HEADER    MEMBRANE PROTEIN                        03-FEB-17   5X33              
TITLE     LEUKOTRIENE B4 RECEPTOR BLT1 IN COMPLEX WITH BIIL260                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LTB4 RECEPTOR,LYSOZYME,LTB4 RECEPTOR;                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: LEUKOTRIENE B4 RECEPTOR;                                    
COMPND   5 EC: 3.2.1.17;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 OTHER_DETAILS: CHIMERA PROTEIN OF UNP RESIDUES 15-213 FROM Q9WTK1,   
COMPND   9 UNP RESIDUES 2-161 FROM A0A097J792, UNP RESIDUES 214-348 FROM Q9WTK1.
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CAVIA PORCELLUS, ENTEROBACTERIA PHAGE RB55;     
SOURCE   3 ORGANISM_COMMON: GUINEA PIG;                                         
SOURCE   4 ORGANISM_TAXID: 10141, 697289;                                       
SOURCE   5 GENE: LTB4R, E, RB55_P125;                                           
SOURCE   6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS CBS 7435;                   
SOURCE   7 EXPRESSION_SYSTEM_COMMON: PICHIA PASTORIS;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 4922                                        
KEYWDS    HELIX, MEMBRANE PROTEIN                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.HORI,K.HIRATA,K.YAMASHITA,Y.KAWANO,M.YAMAMOTO,S.YOKOYAMA            
REVDAT   3   04-APR-18 5X33    1       JRNL                                     
REVDAT   2   07-FEB-18 5X33    1       JRNL                                     
REVDAT   1   03-JAN-18 5X33    0                                                
JRNL        AUTH   T.HORI,T.OKUNO,K.HIRATA,K.YAMASHITA,Y.KAWANO,M.YAMAMOTO,     
JRNL        AUTH 2 M.HATO,M.NAKAMURA,T.SHIMIZU,T.YOKOMIZO,M.MIYANO,S.YOKOYAMA   
JRNL        TITL   NA+-MIMICKING LIGANDS STABILIZE THE INACTIVE STATE OF        
JRNL        TITL 2 LEUKOTRIENE B4RECEPTOR BLT1.                                 
JRNL        REF    NAT. CHEM. BIOL.              V.  14   262 2018              
JRNL        REFN                   ESSN 1552-4469                               
JRNL        PMID   29309055                                                     
JRNL        DOI    10.1038/NCHEMBIO.2547                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.54                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 8262                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.251                           
REMARK   3   R VALUE            (WORKING SET) : 0.248                           
REMARK   3   FREE R VALUE                     : 0.296                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 414                             
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 48.5434 -  5.3350    1.00     2712   143  0.2404 0.2816        
REMARK   3     2  5.3350 -  4.2353    1.00     2594   137  0.2375 0.2664        
REMARK   3     3  4.2353 -  3.7002    1.00     2542   134  0.2745 0.3533        
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)     : 0.480            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.650           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           3448                                  
REMARK   3   ANGLE     :  0.801           4693                                  
REMARK   3   CHIRALITY :  0.042            556                                  
REMARK   3   PLANARITY :  0.007            580                                  
REMARK   3   DIHEDRAL  : 15.004           2015                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 15 THROUGH 148 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): 101.9104 183.8565 283.8529              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0138 T22:   0.8497                                     
REMARK   3      T33:   1.0676 T12:  -0.1505                                     
REMARK   3      T13:   0.0214 T23:   0.0277                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4200 L22:   1.4328                                     
REMARK   3      L33:   1.4670 L12:   0.6852                                     
REMARK   3      L13:  -1.0673 L23:  -0.0161                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0295 S12:   0.2746 S13:  -0.5560                       
REMARK   3      S21:  -0.4465 S22:   0.0836 S23:   0.2806                       
REMARK   3      S31:   0.0671 S32:  -0.1825 S33:  -0.0291                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 149 THROUGH 213 OR RESID 900      
REMARK   3               THROUGH 1021 )                                         
REMARK   3    ORIGIN FOR THE GROUP (A): 101.2925 183.0013 299.1973              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0142 T22:   1.0935                                     
REMARK   3      T33:   0.9258 T12:  -0.0537                                     
REMARK   3      T13:  -0.0270 T23:   0.0508                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6149 L22:   0.3542                                     
REMARK   3      L33:   0.5280 L12:  -0.1861                                     
REMARK   3      L13:  -0.5769 L23:  -0.2662                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0057 S12:  -0.2322 S13:  -0.3922                       
REMARK   3      S21:   0.1086 S22:  -0.0609 S23:   0.1440                       
REMARK   3      S31:  -0.1278 S32:   0.4489 S33:   0.0804                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1022 THROUGH 1136 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  74.7894 178.9009 319.7136              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0163 T22:   0.7631                                     
REMARK   3      T33:   1.1421 T12:   0.1067                                     
REMARK   3      T13:   0.0407 T23:   0.1078                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6544 L22:   0.5786                                     
REMARK   3      L33:   0.6353 L12:  -0.1516                                     
REMARK   3      L13:   0.0209 L23:  -0.4206                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0104 S12:  -0.0477 S13:   0.4890                       
REMARK   3      S21:   0.1199 S22:  -0.0243 S23:  -0.1988                       
REMARK   3      S31:  -0.0985 S32:  -0.3008 S33:   0.0113                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1137 THROUGH 1203 OR RESID 214    
REMARK   3               THROUGH 229 )                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  73.0932 168.6446 312.5627              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2732 T22:   0.7165                                     
REMARK   3      T33:   0.8870 T12:  -0.0334                                     
REMARK   3      T13:  -0.0067 T23:  -0.0518                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5785 L22:   1.0270                                     
REMARK   3      L33:   0.3012 L12:   0.9608                                     
REMARK   3      L13:  -0.3155 L23:  -0.5250                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0086 S12:   0.3957 S13:   0.0206                       
REMARK   3      S21:  -0.1560 S22:   0.3848 S23:  -0.0535                       
REMARK   3      S31:   0.0685 S32:  -0.5876 S33:  -0.2568                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 230 THROUGH 287 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 112.2995 174.5409 291.0606              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1132 T22:   0.8846                                     
REMARK   3      T33:   1.3744 T12:   0.0211                                     
REMARK   3      T13:   0.1005 T23:   0.3121                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2302 L22:   1.5231                                     
REMARK   3      L33:   4.3493 L12:  -0.5823                                     
REMARK   3      L13:  -0.4163 L23:   0.4453                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2272 S12:   0.3327 S13:  -0.3091                       
REMARK   3      S21:   0.1911 S22:   0.0160 S23:  -0.5314                       
REMARK   3      S31:   0.1246 S32:   0.5083 S33:  -0.0980                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 2001 THROUGH 2001 )               
REMARK   3    ORIGIN FOR THE GROUP (A): 114.0156 178.7942 283.4466              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4818 T22:   1.2104                                     
REMARK   3      T33:   1.0363 T12:   0.2284                                     
REMARK   3      T13:   0.2370 T23:  -0.1439                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.2343 L22:   0.0158                                     
REMARK   3      L33:   0.4652 L12:   0.3754                                     
REMARK   3      L13:   1.9573 L23:   0.0901                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0274 S12:  -0.7150 S13:   0.8858                       
REMARK   3      S21:  -0.2159 S22:   0.1442 S23:  -1.0226                       
REMARK   3      S31:   0.1856 S32:   0.5857 S33:  -0.1578                       
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 5X33 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300002841.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-OCT-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL32XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 9M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 8291                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 34.60                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.92                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 31.80                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 4MBS AND 4K5Y                                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.82                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 300, BICINE, LIPIDIC CUBIC PHASE,    
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   X,-Y,-Z                                                 
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-Y+1/2,Z+1/2                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.81000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       67.76500            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.81000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       67.76500            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLU A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     MET A     4                                                      
REMARK 465     ASP A     5                                                      
REMARK 465     TYR A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     ASP A     9                                                      
REMARK 465     ASP A    10                                                      
REMARK 465     ASP A    11                                                      
REMARK 465     LYS A    12                                                      
REMARK 465     GLU A    13                                                      
REMARK 465     PHE A    14                                                      
REMARK 465     THR A   254                                                      
REMARK 465     LEU A   255                                                      
REMARK 465     GLY A   288                                                      
REMARK 465     GLY A   289                                                      
REMARK 465     GLY A   290                                                      
REMARK 465     LEU A   291                                                      
REMARK 465     LEU A   292                                                      
REMARK 465     ARG A   293                                                      
REMARK 465     SER A   294                                                      
REMARK 465     ALA A   295                                                      
REMARK 465     GLY A   296                                                      
REMARK 465     VAL A   297                                                      
REMARK 465     GLY A   298                                                      
REMARK 465     PHE A   299                                                      
REMARK 465     VAL A   300                                                      
REMARK 465     ALA A   301                                                      
REMARK 465     LYS A   302                                                      
REMARK 465     LEU A   303                                                      
REMARK 465     LEU A   304                                                      
REMARK 465     GLU A   305                                                      
REMARK 465     ALA A   306                                                      
REMARK 465     THR A   307                                                      
REMARK 465     GLY A   308                                                      
REMARK 465     ALA A   309                                                      
REMARK 465     GLU A   310                                                      
REMARK 465     ALA A   311                                                      
REMARK 465     PHE A   312                                                      
REMARK 465     SER A   313                                                      
REMARK 465     THR A   314                                                      
REMARK 465     ARG A   315                                                      
REMARK 465     ARG A   316                                                      
REMARK 465     GLY A   317                                                      
REMARK 465     GLY A   318                                                      
REMARK 465     THR A   319                                                      
REMARK 465     LEU A   320                                                      
REMARK 465     ALA A   321                                                      
REMARK 465     GLN A   322                                                      
REMARK 465     THR A   323                                                      
REMARK 465     VAL A   324                                                      
REMARK 465     LYS A   325                                                      
REMARK 465     GLY A   326                                                      
REMARK 465     ILE A   327                                                      
REMARK 465     PRO A   328                                                      
REMARK 465     MET A   329                                                      
REMARK 465     ALA A   330                                                      
REMARK 465     PRO A   331                                                      
REMARK 465     GLU A   332                                                      
REMARK 465     PRO A   333                                                      
REMARK 465     GLY A   334                                                      
REMARK 465     ALA A   335                                                      
REMARK 465     SER A   336                                                      
REMARK 465     GLY A   337                                                      
REMARK 465     SER A   338                                                      
REMARK 465     LEU A   339                                                      
REMARK 465     ASP A   340                                                      
REMARK 465     GLY A   341                                                      
REMARK 465     LEU A   342                                                      
REMARK 465     LYS A   343                                                      
REMARK 465     GLN A   344                                                      
REMARK 465     SER A   345                                                      
REMARK 465     GLU A   346                                                      
REMARK 465     SER A   347                                                      
REMARK 465     ASP A   348                                                      
REMARK 465     GLU A   349                                                      
REMARK 465     PHE A   350                                                      
REMARK 465     LEU A   351                                                      
REMARK 465     GLU A   352                                                      
REMARK 465     VAL A   353                                                      
REMARK 465     LEU A   354                                                      
REMARK 465     PHE A   355                                                      
REMARK 465     GLN A   356                                                      
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  47    CG   CD   CE   NZ                                   
REMARK 470     ARG A  48    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  50    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  51    CG   CD   CE   NZ                                   
REMARK 470     LYS A 133    CG   CD   CE   NZ                                   
REMARK 470     ARG A 211    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A1014    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1016    CG   CD   CE   NZ                                   
REMARK 470     ASP A1020    CG   OD1  OD2                                       
REMARK 470     THR A1021    OG1  CG2                                            
REMARK 470     GLU A1022    CG   CD   OE1  OE2                                  
REMARK 470     TYR A1024    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A1043    CG   CD   CE   NZ                                   
REMARK 470     LYS A1048    CG   CD   CE   NZ                                   
REMARK 470     ARG A1080    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1147    CG   CD   CE   NZ                                   
REMARK 470     ARG A 217    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 218    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 256    CG   OD1  OD2                                       
REMARK 470     GLN A 257    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 259    CG   CD   CE   NZ                                   
REMARK 470     GLN A 260    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 264    CG   OD1  ND2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    LEU A    35     OG1  THR A    39              2.03            
REMARK 500   OG   SER A   903     OE1  GLU A  1064              2.12            
REMARK 500   OG   SER A  1038     OD1  ASN A  1040              2.19            
REMARK 500   O    LEU A   149     OG1  THR A   152              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 117       -7.03    -59.11                                   
REMARK 500    ASP A1010      -60.12    -98.92                                   
REMARK 500    ASP A1020     -179.97    -69.13                                   
REMARK 500    ALA A1112       -8.82    -55.21                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7Y9 A 2001                
DBREF  5X33 A   15   213  UNP    Q9WTK1   Q9WTK1_CAVPO    15    213             
DBREF1 5X33 A 1002  1161  UNP                  A0A097J792_BPT4                  
DBREF2 5X33 A     A0A097J792                          2         161             
DBREF  5X33 A  214   348  UNP    Q9WTK1   Q9WTK1_CAVPO   214    348             
SEQADV 5X33 GLU A    2  UNP  Q9WTK1              EXPRESSION TAG                 
SEQADV 5X33 LEU A    3  UNP  Q9WTK1              EXPRESSION TAG                 
SEQADV 5X33 MET A    4  UNP  Q9WTK1              EXPRESSION TAG                 
SEQADV 5X33 ASP A    5  UNP  Q9WTK1              EXPRESSION TAG                 
SEQADV 5X33 TYR A    6  UNP  Q9WTK1              EXPRESSION TAG                 
SEQADV 5X33 LYS A    7  UNP  Q9WTK1              EXPRESSION TAG                 
SEQADV 5X33 ASP A    8  UNP  Q9WTK1              EXPRESSION TAG                 
SEQADV 5X33 ASP A    9  UNP  Q9WTK1              EXPRESSION TAG                 
SEQADV 5X33 ASP A   10  UNP  Q9WTK1              EXPRESSION TAG                 
SEQADV 5X33 ASP A   11  UNP  Q9WTK1              EXPRESSION TAG                 
SEQADV 5X33 LYS A   12  UNP  Q9WTK1              EXPRESSION TAG                 
SEQADV 5X33 GLU A   13  UNP  Q9WTK1              EXPRESSION TAG                 
SEQADV 5X33 PHE A   14  UNP  Q9WTK1              EXPRESSION TAG                 
SEQADV 5X33 GLY A   83  UNP  Q9WTK1    HIS    83 ENGINEERED MUTATION            
SEQADV 5X33 GLY A   88  UNP  Q9WTK1    LYS    88 ENGINEERED MUTATION            
SEQADV 5X33 ALA A  212  UNP  Q9WTK1    VAL   212 ENGINEERED MUTATION            
SEQADV 5X33 GLY A  900  UNP  Q9WTK1              LINKER                         
SEQADV 5X33 SER A  901  UNP  Q9WTK1              LINKER                         
SEQADV 5X33 GLY A  902  UNP  Q9WTK1              LINKER                         
SEQADV 5X33 SER A  903  UNP  Q9WTK1              LINKER                         
SEQADV 5X33 THR A 1054  UNP  A0A097J79 CYS    54 ENGINEERED MUTATION            
SEQADV 5X33 ALA A 1097  UNP  A0A097J79 CYS    97 ENGINEERED MUTATION            
SEQADV 5X33 GLY A 1200  UNP  A0A097J79           LINKER                         
SEQADV 5X33 SER A 1201  UNP  A0A097J79           LINKER                         
SEQADV 5X33 GLY A 1202  UNP  A0A097J79           LINKER                         
SEQADV 5X33 SER A 1203  UNP  A0A097J79           LINKER                         
SEQADV 5X33 ALA A  309  UNP  Q9WTK1    SER   309 ENGINEERED MUTATION            
SEQADV 5X33 GLU A  349  UNP  Q9WTK1              EXPRESSION TAG                 
SEQADV 5X33 PHE A  350  UNP  Q9WTK1              EXPRESSION TAG                 
SEQADV 5X33 LEU A  351  UNP  Q9WTK1              EXPRESSION TAG                 
SEQADV 5X33 GLU A  352  UNP  Q9WTK1              EXPRESSION TAG                 
SEQADV 5X33 VAL A  353  UNP  Q9WTK1              EXPRESSION TAG                 
SEQADV 5X33 LEU A  354  UNP  Q9WTK1              EXPRESSION TAG                 
SEQADV 5X33 PHE A  355  UNP  Q9WTK1              EXPRESSION TAG                 
SEQADV 5X33 GLN A  356  UNP  Q9WTK1              EXPRESSION TAG                 
SEQRES   1 A  523  GLU LEU MET ASP TYR LYS ASP ASP ASP ASP LYS GLU PHE          
SEQRES   2 A  523  SER ASN THR PHE ILE PRO LEU LEU ALA MET ILE LEU LEU          
SEQRES   3 A  523  SER VAL SER MET VAL VAL GLY LEU PRO GLY ASN THR PHE          
SEQRES   4 A  523  VAL VAL TRP SER ILE LEU LYS ARG MET ARG LYS ARG SER          
SEQRES   5 A  523  VAL THR ALA LEU MET VAL LEU ASN LEU ALA LEU ALA ASP          
SEQRES   6 A  523  LEU ALA VAL LEU LEU THR ALA PRO PHE PHE LEU HIS PHE          
SEQRES   7 A  523  LEU THR TRP GLY THR TRP SER PHE GLY LEU ALA GLY CYS          
SEQRES   8 A  523  ARG LEU CYS HIS TYR ILE CYS GLY VAL SER MET TYR ALA          
SEQRES   9 A  523  SER VAL LEU LEU ILE THR ALA MET SER LEU ASP ARG SER          
SEQRES  10 A  523  LEU ALA VAL ALA SER PRO PHE LEU SER GLN LYS VAL ARG          
SEQRES  11 A  523  THR LYS THR ALA ALA ARG TRP LEU LEU VAL GLY ILE TRP          
SEQRES  12 A  523  GLY ALA SER PHE LEU LEU ALA THR PRO VAL LEU ALA PHE          
SEQRES  13 A  523  ARG LYS VAL VAL LYS LEU THR ASN GLU THR ASP LEU CYS          
SEQRES  14 A  523  LEU ALA VAL TYR PRO SER ASP ARG HIS LYS ALA PHE HIS          
SEQRES  15 A  523  LEU LEU PHE GLU ALA PHE THR GLY PHE VAL VAL PRO PHE          
SEQRES  16 A  523  LEU ILE VAL VAL ALA SER TYR ALA ASP ILE SER ARG ARG          
SEQRES  17 A  523  LEU ARG ALA ARG GLY SER GLY SER ASN ILE PHE GLU MET          
SEQRES  18 A  523  LEU ARG ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS          
SEQRES  19 A  523  ASP THR GLU GLY TYR TYR THR ILE GLY ILE GLY HIS LEU          
SEQRES  20 A  523  LEU THR LYS SER PRO SER LEU ASN ALA ALA LYS SER GLU          
SEQRES  21 A  523  LEU ASP LYS ALA ILE GLY ARG ASN THR ASN GLY VAL ILE          
SEQRES  22 A  523  THR LYS ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL          
SEQRES  23 A  523  ASP ALA ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU          
SEQRES  24 A  523  LYS PRO VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA          
SEQRES  25 A  523  ALA LEU ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY          
SEQRES  26 A  523  VAL ALA GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN          
SEQRES  27 A  523  LYS ARG TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER          
SEQRES  28 A  523  ARG TRP TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL          
SEQRES  29 A  523  ILE THR THR PHE ARG THR GLY THR TRP ASP ALA TYR GLY          
SEQRES  30 A  523  SER GLY SER ARG PHE HIS ARG ARG ARG ARG THR GLY ARG          
SEQRES  31 A  523  LEU VAL VAL ILE ILE ILE LEU ALA PHE ALA ALA PHE TRP          
SEQRES  32 A  523  LEU PRO TYR HIS VAL VAL ASP LEU VAL GLU GLY SER ARG          
SEQRES  33 A  523  VAL LEU ALA GLY THR LEU ASP GLN SER LYS GLN GLN LEU          
SEQRES  34 A  523  ARG ASN ALA ARG LYS VAL CYS ILE ALA LEU ALA PHE LEU          
SEQRES  35 A  523  SER SER SER VAL ASN PRO LEU LEU TYR ALA CYS ALA GLY          
SEQRES  36 A  523  GLY GLY LEU LEU ARG SER ALA GLY VAL GLY PHE VAL ALA          
SEQRES  37 A  523  LYS LEU LEU GLU ALA THR GLY ALA GLU ALA PHE SER THR          
SEQRES  38 A  523  ARG ARG GLY GLY THR LEU ALA GLN THR VAL LYS GLY ILE          
SEQRES  39 A  523  PRO MET ALA PRO GLU PRO GLY ALA SER GLY SER LEU ASP          
SEQRES  40 A  523  GLY LEU LYS GLN SER GLU SER ASP GLU PHE LEU GLU VAL          
SEQRES  41 A  523  LEU PHE GLN                                                  
HET    7Y9  A2001      35                                                       
HETNAM     7Y9 4-[[3-[[4-[2-(4-HYDROXYPHENYL)PROPAN-2-                          
HETNAM   2 7Y9  YL]PHENOXY]METHYL]PHENYL]METHOXY]BENZENECARBOXIMIDAMID          
HETNAM   3 7Y9  E                                                               
FORMUL   2  7Y9    C30 H30 N2 O3                                                
HELIX    1 AA1 THR A   17  ARG A   48  1                                  32    
HELIX    2 AA2 VAL A   54  GLY A   83  1                                  30    
HELIX    3 AA3 PHE A   87  ARG A  117  1                                  31    
HELIX    4 AA4 SER A  118  SER A  123  1                                   6    
HELIX    5 AA5 SER A  123  ARG A  131  1                                   9    
HELIX    6 AA6 THR A  132  LEU A  149  1                                  18    
HELIX    7 AA7 THR A  152  PHE A  157  1                                   6    
HELIX    8 AA8 SER A  176  THR A  190  1                                  15    
HELIX    9 AA9 PHE A  192  GLY A  900  1                                  23    
HELIX   10 AB1 SER A  903  GLY A 1012  1                                  12    
HELIX   11 AB2 SER A 1038  ALA A 1049  1                                  12    
HELIX   12 AB3 THR A 1059  ARG A 1080  1                                  22    
HELIX   13 AB4 LYS A 1083  LEU A 1091  1                                   9    
HELIX   14 AB5 ASP A 1092  GLY A 1107  1                                  16    
HELIX   15 AB6 GLY A 1107  ALA A 1112  1                                   6    
HELIX   16 AB7 PHE A 1114  GLN A 1123  1                                  10    
HELIX   17 AB8 TRP A 1126  VAL A 1131  1                                   6    
HELIX   18 AB9 ASN A 1132  LYS A 1135  5                                   4    
HELIX   19 AC1 SER A 1136  THR A 1142  1                                   7    
HELIX   20 AC2 THR A 1142  GLY A 1156  1                                  15    
HELIX   21 AC3 THR A  221  VAL A  226  1                                   6    
HELIX   22 AC4 ILE A  229  ARG A  249  1                                  21    
HELIX   23 AC5 GLN A  260  ALA A  273  1                                  14    
HELIX   24 AC6 PHE A  274  SER A  278  5                                   5    
HELIX   25 AC7 VAL A  279  ALA A  285  1                                   7    
SHEET    1 AA1 2 ARG A 158  THR A 164  0                                        
SHEET    2 AA1 2 THR A 167  ALA A 172 -1  O  THR A 167   N  THR A 164           
SHEET    1 AA2 3 TYR A1018  LYS A1019  0                                        
SHEET    2 AA2 3 TYR A1025  ILE A1027 -1  O  THR A1026   N  TYR A1018           
SHEET    3 AA2 3 HIS A1031  LEU A1032 -1  O  HIS A1031   N  ILE A1027           
SSBOND   1 CYS A   92    CYS A  170                          1555   1555  2.02  
SITE     1 AC1 15 ASP A  66  VAL A  69  PHE A  76  LEU A  80                    
SITE     2 AC1 15 HIS A  96  CYS A  99  SER A 102  MET A 103                    
SITE     3 AC1 15 SER A 106  TRP A 236  LYS A 267  ILE A 270                    
SITE     4 AC1 15 ALA A 273  SER A 276  SER A 277                               
CRYST1   69.560   77.620  135.530  90.00  90.00  90.00 P 2 21 21     4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014376  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012883  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007378        0.00000                         
ATOM      1  N   SER A  15     126.586 161.341 282.733  1.00 89.58           N  
ANISOU    1  N   SER A  15     5360   9594  19084    300   2537   -121       N  
ATOM      2  CA  SER A  15     125.426 162.085 283.211  1.00100.26           C  
ANISOU    2  CA  SER A  15     6826  11157  20112    208   2343    -56       C  
ATOM      3  C   SER A  15     125.503 163.553 282.795  1.00101.33           C  
ANISOU    3  C   SER A  15     7087  11654  19759    121   2227   -179       C  
ATOM      4  O   SER A  15     124.624 164.350 283.136  1.00 98.95           O  
ANISOU    4  O   SER A  15     6891  11562  19142     43   2067   -136       O  
ATOM      5  CB  SER A  15     125.306 161.972 284.733  1.00 96.81           C  
ANISOU    5  CB  SER A  15     6346  10821  19616    291   2200    311       C  
ATOM      6  OG  SER A  15     124.248 162.776 285.228  1.00 92.16           O  
ANISOU    6  OG  SER A  15     5874  10457  18684    201   2019    364       O  
ATOM      7  N   ASN A  16     126.564 163.905 282.061  1.00105.16           N  
ANISOU    7  N   ASN A  16     7561  12202  20194    135   2318   -328       N  
ATOM      8  CA  ASN A  16     126.709 165.265 281.551  1.00104.00           C  
ANISOU    8  CA  ASN A  16     7528  12363  19623     50   2239   -453       C  
ATOM      9  C   ASN A  16     125.727 165.568 280.423  1.00101.76           C  
ANISOU    9  C   ASN A  16     7350  12034  19282    -98   2270   -733       C  
ATOM     10  O   ASN A  16     125.412 166.740 280.187  1.00 98.21           O  
ANISOU   10  O   ASN A  16     7013  11841  18461   -181   2162   -780       O  
ATOM     11  CB  ASN A  16     128.144 165.502 281.060  1.00106.18           C  
ANISOU   11  CB  ASN A  16     7754  12704  19887    104   2343   -533       C  
ATOM     12  CG  ASN A  16     129.020 166.195 282.096  1.00104.15           C  
ANISOU   12  CG  ASN A  16     7461  12752  19358    182   2214   -294       C  
ATOM     13  OD1 ASN A  16     128.796 166.078 283.302  1.00104.92           O  
ANISOU   13  OD1 ASN A  16     7524  12932  19408    234   2091    -45       O  
ATOM     14  ND2 ASN A  16     130.027 166.925 281.623  1.00101.62           N  
ANISOU   14  ND2 ASN A  16     7146  12606  18858    178   2249   -386       N  
ATOM     15  N   THR A  17     125.234 164.538 279.730  1.00101.59           N  
ANISOU   15  N   THR A  17     7287  11691  19623   -137   2419   -923       N  
ATOM     16  CA  THR A  17     124.395 164.713 278.552  1.00 97.75           C  
ANISOU   16  CA  THR A  17     6875  11158  19107   -289   2473  -1235       C  
ATOM     17  C   THR A  17     122.899 164.589 278.830  1.00 92.90           C  
ANISOU   17  C   THR A  17     6303  10517  18476   -371   2360  -1205       C  
ATOM     18  O   THR A  17     122.097 165.093 278.034  1.00 89.43           O  
ANISOU   18  O   THR A  17     5943  10160  17876   -505   2330  -1408       O  
ATOM     19  CB  THR A  17     124.788 163.694 277.470  1.00100.34           C  
ANISOU   19  CB  THR A  17     7131  11166  19829   -317   2734  -1540       C  
ATOM     20  OG1 THR A  17     125.238 162.477 278.085  1.00102.15           O  
ANISOU   20  OG1 THR A  17     7233  11113  20466   -191   2841  -1393       O  
ATOM     21  CG2 THR A  17     125.894 164.244 276.585  1.00 85.87           C  
ANISOU   21  CG2 THR A  17     5320   9432  17876   -330   2846  -1729       C  
ATOM     22  N   PHE A  18     122.499 163.952 279.932  1.00 92.93           N  
ANISOU   22  N   PHE A  18     6255  10422  18633   -296   2296   -953       N  
ATOM     23  CA  PHE A  18     121.091 163.626 280.144  1.00 93.25           C  
ANISOU   23  CA  PHE A  18     6319  10384  18729   -374   2223   -945       C  
ATOM     24  C   PHE A  18     120.323 164.725 280.870  1.00 91.57           C  
ANISOU   24  C   PHE A  18     6214  10486  18091   -407   1989   -762       C  
ATOM     25  O   PHE A  18     119.104 164.838 280.687  1.00 91.83           O  
ANISOU   25  O   PHE A  18     6300  10535  18057   -508   1915   -829       O  
ATOM     26  CB  PHE A  18     120.976 162.294 280.896  1.00 83.79           C  
ANISOU   26  CB  PHE A  18     5007   8877  17953   -288   2301   -783       C  
ATOM     27  CG  PHE A  18     120.412 162.411 282.284  1.00 82.51           C  
ANISOU   27  CG  PHE A  18     4858   8826  17665   -236   2127   -449       C  
ATOM     28  CD1 PHE A  18     119.120 161.990 282.555  1.00 82.48           C  
ANISOU   28  CD1 PHE A  18     4866   8717  17755   -302   2078   -426       C  
ATOM     29  CD2 PHE A  18     121.180 162.913 283.325  1.00 89.13           C  
ANISOU   29  CD2 PHE A  18     5694   9878  18295   -129   2022   -173       C  
ATOM     30  CE1 PHE A  18     118.599 162.084 283.830  1.00 81.43           C  
ANISOU   30  CE1 PHE A  18     4749   8684  17508   -261   1933   -131       C  
ATOM     31  CE2 PHE A  18     120.661 163.016 284.599  1.00 80.54           C  
ANISOU   31  CE2 PHE A  18     4619   8899  17083    -96   1878    106       C  
ATOM     32  CZ  PHE A  18     119.370 162.598 284.853  1.00 80.48           C  
ANISOU   32  CZ  PHE A  18     4630   8776  17172   -160   1837    131       C  
ATOM     33  N   ILE A  19     120.999 165.533 281.693  1.00 76.85           N  
ANISOU   33  N   ILE A  19     4382   8875  15942   -331   1879   -544       N  
ATOM     34  CA  ILE A  19     120.348 166.719 282.249  1.00 73.96           C  
ANISOU   34  CA  ILE A  19     4131   8820  15150   -378   1687   -423       C  
ATOM     35  C   ILE A  19     120.002 167.722 281.162  1.00 91.98           C  
ANISOU   35  C   ILE A  19     6514  11260  17175   -492   1663   -637       C  
ATOM     36  O   ILE A  19     118.862 168.225 281.156  1.00 91.61           O  
ANISOU   36  O   ILE A  19     6544  11315  16948   -575   1551   -639       O  
ATOM     37  CB  ILE A  19     121.223 167.321 283.376  1.00 72.94           C  
ANISOU   37  CB  ILE A  19     4002   8924  14788   -285   1599   -181       C  
ATOM     38  CG1 ILE A  19     121.031 166.545 284.680  1.00 73.81           C  
ANISOU   38  CG1 ILE A  19     4043   8946  15057   -206   1558     73       C  
ATOM     39  CG2 ILE A  19     120.904 168.797 283.570  1.00 70.06           C  
ANISOU   39  CG2 ILE A  19     3766   8898  13956   -350   1455   -152       C  
ATOM     40  CD1 ILE A  19     119.973 167.129 285.603  1.00 81.08           C  
ANISOU   40  CD1 ILE A  19     5050  10044  15713   -253   1398    214       C  
ATOM     41  N   PRO A  20     120.887 168.057 280.212  1.00 90.23           N  
ANISOU   41  N   PRO A  20     6293  11063  16926   -506   1765   -816       N  
ATOM     42  CA  PRO A  20     120.427 168.841 279.054  1.00 88.17           C  
ANISOU   42  CA  PRO A  20     6115  10905  16479   -630   1762  -1042       C  
ATOM     43  C   PRO A  20     119.349 168.135 278.251  1.00 73.22           C  
ANISOU   43  C   PRO A  20     4203   8828  14790   -740   1812  -1261       C  
ATOM     44  O   PRO A  20     118.482 168.800 277.672  1.00 72.13           O  
ANISOU   44  O   PRO A  20     4135   8817  14453   -850   1735  -1364       O  
ATOM     45  CB  PRO A  20     121.708 169.046 278.232  1.00 87.97           C  
ANISOU   45  CB  PRO A  20     6072  10884  16467   -616   1904  -1202       C  
ATOM     46  CG  PRO A  20     122.810 168.940 279.227  1.00 88.21           C  
ANISOU   46  CG  PRO A  20     6046  10958  16512   -480   1898   -978       C  
ATOM     47  CD  PRO A  20     122.356 167.895 280.204  1.00 90.01           C  
ANISOU   47  CD  PRO A  20     6199  11015  16987   -412   1872   -803       C  
ATOM     48  N   LEU A  21     119.374 166.800 278.210  1.00 75.65           N  
ANISOU   48  N   LEU A  21     4408   8838  15496   -718   1942  -1336       N  
ATOM     49  CA  LEU A  21     118.323 166.048 277.531  1.00 77.07           C  
ANISOU   49  CA  LEU A  21     4559   8837  15886   -836   1995  -1556       C  
ATOM     50  C   LEU A  21     116.987 166.186 278.255  1.00 92.66           C  
ANISOU   50  C   LEU A  21     6574  10886  17748   -869   1819  -1388       C  
ATOM     51  O   LEU A  21     115.937 166.317 277.615  1.00 93.74           O  
ANISOU   51  O   LEU A  21     6741  11060  17815  -1000   1770  -1546       O  
ATOM     52  CB  LEU A  21     118.749 164.580 277.411  1.00 80.16           C  
ANISOU   52  CB  LEU A  21     4829   8869  16758   -796   2199  -1661       C  
ATOM     53  CG  LEU A  21     117.808 163.457 276.956  1.00 82.34           C  
ANISOU   53  CG  LEU A  21     5043   8878  17366   -900   2299  -1867       C  
ATOM     54  CD1 LEU A  21     116.981 162.910 278.118  1.00 82.19           C  
ANISOU   54  CD1 LEU A  21     4996   8763  17469   -848   2198  -1604       C  
ATOM     55  CD2 LEU A  21     116.914 163.901 275.804  1.00 82.10           C  
ANISOU   55  CD2 LEU A  21     5070   8972  17154  -1094   2270  -2168       C  
ATOM     56  N   LEU A  22     117.002 166.154 279.589  1.00 90.38           N  
ANISOU   56  N   LEU A  22     6284  10631  17427   -760   1724  -1076       N  
ATOM     57  CA  LEU A  22     115.755 166.279 280.337  1.00 88.56           C  
ANISOU   57  CA  LEU A  22     6094  10470  17085   -791   1572   -919       C  
ATOM     58  C   LEU A  22     115.195 167.694 280.246  1.00 71.01           C  
ANISOU   58  C   LEU A  22     3991   8565  14425   -851   1412   -882       C  
ATOM     59  O   LEU A  22     113.981 167.881 280.110  1.00 70.45           O  
ANISOU   59  O   LEU A  22     3956   8548  14263   -939   1318   -911       O  
ATOM     60  CB  LEU A  22     115.976 165.866 281.797  1.00 87.99           C  
ANISOU   60  CB  LEU A  22     5987  10358  17087   -668   1532   -611       C  
ATOM     61  CG  LEU A  22     114.791 165.836 282.772  1.00 85.96           C  
ANISOU   61  CG  LEU A  22     5761  10143  16755   -684   1402   -428       C  
ATOM     62  CD1 LEU A  22     114.980 164.731 283.799  1.00 74.35           C  
ANISOU   62  CD1 LEU A  22     4199   8456  15595   -588   1456   -228       C  
ATOM     63  CD2 LEU A  22     114.622 167.175 283.477  1.00 82.16           C  
ANISOU   63  CD2 LEU A  22     5393   9998  15825   -677   1241   -266       C  
ATOM     64  N   ALA A  23     116.059 168.706 280.323  1.00 69.52           N  
ANISOU   64  N   ALA A  23     3859   8585  13972   -805   1384   -815       N  
ATOM     65  CA  ALA A  23     115.571 170.079 280.306  1.00 67.14           C  
ANISOU   65  CA  ALA A  23     3667   8564  13280   -852   1250   -760       C  
ATOM     66  C   ALA A  23     115.060 170.498 278.935  1.00 67.30           C  
ANISOU   66  C   ALA A  23     3715   8624  13233   -976   1259  -1003       C  
ATOM     67  O   ALA A  23     114.313 171.477 278.843  1.00 65.72           O  
ANISOU   67  O   ALA A  23     3589   8613  12768  -1029   1142   -959       O  
ATOM     68  CB  ALA A  23     116.669 171.036 280.770  1.00 65.72           C  
ANISOU   68  CB  ALA A  23     3534   8584  12852   -779   1233   -632       C  
ATOM     69  N   MET A  24     115.439 169.790 277.871  1.00 74.60           N  
ANISOU   69  N   MET A  24     4575   9380  14390  -1030   1402  -1266       N  
ATOM     70  CA  MET A  24     115.030 170.174 276.527  1.00 75.01           C  
ANISOU   70  CA  MET A  24     4647   9495  14358  -1167   1420  -1529       C  
ATOM     71  C   MET A  24     113.726 169.527 276.091  1.00 70.97           C  
ANISOU   71  C   MET A  24     4100   8896  13968  -1288   1383  -1671       C  
ATOM     72  O   MET A  24     113.129 169.979 275.107  1.00 71.14           O  
ANISOU   72  O   MET A  24     4145   9032  13854  -1417   1344  -1851       O  
ATOM     73  CB  MET A  24     116.125 169.827 275.513  1.00 71.51           C  
ANISOU   73  CB  MET A  24     4161   8952  14057  -1192   1611  -1793       C  
ATOM     74  CG  MET A  24     116.309 168.336 275.300  1.00 74.22           C  
ANISOU   74  CG  MET A  24     4399   8992  14808  -1200   1775  -1963       C  
ATOM     75  SD  MET A  24     117.790 167.905 274.365  1.00116.52           S  
ANISOU   75  SD  MET A  24     9706  14216  20350  -1194   2028  -2231       S  
ATOM     76  CE  MET A  24     117.221 168.103 272.680  1.00118.05           C  
ANISOU   76  CE  MET A  24     9922  14491  20440  -1424   2096  -2655       C  
ATOM     77  N   ILE A  25     113.273 168.481 276.784  1.00 71.96           N  
ANISOU   77  N   ILE A  25     4168   8831  14343  -1258   1393  -1595       N  
ATOM     78  CA  ILE A  25     111.956 167.929 276.488  1.00 85.77           C  
ANISOU   78  CA  ILE A  25     5890  10516  16183  -1377   1340  -1704       C  
ATOM     79  C   ILE A  25     110.876 168.674 277.264  1.00 84.31           C  
ANISOU   79  C   ILE A  25     5769  10516  15749  -1367   1142  -1463       C  
ATOM     80  O   ILE A  25     109.877 169.115 276.685  1.00 83.62           O  
ANISOU   80  O   ILE A  25     5703  10557  15510  -1478   1039  -1542       O  
ATOM     81  CB  ILE A  25     111.915 166.411 276.760  1.00 75.35           C  
ANISOU   81  CB  ILE A  25     4474   8879  15278  -1368   1467  -1767       C  
ATOM     82  CG1 ILE A  25     112.625 166.051 278.063  1.00 74.94           C  
ANISOU   82  CG1 ILE A  25     4398   8721  15355  -1195   1494  -1483       C  
ATOM     83  CG2 ILE A  25     112.527 165.650 275.600  1.00 80.35           C  
ANISOU   83  CG2 ILE A  25     5043   9332  16156  -1453   1671  -2117       C  
ATOM     84  CD1 ILE A  25     112.596 164.567 278.378  1.00 77.41           C  
ANISOU   84  CD1 ILE A  25     4607   8699  16107  -1172   1628  -1511       C  
ATOM     85  N   LEU A  26     111.069 168.850 278.575  1.00 84.04           N  
ANISOU   85  N   LEU A  26     5763  10511  15656  -1240   1090  -1174       N  
ATOM     86  CA  LEU A  26     110.095 169.578 279.385  1.00 67.68           C  
ANISOU   86  CA  LEU A  26     3758   8616  13341  -1230    930   -961       C  
ATOM     87  C   LEU A  26     109.805 170.948 278.790  1.00 66.10           C  
ANISOU   87  C   LEU A  26     3632   8671  12811  -1280    832   -973       C  
ATOM     88  O   LEU A  26     108.642 171.341 278.638  1.00 65.70           O  
ANISOU   88  O   LEU A  26     3601   8726  12635  -1351    719   -959       O  
ATOM     89  CB  LEU A  26     110.603 169.727 280.820  1.00 70.27           C  
ANISOU   89  CB  LEU A  26     4117   8981  13601  -1098    910   -690       C  
ATOM     90  CG  LEU A  26     111.057 168.480 281.576  1.00 67.91           C  
ANISOU   90  CG  LEU A  26     3740   8444  13620  -1021   1003   -614       C  
ATOM     91  CD1 LEU A  26     111.341 168.828 283.028  1.00 66.52           C  
ANISOU   91  CD1 LEU A  26     3603   8374  13296   -918    946   -344       C  
ATOM     92  CD2 LEU A  26     110.020 167.377 281.471  1.00 69.70           C  
ANISOU   92  CD2 LEU A  26     3899   8464  14120  -1092   1022   -693       C  
ATOM     93  N   LEU A  27     110.861 171.686 278.437  1.00 65.34           N  
ANISOU   93  N   LEU A  27     3572   8670  12584  -1243    879   -994       N  
ATOM     94  CA  LEU A  27     110.678 172.991 277.814  1.00 64.06           C  
ANISOU   94  CA  LEU A  27     3474   8725  12142  -1288    807  -1005       C  
ATOM     95  C   LEU A  27     109.959 172.880 276.480  1.00 65.48           C  
ANISOU   95  C   LEU A  27     3616   8913  12352  -1432    790  -1250       C  
ATOM     96  O   LEU A  27     109.285 173.826 276.066  1.00 64.71           O  
ANISOU   96  O   LEU A  27     3551   8989  12047  -1485    687  -1228       O  
ATOM     97  CB  LEU A  27     112.028 173.686 277.624  1.00 83.88           C  
ANISOU   97  CB  LEU A  27     6021  11307  14543  -1231    886  -1007       C  
ATOM     98  CG  LEU A  27     112.462 174.712 278.676  1.00 82.32           C  
ANISOU   98  CG  LEU A  27     5903  11273  14103  -1135    834   -758       C  
ATOM     99  CD1 LEU A  27     112.535 174.071 280.054  1.00 82.92           C  
ANISOU   99  CD1 LEU A  27     5967  11288  14252  -1050    823   -584       C  
ATOM    100  CD2 LEU A  27     113.797 175.351 278.305  1.00 60.79           C  
ANISOU  100  CD2 LEU A  27     3202   8609  11288  -1100    920   -796       C  
ATOM    101  N   SER A  28     110.088 171.745 275.795  1.00 67.73           N  
ANISOU  101  N   SER A  28     3826   9018  12892  -1505    894  -1492       N  
ATOM    102  CA  SER A  28     109.376 171.537 274.541  1.00 69.42           C  
ANISOU  102  CA  SER A  28     4002   9258  13117  -1672    877  -1762       C  
ATOM    103  C   SER A  28     107.970 170.989 274.747  1.00 82.77           C  
ANISOU  103  C   SER A  28     5657  10917  14873  -1744    768  -1742       C  
ATOM    104  O   SER A  28     107.065 171.336 273.978  1.00 85.10           O  
ANISOU  104  O   SER A  28     5946  11348  15041  -1867    664  -1845       O  
ATOM    105  CB  SER A  28     110.168 170.601 273.627  1.00 87.46           C  
ANISOU  105  CB  SER A  28     6229  11377  15623  -1746   1060  -2082       C  
ATOM    106  OG  SER A  28     110.251 169.300 274.174  1.00 83.73           O  
ANISOU  106  OG  SER A  28     5695  10647  15473  -1709   1156  -2094       O  
ATOM    107  N   VAL A  29     107.748 170.148 275.762  1.00 80.22           N  
ANISOU  107  N   VAL A  29     5310  10430  14741  -1677    786  -1610       N  
ATOM    108  CA  VAL A  29     106.372 169.739 276.028  1.00 78.71           C  
ANISOU  108  CA  VAL A  29     5093  10229  14585  -1744    680  -1570       C  
ATOM    109  C   VAL A  29     105.589 170.913 276.594  1.00 68.73           C  
ANISOU  109  C   VAL A  29     3890   9191  13034  -1702    517  -1324       C  
ATOM    110  O   VAL A  29     104.381 171.031 276.360  1.00 81.24           O  
ANISOU  110  O   VAL A  29     5456  10865  14547  -1789    399  -1330       O  
ATOM    111  CB  VAL A  29     106.299 168.508 276.956  1.00 78.46           C  
ANISOU  111  CB  VAL A  29     5014   9953  14845  -1691    755  -1500       C  
ATOM    112  CG1 VAL A  29     107.345 167.464 276.573  1.00 73.75           C  
ANISOU  112  CG1 VAL A  29     4357   9109  14555  -1687    950  -1694       C  
ATOM    113  CG2 VAL A  29     106.415 168.899 278.424  1.00 75.92           C  
ANISOU  113  CG2 VAL A  29     4743   9673  14429  -1540    710  -1173       C  
ATOM    114  N   SER A  30     106.254 171.810 277.326  1.00 66.58           N  
ANISOU  114  N   SER A  30     3688   9020  12591  -1577    513  -1117       N  
ATOM    115  CA  SER A  30     105.576 173.013 277.784  1.00 64.68           C  
ANISOU  115  CA  SER A  30     3508   8992  12075  -1546    386   -916       C  
ATOM    116  C   SER A  30     105.231 173.926 276.619  1.00 64.80           C  
ANISOU  116  C   SER A  30     3521   9177  11924  -1632    310  -1014       C  
ATOM    117  O   SER A  30     104.262 174.686 276.697  1.00 66.58           O  
ANISOU  117  O   SER A  30     3757   9553  11988  -1648    190   -899       O  
ATOM    118  CB  SER A  30     106.433 173.749 278.806  1.00 62.60           C  
ANISOU  118  CB  SER A  30     3323   8799  11663  -1413    416   -711       C  
ATOM    119  OG  SER A  30     106.242 173.205 280.098  1.00 62.21           O  
ANISOU  119  OG  SER A  30     3284   8677  11677  -1345    423   -563       O  
ATOM    120  N   MET A  31     106.000 173.861 275.530  1.00 65.85           N  
ANISOU  120  N   MET A  31     3634   9291  12095  -1691    384  -1233       N  
ATOM    121  CA  MET A  31     105.648 174.626 274.337  1.00 66.39           C  
ANISOU  121  CA  MET A  31     3690   9527  12009  -1794    312  -1361       C  
ATOM    122  C   MET A  31     104.438 174.021 273.640  1.00 68.39           C  
ANISOU  122  C   MET A  31     3873   9797  12315  -1942    216  -1517       C  
ATOM    123  O   MET A  31     103.505 174.734 273.256  1.00 77.86           O  
ANISOU  123  O   MET A  31     5056  11167  13359  -1993     73  -1467       O  
ATOM    124  CB  MET A  31     106.832 174.690 273.371  1.00 93.31           C  
ANISOU  124  CB  MET A  31     7104  12932  15418  -1833    438  -1587       C  
ATOM    125  CG  MET A  31     108.057 175.383 273.923  1.00 94.36           C  
ANISOU  125  CG  MET A  31     7303  13073  15477  -1701    527  -1448       C  
ATOM    126  SD  MET A  31     108.812 176.549 272.786  1.00 98.47           S  
ANISOU  126  SD  MET A  31     7855  13766  15792  -1749    573  -1580       S  
ATOM    127  CE  MET A  31     107.738 177.951 273.043  1.00100.63           C  
ANISOU  127  CE  MET A  31     8156  14238  15841  -1723    398  -1333       C  
ATOM    128  N   VAL A  32     104.437 172.698 273.468  1.00 70.27           N  
ANISOU  128  N   VAL A  32     4063   9856  12780  -2014    294  -1707       N  
ATOM    129  CA  VAL A  32     103.356 172.039 272.746  1.00 82.98           C  
ANISOU  129  CA  VAL A  32     5609  11479  14439  -2178    214  -1894       C  
ATOM    130  C   VAL A  32     102.057 172.025 273.551  1.00 82.38           C  
ANISOU  130  C   VAL A  32     5514  11433  14353  -2158     81  -1681       C  
ATOM    131  O   VAL A  32     100.972 171.961 272.964  1.00 73.42           O  
ANISOU  131  O   VAL A  32     4332  10401  13165  -2281    -43  -1760       O  
ATOM    132  CB  VAL A  32     103.827 170.627 272.332  1.00 74.80           C  
ANISOU  132  CB  VAL A  32     4533  10220  13666  -2266    371  -2180       C  
ATOM    133  CG1 VAL A  32     102.657 169.708 271.993  1.00 77.06           C  
ANISOU  133  CG1 VAL A  32     4762  10462  14057  -2419    308  -2330       C  
ATOM    134  CG2 VAL A  32     104.781 170.722 271.146  1.00 75.93           C  
ANISOU  134  CG2 VAL A  32     4686  10406  13757  -2356    479  -2469       C  
ATOM    135  N   VAL A  33     102.123 172.126 274.877  1.00 70.20           N  
ANISOU  135  N   VAL A  33     4010   9828  12834  -2013    102  -1419       N  
ATOM    136  CA  VAL A  33     100.935 172.111 275.719  1.00 69.75           C  
ANISOU  136  CA  VAL A  33     3942   9806  12754  -1995      4  -1231       C  
ATOM    137  C   VAL A  33     100.585 173.503 276.234  1.00 81.52           C  
ANISOU  137  C   VAL A  33     5483  11500  13991  -1905    -90   -980       C  
ATOM    138  O   VAL A  33      99.410 173.871 276.277  1.00 81.64           O  
ANISOU  138  O   VAL A  33     5467  11638  13913  -1942   -211   -895       O  
ATOM    139  CB  VAL A  33     101.099 171.116 276.892  1.00 69.65           C  
ANISOU  139  CB  VAL A  33     3934   9585  12945  -1920    102  -1146       C  
ATOM    140  CG1 VAL A  33      99.831 171.067 277.733  1.00 69.38           C  
ANISOU  140  CG1 VAL A  33     3889   9595  12879  -1919     16   -986       C  
ATOM    141  CG2 VAL A  33     101.448 169.729 276.375  1.00 72.03           C  
ANISOU  141  CG2 VAL A  33     4176   9656  13535  -2006    218  -1396       C  
ATOM    142  N   GLY A  34     101.583 174.289 276.630  1.00 79.99           N  
ANISOU  142  N   GLY A  34     5362  11342  13689  -1791    -28   -868       N  
ATOM    143  CA  GLY A  34     101.330 175.582 277.235  1.00 78.35           C  
ANISOU  143  CA  GLY A  34     5210  11304  13254  -1705    -84   -648       C  
ATOM    144  C   GLY A  34     101.023 176.697 276.258  1.00 78.90           C  
ANISOU  144  C   GLY A  34     5258  11553  13169  -1747   -180   -651       C  
ATOM    145  O   GLY A  34     100.191 177.564 276.546  1.00 78.28           O  
ANISOU  145  O   GLY A  34     5176  11617  12948  -1721   -264   -499       O  
ATOM    146  N   LEU A  35     101.700 176.705 275.108  1.00 64.79           N  
ANISOU  146  N   LEU A  35     3449   9763  11405  -1812   -157   -839       N  
ATOM    147  CA  LEU A  35     101.364 177.679 274.071  1.00 65.30           C  
ANISOU  147  CA  LEU A  35     3478   9998  11334  -1867   -257   -873       C  
ATOM    148  C   LEU A  35      99.917 177.556 273.617  1.00 66.86           C  
ANISOU  148  C   LEU A  35     3587  10294  11521  -1964   -420   -884       C  
ATOM    149  O   LEU A  35      99.159 178.528 273.767  1.00 66.26           O  
ANISOU  149  O   LEU A  35     3490  10353  11332  -1923   -522   -700       O  
ATOM    150  CB  LEU A  35     102.334 177.547 272.897  1.00 78.62           C  
ANISOU  150  CB  LEU A  35     5161  11686  13024  -1945   -186  -1138       C  
ATOM    151  CG  LEU A  35     103.785 177.963 273.085  1.00 65.07           C  
ANISOU  151  CG  LEU A  35     3520   9923  11282  -1857    -36  -1132       C  
ATOM    152  CD1 LEU A  35     104.514 177.686 271.791  1.00 66.73           C  
ANISOU  152  CD1 LEU A  35     3712  10164  11480  -1974     36  -1446       C  
ATOM    153  CD2 LEU A  35     103.863 179.431 273.451  1.00 63.22           C  
ANISOU  153  CD2 LEU A  35     3330   9807  10883  -1758    -62   -907       C  
ATOM    154  N   PRO A  36      99.452 176.402 273.086  1.00 69.00           N  
ANISOU  154  N   PRO A  36     3801  10504  11911  -2093   -448  -1090       N  
ATOM    155  CA  PRO A  36      98.093 176.359 272.525  1.00 70.75           C  
ANISOU  155  CA  PRO A  36     3933  10850  12097  -2201   -620  -1112       C  
ATOM    156  C   PRO A  36      97.012 176.563 273.575  1.00 83.70           C  
ANISOU  156  C   PRO A  36     5555  12519  13728  -2134   -685   -856       C  
ATOM    157  O   PRO A  36      96.053 177.311 273.356  1.00 84.35           O  
ANISOU  157  O   PRO A  36     5576  12759  13714  -2140   -826   -734       O  
ATOM    158  CB  PRO A  36      98.012 174.954 271.920  1.00 73.15           C  
ANISOU  158  CB  PRO A  36     4201  11050  12542  -2354   -591  -1404       C  
ATOM    159  CG  PRO A  36      98.915 174.150 272.756  1.00 72.23           C  
ANISOU  159  CG  PRO A  36     4141  10706  12598  -2280   -410  -1412       C  
ATOM    160  CD  PRO A  36     100.058 175.057 273.119  1.00 70.00           C  
ANISOU  160  CD  PRO A  36     3935  10433  12228  -2141   -320  -1288       C  
ATOM    161  N   GLY A  37      97.167 175.886 274.714  1.00 82.76           N  
ANISOU  161  N   GLY A  37     5484  12256  13705  -2071   -575   -788       N  
ATOM    162  CA  GLY A  37      96.175 175.984 275.768  1.00 82.43           C  
ANISOU  162  CA  GLY A  37     5436  12258  13626  -2020   -603   -605       C  
ATOM    163  C   GLY A  37      95.992 177.405 276.258  1.00 81.50           C  
ANISOU  163  C   GLY A  37     5351  12309  13307  -1908   -624   -399       C  
ATOM    164  O   GLY A  37      94.885 177.947 276.225  1.00 83.70           O  
ANISOU  164  O   GLY A  37     5565  12743  13495  -1920   -725   -313       O  
ATOM    165  N   ASN A  38      97.085 178.040 276.687  1.00 78.54           N  
ANISOU  165  N   ASN A  38     5069  11913  12859  -1802   -520   -338       N  
ATOM    166  CA  ASN A  38      96.990 179.405 277.191  1.00 62.76           C  
ANISOU  166  CA  ASN A  38     3111  10066  10669  -1700   -509   -191       C  
ATOM    167  C   ASN A  38      96.522 180.364 276.108  1.00 80.99           C  
ANISOU  167  C   ASN A  38     5333  12539  12899  -1736   -635   -152       C  
ATOM    168  O   ASN A  38      95.744 181.282 276.388  1.00 63.30           O  
ANISOU  168  O   ASN A  38     3114  10418  10518  -1661   -658    -91       O  
ATOM    169  CB  ASN A  38      98.334 179.843 277.769  1.00 60.84           C  
ANISOU  169  CB  ASN A  38     2982   9762  10371  -1601   -377   -157       C  
ATOM    170  CG  ASN A  38      98.467 179.504 279.241  1.00 76.55           C  
ANISOU  170  CG  ASN A  38     5060  11673  12353  -1521   -277   -119       C  
ATOM    171  OD1 ASN A  38      98.001 180.247 280.103  1.00 77.48           O  
ANISOU  171  OD1 ASN A  38     5221  11866  12350  -1451   -254    -68       O  
ATOM    172  ND2 ASN A  38      99.101 178.374 279.537  1.00 74.76           N  
ANISOU  172  ND2 ASN A  38     4855  11277  12275  -1529   -215   -170       N  
ATOM    173  N   THR A  39      96.963 180.160 274.860  1.00 82.48           N  
ANISOU  173  N   THR A  39     5477  12679  13181  -1818   -700   -259       N  
ATOM    174  CA  THR A  39      96.509 181.027 273.776  1.00 66.26           C  
ANISOU  174  CA  THR A  39     3333  10736  11105  -1847   -847   -233       C  
ATOM    175  C   THR A  39      95.007 180.888 273.561  1.00 67.93           C  
ANISOU  175  C   THR A  39     3452  11036  11323  -1898  -1007   -187       C  
ATOM    176  O   THR A  39      94.334 181.856 273.194  1.00 68.45           O  
ANISOU  176  O   THR A  39     3489  11150  11367  -1833  -1116    -78       O  
ATOM    177  CB  THR A  39      97.266 180.719 272.483  1.00 67.68           C  
ANISOU  177  CB  THR A  39     3506  10892  11319  -1938   -859   -502       C  
ATOM    178  OG1 THR A  39      98.565 180.204 272.791  1.00 66.63           O  
ANISOU  178  OG1 THR A  39     3469  10632  11216  -1918   -684   -606       O  
ATOM    179  CG2 THR A  39      97.446 181.984 271.665  1.00 67.88           C  
ANISOU  179  CG2 THR A  39     3503  11039  11248  -1901   -917   -504       C  
ATOM    180  N   PHE A  40      94.464 179.692 273.792  1.00 68.95           N  
ANISOU  180  N   PHE A  40     3538  11135  11524  -1996  -1018   -275       N  
ATOM    181  CA  PHE A  40      93.018 179.506 273.728  1.00 84.98           C  
ANISOU  181  CA  PHE A  40     5484  13258  13547  -2046  -1149   -231       C  
ATOM    182  C   PHE A  40      92.340 180.066 274.975  1.00 85.28           C  
ANISOU  182  C   PHE A  40     5589  13400  13413  -1915  -1048   -132       C  
ATOM    183  O   PHE A  40      91.345 180.795 274.876  1.00 86.12           O  
ANISOU  183  O   PHE A  40     5652  13678  13390  -1866  -1109   -115       O  
ATOM    184  CB  PHE A  40      92.694 178.021 273.551  1.00 72.27           C  
ANISOU  184  CB  PHE A  40     3825  11557  12079  -2195  -1167   -412       C  
ATOM    185  CG  PHE A  40      91.220 177.705 273.530  1.00 74.04           C  
ANISOU  185  CG  PHE A  40     3935  11883  12315  -2275  -1300   -369       C  
ATOM    186  CD1 PHE A  40      90.285 178.644 273.117  1.00 74.90           C  
ANISOU  186  CD1 PHE A  40     3996  12123  12340  -2225  -1446   -238       C  
ATOM    187  CD2 PHE A  40      90.773 176.456 273.924  1.00 84.66           C  
ANISOU  187  CD2 PHE A  40     5269  13127  13770  -2362  -1257   -479       C  
ATOM    188  CE1 PHE A  40      88.937 178.344 273.109  1.00 76.66           C  
ANISOU  188  CE1 PHE A  40     4130  12430  12566  -2284  -1554   -205       C  
ATOM    189  CE2 PHE A  40      89.427 176.149 273.911  1.00 76.75           C  
ANISOU  189  CE2 PHE A  40     4158  12222  12781  -2444  -1369   -448       C  
ATOM    190  CZ  PHE A  40      88.509 177.095 273.503  1.00 77.56           C  
ANISOU  190  CZ  PHE A  40     4198  12498  12773  -2406  -1517   -314       C  
ATOM    191  N   VAL A  41      92.860 179.730 276.160  1.00 84.35           N  
ANISOU  191  N   VAL A  41     5557  13184  13308  -1850   -884   -154       N  
ATOM    192  CA  VAL A  41      92.242 180.191 277.402  1.00 65.87           C  
ANISOU  192  CA  VAL A  41     3266  10868  10894  -1729   -791   -153       C  
ATOM    193  C   VAL A  41      92.182 181.713 277.436  1.00 79.52           C  
ANISOU  193  C   VAL A  41     5032  12683  12498  -1585   -763   -179       C  
ATOM    194  O   VAL A  41      91.157 182.299 277.806  1.00 65.12           O  
ANISOU  194  O   VAL A  41     3164  10894  10686  -1507   -779   -222       O  
ATOM    195  CB  VAL A  41      92.990 179.624 278.624  1.00 64.15           C  
ANISOU  195  CB  VAL A  41     3138  10492  10743  -1687   -648   -138       C  
ATOM    196  CG1 VAL A  41      92.480 180.263 279.900  1.00 62.74           C  
ANISOU  196  CG1 VAL A  41     3021  10302  10514  -1565   -567   -120       C  
ATOM    197  CG2 VAL A  41      92.826 178.115 278.700  1.00 65.39           C  
ANISOU  197  CG2 VAL A  41     3259  10511  11076  -1794   -657   -177       C  
ATOM    198  N   VAL A  42      93.270 182.379 277.036  1.00 78.72           N  
ANISOU  198  N   VAL A  42     4995  12577  12337  -1546   -722   -168       N  
ATOM    199  CA  VAL A  42      93.262 183.837 276.976  1.00 77.64           C  
ANISOU  199  CA  VAL A  42     4869  12454  12176  -1408   -694   -247       C  
ATOM    200  C   VAL A  42      92.356 184.337 275.862  1.00 78.69           C  
ANISOU  200  C   VAL A  42     4856  12650  12394  -1394   -845   -367       C  
ATOM    201  O   VAL A  42      91.876 185.476 275.916  1.00 77.62           O  
ANISOU  201  O   VAL A  42     4668  12447  12378  -1270   -880   -329       O  
ATOM    202  CB  VAL A  42      94.693 184.383 276.798  1.00 61.93           C  
ANISOU  202  CB  VAL A  42     2976  10426  10130  -1379   -605   -229       C  
ATOM    203  CG1 VAL A  42      95.164 184.204 275.362  1.00 68.98           C  
ANISOU  203  CG1 VAL A  42     3810  11431  10969  -1490   -705   -197       C  
ATOM    204  CG2 VAL A  42      94.768 185.844 277.205  1.00 60.77           C  
ANISOU  204  CG2 VAL A  42     2859  10182  10048  -1231   -540   -250       C  
ATOM    205  N   TRP A  43      92.099 183.505 274.851  1.00 67.38           N  
ANISOU  205  N   TRP A  43     3344  11345  10913  -1535   -961   -423       N  
ATOM    206  CA  TRP A  43      91.268 183.924 273.729  1.00 72.58           C  
ANISOU  206  CA  TRP A  43     3838  11797  11941  -1471  -1179   -575       C  
ATOM    207  C   TRP A  43      89.806 184.028 274.143  1.00 73.96           C  
ANISOU  207  C   TRP A  43     3918  12104  12081  -1442  -1244   -530       C  
ATOM    208  O   TRP A  43      89.181 185.086 274.000  1.00 74.86           O  
ANISOU  208  O   TRP A  43     3940  12245  12260  -1343  -1342   -388       O  
ATOM    209  CB  TRP A  43      91.443 182.941 272.568  1.00 71.70           C  
ANISOU  209  CB  TRP A  43     3679  11384  12181  -1644  -1448   -247       C  
ATOM    210  CG  TRP A  43      90.547 183.182 271.395  1.00 74.45           C  
ANISOU  210  CG  TRP A  43     3842  12035  12410  -1723  -1666   -348       C  
ATOM    211  CD1 TRP A  43      90.000 184.370 271.001  1.00 75.21           C  
ANISOU  211  CD1 TRP A  43     3828  12379  12368  -1635  -1754   -332       C  
ATOM    212  CD2 TRP A  43      90.091 182.201 270.459  1.00 77.05           C  
ANISOU  212  CD2 TRP A  43     4071  12514  12690  -1940  -1849   -383       C  
ATOM    213  NE1 TRP A  43      89.231 184.188 269.877  1.00 78.14           N  
ANISOU  213  NE1 TRP A  43     4099  12995  12595  -1749  -1979   -323       N  
ATOM    214  CE2 TRP A  43      89.270 182.864 269.524  1.00 98.38           C  
ANISOU  214  CE2 TRP A  43     6653  15503  15223  -1939  -2036   -429       C  
ATOM    215  CE3 TRP A  43      90.297 180.824 270.321  1.00 77.86           C  
ANISOU  215  CE3 TRP A  43     4185  12613  12784  -2147  -1845   -425       C  
ATOM    216  CZ2 TRP A  43      88.656 182.198 268.464  1.00100.86           C  
ANISOU  216  CZ2 TRP A  43     6900  16033  15389  -2119  -2219   -535       C  
ATOM    217  CZ3 TRP A  43      89.687 180.164 269.268  1.00 97.29           C  
ANISOU  217  CZ3 TRP A  43     6570  15258  15139  -2318  -2002   -623       C  
ATOM    218  CH2 TRP A  43      88.875 180.852 268.353  1.00100.51           C  
ANISOU  218  CH2 TRP A  43     6883  15910  15395  -2307  -2195   -667       C  
ATOM    219  N   SER A  44      89.246 182.935 274.669  1.00 71.05           N  
ANISOU  219  N   SER A  44     3558  11895  11543  -1559  -1192   -541       N  
ATOM    220  CA  SER A  44      87.821 182.896 274.980  1.00 72.31           C  
ANISOU  220  CA  SER A  44     3609  12092  11775  -1534  -1266   -534       C  
ATOM    221  C   SER A  44      87.418 184.035 275.905  1.00 75.79           C  
ANISOU  221  C   SER A  44     4057  12458  12283  -1368  -1211   -398       C  
ATOM    222  O   SER A  44      86.410 184.711 275.670  1.00 77.44           O  
ANISOU  222  O   SER A  44     4135  12702  12586  -1294  -1329   -345       O  
ATOM    223  CB  SER A  44      87.464 181.546 275.600  1.00 72.56           C  
ANISOU  223  CB  SER A  44     3665  12217  11688  -1700  -1214   -434       C  
ATOM    224  OG  SER A  44      86.306 181.645 276.409  1.00 72.80           O  
ANISOU  224  OG  SER A  44     3633  12226  11801  -1637  -1206   -421       O  
ATOM    225  N   ILE A  45      88.216 184.284 276.944  1.00 73.29           N  
ANISOU  225  N   ILE A  45     3884  12053  11909  -1317  -1040   -317       N  
ATOM    226  CA  ILE A  45      87.906 185.307 277.933  1.00 71.69           C  
ANISOU  226  CA  ILE A  45     3707  11780  11753  -1185   -962   -203       C  
ATOM    227  C   ILE A  45      87.880 186.712 277.341  1.00 71.64           C  
ANISOU  227  C   ILE A  45     3637  11773  11809  -1071  -1030   -104       C  
ATOM    228  O   ILE A  45      87.311 187.628 277.945  1.00 71.38           O  
ANISOU  228  O   ILE A  45     3619  11694  11810   -965   -995     33       O  
ATOM    229  CB  ILE A  45      88.912 185.185 279.097  1.00 64.67           C  
