C  
ATOM   2149  CZ2 TRP A1070     -12.339  13.720   4.136  1.00 82.44           C  
ANISOU 2149  CZ2 TRP A1070    10840   9462  11024    112  -1764   -475       C  
ATOM   2150  CZ3 TRP A1070     -14.073  14.956   3.000  1.00 79.91           C  
ANISOU 2150  CZ3 TRP A1070    10599   8949  10816    169  -2167   -555       C  
ATOM   2151  CH2 TRP A1070     -13.431  13.752   3.314  1.00 79.65           C  
ANISOU 2151  CH2 TRP A1070    10517   9008  10738    136  -1963   -533       C  
ATOM   2152  N   THR A1071     -13.381  20.741   3.312  1.00 75.86           N  
ANISOU 2152  N   THR A1071    10346   8284  10195    214  -2540   -442       N  
ATOM   2153  CA  THR A1071     -14.336  21.845   3.280  1.00 80.70           C  
ANISOU 2153  CA  THR A1071    10933   8798  10932    265  -2750   -488       C  
ATOM   2154  C   THR A1071     -15.739  21.305   3.516  1.00 84.06           C  
ANISOU 2154  C   THR A1071    11182   9174  11582    319  -2845   -594       C  
ATOM   2155  O   THR A1071     -15.978  20.093   3.547  1.00 76.43           O  
ANISOU 2155  O   THR A1071    10142   8242  10657    315  -2765   -626       O  
ATOM   2156  CB  THR A1071     -14.337  22.615   1.950  1.00 75.00           C  
ANISOU 2156  CB  THR A1071    10453   7959  10086    247  -2964   -454       C  
ATOM   2157  OG1 THR A1071     -14.679  21.725   0.879  1.00 80.97           O  
ANISOU 2157  OG1 THR A1071    11313   8658  10792    228  -3052   -469       O  
ATOM   2158  CG2 THR A1071     -12.991  23.273   1.678  1.00 74.88           C  
ANISOU 2158  CG2 THR A1071    10620   7976   9855    191  -2877   -358       C  
ATOM   2159  N   ARG A1072     -16.676  22.228   3.673  1.00 87.77           N  
ANISOU 2159  N   ARG A1072    11584   9557  12207    370  -3018   -652       N  
ATOM   2160  CA  ARG A1072     -18.090  21.897   3.646  1.00 95.64           C  
ANISOU 2160  CA  ARG A1072    12442  10471  13425    422  -3160   -761       C  
ATOM   2161  C   ARG A1072     -18.802  22.866   2.713  1.00 90.34           C  
ANISOU 2161  C   ARG A1072    11885   9650  12790    451  -3455   -783       C  
ATOM   2162  O   ARG A1072     -18.322  23.973   2.451  1.00 87.57           O  
ANISOU 2162  O   ARG A1072    11667   9269  12338    441  -3530   -725       O  
ATOM   2163  CB  ARG A1072     -18.707  21.926   5.046  1.00 93.39           C  
ANISOU 2163  CB  ARG A1072    11895  10227  13361    461  -3054   -839       C  
ATOM   2164  CG  ARG A1072     -18.385  20.705   5.864  1.00 85.06           C  
ANISOU 2164  CG  ARG A1072    10714   9290  12315    441  -2804   -845       C  
ATOM   2165  CD  ARG A1072     -19.313  20.608   7.040  1.00 81.94           C  
ANISOU 2165  CD  ARG A1072    10071   8898  12163    480  -2740   -947       C  
ATOM   2166  NE  ARG A1072     -18.778  19.781   8.118  1.00 81.09           N  
ANISOU 2166  NE  ARG A1072     9853   8915  12040    456  -2475   -934       N  
ATOM   2167  CZ  ARG A1072     -17.779  20.143   8.920  1.00 90.11           C  
ANISOU 2167  CZ  ARG A1072    11003  10155  13081    431  -2309   -864       C  
ATOM   2168  NH1 ARG A1072     -17.176  21.318   8.766  1.00 86.61           N  
ANISOU 2168  NH1 ARG A1072    10666   9704  12538    425  -2369   -802       N  
ATOM   2169  NH2 ARG A1072     -17.376  19.323   9.880  1.00 93.44           N  
ANISOU 2169  NH2 ARG A1072    11327  10678  13499    411  -2085   -857       N  
ATOM   2170  N   SER A1073     -19.944  22.415   2.190  1.00 97.03           N  
ANISOU 2170  N   SER A1073    12685  10400  13782    486  -3627   -868       N  
ATOM   2171  CA  SER A1073     -20.774  23.179   1.261  1.00103.59           C  
ANISOU 2171  CA  SER A1073    13614  11072  14672    520  -3934   -902       C  
ATOM   2172  C   SER A1073     -19.956  23.715   0.086  1.00107.93           C  
ANISOU 2172  C   SER A1073    14468  11578  14963    473  -4039   -799       C  
ATOM   2173  O   SER A1073     -19.766  24.935  -0.023  1.00110.43           O  
ANISOU 2173  O   SER A1073    14876  11843  15237    478  -4144   -762       O  
ATOM   2174  CB  SER A1073     -21.458  24.331   1.998  1.00 98.06           C  
ANISOU 2174  CB  SER A1073    12768  10316  14173    573  -4028   -962       C  
ATOM   2175  OG  SER A1073     -22.188  23.855   3.121  1.00 90.90           O  
ANISOU 2175  OG  SER A1073    11586   9447  13504    607  -3912  -1062       O  
ATOM   2176  N   PRO A1074     -19.452  22.847  -0.820  1.00105.83           N  
ANISOU 2176  N   PRO A1074    14371  11326  14516    422  -4010   -752       N  
ATOM   2177  CA  PRO A1074     -19.566  21.380  -0.791  1.00104.70           C  
ANISOU 2177  CA  PRO A1074    14142  11244  14396    409  -3881   -785       C  
ATOM   2178  C   PRO A1074     -18.430  20.648  -0.050  1.00 94.50           C  
ANISOU 2178  C   PRO A1074    12799  10116  12992    362  -3562   -726       C  
ATOM   2179  O   PRO A1074     -17.360  21.207   0.208  1.00 81.89           O  
ANISOU 2179  O   PRO A1074    11283   8583  11247    326  -3439   -645       O  
ATOM   2180  CB  PRO A1074     -19.546  21.013  -2.274  1.00102.45           C  
ANISOU 2180  CB  PRO A1074    14102  10872  13953    373  -4041   -756       C  
ATOM   2181  CG  PRO A1074     -18.637  22.049  -2.871  1.00100.82           C  
ANISOU 2181  CG  PRO A1074    14144  10636  13527    328  -4088   -658       C  
ATOM   2182  CD  PRO A1074     -18.916  23.321  -2.111  1.00101.50           C  
ANISOU 2182  CD  PRO A1074    14128  10698  13738    377  -4151   -674       C  
ATOM   2183  N   LEU A1075     -18.686  19.375   0.252  1.00 95.03           N  
ANISOU 2183  N   LEU A1075    12734  10241  13133    363  -3437   -771       N  
ATOM   2184  CA  LEU A1075     -17.791  18.504   1.015  1.00 85.09           C  
ANISOU 2184  CA  LEU A1075    11396   9128  11807    326  -3146   -732       C  
ATOM   2185  C   LEU A1075     -16.730  17.904   0.099  1.00 74.25           C  
ANISOU 2185  C   LEU A1075    10235   7789  10189    254  -3068   -649       C  
ATOM   2186  O   LEU A1075     -16.925  16.851  -0.499  1.00 71.91           O  
ANISOU 2186  O   LEU A1075     9966   7484   9871    236  -3066   -668       O  
ATOM   2187  CB  LEU A1075     -18.604  17.409   1.684  1.00 73.17           C  
ANISOU 2187  CB  LEU A1075     9660   7651  10490    359  -3062   -822       C  
ATOM   2188  CG  LEU A1075     -17.895  16.387   2.548  1.00 79.49           C  
ANISOU 2188  CG  LEU A1075    10353   8591  11259    330  -2777   -797       C  
ATOM   2189  CD1 LEU A1075     -17.083  17.100   3.624  1.00 80.31           C  
ANISOU 2189  CD1 LEU A1075    10405   8782  11328    323  -2620   -746       C  
ATOM   2190  CD2 LEU A1075     -18.933  15.442   3.145  1.00 79.09           C  
ANISOU 2190  CD2 LEU A1075    10085   8543  11424    368  -2734   -901       C  
ATOM   2191  N   ILE A1076     -15.581  18.566  -0.013  1.00 77.14           N  
ANISOU 2191  N   ILE A1076    10749   8191  10371    208  -2992   -559       N  
ATOM   2192  CA  ILE A1076     -14.468  18.030  -0.784  1.00 83.55           C  
ANISOU 2192  CA  ILE A1076    11752   9037  10957    132  -2885   -484       C  
ATOM   2193  C   ILE A1076     -13.248  17.858   0.135  1.00 86.53           C  
ANISOU 2193  C   ILE A1076    12066   9548  11262    100  -2614   -426       C  
ATOM   2194  O   ILE A1076     -13.244  18.278   1.296  1.00 82.76           O  
ANISOU 2194  O   ILE A1076    11426   9130  10888    135  -2529   -436       O  
ATOM   2195  CB  ILE A1076     -14.130  18.895  -2.018  1.00 77.99           C  
ANISOU 2195  CB  ILE A1076    11330   8230  10072     92  -3049   -430       C  
ATOM   2196  CG1 ILE A1076     -13.616  20.264  -1.605  1.00 91.54           C  
ANISOU 2196  CG1 ILE A1076    13088   9947  11747     96  -3055   -384       C  
ATOM   2197  CG2 ILE A1076     -15.337  19.050  -2.927  1.00 75.57           C  
ANISOU 2197  CG2 ILE A1076    11093   7783   9837    125  -3334   -487       C  
ATOM   2198  CD1 ILE A1076     -12.160  20.466  -1.932  1.00 91.65           C  
ANISOU 2198  CD1 ILE A1076    13282  10007  11534     19  -2903   -295       C  
ATOM   2199  N   GLU A1077     -12.217  17.202  -0.406  1.00 76.74           N  
ANISOU 2199  N   GLU A1077    10958   8352   9849     31  -2480   -370       N  
ATOM   2200  CA  GLU A1077     -11.010  16.825   0.332  1.00 72.31           C  
ANISOU 2200  CA  GLU A1077    10345   7911   9218     -5  -2224   -319       C  
ATOM   2201  C   GLU A1077      -9.818  17.076  -0.577  1.00 63.76           C  
ANISOU 2201  C   GLU A1077     9502   6813   7911    -85  -2174   -246       C  
ATOM   2202  O   GLU A1077      -9.736  16.501  -1.663  1.00 64.13           O  
ANISOU 2202  O   GLU A1077     9701   6812   7852   -133  -2211   -240       O  
ATOM   2203  CB  GLU A1077     -11.080  15.351   0.770  1.00 68.25           C  
ANISOU 2203  CB  GLU A1077     9684   7475   8775     -6  -2070   -348       C  
ATOM   2204  CG  GLU A1077      -9.804  14.733   1.342  1.00 66.91           C  
ANISOU 2204  CG  GLU A1077     9481   7417   8525    -50  -1817   -296       C  
ATOM   2205  CD  GLU A1077      -9.986  13.246   1.720  1.00 79.83           C  
ANISOU 2205  CD  GLU A1077    10976   9117  10238    -47  -1686   -328       C  
ATOM   2206  OE1 GLU A1077      -9.377  12.785   2.713  1.00 81.10           O  
ANISOU 2206  OE1 GLU A1077    11013   9374  10426    -48  -1499   -311       O  
ATOM   2207  OE2 GLU A1077     -10.751  12.531   1.033  1.00 80.35           O  
ANISOU 2207  OE2 GLU A1077    11056   9134  10340    -44  -1775   -373       O  
ATOM   2208  N   TYR A1078      -8.904  17.940  -0.166  1.00 61.69           N  
ANISOU 2208  N   TYR A1078     9278   6585   7575   -102  -2090   -194       N  
ATOM   2209  CA  TYR A1078      -7.862  18.391  -1.077  1.00 66.36           C  
ANISOU 2209  CA  TYR A1078    10110   7141   7963   -178  -2064   -134       C  
ATOM   2210  C   TYR A1078      -6.468  18.036  -0.568  1.00 65.86           C  
ANISOU 2210  C   TYR A1078    10024   7177   7823   -226  -1812    -88       C  
ATOM   2211  O   TYR A1078      -6.257  17.832   0.630  1.00 59.55           O  
ANISOU 2211  O   TYR A1078     9031   6472   7122   -192  -1682    -92       O  
ATOM   2212  CB  TYR A1078      -7.973  19.902  -1.329  1.00 69.90           C  
ANISOU 2212  CB  TYR A1078    10679   7511   8370   -166  -2219   -113       C  
ATOM   2213  CG  TYR A1078      -7.857  20.796  -0.105  1.00 74.17           C  
ANISOU 2213  CG  TYR A1078    11066   8108   9006   -116  -2172   -108       C  
ATOM   2214  CD1 TYR A1078      -6.620  21.307   0.295  1.00 79.24           C  
ANISOU 2214  CD1 TYR A1078    11744   8808   9555   -152  -2014    -55       C  
ATOM   2215  CD2 TYR A1078      -8.984  21.164   0.626  1.00 72.35           C  
ANISOU 2215  CD2 TYR A1078    10661   7867   8962    -37  -2287   -161       C  
ATOM   2216  CE1 TYR A1078      -6.508  22.142   1.411  1.00 75.60           C  
ANISOU 2216  CE1 TYR A1078    11148   8398   9178   -109  -1975    -50       C  
ATOM   2217  CE2 TYR A1078      -8.880  21.994   1.738  1.00 73.88           C  
ANISOU 2217  CE2 TYR A1078    10722   8109   9239      2  -2240   -158       C  
ATOM   2218  CZ  TYR A1078      -7.641  22.478   2.123  1.00 69.21           C  
ANISOU 2218  CZ  TYR A1078    10171   7579   8544    -34  -2087   -101       C  
ATOM   2219  OH  TYR A1078      -7.533  23.297   3.221  1.00 73.28           O  
ANISOU 2219  OH  TYR A1078    10559   8144   9140      4  -2042    -99       O  
ATOM   2220  N   TYR A1079      -5.517  17.964  -1.505  1.00 69.79           N  
ANISOU 2220  N   TYR A1079    10726   7645   8144   -308  -1748    -49       N  
ATOM   2221  CA  TYR A1079      -4.151  17.522  -1.247  1.00 68.86           C  
ANISOU 2221  CA  TYR A1079    10610   7604   7951   -366  -1514    -14       C  
ATOM   2222  C   TYR A1079      -3.207  18.312  -2.146  1.00 59.75           C  
ANISOU 2222  C   TYR A1079     9703   6386   6615   -443  -1500     29       C  
ATOM   2223  O   TYR A1079      -3.549  18.573  -3.300  1.00 64.26           O  
ANISOU 2223  O   TYR A1079    10478   6854   7084   -478  -1638     30       O  
ATOM   2224  CB  TYR A1079      -3.934  16.014  -1.563  1.00 58.11           C  
ANISOU 2224  CB  TYR A1079     9222   6277   6580   -405  -1394    -28       C  
ATOM   2225  CG  TYR A1079      -4.676  14.953  -0.769  1.00 57.44           C  
ANISOU 2225  CG  TYR A1079     8910   6260   6656   -347  -1362    -70       C  
ATOM   2226  CD1 TYR A1079      -6.031  14.708  -0.975  1.00 57.50           C  
ANISOU 2226  CD1 TYR A1079     8867   6221   6760   -297  -1530   -119       C  
ATOM   2227  CD2 TYR A1079      -3.989  14.134   0.136  1.00 56.09           C  
ANISOU 2227  CD2 TYR A1079     8582   6191   6537   -348  -1161    -62       C  
ATOM   2228  CE1 TYR A1079      -6.697  13.705  -0.255  1.00 61.34           C  
ANISOU 2228  CE1 TYR A1079     9148   6765   7395   -249  -1486   -162       C  
ATOM   2229  CE2 TYR A1079      -4.639  13.137   0.853  1.00 55.70           C  
ANISOU 2229  CE2 TYR A1079     8339   6199   6626   -301  -1122    -99       C  
ATOM   2230  CZ  TYR A1079      -5.982  12.918   0.653  1.00 63.92           C  
ANISOU 2230  CZ  TYR A1079     9331   7195   7761   -254  -1277   -149       C  
ATOM   2231  OH  TYR A1079      -6.601  11.915   1.370  1.00 66.40           O  
ANISOU 2231  OH  TYR A1079     9454   7562   8212   -212  -1224   -190       O  
ATOM   2232  N   VAL A1080      -2.023  18.662  -1.632  1.00 55.09           N  
ANISOU 2232  N   VAL A1080     9098   5850   5984   -472  -1332     61       N  
ATOM   2233  CA  VAL A1080      -0.877  19.112  -2.427  1.00 57.66           C  
ANISOU 2233  CA  VAL A1080     9638   6128   6141   -561  -1247     95       C  
ATOM   2234  C   VAL A1080       0.293  18.238  -1.984  1.00 58.21           C  
ANISOU 2234  C   VAL A1080     9621   6283   6215   -603  -1003    100       C  
ATOM   2235  O   VAL A1080       0.884  18.475  -0.929  1.00 61.24           O  
ANISOU 2235  O   VAL A1080     9860   6744   6666   -574   -892    112       O  
ATOM   2236  CB  VAL A1080      -0.550  20.612  -2.242  1.00 59.71           C  
ANISOU 2236  CB  VAL A1080     9972   6357   6358   -553  -1295    123       C  
ATOM   2237  CG1 VAL A1080       0.587  21.050  -3.140  1.00 52.67           C  
ANISOU 2237  CG1 VAL A1080     9317   5405   5291   -652  -1204    150       C  
ATOM   2238  CG2 VAL A1080      -1.747  21.480  -2.521  1.00 60.00           C  
ANISOU 2238  CG2 VAL A1080    10062   6314   6421   -500  -1542    114       C  
ATOM   2239  N   VAL A1081       0.650  17.249  -2.795  1.00 65.27           N  
ANISOU 2239  N   VAL A1081    10606   7157   7038   -672   -922     91       N  
ATOM   2240  CA  VAL A1081       1.619  16.233  -2.406  1.00 55.55           C  
ANISOU 2240  CA  VAL A1081     9274   6000   5834   -707   -705     88       C  
ATOM   2241  C   VAL A1081       3.001  16.626  -2.914  1.00 56.78           C  
ANISOU 2241  C   VAL A1081     9583   6122   5868   -799   -558    105       C  
ATOM   2242  O   VAL A1081       3.216  16.762  -4.123  1.00 57.62           O  
ANISOU 2242  O   VAL A1081     9920   6137   5834   -880   -575    105       O  
ATOM   2243  CB  VAL A1081       1.209  14.844  -2.932  1.00 55.66           C  
ANISOU 2243  CB  VAL A1081     9273   6014   5860   -729   -688     61       C  
ATOM   2244  CG1 VAL A1081       2.081  13.748  -2.317  1.00 52.84           C  
ANISOU 2244  CG1 VAL A1081     8766   5742   5568   -747   -476     56       C  
ATOM   2245  CG2 VAL A1081      -0.278  14.564  -2.670  1.00 54.61           C  
ANISOU 2245  CG2 VAL A1081     9027   5885   5836   -646   -860     35       C  
ATOM   2246  N   ASP A1082       3.957  16.746  -1.994  1.00 55.99           N  
ANISOU 2246  N   ASP A1082     9358   6093   5825   -791   -407    115       N  
ATOM   2247  CA  ASP A1082       5.327  17.074  -2.351  1.00 56.68           C  
ANISOU 2247  CA  ASP A1082     9558   6152   5825   -875   -249    122       C  
ATOM   2248  C   ASP A1082       6.262  15.878  -2.357  1.00 57.77           C  
ANISOU 2248  C   ASP A1082     9634   6325   5989   -930    -50    102       C  
ATOM   2249  O   ASP A1082       7.325  15.951  -2.980  1.00 69.73           O  
ANISOU 2249  O   ASP A1082    11278   7793   7422  -1020     81     94       O  
ATOM   2250  CB  ASP A1082       5.883  18.131  -1.389  1.00 64.07           C  
ANISOU 2250  CB  ASP A1082    10410   7128   6804   -835   -215    141       C  
ATOM   2251  CG  ASP A1082       5.577  19.568  -1.843  1.00 68.37           C  
ANISOU 2251  CG  ASP A1082    11121   7597   7259   -835   -351    160       C  
ATOM   2252  OD1 ASP A1082       5.039  19.773  -2.957  1.00 59.60           O  
ANISOU 2252  OD1 ASP A1082    10212   6395   6040   -874   -468    160       O  
ATOM   2253  OD2 ASP A1082       5.860  20.499  -1.062  1.00 73.58           O  
ANISOU 2253  OD2 ASP A1082    11710   8288   7958   -795   -348    175       O  
ATOM   2254  N   SER A1083       5.917  14.793  -1.677  1.00 63.92           N  
ANISOU 2254  N   SER A1083    10221   7182   6885   -881    -20     92       N  
ATOM   2255  CA  SER A1083       6.763  13.605  -1.694  1.00 64.17           C  
ANISOU 2255  CA  SER A1083    10188   7242   6950   -931    159     73       C  
ATOM   2256  C   SER A1083       5.937  12.415  -1.229  1.00 63.93           C  
ANISOU 2256  C   SER A1083     9992   7274   7025   -875    130     62       C  
ATOM   2257  O   SER A1083       4.860  12.565  -0.644  1.00 61.26           O  
ANISOU 2257  O   SER A1083     9553   6969   6755   -791     -2     67       O  
ATOM   2258  CB  SER A1083       8.009  13.785  -0.822  1.00 62.72           C  
ANISOU 2258  CB  SER A1083     9892   7108   6831   -933    317     77       C  
ATOM   2259  OG  SER A1083       8.973  12.787  -1.090  1.00 65.62           O  
ANISOU 2259  OG  SER A1083    10243   7474   7215  -1001    491     53       O  
ATOM   2260  N   TRP A1084       6.461  11.225  -1.497  1.00 66.72           N  
ANISOU 2260  N   TRP A1084    10315   7637   7397   -925    262     42       N  
ATOM   2261  CA  TRP A1084       5.740   9.988  -1.234  1.00 52.49           C  
ANISOU 2261  CA  TRP A1084     8379   5882   5681   -886    250     28       C  
ATOM   2262  C   TRP A1084       6.759   8.884  -1.022  1.00 50.69           C  
ANISOU 2262  C   TRP A1084     8059   5690   5511   -928    440     14       C  
ATOM   2263  O   TRP A1084       7.967   9.097  -1.120  1.00 56.55           O  
ANISOU 2263  O   TRP A1084     8841   6413   6231   -986    572     10       O  
ATOM   2264  CB  TRP A1084       4.773   9.666  -2.375  1.00 55.74           C  
ANISOU 2264  CB  TRP A1084     8932   6231   6017   -913    132     11       C  
ATOM   2265  CG  TRP A1084       5.413   9.631  -3.736  1.00 63.33           C  
ANISOU 2265  CG  TRP A1084    10122   7103   6838  -1028    194     -2       C  
ATOM   2266  CD1 TRP A1084       5.953   8.538  -4.363  1.00 62.64           C  
ANISOU 2266  CD1 TRP A1084    10067   7000   6733  -1105    326    -27       C  
ATOM   2267  CD2 TRP A1084       5.571  10.733  -4.649  1.00 63.90           C  
ANISOU 2267  CD2 TRP A1084    10430   7083   6766  -1086    132      7       C  
ATOM   2268  NE1 TRP A1084       6.441   8.893  -5.604  1.00 60.53           N  
ANISOU 2268  NE1 TRP A1084    10044   6637   6319  -1210    356    -37       N  
ATOM   2269  CE2 TRP A1084       6.221  10.232  -5.803  1.00 66.35           C  
ANISOU 2269  CE2 TRP A1084    10914   7324   6971  -1201    239    -15       C  
ATOM   2270  CE3 TRP A1084       5.236  12.092  -4.598  1.00 62.38           C  
ANISOU 2270  CE3 TRP A1084    10322   6857   6523  -1054      0     30       C  
ATOM   2271  CZ2 TRP A1084       6.545  11.047  -6.899  1.00 72.06           C  
ANISOU 2271  CZ2 TRP A1084    11904   7943   7533  -1288    221    -14       C  
ATOM   2272  CZ3 TRP A1084       5.544  12.902  -5.697  1.00 66.80           C  
ANISOU 2272  CZ3 TRP A1084    11144   7313   6925  -1135    -27     34       C  
ATOM   2273  CH2 TRP A1084       6.192  12.371  -6.833  1.00 72.65           C  
ANISOU 2273  CH2 TRP A1084    12064   7984   7555  -1253     84     12       C  
ATOM   2274  N   GLY A1085       6.264   7.701  -0.702  1.00 52.34           N  
ANISOU 2274  N   GLY A1085     8136   5945   5805   -897    454      2       N  
ATOM   2275  CA  GLY A1085       7.150   6.563  -0.611  1.00 50.96           C  
ANISOU 2275  CA  GLY A1085     7881   5794   5686   -939    623    -13       C  
ATOM   2276  C   GLY A1085       7.090   5.745  -1.882  1.00 52.45           C  
ANISOU 2276  C   GLY A1085     8198   5924   5804  -1022    659    -42       C  
ATOM   2277  O   GLY A1085       7.384   6.255  -2.965  1.00 52.51           O  
ANISOU 2277  O   GLY A1085     8408   5853   5689  -1101    660    -52       O  
ATOM   2278  N   THR A1086       6.661   4.489  -1.766  1.00 57.33           N  
ANISOU 2278  N   THR A1086     8708   6578   6495  -1005    684    -57       N  
ATOM   2279  CA  THR A1086       6.621   3.572  -2.891  1.00 50.29           C  
ANISOU 2279  CA  THR A1086     7917   5640   5551  -1082    730    -87       C  
ATOM   2280  C   THR A1086       5.403   3.749  -3.788  1.00 58.37           C  
ANISOU 2280  C   THR A1086     9076   6613   6487  -1082    565    -95       C  
ATOM   2281  O   THR A1086       5.152   2.856  -4.599  1.00 67.04           O  
ANISOU 2281  O   THR A1086    10231   7683   7557  -1130    584   -121       O  
ATOM   2282  CB  THR A1086       6.654   2.127  -2.399  1.00 53.13           C  
ANISOU 2282  CB  THR A1086     8102   6057   6028  -1064    824   -101       C  
ATOM   2283  OG1 THR A1086       5.477   1.861  -1.632  1.00 53.21           O  
ANISOU 2283  OG1 THR A1086     7975   6125   6119   -966    711    -92       O  
ATOM   2284  CG2 THR A1086       7.869   1.889  -1.551  1.00 55.41           C  
ANISOU 2284  CG2 THR A1086     8261   6385   6408  -1066    975    -95       C  
ATOM   2285  N   TYR A1087       4.647   4.848  -3.711  1.00 63.98           N  
ANISOU 2285  N   TYR A1087     9844   7306   7158  -1031    402    -78       N  
ATOM   2286  CA  TYR A1087       3.468   4.957  -4.570  1.00 58.04           C  
ANISOU 2286  CA  TYR A1087     9215   6498   6337  -1027    231    -90       C  
ATOM   2287  C   TYR A1087       3.039   6.408  -4.761  1.00 63.39           C  
ANISOU 2287  C   TYR A1087    10022   7126   6938  -1005     73    -70       C  
ATOM   2288  O   TYR A1087       2.843   7.145  -3.784  1.00 60.51           O  
ANISOU 2288  O   TYR A1087     9547   6804   6639   -928     20    -50       O  
ATOM   2289  CB  TYR A1087       2.294   4.143  -4.008  1.00 53.48           C  
ANISOU 2289  CB  TYR A1087     8467   5974   5878   -943    150   -105       C  
ATOM   2290  CG  TYR A1087       0.980   4.394  -4.716  1.00 50.95           C  
ANISOU 2290  CG  TYR A1087     8245   5597   5516   -919    -52   -122       C  
ATOM   2291  CD1 TYR A1087       0.687   3.755  -5.922  1.00 51.94           C  
ANISOU 2291  CD1 TYR A1087     8512   5661   5562   -983    -79   -148       C  
ATOM   2292  CD2 TYR A1087       0.033   5.263  -4.183  1.00 48.67           C  
ANISOU 2292  CD2 TYR A1087     7907   5311   5274   -833   -219   -116       C  
ATOM   2293  CE1 TYR A1087      -0.508   3.959  -6.565  1.00 52.83           C  
ANISOU 2293  CE1 TYR A1087     8714   5716   5644   -959   -276   -166       C  
ATOM   2294  CE2 TYR A1087      -1.162   5.484  -4.821  1.00 51.11           C  
ANISOU 2294  CE2 TYR A1087     8297   5559   5563   -808   -412   -137       C  
ATOM   2295  CZ  TYR A1087      -1.427   4.832  -6.017  1.00 55.22           C  
ANISOU 2295  CZ  TYR A1087     8960   6018   6004   -870   -445   -161       C  
ATOM   2296  OH  TYR A1087      -2.604   5.050  -6.672  1.00 57.70           O  
ANISOU 2296  OH  TYR A1087     9358   6265   6300   -845   -650   -184       O  
ATOM   2297  N   ARG A1088       2.818   6.788  -6.025  1.00 61.91           N  
ANISOU 2297  N   ARG A1088    10070   6843   6610  -1070    -11    -77       N  
ATOM   2298  CA  ARG A1088       2.415   8.142  -6.350  1.00 65.72           C  
ANISOU 2298  CA  ARG A1088    10701   7262   7007  -1057   -170    -58       C  
ATOM   2299  C   ARG A1088       0.921   8.191  -6.585  1.00 62.68           C  
ANISOU 2299  C   ARG A1088    10322   6849   6645   -993   -392    -71       C  
ATOM   2300  O   ARG A1088       0.428   7.468  -7.460  1.00 57.89           O  
ANISOU 2300  O   ARG A1088     9802   6197   5994  -1029   -439    -95       O  
ATOM   2301  CB  ARG A1088       3.148   8.636  -7.583  1.00 64.67           C  
ANISOU 2301  CB  ARG A1088    10844   7029   6697  -1173   -130    -56       C  
ATOM   2302  CG  ARG A1088       2.735  10.016  -8.039  1.00 59.28           C  
ANISOU 2302  CG  ARG A1088    10345   6268   5911  -1169   -301    -34       C  
ATOM   2303  CD  ARG A1088       3.729  10.515  -9.065  1.00 61.16           C  
ANISOU 2303  CD  ARG A1088    10844   6415   5980  -1291   -209    -31       C  
ATOM   2304  NE  ARG A1088       3.456  11.896  -9.398  1.00 68.18           N  
ANISOU 2304  NE  ARG A1088    11904   7230   6771  -1286   -358     -6       N  
ATOM   2305  CZ  ARG A1088       2.654  12.276 -10.375  1.00 64.91           C  
ANISOU 2305  CZ  ARG A1088    11700   6720   6245  -1306   -542     -4       C  
ATOM   2306  NH1 ARG A1088       2.054  11.367 -11.129  1.00 65.87           N  
ANISOU 2306  NH1 ARG A1088    11884   6808   6335  -1333   -597    -28       N  
ATOM   2307  NH2 ARG A1088       2.450  13.563 -10.583  1.00 65.09           N  
ANISOU 2307  NH2 ARG A1088    11866   6677   6190  -1296   -676     22       N  
ATOM   2308  N   PRO A1089       0.174   9.027  -5.861  1.00 57.97           N  
ANISOU 2308  N   PRO A1089     9638   6269   6119   -902   -533    -60       N  
ATOM   2309  CA  PRO A1089      -1.285   9.062  -6.030  1.00 56.24           C  
ANISOU 2309  CA  PRO A1089     9402   6018   5950   -835   -747    -82       C  
ATOM   2310  C   PRO A1089      -1.675   9.617  -7.389  1.00 59.55           C  
ANISOU 2310  C   PRO A1089    10092   6315   6219   -889   -906    -84       C  
ATOM   2311  O   PRO A1089      -0.865  10.217  -8.100  1.00 59.52           O  
ANISOU 2311  O   PRO A1089    10296   6250   6068   -971   -862    -62       O  
ATOM   2312  CB  PRO A1089      -1.755   9.963  -4.895  1.00 59.06           C  
ANISOU 2312  CB  PRO A1089     9608   6416   6415   -738   -830    -72       C  
ATOM   2313  CG  PRO A1089      -0.546  10.800  -4.554  1.00 59.25           C  
ANISOU 2313  CG  PRO A1089     9675   6457   6379   -772   -710    -34       C  
ATOM   2314  CD  PRO A1089       0.654   9.970  -4.834  1.00 51.19           C  
ANISOU 2314  CD  PRO A1089     8684   5459   5309   -856   -497    -32       C  
ATOM   2315  N   THR A1090      -2.948   9.406  -7.746  1.00 64.44           N  
ANISOU 2315  N   THR A1090    10712   6892   6880   -843  -1096   -113       N  
ATOM   2316  CA  THR A1090      -3.414   9.688  -9.102  1.00 64.22           C  
ANISOU 2316  CA  THR A1090    10943   6743   6714   -895  -1260   -119       C  
ATOM   2317  C   THR A1090      -4.936   9.815  -9.152  1.00 64.44           C  
ANISOU 2317  C   THR A1090    10922   6728   6835   -810  -1509   -152       C  
ATOM   2318  O   THR A1090      -5.648   9.551  -8.177  1.00 65.99           O  
ANISOU 2318  O   THR A1090    10879   6989   7207   -717  -1536   -177       O  
ATOM   2319  CB  THR A1090      -2.956   8.604 -10.085  1.00 78.57           C  
ANISOU 2319  CB  THR A1090    12887   8535   8432   -994  -1150   -134       C  
ATOM   2320  OG1 THR A1090      -3.634   8.786 -11.333  1.00 82.43           O  
ANISOU 2320  OG1 THR A1090    13610   8905   8803  -1031  -1338   -146       O  
ATOM   2321  CG2 THR A1090      -3.262   7.200  -9.552  1.00 66.12           C  
ANISOU 2321  CG2 THR A1090    11083   7043   6995   -958  -1056   -168       C  
ATOM   2322  N   GLY A1091      -5.420  10.211 -10.330  1.00 61.97           N  
ANISOU 2322  N   GLY A1091    10849   6296   6402   -847  -1691   -155       N  
ATOM   2323  CA  GLY A1091      -6.833  10.375 -10.637  1.00 66.58           C  
ANISOU 2323  CA  GLY A1091    11435   6808   7054   -779  -1954   -190       C  
ATOM   2324  C   GLY A1091      -7.040  10.807 -12.082  1.00 69.11           C  
ANISOU 2324  C   GLY A1091    12077   6987   7195   -848  -2127   -183       C  
ATOM   2325  O   GLY A1091      -6.197  10.514 -12.931  1.00 69.09           O  
ANISOU 2325  O   GLY A1091    12276   6952   7024   -956  -2014   -165       O  
ATOM   2326  N   THR A1092      -8.137  11.497 -12.393  1.00 77.75           N  
ANISOU 2326  N   THR A1092    13230   7989   8320   -790  -2399   -199       N  
ATOM   2327  CA  THR A1092      -8.338  12.027 -13.740  1.00 84.80           C  
ANISOU 2327  CA  THR A1092    14449   8737   9035   -853  -2585   -187       C  
ATOM   2328  C   THR A1092      -7.472  13.267 -13.946  1.00 80.48           C  
ANISOU 2328  C   THR A1092    14101   8143   8334   -907  -2559   -130       C  
ATOM   2329  O   THR A1092      -7.586  14.240 -13.198  1.00 77.50           O  
ANISOU 2329  O   THR A1092    13629   7783   8035   -841  -2613   -114       O  
ATOM   2330  CB  THR A1092      -9.803  12.368 -13.993  1.00 81.30           C  
ANISOU 2330  CB  THR A1092    14000   8201   8688   -769  -2900   -226       C  
ATOM   2331  OG1 THR A1092     -10.647  11.419 -13.332  1.00 84.32           O  
ANISOU 2331  OG1 THR A1092    14105   8653   9281   -688  -2904   -285       O  
ATOM   2332  CG2 THR A1092     -10.078  12.332 -15.488  1.00 80.73           C  
ANISOU 2332  CG2 THR A1092    14248   7988   8439   -843  -3072   -226       C  
ATOM   2333  N   TYR A1093      -6.613  13.226 -14.963  1.00 81.62           N  
ANISOU 2333  N   TYR A1093    14522   8226   8264  -1030  -2471   -103       N  
ATOM   2334  CA  TYR A1093      -5.678  14.310 -15.235  1.00 78.94           C  
ANISOU 2334  CA  TYR A1093    14390   7839   7766  -1098  -2413    -54       C  
ATOM   2335  C   TYR A1093      -6.402  15.496 -15.868  1.00 79.47           C  
ANISOU 2335  C   TYR A1093    14671   7766   7756  -1078  -2703    -37       C  
ATOM   2336  O   TYR A1093      -7.098  15.348 -16.880  1.00 80.26           O  
ANISOU 2336  O   TYR A1093    14965   7755   7775  -1101  -2898    -51       O  
ATOM   2337  CB  TYR A1093      -4.563  13.804 -16.147  1.00 77.48           C  
ANISOU 2337  CB  TYR A1093    14433   7624   7383  -1243  -2215    -42       C  
ATOM   2338  CG  TYR A1093      -3.554  14.835 -16.610  1.00 89.75           C  
ANISOU 2338  CG  TYR A1093    16239   9109   8752  -1335  -2139      1       C  
ATOM   2339  CD1 TYR A1093      -3.901  15.822 -17.529  1.00 93.86           C  
ANISOU 2339  CD1 TYR A1093    17061   9484   9118  -1368  -2350     25       C  
ATOM   2340  CD2 TYR A1093      -2.234  14.787 -16.168  1.00 92.76           C  
ANISOU 2340  CD2 TYR A1093    16569   9564   9112  -1393  -1854     15       C  
ATOM   2341  CE1 TYR A1093      -2.980  16.751 -17.962  1.00 96.14           C  
ANISOU 2341  CE1 TYR A1093    17588   9705   9234  -1456  -2271     62       C  
ATOM   2342  CE2 TYR A1093      -1.299  15.713 -16.604  1.00 87.90           C  
ANISOU 2342  CE2 TYR A1093    16182   8881   8334  -1481  -1772     47       C  
ATOM   2343  CZ  TYR A1093      -1.681  16.694 -17.502  1.00 93.58           C  
ANISOU 2343  CZ  TYR A1093    17200   9458   8897  -1513  -1978     71       C  
ATOM   2344  OH  TYR A1093      -0.768  17.629 -17.946  1.00 95.31           O  
ANISOU 2344  OH  TYR A1093    17658   9604   8951  -1604  -1894    101       O  
ATOM   2345  N   LYS A1094      -6.218  16.681 -15.273  1.00 82.67           N  
ANISOU 2345  N   LYS A1094    15047   8176   8188  -1036  -2732     -6       N  
ATOM   2346  CA  LYS A1094      -6.884  17.899 -15.716  1.00 88.09           C  
ANISOU 2346  CA  LYS A1094    15908   8737   8826  -1006  -3005     12       C  
ATOM   2347  C   LYS A1094      -5.929  19.021 -16.096  1.00 86.63           C  
ANISOU 2347  C   LYS A1094    15969   8489   8457  -1084  -2946     65       C  
ATOM   2348  O   LYS A1094      -6.358  19.965 -16.768  1.00 95.91           O  
ANISOU 2348  O   LYS A1094    17372   9534   9536  -1089  -3168     86       O  
ATOM   2349  CB  LYS A1094      -7.851  18.419 -14.638  1.00 81.73           C  
ANISOU 2349  CB  LYS A1094    14827   7973   8253   -863  -3156    -10       C  
ATOM   2350  CG  LYS A1094      -8.913  17.419 -14.222  1.00 79.44           C  
ANISOU 2350  CG  LYS A1094    14289   7733   8163   -779  -3232    -70       C  
ATOM   2351  CD  LYS A1094     -10.279  18.065 -14.213  1.00 83.71           C  
ANISOU 2351  CD  LYS A1094    14789   8184   8833   -680  -3550   -101       C  
ATOM   2352  CE  LYS A1094     -11.367  17.044 -14.528  1.00 90.35           C  
ANISOU 2352  CE  LYS A1094    15545   8999   9783   -639  -3688   -164       C  
ATOM   2353  NZ  LYS A1094     -12.642  17.669 -14.982  1.00 96.88           N  
ANISOU 2353  NZ  LYS A1094    16437   9690  10682   -571  -4037   -195       N  
ATOM   2354  N   GLY A1095      -4.659  18.945 -15.710  1.00 83.01           N  
ANISOU 2354  N   GLY A1095    15477   8112   7950  -1146  -2660     85       N  
ATOM   2355  CA  GLY A1095      -3.722  19.993 -16.061  1.00 86.48           C  
ANISOU 2355  CA  GLY A1095    16144   8490   8223  -1224  -2588    129       C  
ATOM   2356  C   GLY A1095      -2.421  20.020 -15.277  1.00 88.28           C  
ANISOU 2356  C   GLY A1095    16243   8829   8470  -1256  -2283    141       C  
ATOM   2357  O   GLY A1095      -1.834  18.978 -14.974  1.00 79.50           O  
ANISOU 2357  O   GLY A1095    14992   7810   7404  -1285  -2064    120       O  
ATOM   2358  N   THR A1096      -1.947  21.220 -14.958  1.00 95.56           N  
ANISOU 2358  N   THR A1096    17214   9736   9361  -1252  -2271    174       N  
ATOM   2359  CA  THR A1096      -0.674  21.367 -14.269  1.00 93.02           C  
ANISOU 2359  CA  THR A1096    16790   9502   9050  -1286  -1995    184       C  
ATOM   2360  C   THR A1096      -0.657  22.743 -13.613  1.00 94.08           C  
ANISOU 2360  C   THR A1096    16884   9637   9227  -1224  -2066    214       C  
ATOM   2361  O   THR A1096      -1.485  23.605 -13.929  1.00 98.79           O  
ANISOU 2361  O   THR A1096    17594  10140   9800  -1182  -2315    229       O  
ATOM   2362  CB  THR A1096       0.497  21.133 -15.249  1.00 87.57           C  
ANISOU 2362  CB  THR A1096    16369   8749   8156  -1441  -1794    187       C  
ATOM   2363  OG1 THR A1096       0.555  19.737 -15.571  1.00 84.73           O  
ANISOU 2363  OG1 THR A1096    15967   8424   7804  -1485  -1687    154       O  