ANISOU  229  CB  ILE A  45     2996  10782  10795  -1173   -780   -164       C  
ATOM    230  CG1 ILE A  45      88.945 183.733 279.585  1.00 64.64           C  
ANISOU  230  CG1 ILE A  45     3034  10774  10752  -1290   -743   -185       C  
ATOM    231  CG2 ILE A  45      88.553 186.123 280.238  1.00 70.04           C  
ANISOU  231  CG2 ILE A  45     3724  11377  11510  -1063   -689    -64       C  
ATOM    232  CD1 ILE A  45      89.465 183.550 280.996  1.00 71.86           C  
ANISOU  232  CD1 ILE A  45     4080  11571  11652  -1262   -599   -126       C  
ATOM    233  N   LEU A  46      88.453 186.902 276.156  1.00 71.66           N  
ANISOU  233  N   LEU A  46     3597  11812  11817  -1095  -1130   -119       N  
ATOM    234  CA  LEU A  46      88.428 188.201 275.493  1.00 69.15           C  
ANISOU  234  CA  LEU A  46     3253  11518  11502   -999  -1208     77       C  
ATOM    235  C   LEU A  46      87.449 188.283 274.332  1.00 94.08           C  
ANISOU  235  C   LEU A  46     6247  14828  14672  -1015  -1444    146       C  
ATOM    236  O   LEU A  46      86.714 189.266 274.226  1.00 95.71           O  
ANISOU  236  O   LEU A  46     6396  15099  14870   -912  -1505    344       O  
ATOM    237  CB  LEU A  46      89.831 188.570 275.008  1.00 68.07           C  
ANISOU  237  CB  LEU A  46     3203  11350  11310  -1012  -1152    101       C  
ATOM    238  CG  LEU A  46      90.607 189.441 275.989  1.00 65.70           C  
ANISOU  238  CG  LEU A  46     3051  10933  10979   -925   -952    186       C  
ATOM    239  CD1 LEU A  46      92.093 189.267 275.772  1.00 64.36           C  
ANISOU  239  CD1 LEU A  46     2974  10715  10764   -978   -858    109       C  
ATOM    240  CD2 LEU A  46      90.202 190.907 275.838  1.00 66.30           C  
ANISOU  240  CD2 LEU A  46     3101  11041  11048   -805   -967    435       C  
ATOM    241  N   LYS A  47      87.408 187.277 273.462  1.00 73.62           N  
ANISOU  241  N   LYS A  47     3577  12301  12096  -1146  -1582     -1       N  
ATOM    242  CA  LYS A  47      86.593 187.345 272.252  1.00 76.64           C  
ANISOU  242  CA  LYS A  47     3819  12866  12434  -1188  -1832     78       C  
ATOM    243  C   LYS A  47      85.141 186.948 272.476  1.00 87.49           C  
ANISOU  243  C   LYS A  47     5062  14289  13892  -1185  -1925     29       C  
ATOM    244  O   LYS A  47      84.249 187.540 271.862  1.00 88.29           O  
ANISOU  244  O   LYS A  47     5055  14548  13942  -1139  -2091    185       O  
ATOM    245  CB  LYS A  47      87.184 186.448 271.171  1.00 82.79           C  
ANISOU  245  CB  LYS A  47     4584  13699  13174  -1360  -1953    -43       C  
ATOM    246  N   ARG A  48      84.872 185.980 273.354  1.00 90.20           N  
ANISOU  246  N   ARG A  48     5405  14537  14329  -1235  -1813   -171       N  
ATOM    247  CA  ARG A  48      83.549 185.376 273.450  1.00 94.82           C  
ANISOU  247  CA  ARG A  48     5850  15193  14984  -1275  -1903   -257       C  
ATOM    248  C   ARG A  48      82.869 185.645 274.791  1.00 96.72           C  
ANISOU  248  C   ARG A  48     6114  15403  15234  -1186  -1745   -203       C  
ATOM    249  O   ARG A  48      82.077 184.818 275.258  1.00 97.11           O  
ANISOU  249  O   ARG A  48     6126  15475  15297  -1253  -1719   -299       O  
ATOM    250  CB  ARG A  48      83.629 183.866 273.213  1.00 97.07           C  
ANISOU  250  CB  ARG A  48     6172  15416  15294  -1442  -1901   -482       C  
ATOM    251  N   MET A  49      83.137 186.790 275.418  1.00 94.69           N  
ANISOU  251  N   MET A  49     5956  15070  14953  -1047  -1634    -13       N  
ATOM    252  CA  MET A  49      82.501 187.122 276.686  1.00 93.14           C  
ANISOU  252  CA  MET A  49     5793  14808  14789   -970  -1498     60       C  
ATOM    253  C   MET A  49      82.145 188.597 276.731  1.00 90.51           C  
ANISOU  253  C   MET A  49     5448  14458  14485   -812  -1507    300       C  
ATOM    254  O   MET A  49      82.881 189.444 276.218  1.00 88.95           O  
ANISOU  254  O   MET A  49     5303  14251  14244   -752  -1515    429       O  
ATOM    255  CB  MET A  49      83.398 186.786 277.884  1.00 87.69           C  
ANISOU  255  CB  MET A  49     5286  13986  14047   -992  -1276     14       C  
ATOM    256  CG  MET A  49      83.696 185.310 278.032  1.00 86.55           C  
ANISOU  256  CG  MET A  49     5159  13875  13850  -1147  -1237   -161       C  
ATOM    257  SD  MET A  49      83.791 184.787 279.749  1.00 82.85           S  
ANISOU  257  SD  MET A  49     4837  13293  13349  -1165  -1033   -126       S  
ATOM    258  CE  MET A  49      84.614 186.187 280.491  1.00 80.73           C  
ANISOU  258  CE  MET A  49     4735  12869  13071  -1017   -898     10       C  
ATOM    259  N   ARG A  50      81.007 188.894 277.348  1.00 93.82           N  
ANISOU  259  N   ARG A  50     5790  14882  14976   -750  -1495    370       N  
ATOM    260  CA  ARG A  50      80.565 190.270 277.511  1.00 96.00           C  
ANISOU  260  CA  ARG A  50     6042  15134  15300   -600  -1479    601       C  
ATOM    261  C   ARG A  50      80.881 190.788 278.910  1.00 99.78           C  
ANISOU  261  C   ARG A  50     6666  15443  15804   -544  -1251    646       C  
ATOM    262  O   ARG A  50      81.573 191.801 279.066  1.00102.81           O  
ANISOU  262  O   ARG A  50     7143  15742  16178   -464  -1157    776       O  
ATOM    263  CB  ARG A  50      79.061 190.378 277.208  1.00 97.21           C  
ANISOU  263  CB  ARG A  50     5995  15409  15532   -559  -1623    666       C  
ATOM    264  N   LYS A  51      80.381 190.104 279.936  1.00 97.01           N  
ANISOU  264  N   LYS A  51     6331  15048  15480   -596  -1162    544       N  
ATOM    265  CA  LYS A  51      80.661 190.431 281.332  1.00 91.07           C  
ANISOU  265  CA  LYS A  51     5721  14147  14733   -570   -961    569       C  
ATOM    266  C   LYS A  51      81.775 189.505 281.810  1.00 84.73           C  
ANISOU  266  C   LYS A  51     5078  13284  13831   -672   -864    427       C  
ATOM    267  O   LYS A  51      81.536 188.335 282.120  1.00 82.45           O  
ANISOU  267  O   LYS A  51     4780  13027  13521   -773   -865    308       O  
ATOM    268  CB  LYS A  51      79.404 190.289 282.185  1.00 73.20           C  
ANISOU  268  CB  LYS A  51     3375  11884  12554   -563   -930    578       C  
ATOM    269  N   ARG A  52      82.999 190.028 281.858  1.00 81.60           N  
ANISOU  269  N   ARG A  52     4822  12808  13375   -648   -778    454       N  
ATOM    270  CA  ARG A  52      84.155 189.241 282.275  1.00 80.23           C  
ANISOU  270  CA  ARG A  52     4798  12582  13105   -731   -688    341       C  
ATOM    271  C   ARG A  52      84.172 189.156 283.796  1.00 76.43           C  
ANISOU  271  C   ARG A  52     4431  11995  12613   -739   -536    348       C  
ATOM    272  O   ARG A  52      84.492 190.137 284.476  1.00 74.34           O  
ANISOU  272  O   ARG A  52     4248  11636  12363   -675   -428    439       O  
ATOM    273  CB  ARG A  52      85.443 189.860 281.740  1.00 81.75           C  
ANISOU  273  CB  ARG A  52     5081  12739  13240   -704   -657    367       C  
ATOM    274  CG  ARG A  52      85.589 189.774 280.230  1.00 85.21           C  
ANISOU  274  CG  ARG A  52     5416  13285  13676   -720   -813    355       C  
ATOM    275  CD  ARG A  52      86.886 190.411 279.772  1.00 65.39           C  
ANISOU  275  CD  ARG A  52     2998  10736  11112   -698   -766    394       C  
ATOM    276  NE  ARG A  52      87.028 190.352 278.323  1.00 66.97           N  
ANISOU  276  NE  ARG A  52     3097  11046  11303   -721   -924    402       N  
ATOM    277  CZ  ARG A  52      86.496 191.237 277.486  1.00 85.53           C  
ANISOU  277  CZ  ARG A  52     5341  13478  13680   -648  -1040    571       C  
ATOM    278  NH1 ARG A  52      85.782 192.253 277.954  1.00 85.24           N  
ANISOU  278  NH1 ARG A  52     5276  13410  13703   -538  -1001    738       N  
ATOM    279  NH2 ARG A  52      86.678 191.107 276.180  1.00 87.36           N  
ANISOU  279  NH2 ARG A  52     5491  13833  13867   -688  -1199    589       N  
ATOM    280  N   SER A  53      83.825 187.986 284.331  1.00 75.54           N  
ANISOU  280  N   SER A  53     4300  11873  12530   -826   -537    309       N  
ATOM    281  CA  SER A  53      83.753 187.808 285.772  1.00 72.86           C  
ANISOU  281  CA  SER A  53     4031  11405  12249   -841   -421    378       C  
ATOM    282  C   SER A  53      85.117 188.058 286.410  1.00 62.32           C  
ANISOU  282  C   SER A  53     2866   9965  10846   -836   -305    394       C  
ATOM    283  O   SER A  53      86.162 187.991 285.758  1.00 61.39           O  
ANISOU  283  O   SER A  53     2813   9873  10639   -848   -314    335       O  
ATOM    284  CB  SER A  53      83.256 186.401 286.111  1.00 74.70           C  
ANISOU  284  CB  SER A  53     4214  11643  12526   -942   -450    333       C  
ATOM    285  OG  SER A  53      82.946 186.272 287.489  1.00 73.35           O  
ANISOU  285  OG  SER A  53     4081  11356  12432   -949   -353    406       O  
ATOM    286  N   VAL A  54      85.094 188.377 287.707  1.00 83.02           N  
ANISOU  286  N   VAL A  54     5552  12480  13513   -822   -195    468       N  
ATOM    287  CA  VAL A  54      86.341 188.558 288.446  1.00 81.38           C  
ANISOU  287  CA  VAL A  54     5493  12186  13241   -827    -88    477       C  
ATOM    288  C   VAL A  54      87.151 187.269 288.431  1.00 81.33           C  
ANISOU  288  C   VAL A  54     5541  12167  13192   -902   -105    415       C  
ATOM    289  O   VAL A  54      88.382 187.290 288.307  1.00 80.76           O  
ANISOU  289  O   VAL A  54     5566  12080  13039   -906    -70    385       O  
ATOM    290  CB  VAL A  54      86.055 189.034 289.884  1.00 59.79           C  
ANISOU  290  CB  VAL A  54     2797   9362  10558   -815     25    552       C  
ATOM    291  CG1 VAL A  54      87.356 189.273 290.629  1.00 58.19           C  
ANISOU  291  CG1 VAL A  54     2735   9099  10277   -825    125    551       C  
ATOM    292  CG2 VAL A  54      85.206 190.299 289.876  1.00 60.55           C  
ANISOU  292  CG2 VAL A  54     2827   9467  10714   -740     51    618       C  
ATOM    293  N   THR A  55      86.473 186.125 288.543  1.00 60.46           N  
ANISOU  293  N   THR A  55     2829   9530  10613   -963   -153    398       N  
ATOM    294  CA  THR A  55      87.150 184.844 288.398  1.00 70.36           C  
ANISOU  294  CA  THR A  55     4115  10769  11849  -1034   -173    346       C  
ATOM    295  C   THR A  55      87.621 184.596 286.969  1.00 72.15           C  
ANISOU  295  C   THR A  55     4314  11101  11999  -1059   -255    255       C  
ATOM    296  O   THR A  55      88.454 183.710 286.754  1.00 74.01           O  
ANISOU  296  O   THR A  55     4593  11325  12204  -1111   -254    213       O  
ATOM    297  CB  THR A  55      86.226 183.715 288.864  1.00 61.51           C  
ANISOU  297  CB  THR A  55     2918   9621  10832  -1099   -196    355       C  
ATOM    298  OG1 THR A  55      85.467 184.163 289.994  1.00 67.80           O  
ANISOU  298  OG1 THR A  55     3702  10359  11701  -1072   -135    433       O  
ATOM    299  CG2 THR A  55      87.036 182.487 289.277  1.00 61.09           C  
ANISOU  299  CG2 THR A  55     2927   9488  10796  -1157   -167    347       C  
ATOM    300  N   ALA A  56      87.127 185.360 285.996  1.00 73.25           N  
ANISOU  300  N   ALA A  56     4376  11346  12110  -1022   -323    226       N  
ATOM    301  CA  ALA A  56      87.620 185.285 284.626  1.00 73.84           C  
ANISOU  301  CA  ALA A  56     4422  11538  12096  -1044   -399    131       C  
ATOM    302  C   ALA A  56      88.750 186.267 284.350  1.00 72.38           C  
ANISOU  302  C   ALA A  56     4334  11341  11828   -985   -346    129       C  
ATOM    303  O   ALA A  56      89.330 186.234 283.261  1.00 72.74           O  
ANISOU  303  O   ALA A  56     4367  11475  11794  -1004   -392     45       O  
ATOM    304  CB  ALA A  56      86.480 185.527 283.631  1.00 75.74           C  
ANISOU  304  CB  ALA A  56     4509  11916  12354  -1037   -519     87       C  
ATOM    305  N   LEU A  57      89.064 187.151 285.295  1.00 58.63           N  
ANISOU  305  N   LEU A  57     2680   9498  10099   -924   -246    212       N  
ATOM    306  CA  LEU A  57      90.214 188.034 285.167  1.00 57.26           C  
ANISOU  306  CA  LEU A  57     2606   9303   9848   -884   -178    211       C  
ATOM    307  C   LEU A  57      91.451 187.447 285.825  1.00 56.01           C  
ANISOU  307  C   LEU A  57     2561   9077   9643   -922   -102    200       C  
ATOM    308  O   LEU A  57      92.546 187.519 285.263  1.00 90.12           O  
ANISOU  308  O   LEU A  57     6934  13426  13882   -931    -85    147       O  
ATOM    309  CB  LEU A  57      89.907 189.407 285.770  1.00 56.99           C  
ANISOU  309  CB  LEU A  57     2595   9212   9846   -807   -106    303       C  
ATOM    310  CG  LEU A  57      88.734 190.151 285.142  1.00 58.32           C  
ANISOU  310  CG  LEU A  57     2647   9437  10074   -746   -175    342       C  
ATOM    311  CD1 LEU A  57      88.660 191.563 285.689  1.00 63.48           C  
ANISOU  311  CD1 LEU A  57     3336  10029  10756   -671    -79    440       C  
ATOM    312  CD2 LEU A  57      88.883 190.161 283.636  1.00 68.16           C  
ANISOU  312  CD2 LEU A  57     3820  10783  11295   -742   -283    289       C  
ATOM    313  N   MET A  58      91.293 186.878 287.022  1.00 55.94           N  
ANISOU  313  N   MET A  58     2583   8982   9690   -942    -55    253       N  
ATOM    314  CA  MET A  58      92.386 186.132 287.628  1.00 79.90           C  
ANISOU  314  CA  MET A  58     5702  11956  12700   -975     -3    250       C  
ATOM    315  C   MET A  58      92.911 185.095 286.648  1.00 75.99           C  
ANISOU  315  C   MET A  58     5183  11516  12174  -1029    -62    176       C  
ATOM    316  O   MET A  58      94.103 185.078 286.327  1.00 71.42           O  
ANISOU  316  O   MET A  58     4664  10949  11522  -1034    -32    141       O  
ATOM    317  CB  MET A  58      91.925 185.470 288.929  1.00 83.99           C  
ANISOU  317  CB  MET A  58     6224  12385  13303   -994     32    314       C  
ATOM    318  CG  MET A  58      91.344 186.432 289.965  1.00 82.50           C  
ANISOU  318  CG  MET A  58     6049  12157  13142   -957     97    384       C  
ATOM    319  SD  MET A  58      92.517 187.679 290.534  1.00 78.63           S  
ANISOU  319  SD  MET A  58     5669  11650  12555   -923    204    396       S  
ATOM    320  CE  MET A  58      91.610 188.407 291.896  1.00 76.94           C  
ANISOU  320  CE  MET A  58     5445  11393  12396   -910    281    471       C  
ATOM    321  N   VAL A  59      92.016 184.255 286.120  1.00 56.62           N  
ANISOU  321  N   VAL A  59     2633   9108   9772  -1078   -143    147       N  
ATOM    322  CA  VAL A  59      92.422 183.272 285.118  1.00 73.10           C  
ANISOU  322  CA  VAL A  59     4684  11263  11827  -1149   -199     76       C  
ATOM    323  C   VAL A  59      93.070 183.967 283.932  1.00 73.94           C  
ANISOU  323  C   VAL A  59     4792  11487  11815  -1141   -221      8       C  
ATOM    324  O   VAL A  59      94.118 183.539 283.439  1.00 72.22           O  
ANISOU  324  O   VAL A  59     4610  11295  11534  -1178   -208    -24       O  
ATOM    325  CB  VAL A  59      91.224 182.415 284.675  1.00 58.78           C  
ANISOU  325  CB  VAL A  59     2751   9504  10078  -1218   -286     50       C  
ATOM    326  CG1 VAL A  59      91.583 181.618 283.432  1.00 59.46           C  
ANISOU  326  CG1 VAL A  59     2788   9698  10105  -1309   -352    -25       C  
ATOM    327  CG2 VAL A  59      90.812 181.482 285.788  1.00 59.20           C  
ANISOU  327  CG2 VAL A  59     2807   9428  10257  -1242   -253    108       C  
ATOM    328  N   LEU A  60      92.464 185.061 283.468  1.00 78.41           N  
ANISOU  328  N   LEU A  60     5314  12117  12361  -1090   -252     -9       N  
ATOM    329  CA  LEU A  60      92.986 185.792 282.322  1.00 83.28           C  
ANISOU  329  CA  LEU A  60     5914  12801  12927  -1073   -282    -54       C  
ATOM    330  C   LEU A  60      94.440 186.181 282.545  1.00 86.44           C  
ANISOU  330  C   LEU A  60     6444  13152  13248  -1052   -185    -53       C  
ATOM    331  O   LEU A  60      95.326 185.653 281.870  1.00 89.57           O  
ANISOU  331  O   LEU A  60     6857  13569  13605  -1099   -192    -77       O  
ATOM    332  CB  LEU A  60      92.150 187.038 282.034  1.00 57.64           C  
ANISOU  332  CB  LEU A  60     2595   9563   9742   -994   -319    -16       C  
ATOM    333  CG  LEU A  60      92.659 187.819 280.825  1.00 58.14           C  
ANISOU  333  CG  LEU A  60     2612   9661   9817   -971   -363    -21       C  
ATOM    334  CD1 LEU A  60      92.445 187.013 279.566  1.00 59.86           C  
ANISOU  334  CD1 LEU A  60     2716   9976  10053  -1049   -492    -95       C  
ATOM    335  CD2 LEU A  60      91.980 189.164 280.726  1.00 58.66           C  
ANISOU  335  CD2 LEU A  60     2637   9699   9953   -874   -380     92       C  
ATOM    336  N   ASN A  61      94.698 187.076 283.502  1.00 54.23           N  
ANISOU  336  N   ASN A  61     2439   9007   9160   -993    -93    -11       N  
ATOM    337  CA  ASN A  61      96.060 187.560 283.709  1.00 52.94           C  
ANISOU  337  CA  ASN A  61     2385   8806   8924   -979     -4    -13       C  
ATOM    338  C   ASN A  61      96.995 186.428 284.096  1.00 58.42           C  
ANISOU  338  C   ASN A  61     3126   9472   9598  -1027     22     -9       C  
ATOM    339  O   ASN A  61      98.138 186.373 283.629  1.00 57.73           O  
ANISOU  339  O   ASN A  61     3104   9400   9429  -1038     51    -37       O  
ATOM    340  CB  ASN A  61      96.080 188.646 284.775  1.00 52.23           C  
ANISOU  340  CB  ASN A  61     2355   8632   8858   -926     85     60       C  
ATOM    341  CG  ASN A  61      95.046 189.710 284.528  1.00 52.79           C  
ANISOU  341  CG  ASN A  61     2373   8708   8977   -870     65     99       C  
ATOM    342  OD1 ASN A  61      94.164 189.925 285.349  1.00 58.88           O  
ANISOU  342  OD1 ASN A  61     3128   9428   9817   -846     77    174       O  
ATOM    343  ND2 ASN A  61      95.138 190.378 283.388  1.00 53.99           N  
ANISOU  343  ND2 ASN A  61     2477   8904   9133   -847     33     85       N  
ATOM    344  N   LEU A  62      96.535 185.519 284.956  1.00 52.99           N  
ANISOU  344  N   LEU A  62     2421   8717   8997  -1045     14     39       N  
ATOM    345  CA  LEU A  62      97.363 184.376 285.319  1.00 68.61           C  
ANISOU  345  CA  LEU A  62     4429  10642  10997  -1078     35     54       C  
ATOM    346  C   LEU A  62      97.669 183.514 284.099  1.00 75.76           C  
ANISOU  346  C   LEU A  62     5284  11629  11872  -1143    -21      5       C  
ATOM    347  O   LEU A  62      98.819 183.111 283.891  1.00 79.08           O  
ANISOU  347  O   LEU A  62     5740  12044  12262  -1158     11      4       O  
ATOM    348  CB  LEU A  62      96.678 183.571 286.424  1.00 63.79           C  
ANISOU  348  CB  LEU A  62     3805   9924  10507  -1082     36    116       C  
ATOM    349  CG  LEU A  62      96.883 182.074 286.629  1.00 61.27           C  
ANISOU  349  CG  LEU A  62     3465   9532  10281  -1124     25    130       C  
ATOM    350  CD1 LEU A  62      98.341 181.726 286.908  1.00 59.63           C  
ANISOU  350  CD1 LEU A  62     3319   9280  10059  -1111     84    139       C  
ATOM    351  CD2 LEU A  62      95.988 181.623 287.775  1.00 54.60           C  
ANISOU  351  CD2 LEU A  62     2602   8592   9550  -1121     33    196       C  
ATOM    352  N   ALA A  63      96.667 183.248 283.260  1.00 78.08           N  
ANISOU  352  N   ALA A  63     5496  12000  12172  -1185   -107    -26       N  
ATOM    353  CA  ALA A  63      96.931 182.564 282.000  1.00 55.73           C  
ANISOU  353  CA  ALA A  63     2598   9214   9363  -1261   -173    -41       C  
ATOM    354  C   ALA A  63      97.444 183.501 280.914  1.00 55.81           C  
ANISOU  354  C   ALA A  63     2611   9291   9305  -1249   -189    -60       C  
ATOM    355  O   ALA A  63      97.804 183.025 279.835  1.00 56.86           O  
ANISOU  355  O   ALA A  63     2683   9454   9469  -1321   -244    -55       O  
ATOM    356  CB  ALA A  63      95.676 181.838 281.509  1.00 57.50           C  
ANISOU  356  CB  ALA A  63     2697   9476   9674  -1335   -274    -56       C  
ATOM    357  N   LEU A  64      97.479 184.810 281.163  1.00 54.90           N  
ANISOU  357  N   LEU A  64     2551   9180   9130  -1169   -143    -77       N  
ATOM    358  CA  LEU A  64      98.118 185.759 280.256  1.00 54.89           C  
ANISOU  358  CA  LEU A  64     2554   9217   9085  -1152   -133   -101       C  
ATOM    359  C   LEU A  64      99.607 185.875 280.537  1.00 53.62           C  
ANISOU  359  C   LEU A  64     2502   9022   8848  -1141    -36    -76       C  
ATOM    360  O   LEU A  64     100.416 185.896 279.604  1.00 64.80           O  
ANISOU  360  O   LEU A  64     3904  10478  10240  -1177    -39    -57       O  
ATOM    361  CB  LEU A  64      97.458 187.137 280.375  1.00 54.74           C  
ANISOU  361  CB  LEU A  64     2515   9175   9108  -1071   -122   -117       C  
ATOM    362  CG  LEU A  64      97.874 188.272 279.442  1.00 55.02           C  
ANISOU  362  CG  LEU A  64     2516   9211   9178  -1041   -115   -132       C  
ATOM    363  CD1 LEU A  64      97.647 187.877 278.000  1.00 56.81           C  
ANISOU  363  CD1 LEU A  64     2619   9507   9459  -1099   -232   -186       C  
ATOM    364  CD2 LEU A  64      97.113 189.547 279.767  1.00 55.00           C  
ANISOU  364  CD2 LEU A  64     2470   9173   9256   -961   -104    -58       C  
ATOM    365  N   ALA A  65      99.972 185.941 281.819  1.00 82.29           N  
ANISOU  365  N   ALA A  65     6234  12589  12444  -1099     44    -63       N  
ATOM    366  CA  ALA A  65     101.378 185.980 282.207  1.00 81.20           C  
ANISOU  366  CA  ALA A  65     6194  12427  12232  -1088    125    -44       C  
ATOM    367  C   ALA A  65     102.073 184.666 281.881  1.00 51.73           C  
ANISOU  367  C   ALA A  65     2422   8677   8556  -1138    107     -3       C  
ATOM    368  O   ALA A  65     103.197 184.657 281.359  1.00 51.65           O  
ANISOU  368  O   ALA A  65     2425   8666   8535  -1148    139     26       O  
ATOM    369  CB  ALA A  65     101.500 186.288 283.699  1.00 50.21           C  
ANISOU  369  CB  ALA A  65     2335   8430   8312  -1046    195    -35       C  
ATOM    370  N   ASP A  66     101.421 183.543 282.198  1.00 67.81           N  
ANISOU  370  N   ASP A  66     4395  10676  10692  -1170     64      1       N  
ATOM    371  CA  ASP A  66     101.996 182.235 281.907  1.00 53.20           C  
ANISOU  371  CA  ASP A  66     2478   8768   8969  -1221     59     11       C  
ATOM    372  C   ASP A  66     102.334 182.099 280.435  1.00 58.94           C  
ANISOU  372  C   ASP A  66     3126   9500   9770  -1282     17      1       C  
ATOM    373  O   ASP A  66     103.216 181.317 280.066  1.00 60.48           O  
ANISOU  373  O   ASP A  66     3313   9586  10079  -1298     50    -33       O  
ATOM    374  CB  ASP A  66     101.030 181.124 282.331  1.00 85.04           C  
ANISOU  374  CB  ASP A  66     6462  12724  13125  -1250     17      2       C  
ATOM    375  CG  ASP A  66     100.882 181.018 283.839  1.00 88.16           C  
ANISOU  375  CG  ASP A  66     6918  13056  13524  -1196     66     27       C  
ATOM    376  OD1 ASP A  66     101.541 181.796 284.560  1.00 92.01           O  
ANISOU  376  OD1 ASP A  66     7468  13537  13953  -1142    127     44       O  
ATOM    377  OD2 ASP A  66     100.107 180.154 284.304  1.00 87.94           O  
ANISOU  377  OD2 ASP A  66     6852  12941  13619  -1213     43     38       O  
ATOM    378  N   LEU A  67     101.654 182.860 279.580  1.00 54.95           N  
ANISOU  378  N   LEU A  67     2584   9075   9219  -1302    -50      4       N  
ATOM    379  CA  LEU A  67     101.934 182.801 278.152  1.00 89.16           C  
ANISOU  379  CA  LEU A  67     6826  13408  13644  -1373   -102    -10       C  
ATOM    380  C   LEU A  67     103.253 183.497 277.815  1.00 80.00           C  
ANISOU  380  C   LEU A  67     5716  12226  12455  -1340    -20     10       C  
ATOM    381  O   LEU A  67     104.006 183.026 276.953  1.00 72.29           O  
ANISOU  381  O   LEU A  67     4708  11160  11599  -1382      2    -89       O  
ATOM    382  CB  LEU A  67     100.759 183.410 277.386  1.00 57.30           C  
ANISOU  382  CB  LEU A  67     2726   9471   9576  -1400   -216      6       C  
ATOM    383  CG  LEU A  67     100.638 183.177 275.883  1.00 59.21           C  
ANISOU  383  CG  LEU A  67     2835   9704   9960  -1501   -324    -41       C  
ATOM    384  CD1 LEU A  67     101.208 184.371 275.127  1.00 71.50           C  
ANISOU  384  CD1 LEU A  67     4392  11265  11508  -1468   -311     -9       C  
ATOM    385  CD2 LEU A  67     101.324 181.877 275.473  1.00 68.83           C  
ANISOU  385  CD2 LEU A  67     4044  10784  11325  -1571   -285   -223       C  
ATOM    386  N   ALA A  68     103.565 184.601 278.502  1.00 73.06           N  
ANISOU  386  N   ALA A  68     4955  11392  11413  -1258     45     68       N  
ATOM    387  CA  ALA A  68     104.786 185.347 278.202  1.00 85.94           C  
ANISOU  387  CA  ALA A  68     6635  12996  13021  -1230    127    104       C  
ATOM    388  C   ALA A  68     106.031 184.533 278.524  1.00 53.09           C  
ANISOU  388  C   ALA A  68     2489   8759   8925  -1227    207     65       C  
ATOM    389  O   ALA A  68     107.015 184.571 277.776  1.00 53.46           O  
ANISOU  389  O   ALA A  68     2518   8749   9046  -1241    266      7       O  
ATOM    390  CB  ALA A  68     104.800 186.667 278.969  1.00 52.06           C  
ANISOU  390  CB  ALA A  68     2465   8779   8538  -1161    186    135       C  
ATOM    391  N   VAL A  69     106.011 183.791 279.636  1.00 52.56           N  
ANISOU  391  N   VAL A  69     2459   8677   8834  -1203    221     58       N  
ATOM    392  CA  VAL A  69     107.152 182.948 279.990  1.00 56.59           C  
ANISOU  392  CA  VAL A  69     2981   9104   9417  -1185    290     23       C  
ATOM    393  C   VAL A  69     107.451 181.956 278.877  1.00 59.05           C  
ANISOU  393  C   VAL A  69     3223   9286   9929  -1234    297   -112       C  
ATOM    394  O   VAL A  69     108.614 181.717 278.530  1.00 60.13           O  
ANISOU  394  O   VAL A  69     3367   9354  10124  -1223    380   -187       O  
ATOM    395  CB  VAL A  69     106.898 182.217 281.319  1.00 52.05           C  
ANISOU  395  CB  VAL A  69     2436   8513   8829  -1154    291     32       C  
ATOM    396  CG1 VAL A  69     107.702 180.916 281.366  1.00 52.87           C  
ANISOU  396  CG1 VAL A  69     2511   8475   9103  -1144    336    -23       C  
ATOM    397  CG2 VAL A  69     107.269 183.099 282.464  1.00 97.09           C  
ANISOU  397  CG2 VAL A  69     8253  14291  14344  -1100    332     71       C  
ATOM    398  N   LEU A  70     106.408 181.369 278.295  1.00 55.33           N  
ANISOU  398  N   LEU A  70     2680   8787   9557  -1298    219   -179       N  
ATOM    399  CA  LEU A  70     106.622 180.370 277.263  1.00 57.08           C  
ANISOU  399  CA  LEU A  70     2833   8896   9957  -1368    235   -374       C  
ATOM    400  C   LEU A  70     107.111 180.994 275.970  1.00 68.15           C  
ANISOU  400  C   LEU A  70     4216  10337  11340  -1419    262   -507       C  
ATOM    401  O   LEU A  70     107.759 180.309 275.172  1.00 67.91           O  
ANISOU  401  O   LEU A  70     4157  10239  11408  -1473    331   -719       O  
ATOM    402  CB  LEU A  70     105.334 179.582 277.038  1.00 58.38           C  
ANISOU  402  CB  LEU A  70     2925   9037  10218  -1441    138   -427       C  
ATOM    403  CG  LEU A  70     104.875 178.847 278.300  1.00 67.87           C  
ANISOU  403  CG  LEU A  70     4146  10185  11458  -1398    135   -335       C  
ATOM    404  CD1 LEU A  70     103.529 178.178 278.100  1.00 68.49           C  
ANISOU  404  CD1 LEU A  70     4153  10247  11623  -1474     42   -376       C  
ATOM    405  CD2 LEU A  70     105.922 177.828 278.734  1.00 69.02           C  
ANISOU  405  CD2 LEU A  70     4301  10176  11747  -1360    239   -393       C  
ATOM    406  N   LEU A  71     106.837 182.280 275.754  1.00 57.07           N  
ANISOU  406  N   LEU A  71     2827   9047   9810  -1406    227   -409       N  
ATOM    407  CA  LEU A  71     107.357 182.944 274.566  1.00 69.42           C  
ANISOU  407  CA  LEU A  71     4377  10668  11330  -1455    271   -554       C  
ATOM    408  C   LEU A  71     108.881 183.042 274.584  1.00 69.93           C  
ANISOU  408  C   LEU A  71     4506  10687  11376  -1420    422   -620       C  
ATOM    409  O   LEU A  71     109.495 183.166 273.518  1.00 69.82           O  
ANISOU  409  O   LEU A  71     4483  10718  11329  -1487    496   -822       O  
ATOM    410  CB  LEU A  71     106.721 184.330 274.416  1.00 57.25           C  
ANISOU  410  CB  LEU A  71     2828   9239   9686  -1435    212   -420       C  
ATOM    411  CG  LEU A  71     105.316 184.371 273.810  1.00 58.53           C  
ANISOU  411  CG  LEU A  71     2892   9486   9859  -1498     59   -431       C  
ATOM    412  CD1 LEU A  71     104.849 185.802 273.628  1.00 58.20           C  
ANISOU  412  CD1 LEU A  71     2830   9537   9747  -1459     25   -308       C  
ATOM    413  CD2 LEU A  71     105.305 183.647 272.485  1.00 60.64           C  
ANISOU  413  CD2 LEU A  71     3096   9823  10122  -1634     32   -720       C  
ATOM    414  N   THR A  72     109.504 182.974 275.765  1.00 69.13           N  
ANISOU  414  N   THR A  72     4469  10531  11267  -1328    468   -468       N  
ATOM    415  CA  THR A  72     110.959 182.962 275.870  1.00 55.53           C  
ANISOU  415  CA  THR A  72     2795   8766   9537  -1289    596   -516       C  
ATOM    416  C   THR A  72     111.551 181.567 275.714  1.00 85.59           C  
ANISOU  416  C   THR A  72     6563  12458  13501  -1305    658   -677       C  
ATOM    417  O   THR A  72     112.743 181.446 275.405  1.00 86.11           O  
ANISOU  417  O   THR A  72     6641  12488  13587  -1295    774   -785       O  
ATOM    418  CB  THR A  72     111.409 183.549 277.214  1.00 53.77           C  
ANISOU  418  CB  THR A  72     2647   8573   9211  -1195    607   -292       C  
ATOM    419  OG1 THR A  72     111.039 182.664 278.280  1.00 53.51           O  
ANISOU  419  OG1 THR A  72     2606   8517   9207  -1163    556   -211       O  
ATOM    420  CG2 THR A  72     110.776 184.904 277.444  1.00 52.75           C  
ANISOU  420  CG2 THR A  72     2553   8534   8957  -1179    564   -138       C  
ATOM    421  N   ALA A  73     110.743 180.525 275.902  1.00 57.48           N  
ANISOU  421  N   ALA A  73     2949   8828  10063  -1329    594   -703       N  
ATOM    422  CA  ALA A  73     111.227 179.151 275.784  1.00 58.83           C  
ANISOU  422  CA  ALA A  73     3070   8854  10427  -1342    666   -857       C  
ATOM    423  C   ALA A  73     111.989 178.846 274.497  1.00 73.06           C  
ANISOU  423  C   ALA A  73     4840  10626  12295  -1420    781  -1141       C  
ATOM    424  O   ALA A  73     112.996 178.122 274.577  1.00 71.80           O  
ANISOU  424  O   ALA A  73     4665  10355  12260  -1386    896  -1224       O  
ATOM    425  CB  ALA A  73     110.050 178.177 275.938  1.00 59.76           C  
ANISOU  425  CB  ALA A  73     3130   8901  10674  -1387    582   -876       C  
ATOM    426  N   PRO A  74     111.595 179.327 273.309  1.00 76.77           N  
ANISOU  426  N   PRO A  74     5292  11201  12676  -1529    766  -1308       N  
ATOM    427  CA  PRO A  74     112.388 178.999 272.111  1.00 81.58           C  
ANISOU  427  CA  PRO A  74     5879  11812  13307  -1625    901  -1612       C  
ATOM    428  C   PRO A  74     113.812 179.514 272.177  1.00 78.78           C  
ANISOU  428  C   PRO A  74     5579  11460  12894  -1560   1040  -1605       C  
ATOM    429  O   PRO A  74     114.660 179.055 271.401  1.00 78.39           O  
ANISOU  429  O   PRO A  74     5513  11376  12897  -1617   1183  -1842       O  
ATOM    430  CB  PRO A  74     111.608 179.667 270.967  1.00 86.19           C  
ANISOU  430  CB  PRO A  74     6443  12585  13720  -1762    831  -1746       C  
ATOM    431  CG  PRO A  74     110.245 179.884 271.502  1.00 63.17           C  
ANISOU  431  CG  PRO A  74     3507   9705  10789  -1741    650  -1552       C  
ATOM    432  CD  PRO A  74     110.425 180.154 272.960  1.00 61.09           C  
ANISOU  432  CD  PRO A  74     3297   9358  10555  -1583    633  -1247       C  
ATOM    433  N   PHE A  75     114.102 180.446 273.080  1.00 60.35           N  
ANISOU  433  N   PHE A  75     3311   9168  10451  -1453   1009  -1350       N  
ATOM    434  CA  PHE A  75     115.443 180.993 273.203  1.00 66.61           C  
ANISOU  434  CA  PHE A  75     4159   9972  11176  -1396   1127  -1330       C  
ATOM    435  C   PHE A  75     116.324 180.143 274.103  1.00 67.23           C  
ANISOU  435  C   PHE A  75     4222   9922  11399  -1296   1178  -1254       C  
ATOM    436  O   PHE A  75     117.492 179.899 273.779  1.00 68.51           O  
ANISOU  436  O   PHE A  75     4379  10042  11608  -1285   1310  -1373       O  
ATOM    437  CB  PHE A  75     115.378 182.422 273.737  1.00 57.94           C  
ANISOU  437  CB  PHE A  75     3138   8983   9895  -1344   1079  -1110       C  
ATOM    438  CG  PHE A  75     114.684 183.377 272.815  1.00 58.20           C  
ANISOU  438  CG  PHE A  75     3178   9151   9783  -1433   1052  -1177       C  
ATOM    439  CD1 PHE A  75     114.436 183.038 271.494  1.00 60.00           C  
ANISOU  439  CD1 PHE A  75     3357   9451   9991  -1567   1087  -1445       C  
ATOM    440  CD2 PHE A  75     114.286 184.620 273.268  1.00 83.84           C  
ANISOU  440  CD2 PHE A  75     6476  12473  12907  -1391    998   -980       C  
ATOM    441  CE1 PHE A  75     113.800 183.919 270.646  1.00 60.46           C  
ANISOU  441  CE1 PHE A  75     3409   9685   9878  -1661   1051  -1497       C  
ATOM    442  CE2 PHE A  75     113.651 185.509 272.425  1.00 84.04           C  
ANISOU  442  CE2 PHE A  75     6492  12634  12805  -1467    979  -1030       C  
ATOM    443  CZ  PHE A  75     113.409 185.157 271.111  1.00 85.80           C  
ANISOU  443  CZ  PHE A  75     6659  12962  12978  -1603    997  -1281       C  
ATOM    444  N   PHE A  76     115.780 179.682 275.226  1.00 58.94           N  
ANISOU  444  N   PHE A  76     3159   8825  10411  -1228   1079  -1060       N  
ATOM    445  CA  PHE A  76     116.571 178.849 276.120  1.00 59.08           C  
ANISOU  445  CA  PHE A  76     3147   8748  10551  -1139   1119   -980       C  
ATOM    446  C   PHE A  76     116.855 177.496 275.482  1.00 80.02           C  
ANISOU  446  C   PHE A  76     5715  11232  13456  -1171   1221  -1208       C  
ATOM    447  O   PHE A  76     117.939 176.933 275.666  1.00 80.88           O  
ANISOU  447  O   PHE A  76     5790  11257  13683  -1112   1322  -1238       O  
ATOM    448  CB  PHE A  76     115.854 178.678 277.460  1.00 61.92           C  
ANISOU  448  CB  PHE A  76     3515   9127  10886  -1080    998   -743       C  
ATOM    449  CG  PHE A  76     115.791 179.933 278.291  1.00 56.05           C  
ANISOU  449  CG  PHE A  76     2850   8544   9902  -1043    927   -526       C  
ATOM    450  CD1 PHE A  76     115.972 181.186 277.727  1.00 58.84           C  
ANISOU  450  CD1 PHE A  76     3262   8989  10106  -1070    947   -532       C  
ATOM    451  CD2 PHE A  76     115.557 179.851 279.648  1.00 55.10           C  
ANISOU  451  CD2 PHE A  76     2744   8482   9708   -990    856   -340       C  
ATOM    452  CE1 PHE A  76     115.909 182.327 278.499  1.00 53.76           C  
ANISOU  452  CE1 PHE A  76     2686   8464   9276  -1040    898   -342       C  
ATOM    453  CE2 PHE A  76     115.495 180.989 280.419  1.00 68.95           C  
ANISOU  453  CE2 PHE A  76     4568  10392  11238   -974    806   -180       C  
ATOM    454  CZ  PHE A  76     115.673 182.229 279.847  1.00 52.84           C  
ANISOU  454  CZ  PHE A  76     2582   8415   9080   -995    828   -170       C  
ATOM    455  N   LEU A  77     115.894 176.969 274.716  1.00 62.36           N  
ANISOU  455  N   LEU A  77     3438   8947  11310  -1269   1201  -1378       N  
ATOM    456  CA  LEU A  77     116.118 175.729 273.978  1.00 64.62           C  
ANISOU  456  CA  LEU A  77     3646   9069  11839  -1326   1320  -1641       C  
ATOM    457  C   LEU A  77     117.241 175.889 272.969  1.00 73.70           C  
ANISOU  457  C   LEU A  77     4798  10230  12974  -1370   1487  -1872       C  
ATOM    458  O   LEU A  77     118.088 175.001 272.813  1.00 67.16           O  
ANISOU  458  O   LEU A  77     3917   9253  12348  -1345   1628  -2003       O  
ATOM    459  CB  LEU A  77     114.838 175.311 273.268  1.00 65.75           C  
ANISOU  459  CB  LEU A  77     3750   9204  12027  -1456   1257  -1802       C  
ATOM    460  CG  LEU A  77     113.814 174.643 274.166  1.00 69.63           C  
ANISOU  460  CG  LEU A  77     4212   9609  12634  -1424   1142  -1645       C  
ATOM    461  CD1 LEU A  77     112.651 174.141 273.331  1.00 71.17           C  
ANISOU  461  CD1 LEU A  77     4361   9794  12888  -1571   1092  -1844       C  
ATOM    462  CD2 LEU A  77     114.486 173.511 274.923  1.00 70.51           C  
ANISOU  462  CD2 LEU A  77     4272   9518  13001  -1330   1232  -1599       C  
ATOM    463  N   HIS A  78     117.244 177.011 272.251  1.00 75.16           N  
ANISOU  463  N   HIS A  78     5043  10589  12927  -1438   1484  -1931       N  
ATOM    464  CA  HIS A  78     118.343 177.310 271.343  1.00 78.40           C  
ANISOU  464  CA  HIS A  78     5473  11038  13276  -1484   1650  -2135       C  
ATOM    465  C   HIS A  78     119.657 177.442 272.106  1.00 80.34           C  
ANISOU  465  C   HIS A  78     5738  11241  13548  -1348   1716  -1984       C  
ATOM    466  O   HIS A  78     120.673 176.846 271.727  1.00 82.72           O  
ANISOU  466  O   HIS A  78     6004  11446  13979  -1338   1873  -2141       O  
ATOM    467  CB  HIS A  78     118.023 178.586 270.562  1.00 79.09           C  
ANISOU  467  CB  HIS A  78     5627  11339  13086  -1580   1623  -2182       C  
ATOM    468  CG  HIS A  78     119.215 179.449 270.300  1.00 78.92           C  
ANISOU  468  CG  HIS A  78     5671  11397  12919  -1559   1742  -2195       C  
ATOM    469  ND1 HIS A  78     119.975 179.346 269.154  1.00 80.94           N  
ANISOU  469  ND1 HIS A  78     5932  11683  13140  -1660   1923  -2481       N  
ATOM    470  CD2 HIS A  78     119.780 180.430 271.041  1.00 78.64           C  
ANISOU  470  CD2 HIS A  78     5703  11418  12759  -1461   1713  -1964       C  
ATOM    471  CE1 HIS A  78     120.955 180.230 269.201  1.00 80.79           C  
ANISOU  471  CE1 HIS A  78     5983  11730  12984  -1616   1996  -2414       C  
ATOM    472  NE2 HIS A  78     120.861 180.899 270.336  1.00 79.34           N  
ANISOU  472  NE2 HIS A  78     5835  11560  12750  -1497   1868  -2106       N  
ATOM    473  N   PHE A  79     119.648 178.216 273.197  1.00 63.26           N  
ANISOU  473  N   PHE A  79     3624   9156  11256  -1251   1598  -1683       N  
ATOM    474  CA  PHE A  79     120.827 178.335 274.050  1.00 62.66           C  
ANISOU  474  CA  PHE A  79     3554   9074  11179  -1135   1630  -1521       C  
ATOM    475  C   PHE A  79     121.229 176.985 274.630  1.00 63.85           C  
ANISOU  475  C   PHE A  79     3612   9058  11591  -1058   1669  -1503       C  
ATOM    476  O   PHE A  79     122.416 176.742 274.874  1.00 64.43           O  
ANISOU  476  O   PHE A  79     3653   9098  11731   -987   1754  -1486       O  
ATOM    477  CB  PHE A  79     120.549 179.359 275.160  1.00 87.54           C  
ANISOU  477  CB  PHE A  79     6769  12357  14134  -1074   1490  -1220       C  
ATOM    478  CG  PHE A  79     121.655 179.494 276.193  1.00 85.30           C  
ANISOU  478  CG  PHE A  79     6481  12114  13816   -973   1493  -1036       C  
ATOM    479  CD1 PHE A  79     122.991 179.572 275.818  1.00 83.12           C  
ANISOU  479  CD1 PHE A  79     6194  11836  13553   -955   1619  -1127       C  
ATOM    480  CD2 PHE A  79     121.342 179.592 277.548  1.00 83.52           C  
ANISOU  480  CD2 PHE A  79     6259  11957  13519   -909   1368   -780       C  
ATOM    481  CE1 PHE A  79     123.992 179.708 276.777  1.00 80.26           C  
ANISOU  481  CE1 PHE A  79     5809  11538  13147   -871   1607   -955       C  
ATOM    482  CE2 PHE A  79     122.339 179.733 278.505  1.00 82.81           C  
ANISOU  482  CE2 PHE A  79     6149  11949  13365   -837   1363   -627       C  
ATOM    483  CZ  PHE A  79     123.662 179.791 278.118  1.00 59.07           C  
ANISOU  483  CZ  PHE A  79     3118   8941  10385   -816   1476   -707       C  
ATOM    484  N   LEU A  80     120.262 176.084 274.823  1.00 76.94           N  
ANISOU  484  N   LEU A  80     5220  10605  13410  -1072   1614  -1512       N  
ATOM    485  CA  LEU A  80     120.563 174.774 275.389  1.00 77.63           C  
ANISOU  485  CA  LEU A  80     5214  10508  13772   -998   1660  -1488       C  
ATOM    486  C   LEU A  80     121.325 173.889 274.409  1.00 77.14           C  
ANISOU  486  C   LEU A  80     5086  10280  13944  -1028   1857  -1773       C  
ATOM    487  O   LEU A  80     122.110 173.033 274.831  1.00 76.42           O  
ANISOU  487  O   LEU A  80     4919  10047  14069   -939   1939  -1741       O  
ATOM    488  CB  LEU A  80     119.268 174.083 275.820  1.00 79.46           C  
ANISOU  488  CB  LEU A  80     5417  10654  14119  -1017   1559  -1431       C  
ATOM    489  CG  LEU A  80     119.369 173.055 276.945  1.00 66.38           C  
ANISOU  489  CG  LEU A  80     3691   8861  12670   -916   1545  -1266       C  
ATOM    490  CD1 LEU A  80     119.879 173.737 278.181  1.00 64.69           C  
ANISOU  490  CD1 LEU A  80     3513   8811  12256   -820   1453   -984       C  
ATOM    491  CD2 LEU A  80     118.022 172.404 277.213  1.00 69.21           C  
ANISOU  491  CD2 LEU A  80     4028   9127  13142   -957   1462  -1244       C  
ATOM    492  N   THR A  81     121.112 174.072 273.110  1.00 69.05           N  
ANISOU  492  N   THR A  81     4083   9277  12877  -1158   1943  -2056       N  
ATOM    493  CA  THR A  81     121.702 173.204 272.098  1.00 77.73           C  
ANISOU  493  CA  THR A  81     5125  10224  14186  -1218   2151  -2374       C  
ATOM    494  C   THR A  81     122.825 173.861 271.314  1.00 79.61           C  
ANISOU  494  C   THR A  81     5407  10554  14288  -1246   2289  -2521       C  
ATOM    495  O   THR A  81     123.808 173.192 270.978  1.00 82.64           O  
ANISOU  495  O   THR A  81     5740  10805  14855  -1218   2464  -2666       O  
ATOM    496  CB  THR A  81     120.621 172.733 271.120  1.00 78.35           C  
ANISOU  496  CB  THR A  81     5184  10266  14319  -1383   2176  -2649       C  
ATOM    497  OG1 THR A  81     120.207 173.835 270.306  1.00 72.14           O  
ANISOU  497  OG1 THR A  81     4474   9706  13229  -1506   2131  -2745       O  
ATOM    498  CG2 THR A  81     119.418 172.196 271.882  1.00 72.46           C  
ANISOU  498  CG2 THR A  81     4405   9447  13681  -1367   2024  -2495       C  
ATOM    499  N   TRP A  82     122.696 175.155 271.007  1.00 70.42           N  
ANISOU  499  N   TRP A  82     4336   9606  12815  -1300   2226  -2485       N  
ATOM    500  CA  TRP A  82     123.750 175.863 270.285  1.00 87.11           C  
ANISOU  500  CA  TRP A  82     6504  11815  14778  -1333   2359  -2611       C  
ATOM    501  C   TRP A  82     125.071 175.811 271.044  1.00 89.22           C  
ANISOU  501  C   TRP A  82     6747  12037  15117  -1188   2399  -2447       C  
ATOM    502  O   TRP A  82     126.128 175.564 270.451  1.00 92.47           O  
ANISOU  502  O   TRP A  82     7142  12394  15598  -1193   2573  -2617       O  
ATOM    503  CB  TRP A  82     123.322 177.313 270.027  1.00 83.49           C  
ANISOU  503  CB  TRP A  82     6149  11585  13988  -1399   2268  -2542       C  
ATOM    504  CG  TRP A  82     122.916 177.585 268.600  1.00 83.62           C  
ANISOU  504  CG  TRP A  82     6200  11710  13860  -1585   2363  -2847       C  
ATOM    505  CD1 TRP A  82     123.396 178.570 267.782  1.00 83.21           C  
ANISOU  505  CD1 TRP A  82     6231  11820  13564  -1669   2455  -2954       C  
ATOM    506  CD2 TRP A  82     121.966 176.847 267.820  1.00 85.82           C  
ANISOU  506  CD2 TRP A  82     6431  11967  14211  -1727   2382  -3089       C  
ATOM    507  NE1 TRP A  82     122.798 178.494 266.547  1.00 85.35           N  
ANISOU  507  NE1 TRP A  82     6508  12194  13728  -1858   2528  -3239       N  
ATOM    508  CE2 TRP A  82     121.918 177.444 266.544  1.00 88.07           C  
ANISOU  508  CE2 TRP A  82     6768  12434  14261  -1903   2478  -3334       C  
ATOM    509  CE3 TRP A  82     121.151 175.740 268.078  1.00 72.64           C  
ANISOU  509  CE3 TRP A  82     4678  10149  12771  -1736   2327  -3125       C  
ATOM    510  CZ2 TRP A  82     121.086 176.972 265.530  1.00 93.76           C  
ANISOU  510  CZ2 TRP A  82     7455  13221  14949  -2100   2508  -3615       C  
ATOM    511  CZ3 TRP A  82     120.327 175.273 267.072  1.00 98.09           C  
ANISOU  511  CZ3 TRP A  82     7872  13410  15988  -1924   2360  -3411       C  
ATOM    512  CH2 TRP A  82     120.300 175.889 265.813  1.00 97.51           C  
ANISOU  512  CH2 TRP A  82     7846  13545  15657  -2111   2442  -3655       C  
ATOM    513  N   GLY A  83     125.028 176.016 272.359  1.00 68.98           N  
ANISOU  513  N   GLY A  83     4173   9508  12528  -1069   2243  -2122       N  
ATOM    514  CA  GLY A  83     126.204 176.008 273.195  1.00 68.88           C  
ANISOU  514  CA  GLY A  83     4121   9503  12547   -944   2251  -1940       C  
ATOM    515  C   GLY A  83     126.570 177.361 273.759  1.00 66.86           C  
ANISOU  515  C   GLY A  83     3943   9453  12007   -919   2154  -1733       C  
ATOM    516  O   GLY A  83     127.283 177.420 274.767  1.00 66.41           O  
ANISOU  516  O   GLY A  83     3845   9450  11936   -820   2101  -1520       O  
ATOM    517  N   THR A  84     126.106 178.448 273.147  1.00 65.80           N  
ANISOU  517  N   THR A  84     3913   9441  11648  -1013   2137  -1793       N  
ATOM    518  CA  THR A  84     126.402 179.782 273.647  1.00 64.01           C  
ANISOU  518  CA  THR A  84     3766   9381  11174   -998   2064  -1608       C  
ATOM    519  C   THR A  84     125.182 180.679 273.491  1.00 74.06           C  
ANISOU  519  C   THR A  84     5126  10744  12268  -1069   1962  -1565       C  
ATOM    520  O   THR A  84     124.301 180.416 272.669  1.00 75.80           O  
ANISOU  520  O   THR A  84     5350  10936  12514  -1156   1977  -1735       O  
ATOM    521  CB  THR A  84     127.601 180.396 272.922  1.00 64.71           C  
ANISOU  521  CB  THR A  84     3895   9520  11170  -1030   2209  -1742       C  
ATOM    522  OG1 THR A  84     127.951 181.633 273.554  1.00 90.67           O  
ANISOU  522  OG1 THR A  84     7251  12946  14252  -1009   2140  -1548       O  
ATOM    523  CG2 THR A  84     127.266 180.648 271.465  1.00 65.62           C  
ANISOU  523  CG2 THR A  84     4076   9645  11211  -1166   2330  -2030       C  
ATOM    524  N   TRP A  85     125.131 181.735 274.304  1.00 71.28           N  
ANISOU  524  N   TRP A  85     4835  10507  11742  -1036   1861  -1338       N  
ATOM    525  CA  TRP A  85     124.075 182.731 274.176  1.00 59.41           C  
ANISOU  525  CA  TRP A  85     3414   9084  10075  -1093   1780  -1282       C  
ATOM    526  C   TRP A  85     124.235 183.480 272.861  1.00 95.05           C  
ANISOU  526  C   TRP A  85     7998  13656  14461  -1199   1903  -1497       C  
ATOM    527  O   TRP A  85     125.343 183.641 272.351  1.00 96.49           O  
ANISOU  527  O   TRP A  85     8198  13846  14616  -1216   2035  -1616       O  
ATOM    528  CB  TRP A  85     124.103 183.706 275.359  1.00 77.41           C  
ANISOU  528  CB  TRP A  85     5743  11454  12215  -1035   1675  -1008       C  
ATOM    529  CG  TRP A  85     122.862 184.564 275.458  1.00 76.48           C  
ANISOU  529  CG  TRP A  85     5690  11387  11983  -1069   1579   -912       C  
ATOM    530  CD1 TRP A  85     122.776 185.918 275.272  1.00 76.22           C  
ANISOU  530  CD1 TRP A  85     5748  11424  11789  -1104   1597   -877       C  
ATOM    531  CD2 TRP A  85     121.530 184.116 275.751  1.00 55.90           C  
ANISOU  531  CD2 TRP A  85     3055   8756   9428  -1071   1461   -844       C  
ATOM    532  NE1 TRP A  85     121.476 186.335 275.438  1.00 54.58           N  
ANISOU  532  NE1 TRP A  85     3027   8703   9008  -1119   1498   -784       N  
ATOM    533  CE2 TRP A  85     120.695 185.247 275.730  1.00 54.82           C  
ANISOU  533  CE2 TRP A  85     2986   8683   9160  -1101   1407   -761       C  
ATOM    534  CE3 TRP A  85     120.965 182.866 276.025  1.00 56.49           C  
ANISOU  534  CE3 TRP A  85     3052   8754   9658  -1050   1402   -848       C  
ATOM    535  CZ2 TRP A  85     119.334 185.165 275.975  1.00 54.31           C  
ANISOU  535  CZ2 TRP A  85     2907   8619   9109  -1109   1290   -677       C  
ATOM    536  CZ3 TRP A  85     119.618 182.789 276.265  1.00 55.94           C  
ANISOU  536  CZ3 TRP A  85     2979   8686   9590  -1067   1286   -772       C  
ATOM    537  CH2 TRP A  85     118.816 183.927 276.239  1.00 54.85           C  
ANISOU  537  CH2 TRP A  85     2903   8625   9314  -1095   1227   -684       C  
ATOM    538  N   SER A  86     123.115 183.934 272.296  1.00 59.78           N  
ANISOU  538  N   SER A  86     3566   9245   9904  -1278   1860  -1545       N  
ATOM    539  CA  SER A  86     123.155 184.504 270.955  1.00 60.76           C  
ANISOU  539  CA  SER A  86     3742   9457   9888  -1402   1981  -1766       C  
ATOM    540  C   SER A  86     122.382 185.806 270.807  1.00 59.74           C  
ANISOU  540  C   SER A  86     3687   9449   9564  -1449   1930  -1672       C  
ATOM    541  O   SER A  86     122.226 186.288 269.682  1.00 61.92           O  
ANISOU  541  O   SER A  86     4000   9833   9694  -1566   2018  -1836       O  
ATOM    542  CB  SER A  86     122.633 183.490 269.942  1.00 91.56           C  
ANISOU  542  CB  SER A  86     7579  13334  13877  -1501   2033  -2025       C  
ATOM    543  OG  SER A  86     123.148 182.206 270.223  1.00 92.83           O  
ANISOU  543  OG  SER A  86     7659  13346  14267  -1443   2071  -2087       O  
ATOM    544  N   PHE A  87     121.928 186.409 271.899  1.00 72.95           N  
ANISOU  544  N   PHE A  87     5382  11117  11218  -1369   1804  -1416       N  
ATOM    545  CA  PHE A  87     121.000 187.527 271.804  1.00 72.68           C  
ANISOU  545  CA  PHE A  87     5397  11172  11047  -1404   1752  -1322       C  
ATOM    546  C   PHE A  87     121.520 188.806 272.448  1.00 56.02           C  
ANISOU  546  C   PHE A  87     3377   9080   8828  -1358   1775  -1156       C  
ATOM    547  O   PHE A  87     120.775 189.793 272.529  1.00 66.78           O  
ANISOU  547  O   PHE A  87     4779  10492  10101  -1370   1740  -1052       O  
ATOM    548  CB  PHE A  87     119.656 187.124 272.413  1.00 72.81           C  
ANISOU  548  CB  PHE A  87     5354  11159  11150  -1370   1583  -1188       C  
ATOM    549  CG  PHE A  87     119.159 185.796 271.922  1.00 57.81           C  
ANISOU  549  CG  PHE A  87     3364   9219   9384  -1413   1552  -1345       C  
ATOM    550  CD1 PHE A  87     118.433 185.704 270.752  1.00 59.13           C  
ANISOU  550  CD1 PHE A  87     3495   9481   9489  -1538   1562  -1534       C  
ATOM    551  CD2 PHE A  87     119.431 184.640 272.628  1.00 70.02           C  
ANISOU  551  CD2 PHE A  87     4856  10644  11106  -1341   1518  -1309       C  
ATOM    552  CE1 PHE A  87     117.983 184.488 270.301  1.00 60.45           C  
ANISOU  552  CE1 PHE A  87     3580   9607   9783  -1595   1538  -1700       C  
ATOM    553  CE2 PHE A  87     118.981 183.422 272.179  1.00 71.30           C  
ANISOU  553  CE2 PHE A  87     4937  10742  11412  -1385   1508  -1466       C  
ATOM    554  CZ  PHE A  87     118.256 183.345 271.014  1.00 60.48           C  
ANISOU  554  CZ  PHE A  87     3538   9450   9993  -1515   1519  -1671       C  
ATOM    555  N   GLY A  88     122.768 188.827 272.892  1.00 55.90           N  
ANISOU  555  N   GLY A  88     3386   9027   8825  -1310   1836  -1135       N  
ATOM    556  CA  GLY A  88     123.348 190.036 273.429  1.00 70.79           C  
ANISOU  556  CA  GLY A  88     5356  10932  10609  -1286   1869  -1014       C  
ATOM    557  C   GLY A  88     122.841 190.343 274.823  1.00 70.84           C  
ANISOU  557  C   GLY A  88     5360  10906  10650  -1204   1738   -767       C  
ATOM    558  O   GLY A  88     121.976 189.663 275.377  1.00 53.01           O  
ANISOU  558  O   GLY A  88     3041   8618   8481  -1164   1617   -673       O  
ATOM    559  N   LEU A  89     123.407 191.413 275.396  1.00 72.56           N  
ANISOU  559  N   LEU A  89     5649  11133  10789  -1188   1772   -671       N  
ATOM    560  CA  LEU A  89     123.102 191.778 276.777  1.00 74.14           C  
ANISOU  560  CA  LEU A  89     5853  11309  11009  -1122   1671   -455       C  
ATOM    561  C   LEU A  89     121.602 191.915 276.983  1.00 76.82           C  
ANISOU  561  C   LEU A  89     6181  11637  11369  -1114   1577   -357       C  
ATOM    562  O   LEU A  89     121.054 191.426 277.975  1.00 77.93           O  
ANISOU  562  O   LEU A  89     6277  11755  11576  -1060   1460   -207       O  
ATOM    563  CB  LEU A  89     123.809 193.083 277.153  1.00 51.11           C  
ANISOU  563  CB  LEU A  89     3022   8401   7995  -1133   1745   -413       C  
ATOM    564  CG  LEU A  89     123.919 193.343 278.662  1.00 67.94           C  
ANISOU  564  CG  LEU A  89     5148  10514  10153  -1075   1664   -224       C  
ATOM    565  CD1 LEU A  89     125.168 192.672 279.207  1.00 67.81           C  
ANISOU  565  CD1 LEU A  89     5070  10515  10178  -1044   1660   -207       C  
ATOM    566  CD2 LEU A  89     123.897 194.831 279.015  1.00 67.96           C  
ANISOU  566  CD2 LEU A  89     5245  10508  10070  -1098   1721   -180       C  
ATOM    567  N   ALA A  90     120.921 192.565 276.035  1.00 51.21           N  
ANISOU  567  N   ALA A  90     2969   8424   8063  -1172   1629   -434       N  
ATOM    568  CA  ALA A  90     119.475 192.715 276.125  1.00 50.81           C  
ANISOU  568  CA  ALA A  90     2890   8374   8043  -1167   1542   -347       C  
ATOM    569  C   ALA A  90     118.794 191.360 276.224  1.00 73.11           C  
ANISOU  569  C   ALA A  90     5619  11179  10979  -1147   1422   -345       C  
ATOM    570  O   ALA A  90     117.876 191.172 277.029  1.00 74.43           O  
ANISOU  570  O   ALA A  90     5756  11321  11203  -1104   1308   -197       O  
ATOM    571  CB  ALA A  90     118.952 193.490 274.917  1.00 51.66           C  
ANISOU  571  CB  ALA A  90     3018   8552   8057  -1244   1625   -444       C  
ATOM    572  N   GLY A  91     119.248 190.395 275.422  1.00 70.86           N  
ANISOU  572  N   GLY A  91     5291  10904  10728  -1184   1456   -517       N  
ATOM    573  CA  GLY A  91     118.603 189.090 275.407  1.00 68.15           C  
ANISOU  573  CA  GLY A  91     4861  10533  10501  -1178   1360   -546       C  
ATOM    574  C   GLY A  91     118.575 188.428 276.769  1.00 65.75           C  
ANISOU  574  C   GLY A  91     4528  10184  10271  -1097   1257   -364       C  
ATOM    575  O   GLY A  91     117.515 188.039 277.266  1.00 51.22           O  
ANISOU  575  O   GLY A  91     2651   8336   8474  -1079   1144   -260       O  
ATOM    576  N   CYS A  92     119.739 188.305 277.401  1.00 51.41           N  
ANISOU  576  N   CYS A  92     2723   8363   8449  -1055   1294   -319       N  
ATOM    577  CA  CYS A  92     119.803 187.654 278.699  1.00 50.84           C  
ANISOU  577  CA  CYS A  92     2611   8298   8407   -993   1203   -147       C  
ATOM    578  C   CYS A  92     119.434 188.573 279.847  1.00100.78           C  
ANISOU  578  C   CYS A  92     8983  14657  14653   -963   1144     63       C  
ATOM    579  O   CYS A  92     119.057 188.082 280.917  1.00106.11           O  
ANISOU  579  O   CYS A  92     9642  15369  15306   -931   1047    201       O  
ATOM    580  CB  CYS A  92     121.192 187.076 278.945  1.00 51.44           C  
ANISOU  580  CB  CYS A  92     2650   8382   8511   -963   1258   -175       C  
ATOM    581  SG  CYS A  92     121.062 185.402 279.576  1.00158.61           S  
ANISOU  581  SG  CYS A  92    16117  21956  22191   -923   1182   -141       S  
ATOM    582  N   ARG A  93     119.545 189.887 279.656  1.00 91.41           N  
ANISOU  582  N   ARG A  93     7872  13456  13405   -979   1211     63       N  
ATOM    583  CA  ARG A  93     118.999 190.819 280.636  1.00 81.79           C  
ANISOU  583  CA  ARG A  93     6710  12227  12141   -954   1169    225       C  
ATOM    584  C   ARG A  93     117.474 190.773 280.638  1.00 83.16           C  
ANISOU  584  C   ARG A  93     6890  12386  12320   -953   1078    272       C  
ATOM    585  O   ARG A  93     116.852 190.923 281.698  1.00 83.76           O  
ANISOU  585  O   ARG A  93     7023  12450  12353   -921    998    385       O  
ATOM    586  CB  ARG A  93     119.514 192.232 280.348  1.00 74.35           C  
ANISOU  586  CB  ARG A  93     5841  11267  11142   -978   1287    182       C  
ATOM    587  CG  ARG A  93     119.805 193.096 281.561  1.00 71.45           C  
ANISOU  587  CG  ARG A  93     5522  10879  10745   -966   1301    261       C  
ATOM    588  CD  ARG A  93     120.697 194.287 281.201  1.00 74.07           C  
ANISOU  588  CD  ARG A  93     5924  11214  11004  -1001   1433    184       C  
ATOM    589  NE  ARG A  93     120.593 195.370 282.179  1.00 78.61           N  
ANISOU  589  NE  ARG A  93     6542  11776  11551  -1016   1468    220       N  
ATOM    590  CZ  ARG A  93     119.948 196.515 281.965  1.00 82.69           C  
ANISOU  590  CZ  ARG A  93     7124  12273  12022  -1028   1520    243       C  
ATOM    591  NH1 ARG A  93     119.355 196.737 280.797  1.00 86.77           N  
ANISOU  591  NH1 ARG A  93     7660  12788  12519  -1030   1544    234       N  
ATOM    592  NH2 ARG A  93     119.903 197.443 282.917  1.00 81.06           N  
ANISOU  592  NH2 ARG A  93     6952  12058  11790  -1048   1558    260       N  
ATOM    593  N   LEU A  94     116.865 190.519 279.475  1.00 48.50           N  
ANISOU  593  N   LEU A  94     2432   8013   7984   -998   1091    164       N  
ATOM    594  CA  LEU A  94     115.414 190.519 279.298  1.00 48.50           C  
ANISOU  594  CA  LEU A  94     2406   8014   8008  -1007   1009    200       C  
ATOM    595  C   LEU A  94     114.770 189.181 279.646  1.00 78.25           C  
ANISOU  595  C   LEU A  94     6125  11803  11805  -1001    891    215       C  
ATOM    596  O   LEU A  94     113.806 189.148 280.413  1.00 81.16           O  
ANISOU  596  O   LEU A  94     6539  12190  12110   -979    795    308       O  
ATOM    597  CB  LEU A  94     115.054 190.895 277.859  1.00 49.47           C  
ANISOU  597  CB  LEU A  94     2501   8148   8147  -1066   1067     46       C  
ATOM    598  CG  LEU A  94     113.663 191.447 277.557  1.00 49.62           C  
ANISOU  598  CG  LEU A  94     2481   8182   8191  -1078   1015     96       C  
ATOM    599  CD1 LEU A  94     113.698 192.191 276.244  1.00 54.32           C  
ANISOU  599  CD1 LEU A  94     3075   8836   8729  -1143   1110    -51       C  
ATOM    600  CD2 LEU A  94     112.606 190.357 277.499  1.00 50.05           C  
ANISOU  600  CD2 LEU A  94     2449   8249   8318  -1089    880    104       C  
ATOM    601  N   CYS A  95     115.256 188.081 279.063  1.00 74.31           N  
ANISOU  601  N   CYS A  95     5553  11301  11381  -1026    909     89       N  
ATOM    602  CA  CYS A  95     114.585 186.794 279.238  1.00 71.66           C  
ANISOU  602  CA  CYS A  95     5153  10970  11104  -1034    821     69       C  
ATOM    603  C   CYS A  95     114.410 186.452 280.707  1.00 49.22           C  
ANISOU  603  C   CYS A  95     2359   8186   8158   -993    747    194       C  
ATOM    604  O   CYS A  95     113.380 185.901 281.109  1.00 49.22           O  
ANISOU  604  O   CYS A  95     2349   8211   8140  -1002    667    197       O  
ATOM    605  CB  CYS A  95     115.366 185.689 278.533  1.00 72.21           C  
ANISOU  605  CB  CYS A  95     5177  10976  11284  -1050    879   -111       C  
ATOM    606  SG  CYS A  95     115.151 185.693 276.749  1.00 52.71           S  
ANISOU  606  SG  CYS A  95     2674   8473   8879  -1134    939   -363       S  
ATOM    607  N   HIS A  96     115.406 186.776 281.526  1.00 48.65           N  
ANISOU  607  N   HIS A  96     2353   8136   7995   -955    777    257       N  
ATOM    608  CA  HIS A  96     115.263 186.530 282.951  1.00 67.16           C  
ANISOU  608  CA  HIS A  96     4720  10550  10246   -943    732    283       C  
ATOM    609  C   HIS A  96     114.319 187.532 283.603  1.00 66.77           C  
ANISOU  609  C   HIS A  96     4748  10536  10085   -951    698    325       C  
ATOM    610  O   HIS A  96     113.631 187.192 284.572  1.00 67.06           O  
ANISOU  610  O   HIS A  96     4780  10629  10069   -968    662    254       O  
ATOM    611  CB  HIS A  96     116.636 186.547 283.613  1.00 67.17           C  
ANISOU  611  CB  HIS A  96     4708  10574  10238   -922    785    298       C  
ATOM    612  CG  HIS A  96     117.497 185.390 283.219  1.00 49.59           C  
ANISOU  612  CG  HIS A  96     2385   8341   8116   -911    819    234       C  
ATOM    613  ND1 HIS A  96     118.824 185.528 282.878  1.00 75.53           N  
ANISOU  613  ND1 HIS A  96     5645  11615  11437   -894    897    229       N  
ATOM    614  CD2 HIS A  96     117.215 184.072 283.104  1.00 71.92           C  
ANISOU  614  CD2 HIS A  96     5125  11157  11046   -912    799    168       C  
ATOM    615  CE1 HIS A  96     119.326 184.344 282.579  1.00 75.97           C  
ANISOU  615  CE1 HIS A  96     5600  11670  11595   -882    921    161       C  
ATOM    616  NE2 HIS A  96     118.369 183.442 282.707  1.00 74.29           N  
ANISOU  616  NE2 HIS A  96     5345  11444  11436   -892    865    130       N  
ATOM    617  N   TYR A  97     114.254 188.760 283.087  1.00 47.26           N  
ANISOU  617  N   TYR A  97     2338   8010   7610   -941    731    402       N  
ATOM    618  CA  TYR A  97     113.312 189.722 283.646  1.00 46.77           C  
ANISOU  618  CA  TYR A  97     2334   7985   7451   -947    709    436       C  
ATOM    619  C   TYR A  97     111.876 189.315 283.335  1.00 46.84           C  
ANISOU  619  C   TYR A  97     2323   8056   7418   -975    638    355       C  
ATOM    620  O   TYR A  97     111.007 189.354 284.213  1.00 85.56           O  
ANISOU  620  O   TYR A  97     7236  13020  12253  -1000    622    228       O  
ATOM    621  CB  TYR A  97     113.612 191.127 283.122  1.00 46.41           C  
ANISOU  621  CB  TYR A  97     2342   7820   7472   -919    787    526       C  
ATOM    622  CG  TYR A  97     112.748 192.192 283.756  1.00 46.04           C  
ANISOU  622  CG  TYR A  97     2347   7808   7340   -921    783    572       C  
ATOM    623  CD1 TYR A  97     112.561 192.227 285.132  1.00 45.99           C  
ANISOU  623  CD1 TYR A  97     2357   7918   7200   -952    764    526       C  
ATOM    624  CD2 TYR A  97     112.121 193.159 282.982  1.00 45.89           C  
ANISOU  624  CD2 TYR A  97     2353   7742   7343   -907    809    615       C  
ATOM    625  CE1 TYR A  97     111.773 193.190 285.720  1.00 45.79           C  
ANISOU  625  CE1 TYR A  97     2373   7978   7046   -988    781    453       C  
ATOM    626  CE2 TYR A  97     111.331 194.131 283.562  1.00 45.72           C  
ANISOU  626  CE2 TYR A  97     2368   7828   7174   -929    812    605       C  
ATOM    627  CZ  TYR A  97     111.160 194.141 284.933  1.00 78.25           C  
ANISOU  627  CZ  TYR A  97     6507  12083  11143   -983    806    471       C  
ATOM    628  OH  TYR A  97     110.372 195.101 285.527  1.00 78.00           O  
ANISOU  628  OH  TYR A  97     6511  12126  10999  -1045    863    246       O  
ATOM    629  N   ILE A  98     111.616 188.908 282.088  1.00 59.67           N  
ANISOU  629  N   ILE A  98     3899   9627   9144   -976    615    374       N  
ATOM    630  CA  ILE A  98     110.296 188.397 281.717  1.00 60.60           C  
ANISOU  630  CA  ILE A  98     3954   9778   9293  -1007    547    304       C  
ATOM    631  C   ILE A  98     109.956 187.163 282.546  1.00 61.55           C  
ANISOU  631  C   ILE A  98     4055   9924   9409  -1016    505    213       C  
ATOM    632  O   ILE A  98     108.834 187.021 283.054  1.00 47.92           O  
ANISOU  632  O   ILE A  98     2312   8208   7687  -1026    470    135       O  
ATOM    633  CB  ILE A  98     110.245 188.102 280.201  1.00 61.02           C  
ANISOU  633  CB  ILE A  98     3887   9746   9553  -1034    551    287       C  
ATOM    634  CG1 ILE A  98     109.699 189.300 279.414  1.00 60.96           C  
ANISOU  634  CG1 ILE A  98     3864   9715   9584  -1035    567    328       C  
ATOM    635  CG2 ILE A  98     109.376 186.887 279.914  1.00 62.90           C  
ANISOU  635  CG2 ILE A  98     4028   9992   9878  -1074    472    214       C  
ATOM    636  CD1 ILE A  98     110.121 190.665 279.925  1.00 48.35           C  
ANISOU  636  CD1 ILE A  98     2367   8099   7906   -994    642    414       C  
ATOM    637  N   CYS A  99     110.922 186.257 282.706  1.00 62.34           N  
ANISOU  637  N   CYS A  99     4112   9986   9588  -1008    531    206       N  
ATOM    638  CA  CYS A  99     110.713 185.096 283.560  1.00 61.54           C  
ANISOU  638  CA  CYS A  99     3947   9861   9575  -1010    516    139       C  
ATOM    639  C   CYS A  99     110.535 185.513 285.012  1.00 58.88           C  
ANISOU  639  C   CYS A  99     3643   9534   9193  -1001    536     95       C  
ATOM    640  O   CYS A  99     109.701 184.957 285.734  1.00 54.99           O  
ANISOU  640  O   CYS A  99     3110   9000   8784  -1002    511     65       O  
ATOM    641  CB  CYS A  99     111.893 184.139 283.428  1.00 49.25           C  