ATOM   2364  CG2 THR A1096       1.860  21.555 -14.692  1.00 83.50           C  
ANISOU 2364  CG2 THR A1096    15802   8290   7633  -1486  -1532    196       C  
ATOM   2365  N   VAL A1097       0.224  22.897 -12.616  1.00 88.24           N  
ANISOU 2365  N   VAL A1097    15954   9005   8570  -1209  -1857    218       N  
ATOM   2366  CA  VAL A1097       0.595  24.193 -12.059  1.00 93.67           C  
ANISOU 2366  CA  VAL A1097    16630   9694   9266  -1180  -1857    246       C  
ATOM   2367  C   VAL A1097       2.101  24.189 -11.821  1.00 97.03           C  
ANISOU 2367  C   VAL A1097    17055  10169   9642  -1259  -1560    248       C  
ATOM   2368  O   VAL A1097       2.696  23.162 -11.474  1.00 95.56           O  
ANISOU 2368  O   VAL A1097    16723  10070   9515  -1282  -1360    224       O  
ATOM   2369  CB  VAL A1097      -0.149  24.535 -10.739  1.00 94.19           C  
ANISOU 2369  CB  VAL A1097    16382   9855   9550  -1038  -1954    241       C  
ATOM   2370  CG1 VAL A1097      -0.129  26.035 -10.494  1.00 85.76           C  
ANISOU 2370  CG1 VAL A1097    15376   8742   8466  -1007  -2050    271       C  
ATOM   2371  CG2 VAL A1097      -1.576  24.009 -10.731  1.00 91.61           C  
ANISOU 2371  CG2 VAL A1097    15948   9520   9338   -954  -2177    215       C  
ATOM   2372  N   LYS A1098       2.722  25.347 -12.026  1.00 94.62           N  
ANISOU 2372  N   LYS A1098    16917   9801   9234  -1302  -1535    273       N  
ATOM   2373  CA  LYS A1098       4.095  25.581 -11.607  1.00 93.98           C  
ANISOU 2373  CA  LYS A1098    16799   9768   9140  -1357  -1273    271       C  
ATOM   2374  C   LYS A1098       4.082  26.412 -10.331  1.00 94.21           C  
ANISOU 2374  C   LYS A1098    16594   9884   9316  -1254  -1286    285       C  
ATOM   2375  O   LYS A1098       3.307  27.369 -10.209  1.00 92.77           O  
ANISOU 2375  O   LYS A1098    16434   9661   9152  -1188  -1491    307       O  
ATOM   2376  CB  LYS A1098       4.899  26.300 -12.688  1.00 96.95           C  
ANISOU 2376  CB  LYS A1098    17523  10013   9302  -1485  -1205    284       C  
ATOM   2377  CG  LYS A1098       6.369  26.512 -12.326  1.00 98.10           C  
ANISOU 2377  CG  LYS A1098    17636  10197   9441  -1550   -921    271       C  
ATOM   2378  CD  LYS A1098       7.313  25.796 -13.283  1.00100.55           C  
ANISOU 2378  CD  LYS A1098    18142  10446   9618  -1697   -712    241       C  
ATOM   2379  CE  LYS A1098       8.523  25.218 -12.561  1.00 98.81           C  
ANISOU 2379  CE  LYS A1098    17716  10325   9504  -1722   -424    206       C  
ATOM   2380  NZ  LYS A1098       9.298  26.234 -11.792  1.00 99.02           N  
ANISOU 2380  NZ  LYS A1098    17657  10385   9583  -1698   -326    212       N  
ATOM   2381  N   SER A1099       4.936  26.035  -9.381  1.00 93.18           N  
ANISOU 2381  N   SER A1099    16239   9871   9296  -1240  -1071    270       N  
ATOM   2382  CA  SER A1099       4.965  26.722  -8.097  1.00 81.68           C  
ANISOU 2382  CA  SER A1099    14547   8506   7983  -1145  -1068    280       C  
ATOM   2383  C   SER A1099       6.180  26.283  -7.305  1.00 81.26           C  
ANISOU 2383  C   SER A1099    14317   8553   8004  -1164   -804    262       C  
ATOM   2384  O   SER A1099       6.597  25.123  -7.369  1.00 73.97           O  
ANISOU 2384  O   SER A1099    13330   7671   7105  -1202   -662    237       O  
ATOM   2385  CB  SER A1099       3.701  26.454  -7.284  1.00 72.03           C  
ANISOU 2385  CB  SER A1099    13086   7354   6926  -1018  -1242    276       C  
ATOM   2386  OG  SER A1099       3.754  27.187  -6.088  1.00 74.85           O  
ANISOU 2386  OG  SER A1099    13241   7790   7408   -937  -1234    284       O  
ATOM   2387  N   ASP A1100       6.740  27.237  -6.563  1.00 70.70           N  
ANISOU 2387  N   ASP A1100    12904   7250   6710  -1135   -746    273       N  
ATOM   2388  CA  ASP A1100       7.794  26.986  -5.584  1.00 75.14           C  
ANISOU 2388  CA  ASP A1100    13261   7914   7375  -1128   -530    257       C  
ATOM   2389  C   ASP A1100       8.957  26.190  -6.174  1.00 82.81           C  
ANISOU 2389  C   ASP A1100    14319   8864   8282  -1241   -301    227       C  
ATOM   2390  O   ASP A1100       9.621  25.422  -5.467  1.00 92.83           O  
ANISOU 2390  O   ASP A1100    15393  10221   9659  -1232   -138    205       O  
ATOM   2391  CB  ASP A1100       7.224  26.296  -4.341  1.00 74.28           C  
ANISOU 2391  CB  ASP A1100    12834   7935   7453  -1019   -555    251       C  
ATOM   2392  CG  ASP A1100       5.904  26.912  -3.894  1.00 83.57           C  
ANISOU 2392  CG  ASP A1100    13932   9119   8700   -916   -790    269       C  
ATOM   2393  OD1 ASP A1100       5.893  28.015  -3.296  1.00 90.87           O  
ANISOU 2393  OD1 ASP A1100    14811  10055   9660   -868   -838    285       O  
ATOM   2394  OD2 ASP A1100       4.861  26.294  -4.146  1.00 89.23           O  
ANISOU 2394  OD2 ASP A1100    14631   9828   9446   -882   -927    262       O  
ATOM   2395  N   GLY A1101       9.221  26.379  -7.468  1.00 77.75           N  
ANISOU 2395  N   GLY A1101    13976   8099   7467  -1349   -286    224       N  
ATOM   2396  CA  GLY A1101      10.342  25.729  -8.125  1.00 73.52           C  
ANISOU 2396  CA  GLY A1101    13549   7524   6862  -1470    -62    188       C  
ATOM   2397  C   GLY A1101      10.099  24.308  -8.587  1.00 85.33           C  
ANISOU 2397  C   GLY A1101    15029   9030   8362  -1504    -28    166       C  
ATOM   2398  O   GLY A1101      11.066  23.555  -8.767  1.00 77.74           O  
ANISOU 2398  O   GLY A1101    14056   8074   7409  -1581    183    129       O  
ATOM   2399  N   GLY A1102       8.840  23.914  -8.780  1.00 90.20           N  
ANISOU 2399  N   GLY A1102    15640   9648   8983  -1448   -227    182       N  
ATOM   2400  CA  GLY A1102       8.497  22.583  -9.248  1.00 84.46           C  
ANISOU 2400  CA  GLY A1102    14903   8928   8259  -1475   -214    161       C  
ATOM   2401  C   GLY A1102       7.126  22.614  -9.882  1.00 80.94           C  
ANISOU 2401  C   GLY A1102    14578   8424   7752  -1441   -469    180       C  
ATOM   2402  O   GLY A1102       6.368  23.574  -9.722  1.00 82.97           O  
ANISOU 2402  O   GLY A1102    14861   8655   8007  -1375   -662    209       O  
ATOM   2403  N   THR A1103       6.804  21.550 -10.613  1.00 75.56           N  
ANISOU 2403  N   THR A1103    13967   7716   7028  -1488   -473    161       N  
ATOM   2404  CA  THR A1103       5.548  21.488 -11.352  1.00 83.57           C  
ANISOU 2404  CA  THR A1103    15117   8660   7976  -1468   -714    173       C  
ATOM   2405  C   THR A1103       4.693  20.330 -10.848  1.00 79.89           C  
ANISOU 2405  C   THR A1103    14419   8283   7654  -1387   -776    156       C  
ATOM   2406  O   THR A1103       5.202  19.234 -10.586  1.00 77.90           O  
ANISOU 2406  O   THR A1103    14029   8100   7469  -1409   -604    130       O  
ATOM   2407  CB  THR A1103       5.785  21.351 -12.876  1.00 88.76           C  
ANISOU 2407  CB  THR A1103    16124   9179   8422  -1605   -699    164       C  
ATOM   2408  OG1 THR A1103       6.087  19.992 -13.207  1.00100.81           O  
ANISOU 2408  OG1 THR A1103    17614  10730   9957  -1664   -556    130       O  
ATOM   2409  CG2 THR A1103       6.948  22.212 -13.320  1.00 77.65           C  
ANISOU 2409  CG2 THR A1103    14923   7695   6884  -1709   -546    167       C  
ATOM   2410  N   TYR A1104       3.390  20.580 -10.724  1.00 74.25           N  
ANISOU 2410  N   TYR A1104    13662   7559   6992  -1295  -1022    167       N  
ATOM   2411  CA  TYR A1104       2.452  19.645 -10.124  1.00 75.75           C  
ANISOU 2411  CA  TYR A1104    13614   7830   7337  -1204  -1100    149       C  
ATOM   2412  C   TYR A1104       1.420  19.220 -11.162  1.00 80.78           C  
ANISOU 2412  C   TYR A1104    14412   8378   7902  -1218  -1292    138       C  
ATOM   2413  O   TYR A1104       1.077  19.984 -12.064  1.00 78.98           O  
ANISOU 2413  O   TYR A1104    14441   8030   7539  -1254  -1450    155       O  
ATOM   2414  CB  TYR A1104       1.740  20.261  -8.883  1.00 74.86           C  
ANISOU 2414  CB  TYR A1104    13258   7793   7393  -1070  -1218    158       C  
ATOM   2415  CG  TYR A1104       2.702  20.743  -7.807  1.00 82.19           C  
ANISOU 2415  CG  TYR A1104    14027   8808   8394  -1050  -1048    170       C  
ATOM   2416  CD1 TYR A1104       3.583  21.794  -8.063  1.00 85.27           C  
ANISOU 2416  CD1 TYR A1104    14578   9146   8676  -1107   -981    191       C  
ATOM   2417  CD2 TYR A1104       2.742  20.153  -6.549  1.00 78.67           C  
ANISOU 2417  CD2 TYR A1104    13280   8491   8120   -975   -955    158       C  
ATOM   2418  CE1 TYR A1104       4.481  22.240  -7.119  1.00 81.39           C  
ANISOU 2418  CE1 TYR A1104    13946   8728   8251  -1090   -829    197       C  
ATOM   2419  CE2 TYR A1104       3.649  20.604  -5.580  1.00 87.93           C  
ANISOU 2419  CE2 TYR A1104    14318   9737   9353   -958   -807    169       C  
ATOM   2420  CZ  TYR A1104       4.518  21.657  -5.881  1.00 86.89           C  
ANISOU 2420  CZ  TYR A1104    14346   9551   9116  -1015   -747    187       C  
ATOM   2421  OH  TYR A1104       5.440  22.150  -4.974  1.00 78.45           O  
ANISOU 2421  OH  TYR A1104    13156   8547   8106  -1001   -607    194       O  
ATOM   2422  N   ASP A1105       0.939  17.986 -11.042  1.00 76.39           N  
ANISOU 2422  N   ASP A1105    13712   7877   7435  -1193  -1280    110       N  
ATOM   2423  CA  ASP A1105      -0.170  17.515 -11.855  1.00 76.48           C  
ANISOU 2423  CA  ASP A1105    13825   7818   7416  -1186  -1478     93       C  
ATOM   2424  C   ASP A1105      -1.456  17.701 -11.063  1.00 74.28           C  
ANISOU 2424  C   ASP A1105    13335   7578   7312  -1050  -1681     83       C  
ATOM   2425  O   ASP A1105      -1.474  17.520  -9.844  1.00 77.80           O  
ANISOU 2425  O   ASP A1105    13502   8137   7923   -971  -1606     76       O  
ATOM   2426  CB  ASP A1105       0.010  16.039 -12.247  1.00 84.63           C  
ANISOU 2426  CB  ASP A1105    14828   8880   8447  -1240  -1348     62       C  
ATOM   2427  CG  ASP A1105       1.276  15.779 -13.088  1.00 91.21           C  
ANISOU 2427  CG  ASP A1105    15872   9667   9116  -1385  -1135     61       C  
ATOM   2428  OD1 ASP A1105       1.698  16.670 -13.863  1.00 97.90           O  
ANISOU 2428  OD1 ASP A1105    16989  10410   9798  -1462  -1156     81       O  
ATOM   2429  OD2 ASP A1105       1.851  14.667 -12.985  1.00 81.38           O  
ANISOU 2429  OD2 ASP A1105    14526   8483   7912  -1425   -943     37       O  
ATOM   2430  N   ILE A1106      -2.531  18.069 -11.747  1.00 74.46           N  
ANISOU 2430  N   ILE A1106    13492   7500   7300  -1025  -1939     78       N  
ATOM   2431  CA  ILE A1106      -3.835  18.236 -11.112  1.00 72.96           C  
ANISOU 2431  CA  ILE A1106    13113   7326   7284   -901  -2146     57       C  
ATOM   2432  C   ILE A1106      -4.670  17.003 -11.402  1.00 69.55           C  
ANISOU 2432  C   ILE A1106    12605   6899   6921   -881  -2210     14       C  
ATOM   2433  O   ILE A1106      -4.717  16.539 -12.545  1.00 72.92           O  
ANISOU 2433  O   ILE A1106    13247   7245   7216   -956  -2253      8       O  
ATOM   2434  CB  ILE A1106      -4.552  19.500 -11.610  1.00 74.91           C  
ANISOU 2434  CB  ILE A1106    13533   7449   7478   -874  -2412     73       C  
ATOM   2435  CG1 ILE A1106      -3.736  20.755 -11.311  1.00 80.67           C  
ANISOU 2435  CG1 ILE A1106    14336   8173   8142   -892  -2348    115       C  
ATOM   2436  CG2 ILE A1106      -5.902  19.609 -10.972  1.00 72.03           C  
ANISOU 2436  CG2 ILE A1106    12960   7095   7312   -750  -2619     39       C  
ATOM   2437  CD1 ILE A1106      -4.384  22.028 -11.852  1.00 79.04           C  
ANISOU 2437  CD1 ILE A1106    14320   7836   7873   -871  -2609    135       C  
ATOM   2438  N   TYR A1107      -5.341  16.482 -10.377  1.00 70.44           N  
ANISOU 2438  N   TYR A1107    12421   7105   7240   -784  -2214    -18       N  
ATOM   2439  CA  TYR A1107      -6.091  15.240 -10.481  1.00 74.09           C  
ANISOU 2439  CA  TYR A1107    12768   7588   7792   -759  -2243    -64       C  
ATOM   2440  C   TYR A1107      -7.407  15.409  -9.751  1.00 72.41           C  
ANISOU 2440  C   TYR A1107    12341   7386   7784   -637  -2426   -104       C  
ATOM   2441  O   TYR A1107      -7.605  16.354  -8.992  1.00 67.27           O  
ANISOU 2441  O   TYR A1107    11591   6749   7218   -573  -2482    -96       O  
ATOM   2442  CB  TYR A1107      -5.333  14.041  -9.891  1.00 60.84           C  
ANISOU 2442  CB  TYR A1107    10916   6034   6167   -783  -1974    -72       C  
ATOM   2443  CG  TYR A1107      -4.008  13.685 -10.539  1.00 61.46           C  
ANISOU 2443  CG  TYR A1107    11166   6109   6077   -905  -1765    -47       C  
ATOM   2444  CD1 TYR A1107      -3.941  13.167 -11.834  1.00 72.00           C  
ANISOU 2444  CD1 TYR A1107    12737   7359   7261   -996  -1786    -55       C  
ATOM   2445  CD2 TYR A1107      -2.829  13.830  -9.847  1.00 62.17           C  
ANISOU 2445  CD2 TYR A1107    11178   6278   6167   -930  -1541    -22       C  
ATOM   2446  CE1 TYR A1107      -2.713  12.823 -12.411  1.00 67.33           C  
ANISOU 2446  CE1 TYR A1107    12297   6760   6526  -1115  -1577    -41       C  
ATOM   2447  CE2 TYR A1107      -1.608  13.494 -10.403  1.00 64.96           C  
ANISOU 2447  CE2 TYR A1107    11670   6623   6388  -1042  -1341    -10       C  
ATOM   2448  CZ  TYR A1107      -1.547  12.987 -11.682  1.00 68.38           C  
ANISOU 2448  CZ  TYR A1107    12334   6971   6677  -1136  -1352    -21       C  
ATOM   2449  OH  TYR A1107      -0.308  12.649 -12.210  1.00 67.32           O  
ANISOU 2449  OH  TYR A1107    12331   6825   6422  -1253  -1136    -16       O  
ATOM   2450  N   THR A1108      -8.312  14.468  -9.975  1.00 79.42           N  
ANISOU 2450  N   THR A1108    13152   8264   8759   -607  -2511   -152       N  
ATOM   2451  CA  THR A1108      -9.552  14.450  -9.224  1.00 82.97           C  
ANISOU 2451  CA  THR A1108    13370   8728   9428   -495  -2652   -204       C  
ATOM   2452  C   THR A1108     -10.057  13.016  -9.164  1.00 79.12           C  
ANISOU 2452  C   THR A1108    12734   8287   9040   -480  -2599   -255       C  
ATOM   2453  O   THR A1108      -9.856  12.236 -10.098  1.00 77.77           O  
ANISOU 2453  O   THR A1108    12707   8084   8757   -549  -2573   -257       O  
ATOM   2454  CB  THR A1108     -10.602  15.377  -9.843  1.00 89.11           C  
ANISOU 2454  CB  THR A1108    14273   9370  10216   -453  -2963   -221       C  
ATOM   2455  OG1 THR A1108     -11.889  15.095  -9.264  1.00 94.71           O  
ANISOU 2455  OG1 THR A1108    14752  10081  11151   -353  -3097   -289       O  
ATOM   2456  CG2 THR A1108     -10.660  15.171 -11.352  1.00 90.60           C  
ANISOU 2456  CG2 THR A1108    14762   9439  10223   -531  -3089   -214       C  
ATOM   2457  N   THR A1109     -10.671  12.677  -8.032  1.00 79.64           N  
ANISOU 2457  N   THR A1109    12513   8430   9315   -394  -2568   -296       N  
ATOM   2458  CA  THR A1109     -11.321  11.399  -7.806  1.00 71.61           C  
ANISOU 2458  CA  THR A1109    11322   7457   8431   -363  -2531   -353       C  
ATOM   2459  C   THR A1109     -12.645  11.692  -7.115  1.00 77.71           C  
ANISOU 2459  C   THR A1109    11893   8208   9425   -256  -2694   -417       C  
ATOM   2460  O   THR A1109     -12.927  12.827  -6.731  1.00 85.60           O  
ANISOU 2460  O   THR A1109    12874   9174  10474   -211  -2805   -413       O  
ATOM   2461  CB  THR A1109     -10.441  10.453  -6.970  1.00 81.85           C  
ANISOU 2461  CB  THR A1109    12457   8890   9754   -384  -2241   -338       C  
ATOM   2462  OG1 THR A1109      -9.066  10.559  -7.391  1.00 78.52           O  
ANISOU 2462  OG1 THR A1109    12205   8486   9144   -477  -2081   -276       O  
ATOM   2463  CG2 THR A1109     -10.907   8.996  -7.140  1.00 74.32           C  
ANISOU 2463  CG2 THR A1109    11404   7963   8871   -384  -2191   -386       C  
ATOM   2464  N   THR A1110     -13.469  10.662  -6.962  1.00 93.26           N  
ANISOU 2464  N   THR A1110    13706  10193  11535   -218  -2705   -482       N  
ATOM   2465  CA  THR A1110     -14.788  10.800  -6.354  1.00 93.39           C  
ANISOU 2465  CA  THR A1110    13522  10181  11780   -122  -2850   -559       C  
ATOM   2466  C   THR A1110     -15.029   9.582  -5.476  1.00101.66           C  
ANISOU 2466  C   THR A1110    14320  11328  12980    -92  -2677   -605       C  
ATOM   2467  O   THR A1110     -15.184   8.469  -5.989  1.00108.81           O  
ANISOU 2467  O   THR A1110    15232  12235  13875   -117  -2644   -631       O  
ATOM   2468  CB  THR A1110     -15.875  10.929  -7.422  1.00 86.15           C  
ANISOU 2468  CB  THR A1110    12724   9125  10886   -102  -3136   -609       C  
ATOM   2469  OG1 THR A1110     -15.734  12.194  -8.090  1.00 90.92           O  
ANISOU 2469  OG1 THR A1110    13549   9631  11367   -120  -3311   -567       O  
ATOM   2470  CG2 THR A1110     -17.278  10.797  -6.796  1.00 78.71           C  
ANISOU 2470  CG2 THR A1110    11542   8154  10211     -5  -3261   -708       C  
ATOM   2471  N   ARG A1111     -15.047   9.781  -4.163  1.00101.56           N  
ANISOU 2471  N   ARG A1111    14094  11393  13101    -43  -2563   -616       N  
ATOM   2472  CA  ARG A1111     -15.302   8.685  -3.244  1.00 95.28           C  
ANISOU 2472  CA  ARG A1111    13066  10686  12452    -15  -2399   -660       C  
ATOM   2473  C   ARG A1111     -16.801   8.548  -2.985  1.00 90.85           C  
ANISOU 2473  C   ARG A1111    12336  10065  12118     62  -2550   -763       C  
ATOM   2474  O   ARG A1111     -17.565   9.509  -3.103  1.00 85.25           O  
ANISOU 2474  O   ARG A1111    11636   9266  11488    108  -2754   -797       O  
ATOM   2475  CB  ARG A1111     -14.539   8.897  -1.939  1.00 85.99           C  
ANISOU 2475  CB  ARG A1111    11754   9620  11297     -8  -2190   -620       C  
ATOM   2476  N   TYR A1112     -17.215   7.322  -2.664  1.00 96.52           N  
ANISOU 2476  N   TYR A1112    12903  10826  12945     75  -2448   -816       N  
ATOM   2477  CA  TYR A1112     -18.603   6.979  -2.378  1.00100.65           C  
ANISOU 2477  CA  TYR A1112    13247  11299  13698    143  -2553   -924       C  
ATOM   2478  C   TYR A1112     -18.607   5.775  -1.447  1.00104.02           C  
ANISOU 2478  C   TYR A1112    13472  11823  14228    149  -2327   -955       C  
ATOM   2479  O   TYR A1112     -17.790   4.864  -1.605  1.00 92.78           O  
ANISOU 2479  O   TYR A1112    12091  10471  12691     98  -2162   -908       O  
ATOM   2480  CB  TYR A1112     -19.396   6.668  -3.655  1.00 97.27           C  
ANISOU 2480  CB  TYR A1112    12929  10758  13270    144  -2770   -974       C  
ATOM   2481  N   ASN A1113     -19.530   5.777  -0.481  1.00110.24           N  
ANISOU 2481  N   ASN A1113    14043  12608  15235    210  -2320  -1036       N  
ATOM   2482  CA  ASN A1113     -19.462   4.862   0.661  1.00100.32           C  
ANISOU 2482  CA  ASN A1113    12594  11447  14075    217  -2088  -1057       C  
ATOM   2483  C   ASN A1113     -18.105   4.975   1.354  1.00 97.37           C  
ANISOU 2483  C   ASN A1113    12252  11186  13560    176  -1878   -957       C  
ATOM   2484  O   ASN A1113     -17.477   3.970   1.693  1.00102.26           O  
ANISOU 2484  O   ASN A1113    12832  11889  14134    145  -1683   -927       O  
ATOM   2485  CB  ASN A1113     -19.728   3.411   0.245  1.00 98.11           C  
ANISOU 2485  CB  ASN A1113    12276  11180  13822    202  -2023  -1096       C  
ATOM   2486  CG  ASN A1113     -21.151   3.180  -0.213  1.00 95.69           C  
ANISOU 2486  CG  ASN A1113    11892  10770  13697    250  -2206  -1212       C  
ATOM   2487  OD1 ASN A1113     -22.073   3.856   0.227  1.00 90.71           O  
ANISOU 2487  OD1 ASN A1113    11150  10076  13240    305  -2318  -1286       O  
ATOM   2488  ND2 ASN A1113     -21.337   2.203  -1.098  1.00 99.67           N  
ANISOU 2488  ND2 ASN A1113    12448  11252  14170    230  -2235  -1234       N  
ATOM   2489  N   ALA A1114     -17.640   6.206   1.555  1.00 95.27           N  
ANISOU 2489  N   ALA A1114    12055  10915  13227    177  -1924   -906       N  
ATOM   2490  CA  ALA A1114     -16.265   6.431   1.970  1.00 94.80           C  
ANISOU 2490  CA  ALA A1114    12064  10946  13010    133  -1758   -806       C  
ATOM   2491  C   ALA A1114     -16.198   7.285   3.225  1.00100.32           C  
ANISOU 2491  C   ALA A1114    12650  11684  13784    164  -1696   -801       C  
ATOM   2492  O   ALA A1114     -17.060   8.144   3.449  1.00101.12           O  
ANISOU 2492  O   ALA A1114    12692  11720  14009    211  -1834   -856       O  
ATOM   2493  CB  ALA A1114     -15.461   7.106   0.853  1.00 93.08           C  
ANISOU 2493  CB  ALA A1114    12087  10691  12589     84  -1850   -731       C  
ATOM   2494  N   PRO A1115     -15.173   7.077   4.058  1.00 99.56           N  
ANISOU 2494  N   PRO A1115    12524  11688  13618    139  -1493   -738       N  
ATOM   2495  CA  PRO A1115     -15.057   7.848   5.302  1.00 94.99           C  
ANISOU 2495  CA  PRO A1115    11841  11149  13100    164  -1423   -732       C  
ATOM   2496  C   PRO A1115     -14.773   9.315   5.029  1.00 91.81           C  
ANISOU 2496  C   PRO A1115    11551  10705  12626    167  -1550   -693       C  
ATOM   2497  O   PRO A1115     -13.954   9.659   4.174  1.00 96.00           O  
ANISOU 2497  O   PRO A1115    12260  11227  12989    126  -1586   -626       O  
ATOM   2498  CB  PRO A1115     -13.878   7.183   6.023  1.00 87.80           C  
ANISOU 2498  CB  PRO A1115    10911  10348  12100    128  -1191   -663       C  
ATOM   2499  CG  PRO A1115     -13.737   5.838   5.374  1.00 84.08           C  
ANISOU 2499  CG  PRO A1115    10465   9891  11589     97  -1128   -664       C  
ATOM   2500  CD  PRO A1115     -14.110   6.064   3.949  1.00 90.56           C  
ANISOU 2500  CD  PRO A1115    11430  10625  12354     86  -1316   -678       C  
ATOM   2501  N   SER A1116     -15.449  10.180   5.785  1.00 90.44           N  
ANISOU 2501  N   SER A1116    11273  10506  12585    212  -1608   -738       N  
ATOM   2502  CA  SER A1116     -15.301  11.626   5.650  1.00 94.93           C  
ANISOU 2502  CA  SER A1116    11924  11032  13112    221  -1732   -710       C  
ATOM   2503  C   SER A1116     -14.996  12.288   6.993  1.00100.75           C  
ANISOU 2503  C   SER A1116    12555  11830  13896    236  -1618   -697       C  
ATOM   2504  O   SER A1116     -14.591  11.615   7.947  1.00103.22           O  
ANISOU 2504  O   SER A1116    12770  12228  14222    226  -1428   -685       O  
ATOM   2505  CB  SER A1116     -16.573  12.230   5.040  1.00 91.82           C  
ANISOU 2505  CB  SER A1116    11526  10517  12845    265  -1973   -788       C  
ATOM   2506  OG  SER A1116     -17.737  11.737   5.683  1.00 87.26           O  
ANISOU 2506  OG  SER A1116    10753   9917  12484    308  -1969   -892       O  
ATOM   2507  N   ILE A1117     -15.161  13.612   7.068  1.00100.89           N  
ANISOU 2507  N   ILE A1117    12598  11803  13934    258  -1735   -696       N  
ATOM   2508  CA  ILE A1117     -15.258  14.280   8.361  1.00 93.09           C  
ANISOU 2508  CA  ILE A1117    11480  10849  13041    281  -1659   -714       C  
ATOM   2509  C   ILE A1117     -16.703  14.396   8.817  1.00 94.46           C  
ANISOU 2509  C   ILE A1117    11488  10954  13447    330  -1743   -828       C  
ATOM   2510  O   ILE A1117     -16.950  14.641  10.008  1.00 93.78           O  
ANISOU 2510  O   ILE A1117    11264  10898  13470    345  -1646   -864       O  
ATOM   2511  CB  ILE A1117     -14.642  15.688   8.342  1.00 84.92           C  
ANISOU 2511  CB  ILE A1117    10542   9807  11918    277  -1722   -656       C  
ATOM   2512  CG1 ILE A1117     -15.428  16.593   7.392  1.00 80.23           C  
ANISOU 2512  CG1 ILE A1117    10026   9093  11365    304  -1972   -690       C  
ATOM   2513  CG2 ILE A1117     -13.181  15.619   7.975  1.00 74.92           C  
ANISOU 2513  CG2 ILE A1117     9426   8604  10435    226  -1623   -551       C  
ATOM   2514  CD1 ILE A1117     -15.029  18.057   7.465  1.00 79.75           C  
ANISOU 2514  CD1 ILE A1117    10038   9012  11251    308  -2046   -648       C  
ATOM   2515  N   ASP A1118     -17.661  14.217   7.907  1.00 90.31           N  
ANISOU 2515  N   ASP A1118    10976  10334  13005    353  -1917   -892       N  
ATOM   2516  CA  ASP A1118     -19.079  14.355   8.210  1.00 97.10           C  
ANISOU 2516  CA  ASP A1118    11679  11110  14103    400  -2018  -1013       C  
ATOM   2517  C   ASP A1118     -19.685  13.051   8.715  1.00105.34           C  
ANISOU 2517  C   ASP A1118    12574  12178  15274    404  -1891  -1086       C  
ATOM   2518  O   ASP A1118     -20.310  13.025   9.780  1.00112.50           O  
ANISOU 2518  O   ASP A1118    13313  13087  16345    422  -1804  -1160       O  
ATOM   2519  CB  ASP A1118     -19.827  14.846   6.968  1.00101.76           C  
ANISOU 2519  CB  ASP A1118    12359  11575  14732    426  -2286  -1050       C  
ATOM   2520  CG  ASP A1118     -20.030  16.352   6.972  1.00109.21           C  
ANISOU 2520  CG  ASP A1118    13331  12452  15713    452  -2441  -1052       C  
ATOM   2521  OD1 ASP A1118     -20.386  16.898   8.040  1.00110.57           O  
ANISOU 2521  OD1 ASP A1118    13358  12632  16020    473  -2383  -1098       O  
ATOM   2522  OD2 ASP A1118     -19.825  16.991   5.915  1.00111.62           O  
ANISOU 2522  OD2 ASP A1118    13808  12694  15908    447  -2617  -1007       O  
ATOM   2523  N   GLY A1119     -19.516  11.970   7.960  1.00109.69           N  
ANISOU 2523  N   GLY A1119    13188  12741  15749    384  -1875  -1069       N  
ATOM   2524  CA  GLY A1119     -19.990  10.661   8.364  1.00105.47           C  
ANISOU 2524  CA  GLY A1119    12527  12232  15314    384  -1747  -1130       C  
ATOM   2525  C   GLY A1119     -19.057   9.574   7.871  1.00104.07           C  
ANISOU 2525  C   GLY A1119    12451  12128  14964    341  -1634  -1052       C  
ATOM   2526  O   GLY A1119     -17.969   9.871   7.368  1.00107.96           O  
ANISOU 2526  O   GLY A1119    13100  12659  15261    307  -1629   -952       O  
ATOM   2527  N   ASP A1120     -19.465   8.315   7.998  1.00 96.73           N  
ANISOU 2527  N   ASP A1120    11432  11215  14108    338  -1539  -1102       N  
ATOM   2528  CA  ASP A1120     -18.616   7.193   7.617  1.00 98.36           C  
ANISOU 2528  CA  ASP A1120    11712  11491  14168    297  -1416  -1036       C  
ATOM   2529  C   ASP A1120     -18.966   6.618   6.252  1.00104.07           C  
ANISOU 2529  C   ASP A1120    12525  12154  14863    292  -1552  -1055       C  
ATOM   2530  O   ASP A1120     -18.066   6.272   5.478  1.00107.48           O  
ANISOU 2530  O   ASP A1120    13104  12618  15117    251  -1532   -977       O  
ATOM   2531  CB  ASP A1120     -18.698   6.106   8.689  1.00 97.74           C  
ANISOU 2531  CB  ASP A1120    11489  11478  14168    291  -1202  -1065       C  
ATOM   2532  CG  ASP A1120     -18.558   6.675  10.090  1.00108.78           C  
ANISOU 2532  CG  ASP A1120    12793  12920  15618    297  -1080  -1063       C  
ATOM   2533  OD1 ASP A1120     -18.175   7.860  10.211  1.00109.88           O  
ANISOU 2533  OD1 ASP A1120    12989  13057  15705    301  -1142  -1022       O  
ATOM   2534  OD2 ASP A1120     -18.831   5.951  11.069  1.00114.78           O  
ANISOU 2534  OD2 ASP A1120    13430  13714  16469    296   -922  -1103       O  
ATOM   2535  N   ASP A1121     -20.246   6.519   5.929  1.00103.07           N  
ANISOU 2535  N   ASP A1121    12316  11935  14909    331  -1690  -1162       N  
ATOM   2536  CA  ASP A1121     -20.685   6.153   4.590  1.00 99.11           C  
ANISOU 2536  CA  ASP A1121    11909  11360  14389    332  -1859  -1187       C  
ATOM   2537  C   ASP A1121     -21.252   7.414   3.950  1.00 96.65           C  
ANISOU 2537  C   ASP A1121    11668  10939  14114    363  -2114  -1213       C  
ATOM   2538  O   ASP A1121     -22.456   7.667   3.988  1.00 94.26           O  
ANISOU 2538  O   ASP A1121    11256  10546  14012    411  -2248  -1318       O  
ATOM   2539  CB  ASP A1121     -21.701   5.037   4.618  1.00 97.88           C  
ANISOU 2539  CB  ASP A1121    11614  11174  14404    354  -1840  -1292       C  
ATOM   2540  CG  ASP A1121     -21.990   4.499   3.242  1.00105.04           C  
ANISOU 2540  CG  ASP A1121    12628  12018  15266    346  -1989  -1307       C  
ATOM   2541  OD1 ASP A1121     -22.565   5.260   2.435  1.00109.59           O  
ANISOU 2541  OD1 ASP A1121    13277  12491  15870    370  -2225  -1338       O  
ATOM   2542  OD2 ASP A1121     -21.630   3.333   2.965  1.00104.43           O  
ANISOU 2542  OD2 ASP A1121    12568  11991  15121    315  -1875  -1287       O  
ATOM   2543  N   THR A1122     -20.371   8.213   3.372  1.00 93.70           N  
ANISOU 2543  N   THR A1122    11478  10570  13553    335  -2178  -1118       N  
ATOM   2544  CA  THR A1122     -20.774   9.418   2.675  1.00 96.31           C  
ANISOU 2544  CA  THR A1122    11909  10796  13887    358  -2422  -1126       C  
ATOM   2545  C   THR A1122     -20.082   9.458   1.319  1.00 96.60           C  
ANISOU 2545  C   THR A1122    12193  10807  13704    313  -2523  -1048       C  
ATOM   2546  O   THR A1122     -19.230   8.623   0.996  1.00 89.72           O  
ANISOU 2546  O   THR A1122    11404  10004  12682    262  -2388   -987       O  
ATOM   2547  CB  THR A1122     -20.449  10.686   3.487  1.00 92.74           C  
ANISOU 2547  CB  THR A1122    11435  10363  13440    371  -2407  -1094       C  
ATOM   2548  OG1 THR A1122     -19.029  10.860   3.567  1.00 85.76           O  
ANISOU 2548  OG1 THR A1122    10677   9570  12337    320  -2268   -975       O  
ATOM   2549  CG2 THR A1122     -21.039  10.607   4.898  1.00 88.16           C  
ANISOU 2549  CG2 THR A1122    10621   9814  13061    403  -2277  -1168       C  
ATOM   2550  N   THR A1123     -20.469  10.446   0.522  1.00 92.75           N  
ANISOU 2550  N   THR A1123    11825  10212  13202    329  -2763  -1053       N  
ATOM   2551  CA  THR A1123     -19.915  10.660  -0.805  1.00 91.64           C  
ANISOU 2551  CA  THR A1123    11942  10024  12854    285  -2886   -984       C  
ATOM   2552  C   THR A1123     -19.298  12.050  -0.858  1.00 93.36           C  
ANISOU 2552  C   THR A1123    12292  10223  12957    274  -2953   -913       C  
ATOM   2553  O   THR A1123     -19.811  12.987  -0.239  1.00 93.65           O  
ANISOU 2553  O   THR A1123    12232  10226  13124    321  -3030   -948       O  
ATOM   2554  CB  THR A1123     -20.995  10.504  -1.880  1.00 90.18           C  
ANISOU 2554  CB  THR A1123    11813   9709  12744    310  -3140  -1057       C  
ATOM   2555  OG1 THR A1123     -22.136  11.293  -1.519  1.00 98.59           O  
ANISOU 2555  OG1 THR A1123    12750  10683  14028    380  -3315  -1145       O  
ATOM   2556  CG2 THR A1123     -21.430   9.043  -1.990  1.00 88.91           C  
ANISOU 2556  CG2 THR A1123    11553   9572  12658    309  -3060  -1116       C  
ATOM   2557  N   PHE A1124     -18.188  12.175  -1.582  1.00 91.32           N  
ANISOU 2557  N   PHE A1124    12252   9986  12459    210  -2914   -817       N  
ATOM   2558  CA  PHE A1124     -17.435  13.423  -1.647  1.00 78.55           C  
ANISOU 2558  CA  PHE A1124    10775   8360  10710    190  -2946   -741       C  
ATOM   2559  C   PHE A1124     -16.452  13.337  -2.813  1.00 77.38           C  
ANISOU 2559  C   PHE A1124    10897   8198  10306    111  -2942   -659       C  
ATOM   2560  O   PHE A1124     -16.295  12.291  -3.445  1.00 77.04           O  
ANISOU 2560  O   PHE A1124    10915   8166  10192     72  -2892   -658       O  
ATOM   2561  CB  PHE A1124     -16.717  13.716  -0.315  1.00 77.83           C  
ANISOU 2561  CB  PHE A1124    10551   8384  10637    192  -2729   -705       C  
ATOM   2562  CG  PHE A1124     -15.851  12.583   0.191  1.00 76.49           C  
ANISOU 2562  CG  PHE A1124    10320   8339  10405    152  -2463   -670       C  
ATOM   2563  CD1 PHE A1124     -16.385  11.577   0.974  1.00 82.31           C  
ANISOU 2563  CD1 PHE A1124    10850   9128  11296    180  -2348   -731       C  
ATOM   2564  CD2 PHE A1124     -14.495  12.541  -0.106  1.00 76.76           C  
ANISOU 2564  CD2 PHE A1124    10503   8431  10231     85  -2328   -579       C  
ATOM   2565  CE1 PHE A1124     -15.582  10.544   1.437  1.00 90.36           C  
ANISOU 2565  CE1 PHE A1124    11820  10256  12258    144  -2113   -696       C  
ATOM   2566  CE2 PHE A1124     -13.692  11.508   0.348  1.00 70.57           C  
ANISOU 2566  CE2 PHE A1124     9660   7752   9401     50  -2095   -549       C  
ATOM   2567  CZ  PHE A1124     -14.229  10.515   1.119  1.00 77.56           C  
ANISOU 2567  CZ  PHE A1124    10346   8690  10435     81  -1992   -604       C  
ATOM   2568  N   THR A1125     -15.784  14.455  -3.085  1.00 79.58           N  
ANISOU 2568  N   THR A1125    11339   8451  10448     85  -2988   -592       N  
ATOM   2569  CA  THR A1125     -14.843  14.575  -4.189  1.00 78.74           C  
ANISOU 2569  CA  THR A1125    11506   8315  10095      5  -2988   -517       C  
ATOM   2570  C   THR A1125     -13.484  14.989  -3.648  1.00 73.23           C  
ANISOU 2570  C   THR A1125    10843   7710   9270    -39  -2779   -437       C  
ATOM   2571  O   THR A1125     -13.398  15.742  -2.679  1.00 74.59           O  
ANISOU 2571  O   THR A1125    10898   7924   9519     -2  -2736   -431       O  
ATOM   2572  CB  THR A1125     -15.325  15.619  -5.222  1.00 81.26           C  
ANISOU 2572  CB  THR A1125    12035   8489  10352      8  -3268   -512       C  
ATOM   2573  OG1 THR A1125     -16.725  15.434  -5.472  1.00 92.58           O  
ANISOU 2573  OG1 THR A1125    13386   9830  11958     71  -3485   -600       O  
ATOM   2574  CG2 THR A1125     -14.564  15.505  -6.539  1.00 71.52           C  
ANISOU 2574  CG2 THR A1125    11103   7205   8868    -81  -3285   -452       C  
ATOM   2575  N   GLN A1126     -12.419  14.514  -4.290  1.00 74.76           N  
ANISOU 2575  N   GLN A1126    11201   7932   9273   -121  -2650   -380       N  
ATOM   2576  CA  GLN A1126     -11.063  14.859  -3.892  1.00 75.00           C  
ANISOU 2576  CA  GLN A1126    11276   8039   9179   -170  -2451   -309       C  
ATOM   2577  C   GLN A1126     -10.371  15.672  -4.975  1.00 67.31           C  
ANISOU 2577  C   GLN A1126    10594   6986   7995   -239  -2520   -252       C  
ATOM   2578  O   GLN A1126     -10.480  15.360  -6.163  1.00 67.40           O  
ANISOU 2578  O   GLN A1126    10800   6917   7893   -288  -2614   -251       O  
ATOM   2579  CB  GLN A1126     -10.221  13.620  -3.600  1.00 68.71           C  
ANISOU 2579  CB  GLN A1126    10411   7348   8347   -215  -2201   -293       C  
ATOM   2580  CG  GLN A1126     -10.754  12.717  -2.532  1.00 68.38           C  
ANISOU 2580  CG  GLN A1126    10101   7389   8490   -159  -2103   -342       C  
ATOM   2581  CD  GLN A1126      -9.925  11.464  -2.441  1.00 71.96           C  
ANISOU 2581  CD  GLN A1126    10520   7928   8892   -209  -1880   -323       C  
ATOM   2582  OE1 GLN A1126      -9.312  11.042  -3.425  1.00 73.53           O  
ANISOU 2582  OE1 GLN A1126    10892   8102   8943   -282  -1844   -297       O  
ATOM   2583  NE2 GLN A1126      -9.878  10.871  -1.254  1.00 73.05           N  
ANISOU 2583  NE2 GLN A1126    10440   8164   9152   -175  -1727   -338       N  
ATOM   2584  N   TYR A1127      -9.641  16.701  -4.559  1.00 64.73           N  
ANISOU 2584  N   TYR A1127    10304   6679   7612   -248  -2465   -205       N  
ATOM   2585  CA  TYR A1127      -8.846  17.518  -5.464  1.00 71.05           C  
ANISOU 2585  CA  TYR A1127    11376   7411   8210   -319  -2494   -148       C  
ATOM   2586  C   TYR A1127      -7.377  17.334  -5.110  1.00 68.08           C  
ANISOU 2586  C   TYR A1127    11010   7125   7730   -382  -2228    -98       C  
ATOM   2587  O   TYR A1127      -6.958  17.645  -3.993  1.00 73.11           O  
ANISOU 2587  O   TYR A1127    11485   7849   8443   -349  -2106    -86       O  
ATOM   2588  CB  TYR A1127      -9.229  18.998  -5.386  1.00 75.26           C  
ANISOU 2588  CB  TYR A1127    11964   7872   8760   -278  -2671   -137       C  
ATOM   2589  CG  TYR A1127     -10.686  19.318  -5.668  1.00 86.04           C  
ANISOU 2589  CG  TYR A1127    13305   9137  10251   -208  -2949   -191       C  
ATOM   2590  CD1 TYR A1127     -11.530  18.388  -6.263  1.00 83.00           C  
ANISOU 2590  CD1 TYR A1127    12917   8706   9914   -199  -3054   -241       C  
ATOM   2591  CD2 TYR A1127     -11.214  20.569  -5.355  1.00 91.60           C  
ANISOU 2591  CD2 TYR A1127    13989   9785  11032   -153  -3110   -197       C  
ATOM   2592  CE1 TYR A1127     -12.862  18.677  -6.511  1.00 84.11           C  
ANISOU 2592  CE1 TYR A1127    13026   8747  10186   -133  -3314   -298       C  
ATOM   2593  CE2 TYR A1127     -12.547  20.869  -5.603  1.00 90.89           C  
ANISOU 2593  CE2 TYR A1127    13866   9594  11074    -88  -3370   -253       C  
ATOM   2594  CZ  TYR A1127     -13.362  19.918  -6.186  1.00 92.17           C  
ANISOU 2594  CZ  TYR A1127    14022   9710  11290    -78  -3473   -305       C  
ATOM   2595  OH  TYR A1127     -14.682  20.203  -6.441  1.00 99.91           O  
ANISOU 2595  OH  TYR A1127    14964  10583  12416    -12  -3737   -368       O  
ATOM   2596  N   TRP A1128      -6.601  16.832  -6.053  1.00 67.41           N  
ANISOU 2596  N   TRP A1128    11117   7017   7480   -473  -2141    -74       N  
ATOM   2597  CA  TRP A1128      -5.192  16.571  -5.840  1.00 61.46           C  
ANISOU 2597  CA  TRP A1128    10381   6335   6635   -541  -1890    -36       C  
ATOM   2598  C   TRP A1128      -4.395  17.531  -6.708  1.00 66.34           C  
ANISOU 2598  C   TRP A1128    11274   6872   7061   -619  -1901      7       C  
ATOM   2599  O   TRP A1128      -4.814  17.856  -7.818  1.00 66.32           O  
ANISOU 2599  O   TRP A1128    11494   6754   6950   -653  -2067      9       O  
ATOM   2600  CB  TRP A1128      -4.823  15.101  -6.191  1.00 59.72           C  
ANISOU 2600  CB  TRP A1128    10146   6156   6388   -595  -1741    -52       C  
ATOM   2601  CG  TRP A1128      -5.660  14.011  -5.499  1.00 61.15           C  
ANISOU 2601  CG  TRP A1128    10082   6405   6747   -527  -1732    -98       C  
ATOM   2602  CD1 TRP A1128      -6.987  13.725  -5.710  1.00 62.13           C  
ANISOU 2602  CD1 TRP A1128    10155   6483   6970   -471  -1918   -146       C  
ATOM   2603  CD2 TRP A1128      -5.207  13.069  -4.505  1.00 57.67           C  
ANISOU 2603  CD2 TRP A1128     9424   6084   6405   -511  -1527   -105       C  
ATOM   2604  NE1 TRP A1128      -7.385  12.685  -4.896  1.00 64.66           N  
ANISOU 2604  NE1 TRP A1128    10238   6888   7443   -423  -1830   -183       N  
ATOM   2605  CE2 TRP A1128      -6.310  12.260  -4.157  1.00 63.95           C  
ANISOU 2605  CE2 TRP A1128    10049   6900   7349   -448  -1593   -155       C  
ATOM   2606  CE3 TRP A1128      -3.975  12.833  -3.876  1.00 55.84           C  
ANISOU 2606  CE3 TRP A1128     9126   5937   6154   -544  -1299    -74       C  
ATOM   2607  CZ2 TRP A1128      -6.215  11.241  -3.200  1.00 58.91           C  
ANISOU 2607  CZ2 TRP A1128     9189   6363   6829   -420  -1434   -172       C  
ATOM   2608  CZ3 TRP A1128      -3.889  11.815  -2.926  1.00 51.05           C  
ANISOU 2608  CZ3 TRP A1128     8298   5431   5669   -513  -1155    -90       C  
ATOM   2609  CH2 TRP A1128      -4.992  11.043  -2.598  1.00 53.09           C  
ANISOU 2609  CH2 TRP A1128     8403   5708   6062   -453  -1220   -135       C  
ATOM   2610  N   SER A1129      -3.272  18.019  -6.182  1.00 64.21           N  
ANISOU 2610  N   SER A1129    10990   6655   6752   -647  -1731     41       N  
ATOM   2611  CA  SER A1129      -2.130  18.435  -6.984  1.00 61.59           C  
ANISOU 2611  CA  SER A1129    10898   6271   6233   -750  -1630     75       C  
ATOM   2612  C   SER A1129      -0.944  17.632  -6.483  1.00 72.85           C  
ANISOU 2612  C   SER A1129    12217   7795   7669   -794  -1356     78       C  
ATOM   2613  O   SER A1129      -0.701  17.577  -5.275  1.00 68.42           O  
ANISOU 2613  O   SER A1129    11429   7334   7232   -738  -1255     79       O  
ATOM   2614  CB  SER A1129      -1.824  19.937  -6.882  1.00 64.30           C  
ANISOU 2614  CB  SER A1129    11341   6571   6520   -745  -1688    108       C  
ATOM   2615  OG  SER A1129      -3.002  20.728  -6.968  1.00 71.93           O  
ANISOU 2615  OG  SER A1129    12326   7467   7536   -676  -1944    101       O  
ATOM   2616  N   VAL A1130      -0.220  16.992  -7.396  1.00 80.19           N  
ANISOU 2616  N   VAL A1130    13308   8688   8471   -895  -1239     78       N  
ATOM   2617  CA  VAL A1130       0.870  16.100  -7.023  1.00 72.46           C  
ANISOU 2617  CA  VAL A1130    12229   7789   7513   -941   -987     72       C  
ATOM   2618  C   VAL A1130       2.101  16.497  -7.826  1.00 65.95           C  
ANISOU 2618  C   VAL A1130    11633   6902   6524  -1057   -851     87       C  
ATOM   2619  O   VAL A1130       2.060  16.519  -9.060  1.00 72.19           O  
ANISOU 2619  O   VAL A1130    12676   7589   7165  -1137   -904     85       O  
ATOM   2620  CB  VAL A1130       0.513  14.621  -7.266  1.00 60.95           C  
ANISOU 2620  CB  VAL A1130    10697   6361   6101   -951   -945     41       C  
ATOM   2621  CG1 VAL A1130       1.660  13.721  -6.840  1.00 58.34           C  
ANISOU 2621  CG1 VAL A1130    10254   6108   5804   -996   -689     36       C  
ATOM   2622  CG2 VAL A1130      -0.754  14.259  -6.566  1.00 55.15           C  
ANISOU 2622  CG2 VAL A1130     9756   5673   5525   -843  -1082     20       C  
ATOM   2623  N   ARG A1131       3.189  16.800  -7.131  1.00 64.91           N  
ANISOU 2623  N   ARG A1131    11418   6827   6420  -1069   -676     98       N  
ATOM   2624  CA  ARG A1131       4.440  17.133  -7.791  1.00 72.81           C  
ANISOU 2624  CA  ARG A1131    12606   7769   7287  -1181   -518    102       C  
ATOM   2625  C   ARG A1131       4.879  16.008  -8.727  1.00 82.16           C  
ANISOU 2625  C   ARG A1131    13903   8918   8396  -1282   -395     75       C  
ATOM   2626  O   ARG A1131       4.531  14.840  -8.539  1.00 89.66           O  
ANISOU 2626  O   ARG A1131    14714   9923   9430  -1259   -368     55       O  
ATOM   2627  CB  ARG A1131       5.516  17.408  -6.745  1.00 65.76           C  
ANISOU 2627  CB  ARG A1131    11550   6957   6479  -1166   -340    107       C  
ATOM   2628  CG  ARG A1131       6.813  17.864  -7.321  1.00 78.56           C  
ANISOU 2628  CG  ARG A1131    13345   8518   7986  -1274   -175    103       C  
ATOM   2629  CD  ARG A1131       7.811  18.145  -6.254  1.00 79.91           C  
ANISOU 2629  CD  ARG A1131    13342   8766   8256  -1250    -19    104       C  
ATOM   2630  NE  ARG A1131       8.001  19.574  -6.109  1.00 82.91           N  
ANISOU 2630  NE  ARG A1131    13805   9111   8588  -1238    -72    127       N  
ATOM   2631  CZ  ARG A1131       9.178  20.161  -6.203  1.00 86.52           C  
ANISOU 2631  CZ  ARG A1131    14340   9537   8997  -1304     78    120       C  
ATOM   2632  NH1 ARG A1131      10.261  19.425  -6.453  1.00 80.94           N  
ANISOU 2632  NH1 ARG A1131    13637   8826   8291  -1388    290     87       N  
ATOM   2633  NH2 ARG A1131       9.265  21.476  -6.044  1.00 91.79           N  
ANISOU 2633  NH2 ARG A1131    15077  10174   9624  -1286     19    142       N  
ATOM   2634  N   GLN A1132       5.659  16.369  -9.750  1.00 81.77           N  
ANISOU 2634  N   GLN A1132    14111   8772   8186  -1399   -313     72       N  
ATOM   2635  CA  GLN A1132       6.014  15.404 -10.786  1.00 81.76           C  
ANISOU 2635  CA  GLN A1132    14255   8716   8092  -1509   -208     43       C  
ATOM   2636  C   GLN A1132       7.216  14.561 -10.392  1.00 81.45           C  
ANISOU 2636  C   GLN A1132    14081   8739   8129  -1558     58     14       C  
ATOM   2637  O   GLN A1132       7.293  13.383 -10.758  1.00 84.80           O  
ANISOU 2637  O   GLN A1132    14482   9172   8566  -1602    144    -14       O  
ATOM   2638  CB  GLN A1132       6.267  16.127 -12.102  1.00 82.11           C  
ANISOU 2638  CB  GLN A1132    14655   8619   7926  -1621   -236     47       C  
ATOM   2639  CG  GLN A1132       4.995  16.722 -12.694  1.00 85.36           C  
ANISOU 2639  CG  GLN A1132    15227   8952   8256  -1583   -518     71       C  
ATOM   2640  CD  GLN A1132       5.204  17.231 -14.102  1.00 93.54           C  
ANISOU 2640  CD  GLN A1132    16637   9836   9066  -1706   -549     74       C  
ATOM   2641  OE1 GLN A1132       6.269  17.025 -14.697  1.00 98.21           O  
ANISOU 2641  OE1 GLN A1132    17372  10381   9561  -1828   -345     53       O  
ATOM   2642  NE2 GLN A1132       4.187  17.892 -14.652  1.00 83.91           N  
ANISOU 2642  NE2 GLN A1132    15585   8533   7764  -1677   -804     97       N  
ATOM   2643  N   SER A1133       8.162  15.135  -9.664  1.00 78.93           N  
ANISOU 2643  N   SER A1133    13669   8456   7863  -1551    186     18       N  
ATOM   2644  CA  SER A1133       9.202  14.347  -9.027  1.00 83.67           C  
ANISOU 2644  CA  SER A1133    14082   9128   8579  -1568    410     -8       C  
ATOM   2645  C   SER A1133       9.093  14.546  -7.521  1.00 78.56           C  
ANISOU 2645  C   SER A1133    13150   8598   8100  -1444    386     12       C  
ATOM   2646  O   SER A1133       8.295  15.347  -7.039  1.00 77.27           O  
ANISOU 2646  O   SER A1133    12950   8455   7956  -1357    217     43       O  
ATOM   2647  CB  SER A1133      10.590  14.731  -9.551  1.00 87.04           C  
ANISOU 2647  CB  SER A1133    14658   9485   8929  -1688    613    -35       C  
ATOM   2648  OG  SER A1133      11.448  13.601  -9.537  1.00 94.42           O  
ANISOU 2648  OG  SER A1133    15495  10444   9938  -1746    820    -77       O  
ATOM   2649  N   LYS A1134       9.869  13.788  -6.758  1.00 69.05           N  
ANISOU 2649  N   LYS A1134    11744   7468   7023  -1434    551     -7       N  
ATOM   2650  CA  LYS A1134       9.834  13.946  -5.313  1.00 62.78           C  
ANISOU 2650  CA  LYS A1134    10692   6780   6380  -1323    537     13       C  
ATOM   2651  C   LYS A1134      10.611  15.200  -4.935  1.00 80.73           C  
ANISOU 2651  C   LYS A1134    12995   9039   8637  -1326    580     24       C  
ATOM   2652  O   LYS A1134      11.810  15.302  -5.222  1.00 93.19           O  
ANISOU 2652  O   LYS A1134    14637  10578  10193  -1409    751     -2       O  
ATOM   2653  CB  LYS A1134      10.418  12.720  -4.622  1.00 60.14           C  
ANISOU 2653  CB  LYS A1134    10143   6523   6185  -1312    688     -9       C  
ATOM   2654  CG  LYS A1134       9.580  11.476  -4.750  1.00 56.21           C  
ANISOU 2654  CG  LYS A1134     9570   6057   5729  -1289    641    -17       C  
ATOM   2655  CD  LYS A1134      10.121  10.390  -3.850  1.00 56.67           C  
ANISOU 2655  CD  LYS A1134     9394   6199   5939  -1260    774    -30       C  
ATOM   2656  CE  LYS A1134       9.558   9.029  -4.235  1.00 54.52           C  
ANISOU 2656  CE  LYS A1134     9084   5940   5693  -1270    777    -48       C  
ATOM   2657  NZ  LYS A1134       9.785   8.013  -3.184  1.00 61.57           N  
ANISOU 2657  NZ  LYS A1134     9729   6922   6743  -1215    859    -52       N  
ATOM   2658  N   ARG A1135       9.931  16.157  -4.313  1.00 75.25           N  
ANISOU 2658  N   ARG A1135    12257   8374   7962  -1239    428     57       N  
ATOM   2659  CA  ARG A1135      10.609  17.353  -3.838  1.00 71.33           C  
ANISOU 2659  CA  ARG A1135    11766   7874   7463  -1230    461     69       C  
ATOM   2660  C   ARG A1135      11.641  16.987  -2.775  1.00 74.42           C  
ANISOU 2660  C   ARG A1135    11944   8342   7990  -1208    624     54       C  
ATOM   2661  O   ARG A1135      11.329  16.208  -1.863  1.00 75.11           O  
ANISOU 2661  O   ARG A1135    11818   8518   8201  -1136    617     59       O  
ATOM   2662  CB  ARG A1135       9.596  18.326  -3.261  1.00 68.67           C  
ANISOU 2662  CB  ARG A1135    11387   7561   7142  -1132    265    104       C  
ATOM   2663  CG  ARG A1135      10.208  19.541  -2.630  1.00 77.66           C  
ANISOU 2663  CG  ARG A1135    12504   8710   8294  -1110    290    118       C  
ATOM   2664  CD  ARG A1135       9.131  20.587  -2.363  1.00 77.08           C  
ANISOU 2664  CD  ARG A1135    12444   8633   8210  -1031     83    150       C  
ATOM   2665  NE  ARG A1135       9.702  21.922  -2.255  1.00 75.76           N  
ANISOU 2665  NE  ARG A1135    12355   8433   7996  -1042     95    162       N  
ATOM   2666  CZ  ARG A1135       8.988  23.035  -2.149  1.00 76.68           C  
ANISOU 2666  CZ  ARG A1135    12520   8528   8088   -991    -66    188       C  
ATOM   2667  NH1 ARG A1135       7.661  22.977  -2.126  1.00 70.55           N  
ANISOU 2667  NH1 ARG A1135    11714   7755   7336   -925   -256    200       N  
ATOM   2668  NH2 ARG A1135       9.607  24.208  -2.068  1.00 79.06           N  
ANISOU 2668  NH2 ARG A1135    12893   8798   8348  -1007    -36    197       N  
ATOM   2669  N   PRO A1136      12.871  17.511  -2.853  1.00 84.43           N  
ANISOU 2669  N   PRO A1136    13264   9574   9243  -1270    770     34       N  
ATOM   2670  CA  PRO A1136      13.861  17.231  -1.805  1.00 73.06           C  
ANISOU 2670  CA  PRO A1136    11618   8200   7943  -1244    908     19       C  
ATOM   2671  C   PRO A1136      13.392  17.715  -0.445  1.00 66.26           C  
ANISOU 2671  C   PRO A1136    10564   7433   7181  -1123    806     53       C  
ATOM   2672  O   PRO A1136      12.554  18.613  -0.321  1.00 67.22           O  
ANISOU 2672  O   PRO A1136    10727   7555   7259  -1070    654     84       O  
ATOM   2673  CB  PRO A1136      15.106  18.004  -2.266  1.00 71.36           C  
ANISOU 2673  CB  PRO A1136    11531   7909   7676  -1332   1050    -11       C  
ATOM   2674  CG  PRO A1136      14.970  18.091  -3.706  1.00 64.23           C  
ANISOU 2674  CG  PRO A1136    10892   6897   6614  -1434   1053    -25       C  
ATOM   2675  CD  PRO A1136      13.478  18.257  -3.969  1.00 77.73           C  
ANISOU 2675  CD  PRO A1136    12671   8612   8252  -1378    832     18       C  
ATOM   2676  N   THR A1137      13.953  17.090   0.587  1.00 60.56           N  
ANISOU 2676  N   THR A1137     9630   6785   6596  -1082    892     45       N  
ATOM   2677  CA  THR A1137      13.584  17.354   1.966  1.00 59.54           C  
ANISOU 2677  CA  THR A1137     9305   6748   6568   -973    817     73       C  
ATOM   2678  C   THR A1137      14.847  17.541   2.792  1.00 75.10           C  
ANISOU 2678  C   THR A1137    11157   8745   8633   -970    945     57       C  
ATOM   2679  O   THR A1137      15.949  17.149   2.385  1.00 77.51           O  
ANISOU 2679  O   THR A1137    11488   9008   8956  -1044   1097     18       O  
ATOM   2680  CB  THR A1137      12.738  16.220   2.544  1.00 63.86           C  
ANISOU 2680  CB  THR A1137     9699   7368   7198   -909    761     85       C  
ATOM   2681  OG1 THR A1137      13.404  14.968   2.323  1.00 69.10           O  
ANISOU 2681  OG1 THR A1137    10314   8030   7913   -958    895     56       O  
ATOM   2682  CG2 THR A1137      11.341  16.201   1.889  1.00 63.26           C  
ANISOU 2682  CG2 THR A1137     9719   7270   7048   -892    604     99       C  
ATOM   2683  N   GLY A1138      14.670  18.138   3.966  1.00 73.05           N  
ANISOU 2683  N   GLY A1138    10765   8552   8439   -884    881     82       N  
ATOM   2684  CA  GLY A1138      15.786  18.525   4.803  1.00 75.99           C  
ANISOU 2684  CA  GLY A1138    11033   8947   8894   -872    973     70       C  
ATOM   2685  C   GLY A1138      16.138  19.998   4.757  1.00 77.52           C  
ANISOU 2685  C   GLY A1138    11316   9106   9033   -880    959     73       C  
ATOM   2686  O   GLY A1138      17.203  20.379   5.258  1.00 66.32           O  
ANISOU 2686  O   GLY A1138     9835   7688   7674   -886   1051     53       O  
ATOM   2687  N   SER A1139      15.290  20.831   4.159  1.00 70.96           N  
ANISOU 2687  N   SER A1139    10628   8240   8094   -880    843     95       N  
ATOM   2688  CA  SER A1139      15.493  22.272   4.150  1.00 72.21           C  
ANISOU 2688  CA  SER A1139    10871   8367   8198   -880    812    103       C  
ATOM   2689  C   SER A1139      14.138  22.949   4.014  1.00 71.66           C  
ANISOU 2689  C   SER A1139    10868   8297   8061   -831    628    140       C  
ATOM   2690  O   SER A1139      13.164  22.340   3.566  1.00 80.07           O  
ANISOU 2690  O   SER A1139    11967   9358   9096   -824    540    150       O  
ATOM   2691  CB  SER A1139      16.444  22.712   3.024  1.00 87.74           C  
ANISOU 2691  CB  SER A1139    13030  10230  10076   -988    931     69       C  
ATOM   2692  OG  SER A1139      17.646  21.948   3.012  1.00 97.63           O  
ANISOU 2692  OG  SER A1139    14223  11469  11401  -1043   1106     24       O  
ATOM   2693  N   ASN A1140      14.091  24.219   4.420  1.00 73.79           N  
ANISOU 2693  N   ASN A1140    11149   8568   8318   -797    569    156       N  
ATOM   2694  CA  ASN A1140      12.851  24.979   4.396  1.00 66.43           C  
ANISOU 2694  CA  ASN A1140    10264   7633   7344   -745    390    186       C  
ATOM   2695  C   ASN A1140      12.233  24.951   3.009  1.00 70.37           C  
ANISOU 2695  C   ASN A1140    10978   8043   7717   -802    316    189       C  
ATOM   2696  O   ASN A1140      12.923  24.844   1.991  1.00 84.66           O  
ANISOU 2696  O   ASN A1140    12951   9776   9440   -894    411    169       O  
ATOM   2697  CB  ASN A1140      13.095  26.430   4.813  1.00 78.96           C  
ANISOU 2697  CB  ASN A1140    11868   9214   8920   -721    360    198       C  
ATOM   2698  CG  ASN A1140      13.835  26.545   6.137  1.00 87.28           C  
ANISOU 2698  CG  ASN A1140    12728  10347  10087   -673    439    192       C  
ATOM   2699  OD1 ASN A1140      15.048  26.322   6.207  1.00 93.34           O  
ANISOU 2699  OD1 ASN A1140    13472  11108  10886   -715    586    166       O  
ATOM   2700  ND2 ASN A1140      13.109  26.912   7.190  1.00 71.64           N  
ANISOU 2700  ND2 ASN A1140    10611   8435   8174   -588    340    214       N  
ATOM   2701  N   ALA A1141      10.915  25.077   2.978  1.00 70.09           N  
ANISOU 2701  N   ALA A1141    10946   8011   7674   -749    144    209       N  
ATOM   2702  CA  ALA A1141      10.169  24.864   1.753  1.00 72.33           C  
ANISOU 2702  CA  ALA A1141    11412   8216   7855   -790     48    212       C  
ATOM   2703  C   ALA A1141       8.814  25.526   1.910  1.00 67.74           C  
ANISOU 2703  C   ALA A1141    10826   7630   7283   -718   -160    232       C  
ATOM   2704  O   ALA A1141       8.283  25.624   3.016  1.00 75.49           O  
ANISOU 2704  O   ALA A1141    11621   8687   8374   -634   -216    238       O  
ATOM   2705  CB  ALA A1141      10.021  23.366   1.446  1.00 69.85           C  
ANISOU 2705  CB  ALA A1141    11057   7919   7564   -813     98    195       C  
ATOM   2706  N   THR A1142       8.261  25.972   0.793  1.00 67.21           N  
ANISOU 2706  N   THR A1142    10968   7467   7103   -754   -276    240       N  
ATOM   2707  CA  THR A1142       7.013  26.712   0.780  1.00 78.05           C  
ANISOU 2707  CA  THR A1142    12364   8812   8482   -693   -487    256       C  
ATOM   2708  C   THR A1142       5.974  25.932  -0.005  1.00 72.11           C  
ANISOU 2708  C   THR A1142    11680   8016   7703   -696   -611    248       C  
ATOM   2709  O   THR A1142       6.304  25.076  -0.826  1.00 79.42           O  
ANISOU 2709  O   THR A1142    12708   8908   8559   -765   -539    237       O  
ATOM   2710  CB  THR A1142       7.198  28.117   0.153  1.00 92.89           C  
ANISOU 2710  CB  THR A1142    14444  10599  10250   -726   -551    273       C  
ATOM   2711  OG1 THR A1142       8.486  28.650   0.501  1.00100.51           O  
ANISOU 2711  OG1 THR A1142    15403  11581  11204   -761   -386    272       O  
ATOM   2712  CG2 THR A1142       6.124  29.083   0.615  1.00 78.59           C  
ANISOU 2712  CG2 THR A1142    12580   8784   8495   -643   -744    287       C  
ATOM   2713  N   ILE A1143       4.710  26.237   0.280  1.00 67.44           N  
ANISOU 2713  N   ILE A1143    11022   7424   7177   -620   -797    250       N  
ATOM   2714  CA  ILE A1143       3.574  25.869  -0.551  1.00 66.73           C  
ANISOU 2714  CA  ILE A1143    11026   7268   7060   -614   -966    242       C  
ATOM   2715  C   ILE A1143       2.690  27.104  -0.591  1.00 70.65           C  
ANISOU 2715  C   ILE A1143    11574   7705   7564   -564  -1170    253       C  
ATOM   2716  O   ILE A1143       2.027  27.424   0.398  1.00 70.82           O  
ANISOU 2716  O   ILE A1143    11411   7780   7718   -480  -1239    245       O  
ATOM   2717  CB  ILE A1143       2.785  24.661  -0.018  1.00 69.69           C  
ANISOU 2717  CB  ILE A1143    11208   7712   7559   -560   -984    218       C  
ATOM   2718  CG1 ILE A1143       3.570  23.369  -0.248  1.00 72.82           C  
ANISOU 2718  CG1 ILE A1143    11593   8144   7932   -620   -807    208       C  
ATOM   2719  CG2 ILE A1143       1.418  24.563  -0.699  1.00 60.80           C  
ANISOU 2719  CG2 ILE A1143    10150   6515   6438   -532  -1200    204       C  
ATOM   2720  CD1 ILE A1143       2.906  22.131   0.328  1.00 75.28           C  
ANISOU 2720  CD1 ILE A1143    11711   8527   8364   -570   -801    185       C  
ATOM   2721  N   THR A1144       2.700  27.804  -1.722  1.00 77.95           N  
ANISOU 2721  N   THR A1144    12755   8515   8348   -618  -1260    269       N  
ATOM   2722  CA  THR A1144       1.896  29.007  -1.916  1.00 77.87           C  
ANISOU 2722  CA  THR A1144    12826   8428   8332   -578  -1467    281       C  
ATOM   2723  C   THR A1144       0.501  28.556  -2.316  1.00 72.98           C  
ANISOU 2723  C   THR A1144    12201   7762   7765   -534  -1674    261       C  
ATOM   2724  O   THR A1144       0.192  28.363  -3.489  1.00 73.14           O  
ANISOU 2724  O   THR A1144    12429   7684   7675   -582  -1774    264       O  
ATOM   2725  CB  THR A1144       2.534  29.911  -2.965  1.00 80.72           C  
ANISOU 2725  CB  THR A1144    13477   8679   8515   -659  -1474    307       C  
ATOM   2726  OG1 THR A1144       3.954  29.981  -2.739  1.00 77.17           O  
ANISOU 2726  OG1 THR A1144    13036   8271   8015   -719  -1242    314       O  
ATOM   2727  CG2 THR A1144       1.931  31.298  -2.905  1.00 72.09           C  
ANISOU 2727  CG2 THR A1144    12435   7523   7431   -612  -1655    324       C  
ATOM   2728  N   PHE A1145      -0.364  28.395  -1.323  1.00 71.46           N  
ANISOU 2728  N   PHE A1145    11769   7635   7746   -443  -1739    237       N  
ATOM   2729  CA  PHE A1145      -1.630  27.721  -1.571  1.00 76.23           C  
ANISOU 2729  CA  PHE A1145    12322   8211   8430   -399  -1899    205       C  
ATOM   2730  C   PHE A1145      -2.579  28.502  -2.468  1.00 80.08           C  
ANISOU 2730  C   PHE A1145    12983   8567   8879   -387  -2157    205       C  
ATOM   2731  O   PHE A1145      -3.481  27.894  -3.050  1.00 93.22           O  
ANISOU 2731  O   PHE A1145    14677  10178  10565   -375  -2294    181       O  
ATOM   2732  CB  PHE A1145      -2.339  27.393  -0.256  1.00 79.04           C  
ANISOU 2732  CB  PHE A1145    12380   8663   8990   -309  -1897    171       C  
ATOM   2733  CG  PHE A1145      -3.525  26.475  -0.420  1.00 78.58           C  
ANISOU 2733  CG  PHE A1145    12238   8589   9029   -270  -2016    129       C  
ATOM   2734  CD1 PHE A1145      -3.392  25.252  -1.068  1.00 77.44           C  
ANISOU 2734  CD1 PHE A1145    12150   8446   8827   -316  -1955    121       C  
ATOM   2735  CD2 PHE A1145      -4.775  26.836   0.074  1.00 78.23           C  
ANISOU 2735  CD2 PHE A1145    12056   8525   9143   -188  -2184     91       C  
ATOM   2736  CE1 PHE A1145      -4.490  24.406  -1.223  1.00 78.34           C  
ANISOU 2736  CE1 PHE A1145    12186   8544   9035   -279  -2063     79       C  
ATOM   2737  CE2 PHE A1145      -5.878  25.995  -0.069  1.00 76.13           C  
ANISOU 2737  CE2 PHE A1145    11706   8239   8980   -151  -2290     43       C  
ATOM   2738  CZ  PHE A1145      -5.734  24.780  -0.722  1.00 80.66           C  
ANISOU 2738  CZ  PHE A1145    12339   8816   9490   -195  -2231     38       C  
ATOM   2739  N   THR A1146      -2.441  29.820  -2.598  1.00 76.23           N  
ANISOU 2739  N   THR A1146    12606   8017   8340   -387  -2236    231       N  
ATOM   2740  CA  THR A1146      -3.420  30.484  -3.457  1.00 86.80           C  
ANISOU 2740  CA  THR A1146    14106   9221   9652   -371  -2501    229       C  
ATOM   2741  C   THR A1146      -3.104  30.262  -4.931  1.00 89.53           C  
ANISOU 2741  C   THR A1146    14765   9458   9794   -463  -2539    252       C  
ATOM   2742  O   THR A1146      -3.977  30.466  -5.780  1.00 91.27           O  
ANISOU 2742  O   THR A1146    15132   9562   9983   -456  -2765    248       O  
ATOM   2743  CB  THR A1146      -3.542  31.976  -3.138  1.00 89.82           C  
ANISOU 2743  CB  THR A1146    14507   9562  10060   -334  -2604    246       C  
ATOM   2744  OG1 THR A1146      -4.849  32.446  -3.520  1.00 85.98           O  
ANISOU 2744  OG1 THR A1146    14051   8971   9648   -278  -2884    225       O  
ATOM   2745  CG2 THR A1146      -2.482  32.789  -3.894  1.00 77.80           C  
ANISOU 2745  CG2 THR A1146    13251   7973   8337   -418  -2542    295       C  
ATOM   2746  N   ASN A1147      -1.880  29.831  -5.239  1.00 90.10           N  
ANISOU 2746  N   ASN A1147    14939   9561   9733   -550  -2322    273       N  
ATOM   2747  CA  ASN A1147      -1.573  29.294  -6.559  1.00 84.53           C  
ANISOU 2747  CA  ASN A1147    14499   8770   8848   -645  -2316    283       C  
ATOM   2748  C   ASN A1147      -2.444  28.078  -6.866  1.00 92.70           C  
ANISOU 2748  C   ASN A1147    15474   9806   9942   -626  -2398    249       C  
ATOM   2749  O   ASN A1147      -3.251  28.095  -7.805  1.00 98.63           O  
ANISOU 2749  O   ASN A1147    16392  10444  10639   -632  -2606    245       O  
ATOM   2750  CB  ASN A1147      -0.080  28.945  -6.645  1.00 82.42           C  
ANISOU 2750  CB  ASN A1147    14297   8550   8468   -739  -2037    298       C  
ATOM   2751  CG  ASN A1147       0.802  30.180  -6.705  1.00 90.74           C  
ANISOU 2751  CG  ASN A1147    15489   9565   9422   -780  -1972    330       C  
ATOM   2752  OD1 ASN A1147       0.353  31.246  -7.128  1.00 91.19           O  
ANISOU 2752  OD1 ASN A1147    15696   9524   9427   -770  -2149    350       O  
ATOM   2753  ND2 ASN A1147       2.066  30.042  -6.301  1.00 86.88           N  
ANISOU 2753  ND2 ASN A1147    14953   9148   8910   -829  -1720    332       N  
ATOM   2754  N   HIS A1148      -2.326  27.025  -6.049  1.00 94.88           N  
ANISOU 2754  N   HIS A1148    15508  10205  10337   -598  -2247    224       N  
ATOM   2755  CA  HIS A1148      -3.028  25.773  -6.335  1.00 89.26           C  
ANISOU 2755  CA  HIS A1148    14737   9502   9677   -587  -2291    190       C  
ATOM   2756  C   HIS A1148      -4.543  25.972  -6.360  1.00 86.93           C  
ANISOU 2756  C   HIS A1148    14379   9146   9505   -502  -2562    158       C  
ATOM   2757  O   HIS A1148      -5.231  25.399  -7.213  1.00 88.41           O  
ANISOU 2757  O   HIS A1148    14671   9261   9662   -514  -2698    140       O  
ATOM   2758  CB  HIS A1148      -2.632  24.680  -5.318  1.00 71.36           C  
ANISOU 2758  CB  HIS A1148    12206   7381   7529   -566  -2077    169       C  
ATOM   2759  CG  HIS A1148      -1.171  24.312  -5.339  1.00 67.99           C  
ANISOU 2759  CG  HIS A1148    11827   7006   7000   -650  -1816    190       C  
ATOM   2760  ND1 HIS A1148      -0.667  23.294  -6.121  1.00 67.78           N  
ANISOU 2760  ND1 HIS A1148    11912   6967   6874   -731  -1705    184       N  
ATOM   2761  CD2 HIS A1148      -0.106  24.826  -4.671  1.00 69.95           C  
ANISOU 2761  CD2 HIS A1148    12020   7315   7241   -664  -1645    210       C  
ATOM   2762  CE1 HIS A1148       0.642  23.200  -5.943  1.00 67.56           C  
ANISOU 2762  CE1 HIS A1148    11896   6986   6790   -794  -1476    197       C  
ATOM   2763  NE2 HIS A1148       1.008  24.119  -5.067  1.00 69.76           N  
ANISOU 2763  NE2 HIS A1148    12074   7309   7123   -753  -1438    213       N  
ATOM   2764  N   VAL A1149      -5.086  26.794  -5.454  1.00 84.87           N  
ANISOU 2764  N   VAL A1149    13951   8908   9389   -417  -2648    148       N  
ATOM   2765  CA  VAL A1149      -6.544  26.891  -5.361  1.00 90.60           C  
ANISOU 2765  CA  VAL A1149    14574   9580  10268   -332  -2890    105       C  
ATOM   2766  C   VAL A1149      -7.115  27.602  -6.585  1.00 95.90           C  
ANISOU 2766  C   VAL A1149    15515  10088  10835   -351  -3146    117       C  
ATOM   2767  O   VAL A1149      -8.194  27.245  -7.079  1.00 90.71           O  
ANISOU 2767  O   VAL A1149    14870   9357  10240   -317  -3346     81       O  
ATOM   2768  CB  VAL A1149      -6.976  27.586  -4.057  1.00 89.59           C  
ANISOU 2768  CB  VAL A1149    14194   9514  10331   -242  -2905     84       C  
ATOM   2769  CG1 VAL A1149      -6.378  28.963  -3.969  1.00 96.39           C  
ANISOU 2769  CG1 VAL A1149    15159  10346  11119   -255  -2908    126       C  
ATOM   2770  CG2 VAL A1149      -8.495  27.666  -3.982  1.00 87.36           C  
ANISOU 2770  CG2 VAL A1149    13800   9167  10226   -158  -3149     28       C  
ATOM   2771  N   ASN A1150      -6.400  28.611  -7.096  1.00 98.75           N  
ANISOU 2771  N   ASN A1150    16100  10383  11036   -406  -3147    167       N  
ATOM   2772  CA  ASN A1150      -6.868  29.330  -8.277  1.00 95.35           C  
ANISOU 2772  CA  ASN A1150    15954   9789  10486   -431  -3390    185       C  
ATOM   2773  C   ASN A1150      -6.876  28.418  -9.495  1.00 97.77           C  
ANISOU 2773  C   ASN A1150    16476  10025  10645   -505  -3421    185       C  
ATOM   2774  O   ASN A1150      -7.882  28.329 -10.216  1.00100.69           O  
ANISOU 2774  O   ASN A1150    16943  10287  11027   -483  -3665    164       O  
ATOM   2775  CB  ASN A1150      -5.986  30.558  -8.532  1.00 96.76           C  
ANISOU 2775  CB  ASN A1150    16333   9919  10514   -483  -3350    239       C  
ATOM   2776  CG  ASN A1150      -6.316  31.725  -7.614  1.00 90.17           C  
ANISOU 2776  CG  ASN A1150    15344   9099   9818   -402  -3427    238       C  
ATOM   2777  OD1 ASN A1150      -7.433  31.849  -7.116  1.00 91.29           O  
ANISOU 2777  OD1 ASN A1150    15306   9232  10149   -311  -3595    197       O  
ATOM   2778  ND2 ASN A1150      -5.336  32.589  -7.392  1.00 83.56           N  
ANISOU 2778  ND2 ASN A1150    14577   8280   8892   -439  -3297    278       N  
ATOM   2779  N   ALA A1151      -5.760  27.721  -9.730  1.00 96.75           N  
ANISOU 2779  N   ALA A1151    16422   9954  10383   -594  -3176    204       N  
ATOM   2780  CA  ALA A1151      -5.676  26.795 -10.854  1.00 90.04           C  
ANISOU 2780  CA  ALA A1151    15774   9046   9391   -675  -3173    201       C  
ATOM   2781  C   ALA A1151      -6.755  25.720 -10.802  1.00 81.20           C  
ANISOU 2781  C   ALA A1151    14496   7945   8414   -616  -3281    149       C  
ATOM   2782  O   ALA A1151      -7.185  25.238 -11.848  1.00 84.66           O  
ANISOU 2782  O   ALA A1151    15117   8289   8760   -655  -3408    140       O  
ATOM   2783  CB  ALA A1151      -4.294  26.150 -10.900  1.00 87.56           C  
ANISOU 2783  CB  ALA A1151    15502   8809   8957   -772  -2863    219       C  
ATOM   2784  N   TRP A1152      -7.211  25.322  -9.617  1.00 84.94           N  
ANISOU 2784  N   TRP A1152    14637   8530   9106   -527  -3232    111       N  
ATOM   2785  CA  TRP A1152      -8.267  24.314  -9.572  1.00 94.25           C  
ANISOU 2785  CA  TRP A1152    15665   9720  10427   -472  -3333     55       C  
ATOM   2786  C   TRP A1152      -9.601  24.897 -10.030  1.00 93.18           C  
ANISOU 2786  C   TRP A1152    15583   9453  10368   -408  -3667     27       C  
ATOM   2787  O   TRP A1152     -10.319  24.273 -10.820  1.00 96.36           O  
ANISOU 2787  O   TRP A1152    16071   9780  10761   -412  -3818     -2       O  
ATOM   2788  CB  TRP A1152      -8.416  23.718  -8.168  1.00 95.70           C  
ANISOU 2788  CB  TRP A1152    15486  10051  10823   -398  -3184     19       C  
ATOM   2789  CG  TRP A1152      -7.250  22.921  -7.642  1.00 89.28           C  
ANISOU 2789  CG  TRP A1152    14582   9370   9972   -448  -2873     36       C  
ATOM   2790  CD1 TRP A1152      -6.143  22.498  -8.330  1.00 88.14           C  
ANISOU 2790  CD1 TRP A1152    14622   9228   9641   -553  -2704     69       C  
ATOM   2791  CD2 TRP A1152      -7.084  22.467  -6.297  1.00 82.58           C  
ANISOU 2791  CD2 TRP A1152    13433   8663   9282   -396  -2698     17       C  
ATOM   2792  NE1 TRP A1152      -5.294  21.804  -7.487  1.00 72.73           N  
ANISOU 2792  NE1 TRP A1152    12490   7409   7733   -564  -2441     71       N  
ATOM   2793  CE2 TRP A1152      -5.849  21.779  -6.232  1.00 80.64           C  