ANISOU  641  CB  CYS A  99     2327   8271   8115   -998    555    135       C  
ATOM    642  SG  CYS A  99     111.974 183.262 281.845  1.00 58.63           S  
ANISOU  642  SG  CYS A  99     3393   9384   9501  -1033    562     96       S  
ATOM    643  N   GLY A 100     111.305 186.497 285.462  1.00 62.31           N  
ANISOU  643  N   GLY A 100     4145  10011   9520   -996    585    103       N  
ATOM    644  CA  GLY A 100     111.216 186.886 286.854  1.00 65.84           C  
ANISOU  644  CA  GLY A 100     4615  10450   9950  -1002    615     40       C  
ATOM    645  C   GLY A 100     109.943 187.637 287.191  1.00 69.62           C  
ANISOU  645  C   GLY A 100     5126  10898  10430  -1011    610     -2       C  
ATOM    646  O   GLY A 100     109.518 187.663 288.353  1.00 74.24           O  
ANISOU  646  O   GLY A 100     5701  11434  11074  -1013    624    -27       O  
ATOM    647  N   VAL A 101     109.281 188.207 286.188  1.00 67.03           N  
ANISOU  647  N   VAL A 101     4819  10590  10060  -1013    589      8       N  
ATOM    648  CA  VAL A 101     108.094 188.977 286.501  1.00 63.10           C  
ANISOU  648  CA  VAL A 101     4335  10054   9588  -1014    594    -34       C  
ATOM    649  C   VAL A 101     106.865 188.072 286.535  1.00 47.42           C  
ANISOU  649  C   VAL A 101     2273   8024   7721  -1007    526    -19       C  
ATOM    650  O   VAL A 101     105.959 188.287 287.344  1.00 86.73           O  
ANISOU  650  O   VAL A 101     7234  12956  12764  -1002    527    -14       O  
ATOM    651  CB  VAL A 101     107.956 190.129 285.505  1.00 60.95           C  
ANISOU  651  CB  VAL A 101     4109   9822   9227  -1017    615    -46       C  
ATOM    652  CG1 VAL A 101     106.564 190.132 284.875  1.00 46.92           C  
ANISOU  652  CG1 VAL A 101     2285   8024   7519  -1007    563    -69       C  
ATOM    653  CG2 VAL A 101     108.267 191.431 286.206  1.00 46.24           C  
ANISOU  653  CG2 VAL A 101     2313   7944   7313  -1029    699    -78       C  
ATOM    654  N   SER A 102     106.854 186.994 285.727  1.00 47.90           N  
ANISOU  654  N   SER A 102     2280   8101   7818  -1012    470      5       N  
ATOM    655  CA  SER A 102     105.725 186.066 285.729  1.00 48.52           C  
ANISOU  655  CA  SER A 102     2281   8145   8009  -1019    406     17       C  
ATOM    656  C   SER A 102     105.691 185.276 287.027  1.00100.47           C  
ANISOU  656  C   SER A 102     8818  14663  14693  -1015    416     45       C  
ATOM    657  O   SER A 102     104.612 185.081 287.596  1.00101.24           O  
ANISOU  657  O   SER A 102     8874  14725  14868  -1017    391     65       O  
ATOM    658  CB  SER A 102     105.757 185.172 284.519  1.00 49.10           C  
ANISOU  658  CB  SER A 102     2305   8246   8103  -1043    352     31       C  
ATOM    659  OG  SER A 102     105.458 185.894 283.337  1.00 50.15           O  
ANISOU  659  OG  SER A 102     2461   8447   8145  -1055    326     25       O  
ATOM    660  N   MET A 103     106.856 184.853 287.541  1.00 48.81           N  
ANISOU  660  N   MET A 103     2276   8116   8155  -1008    454     55       N  
ATOM    661  CA  MET A 103     106.867 184.185 288.839  1.00 49.18           C  
ANISOU  661  CA  MET A 103     2287   8103   8296  -1000    464     95       C  
ATOM    662  C   MET A 103     106.216 185.061 289.894  1.00 48.87           C  
ANISOU  662  C   MET A 103     2281   8049   8240  -1002    489    105       C  
ATOM    663  O   MET A 103     105.395 184.599 290.697  1.00 49.28           O  
ANISOU  663  O   MET A 103     2317   8033   8376   -996    468    163       O  
ATOM    664  CB  MET A 103     108.281 183.844 289.259  1.00 49.31           C  
ANISOU  664  CB  MET A 103     2294   8134   8306   -989    506     98       C  
ATOM    665  CG  MET A 103     108.292 183.305 290.740  1.00 84.78           C  
ANISOU  665  CG  MET A 103     6768  12558  12885   -974    514    161       C  
ATOM    666  SD  MET A 103     109.878 183.022 291.577  1.00 50.16           S  
ANISOU  666  SD  MET A 103     2353   8200   8504   -960    560    174       S  
ATOM    667  CE  MET A 103     110.501 184.695 291.706  1.00 49.32           C  
ANISOU  667  CE  MET A 103     2318   8187   8234   -994    621     77       C  
ATOM    668  N   TYR A 104     106.614 186.331 289.917  1.00 48.25           N  
ANISOU  668  N   TYR A 104     2269   8010   8054  -1008    538     60       N  
ATOM    669  CA  TYR A 104     106.101 187.273 290.890  1.00 48.04           C  
ANISOU  669  CA  TYR A 104     2272   7967   8013  -1017    579     64       C  
ATOM    670  C   TYR A 104     104.630 187.573 290.634  1.00 69.58           C  
ANISOU  670  C   TYR A 104     4976  10677  10783  -1013    547     85       C  
ATOM    671  O   TYR A 104     103.826 187.577 291.568  1.00 69.96           O  
ANISOU  671  O   TYR A 104     5013  10686  10882  -1014    549    133       O  
ATOM    672  CB  TYR A 104     106.933 188.540 290.857  1.00 47.49           C  
ANISOU  672  CB  TYR A 104     2289   7924   7832  -1028    647      7       C  
ATOM    673  CG  TYR A 104     108.068 188.501 291.865  1.00 65.54           C  
ANISOU  673  CG  TYR A 104     4587  10213  10104  -1044    696    -13       C  
ATOM    674  CD1 TYR A 104     107.893 188.952 293.166  1.00 67.67           C  
ANISOU  674  CD1 TYR A 104     4859  10459  10392  -1069    742     -7       C  
ATOM    675  CD2 TYR A 104     109.273 187.938 291.547  1.00 63.21           C  
ANISOU  675  CD2 TYR A 104     4282   9946   9789  -1038    695    -34       C  
ATOM    676  CE1 TYR A 104     108.886 188.878 294.094  1.00 67.91           C  
ANISOU  676  CE1 TYR A 104     4883  10484  10436  -1087    783    -24       C  
ATOM    677  CE2 TYR A 104     110.283 187.858 292.456  1.00 63.55           C  
ANISOU  677  CE2 TYR A 104     4315   9987   9845  -1050    735    -54       C  
ATOM    678  CZ  TYR A 104     110.098 188.330 293.741  1.00 66.57           C  
ANISOU  678  CZ  TYR A 104     4698  10334  10263  -1075    778    -49       C  
ATOM    679  OH  TYR A 104     111.067 188.286 294.705  1.00 68.38           O  
ANISOU  679  OH  TYR A 104     4902  10548  10533  -1089    818    -54       O  
ATOM    680  N   ALA A 105     104.261 187.864 289.382  1.00 69.31           N  
ANISOU  680  N   ALA A 105     4949  10663  10723  -1002    515     59       N  
ATOM    681  CA  ALA A 105     102.863 188.118 289.055  1.00 48.31           C  
ANISOU  681  CA  ALA A 105     2246   7995   8113   -994    476     75       C  
ATOM    682  C   ALA A 105     102.015 186.867 289.297  1.00 49.03           C  
ANISOU  682  C   ALA A 105     2285   8034   8311   -992    409    126       C  
ATOM    683  O   ALA A 105     100.922 186.952 289.870  1.00 55.96           O  
ANISOU  683  O   ALA A 105     3145   8870   9248   -985    396    171       O  
ATOM    684  CB  ALA A 105     102.755 188.617 287.624  1.00 48.21           C  
ANISOU  684  CB  ALA A 105     2246   8021   8051   -983    449     34       C  
ATOM    685  N   SER A 106     102.494 185.692 288.874  1.00 49.36           N  
ANISOU  685  N   SER A 106     2300   8070   8385  -1001    373    123       N  
ATOM    686  CA  SER A 106     101.689 184.482 289.034  1.00 50.18           C  
ANISOU  686  CA  SER A 106     2353   8110   8605  -1008    318    167       C  
ATOM    687  C   SER A 106     101.447 184.168 290.501  1.00 72.66           C  
ANISOU  687  C   SER A 106     5205  10885  11517  -1001    343    239       C  
ATOM    688  O   SER A 106     100.328 183.814 290.886  1.00 73.06           O  
ANISOU  688  O   SER A 106     5223  10890  11645  -1006    315    283       O  
ATOM    689  CB  SER A 106     102.351 183.286 288.355  1.00 50.61           C  
ANISOU  689  CB  SER A 106     2376   8155   8700  -1022    292    153       C  
ATOM    690  OG  SER A 106     102.212 183.338 286.947  1.00 86.62           O  
ANISOU  690  OG  SER A 106     6907  12788  13215  -1046    250     99       O  
ATOM    691  N   VAL A 107     102.481 184.284 291.335  1.00 71.76           N  
ANISOU  691  N   VAL A 107     5123  10773  11368   -997    396    255       N  
ATOM    692  CA  VAL A 107     102.327 183.862 292.722  1.00 50.50           C  
ANISOU  692  CA  VAL A 107     2423   8031   8733   -999    416    332       C  
ATOM    693  C   VAL A 107     101.470 184.851 293.503  1.00 50.37           C  
ANISOU  693  C   VAL A 107     2424   8026   8689  -1008    447    351       C  
ATOM    694  O   VAL A 107     100.751 184.457 294.429  1.00 68.02           O  
ANISOU  694  O   VAL A 107     4636  10221  10987  -1016    446    419       O  
ATOM    695  CB  VAL A 107     103.703 183.659 293.379  1.00 50.41           C  
ANISOU  695  CB  VAL A 107     2422   8037   8696   -996    457    345       C  
ATOM    696  CG1 VAL A 107     104.364 184.997 293.668  1.00 49.72           C  
ANISOU  696  CG1 VAL A 107     2381   8022   8487  -1010    518    286       C  
ATOM    697  CG2 VAL A 107     103.556 182.843 294.637  1.00 51.14           C  
ANISOU  697  CG2 VAL A 107     2483   8077   8871   -998    459    446       C  
ATOM    698  N   LEU A 108     101.508 186.138 293.144  1.00 49.76           N  
ANISOU  698  N   LEU A 108     2383   8000   8524  -1008    481    294       N  
ATOM    699  CA  LEU A 108     100.686 187.111 293.855  1.00 61.62           C  
ANISOU  699  CA  LEU A 108     3894   9507  10012  -1016    521    311       C  
ATOM    700  C   LEU A 108      99.210 186.944 293.506  1.00 50.31           C  
ANISOU  700  C   LEU A 108     2419   8041   8657  -1003    471    344       C  
ATOM    701  O   LEU A 108      98.346 187.055 294.383  1.00 50.77           O  
ANISOU  701  O   LEU A 108     2457   8078   8754  -1012    490    393       O  
ATOM    702  CB  LEU A 108     101.161 188.538 293.558  1.00 60.87           C  
ANISOU  702  CB  LEU A 108     3843   9464   9820  -1021    583    247       C  
ATOM    703  CG  LEU A 108     102.556 188.964 294.043  1.00 48.71           C  
ANISOU  703  CG  LEU A 108     2341   7967   8199  -1049    650    196       C  
ATOM    704  CD1 LEU A 108     102.684 190.486 294.105  1.00 48.34           C  
ANISOU  704  CD1 LEU A 108     2332   7960   8075  -1071    732    142       C  
ATOM    705  CD2 LEU A 108     102.914 188.331 295.376  1.00 49.15           C  
ANISOU  705  CD2 LEU A 108     2382   8013   8279  -1073    669    238       C  
ATOM    706  N   LEU A 109      98.899 186.669 292.236  1.00 50.41           N  
ANISOU  706  N   LEU A 109     2404   8059   8690   -988    409    313       N  
ATOM    707  CA  LEU A 109      97.520 186.352 291.879  1.00 51.15           C  
ANISOU  707  CA  LEU A 109     2439   8131   8865   -983    351    337       C  
ATOM    708  C   LEU A 109      97.023 185.139 292.654  1.00 75.85           C  
ANISOU  708  C   LEU A 109     5530  11198  12091  -1002    329    396       C  
ATOM    709  O   LEU A 109      95.879 185.119 293.125  1.00 81.43           O  
ANISOU  709  O   LEU A 109     6196  11881  12861  -1007    322    438       O  
ATOM    710  CB  LEU A 109      97.398 186.106 290.377  1.00 58.67           C  
ANISOU  710  CB  LEU A 109     3355   9122   9814   -980    282    281       C  
ATOM    711  CG  LEU A 109      97.823 187.238 289.446  1.00 50.72           C  
ANISOU  711  CG  LEU A 109     2372   8181   8719   -961    297    226       C  
ATOM    712  CD1 LEU A 109      97.552 186.842 288.016  1.00 51.16           C  
ANISOU  712  CD1 LEU A 109     2371   8295   8773   -971    219    172       C  
ATOM    713  CD2 LEU A 109      97.104 188.526 289.786  1.00 64.92           C  
ANISOU  713  CD2 LEU A 109     4174   9977  10517   -934    338    254       C  
ATOM    714  N   ILE A 110      97.876 184.123 292.810  1.00 70.68           N  
ANISOU  714  N   ILE A 110     4881  10515  11460  -1013    325    407       N  
ATOM    715  CA  ILE A 110      97.483 182.935 293.561  1.00 68.05           C  
ANISOU  715  CA  ILE A 110     4510  10112  11234  -1030    313    475       C  
ATOM    716  C   ILE A 110      97.333 183.260 295.040  1.00 67.67           C  
ANISOU  716  C   ILE A 110     4475  10058  11179  -1039    370    543       C  
ATOM    717  O   ILE A 110      96.506 182.658 295.737  1.00 68.42           O  
ANISOU  717  O   ILE A 110     4529  10109  11358  -1056    366    605       O  
ATOM    718  CB  ILE A 110      98.491 181.797 293.320  1.00 52.92           C  
ANISOU  718  CB  ILE A 110     2588   8158   9361  -1032    301    479       C  
ATOM    719  CG1 ILE A 110      98.505 181.428 291.835  1.00 54.00           C  
ANISOU  719  CG1 ILE A 110     2700   8312   9507  -1040    248    403       C  
ATOM    720  CG2 ILE A 110      98.163 180.592 294.189  1.00 53.85           C  
ANISOU  720  CG2 ILE A 110     2664   8191   9604  -1046    300    566       C  
ATOM    721  CD1 ILE A 110      98.911 179.999 291.545  1.00 53.95           C  
ANISOU  721  CD1 ILE A 110     2655   8235   9607  -1054    230    412       C  
ATOM    722  N   THR A 111      98.111 184.214 295.546  1.00 52.17           N  
ANISOU  722  N   THR A 111     2562   8146   9115  -1037    428    525       N  
ATOM    723  CA  THR A 111      97.881 184.691 296.903  1.00 52.37           C  
ANISOU  723  CA  THR A 111     2591   8190   9116  -1060    488    568       C  
ATOM    724  C   THR A 111      96.516 185.362 297.007  1.00 52.71           C  
ANISOU  724  C   THR A 111     2609   8234   9183  -1063    498    571       C  
ATOM    725  O   THR A 111      95.719 185.035 297.893  1.00 53.43           O  
ANISOU  725  O   THR A 111     2664   8307   9330  -1085    513    628       O  
ATOM    726  CB  THR A 111      98.998 185.647 297.318  1.00 51.69           C  
ANISOU  726  CB  THR A 111     2555   8169   8916  -1071    553    523       C  
ATOM    727  OG1 THR A 111     100.205 185.283 296.639  1.00 80.38           O  
ANISOU  727  OG1 THR A 111     6208  11809  12523  -1054    533    489       O  
ATOM    728  CG2 THR A 111      99.240 185.554 298.809  1.00 52.15           C  
ANISOU  728  CG2 THR A 111     2604   8250   8959  -1108    605    574       C  
ATOM    729  N   ALA A 112      96.211 186.274 296.078  1.00 56.22           N  
ANISOU  729  N   ALA A 112     3063   8702   9596  -1039    489    518       N  
ATOM    730  CA  ALA A 112      94.941 186.994 296.125  1.00 52.76           C  
ANISOU  730  CA  ALA A 112     2590   8265   9191  -1032    500    528       C  
ATOM    731  C   ALA A 112      93.756 186.044 295.998  1.00 53.73           C  
ANISOU  731  C   ALA A 112     2641   8343   9430  -1036    440    569       C  
ATOM    732  O   ALA A 112      92.817 186.101 296.801  1.00 54.43           O  
ANISOU  732  O   ALA A 112     2691   8421   9568  -1052    467    611       O  
ATOM    733  CB  ALA A 112      94.897 188.058 295.028  1.00 52.31           C  
ANISOU  733  CB  ALA A 112     2544   8237   9093   -997    493    479       C  
ATOM    734  N   MET A 113      93.779 185.164 294.989  1.00 62.35           N  
ANISOU  734  N   MET A 113     3709   9415  10565  -1031    363    549       N  
ATOM    735  CA  MET A 113      92.706 184.184 294.838  1.00 54.96           C  
ANISOU  735  CA  MET A 113     2699   8441   9743  -1050    308    574       C  
ATOM    736  C   MET A 113      92.498 183.389 296.117  1.00 78.88           C  
ANISOU  736  C   MET A 113     5712  11423  12835  -1082    343    646       C  
ATOM    737  O   MET A 113      91.360 183.174 296.549  1.00 78.40           O  
ANISOU  737  O   MET A 113     5593  11344  12852  -1101    342    680       O  
ATOM    738  CB  MET A 113      93.011 183.224 293.693  1.00 55.13           C  
ANISOU  738  CB  MET A 113     2698   8453   9795  -1059    235    529       C  
ATOM    739  CG  MET A 113      93.087 183.844 292.323  1.00 94.81           C  
ANISOU  739  CG  MET A 113     7718  13543  14761  -1038    189    457       C  
ATOM    740  SD  MET A 113      93.046 182.525 291.092  1.00 93.26           S  
ANISOU  740  SD  MET A 113     7462  13352  14619  -1078    102    399       S  
ATOM    741  CE  MET A 113      93.952 181.243 291.952  1.00 97.28           C  
ANISOU  741  CE  MET A 113     8003  13766  15194  -1098    140    447       C  
ATOM    742  N   SER A 114      93.590 182.943 296.735  1.00 75.72           N  
ANISOU  742  N   SER A 114     5356  11009  12406  -1090    373    674       N  
ATOM    743  CA  SER A 114      93.488 182.158 297.957  1.00 76.40           C  
ANISOU  743  CA  SER A 114     5421  11060  12549  -1120    405    756       C  
ATOM    744  C   SER A 114      93.180 183.029 299.168  1.00 55.94           C  
ANISOU  744  C   SER A 114     2837   8515   9903  -1139    480    782       C  
ATOM    745  O   SER A 114      92.466 182.587 300.077  1.00 56.81           O  
ANISOU  745  O   SER A 114     2904   8610  10073  -1171    505    843       O  
ATOM    746  CB  SER A 114      94.782 181.371 298.172  1.00 75.27           C  
ANISOU  746  CB  SER A 114     5305  10892  12401  -1116    407    789       C  
ATOM    747  OG  SER A 114      94.859 180.857 299.486  1.00 74.71           O  
ANISOU  747  OG  SER A 114     5217  10811  12358  -1142    448    883       O  
ATOM    748  N   LEU A 115      93.697 184.260 299.197  1.00 55.14           N  
ANISOU  748  N   LEU A 115     2784   8475   9691  -1128    525    732       N  
ATOM    749  CA  LEU A 115      93.386 185.184 300.283  1.00 71.03           C  
ANISOU  749  CA  LEU A 115     4798  10541  11651  -1158    608    733       C  
ATOM    750  C   LEU A 115      91.925 185.614 300.260  1.00 73.66           C  
ANISOU  750  C   LEU A 115     5075  10866  12046  -1157    616    735       C  
ATOM    751  O   LEU A 115      91.411 186.087 301.283  1.00 56.55           O  
ANISOU  751  O   LEU A 115     2886   8732   9868  -1192    689    746       O  
ATOM    752  CB  LEU A 115      94.307 186.407 300.200  1.00 68.99           C  
ANISOU  752  CB  LEU A 115     4599  10343  11271  -1153    660    663       C  
ATOM    753  CG  LEU A 115      94.592 187.274 301.427  1.00 54.50           C  
ANISOU  753  CG  LEU A 115     2779   8578   9352  -1205    762    638       C  
ATOM    754  CD1 LEU A 115      96.007 187.821 301.342  1.00 53.68           C  
ANISOU  754  CD1 LEU A 115     2733   8519   9145  -1212    792    577       C  
ATOM    755  CD2 LEU A 115      93.592 188.415 301.534  1.00 56.01           C  
ANISOU  755  CD2 LEU A 115     2948   8791   9541  -1210    821    606       C  
ATOM    756  N   ASP A 116      91.247 185.438 299.121  1.00 75.45           N  
ANISOU  756  N   ASP A 116     5268  11058  12341  -1123    545    720       N  
ATOM    757  CA  ASP A 116      89.856 185.837 298.939  1.00 77.72           C  
ANISOU  757  CA  ASP A 116     5488  11342  12700  -1114    540    724       C  
ATOM    758  C   ASP A 116      88.864 184.744 299.320  1.00 79.92           C  
ANISOU  758  C   ASP A 116     5691  11580  13094  -1147    515    773       C  
ATOM    759  O   ASP A 116      87.882 185.025 300.016  1.00 81.69           O  
ANISOU  759  O   ASP A 116     5863  11814  13362  -1166    561    795       O  
ATOM    760  CB  ASP A 116      89.611 186.258 297.492  1.00 56.76           C  
ANISOU  760  CB  ASP A 116     2818   8692  10055  -1065    472    682       C  
ATOM    761  CG  ASP A 116      88.147 186.242 297.136  1.00 79.56           C  
ANISOU  761  CG  ASP A 116     5609  11574  13046  -1057    435    695       C  
ATOM    762  OD1 ASP A 116      87.461 187.244 297.418  1.00 81.36           O  
ANISOU  762  OD1 ASP A 116     5806  11821  13286  -1037    484    704       O  
ATOM    763  OD2 ASP A 116      87.675 185.216 296.602  1.00 78.50           O  
ANISOU  763  OD2 ASP A 116     5421  11419  12987  -1073    360    694       O  
ATOM    764  N   ARG A 117      89.080 183.500 298.881  1.00 58.38           N  
ANISOU  764  N   ARG A 117     2952   8804  10424  -1158    451    786       N  
ATOM    765  CA  ARG A 117      88.179 182.434 299.302  1.00 59.61           C  
ANISOU  765  CA  ARG A 117     3036   8916  10697  -1199    438    832       C  
ATOM    766  C   ARG A 117      88.146 182.274 300.817  1.00101.41           C  
ANISOU  766  C   ARG A 117     8328  14215  15987  -1241    519    897       C  
ATOM    767  O   ARG A 117      87.309 181.520 301.319  1.00103.00           O  
ANISOU  767  O   ARG A 117     8465  14385  16285  -1280    526    942       O  
ATOM    768  CB  ARG A 117      88.566 181.112 298.636  1.00 59.81           C  
ANISOU  768  CB  ARG A 117     3053   8882  10791  -1211    372    833       C  
ATOM    769  CG  ARG A 117      87.457 180.074 298.650  1.00 61.24           C  
ANISOU  769  CG  ARG A 117     3143   9015  11110  -1256    344    854       C  
ATOM    770  CD  ARG A 117      87.911 178.788 298.015  1.00 91.62           C  
ANISOU  770  CD  ARG A 117     6981  12797  15032  -1277    294    846       C  
ATOM    771  NE  ARG A 117      86.880 177.757 298.073  1.00 92.26           N  
ANISOU  771  NE  ARG A 117     6973  12827  15255  -1332    277    861       N  
ATOM    772  CZ  ARG A 117      87.005 176.603 298.721  1.00 92.14           C  
ANISOU  772  CZ  ARG A 117     6941  12730  15338  -1370    304    928       C  
ATOM    773  NH1 ARG A 117      88.125 176.315 299.374  1.00 90.73           N  
ANISOU  773  NH1 ARG A 117     6822  12520  15132  -1351    343    996       N  
ATOM    774  NH2 ARG A 117      86.007 175.729 298.706  1.00 94.06           N  
ANISOU  774  NH2 ARG A 117     7098  12927  15714  -1427    294    931       N  
ATOM    775  N   SER A 118      89.006 182.981 301.558  1.00 59.35           N  
ANISOU  775  N   SER A 118     3063   8939  10550  -1242    584    898       N  
ATOM    776  CA  SER A 118      88.876 183.052 303.006  1.00 59.94           C  
ANISOU  776  CA  SER A 118     3124   9052  10600  -1294    669    943       C  
ATOM    777  C   SER A 118      88.038 184.229 303.458  1.00 60.29           C  
ANISOU  777  C   SER A 118     3141   9151  10617  -1306    741    905       C  
ATOM    778  O   SER A 118      87.612 184.245 304.614  1.00 64.16           O  
ANISOU  778  O   SER A 118     3598   9677  11104  -1361    816    931       O  
ATOM    779  CB  SER A 118      90.243 183.134 303.694  1.00 63.32           C  
ANISOU  779  CB  SER A 118     3615   9523  10921  -1308    707    957       C  
ATOM    780  OG  SER A 118      90.103 183.043 305.103  1.00 63.94           O  
ANISOU  780  OG  SER A 118     3669   9649  10977  -1370    784   1005       O  
ATOM    781  N   LEU A 119      87.806 185.213 302.593  1.00 59.81           N  
ANISOU  781  N   LEU A 119     3087   9099  10539  -1259    726    849       N  
ATOM    782  CA  LEU A 119      86.857 186.270 302.900  1.00 78.03           C  
ANISOU  782  CA  LEU A 119     5349  11441  12857  -1260    792    826       C  
ATOM    783  C   LEU A 119      85.448 185.943 302.425  1.00 61.49           C  
ANISOU  783  C   LEU A 119     3160   9309  10896  -1245    748    846       C  
ATOM    784  O   LEU A 119      84.489 186.569 302.891  1.00 98.59           O  
ANISOU  784  O   LEU A 119     7796  14029  15633  -1254    809    846       O  
ATOM    785  CB  LEU A 119      87.316 187.594 302.284  1.00 59.50           C  
ANISOU  785  CB  LEU A 119     3049   9122  10436  -1214    812    771       C  
ATOM    786  CG  LEU A 119      86.675 188.842 302.882  1.00 60.06           C  
ANISOU  786  CG  LEU A 119     3089   9235  10496  -1223    916    748       C  
ATOM    787  CD1 LEU A 119      87.107 188.998 304.324  1.00 60.32           C  
ANISOU  787  CD1 LEU A 119     3141   9337  10440  -1308   1024    730       C  
ATOM    788  CD2 LEU A 119      87.028 190.072 302.080  1.00 59.34           C  
ANISOU  788  CD2 LEU A 119     3034   9150  10363  -1167    928    710       C  
ATOM    789  N   ALA A 120      85.299 184.979 301.516  1.00 66.72           N  
ANISOU  789  N   ALA A 120     3798   9921  11630  -1229    648    856       N  
ATOM    790  CA  ALA A 120      83.976 184.526 301.116  1.00 62.88           C  
ANISOU  790  CA  ALA A 120     3208   9413  11271  -1234    602    866       C  
ATOM    791  C   ALA A 120      83.344 183.594 302.138  1.00 64.06           C  
ANISOU  791  C   ALA A 120     3302   9544  11494  -1301    641    914       C  
ATOM    792  O   ALA A 120      82.147 183.306 302.041  1.00 72.97           O  
ANISOU  792  O   ALA A 120     4332  10663  12729  -1317    626    920       O  
ATOM    793  CB  ALA A 120      84.036 183.825 299.759  1.00 62.79           C  
ANISOU  793  CB  ALA A 120     3181   9374  11301  -1212    486    839       C  
ATOM    794  N   VAL A 121      84.111 183.108 303.107  1.00 63.81           N  
ANISOU  794  N   VAL A 121     3321   9511  11411  -1342    690    951       N  
ATOM    795  CA  VAL A 121      83.546 182.332 304.200  1.00 65.01           C  
ANISOU  795  CA  VAL A 121     3420   9656  11623  -1411    743   1007       C  
ATOM    796  C   VAL A 121      83.660 183.048 305.532  1.00 65.18           C  
ANISOU  796  C   VAL A 121     3456   9750  11558  -1454    861   1012       C  
ATOM    797  O   VAL A 121      82.860 182.766 306.435  1.00 66.42           O  
ANISOU  797  O   VAL A 121     3549   9925  11763  -1513    924   1042       O  
ATOM    798  CB  VAL A 121      84.183 180.929 304.290  1.00 65.07           C  
ANISOU  798  CB  VAL A 121     3448   9604  11671  -1437    704   1065       C  
ATOM    799  CG1 VAL A 121      84.748 180.505 302.941  1.00 64.31           C  
ANISOU  799  CG1 VAL A 121     3383   9457  11593  -1390    603   1032       C  
ATOM    800  CG2 VAL A 121      85.244 180.860 305.361  1.00 64.64           C  
ANISOU  800  CG2 VAL A 121     3456   9584  11522  -1463    765   1114       C  
ATOM    801  N   ALA A 122      84.600 183.976 305.685  1.00 64.11           N  
ANISOU  801  N   ALA A 122     3396   9667  11296  -1438    898    974       N  
ATOM    802  CA  ALA A 122      84.670 184.729 306.931  1.00 66.96           C  
ANISOU  802  CA  ALA A 122     3761  10114  11568  -1497   1019    954       C  
ATOM    803  C   ALA A 122      83.456 185.634 307.080  1.00 65.37           C  
ANISOU  803  C   ALA A 122     3487   9940  11410  -1500   1084    919       C  
ATOM    804  O   ALA A 122      82.830 185.681 308.143  1.00 84.00           O  
ANISOU  804  O   ALA A 122     5794  12349  13773  -1570   1177    924       O  
ATOM    805  CB  ALA A 122      85.966 185.542 306.996  1.00 65.38           C  
ANISOU  805  CB  ALA A 122     3649   9966  11225  -1490   1048    903       C  
ATOM    806  N   SER A 123      83.097 186.347 306.019  1.00 65.01           N  
ANISOU  806  N   SER A 123     3430   9865  11404  -1425   1039    889       N  
ATOM    807  CA  SER A 123      81.861 187.116 306.021  1.00 73.30           C  
ANISOU  807  CA  SER A 123     4394  10925  12532  -1409   1087    876       C  
ATOM    808  C   SER A 123      81.396 187.318 304.585  1.00 73.81           C  
ANISOU  808  C   SER A 123     4426  10935  12685  -1318    986    874       C  
ATOM    809  O   SER A 123      81.947 188.175 303.886  1.00 73.36           O  
ANISOU  809  O   SER A 123     4419  10877  12577  -1259    970    847       O  
ATOM    810  CB  SER A 123      82.055 188.466 306.714  1.00 66.06           C  
ANISOU  810  CB  SER A 123     3497  10077  11524  -1428   1212    828       C  
ATOM    811  OG  SER A 123      82.773 189.360 305.878  1.00 69.38           O  
ANISOU  811  OG  SER A 123     3983  10488  11891  -1361   1187    795       O  
ATOM    812  N   PRO A 124      80.400 186.569 304.101  1.00 66.90           N  
ANISOU  812  N   PRO A 124     3461  10022  11936  -1313    917    899       N  
ATOM    813  CA  PRO A 124      80.041 186.670 302.680  1.00 66.85           C  
ANISOU  813  CA  PRO A 124     3416   9989  11996  -1241    808    889       C  
ATOM    814  C   PRO A 124      79.267 187.917 302.322  1.00 75.42           C  
ANISOU  814  C   PRO A 124     4433  11088  13134  -1177    839    883       C  
ATOM    815  O   PRO A 124      78.939 188.100 301.141  1.00 75.67           O  
ANISOU  815  O   PRO A 124     4421  11115  13216  -1115    749    879       O  
ATOM    816  CB  PRO A 124      79.183 185.415 302.440  1.00 68.04           C  
ANISOU  816  CB  PRO A 124     3476  10114  12261  -1279    738    908       C  
ATOM    817  CG  PRO A 124      79.511 184.514 303.577  1.00 68.19           C  
ANISOU  817  CG  PRO A 124     3526  10124  12258  -1359    793    938       C  
ATOM    818  CD  PRO A 124      79.736 185.426 304.738  1.00 68.08           C  
ANISOU  818  CD  PRO A 124     3546  10160  12163  -1382    923    934       C  
ATOM    819  N   PHE A 125      78.932 188.757 303.291  1.00 68.04           N  
ANISOU  819  N   PHE A 125     3480  10176  12196  -1192    966    882       N  
ATOM    820  CA  PHE A 125      78.247 190.001 302.985  1.00 83.37           C  
ANISOU  820  CA  PHE A 125     5355  12115  14205  -1122   1011    885       C  
ATOM    821  C   PHE A 125      79.203 191.139 302.682  1.00 77.84           C  
ANISOU  821  C   PHE A 125     4748  11414  13413  -1072   1049    864       C  
ATOM    822  O   PHE A 125      78.811 192.087 301.994  1.00 76.99           O  
ANISOU  822  O   PHE A 125     4597  11287  13370   -991   1050    877       O  
ATOM    823  CB  PHE A 125      77.331 190.395 304.145  1.00 87.82           C  
ANISOU  823  CB  PHE A 125     5839  12698  14829  -1163   1144    889       C  
ATOM    824  CG  PHE A 125      76.225 189.421 304.393  1.00 71.70           C  
ANISOU  824  CG  PHE A 125     3686  10658  12899  -1207   1117    911       C  
ATOM    825  CD1 PHE A 125      75.453 188.950 303.348  1.00 72.45           C  
ANISOU  825  CD1 PHE A 125     3685  10738  13104  -1166    998    927       C  
ATOM    826  CD2 PHE A 125      75.972 188.964 305.670  1.00 77.94           C  
ANISOU  826  CD2 PHE A 125     4460  11478  13675  -1301   1212    912       C  
ATOM    827  CE1 PHE A 125      74.441 188.048 303.576  1.00 73.93           C  
ANISOU  827  CE1 PHE A 125     3763  10933  13395  -1217    978    940       C  
ATOM    828  CE2 PHE A 125      74.962 188.063 305.903  1.00 79.38           C  
ANISOU  828  CE2 PHE A 125     4537  11660  13964  -1347   1195    932       C  
ATOM    829  CZ  PHE A 125      74.195 187.602 304.857  1.00 74.63           C  
ANISOU  829  CZ  PHE A 125     3841  11035  13480  -1306   1079    945       C  
ATOM    830  N   LEU A 126      80.441 191.065 303.171  1.00 74.40           N  
ANISOU  830  N   LEU A 126     4432  11002  12836  -1120   1082    835       N  
ATOM    831  CA  LEU A 126      81.436 192.076 302.837  1.00 72.57           C  
ANISOU  831  CA  LEU A 126     4290  10774  12510  -1084   1115    807       C  
ATOM    832  C   LEU A 126      82.004 191.857 301.441  1.00 70.81           C  
ANISOU  832  C   LEU A 126     4107  10524  12272  -1021    986    810       C  
ATOM    833  O   LEU A 126      82.394 192.825 300.775  1.00 63.45           O  
ANISOU  833  O   LEU A 126     3207   9581  11320   -961    995    804       O  
ATOM    834  CB  LEU A 126      82.554 192.071 303.883  1.00 73.00           C  
ANISOU  834  CB  LEU A 126     4442  10885  12411  -1168   1195    766       C  
ATOM    835  CG  LEU A 126      83.587 193.195 303.838  1.00 73.13           C  
ANISOU  835  CG  LEU A 126     4545  10925  12317  -1160   1262    724       C  
ATOM    836  CD1 LEU A 126      82.940 194.521 303.442  1.00 74.71           C  
ANISOU  836  CD1 LEU A 126     4697  11085  12605  -1086   1329    736       C  
ATOM    837  CD2 LEU A 126      84.278 193.321 305.191  1.00 63.25           C  
ANISOU  837  CD2 LEU A 126     3341   9764  10926  -1270   1372    676       C  
ATOM    838  N   SER A 127      82.032 190.602 300.984  1.00 63.82           N  
ANISOU  838  N   SER A 127     3217   9631  11402  -1038    873    818       N  
ATOM    839  CA  SER A 127      82.558 190.289 299.661  1.00 68.01           C  
ANISOU  839  CA  SER A 127     3779  10151  11911   -994    752    810       C  
ATOM    840  C   SER A 127      81.796 191.031 298.572  1.00 70.48           C  
ANISOU  840  C   SER A 127     4010  10463  12306   -911    703    828       C  
ATOM    841  O   SER A 127      82.400 191.590 297.652  1.00 67.84           O  
ANISOU  841  O   SER A 127     3717  10133  11925   -860    667    818       O  
ATOM    842  CB  SER A 127      82.508 188.779 299.434  1.00 63.14           C  
ANISOU  842  CB  SER A 127     3146   9523  11320  -1037    655    812       C  
ATOM    843  OG  SER A 127      83.472 188.134 300.246  1.00 62.35           O  
ANISOU  843  OG  SER A 127     3132   9421  11137  -1095    689    806       O  
ATOM    844  N   GLN A 128      80.467 191.066 298.668  1.00 74.18           N  
ANISOU  844  N   GLN A 128     4353  10932  12900   -897    704    857       N  
ATOM    845  CA  GLN A 128      79.683 191.791 297.672  1.00 80.00           C  
ANISOU  845  CA  GLN A 128     4991  11681  13725   -813    655    886       C  
ATOM    846  C   GLN A 128      80.073 193.262 297.635  1.00 82.49           C  
ANISOU  846  C   GLN A 128     5347  11974  14022   -748    747    901       C  
ATOM    847  O   GLN A 128      80.078 193.887 296.566  1.00 79.74           O  
ANISOU  847  O   GLN A 128     4973  11634  13691   -672    695    924       O  
ATOM    848  CB  GLN A 128      78.185 191.651 297.963  1.00 83.27           C  
ANISOU  848  CB  GLN A 128     5253  12104  14283   -810    659    916       C  
ATOM    849  CG  GLN A 128      77.486 190.541 297.190  1.00 85.18           C  
ANISOU  849  CG  GLN A 128     5396  12388  14581   -832    519    908       C  
ATOM    850  CD  GLN A 128      77.125 189.356 298.064  1.00 86.70           C  
ANISOU  850  CD  GLN A 128     5570  12571  14802   -926    534    895       C  
ATOM    851  OE1 GLN A 128      77.415 189.343 299.261  1.00 87.29           O  
ANISOU  851  OE1 GLN A 128     5705  12615  14845   -973    643    897       O  
ATOM    852  NE2 GLN A 128      76.483 188.355 297.471  1.00 88.05           N  
ANISOU  852  NE2 GLN A 128     5649  12777  15029   -959    426    879       N  
ATOM    853  N   LYS A 129      80.405 193.832 298.794  1.00 93.53           N  
ANISOU  853  N   LYS A 129     6803  13351  15384   -782    890    888       N  
ATOM    854  CA  LYS A 129      80.816 195.225 298.886  1.00103.95           C  
ANISOU  854  CA  LYS A 129     8164  14643  16688   -736   1001    892       C  
ATOM    855  C   LYS A 129      82.321 195.414 298.731  1.00114.87           C  
ANISOU  855  C   LYS A 129     9690  16036  17919   -760   1011    849       C  
ATOM    856  O   LYS A 129      82.790 196.558 298.769  1.00120.70           O  
ANISOU  856  O   LYS A 129    10473  16753  18634   -732   1107    845       O  
ATOM    857  CB  LYS A 129      80.355 195.835 300.217  1.00 66.19           C  
ANISOU  857  CB  LYS A 129     3358   9846  11945   -772   1164    885       C  
ATOM    858  CG  LYS A 129      78.989 196.510 300.150  1.00 68.08           C  
ANISOU  858  CG  LYS A 129     3457  10049  12361   -700   1210    937       C  
ATOM    859  CD  LYS A 129      78.784 197.495 301.299  1.00 82.99           C  
ANISOU  859  CD  LYS A 129     5343  11909  14282   -720   1402    920       C  
ATOM    860  CE  LYS A 129      78.786 196.790 302.650  1.00 81.38           C  
ANISOU  860  CE  LYS A 129     5158  11755  14009   -838   1466    874       C  
ATOM    861  NZ  LYS A 129      78.597 197.712 303.810  1.00 80.68           N  
ANISOU  861  NZ  LYS A 129     5063  11659  13932   -876   1657    845       N  
ATOM    862  N   VAL A 130      83.086 194.335 298.550  1.00115.68           N  
ANISOU  862  N   VAL A 130     9860  16166  17928   -809    922    818       N  
ATOM    863  CA  VAL A 130      84.532 194.459 298.401  1.00 60.85           C  
ANISOU  863  CA  VAL A 130     3040   9236  10843   -832    929    775       C  
ATOM    864  C   VAL A 130      84.990 193.818 297.096  1.00 60.11           C  
ANISOU  864  C   VAL A 130     2966   9152  10722   -802    790    769       C  
ATOM    865  O   VAL A 130      85.914 194.322 296.450  1.00 59.34           O  
ANISOU  865  O   VAL A 130     2937   9060  10551   -779    787    749       O  
ATOM    866  CB  VAL A 130      85.258 193.866 299.627  1.00 60.28           C  
ANISOU  866  CB  VAL A 130     3039   9197  10668   -929    985    734       C  
ATOM    867  CG1 VAL A 130      86.142 192.693 299.261  1.00 59.25           C  
ANISOU  867  CG1 VAL A 130     2971   9078  10465   -959    885    714       C  
ATOM    868  CG2 VAL A 130      86.057 194.949 300.324  1.00 59.84           C  
ANISOU  868  CG2 VAL A 130     3054   9168  10516   -961   1117    695       C  
ATOM    869  N   ARG A 131      84.341 192.730 296.676  1.00 60.70           N  
ANISOU  869  N   ARG A 131     2973   9234  10855   -809    680    780       N  
ATOM    870  CA  ARG A 131      84.703 192.053 295.426  1.00 60.25           C  
ANISOU  870  CA  ARG A 131     2922   9201  10771   -794    550    760       C  
ATOM    871  C   ARG A 131      83.962 192.711 294.259  1.00 70.93           C  
ANISOU  871  C   ARG A 131     4181  10577  12192   -715    486    790       C  
ATOM    872  O   ARG A 131      82.982 192.195 293.718  1.00 71.67           O  
ANISOU  872  O   ARG A 131     4164  10701  12365   -704    394    803       O  
ATOM    873  CB  ARG A 131      84.417 190.559 295.531  1.00 60.62           C  
ANISOU  873  CB  ARG A 131     2938   9251  10844   -852    471    747       C  
ATOM    874  CG  ARG A 131      84.685 189.766 294.273  1.00 60.45           C  
ANISOU  874  CG  ARG A 131     2905   9261  10802   -851    343    711       C  
ATOM    875  CD  ARG A 131      84.606 188.275 294.516  1.00 60.74           C  
ANISOU  875  CD  ARG A 131     2930   9286  10864   -919    292    694       C  
ATOM    876  NE  ARG A 131      84.349 187.581 293.261  1.00 65.24           N  
ANISOU  876  NE  ARG A 131     3437   9903  11450   -924    169    655       N  
ATOM    877  CZ  ARG A 131      84.850 186.394 292.937  1.00 65.29           C  
ANISOU  877  CZ  ARG A 131     3464   9906  11438   -975    114    614       C  
ATOM    878  NH1 ARG A 131      85.653 185.754 293.777  1.00 60.33           N  
ANISOU  878  NH1 ARG A 131     2919   9220  10784  -1013    167    623       N  
ATOM    879  NH2 ARG A 131      84.556 185.856 291.761  1.00 61.77           N  
ANISOU  879  NH2 ARG A 131     2948   9522  11001   -990      7    563       N  
ATOM    880  N   THR A 132      84.457 193.892 293.890  1.00 70.62           N  
ANISOU  880  N   THR A 132     4181  10530  12123   -661    539    803       N  
ATOM    881  CA  THR A 132      83.955 194.670 292.764  1.00 61.40           C  
ANISOU  881  CA  THR A 132     2934   9386  11011   -575    489    846       C  
ATOM    882  C   THR A 132      84.925 194.522 291.600  1.00 60.42           C  
ANISOU  882  C   THR A 132     2865   9304  10789   -567    408    808       C  
ATOM    883  O   THR A 132      86.141 194.623 291.791  1.00 64.11           O  
ANISOU  883  O   THR A 132     3450   9755  11153   -599    461    767       O  
ATOM    884  CB  THR A 132      83.817 196.153 293.138  1.00 61.74           C  
ANISOU  884  CB  THR A 132     2976   9380  11104   -515    621    898       C  
ATOM    885  OG1 THR A 132      83.243 196.270 294.444  1.00 84.06           O  
ANISOU  885  OG1 THR A 132     5783  12165  13990   -547    728    906       O  
ATOM    886  CG2 THR A 132      82.936 196.893 292.141  1.00 72.47           C  
ANISOU  886  CG2 THR A 132     4213  10756  12566   -412    569    974       C  
ATOM    887  N   LYS A 133      84.388 194.285 290.399  1.00 61.29           N  
ANISOU  887  N   LYS A 133     2880   9480  10927   -529    279    814       N  
ATOM    888  CA  LYS A 133      85.228 194.225 289.206  1.00 71.56           C  
ANISOU  888  CA  LYS A 133     4216  10835  12139   -520    203    773       C  
ATOM    889  C   LYS A 133      86.076 195.483 289.069  1.00 70.48           C  
ANISOU  889  C   LYS A 133     4157  10664  11958   -474    300    801       C  
ATOM    890  O   LYS A 133      87.222 195.423 288.605  1.00 68.73           O  
ANISOU  890  O   LYS A 133     4022  10457  11634   -497    299    748       O  
ATOM    891  CB  LYS A 133      84.374 194.013 287.960  1.00 62.04           C  
ANISOU  891  CB  LYS A 133     2873   9724  10974   -478     54    782       C  
ATOM    892  N   THR A 134      85.535 196.634 289.486  1.00 73.25           N  
ANISOU  892  N   THR A 134     4474  10967  12392   -411    396    879       N  
ATOM    893  CA  THR A 134      86.319 197.863 289.453  1.00 75.40           C  
ANISOU  893  CA  THR A 134     4820  11195  12634   -375    512    905       C  
ATOM    894  C   THR A 134      87.397 197.861 290.530  1.00 76.51           C  
ANISOU  894  C   THR A 134     5097  11289  12683   -455    633    841       C  
ATOM    895  O   THR A 134      88.470 198.439 290.327  1.00 79.75           O  
ANISOU  895  O   THR A 134     5597  11692  13014   -463    698    816       O  
ATOM    896  CB  THR A 134      85.405 199.094 289.588  1.00 61.13           C  
ANISOU  896  CB  THR A 134     2929   9339  10959   -282    594   1009       C  
ATOM    897  OG1 THR A 134      86.019 200.225 288.954  1.00 66.22           O  
ANISOU  897  OG1 THR A 134     3585   9931  11643   -217    663   1106       O  
ATOM    898  CG2 THR A 134      85.134 199.443 291.050  1.00 61.28           C  
ANISOU  898  CG2 THR A 134     2975   9280  11029   -315    742   1008       C  
ATOM    899  N   ALA A 135      87.154 197.196 291.659  1.00 73.87           N  
ANISOU  899  N   ALA A 135     4777  10936  12356   -517    661    813       N  
ATOM    900  CA  ALA A 135      88.158 197.069 292.705  1.00 69.83           C  
ANISOU  900  CA  ALA A 135     4380  10407  11746   -596    754    753       C  
ATOM    901  C   ALA A 135      88.962 195.783 292.579  1.00 56.18           C  
ANISOU  901  C   ALA A 135     2709   8715   9923   -660    668    687       C  
ATOM    902  O   ALA A 135      89.795 195.500 293.445  1.00 64.19           O  
ANISOU  902  O   ALA A 135     3804   9728  10856   -724    725    642       O  
ATOM    903  CB  ALA A 135      87.503 197.148 294.090  1.00 68.76           C  
ANISOU  903  CB  ALA A 135     4223  10239  11663   -629    847    763       C  
ATOM    904  N   ALA A 136      88.715 194.995 291.535  1.00 56.41           N  
ANISOU  904  N   ALA A 136     2687   8781   9964   -644    535    679       N  
ATOM    905  CA  ALA A 136      89.557 193.861 291.180  1.00 70.65           C  
ANISOU  905  CA  ALA A 136     4541  10615  11688   -695    461    613       C  
ATOM    906  C   ALA A 136      90.522 194.213 290.058  1.00 69.50           C  
ANISOU  906  C   ALA A 136     4438  10504  11464   -677    437    576       C  
ATOM    907  O   ALA A 136      91.708 193.874 290.125  1.00 67.98           O  
ANISOU  907  O   ALA A 136     4332  10318  11181   -720    458    519       O  
ATOM    908  CB  ALA A 136      88.693 192.662 290.773  1.00 56.46           C  
ANISOU  908  CB  ALA A 136     2657   8845   9951   -709    338    607       C  
ATOM    909  N   ARG A 137      90.028 194.891 289.019  1.00 55.48           N  
ANISOU  909  N   ARG A 137     2594   8757   9727   -613    395    610       N  
ATOM    910  CA  ARG A 137      90.911 195.406 287.981  1.00 54.87           C  
ANISOU  910  CA  ARG A 137     2553   8714   9582   -593    390    583       C  
ATOM    911  C   ARG A 137      91.925 196.378 288.569  1.00 77.97           C  
ANISOU  911  C   ARG A 137     5582  11598  12445   -607    534    578       C  
ATOM    912  O   ARG A 137      93.126 196.290 288.287  1.00 77.50           O  
ANISOU  912  O   ARG A 137     5600  11558  12290   -643    554    516       O  
ATOM    913  CB  ARG A 137      90.087 196.074 286.880  1.00 56.03           C  
ANISOU  913  CB  ARG A 137     2594   8900   9793   -512    324    645       C  
ATOM    914  CG  ARG A 137      89.907 195.190 285.659  1.00 56.83           C  
ANISOU  914  CG  ARG A 137     2609   9075   9908   -517    167    628       C  
ATOM    915  CD  ARG A 137      88.484 195.211 285.124  1.00 79.63           C  
ANISOU  915  CD  ARG A 137     5337  12001  12918   -460     56    721       C  
ATOM    916  NE  ARG A 137      88.444 195.641 283.729  1.00 80.60           N  
ANISOU  916  NE  ARG A 137     5357  12178  13088   -405    -43    826       N  
ATOM    917  CZ  ARG A 137      88.796 194.881 282.695  1.00 80.06           C  
ANISOU  917  CZ  ARG A 137     5251  12192  12976   -446   -164    770       C  
ATOM    918  NH1 ARG A 137      89.219 193.639 282.891  1.00 78.31           N  
ANISOU  918  NH1 ARG A 137     5086  11991  12677   -536   -188    607       N  
ATOM    919  NH2 ARG A 137      88.727 195.366 281.461  1.00 82.02           N  
ANISOU  919  NH2 ARG A 137     5399  12508  13255   -398   -260    890       N  
ATOM    920  N   TRP A 138      91.465 197.297 289.416  1.00 54.32           N  
ANISOU  920  N   TRP A 138     2585   8552   9504   -586    640    634       N  
ATOM    921  CA  TRP A 138      92.382 198.250 290.025  1.00 72.81           C  
ANISOU  921  CA  TRP A 138     5018  10864  11783   -613    784    617       C  
ATOM    922  C   TRP A 138      93.312 197.601 291.047  1.00 68.66           C  
ANISOU  922  C   TRP A 138     4578  10348  11160   -701    821    543       C  
ATOM    923  O   TRP A 138      94.159 198.296 291.622  1.00 68.26           O  
ANISOU  923  O   TRP A 138     4600  10297  11037   -742    932    512       O  
ATOM    924  CB  TRP A 138      91.592 199.397 290.658  1.00 78.11           C  
ANISOU  924  CB  TRP A 138     5654  11478  12546   -571    897    687       C  
ATOM    925  CG  TRP A 138      92.063 200.745 290.196  1.00 81.00           C  
ANISOU  925  CG  TRP A 138     6050  11817  12908   -534   1004    717       C  
ATOM    926  CD1 TRP A 138      92.147 201.190 288.904  1.00 85.75           C  
ANISOU  926  CD1 TRP A 138     6606  12410  13565   -465    971    796       C  
ATOM    927  CD2 TRP A 138      92.519 201.822 291.022  1.00 81.67           C  
ANISOU  927  CD2 TRP A 138     6199  11856  12974   -563   1173    708       C  
ATOM    928  NE1 TRP A 138      92.632 202.477 288.877  1.00 86.91           N  
ANISOU  928  NE1 TRP A 138     6784  12488  13750   -441   1122    856       N  
ATOM    929  CE2 TRP A 138      92.868 202.888 290.164  1.00 83.30           C  
ANISOU  929  CE2 TRP A 138     6410  12023  13219   -509   1244    769       C  
ATOM    930  CE3 TRP A 138      92.668 201.989 292.403  1.00 77.98           C  
ANISOU  930  CE3 TRP A 138     5776  11377  12476   -632   1277    666       C  
ATOM    931  CZ2 TRP A 138      93.357 204.102 290.644  1.00 82.18           C  
ANISOU  931  CZ2 TRP A 138     6327  11821  13076   -525   1421    773       C  
ATOM    932  CZ3 TRP A 138      93.152 203.194 292.877  1.00 77.38           C  
ANISOU  932  CZ3 TRP A 138     5756  11265  12380   -655   1440    657       C  
ATOM    933  CH2 TRP A 138      93.491 204.235 292.001  1.00 78.74           C  
ANISOU  933  CH2 TRP A 138     5947  11395  12576   -604   1510    697       C  
ATOM    934  N   LEU A 139      93.182 196.295 291.279  1.00 65.14           N  
ANISOU  934  N   LEU A 139     4120   9918  10713   -733    731    518       N  
ATOM    935  CA  LEU A 139      94.157 195.545 292.058  1.00 61.83           C  
ANISOU  935  CA  LEU A 139     3771   9514  10207   -805    747    460       C  
ATOM    936  C   LEU A 139      95.184 194.859 291.164  1.00 60.44           C  
ANISOU  936  C   LEU A 139     3631   9371   9961   -819    681    402       C  
ATOM    937  O   LEU A 139      96.373 194.824 291.505  1.00 59.01           O  
ANISOU  937  O   LEU A 139     3521   9211   9690   -864    728    351       O  
ATOM    938  CB  LEU A 139      93.444 194.509 292.937  1.00 52.32           C  
ANISOU  938  CB  LEU A 139     2530   8295   9055   -830    707    479       C  
ATOM    939  CG  LEU A 139      94.274 193.376 293.550  1.00 51.78           C  
ANISOU  939  CG  LEU A 139     2506   8239   8929   -888    686    441       C  
ATOM    940  CD1 LEU A 139      93.860 193.143 294.989  1.00 52.24           C  
ANISOU  940  CD1 LEU A 139     2554   8289   9005   -930    739    462       C  
ATOM    941  CD2 LEU A 139      94.125 192.092 292.749  1.00 51.89           C  
ANISOU  941  CD2 LEU A 139     2486   8250   8979   -880    565    435       C  
ATOM    942  N   LEU A 140      94.737 194.306 290.030  1.00 60.48           N  
ANISOU  942  N   LEU A 140     3580   9393  10006   -786    574    402       N  
ATOM    943  CA  LEU A 140      95.637 193.604 289.120  1.00 50.84           C  
ANISOU  943  CA  LEU A 140     2380   8211   8724   -805    514    337       C  
ATOM    944  C   LEU A 140      96.813 194.484 288.737  1.00 93.84           C  
ANISOU  944  C   LEU A 140     7893  13677  14084   -814    591    297       C  
ATOM    945  O   LEU A 140      97.970 194.053 288.787  1.00 94.01           O  
ANISOU  945  O   LEU A 140     7970  13720  14031   -854    607    238       O  
ATOM    946  CB  LEU A 140      94.878 193.166 287.871  1.00 51.55           C  
ANISOU  946  CB  LEU A 140     2384   8339   8864   -774    398    332       C  
ATOM    947  CG  LEU A 140      94.055 191.875 287.865  1.00 78.19           C  
ANISOU  947  CG  LEU A 140     5691  11721  12298   -792    297    330       C  
ATOM    948  CD1 LEU A 140      93.691 191.397 289.256  1.00 52.42           C  
ANISOU  948  CD1 LEU A 140     2441   8401   9075   -817    334    372       C  
ATOM    949  CD2 LEU A 140      92.792 192.098 287.042  1.00 80.12           C  
ANISOU  949  CD2 LEU A 140     5825  12003  12614   -748    212    359       C  
ATOM    950  N   VAL A 141      96.530 195.735 288.368  1.00 50.31           N  
ANISOU  950  N   VAL A 141     2370   8157   8587   -775    646    334       N  
ATOM    951  CA  VAL A 141      97.593 196.698 288.089  1.00 62.06           C  
ANISOU  951  CA  VAL A 141     3923   9659   9999   -790    742    304       C  
ATOM    952  C   VAL A 141      98.546 196.795 289.275  1.00 60.32           C  
ANISOU  952  C   VAL A 141     3781   9440   9697   -855    834    266       C  
ATOM    953  O   VAL A 141      99.774 196.790 289.117  1.00 48.48           O  
ANISOU  953  O   VAL A 141     2337   7977   8106   -898    868    203       O  
ATOM    954  CB  VAL A 141      96.990 198.067 287.733  1.00 50.31           C  
ANISOU  954  CB  VAL A 141     2407   8145   8563   -735    807    376       C  
ATOM    955  CG1 VAL A 141      98.056 199.148 287.807  1.00 53.51           C  
ANISOU  955  CG1 VAL A 141     2891   8552   8888   -768    941    354       C  
ATOM    956  CG2 VAL A 141      96.371 198.015 286.348  1.00 51.21           C  
ANISOU  956  CG2 VAL A 141     2423   8268   8766   -670    711    442       C  
ATOM    957  N   GLY A 142      97.990 196.871 290.484  1.00 59.84           N  
ANISOU  957  N   GLY A 142     3716   9356   9666   -869    872    298       N  
ATOM    958  CA  GLY A 142      98.829 196.856 291.669  1.00 49.11           C  
ANISOU  958  CA  GLY A 142     2412   8024   8224   -939    944    256       C  
ATOM    959  C   GLY A 142      99.712 195.626 291.727  1.00 48.72           C  
ANISOU  959  C   GLY A 142     2382   8000   8128   -972    882    202       C  
ATOM    960  O   GLY A 142     100.924 195.728 291.918  1.00 48.11           O  
ANISOU  960  O   GLY A 142     2363   7958   7959  -1016    926    147       O  
ATOM    961  N   ILE A 143      99.118 194.446 291.541  1.00 48.81           N  
ANISOU  961  N   ILE A 143     2350   7987   8209   -948    780    224       N  
ATOM    962  CA  ILE A 143      99.909 193.218 291.543  1.00 48.50           C  
ANISOU  962  CA  ILE A 143     2321   7959   8146   -970    725    188       C  
ATOM    963  C   ILE A 143     100.950 193.263 290.432  1.00 85.45           C  
ANISOU  963  C   ILE A 143     7027  12677  12765   -972    718    128       C  
ATOM    964  O   ILE A 143     102.127 192.963 290.654  1.00 86.07           O  
ANISOU  964  O   ILE A 143     7162  12765  12776   -998    738     89       O  
ATOM    965  CB  ILE A 143      99.003 191.980 291.425  1.00 49.01           C  
ANISOU  965  CB  ILE A 143     2330   7991   8301   -949    624    228       C  
ATOM    966  CG1 ILE A 143      98.277 191.726 292.745  1.00 49.51           C  
ANISOU  966  CG1 ILE A 143     2375   8024   8413   -965    644    279       C  
ATOM    967  CG2 ILE A 143      99.821 190.763 291.049  1.00 48.81           C  
ANISOU  967  CG2 ILE A 143     2307   7975   8262   -962    568    196       C  
ATOM    968  CD1 ILE A 143      97.566 190.395 292.806  1.00 50.07           C  
ANISOU  968  CD1 ILE A 143     2396   8061   8568   -960    560    318       C  
ATOM    969  N   TRP A 144     100.537 193.666 289.225  1.00 84.57           N  
ANISOU  969  N   TRP A 144     6889  12572  12671   -938    688    128       N  
ATOM    970  CA  TRP A 144     101.474 193.772 288.108  1.00 47.67           C  
ANISOU  970  CA  TRP A 144     2255   7925   7932   -938    685     73       C  
ATOM    971  C   TRP A 144     102.551 194.810 288.384  1.00 47.20           C  
ANISOU  971  C   TRP A 144     2287   7869   7777   -965    791     49       C  
ATOM    972  O   TRP A 144     103.745 194.545 288.207  1.00 55.67           O  
ANISOU  972  O   TRP A 144     3421   8958   8772   -987    802      2       O  
ATOM    973  CB  TRP A 144     100.734 194.131 286.827  1.00 48.05           C  
ANISOU  973  CB  TRP A 144     2242   7991   8025   -902    640     76       C  
ATOM    974  CG  TRP A 144     100.020 193.000 286.218  1.00 48.58           C  
ANISOU  974  CG  TRP A 144     2232   8077   8148   -891    522     68       C  
ATOM    975  CD1 TRP A 144      98.678 192.779 286.232  1.00 49.33           C  
ANISOU  975  CD1 TRP A 144     2255   8159   8331   -861    454    117       C  
ATOM    976  CD2 TRP A 144     100.599 191.919 285.486  1.00 56.18           C  
ANISOU  976  CD2 TRP A 144     3205   9067   9075   -910    458     13       C  
ATOM    977  NE1 TRP A 144      98.382 191.624 285.554  1.00 56.77           N  
ANISOU  977  NE1 TRP A 144     3138   9139   9292   -875    352     80       N  
ATOM    978  CE2 TRP A 144      99.547 191.078 285.085  1.00 56.44           C  
ANISOU  978  CE2 TRP A 144     3148   9123   9175   -906    356     17       C  
ATOM    979  CE3 TRP A 144     101.906 191.580 285.125  1.00 56.29           C  
ANISOU  979  CE3 TRP A 144     3290   9098   9001   -935    480    -37       C  
ATOM    980  CZ2 TRP A 144      99.759 189.919 284.345  1.00 49.66           C  
ANISOU  980  CZ2 TRP A 144     2272   8303   8293   -934    282    -28       C  
ATOM    981  CZ3 TRP A 144     102.112 190.427 284.390  1.00 48.36           C  
ANISOU  981  CZ3 TRP A 144     2262   8135   7977   -954    407    -69       C  
ATOM    982  CH2 TRP A 144     101.044 189.614 284.009  1.00 49.15           C  
ANISOU  982  CH2 TRP A 144     2277   8257   8142   -958    312    -65       C  
ATOM    983  N   GLY A 145     102.140 196.015 288.781  1.00 47.38           N  
ANISOU  983  N   GLY A 145     2313   7885   7803   -965    872     84       N  
ATOM    984  CA  GLY A 145     103.112 197.040 289.119  1.00 47.12           C  
ANISOU  984  CA  GLY A 145     2367   7869   7668  -1003    976     65       C  
ATOM    985  C   GLY A 145     104.040 196.604 290.236  1.00 47.65           C  
ANISOU  985  C   GLY A 145     2493   7953   7660  -1051    993     30       C  
ATOM    986  O   GLY A 145     105.260 196.763 290.146  1.00 46.61           O  
ANISOU  986  O   GLY A 145     2429   7855   7427  -1082   1023    -10       O  
ATOM    987  N   ALA A 146     103.474 196.037 291.301  1.00 47.18           N  
ANISOU  987  N   ALA A 146     2397   7878   7651  -1060    974     47       N  
ATOM    988  CA  ALA A 146     104.278 195.514 292.399  1.00 47.16           C  
ANISOU  988  CA  ALA A 146     2429   7886   7603  -1103    987      8       C  
ATOM    989  C   ALA A 146     104.954 194.200 292.048  1.00 52.26           C  
ANISOU  989  C   ALA A 146     3062   8520   8273  -1088    913    -19       C  
ATOM    990  O   ALA A 146     105.702 193.664 292.870  1.00 50.91           O  
ANISOU  990  O   ALA A 146     2902   8344   8097  -1113    923    -52       O  
ATOM    991  CB  ALA A 146     103.424 195.330 293.655  1.00 51.60           C  
ANISOU  991  CB  ALA A 146     2950   8439   8218  -1121    999     37       C  
ATOM    992  N   SER A 147     104.687 193.661 290.866  1.00 46.82           N  
ANISOU  992  N   SER A 147     2340   7828   7622  -1049    844     -7       N  
ATOM    993  CA  SER A 147     105.444 192.532 290.354  1.00 46.71           C  
ANISOU  993  CA  SER A 147     2318   7822   7607  -1040    785    -30       C  
ATOM    994  C   SER A 147     106.538 192.960 289.391  1.00 55.90           C  
ANISOU  994  C   SER A 147     3540   9023   8676  -1047    811    -77       C  
ATOM    995  O   SER A 147     107.609 192.348 289.376  1.00 46.30           O  
ANISOU  995  O   SER A 147     2339   7832   7422  -1056    803   -105       O  
ATOM    996  CB  SER A 147     104.510 191.539 289.657  1.00 46.99           C  
ANISOU  996  CB  SER A 147     2278   7849   7727  -1010    692      4       C  
ATOM    997  OG  SER A 147     105.230 190.450 289.127  1.00 79.83           O  
ANISOU  997  OG  SER A 147     6425  12027  11879  -1008    643    -12       O  
ATOM    998  N   PHE A 148     106.298 194.012 288.603  1.00 56.13           N  
ANISOU  998  N   PHE A 148     3593   9062   8670  -1042    845    -77       N  
ATOM    999  CA  PHE A 148     107.326 194.545 287.717  1.00 45.96           C  
ANISOU  999  CA  PHE A 148     2363   7825   7276  -1056    880   -104       C  
ATOM   1000  C   PHE A 148     108.518 195.091 288.479  1.00 58.80           C  
ANISOU 1000  C   PHE A 148     4055   9504   8783  -1099    943   -109       C  
ATOM   1001  O   PHE A 148     109.618 195.168 287.921  1.00 45.74           O  
ANISOU 1001  O   PHE A 148     2435   7949   6997  -1109    935    -48       O  
ATOM   1002  CB  PHE A 148     106.750 195.651 286.837  1.00 62.03           C  
ANISOU 1002  CB  PHE A 148     4400   9852   9315  -1044    919    -92       C  
ATOM   1003  CG  PHE A 148     106.123 195.152 285.572  1.00 63.20           C  
ANISOU 1003  CG  PHE A 148     4493   9993   9529  -1011    851   -110       C  
ATOM   1004  CD1 PHE A 148     106.434 193.899 285.082  1.00 46.21           C  
ANISOU 1004  CD1 PHE A 148     2317   7873   7368  -1009    772   -130       C  
ATOM   1005  CD2 PHE A 148     105.225 195.937 284.872  1.00 64.66           C  
ANISOU 1005  CD2 PHE A 148     4638  10152   9779   -986    866    -96       C  
ATOM   1006  CE1 PHE A 148     105.862 193.430 283.921  1.00 46.53           C  
ANISOU 1006  CE1 PHE A 148     2305   7927   7448   -994    705   -156       C  
ATOM   1007  CE2 PHE A 148     104.646 195.476 283.706  1.00 65.86           C  
ANISOU 1007  CE2 PHE A 148     4688  10300  10035   -961    799    -88       C  
ATOM   1008  CZ  PHE A 148     104.966 194.220 283.229  1.00 47.20           C  
ANISOU 1008  CZ  PHE A 148     2309   7970   7655   -972    717   -132       C  
ATOM   1009  N   LEU A 149     108.323 195.481 289.734  1.00 65.01           N  
ANISOU 1009  N   LEU A 149     4076  10897   9727   -846   -323    -15       N  
ATOM   1010  CA  LEU A 149     109.400 196.071 290.511  1.00 65.73           C  
ANISOU 1010  CA  LEU A 149     4160  11094   9721   -925   -317     -7       C  
ATOM   1011  C   LEU A 149     110.229 195.032 291.244  1.00 53.17           C  
ANISOU 1011  C   LEU A 149     2555   9558   8088   -909   -342      5       C  
ATOM   1012  O   LEU A 149     111.438 195.223 291.412  1.00 60.37           O  
ANISOU 1012  O   LEU A 149     3454  10569   8913   -949   -351     17       O  
ATOM   1013  CB  LEU A 149     108.834 197.066 291.525  1.00 65.55           C  
ANISOU 1013  CB  LEU A 149     4142  11076   9688  -1004   -282    -16       C  
ATOM   1014  CG  LEU A 149     108.749 198.530 291.078  1.00 65.54           C  
ANISOU 1014  CG  LEU A 149     4140  11083   9681  -1071   -247    -22       C  
ATOM   1015  CD1 LEU A 149     107.869 198.708 289.834  1.00 64.93           C  
ANISOU 1015  CD1 LEU A 149     4066  10923   9681  -1014   -237    -20       C  
ATOM   1016  CD2 LEU A 149     108.267 199.406 292.227  1.00 53.69           C  
ANISOU 1016  CD2 LEU A 149     2640   9591   8170  -1156   -209    -36       C  
ATOM   1017  N   LEU A 150     109.602 193.941 291.685  1.00 52.92           N  
ANISOU 1017  N   LEU A 150     2519   9475   8115   -852   -349      7       N  
ATOM   1018  CA  LEU A 150     110.273 192.967 292.532  1.00 53.31           C  
ANISOU 1018  CA  LEU A 150     2544   9589   8124   -839   -363     27       C  
ATOM   1019  C   LEU A 150     111.182 192.045 291.727  1.00 53.60           C  
ANISOU 1019  C   LEU A 150     2552   9676   8137   -786   -387     41       C  
ATOM   1020  O   LEU A 150     112.041 191.385 292.317  1.00 54.07           O  
ANISOU 1020  O   LEU A 150     2586   9812   8145   -782   -396     65       O  
ATOM   1021  CB  LEU A 150     109.230 192.182 293.356  1.00 53.06           C  
ANISOU 1021  CB  LEU A 150     2506   9484   8171   -800   -354     27       C  
ATOM   1022  CG  LEU A 150     108.685 192.805 294.664  1.00 53.12           C  
ANISOU 1022  CG  LEU A 150     2524   9499   8160   -857   -330     26       C  
ATOM   1023  CD1 LEU A 150     108.477 194.356 294.531  1.00 58.46           C  
ANISOU 1023  CD1 LEU A 150     3222  10196   8796   -939   -308      8       C  
ATOM   1024  CD2 LEU A 150     107.414 192.073 295.183  1.00 52.74           C  
ANISOU 1024  CD2 LEU A 150     2471   9351   8217   -806   -317     25       C  
ATOM   1025  N   ALA A 151     111.088 192.078 290.393  1.00 53.41           N  
ANISOU 1025  N   ALA A 151     2531   9623   8139   -750   -394     28       N  
ATOM   1026  CA  ALA A 151     112.003 191.369 289.503  1.00 53.72           C  
ANISOU 1026  CA  ALA A 151     2545   9716   8152   -706   -413     38       C  
ATOM   1027  C   ALA A 151     113.098 192.265 288.938  1.00 54.05           C  
ANISOU 1027  C   ALA A 151     2589   9848   8101   -752   -416     47       C  
ATOM   1028  O   ALA A 151     113.885 191.811 288.101  1.00 54.33           O  
ANISOU 1028  O   ALA A 151     2603   9933   8106   -718   -429     56       O  
ATOM   1029  CB  ALA A 151     111.232 190.725 288.348  1.00 53.43           C  
ANISOU 1029  CB  ALA A 151     2501   9601   8198   -632   -422     17       C  
ATOM   1030  N   THR A 152     113.162 193.522 289.372  1.00 69.60           N  
ANISOU 1030  N   THR A 152     4578  11834  10031   -830   -400     45       N  
ATOM   1031  CA  THR A 152     114.165 194.440 288.838  1.00 54.45           C  
ANISOU 1031  CA  THR A 152     2656   9991   8041   -878   -398     54       C  
ATOM   1032  C   THR A 152     115.604 194.044 289.152  1.00 77.04           C  
ANISOU 1032  C   THR A 152     5490  12969  10812   -894   -414     82       C  
ATOM   1033  O   THR A 152     116.466 194.257 288.281  1.00 78.77           O  
ANISOU 1033  O   THR A 152     5696  13246  10987   -893   -420     94       O  
ATOM   1034  CB  THR A 152     113.889 195.864 289.332  1.00 54.44           C  
ANISOU 1034  CB  THR A 152     2674   9971   8039   -964   -373     42       C  
ATOM   1035  OG1 THR A 152     113.413 195.819 290.679  1.00 54.43           O  
ANISOU 1035  OG1 THR A 152     2681   9958   8043   -998   -365     35       O  
ATOM   1036  CG2 THR A 152     112.858 196.538 288.450  1.00 53.97           C  
ANISOU 1036  CG2 THR A 152     2631   9823   8053   -947   -353     26       C  
ATOM   1037  N   PRO A 153     115.950 193.506 290.330  1.00 75.54           N  
ANISOU 1037  N   PRO A 153     5288  12827  10588   -910   -420     98       N  
ATOM   1038  CA  PRO A 153     117.350 193.091 290.530  1.00 75.18           C  
ANISOU 1038  CA  PRO A 153     5210  12901  10454   -919   -435    133       C  
ATOM   1039  C   PRO A 153     117.837 192.096 289.491  1.00 74.31           C  
ANISOU 1039  C   PRO A 153     5075  12804  10354   -840   -447    148       C  
ATOM   1040  O   PRO A 153     119.038 192.058 289.197  1.00 56.69           O  
ANISOU 1040  O   PRO A 153     2820  10668   8052   -849   -456    175       O  
ATOM   1041  CB  PRO A 153     117.338 192.482 291.940  1.00 56.34           C  
ANISOU 1041  CB  PRO A 153     2810  10549   8047   -928   -437    151       C  
ATOM   1042  CG  PRO A 153     116.234 193.176 292.628  1.00 55.94           C  
ANISOU 1042  CG  PRO A 153     2790  10426   8039   -967   -421    121       C  
ATOM   1043  CD  PRO A 153     115.175 193.380 291.579  1.00 55.25           C  
ANISOU 1043  CD  PRO A 153     2727  10219   8045   -927   -411     91       C  
ATOM   1044  N   VAL A 154     116.936 191.308 288.899  1.00 73.21           N  
ANISOU 1044  N   VAL A 154     4938  12573  10305   -765   -448    128       N  
ATOM   1045  CA  VAL A 154     117.361 190.268 287.969  1.00 55.88           C  
ANISOU 1045  CA  VAL A 154     2713  10388   8130   -690   -457    134       C  
ATOM   1046  C   VAL A 154     117.921 190.867 286.683  1.00 85.59           C  
ANISOU 1046  C   VAL A 154     6477  14191  11853   -690   -460    132       C  
ATOM   1047  O   VAL A 154     118.744 190.236 286.010  1.00 86.37           O  
ANISOU 1047  O   VAL A 154     6546  14342  11928   -649   -467    147       O  
ATOM   1048  CB  VAL A 154     116.194 189.302 287.690  1.00 80.25           C  
ANISOU 1048  CB  VAL A 154     5796  13362  11334   -617   -456    106       C  
ATOM   1049  CG1 VAL A 154     116.673 188.082 286.914  1.00 55.77           C  
ANISOU 1049  CG1 VAL A 154     2654  10270   8266   -542   -463    109       C  
ATOM   1050  CG2 VAL A 154     115.536 188.883 289.001  1.00 80.34           C  
ANISOU 1050  CG2 VAL A 154     5807  13329  11390   -622   -449    111       C  
ATOM   1051  N   LEU A 155     117.507 192.078 286.311  1.00 55.70           N  
ANISOU 1051  N   LEU A 155     2720  10382   8063   -733   -451    116       N  
ATOM   1052  CA  LEU A 155     118.110 192.701 285.140  1.00 55.89           C  
ANISOU 1052  CA  LEU A 155     2738  10454   8045   -735   -450    122       C  