ANISOU 2793  CE2 TRP A1152    13201   8498   8940   -469  -2437     43       C  
ATOM   2794  CE3 TRP A1152      -7.855  22.584  -5.137  1.00 80.11           C  
ANISOU 2794  CE3 TRP A1152    12846   8409   9184   -299  -2735    -21       C  
ATOM   2795  CZ2 TRP A1152      -5.369  21.214  -5.047  1.00 81.50           C  
ANISOU 2795  CZ2 TRP A1152    13064   8744   9158   -442  -2229     36       C  
ATOM   2796  CZ3 TRP A1152      -7.384  22.022  -3.967  1.00 83.87           C  
ANISOU 2796  CZ3 TRP A1152    13088   9022   9757   -278  -2519    -27       C  
ATOM   2797  CH2 TRP A1152      -6.148  21.344  -3.929  1.00 79.40           C  
ANISOU 2797  CH2 TRP A1152    12547   8533   9087   -348  -2276      4       C  
ATOM   2798  N   LYS A1153      -9.969  26.079  -9.516  1.00 87.86           N  
ANISOU 2798  N   LYS A1153    14849   8749   9786   -345  -3790     30       N  
ATOM   2799  CA  LYS A1153     -11.219  26.704  -9.948  1.00 89.54           C  
ANISOU 2799  CA  LYS A1153    15111   8825  10084   -282  -4118      0       C  
ATOM   2800  C   LYS A1153     -11.195  27.005 -11.440  1.00 94.86           C  
ANISOU 2800  C   LYS A1153    16160   9341  10540   -355  -4295     35       C  
ATOM   2801  O   LYS A1153     -12.254  27.078 -12.079  1.00 86.90           O  
ANISOU 2801  O   LYS A1153    15230   8210   9580   -319  -4573      4       O  
ATOM   2802  CB  LYS A1153     -11.490  27.979  -9.152  1.00 87.87           C  
ANISOU 2802  CB  LYS A1153    14783   8607   9998   -212  -4201      1       C  
ATOM   2803  N   SER A1154      -9.998  27.177 -12.008  1.00 93.81           N  
ANISOU 2803  N   SER A1154    16268   9204  10172   -460  -4137     96       N  
ATOM   2804  CA  SER A1154      -9.858  27.255 -13.456  1.00 86.77           C  
ANISOU 2804  CA  SER A1154    15751   8169   9048   -549  -4258    127       C  
ATOM   2805  C   SER A1154     -10.410  26.001 -14.127  1.00 95.14           C  
ANISOU 2805  C   SER A1154    16842   9205  10103   -566  -4318     89       C  
ATOM   2806  O   SER A1154     -11.378  26.062 -14.893  1.00106.93           O  
ANISOU 2806  O   SER A1154    18461  10568  11600   -544  -4598     68       O  
ATOM   2807  CB  SER A1154      -8.390  27.468 -13.820  1.00 86.12           C  
ANISOU 2807  CB  SER A1154    15882   8107   8734   -666  -4016    186       C  
ATOM   2808  OG  SER A1154      -8.109  26.955 -15.109  1.00104.48           O  
ANISOU 2808  OG  SER A1154    18516  10340  10843   -772  -4028    202       O  
ATOM   2809  N   HIS A1155      -9.930  24.852 -13.703  1.00 95.40           N  
ANISOU 2809  N   HIS A1155    16712   9367  10167   -588  -4074     71       N  
ATOM   2810  CA  HIS A1155     -10.300  23.600 -14.318  1.00 90.94           C  
ANISOU 2810  CA  HIS A1155    16175   8794   9586   -615  -4089     37       C  
ATOM   2811  C   HIS A1155     -11.623  23.073 -13.828  1.00 93.66           C  
ANISOU 2811  C   HIS A1155    16258   9150  10178   -505  -4252    -34       C  
ATOM   2812  O   HIS A1155     -11.967  21.935 -14.065  1.00 93.79           O  
ANISOU 2812  O   HIS A1155    16217   9189  10230   -510  -4233    -72       O  
ATOM   2813  CB  HIS A1155      -9.205  22.568 -14.153  1.00 83.16           C  
ANISOU 2813  CB  HIS A1155    15143   7930   8525   -692  -3761     46       C  
ATOM   2814  CG  HIS A1155      -7.974  22.863 -14.945  1.00 87.07           C  
ANISOU 2814  CG  HIS A1155    15940   8382   8759   -820  -3613    101       C  
ATOM   2815  ND1 HIS A1155      -6.899  23.536 -14.422  1.00 88.36           N  
ANISOU 2815  ND1 HIS A1155    16097   8605   8871   -852  -3416    140       N  
ATOM   2816  CD2 HIS A1155      -7.639  22.557 -16.215  1.00 90.03           C  
ANISOU 2816  CD2 HIS A1155    16633   8659   8916   -930  -3624    117       C  
ATOM   2817  CE1 HIS A1155      -5.956  23.641 -15.335  1.00 86.61           C  
ANISOU 2817  CE1 HIS A1155    16172   8321   8417   -975  -3308    175       C  
ATOM   2818  NE2 HIS A1155      -6.380  23.055 -16.434  1.00 88.47           N  
ANISOU 2818  NE2 HIS A1155    16613   8459   8543  -1027  -3428    163       N  
ATOM   2819  N   GLY A1156     -12.398  23.938 -13.207  1.00100.31           N  
ANISOU 2819  N   GLY A1156    16955   9965  11192   -408  -4422    -56       N  
ATOM   2820  CA  GLY A1156     -13.701  23.559 -12.710  1.00 98.52           C  
ANISOU 2820  CA  GLY A1156    16475   9736  11221   -302  -4583   -133       C  
ATOM   2821  C   GLY A1156     -13.703  22.984 -11.320  1.00100.06           C  
ANISOU 2821  C   GLY A1156    16301  10094  11624   -241  -4374   -172       C  
ATOM   2822  O   GLY A1156     -14.733  22.560 -10.823  1.00 94.85           O  
ANISOU 2822  O   GLY A1156    15412   9444  11185   -159  -4466   -243       O  
ATOM   2823  N   MET A1157     -12.546  22.975 -10.682  1.00 99.07           N  
ANISOU 2823  N   MET A1157    16121  10090  11429   -283  -4092   -128       N  
ATOM   2824  CA  MET A1157     -12.469  22.447  -9.340  1.00 97.65           C  
ANISOU 2824  CA  MET A1157    15610  10063  11430   -231  -3889   -158       C  
ATOM   2825  C   MET A1157     -12.551  23.601  -8.384  1.00100.37           C  
ANISOU 2825  C   MET A1157    15818  10430  11890   -169  -3910   -154       C  
ATOM   2826  O   MET A1157     -11.619  24.369  -8.269  1.00109.49           O  
ANISOU 2826  O   MET A1157    17070  11604  12925   -209  -3806    -96       O  
ATOM   2827  CB  MET A1157     -11.147  21.728  -9.144  1.00 95.82           C  
ANISOU 2827  CB  MET A1157    15386   9952  11070   -309  -3572   -117       C  
ATOM   2828  CG  MET A1157     -11.045  20.425  -9.899  1.00 99.48           C  
ANISOU 2828  CG  MET A1157    15930  10418  11450   -368  -3508   -130       C  
ATOM   2829  SD  MET A1157      -9.376  19.777  -9.940  1.00105.87           S  
ANISOU 2829  SD  MET A1157    16817  11331  12077   -478  -3162    -77       S  
ATOM   2830  CE  MET A1157      -8.674  20.680 -11.295  1.00 96.01           C  
ANISOU 2830  CE  MET A1157    15983   9948  10549   -584  -3236    -16       C  
ATOM   2831  N   ASN A1158     -13.668  23.706  -7.685  1.00 95.75           N  
ANISOU 2831  N   ASN A1158    14999   9838  11545    -73  -4036   -220       N  
ATOM   2832  CA  ASN A1158     -13.865  24.785  -6.741  1.00 94.95           C  
ANISOU 2832  CA  ASN A1158    14749   9752  11576    -11  -4064   -227       C  
ATOM   2833  C   ASN A1158     -14.276  24.288  -5.373  1.00 92.62           C  
ANISOU 2833  C   ASN A1158    14106   9572  11512     56  -3931   -286       C  
ATOM   2834  O   ASN A1158     -15.170  23.481  -5.247  1.00 93.71           O  
ANISOU 2834  O   ASN A1158    14096   9707  11804     99  -3985   -355       O  
ATOM   2835  CB  ASN A1158     -14.898  25.770  -7.276  1.00 91.67           C  
ANISOU 2835  CB  ASN A1158    14420   9178  11232     40  -4393   -253       C  
ATOM   2836  N   LEU A1159     -13.611  24.803  -4.354  1.00 87.20           N  
ANISOU 2836  N   LEU A1159    13301   8984  10848     63  -3757   -259       N  
ATOM   2837  CA  LEU A1159     -13.838  24.438  -2.968  1.00 87.59           C  
ANISOU 2837  CA  LEU A1159    13041   9146  11091    116  -3605   -304       C  
ATOM   2838  C   LEU A1159     -15.059  25.035  -2.306  1.00 90.50           C  
ANISOU 2838  C   LEU A1159    13213   9466  11707    204  -3766   -380       C  
ATOM   2839  O   LEU A1159     -15.571  26.053  -2.724  1.00105.27           O  
ANISOU 2839  O   LEU A1159    15172  11223  13603    230  -3985   -386       O  
ATOM   2840  CB  LEU A1159     -12.611  24.752  -2.147  1.00 83.55           C  
ANISOU 2840  CB  LEU A1159    12492   8755  10499     84  -3358   -246       C  
ATOM   2841  CG  LEU A1159     -11.368  24.081  -2.688  1.00 81.01           C  
ANISOU 2841  CG  LEU A1159    12331   8488   9962     -3  -3172   -183       C  
ATOM   2842  CD1 LEU A1159     -10.920  24.729  -3.970  1.00 89.93           C  
ANISOU 2842  CD1 LEU A1159    13777   9510  10882    -65  -3288   -129       C  
ATOM   2843  CD2 LEU A1159     -10.268  24.186  -1.676  1.00 75.94           C  
ANISOU 2843  CD2 LEU A1159    11587   7974   9292    -21  -2919   -144       C  
ATOM   2844  N   SER A1161     -17.740  26.473   0.753  1.00101.69           N  
ANISOU 2844  N   SER A1161    13901  10868  13869    419  -3901   -606       N  
ATOM   2845  CA  SER A1161     -17.872  27.638   1.607  1.00101.01           C  
ANISOU 2845  CA  SER A1161    13704  10781  13896    454  -3912   -620       C  
ATOM   2846  C   SER A1161     -17.461  27.509   3.069  1.00 98.14           C  
ANISOU 2846  C   SER A1161    13128  10556  13607    457  -3654   -628       C  
ATOM   2847  O   SER A1161     -16.830  28.393   3.610  1.00101.65           O  
ANISOU 2847  O   SER A1161    13577  11042  14002    450  -3579   -584       O  
ATOM   2848  CB  SER A1161     -19.316  28.092   1.557  1.00 98.68           C  
ANISOU 2848  CB  SER A1161    13293  10353  13846    523  -4158   -721       C  
ATOM   2849  OG  SER A1161     -20.163  26.977   1.663  1.00 92.52           O  
ANISOU 2849  OG  SER A1161    12363   9569  13221    547  -4155   -807       O  
ATOM   2850  N   ASN A1162     -17.821  26.412   3.712  1.00 94.99           N  
ANISOU 2850  N   ASN A1162    12548  10222  13321    467  -3519   -684       N  
ATOM   2851  CA  ASN A1162     -17.511  26.260   5.122  1.00 87.12           C  
ANISOU 2851  CA  ASN A1162    11357   9346  12399    469  -3284   -697       C  
ATOM   2852  C   ASN A1162     -16.200  25.552   5.308  1.00 87.62           C  
ANISOU 2852  C   ASN A1162    11488   9539  12264    413  -3045   -612       C  
ATOM   2853  O   ASN A1162     -16.142  24.345   5.292  1.00 94.63           O  
ANISOU 2853  O   ASN A1162    12339  10477  13136    396  -2939   -621       O  
ATOM   2854  CB  ASN A1162     -18.614  25.455   5.786  1.00 75.62           C  
ANISOU 2854  CB  ASN A1162     9669   7886  11179    507  -3256   -808       C  
ATOM   2855  CG  ASN A1162     -18.457  25.386   7.269  1.00 81.89           C  
ANISOU 2855  CG  ASN A1162    10265   8784  12067    509  -3035   -832       C  
ATOM   2856  OD1 ASN A1162     -17.507  25.905   7.811  1.00 90.83           O  
ANISOU 2856  OD1 ASN A1162    11428   9995  13087    485  -2906   -764       O  
ATOM   2857  ND2 ASN A1162     -19.392  24.753   7.933  1.00 79.83           N  
ANISOU 2857  ND2 ASN A1162     9804   8517  12012    536  -2991   -932       N  
ATOM   2858  N   TRP A1163     -15.152  26.313   5.546  1.00 84.54           N  
ANISOU 2858  N   TRP A1163    11182   9202  11736    385  -2957   -535       N  
ATOM   2859  CA  TRP A1163     -13.831  25.746   5.692  1.00 89.83           C  
ANISOU 2859  CA  TRP A1163    11923   9986  12222    331  -2739   -455       C  
ATOM   2860  C   TRP A1163     -13.557  24.939   6.931  1.00 92.11           C  
ANISOU 2860  C   TRP A1163    12028  10397  12572    329  -2505   -470       C  
ATOM   2861  O   TRP A1163     -14.042  25.235   8.002  1.00 92.88           O  
ANISOU 2861  O   TRP A1163    11948  10518  12823    361  -2460   -520       O  
ATOM   2862  CB  TRP A1163     -12.794  26.836   5.600  1.00 87.71           C  
ANISOU 2862  CB  TRP A1163    11793   9731  11801    303  -2715   -375       C  
ATOM   2863  CG  TRP A1163     -12.734  27.424   4.284  1.00 91.05           C  
ANISOU 2863  CG  TRP A1163    12447  10049  12100    284  -2898   -339       C  
ATOM   2864  CD1 TRP A1163     -13.619  28.269   3.748  1.00 97.91           C  
ANISOU 2864  CD1 TRP A1163    13362  10794  13046    319  -3138   -372       C  
ATOM   2865  CD2 TRP A1163     -11.724  27.222   3.310  1.00 98.62           C  
ANISOU 2865  CD2 TRP A1163    13634  11006  12831    220  -2859   -263       C  
ATOM   2866  NE1 TRP A1163     -13.236  28.623   2.492  1.00106.34           N  
ANISOU 2866  NE1 TRP A1163    14686  11781  13939    282  -3260   -317       N  
ATOM   2867  CE2 TRP A1163     -12.067  27.985   2.199  1.00104.36           C  
ANISOU 2867  CE2 TRP A1163    14552  11605  13496    218  -3084   -251       C  
ATOM   2868  CE3 TRP A1163     -10.560  26.469   3.271  1.00 95.78           C  
ANISOU 2868  CE3 TRP A1163    13337  10737  12320    163  -2656   -208       C  
ATOM   2869  CZ2 TRP A1163     -11.295  28.022   1.064  1.00100.43           C  
ANISOU 2869  CZ2 TRP A1163    14314  11065  12781    155  -3102   -186       C  
ATOM   2870  CZ3 TRP A1163      -9.802  26.503   2.150  1.00 98.58           C  
ANISOU 2870  CZ3 TRP A1163    13933  11050  12474    102  -2670   -149       C  
ATOM   2871  CH2 TRP A1163     -10.166  27.274   1.057  1.00 99.02           C  
ANISOU 2871  CH2 TRP A1163    14186  10977  12461     96  -2886   -138       C  
ATOM   2872  N   ALA A1164     -12.739  23.915   6.752  1.00 89.27           N  
ANISOU 2872  N   ALA A1164    11722  10110  12084    286  -2355   -424       N  
ATOM   2873  CA  ALA A1164     -12.311  23.047   7.843  1.00 81.84           C  
ANISOU 2873  CA  ALA A1164    10639   9287  11171    277  -2128   -424       C  
ATOM   2874  C   ALA A1164     -10.774  23.062   7.922  1.00 79.06           C  
ANISOU 2874  C   ALA A1164    10390   9020  10628    227  -1964   -332       C  
ATOM   2875  O   ALA A1164     -10.113  23.852   7.237  1.00 88.14           O  
ANISOU 2875  O   ALA A1164    11706  10138  11644    201  -2019   -277       O  
ATOM   2876  CB  ALA A1164     -12.898  21.646   7.655  1.00 76.49           C  
ANISOU 2876  CB  ALA A1164     9893   8613  10558    279  -2100   -472       C  
ATOM   2877  N   TYR A1165     -10.208  22.198   8.779  1.00 73.37           N  
ANISOU 2877  N   TYR A1165     9572   8402   9904    212  -1762   -319       N  
ATOM   2878  CA  TYR A1165      -8.781  22.290   9.105  1.00 70.97           C  
ANISOU 2878  CA  TYR A1165     9327   8180   9458    173  -1601   -244       C  
ATOM   2879  C   TYR A1165      -7.928  22.067   7.865  1.00 71.19           C  
ANISOU 2879  C   TYR A1165     9557   8184   9306    121  -1608   -186       C  
ATOM   2880  O   TYR A1165      -8.343  21.421   6.903  1.00 75.66           O  
ANISOU 2880  O   TYR A1165    10199   8699   9850    108  -1687   -202       O  
ATOM   2881  CB  TYR A1165      -8.364  21.282  10.204  1.00 61.33           C  
ANISOU 2881  CB  TYR A1165     7970   7064   8270    167  -1397   -242       C  
ATOM   2882  CG  TYR A1165      -8.556  19.802   9.863  1.00 69.90           C  
ANISOU 2882  CG  TYR A1165     9034   8164   9361    153  -1342   -260       C  
ATOM   2883  CD1 TYR A1165      -7.627  19.106   9.086  1.00 67.90           C  
ANISOU 2883  CD1 TYR A1165     8904   7930   8966    105  -1274   -209       C  
ATOM   2884  CD2 TYR A1165      -9.674  19.103  10.326  1.00 65.62           C  
ANISOU 2884  CD2 TYR A1165     8346   7613   8974    186  -1350   -332       C  
ATOM   2885  CE1 TYR A1165      -7.821  17.771   8.769  1.00 68.95           C  
ANISOU 2885  CE1 TYR A1165     9015   8075   9109     92  -1225   -226       C  
ATOM   2886  CE2 TYR A1165      -9.874  17.779  10.013  1.00 63.91           C  
ANISOU 2886  CE2 TYR A1165     8108   7409   8767    174  -1301   -350       C  
ATOM   2887  CZ  TYR A1165      -8.951  17.111   9.234  1.00 74.40           C  
ANISOU 2887  CZ  TYR A1165     9560   8758   9950    128  -1241   -295       C  
ATOM   2888  OH  TYR A1165      -9.170  15.783   8.929  1.00 69.42           O  
ANISOU 2888  OH  TYR A1165     8903   8138   9335    117  -1191   -315       O  
ATOM   2889  N   GLN A1166      -6.731  22.633   7.888  1.00 60.69           N  
ANISOU 2889  N   GLN A1166     8320   6889   7852     87  -1524   -124       N  
ATOM   2890  CA  GLN A1166      -5.716  22.334   6.898  1.00 67.53           C  
ANISOU 2890  CA  GLN A1166     9364   7746   8548     26  -1475    -72       C  
ATOM   2891  C   GLN A1166      -4.402  22.127   7.636  1.00 70.44           C  
ANISOU 2891  C   GLN A1166     9698   8210   8857     -2  -1271    -27       C  
ATOM   2892  O   GLN A1166      -4.013  22.952   8.464  1.00 80.78           O  
ANISOU 2892  O   GLN A1166    10952   9556  10183     13  -1228    -13       O  
ATOM   2893  CB  GLN A1166      -5.605  23.439   5.838  1.00 73.24           C  
ANISOU 2893  CB  GLN A1166    10285   8377   9165      5  -1617    -46       C  
ATOM   2894  CG  GLN A1166      -5.241  24.820   6.346  1.00 73.75           C  
ANISOU 2894  CG  GLN A1166    10355   8442   9223     19  -1631    -23       C  
ATOM   2895  CD  GLN A1166      -5.119  25.827   5.214  1.00 82.37           C  
ANISOU 2895  CD  GLN A1166    11662   9434  10200     -8  -1770      5       C  
ATOM   2896  OE1 GLN A1166      -5.521  26.989   5.338  1.00 76.20           O  
ANISOU 2896  OE1 GLN A1166    10888   8606   9457     22  -1886      0       O  
ATOM   2897  NE2 GLN A1166      -4.571  25.376   4.097  1.00 84.65           N  
ANISOU 2897  NE2 GLN A1166    12134   9686  10346    -68  -1757     33       N  
ATOM   2898  N   VAL A1167      -3.740  21.004   7.368  1.00 64.80           N  
ANISOU 2898  N   VAL A1167     9008   7534   8081    -42  -1150    -10       N  
ATOM   2899  CA  VAL A1167      -2.529  20.635   8.076  1.00 62.69           C  
ANISOU 2899  CA  VAL A1167     8693   7351   7776    -66   -962     25       C  
ATOM   2900  C   VAL A1167      -1.488  20.200   7.057  1.00 52.56           C  
ANISOU 2900  C   VAL A1167     7567   6049   6352   -136   -889     59       C  
ATOM   2901  O   VAL A1167      -1.807  19.812   5.933  1.00 56.36           O  
ANISOU 2901  O   VAL A1167     8167   6470   6778   -164   -961     51       O  
ATOM   2902  CB  VAL A1167      -2.784  19.519   9.119  1.00 62.16           C  
ANISOU 2902  CB  VAL A1167     8444   7359   7815    -40   -855      2       C  
ATOM   2903  CG1 VAL A1167      -4.002  19.848   9.978  1.00 58.77           C  
ANISOU 2903  CG1 VAL A1167     7869   6929   7531     20   -931    -47       C  
ATOM   2904  CG2 VAL A1167      -2.961  18.192   8.433  1.00 53.66           C  
ANISOU 2904  CG2 VAL A1167     7389   6274   6725    -65   -830    -11       C  
ATOM   2905  N   MET A1168      -0.227  20.305   7.452  1.00 49.92           N  
ANISOU 2905  N   MET A1168     7238   5764   5965   -165   -748     93       N  
ATOM   2906  CA  MET A1168       0.897  19.783   6.676  1.00 52.62           C  
ANISOU 2906  CA  MET A1168     7699   6098   6197   -234   -640    118       C  
ATOM   2907  C   MET A1168       1.199  18.401   7.241  1.00 53.40           C  
ANISOU 2907  C   MET A1168     7674   6266   6351   -236   -506    112       C  
ATOM   2908  O   MET A1168       1.778  18.272   8.325  1.00 54.08           O  
ANISOU 2908  O   MET A1168     7641   6422   6487   -218   -399    123       O  
ATOM   2909  CB  MET A1168       2.096  20.721   6.762  1.00 53.34           C  
ANISOU 2909  CB  MET A1168     7862   6192   6214   -265   -566    150       C  
ATOM   2910  CG  MET A1168       3.211  20.408   5.807  1.00 59.76           C  
ANISOU 2910  CG  MET A1168     8823   6972   6912   -345   -466    165       C  
ATOM   2911  SD  MET A1168       2.758  20.458   4.047  1.00 65.11           S  
ANISOU 2911  SD  MET A1168     9739   7535   7465   -402   -582    160       S  
ATOM   2912  CE  MET A1168       4.056  19.389   3.428  1.00 63.92           C  
ANISOU 2912  CE  MET A1168     9658   7387   7240   -490   -392    163       C  
ATOM   2913  N   ALA A1169       0.784  17.364   6.519  1.00 51.72           N  
ANISOU 2913  N   ALA A1169     7491   6030   6129   -256   -517     94       N  
ATOM   2914  CA  ALA A1169       0.559  16.064   7.131  1.00 58.41           C  
ANISOU 2914  CA  ALA A1169     8196   6935   7062   -238   -437     78       C  
ATOM   2915  C   ALA A1169       1.479  14.969   6.602  1.00 51.94           C  
ANISOU 2915  C   ALA A1169     7420   6126   6189   -297   -306     88       C  
ATOM   2916  O   ALA A1169       2.010  15.026   5.489  1.00 52.28           O  
ANISOU 2916  O   ALA A1169     7620   6115   6128   -359   -298     96       O  
ATOM   2917  CB  ALA A1169      -0.897  15.626   6.931  1.00 67.68           C  
ANISOU 2917  CB  ALA A1169     9323   8082   8311   -200   -558     36       C  
ATOM   2918  N   THR A1170       1.645  13.961   7.435  1.00 48.52           N  
ANISOU 2918  N   THR A1170     6847   5758   5832   -280   -203     85       N  
ATOM   2919  CA  THR A1170       2.102  12.654   7.001  1.00 56.33           C  
ANISOU 2919  CA  THR A1170     7839   6756   6809   -322   -102     81       C  
ATOM   2920  C   THR A1170       0.882  11.747   6.940  1.00 51.10           C  
ANISOU 2920  C   THR A1170     7106   6094   6217   -292   -161     48       C  
ATOM   2921  O   THR A1170       0.183  11.590   7.948  1.00 46.77           O  
ANISOU 2921  O   THR A1170     6418   5586   5768   -236   -174     33       O  
ATOM   2922  CB  THR A1170       3.152  12.098   7.957  1.00 52.34           C  
ANISOU 2922  CB  THR A1170     7227   6316   6345   -324     50    101       C  
ATOM   2923  OG1 THR A1170       4.283  12.980   7.980  1.00 49.59           O  
ANISOU 2923  OG1 THR A1170     6940   5961   5939   -352    101    125       O  
ATOM   2924  CG2 THR A1170       3.593  10.722   7.520  1.00 48.41           C  
ANISOU 2924  CG2 THR A1170     6722   5823   5847   -366    152     94       C  
ATOM   2925  N   GLU A1171       0.586  11.212   5.751  1.00 48.30           N  
ANISOU 2925  N   GLU A1171     6854   5687   5810   -331   -200     31       N  
ATOM   2926  CA  GLU A1171      -0.440  10.188   5.588  1.00 51.27           C  
ANISOU 2926  CA  GLU A1171     7167   6061   6251   -310   -238     -4       C  
ATOM   2927  C   GLU A1171       0.235   8.864   5.277  1.00 56.24           C  
ANISOU 2927  C   GLU A1171     7789   6712   6868   -357   -105     -2       C  
ATOM   2928  O   GLU A1171       1.320   8.835   4.685  1.00 61.16           O  
ANISOU 2928  O   GLU A1171     8512   7319   7408   -419    -22     18       O  
ATOM   2929  CB  GLU A1171      -1.438  10.527   4.475  1.00 49.51           C  
ANISOU 2929  CB  GLU A1171     7061   5759   5992   -313   -403    -31       C  
ATOM   2930  CG  GLU A1171      -2.546   9.501   4.331  1.00 62.14           C  
ANISOU 2930  CG  GLU A1171     8584   7353   7672   -288   -450    -75       C  
ATOM   2931  CD  GLU A1171      -3.784   9.997   3.574  1.00 81.23           C  
ANISOU 2931  CD  GLU A1171    11071   9693  10100   -264   -646   -111       C  
ATOM   2932  OE1 GLU A1171      -4.632  10.720   4.164  1.00 85.74           O  
ANISOU 2932  OE1 GLU A1171    11566  10255  10756   -205   -748   -133       O  
ATOM   2933  OE2 GLU A1171      -3.921   9.634   2.386  1.00 89.21           O  
ANISOU 2933  OE2 GLU A1171    12211  10646  11038   -306   -700   -121       O  
ATOM   2934  N   GLY A1172      -0.401   7.767   5.696  1.00 50.31           N  
ANISOU 2934  N   GLY A1172     6916   5993   6206   -329    -78    -26       N  
ATOM   2935  CA  GLY A1172       0.094   6.450   5.337  1.00 47.98           C  
ANISOU 2935  CA  GLY A1172     6610   5712   5907   -371     36    -28       C  
ATOM   2936  C   GLY A1172      -1.009   5.423   5.175  1.00 51.16           C  
ANISOU 2936  C   GLY A1172     6946   6112   6379   -348     -1    -68       C  
ATOM   2937  O   GLY A1172      -2.168   5.636   5.552  1.00 54.60           O  
ANISOU 2937  O   GLY A1172     7313   6544   6890   -293   -100    -98       O  
ATOM   2938  N   TYR A1173      -0.621   4.290   4.593  1.00 49.78           N  
ANISOU 2938  N   TYR A1173     6790   5938   6187   -394     84    -74       N  
ATOM   2939  CA  TYR A1173      -1.525   3.163   4.380  1.00 48.02           C  
ANISOU 2939  CA  TYR A1173     6504   5714   6028   -380     72   -112       C  
ATOM   2940  C   TYR A1173      -0.677   1.935   4.108  1.00 51.36           C  
ANISOU 2940  C   TYR A1173     6917   6157   6440   -432    217   -104       C  
ATOM   2941  O   TYR A1173       0.167   1.964   3.206  1.00 52.35           O  
ANISOU 2941  O   TYR A1173     7166   6250   6473   -500    261    -93       O  
ATOM   2942  CB  TYR A1173      -2.484   3.412   3.222  1.00 46.79           C  
ANISOU 2942  CB  TYR A1173     6459   5487   5832   -388    -79   -146       C  
ATOM   2943  CG  TYR A1173      -3.477   2.289   3.062  1.00 57.14           C  
ANISOU 2943  CG  TYR A1173     7692   6796   7222   -369    -98   -192       C  
ATOM   2944  CD1 TYR A1173      -4.377   1.988   4.094  1.00 64.66           C  
ANISOU 2944  CD1 TYR A1173     8480   7783   8306   -302   -107   -221       C  
ATOM   2945  CD2 TYR A1173      -3.505   1.496   1.904  1.00 51.31           C  
ANISOU 2945  CD2 TYR A1173     7044   6020   6431   -420    -97   -210       C  
ATOM   2946  CE1 TYR A1173      -5.274   0.938   3.976  1.00 59.03           C  
ANISOU 2946  CE1 TYR A1173     7689   7066   7672   -284   -114   -268       C  
ATOM   2947  CE2 TYR A1173      -4.407   0.449   1.776  1.00 52.62           C  
ANISOU 2947  CE2 TYR A1173     7132   6186   6675   -401   -112   -255       C  
ATOM   2948  CZ  TYR A1173      -5.294   0.180   2.815  1.00 57.83           C  
ANISOU 2948  CZ  TYR A1173     7623   6880   7470   -331   -121   -284       C  
ATOM   2949  OH  TYR A1173      -6.210  -0.848   2.719  1.00 71.69           O  
ANISOU 2949  OH  TYR A1173     9296   8632   9312   -311   -129   -335       O  
ATOM   2950  N   GLN A1174      -0.876   0.882   4.906  1.00 48.83           N  
ANISOU 2950  N   GLN A1174     6452   5885   6215   -403    297   -113       N  
ATOM   2951  CA  GLN A1174      -0.190  -0.411   4.749  1.00 52.23           C  
ANISOU 2951  CA  GLN A1174     6850   6337   6660   -444    432   -110       C  
ATOM   2952  C   GLN A1174       1.314  -0.265   4.536  1.00 47.52           C  
ANISOU 2952  C   GLN A1174     6317   5738   6000   -503    538    -77       C  
ATOM   2953  O   GLN A1174       1.888  -0.810   3.589  1.00 53.18           O  
ANISOU 2953  O   GLN A1174     7113   6425   6667   -569    600    -84       O  
ATOM   2954  CB  GLN A1174      -0.826  -1.222   3.624  1.00 50.85           C  
ANISOU 2954  CB  GLN A1174     6729   6124   6469   -475    399   -148       C  
ATOM   2955  CG  GLN A1174      -2.143  -1.795   4.059  1.00 55.13           C  
ANISOU 2955  CG  GLN A1174     7158   6678   7112   -417    345   -187       C  
ATOM   2956  CD  GLN A1174      -2.918  -2.390   2.926  1.00 61.78           C  
ANISOU 2956  CD  GLN A1174     8060   7475   7940   -439    279   -230       C  
ATOM   2957  OE1 GLN A1174      -2.575  -2.181   1.770  1.00 66.95           O  
ANISOU 2957  OE1 GLN A1174     8863   8082   8494   -497    250   -229       O  
ATOM   2958  NE2 GLN A1174      -3.979  -3.140   3.247  1.00 60.77           N  
ANISOU 2958  NE2 GLN A1174     7821   7356   7911   -396    258   -272       N  
ATOM   2959  N   SER A1175       1.957   0.457   5.451  1.00 46.22           N  
ANISOU 2959  N   SER A1175     6113   5602   5846   -480    565    -45       N  
ATOM   2960  CA  SER A1175       3.374   0.784   5.326  1.00 50.23           C  
ANISOU 2960  CA  SER A1175     6675   6102   6307   -529    655    -19       C  
ATOM   2961  C   SER A1175       4.023   0.938   6.698  1.00 46.85           C  
ANISOU 2961  C   SER A1175     6132   5725   5942   -490    715     11       C  
ATOM   2962  O   SER A1175       3.371   0.893   7.742  1.00 44.72           O  
ANISOU 2962  O   SER A1175     5758   5496   5739   -427    686     16       O  
ATOM   2963  CB  SER A1175       3.576   2.072   4.522  1.00 52.08           C  
ANISOU 2963  CB  SER A1175     7066   6286   6437   -562    583    -15       C  
ATOM   2964  OG  SER A1175       3.000   3.181   5.193  1.00 46.63           O  
ANISOU 2964  OG  SER A1175     6354   5608   5754   -503    481     -4       O  
ATOM   2965  N   SER A1176       5.333   1.122   6.679  1.00 52.95           N  
ANISOU 2965  N   SER A1176     6933   6491   6696   -530    802     28       N  
ATOM   2966  CA  SER A1176       6.080   1.559   7.851  1.00 50.01           C  
ANISOU 2966  CA  SER A1176     6483   6154   6366   -498    839     58       C  
ATOM   2967  C   SER A1176       6.903   2.760   7.447  1.00 51.73           C  
ANISOU 2967  C   SER A1176     6803   6338   6512   -531    835     66       C  
ATOM   2968  O   SER A1176       7.102   3.020   6.260  1.00 61.55           O  
ANISOU 2968  O   SER A1176     8176   7531   7679   -591    834     50       O  
ATOM   2969  CB  SER A1176       7.001   0.476   8.427  1.00 47.74           C  
ANISOU 2969  CB  SER A1176     6098   5888   6155   -507    958     67       C  
ATOM   2970  OG  SER A1176       6.347  -0.775   8.535  1.00 53.09           O  
ANISOU 2970  OG  SER A1176     6701   6584   6888   -493    980     55       O  
ATOM   2971  N   GLY A1177       7.363   3.515   8.438  1.00 48.76           N  
ANISOU 2971  N   GLY A1177     6378   5990   6159   -495    831     91       N  
ATOM   2972  CA  GLY A1177       8.278   4.588   8.126  1.00 49.93           C  
ANISOU 2972  CA  GLY A1177     6611   6107   6251   -529    845     96       C  
ATOM   2973  C   GLY A1177       8.445   5.529   9.296  1.00 47.41           C  
ANISOU 2973  C   GLY A1177     6233   5825   5957   -475    810    122       C  
ATOM   2974  O   GLY A1177       8.053   5.230  10.421  1.00 50.04           O  
ANISOU 2974  O   GLY A1177     6455   6205   6354   -418    796    136       O  
ATOM   2975  N   SER A1178       9.039   6.679   8.989  1.00 54.36           N  
ANISOU 2975  N   SER A1178     7198   6676   6780   -498    800    125       N  
ATOM   2976  CA  SER A1178       9.294   7.709   9.982  1.00 54.79           C  
ANISOU 2976  CA  SER A1178     7211   6758   6848   -454    768    146       C  
ATOM   2977  C   SER A1178       9.375   9.054   9.284  1.00 47.87           C  
ANISOU 2977  C   SER A1178     6463   5840   5884   -478    717    144       C  
ATOM   2978  O   SER A1178       9.825   9.154   8.138  1.00 52.14           O  
ANISOU 2978  O   SER A1178     7124   6327   6362   -544    751    128       O  
ATOM   2979  CB  SER A1178      10.593   7.446  10.746  1.00 59.98           C  
ANISOU 2979  CB  SER A1178     7789   7430   7569   -457    864    156       C  
ATOM   2980  OG  SER A1178      11.682   7.906   9.967  1.00 78.07           O  
ANISOU 2980  OG  SER A1178    10167   9671   9825   -519    928    140       O  
ATOM   2981  N   SER A1179       8.932  10.087   9.982  1.00 44.81           N  
ANISOU 2981  N   SER A1179     6056   5476   5494   -428    637    160       N  
ATOM   2982  CA  SER A1179       9.072  11.433   9.466  1.00 58.51           C  
ANISOU 2982  CA  SER A1179     7903   7173   7153   -446    588    161       C  
ATOM   2983  C   SER A1179       9.279  12.387  10.632  1.00 58.76           C  
ANISOU 2983  C   SER A1179     7866   7244   7217   -395    564    180       C  
ATOM   2984  O   SER A1179       9.017  12.063  11.791  1.00 57.54           O  
ANISOU 2984  O   SER A1179     7588   7142   7131   -343    560    192       O  
ATOM   2985  CB  SER A1179       7.857  11.843   8.633  1.00 58.36           C  
ANISOU 2985  CB  SER A1179     7980   7120   7073   -444    469    152       C  
ATOM   2986  OG  SER A1179       6.777  12.195   9.468  1.00 55.41           O  
ANISOU 2986  OG  SER A1179     7526   6783   6744   -374    373    157       O  
ATOM   2987  N   ASN A1180       9.799  13.560  10.318  1.00 59.56           N  
ANISOU 2987  N   ASN A1180     8052   7314   7263   -415    553    183       N  
ATOM   2988  CA  ASN A1180       9.907  14.618  11.311  1.00 53.99           C  
ANISOU 2988  CA  ASN A1180     7296   6641   6577   -370    518    199       C  
ATOM   2989  C   ASN A1180       9.796  15.929  10.559  1.00 48.96           C  
ANISOU 2989  C   ASN A1180     6790   5955   5856   -390    455    198       C  
ATOM   2990  O   ASN A1180      10.563  16.183   9.627  1.00 54.02           O  
ANISOU 2990  O   ASN A1180     7545   6542   6438   -452    507    188       O  
ATOM   2991  CB  ASN A1180      11.217  14.531  12.087  1.00 56.35           C  
ANISOU 2991  CB  ASN A1180     7521   6960   6928   -372    616    204       C  
ATOM   2992  CG  ASN A1180      11.279  15.525  13.235  1.00 63.20           C  
ANISOU 2992  CG  ASN A1180     8325   7867   7821   -321    578    221       C  
ATOM   2993  OD1 ASN A1180      10.812  16.664  13.131  1.00 68.89           O  
ANISOU 2993  OD1 ASN A1180     9098   8577   8498   -307    504    224       O  
ATOM   2994  ND2 ASN A1180      11.838  15.091  14.344  1.00 63.60           N  
ANISOU 2994  ND2 ASN A1180     8264   7959   7942   -293    623    230       N  
ATOM   2995  N   VAL A1181       8.835  16.743  10.946  1.00 51.12           N  
ANISOU 2995  N   VAL A1181     7051   6241   6129   -342    346    205       N  
ATOM   2996  CA  VAL A1181       8.453  17.903  10.154  1.00 62.22           C  
ANISOU 2996  CA  VAL A1181     8588   7595   7458   -356    258    204       C  
ATOM   2997  C   VAL A1181       8.189  19.065  11.102  1.00 61.27           C  
ANISOU 2997  C   VAL A1181     8411   7504   7365   -303    197    216       C  
ATOM   2998  O   VAL A1181       7.690  18.861  12.213  1.00 58.67           O  
ANISOU 2998  O   VAL A1181     7951   7229   7110   -249    180    218       O  
ATOM   2999  CB  VAL A1181       7.222  17.572   9.278  1.00 55.01           C  
ANISOU 2999  CB  VAL A1181     7742   6644   6516   -357    156    192       C  
ATOM   3000  CG1 VAL A1181       6.643  18.798   8.620  1.00 48.99           C  
ANISOU 3000  CG1 VAL A1181     7102   5826   5687   -358     35    194       C  
ATOM   3001  CG2 VAL A1181       7.601  16.547   8.246  1.00 52.29           C  
ANISOU 3001  CG2 VAL A1181     7474   6263   6129   -420    223    180       C  
ATOM   3002  N   THR A1182       8.556  20.280  10.676  1.00 60.24           N  
ANISOU 3002  N   THR A1182     8382   7334   7174   -322    171    221       N  
ATOM   3003  CA  THR A1182       8.178  21.508  11.366  1.00 59.64           C  
ANISOU 3003  CA  THR A1182     8274   7273   7113   -276     96    229       C  
ATOM   3004  C   THR A1182       7.412  22.403  10.408  1.00 58.58           C  
ANISOU 3004  C   THR A1182     8273   7072   6911   -285    -26    227       C  
ATOM   3005  O   THR A1182       7.772  22.518   9.244  1.00 63.08           O  
ANISOU 3005  O   THR A1182     8994   7578   7395   -341    -18    226       O  
ATOM   3006  CB  THR A1182       9.383  22.287  11.921  1.00 70.72           C  
ANISOU 3006  CB  THR A1182     9662   8692   8516   -283    173    238       C  
ATOM   3007  OG1 THR A1182      10.270  21.405  12.645  1.00 66.19           O  
ANISOU 3007  OG1 THR A1182     8986   8164   8000   -284    285    238       O  
ATOM   3008  CG2 THR A1182       8.879  23.435  12.830  1.00 64.69           C  
ANISOU 3008  CG2 THR A1182     8838   7956   7784   -228     97    245       C  
ATOM   3009  N   VAL A1183       6.381  23.060  10.926  1.00 67.60           N  
ANISOU 3009  N   VAL A1183     9362   8224   8097   -231   -136    224       N  
ATOM   3010  CA  VAL A1183       5.326  23.694  10.144  1.00 67.20           C  
ANISOU 3010  CA  VAL A1183     9406   8112   8015   -223   -283    216       C  
ATOM   3011  C   VAL A1183       5.106  25.102  10.691  1.00 73.96           C  
ANISOU 3011  C   VAL A1183    10246   8967   8889   -187   -353    221       C  
ATOM   3012  O   VAL A1183       5.049  25.294  11.910  1.00 71.35           O  
ANISOU 3012  O   VAL A1183     9777   8697   8635   -144   -328    220       O  
ATOM   3013  CB  VAL A1183       4.022  22.859  10.227  1.00 64.59           C  
ANISOU 3013  CB  VAL A1183     8999   7788   7754   -187   -361    194       C  
ATOM   3014  CG1 VAL A1183       2.900  23.482   9.420  1.00 65.54           C  
ANISOU 3014  CG1 VAL A1183     9209   7836   7858   -175   -528    181       C  
ATOM   3015  CG2 VAL A1183       4.269  21.415   9.795  1.00 63.11           C  
ANISOU 3015  CG2 VAL A1183     8812   7610   7558   -220   -282    189       C  
ATOM   3016  N   TRP A1184       4.965  26.087   9.796  1.00 77.98           N  
ANISOU 3016  N   TRP A1184    10901   9402   9324   -207   -441    227       N  
ATOM   3017  CA  TRP A1184       4.719  27.457  10.239  1.00 74.79           C  
ANISOU 3017  CA  TRP A1184    10488   8991   8939   -174   -515    231       C  
ATOM   3018  C   TRP A1184       4.229  28.313   9.085  1.00 86.40           C  
ANISOU 3018  C   TRP A1184    12130  10364  10333   -192   -648    235       C  
ATOM   3019  O   TRP A1184       4.696  28.155   7.951  1.00 94.05           O  
ANISOU 3019  O   TRP A1184    13265  11274  11198   -251   -632    244       O  
ATOM   3020  CB  TRP A1184       5.985  28.086  10.836  1.00 64.23           C  
ANISOU 3020  CB  TRP A1184     9132   7689   7583   -187   -400    247       C  
ATOM   3021  CG  TRP A1184       7.145  28.281   9.883  1.00 61.99           C  
ANISOU 3021  CG  TRP A1184     9007   7356   7192   -256   -320    259       C  
ATOM   3022  CD1 TRP A1184       7.487  29.431   9.238  1.00 68.64           C  
ANISOU 3022  CD1 TRP A1184     9991   8135   7955   -285   -350    268       C  
ATOM   3023  CD2 TRP A1184       8.136  27.309   9.509  1.00 63.78           C  
ANISOU 3023  CD2 TRP A1184     9262   7587   7385   -309   -185    256       C  
ATOM   3024  NE1 TRP A1184       8.621  29.239   8.479  1.00 65.12           N  
ANISOU 3024  NE1 TRP A1184     9665   7652   7426   -356   -237    270       N  
ATOM   3025  CE2 TRP A1184       9.038  27.946   8.628  1.00 61.37           C  
ANISOU 3025  CE2 TRP A1184     9118   7217   6982   -372   -134    260       C  
ATOM   3026  CE3 TRP A1184       8.342  25.963   9.824  1.00 74.36           C  
ANISOU 3026  CE3 TRP A1184    10508   8974   8772   -312   -101    249       C  
ATOM   3027  CZ2 TRP A1184      10.118  27.286   8.059  1.00 65.55           C  
ANISOU 3027  CZ2 TRP A1184     9712   7727   7469   -438      1    251       C  
ATOM   3028  CZ3 TRP A1184       9.429  25.305   9.258  1.00 76.82           C  
ANISOU 3028  CZ3 TRP A1184    10880   9268   9042   -374     25    244       C  
ATOM   3029  CH2 TRP A1184      10.302  25.969   8.385  1.00 73.78           C  
ANISOU 3029  CH2 TRP A1184    10650   8816   8567   -438     78    242       C  
ATOM   3030  N   GLY A 243       3.313  29.236   9.392  1.00 82.49           N  
ANISOU 3030  N   GLY A 243    11601   9850   9893   -145   -778    226       N  
ATOM   3031  CA  GLY A 243       2.909  30.287   8.469  1.00 86.08           C  
ANISOU 3031  CA  GLY A 243    12213  10211  10284   -155   -916    233       C  
ATOM   3032  C   GLY A 243       4.012  31.303   8.205  1.00 88.88           C  
ANISOU 3032  C   GLY A 243    12684  10540  10545   -194   -854    258       C  
ATOM   3033  O   GLY A 243       5.198  30.977   8.305  1.00 88.36           O  
ANISOU 3033  O   GLY A 243    12628  10509  10437   -234   -700    268       O  
ATOM   3034  N   SER A 244       3.642  32.529   7.841  1.00 83.00           N  
ANISOU 3034  N   SER A 244    12033   9730   9774   -185   -974    265       N  
ATOM   3035  CA  SER A 244       4.595  33.625   7.744  1.00 83.81           C  
ANISOU 3035  CA  SER A 244    12228   9811   9804   -214   -919    286       C  
ATOM   3036  C   SER A 244       3.952  34.877   8.323  1.00 85.76           C  
ANISOU 3036  C   SER A 244    12416  10050  10119   -160  -1031    283       C  
ATOM   3037  O   SER A 244       2.724  35.019   8.329  1.00 77.72           O  
ANISOU 3037  O   SER A 244    11357   9000   9172   -116  -1184    266       O  
ATOM   3038  CB  SER A 244       5.057  33.864   6.302  1.00 82.41           C  
ANISOU 3038  CB  SER A 244    12305   9533   9475   -287   -933    303       C  
ATOM   3039  OG  SER A 244       3.951  34.086   5.449  1.00 87.99           O  
ANISOU 3039  OG  SER A 244    13125  10151  10158   -278  -1121    303       O  
ATOM   3040  N   SER A 245       4.794  35.777   8.832  1.00 86.77           N  
ANISOU 3040  N   SER A 245    12531  10202  10234   -164   -952    294       N  
ATOM   3041  CA  SER A 245       4.335  36.925   9.600  1.00 80.39           C  
ANISOU 3041  CA  SER A 245    11636   9405   9504   -113  -1025    289       C  
ATOM   3042  C   SER A 245       4.659  38.239   8.895  1.00 85.28           C  
ANISOU 3042  C   SER A 245    12425   9942  10035   -139  -1080    309       C  
ATOM   3043  O   SER A 245       5.470  38.310   7.965  1.00 78.62           O  
ANISOU 3043  O   SER A 245    11762   9045   9067   -202  -1024    327       O  
ATOM   3044  CB  SER A 245       4.961  36.955  11.003  1.00 68.57           C  
ANISOU 3044  CB  SER A 245     9955   8015   8085    -87   -893    282       C  
ATOM   3045  OG  SER A 245       6.370  36.836  10.926  1.00 78.38           O  
ANISOU 3045  OG  SER A 245    11249   9280   9253   -134   -736    296       O  
ATOM   3046  N   LYS A 246       4.008  39.285   9.377  1.00 90.26           N  
ANISOU 3046  N   LYS A 246    12996  10560  10737    -92  -1185    303       N  
ATOM   3047  CA  LYS A 246       4.251  40.646   8.942  1.00 90.86           C  
ANISOU 3047  CA  LYS A 246    13202  10567  10752   -105  -1240    320       C  
ATOM   3048  C   LYS A 246       5.313  41.350   9.780  1.00 82.83           C  
ANISOU 3048  C   LYS A 246    12117   9613   9742   -107  -1100    325       C  
ATOM   3049  O   LYS A 246       5.663  42.494   9.472  1.00 86.34           O  
ANISOU 3049  O   LYS A 246    12665  10005  10133   -122  -1121    339       O  
ATOM   3050  CB  LYS A 246       2.933  41.424   8.985  1.00 96.53           C  
ANISOU 3050  CB  LYS A 246    13890  11230  11558    -51  -1440    307       C  
ATOM   3051  CG  LYS A 246       2.128  41.171  10.258  1.00 94.43           C  
ANISOU 3051  CG  LYS A 246    13377  11043  11460     14  -1453    272       C  
ATOM   3052  CD  LYS A 246       0.668  40.885   9.959  1.00 89.84           C  
ANISOU 3052  CD  LYS A 246    12763  10404  10967     52  -1633    243       C  
ATOM   3053  CE  LYS A 246       0.464  39.451   9.505  1.00 92.10           C  
ANISOU 3053  CE  LYS A 246    13062  10700  11232     35  -1614    236       C  
ATOM   3054  NZ  LYS A 246      -0.984  39.079   9.478  1.00 93.43           N  
ANISOU 3054  NZ  LYS A 246    13148  10830  11522     80  -1770    196       N  
ATOM   3055  N   ARG A 247       5.835  40.702  10.822  1.00 71.50           N  
ANISOU 3055  N   ARG A 247    10514   8283   8369    -94   -964    313       N  
ATOM   3056  CA  ARG A 247       6.808  41.315  11.714  1.00 73.61           C  
ANISOU 3056  CA  ARG A 247    10699   8612   8656    -91   -840    314       C  
ATOM   3057  C   ARG A 247       8.159  40.621  11.589  1.00 67.97           C  
ANISOU 3057  C   ARG A 247    10018   7930   7877   -142   -664    318       C  
ATOM   3058  O   ARG A 247       8.238  39.399  11.426  1.00 63.18           O  
ANISOU 3058  O   ARG A 247     9394   7346   7266   -158   -614    314       O  
ATOM   3059  CB  ARG A 247       6.317  41.304  13.166  1.00 75.94           C  
ANISOU 3059  CB  ARG A 247    10768   8998   9086    -30   -835    293       C  
ATOM   3060  CG  ARG A 247       5.983  39.950  13.755  1.00 79.06           C  
ANISOU 3060  CG  ARG A 247    11030   9462   9546    -13   -793    278       C  
ATOM   3061  CD  ARG A 247       5.909  40.043  15.287  1.00 78.02           C  
ANISOU 3061  CD  ARG A 247    10697   9423   9523     31   -740    260       C  
ATOM   3062  NE  ARG A 247       6.131  38.752  15.937  1.00 74.29           N  
ANISOU 3062  NE  ARG A 247    10118   9024   9084     33   -643    254       N  
ATOM   3063  CZ  ARG A 247       6.605  38.596  17.171  1.00 76.52           C  
ANISOU 3063  CZ  ARG A 247    10266   9390   9419     50   -548    247       C  
ATOM   3064  NH1 ARG A 247       6.933  39.656  17.908  1.00 85.36           N  
ANISOU 3064  NH1 ARG A 247    11334  10534  10564     66   -529    245       N  
ATOM   3065  NH2 ARG A 247       6.766  37.373  17.662  1.00 73.00           N  
ANISOU 3065  NH2 ARG A 247     9741   8999   8996     50   -473    244       N  
ATOM   3066  N   LYS A 248       9.221  41.415  11.661  1.00 65.11           N  
ANISOU 3066  N   LYS A 248     9700   7564   7475   -167   -570    321       N  
ATOM   3067  CA  LYS A 248      10.526  40.958  11.227  1.00 64.38           C  
ANISOU 3067  CA  LYS A 248     9684   7464   7312   -228   -415    319       C  
ATOM   3068  C   LYS A 248      11.199  40.147  12.320  1.00 59.89           C  
ANISOU 3068  C   LYS A 248     8938   6997   6822   -210   -289    304       C  
ATOM   3069  O   LYS A 248      10.960  40.361  13.514  1.00 66.06           O  
ANISOU 3069  O   LYS A 248     9554   7852   7694   -157   -298    298       O  
ATOM   3070  CB  LYS A 248      11.406  42.143  10.820  1.00 76.04           C  
ANISOU 3070  CB  LYS A 248    11285   8886   8720   -266   -361    322       C  
ATOM   3071  CG  LYS A 248      12.698  41.717  10.143  1.00 93.13           C  
ANISOU 3071  CG  LYS A 248    13559  11018  10809   -340   -204    310       C  
ATOM   3072  CD  LYS A 248      13.865  42.556  10.603  1.00 94.97           C  
ANISOU 3072  CD  LYS A 248    13767  11263  11054   -354    -83    295       C  
ATOM   3073  CE  LYS A 248      15.140  42.224   9.839  1.00 89.53           C  
ANISOU 3073  CE  LYS A 248    13198  10523  10298   -435     77    273       C  
ATOM   3074  NZ  LYS A 248      15.903  43.445   9.444  1.00 87.08           N  
ANISOU 3074  NZ  LYS A 248    13009  10147   9931   -474    136    264       N  
ATOM   3075  N   LYS A 249      12.034  39.187  11.892  1.00 70.13           N  
ANISOU 3075  N   LYS A 249    10274   8291   8083   -258   -174    296       N  
ATOM   3076  CA  LYS A 249      12.726  38.303  12.826  1.00 71.10           C  
ANISOU 3076  CA  LYS A 249    10240   8496   8277   -246    -60    283       C  
ATOM   3077  C   LYS A 249      13.569  39.096  13.819  1.00 65.71           C  
ANISOU 3077  C   LYS A 249     9460   7860   7646   -225     14    272       C  
ATOM   3078  O   LYS A 249      13.756  38.665  14.964  1.00 62.24           O  
ANISOU 3078  O   LYS A 249     8858   7501   7288   -188     53    266       O  
ATOM   3079  CB  LYS A 249      13.592  37.300  12.052  1.00 61.33           C  
ANISOU 3079  CB  LYS A 249     9081   7228   6993   -309     55    271       C  
ATOM   3080  CG  LYS A 249      13.654  35.896  12.676  1.00 59.89           C  
ANISOU 3080  CG  LYS A 249     8761   7114   6880   -292    107    264       C  
ATOM   3081  CD  LYS A 249      14.089  34.849  11.672  1.00 68.34           C  
ANISOU 3081  CD  LYS A 249     9929   8139   7899   -354    179    255       C  
ATOM   3082  CE  LYS A 249      12.993  34.500  10.663  1.00 80.25           C  
ANISOU 3082  CE  LYS A 249    11555   9594   9341   -368     70    268       C  
ATOM   3083  NZ  LYS A 249      13.470  33.535   9.615  1.00 72.50           N  
ANISOU 3083  NZ  LYS A 249    10686   8562   8299   -438    149    257       N  
ATOM   3084  N   SER A 250      14.047  40.274  13.407  1.00 69.50           N  
ANISOU 3084  N   SER A 250    10041   8287   8077   -249     28    270       N  
ATOM   3085  CA  SER A 250      14.844  41.121  14.292  1.00 72.47           C  
ANISOU 3085  CA  SER A 250    10331   8702   8500   -231     93    258       C  
ATOM   3086  C   SER A 250      14.016  41.666  15.455  1.00 68.73           C  
ANISOU 3086  C   SER A 250     9714   8294   8104   -161      4    265       C  
ATOM   3087  O   SER A 250      14.514  41.805  16.581  1.00 52.09           O  
ANISOU 3087  O   SER A 250     7472   6255   6065   -132     58    254       O  
ATOM   3088  CB  SER A 250      15.457  42.266  13.488  1.00 61.55           C  
ANISOU 3088  CB  SER A 250     9104   7239   7043   -276    126    253       C  
ATOM   3089  OG  SER A 250      15.942  43.294  14.329  1.00 77.48           O  
ANISOU 3089  OG  SER A 250    11041   9289   9107   -248    156    243       O  
ATOM   3090  N   GLU A 251      12.761  41.994  15.206  1.00 73.21           N  
ANISOU 3090  N   GLU A 251    10311   8839   8667   -136   -132    280       N  
ATOM   3091  CA  GLU A 251      11.954  42.502  16.298  1.00 68.02           C  
ANISOU 3091  CA  GLU A 251     9515   8238   8093    -76   -207    278       C  
ATOM   3092  C   GLU A 251      11.356  41.387  17.140  1.00 60.88           C  
ANISOU 3092  C   GLU A 251     8467   7404   7262    -42   -216    274       C  
ATOM   3093  O   GLU A 251      11.131  41.599  18.332  1.00 61.20           O  
ANISOU 3093  O   GLU A 251     8367   7509   7376     -2   -217    266       O  
ATOM   3094  CB  GLU A 251      10.917  43.453  15.721  1.00 57.89           C  
ANISOU 3094  CB  GLU A 251     8315   6889   6791    -63   -348    288       C  
ATOM   3095  CG  GLU A 251      11.606  44.632  15.011  1.00 55.46           C  
ANISOU 3095  CG  GLU A 251     8150   6512   6409    -98   -327    294       C  
ATOM   3096  CD  GLU A 251      12.753  45.267  15.840  1.00 80.91           C  
ANISOU 3096  CD  GLU A 251    11298   9783   9661    -96   -210    280       C  
ATOM   3097  OE1 GLU A 251      12.487  46.240  16.577  1.00 85.86           O  
ANISOU 3097  OE1 GLU A 251    11848  10435  10339    -60   -248    276       O  
ATOM   3098  OE2 GLU A 251      13.929  44.834  15.747  1.00 92.65           O  
ANISOU 3098  OE2 GLU A 251    12800  11277  11125   -132    -80    268       O  
ATOM   3099  N   LYS A 252      11.167  40.193  16.563  1.00 59.73           N  
ANISOU 3099  N   LYS A 252     8356   7246   7092    -61   -211    278       N  
ATOM   3100  CA  LYS A 252      10.848  39.013  17.363  1.00 52.41           C  
ANISOU 3100  CA  LYS A 252     7298   6387   6229    -37   -189    272       C  
ATOM   3101  C   LYS A 252      11.961  38.711  18.355  1.00 48.58           C  
ANISOU 3101  C   LYS A 252     6711   5967   5779    -34    -71    266       C  
ATOM   3102  O   LYS A 252      11.699  38.341  19.505  1.00 50.55           O  
ANISOU 3102  O   LYS A 252     6828   6285   6096      1    -64    261       O  
ATOM   3103  CB  LYS A 252      10.630  37.804  16.456  1.00 64.56           C  
ANISOU 3103  CB  LYS A 252     8906   7895   7728    -65   -191    277       C  
ATOM   3104  CG  LYS A 252       9.397  37.854  15.576  1.00 73.01           C  
ANISOU 3104  CG  LYS A 252    10060   8905   8777    -62   -323    280       C  
ATOM   3105  CD  LYS A 252       9.124  36.473  14.977  1.00 84.95           C  
ANISOU 3105  CD  LYS A 252    11599  10407  10271    -82   -317    281       C  
ATOM   3106  CE  LYS A 252       9.149  35.385  16.075  1.00 85.56           C  
ANISOU 3106  CE  LYS A 252    11516  10569  10424    -56   -252    273       C  
ATOM   3107  NZ  LYS A 252       8.700  34.024  15.611  1.00 88.22           N  
ANISOU 3107  NZ  LYS A 252    11858  10903  10760    -67   -255    271       N  
ATOM   3108  N   LYS A 253      13.216  38.873  17.926  1.00 59.10           N  
ANISOU 3108  N   LYS A 253     8110   7276   7071    -72     24    261       N  
ATOM   3109  CA  LYS A 253      14.352  38.581  18.796  1.00 60.11           C  
ANISOU 3109  CA  LYS A 253     8144   7454   7242    -69    129    250       C  
ATOM   3110  C   LYS A 253      14.487  39.603  19.924  1.00 52.48           C  
ANISOU 3110  C   LYS A 253     7084   6533   6322    -32    123    244       C  
ATOM   3111  O   LYS A 253      14.796  39.225  21.064  1.00 48.73           O  
ANISOU 3111  O   LYS A 253     6490   6121   5904     -7    157    240       O  
ATOM   3112  CB  LYS A 253      15.639  38.506  17.972  1.00 59.63           C  
ANISOU 3112  CB  LYS A 253     8176   7342   7139   -123    234    236       C  
ATOM   3113  CG  LYS A 253      15.826  37.187  17.239  1.00 55.78           C  
ANISOU 3113  CG  LYS A 253     7732   6831   6630   -160    279    234       C  
ATOM   3114  CD  LYS A 253      17.292  36.829  17.062  1.00 61.20           C  
ANISOU 3114  CD  LYS A 253     8426   7497   7329   -200    410    208       C  
ATOM   3115  CE  LYS A 253      17.909  36.237  18.325  1.00 66.52           C  
ANISOU 3115  CE  LYS A 253     8942   8240   8093   -167    457    199       C  
ATOM   3116  NZ  LYS A 253      19.380  36.048  18.136  1.00 76.21           N  
ANISOU 3116  NZ  LYS A 253    10172   9435   9350   -204    578    165       N  
ATOM   3117  N   VAL A 254      14.259  40.893  19.638  1.00 46.04           N  
ANISOU 3117  N   VAL A 254     6327   5684   5484    -31     77    245       N  
ATOM   3118  CA  VAL A 254      14.323  41.906  20.695  1.00 48.52           C  
ANISOU 3118  CA  VAL A 254     6552   6040   5843      3     69    238       C  
ATOM   3119  C   VAL A 254      13.215  41.688  21.714  1.00 49.42           C  
ANISOU 3119  C   VAL A 254     6549   6211   6018     47      1    240       C  
ATOM   3120  O   VAL A 254      13.461  41.700  22.928  1.00 47.06           O  
ANISOU 3120  O   VAL A 254     6138   5974   5769     71     32    232       O  
ATOM   3121  CB  VAL A 254      14.248  43.328  20.109  1.00 49.80           C  
ANISOU 3121  CB  VAL A 254     6805   6147   5969     -6     30    238       C  
ATOM   3122  CG1 VAL A 254      14.080  44.376  21.242  1.00 41.92           C  
ANISOU 3122  CG1 VAL A 254     5704   5196   5027     33      8    230       C  
ATOM   3123  CG2 VAL A 254      15.445  43.610  19.255  1.00 45.56           C  
ANISOU 3123  CG2 VAL A 254     6380   5556   5377    -53    118    230       C  
ATOM   3124  N   THR A 255      11.970  41.511  21.228  1.00 44.88           N  
ANISOU 3124  N   THR A 255     6003   5609   5442     55    -92    245       N  
ATOM   3125  CA  THR A 255      10.840  41.221  22.107  1.00 45.80           C  
ANISOU 3125  CA  THR A 255     6010   5767   5625     90   -149    238       C  
ATOM   3126  C   THR A 255      11.084  39.980  22.976  1.00 53.67           C  
ANISOU 3126  C   THR A 255     6913   6825   6652     97    -86    237       C  
ATOM   3127  O   THR A 255      10.756  39.975  24.173  1.00 54.08           O  
ANISOU 3127  O   THR A 255     6859   6931   6758    121    -81    228       O  
ATOM   3128  CB  THR A 255       9.568  41.072  21.269  1.00 53.21           C  
ANISOU 3128  CB  THR A 255     7001   6653   6562     93   -256    238       C  
ATOM   3129  OG1 THR A 255       9.192  42.362  20.762  1.00 52.05           O  
ANISOU 3129  OG1 THR A 255     6918   6453   6405     97   -333    237       O  
ATOM   3130  CG2 THR A 255       8.390  40.460  22.093  1.00 48.04           C  
ANISOU 3130  CG2 THR A 255     6231   6036   5986    123   -298    221       C  
ATOM   3131  N   ARG A 256      11.671  38.919  22.407  1.00 49.79           N  
ANISOU 3131  N   ARG A 256     6466   6325   6129     72    -34    246       N  
ATOM   3132  CA  ARG A 256      12.012  37.777  23.248  1.00 53.00           C  
ANISOU 3132  CA  ARG A 256     6788   6785   6565     79     25    247       C  
ATOM   3133  C   ARG A 256      13.020  38.175  24.329  1.00 49.13           C  
ANISOU 3133  C   ARG A 256     6229   6340   6099     89     87    243       C  
ATOM   3134  O   ARG A 256      12.827  37.879  25.516  1.00 56.98           O  
ANISOU 3134  O   ARG A 256     7131   7386   7133    111     94    240       O  
ATOM   3135  CB  ARG A 256      12.531  36.620  22.397  1.00 45.45           C  
ANISOU 3135  CB  ARG A 256     5889   5804   5575     49     70    255       C  
ATOM   3136  CG  ARG A 256      12.687  35.343  23.192  1.00 46.14           C  
ANISOU 3136  CG  ARG A 256     5893   5938   5698     58    114    258       C  
ATOM   3137  CD  ARG A 256      13.216  34.226  22.316  1.00 65.51           C  
ANISOU 3137  CD  ARG A 256     8401   8365   8127     26    162    262       C  
ATOM   3138  NE  ARG A 256      13.667  33.074  23.097  1.00 77.80           N  
ANISOU 3138  NE  ARG A 256     9880   9962   9720     34    213    266       N  
ATOM   3139  CZ  ARG A 256      14.935  32.683  23.215  1.00 70.42           C  
ANISOU 3139  CZ  ARG A 256     8933   9026   8798     19    286    262       C  
ATOM   3140  NH1 ARG A 256      15.910  33.341  22.582  1.00 57.39           N  
ANISOU 3140  NH1 ARG A 256     7341   7337   7129     -6    330    250       N  
ATOM   3141  NH2 ARG A 256      15.218  31.607  23.946  1.00 66.99           N  
ANISOU 3141  NH2 ARG A 256     8429   8623   8399     29    316    268       N  
ATOM   3142  N   MET A 257      14.069  38.903  23.947  1.00 44.91           N  
ANISOU 3142  N   MET A 257     5743   5781   5541     73    130    238       N  
ATOM   3143  CA  MET A 257      15.143  39.222  24.886  1.00 44.12           C  
ANISOU 3143  CA  MET A 257     5579   5716   5468     81    188    229       C  
ATOM   3144  C   MET A 257      14.627  39.970  26.109  1.00 43.59           C  
ANISOU 3144  C   MET A 257     5429   5697   5437    113    154    225       C  
ATOM   3145  O   MET A 257      15.023  39.659  27.239  1.00 50.36           O  
ANISOU 3145  O   MET A 257     6209   6601   6325    128    181    222       O  
ATOM   3146  CB  MET A 257      16.232  40.036  24.192  1.00 51.16           C  
ANISOU 3146  CB  MET A 257     6539   6563   6335     57    238    217       C  
ATOM   3147  CG  MET A 257      17.416  40.349  25.092  1.00 57.74           C  
ANISOU 3147  CG  MET A 257     7305   7426   7208     66    297    201       C  
ATOM   3148  SD  MET A 257      18.691  41.363  24.302  1.00 71.57           S  
ANISOU 3148  SD  MET A 257     9130   9119   8944     35    367    176       S  
ATOM   3149  CE  MET A 257      17.822  42.920  24.083  1.00 56.43           C  
ANISOU 3149  CE  MET A 257     7259   7187   6995     45    300    182       C  
ATOM   3150  N   VAL A 258      13.764  40.973  25.913  1.00 42.23           N  
ANISOU 3150  N   VAL A 258     5273   5508   5263    122     93    221       N  
ATOM   3151  CA  VAL A 258      13.248  41.717  27.066  1.00 42.69           C  
ANISOU 3151  CA  VAL A 258     5250   5608   5362    147     68    210       C  
ATOM   3152  C   VAL A 258      12.513  40.783  28.028  1.00 43.45           C  
ANISOU 3152  C   VAL A 258     5270   5748   5492    160     61    210       C  
ATOM   3153  O   VAL A 258      12.655  40.894  29.254  1.00 55.05           O  
ANISOU 3153  O   VAL A 258     6669   7263   6986    172     83    203       O  
ATOM   3154  CB  VAL A 258      12.364  42.898  26.617  1.00 49.52           C  
ANISOU 3154  CB  VAL A 258     6145   6439   6233    153     -2    203       C  
ATOM   3155  CG1 VAL A 258      11.698  43.557  27.826  1.00 50.89           C  
ANISOU 3155  CG1 VAL A 258     6224   6652   6458    175    -24    186       C  
ATOM   3156  CG2 VAL A 258      13.186  43.937  25.828  1.00 41.62           C  
ANISOU 3156  CG2 VAL A 258     5224   5395   5194    138     14    204       C  
ATOM   3157  N   SER A 259      11.756  39.822  27.501  1.00 42.78           N  
ANISOU 3157  N   SER A 259     5203   5647   5404    155     36    215       N  
ATOM   3158  CA  SER A 259      11.056  38.887  28.381  1.00 43.01           C  
ANISOU 3158  CA  SER A 259     5166   5712   5465    163     40    211       C  
ATOM   3159  C   SER A 259      12.032  38.096  29.256  1.00 47.00           C  
ANISOU 3159  C   SER A 259     5635   6258   5966    163    102    222       C  
ATOM   3160  O   SER A 259      11.737  37.800  30.421  1.00 52.15           O  
ANISOU 3160  O   SER A 259     6229   6948   6639    170    114    217       O  
ATOM   3161  CB  SER A 259      10.191  37.937  27.557  1.00 45.17           C  
ANISOU 3161  CB  SER A 259     5468   5956   5738    157      6    214       C  
ATOM   3162  OG  SER A 259      10.928  36.795  27.108  1.00 47.18           O  
ANISOU 3162  OG  SER A 259     5756   6209   5964    143     51    231       O  
ATOM   3163  N   ILE A 260      13.196  37.734  28.718  1.00 45.23           N  
ANISOU 3163  N   ILE A 260     5450   6019   5717    151    142    233       N  
ATOM   3164  CA  ILE A 260      14.159  36.983  29.520  1.00 43.18           C  
ANISOU 3164  CA  ILE A 260     5153   5788   5465    153    189    240       C  
ATOM   3165  C   ILE A 260      14.833  37.896  30.534  1.00 45.41           C  
ANISOU 3165  C   ILE A 260     5394   6098   5760    166    201    232       C  
ATOM   3166  O   ILE A 260      15.093  37.497  31.679  1.00 45.20           O  
ANISOU 3166  O   ILE A 260     5323   6106   5746    174    212    235       O  
ATOM   3167  CB  ILE A 260      15.184  36.283  28.608  1.00 55.22           C  
ANISOU 3167  CB  ILE A 260     6722   7280   6978    136    229    246       C  
ATOM   3168  CG1 ILE A 260      14.467  35.341  27.617  1.00 54.96           C  
ANISOU 3168  CG1 ILE A 260     6732   7220   6928    121    217    255       C  
ATOM   3169  CG2 ILE A 260      16.222  35.526  29.446  1.00 49.29           C  
ANISOU 3169  CG2 ILE A 260     5927   6550   6250    141    266    250       C  
ATOM   3170  CD1 ILE A 260      15.393  34.432  26.826  1.00 56.30           C  
ANISOU 3170  CD1 ILE A 260     6939   7361   7091     99    265    258       C  
ATOM   3171  N   VAL A 261      15.113  39.143  30.140  1.00 49.92           N  
ANISOU 3171  N   VAL A 261     5988   6653   6328    165    196    220       N  
ATOM   3172  CA  VAL A 261      15.614  40.126  31.099  1.00 47.98           C  
ANISOU 3172  CA  VAL A 261     5699   6434   6096    177    203    208       C  
ATOM   3173  C   VAL A 261      14.608  40.324  32.234  1.00 46.14           C  
ANISOU 3173  C   VAL A 261     5414   6239   5878    188    178    203       C  
ATOM   3174  O   VAL A 261      14.987  40.455  33.407  1.00 44.84           O  
ANISOU 3174  O   VAL A 261     5209   6109   5721    194    190    199       O  
ATOM   3175  CB  VAL A 261      15.961  41.444  30.376  1.00 45.28           C  
ANISOU 3175  CB  VAL A 261     5395   6062   5747    173    204    196       C  
ATOM   3176  CG1 VAL A 261      15.897  42.631  31.328  1.00 40.35           C  
ANISOU 3176  CG1 VAL A 261     4724   5468   5141    187    194    182       C  
ATOM   3177  CG2 VAL A 261      17.343  41.338  29.802  1.00 39.75           C  
ANISOU 3177  CG2 VAL A 261     4725   5334   5045    161    254    190       C  
ATOM   3178  N   VAL A 262      13.312  40.282  31.917  1.00 43.01           N  
ANISOU 3178  N   VAL A 262     5021   5832   5488    185    144    199       N  
ATOM   3179  CA  VAL A 262      12.306  40.425  32.964  1.00 47.33           C  
ANISOU 3179  CA  VAL A 262     5516   6406   6059    188    132    184       C  
ATOM   3180  C   VAL A 262      12.278  39.201  33.872  1.00 53.83           C  
ANISOU 3180  C   VAL A 262     6318   7256   6877    184    158    193       C  
ATOM   3181  O   VAL A 262      12.108  39.322  35.099  1.00 51.96           O  
ANISOU 3181  O   VAL A 262     6047   7049   6646    181    172    184       O  
ATOM   3182  CB  VAL A 262      10.934  40.697  32.338  1.00 52.61           C  
ANISOU 3182  CB  VAL A 262     6188   7047   6756    188     86    169       C  
ATOM   3183  CG1 VAL A 262       9.839  40.464  33.384  1.00 49.52           C  
ANISOU 3183  CG1 VAL A 262     5739   6675   6400    183     90    146       C  
ATOM   3184  CG2 VAL A 262      10.908  42.138  31.771  1.00 41.16           C  
ANISOU 3184  CG2 VAL A 262     4754   5571   5314    193     53    158       C  
ATOM   3185  N   ALA A 263      12.445  38.002  33.300  1.00 59.10           N  
ANISOU 3185  N   ALA A 263     7012   7911   7533    180    166    211       N  
ATOM   3186  CA  ALA A 263      12.419  36.804  34.137  1.00 42.09           C  
ANISOU 3186  CA  ALA A 263     4844   5778   5372    176    188    222       C  
ATOM   3187  C   ALA A 263      13.628  36.751  35.072  1.00 43.91           C  
ANISOU 3187  C   ALA A 263     5065   6029   5589    180    207    233       C  
ATOM   3188  O   ALA A 263      13.507  36.318  36.226  1.00 44.17           O  
ANISOU 3188  O   ALA A 263     5086   6084   5613    176    217    236       O  
ATOM   3189  CB  ALA A 263      12.340  35.551  33.272  1.00 48.83           C  
ANISOU 3189  CB  ALA A 263     5724   6609   6219    170    192    238       C  
ATOM   3190  N   VAL A 264      14.795  37.215  34.612  1.00 43.36           N  
ANISOU 3190  N   VAL A 264     5006   5949   5520    187    212    235       N  
ATOM   3191  CA  VAL A 264      15.972  37.255  35.484  1.00 39.01           C  
ANISOU 3191  CA  VAL A 264     4440   5411   4971    196    219    238       C  
ATOM   3192  C   VAL A 264      15.802  38.305  36.578  1.00 41.44           C  
ANISOU 3192  C   VAL A 264     4722   5747   5275    198    212    223       C  
ATOM   3193  O   VAL A 264      16.170  38.071  37.733  1.00 44.56           O  
ANISOU 3193  O   VAL A 264     5109   6161   5660    200    208    227       O  
ATOM   3194  CB  VAL A 264      17.252  37.486  34.656  1.00 42.64           C  
ANISOU 3194  CB  VAL A 264     4911   5843   5448    200    233    233       C  
ATOM   3195  CG1 VAL A 264      18.445  37.757  35.556  1.00 44.68           C  
ANISOU 3195  CG1 VAL A 264     5143   6110   5724    212    232    226       C  
ATOM   3196  CG2 VAL A 264      17.529  36.268  33.781  1.00 41.04           C  
ANISOU 3196  CG2 VAL A 264     4731   5612   5250    192    249    246       C  
ATOM   3197  N   PHE A 265      15.219  39.461  36.250  1.00 48.22           N  
ANISOU 3197  N   PHE A 265     5573   6605   6142    198    205    206       N  
ATOM   3198  CA  PHE A 265      14.908  40.461  37.278  1.00 50.32           C  
ANISOU 3198  CA  PHE A 265     5812   6898   6411    196    203    187       C  
ATOM   3199  C   PHE A 265      14.103  39.853  38.435  1.00 56.59           C  
ANISOU 3199  C   PHE A 265     6599   7712   7192    182    211    186       C  
ATOM   3200  O   PHE A 265      14.403  40.074  39.624  1.00 54.11           O  
ANISOU 3200  O   PHE A 265     6279   7419   6861    176    216    182       O  
ATOM   3201  CB  PHE A 265      14.133  41.637  36.664  1.00 36.39           C  
ANISOU 3201  CB  PHE A 265     4038   5123   4666    196    191    168       C  
ATOM   3202  CG  PHE A 265      13.479  42.485  37.674  1.00 38.95           C  
ANISOU 3202  CG  PHE A 265     4328   5470   5003    188    194    144       C  
ATOM   3203  CD1 PHE A 265      14.197  43.481  38.318  1.00 49.21           C  
ANISOU 3203  CD1 PHE A 265     5609   6787   6302    194    200    133       C  
ATOM   3204  CD2 PHE A 265      12.153  42.276  38.034  1.00 38.84           C  
ANISOU 3204  CD2 PHE A 265     4296   5456   5006    174    196    128       C  
ATOM   3205  CE1 PHE A 265      13.599  44.278  39.305  1.00 40.13           C  
ANISOU 3205  CE1 PHE A 265     4428   5658   5163    182    208    108       C  
ATOM   3206  CE2 PHE A 265      11.556  43.051  39.028  1.00 45.76           C  
ANISOU 3206  CE2 PHE A 265     5139   6348   5900    160    209     99       C  
ATOM   3207  CZ  PHE A 265      12.285  44.065  39.660  1.00 40.21           C  
ANISOU 3207  CZ  PHE A 265     4422   5666   5190    164    216     91       C  
ATOM   3208  N   ILE A 266      13.056  39.098  38.093  1.00 56.72           N  
ANISOU 3208  N   ILE A 266     6620   7717   7213    171    215    186       N  
ATOM   3209  CA  ILE A 266      12.199  38.493  39.104  1.00 44.29           C  
ANISOU 3209  CA  ILE A 266     5045   6154   5629    151    235    179       C  
ATOM   3210  C   ILE A 266      13.008  37.535  39.968  1.00 47.27           C  
ANISOU 3210  C   ILE A 266     5451   6541   5969    149    241    204       C  
ATOM   3211  O   ILE A 266      12.887  37.516  41.201  1.00 48.05           O  
ANISOU 3211  O   ILE A 266     5561   6652   6042    132    255    199       O  
ATOM   3212  CB  ILE A 266      11.017  37.791  38.406  1.00 46.27           C  
ANISOU 3212  CB  ILE A 266     5294   6384   5904    144    238    171       C  
ATOM   3213  CG1 ILE A 266       9.999  38.817  37.905  1.00 43.76           C  
ANISOU 3213  CG1 ILE A 266     4944   6052   5632    143    222    138       C  
ATOM   3214  CG2 ILE A 266      10.387  36.717  39.300  1.00 41.22           C  
ANISOU 3214  CG2 ILE A 266     4665   5747   5249    122    269    170       C  
ATOM   3215  CD1 ILE A 266       8.938  38.194  36.991  1.00 44.05           C  
ANISOU 3215  CD1 ILE A 266     4977   6059   5701    142    207    128       C  
ATOM   3216  N   PHE A 267      13.867  36.744  39.339  1.00 49.23           N  
ANISOU 3216  N   PHE A 267     5715   6776   6214    163    229    229       N  
ATOM   3217  CA  PHE A 267      14.634  35.773  40.102  1.00 46.08           C  
ANISOU 3217  CA  PHE A 267     5342   6377   5790    164    223    253       C  
ATOM   3218  C   PHE A 267      15.544  36.462  41.108  1.00 38.24           C  
ANISOU 3218  C   PHE A 267     4350   5397   4783    169    205    250       C  
ATOM   3219  O   PHE A 267      15.702  35.991  42.234  1.00 49.42           O  
ANISOU 3219  O   PHE A 267     5796   6816   6165    159    197    260       O  
ATOM   3220  CB  PHE A 267      15.422  34.882  39.140  1.00 49.84           C  
ANISOU 3220  CB  PHE A 267     5824   6831   6282    178    214    273       C  
ATOM   3221  CG  PHE A 267      16.172  33.778  39.802  1.00 51.23           C  
ANISOU 3221  CG  PHE A 267     6023   6998   6446    181    199    297       C  
ATOM   3222  CD1 PHE A 267      17.452  33.991  40.329  1.00 57.30           C  
ANISOU 3222  CD1 PHE A 267     6788   7761   7223    197    169    300       C  
ATOM   3223  CD2 PHE A 267      15.627  32.508  39.871  1.00 63.46           C  