ATOM   1053  C   LEU A 155     119.367 193.490 285.475  1.00 56.46           C  
ANISOU 1053  C   LEU A 155     2798  10627   8026   -807   -447    153       C  
ATOM   1054  O   LEU A 155     120.068 193.935 284.560  1.00 72.63           O  
ANISOU 1054  O   LEU A 155     4833  12729  10035   -809   -446    167       O  
ATOM   1055  CB  LEU A 155     117.104 193.606 284.415  1.00 55.45           C  
ANISOU 1055  CB  LEU A 155     2706  10328   8033   -739   -437     98       C  
ATOM   1056  CG  LEU A 155     116.339 194.750 285.085  1.00 55.15           C  
ANISOU 1056  CG  LEU A 155     2697  10233   8024   -805   -417     86       C  
ATOM   1057  CD1 LEU A 155     117.248 195.866 285.576  1.00 93.63           C  
ANISOU 1057  CD1 LEU A 155     7566  15171  12837   -895   -404    103       C  
ATOM   1058  CD2 LEU A 155     115.336 195.303 284.093  1.00 55.10           C  
ANISOU 1058  CD2 LEU A 155     2703  10161   8072   -779   -404     69       C  
ATOM   1059  N   ALA A 156     119.661 193.694 286.753  1.00 82.69           N  
ANISOU 1059  N   ALA A 156     6121  13981  11315   -867   -447    164       N  
ATOM   1060  CA  ALA A 156     120.909 194.346 287.113  1.00 79.45           C  
ANISOU 1060  CA  ALA A 156     5693  13675  10819   -938   -449    192       C  
ATOM   1061  C   ALA A 156     122.040 193.346 287.308  1.00 79.63           C  
ANISOU 1061  C   ALA A 156     5680  13795  10782   -909   -464    231       C  
ATOM   1062  O   ALA A 156     123.211 193.696 287.112  1.00 72.58           O  
ANISOU 1062  O   ALA A 156     4764  12996   9818   -942   -468    261       O  
ATOM   1063  CB  ALA A 156     120.721 195.184 288.381  1.00 72.31           C  
ANISOU 1063  CB  ALA A 156     4802  12772   9899  -1028   -441    179       C  
ATOM   1064  N   PHE A 157     121.708 192.101 287.646  1.00 84.82           N  
ANISOU 1064  N   PHE A 157     6327  14425  11474   -845   -471    235       N  
ATOM   1065  CA  PHE A 157     122.686 191.112 288.068  1.00 58.38           C  
ANISOU 1065  CA  PHE A 157     2938  11162   8080   -819   -480    279       C  
ATOM   1066  C   PHE A 157     122.916 190.006 287.050  1.00 58.41           C  
ANISOU 1066  C   PHE A 157     2916  11157   8122   -727   -481    285       C  
ATOM   1067  O   PHE A 157     123.782 189.160 287.277  1.00 58.97           O  
ANISOU 1067  O   PHE A 157     2948  11296   8163   -699   -484    326       O  
ATOM   1068  CB  PHE A 157     122.263 190.487 289.405  1.00 64.81           C  
ANISOU 1068  CB  PHE A 157     3748  11967   8909   -819   -480    289       C  
ATOM   1069  CG  PHE A 157     122.345 191.429 290.578  1.00 58.64           C  
ANISOU 1069  CG  PHE A 157     2980  11234   8067   -913   -480    290       C  
ATOM   1070  CD1 PHE A 157     121.593 192.589 290.612  1.00 70.01           C  
ANISOU 1070  CD1 PHE A 157     4458  12613   9530   -970   -471    247       C  
ATOM   1071  CD2 PHE A 157     123.162 191.145 291.652  1.00 59.34           C  
ANISOU 1071  CD2 PHE A 157     3039  11433   8076   -944   -487    333       C  
ATOM   1072  CE1 PHE A 157     121.664 193.449 291.684  1.00 70.66           C  
ANISOU 1072  CE1 PHE A 157     4548  12737   9564  -1059   -468    239       C  
ATOM   1073  CE2 PHE A 157     123.236 191.995 292.734  1.00 72.42           C  
ANISOU 1073  CE2 PHE A 157     4702  13143   9672  -1032   -489    326       C  
ATOM   1074  CZ  PHE A 157     122.488 193.151 292.751  1.00 71.46           C  
ANISOU 1074  CZ  PHE A 157     4618  12953   9579  -1092   -479    275       C  
ATOM   1075  N   ARG A 158     122.171 189.976 285.945  1.00 57.94           N  
ANISOU 1075  N   ARG A 158     2871  11017   8125   -680   -478    247       N  
ATOM   1076  CA  ARG A 158     122.335 188.942 284.924  1.00 58.04           C  
ANISOU 1076  CA  ARG A 158     2855  11019   8178   -595   -480    242       C  
ATOM   1077  C   ARG A 158     122.824 189.599 283.641  1.00 87.15           C  
ANISOU 1077  C   ARG A 158     6542  14750  11822   -594   -479    240       C  
ATOM   1078  O   ARG A 158     122.090 190.369 283.011  1.00 86.44           O  
ANISOU 1078  O   ARG A 158     6480  14611  11751   -603   -476    211       O  
ATOM   1079  CB  ARG A 158     121.034 188.171 284.686  1.00 66.61           C  
ANISOU 1079  CB  ARG A 158     3946  11983   9378   -533   -478    196       C  
ATOM   1080  CG  ARG A 158     121.016 186.772 285.315  1.00 57.76           C  
ANISOU 1080  CG  ARG A 158     2788  10835   8323   -481   -474    207       C  
ATOM   1081  CD  ARG A 158     119.611 186.361 285.750  1.00 76.94           C  
ANISOU 1081  CD  ARG A 158     5231  13141  10861   -458   -470    171       C  
ATOM   1082  NE  ARG A 158     119.614 185.289 286.746  1.00 78.14           N  
ANISOU 1082  NE  ARG A 158     5348  13276  11066   -430   -462    193       N  
ATOM   1083  CZ  ARG A 158     119.551 185.487 288.061  1.00 79.45           C  
ANISOU 1083  CZ  ARG A 158     5521  13463  11202   -472   -458    221       C  
ATOM   1084  NH1 ARG A 158     119.481 186.720 288.550  1.00 57.34           N  
ANISOU 1084  NH1 ARG A 158     2764  10698   8326   -548   -463    223       N  
ATOM   1085  NH2 ARG A 158     119.558 184.452 288.893  1.00 57.88           N  
ANISOU 1085  NH2 ARG A 158     2751  10722   8520   -437   -447    246       N  
ATOM   1086  N   LYS A 159     124.062 189.293 283.259  1.00 88.25           N  
ANISOU 1086  N   LYS A 159     6646  14984  11902   -580   -480    277       N  
ATOM   1087  CA  LYS A 159     124.674 189.843 282.059  1.00 87.64           C  
ANISOU 1087  CA  LYS A 159     6561  14963  11777   -574   -478    285       C  
ATOM   1088  C   LYS A 159     125.504 188.749 281.397  1.00 89.49           C  
ANISOU 1088  C   LYS A 159     6749  15249  12005   -504   -477    303       C  
ATOM   1089  O   LYS A 159     125.931 187.793 282.048  1.00 89.09           O  
ANISOU 1089  O   LYS A 159     6669  15215  11968   -481   -477    326       O  
ATOM   1090  CB  LYS A 159     125.538 191.077 282.386  1.00 84.86           C  
ANISOU 1090  CB  LYS A 159     6212  14692  11339   -661   -477    323       C  
ATOM   1091  CG  LYS A 159     124.767 192.249 283.008  1.00 79.54           C  
ANISOU 1091  CG  LYS A 159     5577  13966  10680   -735   -472    301       C  
ATOM   1092  CD  LYS A 159     125.683 193.398 283.419  1.00 78.23           C  
ANISOU 1092  CD  LYS A 159     5404  13877  10444   -827   -469    332       C  
ATOM   1093  CE  LYS A 159     126.552 193.047 284.628  1.00 78.03           C  
ANISOU 1093  CE  LYS A 159     5356  13931  10360   -868   -479    367       C  
ATOM   1094  NZ  LYS A 159     127.814 192.334 284.271  1.00 81.29           N  
ANISOU 1094  NZ  LYS A 159     5726  14445  10717   -833   -485    417       N  
ATOM   1095  N   VAL A 160     125.712 188.884 280.083  1.00 90.15           N  
ANISOU 1095  N   VAL A 160     6822  15358  12071   -467   -474    293       N  
ATOM   1096  CA  VAL A 160     126.510 187.908 279.345  1.00 60.11           C  
ANISOU 1096  CA  VAL A 160     2971  11606   8261   -400   -470    305       C  
ATOM   1097  C   VAL A 160     127.986 188.183 279.579  1.00 60.77           C  
ANISOU 1097  C   VAL A 160     3028  11809   8254   -435   -469    372       C  
ATOM   1098  O   VAL A 160     128.437 189.336 279.575  1.00 60.88           O  
ANISOU 1098  O   VAL A 160     3054  11876   8200   -498   -469    400       O  
ATOM   1099  CB  VAL A 160     126.174 187.927 277.843  1.00 60.06           C  
ANISOU 1099  CB  VAL A 160     2962  11597   8262   -344   -468    268       C  
ATOM   1100  CG1 VAL A 160     126.522 189.272 277.222  1.00 77.50           C  
ANISOU 1100  CG1 VAL A 160     5186  13868  10394   -388   -464    293       C  
ATOM   1101  CG2 VAL A 160     126.923 186.814 277.127  1.00 60.65           C  
ANISOU 1101  CG2 VAL A 160     2984  11717   8342   -271   -461    271       C  
ATOM   1102  N   VAL A 161     128.747 187.117 279.797  1.00 61.29           N  
ANISOU 1102  N   VAL A 161     3050  11914   8324   -394   -464    401       N  
ATOM   1103  CA  VAL A 161     130.191 187.198 279.963  1.00 74.56           C  
ANISOU 1103  CA  VAL A 161     4696  13713   9920   -416   -462    470       C  
ATOM   1104  C   VAL A 161     130.830 186.293 278.922  1.00 75.05           C  
ANISOU 1104  C   VAL A 161     4711  13813   9991   -335   -451    474       C  
ATOM   1105  O   VAL A 161     130.418 185.139 278.755  1.00 75.20           O  
ANISOU 1105  O   VAL A 161     4707  13772  10095   -266   -443    441       O  
ATOM   1106  CB  VAL A 161     130.627 186.808 281.389  1.00 74.16           C  
ANISOU 1106  CB  VAL A 161     4630  13695   9854   -449   -465    517       C  
ATOM   1107  CG1 VAL A 161     130.213 187.892 282.389  1.00 62.02           C  
ANISOU 1107  CG1 VAL A 161     3134  12148   8284   -541   -476    515       C  
ATOM   1108  CG2 VAL A 161     130.031 185.471 281.785  1.00 73.81           C  
ANISOU 1108  CG2 VAL A 161     4564  13572   9907   -384   -458    494       C  
ATOM   1109  N   LYS A 162     131.815 186.825 278.207  1.00 75.84           N  
ANISOU 1109  N   LYS A 162     4794  14009  10013   -344   -447    513       N  
ATOM   1110  CA  LYS A 162     132.493 186.061 277.168  1.00 75.94           C  
ANISOU 1110  CA  LYS A 162     4761  14069  10024   -269   -435    519       C  
ATOM   1111  C   LYS A 162     133.441 185.065 277.824  1.00 75.34           C  
ANISOU 1111  C   LYS A 162     4635  14042   9950   -245   -426    573       C  
ATOM   1112  O   LYS A 162     134.422 185.458 278.463  1.00 64.60           O  
ANISOU 1112  O   LYS A 162     3261  12771   8513   -296   -429    644       O  
ATOM   1113  CB  LYS A 162     133.232 187.005 276.224  1.00 76.70           C  
ANISOU 1113  CB  LYS A 162     4853  14255  10033   -286   -431    551       C  
ATOM   1114  CG  LYS A 162     132.517 188.340 276.026  1.00 75.41           C  
ANISOU 1114  CG  LYS A 162     4737  14063   9851   -343   -438    530       C  
ATOM   1115  CD  LYS A 162     132.466 188.760 274.564  1.00 74.47           C  
ANISOU 1115  CD  LYS A 162     4614  13976   9705   -303   -429    515       C  
ATOM   1116  CE  LYS A 162     131.634 190.027 274.394  1.00 62.82           C  
ANISOU 1116  CE  LYS A 162     3181  12461   8228   -353   -432    496       C  
ATOM   1117  NZ  LYS A 162     131.471 190.404 272.963  1.00 62.93           N  
ANISOU 1117  NZ  LYS A 162     3187  12509   8215   -307   -422    485       N  
ATOM   1118  N   LEU A 163     133.141 183.775 277.682  1.00 75.09           N  
ANISOU 1118  N   LEU A 163     4569  13950  10010   -169   -413    540       N  
ATOM   1119  CA  LEU A 163     133.915 182.711 278.311  1.00 76.64           C  
ANISOU 1119  CA  LEU A 163     4711  14178  10232   -136   -399    590       C  
ATOM   1120  C   LEU A 163     135.045 182.223 277.408  1.00 79.19           C  
ANISOU 1120  C   LEU A 163     4979  14583  10526    -81   -381    623       C  
ATOM   1121  O   LEU A 163     136.204 182.172 277.830  1.00 79.61           O  
ANISOU 1121  O   LEU A 163     5000  14734  10515    -96   -376    705       O  
ATOM   1122  CB  LEU A 163     132.990 181.544 278.678  1.00 64.72           C  
ANISOU 1122  CB  LEU A 163     3183  12548   8858    -82   -388    539       C  
ATOM   1123  CG  LEU A 163     133.536 180.476 279.624  1.00 65.33           C  
ANISOU 1123  CG  LEU A 163     3206  12636   8980    -54   -370    594       C  
ATOM   1124  CD1 LEU A 163     133.227 180.853 281.062  1.00 71.76           C  
ANISOU 1124  CD1 LEU A 163     4050  13448   9766   -118   -383    630       C  
ATOM   1125  CD2 LEU A 163     132.983 179.097 279.287  1.00 65.49           C  
ANISOU 1125  CD2 LEU A 163     3178  12550   9156     34   -344    537       C  
ATOM   1126  N   THR A 164     134.710 181.863 276.167  1.00 80.91           N  
ANISOU 1126  N   THR A 164     5185  14769  10789    -17   -371    560       N  
ATOM   1127  CA  THR A 164     135.652 181.404 275.156  1.00 66.38           C  
ANISOU 1127  CA  THR A 164     3293  13001   8927     43   -352    577       C  
ATOM   1128  C   THR A 164     135.409 182.199 273.878  1.00 83.92           C  
ANISOU 1128  C   THR A 164     5541  15252  11094     49   -358    537       C  
ATOM   1129  O   THR A 164     134.331 182.768 273.681  1.00 83.60           O  
ANISOU 1129  O   THR A 164     5548  15150  11067     27   -373    481       O  
ATOM   1130  CB  THR A 164     135.494 179.889 274.895  1.00 66.79           C  
ANISOU 1130  CB  THR A 164     3285  12984   9108    133   -325    532       C  
ATOM   1131  OG1 THR A 164     135.557 179.177 276.136  1.00 66.97           O  
ANISOU 1131  OG1 THR A 164     3283  12969   9192    130   -316    570       O  
ATOM   1132  CG2 THR A 164     136.580 179.356 273.972  1.00 67.65           C  
ANISOU 1132  CG2 THR A 164     3333  13174   9197    196   -299    555       C  
ATOM   1133  N   ASN A 165     136.431 182.250 273.016  1.00 66.80           N  
ANISOU 1133  N   ASN A 165     3338  13184   8860     78   -345    573       N  
ATOM   1134  CA  ASN A 165     136.307 182.931 271.728  1.00 66.76           C  
ANISOU 1134  CA  ASN A 165     3346  13224   8795     95   -346    544       C  
ATOM   1135  C   ASN A 165     135.031 182.533 271.000  1.00 66.36           C  
ANISOU 1135  C   ASN A 165     3308  13086   8819    143   -348    439       C  
ATOM   1136  O   ASN A 165     134.357 183.378 270.402  1.00 74.80           O  
ANISOU 1136  O   ASN A 165     4417  14156   9849    127   -360    408       O  
ATOM   1137  CB  ASN A 165     137.522 182.623 270.851  1.00 82.42           C  
ANISOU 1137  CB  ASN A 165     5275  15315  10725    146   -325    586       C  
ATOM   1138  CG  ASN A 165     138.497 183.785 270.761  1.00 82.84           C  
ANISOU 1138  CG  ASN A 165     5336  15483  10656     90   -330    675       C  
ATOM   1139  OD1 ASN A 165     138.753 184.486 271.741  1.00 84.52           O  
ANISOU 1139  OD1 ASN A 165     5573  15708  10832     10   -344    731       O  
ATOM   1140  ND2 ASN A 165     139.044 183.993 269.572  1.00 81.20           N  
ANISOU 1140  ND2 ASN A 165     5104  15360  10388    131   -317    686       N  
ATOM   1141  N   GLU A 166     134.678 181.251 271.047  1.00 66.54           N  
ANISOU 1141  N   GLU A 166     3293  13035   8956    204   -335    386       N  
ATOM   1142  CA  GLU A 166     133.504 180.745 270.352  1.00 80.93           C  
ANISOU 1142  CA  GLU A 166     5116  14775  10858    252   -335    285       C  
ATOM   1143  C   GLU A 166     132.354 180.415 271.293  1.00 81.06           C  
ANISOU 1143  C   GLU A 166     5158  14659  10982    229   -346    244       C  
ATOM   1144  O   GLU A 166     131.358 179.830 270.856  1.00 83.07           O  
ANISOU 1144  O   GLU A 166     5405  14833  11323    268   -345    163       O  
ATOM   1145  CB  GLU A 166     133.876 179.513 269.525  1.00 67.11           C  
ANISOU 1145  CB  GLU A 166     3293  13032   9173    342   -306    242       C  
ATOM   1146  CG  GLU A 166     134.998 179.768 268.541  1.00 87.78           C  
ANISOU 1146  CG  GLU A 166     5881  15784  11686    373   -293    279       C  
ATOM   1147  CD  GLU A 166     134.669 180.863 267.538  1.00 88.72           C  
ANISOU 1147  CD  GLU A 166     6040  15975  11694    362   -308    263       C  
ATOM   1148  OE1 GLU A 166     133.472 181.106 267.274  1.00 67.05           O  
ANISOU 1148  OE1 GLU A 166     3331  13174   8972    357   -325    195       O  
ATOM   1149  OE2 GLU A 166     135.616 181.485 267.010  1.00 89.89           O  
ANISOU 1149  OE2 GLU A 166     6181  16239  11735    359   -303    323       O  
ATOM   1150  N   THR A 167     132.457 180.782 272.568  1.00 79.09           N  
ANISOU 1150  N   THR A 167     4936  14390  10725    166   -356    300       N  
ATOM   1151  CA  THR A 167     131.406 180.464 273.532  1.00 64.78           C  
ANISOU 1151  CA  THR A 167     3145  12456   9011    145   -364    270       C  
ATOM   1152  C   THR A 167     131.342 181.576 274.565  1.00 64.23           C  
ANISOU 1152  C   THR A 167     3134  12400   8869     56   -385    322       C  
ATOM   1153  O   THR A 167     132.283 181.759 275.340  1.00 64.52           O  
ANISOU 1153  O   THR A 167     3162  12503   8851     20   -383    398       O  
ATOM   1154  CB  THR A 167     131.660 179.118 274.203  1.00 65.25           C  
ANISOU 1154  CB  THR A 167     3145  12459   9189    189   -340    277       C  
ATOM   1155  OG1 THR A 167     131.381 178.059 273.280  1.00 66.58           O  
ANISOU 1155  OG1 THR A 167     3259  12578   9461    268   -319    208       O  
ATOM   1156  CG2 THR A 167     130.773 178.963 275.423  1.00 64.72           C  
ANISOU 1156  CG2 THR A 167     3101  12288   9201    155   -348    272       C  
ATOM   1157  N   ASP A 168     130.241 182.315 274.575  1.00 63.50           N  
ANISOU 1157  N   ASP A 168     3097  12252   8778     21   -403    282       N  
ATOM   1158  CA  ASP A 168     129.943 183.255 275.646  1.00 62.96           C  
ANISOU 1158  CA  ASP A 168     3081  12169   8672    -61   -419    314       C  
ATOM   1159  C   ASP A 168     128.700 182.761 276.371  1.00 62.43           C  
ANISOU 1159  C   ASP A 168     3031  11974   8715    -59   -423    267       C  
ATOM   1160  O   ASP A 168     127.644 182.580 275.754  1.00 62.09           O  
ANISOU 1160  O   ASP A 168     2999  11858   8735    -29   -427    200       O  
ATOM   1161  CB  ASP A 168     129.747 184.678 275.115  1.00 62.60           C  
ANISOU 1161  CB  ASP A 168     3083  12165   8537   -110   -430    318       C  
ATOM   1162  CG  ASP A 168     129.401 184.714 273.643  1.00 77.94           C  
ANISOU 1162  CG  ASP A 168     5020  14124  10470    -57   -427    268       C  
ATOM   1163  OD1 ASP A 168     128.880 183.707 273.124  1.00 79.88           O  
ANISOU 1163  OD1 ASP A 168     5238  14319  10794      9   -422    209       O  
ATOM   1164  OD2 ASP A 168     129.652 185.756 272.999  1.00 75.94           O  
ANISOU 1164  OD2 ASP A 168     4783  13939  10130    -81   -429    290       O  
ATOM   1165  N   LEU A 169     128.837 182.516 277.666  1.00 68.46           N  
ANISOU 1165  N   LEU A 169     3793  12719   9501    -90   -422    306       N  
ATOM   1166  CA  LEU A 169     127.730 182.054 278.484  1.00 61.98           C  
ANISOU 1166  CA  LEU A 169     2984  11782   8782    -90   -424    273       C  
ATOM   1167  C   LEU A 169     127.068 183.235 279.176  1.00 72.66           C  
ANISOU 1167  C   LEU A 169     4402  13117  10087   -167   -441    277       C  
ATOM   1168  O   LEU A 169     127.635 184.326 279.281  1.00 69.56           O  
ANISOU 1168  O   LEU A 169     4037  12805   9588   -227   -449    316       O  
ATOM   1169  CB  LEU A 169     128.200 181.031 279.523  1.00 62.44           C  
ANISOU 1169  CB  LEU A 169     2995  11832   8898    -70   -408    314       C  
ATOM   1170  CG  LEU A 169     128.717 179.694 278.983  1.00 63.16           C  
ANISOU 1170  CG  LEU A 169     3010  11913   9075     12   -382    306       C  
ATOM   1171  CD1 LEU A 169     128.638 178.608 280.044  1.00 63.48           C  
ANISOU 1171  CD1 LEU A 169     3005  11894   9220     39   -361    327       C  
ATOM   1172  CD2 LEU A 169     127.949 179.286 277.737  1.00 68.28           C  
ANISOU 1172  CD2 LEU A 169     3649  12491   9805     67   -379    222       C  
ATOM   1173  N   CYS A 170     125.847 183.005 279.641  1.00 77.13           N  
ANISOU 1173  N   CYS A 170     4989  13574  10743   -165   -445    235       N  
ATOM   1174  CA  CYS A 170     125.114 184.004 280.396  1.00 83.61           C  
ANISOU 1174  CA  CYS A 170     5868  14363  11538   -233   -457    234       C  
ATOM   1175  C   CYS A 170     124.558 183.391 281.671  1.00 83.77           C  
ANISOU 1175  C   CYS A 170     5883  14313  11633   -237   -453    240       C  
ATOM   1176  O   CYS A 170     123.897 182.348 281.626  1.00 84.00           O  
ANISOU 1176  O   CYS A 170     5884  14251  11783   -181   -444    205       O  
ATOM   1177  CB  CYS A 170     123.966 184.595 279.592  1.00 90.12           C  
ANISOU 1177  CB  CYS A 170     6732  15124  12386   -231   -466    177       C  
ATOM   1178  SG  CYS A 170     122.709 185.191 280.722  1.00 91.89           S  
ANISOU 1178  SG  CYS A 170     7009  15256  12650   -285   -473    163       S  
ATOM   1179  N   LEU A 171     124.823 184.046 282.796  1.00 59.98           N  
ANISOU 1179  N   LEU A 171     2893  11344   8551   -303   -458    284       N  
ATOM   1180  CA  LEU A 171     124.172 183.755 284.067  1.00 79.27           C  
ANISOU 1180  CA  LEU A 171     5343  13732  11045   -319   -455    290       C  
ATOM   1181  C   LEU A 171     124.455 184.938 284.983  1.00 79.03           C  
ANISOU 1181  C   LEU A 171     5351  13771  10907   -408   -465    326       C  
ATOM   1182  O   LEU A 171     125.149 185.888 284.606  1.00 59.82           O  
ANISOU 1182  O   LEU A 171     2933  11417   8379   -454   -472    344       O  
ATOM   1183  CB  LEU A 171     124.647 182.424 284.679  1.00 78.62           C  
ANISOU 1183  CB  LEU A 171     5198  13653  11020   -268   -438    325       C  
ATOM   1184  CG  LEU A 171     123.836 181.788 285.829  1.00 75.96           C  
ANISOU 1184  CG  LEU A 171     4852  13240  10769   -258   -428    326       C  
ATOM   1185  CD1 LEU A 171     122.340 181.760 285.520  1.00 59.56           C  
ANISOU 1185  CD1 LEU A 171     2802  11024   8803   -241   -430    255       C  
ATOM   1186  CD2 LEU A 171     124.337 180.389 286.196  1.00 74.70           C  
ANISOU 1186  CD2 LEU A 171     4619  13080  10684   -194   -403    359       C  
ATOM   1187  N   ALA A 172     123.891 184.875 286.187  1.00 77.37           N  
ANISOU 1187  N   ALA A 172     5151  13528  10718   -433   -463    334       N  
ATOM   1188  CA  ALA A 172     124.035 185.946 287.162  1.00 74.99           C  
ANISOU 1188  CA  ALA A 172     4881  13285  10325   -519   -471    358       C  
ATOM   1189  C   ALA A 172     125.499 186.192 287.507  1.00 72.91           C  
ANISOU 1189  C   ALA A 172     4591  13167   9944   -559   -476    424       C  
ATOM   1190  O   ALA A 172     126.243 185.259 287.826  1.00 72.71           O  
ANISOU 1190  O   ALA A 172     4517  13198   9913   -522   -469    473       O  
ATOM   1191  CB  ALA A 172     123.247 185.593 288.423  1.00 59.34           C  
ANISOU 1191  CB  ALA A 172     2903  11256   8389   -525   -466    361       C  
ATOM   1192  N   VAL A 173     125.909 187.456 287.435  1.00 71.16           N  
ANISOU 1192  N   VAL A 173     4396  13005   9637   -634   -485    426       N  
ATOM   1193  CA  VAL A 173     127.234 187.885 287.866  1.00 61.04           C  
ANISOU 1193  CA  VAL A 173     3090  11862   8240   -689   -491    484       C  
ATOM   1194  C   VAL A 173     127.038 188.668 289.160  1.00 76.18           C  
ANISOU 1194  C   VAL A 173     5028  13812  10105   -774   -498    488       C  
ATOM   1195  O   VAL A 173     126.669 189.847 289.145  1.00 76.12           O  
ANISOU 1195  O   VAL A 173     5058  13783  10083   -841   -501    452       O  
ATOM   1196  CB  VAL A 173     127.949 188.712 286.790  1.00 61.18           C  
ANISOU 1196  CB  VAL A 173     3111  11927   8207   -713   -494    484       C  
ATOM   1197  CG1 VAL A 173     128.519 187.802 285.717  1.00 61.43           C  
ANISOU 1197  CG1 VAL A 173     3107  11973   8261   -631   -488    500       C  
ATOM   1198  CG2 VAL A 173     127.004 189.729 286.163  1.00 60.48           C  
ANISOU 1198  CG2 VAL A 173     3071  11752   8156   -739   -492    425       C  
ATOM   1199  N   TYR A 174     127.254 188.012 290.290  1.00 61.55           N  
ANISOU 1199  N   TYR A 174     3147  12013   8228   -772   -498    531       N  
ATOM   1200  CA  TYR A 174     127.091 188.683 291.565  1.00 61.73           C  
ANISOU 1200  CA  TYR A 174     3182  12082   8191   -850   -505    534       C  
ATOM   1201  C   TYR A 174     128.449 189.170 292.036  1.00 74.38           C  
ANISOU 1201  C   TYR A 174     4752  13842   9667   -918   -517    585       C  
ATOM   1202  O   TYR A 174     129.364 188.346 292.188  1.00 74.77           O  
ANISOU 1202  O   TYR A 174     4753  13982   9675   -882   -518    652       O  
ATOM   1203  CB  TYR A 174     126.474 187.743 292.593  1.00 73.10           C  
ANISOU 1203  CB  TYR A 174     4606  13498   9669   -811   -498    554       C  
ATOM   1204  CG  TYR A 174     125.044 187.308 292.306  1.00 73.89           C  
ANISOU 1204  CG  TYR A 174     4735  13440   9900   -754   -486    500       C  
ATOM   1205  CD1 TYR A 174     124.001 188.221 292.307  1.00 60.17           C  
ANISOU 1205  CD1 TYR A 174     3049  11615   8197   -796   -486    438       C  
ATOM   1206  CD2 TYR A 174     124.739 185.975 292.074  1.00 76.75           C  
ANISOU 1206  CD2 TYR A 174     5066  13738  10356   -661   -473    512       C  
ATOM   1207  CE1 TYR A 174     122.693 187.826 292.060  1.00 59.43           C  
ANISOU 1207  CE1 TYR A 174     2978  11382   8219   -745   -476    393       C  
ATOM   1208  CE2 TYR A 174     123.441 185.567 291.838  1.00 79.93           C  
ANISOU 1208  CE2 TYR A 174     5489  13997  10882   -613   -463    460       C  
ATOM   1209  CZ  TYR A 174     122.419 186.494 291.826  1.00 81.97           C  
ANISOU 1209  CZ  TYR A 174     5802  14178  11165   -655   -466    403       C  
ATOM   1210  OH  TYR A 174     121.127 186.077 291.582  1.00 58.75           O  
ANISOU 1210  OH  TYR A 174     2877  11099   8347   -608   -457    356       O  
ATOM   1211  N   PRO A 175     128.641 190.479 292.251  1.00 62.81           N  
ANISOU 1211  N   PRO A 175     3307  12414   8144  -1015   -526    557       N  
ATOM   1212  CA  PRO A 175     129.982 190.975 292.627  1.00 65.33           C  
ANISOU 1212  CA  PRO A 175     3590  12885   8347  -1085   -539    601       C  
ATOM   1213  C   PRO A 175     130.617 190.262 293.811  1.00 64.66           C  
ANISOU 1213  C   PRO A 175     3458  12929   8182  -1087   -546    669       C  
ATOM   1214  O   PRO A 175     131.797 189.896 293.744  1.00 65.46           O  
ANISOU 1214  O   PRO A 175     3511  13145   8214  -1080   -552    735       O  
ATOM   1215  CB  PRO A 175     129.730 192.465 292.920  1.00 63.78           C  
ANISOU 1215  CB  PRO A 175     3424  12678   8131  -1194   -542    541       C  
ATOM   1216  CG  PRO A 175     128.231 192.652 292.903  1.00 62.79           C  
ANISOU 1216  CG  PRO A 175     3350  12406   8103  -1177   -530    478       C  
ATOM   1217  CD  PRO A 175     127.699 191.582 292.009  1.00 62.14           C  
ANISOU 1217  CD  PRO A 175     3273  12229   8107  -1064   -521    484       C  
ATOM   1218  N   SER A 176     129.875 190.063 294.897  1.00 64.58           N  
ANISOU 1218  N   SER A 176     3454  12908   8174  -1095   -545    661       N  
ATOM   1219  CA  SER A 176     130.347 189.308 296.048  1.00 65.40           C  
ANISOU 1219  CA  SER A 176     3510  13133   8205  -1085   -549    733       C  
ATOM   1220  C   SER A 176     129.334 188.217 296.366  1.00 64.89           C  
ANISOU 1220  C   SER A 176     3447  12977   8230   -998   -533    743       C  
ATOM   1221  O   SER A 176     128.236 188.181 295.808  1.00 67.45           O  
ANISOU 1221  O   SER A 176     3814  13149   8666   -960   -522    684       O  
ATOM   1222  CB  SER A 176     130.570 190.215 297.268  1.00 74.89           C  
ANISOU 1222  CB  SER A 176     4705  14450   9300  -1194   -564    719       C  
ATOM   1223  OG  SER A 176     131.200 189.511 298.326  1.00 76.08           O  
ANISOU 1223  OG  SER A 176     4800  14749   9359  -1186   -570    800       O  
ATOM   1224  N   ASP A 177     129.714 187.316 297.275  1.00 85.16           N  
ANISOU 1224  N   ASP A 177     5964  15641  10752   -965   -530    822       N  
ATOM   1225  CA  ASP A 177     128.827 186.220 297.651  1.00 84.10           C  
ANISOU 1225  CA  ASP A 177     5820  15425  10708   -880   -510    843       C  
ATOM   1226  C   ASP A 177     127.733 186.661 298.609  1.00 64.94           C  
ANISOU 1226  C   ASP A 177     3424  12960   8289   -918   -509    799       C  
ATOM   1227  O   ASP A 177     126.646 186.071 298.612  1.00 64.29           O  
ANISOU 1227  O   ASP A 177     3357  12752   8317   -858   -492    779       O  
ATOM   1228  CB  ASP A 177     129.629 185.082 298.270  1.00 83.26           C  
ANISOU 1228  CB  ASP A 177     5642  15437  10557   -825   -501    955       C  
ATOM   1229  CG  ASP A 177     130.459 184.353 297.249  1.00 82.02           C  
ANISOU 1229  CG  ASP A 177     5452  15278  10434   -759   -492    997       C  
ATOM   1230  OD1 ASP A 177     130.035 184.323 296.072  1.00 79.41           O  
ANISOU 1230  OD1 ASP A 177     5153  14814  10205   -723   -486    935       O  
ATOM   1231  OD2 ASP A 177     131.530 183.822 297.616  1.00 82.86           O  
ANISOU 1231  OD2 ASP A 177     5499  15520  10464   -744   -491   1092       O  
ATOM   1232  N   ARG A 178     128.005 187.669 299.439  1.00 65.41           N  
ANISOU 1232  N   ARG A 178     3489  13127   8237  -1018   -526    783       N  
ATOM   1233  CA  ARG A 178     126.935 188.276 300.222  1.00 65.01           C  
ANISOU 1233  CA  ARG A 178     3474  13030   8198  -1064   -524    724       C  
ATOM   1234  C   ARG A 178     125.864 188.858 299.308  1.00 91.33           C  
ANISOU 1234  C   ARG A 178     6872  16179  11649  -1062   -516    632       C  
ATOM   1235  O   ARG A 178     124.664 188.736 299.586  1.00 92.23           O  
ANISOU 1235  O   ARG A 178     7014  16186  11843  -1038   -503    599       O  
ATOM   1236  CB  ARG A 178     127.505 189.351 301.146  1.00 65.83           C  
ANISOU 1236  CB  ARG A 178     3569  13282   8163  -1181   -543    707       C  
ATOM   1237  CG  ARG A 178     128.278 188.801 302.326  1.00 67.11           C  
ANISOU 1237  CG  ARG A 178     3662  13644   8192  -1188   -550    798       C  
ATOM   1238  CD  ARG A 178     127.426 187.826 303.116  1.00 75.40           C  
ANISOU 1238  CD  ARG A 178     4694  14672   9284  -1114   -532    845       C  
ATOM   1239  NE  ARG A 178     127.712 187.861 304.547  1.00 76.62           N  
ANISOU 1239  NE  ARG A 178     4795  15034   9284  -1163   -539    899       N  
ATOM   1240  CZ  ARG A 178     127.157 188.723 305.395  1.00 76.74           C  
ANISOU 1240  CZ  ARG A 178     4820  15115   9224  -1248   -544    844       C  
ATOM   1241  NH1 ARG A 178     126.290 189.628 304.956  1.00 75.53           N  
ANISOU 1241  NH1 ARG A 178     4729  14827   9142  -1293   -541    737       N  
ATOM   1242  NH2 ARG A 178     127.467 188.682 306.681  1.00 69.79           N  
ANISOU 1242  NH2 ARG A 178     3882  14441   8193  -1287   -551    895       N  
ATOM   1243  N   HIS A 179     126.285 189.492 298.208  1.00 88.43           N  
ANISOU 1243  N   HIS A 179     6527  15778  11293  -1086   -522    597       N  
ATOM   1244  CA  HIS A 179     125.339 189.936 297.189  1.00 85.47           C  
ANISOU 1244  CA  HIS A 179     6207  15236  11030  -1070   -513    524       C  
ATOM   1245  C   HIS A 179     124.524 188.760 296.658  1.00 61.84           C  
ANISOU 1245  C   HIS A 179     3216  12117   8163   -959   -498    531       C  
ATOM   1246  O   HIS A 179     123.290 188.817 296.600  1.00 61.06           O  
ANISOU 1246  O   HIS A 179     3153  11891   8157   -940   -487    482       O  
ATOM   1247  CB  HIS A 179     126.086 190.636 296.049  1.00 62.51           C  
ANISOU 1247  CB  HIS A 179     3309  12335   8108  -1100   -520    505       C  
ATOM   1248  CG  HIS A 179     126.529 192.032 296.372  1.00 62.94           C  
ANISOU 1248  CG  HIS A 179     3374  12455   8086  -1216   -529    468       C  
ATOM   1249  ND1 HIS A 179     127.538 192.306 297.271  1.00 64.01           N  
ANISOU 1249  ND1 HIS A 179     3470  12753   8098  -1286   -544    500       N  
ATOM   1250  CD2 HIS A 179     126.109 193.231 295.903  1.00 62.54           C  
ANISOU 1250  CD2 HIS A 179     3361  12329   8071  -1277   -524    401       C  
ATOM   1251  CE1 HIS A 179     127.713 193.613 297.349  1.00 74.95           C  
ANISOU 1251  CE1 HIS A 179     4870  14155   9453  -1389   -547    445       C  
ATOM   1252  NE2 HIS A 179     126.858 194.198 296.529  1.00 73.85           N  
ANISOU 1252  NE2 HIS A 179     4777  13869   9413  -1384   -533    387       N  
ATOM   1253  N   LYS A 180     125.205 187.676 296.279  1.00 62.21           N  
ANISOU 1253  N   LYS A 180     3220  12198   8220   -887   -495    589       N  
ATOM   1254  CA  LYS A 180     124.507 186.487 295.800  1.00 61.76           C  
ANISOU 1254  CA  LYS A 180     3152  12022   8291   -784   -477    590       C  
ATOM   1255  C   LYS A 180     123.591 185.915 296.873  1.00 79.31           C  
ANISOU 1255  C   LYS A 180     5366  14209  10558   -758   -464    603       C  
ATOM   1256  O   LYS A 180     122.443 185.555 296.587  1.00 79.83           O  
ANISOU 1256  O   LYS A 180     5453  14134  10746   -710   -451    560       O  
ATOM   1257  CB  LYS A 180     125.517 185.434 295.343  1.00 62.37           C  
ANISOU 1257  CB  LYS A 180     3174  12156   8367   -718   -472    654       C  
ATOM   1258  CG  LYS A 180     124.908 184.077 295.027  1.00 62.15           C  
ANISOU 1258  CG  LYS A 180     3120  12019   8477   -614   -450    659       C  
ATOM   1259  CD  LYS A 180     125.790 183.269 294.084  1.00 70.50           C  
ANISOU 1259  CD  LYS A 180     4134  13092   9560   -551   -442    688       C  
ATOM   1260  CE  LYS A 180     125.082 181.995 293.634  1.00 70.58           C  
ANISOU 1260  CE  LYS A 180     4117  12971   9731   -452   -417    667       C  
ATOM   1261  NZ  LYS A 180     125.568 181.473 292.319  1.00 71.17           N  
ANISOU 1261  NZ  LYS A 180     4169  13009   9862   -397   -411    648       N  
ATOM   1262  N   ALA A 181     124.079 185.830 298.114  1.00 79.27           N  
ANISOU 1262  N   ALA A 181     5327  14337  10455   -788   -467    664       N  
ATOM   1263  CA  ALA A 181     123.314 185.196 299.185  1.00 78.58           C  
ANISOU 1263  CA  ALA A 181     5222  14235  10401   -755   -451    693       C  
ATOM   1264  C   ALA A 181     121.943 185.835 299.337  1.00 77.56           C  
ANISOU 1264  C   ALA A 181     5147  13985  10339   -780   -446    617       C  
ATOM   1265  O   ALA A 181     120.910 185.179 299.154  1.00 76.70           O  
ANISOU 1265  O   ALA A 181     5042  13742  10357   -716   -428    596       O  
ATOM   1266  CB  ALA A 181     124.082 185.281 300.504  1.00 63.62           C  
ANISOU 1266  CB  ALA A 181     3285  12526   8360   -801   -459    766       C  
ATOM   1267  N   PHE A 182     121.918 187.127 299.667  1.00 61.63           N  
ANISOU 1267  N   PHE A 182     3165  12009   8242   -876   -460    572       N  
ATOM   1268  CA  PHE A 182     120.657 187.764 300.017  1.00 73.16           C  
ANISOU 1268  CA  PHE A 182     4671  13372   9755   -905   -451    510       C  
ATOM   1269  C   PHE A 182     119.676 187.720 298.854  1.00 59.91           C  
ANISOU 1269  C   PHE A 182     3032  11511   8219   -858   -442    449       C  
ATOM   1270  O   PHE A 182     118.503 187.381 299.041  1.00 69.72           O  
ANISOU 1270  O   PHE A 182     4288  12642   9559   -819   -427    428       O  
ATOM   1271  CB  PHE A 182     120.904 189.198 300.491  1.00 72.93           C  
ANISOU 1271  CB  PHE A 182     4666  13424   9620  -1021   -464    468       C  
ATOM   1272  CG  PHE A 182     121.235 189.300 301.961  1.00 73.27           C  
ANISOU 1272  CG  PHE A 182     4667  13649   9522  -1075   -468    511       C  
ATOM   1273  CD1 PHE A 182     120.252 189.095 302.920  1.00 73.26           C  
ANISOU 1273  CD1 PHE A 182     4660  13642   9532  -1065   -453    516       C  
ATOM   1274  CD2 PHE A 182     122.523 189.593 302.384  1.00 73.40           C  
ANISOU 1274  CD2 PHE A 182     4646  13851   9393  -1135   -487    548       C  
ATOM   1275  CE1 PHE A 182     120.546 189.183 304.270  1.00 74.63           C  
ANISOU 1275  CE1 PHE A 182     4790  14000   9566  -1114   -456    558       C  
ATOM   1276  CE2 PHE A 182     122.823 189.682 303.739  1.00 64.43           C  
ANISOU 1276  CE2 PHE A 182     3466  12900   8116  -1187   -492    586       C  
ATOM   1277  CZ  PHE A 182     121.833 189.478 304.680  1.00 76.19           C  
ANISOU 1277  CZ  PHE A 182     4948  14389   9610  -1176   -477    591       C  
ATOM   1278  N   HIS A 183     120.142 188.010 297.640  1.00 59.68           N  
ANISOU 1278  N   HIS A 183     3019  11456   8202   -857   -452    425       N  
ATOM   1279  CA  HIS A 183     119.238 187.973 296.497  1.00 67.13           C  
ANISOU 1279  CA  HIS A 183     3996  12243   9269   -812   -445    370       C  
ATOM   1280  C   HIS A 183     118.698 186.565 296.258  1.00 67.38           C  
ANISOU 1280  C   HIS A 183     3997  12185   9419   -711   -431    385       C  
ATOM   1281  O   HIS A 183     117.530 186.396 295.887  1.00 57.95           O  
ANISOU 1281  O   HIS A 183     2825  10855   8340   -675   -421    340       O  
ATOM   1282  CB  HIS A 183     119.937 188.499 295.250  1.00 67.10           C  
ANISOU 1282  CB  HIS A 183     4005  12247   9242   -827   -457    351       C  
ATOM   1283  CG  HIS A 183     119.054 188.526 294.046  1.00 67.51           C  
ANISOU 1283  CG  HIS A 183     4087  12159   9404   -784   -452    299       C  
ATOM   1284  ND1 HIS A 183     119.047 187.519 293.106  1.00 57.81           N  
ANISOU 1284  ND1 HIS A 183     2837  10874   8254   -701   -450    298       N  
ATOM   1285  CD2 HIS A 183     118.123 189.424 293.645  1.00 69.16           C  
ANISOU 1285  CD2 HIS A 183     4343  12277   9658   -811   -448    246       C  
ATOM   1286  CE1 HIS A 183     118.162 187.805 292.167  1.00 72.32           C  
ANISOU 1286  CE1 HIS A 183     4707  12601  10172   -681   -449    247       C  
ATOM   1287  NE2 HIS A 183     117.586 188.955 292.471  1.00 70.70           N  
ANISOU 1287  NE2 HIS A 183     4543  12373   9947   -745   -447    219       N  
ATOM   1288  N   LEU A 184     119.529 185.539 296.464  1.00 68.80           N  
ANISOU 1288  N   LEU A 184     4123  12437   9581   -664   -428    446       N  
ATOM   1289  CA  LEU A 184     119.033 184.170 296.357  1.00 69.57           C  
ANISOU 1289  CA  LEU A 184     4181  12448   9804   -570   -408    458       C  
ATOM   1290  C   LEU A 184     118.034 183.854 297.456  1.00 70.50           C  
ANISOU 1290  C   LEU A 184     4294  12523   9970   -558   -390    466       C  
ATOM   1291  O   LEU A 184     117.093 183.082 297.241  1.00 70.83           O  
ANISOU 1291  O   LEU A 184     4325  12438  10149   -495   -373    439       O  
ATOM   1292  CB  LEU A 184     120.186 183.175 296.408  1.00 60.18           C  
ANISOU 1292  CB  LEU A 184     2929  11350   8585   -525   -402    529       C  
ATOM   1293  CG  LEU A 184     120.965 183.013 295.110  1.00 61.57           C  
ANISOU 1293  CG  LEU A 184     3096  11526   8771   -500   -410    516       C  
ATOM   1294  CD1 LEU A 184     121.633 181.662 295.116  1.00 62.30           C  
ANISOU 1294  CD1 LEU A 184     3118  11646   8906   -425   -391    573       C  
ATOM   1295  CD2 LEU A 184     120.059 183.177 293.895  1.00 59.39           C  
ANISOU 1295  CD2 LEU A 184     2856  11103   8605   -476   -412    431       C  
ATOM   1296  N   LEU A 185     118.236 184.419 298.643  1.00 59.60           N  
ANISOU 1296  N   LEU A 185     2916  11251   8480   -617   -394    501       N  
ATOM   1297  CA  LEU A 185     117.222 184.318 299.681  1.00 59.48           C  
ANISOU 1297  CA  LEU A 185     2901  11199   8498   -613   -377    504       C  
ATOM   1298  C   LEU A 185     116.062 185.261 299.404  1.00 92.50           C  
ANISOU 1298  C   LEU A 185     7145  15267  12734   -650   -378    426       C  
ATOM   1299  O   LEU A 185     114.908 184.923 299.684  1.00 79.40           O  
ANISOU 1299  O   LEU A 185     5491  13504  11175   -616   -360    406       O  
ATOM   1300  CB  LEU A 185     117.834 184.624 301.045  1.00 60.28           C  
ANISOU 1300  CB  LEU A 185     2980  11469   8455   -665   -381    567       C  
ATOM   1301  CG  LEU A 185     118.262 183.445 301.909  1.00 61.17           C  
ANISOU 1301  CG  LEU A 185     3023  11666   8551   -606   -364    662       C  
ATOM   1302  CD1 LEU A 185     118.828 182.325 301.068  1.00 61.41           C  
ANISOU 1302  CD1 LEU A 185     3013  11662   8658   -528   -355    691       C  
ATOM   1303  CD2 LEU A 185     119.289 183.936 302.889  1.00 62.09           C  
ANISOU 1303  CD2 LEU A 185     3117  11985   8489   -671   -380    722       C  
ATOM   1304  N   PHE A 186     116.352 186.440 298.845  1.00 58.29           N  
ANISOU 1304  N   PHE A 186     2856  10952   8340   -718   -396    384       N  
ATOM   1305  CA  PHE A 186     115.315 187.449 298.656  1.00 57.54           C  
ANISOU 1305  CA  PHE A 186     2816  10760   8286   -760   -393    319       C  
ATOM   1306  C   PHE A 186     114.238 186.973 297.693  1.00 63.86           C  
ANISOU 1306  C   PHE A 186     3632  11394   9239   -694   -384    276       C  
ATOM   1307  O   PHE A 186     113.055 187.281 297.877  1.00 62.79           O  
ANISOU 1307  O   PHE A 186     3523  11161   9174   -697   -371    242       O  
ATOM   1308  CB  PHE A 186     115.925 188.753 298.154  1.00 57.51           C  
ANISOU 1308  CB  PHE A 186     2848  10806   8198   -841   -409    288       C  
ATOM   1309  CG  PHE A 186     114.912 189.821 297.872  1.00 68.96           C  
ANISOU 1309  CG  PHE A 186     4349  12156   9696   -883   -400    227       C  
ATOM   1310  CD1 PHE A 186     114.435 190.624 298.893  1.00 69.54           C  
ANISOU 1310  CD1 PHE A 186     4433  12271   9717   -951   -390    215       C  
ATOM   1311  CD2 PHE A 186     114.440 190.029 296.585  1.00 68.84           C  
ANISOU 1311  CD2 PHE A 186     4362  12033   9762   -856   -401    190       C  
ATOM   1312  CE1 PHE A 186     113.504 191.614 298.637  1.00 68.77           C  
ANISOU 1312  CE1 PHE A 186     4375  12096   9659   -991   -376    166       C  
ATOM   1313  CE2 PHE A 186     113.507 191.016 296.324  1.00 68.39           C  
ANISOU 1313  CE2 PHE A 186     4347  11888   9750   -891   -390    144       C  
ATOM   1314  CZ  PHE A 186     113.039 191.809 297.351  1.00 55.75           C  
ANISOU 1314  CZ  PHE A 186     2756  10320   8105   -958   -376    134       C  
ATOM   1315  N   GLU A 187     114.621 186.236 296.652  1.00 56.79           N  
ANISOU 1315  N   GLU A 187     2716  10465   8396   -637   -390    275       N  
ATOM   1316  CA  GLU A 187     113.631 185.711 295.723  1.00 66.81           C  
ANISOU 1316  CA  GLU A 187     3990  11585   9810   -575   -384    229       C  
ATOM   1317  C   GLU A 187     112.996 184.419 296.215  1.00 70.53           C  
ANISOU 1317  C   GLU A 187     4416  11987  10394   -503   -363    241       C  
ATOM   1318  O   GLU A 187     112.218 183.810 295.473  1.00 72.54           O  
ANISOU 1318  O   GLU A 187     4662  12118  10781   -448   -357    200       O  
ATOM   1319  CB  GLU A 187     114.252 185.479 294.344  1.00 64.01           C  
ANISOU 1319  CB  GLU A 187     3628  11223   9470   -545   -398    213       C  
ATOM   1320  CG  GLU A 187     115.205 184.293 294.257  1.00 63.54           C  
ANISOU 1320  CG  GLU A 187     3509  11216   9417   -490   -394    253       C  
ATOM   1321  CD  GLU A 187     115.671 184.041 292.834  1.00 63.09           C  
ANISOU 1321  CD  GLU A 187     3444  11139   9389   -456   -405    228       C  
ATOM   1322  OE1 GLU A 187     115.057 184.603 291.906  1.00 62.41           O  
ANISOU 1322  OE1 GLU A 187     3394  10982   9338   -461   -414    181       O  
ATOM   1323  OE2 GLU A 187     116.651 183.290 292.640  1.00 57.46           O  
ANISOU 1323  OE2 GLU A 187     2686  10486   8660   -422   -403    261       O  
ATOM   1324  N   ALA A 188     113.314 183.982 297.434  1.00 56.92           N  
ANISOU 1324  N   ALA A 188     2659  10344   8623   -502   -350    295       N  
ATOM   1325  CA  ALA A 188     112.689 182.808 298.024  1.00 57.14           C  
ANISOU 1325  CA  ALA A 188     2641  10313   8756   -435   -323    311       C  
ATOM   1326  C   ALA A 188     111.592 183.207 299.000  1.00 56.83           C  
ANISOU 1326  C   ALA A 188     2623  10237   8733   -456   -307    304       C  
ATOM   1327  O   ALA A 188     110.466 182.707 298.927  1.00 65.11           O  
ANISOU 1327  O   ALA A 188     3665  11161   9912   -412   -289    267       O  
ATOM   1328  CB  ALA A 188     113.742 181.935 298.721  1.00 58.09           C  
ANISOU 1328  CB  ALA A 188     2701  10552   8818   -406   -313    390       C  
ATOM   1329  N   PHE A 189     111.913 184.089 299.942  1.00 57.03           N  
ANISOU 1329  N   PHE A 189     2669  10373   8628   -524   -313    335       N  
ATOM   1330  CA  PHE A 189     110.879 184.580 300.837  1.00 56.74           C  
ANISOU 1330  CA  PHE A 189     2654  10304   8602   -550   -297    324       C  
ATOM   1331  C   PHE A 189     109.781 185.246 300.039  1.00 55.84           C  
ANISOU 1331  C   PHE A 189     2590  10049   8577   -561   -298    252       C  
ATOM   1332  O   PHE A 189     108.602 184.913 300.175  1.00 68.19           O  
ANISOU 1332  O   PHE A 189     4153  11503  10253   -525   -278    227       O  
ATOM   1333  CB  PHE A 189     111.441 185.577 301.844  1.00 57.14           C  
ANISOU 1333  CB  PHE A 189     2718  10498   8493   -633   -305    353       C  
ATOM   1334  CG  PHE A 189     112.385 184.985 302.836  1.00 80.69           C  
ANISOU 1334  CG  PHE A 189     5646  13641  11370   -626   -304    436       C  
ATOM   1335  CD1 PHE A 189     112.577 183.614 302.939  1.00 80.91           C  
ANISOU 1335  CD1 PHE A 189     5619  13660  11463   -543   -287    487       C  
ATOM   1336  CD2 PHE A 189     113.080 185.821 303.686  1.00 81.64           C  
ANISOU 1336  CD2 PHE A 189     5760  13946  11312   -708   -317    469       C  
ATOM   1337  CE1 PHE A 189     113.462 183.101 303.870  1.00 59.57           C  
ANISOU 1337  CE1 PHE A 189     2865  11109   8660   -535   -284    577       C  
ATOM   1338  CE2 PHE A 189     113.957 185.316 304.614  1.00 83.94           C  
ANISOU 1338  CE2 PHE A 189     5996  14405  11491   -705   -318    553       C  
ATOM   1339  CZ  PHE A 189     114.151 183.955 304.709  1.00 85.46           C  
ANISOU 1339  CZ  PHE A 189     6140  14576  11755   -615   -301    615       C  
ATOM   1340  N   THR A 190     110.162 186.188 299.179  1.00 55.53           N  
ANISOU 1340  N   THR A 190     2591  10017   8491   -608   -319    221       N  
ATOM   1341  CA  THR A 190     109.159 187.003 298.507  1.00 61.84           C  
ANISOU 1341  CA  THR A 190     3439  10704   9355   -627   -318    166       C  
ATOM   1342  C   THR A 190     108.455 186.225 297.407  1.00 61.15           C  
ANISOU 1342  C   THR A 190     3341  10482   9411   -556   -319    132       C  
ATOM   1343  O   THR A 190     107.237 186.326 297.250  1.00 53.83           O  
ANISOU 1343  O   THR A 190     2431   9441   8582   -540   -307     99       O  
ATOM   1344  CB  THR A 190     109.791 188.274 297.955  1.00 54.65           C  
ANISOU 1344  CB  THR A 190     2568   9848   8350   -700   -335    149       C  
ATOM   1345  OG1 THR A 190     110.641 188.839 298.971  1.00 55.24           O  
ANISOU 1345  OG1 THR A 190     2638  10064   8288   -767   -338    178       O  
ATOM   1346  CG2 THR A 190     108.665 189.278 297.473  1.00 60.32           C  
ANISOU 1346  CG2 THR A 190     3333  10457   9127   -726   -326    103       C  
ATOM   1347  N   GLY A 191     109.198 185.437 296.639  1.00 60.96           N  
ANISOU 1347  N   GLY A 191     3286  10472   9404   -513   -331    137       N  
ATOM   1348  CA  GLY A 191     108.570 184.652 295.595  1.00 54.39           C  
ANISOU 1348  CA  GLY A 191     2436   9518   8710   -448   -333     98       C  
ATOM   1349  C   GLY A 191     107.647 183.593 296.155  1.00 54.46           C  
ANISOU 1349  C   GLY A 191     2405   9438   8849   -390   -307     86       C  
ATOM   1350  O   GLY A 191     106.487 183.487 295.756  1.00 54.02           O  
ANISOU 1350  O   GLY A 191     2355   9261   8909   -366   -302     44       O  
ATOM   1351  N   PHE A 192     108.136 182.826 297.119  1.00 55.07           N  
ANISOU 1351  N   PHE A 192     2438   9582   8904   -369   -290    125       N  
ATOM   1352  CA  PHE A 192     107.425 181.651 297.595  1.00 55.31           C  
ANISOU 1352  CA  PHE A 192     2418   9541   9057   -305   -260    108       C  
ATOM   1353  C   PHE A 192     107.052 181.704 299.064  1.00 55.52           C  
ANISOU 1353  C   PHE A 192     2440   9617   9039   -317   -235    148       C  
ATOM   1354  O   PHE A 192     105.918 181.363 299.422  1.00 70.06           O  
ANISOU 1354  O   PHE A 192     4272  11374  10975   -289   -211    113       O  
ATOM   1355  CB  PHE A 192     108.287 180.412 297.345  1.00 56.02           C  
ANISOU 1355  CB  PHE A 192     2443   9660   9182   -248   -252    121       C  
ATOM   1356  CG  PHE A 192     107.576 179.118 297.561  1.00 56.34           C  
ANISOU 1356  CG  PHE A 192     2423   9620   9365   -177   -219     78       C  
ATOM   1357  CD1 PHE A 192     106.899 178.498 296.514  1.00 75.68           C  
ANISOU 1357  CD1 PHE A 192     4855  11940  11960   -134   -217    -12       C  
ATOM   1358  CD2 PHE A 192     107.592 178.504 298.801  1.00 63.55           C  
ANISOU 1358  CD2 PHE A 192     3299  10595  10252   -154   -186    128       C  
ATOM   1359  CE1 PHE A 192     106.252 177.282 296.716  1.00 75.61           C  
ANISOU 1359  CE1 PHE A 192     4828  11874  12026    -71   -181    -70       C  
ATOM   1360  CE2 PHE A 192     106.953 177.296 299.003  1.00 57.31           C  
ANISOU 1360  CE2 PHE A 192     2451   9750   9573    -88   -150     83       C  
ATOM   1361  CZ  PHE A 192     106.281 176.683 297.963  1.00 75.96           C  
ANISOU 1361  CZ  PHE A 192     4809  11998  12053    -48   -147    -32       C  
ATOM   1362  N   VAL A 193     107.982 182.073 299.938  1.00 55.99           N  
ANISOU 1362  N   VAL A 193     2499   9819   8954   -356   -239    220       N  
ATOM   1363  CA  VAL A 193     107.753 181.789 301.349  1.00 56.43           C  
ANISOU 1363  CA  VAL A 193     2530   9936   8975   -350   -212    274       C  
ATOM   1364  C   VAL A 193     106.720 182.726 301.933  1.00 55.90           C  
ANISOU 1364  C   VAL A 193     2507   9834   8900   -393   -203    253       C  
ATOM   1365  O   VAL A 193     105.859 182.308 302.706  1.00 55.97           O  
ANISOU 1365  O   VAL A 193     2497   9808   8962   -364   -173    257       O  
ATOM   1366  CB  VAL A 193     109.069 181.820 302.134  1.00 57.23           C  
ANISOU 1366  CB  VAL A 193     2608  10213   8923   -375   -219    363       C  
ATOM   1367  CG1 VAL A 193     108.771 182.138 303.566  1.00 87.42           C  
ANISOU 1367  CG1 VAL A 193     6429  14119  12669   -401   -203    414       C  
ATOM   1368  CG2 VAL A 193     109.719 180.468 302.030  1.00 57.95           C  
ANISOU 1368  CG2 VAL A 193     2632  10326   9059   -304   -205    403       C  
ATOM   1369  N   VAL A 194     106.783 183.997 301.579  1.00 55.43           N  
ANISOU 1369  N   VAL A 194     2503   9783   8774   -462   -225    229       N  
ATOM   1370  CA  VAL A 194     105.731 184.931 301.997  1.00 66.91           C  
ANISOU 1370  CA  VAL A 194     3997  11187  10237   -503   -212    202       C  
ATOM   1371  C   VAL A 194     104.363 184.488 301.479  1.00 63.11           C  
ANISOU 1371  C   VAL A 194     3518  10540   9921   -451   -194    142       C  
ATOM   1372  O   VAL A 194     103.409 184.453 302.273  1.00 61.06           O  
ANISOU 1372  O   VAL A 194     3253  10248   9698   -442   -165    139       O  
ATOM   1373  CB  VAL A 194     106.097 186.367 301.584  1.00 68.94           C  
ANISOU 1373  CB  VAL A 194     4304  11497  10392   -587   -234    188       C  
ATOM   1374  CG1 VAL A 194     104.855 187.177 301.260  1.00 70.29           C  
ANISOU 1374  CG1 VAL A 194     4516  11561  10631   -608   -222    142       C  
ATOM   1375  CG2 VAL A 194     106.911 187.028 302.662  1.00 55.45           C  
ANISOU 1375  CG2 VAL A 194     2586   9979   8504   -659   -237    238       C  
ATOM   1376  N   PRO A 195     104.186 184.142 300.181  1.00 64.21           N  
ANISOU 1376  N   PRO A 195     3658  10583  10157   -417   -209     93       N  
ATOM   1377  CA  PRO A 195     102.896 183.585 299.734  1.00 66.18           C  
ANISOU 1377  CA  PRO A 195     3896  10690  10561   -367   -194     27       C  
ATOM   1378  C   PRO A 195     102.548 182.240 300.347  1.00 70.93           C  
ANISOU 1378  C   PRO A 195     4437  11280  11233   -300   -163     12       C  
ATOM   1379  O   PRO A 195     101.415 182.043 300.793  1.00 72.59           O  
ANISOU 1379  O   PRO A 195     4658  11432  11491   -279   -136    -25       O  
ATOM   1380  CB  PRO A 195     103.089 183.456 298.219  1.00 53.41           C  
ANISOU 1380  CB  PRO A 195     2282   9006   9006   -349   -223     -9       C  
ATOM   1381  CG  PRO A 195     104.072 184.493 297.884  1.00 53.34           C  
ANISOU 1381  CG  PRO A 195     2314   9086   8867   -409   -250     30       C  
ATOM   1382  CD  PRO A 195     105.033 184.485 299.023  1.00 53.92           C  
ANISOU 1382  CD  PRO A 195     2372   9298   8816   -435   -243     87       C  
ATOM   1383  N   PHE A 196     103.494 181.298 300.345  1.00 54.78           N  
ANISOU 1383  N   PHE A 196     2344   9296   9174   -264   -164     41       N  
ATOM   1384  CA  PHE A 196     103.199 179.991 300.928  1.00 55.36           C  
ANISOU 1384  CA  PHE A 196     2357   9375   9304   -199   -129     31       C  
ATOM   1385  C   PHE A 196     102.755 180.120 302.381  1.00 85.12           C  
ANISOU 1385  C   PHE A 196     6125  13203  13015   -206    -99     92       C  
ATOM   1386  O   PHE A 196     101.908 179.347 302.835  1.00 85.47           O  
ANISOU 1386  O   PHE A 196     6138  13223  13113   -159    -66     68       O  
ATOM   1387  CB  PHE A 196     104.408 179.058 300.817  1.00 86.11           C  
ANISOU 1387  CB  PHE A 196     6198  13341  13177   -163   -130     77       C  
ATOM   1388  CG  PHE A 196     104.100 177.612 301.142  1.00 83.47           C  
ANISOU 1388  CG  PHE A 196     5796  13006  12912    -88    -91     58       C  
ATOM   1389  CD1 PHE A 196     103.244 176.872 300.335  1.00 81.59           C  
ANISOU 1389  CD1 PHE A 196     5565  12684  12753    -42    -80    -56       C  
ATOM   1390  CD2 PHE A 196     104.670 176.991 302.247  1.00 80.64           C  
ANISOU 1390  CD2 PHE A 196     5396  12748  12494    -62    -65    170       C  
ATOM   1391  CE1 PHE A 196     102.959 175.542 300.630  1.00 78.77           C  
ANISOU 1391  CE1 PHE A 196     5149  12361  12418     25    -43    -66       C  
ATOM   1392  CE2 PHE A 196     104.389 175.663 302.542  1.00 77.79           C  
ANISOU 1392  CE2 PHE A 196     4975  12392  12191     11    -26    176       C  
ATOM   1393  CZ  PHE A 196     103.534 174.940 301.732  1.00 76.98           C  
ANISOU 1393  CZ  PHE A 196     4850  12221  12177     54    -14     52       C  
ATOM   1394  N   LEU A 197     103.287 181.105 303.116  1.00 84.39           N  
ANISOU 1394  N   LEU A 197     6064  13201  12799   -267   -109    168       N  
ATOM   1395  CA  LEU A 197     102.814 181.327 304.481  1.00 82.57           C  
ANISOU 1395  CA  LEU A 197     5831  13026  12514   -278    -81    223       C  
ATOM   1396  C   LEU A 197     101.441 181.981 304.492  1.00 79.79           C  
ANISOU 1396  C   LEU A 197     5516  12581  12220   -295    -66    161       C  
ATOM   1397  O   LEU A 197     100.602 181.656 305.339  1.00 80.39           O  
ANISOU 1397  O   LEU A 197     5572  12662  12311   -270    -32    179       O  
ATOM   1398  CB  LEU A 197     103.805 182.181 305.269  1.00 56.33           C  
ANISOU 1398  CB  LEU A 197     2515   9872   9015   -344    -98    316       C  
ATOM   1399  CG  LEU A 197     105.152 181.548 305.614  1.00 57.18           C  
ANISOU 1399  CG  LEU A 197     2580  10110   9036   -328   -106    398       C  
ATOM   1400  CD1 LEU A 197     105.766 182.224 306.835  1.00 57.96           C  
ANISOU 1400  CD1 LEU A 197     2666  10410   8946   -385   -111    494       C  
ATOM   1401  CD2 LEU A 197     105.021 180.042 305.810  1.00 57.68           C  
ANISOU 1401  CD2 LEU A 197     2584  10135   9195   -238    -75    420       C  
ATOM   1402  N   ILE A 198     101.196 182.911 303.569  1.00 77.19           N  
ANISOU 1402  N   ILE A 198     5236  12176  11915   -337    -90    102       N  
ATOM   1403  CA  ILE A 198      99.902 183.583 303.525  1.00 53.86           C  
ANISOU 1403  CA  ILE A 198     2313   9139   9013   -354    -74     53       C  
ATOM   1404  C   ILE A 198      98.808 182.606 303.123  1.00 53.64           C  
ANISOU 1404  C   ILE A 198     2288   9005   9088   -286    -53    -38       C  
ATOM   1405  O   ILE A 198      97.743 182.551 303.748  1.00 53.58           O  
ANISOU 1405  O   ILE A 198     2289   8983   9085   -272    -21    -56       O  
ATOM   1406  CB  ILE A 198      99.948 184.793 302.576  1.00 53.24           C  
ANISOU 1406  CB  ILE A 198     2289   9015   8926   -410   -102     29       C  
ATOM   1407  CG1 ILE A 198     100.767 185.927 303.201  1.00 53.60           C  
ANISOU 1407  CG1 ILE A 198     2354   9205   8805   -492   -112    103       C  
ATOM   1408  CG2 ILE A 198      98.543 185.258 302.253  1.00 52.63           C  
ANISOU 1408  CG2 ILE A 198     2258   8822   8918   -408    -84    -29       C  
ATOM   1409  CD1 ILE A 198     100.635 187.272 302.492  1.00 53.10           C  
ANISOU 1409  CD1 ILE A 198     2343   9119   8714   -556   -126     82       C  
ATOM   1410  N   VAL A 199      99.056 181.810 302.086  1.00 53.72           N  
ANISOU 1410  N   VAL A 199     2302   8976   9132   -245    -71    -85       N  
ATOM   1411  CA  VAL A 199      98.014 180.937 301.553  1.00 81.11           C  
ANISOU 1411  CA  VAL A 199     5796  12395  12628   -189    -56   -182       C  
ATOM   1412  C   VAL A 199      97.859 179.724 302.464  1.00 80.82           C  
ANISOU 1412  C   VAL A 199     5686  12443  12580   -134    -22   -153       C  
ATOM   1413  O   VAL A 199      96.993 178.870 302.244  1.00 79.90           O  
ANISOU 1413  O   VAL A 199     5566  12350  12442    -86     -5   -203       O  
ATOM   1414  CB  VAL A 199      98.302 180.512 300.091  1.00 53.57           C  
ANISOU 1414  CB  VAL A 199     2333   8854   9167   -167    -85   -254       C  
ATOM   1415  CG1 VAL A 199      98.685 181.713 299.241  1.00 53.01           C  
ANISOU 1415  CG1 VAL A 199     2314   8706   9122   -218   -121   -222       C  
ATOM   1416  CG2 VAL A 199      99.340 179.392 300.018  1.00 54.30           C  
ANISOU 1416  CG2 VAL A 199     2355   9006   9271   -127    -86   -231       C  
ATOM   1417  N   VAL A 200      98.684 179.642 303.501  1.00 54.91           N  
ANISOU 1417  N   VAL A 200     2334   9235   9294   -140    -11    -52       N  
ATOM   1418  CA  VAL A 200      98.557 178.554 304.458  1.00 55.68           C  
ANISOU 1418  CA  VAL A 200     2354   9404   9398    -84     25      8       C  
ATOM   1419  C   VAL A 200      97.762 179.048 305.658  1.00 67.87           C  
ANISOU 1419  C   VAL A 200     3916  10962  10909    -98     55     66       C  
ATOM   1420  O   VAL A 200      96.998 178.289 306.262  1.00 67.53           O  
ANISOU 1420  O   VAL A 200     3850  10934  10874    -48     89    101       O  
ATOM   1421  CB  VAL A 200      99.939 178.003 304.852  1.00 56.48           C  
ANISOU 1421  CB  VAL A 200     2414   9579   9466    -69     23    116       C  
ATOM   1422  CG1 VAL A 200      99.954 177.546 306.294  1.00 58.17           C  
ANISOU 1422  CG1 VAL A 200     2596   9870   9636    -40     60    248       C  
ATOM   1423  CG2 VAL A 200     100.304 176.856 303.925  1.00 56.85           C  
ANISOU 1423  CG2 VAL A 200     2416   9618   9567    -15     21     66       C  
ATOM   1424  N   ALA A 201      97.893 180.336 305.983  1.00 69.72           N  
ANISOU 1424  N   ALA A 201     4192  11199  11100   -166     44     90       N  
ATOM   1425  CA  ALA A 201      97.089 180.900 307.062  1.00 73.24           C  
ANISOU 1425  CA  ALA A 201     4643  11679  11505   -184     74    154       C  
ATOM   1426  C   ALA A 201      95.628 181.021 306.648  1.00 76.04           C  
ANISOU 1426  C   ALA A 201     5025  11954  11913   -172     89     52       C  
ATOM   1427  O   ALA A 201      94.728 180.563 307.362  1.00 78.14           O  
ANISOU 1427  O   ALA A 201     5278  12235  12178   -134    123     90       O  
ATOM   1428  CB  ALA A 201      97.646 182.261 307.484  1.00 55.41           C  
ANISOU 1428  CB  ALA A 201     2411   9491   9153   -265     58    217       C  
ATOM   1429  N   SER A 202      95.376 181.623 305.483  1.00 75.32           N  
ANISOU 1429  N   SER A 202     5003  11782  11835   -200     63    -52       N  
ATOM   1430  CA  SER A 202      94.003 181.832 305.037  1.00 72.90           C  
ANISOU 1430  CA  SER A 202     4763  11427  11510   -193     73   -129       C  
ATOM   1431  C   SER A 202      93.323 180.511 304.694  1.00 73.91           C  
ANISOU 1431  C   SER A 202     4875  11593  11613   -122     80   -153       C  
ATOM   1432  O   SER A 202      92.190 180.258 305.121  1.00 74.14           O  
ANISOU 1432  O   SER A 202     4897  11645  11626    -95    106   -124       O  
ATOM   1433  CB  SER A 202      93.982 182.775 303.834  1.00 70.12           C  
ANISOU 1433  CB  SER A 202     4495  10992  11154   -234     42   -210       C  
ATOM   1434  OG  SER A 202      94.420 182.110 302.663  1.00 52.61           O  
ANISOU 1434  OG  SER A 202     2291   8763   8934   -206     12   -272       O  
ATOM   1435  N   TYR A 203      93.995 179.652 303.927  1.00 53.89           N  
ANISOU 1435  N   TYR A 203     2314   9077   9083    -90     60   -169       N  
ATOM   1436  CA  TYR A 203      93.351 178.432 303.455  1.00 54.22           C  
ANISOU 1436  CA  TYR A 203     2324   9172   9107    -27     66   -151       C  
ATOM   1437  C   TYR A 203      93.279 177.341 304.511  1.00 55.06           C  
ANISOU 1437  C   TYR A 203     2336   9303   9280     32    105    -45       C  
ATOM   1438  O   TYR A 203      92.603 176.332 304.283  1.00 55.42           O  
ANISOU 1438  O   TYR A 203     2344   9356   9358     88    120      3       O  
ATOM   1439  CB  TYR A 203      94.065 177.883 302.223  1.00 61.83           C  
ANISOU 1439  CB  TYR A 203     3289  10157  10047    -13     36   -201       C  
ATOM   1440  CG  TYR A 203      93.154 177.661 301.038  1.00 54.05           C  
ANISOU 1440  CG  TYR A 203     2336   9219   8983      2     21   -212       C  
ATOM   1441  CD1 TYR A 203      92.142 176.715 301.081  1.00 73.02           C  
ANISOU 1441  CD1 TYR A 203     4689  11626  11431     55     43   -120       C  
ATOM   1442  CD2 TYR A 203      93.319 178.390 299.870  1.00 53.51           C  
ANISOU 1442  CD2 TYR A 203     2334   9171   8826    -35    -14   -289       C  
ATOM   1443  CE1 TYR A 203      91.314 176.512 299.996  1.00 75.75           C  
ANISOU 1443  CE1 TYR A 203     5046  11977  11757     66     28    -91       C  
ATOM   1444  CE2 TYR A 203      92.506 178.194 298.783  1.00 53.34           C  
ANISOU 1444  CE2 TYR A 203     2327   9213   8725    -21    -29   -236       C  
ATOM   1445  CZ  TYR A 203      91.501 177.256 298.849  1.00 78.72           C  
ANISOU 1445  CZ  TYR A 203     5487  12401  12021     27     -9   -134       C  
ATOM   1446  OH  TYR A 203      90.679 177.054 297.763  1.00 81.01           O  
ANISOU 1446  OH  TYR A 203     5777  12682  12321     38    -24    -79       O  
ATOM   1447  N   ALA A 204      93.966 177.499 305.642  1.00 55.45           N  
ANISOU 1447  N   ALA A 204     2347   9361   9362     23    123     15       N  
ATOM   1448  CA  ALA A 204      93.760 176.601 306.769  1.00 83.86           C  
ANISOU 1448  CA  ALA A 204     5909  12961  12992     80    165    153       C  
ATOM   1449  C   ALA A 204      92.846 177.193 307.830  1.00 56.12           C  
ANISOU 1449  C   ALA A 204     2421   9435   9466     69    194    204       C  
ATOM   1450  O   ALA A 204      92.265 176.436 308.613  1.00 59.11           O  
ANISOU 1450  O   ALA A 204     2779   9798   9882    124    232    314       O  
ATOM   1451  CB  ALA A 204      95.099 176.206 307.408  1.00 84.86           C  
ANISOU 1451  CB  ALA A 204     5991  13130  13123     90    170    239       C  
ATOM   1452  N   ASP A 205      92.711 178.521 307.876  1.00 55.49           N  
ANISOU 1452  N   ASP A 205     2380   9353   9350      2    182    146       N  
ATOM   1453  CA  ASP A 205      91.668 179.124 308.700  1.00 55.44           C  
ANISOU 1453  CA  ASP A 205     2392   9338   9335     -8    213    200       C  
ATOM   1454  C   ASP A 205      90.292 178.652 308.256  1.00 55.11           C  
ANISOU 1454  C   ASP A 205     2376   9250   9314     32    223    186       C  
ATOM   1455  O   ASP A 205      89.420 178.378 309.088  1.00 89.64           O  
ANISOU 1455  O   ASP A 205     6746  13596  13717     68    260    283       O  
ATOM   1456  CB  ASP A 205      91.763 180.652 308.637  1.00 54.91           C  
ANISOU 1456  CB  ASP A 205     2358   9271   9236    -91    201    147       C  
ATOM   1457  CG  ASP A 205      90.418 181.339 308.856  1.00 60.52           C  
ANISOU 1457  CG  ASP A 205     3101   9955   9939   -104    225    139       C  
ATOM   1458  OD1 ASP A 205      90.148 181.782 309.993  1.00 54.94           O  
ANISOU 1458  OD1 ASP A 205     2382   9274   9219   -115    260    229       O  
ATOM   1459  OD2 ASP A 205      89.633 181.447 307.886  1.00 59.94           O  
ANISOU 1459  OD2 ASP A 205     3064   9853   9857   -104    211     54       O  
ATOM   1460  N   ILE A 206      90.084 178.544 306.943  1.00 54.56           N  
ANISOU 1460  N   ILE A 206     2330   9174   9225     29    191     91       N  
ATOM   1461  CA  ILE A 206      88.802 178.086 306.414  1.00 54.42           C  
ANISOU 1461  CA  ILE A 206     2336   9110   9233     66    196    127       C  
ATOM   1462  C   ILE A 206      88.506 176.670 306.895  1.00 55.30           C  
ANISOU 1462  C   ILE A 206     2410   9158   9445    144    228    252       C  
ATOM   1463  O   ILE A 206      87.491 176.417 307.553  1.00 58.72           O  
ANISOU 1463  O   ILE A 206     2853   9521   9936    177    262    337       O  
ATOM   1464  CB  ILE A 206      88.794 178.159 304.878  1.00 62.39           C  
ANISOU 1464  CB  ILE A 206     3363  10141  10203     50    154     49       C  