ANISOU 3223  CD2 PHE A 267     7594   8538   7981    171    210    314       C  
ATOM   3224  CE1 PHE A 267      18.165  32.951  40.937  1.00 58.16           C  
ANISOU 3224  CE1 PHE A 267     6919   7852   7328    202    140    322       C  
ATOM   3225  CE2 PHE A 267      16.333  31.462  40.471  1.00 65.14           C  
ANISOU 3225  CE2 PHE A 267     7832   8736   8184    174    189    338       C  
ATOM   3226  CZ  PHE A 267      17.605  31.690  41.007  1.00 59.32           C  
ANISOU 3226  CZ  PHE A 267     7093   7988   7456    191    149    343       C  
ATOM   3227  N   CYS A 268      16.126  37.596  40.741  1.00 49.13           N  
ANISOU 3227  N   CYS A 268     5702   6780   6184    183    197    235       N  
ATOM   3228  CA  CYS A 268      17.065  38.255  41.649  1.00 48.76           C  
ANISOU 3228  CA  CYS A 268     5652   6744   6131    191    176    229       C  
ATOM   3229  C   CYS A 268      16.402  39.125  42.712  1.00 44.80           C  
ANISOU 3229  C   CYS A 268     5151   6267   5605    172    188    210       C  
ATOM   3230  O   CYS A 268      17.011  39.334  43.770  1.00 54.99           O  
ANISOU 3230  O   CYS A 268     6457   7565   6872    171    168    209       O  
ATOM   3231  CB  CYS A 268      18.073  39.102  40.863  1.00 48.28           C  
ANISOU 3231  CB  CYS A 268     5561   6673   6109    213    170    216       C  
ATOM   3232  SG  CYS A 268      19.109  38.139  39.727  1.00 64.62           S  
ANISOU 3232  SG  CYS A 268     7631   8705   8215    228    168    228       S  
ATOM   3233  N   TRP A 269      15.196  39.657  42.476  1.00 41.99           N  
ANISOU 3233  N   TRP A 269     4778   5918   5258    156    216    190       N  
ATOM   3234  CA  TRP A 269      14.630  40.607  43.442  1.00 50.18           C  
ANISOU 3234  CA  TRP A 269     5807   6974   6286    135    234    163       C  
ATOM   3235  C   TRP A 269      13.550  40.024  44.348  1.00 48.60           C  
ANISOU 3235  C   TRP A 269     5635   6773   6057     99    267    154       C  
ATOM   3236  O   TRP A 269      13.213  40.656  45.359  1.00 44.50           O  
ANISOU 3236  O   TRP A 269     5122   6265   5521     74    288    131       O  
ATOM   3237  CB  TRP A 269      14.085  41.848  42.723  1.00 42.70           C  
ANISOU 3237  CB  TRP A 269     4814   6028   5382    140    242    136       C  
ATOM   3238  CG  TRP A 269      15.196  42.737  42.198  1.00 40.57           C  
ANISOU 3238  CG  TRP A 269     4524   5760   5131    167    222    135       C  
ATOM   3239  CD1 TRP A 269      15.850  42.594  41.027  1.00 39.71           C  
ANISOU 3239  CD1 TRP A 269     4415   5632   5042    188    209    148       C  
ATOM   3240  CD2 TRP A 269      15.805  43.848  42.863  1.00 43.46           C  
ANISOU 3240  CD2 TRP A 269     4872   6143   5497    170    219    118       C  
ATOM   3241  NE1 TRP A 269      16.810  43.552  40.893  1.00 52.99           N  
ANISOU 3241  NE1 TRP A 269     6078   7315   6739    204    204    137       N  
ATOM   3242  CE2 TRP A 269      16.799  44.348  42.005  1.00 49.96           C  
ANISOU 3242  CE2 TRP A 269     5680   6955   6346    196    206    119       C  
ATOM   3243  CE3 TRP A 269      15.592  44.485  44.092  1.00 46.99           C  
ANISOU 3243  CE3 TRP A 269     5316   6612   5927    151    230     98       C  
ATOM   3244  CZ2 TRP A 269      17.583  45.457  42.330  1.00 37.72           C  
ANISOU 3244  CZ2 TRP A 269     4106   5415   4809    207    203    101       C  
ATOM   3245  CZ3 TRP A 269      16.370  45.590  44.412  1.00 36.93           C  
ANISOU 3245  CZ3 TRP A 269     4019   5350   4662    162    222     82       C  
ATOM   3246  CH2 TRP A 269      17.343  46.062  43.533  1.00 40.81           C  
ANISOU 3246  CH2 TRP A 269     4490   5832   5184    191    208     84       C  
ATOM   3247  N   LEU A 270      13.032  38.829  44.031  1.00 42.69           N  
ANISOU 3247  N   LEU A 270     4907   6009   5303     92    278    169       N  
ATOM   3248  CA  LEU A 270      12.004  38.220  44.878  1.00 44.44           C  
ANISOU 3248  CA  LEU A 270     5160   6223   5500     53    320    156       C  
ATOM   3249  C   LEU A 270      12.530  37.763  46.231  1.00 49.92           C  
ANISOU 3249  C   LEU A 270     5922   6918   6127     32    318    172       C  
ATOM   3250  O   LEU A 270      11.902  38.102  47.257  1.00 61.20           O  
ANISOU 3250  O   LEU A 270     7376   8348   7530     -7    358    146       O  
ATOM   3251  CB  LEU A 270      11.334  37.071  44.120  1.00 48.83           C  
ANISOU 3251  CB  LEU A 270     5719   6761   6074     53    332    165       C  
ATOM   3252  CG  LEU A 270      10.126  36.481  44.842  1.00 54.67           C  
ANISOU 3252  CG  LEU A 270     6482   7486   6804     11    388    141       C  
ATOM   3253  CD1 LEU A 270       9.212  37.602  45.317  1.00 52.60           C  
ANISOU 3253  CD1 LEU A 270     6185   7226   6574    -17    427     90       C  
ATOM   3254  CD2 LEU A 270       9.394  35.572  43.881  1.00 56.97           C  
ANISOU 3254  CD2 LEU A 270     6755   7758   7131     17    397    142       C  
ATOM   3255  N   PRO A 271      13.619  36.982  46.348  1.00 50.34           N  
ANISOU 3255  N   PRO A 271     6012   6963   6150     52    273    210       N  
ATOM   3256  CA  PRO A 271      14.137  36.662  47.698  1.00 43.27           C  
ANISOU 3256  CA  PRO A 271     5192   6062   5188     33    255    225       C  
ATOM   3257  C   PRO A 271      14.273  37.890  48.595  1.00 46.50           C  
ANISOU 3257  C   PRO A 271     5604   6488   5577     16    258    200       C  
ATOM   3258  O   PRO A 271      13.904  37.849  49.778  1.00 49.07           O  
ANISOU 3258  O   PRO A 271     5993   6806   5844    -26    283    191       O  
ATOM   3259  CB  PRO A 271      15.505  36.016  47.407  1.00 50.79           C  
ANISOU 3259  CB  PRO A 271     6153   7001   6144     72    186    262       C  
ATOM   3260  CG  PRO A 271      15.397  35.495  45.971  1.00 41.49           C  
ANISOU 3260  CG  PRO A 271     4925   5818   5021     97    192    270       C  
ATOM   3261  CD  PRO A 271      14.440  36.379  45.258  1.00 41.69           C  
ANISOU 3261  CD  PRO A 271     4895   5859   5085     91    234    238       C  
ATOM   3262  N   PHE A 272      14.754  39.002  48.025  1.00 51.89           N  
ANISOU 3262  N   PHE A 272     6221   7188   6306     45    241    185       N  
ATOM   3263  CA  PHE A 272      14.927  40.252  48.759  1.00 43.54           C  
ANISOU 3263  CA  PHE A 272     5155   6150   5240     33    244    158       C  
ATOM   3264  C   PHE A 272      13.615  40.743  49.339  1.00 49.61           C  
ANISOU 3264  C   PHE A 272     5926   6922   6002    -16    314    120       C  
ATOM   3265  O   PHE A 272      13.522  41.054  50.536  1.00 46.15           O  
ANISOU 3265  O   PHE A 272     5538   6484   5514    -53    333    105       O  
ATOM   3266  CB  PHE A 272      15.524  41.306  47.829  1.00 47.08           C  
ANISOU 3266  CB  PHE A 272     5527   6613   5749     72    224    147       C  
ATOM   3267  CG  PHE A 272      15.577  42.700  48.412  1.00 47.04           C  
ANISOU 3267  CG  PHE A 272     5497   6628   5748     62    235    115       C  
ATOM   3268  CD1 PHE A 272      16.529  43.033  49.372  1.00 40.75           C  
ANISOU 3268  CD1 PHE A 272     4731   5837   4916     64    198    117       C  
ATOM   3269  CD2 PHE A 272      14.706  43.691  47.958  1.00 42.00           C  
ANISOU 3269  CD2 PHE A 272     4802   6000   5156     54    275     82       C  
ATOM   3270  CE1 PHE A 272      16.603  44.315  49.878  1.00 39.80           C  
ANISOU 3270  CE1 PHE A 272     4586   5736   4801     55    210     87       C  
ATOM   3271  CE2 PHE A 272      14.771  44.983  48.461  1.00 45.02           C  
ANISOU 3271  CE2 PHE A 272     5156   6400   5548     45    287     52       C  
ATOM   3272  CZ  PHE A 272      15.727  45.294  49.427  1.00 45.29           C  
ANISOU 3272  CZ  PHE A 272     5222   6445   5543     45    258     54       C  
ATOM   3273  N   TYR A 273      12.584  40.828  48.497  1.00 49.35           N  
ANISOU 3273  N   TYR A 273     5841   6886   6025    -18    353     98       N  
ATOM   3274  CA  TYR A 273      11.318  41.353  48.978  1.00 45.04           C  
ANISOU 3274  CA  TYR A 273     5281   6336   5498    -64    420     50       C  
ATOM   3275  C   TYR A 273      10.654  40.381  49.937  1.00 46.22           C  
ANISOU 3275  C   TYR A 273     5507   6463   5593   -115    470     46       C  
ATOM   3276  O   TYR A 273      10.029  40.810  50.905  1.00 48.42           O  
ANISOU 3276  O   TYR A 273     5810   6735   5852   -166    528      8       O  
ATOM   3277  CB  TYR A 273      10.422  41.707  47.784  1.00 51.18           C  
ANISOU 3277  CB  TYR A 273     5979   7108   6362    -48    433     25       C  
ATOM   3278  CG  TYR A 273      10.770  43.067  47.235  1.00 42.53           C  
ANISOU 3278  CG  TYR A 273     4819   6028   5314    -20    407     11       C  
ATOM   3279  CD1 TYR A 273      10.598  44.202  48.005  1.00 48.75           C  
ANISOU 3279  CD1 TYR A 273     5588   6827   6109    -44    434    -25       C  
ATOM   3280  CD2 TYR A 273      11.340  43.210  45.995  1.00 42.63           C  
ANISOU 3280  CD2 TYR A 273     4798   6043   5358     26    360     34       C  
ATOM   3281  CE1 TYR A 273      10.939  45.450  47.526  1.00 47.66           C  
ANISOU 3281  CE1 TYR A 273     5392   6702   6013    -19    411    -37       C  
ATOM   3282  CE2 TYR A 273      11.686  44.460  45.505  1.00 48.63           C  
ANISOU 3282  CE2 TYR A 273     5510   6812   6156     49    340     22       C  
ATOM   3283  CZ  TYR A 273      11.469  45.576  46.274  1.00 40.36           C  
ANISOU 3283  CZ  TYR A 273     4440   5777   5119     28    364    -13       C  
ATOM   3284  OH  TYR A 273      11.814  46.822  45.807  1.00 54.44           O  
ANISOU 3284  OH  TYR A 273     6176   7568   6940     50    346    -25       O  
ATOM   3285  N   ILE A 274      10.833  39.074  49.733  1.00 52.39           N  
ANISOU 3285  N   ILE A 274     6333   7228   6344   -106    454     82       N  
ATOM   3286  CA  ILE A 274      10.270  38.114  50.673  1.00 47.52           C  
ANISOU 3286  CA  ILE A 274     5803   6586   5668   -157    502     81       C  
ATOM   3287  C   ILE A 274      10.917  38.281  52.042  1.00 54.08           C  
ANISOU 3287  C   ILE A 274     6725   7413   6408   -187    491     91       C  
ATOM   3288  O   ILE A 274      10.232  38.302  53.069  1.00 52.59           O  
ANISOU 3288  O   ILE A 274     6599   7207   6176   -249    557     61       O  
ATOM   3289  CB  ILE A 274      10.403  36.681  50.133  1.00 52.85           C  
ANISOU 3289  CB  ILE A 274     6505   7244   6330   -138    481    121       C  
ATOM   3290  CG1 ILE A 274       9.423  36.488  48.983  1.00 50.57           C  
ANISOU 3290  CG1 ILE A 274     6140   6950   6123   -126    511     98       C  
ATOM   3291  CG2 ILE A 274      10.052  35.659  51.213  1.00 49.26           C  
ANISOU 3291  CG2 ILE A 274     6161   6759   5798   -189    522    128       C  
ATOM   3292  CD1 ILE A 274       9.532  35.158  48.305  1.00 52.68           C  
ANISOU 3292  CD1 ILE A 274     6423   7204   6390   -105    492    134       C  
ATOM   3293  N   PHE A 275      12.242  38.446  52.074  1.00 58.77           N  
ANISOU 3293  N   PHE A 275     7331   8022   6979   -147    408    127       N  
ATOM   3294  CA  PHE A 275      12.911  38.710  53.345  1.00 55.81           C  
ANISOU 3294  CA  PHE A 275     7041   7641   6524   -171    380    135       C  
ATOM   3295  C   PHE A 275      12.386  39.990  53.988  1.00 60.45           C  
ANISOU 3295  C   PHE A 275     7611   8242   7114   -210    436     84       C  
ATOM   3296  O   PHE A 275      12.087  40.019  55.187  1.00 60.84           O  
ANISOU 3296  O   PHE A 275     7751   8274   7091   -269    476     68       O  
ATOM   3297  CB  PHE A 275      14.427  38.794  53.141  1.00 51.83           C  
ANISOU 3297  CB  PHE A 275     6527   7145   6020   -114    276    172       C  
ATOM   3298  CG  PHE A 275      15.199  38.826  54.416  1.00 46.56           C  
ANISOU 3298  CG  PHE A 275     5958   6463   5270   -132    225    186       C  
ATOM   3299  CD1 PHE A 275      15.416  40.023  55.088  1.00 56.20           C  
ANISOU 3299  CD1 PHE A 275     7176   7700   6476   -147    227    158       C  
ATOM   3300  CD2 PHE A 275      15.695  37.662  54.961  1.00 53.61           C  
ANISOU 3300  CD2 PHE A 275     6951   7320   6098   -135    171    228       C  
ATOM   3301  CE1 PHE A 275      16.119  40.054  56.283  1.00 56.25           C  
ANISOU 3301  CE1 PHE A 275     7282   7689   6401   -166    173    170       C  
ATOM   3302  CE2 PHE A 275      16.404  37.684  56.146  1.00 65.60           C  
ANISOU 3302  CE2 PHE A 275     8572   8816   7536   -152    110    242       C  
ATOM   3303  CZ  PHE A 275      16.615  38.888  56.811  1.00 62.46           C  
ANISOU 3303  CZ  PHE A 275     8174   8436   7120   -168    110    212       C  
ATOM   3304  N   ASN A 276      12.289  41.069  53.209  1.00 57.01           N  
ANISOU 3304  N   ASN A 276     7066   7834   6760   -182    440     58       N  
ATOM   3305  CA  ASN A 276      11.875  42.347  53.775  1.00 58.39           C  
ANISOU 3305  CA  ASN A 276     7214   8022   6949   -215    488      9       C  
ATOM   3306  C   ASN A 276      10.487  42.240  54.387  1.00 61.51           C  
ANISOU 3306  C   ASN A 276     7638   8394   7341   -287    592    -40       C  
ATOM   3307  O   ASN A 276      10.253  42.729  55.503  1.00 67.40           O  
ANISOU 3307  O   ASN A 276     8438   9132   8040   -343    640    -71       O  
ATOM   3308  CB  ASN A 276      11.900  43.436  52.701  1.00 63.78           C  
ANISOU 3308  CB  ASN A 276     7775   8731   7727   -171    474    -10       C  
ATOM   3309  CG  ASN A 276      13.234  44.201  52.630  1.00 68.10           C  
ANISOU 3309  CG  ASN A 276     8298   9302   8273   -126    402      9       C  
ATOM   3310  OD1 ASN A 276      14.088  44.143  53.525  1.00 70.87           O  
ANISOU 3310  OD1 ASN A 276     8717   9653   8559   -131    362     26       O  
ATOM   3311  ND2 ASN A 276      13.402  44.934  51.541  1.00 77.07           N  
ANISOU 3311  ND2 ASN A 276     9343  10455   9486    -82    384      3       N  
ATOM   3312  N   VAL A 277       9.556  41.578  53.687  1.00 53.41           N  
ANISOU 3312  N   VAL A 277     6576   7350   6367   -289    633    -51       N  
ATOM   3313  CA  VAL A 277       8.209  41.425  54.234  1.00 59.91           C  
ANISOU 3313  CA  VAL A 277     7418   8142   7204   -359    740   -107       C  
ATOM   3314  C   VAL A 277       8.254  40.609  55.528  1.00 57.74           C  
ANISOU 3314  C   VAL A 277     7289   7837   6813   -420    776    -97       C  
ATOM   3315  O   VAL A 277       7.554  40.921  56.495  1.00 58.48           O  
ANISOU 3315  O   VAL A 277     7430   7907   6882   -494    864   -147       O  
ATOM   3316  CB  VAL A 277       7.257  40.812  53.185  1.00 55.01           C  
ANISOU 3316  CB  VAL A 277     6728   7503   6668   -344    765   -123       C  
ATOM   3317  CG1 VAL A 277       5.961  40.388  53.825  1.00 51.76           C  
ANISOU 3317  CG1 VAL A 277     6348   7049   6268   -418    877   -181       C  
ATOM   3318  CG2 VAL A 277       6.948  41.840  52.109  1.00 52.45           C  
ANISOU 3318  CG2 VAL A 277     6274   7197   6459   -303    743   -150       C  
ATOM   3319  N   SER A 278       9.116  39.590  55.583  1.00 57.55           N  
ANISOU 3319  N   SER A 278     7343   7808   6716   -394    707    -33       N  
ATOM   3320  CA  SER A 278       9.385  38.909  56.848  1.00 54.11           C  
ANISOU 3320  CA  SER A 278     7063   7341   6156   -446    715    -13       C  
ATOM   3321  C   SER A 278       9.880  39.873  57.921  1.00 57.17           C  
ANISOU 3321  C   SER A 278     7506   7735   6480   -479    708    -27       C  
ATOM   3322  O   SER A 278       9.391  39.854  59.053  1.00 66.08           O  
ANISOU 3322  O   SER A 278     8739   8832   7535   -557    781    -56       O  
ATOM   3323  CB  SER A 278      10.408  37.805  56.634  1.00 51.59           C  
ANISOU 3323  CB  SER A 278     6801   7015   5785   -399    616     60       C  
ATOM   3324  OG  SER A 278       9.905  36.851  55.735  1.00 61.50           O  
ANISOU 3324  OG  SER A 278     8017   8262   7090   -378    632     71       O  
ATOM   3325  N   SER A 279      10.868  40.711  57.591  1.00 64.31           N  
ANISOU 3325  N   SER A 279     8347   8677   7411   -422    624     -9       N  
ATOM   3326  CA  SER A 279      11.550  41.497  58.616  1.00 60.01           C  
ANISOU 3326  CA  SER A 279     7865   8138   6798   -444    595    -13       C  
ATOM   3327  C   SER A 279      10.578  42.391  59.372  1.00 59.53           C  
ANISOU 3327  C   SER A 279     7810   8070   6739   -521    708    -83       C  
ATOM   3328  O   SER A 279      10.806  42.707  60.545  1.00 64.93           O  
ANISOU 3328  O   SER A 279     8598   8740   7334   -573    719    -93       O  
ATOM   3329  CB  SER A 279      12.684  42.321  57.984  1.00 59.01           C  
ANISOU 3329  CB  SER A 279     7645   8052   6725   -367    498      7       C  
ATOM   3330  OG  SER A 279      12.236  43.563  57.442  1.00 61.45           O  
ANISOU 3330  OG  SER A 279     7830   8392   7126   -358    542    -40       O  
ATOM   3331  N   VAL A 280       9.491  42.727  58.730  1.00 64.41           N  
ANISOU 3331  N   VAL A 280     8325   8691   7458   -531    790   -132       N  
ATOM   3332  CA  VAL A 280       8.498  43.552  59.341  1.00 71.45           C  
ANISOU 3332  CA  VAL A 280     9202   9569   8377   -603    903   -208       C  
ATOM   3333  C   VAL A 280       7.969  42.816  60.537  1.00 79.69           C  
ANISOU 3333  C   VAL A 280    10400  10561   9317   -695    986   -225       C  
ATOM   3334  O   VAL A 280       7.642  43.408  61.545  1.00 79.84           O  
ANISOU 3334  O   VAL A 280    10479  10563   9295   -768   1060   -271       O  
ATOM   3335  CB  VAL A 280       7.351  43.829  58.397  1.00 74.78           C  
ANISOU 3335  CB  VAL A 280     9488   9988   8938   -596    968   -259       C  
ATOM   3336  CG1 VAL A 280       6.096  44.096  59.189  1.00 72.37           C  
ANISOU 3336  CG1 VAL A 280     9202   9642   8653   -692   1108   -342       C  
ATOM   3337  CG2 VAL A 280       7.691  44.988  57.500  1.00 66.65           C  
ANISOU 3337  CG2 VAL A 280     8318   9000   8005   -532    912   -264       C  
ATOM   3338  N   SER A 281       7.927  41.502  60.430  1.00 78.54           N  
ANISOU 3338  N   SER A 281    10327  10389   9126   -693    974   -186       N  
ATOM   3339  CA  SER A 281       7.364  40.700  61.486  1.00 73.08           C  
ANISOU 3339  CA  SER A 281     9790   9641   8335   -782   1060   -201       C  
ATOM   3340  C   SER A 281       8.297  40.386  62.631  1.00 86.69           C  
ANISOU 3340  C   SER A 281    11692  11345   9901   -811   1000   -154       C  
ATOM   3341  O   SER A 281       8.465  39.232  62.984  1.00 90.28           O  
ANISOU 3341  O   SER A 281    12273  11762  10266   -826    980   -112       O  
ATOM   3342  CB  SER A 281       6.859  39.392  60.903  1.00 70.24           C  
ANISOU 3342  CB  SER A 281     9438   9256   7994   -772   1080   -182       C  
ATOM   3343  OG  SER A 281       6.307  39.583  59.632  1.00 71.39           O  
ANISOU 3343  OG  SER A 281     9416   9425   8283   -720   1085   -205       O  
ATOM   3344  N   MET A 282       8.894  41.419  63.209  1.00 93.50           N  
ANISOU 3344  N   MET A 282    12567  12228  10731   -817    967   -163       N  
ATOM   3345  CA  MET A 282       9.726  41.267  64.397  1.00101.19           C  
ANISOU 3345  CA  MET A 282    13716  13177  11554   -851    907   -128       C  
ATOM   3346  C   MET A 282      10.767  40.170  64.318  1.00100.87           C  
ANISOU 3346  C   MET A 282    13761  13124  11441   -796    770    -43       C  
ATOM   3347  O   MET A 282      10.863  39.340  65.198  1.00104.30           O  
ANISOU 3347  O   MET A 282    14372  13506  11750   -846    763    -16       O  
ATOM   3348  CB  MET A 282       8.846  41.053  65.621  1.00 98.05           C  
ANISOU 3348  CB  MET A 282    13478  12719  11059   -975   1040   -176       C  
ATOM   3349  N   ALA A 283      11.560  40.170  63.273  1.00 97.43           N  
ANISOU 3349  N   ALA A 283    13203  12729  11086   -695    661     -2       N  
ATOM   3350  CA  ALA A 283      12.532  39.117  63.088  1.00 99.24           C  
ANISOU 3350  CA  ALA A 283    13491  12944  11274   -639    534     72       C  
ATOM   3351  C   ALA A 283      13.898  39.458  63.635  1.00104.91           C  
ANISOU 3351  C   ALA A 283    14264  13662  11934   -603    394    109       C  
ATOM   3352  O   ALA A 283      14.870  38.786  63.325  1.00 95.08           O  
ANISOU 3352  O   ALA A 283    13028  12410  10689   -540    270    164       O  
ATOM   3353  CB  ALA A 283      12.632  38.752  61.617  1.00 90.46           C  
ANISOU 3353  CB  ALA A 283    12224  11865  10283   -554    499     94       C  
ATOM   3354  N   ILE A 284      13.988  40.446  64.510  1.00111.85           N  
ANISOU 3354  N   ILE A 284    15190  14545  12764   -647    411     76       N  
ATOM   3355  CA  ILE A 284      15.291  40.864  64.978  1.00108.45           C  
ANISOU 3355  CA  ILE A 284    14796  14116  12293   -608    273    104       C  
ATOM   3356  C   ILE A 284      15.903  39.954  66.014  1.00119.16           C  
ANISOU 3356  C   ILE A 284    16356  15409  13510   -635    179    152       C  
ATOM   3357  O   ILE A 284      15.826  40.194  67.210  1.00123.05           O  
ANISOU 3357  O   ILE A 284    17001  15867  13884   -708    194    139       O  
ATOM   3358  CB  ILE A 284      15.237  42.259  65.596  1.00101.66           C  
ANISOU 3358  CB  ILE A 284    13920  13281  11426   -646    316     52       C  
ATOM   3359  CG1 ILE A 284      14.135  43.081  64.948  1.00 96.52           C  
ANISOU 3359  CG1 ILE A 284    13122  12670  10881   -664    456    -10       C  
ATOM   3360  CG2 ILE A 284      16.583  42.942  65.447  1.00101.68           C  
ANISOU 3360  CG2 ILE A 284    13856  13311  11466   -569    178     70       C  
ATOM   3361  CD1 ILE A 284      14.077  44.506  65.442  1.00 91.78           C  
ANISOU 3361  CD1 ILE A 284    12482  12096  10292   -695    501    -63       C  
ATOM   3362  N   SER A 285      16.480  38.879  65.496  1.00118.08           N  
ANISOU 3362  N   SER A 285    16222  15253  13391   -576     82    207       N  
ATOM   3363  CA  SER A 285      17.215  37.881  66.220  1.00108.45           C  
ANISOU 3363  CA  SER A 285    15170  13969  12067   -577    -40    263       C  
ATOM   3364  C   SER A 285      18.381  37.753  65.281  1.00100.56           C  
ANISOU 3364  C   SER A 285    14037  12991  11179   -467   -177    295       C  
ATOM   3365  O   SER A 285      18.454  36.795  64.542  1.00108.13           O  
ANISOU 3365  O   SER A 285    14957  13941  12187   -425   -202    327       O  
ATOM   3366  CB  SER A 285      16.441  36.580  66.227  1.00108.96           C  
ANISOU 3366  CB  SER A 285    15330  13990  12078   -618     23    286       C  
ATOM   3367  OG  SER A 285      16.401  36.047  64.923  1.00111.10           O  
ANISOU 3367  OG  SER A 285    15451  14292  12471   -549     23    301       O  
ATOM   3368  N   PRO A 286      19.281  38.731  65.274  1.00 85.75           N  
ANISOU 3368  N   PRO A 286    12086  11143   9353   -421   -257    280       N  
ATOM   3369  CA  PRO A 286      20.348  38.613  64.293  1.00 81.14           C  
ANISOU 3369  CA  PRO A 286    11363  10574   8891   -320   -368    300       C  
ATOM   3370  C   PRO A 286      21.210  37.457  64.622  1.00 80.75           C  
ANISOU 3370  C   PRO A 286    11418  10460   8804   -290   -514    354       C  
ATOM   3371  O   PRO A 286      21.896  37.413  65.605  1.00 89.82           O  
ANISOU 3371  O   PRO A 286    12692  11560   9873   -300   -626    370       O  
ATOM   3372  CB  PRO A 286      21.134  39.883  64.503  1.00 86.98           C  
ANISOU 3372  CB  PRO A 286    12038  11342   9670   -291   -424    269       C  
ATOM   3373  CG  PRO A 286      20.142  40.841  65.041  1.00 88.92           C  
ANISOU 3373  CG  PRO A 286    12306  11617   9863   -367   -290    223       C  
ATOM   3374  CD  PRO A 286      19.299  40.023  65.955  1.00 86.26           C  
ANISOU 3374  CD  PRO A 286    12156  11230   9388   -455   -231    237       C  
ATOM   3375  N   THR A 287      21.256  36.563  63.674  1.00 86.19           N  
ANISOU 3375  N   THR A 287    12035  11147   9568   -245   -522    380       N  
ATOM   3376  CA  THR A 287      21.955  35.324  63.801  1.00 82.81           C  
ANISOU 3376  CA  THR A 287    11686  10655   9124   -215   -647    430       C  
ATOM   3377  C   THR A 287      22.824  35.185  62.596  1.00 90.15           C  
ANISOU 3377  C   THR A 287    12444  11602  10209   -123   -713    433       C  
ATOM   3378  O   THR A 287      22.572  35.759  61.551  1.00 92.05           O  
ANISOU 3378  O   THR A 287    12525  11901  10550    -95   -630    404       O  
ATOM   3379  CB  THR A 287      20.928  34.184  63.770  1.00 75.53           C  
ANISOU 3379  CB  THR A 287    10850   9709   8138   -263   -559    456       C  
ATOM   3380  OG1 THR A 287      19.829  34.544  64.591  1.00 82.19           O  
ANISOU 3380  OG1 THR A 287    11806  10555   8868   -356   -435    431       O  
ATOM   3381  CG2 THR A 287      21.461  32.916  64.312  1.00 82.95           C  
ANISOU 3381  CG2 THR A 287    11934  10571   9013   -259   -679    510       C  
ATOM   3382  N   PRO A 288      23.855  34.369  62.713  1.00 87.32           N  
ANISOU 3382  N   PRO A 288    12120  11184   9874    -77   -863    467       N  
ATOM   3383  CA  PRO A 288      24.763  34.064  61.628  1.00 78.62           C  
ANISOU 3383  CA  PRO A 288    10869  10081   8924      5   -930    467       C  
ATOM   3384  C   PRO A 288      23.973  33.412  60.510  1.00 81.14           C  
ANISOU 3384  C   PRO A 288    11106  10431   9293      8   -816    475       C  
ATOM   3385  O   PRO A 288      24.238  33.721  59.371  1.00 85.15           O  
ANISOU 3385  O   PRO A 288    11454  10975   9924     56   -786    454       O  
ATOM   3386  CB  PRO A 288      25.727  33.074  62.262  1.00 78.57           C  
ANISOU 3386  CB  PRO A 288    10967   9986   8899     31  -1104    506       C  
ATOM   3387  CG  PRO A 288      25.010  32.528  63.431  1.00 73.77           C  
ANISOU 3387  CG  PRO A 288    10573   9338   8118    -45  -1095    539       C  
ATOM   3388  CD  PRO A 288      24.195  33.653  63.942  1.00 76.05           C  
ANISOU 3388  CD  PRO A 288    10893   9677   8327   -107   -979    505       C  
ATOM   3389  N   ALA A 289      23.043  32.516  60.815  1.00 82.86           N  
ANISOU 3389  N   ALA A 289    11436  10630   9419    -44   -755    504       N  
ATOM   3390  CA  ALA A 289      22.221  31.909  59.795  1.00 78.95           C  
ANISOU 3390  CA  ALA A 289    10866  10163   8968    -45   -645    508       C  
ATOM   3391  C   ALA A 289      21.340  32.925  59.084  1.00 81.25           C  
ANISOU 3391  C   ALA A 289    11041  10530   9302    -59   -502    464       C  
ATOM   3392  O   ALA A 289      21.236  32.885  57.877  1.00 80.54           O  
ANISOU 3392  O   ALA A 289    10818  10472   9311    -23   -455    454       O  
ATOM   3393  CB  ALA A 289      21.373  30.813  60.395  1.00 72.26           C  
ANISOU 3393  CB  ALA A 289    10172   9276   8008   -103   -603    541       C  
ATOM   3394  N   LEU A 290      20.718  33.840  59.822  1.00 80.42           N  
ANISOU 3394  N   LEU A 290    10986  10446   9123   -113   -435    436       N  
ATOM   3395  CA  LEU A 290      19.868  34.840  59.192  1.00 78.19           C  
ANISOU 3395  CA  LEU A 290    10593  10229   8888   -127   -307    391       C  
ATOM   3396  C   LEU A 290      20.634  36.073  58.748  1.00 77.09           C  
ANISOU 3396  C   LEU A 290    10327  10128   8837    -79   -341    360       C  
ATOM   3397  O   LEU A 290      20.161  36.791  57.863  1.00 80.60           O  
ANISOU 3397  O   LEU A 290    10649  10622   9353    -68   -258    329       O  
ATOM   3398  CB  LEU A 290      18.754  35.254  60.147  1.00 76.73           C  
ANISOU 3398  CB  LEU A 290    10510  10046   8598   -212   -203    366       C  
ATOM   3399  CG  LEU A 290      17.935  34.064  60.613  1.00 81.47           C  
ANISOU 3399  CG  LEU A 290    11243  10603   9110   -268   -152    390       C  
ATOM   3400  CD1 LEU A 290      16.852  34.548  61.531  1.00 88.33           C  
ANISOU 3400  CD1 LEU A 290    12207  11469   9887   -358    -35    355       C  
ATOM   3401  CD2 LEU A 290      17.354  33.350  59.405  1.00 85.77           C  
ANISOU 3401  CD2 LEU A 290    11688  11166   9736   -243    -89    395       C  
ATOM   3402  N   LYS A 291      21.794  36.338  59.339  1.00 73.21           N  
ANISOU 3402  N   LYS A 291     9864   9610   8341    -50   -463    365       N  
ATOM   3403  CA  LYS A 291      22.575  37.494  58.931  1.00 71.10           C  
ANISOU 3403  CA  LYS A 291     9477   9374   8163     -5   -493    331       C  
ATOM   3404  C   LYS A 291      23.317  37.237  57.622  1.00 77.16           C  
ANISOU 3404  C   LYS A 291    10105  10146   9066     66   -525    331       C  
ATOM   3405  O   LYS A 291      23.562  38.179  56.851  1.00 74.24           O  
ANISOU 3405  O   LYS A 291     9611   9815   8783     97   -492    298       O  
ATOM   3406  CB  LYS A 291      23.541  37.876  60.052  1.00 74.57           C  
ANISOU 3406  CB  LYS A 291     9996   9780   8558     -1   -613    330       C  
ATOM   3407  CG  LYS A 291      24.422  39.073  59.764  1.00 81.01           C  
ANISOU 3407  CG  LYS A 291    10695  10622   9465     45   -650    291       C  
ATOM   3408  CD  LYS A 291      25.809  38.643  59.346  1.00 84.21           C  
ANISOU 3408  CD  LYS A 291    11038  10986   9973    117   -779    296       C  
ATOM   3409  CE  LYS A 291      26.624  39.820  58.818  1.00 87.02           C  
ANISOU 3409  CE  LYS A 291    11255  11369  10441    164   -790    250       C  
ATOM   3410  NZ  LYS A 291      27.590  39.423  57.750  1.00 81.74           N  
ANISOU 3410  NZ  LYS A 291    10468  10676   9914    230   -837    241       N  
ATOM   3411  N   GLY A 292      23.671  35.982  57.349  1.00 73.29           N  
ANISOU 3411  N   GLY A 292     9639   9614   8595     89   -582    366       N  
ATOM   3412  CA  GLY A 292      24.253  35.636  56.067  1.00 70.75           C  
ANISOU 3412  CA  GLY A 292     9192   9292   8399    145   -592    363       C  
ATOM   3413  C   GLY A 292      23.168  35.546  55.014  1.00 73.33           C  
ANISOU 3413  C   GLY A 292     9454   9661   8746    131   -464    359       C  
ATOM   3414  O   GLY A 292      23.369  35.926  53.851  1.00 63.90           O  
ANISOU 3414  O   GLY A 292     8139   8492   7649    164   -428    339       O  
ATOM   3415  N   MET A 293      22.007  35.033  55.438  1.00 74.15           N  
ANISOU 3415  N   MET A 293     9645   9768   8760     78   -396    376       N  
ATOM   3416  CA  MET A 293      20.821  35.018  54.592  1.00 65.21           C  
ANISOU 3416  CA  MET A 293     8461   8674   7643     58   -274    366       C  
ATOM   3417  C   MET A 293      20.501  36.413  54.069  1.00 66.73           C  
ANISOU 3417  C   MET A 293     8554   8919   7883     60   -207    323       C  
ATOM   3418  O   MET A 293      20.168  36.590  52.891  1.00 62.29           O  
ANISOU 3418  O   MET A 293     7896   8382   7390     79   -151    311       O  
ATOM   3419  CB  MET A 293      19.638  34.467  55.385  1.00 60.77           C  
ANISOU 3419  CB  MET A 293     8014   8101   6975     -8   -208    377       C  
ATOM   3420  CG  MET A 293      18.377  34.314  54.565  1.00 76.49           C  
ANISOU 3420  CG  MET A 293     9952  10120   8990    -29    -91    362       C  
ATOM   3421  SD  MET A 293      18.648  33.065  53.291  1.00101.36           S  
ANISOU 3421  SD  MET A 293    13041  13255  12216     17   -110    392       S  
ATOM   3422  CE  MET A 293      16.973  32.542  52.948  1.00 87.87           C  
ANISOU 3422  CE  MET A 293    11342  11558  10486    -31     16    381       C  
ATOM   3423  N   PHE A 294      20.611  37.417  54.934  1.00 59.85           N  
ANISOU 3423  N   PHE A 294     7709   8058   6971     41   -214    301       N  
ATOM   3424  CA  PHE A 294      20.315  38.784  54.539  1.00 53.13           C  
ANISOU 3424  CA  PHE A 294     6770   7253   6163     42   -154    261       C  
ATOM   3425  C   PHE A 294      21.374  39.321  53.583  1.00 52.72           C  
ANISOU 3425  C   PHE A 294     6604   7210   6216    102   -196    247       C  
ATOM   3426  O   PHE A 294      21.045  39.903  52.542  1.00 62.76           O  
ANISOU 3426  O   PHE A 294     7783   8510   7550    117   -136    228       O  
ATOM   3427  CB  PHE A 294      20.207  39.654  55.790  1.00 55.07           C  
ANISOU 3427  CB  PHE A 294     7081   7506   6337      1   -152    240       C  
ATOM   3428  CG  PHE A 294      19.923  41.088  55.505  1.00 54.46           C  
ANISOU 3428  CG  PHE A 294     6917   7473   6304      0    -93    197       C  
ATOM   3429  CD1 PHE A 294      18.841  41.452  54.706  1.00 52.24           C  
ANISOU 3429  CD1 PHE A 294     6566   7221   6063    -14      5    176       C  
ATOM   3430  CD2 PHE A 294      20.727  42.080  56.033  1.00 57.47           C  
ANISOU 3430  CD2 PHE A 294     7284   7862   6690     13   -140    176       C  
ATOM   3431  CE1 PHE A 294      18.567  42.782  54.440  1.00 51.07           C  
ANISOU 3431  CE1 PHE A 294     6339   7107   5958    -14     53    137       C  
ATOM   3432  CE2 PHE A 294      20.456  43.423  55.775  1.00 66.64           C  
ANISOU 3432  CE2 PHE A 294     8364   9062   7893     11    -83    136       C  
ATOM   3433  CZ  PHE A 294      19.378  43.772  54.973  1.00 64.62           C  
ANISOU 3433  CZ  PHE A 294     8042   8834   7676     -3     12    118       C  
ATOM   3434  N   ASP A 295      22.655  39.134  53.917  1.00 57.92           N  
ANISOU 3434  N   ASP A 295     7272   7836   6898    138   -299    255       N  
ATOM   3435  CA  ASP A 295      23.741  39.569  53.038  1.00 57.79           C  
ANISOU 3435  CA  ASP A 295     7150   7817   6991    192   -333    234       C  
ATOM   3436  C   ASP A 295      23.671  38.884  51.690  1.00 54.96           C  
ANISOU 3436  C   ASP A 295     6726   7454   6701    215   -298    244       C  
ATOM   3437  O   ASP A 295      23.978  39.492  50.658  1.00 60.54           O  
ANISOU 3437  O   ASP A 295     7341   8175   7487    241   -265    220       O  
ATOM   3438  CB  ASP A 295      25.102  39.273  53.663  1.00 72.19           C  
ANISOU 3438  CB  ASP A 295     8995   9594   8840    225   -457    237       C  
ATOM   3439  CG  ASP A 295      25.321  39.990  54.970  1.00 71.16           C  
ANISOU 3439  CG  ASP A 295     8930   9462   8644    206   -506    225       C  
ATOM   3440  OD1 ASP A 295      24.897  41.154  55.109  1.00 75.75           O  
ANISOU 3440  OD1 ASP A 295     9485  10086   9212    187   -446    197       O  
ATOM   3441  OD2 ASP A 295      25.939  39.381  55.854  1.00 73.00           O  
ANISOU 3441  OD2 ASP A 295     9245   9649   8843    210   -610    243       O  
ATOM   3442  N   PHE A 296      23.294  37.609  51.675  1.00 57.44           N  
ANISOU 3442  N   PHE A 296     7095   7746   6984    204   -304    278       N  
ATOM   3443  CA  PHE A 296      23.161  36.924  50.399  1.00 61.66           C  
ANISOU 3443  CA  PHE A 296     7574   8276   7580    221   -266    287       C  
ATOM   3444  C   PHE A 296      21.990  37.480  49.599  1.00 58.89           C  
ANISOU 3444  C   PHE A 296     7181   7968   7226    201   -163    273       C  
ATOM   3445  O   PHE A 296      22.131  37.826  48.415  1.00 60.61           O  
ANISOU 3445  O   PHE A 296     7323   8195   7513    222   -128    258       O  
ATOM   3446  CB  PHE A 296      22.978  35.427  50.616  1.00 62.38           C  
ANISOU 3446  CB  PHE A 296     7733   8333   7636    213   -294    326       C  
ATOM   3447  CG  PHE A 296      22.359  34.743  49.441  1.00 70.71           C  
ANISOU 3447  CG  PHE A 296     8749   9395   8723    213   -230    336       C  
ATOM   3448  CD1 PHE A 296      23.134  34.419  48.328  1.00 60.95           C  
ANISOU 3448  CD1 PHE A 296     7438   8139   7580    248   -240    329       C  
ATOM   3449  CD2 PHE A 296      20.995  34.455  49.421  1.00 69.53           C  
ANISOU 3449  CD2 PHE A 296     8636   9268   8516    175   -155    345       C  
ATOM   3450  CE1 PHE A 296      22.575  33.794  47.233  1.00 48.28           C  
ANISOU 3450  CE1 PHE A 296     5806   6540   6000    245   -182    337       C  
ATOM   3451  CE2 PHE A 296      20.433  33.837  48.324  1.00 64.42           C  
ANISOU 3451  CE2 PHE A 296     7952   8625   7901    177   -103    352       C  
ATOM   3452  CZ  PHE A 296      21.230  33.512  47.223  1.00 54.95           C  
ANISOU 3452  CZ  PHE A 296     6686   7408   6784    212   -119    350       C  
ATOM   3453  N   VAL A 297      20.811  37.525  50.220  1.00 48.66           N  
ANISOU 3453  N   VAL A 297     5941   6691   5855    157   -112    277       N  
ATOM   3454  CA  VAL A 297      19.599  37.930  49.523  1.00 47.80           C  
ANISOU 3454  CA  VAL A 297     5795   6613   5753    137    -24    262       C  
ATOM   3455  C   VAL A 297      19.707  39.358  48.999  1.00 48.14           C  
ANISOU 3455  C   VAL A 297     5761   6686   5846    151      2    227       C  
ATOM   3456  O   VAL A 297      19.040  39.708  48.014  1.00 44.60           O  
ANISOU 3456  O   VAL A 297     5262   6252   5433    152     55    215       O  
ATOM   3457  CB  VAL A 297      18.408  37.700  50.480  1.00 52.95           C  
ANISOU 3457  CB  VAL A 297     6524   7270   6325     83     24    262       C  
ATOM   3458  CG1 VAL A 297      17.268  38.615  50.196  1.00 46.70           C  
ANISOU 3458  CG1 VAL A 297     5690   6509   5547     58    104    228       C  
ATOM   3459  CG2 VAL A 297      17.951  36.245  50.404  1.00 57.18           C  
ANISOU 3459  CG2 VAL A 297     7112   7780   6833     70     32    293       C  
ATOM   3460  N   VAL A 298      20.594  40.172  49.585  1.00 45.94           N  
ANISOU 3460  N   VAL A 298     5473   6409   5573    164    -40    211       N  
ATOM   3461  CA  VAL A 298      20.839  41.513  49.055  1.00 46.24           C  
ANISOU 3461  CA  VAL A 298     5437   6470   5662    181    -18    179       C  
ATOM   3462  C   VAL A 298      21.840  41.483  47.895  1.00 46.63           C  
ANISOU 3462  C   VAL A 298     5422   6500   5794    223    -35    174       C  
ATOM   3463  O   VAL A 298      21.652  42.177  46.887  1.00 45.92           O  
ANISOU 3463  O   VAL A 298     5278   6422   5746    232      8    157       O  
ATOM   3464  CB  VAL A 298      21.302  42.462  50.182  1.00 57.29           C  
ANISOU 3464  CB  VAL A 298     6852   7879   7036    174    -46    158       C  
ATOM   3465  CG1 VAL A 298      21.730  43.843  49.612  1.00 48.80           C  
ANISOU 3465  CG1 VAL A 298     5695   6824   6022    196    -27    124       C  
ATOM   3466  CG2 VAL A 298      20.207  42.621  51.232  1.00 55.76           C  
ANISOU 3466  CG2 VAL A 298     6721   7701   6763    122     -7    154       C  
ATOM   3467  N   VAL A 299      22.920  40.701  47.998  1.00 44.72           N  
ANISOU 3467  N   VAL A 299     5189   6224   5579    248    -98    185       N  
ATOM   3468  CA  VAL A 299      23.896  40.723  46.906  1.00 47.01           C  
ANISOU 3468  CA  VAL A 299     5414   6490   5957    281   -102    170       C  
ATOM   3469  C   VAL A 299      23.282  40.150  45.639  1.00 50.10           C  
ANISOU 3469  C   VAL A 299     5791   6879   6365    277    -48    182       C  
ATOM   3470  O   VAL A 299      23.711  40.497  44.523  1.00 47.15           O  
ANISOU 3470  O   VAL A 299     5369   6494   6051    291    -18    164       O  
ATOM   3471  CB  VAL A 299      25.217  39.998  47.271  1.00 50.69           C  
ANISOU 3471  CB  VAL A 299     5881   6910   6470    309   -183    170       C  
ATOM   3472  CG1 VAL A 299      25.073  38.491  47.209  1.00 62.14           C  
ANISOU 3472  CG1 VAL A 299     7371   8332   7907    306   -207    205       C  
ATOM   3473  CG2 VAL A 299      26.352  40.450  46.364  1.00 39.84           C  
ANISOU 3473  CG2 VAL A 299     4428   5509   5200    339   -177    133       C  
ATOM   3474  N   LEU A 300      22.242  39.323  45.795  1.00 47.55           N  
ANISOU 3474  N   LEU A 300     5514   6564   5987    253    -31    210       N  
ATOM   3475  CA  LEU A 300      21.510  38.796  44.652  1.00 41.26           C  
ANISOU 3475  CA  LEU A 300     4709   5768   5202    247     17    221       C  
ATOM   3476  C   LEU A 300      20.770  39.898  43.883  1.00 43.27           C  
ANISOU 3476  C   LEU A 300     4930   6046   5465    239     72    201       C  
ATOM   3477  O   LEU A 300      20.629  39.807  42.659  1.00 44.70           O  
ANISOU 3477  O   LEU A 300     5091   6216   5676    244    100    199       O  
ATOM   3478  CB  LEU A 300      20.555  37.707  45.135  1.00 45.52           C  
ANISOU 3478  CB  LEU A 300     5304   6308   5683    222     23    250       C  
ATOM   3479  CG  LEU A 300      19.801  36.974  44.031  1.00 48.98           C  
ANISOU 3479  CG  LEU A 300     5735   6741   6132    216     64    262       C  
ATOM   3480  CD1 LEU A 300      20.844  36.450  43.051  1.00 60.47           C  
ANISOU 3480  CD1 LEU A 300     7160   8165   7650    242     50    263       C  
ATOM   3481  CD2 LEU A 300      18.921  35.848  44.586  1.00 41.41           C  
ANISOU 3481  CD2 LEU A 300     4832   5780   5123    192     72    286       C  
ATOM   3482  N   THR A 301      20.319  40.963  44.556  1.00 50.24           N  
ANISOU 3482  N   THR A 301     5809   6956   6324    226     83    183       N  
ATOM   3483  CA  THR A 301      19.768  42.093  43.800  1.00 54.14           C  
ANISOU 3483  CA  THR A 301     6267   7465   6840    224    123    162       C  
ATOM   3484  C   THR A 301      20.852  42.810  42.986  1.00 44.71           C  
ANISOU 3484  C   THR A 301     5033   6255   5700    249    123    142       C  
ATOM   3485  O   THR A 301      20.598  43.261  41.859  1.00 40.92           O  
ANISOU 3485  O   THR A 301     4537   5767   5242    251    153    135       O  
ATOM   3486  CB  THR A 301      19.049  43.077  44.731  1.00 49.29           C  
ANISOU 3486  CB  THR A 301     5652   6880   6196    203    138    143       C  
ATOM   3487  OG1 THR A 301      20.003  43.869  45.460  1.00 57.85           O  
ANISOU 3487  OG1 THR A 301     6722   7970   7286    214    113    126       O  
ATOM   3488  CG2 THR A 301      18.150  42.342  45.694  1.00 40.95           C  
ANISOU 3488  CG2 THR A 301     4643   5830   5086    172    146    154       C  
ATOM   3489  N   TYR A 302      22.073  42.910  43.531  1.00 49.63           N  
ANISOU 3489  N   TYR A 302     5643   6866   6346    267     89    131       N  
ATOM   3490  CA  TYR A 302      23.161  43.559  42.801  1.00 42.87           C  
ANISOU 3490  CA  TYR A 302     4747   5988   5553    288     98    104       C  
ATOM   3491  C   TYR A 302      23.627  42.703  41.628  1.00 47.86           C  
ANISOU 3491  C   TYR A 302     5377   6582   6224    294    114    109       C  
ATOM   3492  O   TYR A 302      23.813  43.214  40.513  1.00 49.10           O  
ANISOU 3492  O   TYR A 302     5522   6722   6413    294    155     93       O  
ATOM   3493  CB  TYR A 302      24.314  43.893  43.756  1.00 40.74           C  
ANISOU 3493  CB  TYR A 302     4458   5712   5311    306     53     83       C  
ATOM   3494  CG  TYR A 302      23.937  45.024  44.691  1.00 44.30           C  
ANISOU 3494  CG  TYR A 302     4906   6199   5729    297     52     69       C  
ATOM   3495  CD1 TYR A 302      23.830  46.333  44.227  1.00 51.21           C  
ANISOU 3495  CD1 TYR A 302     5747   7087   6624    297     92     43       C  
ATOM   3496  CD2 TYR A 302      23.637  44.780  46.016  1.00 53.59           C  
ANISOU 3496  CD2 TYR A 302     6119   7392   6849    284     15     81       C  
ATOM   3497  CE1 TYR A 302      23.461  47.358  45.057  1.00 46.60           C  
ANISOU 3497  CE1 TYR A 302     5155   6535   6016    287     95     28       C  
ATOM   3498  CE2 TYR A 302      23.255  45.802  46.860  1.00 59.36           C  
ANISOU 3498  CE2 TYR A 302     6851   8154   7549    269     22     65       C  
ATOM   3499  CZ  TYR A 302      23.164  47.088  46.376  1.00 56.32           C  
ANISOU 3499  CZ  TYR A 302     6421   7785   7195    272     63     38       C  
ATOM   3500  OH  TYR A 302      22.777  48.099  47.239  1.00 59.32           O  
ANISOU 3500  OH  TYR A 302     6796   8194   7548    255     72     19       O  
ATOM   3501  N   ALA A 303      23.764  41.392  41.839  1.00 50.56           N  
ANISOU 3501  N   ALA A 303     5740   6908   6564    296     86    132       N  
ATOM   3502  CA  ALA A 303      24.127  40.488  40.745  1.00 53.78           C  
ANISOU 3502  CA  ALA A 303     6146   7279   7009    297    105    136       C  
ATOM   3503  C   ALA A 303      23.138  40.526  39.583  1.00 45.66           C  
ANISOU 3503  C   ALA A 303     5138   6255   5957    279    154    146       C  
ATOM   3504  O   ALA A 303      23.467  40.045  38.497  1.00 46.56           O  
ANISOU 3504  O   ALA A 303     5254   6336   6100    276    182    143       O  
ATOM   3505  CB  ALA A 303      24.262  39.046  41.258  1.00 49.91           C  
ANISOU 3505  CB  ALA A 303     5678   6774   6514    300     64    162       C  
ATOM   3506  N   ASN A 304      21.938  41.080  39.777  1.00 60.97           N  
ANISOU 3506  N   ASN A 304     7091   8228   7847    267    163    156       N  
ATOM   3507  CA  ASN A 304      21.042  41.314  38.643  1.00 60.02           C  
ANISOU 3507  CA  ASN A 304     6987   8105   7714    254    196    159       C  
ATOM   3508  C   ASN A 304      21.654  42.271  37.617  1.00 60.76           C  
ANISOU 3508  C   ASN A 304     7074   8173   7840    256    228    134       C  
ATOM   3509  O   ASN A 304      21.415  42.120  36.408  1.00 71.01           O  
ANISOU 3509  O   ASN A 304     8399   9445   9136    245    253    137       O  
ATOM   3510  CB  ASN A 304      19.694  41.850  39.131  1.00 53.70           C  
ANISOU 3510  CB  ASN A 304     6191   7337   6875    242    194    163       C  
ATOM   3511  CG  ASN A 304      18.747  42.139  37.987  1.00 55.12           C  
ANISOU 3511  CG  ASN A 304     6386   7506   7051    232    211    164       C  
ATOM   3512  OD1 ASN A 304      18.247  41.222  37.343  1.00 56.91           O  
ANISOU 3512  OD1 ASN A 304     6634   7718   7269    225    214    180       O  
ATOM   3513  ND2 ASN A 304      18.509  43.416  37.716  1.00 52.68           N  
ANISOU 3513  ND2 ASN A 304     6066   7200   6749    232    217    146       N  
ATOM   3514  N   SER A 305      22.460  43.241  38.062  1.00 45.78           N  
ANISOU 3514  N   SER A 305     5147   6278   5968    267    228    108       N  
ATOM   3515  CA  SER A 305      23.087  44.151  37.105  1.00 52.53           C  
ANISOU 3515  CA  SER A 305     6002   7104   6855    265    267     81       C  
ATOM   3516  C   SER A 305      24.255  43.519  36.336  1.00 56.81           C  
ANISOU 3516  C   SER A 305     6543   7595   7447    264    296     63       C  
ATOM   3517  O   SER A 305      24.598  44.016  35.257  1.00 58.65           O  
ANISOU 3517  O   SER A 305     6798   7793   7695    251    343     44       O  
ATOM   3518  CB  SER A 305      23.541  45.429  37.812  1.00 51.80           C  
ANISOU 3518  CB  SER A 305     5875   7029   6780    277    265     54       C  
ATOM   3519  OG  SER A 305      22.490  45.975  38.592  1.00 67.93           O  
ANISOU 3519  OG  SER A 305     7914   9114   8782    274    243     65       O  
ATOM   3520  N   CYS A 306      24.855  42.428  36.834  1.00 59.48           N  
ANISOU 3520  N   CYS A 306     6863   7924   7814    273    272     67       N  
ATOM   3521  CA  CYS A 306      25.862  41.698  36.056  1.00 49.90           C  
ANISOU 3521  CA  CYS A 306     5644   6656   6660    268    302     46       C  
ATOM   3522  C   CYS A 306      25.266  40.825  34.969  1.00 53.92           C  
ANISOU 3522  C   CYS A 306     6198   7147   7142    246    330     68       C  
ATOM   3523  O   CYS A 306      25.924  40.585  33.950  1.00 56.13           O  
ANISOU 3523  O   CYS A 306     6490   7378   7460    230    380     45       O  
ATOM   3524  CB  CYS A 306      26.720  40.790  36.934  1.00 52.64           C  
ANISOU 3524  CB  CYS A 306     5951   6990   7058    287    257     41       C  
ATOM   3525  SG  CYS A 306      27.306  41.462  38.498  1.00 61.29           S  
ANISOU 3525  SG  CYS A 306     7005   8109   8174    314    195     26       S  
ATOM   3526  N   ALA A 307      24.054  40.305  35.179  1.00 65.77           N  
ANISOU 3526  N   ALA A 307     7724   8682   8584    243    302    107       N  
ATOM   3527  CA  ALA A 307      23.486  39.345  34.238  1.00 61.33           C  
ANISOU 3527  CA  ALA A 307     7200   8102   7999    225    320    128       C  
ATOM   3528  C   ALA A 307      23.054  40.015  32.945  1.00 60.42           C  
ANISOU 3528  C   ALA A 307     7135   7964   7856    203    359    122       C  
ATOM   3529  O   ALA A 307      23.121  39.387  31.881  1.00 56.54           O  
ANISOU 3529  O   ALA A 307     6681   7437   7364    182    392    122       O  
ATOM   3530  CB  ALA A 307      22.300  38.616  34.868  1.00 56.20           C  
ANISOU 3530  CB  ALA A 307     6560   7492   7301    228    281    165       C  
ATOM   3531  N   ASN A 308      22.619  41.285  33.008  1.00 57.29           N  
ANISOU 3531  N   ASN A 308     6747   7586   7437    206    354    117       N  
ATOM   3532  CA  ASN A 308      22.029  41.907  31.824  1.00 49.33           C  
ANISOU 3532  CA  ASN A 308     5798   6552   6392    186    373    118       C  
ATOM   3533  C   ASN A 308      23.000  41.972  30.664  1.00 55.55           C  
ANISOU 3533  C   ASN A 308     6626   7280   7201    162    436     91       C  
ATOM   3534  O   ASN A 308      22.640  41.493  29.574  1.00 61.32           O  
ANISOU 3534  O   ASN A 308     7419   7978   7902    138    453    101       O  
ATOM   3535  CB  ASN A 308      21.479  43.295  32.160  1.00 59.97           C  
ANISOU 3535  CB  ASN A 308     7141   7923   7722    195    353    114       C  
ATOM   3536  CG  ASN A 308      20.208  43.230  32.989  1.00 63.18           C  
ANISOU 3536  CG  ASN A 308     7525   8377   8103    207    303    136       C  
ATOM   3537  OD1 ASN A 308      19.712  42.136  33.331  1.00 48.57           O  
ANISOU 3537  OD1 ASN A 308     5668   6543   6244    208    284    156       O  
ATOM   3538  ND2 ASN A 308      19.682  44.405  33.338  1.00 56.76           N  
ANISOU 3538  ND2 ASN A 308     6700   7583   7283    213    286    129       N  
ATOM   3539  N   PRO A 309      24.221  42.521  30.809  1.00 52.33           N  
ANISOU 3539  N   PRO A 309     6190   6849   6845    164    474     54       N  
ATOM   3540  CA  PRO A 309      25.151  42.530  29.662  1.00 47.97           C  
ANISOU 3540  CA  PRO A 309     5679   6229   6319    132    550     20       C  
ATOM   3541  C   PRO A 309      25.425  41.154  29.087  1.00 45.43           C  
ANISOU 3541  C   PRO A 309     5370   5875   6016    113    576     20       C  
ATOM   3542  O   PRO A 309      25.449  41.004  27.863  1.00 43.72           O  
ANISOU 3542  O   PRO A 309     5227   5609   5776     76    626     13       O  
ATOM   3543  CB  PRO A 309      26.412  43.171  30.251  1.00 42.17           C  
ANISOU 3543  CB  PRO A 309     4883   5481   5658    144    578    -27       C  
ATOM   3544  CG  PRO A 309      25.888  44.038  31.330  1.00 40.44           C  
ANISOU 3544  CG  PRO A 309     4625   5320   5420    175    522    -12       C  
ATOM   3545  CD  PRO A 309      24.786  43.262  31.952  1.00 42.08           C  
ANISOU 3545  CD  PRO A 309     4826   5579   5585    190    457     34       C  
ATOM   3546  N   ILE A 310      25.601  40.138  29.935  1.00 57.32           N  
ANISOU 3546  N   ILE A 310     6815   7405   7558    134    541     30       N  
ATOM   3547  CA  ILE A 310      25.761  38.769  29.439  1.00 56.16           C  
ANISOU 3547  CA  ILE A 310     6676   7232   7431    118    560     34       C  
ATOM   3548  C   ILE A 310      24.516  38.305  28.683  1.00 51.42           C  
ANISOU 3548  C   ILE A 310     6144   6640   6753    101    546     73       C  
ATOM   3549  O   ILE A 310      24.612  37.589  27.679  1.00 57.32           O  
ANISOU 3549  O   ILE A 310     6937   7346   7496     70    588     68       O  
ATOM   3550  CB  ILE A 310      26.084  37.817  30.603  1.00 52.45           C  
ANISOU 3550  CB  ILE A 310     6131   6786   7010    148    511     44       C  
ATOM   3551  CG1 ILE A 310      27.077  38.466  31.549  1.00 57.82           C  
ANISOU 3551  CG1 ILE A 310     6746   7467   7756    173    496     11       C  
ATOM   3552  CG2 ILE A 310      26.596  36.496  30.070  1.00 50.79           C  
ANISOU 3552  CG2 ILE A 310     5916   6534   6847    130    541     34       C  
ATOM   3553  CD1 ILE A 310      27.438  37.606  32.747  1.00 62.14           C  
ANISOU 3553  CD1 ILE A 310     7232   8030   8347    203    433     21       C  
ATOM   3554  N   LEU A 311      23.329  38.686  29.161  1.00 49.91           N  
ANISOU 3554  N   LEU A 311     5959   6499   6506    119    487    107       N  
ATOM   3555  CA  LEU A 311      22.094  38.325  28.472  1.00 43.54           C  
ANISOU 3555  CA  LEU A 311     5210   5696   5636    107    464    138       C  
ATOM   3556  C   LEU A 311      22.057  38.890  27.053  1.00 50.74           C  
ANISOU 3556  C   LEU A 311     6214   6554   6509     71    502    127       C  
ATOM   3557  O   LEU A 311      21.725  38.175  26.101  1.00 59.00           O  
ANISOU 3557  O   LEU A 311     7319   7571   7527     45    516    136       O  
ATOM   3558  CB  LEU A 311      20.903  38.811  29.286  1.00 44.35           C  
ANISOU 3558  CB  LEU A 311     5292   5853   5705    132    399    163       C  
ATOM   3559  CG  LEU A 311      20.530  37.840  30.399  1.00 48.85           C  
ANISOU 3559  CG  LEU A 311     5807   6466   6286    153    363    184       C  
ATOM   3560  CD1 LEU A 311      19.362  38.376  31.198  1.00 46.69           C  
ANISOU 3560  CD1 LEU A 311     5515   6238   5985    170    314    199       C  
ATOM   3561  CD2 LEU A 311      20.191  36.514  29.764  1.00 54.57           C  
ANISOU 3561  CD2 LEU A 311     6557   7176   7003    138    371    200       C  
ATOM   3562  N   TYR A 312      22.423  40.169  26.891  1.00 46.46           N  
ANISOU 3562  N   TYR A 312     5694   5996   5964     67    521    107       N  
ATOM   3563  CA  TYR A 312      22.450  40.790  25.569  1.00 46.31           C  
ANISOU 3563  CA  TYR A 312     5778   5918   5901     29    559     96       C  
ATOM   3564  C   TYR A 312      23.435  40.108  24.619  1.00 49.87           C  
ANISOU 3564  C   TYR A 312     6272   6304   6372    -13    644     67       C  
ATOM   3565  O   TYR A 312      23.198  40.060  23.407  1.00 64.34           O  
ANISOU 3565  O   TYR A 312     8210   8087   8152    -53    670     68       O  
ATOM   3566  CB  TYR A 312      22.826  42.271  25.668  1.00 52.81           C  
ANISOU 3566  CB  TYR A 312     6611   6731   6725     32    573     76       C  
ATOM   3567  CG  TYR A 312      22.076  43.114  26.670  1.00 49.29           C  
ANISOU 3567  CG  TYR A 312     6112   6342   6275     71    505     93       C  
ATOM   3568  CD1 TYR A 312      20.801  42.768  27.113  1.00 48.98           C  
ANISOU 3568  CD1 TYR A 312     6052   6347   6211     92    430    127       C  
ATOM   3569  CD2 TYR A 312      22.660  44.275  27.180  1.00 57.96           C  
ANISOU 3569  CD2 TYR A 312     7177   7447   7399     83    521     70       C  
ATOM   3570  CE1 TYR A 312      20.130  43.560  28.033  1.00 49.74           C  
ANISOU 3570  CE1 TYR A 312     6098   6489   6311    121    379    134       C  
ATOM   3571  CE2 TYR A 312      22.002  45.070  28.109  1.00 51.55           C  
ANISOU 3571  CE2 TYR A 312     6315   6685   6586    114    465     81       C  
ATOM   3572  CZ  TYR A 312      20.734  44.713  28.521  1.00 56.33           C  
ANISOU 3572  CZ  TYR A 312     6903   7330   7168    131    396    113       C  
ATOM   3573  OH  TYR A 312      20.087  45.499  29.435  1.00 52.81           O  
ANISOU 3573  OH  TYR A 312     6408   6930   6729    155    352    117       O  
ATOM   3574  N   ALA A 313      24.553  39.609  25.133  1.00 44.32           N  
ANISOU 3574  N   ALA A 313     5496   5597   5749     -9    688     36       N  
ATOM   3575  CA  ALA A 313      25.543  38.978  24.271  1.00 44.08           C  
ANISOU 3575  CA  ALA A 313     5493   5498   5756    -52    778     -3       C  
ATOM   3576  C   ALA A 313      25.028  37.683  23.641  1.00 60.35           C  
ANISOU 3576  C   ALA A 313     7590   7549   7790    -73    776     19       C  
ATOM   3577  O   ALA A 313      25.459  37.327  22.536  1.00 64.18           O  
ANISOU 3577  O   ALA A 313     8146   7970   8268   -124    850     -6       O  
ATOM   3578  CB  ALA A 313      26.826  38.720  25.065  1.00 44.09           C  
ANISOU 3578  CB  ALA A 313     5390   5492   5868    -36    810    -46       C  
ATOM   3579  N   PHE A 314      24.115  36.966  24.309  1.00 59.83           N  
ANISOU 3579  N   PHE A 314     7482   7543   7710    -39    700     61       N  
ATOM   3580  CA  PHE A 314      23.602  35.702  23.788  1.00 59.74           C  
ANISOU 3580  CA  PHE A 314     7495   7525   7678    -55    696     81       C  
ATOM   3581  C   PHE A 314      22.241  35.827  23.124  1.00 56.75           C  
ANISOU 3581  C   PHE A 314     7200   7154   7209    -62    644    117       C  
ATOM   3582  O   PHE A 314      21.836  34.909  22.399  1.00 69.40           O  
ANISOU 3582  O   PHE A 314     8847   8738   8784    -86    650    128       O  
ATOM   3583  CB  PHE A 314      23.522  34.644  24.899  1.00 63.08           C  
ANISOU 3583  CB  PHE A 314     7820   7998   8150    -18    653    100       C  
ATOM   3584  CG  PHE A 314      24.856  34.107  25.308  1.00 65.64           C  
ANISOU 3584  CG  PHE A 314     8071   8296   8572    -17    698     63       C  
ATOM   3585  CD1 PHE A 314      25.868  33.937  24.364  1.00 67.09           C  
ANISOU 3585  CD1 PHE A 314     8284   8408   8800    -62    789     16       C  
ATOM   3586  CD2 PHE A 314      25.114  33.787  26.635  1.00 68.26           C  
ANISOU 3586  CD2 PHE A 314     8311   8669   8957     26    648     72       C  
ATOM   3587  CE1 PHE A 314      27.122  33.440  24.731  1.00 70.90           C  
ANISOU 3587  CE1 PHE A 314     8688   8858   9393    -62    829    -27       C  
ATOM   3588  CE2 PHE A 314      26.361  33.293  27.022  1.00 66.65           C  
ANISOU 3588  CE2 PHE A 314     8037   8432   8854     30    674     36       C  
ATOM   3589  CZ  PHE A 314      27.373  33.124  26.063  1.00 75.28           C  
ANISOU 3589  CZ  PHE A 314     9144   9451  10006    -12    764    -17       C  
ATOM   3590  N   LEU A 315      21.542  36.935  23.326  1.00 51.84           N  
ANISOU 3590  N   LEU A 315     6598   6554   6545    -43    590    132       N  
ATOM   3591  CA  LEU A 315      20.183  37.077  22.828  1.00 53.65           C  
ANISOU 3591  CA  LEU A 315     6891   6788   6706    -42    522    163       C  
ATOM   3592  C   LEU A 315      20.014  38.217  21.854  1.00 53.77           C  
ANISOU 3592  C   LEU A 315     7016   6752   6661    -68    521    159       C  
ATOM   3593  O   LEU A 315      18.903  38.409  21.342  1.00 74.26           O  
ANISOU 3593  O   LEU A 315     9674   9339   9204    -68    454    181       O  
ATOM   3594  CB  LEU A 315      19.190  37.291  23.980  1.00 44.97           C  
ANISOU 3594  CB  LEU A 315     5715   5757   5616      7    440    188       C  
ATOM   3595  CG  LEU A 315      19.254  36.250  25.080  1.00 55.80           C  
ANISOU 3595  CG  LEU A 315     6988   7178   7036     34    433    197       C  
ATOM   3596  CD1 LEU A 315      18.725  36.859  26.366  1.00 56.17           C  
ANISOU 3596  CD1 LEU A 315     6963   7282   7097     73    381    207       C  
ATOM   3597  CD2 LEU A 315      18.474  35.020  24.665  1.00 54.41           C  
ANISOU 3597  CD2 LEU A 315     6828   7003   6843     26    415    216       C  
ATOM   3598  N   ASP A 316      21.049  39.001  21.618  1.00 50.43           N  
ANISOU 3598  N   ASP A 316     6620   6292   6250    -90    588    128       N  
ATOM   3599  CA  ASP A 316      21.012  40.055  20.619  1.00 48.24           C  
ANISOU 3599  CA  ASP A 316     6465   5954   5909   -123    598    122       C  
ATOM   3600  C   ASP A 316      22.240  39.891  19.748  1.00 56.07           C  
ANISOU 3600  C   ASP A 316     7523   6874   6906   -181    715     82       C  
ATOM   3601  O   ASP A 316      23.351  39.761  20.273  1.00 68.91           O  
ANISOU 3601  O   ASP A 316     9072   8503   8608   -179    784     47       O  
ATOM   3602  CB  ASP A 316      21.004  41.421  21.284  1.00 51.43           C  
ANISOU 3602  CB  ASP A 316     6836   6380   6323    -94    570    120       C  
ATOM   3603  CG  ASP A 316      20.665  42.524  20.330  1.00 63.49           C  
ANISOU 3603  CG  ASP A 316     8492   7850   7779   -120    553    124       C  
ATOM   3604  OD1 ASP A 316      21.287  42.615  19.257  1.00 74.30           O  
ANISOU 3604  OD1 ASP A 316     9976   9146   9110   -174    625    104       O  
ATOM   3605  OD2 ASP A 316      19.763  43.313  20.649  1.00 72.21           O  
ANISOU 3605  OD2 ASP A 316     9590   8978   8868    -89    469    146       O  
ATOM   3606  N   ASP A 317      22.049  39.880  18.428  1.00 55.11           N  
ANISOU 3606  N   ASP A 317     7548   6684   6709   -233    737     82       N  
ATOM   3607  CA  ASP A 317      23.199  39.715  17.539  1.00 52.42           C  
ANISOU 3607  CA  ASP A 317     7282   6264   6370   -299    862     37       C  
ATOM   3608  C   ASP A 317      24.039  40.985  17.470  1.00 52.08           C  
ANISOU 3608  C   ASP A 317     7272   6181   6335   -317    927      3       C  
ATOM   3609  O   ASP A 317      25.271  40.925  17.390  1.00 64.66           O  
ANISOU 3609  O   ASP A 317     8844   7734   7988   -348   1040    -50       O  
ATOM   3610  CB  ASP A 317      22.738  39.303  16.145  1.00 65.42           C  
ANISOU 3610  CB  ASP A 317     9090   7844   7924   -357    870     48       C  
ATOM   3611  CG  ASP A 317      22.231  37.870  16.101  1.00 86.44           C  
ANISOU 3611  CG  ASP A 317    11716  10534  10595   -352    842     66       C  
ATOM   3612  OD1 ASP A 317      22.725  37.046  16.908  1.00 94.32           O  
ANISOU 3612  OD1 ASP A 317    12582  11576  11681   -327    870     53       O  
ATOM   3613  OD2 ASP A 317      21.351  37.571  15.258  1.00 90.61           O  
ANISOU 3613  OD2 ASP A 317    12350  11035  11042   -373    790     92       O  
ATOM   3614  N   ASN A 318      23.400  42.142  17.521  1.00 54.25           N  
ANISOU 3614  N   ASN A 318     7592   6462   6559   -296    858     27       N  
ATOM   3615  CA  ASN A 318      24.159  43.374  17.398  1.00 50.92           C  
ANISOU 3615  CA  ASN A 318     7211   5998   6138   -316    922     -5       C  
ATOM   3616  C   ASN A 318      24.982  43.634  18.638  1.00 52.14           C  
ANISOU 3616  C   ASN A 318     7206   6204   6401   -274    951    -35       C  
ATOM   3617  O   ASN A 318      26.130  44.078  18.537  1.00 46.21           O  
ANISOU 3617  O   ASN A 318     6453   5409   5696   -302   1055    -87       O  
ATOM   3618  CB  ASN A 318      23.214  44.517  17.096  1.00 57.93           C  
ANISOU 3618  CB  ASN A 318     8192   6874   6945   -305    833     31       C  
ATOM   3619  CG  ASN A 318      22.488  44.296  15.790  1.00 77.11           C  
ANISOU 3619  CG  ASN A 318    10796   9237   9266   -351    798     56       C  
ATOM   3620  OD1 ASN A 318      23.034  44.557  14.718  1.00 77.01           O  
ANISOU 3620  OD1 ASN A 318    10932   9134   9193   -419    880     33       O  
ATOM   3621  ND2 ASN A 318      21.284  43.728  15.865  1.00 81.29           N  
ANISOU 3621  ND2 ASN A 318    11311   9804   9771   -319    683     99       N  
ATOM   3622  N   PHE A 319      24.432  43.331  19.816  1.00 51.71           N  
ANISOU 3622  N   PHE A 319     7020   6239   6391   -209    864     -6       N  
ATOM   3623  CA  PHE A 319      25.246  43.410  21.021  1.00 52.39           C  
ANISOU 3623  CA  PHE A 319     6958   6370   6576   -171    885    -34       C  
ATOM   3624  C   PHE A 319      26.398  42.417  20.952  1.00 49.82           C  
ANISOU 3624  C   PHE A 319     6584   6014   6331   -196    978    -80       C  
ATOM   3625  O   PHE A 319      27.530  42.763  21.313  1.00 51.16           O  
ANISOU 3625  O   PHE A 319     6692   6163   6582   -198   1047   -131       O  
ATOM   3626  CB  PHE A 319      24.383  43.201  22.271  1.00 52.99           C  
ANISOU 3626  CB  PHE A 319     6921   6540   6672   -105    777      6       C  
ATOM   3627  CG  PHE A 319      23.710  44.464  22.743  1.00 53.41           C  
ANISOU 3627  CG  PHE A 319     6969   6626   6697    -74    710     26       C  
ATOM   3628  CD1 PHE A 319      24.458  45.500  23.306  1.00 49.96           C  
ANISOU 3628  CD1 PHE A 319     6486   6194   6304    -61    744     -4       C  
ATOM   3629  CD2 PHE A 319      22.341  44.641  22.587  1.00 49.59           C  
ANISOU 3629  CD2 PHE A 319     6527   6162   6152    -58    615     70       C  
ATOM   3630  CE1 PHE A 319      23.850  46.685  23.719  1.00 45.02           C  
ANISOU 3630  CE1 PHE A 319     5854   5595   5656    -34    687     12       C  
ATOM   3631  CE2 PHE A 319      21.722  45.820  23.010  1.00 48.49           C  
ANISOU 3631  CE2 PHE A 319     6379   6046   6001    -31    555     83       C  
ATOM   3632  CZ  PHE A 319      22.485  46.843  23.585  1.00 45.72           C  
ANISOU 3632  CZ  PHE A 319     5980   5702   5688    -19    593     55       C  
ATOM   3633  N   LYS A 320      26.136  41.204  20.431  1.00 44.70           N  
ANISOU 3633  N   LYS A 320     5963   5353   5667   -218    982    -68       N  
ATOM   3634  CA  LYS A 320      27.166  40.172  20.291  1.00 45.08           C  
ANISOU 3634  CA  LYS A 320     5965   5366   5798   -245   1068   -113       C  
ATOM   3635  C   LYS A 320      28.261  40.597  19.312  1.00 53.02           C  
ANISOU 3635  C   LYS A 320     7052   6274   6821   -314   1204   -177       C  
ATOM   3636  O   LYS A 320      29.459  40.408  19.573  1.00 44.87           O  
ANISOU 3636  O   LYS A 320     5942   5210   5898   -323   1284   -238       O  
ATOM   3637  CB  LYS A 320      26.536  38.854  19.827  1.00 45.78           C  
ANISOU 3637  CB  LYS A 320     6082   5460   5855   -259   1046    -83       C  
ATOM   3638  CG  LYS A 320      27.540  37.712  19.642  1.00 46.36           C  
ANISOU 3638  CG  LYS A 320     6105   5492   6017   -289   1132   -129       C  
ATOM   3639  CD  LYS A 320      26.856  36.441  19.197  1.00 60.81           C  
ANISOU 3639  CD  LYS A 320     7962   7330   7812   -301   1107    -98       C  
ATOM   3640  CE  LYS A 320      27.644  35.214  19.641  1.00 77.08           C  
ANISOU 3640  CE  LYS A 320     9913   9389   9986   -296   1143   -127       C  
ATOM   3641  NZ  LYS A 320      28.424  34.562  18.542  1.00 77.71           N  
ANISOU 3641  NZ  LYS A 320    10049   9382  10096   -369   1264   -180       N  
ATOM   3642  N   LYS A 321      27.864  41.150  18.164  1.00 48.45           N  
ANISOU 3642  N   LYS A 321     6633   5638   6137   -364   1230   -169       N  
ATOM   3643  CA  LYS A 321      28.850  41.615  17.198  1.00 49.94           C  
ANISOU 3643  CA  LYS A 321     6920   5726   6328   -438   1368   -232       C  
ATOM   3644  C   LYS A 321      29.661  42.788  17.743  1.00 48.81           C  
ANISOU 3644  C   LYS A 321     6724   5574   6247   -423   1412   -274       C  
ATOM   3645  O   LYS A 321      30.871  42.858  17.522  1.00 58.13           O  
ANISOU 3645  O   LYS A 321     7887   6689   7511   -463   1535   -349       O  
ATOM   3646  CB  LYS A 321      28.156  42.008  15.896  1.00 50.07           C  
ANISOU 3646  CB  LYS A 321     7138   5682   6202   -495   1372   -205       C  
ATOM   3647  CG  LYS A 321      28.144  40.928  14.855  1.00 70.65           C  
ANISOU 3647  CG  LYS A 321     9839   8233   8771   -558   1429   -214       C  
ATOM   3648  CD  LYS A 321      27.370  41.392  13.630  1.00 85.16           C  
ANISOU 3648  CD  LYS A 321    11888  10011  10457   -610   1409   -182       C  
ATOM   3649  CE  LYS A 321      25.910  40.965  13.721  1.00 84.07           C  
ANISOU 3649  CE  LYS A 321    11761   9935  10245   -565   1254   -106       C  
ATOM   3650  NZ  LYS A 321      25.056  41.855  12.891  1.00 77.30           N  
ANISOU 3650  NZ  LYS A 321    11081   9034   9255   -586   1188    -68       N  
ATOM   3651  N   SER A 322      29.008  43.734  18.438  1.00 52.65           N  
ANISOU 3651  N   SER A 322     7183   6122   6700   -369   1316   -233       N  
ATOM   3652  CA  SER A 322      29.728  44.864  19.032  1.00 51.93           C  
ANISOU 3652  CA  SER A 322     7033   6030   6668   -350   1349   -271       C  