ATOM   1465  CG1 ILE A 206      89.085 179.575 304.383  1.00 53.17           C  
ANISOU 1465  CG1 ILE A 206     2261   9003   8938    -24    127    -55       C  
ATOM   1466  CG2 ILE A 206      87.463 177.671 304.336  1.00 62.43           C  
ANISOU 1466  CG2 ILE A 206     3392  10066  10264     86    159    110       C  
ATOM   1467  CD1 ILE A 206      89.405 179.612 302.905  1.00 52.87           C  
ANISOU 1467  CD1 ILE A 206     2263   8989   8836    -37     85   -109       C  
ATOM   1468  N   SER A 207      89.392 175.722 306.567  1.00 55.89           N  
ANISOU 1468  N   SER A 207     2440   9244   9552    175    222    267       N  
ATOM   1469  CA  SER A 207      89.182 174.327 306.952  1.00 77.14           C  
ANISOU 1469  CA  SER A 207     5092  11860  12359    249    259    386       C  
ATOM   1470  C   SER A 207      89.075 174.154 308.461  1.00 57.44           C  
ANISOU 1470  C   SER A 207     2576   9357   9892    278    305    503       C  
ATOM   1471  O   SER A 207      88.571 173.125 308.925  1.00 58.21           O  
ANISOU 1471  O   SER A 207     2650   9371  10097    340    345    617       O  
ATOM   1472  CB  SER A 207      90.314 173.444 306.412  1.00 77.78           C  
ANISOU 1472  CB  SER A 207     5123  11966  12462    273    250    380       C  
ATOM   1473  OG  SER A 207      90.368 173.457 304.994  1.00 77.53           O  
ANISOU 1473  OG  SER A 207     5104  11947  12408    255    212    289       O  
ATOM   1474  N   ARG A 208      89.549 175.130 309.230  1.00 57.18           N  
ANISOU 1474  N   ARG A 208     2550   9403   9774    234    302    481       N  
ATOM   1475  CA  ARG A 208      89.350 175.188 310.669  1.00 74.27           C  
ANISOU 1475  CA  ARG A 208     4700  11581  11939    254    344    590       C  
ATOM   1476  C   ARG A 208      88.113 175.997 311.044  1.00 75.53           C  
ANISOU 1476  C   ARG A 208     4898  11705  12094    236    360    599       C  
ATOM   1477  O   ARG A 208      87.690 175.960 312.204  1.00 79.74           O  
ANISOU 1477  O   ARG A 208     5415  12238  12645    264    403    717       O  
ATOM   1478  CB  ARG A 208      90.598 175.789 311.331  1.00 72.79           C  
ANISOU 1478  CB  ARG A 208     4481  11497  11677    216    337    612       C  
ATOM   1479  CG  ARG A 208      90.910 175.305 312.741  1.00 72.09           C  
ANISOU 1479  CG  ARG A 208     4341  11461  11589    261    381    785       C  
ATOM   1480  CD  ARG A 208      90.915 176.464 313.736  1.00 70.15           C  
ANISOU 1480  CD  ARG A 208     4095  11300  11257    215    392    831       C  
ATOM   1481  NE  ARG A 208      91.273 177.743 313.120  1.00 66.43           N  
ANISOU 1481  NE  ARG A 208     3659  10857  10725    127    352    703       N  
ATOM   1482  CZ  ARG A 208      90.397 178.692 312.793  1.00 63.69           C  
ANISOU 1482  CZ  ARG A 208     3358  10468  10375     83    348    620       C  
ATOM   1483  NH1 ARG A 208      89.100 178.509 313.016  1.00 63.24           N  
ANISOU 1483  NH1 ARG A 208     3320  10345  10365    119    378    650       N  
ATOM   1484  NH2 ARG A 208      90.816 179.820 312.238  1.00 62.27           N  
ANISOU 1484  NH2 ARG A 208     3205  10304  10149      6    317    519       N  
ATOM   1485  N   ARG A 209      87.532 176.726 310.088  1.00 71.88           N  
ANISOU 1485  N   ARG A 209     4487  11221  11604    194    331    488       N  
ATOM   1486  CA  ARG A 209      86.295 177.462 310.328  1.00 69.50           C  
ANISOU 1486  CA  ARG A 209     4225  10875  11307    180    348    500       C  
ATOM   1487  C   ARG A 209      85.085 176.560 310.137  1.00 56.05           C  
ANISOU 1487  C   ARG A 209     2539   9052   9706    239    368    563       C  
ATOM   1488  O   ARG A 209      84.123 176.625 310.912  1.00 56.28           O  
ANISOU 1488  O   ARG A 209     2577   9024   9782    263    405    648       O  
ATOM   1489  CB  ARG A 209      86.227 178.667 309.385  1.00 54.95           C  
ANISOU 1489  CB  ARG A 209     2426   9061   9390    109    310    370       C  
ATOM   1490  CG  ARG A 209      85.407 179.839 309.870  1.00 54.62           C  
ANISOU 1490  CG  ARG A 209     2414   9013   9327     71    332    376       C  
ATOM   1491  CD  ARG A 209      86.093 181.153 309.512  1.00 54.11           C  
ANISOU 1491  CD  ARG A 209     2362   9015   9184    -12    309    271       C  
ATOM   1492  NE  ARG A 209      86.908 181.662 310.613  1.00 67.85           N  
ANISOU 1492  NE  ARG A 209     4064  10814  10901    -43    331    313       N  
ATOM   1493  CZ  ARG A 209      86.588 182.720 311.353  1.00 68.48           C  
ANISOU 1493  CZ  ARG A 209     4146  10915  10957    -85    362    337       C  
ATOM   1494  NH1 ARG A 209      85.474 183.394 311.098  1.00 67.21           N  
ANISOU 1494  NH1 ARG A 209     4024  10712  10799   -100    377    313       N  
ATOM   1495  NH2 ARG A 209      87.387 183.110 312.342  1.00 68.72           N  
ANISOU 1495  NH2 ARG A 209     4138  11019  10952   -113    381    397       N  
ATOM   1496  N   LEU A 210      85.139 175.692 309.125  1.00 56.17           N  
ANISOU 1496  N   LEU A 210     2548   9012   9781    263    347    547       N  
ATOM   1497  CA  LEU A 210      84.008 174.833 308.794  1.00 66.82           C  
ANISOU 1497  CA  LEU A 210     3906  10214  11267    310    366    613       C  
ATOM   1498  C   LEU A 210      83.762 173.778 309.865  1.00 68.54           C  
ANISOU 1498  C   LEU A 210     4086  10359  11596    377    421    755       C  
ATOM   1499  O   LEU A 210      82.621 173.335 310.041  1.00 69.24           O  
ANISOU 1499  O   LEU A 210     4188  10320  11799    410    451    824       O  
ATOM   1500  CB  LEU A 210      84.243 174.171 307.436  1.00 66.31           C  
ANISOU 1500  CB  LEU A 210     3834  10109  11252    313    334    559       C  
ATOM   1501  CG  LEU A 210      83.898 174.920 306.144  1.00 55.67           C  
ANISOU 1501  CG  LEU A 210     2529   8773   9850    265    287    454       C  
ATOM   1502  CD1 LEU A 210      84.430 176.341 306.124  1.00 54.82           C  
ANISOU 1502  CD1 LEU A 210     2450   8802   9579    201    259    366       C  
ATOM   1503  CD2 LEU A 210      84.445 174.149 304.959  1.00 55.93           C  
ANISOU 1503  CD2 LEU A 210     2537   8795   9919    274    260    411       C  
ATOM   1504  N   ARG A 211      84.811 173.364 310.584  1.00 58.17           N  
ANISOU 1504  N   ARG A 211     2724   9121  10256    397    437    808       N  
ATOM   1505  CA  ARG A 211      84.641 172.393 311.664  1.00 82.33           C  
ANISOU 1505  CA  ARG A 211     5745  12127  13411    464    494    962       C  
ATOM   1506  C   ARG A 211      83.624 172.877 312.692  1.00 83.29           C  
ANISOU 1506  C   ARG A 211     5889  12226  13531    475    531   1032       C  
ATOM   1507  O   ARG A 211      82.845 172.082 313.232  1.00 87.09           O  
ANISOU 1507  O   ARG A 211     6359  12599  14133    531    578   1152       O  
ATOM   1508  CB  ARG A 211      85.985 172.109 312.335  1.00 59.91           C  
ANISOU 1508  CB  ARG A 211     2850   9400  10512    478    503   1011       C  
ATOM   1509  N   ALA A 212      83.617 174.181 312.976  1.00 78.90           N  
ANISOU 1509  N   ALA A 212     5360  11763  12855    423    515    969       N  
ATOM   1510  CA  ALA A 212      82.574 174.745 313.825  1.00 76.94           C  
ANISOU 1510  CA  ALA A 212     5130  11485  12619    430    551   1039       C  
ATOM   1511  C   ALA A 212      81.238 174.768 313.095  1.00 75.69           C  
ANISOU 1511  C   ALA A 212     5026  11191  12542    430    546   1005       C  
ATOM   1512  O   ALA A 212      80.211 174.348 313.641  1.00 74.24           O  
ANISOU 1512  O   ALA A 212     4848  10904  12455    474    588   1103       O  
ATOM   1513  CB  ALA A 212      82.965 176.151 314.272  1.00 58.17           C  
ANISOU 1513  CB  ALA A 212     2756   9233  10112    369    543    992       C  
ATOM   1514  N   ARG A 213      81.242 175.248 311.846  1.00 75.71           N  
ANISOU 1514  N   ARG A 213     5066  11193  12508    383    496    874       N  
ATOM   1515  CA  ARG A 213      80.019 175.367 311.060  1.00 74.76           C  
ANISOU 1515  CA  ARG A 213     4994  10954  12459    377    486    844       C  
ATOM   1516  C   ARG A 213      79.422 174.020 310.681  1.00 73.04           C  
ANISOU 1516  C   ARG A 213     4759  10572  12422    428    504    914       C  
ATOM   1517  O   ARG A 213      78.271 173.975 310.235  1.00 70.85           O  
ANISOU 1517  O   ARG A 213     4512  10170  12238    431    506    916       O  
ATOM   1518  CB  ARG A 213      80.285 176.170 309.788  1.00 55.69           C  
ANISOU 1518  CB  ARG A 213     2612   8589   9960    317    429    708       C  
ATOM   1519  CG  ARG A 213      80.476 177.642 310.026  1.00 55.04           C  
ANISOU 1519  CG  ARG A 213     2552   8612   9749    258    421    649       C  
ATOM   1520  CD  ARG A 213      80.791 178.368 308.741  1.00 54.21           C  
ANISOU 1520  CD  ARG A 213     2476   8559   9561    203    368    524       C  
ATOM   1521  NE  ARG A 213      81.068 179.774 308.999  1.00 83.23           N  
ANISOU 1521  NE  ARG A 213     6164  12324  13135    142    368    477       N  
ATOM   1522  CZ  ARG A 213      81.437 180.644 308.069  1.00 84.14           C  
ANISOU 1522  CZ  ARG A 213     6302  12501  13165     86    330    377       C  
ATOM   1523  NH1 ARG A 213      81.575 180.250 306.810  1.00 81.60           N  
ANISOU 1523  NH1 ARG A 213     5994  12176  12833     86    288    318       N  
ATOM   1524  NH2 ARG A 213      81.671 181.908 308.401  1.00 87.31           N  
ANISOU 1524  NH2 ARG A 213     6709  12969  13494     29    340    342       N  
ATOM   1525  N   GLY A 900      80.171 172.932 310.825  1.00 58.19           N  
ANISOU 1525  N   GLY A 900     2827   8681  10601    465    519    968       N  
ATOM   1526  CA  GLY A 900      79.663 171.628 310.452  1.00 59.00           C  
ANISOU 1526  CA  GLY A 900     2906   8619  10892    508    542   1027       C  
ATOM   1527  C   GLY A 900      79.553 171.459 308.950  1.00 79.44           C  
ANISOU 1527  C   GLY A 900     5508  11147  13527    479    497    918       C  
ATOM   1528  O   GLY A 900      79.244 172.415 308.232  1.00 77.28           O  
ANISOU 1528  O   GLY A 900     5279  10911  13173    433    456    822       O  
ATOM   1529  N   SER A 901      79.802 170.250 308.460  1.00 82.04           N  
ANISOU 1529  N   SER A 901     5797  11385  13989    507    508    932       N  
ATOM   1530  CA  SER A 901      79.780 170.015 307.024  1.00 81.81           C  
ANISOU 1530  CA  SER A 901     5771  11308  14004    481    467    824       C  
ATOM   1531  C   SER A 901      78.353 170.092 306.490  1.00 82.27           C  
ANISOU 1531  C   SER A 901     5864  11225  14171    468    462    799       C  
ATOM   1532  O   SER A 901      77.383 169.789 307.192  1.00 79.67           O  
ANISOU 1532  O   SER A 901     5538  10781  13953    495    504    884       O  
ATOM   1533  CB  SER A 901      80.401 168.656 306.694  1.00 84.82           C  
ANISOU 1533  CB  SER A 901     6094  11618  14514    514    488    845       C  
ATOM   1534  OG  SER A 901      80.599 168.498 305.299  1.00 84.17           O  
ANISOU 1534  OG  SER A 901     6009  11524  14447    487    444    729       O  
ATOM   1535  N   GLY A 902      78.235 170.506 305.228  1.00 81.87           N  
ANISOU 1535  N   GLY A 902     5834  11189  14084    428    410    683       N  
ATOM   1536  CA  GLY A 902      76.947 170.705 304.601  1.00 84.48           C  
ANISOU 1536  CA  GLY A 902     6195  11409  14496    410    397    643       C  
ATOM   1537  C   GLY A 902      76.166 171.799 305.315  1.00 85.40           C  
ANISOU 1537  C   GLY A 902     6360  11552  14536    399    405    680       C  
ATOM   1538  O   GLY A 902      76.702 172.599 306.086  1.00 90.32           O  
ANISOU 1538  O   GLY A 902     7000  12302  15016    393    410    706       O  
ATOM   1539  N   SER A 903      74.867 171.823 305.036  1.00 80.62           N  
ANISOU 1539  N   SER A 903     5775  10822  14034    396    408    678       N  
ATOM   1540  CA  SER A 903      73.945 172.689 305.754  1.00 72.38           C  
ANISOU 1540  CA  SER A 903     4774   9769  12957    394    428    728       C  
ATOM   1541  C   SER A 903      73.340 172.002 306.976  1.00 73.02           C  
ANISOU 1541  C   SER A 903     4840   9740  13164    440    492    858       C  
ATOM   1542  O   SER A 903      72.401 172.541 307.573  1.00 71.18           O  
ANISOU 1542  O   SER A 903     4638   9470  12939    446    515    910       O  
ATOM   1543  CB  SER A 903      72.832 173.165 304.816  1.00 68.46           C  
ANISOU 1543  CB  SER A 903     4307   9206  12497    366    398    662       C  
ATOM   1544  OG  SER A 903      72.644 174.566 304.908  1.00 64.64           O  
ANISOU 1544  OG  SER A 903     3873   8821  11866    338    383    642       O  
ATOM   1545  N   ASN A1002      73.875 170.838 307.366  1.00 72.42           N  
ANISOU 1545  N   ASN A1002     4714   9615  13186    476    525    920       N  
ATOM   1546  CA  ASN A1002      73.226 169.997 308.370  1.00 75.67           C  
ANISOU 1546  CA  ASN A1002     5104   9897  13751    523    590   1051       C  
ATOM   1547  C   ASN A1002      72.981 170.736 309.680  1.00 77.53           C  
ANISOU 1547  C   ASN A1002     5363  10200  13893    542    625   1148       C  
ATOM   1548  O   ASN A1002      71.977 170.480 310.355  1.00 83.16           O  
ANISOU 1548  O   ASN A1002     6080  10803  14714    569    671   1242       O  
ATOM   1549  CB  ASN A1002      74.063 168.743 308.631  1.00 75.87           C  
ANISOU 1549  CB  ASN A1002     5070   9888  13871    559    623   1109       C  
ATOM   1550  CG  ASN A1002      74.153 167.833 307.418  1.00 79.10           C  
ANISOU 1550  CG  ASN A1002     5445  10196  14412    546    601   1022       C  
ATOM   1551  OD1 ASN A1002      74.122 168.293 306.273  1.00 81.57           O  
ANISOU 1551  OD1 ASN A1002     5777  10540  14674    505    545    895       O  
ATOM   1552  ND2 ASN A1002      74.263 166.532 307.664  1.00 79.35           N  
ANISOU 1552  ND2 ASN A1002     5424  10105  14619    581    650   1090       N  
ATOM   1553  N   ILE A1003      73.877 171.647 310.064  1.00 74.83           N  
ANISOU 1553  N   ILE A1003     5035  10039  13357    527    607   1123       N  
ATOM   1554  CA  ILE A1003      73.703 172.324 311.344  1.00 72.49           C  
ANISOU 1554  CA  ILE A1003     4754   9816  12973    544    644   1206       C  
ATOM   1555  C   ILE A1003      72.574 173.342 311.260  1.00 70.00           C  
ANISOU 1555  C   ILE A1003     4491   9472  12632    520    639   1180       C  
ATOM   1556  O   ILE A1003      71.921 173.637 312.269  1.00 58.22           O  
ANISOU 1556  O   ILE A1003     3013   7967  11142    544    683   1267       O  
ATOM   1557  CB  ILE A1003      75.029 172.969 311.790  1.00 74.15           C  
ANISOU 1557  CB  ILE A1003     4953  10228  12994    529    628   1175       C  
ATOM   1558  CG1 ILE A1003      75.051 173.175 313.307  1.00 58.81           C  
ANISOU 1558  CG1 ILE A1003     2997   8353  10995    563    680   1287       C  
ATOM   1559  CG2 ILE A1003      75.271 174.282 311.055  1.00 74.73           C  
ANISOU 1559  CG2 ILE A1003     5068  10412  12913    467    574   1043       C  
ATOM   1560  CD1 ILE A1003      74.521 174.514 313.770  1.00 58.10           C  
ANISOU 1560  CD1 ILE A1003     2947   8330  10797    537    684   1265       C  
ATOM   1561  N   PHE A1004      72.305 173.871 310.063  1.00 57.39           N  
ANISOU 1561  N   PHE A1004     2925   7865  11015    476    589   1067       N  
ATOM   1562  CA  PHE A1004      71.310 174.929 309.912  1.00 56.69           C  
ANISOU 1562  CA  PHE A1004     2887   7762  10892    453    583   1040       C  
ATOM   1563  C   PHE A1004      69.899 174.387 310.096  1.00 57.25           C  
ANISOU 1563  C   PHE A1004     2962   7653  11136    480    618   1115       C  
ATOM   1564  O   PHE A1004      69.148 174.857 310.959  1.00 83.19           O  
ANISOU 1564  O   PHE A1004     6269  10920  14419    498    658   1189       O  
ATOM   1565  CB  PHE A1004      71.458 175.593 308.542  1.00 55.92           C  
ANISOU 1565  CB  PHE A1004     2814   7709  10725    402    521    908       C  
ATOM   1566  CG  PHE A1004      70.454 176.686 308.278  1.00 75.00           C  
ANISOU 1566  CG  PHE A1004     5278  10108  13110    378    515    882       C  
ATOM   1567  CD1 PHE A1004      70.016 177.515 309.297  1.00 72.78           C  
ANISOU 1567  CD1 PHE A1004     5024   9859  12770    385    555    939       C  
ATOM   1568  CD2 PHE A1004      69.945 176.881 307.003  1.00 76.57           C  
ANISOU 1568  CD2 PHE A1004     5491  10263  13338    350    472    802       C  
ATOM   1569  CE1 PHE A1004      69.095 178.519 309.046  1.00 54.44           C  
ANISOU 1569  CE1 PHE A1004     2744   7516  10426    366    555    919       C  
ATOM   1570  CE2 PHE A1004      69.021 177.883 306.750  1.00 75.64           C  
ANISOU 1570  CE2 PHE A1004     5414  10131  13194    331    470    786       C  
ATOM   1571  CZ  PHE A1004      68.596 178.701 307.775  1.00 74.21           C  
ANISOU 1571  CZ  PHE A1004     5262   9972  12962    340    513    847       C  
ATOM   1572  N   GLU A1005      69.515 173.401 309.281  1.00 57.81           N  
ANISOU 1572  N   GLU A1005     3009   7591  11364    482    606   1094       N  
ATOM   1573  CA  GLU A1005      68.160 172.864 309.364  1.00 58.40           C  
ANISOU 1573  CA  GLU A1005     3082   7489  11617    500    636   1154       C  
ATOM   1574  C   GLU A1005      67.857 172.334 310.758  1.00 68.68           C  
ANISOU 1574  C   GLU A1005     4367   8737  12991    551    707   1306       C  
ATOM   1575  O   GLU A1005      66.723 172.451 311.237  1.00 69.42           O  
ANISOU 1575  O   GLU A1005     4477   8738  13160    566    743   1377       O  
ATOM   1576  CB  GLU A1005      67.973 171.767 308.323  1.00 83.47           C  
ANISOU 1576  CB  GLU A1005     6219  10538  14956    492    615   1097       C  
ATOM   1577  CG  GLU A1005      68.521 172.145 306.972  1.00 83.88           C  
ANISOU 1577  CG  GLU A1005     6277  10670  14925    448    546    951       C  
ATOM   1578  CD  GLU A1005      67.461 172.110 305.902  1.00 87.41           C  
ANISOU 1578  CD  GLU A1005     6726  11017  15470    423    515    878       C  
ATOM   1579  OE1 GLU A1005      66.716 171.108 305.842  1.00 89.72           O  
ANISOU 1579  OE1 GLU A1005     6984  11149  15955    436    538    904       O  
ATOM   1580  OE2 GLU A1005      67.366 173.088 305.131  1.00 87.47           O  
ANISOU 1580  OE2 GLU A1005     6763  11107  15365    390    470    795       O  
ATOM   1581  N   MET A1006      68.859 171.752 311.424  1.00 59.65           N  
ANISOU 1581  N   MET A1006     3189   7654  11823    579    731   1364       N  
ATOM   1582  CA  MET A1006      68.694 171.338 312.815  1.00 60.41           C  
ANISOU 1582  CA  MET A1006     3265   7730  11957    631    800   1518       C  
ATOM   1583  C   MET A1006      68.275 172.512 313.679  1.00 59.82           C  
ANISOU 1583  C   MET A1006     3230   7744  11753    635    820   1555       C  
ATOM   1584  O   MET A1006      67.359 172.402 314.500  1.00 60.28           O  
ANISOU 1584  O   MET A1006     3293   7726  11884    668    873   1665       O  
ATOM   1585  CB  MET A1006      69.991 170.734 313.355  1.00 90.67           C  
ANISOU 1585  CB  MET A1006     7052  11655  15742    658    815   1565       C  
ATOM   1586  CG  MET A1006      70.236 170.997 314.853  1.00 90.80           C  
ANISOU 1586  CG  MET A1006     7060  11775  15666    701    867   1688       C  
ATOM   1587  SD  MET A1006      71.774 170.276 315.480  1.00 90.41           S  
ANISOU 1587  SD  MET A1006     6949  11844  15558    735    884   1750       S  
ATOM   1588  CE  MET A1006      71.912 171.016 317.094  1.00 62.09           C  
ANISOU 1588  CE  MET A1006     3361   8414  11816    769    928   1854       C  
ATOM   1589  N   LEU A1007      68.940 173.651 313.506  1.00 58.84           N  
ANISOU 1589  N   LEU A1007     3134   7782  11442    601    782   1462       N  
ATOM   1590  CA  LEU A1007      68.612 174.813 314.317  1.00 70.87           C  
ANISOU 1590  CA  LEU A1007     4689   9393  12847    600    805   1485       C  
ATOM   1591  C   LEU A1007      67.294 175.444 313.886  1.00 71.39           C  
ANISOU 1591  C   LEU A1007     4799   9359  12966    583    804   1466       C  
ATOM   1592  O   LEU A1007      66.596 176.039 314.716  1.00 72.96           O  
ANISOU 1592  O   LEU A1007     5012   9547  13161    602    851   1545       O  
ATOM   1593  CB  LEU A1007      69.752 175.829 314.258  1.00 69.07           C  
ANISOU 1593  CB  LEU A1007     4460   9345  12437    562    774   1403       C  
ATOM   1594  CG  LEU A1007      70.612 175.897 315.519  1.00 68.38           C  
ANISOU 1594  CG  LEU A1007     4333   9387  12263    588    812   1485       C  
ATOM   1595  CD1 LEU A1007      69.818 176.523 316.648  1.00 58.57           C  
ANISOU 1595  CD1 LEU A1007     3096   8144  11014    615    874   1588       C  
ATOM   1596  CD2 LEU A1007      71.095 174.511 315.916  1.00 59.20           C  
ANISOU 1596  CD2 LEU A1007     3123   8193  11177    635    833   1569       C  
ATOM   1597  N   ARG A1008      66.928 175.319 312.607  1.00 69.22           N  
ANISOU 1597  N   ARG A1008     4538   9006  12756    551    757   1376       N  
ATOM   1598  CA  ARG A1008      65.667 175.896 312.148  1.00 67.20           C  
ANISOU 1598  CA  ARG A1008     4320   8660  12552    535    754   1359       C  
ATOM   1599  C   ARG A1008      64.484 175.272 312.873  1.00 67.38           C  
ANISOU 1599  C   ARG A1008     4336   8534  12732    577    812   1486       C  
ATOM   1600  O   ARG A1008      63.621 175.980 313.403  1.00 66.75           O  
ANISOU 1600  O   ARG A1008     4287   8439  12637    587    845   1534       O  
ATOM   1601  CB  ARG A1008      65.515 175.721 310.638  1.00 57.03           C  
ANISOU 1601  CB  ARG A1008     3032   7317  11320    497    694   1247       C  
ATOM   1602  CG  ARG A1008      64.065 175.791 310.194  1.00 57.14           C  
ANISOU 1602  CG  ARG A1008     3063   7194  11455    494    698   1257       C  
ATOM   1603  CD  ARG A1008      63.833 175.015 308.922  1.00 79.11           C  
ANISOU 1603  CD  ARG A1008     5818   9884  14357    472    653   1178       C  
ATOM   1604  NE  ARG A1008      64.218 175.782 307.744  1.00 77.51           N  
ANISOU 1604  NE  ARG A1008     5632   9776  14043    428    590   1050       N  
ATOM   1605  CZ  ARG A1008      64.069 175.355 306.494  1.00 77.96           C  
ANISOU 1605  CZ  ARG A1008     5666   9791  14165    404    542    958       C  
ATOM   1606  NH1 ARG A1008      63.544 174.160 306.259  1.00 80.70           N  
ANISOU 1606  NH1 ARG A1008     5971   9996  14696    414    549    970       N  
ATOM   1607  NH2 ARG A1008      64.445 176.123 305.479  1.00 75.37           N  
ANISOU 1607  NH2 ARG A1008     5353   9566  13720    368    489    854       N  
ATOM   1608  N   ILE A1009      64.437 173.936 312.907  1.00 67.68           N  
ANISOU 1608  N   ILE A1009     4330   8457  12927    601    830   1544       N  
ATOM   1609  CA  ILE A1009      63.409 173.194 313.637  1.00 59.96           C  
ANISOU 1609  CA  ILE A1009     3337   7332  12113    640    891   1678       C  
ATOM   1610  C   ILE A1009      63.275 173.697 315.069  1.00 78.16           C  
ANISOU 1610  C   ILE A1009     5655   9707  14334    681    952   1795       C  
ATOM   1611  O   ILE A1009      62.180 173.691 315.645  1.00 78.89           O  
ANISOU 1611  O   ILE A1009     5757   9707  14509    706    999   1890       O  
ATOM   1612  CB  ILE A1009      63.735 171.683 313.604  1.00 61.07           C  
ANISOU 1612  CB  ILE A1009     3420   7368  12415    660    909   1727       C  
ATOM   1613  CG1 ILE A1009      63.611 171.112 312.192  1.00 61.16           C  
ANISOU 1613  CG1 ILE A1009     3413   7283  12541    621    857   1610       C  
ATOM   1614  CG2 ILE A1009      62.843 170.899 314.549  1.00 62.15           C  
ANISOU 1614  CG2 ILE A1009     3535   7368  12711    705    984   1887       C  
ATOM   1615  CD1 ILE A1009      63.811 169.600 312.130  1.00 62.36           C  
ANISOU 1615  CD1 ILE A1009     3506   7308  12881    639    883   1654       C  
ATOM   1616  N   ASP A1010      64.373 174.169 315.654  1.00 77.96           N  
ANISOU 1616  N   ASP A1010     5626   9853  14142    688    950   1784       N  
ATOM   1617  CA  ASP A1010      64.470 174.380 317.092  1.00 79.15           C  
ANISOU 1617  CA  ASP A1010     5762  10074  14238    734   1015   1914       C  
ATOM   1618  C   ASP A1010      64.242 175.833 317.502  1.00 79.62           C  
ANISOU 1618  C   ASP A1010     5851  10224  14176    722   1029   1904       C  
ATOM   1619  O   ASP A1010      63.325 176.126 318.276  1.00 60.05           O  
ANISOU 1619  O   ASP A1010     3384   7700  11733    753   1086   2004       O  
ATOM   1620  CB  ASP A1010      65.843 173.872 317.545  1.00 60.67           C  
ANISOU 1620  CB  ASP A1010     3376   7853  11823    751   1014   1933       C  
ATOM   1621  CG  ASP A1010      65.967 172.376 317.398  1.00 61.56           C  
ANISOU 1621  CG  ASP A1010     3449   7855  12086    776   1026   1988       C  
ATOM   1622  OD1 ASP A1010      65.334 171.841 316.467  1.00 76.40           O  
ANISOU 1622  OD1 ASP A1010     5330   9580  14117    755   1007   1951       O  
ATOM   1623  OD2 ASP A1010      66.673 171.738 318.205  1.00 62.34           O  
ANISOU 1623  OD2 ASP A1010     3505   8009  12173    817   1061   2082       O  
ATOM   1624  N   GLU A1011      65.072 176.748 317.009  1.00 78.56           N  
ANISOU 1624  N   GLU A1011     5728  10217  13903    678    985   1788       N  
ATOM   1625  CA  GLU A1011      64.954 178.156 317.360  1.00 76.98           C  
ANISOU 1625  CA  GLU A1011     5550  10104  13593    660   1004   1770       C  
ATOM   1626  C   GLU A1011      63.969 178.902 316.474  1.00 57.76           C  
ANISOU 1626  C   GLU A1011     3166   7583  11198    627    984   1705       C  
ATOM   1627  O   GLU A1011      63.717 180.087 316.714  1.00 57.44           O  
ANISOU 1627  O   GLU A1011     3146   7589  11088    613   1008   1697       O  
ATOM   1628  CB  GLU A1011      66.325 178.842 317.290  1.00 78.20           C  
ANISOU 1628  CB  GLU A1011     5688  10437  13587    622    973   1681       C  
ATOM   1629  CG  GLU A1011      67.313 178.438 318.384  1.00 80.58           C  
ANISOU 1629  CG  GLU A1011     5936  10863  13817    654   1003   1755       C  
ATOM   1630  CD  GLU A1011      67.320 179.391 319.578  1.00 84.47           C  
ANISOU 1630  CD  GLU A1011     6412  11471  14212    668   1064   1817       C  
ATOM   1631  OE1 GLU A1011      67.160 180.615 319.374  1.00 85.96           O  
ANISOU 1631  OE1 GLU A1011     6625  11699  14335    627   1066   1749       O  
ATOM   1632  OE2 GLU A1011      67.495 178.914 320.723  1.00 86.94           O  
ANISOU 1632  OE2 GLU A1011     6683  11836  14513    720   1113   1936       O  
ATOM   1633  N   GLY A1012      63.411 178.246 315.462  1.00 57.63           N  
ANISOU 1633  N   GLY A1012     3163   7444  11290    614    944   1661       N  
ATOM   1634  CA  GLY A1012      62.450 178.895 314.598  1.00 57.09           C  
ANISOU 1634  CA  GLY A1012     3134   7299  11258    586    923   1606       C  
ATOM   1635  C   GLY A1012      63.094 179.791 313.565  1.00 56.20           C  
ANISOU 1635  C   GLY A1012     3040   7278  11034    530    865   1469       C  
ATOM   1636  O   GLY A1012      63.918 180.653 313.887  1.00 55.89           O  
ANISOU 1636  O   GLY A1012     2999   7368  10868    512    871   1439       O  
ATOM   1637  N   LEU A1013      62.713 179.590 312.313  1.00 55.86           N  
ANISOU 1637  N   LEU A1013     3010   7173  11041    503    812   1386       N  
ATOM   1638  CA  LEU A1013      63.235 180.351 311.188  1.00 69.43           C  
ANISOU 1638  CA  LEU A1013     4746   8972  12664    453    754   1260       C  
ATOM   1639  C   LEU A1013      62.215 181.416 310.795  1.00 71.97           C  
ANISOU 1639  C   LEU A1013     5103   9250  12994    439    764   1255       C  
ATOM   1640  O   LEU A1013      61.156 181.095 310.244  1.00 74.07           O  
ANISOU 1640  O   LEU A1013     5375   9406  13361    444    754   1261       O  
ATOM   1641  CB  LEU A1013      63.531 179.417 310.018  1.00 67.53           C  
ANISOU 1641  CB  LEU A1013     4488   8709  12461    436    690   1171       C  
ATOM   1642  CG  LEU A1013      63.820 180.072 308.669  1.00 65.48           C  
ANISOU 1642  CG  LEU A1013     4243   8514  12121    389    628   1047       C  
ATOM   1643  CD1 LEU A1013      65.214 180.690 308.646  1.00 53.90           C  
ANISOU 1643  CD1 LEU A1013     2774   7202  10502    360    608    987       C  
ATOM   1644  CD2 LEU A1013      63.641 179.063 307.544  1.00 65.58           C  
ANISOU 1644  CD2 LEU A1013     4226   8453  12237    381    579    990       C  
ATOM   1645  N   ARG A1014      62.531 182.678 311.076  1.00 71.09           N  
ANISOU 1645  N   ARG A1014     5009   9222  12780    420    787   1245       N  
ATOM   1646  CA  ARG A1014      61.718 183.810 310.649  1.00 53.98           C  
ANISOU 1646  CA  ARG A1014     2874   7025  10612    405    800   1237       C  
ATOM   1647  C   ARG A1014      62.571 184.755 309.815  1.00 82.33           C  
ANISOU 1647  C   ARG A1014     6473  10726  14084    354    761   1133       C  
ATOM   1648  O   ARG A1014      63.726 185.022 310.158  1.00 82.40           O  
ANISOU 1648  O   ARG A1014     6468  10847  13992    334    761   1101       O  
ATOM   1649  CB  ARG A1014      61.127 184.554 311.849  1.00 54.28           C  
ANISOU 1649  CB  ARG A1014     2924   7039  10660    432    885   1339       C  
ATOM   1650  N   LEU A1015      62.005 185.265 308.718  1.00 53.00           N  
ANISOU 1650  N   LEU A1015     2776   6983  10378    334    731   1084       N  
ATOM   1651  CA  LEU A1015      62.750 186.100 307.780  1.00 52.44           C  
ANISOU 1651  CA  LEU A1015     2711   7011  10202    287    692    989       C  
ATOM   1652  C   LEU A1015      62.397 187.581 307.892  1.00 52.25           C  
ANISOU 1652  C   LEU A1015     2711   6992  10149    272    741   1010       C  
ATOM   1653  O   LEU A1015      62.685 188.353 306.971  1.00 51.86           O  
ANISOU 1653  O   LEU A1015     2669   6996  10039    237    715    946       O  
ATOM   1654  CB  LEU A1015      62.526 185.623 306.346  1.00 52.28           C  
ANISOU 1654  CB  LEU A1015     2684   6982  10197    274    620    911       C  
ATOM   1655  CG  LEU A1015      62.667 184.123 306.101  1.00 52.60           C  
ANISOU 1655  CG  LEU A1015     2698   6993  10295    290    578    889       C  
ATOM   1656  CD1 LEU A1015      62.588 183.809 304.612  1.00 62.13           C  
ANISOU 1656  CD1 LEU A1015     3890   8222  11493    270    508    796       C  
ATOM   1657  CD2 LEU A1015      63.957 183.605 306.689  1.00 52.63           C  
ANISOU 1657  CD2 LEU A1015     2683   7075  10238    287    574    877       C  
ATOM   1658  N   LYS A1016      61.778 187.994 308.996  1.00 52.58           N  
ANISOU 1658  N   LYS A1016     2764   6980  10235    298    819   1102       N  
ATOM   1659  CA  LYS A1016      61.440 189.391 309.219  1.00 52.53           C  
ANISOU 1659  CA  LYS A1016     2778   6969  10212    287    882   1129       C  
ATOM   1660  C   LYS A1016      61.753 189.752 310.660  1.00 68.48           C  
ANISOU 1660  C   LYS A1016     4789   9022  12207    297    961   1189       C  
ATOM   1661  O   LYS A1016      61.781 188.887 311.539  1.00 69.99           O  
ANISOU 1661  O   LYS A1016     4964   9205  12423    331    974   1241       O  
ATOM   1662  CB  LYS A1016      59.965 189.684 308.921  1.00 52.69           C  
ANISOU 1662  CB  LYS A1016     2820   6869  10331    315    908   1190       C  
ATOM   1663  N   ILE A1017      61.988 191.044 310.892  1.00 66.95           N  
ANISOU 1663  N   ILE A1017     4604   8869  11965    268   1019   1180       N  
ATOM   1664  CA  ILE A1017      62.315 191.513 312.232  1.00 65.54           C  
ANISOU 1664  CA  ILE A1017     4412   8741  11751    271   1102   1223       C  
ATOM   1665  C   ILE A1017      61.139 191.237 313.159  1.00 53.86           C  
ANISOU 1665  C   ILE A1017     2941   7161  10362    333   1168   1337       C  
ATOM   1666  O   ILE A1017      59.983 191.505 312.814  1.00 70.76           O  
ANISOU 1666  O   ILE A1017     5110   9190  12585    358   1189   1384       O  
ATOM   1667  CB  ILE A1017      62.666 193.008 312.201  1.00 63.22           C  
ANISOU 1667  CB  ILE A1017     4125   8492  11404    222   1163   1186       C  
ATOM   1668  CG1 ILE A1017      64.005 193.256 311.489  1.00 61.07           C  
ANISOU 1668  CG1 ILE A1017     3836   8337  11030    156   1105   1079       C  
ATOM   1669  CG2 ILE A1017      62.711 193.563 313.605  1.00 53.92           C  
ANISOU 1669  CG2 ILE A1017     2932   7350  10205    228   1269   1235       C  
ATOM   1670  CD1 ILE A1017      63.926 193.338 309.971  1.00 52.31           C  
ANISOU 1670  CD1 ILE A1017     2746   7203   9925    137   1031   1023       C  
ATOM   1671  N   TYR A1018      61.418 190.686 314.338  1.00 54.35           N  
ANISOU 1671  N   TYR A1018     2976   7267  10408    362   1202   1389       N  
ATOM   1672  CA  TYR A1018      60.366 190.439 315.325  1.00 81.28           C  
ANISOU 1672  CA  TYR A1018     6392  10596  13895    424   1272   1505       C  
ATOM   1673  C   TYR A1018      60.906 190.789 316.711  1.00 81.71           C  
ANISOU 1673  C   TYR A1018     6414  10754  13877    432   1354   1539       C  
ATOM   1674  O   TYR A1018      61.968 191.408 316.849  1.00 81.60           O  
ANISOU 1674  O   TYR A1018     6376  10865  13762    381   1364   1468       O  
ATOM   1675  CB  TYR A1018      59.842 188.998 315.228  1.00 81.07           C  
ANISOU 1675  CB  TYR A1018     6362  10488  13954    468   1221   1557       C  
ATOM   1676  CG  TYR A1018      60.852 187.901 315.526  1.00 80.42           C  
ANISOU 1676  CG  TYR A1018     6242  10487  13828    470   1173   1540       C  
ATOM   1677  CD1 TYR A1018      61.565 187.284 314.501  1.00 79.34           C  
ANISOU 1677  CD1 TYR A1018     6099  10378  13670    437   1081   1450       C  
ATOM   1678  CD2 TYR A1018      61.064 187.461 316.827  1.00 55.87           C  
ANISOU 1678  CD2 TYR A1018     3101   7427  10701    510   1224   1620       C  
ATOM   1679  CE1 TYR A1018      62.474 186.278 314.769  1.00 54.89           C  
ANISOU 1679  CE1 TYR A1018     2968   7347  10541    444   1045   1440       C  
ATOM   1680  CE2 TYR A1018      61.967 186.459 317.102  1.00 56.07           C  
ANISOU 1680  CE2 TYR A1018     3089   7524  10691    517   1185   1616       C  
ATOM   1681  CZ  TYR A1018      62.669 185.871 316.073  1.00 55.57           C  
ANISOU 1681  CZ  TYR A1018     3023   7477  10615    483   1097   1526       C  
ATOM   1682  OH  TYR A1018      63.569 184.871 316.358  1.00 55.83           O  
ANISOU 1682  OH  TYR A1018     3019   7575  10620    494   1066   1527       O  
ATOM   1683  N   LYS A1019      60.160 190.429 317.754  1.00 56.22           N  
ANISOU 1683  N   LYS A1019     3181   7483  10697    494   1417   1649       N  
ATOM   1684  CA  LYS A1019      60.594 190.658 319.124  1.00 56.96           C  
ANISOU 1684  CA  LYS A1019     3237   7688  10717    511   1498   1690       C  
ATOM   1685  C   LYS A1019      60.918 189.322 319.782  1.00 76.46           C  
ANISOU 1685  C   LYS A1019     5670  10197  13186    556   1467   1753       C  
ATOM   1686  O   LYS A1019      60.144 188.365 319.677  1.00 57.46           O  
ANISOU 1686  O   LYS A1019     3277   7677  10878    602   1442   1825       O  
ATOM   1687  CB  LYS A1019      59.538 191.422 319.922  1.00 72.87           C  
ANISOU 1687  CB  LYS A1019     5273   9643  12772    552   1613   1772       C  
ATOM   1688  CG  LYS A1019      59.487 192.915 319.601  1.00 71.93           C  
ANISOU 1688  CG  LYS A1019     5179   9522  12629    504   1677   1709       C  
ATOM   1689  CD  LYS A1019      58.863 193.701 320.754  1.00 71.97           C  
ANISOU 1689  CD  LYS A1019     5188   9528  12629    540   1816   1774       C  
ATOM   1690  CE  LYS A1019      58.957 195.205 320.544  1.00 70.53           C  
ANISOU 1690  CE  LYS A1019     5029   9350  12419    485   1900   1703       C  
ATOM   1691  NZ  LYS A1019      60.365 195.684 320.555  1.00 69.22           N  
ANISOU 1691  NZ  LYS A1019     4825   9342  12135    403   1895   1590       N  
ATOM   1692  N   ASP A1020      62.066 189.262 320.451  1.00 77.08           N  
ANISOU 1692  N   ASP A1020     5698  10436  13154    539   1473   1727       N  
ATOM   1693  CA  ASP A1020      62.561 188.019 321.024  1.00 78.15           C  
ANISOU 1693  CA  ASP A1020     5792  10625  13278    578   1443   1783       C  
ATOM   1694  C   ASP A1020      61.685 187.581 322.196  1.00 79.06           C  
ANISOU 1694  C   ASP A1020     5898  10702  13441    659   1518   1928       C  
ATOM   1695  O   ASP A1020      60.703 188.236 322.561  1.00 77.98           O  
ANISOU 1695  O   ASP A1020     5787  10499  13342    685   1593   1979       O  
ATOM   1696  CB  ASP A1020      64.016 188.183 321.463  1.00 58.40           C  
ANISOU 1696  CB  ASP A1020     3233   8318  10637    537   1435   1722       C  
ATOM   1697  N   THR A1021      62.057 186.445 322.795  1.00 80.24           N  
ANISOU 1697  N   THR A1021     6009  10892  13587    703   1502   2000       N  
ATOM   1698  CA  THR A1021      61.321 185.938 323.948  1.00 80.59           C  
ANISOU 1698  CA  THR A1021     6038  10913  13669    783   1572   2149       C  
ATOM   1699  C   THR A1021      61.327 186.947 325.091  1.00 79.86           C  
ANISOU 1699  C   THR A1021     5920  10948  13476    799   1676   2177       C  
ATOM   1700  O   THR A1021      60.311 187.128 325.774  1.00 61.82           O  
ANISOU 1700  O   THR A1021     3650   8605  11234    854   1754   2274       O  
ATOM   1701  CB  THR A1021      61.914 184.604 324.402  1.00 61.09           C  
ANISOU 1701  CB  THR A1021     3524   8486  11200    823   1541   2220       C  
ATOM   1702  N   GLU A1022      62.457 187.627 325.296  1.00 76.93           N  
ANISOU 1702  N   GLU A1022     5135  11518  12577   1523    402    117       N  
ATOM   1703  CA  GLU A1022      62.605 188.655 326.317  1.00 77.29           C  
ANISOU 1703  CA  GLU A1022     5145  11500  12721   1617    410     94       C  
ATOM   1704  C   GLU A1022      62.209 190.044 325.819  1.00 62.04           C  
ANISOU 1704  C   GLU A1022     3189   9491  10893   1701    437    117       C  
ATOM   1705  O   GLU A1022      62.558 191.045 326.457  1.00 64.78           O  
ANISOU 1705  O   GLU A1022     3517   9731  11364   1774    441    101       O  
ATOM   1706  CB  GLU A1022      64.046 188.676 326.835  1.00 60.80           C  
ANISOU 1706  CB  GLU A1022     3091   9277  10735   1584    377     95       C  
ATOM   1707  N   GLY A1023      61.499 190.127 324.696  1.00 61.95           N  
ANISOU 1707  N   GLY A1023     3176   9518  10845   1691    454    152       N  
ATOM   1708  CA  GLY A1023      61.078 191.405 324.156  1.00 73.33           C  
ANISOU 1708  CA  GLY A1023     4593  10891  12378   1768    481    182       C  
ATOM   1709  C   GLY A1023      62.222 192.245 323.626  1.00 74.38           C  
ANISOU 1709  C   GLY A1023     4760  10840  12662   1762    469    231       C  
ATOM   1710  O   GLY A1023      62.496 193.332 324.144  1.00 75.37           O  
ANISOU 1710  O   GLY A1023     4865  10854  12918   1836    476    218       O  
ATOM   1711  N   TYR A1024      62.895 191.749 322.590  1.00 77.01           N  
ANISOU 1711  N   TYR A1024     5142  11132  12987   1673    453    285       N  
ATOM   1712  CA  TYR A1024      64.022 192.449 321.991  1.00 80.67           C  
ANISOU 1712  CA  TYR A1024     5637  11423  13591   1655    442    336       C  
ATOM   1713  C   TYR A1024      64.079 192.104 320.509  1.00 89.83           C  
ANISOU 1713  C   TYR A1024     6832  12586  14712   1591    446    408       C  
ATOM   1714  O   TYR A1024      63.567 191.070 320.075  1.00 93.51           O  
ANISOU 1714  O   TYR A1024     7313  13171  15047   1538    446    409       O  
ATOM   1715  CB  TYR A1024      65.342 192.095 322.685  1.00 77.62           C  
ANISOU 1715  CB  TYR A1024     5281  10942  13268   1605    405    312       C  
ATOM   1716  N   TYR A1025      64.719 192.980 319.735  1.00 90.89           N  
ANISOU 1716  N   TYR A1025     6980  12583  14971   1596    451    468       N  
ATOM   1717  CA  TYR A1025      64.729 192.862 318.280  1.00 89.70           C  
ANISOU 1717  CA  TYR A1025     6857  12426  14800   1553    462    546       C  
ATOM   1718  C   TYR A1025      65.674 191.755 317.825  1.00 85.17           C  
ANISOU 1718  C   TYR A1025     6342  11843  14176   1455    439    567       C  
ATOM   1719  O   TYR A1025      66.870 191.780 318.138  1.00 84.26           O  
ANISOU 1719  O   TYR A1025     6252  11619  14143   1425    417    568       O  
ATOM   1720  CB  TYR A1025      65.129 194.194 317.646  1.00 62.20           C  
ANISOU 1720  CB  TYR A1025     3366   8796  11473   1593    476    607       C  
ATOM   1721  CG  TYR A1025      63.989 195.176 317.567  1.00 77.40           C  
ANISOU 1721  CG  TYR A1025     5238  10748  13421   1683    508    612       C  
ATOM   1722  CD1 TYR A1025      63.232 195.290 316.413  1.00 77.11           C  
ANISOU 1722  CD1 TYR A1025     5195  10764  13339   1686    532    672       C  
ATOM   1723  CD2 TYR A1025      63.656 195.976 318.649  1.00 79.66           C  
ANISOU 1723  CD2 TYR A1025     5482  11008  13776   1769    516    556       C  
ATOM   1724  CE1 TYR A1025      62.179 196.182 316.329  1.00 78.70           C  
ANISOU 1724  CE1 TYR A1025     5348  10991  13564   1769    562    681       C  
ATOM   1725  CE2 TYR A1025      62.602 196.869 318.577  1.00 80.96           C  
ANISOU 1725  CE2 TYR A1025     5601  11198  13961   1858    548    561       C  
ATOM   1726  CZ  TYR A1025      61.868 196.970 317.412  1.00 80.33           C  
ANISOU 1726  CZ  TYR A1025     5514  11172  13836   1856    571    625       C  
ATOM   1727  OH  TYR A1025      60.819 197.855 317.324  1.00 81.25           O  
ANISOU 1727  OH  TYR A1025     5584  11313  13976   1944    603    634       O  
ATOM   1728  N   THR A1026      65.139 190.787 317.079  1.00 83.76           N  
ANISOU 1728  N   THR A1026     6183  11772  13871   1406    444    583       N  
ATOM   1729  CA  THR A1026      65.948 189.760 316.434  1.00 82.09           C  
ANISOU 1729  CA  THR A1026     6029  11551  13612   1320    429    612       C  
ATOM   1730  C   THR A1026      65.397 189.511 315.033  1.00 82.23           C  
ANISOU 1730  C   THR A1026     6059  11611  13575   1297    448    674       C  
ATOM   1731  O   THR A1026      64.321 189.996 314.667  1.00 58.70           O  
ANISOU 1731  O   THR A1026     3040   8681  10582   1339    469    688       O  
ATOM   1732  CB  THR A1026      65.978 188.443 317.232  1.00 81.40           C  
ANISOU 1732  CB  THR A1026     5959  11557  13412   1269    407    548       C  
ATOM   1733  OG1 THR A1026      64.689 187.818 317.190  1.00 81.24           O  
ANISOU 1733  OG1 THR A1026     5916  11680  13273   1266    417    517       O  
ATOM   1734  CG2 THR A1026      66.384 188.677 318.683  1.00 57.90           C  
ANISOU 1734  CG2 THR A1026     2962   8553  10483   1298    389    487       C  
ATOM   1735  N   ILE A1027      66.156 188.749 314.246  1.00 80.53           N  
ANISOU 1735  N   ILE A1027     5889  11358  13352   1230    445    728       N  
ATOM   1736  CA  ILE A1027      65.717 188.317 312.924  1.00 79.46           C  
ANISOU 1736  CA  ILE A1027     5761  11250  13182   1200    466    806       C  
ATOM   1737  C   ILE A1027      66.444 187.021 312.601  1.00 56.34           C  
ANISOU 1737  C   ILE A1027     2883   8324  10199   1123    454    820       C  
ATOM   1738  O   ILE A1027      67.561 186.788 313.068  1.00 55.93           O  
ANISOU 1738  O   ILE A1027     2864   8206  10179   1098    437    803       O  
ATOM   1739  CB  ILE A1027      65.980 189.407 311.855  1.00 57.91           C  
ANISOU 1739  CB  ILE A1027     3025   8422  10558   1231    489    899       C  
ATOM   1740  CG1 ILE A1027      65.416 188.966 310.501  1.00 57.84           C  
ANISOU 1740  CG1 ILE A1027     3019   8456  10502   1206    511    982       C  
ATOM   1741  CG2 ILE A1027      67.461 189.727 311.780  1.00 57.76           C  
ANISOU 1741  CG2 ILE A1027     3041   8265  10641   1213    481    930       C  
ATOM   1742  CD1 ILE A1027      66.098 189.576 309.327  1.00 62.99           C  
ANISOU 1742  CD1 ILE A1027     3686   9007  11242   1209    531   1086       C  
ATOM   1743  N   GLY A1028      65.801 186.166 311.806  1.00 56.03           N  
ANISOU 1743  N   GLY A1028     2850   8359  10079   1086    464    853       N  
ATOM   1744  CA  GLY A1028      66.415 184.893 311.505  1.00 55.17           C  
ANISOU 1744  CA  GLY A1028     2789   8258   9914   1018    455    863       C  
ATOM   1745  C   GLY A1028      66.372 183.953 312.697  1.00 65.52           C  
ANISOU 1745  C   GLY A1028     4108   9638  11150    987    430    770       C  
ATOM   1746  O   GLY A1028      65.480 184.018 313.548  1.00 64.21           O  
ANISOU 1746  O   GLY A1028     3904   9551  10940   1009    425    703       O  
ATOM   1747  N   ILE A1029      67.361 183.062 312.759  1.00 68.56           N  
ANISOU 1747  N   ILE A1029     4539   9990  11519    936    417    770       N  
ATOM   1748  CA  ILE A1029      67.473 182.104 313.855  1.00 53.34           C  
ANISOU 1748  CA  ILE A1029     2624   8120   9524    901    394    690       C  
ATOM   1749  C   ILE A1029      68.170 182.766 315.041  1.00 80.60           C  
ANISOU 1749  C   ILE A1029     6070  11522  13034    932    375    638       C  
ATOM   1750  O   ILE A1029      69.349 182.507 315.315  1.00 80.74           O  
ANISOU 1750  O   ILE A1029     6122  11469  13086    906    360    640       O  
ATOM   1751  CB  ILE A1029      68.202 180.827 313.393  1.00 52.53           C  
ANISOU 1751  CB  ILE A1029     2574   8006   9379    835    389    714       C  
ATOM   1752  CG1 ILE A1029      67.519 180.270 312.146  1.00 52.45           C  
ANISOU 1752  CG1 ILE A1029     2569   8039   9319    810    408    772       C  
ATOM   1753  CG2 ILE A1029      68.212 179.765 314.489  1.00 51.98           C  
ANISOU 1753  CG2 ILE A1029     2515   8002   9233    796    367    635       C  
ATOM   1754  CD1 ILE A1029      67.580 178.770 312.033  1.00 51.71           C  
ANISOU 1754  CD1 ILE A1029     2510   7994   9142    746    400    759       C  
ATOM   1755  N   GLY A1030      67.445 183.642 315.739  1.00 54.16           N  
ANISOU 1755  N   GLY A1030     2674   8207   9697    989    376    592       N  
ATOM   1756  CA  GLY A1030      67.904 184.239 316.976  1.00 60.20           C  
ANISOU 1756  CA  GLY A1030     3426   8945  10502   1024    356    533       C  
ATOM   1757  C   GLY A1030      69.000 185.279 316.861  1.00 54.73           C  
ANISOU 1757  C   GLY A1030     2745   8111   9940   1048    352    571       C  
ATOM   1758  O   GLY A1030      69.553 185.675 317.896  1.00 57.16           O  
ANISOU 1758  O   GLY A1030     3039   8365  10314   1066    334    537       O  
ATOM   1759  N   HIS A1031      69.336 185.736 315.654  1.00 54.91           N  
ANISOU 1759  N   HIS A1031     2781   8051  10033   1047    371    655       N  
ATOM   1760  CA  HIS A1031      70.357 186.769 315.503  1.00 71.75           C  
ANISOU 1760  CA  HIS A1031     4919  10040  12302   1066    368    693       C  
ATOM   1761  C   HIS A1031      69.860 188.062 316.136  1.00 72.75           C  
ANISOU 1761  C   HIS A1031     4994  10138  12511   1139    372    668       C  
ATOM   1762  O   HIS A1031      68.912 188.682 315.646  1.00 56.85           O  
ANISOU 1762  O   HIS A1031     2949   8160  10492   1183    394    687       O  
ATOM   1763  CB  HIS A1031      70.715 186.995 314.037  1.00 71.62           C  
ANISOU 1763  CB  HIS A1031     4921   9950  12343   1053    393    797       C  
ATOM   1764  CG  HIS A1031      71.803 188.011 313.829  1.00 72.54           C  
ANISOU 1764  CG  HIS A1031     5041   9914  12605   1066    392    842       C  
ATOM   1765  ND1 HIS A1031      73.094 187.825 314.278  1.00 72.66           N  
ANISOU 1765  ND1 HIS A1031     5085   9840  12681   1032    368    835       N  
ATOM   1766  CD2 HIS A1031      71.789 189.223 313.224  1.00 56.60           C  
ANISOU 1766  CD2 HIS A1031     3000   7814  10690   1106    410    897       C  
ATOM   1767  CE1 HIS A1031      73.827 188.877 313.960  1.00 56.11           C  
ANISOU 1767  CE1 HIS A1031     2982   7614  10725   1048    371    883       C  
ATOM   1768  NE2 HIS A1031      73.059 189.740 313.320  1.00 56.75           N  
ANISOU 1768  NE2 HIS A1031     3033   7696  10832   1093    397    920       N  
ATOM   1769  N   LEU A1032      70.507 188.468 317.226  1.00 73.19           N  
ANISOU 1769  N   LEU A1032     5035  10119  12653   1152    349    629       N  
ATOM   1770  CA  LEU A1032      70.177 189.708 317.918  1.00 74.34           C  
ANISOU 1770  CA  LEU A1032     5130  10212  12905   1222    351    603       C  
ATOM   1771  C   LEU A1032      70.734 190.888 317.133  1.00 58.41           C  
ANISOU 1771  C   LEU A1032     3107   8048  11037   1243    363    672       C  
ATOM   1772  O   LEU A1032      71.949 191.002 316.952  1.00 59.17           O  
ANISOU 1772  O   LEU A1032     3228   8023  11231   1206    348    705       O  
ATOM   1773  CB  LEU A1032      70.738 189.674 319.335  1.00 57.94           C  
ANISOU 1773  CB  LEU A1032     3040   8095  10879   1224    320    536       C  
ATOM   1774  CG  LEU A1032      70.880 190.995 320.090  1.00 59.10           C  
ANISOU 1774  CG  LEU A1032     3142   8127  11187   1287    312    508       C  
ATOM   1775  CD1 LEU A1032      69.536 191.697 320.198  1.00 59.89           C  
ANISOU 1775  CD1 LEU A1032     3194   8299  11262   1368    341    490       C  
ATOM   1776  CD2 LEU A1032      71.480 190.751 321.468  1.00 59.19           C  
ANISOU 1776  CD2 LEU A1032     3144   8105  11239   1277    275    436       C  
ATOM   1777  N   LEU A1033      69.846 191.760 316.655  1.00 65.04           N  
ANISOU 1777  N   LEU A1033     3913   8900  11898   1301    390    697       N  
ATOM   1778  CA  LEU A1033      70.286 192.906 315.867  1.00 59.81           C  
ANISOU 1778  CA  LEU A1033     3243   8105  11378   1322    405    768       C  
ATOM   1779  C   LEU A1033      70.933 193.971 316.744  1.00 74.08           C  
ANISOU 1779  C   LEU A1033     5020   9764  13362   1355    387    739       C  
ATOM   1780  O   LEU A1033      72.034 194.447 316.444  1.00 70.51           O  
ANISOU 1780  O   LEU A1033     4578   9167  13045   1328    376    782       O  
ATOM   1781  CB  LEU A1033      69.114 193.500 315.088  1.00 88.47           C  
ANISOU 1781  CB  LEU A1033     6844  11794  14977   1374    440    805       C  
ATOM   1782  CG  LEU A1033      68.545 192.608 313.996  1.00 59.57           C  
ANISOU 1782  CG  LEU A1033     3211   8249  11175   1338    456    846       C  
ATOM   1783  CD1 LEU A1033      67.884 193.440 312.916  1.00 60.20           C  
ANISOU 1783  CD1 LEU A1033     3268   8321  11285   1378    488    917       C  
ATOM   1784  CD2 LEU A1033      69.658 191.767 313.409  1.00 77.19           C  
ANISOU 1784  CD2 LEU A1033     5497  10440  13391   1263    445    884       C  
ATOM   1785  N   THR A1034      70.261 194.367 317.822  1.00 78.82           N  
ANISOU 1785  N   THR A1034     5580  10395  13974   1414    383    667       N  
ATOM   1786  CA  THR A1034      70.778 195.436 318.666  1.00 86.64           C  
ANISOU 1786  CA  THR A1034     6538  11238  15145   1452    365    630       C  
ATOM   1787  C   THR A1034      70.104 195.395 320.028  1.00 92.05           C  
ANISOU 1787  C   THR A1034     7189  11989  15797   1505    356    533       C  
ATOM   1788  O   THR A1034      68.961 194.943 320.162  1.00 91.97           O  
ANISOU 1788  O   THR A1034     7167  12136  15643   1537    377    510       O  
ATOM   1789  CB  THR A1034      70.543 196.810 318.037  1.00 89.11           C  
ANISOU 1789  CB  THR A1034     6819  11448  15589   1508    390    682       C  
ATOM   1790  OG1 THR A1034      71.093 197.820 318.892  1.00 91.74           O  
ANISOU 1790  OG1 THR A1034     7120  11624  16112   1541    367    637       O  
ATOM   1791  CG2 THR A1034      69.053 197.053 317.881  1.00 87.83           C  
ANISOU 1791  CG2 THR A1034     6627  11413  15331   1580    427    677       C  
ATOM   1792  N   LYS A1035      70.827 195.882 321.037  1.00 93.13           N  
ANISOU 1792  N   LYS A1035     7308  12003  16075   1514    322    475       N  
ATOM   1793  CA  LYS A1035      70.244 196.129 322.354  1.00 90.41           C  
ANISOU 1793  CA  LYS A1035     6924  11686  15740   1581    315    380       C  
ATOM   1794  C   LYS A1035      69.691 197.555 322.370  1.00 92.86           C  
ANISOU 1794  C   LYS A1035     7191  11910  16180   1674    338    374       C  
ATOM   1795  O   LYS A1035      70.247 198.470 322.978  1.00 96.87           O  
ANISOU 1795  O   LYS A1035     7677  12259  16871   1703    314    330       O  
ATOM   1796  CB  LYS A1035      71.278 195.903 323.453  1.00 82.54           C  
ANISOU 1796  CB  LYS A1035     5929  10599  14834   1545    262    309       C  
ATOM   1797  CG  LYS A1035      71.510 194.439 323.820  1.00 76.17           C  
ANISOU 1797  CG  LYS A1035     5155   9912  13875   1477    243    290       C  
ATOM   1798  CD  LYS A1035      72.177 194.325 325.192  1.00 72.75           C  
ANISOU 1798  CD  LYS A1035     4706   9414  13521   1469    193    198       C  
ATOM   1799  CE  LYS A1035      72.088 192.911 325.751  1.00 62.26           C  
ANISOU 1799  CE  LYS A1035     3400   8234  12023   1424    183    171       C  
ATOM   1800  NZ  LYS A1035      70.685 192.421 325.681  1.00 64.80           N  
ANISOU 1800  NZ  LYS A1035     3711   8748  12162   1466    228    174       N  
ATOM   1801  N   SER A1036      68.573 197.733 321.661  1.00 90.00           N  
ANISOU 1801  N   SER A1036     6819  11653  15724   1721    384    418       N  
ATOM   1802  CA  SER A1036      68.013 199.062 321.456  1.00 86.36           C  
ANISOU 1802  CA  SER A1036     6322  11117  15375   1809    413    432       C  
ATOM   1803  C   SER A1036      66.526 198.948 321.170  1.00 67.03           C  
ANISOU 1803  C   SER A1036     3853   8840  12776   1871    458    444       C  
ATOM   1804  O   SER A1036      66.063 197.910 320.681  1.00 66.01           O  
ANISOU 1804  O   SER A1036     3743   8864  12474   1826    466    470       O  
ATOM   1805  CB  SER A1036      68.713 199.798 320.310  1.00 83.13           C  
ANISOU 1805  CB  SER A1036     5923  10568  15095   1777    417    522       C  
ATOM   1806  OG  SER A1036      68.354 201.167 320.305  1.00 68.56           O  
ANISOU 1806  OG  SER A1036     4041   8617  13392   1861    438    524       O  
ATOM   1807  N   PRO A1037      65.759 199.991 321.463  1.00 79.60           N  
ANISOU 1807  N   PRO A1037     5405  10406  14435   1974    487    423       N  
ATOM   1808  CA  PRO A1037      64.305 199.952 321.244  1.00 79.64           C  
ANISOU 1808  CA  PRO A1037     5383  10572  14306   2040    529    432       C  
ATOM   1809  C   PRO A1037      63.855 200.284 319.827  1.00 78.50           C  
ANISOU 1809  C   PRO A1037     5239  10447  14140   2034    557    529       C  
ATOM   1810  O   PRO A1037      62.902 199.681 319.334  1.00 77.66           O  
ANISOU 1810  O   PRO A1037     5127  10500  13882   2030    576    550       O  
ATOM   1811  CB  PRO A1037      63.784 200.997 322.245  1.00 82.34           C  
ANISOU 1811  CB  PRO A1037     5684  10857  14746   2162    548    363       C  
ATOM   1812  CG  PRO A1037      64.935 201.234 323.213  1.00 81.98           C  
ANISOU 1812  CG  PRO A1037     5647  10651  14851   2146    506    293       C  
ATOM   1813  CD  PRO A1037      66.150 201.081 322.370  1.00 80.87           C  
ANISOU 1813  CD  PRO A1037     5541  10401  14785   2040    474    358       C  
ATOM   1814  N   SER A1038      64.510 201.227 319.154  1.00 76.95           N  
ANISOU 1814  N   SER A1038     5046  10090  14100   2032    559    587       N  
ATOM   1815  CA  SER A1038      63.951 201.795 317.927  1.00 76.41           C  
ANISOU 1815  CA  SER A1038     4968  10031  14035   2052    593    676       C  
ATOM   1816  C   SER A1038      64.038 200.844 316.742  1.00 68.13           C  
ANISOU 1816  C   SER A1038     3954   9070  12863   1961    590    749       C  
ATOM   1817  O   SER A1038      65.075 200.229 316.495  1.00 67.25           O  
ANISOU 1817  O   SER A1038     3881   8913  12757   1875    563    767       O  
ATOM   1818  CB  SER A1038      64.654 203.101 317.569  1.00 70.40           C  
ANISOU 1818  CB  SER A1038     4198   9067  13485   2075    597    722       C  
ATOM   1819  OG  SER A1038      64.044 203.678 316.430  1.00 70.82           O  
ANISOU 1819  OG  SER A1038     4237   9133  13538   2102    632    810       O  
ATOM   1820  N   LEU A1039      62.945 200.772 315.978  1.00 83.55           N  
ANISOU 1820  N   LEU A1039     5889  11140  14715   1983    618    791       N  
ATOM   1821  CA  LEU A1039      62.924 199.925 314.788  1.00 81.45           C  
ANISOU 1821  CA  LEU A1039     5655  10953  14341   1904    617    857       C  
ATOM   1822  C   LEU A1039      63.916 200.422 313.743  1.00 82.45           C  
ANISOU 1822  C   LEU A1039     5805  10941  14581   1863    619    949       C  
ATOM   1823  O   LEU A1039      64.759 199.656 313.263  1.00 81.80           O  
ANISOU 1823  O   LEU A1039     5767  10846  14468   1779    600    977       O  
ATOM   1824  CB  LEU A1039      61.508 199.852 314.201  1.00 82.59           C  
ANISOU 1824  CB  LEU A1039     5768  11236  14377   1939    645    881       C  
ATOM   1825  CG  LEU A1039      61.309 199.781 312.674  1.00 82.38           C  
ANISOU 1825  CG  LEU A1039     5752  11229  14319   1900    660    982       C  
ATOM   1826  CD1 LEU A1039      61.794 198.471 312.024  1.00 81.86           C  
ANISOU 1826  CD1 LEU A1039     5737  11221  14146   1796    638   1002       C  
ATOM   1827  CD2 LEU A1039      59.856 200.051 312.296  1.00 67.72           C  
ANISOU 1827  CD2 LEU A1039     3851   9480  12401   1956    689   1002       C  
ATOM   1828  N   ASN A1040      63.823 201.704 313.370  1.00 81.71           N  
ANISOU 1828  N   ASN A1040     5682  10742  14621   1922    643   1000       N  
ATOM   1829  CA  ASN A1040      64.729 202.245 312.361  1.00 82.82           C  
ANISOU 1829  CA  ASN A1040     5840  10751  14878   1886    649   1095       C  
ATOM   1830  C   ASN A1040      66.180 202.063 312.780  1.00 84.79           C  
ANISOU 1830  C   ASN A1040     6120  10873  15222   1824    615   1077       C  
ATOM   1831  O   ASN A1040      67.047 201.795 311.941  1.00 87.58           O  
ANISOU 1831  O   ASN A1040     6505  11174  15597   1756    611   1146       O  
ATOM   1832  CB  ASN A1040      64.428 203.722 312.100  1.00 69.83           C  
ANISOU 1832  CB  ASN A1040     4154   9000  13380   1965    679   1142       C  
ATOM   1833  CG  ASN A1040      64.366 204.543 313.375  1.00 88.24           C  
ANISOU 1833  CG  ASN A1040     6455  11247  15826   2042    675   1060       C  
ATOM   1834  OD1 ASN A1040      63.683 204.174 314.331  1.00 89.78           O  
ANISOU 1834  OD1 ASN A1040     6637  11540  15937   2083    671    973       O  
ATOM   1835  ND2 ASN A1040      65.076 205.668 313.393  1.00 87.64           N  
ANISOU 1835  ND2 ASN A1040     6365  10987  15948   2063    677   1086       N  
ATOM   1836  N   ALA A1041      66.462 202.199 314.078  1.00 83.12           N  
ANISOU 1836  N   ALA A1041     5898  10611  15072   1847    592    986       N  
ATOM   1837  CA  ALA A1041      67.775 201.834 314.596  1.00 81.51           C  
ANISOU 1837  CA  ALA A1041     5722  10307  14941   1781    554    957       C  
ATOM   1838  C   ALA A1041      68.035 200.344 314.409  1.00 66.31           C  
ANISOU 1838  C   ALA A1041     3843   8500  12852   1699    536    950       C  
ATOM   1839  O   ALA A1041      69.109 199.941 313.948  1.00 71.22           O  
ANISOU 1839  O   ALA A1041     4500   9058  13503   1626    519    991       O  
ATOM   1840  CB  ALA A1041      67.884 202.222 316.070  1.00 82.38           C  
ANISOU 1840  CB  ALA A1041     5808  10352  15139   1827    531    853       C  
ATOM   1841  N   ALA A1042      67.053 199.509 314.755  1.00 65.78           N  
ANISOU 1841  N   ALA A1042     3776   8605  12614   1711    539    899       N  
ATOM   1842  CA  ALA A1042      67.205 198.068 314.576  1.00 64.43           C  
ANISOU 1842  CA  ALA A1042     3646   8548  12286   1635    523    889       C  
ATOM   1843  C   ALA A1042      67.249 197.698 313.097  1.00 73.54           C  
ANISOU 1843  C   ALA A1042     4829   9733  13381   1589    540    982       C  
ATOM   1844  O   ALA A1042      68.096 196.903 312.671  1.00 62.95           O  
ANISOU 1844  O   ALA A1042     3531   8379  12007   1516    526   1008       O  
ATOM   1845  CB  ALA A1042      66.071 197.330 315.288  1.00 70.05           C  
ANISOU 1845  CB  ALA A1042     4343   9432  12842   1660    524    814       C  
ATOM   1846  N   LYS A1043      66.340 198.269 312.298  1.00 73.50           N  
ANISOU 1846  N   LYS A1043     4797   9765  13363   1633    571   1035       N  
ATOM   1847  CA  LYS A1043      66.301 197.977 310.866  1.00 71.43           C  
ANISOU 1847  CA  LYS A1043     4557   9533  13050   1596    589   1127       C  
ATOM   1848  C   LYS A1043      67.578 198.433 310.175  1.00 69.43           C  
ANISOU 1848  C   LYS A1043     4327   9129  12926   1560    590   1206       C  
ATOM   1849  O   LYS A1043      68.174 197.687 309.388  1.00 63.24           O  
ANISOU 1849  O   LYS A1043     3584   8354  12091   1498    588   1253       O  
ATOM   1850  CB  LYS A1043      65.083 198.645 310.227  1.00 64.76           C  
ANISOU 1850  CB  LYS A1043     3672   8745  12188   1657    621   1170       C  
ATOM   1851  N   SER A1044      68.004 199.669 310.444  1.00 68.59           N  
ANISOU 1851  N   SER A1044     4192   8878  12992   1600    595   1223       N  
ATOM   1852  CA  SER A1044      69.244 200.162 309.857  1.00 68.09           C  
ANISOU 1852  CA  SER A1044     4143   8661  13068   1563    596   1298       C  
ATOM   1853  C   SER A1044      70.434 199.331 310.312  1.00 64.41           C  
ANISOU 1853  C   SER A1044     3716   8153  12603   1492    562   1266       C  
ATOM   1854  O   SER A1044      71.325 199.025 309.512  1.00 63.96           O  
ANISOU 1854  O   SER A1044     3690   8047  12563   1438    564   1335       O  
ATOM   1855  CB  SER A1044      69.449 201.634 310.210  1.00 66.62           C  
ANISOU 1855  CB  SER A1044     3913   8321  13080   1617    602   1310       C  
ATOM   1856  OG  SER A1044      70.786 202.034 309.982  1.00 87.76           O  
ANISOU 1856  OG  SER A1044     6599  10837  15909   1572    592   1360       O  
ATOM   1857  N   GLU A1045      70.462 198.951 311.592  1.00 64.22           N  
ANISOU 1857  N   GLU A1045     3691   8150  12560   1493    532   1165       N  
ATOM   1858  CA  GLU A1045      71.558 198.128 312.095  1.00 85.72           C  
ANISOU 1858  CA  GLU A1045     6450  10839  15282   1426    498   1131       C  
ATOM   1859  C   GLU A1045      71.717 196.865 311.262  1.00 85.64           C  
ANISOU 1859  C   GLU A1045     6490  10929  15122   1366    503   1167       C  
ATOM   1860  O   GLU A1045      72.841 196.445 310.959  1.00 86.44           O  
ANISOU 1860  O   GLU A1045     6624  10964  15254   1309    492   1202       O  
ATOM   1861  CB  GLU A1045      71.325 197.770 313.562  1.00 63.36           C  
ANISOU 1861  CB  GLU A1045     3607   8050  12417   1441    469   1016       C  
ATOM   1862  CG  GLU A1045      72.505 198.083 314.466  1.00 63.67           C  
ANISOU 1862  CG  GLU A1045     3642   7942  12609   1416    431    977       C  
ATOM   1863  CD  GLU A1045      73.764 197.323 314.083  1.00 79.84           C  
ANISOU 1863  CD  GLU A1045     5734   9943  14660   1333    413   1016       C  
ATOM   1864  OE1 GLU A1045      73.658 196.203 313.539  1.00 77.68           O  
ANISOU 1864  OE1 GLU A1045     5501   9783  14230   1295    421   1034       O  
ATOM   1865  OE2 GLU A1045      74.868 197.849 314.332  1.00 81.18           O  
ANISOU 1865  OE2 GLU A1045     5895   9956  14992   1308    389   1028       O  
ATOM   1866  N   LEU A1046      70.598 196.260 310.863  1.00 61.81           N  
ANISOU 1866  N   LEU A1046     3475   8063  11946   1379    519   1160       N  
ATOM   1867  CA  LEU A1046      70.654 195.073 310.020  1.00 60.76           C  
ANISOU 1867  CA  LEU A1046     3387   8022  11678   1325    524   1191       C  
ATOM   1868  C   LEU A1046      71.296 195.388 308.670  1.00 70.88           C  
ANISOU 1868  C   LEU A1046     4679   9217  13034   1304    551   1314       C  
ATOM   1869  O   LEU A1046      72.241 194.713 308.247  1.00 70.55           O  
ANISOU 1869  O   LEU A1046     4673   9138  12993   1250    548   1355       O  
ATOM   1870  CB  LEU A1046      69.246 194.502 309.853  1.00 60.62           C  
ANISOU 1870  CB  LEU A1046     3353   8161  11518   1343    538   1172       C  
ATOM   1871  CG  LEU A1046      68.993 193.499 308.735  1.00 60.05           C  
ANISOU 1871  CG  LEU A1046     3303   8164  11350   1300    555   1239       C  
ATOM   1872  CD1 LEU A1046      67.986 192.474 309.162  1.00 59.54           C  
ANISOU 1872  CD1 LEU A1046     3236   8250  11137   1288    546   1173       C  
ATOM   1873  CD2 LEU A1046      68.476 194.227 307.535  1.00 65.43           C  
ANISOU 1873  CD2 LEU A1046     3960   8833  12068   1331    590   1338       C  
ATOM   1874  N   ASP A1047      70.805 196.434 307.990  1.00 61.83           N  
ANISOU 1874  N   ASP A1047     3500   8038  11956   1351    579   1379       N  
ATOM   1875  CA  ASP A1047      71.298 196.778 306.654  1.00 77.84           C  
ANISOU 1875  CA  ASP A1047     5532   9995  14049   1337    609   1505       C  
ATOM   1876  C   ASP A1047      72.811 196.936 306.621  1.00 78.45           C  