ATOM   3653  C   SER A 322      30.706  44.408  20.108  1.00 51.64           C  
ANISOU 3653  C   SER A 322     6821   6023   6779   -312   1368   -317       C  
ATOM   3654  O   SER A 322      31.837  44.902  20.166  1.00 54.79           O  
ANISOU 3654  O   SER A 322     7182   6373   7263   -329   1461   -387       O  
ATOM   3655  CB  SER A 322      28.755  45.881  19.640  1.00 46.93           C  
ANISOU 3655  CB  SER A 322     6393   5462   5975   -296   1234   -216       C  
ATOM   3656  OG  SER A 322      27.889  46.438  18.675  1.00 49.80           O  
ANISOU 3656  OG  SER A 322     6917   5789   6213   -327   1204   -178       O  
ATOM   3657  N   PHE A 323      30.269  43.497  20.989  1.00 43.69           N  
ANISOU 3657  N   PHE A 323     5706   5091   5804   -259   1275   -280       N  
ATOM   3658  CA  PHE A 323      31.140  42.974  22.028  1.00 44.13           C  
ANISOU 3658  CA  PHE A 323     5604   5169   5992   -222   1273   -317       C  
ATOM   3659  C   PHE A 323      32.364  42.288  21.429  1.00 45.61           C  
ANISOU 3659  C   PHE A 323     5779   5269   6280   -273   1397   -394       C  
ATOM   3660  O   PHE A 323      33.495  42.482  21.894  1.00 44.53           O  
ANISOU 3660  O   PHE A 323     5548   5103   6268   -266   1448   -461       O  
ATOM   3661  CB  PHE A 323      30.369  41.989  22.923  1.00 54.27           C  
ANISOU 3661  CB  PHE A 323     6808   6537   7274   -167   1157   -258       C  
ATOM   3662  CG  PHE A 323      29.329  42.629  23.815  1.00 45.53           C  
ANISOU 3662  CG  PHE A 323     5675   5517   6106   -111   1041   -198       C  
ATOM   3663  CD1 PHE A 323      29.145  44.011  23.842  1.00 45.07           C  
ANISOU 3663  CD1 PHE A 323     5653   5464   6007   -106   1036   -197       C  
ATOM   3664  CD2 PHE A 323      28.526  41.843  24.616  1.00 42.81           C  
ANISOU 3664  CD2 PHE A 323     5273   5245   5748    -68    942   -146       C  
ATOM   3665  CE1 PHE A 323      28.183  44.599  24.663  1.00 42.63           C  
ANISOU 3665  CE1 PHE A 323     5315   5230   5652    -58    935   -148       C  
ATOM   3666  CE2 PHE A 323      27.559  42.424  25.441  1.00 51.35           C  
ANISOU 3666  CE2 PHE A 323     6330   6400   6780    -23    848    -99       C  
ATOM   3667  CZ  PHE A 323      27.394  43.811  25.466  1.00 43.32           C  
ANISOU 3667  CZ  PHE A 323     5342   5386   5730    -18    844   -102       C  
ATOM   3668  N   GLN A 324      32.163  41.467  20.404  1.00 49.09           N  
ANISOU 3668  N   GLN A 324     6310   5666   6678   -326   1446   -391       N  
ATOM   3669  CA  GLN A 324      33.312  40.761  19.858  1.00 53.93           C  
ANISOU 3669  CA  GLN A 324     6902   6193   7396   -379   1569   -470       C  
ATOM   3670  C   GLN A 324      34.218  41.732  19.114  1.00 59.53           C  
ANISOU 3670  C   GLN A 324     7682   6809   8129   -440   1708   -546       C  
ATOM   3671  O   GLN A 324      35.450  41.570  19.114  1.00 66.76           O  
ANISOU 3671  O   GLN A 324     8525   7657   9183   -465   1808   -634       O  
ATOM   3672  CB  GLN A 324      32.851  39.580  18.986  1.00 53.43           C  
ANISOU 3672  CB  GLN A 324     6914   6107   7281   -423   1589   -448       C  
ATOM   3673  CG  GLN A 324      32.120  39.972  17.721  1.00 72.03           C  
ANISOU 3673  CG  GLN A 324     9460   8422   9484   -483   1622   -420       C  
ATOM   3674  CD  GLN A 324      31.447  38.789  17.005  1.00 75.80           C  
ANISOU 3674  CD  GLN A 324    10007   8896   9898   -514   1610   -384       C  
ATOM   3675  OE1 GLN A 324      30.637  38.061  17.597  1.00 68.06           O  
ANISOU 3675  OE1 GLN A 324     8965   7993   8900   -461   1499   -325       O  
ATOM   3676  NE2 GLN A 324      31.773  38.613  15.715  1.00 57.75           N  
ANISOU 3676  NE2 GLN A 324     7855   6517   7572   -602   1728   -424       N  
ATOM   3677  N   ASN A 325      33.641  42.786  18.544  1.00 52.77           N  
ANISOU 3677  N   ASN A 325     6958   5942   7148   -462   1711   -517       N  
ATOM   3678  CA  ASN A 325      34.455  43.858  17.983  1.00 56.22           C  
ANISOU 3678  CA  ASN A 325     7463   6297   7602   -513   1835   -585       C  
ATOM   3679  C   ASN A 325      35.442  44.433  19.006  1.00 60.00           C  
ANISOU 3679  C   ASN A 325     7788   6784   8225   -469   1848   -645       C  
ATOM   3680  O   ASN A 325      36.571  44.783  18.653  1.00 55.21           O  
ANISOU 3680  O   ASN A 325     7175   6090   7712   -515   1982   -737       O  
ATOM   3681  CB  ASN A 325      33.549  44.963  17.430  1.00 49.02           C  
ANISOU 3681  CB  ASN A 325     6707   5388   6531   -526   1801   -530       C  
ATOM   3682  CG  ASN A 325      34.290  45.914  16.512  1.00 50.02           C  
ANISOU 3682  CG  ASN A 325     6956   5407   6641   -602   1948   -595       C  
ATOM   3683  OD1 ASN A 325      34.358  47.108  16.768  1.00 57.27           O  
ANISOU 3683  OD1 ASN A 325     7885   6330   7546   -586   1945   -599       O  
ATOM   3684  ND2 ASN A 325      34.839  45.391  15.437  1.00 53.18           N  
ANISOU 3684  ND2 ASN A 325     7455   5709   7043   -689   2081   -649       N  
ATOM   3685  N   VAL A 326      35.042  44.551  20.275  1.00 63.46           N  
ANISOU 3685  N   VAL A 326     8105   7321   8685   -384   1715   -599       N  
ATOM   3686  CA  VAL A 326      35.972  45.090  21.265  1.00 61.16           C  
ANISOU 3686  CA  VAL A 326     7672   7037   8528   -341   1717   -656       C  
ATOM   3687  C   VAL A 326      36.856  43.986  21.838  1.00 57.72           C  
ANISOU 3687  C   VAL A 326     7092   6587   8254   -322   1719   -707       C  
ATOM   3688  O   VAL A 326      38.064  44.170  22.006  1.00 59.01           O  
ANISOU 3688  O   VAL A 326     7171   6687   8564   -332   1797   -800       O  
ATOM   3689  CB  VAL A 326      35.204  45.838  22.379  1.00 60.84           C  
ANISOU 3689  CB  VAL A 326     7578   7101   8436   -264   1579   -589       C  
ATOM   3690  CG1 VAL A 326      36.014  45.870  23.683  1.00 58.79           C  
ANISOU 3690  CG1 VAL A 326     7145   6872   8320   -204   1534   -630       C  
ATOM   3691  CG2 VAL A 326      34.867  47.246  21.948  1.00 46.15           C  
ANISOU 3691  CG2 VAL A 326     5822   5230   6484   -282   1607   -578       C  
ATOM   3692  N   LEU A 327      36.281  42.824  22.124  1.00 52.64           N  
ANISOU 3692  N   LEU A 327     6416   5992   7594   -297   1634   -654       N  
ATOM   3693  CA  LEU A 327      36.981  41.802  22.889  1.00 52.21           C  
ANISOU 3693  CA  LEU A 327     6215   5937   7686   -263   1598   -687       C  
ATOM   3694  C   LEU A 327      37.771  40.827  22.030  1.00 60.92           C  
ANISOU 3694  C   LEU A 327     7320   6944   8883   -325   1714   -757       C  
ATOM   3695  O   LEU A 327      38.669  40.164  22.555  1.00 75.09           O  
ANISOU 3695  O   LEU A 327     8986   8706  10838   -306   1712   -814       O  
ATOM   3696  CB  LEU A 327      35.981  41.028  23.759  1.00 48.47           C  
ANISOU 3696  CB  LEU A 327     5699   5564   7153   -200   1445   -594       C  
ATOM   3697  CG  LEU A 327      35.296  41.883  24.831  1.00 47.23           C  
ANISOU 3697  CG  LEU A 327     5513   5502   6931   -135   1327   -535       C  
ATOM   3698  CD1 LEU A 327      34.195  41.147  25.552  1.00 49.42           C  
ANISOU 3698  CD1 LEU A 327     5773   5870   7134    -87   1195   -446       C  
ATOM   3699  CD2 LEU A 327      36.320  42.409  25.820  1.00 46.16           C  
ANISOU 3699  CD2 LEU A 327     5252   5358   6929    -95   1311   -594       C  
ATOM   3700  N   CYS A 328      37.472  40.733  20.736  1.00 61.91           N  
ANISOU 3700  N   CYS A 328     7589   7017   8917   -400   1812   -757       N  
ATOM   3701  CA  CYS A 328      38.122  39.788  19.830  1.00 57.25           C  
ANISOU 3701  CA  CYS A 328     7017   6334   8402   -470   1932   -822       C  
ATOM   3702  C   CYS A 328      39.212  40.510  19.029  1.00 73.31           C  
ANISOU 3702  C   CYS A 328     9094   8250  10510   -545   2109   -932       C  
ATOM   3703  O   CYS A 328      38.938  41.507  18.345  1.00 72.03           O  
ANISOU 3703  O   CYS A 328     9068   8065  10236   -587   2170   -925       O  
ATOM   3704  CB  CYS A 328      37.087  39.167  18.888  1.00 52.49           C  
ANISOU 3704  CB  CYS A 328     6556   5743   7645   -513   1932   -755       C  
ATOM   3705  SG  CYS A 328      36.101  37.813  19.592  1.00 78.02           S  
ANISOU 3705  SG  CYS A 328     9723   9076  10844   -449   1775   -661       S  
ATOM   3706  N   LEU A 329      40.441  40.009  19.104  1.00 74.57           N  
ANISOU 3706  N   LEU A 329     9140   8329  10864   -564   2192  -1036       N  
ATOM   3707  CA  LEU A 329      41.586  40.680  18.491  1.00 71.69           C  
ANISOU 3707  CA  LEU A 329     8789   7847  10604   -632   2365  -1156       C  
ATOM   3708  C   LEU A 329      41.816  40.206  17.055  1.00 66.33           C  
ANISOU 3708  C   LEU A 329     8240   7061   9900   -744   2536  -1209       C  
ATOM   3709  O   LEU A 329      41.673  39.019  16.753  1.00 82.32           O  
ANISOU 3709  O   LEU A 329    10258   9079  11942   -764   2536  -1200       O  
ATOM   3710  CB  LEU A 329      42.840  40.434  19.333  1.00 74.74           C  
ANISOU 3710  CB  LEU A 329     8975   8189  11234   -594   2367  -1254       C  
ATOM   3711  CG  LEU A 329      43.200  41.380  20.490  1.00 70.47           C  
ANISOU 3711  CG  LEU A 329     8321   7692  10765   -518   2282  -1266       C  
ATOM   3712  CD1 LEU A 329      41.994  41.748  21.333  1.00 78.62           C  
ANISOU 3712  CD1 LEU A 329     9372   8863  11637   -438   2105  -1136       C  
ATOM   3713  CD2 LEU A 329      44.256  40.745  21.366  1.00 72.97           C  
ANISOU 3713  CD2 LEU A 329     8438   7972  11316   -472   2240  -1344       C  
ATOM   3714  N   VAL A 330      42.177  41.139  16.172  1.00 61.09           N  
ANISOU 3714  N   VAL A 330     7702   6314   9195   -822   2686  -1266       N  
ATOM   3715  CA  VAL A 330      42.551  40.815  14.791  1.00 78.85           C  
ANISOU 3715  CA  VAL A 330    10087   8443  11427   -942   2873  -1334       C  
ATOM   3716  C   VAL A 330      44.015  41.188  14.529  1.00 82.41           C  
ANISOU 3716  C   VAL A 330    10478   8761  12072  -1003   3059  -1490       C  
ATOM   3717  O   VAL A 330      44.801  41.345  15.468  1.00 83.95           O  
ANISOU 3717  O   VAL A 330    10491   8957  12449   -944   3026  -1550       O  
ATOM   3718  CB  VAL A 330      41.601  41.506  13.786  1.00 87.36           C  
ANISOU 3718  CB  VAL A 330    11410   9520  12262   -999   2900  -1263       C  
ATOM   3719  CG1 VAL A 330      40.151  41.211  14.138  1.00 66.85           C  
ANISOU 3719  CG1 VAL A 330     8852   7053   9496   -930   2707  -1117       C  
ATOM   3720  CG2 VAL A 330      41.835  43.025  13.724  1.00 88.23           C  
ANISOU 3720  CG2 VAL A 330    11592   9603  12330  -1011   2956  -1288       C  
ATOM   3721  N   LYS A 331      44.407  41.320  13.263  1.00 89.30           N  
ANISOU 3721  N   LYS A 331    11503   9514  12914  -1123   3256  -1563       N  
ATOM   3722  CA  LYS A 331      45.787  41.702  12.932  1.00 83.55           C  
ANISOU 3722  CA  LYS A 331    10728   8647  12371  -1193   3454  -1722       C  
ATOM   3723  C   LYS A 331      45.892  42.478  11.624  1.00 77.05           C  
ANISOU 3723  C   LYS A 331    10137   7714  11424  -1317   3649  -1766       C  
ATOM   3724  O   LYS A 331      46.808  43.285  11.449  1.00 89.45           O  
ANISOU 3724  O   LYS A 331    11703   9190  13094  -1363   3796  -1875       O  
ATOM   3725  CB  LYS A 331      46.679  40.464  12.876  1.00 79.42           C  
ANISOU 3725  CB  LYS A 331    10065   8046  12066  -1223   3532  -1824       C  
TER    3726      LYS A 331                                                      
HETATM 3727  N1  EPE A1201     -10.163  10.549   7.297  1.00 86.46           N  
ANISOU 3727  N1  EPE A1201    10984  10314  11552     65  -1026   -406       N  
HETATM 3728  C2  EPE A1201      -8.755  10.119   7.248  1.00 88.71           C  
ANISOU 3728  C2  EPE A1201    11342  10662  11700     14   -877   -332       C  
HETATM 3729  C3  EPE A1201      -8.379   9.582   5.873  1.00100.21           C  
ANISOU 3729  C3  EPE A1201    12950  12084  13041    -35   -908   -313       C  
HETATM 3730  N4  EPE A1201      -9.366   8.628   5.414  1.00 96.89           N  
ANISOU 3730  N4  EPE A1201    12484  11629  12701    -22   -960   -372       N  
HETATM 3731  C5  EPE A1201     -10.757   9.021   5.462  1.00 95.72           C  
ANISOU 3731  C5  EPE A1201    12262  11418  12689     32  -1114   -445       C  
HETATM 3732  C6  EPE A1201     -11.118   9.519   6.852  1.00 89.80           C  
ANISOU 3732  C6  EPE A1201    11355  10704  12062     77  -1067   -469       C  
HETATM 3733  C7  EPE A1201      -8.961   7.564   4.523  1.00 88.18           C  
ANISOU 3733  C7  EPE A1201    11460  10527  11519    -70   -908   -360       C  
HETATM 3734  C8  EPE A1201      -9.442   6.216   5.034  1.00 73.51           C  
ANISOU 3734  C8  EPE A1201     9454   8708   9767    -54   -809   -401       C  
HETATM 3735  O8  EPE A1201     -10.485   5.781   4.200  1.00 70.43           O  
ANISOU 3735  O8  EPE A1201     9077   8252   9431    -42   -934   -461       O  
HETATM 3736  C9  EPE A1201     -10.478  10.851   8.695  1.00 87.17           C  
ANISOU 3736  C9  EPE A1201    10919  10445  11757    102   -958   -430       C  
HETATM 3737  C10 EPE A1201     -10.038  12.277   8.980  1.00 95.81           C  
ANISOU 3737  C10 EPE A1201    12062  11534  12806    108  -1004   -394       C  
HETATM 3738  S   EPE A1201     -11.001  13.028  10.312  1.00111.27           S  
ANISOU 3738  S   EPE A1201    13850  13489  14939    161  -1021   -456       S  
HETATM 3739  O1S EPE A1201     -12.410  13.031   9.915  1.00107.92           O  
ANISOU 3739  O1S EPE A1201    13368  12981  14654    197  -1167   -543       O  
HETATM 3740  O2S EPE A1201     -10.533  14.395  10.535  1.00 99.96           O  
ANISOU 3740  O2S EPE A1201    12470  12054  13458    165  -1065   -419       O  
HETATM 3741  O3S EPE A1201     -10.848  12.258  11.540  1.00110.25           O  
ANISOU 3741  O3S EPE A1201    13592  13433  14864    162   -845   -461       O  
HETATM 3742  N12 GI9 A1202      19.133  48.389  47.076  1.00 72.30           N  
ANISOU 3742  N12 GI9 A1202     8462   9880   9130    179    181     26       N  
HETATM 3743  C13 GI9 A1202      17.417  43.719  59.277  1.00 68.59           C  
ANISOU 3743  C13 GI9 A1202     8920   9288   7851   -233    128     83       C  
HETATM 3744  C14 GI9 A1202      17.123  44.969  59.952  1.00 55.36           C  
ANISOU 3744  C14 GI9 A1202     7238   7633   6162   -273    180     37       C  
HETATM 3745  C15 GI9 A1202      16.608  43.535  58.051  1.00 68.68           C  
ANISOU 3745  C15 GI9 A1202     8829   9318   7948   -215    195     76       C  
HETATM 3746  C16 GI9 A1202      17.634  46.069  59.073  1.00 52.44           C  
ANISOU 3746  C16 GI9 A1202     6722   7305   5898   -215    164     17       C  
HETATM 3747  C17 GI9 A1202      16.150  44.850  57.460  1.00 69.46           C  
ANISOU 3747  C17 GI9 A1202     8804   9455   8131   -208    256     31       C  
HETATM 3748  C18 GI9 A1202      17.902  41.393  60.217  1.00 56.14           C  
ANISOU 3748  C18 GI9 A1202     7569   7629   6132   -252     25    162       C  
HETATM 3749  C19 GI9 A1202      17.437  46.913  56.672  1.00 59.47           C  
ANISOU 3749  C19 GI9 A1202     7369   8244   6984   -128    201      1       C  
HETATM 3750  C20 GI9 A1202      17.311  47.798  54.413  1.00 57.06           C  
ANISOU 3750  C20 GI9 A1202     6864   7970   6845    -52    227    -13       C  
HETATM 3751  C22 GI9 A1202      16.083  42.492  61.223  1.00 72.88           C  
ANISOU 3751  C22 GI9 A1202     9735   9762   8193   -377    220     85       C  
HETATM 3752  C23 GI9 A1202      17.352  40.518  61.234  1.00 66.40           C  
ANISOU 3752  C23 GI9 A1202     9034   8883   7313   -321     50    177       C  
HETATM 3753  C24 GI9 A1202      16.323  49.211  52.641  1.00 58.82           C  
ANISOU 3753  C24 GI9 A1202     6920   8219   7209    -25    300    -53       C  
HETATM 3754  C25 GI9 A1202      19.100  40.983  59.370  1.00 50.69           C  
ANISOU 3754  C25 GI9 A1202     6805   6936   5518   -167    -87    195       C  
HETATM 3755  C26 GI9 A1202      18.204  47.080  53.468  1.00 57.48           C  
ANISOU 3755  C26 GI9 A1202     6893   8012   6933      6    164     22       C  
HETATM 3756  C27 GI9 A1202      15.307  49.011  54.871  1.00 56.55           C  
ANISOU 3756  C27 GI9 A1202     6761   7921   6806   -134    370    -85       C  
HETATM 3757  C28 GI9 A1202      17.976  39.141  61.476  1.00 76.18           C  
ANISOU 3757  C28 GI9 A1202    10378  10070   8496   -304    -48    234       C  
HETATM 3758  C29 GI9 A1202      15.597  49.241  51.525  1.00 54.70           C  
ANISOU 3758  C29 GI9 A1202     6340   7693   6749    -12    326    -56       C  
HETATM 3759  C21 GI9 A1202      16.050  48.271  53.784  1.00 57.02           C  
ANISOU 3759  C21 GI9 A1202     6796   7974   6894    -72    306    -42       C  
HETATM 3760  C30 GI9 A1202      20.447  46.894  52.456  1.00 65.72           C  
ANISOU 3760  C30 GI9 A1202     7876   9040   8055    102     47     47       C  
HETATM 3761  C31 GI9 A1202      17.294  50.166  52.555  1.00 58.92           C  
ANISOU 3761  C31 GI9 A1202     6890   8248   7251      7    267    -62       C  
HETATM 3762  C32 GI9 A1202      19.735  39.629  59.588  1.00 71.65           C  
ANISOU 3762  C32 GI9 A1202     9550   9541   8132   -148   -183    245       C  
HETATM 3763  C33 GI9 A1202      20.824  47.815  51.326  1.00 56.88           C  
ANISOU 3763  C33 GI9 A1202     6661   7933   7020    139     63     27       C  
HETATM 3764  C34 GI9 A1202      16.105  50.212  50.718  1.00 51.83           C  
ANISOU 3764  C34 GI9 A1202     5907   7341   6446     27    310    -65       C  
HETATM 3765  C35 GI9 A1202      19.171  38.700  60.650  1.00 75.23           C  
ANISOU 3765  C35 GI9 A1202    10179   9947   8459   -215   -170    268       C  
HETATM 3766  C36 GI9 A1202      20.155  47.212  50.109  1.00 62.18           C  
ANISOU 3766  C36 GI9 A1202     7309   8596   7721    146     98     44       C  
HETATM 3767  C37 GI9 A1202      14.375  48.388  51.093  1.00 42.84           C  
ANISOU 3767  C37 GI9 A1202     4846   6172   5259    -34    365    -55       C  
HETATM 3768  C38 GI9 A1202      21.668  46.501  53.271  1.00 63.66           C  
ANISOU 3768  C38 GI9 A1202     7663   8755   7768    120    -42     58       C  
HETATM 3769  C39 GI9 A1202      19.244  48.227  49.472  1.00 61.45           C  
ANISOU 3769  C39 GI9 A1202     7161   8523   7665    137    158     19       C  
HETATM 3770  C40 GI9 A1202      15.464  50.483  49.333  1.00 43.73           C  
ANISOU 3770  C40 GI9 A1202     4819   6306   5490     49    324    -68       C  
HETATM 3771  C41 GI9 A1202      23.614  45.204  53.613  1.00 65.77           C  
ANISOU 3771  C41 GI9 A1202     7974   8962   8052    174   -197     88       C  
HETATM 3772  C42 GI9 A1202      13.751  48.633  49.772  1.00 59.00           C  
ANISOU 3772  C42 GI9 A1202     6823   8211   7381    -10    374    -61       C  
HETATM 3773  C43 GI9 A1202      14.290  49.681  48.901  1.00 54.17           C  
ANISOU 3773  C43 GI9 A1202     6148   7609   6824     30    350    -66       C  
HETATM 3774  C44 GI9 A1202      18.703  47.597  48.202  1.00 68.74           C  
ANISOU 3774  C44 GI9 A1202     8067   9432   8618    148    176     37       C  
HETATM 3775  C45 GI9 A1202      24.398  44.075  53.006  1.00 76.40           C  
ANISOU 3775  C45 GI9 A1202     9312  10270   9446    212   -255    111       C  
HETATM 3776  C46 GI9 A1202      23.175  44.778  54.989  1.00 82.34           C  
ANISOU 3776  C46 GI9 A1202    10191  11051  10043    127   -220    104       C  
HETATM 3777  C47 GI9 A1202      24.464  46.442  53.767  1.00 66.09           C  
ANISOU 3777  C47 GI9 A1202     7955   9014   8141    197   -218     50       C  
HETATM 3778  N06 GI9 A1202      17.088  45.976  57.686  1.00 54.71           N  
ANISOU 3778  N06 GI9 A1202     6896   7610   6283   -180    207     16       N  
HETATM 3779  N07 GI9 A1202      17.127  42.593  60.212  1.00 69.24           N  
ANISOU 3779  N07 GI9 A1202     9161   9325   7822   -285    125    109       N  
HETATM 3780  N08 GI9 A1202      16.902  46.812  55.362  1.00 56.07           N  
ANISOU 3780  N08 GI9 A1202     6848   7821   6633   -100    236      1       N  
HETATM 3781  N09 GI9 A1202      16.235  41.192  61.856  1.00 73.91           N  
ANISOU 3781  N09 GI9 A1202    10017   9841   8225   -401    176    128       N  
HETATM 3782  N10 GI9 A1202      19.521  47.578  53.309  1.00 65.22           N  
ANISOU 3782  N10 GI9 A1202     7837   8995   7948     52    101     22       N  
HETATM 3783  N11 GI9 A1202      17.153  50.777  51.354  1.00 66.16           N  
ANISOU 3783  N11 GI9 A1202     7727   9168   8241     38    279    -70       N  
HETATM 3784  O01 GI9 A1202      18.174  47.778  56.904  1.00 74.66           O  
ANISOU 3784  O01 GI9 A1202     9264  10182   8922   -109    167    -14       O  
HETATM 3785  O02 GI9 A1202      15.269  43.285  61.492  1.00 76.08           O  
ANISOU 3785  O02 GI9 A1202    10119  10182   8606   -426    317     37       O  
HETATM 3786  O03 GI9 A1202      17.850  46.135  52.920  1.00 50.34           O  
ANISOU 3786  O03 GI9 A1202     6001   7094   6033     10    169     45       O  
HETATM 3787  O04 GI9 A1202      22.518  45.518  52.808  1.00 66.45           O  
ANISOU 3787  O04 GI9 A1202     8019   9078   8152    157   -104     83       O  
HETATM 3788  O05 GI9 A1202      21.883  47.040  54.297  1.00 67.33           O  
ANISOU 3788  O05 GI9 A1202     8164   9225   8192    101    -62     43       O  
HETATM 3789 H122 GI9 A1202      18.524  48.338  46.428  1.00 86.76           H  
HETATM 3790 H121 GI9 A1202      19.227  49.237  47.328  1.00 86.76           H  
HETATM 3791 H131 GI9 A1202      18.357  43.704  59.038  1.00 82.30           H  
HETATM 3792 H142 GI9 A1202      16.165  45.062  60.073  1.00 66.43           H  
HETATM 3793 H141 GI9 A1202      17.575  44.995  60.810  1.00 66.43           H  
HETATM 3794 H152 GI9 A1202      17.142  43.065  57.391  1.00 82.41           H  
HETATM 3795 H151 GI9 A1202      15.828  43.001  58.268  1.00 82.41           H  
HETATM 3796 H162 GI9 A1202      17.376  46.922  59.455  1.00 62.93           H  
HETATM 3797 H161 GI9 A1202      18.602  46.016  59.034  1.00 62.93           H  
HETATM 3798 H172 GI9 A1202      16.036  44.734  56.504  1.00 83.35           H  
HETATM 3799 H171 GI9 A1202      15.294  45.081  57.852  1.00 83.35           H  
HETATM 3800 H201 GI9 A1202      17.778  48.527  54.850  1.00 68.47           H  
HETATM 3801 H251 GI9 A1202      19.434  41.559  58.721  1.00 60.83           H  
HETATM 3802 H271 GI9 A1202      14.892  49.804  54.497  1.00 67.86           H  
HETATM 3803 H272 GI9 A1202      15.928  49.270  55.569  1.00 67.86           H  
HETATM 3804 H273 GI9 A1202      14.623  48.434  55.246  1.00 67.86           H  
HETATM 3805 H281 GI9 A1202      17.627  38.579  62.130  1.00 91.41           H  
HETATM 3806 H211 GI9 A1202      15.525  47.514  53.477  1.00 68.42           H  
HETATM 3807 H301 GI9 A1202      20.028  46.096  52.096  1.00 78.87           H  
HETATM 3808 H311 GI9 A1202      17.938  50.357  53.198  1.00 70.71           H  
HETATM 3809 H321 GI9 A1202      20.467  39.366  59.077  1.00 85.98           H  
HETATM 3810 H331 GI9 A1202      20.485  48.709  51.491  1.00 68.26           H  
HETATM 3811 H332 GI9 A1202      21.787  47.833  51.210  1.00 68.26           H  
HETATM 3812 H351 GI9 A1202      19.556  37.866  60.794  1.00 90.28           H  
HETATM 3813 H361 GI9 A1202      20.833  46.941  49.470  1.00 74.62           H  
HETATM 3814 H362 GI9 A1202      19.637  46.437  50.377  1.00 74.62           H  
HETATM 3815 H371 GI9 A1202      14.037  47.731  51.657  1.00 51.41           H  
HETATM 3816 H392 GI9 A1202      18.514  48.440  50.074  1.00 73.74           H  
HETATM 3817 H391 GI9 A1202      19.742  49.032  49.258  1.00 73.74           H  
HETATM 3818 H401 GI9 A1202      15.810  51.144  48.778  1.00 52.47           H  
HETATM 3819 H421 GI9 A1202      13.016  48.131  49.501  1.00 70.79           H  
HETATM 3820 H431 GI9 A1202      13.905  49.835  48.068  1.00 65.00           H  
HETATM 3821 H442 GI9 A1202      19.045  46.694  48.115  1.00 82.48           H  
HETATM 3822 H441 GI9 A1202      17.734  47.577  48.235  1.00 82.48           H  
HETATM 3823 H451 GI9 A1202      23.998  43.822  52.159  1.00 91.68           H  
HETATM 3824 H452 GI9 A1202      24.390  43.315  53.607  1.00 91.68           H  
HETATM 3825 H453 GI9 A1202      25.314  44.360  52.858  1.00 91.68           H  
HETATM 3826 H462 GI9 A1202      22.538  44.051  54.914  1.00 98.81           H  
HETATM 3827 H461 GI9 A1202      22.759  45.529  55.441  1.00 98.81           H  
HETATM 3828 H463 GI9 A1202      23.946  44.482  55.497  1.00 98.81           H  
HETATM 3829 H473 GI9 A1202      24.399  46.981  52.963  1.00 79.31           H  
HETATM 3830 H471 GI9 A1202      25.388  46.183  53.909  1.00 79.31           H  
HETATM 3831 H472 GI9 A1202      24.151  46.956  54.528  1.00 79.31           H  
HETATM 3832 H081 GI9 A1202      16.352  46.186  55.149  1.00 67.28           H  
HETATM 3833 H091 GI9 A1202      15.743  40.878  62.487  1.00 88.69           H  
HETATM 3834 H101 GI9 A1202      19.774  48.272  53.749  1.00 78.26           H  
HETATM 3835 H111 GI9 A1202      17.643  51.416  51.052  1.00 79.39           H  
CONECT  626 1244                                                                
CONECT 1244  626                                                                
CONECT 3727 3728 3732 3736                                                      
CONECT 3728 3727 3729                                                           
CONECT 3729 3728 3730                                                           
CONECT 3730 3729 3731 3733                                                      
CONECT 3731 3730 3732                                                           
CONECT 3732 3727 3731                                                           
CONECT 3733 3730 3734                                                           
CONECT 3734 3733 3735                                                           
CONECT 3735 3734                                                                
CONECT 3736 3727 3737                                                           
CONECT 3737 3736 3738                                                           
CONECT 3738 3737 3739 3740 3741                                                 
CONECT 3739 3738                                                                
CONECT 3740 3738                                                                
CONECT 3741 3738                                                                
CONECT 3742 3774 3789 3790                                                      
CONECT 3743 3744 3745 3779 3791                                                 
CONECT 3744 3743 3746 3792 3793                                                 
CONECT 3745 3743 3747 3794 3795                                                 
CONECT 3746 3744 3778 3796 3797                                                 
CONECT 3747 3745 3778 3798 3799                                                 
CONECT 3748 3752 3754 3779                                                      
CONECT 3749 3778 3780 3784                                                      
CONECT 3750 3755 3759 3780 3800                                                 
CONECT 3751 3779 3781 3785                                                      
CONECT 3752 3748 3757 3781                                                      
CONECT 3753 3758 3759 3761                                                      
CONECT 3754 3748 3762 3801                                                      
CONECT 3755 3750 3782 3786                                                      
CONECT 3756 3759 3802 3803 3804                                                 
CONECT 3757 3752 3765 3805                                                      
CONECT 3758 3753 3764 3767                                                      
CONECT 3759 3750 3753 3756 3806                                                 
CONECT 3760 3763 3768 3782 3807                                                 
CONECT 3761 3753 3783 3808                                                      
CONECT 3762 3754 3765 3809                                                      
CONECT 3763 3760 3766 3810 3811                                                 
CONECT 3764 3758 3770 3783                                                      
CONECT 3765 3757 3762 3812                                                      
CONECT 3766 3763 3769 3813 3814                                                 
CONECT 3767 3758 3772 3815                                                      
CONECT 3768 3760 3787 3788                                                      
CONECT 3769 3766 3774 3816 3817                                                 
CONECT 3770 3764 3773 3818                                                      
CONECT 3771 3775 3776 3777 3787                                                 
CONECT 3772 3767 3773 3819                                                      
CONECT 3773 3770 3772 3820                                                      
CONECT 3774 3742 3769 3821 3822                                                 
CONECT 3775 3771 3823 3824 3825                                                 
CONECT 3776 3771 3826 3827 3828                                                 
CONECT 3777 3771 3829 3830 3831                                                 
CONECT 3778 3746 3747 3749                                                      
CONECT 3779 3743 3748 3751                                                      
CONECT 3780 3749 3750 3832                                                      
CONECT 3781 3751 3752 3833                                                      
CONECT 3782 3755 3760 3834                                                      
CONECT 3783 3761 3764 3835                                                      
CONECT 3784 3749                                                                
CONECT 3785 3751                                                                
CONECT 3786 3755                                                                
CONECT 3787 3768 3771                                                           
CONECT 3788 3768                                                                
CONECT 3789 3742                                                                
CONECT 3790 3742                                                                
CONECT 3791 3743                                                                
CONECT 3792 3744                                                                
CONECT 3793 3744                                                                
CONECT 3794 3745                                                                
CONECT 3795 3745                                                                
CONECT 3796 3746                                                                
CONECT 3797 3746                                                                
CONECT 3798 3747                                                                
CONECT 3799 3747                                                                
CONECT 3800 3750                                                                
CONECT 3801 3754                                                                
CONECT 3802 3756                                                                
CONECT 3803 3756                                                                
CONECT 3804 3756                                                                
CONECT 3805 3757                                                                
CONECT 3806 3759                                                                
CONECT 3807 3760                                                                
CONECT 3808 3761                                                                
CONECT 3809 3762                                                                
CONECT 3810 3763                                                                
CONECT 3811 3763                                                                
CONECT 3812 3765                                                                
CONECT 3813 3766                                                                
CONECT 3814 3766                                                                
CONECT 3815 3767                                                                
CONECT 3816 3769                                                                
CONECT 3817 3769                                                                
CONECT 3818 3770                                                                
CONECT 3819 3772                                                                
CONECT 3820 3773                                                                
CONECT 3821 3774                                                                
CONECT 3822 3774                                                                
CONECT 3823 3775                                                                
CONECT 3824 3775                                                                
CONECT 3825 3775                                                                
CONECT 3826 3776                                                                
CONECT 3827 3776                                                                
CONECT 3828 3776                                                                
CONECT 3829 3777                                                                
CONECT 3830 3777                                                                
CONECT 3831 3777                                                                
CONECT 3832 3780                                                                
CONECT 3833 3781                                                                
CONECT 3834 3782                                                                
CONECT 3835 3783                                                                
MASTER      380    0    2   14   15    0    0    6 3787    1  111   46          
END