ANISOU 1876  C   ASP A1047     5632   9933  14243   1296    599   1540       C  
ATOM   1877  O   ASP A1047      73.445 196.636 305.603  1.00 76.60           O  
ANISOU 1877  O   ASP A1047     5418   9666  14021   1263    619   1635       O  
ATOM   1878  CB  ASP A1047      70.646 198.070 306.154  1.00 80.46           C  
ANISOU 1878  CB  ASP A1047     5820  10291  14462   1398    637   1560       C  
ATOM   1879  CG  ASP A1047      69.166 197.904 305.822  1.00 84.45           C  
ANISOU 1879  CG  ASP A1047     6300  10933  14855   1436    656   1561       C  
ATOM   1880  OD1 ASP A1047      68.767 196.843 305.287  1.00 86.17           O  
ANISOU 1880  OD1 ASP A1047     6536  11255  14949   1404    661   1579       O  
ATOM   1881  OD2 ASP A1047      68.398 198.856 306.081  1.00 85.61           O  
ANISOU 1881  OD2 ASP A1047     6406  11078  15042   1498    665   1546       O  
ATOM   1882  N   LYS A1048      73.405 197.410 307.719  1.00 82.34           N  
ANISOU 1882  N   LYS A1048     6117  10341  14829   1298    568   1471       N  
ATOM   1883  CA  LYS A1048      74.858 197.500 307.796  1.00 86.13           C  
ANISOU 1883  CA  LYS A1048     6611  10683  15430   1252    553   1503       C  
ATOM   1884  C   LYS A1048      75.501 196.123 307.679  1.00 88.69           C  
ANISOU 1884  C   LYS A1048     6987  11062  15648   1192    542   1495       C  
ATOM   1885  O   LYS A1048      76.530 195.965 307.012  1.00 90.92           O  
ANISOU 1885  O   LYS A1048     7288  11269  15987   1155    552   1574       O  
ATOM   1886  CB  LYS A1048      75.279 198.181 309.099  1.00 62.90           C  
ANISOU 1886  CB  LYS A1048     3638   7632  12630   1262    520   1433       C  
ATOM   1887  N   ALA A1049      74.905 195.110 308.302  1.00 60.40           N  
ANISOU 1887  N   ALA A1049     3422   7602  11926   1184    525   1413       N  
ATOM   1888  CA  ALA A1049      75.496 193.781 308.292  1.00 59.45           C  
ANISOU 1888  CA  ALA A1049     3345   7522  11720   1129    515   1406       C  
ATOM   1889  C   ALA A1049      75.095 192.951 307.077  1.00 59.03           C  
ANISOU 1889  C   ALA A1049     3313   7554  11562   1114    548   1480       C  
ATOM   1890  O   ALA A1049      75.447 191.770 307.021  1.00 58.24           O  
ANISOU 1890  O   ALA A1049     3249   7501  11377   1073    542   1471       O  
ATOM   1891  CB  ALA A1049      75.116 193.024 309.562  1.00 58.86           C  
ANISOU 1891  CB  ALA A1049     3279   7537  11548   1122    481   1285       C  
ATOM   1892  N   ILE A1050      74.369 193.514 306.116  1.00 59.57           N  
ANISOU 1892  N   ILE A1050     3358   7643  11631   1148    581   1551       N  
ATOM   1893  CA  ILE A1050      73.936 192.754 304.950  1.00 59.23           C  
ANISOU 1893  CA  ILE A1050     3332   7685  11488   1137    609   1620       C  
ATOM   1894  C   ILE A1050      74.387 193.519 303.714  1.00 59.87           C  
ANISOU 1894  C   ILE A1050     3403   7683  11661   1149    645   1749       C  
ATOM   1895  O   ILE A1050      74.671 192.937 302.660  1.00 59.61           O  
ANISOU 1895  O   ILE A1050     3393   7670  11586   1130    669   1829       O  
ATOM   1896  CB  ILE A1050      72.408 192.519 304.961  1.00 64.51           C  
ANISOU 1896  CB  ILE A1050     3980   8493  12039   1165    613   1581       C  
ATOM   1897  CG1 ILE A1050      72.040 191.383 305.925  1.00 58.43           C  
ANISOU 1897  CG1 ILE A1050     3227   7824  11149   1139    583   1474       C  
ATOM   1898  CG2 ILE A1050      71.893 192.148 303.580  1.00 64.72           C  
ANISOU 1898  CG2 ILE A1050     4010   8586  11996   1165    645   1673       C  
ATOM   1899  CD1 ILE A1050      71.829 191.818 307.350  1.00 58.59           C  
ANISOU 1899  CD1 ILE A1050     3227   7840  11195   1161    554   1367       C  
ATOM   1900  N   GLY A1051      74.452 194.838 303.846  1.00 61.49           N  
ANISOU 1900  N   GLY A1051     3573   7796  11996   1182    650   1769       N  
ATOM   1901  CA  GLY A1051      74.949 195.703 302.808  1.00 61.45           C  
ANISOU 1901  CA  GLY A1051     3553   7697  12100   1194    683   1889       C  
ATOM   1902  C   GLY A1051      73.922 196.134 301.788  1.00 61.99           C  
ANISOU 1902  C   GLY A1051     3594   7827  12132   1234    718   1964       C  
ATOM   1903  O   GLY A1051      74.259 196.914 300.888  1.00 74.82           O  
ANISOU 1903  O   GLY A1051     5202   9379  13847   1247    749   2071       O  
ATOM   1904  N   ARG A1052      72.683 195.658 301.892  1.00 61.76           N  
ANISOU 1904  N   ARG A1052     3558   7929  11978   1252    715   1915       N  
ATOM   1905  CA  ARG A1052      71.631 196.023 300.954  1.00 62.28           C  
ANISOU 1905  CA  ARG A1052     3596   8064  12004   1289    744   1984       C  
ATOM   1906  C   ARG A1052      70.412 196.536 301.707  1.00 79.28           C  
ANISOU 1906  C   ARG A1052     5711  10277  14135   1335    734   1908       C  
ATOM   1907  O   ARG A1052      70.202 196.215 302.878  1.00 73.06           O  
ANISOU 1907  O   ARG A1052     4927   9522  13312   1332    703   1795       O  
ATOM   1908  CB  ARG A1052      71.236 194.840 300.062  1.00 79.96           C  
ANISOU 1908  CB  ARG A1052     5860  10420  14101   1266    755   2021       C  
ATOM   1909  CG  ARG A1052      70.392 193.776 300.736  1.00 60.94           C  
ANISOU 1909  CG  ARG A1052     3462   8140  11552   1250    728   1919       C  
ATOM   1910  CD  ARG A1052      70.029 192.710 299.724  1.00 69.35           C  
ANISOU 1910  CD  ARG A1052     4549   9308  12493   1227    740   1967       C  
ATOM   1911  NE  ARG A1052      69.239 191.620 300.284  1.00 59.78           N  
ANISOU 1911  NE  ARG A1052     3346   8219  11149   1204    715   1877       N  
ATOM   1912  CZ  ARG A1052      67.915 191.643 300.391  1.00 85.78           C  
ANISOU 1912  CZ  ARG A1052     6607  11613  14374   1226    711   1849       C  
ATOM   1913  NH1 ARG A1052      67.271 190.603 300.900  1.00 85.18           N  
ANISOU 1913  NH1 ARG A1052     6539  11642  14183   1198    688   1771       N  
ATOM   1914  NH2 ARG A1052      67.234 192.709 299.997  1.00 86.37           N  
ANISOU 1914  NH2 ARG A1052     6638  11681  14498   1274    731   1901       N  
ATOM   1915  N   ASN A1053      69.597 197.336 301.017  1.00 63.49           N  
ANISOU 1915  N   ASN A1053     3674   8295  12156   1380    761   1974       N  
ATOM   1916  CA  ASN A1053      68.409 197.940 301.626  1.00 70.74           C  
ANISOU 1916  CA  ASN A1053     4550   9266  13062   1433    757   1917       C  
ATOM   1917  C   ASN A1053      67.305 196.898 301.692  1.00 73.56           C  
ANISOU 1917  C   ASN A1053     4909   9782  13258   1425    747   1869       C  
ATOM   1918  O   ASN A1053      66.487 196.756 300.781  1.00 63.71           O  
ANISOU 1918  O   ASN A1053     3646   8616  11946   1436    767   1935       O  
ATOM   1919  CB  ASN A1053      67.960 199.173 300.857  1.00 69.85           C  
ANISOU 1919  CB  ASN A1053     4395   9111  13033   1485    791   2011       C  
ATOM   1920  CG  ASN A1053      68.948 200.308 300.962  1.00 69.98           C  
ANISOU 1920  CG  ASN A1053     4401   8965  13222   1496    798   2046       C  
ATOM   1921  OD1 ASN A1053      68.922 201.088 301.915  1.00 66.28           O  
ANISOU 1921  OD1 ASN A1053     3912   8436  12835   1529    784   1977       O  
ATOM   1922  ND2 ASN A1053      69.837 200.403 299.984  1.00 70.17           N  
ANISOU 1922  ND2 ASN A1053     4440   8918  13305   1470    821   2154       N  
ATOM   1923  N   THR A1054      67.282 196.169 302.807  1.00 76.76           N  
ANISOU 1923  N   THR A1054     5331  10232  13602   1403    715   1754       N  
ATOM   1924  CA  THR A1054      66.324 195.085 302.981  1.00 78.88           C  
ANISOU 1924  CA  THR A1054     5602  10646  13722   1385    702   1701       C  
ATOM   1925  C   THR A1054      64.917 195.614 303.198  1.00 81.58           C  
ANISOU 1925  C   THR A1054     5894  11069  14034   1439    710   1680       C  
ATOM   1926  O   THR A1054      63.939 194.994 302.761  1.00 81.85           O  
ANISOU 1926  O   THR A1054     5917  11220  13964   1432    713   1694       O  
ATOM   1927  CB  THR A1054      66.734 194.238 304.175  1.00 61.44           C  
ANISOU 1927  CB  THR A1054     3423   8457  11466   1350    668   1587       C  
ATOM   1928  OG1 THR A1054      66.570 195.019 305.362  1.00 61.89           O  
ANISOU 1928  OG1 THR A1054     3453   8480  11582   1392    654   1504       O  
ATOM   1929  CG2 THR A1054      68.182 193.811 304.036  1.00 60.92           C  
ANISOU 1929  CG2 THR A1054     3404   8300  11444   1301    660   1609       C  
ATOM   1930  N   ASN A1055      64.799 196.750 303.885  1.00 82.61           N  
ANISOU 1930  N   ASN A1055     5993  11137  14259   1494    712   1646       N  
ATOM   1931  CA  ASN A1055      63.517 197.266 304.360  1.00 64.36           C  
ANISOU 1931  CA  ASN A1055     3633   8897  11924   1553    718   1606       C  
ATOM   1932  C   ASN A1055      62.817 196.269 305.275  1.00 63.76           C  
ANISOU 1932  C   ASN A1055     3557   8943  11726   1536    694   1501       C  
ATOM   1933  O   ASN A1055      61.591 196.275 305.395  1.00 82.09           O  
ANISOU 1933  O   ASN A1055     5842  11363  13987   1566    700   1484       O  
ATOM   1934  CB  ASN A1055      62.604 197.666 303.198  1.00 65.04           C  
ANISOU 1934  CB  ASN A1055     3686   9032  11996   1582    749   1710       C  
ATOM   1935  CG  ASN A1055      62.789 199.108 302.789  1.00 98.15           C  
ANISOU 1935  CG  ASN A1055     7851  13118  16325   1637    776   1781       C  
ATOM   1936  OD1 ASN A1055      63.103 199.964 303.617  1.00 66.56           O  
ANISOU 1936  OD1 ASN A1055     3838   9032  12419   1676    771   1729       O  
ATOM   1937  ND2 ASN A1055      62.592 199.392 301.505  1.00 99.09           N  
ANISOU 1937  ND2 ASN A1055     7958  13238  16455   1642    805   1903       N  
ATOM   1938  N   GLY A1056      63.585 195.401 305.924  1.00 62.87           N  
ANISOU 1938  N   GLY A1056     3484   8824  11578   1485    667   1434       N  
ATOM   1939  CA  GLY A1056      63.040 194.499 306.912  1.00 62.32           C  
ANISOU 1939  CA  GLY A1056     3416   8859  11404   1468    643   1331       C  
ATOM   1940  C   GLY A1056      62.911 193.047 306.508  1.00 61.41           C  
ANISOU 1940  C   GLY A1056     3330   8835  11168   1398    632   1334       C  
ATOM   1941  O   GLY A1056      62.336 192.263 307.272  1.00 61.01           O  
ANISOU 1941  O   GLY A1056     3275   8878  11028   1381    615   1255       O  
ATOM   1942  N   VAL A1057      63.434 192.655 305.348  1.00 77.29           N  
ANISOU 1942  N   VAL A1057     5370  10821  13175   1359    642   1424       N  
ATOM   1943  CA  VAL A1057      63.273 191.296 304.845  1.00 74.63           C  
ANISOU 1943  CA  VAL A1057     5062  10569  12725   1298    634   1434       C  
ATOM   1944  C   VAL A1057      64.618 190.773 304.354  1.00 72.22           C  
ANISOU 1944  C   VAL A1057     4810  10188  12441   1251    631   1472       C  
ATOM   1945  O   VAL A1057      65.392 191.500 303.723  1.00 71.30           O  
ANISOU 1945  O   VAL A1057     4701   9971  12418   1265    648   1546       O  
ATOM   1946  CB  VAL A1057      62.213 191.229 303.724  1.00 75.31           C  
ANISOU 1946  CB  VAL A1057     5121  10737  12757   1304    652   1516       C  
ATOM   1947  CG1 VAL A1057      62.643 192.053 302.510  1.00 75.90           C  
ANISOU 1947  CG1 VAL A1057     5193  10735  12909   1328    680   1636       C  
ATOM   1948  CG2 VAL A1057      61.953 189.790 303.331  1.00 74.67           C  
ANISOU 1948  CG2 VAL A1057     5066  10748  12557   1241    639   1514       C  
ATOM   1949  N   ILE A1058      64.898 189.504 304.650  1.00 58.77           N  
ANISOU 1949  N   ILE A1058     3144   8532  10655   1195    611   1424       N  
ATOM   1950  CA  ILE A1058      66.113 188.851 304.190  1.00 58.12           C  
ANISOU 1950  CA  ILE A1058     3113   8391  10580   1150    609   1457       C  
ATOM   1951  C   ILE A1058      65.745 187.533 303.523  1.00 57.51           C  
ANISOU 1951  C   ILE A1058     3058   8407  10386   1101    606   1473       C  
ATOM   1952  O   ILE A1058      64.677 186.965 303.757  1.00 76.53           O  
ANISOU 1952  O   ILE A1058     5448  10923  12708   1089    595   1433       O  
ATOM   1953  CB  ILE A1058      67.109 188.609 305.337  1.00 57.62           C  
ANISOU 1953  CB  ILE A1058     3077   8267  10548   1129    585   1377       C  
ATOM   1954  CG1 ILE A1058      66.519 187.615 306.331  1.00 57.06           C  
ANISOU 1954  CG1 ILE A1058     3008   8297  10374   1101    560   1275       C  
ATOM   1955  CG2 ILE A1058      67.439 189.914 306.032  1.00 58.27           C  
ANISOU 1955  CG2 ILE A1058     3135   8257  10749   1177    585   1356       C  
ATOM   1956  CD1 ILE A1058      67.516 187.092 307.315  1.00 56.44           C  
ANISOU 1956  CD1 ILE A1058     2963   8176  10304   1070    536   1207       C  
ATOM   1957  N   THR A1059      66.657 187.048 302.685  1.00 57.12           N  
ANISOU 1957  N   THR A1059     3049   8316  10339   1073    615   1535       N  
ATOM   1958  CA  THR A1059      66.446 185.816 301.943  1.00 56.57           C  
ANISOU 1958  CA  THR A1059     3004   8324  10166   1029    613   1557       C  
ATOM   1959  C   THR A1059      66.681 184.602 302.838  1.00 55.71           C  
ANISOU 1959  C   THR A1059     2927   8253   9989    980    586   1464       C  
ATOM   1960  O   THR A1059      67.213 184.704 303.945  1.00 55.50           O  
ANISOU 1960  O   THR A1059     2908   8183   9998    978    571   1394       O  
ATOM   1961  CB  THR A1059      67.377 185.752 300.730  1.00 73.63           C  
ANISOU 1961  CB  THR A1059     5194  10426  12355   1024    636   1655       C  
ATOM   1962  OG1 THR A1059      67.605 187.073 300.221  1.00 72.88           O  
ANISOU 1962  OG1 THR A1059     5076  10252  12363   1071    661   1732       O  
ATOM   1963  CG2 THR A1059      66.767 184.896 299.628  1.00 75.15           C  
ANISOU 1963  CG2 THR A1059     5392  10713  12448   1003    642   1705       C  
ATOM   1964  N   LYS A1060      66.268 183.432 302.341  1.00 55.25           N  
ANISOU 1964  N   LYS A1060     2884   8278   9830    938    581   1467       N  
ATOM   1965  CA  LYS A1060      66.622 182.181 303.005  1.00 77.95           C  
ANISOU 1965  CA  LYS A1060     5795  11181  12643    887    559   1395       C  
ATOM   1966  C   LYS A1060      68.134 182.021 303.089  1.00 76.49           C  
ANISOU 1966  C   LYS A1060     5655  10897  12512    876    562   1404       C  
ATOM   1967  O   LYS A1060      68.662 181.522 304.090  1.00 53.49           O  
ANISOU 1967  O   LYS A1060     2763   7967   9595    852    543   1332       O  
ATOM   1968  CB  LYS A1060      65.997 180.996 302.264  1.00 78.00           C  
ANISOU 1968  CB  LYS A1060     5811  11281  12544    845    555   1411       C  
ATOM   1969  CG  LYS A1060      66.267 179.629 302.900  1.00 76.54           C  
ANISOU 1969  CG  LYS A1060     5661  11130  12291    788    534   1339       C  
ATOM   1970  CD  LYS A1060      65.499 178.515 302.180  1.00 74.63           C  
ANISOU 1970  CD  LYS A1060     5423  10983  11950    746    529   1353       C  
ATOM   1971  CE  LYS A1060      65.884 178.424 300.700  1.00 72.27           C  
ANISOU 1971  CE  LYS A1060     5140  10672  11646    752    550   1449       C  
ATOM   1972  NZ  LYS A1060      65.192 177.303 299.991  1.00 70.41           N  
ANISOU 1972  NZ  LYS A1060     4909  10530  11314    709    541   1462       N  
ATOM   1973  N   ASP A1061      68.847 182.442 302.043  1.00 76.09           N  
ANISOU 1973  N   ASP A1061     5617  10780  12514    893    587   1496       N  
ATOM   1974  CA  ASP A1061      70.303 182.420 302.085  1.00 75.91           C  
ANISOU 1974  CA  ASP A1061     5632  10654  12557    887    593   1517       C  
ATOM   1975  C   ASP A1061      70.822 183.397 303.128  1.00 54.24           C  
ANISOU 1975  C   ASP A1061     2874   7821   9912    909    583   1478       C  
ATOM   1976  O   ASP A1061      71.555 183.014 304.045  1.00 58.44           O  
ANISOU 1976  O   ASP A1061     3430   8317  10459    887    565   1420       O  
ATOM   1977  CB  ASP A1061      70.875 182.746 300.705  1.00 77.91           C  
ANISOU 1977  CB  ASP A1061     5895  10859  12848    905    626   1631       C  
ATOM   1978  CG  ASP A1061      70.486 181.722 299.653  1.00 81.24           C  
ANISOU 1978  CG  ASP A1061     6333  11366  13170    884    635   1668       C  
ATOM   1979  OD1 ASP A1061      69.643 180.844 299.944  1.00 81.97           O  
ANISOU 1979  OD1 ASP A1061     6422  11554  13168    854    615   1609       O  
ATOM   1980  OD2 ASP A1061      71.020 181.806 298.526  1.00 83.45           O  
ANISOU 1980  OD2 ASP A1061     6624  11616  13466    897    662   1758       O  
ATOM   1981  N   GLU A1062      70.429 184.670 303.014  1.00 55.01           N  
ANISOU 1981  N   GLU A1062     2933   7886  10081    954    594   1510       N  
ATOM   1982  CA  GLU A1062      70.920 185.677 303.948  1.00 55.37           C  
ANISOU 1982  CA  GLU A1062     2963   7843  10231    978    585   1476       C  
ATOM   1983  C   GLU A1062      70.646 185.285 305.395  1.00 61.14           C  
ANISOU 1983  C   GLU A1062     3691   8616  10924    964    553   1359       C  
ATOM   1984  O   GLU A1062      71.431 185.625 306.286  1.00 62.28           O  
ANISOU 1984  O   GLU A1062     3841   8686  11136    964    537   1318       O  
ATOM   1985  CB  GLU A1062      70.300 187.036 303.624  1.00 56.29           C  
ANISOU 1985  CB  GLU A1062     3034   7936  10418   1030    602   1520       C  
ATOM   1986  CG  GLU A1062      70.447 187.438 302.168  1.00 72.91           C  
ANISOU 1986  CG  GLU A1062     5137  10011  12553   1046    635   1641       C  
ATOM   1987  CD  GLU A1062      70.026 188.872 301.914  1.00 74.99           C  
ANISOU 1987  CD  GLU A1062     5357  10231  12906   1098    653   1689       C  
ATOM   1988  OE1 GLU A1062      69.928 189.641 302.893  1.00 76.66           O  
ANISOU 1988  OE1 GLU A1062     5544  10403  13180   1122    640   1631       O  
ATOM   1989  OE2 GLU A1062      69.794 189.229 300.736  1.00 58.11           O  
ANISOU 1989  OE2 GLU A1062     3208   8098  10775   1117    681   1785       O  
ATOM   1990  N   ALA A1063      69.561 184.549 305.648  1.00 59.62           N  
ANISOU 1990  N   ALA A1063     3487   8542  10624    949    542   1306       N  
ATOM   1991  CA  ALA A1063      69.306 184.070 307.004  1.00 54.39           C  
ANISOU 1991  CA  ALA A1063     2822   7929   9916    934    513   1198       C  
ATOM   1992  C   ALA A1063      70.302 182.997 307.414  1.00 87.44           C  
ANISOU 1992  C   ALA A1063     7055  12095  14075    886    498   1168       C  
ATOM   1993  O   ALA A1063      70.606 182.855 308.605  1.00 87.09           O  
ANISOU 1993  O   ALA A1063     7013  12044  14033    877    475   1092       O  
ATOM   1994  CB  ALA A1063      67.877 183.539 307.122  1.00 54.37           C  
ANISOU 1994  CB  ALA A1063     2793   8057   9810    927    508   1158       C  
ATOM   1995  N   GLU A1064      70.821 182.241 306.450  1.00 53.21           N  
ANISOU 1995  N   GLU A1064     2755   7750   9713    857    511   1227       N  
ATOM   1996  CA  GLU A1064      71.744 181.151 306.734  1.00 52.48           C  
ANISOU 1996  CA  GLU A1064     2707   7641   9591    813    500   1205       C  
ATOM   1997  C   GLU A1064      73.173 181.648 306.923  1.00 65.28           C  
ANISOU 1997  C   GLU A1064     4350   9135  11320    819    501   1233       C  
ATOM   1998  O   GLU A1064      73.821 181.308 307.917  1.00 52.19           O  
ANISOU 1998  O   GLU A1064     2707   7450   9672    799    479   1177       O  
ATOM   1999  CB  GLU A1064      71.675 180.117 305.612  1.00 52.09           C  
ANISOU 1999  CB  GLU A1064     2686   7639   9468    785    516   1255       C  
ATOM   2000  CG  GLU A1064      72.631 178.963 305.770  1.00 85.24           C  
ANISOU 2000  CG  GLU A1064     6932  11819  13638    744    510   1241       C  
ATOM   2001  CD  GLU A1064      72.333 177.845 304.798  1.00 76.65           C  
ANISOU 2001  CD  GLU A1064     5866  10798  12461    716    521   1271       C  
ATOM   2002  OE1 GLU A1064      72.537 176.670 305.166  1.00 67.68           O  
ANISOU 2002  OE1 GLU A1064     4757   9695  11263    677    510   1228       O  
ATOM   2003  OE2 GLU A1064      71.881 178.141 303.672  1.00 72.50           O  
ANISOU 2003  OE2 GLU A1064     5327  10293  11928    735    542   1339       O  
ATOM   2004  N   LYS A1065      73.676 182.447 305.978  1.00 63.35           N  
ANISOU 2004  N   LYS A1065     4102   8811  11157    843    526   1323       N  
ATOM   2005  CA  LYS A1065      74.997 183.048 306.139  1.00 63.00           C  
ANISOU 2005  CA  LYS A1065     4069   8637  11230    847    527   1357       C  
ATOM   2006  C   LYS A1065      75.081 183.808 307.455  1.00 62.61           C  
ANISOU 2006  C   LYS A1065     3996   8547  11245    861    499   1284       C  
ATOM   2007  O   LYS A1065      76.027 183.634 308.233  1.00 60.84           O  
ANISOU 2007  O   LYS A1065     3789   8263  11063    841    479   1252       O  
ATOM   2008  CB  LYS A1065      75.307 183.985 304.965  1.00 64.94           C  
ANISOU 2008  CB  LYS A1065     4305   8810  11560    877    559   1465       C  
ATOM   2009  CG  LYS A1065      75.302 183.331 303.588  1.00 53.65           C  
ANISOU 2009  CG  LYS A1065     2896   7417  10073    870    589   1546       C  
ATOM   2010  CD  LYS A1065      75.395 184.380 302.485  1.00 54.39           C  
ANISOU 2010  CD  LYS A1065     2969   7453  10243    906    622   1651       C  
ATOM   2011  CE  LYS A1065      75.265 183.760 301.096  1.00 54.28           C  
ANISOU 2011  CE  LYS A1065     2972   7491  10162    905    652   1731       C  
ATOM   2012  NZ  LYS A1065      75.274 184.789 300.015  1.00 55.05           N  
ANISOU 2012  NZ  LYS A1065     3046   7543  10327    942    685   1837       N  
ATOM   2013  N   LEU A1066      74.080 184.652 307.720  1.00 63.01           N  
ANISOU 2013  N   LEU A1066     4006   8633  11303    897    497   1257       N  
ATOM   2014  CA  LEU A1066      74.037 185.393 308.975  1.00 54.29           C  
ANISOU 2014  CA  LEU A1066     2874   7501  10251    917    472   1183       C  
ATOM   2015  C   LEU A1066      74.060 184.448 310.169  1.00 64.14           C  
ANISOU 2015  C   LEU A1066     4137   8809  11424    887    441   1087       C  
ATOM   2016  O   LEU A1066      74.661 184.758 311.206  1.00 64.71           O  
ANISOU 2016  O   LEU A1066     4206   8829  11551    887    416   1037       O  
ATOM   2017  CB  LEU A1066      72.789 186.275 309.006  1.00 54.93           C  
ANISOU 2017  CB  LEU A1066     2908   7633  10328    965    480   1168       C  
ATOM   2018  CG  LEU A1066      72.982 187.725 309.439  1.00 55.72           C  
ANISOU 2018  CG  LEU A1066     2976   7641  10554   1009    477   1165       C  
ATOM   2019  CD1 LEU A1066      71.658 188.460 309.474  1.00 56.33           C  
ANISOU 2019  CD1 LEU A1066     3007   7784  10612   1059    487   1148       C  
ATOM   2020  CD2 LEU A1066      73.652 187.756 310.793  1.00 90.61           C  
ANISOU 2020  CD2 LEU A1066     7398  12019  15011   1000    442   1085       C  
ATOM   2021  N   PHE A1067      73.418 183.285 310.036  1.00 62.58           N  
ANISOU 2021  N   PHE A1067     3954   8720  11103    859    442   1064       N  
ATOM   2022  CA  PHE A1067      73.435 182.296 311.107  1.00 61.18           C  
ANISOU 2022  CA  PHE A1067     3791   8603  10850    827    416    980       C  
ATOM   2023  C   PHE A1067      74.828 181.726 311.328  1.00 60.63           C  
ANISOU 2023  C   PHE A1067     3762   8458  10818    792    404    991       C  
ATOM   2024  O   PHE A1067      75.180 181.358 312.455  1.00 60.75           O  
ANISOU 2024  O   PHE A1067     3783   8479  10820    775    377    924       O  
ATOM   2025  CB  PHE A1067      72.451 181.170 310.794  1.00 60.04           C  
ANISOU 2025  CB  PHE A1067     3652   8583  10576    800    421    962       C  
ATOM   2026  CG  PHE A1067      72.677 179.931 311.604  1.00 51.36           C  
ANISOU 2026  CG  PHE A1067     2579   7535   9401    756    399    899       C  
ATOM   2027  CD1 PHE A1067      72.461 179.939 312.973  1.00 73.25           C  
ANISOU 2027  CD1 PHE A1067     5333  10346  12152    759    374    812       C  
ATOM   2028  CD2 PHE A1067      73.100 178.757 311.001  1.00 50.76           C  
ANISOU 2028  CD2 PHE A1067     2544   7470   9274    714    406    928       C  
ATOM   2029  CE1 PHE A1067      72.666 178.799 313.727  1.00 72.42           C  
ANISOU 2029  CE1 PHE A1067     5250  10290  11978    717    355    759       C  
ATOM   2030  CE2 PHE A1067      73.304 177.615 311.747  1.00 50.16           C  
ANISOU 2030  CE2 PHE A1067     2490   7436   9131    673    388    872       C  
ATOM   2031  CZ  PHE A1067      73.087 177.636 313.113  1.00 71.91           C  
ANISOU 2031  CZ  PHE A1067     5226  10229  11866    673    362    789       C  
ATOM   2032  N   ASN A1068      75.635 181.638 310.271  1.00 52.01           N  
ANISOU 2032  N   ASN A1068     2696   7295   9770    782    426   1076       N  
ATOM   2033  CA  ASN A1068      76.994 181.144 310.443  1.00 51.66           C  
ANISOU 2033  CA  ASN A1068     2687   7172   9769    753    418   1093       C  
ATOM   2034  C   ASN A1068      77.813 182.087 311.311  1.00 52.06           C  
ANISOU 2034  C   ASN A1068     2723   7122   9937    764    395   1073       C  
ATOM   2035  O   ASN A1068      78.561 181.642 312.188  1.00 51.76           O  
ANISOU 2035  O   ASN A1068     2700   7059   9909    740    370   1032       O  
ATOM   2036  CB  ASN A1068      77.649 180.924 309.084  1.00 51.63           C  
ANISOU 2036  CB  ASN A1068     2710   7117   9790    748    451   1194       C  
ATOM   2037  CG  ASN A1068      77.100 179.703 308.387  1.00 62.04           C  
ANISOU 2037  CG  ASN A1068     4052   8532  10988    726    466   1203       C  
ATOM   2038  OD1 ASN A1068      76.577 178.794 309.036  1.00 61.35           O  
ANISOU 2038  OD1 ASN A1068     3971   8530  10808    701    448   1133       O  
ATOM   2039  ND2 ASN A1068      77.205 179.673 307.064  1.00 62.28           N  
ANISOU 2039  ND2 ASN A1068     4093   8549  11021    735    498   1289       N  
ATOM   2040  N   GLN A1069      77.664 183.394 311.108  1.00 52.78           N  
ANISOU 2040  N   GLN A1069     2782   7153  10120    801    402   1100       N  
ATOM   2041  CA  GLN A1069      78.295 184.343 312.016  1.00 53.24           C  
ANISOU 2041  CA  GLN A1069     2818   7119  10290    813    376   1068       C  
ATOM   2042  C   GLN A1069      77.785 184.191 313.441  1.00 53.10           C  
ANISOU 2042  C   GLN A1069     2785   7171  10220    816    341    959       C  
ATOM   2043  O   GLN A1069      78.494 184.556 314.384  1.00 63.25           O  
ANISOU 2043  O   GLN A1069     4064   8394  11576    812    311    920       O  
ATOM   2044  CB  GLN A1069      78.076 185.770 311.515  1.00 60.92           C  
ANISOU 2044  CB  GLN A1069     3757   8023  11367    854    391   1114       C  
ATOM   2045  CG  GLN A1069      79.054 186.209 310.427  1.00 60.64           C  
ANISOU 2045  CG  GLN A1069     3731   7873  11435    849    416   1223       C  
ATOM   2046  CD  GLN A1069      78.841 185.505 309.095  1.00 59.57           C  
ANISOU 2046  CD  GLN A1069     3620   7785  11227    841    454   1300       C  
ATOM   2047  OE1 GLN A1069      78.733 184.279 309.025  1.00 58.28           O  
ANISOU 2047  OE1 GLN A1069     3486   7699  10957    815    455   1283       O  
ATOM   2048  NE2 GLN A1069      78.786 186.289 308.027  1.00 54.65           N  
ANISOU 2048  NE2 GLN A1069     2982   7116  10665    866    485   1388       N  
ATOM   2049  N   ASP A1070      76.585 183.645 313.620  1.00 72.37           N  
ANISOU 2049  N   ASP A1070     5217   9740  12539    823    345    912       N  
ATOM   2050  CA  ASP A1070      76.070 183.406 314.960  1.00 73.59           C  
ANISOU 2050  CA  ASP A1070     5355   9975  12632    826    317    813       C  
ATOM   2051  C   ASP A1070      76.626 182.135 315.588  1.00 75.39           C  
ANISOU 2051  C   ASP A1070     5615  10236  12792    779    297    776       C  
ATOM   2052  O   ASP A1070      76.545 181.993 316.811  1.00 78.74           O  
ANISOU 2052  O   ASP A1070     6028  10702  13188    779    269    701       O  
ATOM   2053  CB  ASP A1070      74.539 183.350 314.940  1.00 73.72           C  
ANISOU 2053  CB  ASP A1070     5344  10118  12550    852    330    779       C  
ATOM   2054  CG  ASP A1070      73.900 184.706 315.202  1.00 75.50           C  
ANISOU 2054  CG  ASP A1070     5522  10328  12835    911    332    762       C  
ATOM   2055  OD1 ASP A1070      73.440 184.939 316.344  1.00 77.14           O  
ANISOU 2055  OD1 ASP A1070     5704  10587  13019    936    313    684       O  
ATOM   2056  OD2 ASP A1070      73.862 185.541 314.270  1.00 74.35           O  
ANISOU 2056  OD2 ASP A1070     5366  10121  12761    936    355    828       O  
ATOM   2057  N   VAL A1071      77.174 181.214 314.797  1.00 73.14           N  
ANISOU 2057  N   VAL A1071     5370   9940  12481    743    312    829       N  
ATOM   2058  CA  VAL A1071      77.856 180.037 315.329  1.00 50.85           C  
ANISOU 2058  CA  VAL A1071     2579   7132   9609    699    295    804       C  
ATOM   2059  C   VAL A1071      79.372 180.195 315.275  1.00 67.83           C  
ANISOU 2059  C   VAL A1071     4750   9153  11868    682    286    849       C  
ATOM   2060  O   VAL A1071      80.078 179.724 316.168  1.00 66.98           O  
ANISOU 2060  O   VAL A1071     4654   9031  11763    658    258    812       O  
ATOM   2061  CB  VAL A1071      77.398 178.751 314.599  1.00 50.25           C  
ANISOU 2061  CB  VAL A1071     2532   7139   9420    670    316    823       C  
ATOM   2062  CG1 VAL A1071      77.342 178.951 313.110  1.00 50.39           C  
ANISOU 2062  CG1 VAL A1071     2560   7126   9461    680    351    911       C  
ATOM   2063  CG2 VAL A1071      78.320 177.586 314.919  1.00 49.64           C  
ANISOU 2063  CG2 VAL A1071     2494   7051   9317    627    305    818       C  
ATOM   2064  N   ASP A1072      79.883 180.867 314.241  1.00 68.96           N  
ANISOU 2064  N   ASP A1072     4896   9204  12102    695    309    932       N  
ATOM   2065  CA  ASP A1072      81.303 181.204 314.192  1.00 68.83           C  
ANISOU 2065  CA  ASP A1072     4890   9058  12205    682    301    979       C  
ATOM   2066  C   ASP A1072      81.730 181.962 315.441  1.00 51.85           C  
ANISOU 2066  C   ASP A1072     2712   6853  10135    687    259    919       C  
ATOM   2067  O   ASP A1072      82.735 181.625 316.077  1.00 63.84           O  
ANISOU 2067  O   ASP A1072     4242   8322  11691    660    233    907       O  
ATOM   2068  CB  ASP A1072      81.604 182.038 312.946  1.00 69.31           C  
ANISOU 2068  CB  ASP A1072     4945   9032  12357    701    333   1076       C  
ATOM   2069  CG  ASP A1072      81.950 181.190 311.750  1.00 51.60           C  
ANISOU 2069  CG  ASP A1072     2738   6795  10073    686    369   1155       C  
ATOM   2070  OD1 ASP A1072      81.651 179.978 311.776  1.00 54.05           O  
ANISOU 2070  OD1 ASP A1072     3074   7191  10270    666    372   1130       O  
ATOM   2071  OD2 ASP A1072      82.523 181.737 310.786  1.00 51.99           O  
ANISOU 2071  OD2 ASP A1072     2786   6762  10204    697    395   1244       O  
ATOM   2072  N   ALA A1073      80.977 183.001 315.802  1.00 52.38           N  
ANISOU 2072  N   ALA A1073     2742   6928  10231    723    252    882       N  
ATOM   2073  CA  ALA A1073      81.282 183.763 317.002  1.00 52.90           C  
ANISOU 2073  CA  ALA A1073     2774   6938  10386    733    212    825       C  
ATOM   2074  C   ALA A1073      80.797 183.077 318.275  1.00 73.22           C  
ANISOU 2074  C   ALA A1073     5339   9606  12874    726    184    736       C  
ATOM   2075  O   ALA A1073      81.248 183.440 319.366  1.00 75.37           O  
ANISOU 2075  O   ALA A1073     5585   9824  13229    724    147    691       O  
ATOM   2076  CB  ALA A1073      80.679 185.165 316.908  1.00 61.87           C  
ANISOU 2076  CB  ALA A1073     3865   8027  11614    780    218    829       C  
ATOM   2077  N   ALA A1074      79.893 182.102 318.168  1.00 70.97           N  
ANISOU 2077  N   ALA A1074     5073   9460  12433    720    200    709       N  
ATOM   2078  CA  ALA A1074      79.492 181.335 319.340  1.00 51.69           C  
ANISOU 2078  CA  ALA A1074     2624   7111   9905    708    177    633       C  
ATOM   2079  C   ALA A1074      80.417 180.163 319.616  1.00 51.05           C  
ANISOU 2079  C   ALA A1074     2581   7029   9788    659    162    634       C  
ATOM   2080  O   ALA A1074      80.303 179.549 320.681  1.00 50.87           O  
ANISOU 2080  O   ALA A1074     2551   7067   9712    645    138    576       O  
ATOM   2081  CB  ALA A1074      78.060 180.818 319.189  1.00 55.34           C  
ANISOU 2081  CB  ALA A1074     3082   7724  10222    721    198    601       C  
ATOM   2082  N   VAL A1075      81.319 179.844 318.690  1.00 50.76           N  
ANISOU 2082  N   VAL A1075     2581   6926   9778    637    178    701       N  
ATOM   2083  CA  VAL A1075      82.274 178.763 318.897  1.00 66.60           C  
ANISOU 2083  CA  VAL A1075     4622   8921  11763    596    167    710       C  
ATOM   2084  C   VAL A1075      83.577 179.274 319.507  1.00 50.68           C  
ANISOU 2084  C   VAL A1075     2593   6778   9885    583    134    721       C  
ATOM   2085  O   VAL A1075      84.224 178.550 320.270  1.00 50.45           O  
ANISOU 2085  O   VAL A1075     2573   6749   9845    554    108    698       O  
ATOM   2086  CB  VAL A1075      82.526 178.017 317.572  1.00 66.72           C  
ANISOU 2086  CB  VAL A1075     4674   8922  11753    580    207    790       C  
ATOM   2087  CG1 VAL A1075      83.884 178.382 316.972  1.00 67.99           C  
ANISOU 2087  CG1 VAL A1075     4847   8947  12038    572    213    869       C  
ATOM   2088  CG2 VAL A1075      82.411 176.523 317.780  1.00 49.15           C  
ANISOU 2088  CG2 VAL A1075     2479   6783   9412    547    209    768       C  
ATOM   2089  N   ARG A1076      83.973 180.512 319.194  1.00 51.38           N  
ANISOU 2089  N   ARG A1076     2657   6756  10110    603    131    757       N  
ATOM   2090  CA  ARG A1076      85.115 181.112 319.871  1.00 51.97           C  
ANISOU 2090  CA  ARG A1076     2708   6706  10332    589     92    759       C  
ATOM   2091  C   ARG A1076      84.828 181.294 321.354  1.00 66.90           C  
ANISOU 2091  C   ARG A1076     4561   8620  12239    593     46    671       C  
ATOM   2092  O   ARG A1076      85.697 181.044 322.197  1.00 67.56           O  
ANISOU 2092  O   ARG A1076     4637   8658  12375    566      6    649       O  
ATOM   2093  CB  ARG A1076      85.464 182.455 319.232  1.00 63.12           C  
ANISOU 2093  CB  ARG A1076     4094   7994  11893    609     98    813       C  
ATOM   2094  CG  ARG A1076      85.864 182.397 317.768  1.00 65.44           C  
ANISOU 2094  CG  ARG A1076     4420   8253  12192    608    143    910       C  
ATOM   2095  CD  ARG A1076      85.992 183.810 317.232  1.00 69.90           C  
ANISOU 2095  CD  ARG A1076     4951   8707  12899    631    150    958       C  
ATOM   2096  NE  ARG A1076      86.736 184.654 318.164  1.00 73.80           N  
ANISOU 2096  NE  ARG A1076     5403   9083  13555    622    101    934       N  
ATOM   2097  CZ  ARG A1076      86.598 185.973 318.255  1.00 75.50           C  
ANISOU 2097  CZ  ARG A1076     5572   9208  13906    645     89    935       C  
ATOM   2098  NH1 ARG A1076      85.733 186.604 317.471  1.00 55.29           N  
ANISOU 2098  NH1 ARG A1076     3005   6669  11332    680    126    961       N  
ATOM   2099  NH2 ARG A1076      87.318 186.658 319.135  1.00 75.72           N  
ANISOU 2099  NH2 ARG A1076     5559   9123  14087    631     38    907       N  
ATOM   2100  N   GLY A1077      83.612 181.731 321.690  1.00 66.40           N  
ANISOU 2100  N   GLY A1077     4469   8628  12132    628     51    620       N  
ATOM   2101  CA  GLY A1077      83.219 181.786 323.087  1.00 66.80           C  
ANISOU 2101  CA  GLY A1077     4483   8719  12178    637     13    534       C  
ATOM   2102  C   GLY A1077      83.337 180.439 323.777  1.00 65.66           C  
ANISOU 2102  C   GLY A1077     4362   8668  11919    603     -1    501       C  
ATOM   2103  O   GLY A1077      83.720 180.363 324.946  1.00 65.35           O  
ANISOU 2103  O   GLY A1077     4298   8615  11916    591    -45    450       O  
ATOM   2104  N   ILE A1078      83.020 179.359 323.059  1.00 51.35           N  
ANISOU 2104  N   ILE A1078     2593   6945   9971    586     35    529       N  
ATOM   2105  CA  ILE A1078      83.194 178.019 323.611  1.00 50.70           C  
ANISOU 2105  CA  ILE A1078     2537   6942   9786    550     25    505       C  
ATOM   2106  C   ILE A1078      84.673 177.693 323.748  1.00 50.67           C  
ANISOU 2106  C   ILE A1078     2550   6841   9860    516      0    538       C  
ATOM   2107  O   ILE A1078      85.152 177.314 324.824  1.00 63.52           O  
ANISOU 2107  O   ILE A1078     4165   8470  11498    495    -39    499       O  
ATOM   2108  CB  ILE A1078      82.483 176.975 322.737  1.00 49.90           C  
ANISOU 2108  CB  ILE A1078     2475   6947   9537    540     67    526       C  
ATOM   2109  CG1 ILE A1078      80.993 177.266 322.658  1.00 70.37           C  
ANISOU 2109  CG1 ILE A1078     5044   9643  12050    572     88    493       C  
ATOM   2110  CG2 ILE A1078      82.690 175.591 323.311  1.00 49.30           C  
ANISOU 2110  CG2 ILE A1078     2423   6941   9366    502     58    503       C  
ATOM   2111  CD1 ILE A1078      80.242 176.237 321.859  1.00 69.98           C  
ANISOU 2111  CD1 ILE A1078     5028   9697  11865    556    122    505       C  
ATOM   2112  N   LEU A1079      85.417 177.823 322.650  1.00 72.84           N  
ANISOU 2112  N   LEU A1079     5385   9566  12723    509     24    613       N  
ATOM   2113  CA  LEU A1079      86.839 177.512 322.683  1.00 76.88           C  
ANISOU 2113  CA  LEU A1079     5913   9987  13312    479      6    654       C  
ATOM   2114  C   LEU A1079      87.612 178.450 323.603  1.00 82.71           C  
ANISOU 2114  C   LEU A1079     6606  10618  14203    476    -48    631       C  
ATOM   2115  O   LEU A1079      88.700 178.087 324.063  1.00 86.99           O  
ANISOU 2115  O   LEU A1079     7150  11107  14797    447    -79    642       O  
ATOM   2116  CB  LEU A1079      87.421 177.546 321.265  1.00 75.40           C  
ANISOU 2116  CB  LEU A1079     5758   9734  13157    479     46    745       C  
ATOM   2117  CG  LEU A1079      87.502 176.236 320.460  1.00 49.61           C  
ANISOU 2117  CG  LEU A1079     2544   6527   9779    463     85    784       C  
ATOM   2118  CD1 LEU A1079      86.830 175.060 321.164  1.00 49.02           C  
ANISOU 2118  CD1 LEU A1079     2483   6577   9567    447     79    723       C  
ATOM   2119  CD2 LEU A1079      86.926 176.422 319.058  1.00 49.52           C  
ANISOU 2119  CD2 LEU A1079     2548   6522   9744    484    136    840       C  
ATOM   2120  N   ARG A1080      87.084 179.639 323.892  1.00 52.14           N  
ANISOU 2120  N   ARG A1080     2691   6710  10409    504    -63    598       N  
ATOM   2121  CA  ARG A1080      87.700 180.529 324.865  1.00 53.03           C  
ANISOU 2121  CA  ARG A1080     2755   6721  10674    501   -122    561       C  
ATOM   2122  C   ARG A1080      87.028 180.446 326.229  1.00 53.25           C  
ANISOU 2122  C   ARG A1080     2749   6823  10662    510   -160    465       C  
ATOM   2123  O   ARG A1080      87.226 181.337 327.062  1.00 69.23           O  
ANISOU 2123  O   ARG A1080     4723   8770  12810    519   -209    416       O  
ATOM   2124  CB  ARG A1080      87.694 181.972 324.358  1.00 53.84           C  
ANISOU 2124  CB  ARG A1080     2825   6711  10921    527   -121    586       C  
ATOM   2125  N   ASN A1081      86.241 179.399 326.477  1.00 52.55           N  
ANISOU 2125  N   ASN A1081     2681   6876  10409    509   -139    436       N  
ATOM   2126  CA  ASN A1081      85.589 179.202 327.764  1.00 66.46           C  
ANISOU 2126  CA  ASN A1081     4410   8721  12120    518   -170    353       C  
ATOM   2127  C   ASN A1081      86.371 178.194 328.590  1.00 65.23           C  
ANISOU 2127  C   ASN A1081     4264   8588  11932    477   -206    337       C  
ATOM   2128  O   ASN A1081      86.893 177.207 328.061  1.00 63.53           O  
ANISOU 2128  O   ASN A1081     4095   8393  11652    448   -184    386       O  
ATOM   2129  CB  ASN A1081      84.143 178.723 327.604  1.00 66.54           C  
ANISOU 2129  CB  ASN A1081     4428   8882  11972    542   -127    331       C  
ATOM   2130  CG  ASN A1081      83.274 179.082 328.798  1.00 52.78           C  
ANISOU 2130  CG  ASN A1081     2635   7202  10217    573   -151    250       C  
ATOM   2131  OD1 ASN A1081      83.098 178.285 329.723  1.00 52.59           O  
ANISOU 2131  OD1 ASN A1081     2603   7265  10112    558   -170    209       O  
ATOM   2132  ND2 ASN A1081      82.729 180.295 328.784  1.00 53.51           N  
ANISOU 2132  ND2 ASN A1081     2689   7250  10393    618   -150    228       N  
ATOM   2133  N   ALA A1082      86.437 178.450 329.896  1.00 66.23           N  
ANISOU 2133  N   ALA A1082     4347   8711  12108    478   -262    267       N  
ATOM   2134  CA  ALA A1082      87.230 177.615 330.787  1.00 67.06           C  
ANISOU 2134  CA  ALA A1082     4452   8829  12197    440   -305    249       C  
ATOM   2135  C   ALA A1082      86.682 176.196 330.880  1.00 66.76           C  
ANISOU 2135  C   ALA A1082     4448   8939  11980    424   -273    251       C  
ATOM   2136  O   ALA A1082      87.459 175.238 330.981  1.00 51.66           O  
ANISOU 2136  O   ALA A1082     2562   7033  10033    388   -281    277       O  
ATOM   2137  CB  ALA A1082      87.289 178.254 332.171  1.00 53.90           C  
ANISOU 2137  CB  ALA A1082     2726   7133  10622    448   -375    164       C  
ATOM   2138  N   LYS A1083      85.363 176.032 330.828  1.00 65.56           N  
ANISOU 2138  N   LYS A1083     4293   8902  11715    450   -236    226       N  
ATOM   2139  CA  LYS A1083      84.759 174.761 331.200  1.00 62.57           C  
ANISOU 2139  CA  LYS A1083     3931   8665  11179    433   -219    213       C  
ATOM   2140  C   LYS A1083      84.347 173.906 330.009  1.00 60.30           C  
ANISOU 2140  C   LYS A1083     3698   8438  10777    422   -159    265       C  
ATOM   2141  O   LYS A1083      84.571 172.692 330.030  1.00 58.78           O  
ANISOU 2141  O   LYS A1083     3536   8299  10499    390   -150    279       O  
ATOM   2142  CB  LYS A1083      83.545 175.006 332.103  1.00 62.19           C  
ANISOU 2142  CB  LYS A1083     3836   8718  11075    466   -224    147       C  
ATOM   2143  CG  LYS A1083      83.282 173.894 333.113  1.00 51.28           C  
ANISOU 2143  CG  LYS A1083     2447   7454   9583    443   -238    116       C  
ATOM   2144  CD  LYS A1083      82.151 174.260 334.072  1.00 51.81           C  
ANISOU 2144  CD  LYS A1083     2459   7612   9614    482   -245     55       C  
ATOM   2145  CE  LYS A1083      82.637 175.108 335.244  1.00 72.56           C  
ANISOU 2145  CE  LYS A1083     5033  10165  12370    498   -312    -10       C  
ATOM   2146  NZ  LYS A1083      82.994 176.505 334.865  1.00 73.48           N  
ANISOU 2146  NZ  LYS A1083     5132  10141  12645    527   -328    -20       N  
ATOM   2147  N   LEU A1084      83.746 174.491 328.972  1.00 59.90           N  
ANISOU 2147  N   LEU A1084     3656   8377  10726    449   -119    291       N  
ATOM   2148  CA  LEU A1084      83.197 173.701 327.876  1.00 49.45           C  
ANISOU 2148  CA  LEU A1084     2377   7119   9292    440    -67    328       C  
ATOM   2149  C   LEU A1084      84.147 173.560 326.697  1.00 57.34           C  
ANISOU 2149  C   LEU A1084     3422   8023  10341    424    -46    399       C  
ATOM   2150  O   LEU A1084      83.793 172.900 325.715  1.00 57.51           O  
ANISOU 2150  O   LEU A1084     3482   8086  10284    416     -6    432       O  
ATOM   2151  CB  LEU A1084      81.857 174.282 327.398  1.00 49.55           C  
ANISOU 2151  CB  LEU A1084     2373   7198   9257    477    -35    316       C  
ATOM   2152  CG  LEU A1084      81.574 175.783 327.393  1.00 58.91           C  
ANISOU 2152  CG  LEU A1084     3518   8318  10546    523    -41    305       C  
ATOM   2153  CD1 LEU A1084      80.614 176.111 326.268  1.00 58.43           C  
ANISOU 2153  CD1 LEU A1084     3466   8296  10438    548      5    331       C  
ATOM   2154  CD2 LEU A1084      80.968 176.211 328.716  1.00 60.03           C  
ANISOU 2154  CD2 LEU A1084     3604   8511  10693    549    -70    237       C  
ATOM   2155  N   LYS A1085      85.340 174.158 326.761  1.00 56.88           N  
ANISOU 2155  N   LYS A1085     3358   7839  10414    419    -73    425       N  
ATOM   2156  CA  LYS A1085      86.324 173.905 325.709  1.00 57.86           C  
ANISOU 2156  CA  LYS A1085     3523   7879  10581    404    -52    499       C  
ATOM   2157  C   LYS A1085      86.787 172.453 325.686  1.00 48.60           C  
ANISOU 2157  C   LYS A1085     2389   6748   9328    371    -42    518       C  
ATOM   2158  O   LYS A1085      86.750 171.835 324.606  1.00 48.08           O  
ANISOU 2158  O   LYS A1085     2364   6691   9212    367      0    564       O  
ATOM   2159  CB  LYS A1085      87.509 174.865 325.848  1.00 61.55           C  
ANISOU 2159  CB  LYS A1085     3969   8205  11214    404    -85    524       C  
ATOM   2160  CG  LYS A1085      88.672 174.488 324.935  1.00 65.16           C  
ANISOU 2160  CG  LYS A1085     4463   8579  11716    386    -66    605       C  
ATOM   2161  CD  LYS A1085      89.930 175.295 325.217  1.00 68.20           C  
ANISOU 2161  CD  LYS A1085     4821   8828  12263    377   -105    631       C  
ATOM   2162  CE  LYS A1085      91.112 174.764 324.413  1.00 50.20           C  
ANISOU 2162  CE  LYS A1085     2575   6480  10019    360    -84    715       C  
ATOM   2163  NZ  LYS A1085      90.852 174.758 322.944  1.00 49.85           N  
ANISOU 2163  NZ  LYS A1085     2566   6430   9945    378    -24    779       N  
ATOM   2164  N   PRO A1086      87.226 171.847 326.798  1.00 48.63           N  
ANISOU 2164  N   PRO A1086     2382   6775   9320    348    -78    486       N  
ATOM   2165  CA  PRO A1086      87.779 170.482 326.699  1.00 48.05           C  
ANISOU 2165  CA  PRO A1086     2347   6725   9186    318    -66    513       C  
ATOM   2166  C   PRO A1086      86.789 169.465 326.162  1.00 55.84           C  
ANISOU 2166  C   PRO A1086     3364   7817  10037    311    -25    508       C  
ATOM   2167  O   PRO A1086      87.123 168.687 325.260  1.00 56.59           O  
ANISOU 2167  O   PRO A1086     3500   7895  10106    300      9    558       O  
ATOM   2168  CB  PRO A1086      88.190 170.172 328.147  1.00 57.86           C  
ANISOU 2168  CB  PRO A1086     3560   7989  10436    298   -118    468       C  
ATOM   2169  CG  PRO A1086      87.330 171.055 328.986  1.00 57.92           C  
ANISOU 2169  CG  PRO A1086     3518   8039  10450    319   -145    403       C  
ATOM   2170  CD  PRO A1086      87.216 172.323 328.195  1.00 49.22           C  
ANISOU 2170  CD  PRO A1086     2407   6858   9435    349   -132    424       C  
ATOM   2171  N   VAL A1087      85.567 169.464 326.693  1.00 54.95           N  
ANISOU 2171  N   VAL A1087     3228   7809   9842    317    -27    451       N  
ATOM   2172  CA  VAL A1087      84.558 168.499 326.269  1.00 46.80           C  
ANISOU 2172  CA  VAL A1087     2217   6880   8684    305      7    442       C  
ATOM   2173  C   VAL A1087      84.268 168.651 324.782  1.00 72.47           C  
ANISOU 2173  C   VAL A1087     5498  10105  11931    318     51    488       C  
ATOM   2174  O   VAL A1087      84.234 167.665 324.036  1.00 72.45           O  
ANISOU 2174  O   VAL A1087     5533  10120  11875    300     80    517       O  
ATOM   2175  CB  VAL A1087      83.288 168.667 327.118  1.00 51.34           C  
ANISOU 2175  CB  VAL A1087     2752   7569   9185    314     -3    376       C  
ATOM   2176  CG1 VAL A1087      83.098 170.134 327.446  1.00 51.89           C  
ANISOU 2176  CG1 VAL A1087     2779   7603   9334    352    -23    355       C  
ATOM   2177  CG2 VAL A1087      82.075 168.113 326.392  1.00 46.56           C  
ANISOU 2177  CG2 VAL A1087     2161   7055   8475    309     34    369       C  
ATOM   2178  N   TYR A1088      84.062 169.893 324.331  1.00 46.94           N  
ANISOU 2178  N   TYR A1088     2247   6828   8760    350     55    497       N  
ATOM   2179  CA  TYR A1088      83.802 170.156 322.918  1.00 71.79           C  
ANISOU 2179  CA  TYR A1088     5418   9950  11910    365     95    545       C  
ATOM   2180  C   TYR A1088      84.871 169.518 322.033  1.00 72.90           C  
ANISOU 2180  C   TYR A1088     5601  10014  12082    352    116    613       C  
ATOM   2181  O   TYR A1088      84.554 168.841 321.047  1.00 74.26           O  
ANISOU 2181  O   TYR A1088     5803  10209  12202    346    152    645       O  
ATOM   2182  CB  TYR A1088      83.716 171.670 322.692  1.00 47.38           C  
ANISOU 2182  CB  TYR A1088     2298   6798   8908    401     91    552       C  
ATOM   2183  CG  TYR A1088      83.571 172.148 321.254  1.00 63.88           C  
ANISOU 2183  CG  TYR A1088     4405   8845  11020    421    128    608       C  
ATOM   2184  CD1 TYR A1088      83.238 171.285 320.220  1.00 62.64           C  
ANISOU 2184  CD1 TYR A1088     4279   8719  10804    410    165    647       C  
ATOM   2185  CD2 TYR A1088      83.768 173.479 320.939  1.00 67.00           C  
ANISOU 2185  CD2 TYR A1088     4778   9160  11518    451    127    632       C  
ATOM   2186  CE1 TYR A1088      83.124 171.732 318.925  1.00 61.31           C  
ANISOU 2186  CE1 TYR A1088     4119   8506  10671    428    199    709       C  
ATOM   2187  CE2 TYR A1088      83.647 173.935 319.641  1.00 68.19           C  
ANISOU 2187  CE2 TYR A1088     4937   9264  11707    468    162    696       C  
ATOM   2188  CZ  TYR A1088      83.323 173.054 318.637  1.00 65.18           C  
ANISOU 2188  CZ  TYR A1088     4586   8920  11259    458    198    735       C  
ATOM   2189  OH  TYR A1088      83.198 173.486 317.337  1.00 67.11           O  
ANISOU 2189  OH  TYR A1088     4837   9125  11537    477    233    800       O  
ATOM   2190  N   ASP A1089      86.145 169.709 322.377  1.00 70.21           N  
ANISOU 2190  N   ASP A1089     5261   9581  11835    347     96    641       N  
ATOM   2191  CA  ASP A1089      87.209 169.134 321.561  1.00 67.49           C  
ANISOU 2191  CA  ASP A1089     4953   9164  11528    340    119    712       C  
ATOM   2192  C   ASP A1089      87.068 167.622 321.420  1.00 62.69           C  
ANISOU 2192  C   ASP A1089     4377   8615  10826    315    138    715       C  
ATOM   2193  O   ASP A1089      87.429 167.062 320.379  1.00 53.96           O  
ANISOU 2193  O   ASP A1089     3303   7478   9720    316    174    774       O  
ATOM   2194  CB  ASP A1089      88.573 169.501 322.145  1.00 66.26           C  
ANISOU 2194  CB  ASP A1089     4784   8908  11482    334     87    735       C  
ATOM   2195  CG  ASP A1089      88.930 170.961 321.917  1.00 63.08           C  
ANISOU 2195  CG  ASP A1089     4355   8415  11197    357     76    757       C  
ATOM   2196  OD1 ASP A1089      88.792 171.438 320.767  1.00 47.62           O  
ANISOU 2196  OD1 ASP A1089     2407   6420   9268    376    111    808       O  
ATOM   2197  OD2 ASP A1089      89.336 171.635 322.889  1.00 62.15           O  
ANISOU 2197  OD2 ASP A1089     4202   8257  11154    354     32    727       O  
ATOM   2198  N   SER A1090      86.519 166.947 322.434  1.00 45.76           N  
ANISOU 2198  N   SER A1090     2222   6557   8608    293    117    656       N  
ATOM   2199  CA  SER A1090      86.363 165.497 322.357  1.00 52.74           C  
ANISOU 2199  CA  SER A1090     3133   7493   9412    266    134    658       C  
ATOM   2200  C   SER A1090      85.161 165.081 321.518  1.00 50.85           C  
ANISOU 2200  C   SER A1090     2907   7328   9087    263    167    652       C  
ATOM   2201  O   SER A1090      85.186 164.013 320.896  1.00 49.54           O  
ANISOU 2201  O   SER A1090     2770   7170   8883    247    194    683       O  
ATOM   2202  CB  SER A1090      86.240 164.904 323.762  1.00 54.36           C  
ANISOU 2202  CB  SER A1090     3320   7761   9573    241    100    602       C  
ATOM   2203  OG  SER A1090      85.227 165.555 324.511  1.00 55.60           O  
ANISOU 2203  OG  SER A1090     3439   7993   9693    248     78    537       O  
ATOM   2204  N   LEU A1091      84.113 165.899 321.483  1.00 45.12           N  
ANISOU 2204  N   LEU A1091     2156   6653   8336    278    165    615       N  
ATOM   2205  CA  LEU A1091      82.876 165.510 320.821  1.00 52.56           C  
ANISOU 2205  CA  LEU A1091     3102   7675   9194    271    190    602       C  
ATOM   2206  C   LEU A1091      83.039 165.475 319.307  1.00 52.23           C  
ANISOU 2206  C   LEU A1091     3088   7586   9171    283    228    668       C  
ATOM   2207  O   LEU A1091      83.627 166.379 318.705  1.00 45.09           O  
ANISOU 2207  O   LEU A1091     2183   6600   8348    312    237    715       O  
ATOM   2208  CB  LEU A1091      81.754 166.472 321.199  1.00 45.19           C  
ANISOU 2208  CB  LEU A1091     2130   6806   8236    289    177    550       C  
ATOM   2209  CG  LEU A1091      81.431 166.485 322.687  1.00 45.36           C  
ANISOU 2209  CG  LEU A1091     2117   6890   8228    280    143    483       C  
ATOM   2210  CD1 LEU A1091      80.438 167.581 323.000  1.00 45.77           C  
ANISOU 2210  CD1 LEU A1091     2126   6992   8272    310    135    442       C  
ATOM   2211  CD2 LEU A1091      80.894 165.129 323.094  1.00 45.00           C  
ANISOU 2211  CD2 LEU A1091     2078   6927   8092    240    145    455       C  
ATOM   2212  N   ASP A1092      82.492 164.426 318.695  1.00 44.47           N  
ANISOU 2212  N   ASP A1092     2124   6650   8122    261    252    679       N  
ATOM   2213  CA  ASP A1092      82.542 164.245 317.253  1.00 70.61           C  
ANISOU 2213  CA  ASP A1092     5458   9930  11441    271    289    741       C  
ATOM   2214  C   ASP A1092      81.697 165.309 316.547  1.00 71.53           C  
ANISOU 2214  C   ASP A1092     5556  10066  11558    297    299    741       C  
ATOM   2215  O   ASP A1092      80.962 166.074 317.175  1.00 72.07           O  
ANISOU 2215  O   ASP A1092     5590  10175  11618    305    279    694       O  
ATOM   2216  CB  ASP A1092      82.071 162.838 316.882  1.00 70.75           C  
ANISOU 2216  CB  ASP A1092     5493   9998  11390    237    308    749       C  
ATOM   2217  CG  ASP A1092      80.776 162.442 317.585  1.00 71.17           C  
ANISOU 2217  CG  ASP A1092     5523  10157  11360    205    291    680       C  
ATOM   2218  OD1 ASP A1092      79.928 163.323 317.834  1.00 44.20           O  
ANISOU 2218  OD1 ASP A1092     2079   6788   7928    217    278    637       O  
ATOM   2219  OD2 ASP A1092      80.604 161.242 317.885  1.00 71.37           O  
ANISOU 2219  OD2 ASP A1092     5558  10218  11341    167    292    671       O  
ATOM   2220  N   ALA A1093      81.798 165.338 315.214  1.00 44.67           N  
ANISOU 2220  N   ALA A1093     2170   6632   8172    312    332    803       N  
ATOM   2221  CA  ALA A1093      81.140 166.387 314.439  1.00 45.04           C  
ANISOU 2221  CA  ALA A1093     2196   6679   8239    341    344    825       C  
ATOM   2222  C   ALA A1093      79.637 166.415 314.687  1.00 45.06           C  
ANISOU 2222  C   ALA A1093     2170   6785   8164    327    334    765       C  
ATOM   2223  O   ALA A1093      79.026 167.490 314.716  1.00 45.45           O  
ANISOU 2223  O   ALA A1093     2188   6845   8235    352    328    755       O  
ATOM   2224  CB  ALA A1093      81.431 166.202 312.949  1.00 55.34           C  
ANISOU 2224  CB  ALA A1093     3523   7949   9556    356    383    900       C  
ATOM   2225  N   VAL A1094      79.024 165.246 314.874  1.00 44.71           N  
ANISOU 2225  N   VAL A1094     2134   6815   8038    288    332    731       N  
ATOM   2226  CA  VAL A1094      77.578 165.187 315.076  1.00 44.77           C  
ANISOU 2226  CA  VAL A1094     2113   6921   7976    270    325    680       C  
ATOM   2227  C   VAL A1094      77.200 165.821 316.410  1.00 44.95           C  
ANISOU 2227  C   VAL A1094     2104   6981   7995    277    294    611       C  
ATOM   2228  O   VAL A1094      76.450 166.802 316.462  1.00 45.34           O  
ANISOU 2228  O   VAL A1094     2118   7055   8054    302    291    594       O  
ATOM   2229  CB  VAL A1094      77.078 163.735 314.988  1.00 44.50           C  
ANISOU 2229  CB  VAL A1094     2090   6941   7877    221    331    675       C  
ATOM   2230  CG1 VAL A1094      75.570 163.708 315.137  1.00 44.64           C  
ANISOU 2230  CG1 VAL A1094     2075   7052   7833    200    324    629       C  
ATOM   2231  CG2 VAL A1094      77.509 163.091 313.676  1.00 45.93           C  
ANISOU 2231  CG2 VAL A1094     2299   7085   8069    219    363    752       C  
ATOM   2232  N   ARG A1095      77.723 165.267 317.508  1.00 72.49           N  
ANISOU 2232  N   ARG A1095     5597  10471  11475    257    274    577       N  
ATOM   2233  CA  ARG A1095      77.397 165.718 318.859  1.00 69.47           C  
ANISOU 2233  CA  ARG A1095     5182  10133  11081    261    245    511       C  
ATOM   2234  C   ARG A1095      77.889 167.129 319.159  1.00 66.12           C  
ANISOU 2234  C   ARG A1095     4736   9651  10735    307    233    518       C  
ATOM   2235  O   ARG A1095      77.534 167.677 320.208  1.00 45.63           O  
ANISOU 2235  O   ARG A1095     2108   7097   8134    320    211    464       O  
ATOM   2236  CB  ARG A1095      77.980 164.746 319.895  1.00 44.71           C  
ANISOU 2236  CB  ARG A1095     2056   7003   7927    229    228    488       C  
ATOM   2237  CG  ARG A1095      77.413 163.323 319.825  1.00 44.40           C  
ANISOU 2237  CG  ARG A1095     2030   7020   7821    179    237    480       C  
ATOM   2238  CD  ARG A1095      78.117 162.374 320.793  1.00 44.20           C  
ANISOU 2238  CD  ARG A1095     2016   6989   7788    151    221    469       C  
ATOM   2239  NE  ARG A1095      77.549 161.024 320.773  1.00 67.37           N  
ANISOU 2239  NE  ARG A1095     4960   9971  10665    100    230    464       N  
ATOM   2240  CZ  ARG A1095      77.967 160.036 319.986  1.00 68.76           C  
ANISOU 2240  CZ  ARG A1095     5170  10112  10844     78    251    518       C  
ATOM   2241  NH1 ARG A1095      78.961 160.237 319.132  1.00 70.97           N  
ANISOU 2241  NH1 ARG A1095     5476  10310  11178    105    268    580       N  
ATOM   2242  NH2 ARG A1095      77.389 158.841 320.047  1.00 67.91           N  
ANISOU 2242  NH2 ARG A1095     5066  10048  10689     30    256    515       N  
ATOM   2243  N   ARG A1096      78.698 167.724 318.284  1.00 64.05           N  
ANISOU 2243  N   ARG A1096     4490   9294  10553    332    248    584       N  
ATOM   2244  CA  ARG A1096      79.187 169.074 318.538  1.00 46.01           C  
ANISOU 2244  CA  ARG A1096     2183   6940   8358    371    237    595       C  
ATOM   2245  C   ARG A1096      78.081 170.098 318.373  1.00 46.44           C  
ANISOU 2245  C   ARG A1096     2199   7036   8409    402    241    576       C  
ATOM   2246  O   ARG A1096      77.979 171.046 319.159  1.00 47.20           O  
ANISOU 2246  O   ARG A1096     2264   7131   8540    428    221    542       O  
ATOM   2247  CB  ARG A1096      80.333 169.405 317.596  1.00 46.10           C  
ANISOU 2247  CB  ARG A1096     2220   6836   8460    387    254    675       C  
ATOM   2248  CG  ARG A1096      81.647 168.850 318.023  1.00 45.90           C  
ANISOU 2248  CG  ARG A1096     2220   6746   8475    371    244    692       C  
ATOM   2249  CD  ARG A1096      82.666 169.142 316.970  1.00 46.04           C  
ANISOU 2249  CD  ARG A1096     2259   6656   8577    387    268    777       C  
ATOM   2250  NE  ARG A1096      83.986 168.695 317.374  1.00 71.91           N  
ANISOU 2250  NE  ARG A1096     5556   9864  11904    375    258    799       N  
ATOM   2251  CZ  ARG A1096      85.108 169.171 316.857  1.00 66.27           C  
ANISOU 2251  CZ  ARG A1096     4850   9042  11289    390    268    866       C  
ATOM   2252  NH1 ARG A1096      85.054 170.120 315.932  1.00 62.01           N  
ANISOU 2252  NH1 ARG A1096     4301   8453  10808    418    289    916       N  
ATOM   2253  NH2 ARG A1096      86.281 168.707 317.267  1.00 64.77           N  
ANISOU 2253  NH2 ARG A1096     4673   8794  11141    378    258    886       N  
ATOM   2254  N   ALA A1097      77.256 169.933 317.339  1.00 46.41           N  
ANISOU 2254  N   ALA A1097     2197   7069   8367    400    265    600       N  
ATOM   2255  CA  ALA A1097      76.248 170.938 317.033  1.00 61.53           C  
ANISOU 2255  CA  ALA A1097     4075   9016  10287    433    273    594       C  
ATOM   2256  C   ALA A1097      75.278 171.127 318.188  1.00 47.05           C  
ANISOU 2256  C   ALA A1097     2201   7274   8400    437    253    515       C  
ATOM   2257  O   ALA A1097      74.731 172.220 318.368  1.00 68.62           O  
ANISOU 2257  O   ALA A1097     4895  10016  11160    476    251    500       O  
ATOM   2258  CB  ALA A1097      75.496 170.556 315.759  1.00 61.90           C  
ANISOU 2258  CB  ALA A1097     4131   9097  10293    424    300    632       C  
ATOM   2259  N   ALA A1098      75.067 170.089 318.993  1.00 46.69           N  
ANISOU 2259  N   ALA A1098     2160   7297   8282    400    239    464       N  
ATOM   2260  CA  ALA A1098      74.162 170.221 320.124  1.00 46.89           C  
ANISOU 2260  CA  ALA A1098     2144   7416   8255    405    223    389       C  
ATOM   2261  C   ALA A1098      74.773 171.035 321.256  1.00 47.18           C  
ANISOU 2261  C   ALA A1098     2160   7428   8337    436    197    359       C  
ATOM   2262  O   ALA A1098      74.052 171.765 321.944  1.00 47.62           O  
ANISOU 2262  O   ALA A1098     2172   7537   8385    468    190    317       O  
ATOM   2263  CB  ALA A1098      73.743 168.845 320.623  1.00 46.46           C  
ANISOU 2263  CB  ALA A1098     2099   7438   8115    354    218    346       C  
ATOM   2264  N   LEU A1099      76.084 170.916 321.477  1.00 67.21           N  
ANISOU 2264  N   LEU A1099     4725   9882  10928    428    184    384       N  
ATOM   2265  CA  LEU A1099      76.759 171.883 322.335  1.00 65.27           C  
ANISOU 2265  CA  LEU A1099     4456   9579  10763    459    160    376       C  
ATOM   2266  C   LEU A1099      76.573 173.288 321.785  1.00 61.81           C  
ANISOU 2266  C   LEU A1099     3997   9089  10400    507    169    399       C  
ATOM   2267  O   LEU A1099      76.311 174.234 322.538  1.00 61.17           O  
ANISOU 2267  O   LEU A1099     3873   9009  10360    543    156    371       O  
ATOM   2268  CB  LEU A1099      78.247 171.545 322.450  1.00 47.25           C  
ANISOU 2268  CB  LEU A1099     2208   7199   8546    438    146    409       C  
ATOM   2269  CG  LEU A1099      78.961 171.756 323.789  1.00 47.54           C  
ANISOU 2269  CG  LEU A1099     2223   7208   8632    439    109    381       C  
ATOM   2270  CD1 LEU A1099      78.579 173.070 324.456  1.00 48.27           C  
ANISOU 2270  CD1 LEU A1099     2264   7293   8783    484     93    352       C  
ATOM   2271  CD2 LEU A1099      78.695 170.588 324.715  1.00 55.99           C  
ANISOU 2271  CD2 LEU A1099     3291   8370   9613    405     96    338       C  
ATOM   2272  N   ILE A1100      76.692 173.435 320.463  1.00 59.88           N  
ANISOU 2272  N   ILE A1100     3775   8789  10188    509    195    460       N  
ATOM   2273  CA  ILE A1100      76.387 174.704 319.816  1.00 59.68           C  
ANISOU 2273  CA  ILE A1100     3728   8718  10231    553    209    490       C  
ATOM   2274  C   ILE A1100      74.908 175.030 319.961  1.00 48.76           C  
ANISOU 2274  C   ILE A1100     2303   7440   8782    577    218    448       C  
ATOM   2275  O   ILE A1100      74.513 176.202 319.930  1.00 50.74           O  
ANISOU 2275  O   ILE A1100     2522   7675   9082    623    221    448       O  
ATOM   2276  CB  ILE A1100      76.827 174.649 318.337  1.00 48.37           C  
ANISOU 2276  CB  ILE A1100     2327   7210   8843    547    238    573       C  
ATOM   2277  CG1 ILE A1100      78.346 174.463 318.248  1.00 48.21           C  
ANISOU 2277  CG1 ILE A1100     2340   7079   8899    530    231    617       C  
ATOM   2278  CG2 ILE A1100      76.401 175.902 317.593  1.00 54.00           C  
ANISOU 2278  CG2 ILE A1100     3015   7885   9618    590    255    609       C  
ATOM   2279  CD1 ILE A1100      78.887 174.446 316.831  1.00 59.50           C  
ANISOU 2279  CD1 ILE A1100     3798   8433  10376    530    262    704       C  
ATOM   2280  N   ASN A1101      74.070 174.012 320.152  1.00 48.42           N  
ANISOU 2280  N   ASN A1101     2259   7503   8635    547    221    411       N  
ATOM   2281  CA  ASN A1101      72.643 174.258 320.310  1.00 58.48           C  
ANISOU 2281  CA  ASN A1101     3491   8879   9850    567    229    370       C  
ATOM   2282  C   ASN A1101      72.319 174.763 321.710  1.00 57.80           C  
ANISOU 2282  C   ASN A1101     3361   8848   9754    598    209    306       C  
ATOM   2283  O   ASN A1101      71.626 175.773 321.871  1.00 59.47           O  
ANISOU 2283  O   ASN A1101     3529   9077   9989    649    215    293       O  
ATOM   2284  CB  ASN A1101      71.860 172.985 320.004  1.00 59.87           C  
ANISOU 2284  CB  ASN A1101     3678   9137   9934    518    239    354       C  
ATOM   2285  CG  ASN A1101      70.489 173.273 319.456  1.00 62.19           C  
ANISOU 2285  CG  ASN A1101     3938   9494  10198    533    257    349       C  
ATOM   2286  OD1 ASN A1101      70.106 174.431 319.298  1.00 65.49           O  
ANISOU 2286  OD1 ASN A1101     4324   9900  10659    583    264    358       O  
ATOM   2287  ND2 ASN A1101      69.743 172.225 319.143  1.00 61.07           N  
ANISOU 2287  ND2 ASN A1101     3802   9411   9991    487    265    338       N  
ATOM   2288  N   MET A1102      72.813 174.074 322.736  1.00 55.89           N  
ANISOU 2288  N   MET A1102     3122   8623   9489    573    188    276       N  
ATOM   2289  CA  MET A1102      72.570 174.530 324.098  1.00 49.43           C  
ANISOU 2289  CA  MET A1102     2256   7849   8676    605    170    229       C  
ATOM   2290  C   MET A1102      73.190 175.899 324.337  1.00 83.41           C  
ANISOU 2290  C   MET A1102     6539  12052  13100    656    159    248       C  
ATOM   2291  O   MET A1102      72.589 176.751 325.002  1.00 84.50           O  
ANISOU 2291  O   MET A1102     6627  12218  13260    707    158    221       O  
ATOM   2292  CB  MET A1102      73.116 173.512 325.088  1.00 49.09           C  
ANISOU 2292  CB  MET A1102     2223   7834   8595    564    147    203       C  
ATOM   2293  CG  MET A1102      72.666 172.110 324.806  1.00 48.47           C  
ANISOU 2293  CG  MET A1102     2170   7828   8420    507    157    187       C  
ATOM   2294  SD  MET A1102      72.946 171.131 326.267  1.00 48.34           S  
ANISOU 2294  SD  MET A1102     2142   7872   8353    475    131    143       S  
ATOM   2295  CE  MET A1102      72.808 169.483 325.615  1.00 61.60           C  
ANISOU 2295  CE  MET A1102     3869   9575   9960    400    144    144       C  
ATOM   2296  N   VAL A1103      74.392 176.130 323.799  1.00 49.92           N  
ANISOU 2296  N   VAL A1103     2334   7686   8946    643    153    295       N  
ATOM   2297  CA  VAL A1103      75.022 177.442 323.926  1.00 50.57           C  
ANISOU 2297  CA  VAL A1103     2398   7652   9164    683    141    312       C  
ATOM   2298  C   VAL A1103      74.173 178.503 323.242  1.00 51.08           C  
ANISOU 2298  C   VAL A1103     2436   7716   9255    734    166    326       C  
ATOM   2299  O   VAL A1103      74.057 179.635 323.726  1.00 68.48           O  
ANISOU 2299  O   VAL A1103     4599   9875  11544    784    160    313       O  
ATOM   2300  CB  VAL A1103      76.452 177.408 323.360  1.00 50.31           C  
ANISOU 2300  CB  VAL A1103     2409   7487   9219    654    133    362       C  
ATOM   2301  CG1 VAL A1103      76.978 178.816 323.151  1.00 59.08           C  
ANISOU 2301  CG1 VAL A1103     3502   8469  10477    691    127    388       C  
ATOM   2302  CG2 VAL A1103      77.361 176.648 324.295  1.00 56.19           C  
ANISOU 2302  CG2 VAL A1103     3167   8216   9967    617    101    342       C  
ATOM   2303  N   PHE A1104      73.565 178.153 322.106  1.00 50.72           N  
ANISOU 2303  N   PHE A1104     2411   7715   9145    722    193    353       N  
ATOM   2304  CA  PHE A1104      72.588 179.042 321.487  1.00 51.21           C  
ANISOU 2304  CA  PHE A1104     2443   7799   9215    768    217    364       C  
ATOM   2305  C   PHE A1104      71.374 179.231 322.386  1.00 51.67           C  
ANISOU 2305  C   PHE A1104     2447   7970   9216    805    219    306       C  
ATOM   2306  O   PHE A1104      70.761 180.304 322.400  1.00 52.39           O  
ANISOU 2306  O   PHE A1104     2497   8056   9351    863    230    303       O  
ATOM   2307  CB  PHE A1104      72.148 178.486 320.132  1.00 65.42           C  
ANISOU 2307  CB  PHE A1104     4274   9630  10952    741    242    401       C  
ATOM   2308  CG  PHE A1104      72.822 179.127 318.945  1.00 64.43           C  
ANISOU 2308  CG  PHE A1104     4171   9387  10923    748    257    479       C  
ATOM   2309  CD1 PHE A1104      73.535 178.355 318.042  1.00 50.38           C  
ANISOU 2309  CD1 PHE A1104     2437   7558   9149    705    267    536       C  
ATOM   2310  CD2 PHE A1104      72.725 180.492 318.719  1.00 64.18           C  
ANISOU 2310  CD2 PHE A1104     4112   9295  10980    801    264    499       C  
ATOM   2311  CE1 PHE A1104      74.147 178.928 316.945  1.00 50.57           C  
ANISOU 2311  CE1 PHE A1104     2477   7478   9259    714    284    613       C  
ATOM   2312  CE2 PHE A1104      73.338 181.071 317.619  1.00 51.75           C  
ANISOU 2312  CE2 PHE A1104     2554   7611   9497    806    281    576       C  
ATOM   2313  CZ  PHE A1104      74.046 180.285 316.732  1.00 51.25           C  
ANISOU 2313  CZ  PHE A1104     2535   7505   9434    762    291    634       C  
ATOM   2314  N   GLN A1105      71.005 178.193 323.134  1.00 74.69           N  
ANISOU 2314  N   GLN A1105     5357  10986  12034    774    210    260       N  
ATOM   2315  CA  GLN A1105      69.795 178.254 323.941  1.00 75.55           C  
ANISOU 2315  CA  GLN A1105     5412  11214  12079    807    215    206       C  
ATOM   2316  C   GLN A1105      69.987 179.154 325.153  1.00 80.46           C  
ANISOU 2316  C   GLN A1105     5989  11810  12772    864    201    182       C  
ATOM   2317  O   GLN A1105      69.282 180.155 325.319  1.00 82.65           O  
ANISOU 2317  O   GLN A1105     6221  12099  13084    929    215    172       O  
ATOM   2318  CB  GLN A1105      69.400 176.855 324.391  1.00 71.43           C  
ANISOU 2318  CB  GLN A1105     4898  10798  11445    753    210    165       C  
ATOM   2319  CG  GLN A1105      68.249 176.875 325.359  1.00 71.27           C  
ANISOU 2319  CG  GLN A1105     4818  10897  11366    784    215    105       C  
ATOM   2320  CD  GLN A1105      67.562 175.546 325.478  1.00 70.85           C  
ANISOU 2320  CD  GLN A1105     4768  10938  11213    725    217     60       C  
ATOM   2321  OE1 GLN A1105      68.146 174.501 325.187  1.00 67.63           O  
ANISOU 2321  OE1 GLN A1105     4409  10509  10780    661    209     71       O  
ATOM   2322  NE2 GLN A1105      66.308 175.571 325.902  1.00 75.44           N  
ANISOU 2322  NE2 GLN A1105     5298  11611  11756    746    230      6       N  
ATOM   2323  N   MET A1106      70.960 178.822 326.003  1.00 52.40           N  
ANISOU 2323  N   MET A1106     2447   8212   9250    841    173    173       N  
ATOM   2324  CA  MET A1106      71.103 179.443 327.311  1.00 53.12           C  
ANISOU 2324  CA  MET A1106     2493   8286   9403    886    155    139       C  
ATOM   2325  C   MET A1106      72.387 180.246 327.496  1.00 53.46           C  
ANISOU 2325  C   MET A1106     2547   8162   9605    892    128    152       C  
ATOM   2326  O   MET A1106      72.594 180.803 328.580  1.00 82.03           O  
ANISOU 2326  O   MET A1106     6127  11741  13299    927    106    114       O  
ATOM   2327  CB  MET A1106      71.011 178.352 328.386  1.00 52.83           C  
ANISOU 2327  CB  MET A1106     2447   8352   9275    855    140    103       C  
ATOM   2328  CG  MET A1106      71.147 176.940 327.805  1.00 51.84           C  
ANISOU 2328  CG  MET A1106     2371   8278   9047    777    141    113       C  
ATOM   2329  SD  MET A1106      70.615 175.609 328.902  1.00 75.44           S  
ANISOU 2329  SD  MET A1106     5341  11416  11907    741    134     66       S  
ATOM   2330  CE  MET A1106      71.115 174.157 327.989  1.00 50.46           C  
ANISOU 2330  CE  MET A1106     2249   8242   8682    649    134     82       C  
ATOM   2331  N   GLY A1107      73.248 180.333 326.484  1.00 53.09           N  
ANISOU 2331  N   GLY A1107     2546   8010   9617    860    126    199       N  
ATOM   2332  CA  GLY A1107      74.514 181.024 326.643  1.00 53.43           C  
ANISOU 2332  CA  GLY A1107     2596   7891   9814    856     97    208       C  
ATOM   2333  C   GLY A1107      75.526 180.176 327.384  1.00 69.08           C  
ANISOU 2333  C   GLY A1107     4599   9851  11798    804     61    193       C  
ATOM   2334  O   GLY A1107      75.150 179.397 328.265  1.00 68.12           O  
ANISOU 2334  O   GLY A1107     4464   9833  11587    793     53    157       O  
ATOM   2335  N   GLU A1108      76.809 180.326 327.040  1.00 69.58           N  
ANISOU 2335  N   GLU A1108     4692   9781  11965    772     40    223       N  
ATOM   2336  CA  GLU A1108      77.851 179.475 327.614  1.00 68.60           C  
ANISOU 2336  CA  GLU A1108     4592   9631  11843    720      6    216       C  
ATOM   2337  C   GLU A1108      77.828 179.518 329.135  1.00 68.10           C  
ANISOU 2337  C   GLU A1108     4484   9590  11802    733    -31    149       C  
ATOM   2338  O   GLU A1108      77.896 178.475 329.798  1.00 52.66           O  
ANISOU 2338  O   GLU A1108     2536   7714   9760    700    -44    130       O  
ATOM   2339  CB  GLU A1108      79.219 179.899 327.092  1.00 52.62           C  
ANISOU 2339  CB  GLU A1108     2593   7448   9953    695    -12    257       C  
ATOM   2340  CG  GLU A1108      79.229 180.189 325.619  1.00 81.20           C  
ANISOU 2340  CG  GLU A1108     6244  11026  13583    696     25    324       C  
ATOM   2341  CD  GLU A1108      80.092 181.383 325.286  1.00 82.27           C  
ANISOU 2341  CD  GLU A1108     6368  10997  13895    708     10    353       C  
ATOM   2342  OE1 GLU A1108      81.215 181.473 325.831  1.00 80.03           O  
ANISOU 2342  OE1 GLU A1108     6080  10615  13711    683    -30    346       O  
ATOM   2343  OE2 GLU A1108      79.639 182.240 324.494  1.00 83.81           O  
ANISOU 2343  OE2 GLU A1108     6554  11161  14130    742     37    383       O  
ATOM   2344  N   THR A1109      77.728 180.720 329.705  1.00 54.05           N  
ANISOU 2344  N   THR A1109     2655   7737  10143    782    -50    108       N  
ATOM   2345  CA  THR A1109      77.686 180.850 331.155  1.00 64.09           C  
ANISOU 2345  CA  THR A1109     3880   9020  11451    802    -89     34       C  
ATOM   2346  C   THR A1109      76.599 179.971 331.773  1.00 66.86           C  
ANISOU 2346  C   THR A1109     4215   9549  11641    811    -67     13       C  
ATOM   2347  O   THR A1109      76.764 179.476 332.894  1.00 54.53           O  
ANISOU 2347  O   THR A1109     2633   8025  10061    800    -99    -30       O  
ATOM   2348  CB  THR A1109      77.489 182.323 331.525  1.00 61.90           C  
ANISOU 2348  CB  THR A1109     3552   8644  11324    866   -104    -13       C  
ATOM   2349  OG1 THR A1109      76.193 182.762 331.096  1.00 59.13           O  
ANISOU 2349  OG1 THR A1109     3182   8374  10912    924    -53     -3       O  
ATOM   2350  CG2 THR A1109      78.547 183.178 330.836  1.00 62.65           C  
ANISOU 2350  CG2 THR A1109     3660   8562  11581    851   -124     17       C  
ATOM   2351  N   GLY A1110      75.510 179.729 331.046  1.00 54.04           N  
ANISOU 2351  N   GLY A1110     2598   8036   9899    827    -17     45       N  
ATOM   2352  CA  GLY A1110      74.434 178.896 331.547  1.00 53.81           C  
ANISOU 2352  CA  GLY A1110     2550   8178   9717    832      5     31       C  
ATOM   2353  C   GLY A1110      74.651 177.409 331.343  1.00 67.40           C  
ANISOU 2353  C   GLY A1110     4315   9981  11312    762      7     56       C  
ATOM   2354  O   GLY A1110      74.452 176.619 332.271  1.00 52.73           O  
ANISOU 2354  O   GLY A1110     2440   8215   9380    746     -4     33       O  
ATOM   2355  N   VAL A1111      75.048 177.014 330.128  1.00 67.19           N  
ANISOU 2355  N   VAL A1111     4344   9920  11267    722     23    101       N  
ATOM   2356  CA  VAL A1111      75.297 175.604 329.847  1.00 66.62           C  
ANISOU 2356  CA  VAL A1111     4317   9907  11090    657     26    119       C  
ATOM   2357  C   VAL A1111      76.528 175.098 330.592  1.00 66.29           C  
ANISOU 2357  C   VAL A1111     4290   9802  11095    618    -15    113       C  
ATOM   2358  O   VAL A1111      76.582 173.919 330.962  1.00 66.11           O  
ANISOU 2358  O   VAL A1111     4283   9854  10983    575    -19    108       O  
ATOM   2359  CB  VAL A1111      75.391 175.361 328.324  1.00 50.59           C  
ANISOU 2359  CB  VAL A1111     2338   7843   9039    632     54    166       C  
ATOM   2360  CG1 VAL A1111      75.997 176.541 327.626  1.00 50.96           C  
ANISOU 2360  CG1 VAL A1111     2392   7752   9218    659     54    198       C  
ATOM   2361  CG2 VAL A1111      76.192 174.111 327.994  1.00 49.77           C  
ANISOU 2361  CG2 VAL A1111     2290   7728   8894    567     49    188       C  
ATOM   2362  N   ALA A1112      77.491 175.970 330.895  1.00 66.28           N  
ANISOU 2362  N   ALA A1112     4278   9666  11238    630    -48    107       N  
ATOM   2363  CA  ALA A1112      78.590 175.587 331.776  1.00 66.73           C  
ANISOU 2363  CA  ALA A1112     4338   9670  11348    597    -95     89       C  
ATOM   2364  C   ALA A1112      78.127 175.050 333.129  1.00 51.89           C  
ANISOU 2364  C   ALA A1112     2418   7896   9403    599   -115     43       C  
ATOM   2365  O   ALA A1112      78.959 174.528 333.875  1.00 51.87           O  
ANISOU 2365  O   ALA A1112     2417   7871   9420    566   -154     29       O  
ATOM   2366  CB  ALA A1112      79.521 176.780 332.005  1.00 68.51           C  
ANISOU 2366  CB  ALA A1112     4543   9736  11753    615   -135     74       C  
ATOM   2367  N   GLY A1113      76.839 175.137 333.464  1.00 52.15           N  
ANISOU 2367  N   GLY A1113     2412   8045   9356    638    -89     23       N  
ATOM   2368  CA  GLY A1113      76.405 174.671 334.771  1.00 52.45           C  
ANISOU 2368  CA  GLY A1113     2408   8183   9339    644   -105    -13       C  
ATOM   2369  C   GLY A1113      76.341 173.157 334.875  1.00 58.59           C  
ANISOU 2369  C   GLY A1113     3211   9070   9981    586    -97      7       C  
ATOM   2370  O   GLY A1113      76.602 172.588 335.941  1.00 58.46           O  
ANISOU 2370  O   GLY A1113     3175   9092   9946    568   -126    -11       O  
ATOM   2371  N   PHE A1114      75.981 172.481 333.778  1.00 58.02           N  
ANISOU 2371  N   PHE A1114     3183   9044   9819    557    -60     39       N  
ATOM   2372  CA  PHE A1114      75.772 171.029 333.796  1.00 50.24           C  
ANISOU 2372  CA  PHE A1114     2221   8159   8709    502    -50     43       C  
ATOM   2373  C   PHE A1114      77.120 170.319 333.706  1.00 60.27           C  
ANISOU 2373  C   PHE A1114     3540   9344  10016    450    -75     62       C  
ATOM   2374  O   PHE A1114      77.413 169.600 332.752  1.00 59.52           O  
ANISOU 2374  O   PHE A1114     3498   9225   9890    412    -56     87       O  
ATOM   2375  CB  PHE A1114      74.892 170.532 332.652  1.00 49.68           C  
ANISOU 2375  CB  PHE A1114     2178   8151   8548    486     -7     49       C  
ATOM   2376  CG  PHE A1114      73.744 171.430 332.269  1.00 79.21           C  
ANISOU 2376  CG  PHE A1114     5883  11936  12278    539     22     39       C  
ATOM   2377  CD1 PHE A1114      73.201 172.370 333.135  1.00 79.59           C  
ANISOU 2377  CD1 PHE A1114     5868  12016  12355    601     19     24       C  
ATOM   2378  CD2 PHE A1114      73.178 171.284 331.017  1.00 49.70           C  
ANISOU 2378  CD2 PHE A1114     2174   8205   8503    526     53     45       C  
ATOM   2379  CE1 PHE A1114      72.141 173.160 332.735  1.00 80.57           C  
ANISOU 2379  CE1 PHE A1114     5962  12183  12469    653     49     17       C  
ATOM   2380  CE2 PHE A1114      72.125 172.059 330.619  1.00 50.09           C  
ANISOU 2380  CE2 PHE A1114     2192   8296   8543    572     78     34       C  
ATOM   2381  CZ  PHE A1114      71.602 172.998 331.473  1.00 50.91           C  
ANISOU 2381  CZ  PHE A1114     2235   8438   8671    637     77     20       C  
ATOM   2382  N   THR A1115      77.942 170.522 334.735  1.00 60.66           N  
ANISOU 2382  N   THR A1115     3567   9344  10138    451   -120     47       N  
ATOM   2383  CA  THR A1115      79.278 169.935 334.740  1.00 49.86           C  
ANISOU 2383  CA  THR A1115     2238   7892   8814    406   -148     64       C  
ATOM   2384  C   THR A1115      79.219 168.408 334.692  1.00 50.20           C  
ANISOU 2384  C   THR A1115     2313   8017   8745    354   -134     75       C  
ATOM   2385  O   THR A1115      79.844 167.778 333.831  1.00 49.91           O  
ANISOU 2385  O   THR A1115     2331   7925   8708    320   -120    106       O  
ATOM   2386  CB  THR A1115      80.038 170.417 335.969  1.00 50.56           C  
ANISOU 2386  CB  THR A1115     2288   7926   8997    415   -206     33       C  
ATOM   2387  OG1 THR A1115      79.392 169.919 337.145  1.00 50.84           O  
ANISOU 2387  OG1 THR A1115     2278   8081   8957    417   -218      5       O  
ATOM   2388  CG2 THR A1115      80.027 171.934 336.016  1.00 51.34           C  
ANISOU 2388  CG2 THR A1115     2353   7934   9221    466   -222      6       C  
ATOM   2389  N   ASN A1116      78.458 167.793 335.602  1.00 49.27           N  
ANISOU 2389  N   ASN A1116     2159   8026   8536    348   -135     50       N  
ATOM   2390  CA  ASN A1116      78.398 166.333 335.637  1.00 48.69           C  
ANISOU 2390  CA  ASN A1116     2111   8020   8368    296   -124     49       C  
ATOM   2391  C   ASN A1116      77.827 165.756 334.353  1.00 48.03           C  
ANISOU 2391  C   ASN A1116     2074   7947   8229    273    -79     55       C  
ATOM   2392  O   ASN A1116      78.243 164.677 333.923  1.00 54.65           O  
ANISOU 2392  O   ASN A1116     2957   8762   9045    227    -70     68       O  
ATOM   2393  CB  ASN A1116      77.584 165.863 336.834  1.00 49.03           C  
ANISOU 2393  CB  ASN A1116     2100   8201   8328    296   -132     19       C  
ATOM   2394  CG  ASN A1116      78.397 165.842 338.098  1.00 49.49           C  
ANISOU 2394  CG  ASN A1116     2128   8246   8430    293   -182     19       C  
ATOM   2395  OD1 ASN A1116      78.618 166.877 338.723  1.00 50.18           O  
ANISOU 2395  OD1 ASN A1116     2177   8288   8602    332   -213     12       O  
ATOM   2396  ND2 ASN A1116      78.869 164.660 338.477  1.00 65.66           N  
ANISOU 2396  ND2 ASN A1116     4194  10320  10435    245   -194     18       N  
ATOM   2397  N   SER A1117      76.876 166.446 333.731  1.00 76.46           N  
ANISOU 2397  N   SER A1117     5661  11575  11815    304    -51     48       N  
ATOM   2398  CA  SER A1117      76.453 166.057 332.395  1.00 75.46           C  
ANISOU 2398  CA  SER A1117     5579  11431  11662    284    -14     57       C  
ATOM   2399  C   SER A1117      77.413 166.543 331.323  1.00 47.36           C  
ANISOU 2399  C   SER A1117     2068   7741   8187    290    -10    109       C  
ATOM   2400  O   SER A1117      77.345 166.057 330.189  1.00 46.87           O  
ANISOU 2400  O   SER A1117     2050   7649   8111    268     17    132       O  
ATOM   2401  CB  SER A1117      75.049 166.584 332.105  1.00 75.55           C  
ANISOU 2401  CB  SER A1117     5556  11521  11630    313     12     26       C  
ATOM   2402  OG  SER A1117      74.119 166.076 333.044  1.00 76.63           O  
ANISOU 2402  OG  SER A1117     5669  11753  11693    303     12    -25       O  
ATOM   2403  N   LEU A1118      78.291 167.492 331.648  1.00 47.77           N  
ANISOU 2403  N   LEU A1118     2108   7707   8334    319    -36    125       N  
ATOM   2404  CA  LEU A1118      79.292 167.931 330.684  1.00 47.60           C  
ANISOU 2404  CA  LEU A1118     2129   7554   8403    322    -33    171       C  
ATOM   2405  C   LEU A1118      80.416 166.915 330.573  1.00 47.14           C  
ANISOU 2405  C   LEU A1118     2115   7439   8358    280    -41    201       C  
ATOM   2406  O   LEU A1118      80.751 166.467 329.472  1.00 60.33           O  
ANISOU 2406  O   LEU A1118     3832   9057  10032    263    -15    241       O  
ATOM   2407  CB  LEU A1118      79.858 169.299 331.077  1.00 48.27           C  
ANISOU 2407  CB  LEU A1118     2183   7552   8605    362    -61    171       C  
ATOM   2408  CG  LEU A1118      79.781 170.447 330.068  1.00 48.47           C  
ANISOU 2408  CG  LEU A1118     2214   7499   8702    397    -43    195       C  
ATOM   2409  CD1 LEU A1118      79.891 169.911 328.663  1.00 47.83           C  
ANISOU 2409  CD1 LEU A1118     2188   7389   8597    376     -6    240       C  
ATOM   2410  CD2 LEU A1118      78.510 171.265 330.232  1.00 48.93           C  
ANISOU 2410  CD2 LEU A1118     2226   7630   8735    442    -29    165       C  
ATOM   2411  N   ARG A1119      81.011 166.541 331.706  1.00 47.33           N  
ANISOU 2411  N   ARG A1119     2121   7472   8391    264    -76    185       N  
ATOM   2412  CA  ARG A1119      82.169 165.660 331.648  1.00 46.99           C  
ANISOU 2412  CA  ARG A1119     2116   7366   8372    230    -85    216       C  
ATOM   2413  C   ARG A1119      81.786 164.259 331.201  1.00 69.02           C  
ANISOU 2413  C   ARG A1119     4941  10209  11074    191    -55    224       C  
ATOM   2414  O   ARG A1119      82.607 163.566 330.592  1.00 60.74           O  
ANISOU 2414  O   ARG A1119     3937   9093  10049    170    -44    267       O  
ATOM   2415  CB  ARG A1119      82.888 165.615 333.002  1.00 60.69           C  
ANISOU 2415  CB  ARG A1119     3818   9099  10141    223   -135    196       C  
ATOM   2416  CG  ARG A1119      82.117 164.927 334.127  1.00 61.44           C  
ANISOU 2416  CG  ARG A1119     3877   9323  10143    208   -146    153       C  
ATOM   2417  CD  ARG A1119      82.960 164.747 335.398  1.00 47.91           C  
ANISOU 2417  CD  ARG A1119     2136   7604   8465    196   -198    140       C  
ATOM   2418  NE  ARG A1119      82.203 164.104 336.475  1.00 65.86           N  
ANISOU 2418  NE  ARG A1119     4371  10005  10648    185   -208    104       N  
ATOM   2419  CZ  ARG A1119      82.166 162.790 336.692  1.00 67.39           C  
ANISOU 2419  CZ  ARG A1119     4581  10252  10772    145   -199    103       C  
ATOM   2420  NH1 ARG A1119      81.445 162.299 337.694  1.00 47.91           N  
ANISOU 2420  NH1 ARG A1119     2073   7901   8230    137   -208     68       N  
ATOM   2421  NH2 ARG A1119      82.850 161.962 335.912  1.00 68.76           N  
ANISOU 2421  NH2 ARG A1119     4810  10358  10957    116   -180    140       N  
ATOM   2422  N   MET A1120      80.553 163.823 331.474  1.00 46.31           N  
ANISOU 2422  N   MET A1120     2045   7446   8106    181    -42    185       N  
ATOM   2423  CA  MET A1120      80.159 162.489 331.040  1.00 45.80           C  
ANISOU 2423  CA  MET A1120     2012   7416   7974    139    -15    189       C  
ATOM   2424  C   MET A1120      80.263 162.351 329.530  1.00 57.04           C  
ANISOU 2424  C   MET A1120     3485   8773   9416    135     20    236       C  
ATOM   2425  O   MET A1120      80.637 161.288 329.026  1.00 55.72           O  
ANISOU 2425  O   MET A1120     3357   8574   9240    104     36    268       O  
ATOM   2426  CB  MET A1120      78.749 162.173 331.525  1.00 45.91           C  
ANISOU 2426  CB  MET A1120     1990   7550   7903    128     -6    133       C  
ATOM   2427  CG  MET A1120      78.728 161.739 332.977  1.00 92.52           C  
ANISOU 2427  CG  MET A1120     7853  13524  13775    116    -35     93       C  
ATOM   2428  SD  MET A1120      77.097 161.688 333.748  1.00 90.86           S  
ANISOU 2428  SD  MET A1120     7585  13450  13488    117    -28     16       S  
ATOM   2429  CE  MET A1120      77.485 160.757 335.238  1.00 93.41           C  
ANISOU 2429  CE  MET A1120     7889  13813  13789     88    -59    -10       C  
ATOM   2430  N   LEU A1121      79.977 163.424 328.796  1.00 58.02           N  
ANISOU 2430  N   LEU A1121     3605   8870   9571    170     32    245       N  
ATOM   2431  CA  LEU A1121      80.208 163.423 327.356  1.00 45.21           C  
ANISOU 2431  CA  LEU A1121     2025   7177   7976    173     63    296       C  
ATOM   2432  C   LEU A1121      81.693 163.357 327.046  1.00 49.69           C  
ANISOU 2432  C   LEU A1121     2625   7631   8623    175     58    351       C  
ATOM   2433  O   LEU A1121      82.129 162.571 326.196  1.00 48.87           O  
ANISOU 2433  O   LEU A1121     2563   7483   8524    158     82    397       O  
ATOM   2434  CB  LEU A1121      79.594 164.672 326.743  1.00 45.48           C  
ANISOU 2434  CB  LEU A1121     2041   7208   8031    212     74    294       C  
ATOM   2435  CG  LEU A1121      78.182 164.831 327.269  1.00 45.71           C  
ANISOU 2435  CG  LEU A1121     2027   7351   7988    216     75    236       C  
ATOM   2436  CD1 LEU A1121      77.677 166.231 327.012  1.00 46.13           C  
ANISOU 2436  CD1 LEU A1121     2051   7403   8075    265     78    229       C  
ATOM   2437  CD2 LEU A1121      77.335 163.779 326.594  1.00 45.33           C  
ANISOU 2437  CD2 LEU A1121     1999   7350   7873    178    102    232       C  
ATOM   2438  N   GLN A1122      82.481 164.191 327.723  1.00 45.50           N  
ANISOU 2438  N   GLN A1122     2074   7050   8164    196     27    349       N  
ATOM   2439  CA  GLN A1122      83.921 164.209 327.507  1.00 45.51           C  
ANISOU 2439  CA  GLN A1122     2099   6940   8252    198     19    398       C  
ATOM   2440  C   GLN A1122      84.527 162.828 327.714  1.00 45.17           C  
ANISOU 2440  C   GLN A1122     2083   6894   8186    163     21    419       C  
ATOM   2441  O   GLN A1122      85.461 162.441 327.006  1.00 93.23           O  
ANISOU 2441  O   GLN A1122     8204  12899  14319    161     37    476       O  
ATOM   2442  CB  GLN A1122      84.548 165.243 328.440  1.00 46.08           C  
ANISOU 2442  CB  GLN A1122     2135   6970   8405    218    -24    380       C  
ATOM   2443  CG  GLN A1122      86.054 165.277 328.478  1.00 68.81           C  
ANISOU 2443  CG  GLN A1122     5027   9738  11379    214    -43    423       C  
ATOM   2444  CD  GLN A1122      86.559 166.388 329.380  1.00 72.61           C  
ANISOU 2444  CD  GLN A1122     5465  10174  11948    230    -90    399       C  
ATOM   2445  OE1 GLN A1122      86.363 167.571 329.093  1.00 71.78           O  
ANISOU 2445  OE1 GLN A1122     5342  10029  11902    258    -92    395       O  
ATOM   2446  NE2 GLN A1122      87.191 166.013 330.489  1.00 76.17           N  
ANISOU 2446  NE2 GLN A1122     5897  10630  12414    212   -130    382       N  
ATOM   2447  N   GLN A1123      83.983 162.055 328.651  1.00 45.12           N  
ANISOU 2447  N   GLN A1123     2060   6976   8109    137      8    377       N  
ATOM   2448  CA  GLN A1123      84.462 160.703 328.919  1.00 62.53           C  
ANISOU 2448  CA  GLN A1123     4287   9182  10290    103     10    396       C  
ATOM   2449  C   GLN A1123      83.794 159.657 328.037  1.00 44.40           C  
ANISOU 2449  C   GLN A1123     2022   6913   7934     78     49    415       C  
ATOM   2450  O   GLN A1123      83.942 158.451 328.296  1.00 44.20           O  
ANISOU 2450  O   GLN A1123     2011   6902   7881     46     54    426       O  
ATOM   2451  CB  GLN A1123      84.246 160.357 330.391  1.00 61.49           C  
ANISOU 2451  CB  GLN A1123     4117   9127  10118     86    -25    346       C  
ATOM   2452  CG  GLN A1123      84.798 161.400 331.341  1.00 61.54           C  
ANISOU 2452  CG  GLN A1123     4084   9116  10184    109    -70    324       C  
ATOM   2453  CD  GLN A1123      84.550 161.043 332.783  1.00 45.90           C  
ANISOU 2453  CD  GLN A1123     2063   7219   8159     94   -105    277       C  
ATOM   2454  OE1 GLN A1123      84.035 159.967 333.085  1.00 45.68           O  
ANISOU 2454  OE1 GLN A1123     2037   7258   8060     64    -94    263       O  
ATOM   2455  NE2 GLN A1123      84.913 161.941 333.687  1.00 49.07           N  
ANISOU 2455  NE2 GLN A1123     2422   7614   8609    113   -147    253       N  
ATOM   2456  N   LYS A1124      83.051 160.121 327.031  1.00 44.31           N  
ANISOU 2456  N   LYS A1124     2018   6909   7907     91     76    419       N  
ATOM   2457  CA  LYS A1124      82.405 159.309 326.003  1.00 58.43           C  
ANISOU 2457  CA  LYS A1124     3834   8713   9652     70    113    442       C  
ATOM   2458  C   LYS A1124      81.357 158.350 326.556  1.00 58.67           C  
ANISOU 2458  C   LYS A1124     3852   8837   9604     29    113    402       C  
ATOM   2459  O   LYS A1124      81.056 157.342 325.921  1.00 59.31           O  
ANISOU 2459  O   LYS A1124     3957   8920   9657     -1    138    429       O  
ATOM   2460  CB  LYS A1124      83.433 158.526 325.179  1.00 58.49           C  
ANISOU 2460  CB  LYS A1124     3885   8636   9703     66    136    515       C  
ATOM   2461  CG  LYS A1124      84.627 159.365 324.708  1.00 58.15           C  
ANISOU 2461  CG  LYS A1124     3853   8490   9750    103    136    561       C  
ATOM   2462  CD  LYS A1124      84.538 159.713 323.233  1.00 57.23           C  
ANISOU 2462  CD  LYS A1124     3759   8330   9654    124    172    607       C  
ATOM   2463  CE  LYS A1124      85.630 160.702 322.861  1.00 44.01           C  
ANISOU 2463  CE  LYS A1124     2089   6558   8074    160    170    648       C  
ATOM   2464  NZ  LYS A1124      86.907 160.410 323.582  1.00 48.44           N  
ANISOU 2464  NZ  LYS A1124     2653   7061   8692    158    150    669       N  
ATOM   2465  N   ARG A1125      80.783 158.635 327.720  1.00 44.13           N  
ANISOU 2465  N   ARG A1125     1970   7070   7728     27     87    340       N  
ATOM   2466  CA  ARG A1125      79.697 157.829 328.269  1.00 51.55           C  
ANISOU 2466  CA  ARG A1125     2891   8096   8599    -11     89    298       C  
ATOM   2467  C   ARG A1125      78.410 158.612 328.044  1.00 44.31           C  
ANISOU 2467  C   ARG A1125     1945   7242   7648      3     97    254       C  
ATOM   2468  O   ARG A1125      78.123 159.572 328.764  1.00 50.35           O  
ANISOU 2468  O   ARG A1125     2670   8049   8413     33     78    210       O  
ATOM   2469  CB  ARG A1125      79.916 157.539 329.751  1.00 51.71           C  
ANISOU 2469  CB  ARG A1125     2882   8160   8606    -22     57    261       C  
ATOM   2470  CG  ARG A1125      80.316 158.769 330.543  1.00 52.89           C  
ANISOU 2470  CG  ARG A1125     2995   8316   8786     19     25    232       C  
ATOM   2471  CD  ARG A1125      80.052 158.605 332.014  1.00 53.77           C  
ANISOU 2471  CD  ARG A1125     3061   8504   8866     11     -4    180       C  
ATOM   2472  NE  ARG A1125      81.250 158.212 332.736  1.00 45.14           N  
ANISOU 2472  NE  ARG A1125     1972   7372   7808      4    -32    202       N  
ATOM   2473  CZ  ARG A1125      81.223 157.729 333.967  1.00 63.65           C  
ANISOU 2473  CZ  ARG A1125     4284   9772  10127    -13    -57    170       C  
ATOM   2474  NH1 ARG A1125      80.060 157.585 334.580  1.00 62.59           N  
ANISOU 2474  NH1 ARG A1125     4114   9730   9939    -23    -56    113       N  
ATOM   2475  NH2 ARG A1125      82.344 157.389 334.580  1.00 64.78           N  
ANISOU 2475  NH2 ARG A1125     4431   9877  10307    -19    -84    194       N  
ATOM   2476  N   TRP A1126      77.629 158.200 327.047  1.00 44.13           N  
ANISOU 2476  N   TRP A1126     1939   7226   7603    -17    125    270       N  
ATOM   2477  CA  TRP A1126      76.448 158.969 326.681  1.00 59.01           C  
ANISOU 2477  CA  TRP A1126     3797   9157   9466     -2    134    236       C  
ATOM   2478  C   TRP A1126      75.233 158.590 327.521  1.00 60.47           C  
ANISOU 2478  C   TRP A1126     3945   9422   9609    -28    130    177       C  
ATOM   2479  O   TRP A1126      74.519 159.468 328.019  1.00 62.26           O  
ANISOU 2479  O   TRP A1126     4128   9698   9830      0    123    125       O  
ATOM   2480  CB  TRP A1126      76.149 158.786 325.190  1.00 58.56           C  
ANISOU 2480  CB  TRP A1126     3771   9068   9412    -10    164    284       C  
ATOM   2481  CG  TRP A1126      77.335 159.027 324.313  1.00 59.78           C  
ANISOU 2481  CG  TRP A1126     3962   9135   9617     15    173    347       C  
ATOM   2482  CD1 TRP A1126      77.773 160.225 323.823  1.00 59.15           C  
ANISOU 2482  CD1 TRP A1126     3882   9011   9583     63    174    363       C  
ATOM   2483  CD2 TRP A1126      78.244 158.040 323.828  1.00 63.01           C  
ANISOU 2483  CD2 TRP A1126     4411   9483  10046     -5    186    406       C  
ATOM   2484  NE1 TRP A1126      78.901 160.043 323.063  1.00 43.86           N  
ANISOU 2484  NE1 TRP A1126     1983   6986   7695     72    187    428       N  
ATOM   2485  CE2 TRP A1126      79.209 158.708 323.046  1.00 65.65           C  
ANISOU 2485  CE2 TRP A1126     4768   9737  10440     34    195    454       C  
ATOM   2486  CE3 TRP A1126      78.336 156.654 323.977  1.00 65.90           C  
ANISOU 2486  CE3 TRP A1126     4795   9852  10391    -51    192    427       C  
ATOM   2487  CZ2 TRP A1126      80.252 158.036 322.417  1.00 68.40           C  
ANISOU 2487  CZ2 TRP A1126     5153  10010  10827     32    213    519       C  
ATOM   2488  CZ3 TRP A1126      79.370 155.989 323.355  1.00 68.57           C  
ANISOU 2488  CZ3 TRP A1126     5171  10118  10766    -52    208    493       C  
ATOM   2489  CH2 TRP A1126      80.317 156.679 322.583  1.00 69.68           C  
ANISOU 2489  CH2 TRP A1126     5330  10181  10965     -9    219    538       C  
ATOM   2490  N   ASP A1127      75.001 157.289 327.702  1.00 61.14           N  
ANISOU 2490  N   ASP A1127     4044   9511   9674    -81    136    189       N  
ATOM   2491  CA  ASP A1127      73.808 156.836 328.408  1.00 61.92           C  
ANISOU 2491  CA  ASP A1127     4111   9663   9751   -111    136    149       C  
ATOM   2492  C   ASP A1127      73.717 157.415 329.809  1.00 60.34           C  
ANISOU 2492  C   ASP A1127     3863   9507   9556    -84    113     82       C  
ATOM   2493  O   ASP A1127      72.612 157.622 330.318  1.00 61.38           O  
ANISOU 2493  O   ASP A1127     3956   9675   9689    -83    115     41       O  
ATOM   2494  CB  ASP A1127      73.782 155.313 328.465  1.00 68.76           C  
ANISOU 2494  CB  ASP A1127     5005  10517  10602   -172    143    191       C  
ATOM   2495  CG  ASP A1127      73.633 154.699 327.098  1.00 75.10           C  
ANISOU 2495  CG  ASP A1127     5847  11291  11397   -201    166    255       C  
ATOM   2496  OD1 ASP A1127      72.724 155.133 326.357  1.00 74.63           O  
ANISOU 2496  OD1 ASP A1127     5778  11247  11332   -197    178    256       O  
ATOM   2497  OD2 ASP A1127      74.435 153.804 326.756  1.00 80.57           O  
ANISOU 2497  OD2 ASP A1127     6575  11946  12092   -224    171    307       O  
ATOM   2498  N   GLU A1128      74.850 157.689 330.444  1.00 57.16           N  
ANISOU 2498  N   GLU A1128     3459   9097   9162    -62     90     79       N  
ATOM   2499  CA  GLU A1128      74.829 158.317 331.755  1.00 57.56           C  
ANISOU 2499  CA  GLU A1128     3458   9198   9214    -32     64     20       C  
ATOM   2500  C   GLU A1128      74.728 159.833 331.682  1.00 55.49           C  
ANISOU 2500  C   GLU A1128     3164   8961   8957     28     57     -3       C  
ATOM   2501  O   GLU A1128      74.529 160.473 332.718  1.00 55.26           O  
ANISOU 2501  O   GLU A1128     3107   8970   8920     59     37    -42       O  
ATOM   2502  CB  GLU A1128      76.068 157.911 332.552  1.00 60.79           C  
ANISOU 2502  CB  GLU A1128     3874   9592   9631    -37     37     36       C  
ATOM   2503  CG  GLU A1128      76.093 156.437 332.897  1.00 65.75           C  
ANISOU 2503  CG  GLU A1128     4523  10206  10252    -93     41     56       C  
ATOM   2504  CD  GLU A1128      77.390 156.022 333.550  1.00 71.36           C  
ANISOU 2504  CD  GLU A1128     5245  10894  10976    -96     16     81       C  
ATOM   2505  OE1 GLU A1128      77.982 155.014 333.109  1.00 74.40           O  
ANISOU 2505  OE1 GLU A1128     5672  11230  11366   -129     26    138       O  
ATOM   2506  OE2 GLU A1128      77.823 156.711 334.499  1.00 72.49           O  
ANISOU 2506  OE2 GLU A1128     5350  11068  11126    -66    -15     49       O  
ATOM   2507  N   ALA A1129      74.862 160.418 330.495  1.00 45.58           N  
ANISOU 2507  N   ALA A1129     1936   7668   7716     48     72     37       N  
ATOM   2508  CA  ALA A1129      74.579 161.833 330.296  1.00 46.74           C  
ANISOU 2508  CA  ALA A1129     2053   7832   7874    103     71     26       C  
ATOM   2509  C   ALA A1129      73.207 162.072 329.695  1.00 46.05           C  
ANISOU 2509  C   ALA A1129     1948   7774   7775    105     96     -2       C  
ATOM   2510  O   ALA A1129      72.597 163.114 329.958  1.00 60.57           O  
ANISOU 2510  O   ALA A1129     3758   9644   9612    149     95    -29       O  
ATOM   2511  CB  ALA A1129      75.636 162.468 329.391  1.00 46.72           C  
ANISOU 2511  CB  ALA A1129     2087   7745   7918    129     72     91       C  
ATOM   2512  N   ALA A1130      72.717 161.129 328.892  1.00 66.79           N  
ANISOU 2512  N   ALA A1130     4607  10376  10395     58    118     21       N  
ATOM   2513  CA  ALA A1130      71.359 161.225 328.373  1.00 67.33           C  
ANISOU 2513  CA  ALA A1130     4658  10461  10464     52    140      7       C  
ATOM   2514  C   ALA A1130      70.341 161.133 329.501  1.00 65.28           C  
ANISOU 2514  C   ALA A1130     4367  10228  10208     48    137    -41       C  
ATOM   2515  O   ALA A1130      69.415 161.950 329.586  1.00 62.32           O  
ANISOU 2515  O   ALA A1130     3963   9870   9846     81    145    -66       O  
ATOM   2516  CB  ALA A1130      71.120 160.127 327.336  1.00 62.59           C  
ANISOU 2516  CB  ALA A1130     4103   9824   9854     -3    160     64       C  
ATOM   2517  N   VAL A1131      70.507 160.149 330.390  1.00 65.76           N  
ANISOU 2517  N   VAL A1131     4432  10285  10269     12    128    -44       N  
ATOM   2518  CA  VAL A1131      69.565 159.983 331.493  1.00 65.91           C  
ANISOU 2518  CA  VAL A1131     4417  10313  10313      8    127    -67       C  
ATOM   2519  C   VAL A1131      69.785 161.049 332.562  1.00 70.74           C  
ANISOU 2519  C   VAL A1131     5001  10943  10935     67    108   -125       C  
ATOM   2520  O   VAL A1131      68.852 161.403 333.295  1.00 71.43           O  
ANISOU 2520  O   VAL A1131     5047  11031  11062     88    114   -143       O  
ATOM   2521  CB  VAL A1131      69.658 158.560 332.085  1.00 61.95           C  
ANISOU 2521  CB  VAL A1131     3922   9805   9811    -50    124    -34       C  
ATOM   2522  CG1 VAL A1131      69.551 157.508 330.982  1.00 56.86           C  
ANISOU 2522  CG1 VAL A1131     3314   9149   9141   -107    141     30       C  
ATOM   2523  CG2 VAL A1131      70.933 158.379 332.908  1.00 46.49           C  
ANISOU 2523  CG2 VAL A1131     1978   7842   7845    -44     97    -57       C  
ATOM   2524  N   ASN A1132      71.005 161.587 332.668  1.00 47.14           N  
ANISOU 2524  N   ASN A1132     2023   7975   7912     96     84   -135       N  
ATOM   2525  CA  ASN A1132      71.279 162.601 333.683  1.00 61.36           C  
ANISOU 2525  CA  ASN A1132     3791   9819   9703    152     61   -174       C  
ATOM   2526  C   ASN A1132      70.686 163.948 333.293  1.00 61.24           C  
ANISOU 2526  C   ASN A1132     3749   9834   9684    211     71   -184       C  
ATOM   2527  O   ASN A1132      70.222 164.704 334.156  1.00 61.12           O  
ANISOU 2527  O   ASN A1132     3694   9856   9674    257     65   -225       O  
ATOM   2528  CB  ASN A1132      72.786 162.732 333.907  1.00 62.37           C  
ANISOU 2528  CB  ASN A1132     3928   9965   9803    161     32   -134       C  
ATOM   2529  CG  ASN A1132      73.126 163.645 335.069  1.00 63.39           C  
ANISOU 2529  CG  ASN A1132     4015  10155   9917    214      3   -140       C  
ATOM   2530  OD1 ASN A1132      73.224 164.863 334.917  1.00 48.45           O  
ANISOU 2530  OD1 ASN A1132     2094   8281   8034    268      0   -106       O  
ATOM   2531  ND2 ASN A1132      73.310 163.053 336.243  1.00 63.83           N  
ANISOU 2531  ND2 ASN A1132     4060  10230   9964    198    -18   -171       N  
ATOM   2532  N   LEU A1133      70.704 164.275 332.002  1.00 47.77           N  
ANISOU 2532  N   LEU A1133     2061   8113   7977    214     88   -143       N  
ATOM   2533  CA  LEU A1133      70.100 165.518 331.547  1.00 48.16           C  
ANISOU 2533  CA  LEU A1133     2083   8184   8033    269    100   -145       C  
ATOM   2534  C   LEU A1133      68.580 165.492 331.626  1.00 85.29           C  
ANISOU 2534  C   LEU A1133     6761  12876  12769    266    124   -189       C  
ATOM   2535  O   LEU A1133      67.957 166.551 331.509  1.00 89.94           O  
ANISOU 2535  O   LEU A1133     7318  13487  13367    318    134   -203       O  
ATOM   2536  CB  LEU A1133      70.547 165.815 330.117  1.00 47.76           C  
ANISOU 2536  CB  LEU A1133     2053   8097   7996    270    112    -88       C  
ATOM   2537  CG  LEU A1133      71.990 166.275 329.909  1.00 47.57           C  
ANISOU 2537  CG  LEU A1133     2033   8041   8000    291     94    -33       C  
ATOM   2538  CD1 LEU A1133      72.354 166.195 328.444  1.00 47.10           C  
ANISOU 2538  CD1 LEU A1133     2010   7918   7969    277    111     17       C  
ATOM   2539  CD2 LEU A1133      72.157 167.690 330.408  1.00 48.18           C  
ANISOU 2539  CD2 LEU A1133     2063   8135   8110    362     82    -23       C  
ATOM   2540  N   ALA A1134      67.972 164.320 331.843  1.00 78.51           N  
ANISOU 2540  N   ALA A1134     5908  11976  11946    209    135   -185       N  
ATOM   2541  CA  ALA A1134      66.517 164.190 331.865  1.00 71.95           C  
ANISOU 2541  CA  ALA A1134     5042  11128  11168    201    163   -167       C  
ATOM   2542  C   ALA A1134      65.862 164.889 333.051  1.00 67.31           C  
ANISOU 2542  C   ALA A1134     4400  10539  10637    250    166   -196       C  
ATOM   2543  O   ALA A1134      64.644 165.098 333.026  1.00 64.10           O  
ANISOU 2543  O   ALA A1134     3951  10140  10264    262    193   -161       O  
ATOM   2544  CB  ALA A1134      66.119 162.712 331.871  1.00 48.47           C  
ANISOU 2544  CB  ALA A1134     2078   8144   8196    129    173   -107       C  
ATOM   2545  N   LYS A1135      66.622 165.253 334.081  1.00 49.79           N  
ANISOU 2545  N   LYS A1135     2172   8321   8424    282    141   -245       N  
ATOM   2546  CA  LYS A1135      66.045 165.829 335.286  1.00 73.48           C  
ANISOU 2546  CA  LYS A1135     5115  11296  11509    328    146   -253       C  
ATOM   2547  C   LYS A1135      66.244 167.335 335.379  1.00 80.03           C  
ANISOU 2547  C   LYS A1135     5922  12166  12320    408    135   -329       C  
ATOM   2548  O   LYS A1135      65.931 167.926 336.417  1.00 84.58           O  
ANISOU 2548  O   LYS A1135     6448  12691  12998    455    139   -334       O  
ATOM   2549  CB  LYS A1135      66.632 165.151 336.523  1.00 67.40           C  
ANISOU 2549  CB  LYS A1135     4336  10495  10777    310    125   -234       C  
ATOM   2550  CG  LYS A1135      66.850 163.658 336.370  1.00 63.27           C  
ANISOU 2550  CG  LYS A1135     3846   9983  10210    234    123   -182       C  
ATOM   2551  CD  LYS A1135      67.376 163.059 337.661  1.00 50.21           C  
ANISOU 2551  CD  LYS A1135     2173   8321   8582    223    100   -155       C  
ATOM   2552  CE  LYS A1135      67.826 161.625 337.470  1.00 49.57           C  
ANISOU 2552  CE  LYS A1135     2132   8257   8447    150     93   -124       C  
ATOM   2553  NZ  LYS A1135      68.442 161.086 338.713  1.00 49.75           N  
ANISOU 2553  NZ  LYS A1135     2136   8284   8484    142     66   -104       N  
ATOM   2554  N   SER A1136      66.747 167.971 334.329  1.00 50.83           N  
ANISOU 2554  N   SER A1136     2251   8569   8493    431    127   -329       N  
ATOM   2555  CA  SER A1136      67.019 169.397 334.390  1.00 59.37           C  
ANISOU 2555  CA  SER A1136     3302   9770   9484    519    120   -306       C  
ATOM   2556  C   SER A1136      65.746 170.203 334.162  1.00 58.26           C  
ANISOU 2556  C   SER A1136     3122   9598   9417    562    150   -347       C  
ATOM   2557  O   SER A1136      64.808 169.747 333.501  1.00 61.20           O  
ANISOU 2557  O   SER A1136     3495   9878   9879    521    179   -336       O  
ATOM   2558  CB  SER A1136      68.073 169.783 333.353  1.00 61.23           C  
ANISOU 2558  CB  SER A1136     3565  10017   9684    524    112   -200       C  
ATOM   2559  OG  SER A1136      67.639 169.452 332.045  1.00 50.37           O  
ANISOU 2559  OG  SER A1136     2220   8582   8338    484    132   -204       O  
ATOM   2560  N   ARG A1137      65.712 171.409 334.738  1.00 58.34           N  
ANISOU 2560  N   ARG A1137     3417   9430   9319    166    434   -280       N  
ATOM   2561  CA  ARG A1137      64.635 172.344 334.422  1.00 57.48           C  
ANISOU 2561  CA  ARG A1137     3227   9351   9260    293    614   -250       C  
ATOM   2562  C   ARG A1137      64.609 172.638 332.933  1.00 56.51           C  
ANISOU 2562  C   ARG A1137     3100   9084   9289    387    616   -186       C  
ATOM   2563  O   ARG A1137      63.539 172.795 332.335  1.00 56.89           O  
ANISOU 2563  O   ARG A1137     3058   9184   9374    450    666    -47       O  
ATOM   2564  CB  ARG A1137      64.803 173.643 335.212  1.00 62.45           C  
ANISOU 2564  CB  ARG A1137     3865   9964   9901    363    826   -442       C  
ATOM   2565  CG  ARG A1137      64.540 173.510 336.695  1.00 72.94           C  
ANISOU 2565  CG  ARG A1137     5174  11483  11056    270    866   -502       C  
ATOM   2566  CD  ARG A1137      65.139 174.677 337.456  1.00 80.66           C  
ANISOU 2566  CD  ARG A1137     6195  12413  12040    301   1042   -746       C  
ATOM   2567  NE  ARG A1137      65.197 174.412 338.892  1.00 85.40           N  
ANISOU 2567  NE  ARG A1137     6800  13205  12442    170   1042   -823       N  
ATOM   2568  CZ  ARG A1137      66.190 173.766 339.499  1.00 84.27           C  
ANISOU 2568  CZ  ARG A1137     6730  13097  12192     32    889   -862       C  
ATOM   2569  NH1 ARG A1137      67.224 173.310 338.798  1.00 80.47           N  
ANISOU 2569  NH1 ARG A1137     6323  12453  11800     15    732   -841       N  
ATOM   2570  NH2 ARG A1137      66.148 173.575 340.813  1.00 85.77           N  
ANISOU 2570  NH2 ARG A1137     6910  13492  12187    -96    896   -915       N  
ATOM   2571  N   TRP A1138      65.791 172.718 332.321  1.00 57.11           N  
ANISOU 2571  N   TRP A1138     3267   8985   9449    391    561   -279       N  
ATOM   2572  CA  TRP A1138      65.884 172.844 330.872  1.00 59.20           C  
ANISOU 2572  CA  TRP A1138     3533   9128   9831    451    539   -215       C  
ATOM   2573  C   TRP A1138      65.060 171.767 330.166  1.00 61.99           C  
ANISOU 2573  C   TRP A1138     3830   9578  10144    388    403    -17       C  
ATOM   2574  O   TRP A1138      64.334 172.059 329.208  1.00 64.83           O  
ANISOU 2574  O   TRP A1138     4125   9950  10559    449    440     99       O  
ATOM   2575  CB  TRP A1138      67.356 172.797 330.457  1.00 55.29           C  
ANISOU 2575  CB  TRP A1138     3149   8453   9406    429    469   -342       C  
ATOM   2576  CG  TRP A1138      67.563 172.540 329.011  1.00 52.51           C  
ANISOU 2576  CG  TRP A1138     2809   8005   9136    440    400   -274       C  
ATOM   2577  CD1 TRP A1138      67.211 173.351 327.982  1.00 52.59           C  
ANISOU 2577  CD1 TRP A1138     2776   7966   9238    542    492   -221       C  
ATOM   2578  CD2 TRP A1138      68.171 171.386 328.427  1.00 51.53           C  
ANISOU 2578  CD2 TRP A1138     2736   7832   9011    336    227   -251       C  
ATOM   2579  NE1 TRP A1138      67.553 172.773 326.788  1.00 51.74           N  
ANISOU 2579  NE1 TRP A1138     2695   7802   9160    498    386   -169       N  
ATOM   2580  CE2 TRP A1138      68.148 171.565 327.035  1.00 51.08           C  
ANISOU 2580  CE2 TRP A1138     2672   7710   9027    374    229   -200       C  
ATOM   2581  CE3 TRP A1138      68.729 170.216 328.948  1.00 52.21           C  
ANISOU 2581  CE3 TRP A1138     2862   7921   9054    210     74   -263       C  
ATOM   2582  CZ2 TRP A1138      68.663 170.618 326.152  1.00 50.28           C  
ANISOU 2582  CZ2 TRP A1138     2612   7549   8944    286     97   -189       C  
ATOM   2583  CZ3 TRP A1138      69.244 169.275 328.068  1.00 52.21           C  
ANISOU 2583  CZ3 TRP A1138     2895   7838   9105    134    -57   -245       C  
ATOM   2584  CH2 TRP A1138      69.205 169.482 326.686  1.00 50.22           C  
ANISOU 2584  CH2 TRP A1138     2643   7524   8913    171    -39   -221       C  
ATOM   2585  N   TYR A1139      65.138 170.519 330.643  1.00 61.15           N  
ANISOU 2585  N   TYR A1139     3738   9549   9949    259    244     31       N  
ATOM   2586  CA  TYR A1139      64.294 169.455 330.100  1.00 60.49           C  
ANISOU 2586  CA  TYR A1139     3593   9564   9828    187    118    211       C  
ATOM   2587  C   TYR A1139      62.824 169.702 330.403  1.00 60.29           C  
ANISOU 2587  C   TYR A1139     3451   9709   9746    230    201    349       C  
ATOM   2588  O   TYR A1139      61.954 169.330 329.609  1.00 58.90           O  
ANISOU 2588  O   TYR A1139     3206   9597   9575    222    155    506       O  
ATOM   2589  CB  TYR A1139      64.717 168.100 330.668  1.00 59.12           C  
ANISOU 2589  CB  TYR A1139     3445   9421   9596     41    -61    233       C  
ATOM   2590  CG  TYR A1139      63.974 166.904 330.102  1.00 60.39           C  
ANISOU 2590  CG  TYR A1139     3548   9659   9740    -47   -202    399       C  
ATOM   2591  CD1 TYR A1139      62.698 166.565 330.547  1.00 62.49           C  
ANISOU 2591  CD1 TYR A1139     3714  10108   9922    -68   -206    553       C  
ATOM   2592  CD2 TYR A1139      64.564 166.095 329.145  1.00 59.47           C  
ANISOU 2592  CD2 TYR A1139     3472   9429   9694   -117   -328    393       C  
ATOM   2593  CE1 TYR A1139      62.025 165.469 330.028  1.00 62.52           C  
ANISOU 2593  CE1 TYR A1139     3662  10178   9916   -156   -339    702       C  
ATOM   2594  CE2 TYR A1139      63.901 164.997 328.626  1.00 59.16           C  
ANISOU 2594  CE2 TYR A1139     3379   9453   9647   -209   -452    524       C  
ATOM   2595  CZ  TYR A1139      62.635 164.690 329.069  1.00 58.64           C  
ANISOU 2595  CZ  TYR A1139     3214   9567   9498   -228   -462    681       C  
ATOM   2596  OH  TYR A1139      61.989 163.598 328.545  1.00 56.68           O  
ANISOU 2596  OH  TYR A1139     2911   9377   9248   -325   -589    808       O  
ATOM   2597  N   ASN A1140      62.525 170.304 331.554  1.00 66.66           N  
ANISOU 2597  N   ASN A1140     4230  10599  10498    265    325    292       N  
ATOM   2598  CA  ASN A1140      61.136 170.529 331.935  1.00 71.14           C  
ANISOU 2598  CA  ASN A1140     4680  11328  11021    304    418    416       C  
ATOM   2599  C   ASN A1140      60.543 171.736 331.224  1.00 69.66           C  
ANISOU 2599  C   ASN A1140     4425  11091  10953    450    588    446       C  
ATOM   2600  O   ASN A1140      59.417 171.665 330.718  1.00 69.30           O  
ANISOU 2600  O   ASN A1140     4274  11133  10923    476    597    623       O  
ATOM   2601  CB  ASN A1140      61.025 170.701 333.450  1.00 81.41           C  
ANISOU 2601  CB  ASN A1140     5970  12749  12212    274    499    333       C  
ATOM   2602  CG  ASN A1140      61.309 169.409 334.202  1.00 88.73           C  
ANISOU 2602  CG  ASN A1140     6922  13775  13015    119    320    377       C  
ATOM   2603  OD1 ASN A1140      61.366 168.331 333.601  1.00 91.94           O  
ANISOU 2603  OD1 ASN A1140     7332  14167  13433     40    144    488       O  
ATOM   2604  ND2 ASN A1140      61.479 169.508 335.519  1.00 90.95           N  
ANISOU 2604  ND2 ASN A1140     7211  14164  13183     66    367    291       N  
ATOM   2605  N   GLN A1141      61.270 172.855 331.172  1.00 65.78           N  
ANISOU 2605  N   GLN A1141     3980  10456  10559    543    722    288       N  
ATOM   2606  CA  GLN A1141      60.664 174.059 330.607  1.00 66.35           C  
ANISOU 2606  CA  GLN A1141     3964  10476  10770    685    897    330       C  
ATOM   2607  C   GLN A1141      60.474 173.951 329.098  1.00 65.02           C  
ANISOU 2607  C   GLN A1141     3765  10259  10682    705    819    484       C  
ATOM   2608  O   GLN A1141      59.563 174.576 328.543  1.00 72.78           O  
ANISOU 2608  O   GLN A1141     4631  11267  11755    790    912    624       O  
ATOM   2609  CB  GLN A1141      61.494 175.295 330.955  1.00 62.58           C  
ANISOU 2609  CB  GLN A1141     3535   9847  10395    776   1063    120       C  
ATOM   2610  CG  GLN A1141      61.867 175.437 332.438  1.00 64.84           C  
ANISOU 2610  CG  GLN A1141     3870  10183  10584    734   1137    -68       C  
ATOM   2611  CD  GLN A1141      60.687 175.284 333.394  1.00 68.73           C  
ANISOU 2611  CD  GLN A1141     4264  10869  10980    715   1214     -4       C  
ATOM   2612  OE1 GLN A1141      60.178 174.183 333.600  1.00 71.87           O  
ANISOU 2612  OE1 GLN A1141     4641  11416  11252    617   1075    129       O  
ATOM   2613  NE2 GLN A1141      60.252 176.394 333.984  1.00 69.68           N  
ANISOU 2613  NE2 GLN A1141     4319  10984  11173    806   1444   -104       N  
ATOM   2614  N   THR A1142      61.319 173.182 328.417  1.00 60.55           N  
ANISOU 2614  N   THR A1142     3291   9628  10087    622    655    464       N  
ATOM   2615  CA  THR A1142      61.205 172.966 326.978  1.00 56.66           C  
ANISOU 2615  CA  THR A1142     2779   9113   9637    610    571    592       C  
ATOM   2616  C   THR A1142      61.620 171.547 326.647  1.00 55.90           C  
ANISOU 2616  C   THR A1142     2753   9039   9448    462    362    604       C  
ATOM   2617  O   THR A1142      62.805 171.254 326.469  1.00 54.15           O  
ANISOU 2617  O   THR A1142     2640   8695   9238    418    294    470       O  
ATOM   2618  CB  THR A1142      62.076 173.897 326.189  1.00 59.09           C  
ANISOU 2618  CB  THR A1142     3130   9254  10067    689    641    507       C  
ATOM   2619  OG1 THR A1142      62.358 173.254 324.949  1.00 58.31           O  
ANISOU 2619  OG1 THR A1142     3062   9143   9952    615    503    576       O  
ATOM   2620  CG2 THR A1142      63.406 174.073 326.917  1.00 55.03           C  
ANISOU 2620  CG2 THR A1142     2741   8606   9561    685    659    273       C  
ATOM   2621  N   PRO A1143      60.654 170.643 326.510  1.00 55.44           N  
ANISOU 2621  N   PRO A1143     2626   9126   9313    384    260    767       N  
ATOM   2622  CA  PRO A1143      60.952 169.203 326.373  1.00 57.58           C  
ANISOU 2622  CA  PRO A1143     2949   9419   9511    235     68    774       C  
ATOM   2623  C   PRO A1143      60.890 168.655 324.957  1.00 59.82           C  
ANISOU 2623  C   PRO A1143     3229   9699   9800    164    -41    853       C  
ATOM   2624  O   PRO A1143      61.303 167.508 324.734  1.00 58.83           O  
ANISOU 2624  O   PRO A1143     3154   9553   9645     41   -186    824       O  
ATOM   2625  CB  PRO A1143      59.847 168.550 327.221  1.00 57.36           C  
ANISOU 2625  CB  PRO A1143     2835   9563   9395    186     31    904       C  
ATOM   2626  CG  PRO A1143      59.158 169.645 327.953  1.00 58.84           C  
ANISOU 2626  CG  PRO A1143     2948   9810   9600    306    213    922       C  
ATOM   2627  CD  PRO A1143      59.389 170.913 327.219  1.00 59.57           C  
ANISOU 2627  CD  PRO A1143     3032   9794   9809    430    349    887       C  
ATOM   2628  N   ASN A1144      60.331 169.411 324.017  1.00 63.39           N  
ANISOU 2628  N   ASN A1144     3619  10178  10287    228     27    958       N  
ATOM   2629  CA  ASN A1144      60.343 168.965 322.634  1.00 65.99           C  
ANISOU 2629  CA  ASN A1144     3973  10510  10589    146    -70   1008       C  
ATOM   2630  C   ASN A1144      61.730 169.106 322.041  1.00 64.28           C  
ANISOU 2630  C   ASN A1144     3841  10144  10438    138    -77    851       C  
ATOM   2631  O   ASN A1144      62.188 168.221 321.306  1.00 64.81           O  
ANISOU 2631  O   ASN A1144     3961  10187  10477     20   -193    805       O  
ATOM   2632  CB  ASN A1144      59.303 169.762 321.841  1.00 65.89           C  
ANISOU 2632  CB  ASN A1144     3914  10561  10561    204     -2   1165       C  
ATOM   2633  CG  ASN A1144      57.898 169.335 322.179  1.00 64.41           C  
ANISOU 2633  CG  ASN A1144     3681  10504  10287    175    -32   1321       C  
ATOM   2634  OD1 ASN A1144      57.661 168.163 322.472  1.00 60.54           O  
ANISOU 2634  OD1 ASN A1144     3208  10073   9722     65   -152   1333       O  
ATOM   2635  ND2 ASN A1144      56.960 170.275 322.163  1.00 65.73           N  
ANISOU 2635  ND2 ASN A1144     3792  10702  10479    271     77   1441       N  
ATOM   2636  N   ARG A1145      62.420 170.187 322.391  1.00 62.86           N  
ANISOU 2636  N   ARG A1145     3700   9845  10340    257     51    742       N  
ATOM   2637  CA  ARG A1145      63.775 170.411 321.923  1.00 58.28           C  
ANISOU 2637  CA  ARG A1145     3226   9099   9817    260     56    577       C  
ATOM   2638  C   ARG A1145      64.805 169.765 322.824  1.00 52.86           C  
ANISOU 2638  C   ARG A1145     2646   8305   9134    211     -1    403       C  
ATOM   2639  O   ARG A1145      65.945 169.566 322.397  1.00 51.06           O  
ANISOU 2639  O   ARG A1145     2507   7944   8948    177    -37    271       O  
ATOM   2640  CB  ARG A1145      64.056 171.910 321.817  1.00 61.79           C  
ANISOU 2640  CB  ARG A1145     3655   9457  10367    409    217    551       C  
ATOM   2641  CG  ARG A1145      64.962 172.304 320.665  1.00 64.12           C  
ANISOU 2641  CG  ARG A1145     4000   9647  10715    412    224    494       C  
ATOM   2642  CD  ARG A1145      65.110 173.812 320.609  1.00 64.31           C  
ANISOU 2642  CD  ARG A1145     3985   9588  10863    564    386    497       C  
ATOM   2643  NE  ARG A1145      65.941 174.372 321.664  1.00 61.96           N  
ANISOU 2643  NE  ARG A1145     3757   9148  10636    642    474    316       N  
ATOM   2644  CZ  ARG A1145      66.790 175.380 321.494  1.00 57.38           C  
ANISOU 2644  CZ  ARG A1145     3210   8420  10171    732    574    219       C  
ATOM   2645  NH1 ARG A1145      66.973 175.928 320.303  1.00 57.03           N  
ANISOU 2645  NH1 ARG A1145     3156   8347  10164    755    593    287       N  
ATOM   2646  NH2 ARG A1145      67.469 175.822 322.525  1.00 56.12           N  
ANISOU 2646  NH2 ARG A1145     3111   8149  10062    786    646     53       N  
ATOM   2647  N   ALA A1146      64.445 169.451 324.060  1.00 52.09           N  
ANISOU 2647  N   ALA A1146     2531   8266   8994    204     -8    407       N  
ATOM   2648  CA  ALA A1146      65.395 168.761 324.915  1.00 53.31           C  
ANISOU 2648  CA  ALA A1146     2769   8337   9148    139    -81    274       C  
ATOM   2649  C   ALA A1146      65.384 167.258 324.692  1.00 53.97           C  
ANISOU 2649  C   ALA A1146     2859   8447   9201    -10   -251    310       C  
ATOM   2650  O   ALA A1146      66.416 166.605 324.877  1.00 53.22           O  
ANISOU 2650  O   ALA A1146     2836   8234   9150    -78   -329    198       O  
ATOM   2651  CB  ALA A1146      65.113 169.076 326.385  1.00 56.92           C  
ANISOU 2651  CB  ALA A1146     3205   8858   9563    178    -18    257       C  
ATOM   2652  N   LYS A1147      64.249 166.691 324.290  1.00 55.89           N  
ANISOU 2652  N   LYS A1147     3020   8831   9384    -66   -309    464       N  
ATOM   2653  CA  LYS A1147      64.178 165.252 324.076  1.00 59.12           C  
ANISOU 2653  CA  LYS A1147     3425   9258   9780   -212   -466    495       C  
ATOM   2654  C   LYS A1147      64.894 164.811 322.809  1.00 59.69           C  
ANISOU 2654  C   LYS A1147     3552   9225   9901   -286   -520    409       C  
ATOM   2655  O   LYS A1147      65.167 163.615 322.656  1.00 61.60           O  
ANISOU 2655  O   LYS A1147     3808   9426  10173   -410   -638    378       O  
ATOM   2656  CB  LYS A1147      62.716 164.796 324.040  1.00 59.37           C  
ANISOU 2656  CB  LYS A1147     3349   9477   9733   -254   -510    685       C  
ATOM   2657  N   ARG A1148      65.213 165.741 321.912  1.00 60.77           N  
ANISOU 2657  N   ARG A1148     3715   9319  10057   -217   -433    369       N  
ATOM   2658  CA  ARG A1148      65.910 165.447 320.665  1.00 60.68           C  
ANISOU 2658  CA  ARG A1148     3755   9225  10075   -287   -464    280       C  
ATOM   2659  C   ARG A1148      67.371 165.853 320.681  1.00 58.57           C  
ANISOU 2659  C   ARG A1148     3587   8765   9903   -243   -417     99       C  
ATOM   2660  O   ARG A1148      68.214 165.124 320.154  1.00 58.43           O  
ANISOU 2660  O   ARG A1148     3624   8635   9940   -332   -475    -18       O  
ATOM   2661  CB  ARG A1148      65.208 166.142 319.499  1.00 63.79           C  
ANISOU 2661  CB  ARG A1148     4094   9733  10412   -264   -412    388       C  
ATOM   2662  CG  ARG A1148      63.762 165.733 319.357  1.00 63.70           C  
ANISOU 2662  CG  ARG A1148     3976   9916  10310   -317   -466    579       C  
ATOM   2663  CD  ARG A1148      63.241 166.129 318.001  1.00 60.65           C  
ANISOU 2663  CD  ARG A1148     3539   9641   9864   -347   -454    679       C  
ATOM   2664  NE  ARG A1148      63.544 167.523 317.696  1.00 55.87           N  
ANISOU 2664  NE  ARG A1148     2931   8996   9302   -214   -326    692       N  
ATOM   2665  CZ  ARG A1148      62.825 168.553 318.126  1.00 53.32           C  
ANISOU 2665  CZ  ARG A1148     2527   8732   9002    -84   -229    824       C  
ATOM   2666  NH1 ARG A1148      61.762 168.352 318.893  1.00 53.85           N  
ANISOU 2666  NH1 ARG A1148     2514   8909   9039    -69   -240    951       N  
ATOM   2667  NH2 ARG A1148      63.170 169.787 317.790  1.00 53.39           N  
ANISOU 2667  NH2 ARG A1148     2526   8683   9077     31   -114    830       N  
ATOM   2668  N   VAL A1149      67.688 167.011 321.264  1.00 57.07           N  
ANISOU 2668  N   VAL A1149     3415   8526   9742   -110   -306     68       N  
ATOM   2669  CA  VAL A1149      69.086 167.366 321.493  1.00 55.85           C  
ANISOU 2669  CA  VAL A1149     3353   8187   9681    -70   -270   -101       C  
ATOM   2670  C   VAL A1149      69.779 166.270 322.295  1.00 62.31           C  
ANISOU 2670  C   VAL A1149     4211   8917  10548   -160   -374   -180       C  
ATOM   2671  O   VAL A1149      70.852 165.783 321.920  1.00 72.13           O  
ANISOU 2671  O   VAL A1149     5516  10013  11879   -215   -414   -301       O  
ATOM   2672  CB  VAL A1149      69.186 168.733 322.191  1.00 50.54           C  
ANISOU 2672  CB  VAL A1149     2682   7489   9031     78   -137   -120       C  
ATOM   2673  CG1 VAL A1149      70.496 168.851 322.942  1.00 48.47           C  
ANISOU 2673  CG1 VAL A1149     2506   7064   8847     95   -130   -281       C  
ATOM   2674  CG2 VAL A1149      69.063 169.840 321.171  1.00 49.28           C  
ANISOU 2674  CG2 VAL A1149     2501   7332   8893    164    -33    -83       C  
ATOM   2675  N   ILE A1150      69.156 165.844 323.395  1.00 54.12           N  
ANISOU 2675  N   ILE A1150     3128   7971   9463   -181   -421   -100       N  
ATOM   2676  CA  ILE A1150      69.706 164.749 324.186  1.00 48.93           C  
ANISOU 2676  CA  ILE A1150     2484   7250   8857   -277   -534   -133       C  
ATOM   2677  C   ILE A1150      69.766 163.464 323.370  1.00 48.97           C  
ANISOU 2677  C   ILE A1150     2478   7213   8915   -410   -644   -137       C  
ATOM   2678  O   ILE A1150      70.687 162.654 323.534  1.00 48.74           O  
ANISOU 2678  O   ILE A1150     2477   7043   8998   -484   -718   -217       O  
ATOM   2679  CB  ILE A1150      68.878 164.585 325.474  1.00 49.50           C  
ANISOU 2679  CB  ILE A1150     2495   7467   8847   -281   -558    -21       C  
ATOM   2680  CG1 ILE A1150      69.078 165.810 326.370  1.00 49.66           C  
ANISOU 2680  CG1 ILE A1150     2538   7498   8833   -167   -439    -70       C  
ATOM   2681  CG2 ILE A1150      69.226 163.287 326.202  1.00 49.61           C  
ANISOU 2681  CG2 ILE A1150     2492   7447   8910   -402   -698      0       C  
ATOM   2682  CD1 ILE A1150      68.099 165.896 327.514  1.00 50.52           C  
ANISOU 2682  CD1 ILE A1150     2579   7780   8835   -157   -420     32       C  
ATOM   2683  N   THR A1151      68.811 163.265 322.461  1.00 52.41           N  
ANISOU 2683  N   THR A1151     2867   7763   9283   -446   -654    -55       N  
ATOM   2684  CA  THR A1151      68.827 162.063 321.634  1.00 59.69           C  
ANISOU 2684  CA  THR A1151     3778   8651  10252   -585   -747    -81       C  
ATOM   2685  C   THR A1151      70.002 162.072 320.661  1.00 68.83           C  
ANISOU 2685  C   THR A1151     5009   9642  11502   -609   -717   -250       C  
ATOM   2686  O   THR A1151      70.589 161.020 320.381  1.00 75.26           O  
ANISOU 2686  O   THR A1151     5834  10337  12424   -717   -785   -338       O  
ATOM   2687  CB  THR A1151      67.499 161.924 320.888  1.00 59.20           C  
ANISOU 2687  CB  THR A1151     3645   8772  10076   -628   -763     48       C  
ATOM   2688  OG1 THR A1151      66.462 161.641 321.835  1.00 61.34           O  
ANISOU 2688  OG1 THR A1151     3840   9180  10286   -629   -808    201       O  
ATOM   2689  CG2 THR A1151      67.564 160.793 319.868  1.00 56.24           C  
ANISOU 2689  CG2 THR A1151     3266   8363   9740   -780   -841    -13       C  
ATOM   2690  N   THR A1152      70.374 163.246 320.148  1.00 66.99           N  
ANISOU 2690  N   THR A1152     4821   9390  11243   -509   -609   -298       N  
ATOM   2691  CA  THR A1152      71.549 163.322 319.287  1.00 61.28           C  
ANISOU 2691  CA  THR A1152     4167   8510  10605   -526   -572   -458       C  
ATOM   2692  C   THR A1152      72.841 162.991 320.037  1.00 65.49           C  
ANISOU 2692  C   THR A1152     4751   8841  11290   -525   -596   -577       C  
ATOM   2693  O   THR A1152      73.834 162.613 319.400  1.00 69.72           O  
ANISOU 2693  O   THR A1152     5331   9225  11933   -576   -592   -714       O  
ATOM   2694  CB  THR A1152      71.641 164.707 318.640  1.00 52.12           C  
ANISOU 2694  CB  THR A1152     3031   7381   9392   -414   -453   -459       C  
ATOM   2695  OG1 THR A1152      71.625 165.717 319.655  1.00 48.76           O  
ANISOU 2695  OG1 THR A1152     2607   6955   8963   -280   -388   -419       O  
ATOM   2696  CG2 THR A1152      70.476 164.932 317.688  1.00 49.01           C  
ANISOU 2696  CG2 THR A1152     2576   7180   8867   -440   -441   -334       C  
ATOM   2697  N   PHE A1153      72.850 163.098 321.370  1.00 58.45           N  
ANISOU 2697  N   PHE A1153     3848   7952  10408   -479   -621   -525       N  
ATOM   2698  CA  PHE A1153      74.042 162.733 322.134  1.00 52.96           C  
ANISOU 2698  CA  PHE A1153     3187   7083   9853   -495   -661   -609       C  
ATOM   2699  C   PHE A1153      74.201 161.218 322.209  1.00 52.89           C  
ANISOU 2699  C   PHE A1153     3203   6997   9896   -623   -766   -596       C  
ATOM   2700  O   PHE A1153      75.243 160.671 321.830  1.00 57.57           O  
ANISOU 2700  O   PHE A1153     3869   7407  10598   -665   -771   -700       O  
ATOM   2701  CB  PHE A1153      73.983 163.329 323.543  1.00 48.50           C  
ANISOU 2701  CB  PHE A1153     2617   6571   9240   -423   -653   -550       C  
ATOM   2702  CG  PHE A1153      74.364 164.788 323.621  1.00 47.01           C  
ANISOU 2702  CG  PHE A1153     2482   6365   9016   -290   -530   -610       C  
ATOM   2703  CD1 PHE A1153      75.600 165.178 324.105  1.00 46.60           C  
ANISOU 2703  CD1 PHE A1153     2486   6164   9057   -257   -511   -715       C  
ATOM   2704  CD2 PHE A1153      73.474 165.770 323.238  1.00 47.19           C  
ANISOU 2704  CD2 PHE A1153     2486   6515   8928   -201   -434   -552       C  
ATOM   2705  CE1 PHE A1153      75.941 166.519 324.189  1.00 46.35           C  
ANISOU 2705  CE1 PHE A1153     2498   6107   9004   -139   -396   -775       C  
ATOM   2706  CE2 PHE A1153      73.811 167.103 323.327  1.00 46.98           C  
ANISOU 2706  CE2 PHE A1153     2494   6456   8899    -79   -316   -604       C  
ATOM   2707  CZ  PHE A1153      75.048 167.479 323.795  1.00 46.55           C  
ANISOU 2707  CZ  PHE A1153     2502   6249   8934    -49   -296   -723       C  
ATOM   2708  N   ARG A1154      73.175 160.519 322.701  1.00 50.01           N  
ANISOU 2708  N   ARG A1154     2787   6763   9451   -678   -838   -462       N  
ATOM   2709  CA  ARG A1154      73.289 159.081 322.923  1.00 50.67           C  
ANISOU 2709  CA  ARG A1154     2901   6772   9580   -788   -929   -430       C  
ATOM   2710  C   ARG A1154      73.370 158.288 321.624  1.00 49.85           C  
ANISOU 2710  C   ARG A1154     2825   6590   9524   -877   -927   -519       C  
ATOM   2711  O   ARG A1154      73.876 157.159 321.638  1.00 49.64           O  
ANISOU 2711  O   ARG A1154     2845   6426   9591   -953   -971   -548       O  
ATOM   2712  CB  ARG A1154      72.114 158.589 323.770  1.00 56.31           C  
ANISOU 2712  CB  ARG A1154     3549   7659  10189   -822   -999   -261       C  
ATOM   2713  CG  ARG A1154      70.858 159.441 323.633  1.00 63.43           C  
ANISOU 2713  CG  ARG A1154     4363   8777  10962   -765   -960   -174       C  
ATOM   2714  CD  ARG A1154      69.620 158.749 324.199  1.00 69.82           C  
ANISOU 2714  CD  ARG A1154     5110   9751  11669   -817  -1029    -15       C  
ATOM   2715  NE  ARG A1154      69.318 157.499 323.503  1.00 73.32           N  
ANISOU 2715  NE  ARG A1154     5568  10163  12129   -933  -1090    -15       N  
ATOM   2716  CZ  ARG A1154      69.453 156.287 324.038  1.00 74.85           C  
ANISOU 2716  CZ  ARG A1154     5787  10288  12366  -1012  -1165     22       C  
ATOM   2717  NH1 ARG A1154      69.875 156.148 325.291  1.00 73.50           N  
ANISOU 2717  NH1 ARG A1154     5625  10090  12210   -995  -1200     79       N  
ATOM   2718  NH2 ARG A1154      69.154 155.211 323.320  1.00 76.82           N  
ANISOU 2718  NH2 ARG A1154     6043  10501  12645  -1112  -1204      3       N  
ATOM   2719  N   THR A1155      72.895 158.849 320.506  1.00 53.77           N  
ANISOU 2719  N   THR A1155     3290   7179   9963   -874   -872   -564       N  
ATOM   2720  CA  THR A1155      72.936 158.167 319.218  1.00 58.21           C  
ANISOU 2720  CA  THR A1155     3868   7699  10549   -978   -863   -664       C  
ATOM   2721  C   THR A1155      73.995 158.702 318.259  1.00 56.05           C  
ANISOU 2721  C   THR A1155     3648   7301  10349   -958   -776   -838       C  
ATOM   2722  O   THR A1155      74.376 157.982 317.328  1.00 55.85           O  
ANISOU 2722  O   THR A1155     3659   7189  10374  -1052   -760   -957       O  
ATOM   2723  CB  THR A1155      71.565 158.231 318.517  1.00 65.77           C  
ANISOU 2723  CB  THR A1155     4740   8878  11371  -1029   -878   -582       C  
ATOM   2724  OG1 THR A1155      70.980 159.529 318.692  1.00 67.48           O  
ANISOU 2724  OG1 THR A1155     4889   9247  11502   -919   -832   -492       O  
ATOM   2725  CG2 THR A1155      70.614 157.157 319.062  1.00 68.80           C  
ANISOU 2725  CG2 THR A1155     5089   9343  11708  -1108   -971   -455       C  
ATOM   2726  N   GLY A1156      74.481 159.928 318.457  1.00 52.62           N  
ANISOU 2726  N   GLY A1156     3216   6855   9921   -842   -710   -860       N  
ATOM   2727  CA  GLY A1156      75.520 160.473 317.600  1.00 51.46           C  
ANISOU 2727  CA  GLY A1156     3118   6591   9845   -818   -624  -1016       C  
ATOM   2728  C   GLY A1156      75.142 160.559 316.140  1.00 53.56           C  
ANISOU 2728  C   GLY A1156     3348   6958  10044   -894   -579  -1084       C  
ATOM   2729  O   GLY A1156      76.023 160.519 315.273  1.00 56.46           O  
ANISOU 2729  O   GLY A1156     3765   7216  10473   -930   -518  -1236       O  
ATOM   2730  N   THR A1157      73.849 160.667 315.840  1.00 51.65           N  
ANISOU 2730  N   THR A1157     3040   6934   9651   -923   -603   -962       N  
ATOM   2731  CA  THR A1157      73.370 160.774 314.471  1.00 52.36           C  
ANISOU 2731  CA  THR A1157     3125   7162   9607  -1002   -565   -984       C  
ATOM   2732  C   THR A1157      72.273 161.824 314.407  1.00 50.14           C  
ANISOU 2732  C   THR A1157     2808   7103   9140   -917   -541   -797       C  
ATOM   2733  O   THR A1157      71.727 162.254 315.426  1.00 49.78           O  
ANISOU 2733  O   THR A1157     2734   7108   9074   -818   -557   -662       O  
ATOM   2734  CB  THR A1157      72.838 159.436 313.935  1.00 56.98           C  
ANISOU 2734  CB  THR A1157     3666   7786  10196  -1182   -636  -1029       C  
ATOM   2735  OG1 THR A1157      71.761 158.980 314.764  1.00 58.82           O  
ANISOU 2735  OG1 THR A1157     3831   8123  10395  -1191   -728   -868       O  
ATOM   2736  CG2 THR A1157      73.939 158.379 313.904  1.00 61.23           C  
ANISOU 2736  CG2 THR A1157     4287   8083  10893  -1251   -633  -1198       C  
ATOM   2737  N   TRP A1158      71.938 162.227 313.183  1.00 52.35           N  
ANISOU 2737  N   TRP A1158     3080   7521   9288   -967   -498   -786       N  
ATOM   2738  CA  TRP A1158      70.835 163.146 312.954  1.00 60.84           C  
ANISOU 2738  CA  TRP A1158     4099   8813  10204   -907   -479   -589       C  
ATOM   2739  C   TRP A1158      69.487 162.434 312.862  1.00 78.27           C  
ANISOU 2739  C   TRP A1158     6228  11207  12304  -1011   -567   -459       C  
ATOM   2740  O   TRP A1158      68.539 162.999 312.301  1.00 87.96           O  
ANISOU 2740  O   TRP A1158     7395  12636  13388  -1013   -561   -302       O  
ATOM   2741  CB  TRP A1158      71.071 163.953 311.677  1.00 55.51           C  
ANISOU 2741  CB  TRP A1158     3435   8221   9435   -918   -402   -601       C  
ATOM   2742  CG  TRP A1158      72.430 164.534 311.568  1.00 51.65           C  
ANISOU 2742  CG  TRP A1158     3021   7552   9051   -842   -318   -743       C  
ATOM   2743  CD1 TRP A1158      73.487 164.019 310.875  1.00 52.91           C  
ANISOU 2743  CD1 TRP A1158     3240   7590   9275   -933   -289   -945       C  
ATOM   2744  CD2 TRP A1158      72.892 165.750 312.163  1.00 50.02           C  
ANISOU 2744  CD2 TRP A1158     2835   7263   8908   -663   -244   -700       C  
ATOM   2745  NE1 TRP A1158      74.581 164.841 311.002  1.00 53.19           N  
ANISOU 2745  NE1 TRP A1158     3330   7474   9406   -818   -209  -1018       N  
ATOM   2746  CE2 TRP A1158      74.241 165.910 311.791  1.00 49.61           C  
ANISOU 2746  CE2 TRP A1158     2855   7040   8953   -653   -183   -871       C  
ATOM   2747  CE3 TRP A1158      72.298 166.717 312.974  1.00 49.72           C  
ANISOU 2747  CE3 TRP A1158     2757   7272   8863   -514   -216   -543       C  
ATOM   2748  CZ2 TRP A1158      75.004 166.998 312.206  1.00 48.86           C  
ANISOU 2748  CZ2 TRP A1158     2796   6825   8945   -502   -106   -882       C  
ATOM   2749  CZ3 TRP A1158      73.055 167.795 313.380  1.00 49.06           C  
ANISOU 2749  CZ3 TRP A1158     2708   7065   8869   -367   -132   -570       C  
ATOM   2750  CH2 TRP A1158      74.394 167.927 312.997  1.00 48.62           C  
ANISOU 2750  CH2 TRP A1158     2726   6842   8904   -363    -83   -735       C  
ATOM   2751  N   ASP A1159      69.385 161.207 313.390  1.00 81.48           N  
ANISOU 2751  N   ASP A1159     6623  11548  12788  -1101   -652   -508       N  
ATOM   2752  CA  ASP A1159      68.165 160.420 313.218  1.00 80.21           C  
ANISOU 2752  CA  ASP A1159     6387  11552  12537  -1220   -741   -401       C  
ATOM   2753  C   ASP A1159      66.948 161.150 313.777  1.00 73.24           C  
ANISOU 2753  C   ASP A1159     5430  10847  11549  -1119   -750   -158       C  
ATOM   2754  O   ASP A1159      65.883 161.168 313.148  1.00 73.15           O  
ANISOU 2754  O   ASP A1159     5352  11040  11403  -1187   -781    -26       O  
ATOM   2755  CB  ASP A1159      68.324 159.045 313.881  1.00 79.53           C  
ANISOU 2755  CB  ASP A1159     6291  11335  12591  -1310   -827   -479       C  
ATOM   2756  CG  ASP A1159      69.049 158.031 312.991  1.00 80.10           C  
ANISOU 2756  CG  ASP A1159     6397  11292  12747  -1474   -831   -700       C  
ATOM   2757  OD1 ASP A1159      68.922 158.125 311.754  1.00 80.74           O  
ANISOU 2757  OD1 ASP A1159     6485  11485  12709  -1574   -798   -759       O  
ATOM   2758  OD2 ASP A1159      69.741 157.135 313.528  1.00 79.34           O  
ANISOU 2758  OD2 ASP A1159     6333  10995  12817  -1504   -858   -804       O  
ATOM   2759  N   ALA A1160      67.097 161.784 314.944  1.00 68.50           N  
ANISOU 2759  N   ALA A1160     4837  10177  11011   -962   -717   -100       N  
ATOM   2760  CA  ALA A1160      65.956 162.375 315.634  1.00 65.95           C  
ANISOU 2760  CA  ALA A1160     4438  10002  10617   -867   -714    111       C  
ATOM   2761  C   ALA A1160      65.434 163.632 314.952  1.00 62.94           C  
ANISOU 2761  C   ALA A1160     4016   9761  10139   -787   -635    242       C  
ATOM   2762  O   ALA A1160      64.307 164.053 315.238  1.00 59.74           O  
ANISOU 2762  O   ALA A1160     3525   9505   9670   -735   -633    434       O  
ATOM   2763  CB  ALA A1160      66.334 162.693 317.080  1.00 67.01           C  
ANISOU 2763  CB  ALA A1160     4593  10025  10841   -737   -689    108       C  
ATOM   2764  N   TYR A1161      66.211 164.228 314.052  1.00 64.67           N  
ANISOU 2764  N   TYR A1161     4283   9934  10355   -779   -569    154       N  
ATOM   2765  CA  TYR A1161      65.867 165.523 313.472  1.00 63.17           C  
ANISOU 2765  CA  TYR A1161     4046   9849  10106   -688   -487    287       C  
ATOM   2766  C   TYR A1161      65.247 165.444 312.079  1.00 65.44           C  
ANISOU 2766  C   TYR A1161     4277  10333  10253   -821   -519    378       C  
ATOM   2767  O   TYR A1161      64.275 166.152 311.809  1.00 67.21           O  
ANISOU 2767  O   TYR A1161     4405  10724  10409   -781   -505    591       O  
ATOM   2768  CB  TYR A1161      67.111 166.420 313.443  1.00 60.47           C  
ANISOU 2768  CB  TYR A1161     3780   9340   9857   -578   -387    164       C  
ATOM   2769  CG  TYR A1161      67.254 167.280 314.677  1.00 53.05           C  
ANISOU 2769  CG  TYR A1161     2844   8300   9013   -397   -314    189       C  
ATOM   2770  CD1 TYR A1161      67.444 166.709 315.931  1.00 50.98           C  
ANISOU 2770  CD1 TYR A1161     2613   7940   8816   -376   -350    122       C  
ATOM   2771  CD2 TYR A1161      67.191 168.663 314.590  1.00 52.11           C  
ANISOU 2771  CD2 TYR A1161     2687   8189   8922   -257   -208    280       C  
ATOM   2772  CE1 TYR A1161      67.569 167.496 317.064  1.00 50.55           C  
ANISOU 2772  CE1 TYR A1161     2563   7815   8827   -229   -279    130       C  
ATOM   2773  CE2 TYR A1161      67.317 169.457 315.712  1.00 51.25           C  
ANISOU 2773  CE2 TYR A1161     2581   7988   8905   -102   -129    278       C  
ATOM   2774  CZ  TYR A1161      67.507 168.871 316.947  1.00 50.69           C  
ANISOU 2774  CZ  TYR A1161     2551   7837   8873    -94   -164    195       C  
ATOM   2775  OH  TYR A1161      67.631 169.664 318.066  1.00 50.43           O  
ANISOU 2775  OH  TYR A1161     2522   7732   8909     42    -81    179       O  
ATOM   2776  N   GLY A1200      65.768 164.613 311.187  1.00 60.91           N  
ANISOU 2776  N   GLY A1200     3753   9752   9638   -984   -559    224       N  
ATOM   2777  CA  GLY A1200      65.254 164.587 309.830  1.00 60.45           C  
ANISOU 2777  CA  GLY A1200     3645   9900   9423  -1128   -585    296       C  
ATOM   2778  C   GLY A1200      65.733 163.363 309.084  1.00 60.45           C  
ANISOU 2778  C   GLY A1200     3701   9880   9387  -1332   -636     87       C  
ATOM   2779  O   GLY A1200      66.405 162.496 309.645  1.00 62.55           O  
ANISOU 2779  O   GLY A1200     4032   9960   9773  -1356   -655    -96       O  
ATOM   2780  N   SER A1201      65.380 163.300 307.800  1.00 60.18           N  
ANISOU 2780  N   SER A1201     3632  10042   9191  -1489   -655    117       N  
ATOM   2781  CA  SER A1201      65.800 162.164 306.979  1.00 62.52           C  
ANISOU 2781  CA  SER A1201     3976  10337   9440  -1704   -686   -103       C  
ATOM   2782  C   SER A1201      65.848 162.603 305.514  1.00 66.21           C  
ANISOU 2782  C   SER A1201     4427  11002   9727  -1833   -656    -91       C  
ATOM   2783  O   SER A1201      64.820 162.634 304.835  1.00 69.16           O  
ANISOU 2783  O   SER A1201     4715  11634   9929  -1947   -715     77       O  
ATOM   2784  CB  SER A1201      64.865 160.977 307.166  1.00 62.85           C  
ANISOU 2784  CB  SER A1201     3972  10459   9451  -1843   -795    -83       C  
ATOM   2785  OG  SER A1201      64.972 160.439 308.471  1.00 62.36           O  
ANISOU 2785  OG  SER A1201     3928  10206   9559  -1749   -824   -117       O  
ATOM   2786  N   GLY A1202      67.046 162.958 305.049  1.00 67.77           N  
ANISOU 2786  N   GLY A1202     4700  11086   9963  -1816   -568   -258       N  
ATOM   2787  CA  GLY A1202      67.314 163.173 303.631  1.00 68.74           C  
ANISOU 2787  CA  GLY A1202     4822  11379   9916  -1970   -533   -306       C  
ATOM   2788  C   GLY A1202      67.091 164.563 303.055  1.00 69.18           C  
ANISOU 2788  C   GLY A1202     4811  11603   9870  -1893   -492    -73       C  
ATOM   2789  O   GLY A1202      67.076 164.700 301.828  1.00 68.72           O  
ANISOU 2789  O   GLY A1202     4727  11750   9632  -2051   -485    -61       O  
ATOM   2790  N   SER A1203      66.921 165.595 303.879  1.00 69.48           N  
ANISOU 2790  N   SER A1203     4813  11566  10021  -1666   -461    114       N  
ATOM   2791  CA  SER A1203      66.699 166.937 303.358  1.00 74.47           C  
ANISOU 2791  CA  SER A1203     5364  12335  10597  -1585   -418    350       C  
ATOM   2792  C   SER A1203      67.861 167.876 303.633  1.00 72.69           C  
ANISOU 2792  C   SER A1203     5196  11900  10521  -1407   -308    278       C  
ATOM   2793  O   SER A1203      67.729 169.083 303.415  1.00 72.53           O  
ANISOU 2793  O   SER A1203     5104  11941  10513  -1299   -261    481       O  
ATOM   2794  CB  SER A1203      65.413 167.526 303.936  1.00 75.97           C  
ANISOU 2794  CB  SER A1203     5431  12635  10800  -1474   -459    660       C  
ATOM   2795  OG  SER A1203      65.497 167.650 305.347  1.00 76.62           O  
ANISOU 2795  OG  SER A1203     5544  12495  11073  -1277   -432    637       O  
ATOM   2796  N   ARG A 214      68.998 167.356 304.084  1.00 77.27           N  
ANISOU 2796  N   ARG A 214     5897  12233  11230  -1379   -266      5       N  
ATOM   2797  CA  ARG A 214      70.111 168.196 304.483  1.00 80.16           C  
ANISOU 2797  CA  ARG A 214     6322  12382  11755  -1205   -168    -69       C  
ATOM   2798  C   ARG A 214      71.317 168.086 303.566  1.00 89.70           C  
ANISOU 2798  C   ARG A 214     7604  13540  12938  -1299   -104   -277       C  
ATOM   2799  O   ARG A 214      72.247 168.893 303.696  1.00 95.10           O  
ANISOU 2799  O   ARG A 214     8325  14073  13737  -1167    -21   -316       O  
ATOM   2800  CB  ARG A 214      70.541 167.849 305.913  1.00 77.83           C  
ANISOU 2800  CB  ARG A 214     6095  11819  11656  -1066   -166   -194       C  
ATOM   2801  CG  ARG A 214      70.640 166.354 306.165  1.00 76.63           C  
ANISOU 2801  CG  ARG A 214     6001  11595  11521  -1202   -231   -393       C  
ATOM   2802  CD  ARG A 214      69.445 165.838 306.952  1.00 76.27           C  
ANISOU 2802  CD  ARG A 214     5896  11622  11461  -1200   -321   -260       C  
ATOM   2803  NE  ARG A 214      69.669 165.914 308.394  1.00 74.91           N  
ANISOU 2803  NE  ARG A 214     5755  11250  11459  -1035   -316   -275       N  
ATOM   2804  CZ  ARG A 214      69.419 166.984 309.144  1.00 73.74           C  
ANISOU 2804  CZ  ARG A 214     5571  11074  11373   -849   -272   -125       C  
ATOM   2805  NH1 ARG A 214      68.930 168.090 308.599  1.00 75.45           N  
ANISOU 2805  NH1 ARG A 214     5712  11431  11525   -790   -228     67       N  
ATOM   2806  NH2 ARG A 214      69.661 166.946 310.447  1.00 71.20           N  
ANISOU 2806  NH2 ARG A 214     5282  10586  11185   -728   -269   -166       N  
ATOM   2807  N   PHE A 215      71.330 167.126 302.649  1.00 86.91           N  
ANISOU 2807  N   PHE A 215     7271  13309  12443  -1524   -133   -418       N  
ATOM   2808  CA  PHE A 215      72.536 166.831 301.887  1.00 84.63           C  
ANISOU 2808  CA  PHE A 215     7061  12943  12150  -1623    -59   -667       C  
ATOM   2809  C   PHE A 215      72.807 167.924 300.860  1.00 87.81           C  
ANISOU 2809  C   PHE A 215     7421  13501  12441  -1630      2   -545       C  
ATOM   2810  O   PHE A 215      72.008 168.142 299.942  1.00 91.47           O  
ANISOU 2810  O   PHE A 215     7799  14257  12697  -1760    -36   -372       O  
ATOM   2811  CB  PHE A 215      72.405 165.472 301.212  1.00 79.44           C  
ANISOU 2811  CB  PHE A 215     6429  12377  11378  -1873    -96   -867       C  
ATOM   2812  CG  PHE A 215      72.530 164.327 302.160  1.00 76.69           C  
ANISOU 2812  CG  PHE A 215     6134  11811  11194  -1870   -135  -1042       C  
ATOM   2813  CD1 PHE A 215      71.625 164.167 303.194  1.00 76.47           C  
ANISOU 2813  CD1 PHE A 215     6065  11766  11224  -1780   -219   -891       C  
ATOM   2814  CD2 PHE A 215      73.556 163.415 302.024  1.00 77.54           C  
ANISOU 2814  CD2 PHE A 215     6321  11729  11411  -1957    -85  -1348       C  
ATOM   2815  CE1 PHE A 215      71.741 163.118 304.075  1.00 78.75           C  
ANISOU 2815  CE1 PHE A 215     6390  11864  11666  -1781   -261  -1029       C  
ATOM   2816  CE2 PHE A 215      73.677 162.360 302.898  1.00 79.75           C  
ANISOU 2816  CE2 PHE A 215     6631  11803  11868  -1955   -125  -1485       C  
ATOM   2817  CZ  PHE A 215      72.770 162.212 303.928  1.00 80.02           C  
ANISOU 2817  CZ  PHE A 215     6623  11833  11948  -1869   -218  -1319       C  
ATOM   2818  N   HIS A 216      73.936 168.612 301.024  1.00 84.94           N  
ANISOU 2818  N   HIS A 216     7110  12945  12219  -1494     93   -621       N  
ATOM   2819  CA  HIS A 216      74.371 169.648 300.103  1.00 81.36           C  
ANISOU 2819  CA  HIS A 216     6620  12600  11693  -1490    160   -521       C  
ATOM   2820  C   HIS A 216      75.849 169.451 299.795  1.00 78.56           C  
ANISOU 2820  C   HIS A 216     6365  12062  11422  -1508    256   -795       C  
ATOM   2821  O   HIS A 216      76.565 168.727 300.495  1.00 72.64           O  
ANISOU 2821  O   HIS A 216     5704  11058  10836  -1472    273  -1026       O  
ATOM   2822  CB  HIS A 216      74.141 171.060 300.671  1.00 75.72           C  
ANISOU 2822  CB  HIS A 216     5835  11838  11099  -1259    184   -260       C  
ATOM   2823  CG  HIS A 216      72.699 171.425 300.863  1.00 75.91           C  
ANISOU 2823  CG  HIS A 216     5738  12050  11054  -1233    109     38       C  
ATOM   2824  ND1 HIS A 216      71.845 170.709 301.676  1.00 75.69           N  
ANISOU 2824  ND1 HIS A 216     5705  12010  11042  -1230     33     50       N  
ATOM   2825  CD2 HIS A 216      71.967 172.450 300.364  1.00 76.75           C  
ANISOU 2825  CD2 HIS A 216     5712  12353  11095  -1204    102    349       C  
ATOM   2826  CE1 HIS A 216      70.649 171.268 301.659  1.00 76.86           C  
ANISOU 2826  CE1 HIS A 216     5729  12341  11132  -1200    -14    345       C  
ATOM   2827  NE2 HIS A 216      70.696 172.328 300.872  1.00 77.64           N  
ANISOU 2827  NE2 HIS A 216     5745  12566  11190  -1183     26    534       N  
ATOM   2828  N   ARG A 217      76.289 170.114 298.726  1.00 85.40           N  
ANISOU 2828  N   ARG A 217     7204  13067  12179  -1570    317   -750       N  
ATOM   2829  CA  ARG A 217      77.695 170.201 298.326  1.00 88.85           C  
ANISOU 2829  CA  ARG A 217     7716  13353  12690  -1571    422   -962       C  
ATOM   2830  C   ARG A 217      78.180 171.614 298.658  1.00 93.55           C  
ANISOU 2830  C   ARG A 217     8283  13832  13431  -1351    476   -795       C  
ATOM   2831  O   ARG A 217      78.166 172.507 297.808  1.00 96.03           O  
ANISOU 2831  O   ARG A 217     8524  14320  13643  -1371    507   -622       O  
ATOM   2832  CB  ARG A 217      77.868 169.878 296.842  1.00 90.46           C  
ANISOU 2832  CB  ARG A 217     7907  13810  12652  -1820    459  -1048       C  
ATOM   2833  N   ARG A 218      78.615 171.805 299.908  1.00 91.33           N  
ANISOU 2833  N   ARG A 218     8053  13256  13392  -1148    487   -847       N  
ATOM   2834  CA  ARG A 218      79.045 173.125 300.366  1.00 89.70           C  
ANISOU 2834  CA  ARG A 218     7821  12913  13348   -932    540   -708       C  
ATOM   2835  C   ARG A 218      80.275 173.623 299.613  1.00 90.80           C  
ANISOU 2835  C   ARG A 218     7989  12995  13515   -940    638   -800       C  
ATOM   2836  O   ARG A 218      80.481 174.839 299.498  1.00 90.75           O  
ANISOU 2836  O   ARG A 218     7925  12978  13576   -817    682   -629       O  
ATOM   2837  CB  ARG A 218      79.324 173.088 301.868  1.00 84.45           C  
ANISOU 2837  CB  ARG A 218     7216  11954  12916   -746    532   -787       C  
ATOM   2838  N   ARG A 219      81.104 172.709 299.105  1.00 92.70           N  
ANISOU 2838  N   ARG A 219     8309  13189  13723  -1081    678  -1068       N  
ATOM   2839  CA  ARG A 219      82.302 173.101 298.371  1.00 92.34           C  
ANISOU 2839  CA  ARG A 219     8291  13092  13702  -1099    779  -1173       C  
ATOM   2840  C   ARG A 219      81.929 173.841 297.091  1.00 93.03           C  
ANISOU 2840  C   ARG A 219     8281  13492  13573  -1205    796   -966       C  
ATOM   2841  O   ARG A 219      81.049 173.408 296.341  1.00 93.94           O  
ANISOU 2841  O   ARG A 219     8344  13896  13452  -1389    745   -894       O  
ATOM   2842  CB  ARG A 219      83.156 171.868 298.054  1.00 93.21           C  
ANISOU 2842  CB  ARG A 219     8494  13101  13820  -1247    827  -1509       C  
ATOM   2843  CG  ARG A 219      82.382 170.673 297.497  1.00 95.82           C  
ANISOU 2843  CG  ARG A 219     8821  13635  13951  -1478    779  -1608       C  
ATOM   2844  CD  ARG A 219      82.907 169.354 298.073  1.00 96.29           C  
ANISOU 2844  CD  ARG A 219     8968  13457  14162  -1523    785  -1909       C  
ATOM   2845  NE  ARG A 219      82.436 168.184 297.328  1.00 97.99           N  
ANISOU 2845  NE  ARG A 219     9183  13844  14203  -1770    773  -2064       N  
ATOM   2846  CZ  ARG A 219      82.769 166.926 297.612  1.00 96.72           C  
ANISOU 2846  CZ  ARG A 219     9077  13514  14157  -1854    783  -2328       C  
ATOM   2847  NH1 ARG A 219      83.577 166.663 298.631  1.00 96.15           N  
ANISOU 2847  NH1 ARG A 219     9059  13105  14369  -1711    796  -2447       N  
ATOM   2848  NH2 ARG A 219      82.294 165.930 296.875  1.00 95.97           N  
ANISOU 2848  NH2 ARG A 219     8974  13588  13901  -2087    779  -2469       N  
ATOM   2849  N   ARG A 220      82.599 174.966 296.850  1.00 93.14           N  
ANISOU 2849  N   ARG A 220     8263  13455  13672  -1095    863   -858       N  
ATOM   2850  CA  ARG A 220      82.331 175.824 295.706  1.00 95.36           C  
ANISOU 2850  CA  ARG A 220     8434  14016  13784  -1172    879   -622       C  
ATOM   2851  C   ARG A 220      83.431 175.659 294.655  1.00105.52           C  
ANISOU 2851  C   ARG A 220     9759  15352  14982  -1309    974   -797       C  
ATOM   2852  O   ARG A 220      84.329 174.819 294.797  1.00111.09           O  
ANISOU 2852  O   ARG A 220    10573  15875  15762  -1349   1030  -1108       O  
ATOM   2853  CB  ARG A 220      82.191 177.279 296.164  1.00 89.46           C  
ANISOU 2853  CB  ARG A 220     7596  13186  13207   -950    886   -339       C  
ATOM   2854  CG  ARG A 220      80.777 177.670 296.580  1.00 84.31           C  
ANISOU 2854  CG  ARG A 220     6838  12660  12536   -890    800    -57       C  
ATOM   2855  CD  ARG A 220      80.702 179.153 296.881  1.00 81.54           C  
ANISOU 2855  CD  ARG A 220     6381  12229  12371   -686    830    214       C  
ATOM   2856  NE  ARG A 220      81.916 179.597 297.557  1.00 79.67           N  
ANISOU 2856  NE  ARG A 220     6226  11663  12383   -514    910     55       N  
ATOM   2857  CZ  ARG A 220      82.162 179.408 298.849  1.00 79.01           C  
ANISOU 2857  CZ  ARG A 220     6228  11297  12496   -363    911    -97       C  
ATOM   2858  NH1 ARG A 220      81.272 178.782 299.609  1.00 78.86           N  
ANISOU 2858  NH1 ARG A 220     6224  11282  12456   -358    840   -109       N  
ATOM   2859  NH2 ARG A 220      83.301 179.840 299.379  1.00 78.02           N  
ANISOU 2859  NH2 ARG A 220     6169  10894  12582   -226    979   -232       N  
ATOM   2860  N   THR A 221      83.355 176.475 293.592  1.00101.60           N  
ANISOU 2860  N   THR A 221     9162  15107  14336  -1384    996   -584       N  
ATOM   2861  CA  THR A 221      84.335 176.436 292.508  1.00 97.49           C  
ANISOU 2861  CA  THR A 221     8660  14679  13703  -1525   1092   -716       C  
ATOM   2862  C   THR A 221      85.755 176.700 293.002  1.00 98.64           C  
ANISOU 2862  C   THR A 221     8890  14479  14111  -1366   1190   -903       C  
ATOM   2863  O   THR A 221      86.712 176.474 292.250  1.00105.53           O  
ANISOU 2863  O   THR A 221     9800  15367  14929  -1473   1284  -1080       O  
ATOM   2864  CB  THR A 221      83.963 177.453 291.418  1.00 82.27           C  
ANISOU 2864  CB  THR A 221     6588  13076  11596  -1603   1087   -391       C  
ATOM   2865  OG1 THR A 221      84.671 177.154 290.209  1.00 79.95           O  
ANISOU 2865  OG1 THR A 221     6308  12969  11100  -1814   1168   -532       O  
ATOM   2866  CG2 THR A 221      84.313 178.869 291.856  1.00 77.02           C  
ANISOU 2866  CG2 THR A 221     5853  12238  11174  -1359   1112   -154       C  
ATOM   2867  N   GLY A 222      85.907 177.179 294.243  1.00 93.95           N  
ANISOU 2867  N   GLY A 222     8321  13581  13794  -1121   1172   -867       N  
ATOM   2868  CA  GLY A 222      87.212 177.309 294.871  1.00 84.55           C  
ANISOU 2868  CA  GLY A 222     7217  12045  12864   -973   1248  -1058       C  
ATOM   2869  C   GLY A 222      87.905 175.988 295.133  1.00 77.26           C  
ANISOU 2869  C   GLY A 222     6416  10946  11992  -1054   1281  -1420       C  
ATOM   2870  O   GLY A 222      89.115 175.970 295.380  1.00 73.99           O  
ANISOU 2870  O   GLY A 222     6067  10281  11763   -982   1356  -1598       O  
ATOM   2871  N   ARG A 223      87.159 174.880 295.102  1.00 73.66           N  
ANISOU 2871  N   ARG A 223     5985  10606  11398  -1201   1226  -1525       N  
ATOM   2872  CA  ARG A 223      87.777 173.559 295.083  1.00 75.05           C  
ANISOU 2872  CA  ARG A 223     6254  10656  11605  -1322   1271  -1868       C  
ATOM   2873  C   ARG A 223      88.639 173.365 293.834  1.00 75.46           C  
ANISOU 2873  C   ARG A 223     6315  10821  11536  -1494   1390  -2032       C  
ATOM   2874  O   ARG A 223      89.652 172.657 293.882  1.00 78.48           O  
ANISOU 2874  O   ARG A 223     6769  10996  12052  -1523   1473  -2316       O  
ATOM   2875  CB  ARG A 223      86.692 172.485 295.171  1.00 78.63           C  
ANISOU 2875  CB  ARG A 223     6711  11246  11917  -1463   1187  -1919       C  
ATOM   2876  CG  ARG A 223      87.079 171.222 295.921  1.00 82.06           C  
ANISOU 2876  CG  ARG A 223     7233  11423  12523  -1476   1186  -2205       C  
ATOM   2877  CD  ARG A 223      85.940 170.209 295.882  1.00 86.68           C  
ANISOU 2877  CD  ARG A 223     7807  12173  12953  -1631   1103  -2235       C  
ATOM   2878  NE  ARG A 223      85.615 169.792 294.518  1.00 91.70           N  
ANISOU 2878  NE  ARG A 223     8413  13128  13301  -1891   1140  -2300       N  
ATOM   2879  CZ  ARG A 223      86.087 168.690 293.942  1.00 94.35           C  
ANISOU 2879  CZ  ARG A 223     8794  13452  13604  -2080   1217  -2607       C  
ATOM   2880  NH1 ARG A 223      86.904 167.889 294.615  1.00 94.74           N  
ANISOU 2880  NH1 ARG A 223     8910  13171  13916  -2029   1260  -2858       N  
ATOM   2881  NH2 ARG A 223      85.739 168.384 292.696  1.00 95.85           N  
ANISOU 2881  NH2 ARG A 223     8953  13961  13506  -2329   1252  -2662       N  
ATOM   2882  N   LEU A 224      88.258 173.975 292.704  1.00 74.66           N  
ANISOU 2882  N   LEU A 224     6131  11051  11184  -1615   1403  -1853       N  
ATOM   2883  CA  LEU A 224      89.170 174.024 291.561  1.00 73.63           C  
ANISOU 2883  CA  LEU A 224     6001  11029  10947  -1754   1527  -1978       C  
ATOM   2884  C   LEU A 224      90.299 175.008 291.815  1.00 71.87           C  
ANISOU 2884  C   LEU A 224     5780  10577  10949  -1563   1597  -1929       C  
ATOM   2885  O   LEU A 224      91.444 174.771 291.419  1.00 74.47           O  
ANISOU 2885  O   LEU A 224     6155  10796  11346  -1605   1714  -2145       O  
ATOM   2886  CB  LEU A 224      88.426 174.407 290.279  1.00 74.15           C  
ANISOU 2886  CB  LEU A 224     5967  11544  10663  -1955   1512  -1777       C  
ATOM   2887  CG  LEU A 224      89.249 175.103 289.178  1.00 74.18           C  
ANISOU 2887  CG  LEU A 224     5926  11698  10560  -2031   1618  -1737       C  
ATOM   2888  CD1 LEU A 224      88.891 174.560 287.807  1.00 76.75           C  
ANISOU 2888  CD1 LEU A 224     6216  12432  10512  -2352   1653  -1804       C  
ATOM   2889  CD2 LEU A 224      89.074 176.626 289.204  1.00 74.62           C  
ANISOU 2889  CD2 LEU A 224     5874  11808  10670  -1866   1577  -1348       C  
ATOM   2890  N   VAL A 225      89.990 176.129 292.466  1.00 68.53           N  
ANISOU 2890  N   VAL A 225     5304  10080  10655  -1355   1534  -1651       N  
ATOM   2891  CA  VAL A 225      91.001 177.133 292.758  1.00 65.21           C  
ANISOU 2891  CA  VAL A 225     4880   9437  10461  -1168   1594  -1591       C  
ATOM   2892  C   VAL A 225      92.078 176.592 293.697  1.00 65.37           C  
ANISOU 2892  C   VAL A 225     5007   9061  10768  -1051   1637  -1863       C  
ATOM   2893  O   VAL A 225      93.166 177.168 293.782  1.00 66.57           O  
ANISOU 2893  O   VAL A 225     5173   9022  11099   -942   1709  -1895       O  
ATOM   2894  CB  VAL A 225      90.302 178.394 293.321  1.00 64.45           C  
ANISOU 2894  CB  VAL A 225     4694   9339  10454   -978   1516  -1245       C  
ATOM   2895  CG1 VAL A 225      91.292 179.514 293.592  1.00 63.53           C  
ANISOU 2895  CG1 VAL A 225     4562   9002  10576   -789   1577  -1168       C  
ATOM   2896  CG2 VAL A 225      89.215 178.866 292.354  1.00 64.59           C  
ANISOU 2896  CG2 VAL A 225     4587   9755  10199  -1108   1468   -955       C  
ATOM   2897  N   VAL A 226      91.820 175.470 294.380  1.00 61.69           N  
ANISOU 2897  N   VAL A 226     4612   8472  10356  -1080   1593  -2053       N  
ATOM   2898  CA  VAL A 226      92.768 174.921 295.349  1.00 57.82           C  
ANISOU 2898  CA  VAL A 226     4208   7610  10151   -972   1616  -2279       C  
ATOM   2899  C   VAL A 226      93.671 173.849 294.754  1.00 58.11           C  
ANISOU 2899  C   VAL A 226     4298   7579  10202  -1129   1723  -2599       C  
ATOM   2900  O   VAL A 226      94.519 173.303 295.472  1.00 57.11           O  
ANISOU 2900  O   VAL A 226     4231   7143  10326  -1058   1748  -2790       O  
ATOM   2901  CB  VAL A 226      92.050 174.361 296.596  1.00 55.91           C  
ANISOU 2901  CB  VAL A 226     4001   7232  10011   -892   1503  -2283       C  
ATOM   2902  CG1 VAL A 226      91.578 172.933 296.358  1.00 56.68           C  
ANISOU 2902  CG1 VAL A 226     4128   7412   9995  -1082   1487  -2480       C  
ATOM   2903  CG2 VAL A 226      92.963 174.428 297.814  1.00 54.15           C  
ANISOU 2903  CG2 VAL A 226     3835   6634  10107   -708   1498  -2372       C  
ATOM   2904  N   ILE A 227      93.528 173.526 293.474  1.00 60.28           N  
ANISOU 2904  N   ILE A 227     4547   8134  10224  -1345   1792  -2665       N  
ATOM   2905  CA  ILE A 227      94.481 172.642 292.822  1.00 64.43           C  
ANISOU 2905  CA  ILE A 227     5113   8594  10774  -1492   1924  -2979       C  
ATOM   2906  C   ILE A 227      95.495 173.425 291.998  1.00 65.78           C  
ANISOU 2906  C   ILE A 227     5259   8799  10936  -1493   2046  -2967       C  
ATOM   2907  O   ILE A 227      96.671 173.063 291.962  1.00 66.77           O  
ANISOU 2907  O   ILE A 227     5422   8704  11244  -1487   2156  -3189       O  
ATOM   2908  CB  ILE A 227      93.769 171.567 291.971  1.00 72.22           C  
ANISOU 2908  CB  ILE A 227     6097   9844  11499  -1759   1943  -3137       C  
ATOM   2909  CG1 ILE A 227      92.834 172.197 290.939  1.00 79.35           C  
ANISOU 2909  CG1 ILE A 227     6924  11183  12042  -1895   1911  -2908       C  
ATOM   2910  CG2 ILE A 227      93.026 170.590 292.877  1.00 71.62           C  
ANISOU 2910  CG2 ILE A 227     6055   9653  11505  -1754   1841  -3211       C  
ATOM   2911  CD1 ILE A 227      92.216 171.208 289.969  1.00 85.20           C  
ANISOU 2911  CD1 ILE A 227     7660  12219  12495  -2187   1939  -3072       C  
ATOM   2912  N   ILE A 228      95.081 174.525 291.363  1.00 66.03           N  
ANISOU 2912  N   ILE A 228     5216   9093  10781  -1493   2027  -2693       N  
ATOM   2913  CA  ILE A 228      96.030 175.291 290.559  1.00 65.04           C  
ANISOU 2913  CA  ILE A 228     5056   9013  10643  -1499   2139  -2661       C  
ATOM   2914  C   ILE A 228      97.095 175.963 291.411  1.00 62.24           C  
ANISOU 2914  C   ILE A 228     4726   8294  10628  -1259   2159  -2643       C  
ATOM   2915  O   ILE A 228      98.109 176.425 290.871  1.00 62.27           O  
ANISOU 2915  O   ILE A 228     4715   8257  10686  -1252   2266  -2675       O  
ATOM   2916  CB  ILE A 228      95.297 176.321 289.675  1.00 66.21           C  
ANISOU 2916  CB  ILE A 228     5100   9537  10521  -1561   2103  -2338       C  
ATOM   2917  CG1 ILE A 228      95.166 177.662 290.389  1.00 67.40           C  
ANISOU 2917  CG1 ILE A 228     5197   9568  10844  -1315   2025  -2022       C  
ATOM   2918  CG2 ILE A 228      93.921 175.811 289.288  1.00 65.96           C  
ANISOU 2918  CG2 ILE A 228     5036   9829  10197  -1735   2016  -2265       C  
ATOM   2919  CD1 ILE A 228      94.596 178.737 289.504  1.00 70.50           C  
ANISOU 2919  CD1 ILE A 228     5466  10294  11027  -1364   2002  -1687       C  
ATOM   2920  N   ILE A 229      96.892 176.014 292.729  1.00 62.20           N  
ANISOU 2920  N   ILE A 229     4755   8032  10845  -1073   2059  -2596       N  
ATOM   2921  CA  ILE A 229      97.949 176.428 293.645  1.00 65.08           C  
ANISOU 2921  CA  ILE A 229     5156   8030  11542   -869   2074  -2632       C  
ATOM   2922  C   ILE A 229      98.856 175.256 294.023  1.00 73.04           C  
ANISOU 2922  C   ILE A 229     6238   8763  12752   -902   2137  -2955       C  
ATOM   2923  O   ILE A 229     100.048 175.458 294.274  1.00 69.47           O  
ANISOU 2923  O   ILE A 229     5804   8058  12533   -808   2203  -3041       O  
ATOM   2924  CB  ILE A 229      97.370 177.098 294.911  1.00 67.14           C  
ANISOU 2924  CB  ILE A 229     5414   8148  11947   -661   1945  -2433       C  
ATOM   2925  CG1 ILE A 229      97.201 176.081 296.049  1.00 67.48           C  
ANISOU 2925  CG1 ILE A 229     5527   7973  12138   -625   1873  -2591       C  
ATOM   2926  CG2 ILE A 229      96.046 177.791 294.610  1.00 64.10           C  
ANISOU 2926  CG2 ILE A 229     4952   8061  11341   -674   1865  -2147       C  
ATOM   2927  CD1 ILE A 229      97.200 176.689 297.439  1.00 69.46           C  
ANISOU 2927  CD1 ILE A 229     5794   7983  12614   -407   1783  -2479       C  
ATOM   2928  N   LEU A 230      98.324 174.031 294.061  1.00 77.26           N  
ANISOU 2928  N   LEU A 230     5734  10435  13187   -138    915   2771       N  
ATOM   2929  CA  LEU A 230      99.148 172.887 294.438  1.00 58.44           C  
ANISOU 2929  CA  LEU A 230     3327   7874  11005   -197    851   2776       C  
ATOM   2930  C   LEU A 230     100.035 172.435 293.282  1.00 80.55           C  
ANISOU 2930  C   LEU A 230     6067  10683  13855   -167    832   2651       C  
ATOM   2931  O   LEU A 230     101.220 172.148 293.486  1.00 81.98           O  
ANISOU 2931  O   LEU A 230     6252  10722  14175   -141    784   2673       O  
ATOM   2932  CB  LEU A 230      98.270 171.737 294.934  1.00 59.50           C  
ANISOU 2932  CB  LEU A 230     3402   7998  11206   -323    848   2781       C  
ATOM   2933  CG  LEU A 230      97.474 172.037 296.208  1.00 59.48           C  
ANISOU 2933  CG  LEU A 230     3455   7971  11175   -361    871   2914       C  
ATOM   2934  CD1 LEU A 230      96.807 170.789 296.765  1.00 60.77           C  
ANISOU 2934  CD1 LEU A 230     3567   8089  11434   -518    875   2923       C  
ATOM   2935  CD2 LEU A 230      98.364 172.680 297.252  1.00 58.62           C  
ANISOU 2935  CD2 LEU A 230     3446   7676  11150   -288    834   3067       C  
ATOM   2936  N   ALA A 231      99.487 172.367 292.065  1.00 78.74           N  
ANISOU 2936  N   ALA A 231     5770  10633  13516   -164    868   2519       N  
ATOM   2937  CA  ALA A 231     100.335 172.146 290.898  1.00 77.02           C  
ANISOU 2937  CA  ALA A 231     5502  10440  13321   -113    863   2408       C  
ATOM   2938  C   ALA A 231     101.404 173.221 290.805  1.00 58.39           C  
ANISOU 2938  C   ALA A 231     3214   8039  10933    -25    873   2438       C  
ATOM   2939  O   ALA A 231     102.552 172.942 290.443  1.00 81.95           O  
ANISOU 2939  O   ALA A 231     6170  10960  14006      6    849   2398       O  
ATOM   2940  CB  ALA A 231      99.494 172.118 289.625  1.00 59.71           C  
ANISOU 2940  CB  ALA A 231     3230   8461  10996   -110    905   2272       C  
ATOM   2941  N   PHE A 232     101.044 174.458 291.146  1.00 57.67           N  
ANISOU 2941  N   PHE A 232     3202   7987  10724     11    915   2516       N  
ATOM   2942  CA  PHE A 232     102.033 175.525 291.197  1.00 57.11           C  
ANISOU 2942  CA  PHE A 232     3194   7863  10643     63    934   2569       C  
ATOM   2943  C   PHE A 232     103.070 175.252 292.280  1.00 57.09           C  
ANISOU 2943  C   PHE A 232     3212   7679  10799     35    869   2652       C  
ATOM   2944  O   PHE A 232     104.278 175.283 292.019  1.00 97.89           O  
ANISOU 2944  O   PHE A 232     8352  12808  16033     51    851   2614       O  
ATOM   2945  CB  PHE A 232     101.337 176.866 291.431  1.00 56.58           C  
ANISOU 2945  CB  PHE A 232     3202   7859  10435    108    999   2669       C  
ATOM   2946  CG  PHE A 232     102.210 178.056 291.166  1.00 56.29           C  
ANISOU 2946  CG  PHE A 232     3214   7802  10371    153   1048   2717       C  
ATOM   2947  CD1 PHE A 232     103.147 178.465 292.099  1.00 71.02           C  
ANISOU 2947  CD1 PHE A 232     5123   9529  12332    126   1021   2818       C  
ATOM   2948  CD2 PHE A 232     102.093 178.769 289.984  1.00 69.64           C  
ANISOU 2948  CD2 PHE A 232     4895   9618  11946    216   1127   2666       C  
ATOM   2949  CE1 PHE A 232     103.954 179.556 291.859  1.00 70.71           C  
ANISOU 2949  CE1 PHE A 232     5110   9482  12276    141   1075   2860       C  
ATOM   2950  CE2 PHE A 232     102.896 179.864 289.739  1.00 69.76           C  
ANISOU 2950  CE2 PHE A 232     4948   9610  11946    242   1190   2724       C  
ATOM   2951  CZ  PHE A 232     103.828 180.258 290.679  1.00 70.25           C  
ANISOU 2951  CZ  PHE A 232     5046   9540  12107    194   1167   2818       C  
ATOM   2952  N   ALA A 233     102.615 174.970 293.503  1.00 57.00           N  
ANISOU 2952  N   ALA A 233     3236   7569  10852     -3    833   2763       N  
ATOM   2953  CA  ALA A 233     103.548 174.773 294.609  1.00 72.09           C  
ANISOU 2953  CA  ALA A 233     5164   9309  12919    -18    766   2856       C  
ATOM   2954  C   ALA A 233     104.447 173.564 294.372  1.00 73.64           C  
ANISOU 2954  C   ALA A 233     5270   9437  13273    -20    704   2781       C  
ATOM   2955  O   ALA A 233     105.647 173.609 294.668  1.00 74.79           O  
ANISOU 2955  O   ALA A 233     5389   9515  13514      1    657   2789       O  
ATOM   2956  CB  ALA A 233     102.784 174.628 295.927  1.00 56.95           C  
ANISOU 2956  CB  ALA A 233     3296   7299  11045    -53    746   2996       C  
ATOM   2957  N   ALA A 234     103.891 172.481 293.825  1.00 58.50           N  
ANISOU 2957  N   ALA A 234     3289   7551  11389    -42    704   2707       N  
ATOM   2958  CA  ALA A 234     104.688 171.287 293.566  1.00 59.50           C  
ANISOU 2958  CA  ALA A 234     3321   7605  11682    -25    652   2654       C  
ATOM   2959  C   ALA A 234     105.731 171.501 292.477  1.00 73.54           C  
ANISOU 2959  C   ALA A 234     5045   9470  13425     43    664   2534       C  
ATOM   2960  O   ALA A 234     106.699 170.737 292.409  1.00 74.12           O  
ANISOU 2960  O   ALA A 234     5038   9489  13636     90    615   2502       O  
ATOM   2961  CB  ALA A 234     103.779 170.119 293.186  1.00 60.28           C  
ANISOU 2961  CB  ALA A 234     3357   7713  11833    -81    661   2614       C  
ATOM   2962  N   PHE A 235     105.562 172.518 291.630  1.00 72.83           N  
ANISOU 2962  N   PHE A 235     4989   9521  13163     57    731   2474       N  
ATOM   2963  CA  PHE A 235     106.518 172.788 290.561  1.00 71.95           C  
ANISOU 2963  CA  PHE A 235     4823   9502  13014    111    759   2365       C  
ATOM   2964  C   PHE A 235     107.570 173.814 290.951  1.00 69.13           C  
ANISOU 2964  C   PHE A 235     4485   9135  12647    114    761   2401       C  
ATOM   2965  O   PHE A 235     108.669 173.814 290.385  1.00 67.40           O  
ANISOU 2965  O   PHE A 235     4189   8971  12450    147    763   2321       O  
ATOM   2966  CB  PHE A 235     105.792 173.274 289.302  1.00 59.19           C  
ANISOU 2966  CB  PHE A 235     3212   8041  11235    125    837   2280       C  
ATOM   2967  CG  PHE A 235     105.138 172.176 288.518  1.00 59.82           C  
ANISOU 2967  CG  PHE A 235     3219   8174  11334    126    835   2194       C  
ATOM   2968  CD1 PHE A 235     105.138 170.877 288.992  1.00 60.58           C  
ANISOU 2968  CD1 PHE A 235     3259   8164  11595    104    777   2215       C  
ATOM   2969  CD2 PHE A 235     104.536 172.438 287.302  1.00 59.84           C  
ANISOU 2969  CD2 PHE A 235     3199   8329  11207    150    893   2101       C  
ATOM   2970  CE1 PHE A 235     104.541 169.864 288.274  1.00 61.39           C  
ANISOU 2970  CE1 PHE A 235     3281   8307  11736     87    780   2148       C  
ATOM   2971  CE2 PHE A 235     103.936 171.428 286.577  1.00 60.59           C  
ANISOU 2971  CE2 PHE A 235     3211   8485  11327    140    888   2022       C  
ATOM   2972  CZ  PHE A 235     103.941 170.139 287.062  1.00 61.39           C  
ANISOU 2972  CZ  PHE A 235     3254   8476  11596    100    834   2046       C  
ATOM   2973  N   TRP A 236     107.259 174.684 291.902  1.00 58.63           N  
ANISOU 2973  N   TRP A 236     3241   7747  11287     77    763   2519       N  
ATOM   2974  CA  TRP A 236     108.143 175.773 292.277  1.00 58.61           C  
ANISOU 2974  CA  TRP A 236     3253   7742  11276     58    775   2565       C  
ATOM   2975  C   TRP A 236     108.864 175.529 293.592  1.00 90.59           C  
ANISOU 2975  C   TRP A 236     7282  11671  15466     37    683   2647       C  
ATOM   2976  O   TRP A 236     109.732 176.323 293.968  1.00 95.32           O  
ANISOU 2976  O   TRP A 236     7862  12276  16079      7    677   2675       O  
ATOM   2977  CB  TRP A 236     107.347 177.074 292.350  1.00 57.76           C  
ANISOU 2977  CB  TRP A 236     3248   7659  11039     43    851   2655       C  
ATOM   2978  CG  TRP A 236     107.082 177.656 291.008  1.00 57.70           C  
ANISOU 2978  CG  TRP A 236     3239   7784  10902     74    947   2578       C  
ATOM   2979  CD1 TRP A 236     106.019 177.399 290.189  1.00 74.97           C  
ANISOU 2979  CD1 TRP A 236     5435  10059  12993    111    986   2524       C  
ATOM   2980  CD2 TRP A 236     107.906 178.596 290.316  1.00 82.02           C  
ANISOU 2980  CD2 TRP A 236     6294  10930  13941     66   1019   2550       C  
ATOM   2981  NE1 TRP A 236     106.130 178.131 289.029  1.00 77.17           N  
ANISOU 2981  NE1 TRP A 236     5703  10444  13173    145   1074   2470       N  
ATOM   2982  CE2 TRP A 236     107.282 178.873 289.085  1.00 80.44           C  
ANISOU 2982  CE2 TRP A 236     6101  10840  13623    115   1104   2491       C  
ATOM   2983  CE3 TRP A 236     109.114 179.236 290.621  1.00 82.97           C  
ANISOU 2983  CE3 TRP A 236     6373  11037  14114     13   1025   2567       C  
ATOM   2984  CZ2 TRP A 236     107.824 179.760 288.160  1.00 82.22           C  
ANISOU 2984  CZ2 TRP A 236     6308  11141  13791    120   1203   2466       C  
ATOM   2985  CZ3 TRP A 236     109.657 180.112 289.693  1.00 83.63           C  
ANISOU 2985  CZ3 TRP A 236     6429  11209  14138     -4   1127   2531       C  
ATOM   2986  CH2 TRP A 236     109.007 180.369 288.481  1.00 83.25           C  
ANISOU 2986  CH2 TRP A 236     6403  11249  13980     53   1220   2489       C  
ATOM   2987  N   LEU A 237     108.538 174.465 294.296  1.00 84.88           N  
ANISOU 2987  N   LEU A 237     6552  10843  14856     47    614   2691       N  
ATOM   2988  CA  LEU A 237     109.284 174.209 295.515  1.00 80.36           C  
ANISOU 2988  CA  LEU A 237     5948  10157  14428     44    520   2770       C  
ATOM   2989  C   LEU A 237     110.673 173.660 295.190  1.00 77.61           C  
ANISOU 2989  C   LEU A 237     5460   9863  14165     95    464   2664       C  
ATOM   2990  O   LEU A 237     111.656 174.140 295.771  1.00 61.70           O  
ANISOU 2990  O   LEU A 237     3391   7861  12191     82    415   2678       O  
ATOM   2991  CB  LEU A 237     108.507 173.268 296.437  1.00 59.72           C  
ANISOU 2991  CB  LEU A 237     3365   7397  11930     41    468   2871       C  
ATOM   2992  CG  LEU A 237     109.099 173.158 297.835  1.00 60.21           C  
ANISOU 2992  CG  LEU A 237     3413   7325  12139     41    369   2986       C  
ATOM   2993  CD1 LEU A 237     109.143 174.532 298.474  1.00 59.55           C  
ANISOU 2993  CD1 LEU A 237     3402   7243  11980     -8    387   3080       C  
ATOM   2994  CD2 LEU A 237     108.283 172.195 298.664  1.00 60.33           C  
ANISOU 2994  CD2 LEU A 237     3453   7187  12282     34    333   3095       C  
ATOM   2995  N   PRO A 238     110.814 172.667 294.284  1.00 74.94           N  
ANISOU 2995  N   PRO A 238     5045   9574  13856    159    467   2555       N  
ATOM   2996  CA  PRO A 238     112.169 172.201 293.932  1.00 73.28           C  
ANISOU 2996  CA  PRO A 238     4688   9447  13707    236    420   2448       C  
ATOM   2997  C   PRO A 238     113.140 173.321 293.620  1.00 63.60           C  
ANISOU 2997  C   PRO A 238     3406   8364  12394    198    455   2387       C  
ATOM   2998  O   PRO A 238     114.288 173.293 294.081  1.00 64.85           O  
ANISOU 2998  O   PRO A 238     3449   8575  12616    224    385   2356       O  
ATOM   2999  CB  PRO A 238     111.933 171.323 292.697  1.00 71.79           C  
ANISOU 2999  CB  PRO A 238     4453   9317  13507    302    461   2343       C  
ATOM   3000  CG  PRO A 238     110.495 170.978 292.695  1.00 62.65           C  
ANISOU 3000  CG  PRO A 238     3394   8071  12341    255    494   2407       C  
ATOM   3001  CD  PRO A 238     109.789 171.737 293.769  1.00 74.34           C  
ANISOU 3001  CD  PRO A 238     4990   9463  13794    172    492   2540       C  
ATOM   3002  N   TYR A 239     112.707 174.316 292.848  1.00 62.74           N  
ANISOU 3002  N   TYR A 239     3364   8329  12147    137    561   2370       N  
ATOM   3003  CA  TYR A 239     113.616 175.399 292.496  1.00 79.66           C  
ANISOU 3003  CA  TYR A 239     5445  10598  14226     82    613   2321       C  
ATOM   3004  C   TYR A 239     113.994 176.218 293.722  1.00 79.58           C  
ANISOU 3004  C   TYR A 239     5447  10533  14256      1    566   2424       C  
ATOM   3005  O   TYR A 239     115.170 176.541 293.923  1.00 82.73           O  
ANISOU 3005  O   TYR A 239     5717  11028  14687    -32    536   2374       O  
ATOM   3006  CB  TYR A 239     112.996 176.291 291.421  1.00 78.58           C  
ANISOU 3006  CB  TYR A 239     5384  10527  13947     45    742   2302       C  
ATOM   3007  CG  TYR A 239     113.730 177.601 291.257  1.00 63.04           C  
ANISOU 3007  CG  TYR A 239     3381   8644  11926    -45    813   2300       C  
ATOM   3008  CD1 TYR A 239     115.087 177.624 290.965  1.00 64.68           C  
ANISOU 3008  CD1 TYR A 239     3422   8987  12165    -65    810   2196       C  
ATOM   3009  CD2 TYR A 239     113.072 178.814 291.403  1.00 76.64           C  
ANISOU 3009  CD2 TYR A 239     5226  10323  13572   -112    890   2406       C  
ATOM   3010  CE1 TYR A 239     115.772 178.818 290.823  1.00 65.46           C  
ANISOU 3010  CE1 TYR A 239     3474   9173  12224   -181    888   2193       C  
ATOM   3011  CE2 TYR A 239     113.750 180.017 291.258  1.00 77.72           C  
ANISOU 3011  CE2 TYR A 239     5332  10525  13674   -212    969   2418       C  
ATOM   3012  CZ  TYR A 239     115.101 180.009 290.966  1.00 64.56           C  
ANISOU 3012  CZ  TYR A 239     3496   8988  12044   -263    970   2308       C  
ATOM   3013  OH  TYR A 239     115.789 181.192 290.825  1.00 65.57           O  
ANISOU 3013  OH  TYR A 239     3583   9190  12140   -398   1061   2313       O  
ATOM   3014  N   HIS A 240     113.018 176.546 294.566  1.00 77.69           N  
ANISOU 3014  N   HIS A 240     5347  10155  14017    -31    557   2565       N  
ATOM   3015  CA  HIS A 240     113.281 177.519 295.620  1.00 76.98           C  
ANISOU 3015  CA  HIS A 240     5285  10014  13950   -115    531   2677       C  
ATOM   3016  C   HIS A 240     114.102 176.949 296.762  1.00 79.78           C  
ANISOU 3016  C   HIS A 240     5543  10323  14445   -100    392   2701       C  
ATOM   3017  O   HIS A 240     114.847 177.695 297.406  1.00 81.93           O  
ANISOU 3017  O   HIS A 240     5759  10625  14744   -178    355   2732       O  
ATOM   3018  CB  HIS A 240     111.972 178.085 296.147  1.00 73.51           C  
ANISOU 3018  CB  HIS A 240     5018   9455  13459   -133    570   2828       C  
ATOM   3019  CG  HIS A 240     111.428 179.181 295.296  1.00 60.08           C  
ANISOU 3019  CG  HIS A 240     3394   7817  11616   -161    702   2837       C  
ATOM   3020  ND1 HIS A 240     111.506 180.508 295.655  1.00 60.07           N  
ANISOU 3020  ND1 HIS A 240     3445   7806  11573   -236    756   2935       N  
ATOM   3021  CD2 HIS A 240     110.841 179.152 294.078  1.00 81.20           C  
ANISOU 3021  CD2 HIS A 240     6096  10570  14187   -118    791   2762       C  
ATOM   3022  CE1 HIS A 240     110.963 181.248 294.705  1.00 85.85           C  
ANISOU 3022  CE1 HIS A 240     6771  11132  14717   -226    880   2931       C  
ATOM   3023  NE2 HIS A 240     110.553 180.449 293.737  1.00 82.99           N  
ANISOU 3023  NE2 HIS A 240     6391  10828  14313   -152    898   2824       N  
ATOM   3024  N   VAL A 241     113.977 175.653 297.041  1.00 63.53           N  
ANISOU 3024  N   VAL A 241     3460   8196  12483     -5    311   2691       N  
ATOM   3025  CA  VAL A 241     114.802 175.058 298.086  1.00 64.81           C  
ANISOU 3025  CA  VAL A 241     3519   8323  12781     41    169   2709       C  
ATOM   3026  C   VAL A 241     116.277 175.236 297.756  1.00 66.65           C  
ANISOU 3026  C   VAL A 241     3557   8755  13011     47    134   2571       C  
ATOM   3027  O   VAL A 241     117.101 175.487 298.643  1.00 67.82           O  
ANISOU 3027  O   VAL A 241     3609   8938  13220     25     34   2586       O  
ATOM   3028  CB  VAL A 241     114.423 173.581 298.289  1.00 65.02           C  
ANISOU 3028  CB  VAL A 241     3547   8239  12918    160    101   2719       C  
ATOM   3029  CG1 VAL A 241     115.600 172.795 298.832  1.00 66.96           C  
ANISOU 3029  CG1 VAL A 241     3637   8527  13277    275    -42   2661       C  
ATOM   3030  CG2 VAL A 241     113.239 173.485 299.235  1.00 63.82           C  
ANISOU 3030  CG2 VAL A 241     3542   7885  12820    127     90   2891       C  
ATOM   3031  N   VAL A 242     116.629 175.150 296.472  1.00 67.09           N  
ANISOU 3031  N   VAL A 242     3539   8963  12989     72    217   2432       N  
ATOM   3032  CA  VAL A 242     118.013 175.391 296.073  1.00 84.79           C  
ANISOU 3032  CA  VAL A 242     5577  11428  15213     65    207   2293       C  
ATOM   3033  C   VAL A 242     118.396 176.842 296.344  1.00 91.21           C  
ANISOU 3033  C   VAL A 242     6375  12303  15977   -113    254   2325       C  
ATOM   3034  O   VAL A 242     119.455 177.122 296.919  1.00 97.29           O  
ANISOU 3034  O   VAL A 242     6985  13193  16787   -160    178   2283       O  
ATOM   3035  CB  VAL A 242     118.227 175.013 294.597  1.00 79.85           C  
ANISOU 3035  CB  VAL A 242     4882  10943  14514    127    300   2150       C  
ATOM   3036  CG1 VAL A 242     119.622 175.415 294.161  1.00 79.42           C  
ANISOU 3036  CG1 VAL A 242     4605  11141  14429     96    313   2009       C  
ATOM   3037  CG2 VAL A 242     118.021 173.522 294.403  1.00 69.71           C  
ANISOU 3037  CG2 VAL A 242     3585   9604  13296    305    238   2117       C  
ATOM   3038  N   ASP A 243     117.541 177.787 295.937  1.00 67.74           N  
ANISOU 3038  N   ASP A 243     3561   9261  12918   -211    378   2399       N  
ATOM   3039  CA  ASP A 243     117.759 179.184 296.308  1.00 67.96           C  
ANISOU 3039  CA  ASP A 243     3608   9303  12909   -382    427   2464       C  
ATOM   3040  C   ASP A 243     117.857 179.336 297.816  1.00 79.29           C  
ANISOU 3040  C   ASP A 243     5054  10633  14438   -423    298   2584       C  
ATOM   3041  O   ASP A 243     118.653 180.134 298.323  1.00 78.72           O  
ANISOU 3041  O   ASP A 243     4890  10639  14381   -559    271   2585       O  
ATOM   3042  CB  ASP A 243     116.631 180.065 295.778  1.00 66.25           C  
ANISOU 3042  CB  ASP A 243     3589   8994  12589   -430    566   2555       C  
ATOM   3043  CG  ASP A 243     116.737 180.314 294.302  1.00 92.07           C  
ANISOU 3043  CG  ASP A 243     6830  12391  15760   -435    702   2443       C  
ATOM   3044  OD1 ASP A 243     117.757 179.907 293.704  1.00 93.45           O  
ANISOU 3044  OD1 ASP A 243     6826  12733  15946   -424    699   2296       O  
ATOM   3045  OD2 ASP A 243     115.805 180.928 293.744  1.00 90.65           O  
ANISOU 3045  OD2 ASP A 243     6798  12154  15490   -440    812   2505       O  
ATOM   3046  N   LEU A 244     117.042 178.579 298.548  1.00 79.82           N  
ANISOU 3046  N   LEU A 244     5231  10524  14572   -321    220   2689       N  
ATOM   3047  CA  LEU A 244     117.100 178.619 299.999  1.00 67.26           C  
ANISOU 3047  CA  LEU A 244     3652   8820  13084   -341     89   2813       C  
ATOM   3048  C   LEU A 244     118.360 177.939 300.523  1.00 85.85           C  
ANISOU 3048  C   LEU A 244     5793  11294  15531   -283    -66   2715       C  
ATOM   3049  O   LEU A 244     118.903 178.360 301.550  1.00 87.68           O  
ANISOU 3049  O   LEU A 244     5960  11530  15824   -353   -176   2767       O  
ATOM   3050  CB  LEU A 244     115.854 177.955 300.584  1.00 65.64           C  
ANISOU 3050  CB  LEU A 244     3615   8398  12926   -252     63   2951       C  
ATOM   3051  CG  LEU A 244     115.297 178.536 301.882  1.00 64.98           C  
ANISOU 3051  CG  LEU A 244     3645   8149  12894   -312     10   3147       C  
ATOM   3052  CD1 LEU A 244     114.644 179.884 301.622  1.00 63.93           C  
ANISOU 3052  CD1 LEU A 244     3646   7999  12645   -418    144   3235       C  
ATOM   3053  CD2 LEU A 244     114.318 177.562 302.531  1.00 69.92           C  
ANISOU 3053  CD2 LEU A 244     4375   8591  13599   -211    -37   3256       C  
ATOM   3054  N   VAL A 245     118.846 176.900 299.836  1.00 85.95           N  
ANISOU 3054  N   VAL A 245     5687  11419  15550   -145    -86   2572       N  
ATOM   3055  CA  VAL A 245     119.997 176.173 300.360  1.00 72.52           C  
ANISOU 3055  CA  VAL A 245     3781   9849  13924    -37   -244   2477       C  
ATOM   3056  C   VAL A 245     121.304 176.819 299.912  1.00 84.50           C  
ANISOU 3056  C   VAL A 245     5066  11653  15386   -130   -228   2322       C  
ATOM   3057  O   VAL A 245     122.320 176.706 300.604  1.00 82.50           O  
ANISOU 3057  O   VAL A 245     4625  11542  15178   -105   -368   2260       O  
ATOM   3058  CB  VAL A 245     119.940 174.687 299.958  1.00 72.83           C  
ANISOU 3058  CB  VAL A 245     3797   9874  14002    185   -288   2406       C  
ATOM   3059  CG1 VAL A 245     120.795 174.417 298.727  1.00 86.87           C  
ANISOU 3059  CG1 VAL A 245     5398  11900  15707    247   -226   2215       C  
ATOM   3060  CG2 VAL A 245     120.391 173.820 301.115  1.00 74.21           C  
ANISOU 3060  CG2 VAL A 245     3908  10002  14285    344   -487   2430       C  
ATOM   3061  N   GLU A 246     121.309 177.505 298.767  1.00 77.16           N  
ANISOU 3061  N   GLU A 246     4136  10825  14357   -241    -62   2254       N  
ATOM   3062  CA  GLU A 246     122.531 178.160 298.318  1.00 76.63           C  
ANISOU 3062  CA  GLU A 246     3841  11033  14241   -363    -25   2106       C  
ATOM   3063  C   GLU A 246     122.872 179.342 299.217  1.00 77.37           C  
ANISOU 3063  C   GLU A 246     3913  11135  14350   -586    -57   2175       C  
ATOM   3064  O   GLU A 246     123.997 179.449 299.713  1.00 80.66           O  
ANISOU 3064  O   GLU A 246     4100  11752  14794   -639   -160   2081       O  
ATOM   3065  CB  GLU A 246     122.393 178.590 296.857  1.00 92.59           C  
ANISOU 3065  CB  GLU A 246     5886  13136  16157   -427    169   2028       C  
ATOM   3066  CG  GLU A 246     123.371 177.877 295.929  1.00 97.43           C  
ANISOU 3066  CG  GLU A 246     6266  14008  16745   -314    181   1830       C  
ATOM   3067  CD  GLU A 246     122.996 177.974 294.460  1.00100.62           C  
ANISOU 3067  CD  GLU A 246     6734  14437  17061   -314    354   1775       C  
ATOM   3068  OE1 GLU A 246     122.902 179.102 293.938  1.00101.20           O  
ANISOU 3068  OE1 GLU A 246     6857  14527  17066   -502    496   1787       O  
ATOM   3069  OE2 GLU A 246     122.797 176.917 293.823  1.00103.05           O  
ANISOU 3069  OE2 GLU A 246     7044  14744  17368   -124    346   1722       O  
ATOM   3070  N   GLY A 247     121.900 180.219 299.471  1.00 75.47           N  
ANISOU 3070  N   GLY A 247     3903  10685  14088   -712     20   2340       N  
ATOM   3071  CA  GLY A 247     122.149 181.344 300.358  1.00 90.22           C  
ANISOU 3071  CA  GLY A 247     5778  12531  15969   -931    -12   2425       C  
ATOM   3072  C   GLY A 247     122.516 180.917 301.768  1.00 92.28           C  
ANISOU 3072  C   GLY A 247     5962  12760  16341   -879   -233   2478       C  
ATOM   3073  O   GLY A 247     123.341 181.556 302.427  1.00 95.30           O  
ANISOU 3073  O   GLY A 247     6209  13258  16741  -1046   -315   2453       O  
ATOM   3074  N   SER A 248     121.914 179.827 302.249  1.00 75.96           N  
ANISOU 3074  N   SER A 248     3980  10536  14347   -658   -335   2549       N  
ATOM   3075  CA  SER A 248     122.248 179.325 303.578  1.00 76.95           C  
ANISOU 3075  CA  SER A 248     4040  10619  14580   -575   -556   2602       C  
ATOM   3076  C   SER A 248     123.667 178.770 303.613  1.00 79.95           C  
ANISOU 3076  C   SER A 248     4114  11295  14969   -489   -688   2404       C  
ATOM   3077  O   SER A 248     124.437 179.061 304.537  1.00 81.88           O  
ANISOU 3077  O   SER A 248     4215  11645  15252   -554   -847   2387       O  
ATOM   3078  CB  SER A 248     121.243 178.252 304.000  1.00 98.61           C  
ANISOU 3078  CB  SER A 248     6958  13116  17394   -363   -612   2719       C  
ATOM   3079  OG  SER A 248     121.336 177.106 303.170  1.00 98.92           O  
ANISOU 3079  OG  SER A 248     6944  13223  17417   -167   -586   2595       O  
ATOM   3080  N   ARG A 249     124.032 177.977 302.606  1.00 95.94           N  
ANISOU 3080  N   ARG A 249     6028  13474  16951   -336   -631   2250       N  
ATOM   3081  CA  ARG A 249     125.321 177.301 302.544  1.00 97.96           C  
ANISOU 3081  CA  ARG A 249     5988  14032  17200   -193   -748   2055       C  
ATOM   3082  C   ARG A 249     126.377 178.103 301.781  1.00 99.09           C  
ANISOU 3082  C   ARG A 249     5885  14500  17265   -383   -650   1878       C  
ATOM   3083  O   ARG A 249     127.412 177.542 301.401  1.00 88.16           O  
ANISOU 3083  O   ARG A 249     4234  13409  15854   -258   -698   1689       O  
ATOM   3084  CB  ARG A 249     125.152 175.913 301.919  1.00 83.24           C  
ANISOU 3084  CB  ARG A 249     4138  12156  15335    100   -750   1990       C  
ATOM   3085  CG  ARG A 249     124.056 175.070 302.571  1.00 81.25           C  
ANISOU 3085  CG  ARG A 249     4137  11574  15162    262   -820   2155       C  
ATOM   3086  CD  ARG A 249     124.627 173.881 303.319  1.00 83.15           C  
ANISOU 3086  CD  ARG A 249     4286  11857  15451    553  -1034   2106       C  
ATOM   3087  NE  ARG A 249     124.170 172.615 302.756  1.00 82.59           N  
ANISOU 3087  NE  ARG A 249     4312  11678  15389    790  -1009   2091       N  
ATOM   3088  CZ  ARG A 249     124.663 172.073 301.648  1.00 83.62           C  
ANISOU 3088  CZ  ARG A 249     4315  12000  15457    911   -939   1939       C  
ATOM   3089  NH1 ARG A 249     125.625 172.690 300.978  1.00 85.26           N  
ANISOU 3089  NH1 ARG A 249     4285  12523  15588    815   -878   1784       N  
ATOM   3090  NH2 ARG A 249     124.191 170.918 301.205  1.00 83.17           N  
ANISOU 3090  NH2 ARG A 249     4366  11815  15419   1119   -928   1943       N  
ATOM   3091  N   VAL A 250     126.132 179.392 301.541  1.00 98.89           N  
ANISOU 3091  N   VAL A 250     5944  14429  17199   -678   -507   1934       N  
ATOM   3092  CA  VAL A 250     127.119 180.305 300.975  1.00102.41           C  
ANISOU 3092  CA  VAL A 250     6175  15154  17581   -920   -408   1781       C  
ATOM   3093  C   VAL A 250     127.688 181.232 302.042  1.00105.83           C  
ANISOU 3093  C   VAL A 250     6516  15651  18042  -1166   -514   1803       C  
ATOM   3094  O   VAL A 250     128.430 182.170 301.724  1.00109.93           O  
ANISOU 3094  O   VAL A 250     6888  16366  18515  -1441   -423   1693       O  
ATOM   3095  CB  VAL A 250     126.535 181.109 299.799  1.00 85.77           C  
ANISOU 3095  CB  VAL A 250     4231  12967  15391  -1086   -154   1805       C  
ATOM   3096  CG1 VAL A 250     125.662 182.232 300.306  1.00 83.99           C  
ANISOU 3096  CG1 VAL A 250     4273  12482  15157  -1301    -91   2002       C  
ATOM   3097  CG2 VAL A 250     127.636 181.626 298.873  1.00 88.44           C  
ANISOU 3097  CG2 VAL A 250     4314  13624  15665  -1259    -27   1598       C  
ATOM   3098  N   LEU A 251     127.353 180.995 303.308  1.00103.91           N  
ANISOU 3098  N   LEU A 251     6364  15242  17876  -1090   -705   1940       N  
ATOM   3099  CA  LEU A 251     128.010 181.663 304.419  1.00 90.62           C  
ANISOU 3099  CA  LEU A 251     4561  13648  16224  -1282   -863   1943       C  
ATOM   3100  C   LEU A 251     128.971 180.758 305.171  1.00 93.26           C  
ANISOU 3100  C   LEU A 251     4624  14213  16598  -1065  -1116   1816       C  
ATOM   3101  O   LEU A 251     129.954 181.250 305.727  1.00100.71           O  
ANISOU 3101  O   LEU A 251     5334  15396  17535  -1227  -1233   1707       O  
ATOM   3102  CB  LEU A 251     126.964 182.234 305.381  1.00 88.36           C  
ANISOU 3102  CB  LEU A 251     4578  13009  15987  -1382   -909   2200       C  
ATOM   3103  CG  LEU A 251     126.147 183.298 304.648  1.00 86.38           C  
ANISOU 3103  CG  LEU A 251     4575  12581  15665  -1606   -659   2305       C  
ATOM   3104  CD1 LEU A 251     124.974 183.771 305.478  1.00 83.96           C  
ANISOU 3104  CD1 LEU A 251     4584  11923  15394  -1652   -680   2565       C  
ATOM   3105  CD2 LEU A 251     127.047 184.460 304.271  1.00 88.89           C  
ANISOU 3105  CD2 LEU A 251     4753  13115  15905  -1960   -552   2177       C  
ATOM   3106  N   ALA A 252     128.725 179.452 305.181  1.00 92.53           N  
ANISOU 3106  N   ALA A 252     4559  14063  16534   -702  -1202   1817       N  
ATOM   3107  CA  ALA A 252     129.722 178.459 305.564  1.00 95.36           C  
ANISOU 3107  CA  ALA A 252     4649  14692  16891   -426  -1407   1654       C  
ATOM   3108  C   ALA A 252     129.937 177.527 304.379  1.00109.63           C  
ANISOU 3108  C   ALA A 252     6362  16644  18648   -189  -1299   1510       C  
ATOM   3109  O   ALA A 252     128.996 176.861 303.932  1.00108.12           O  
ANISOU 3109  O   ALA A 252     6407  16202  18470    -27  -1217   1612       O  
ATOM   3110  CB  ALA A 252     129.286 177.675 306.802  1.00 94.72           C  
ANISOU 3110  CB  ALA A 252     4717  14393  16880   -173  -1641   1791       C  
ATOM   3111  N   GLY A 253     131.164 177.496 303.863  1.00111.09           N  
ANISOU 3111  N   GLY A 253     6197  17235  18778   -183  -1300   1268       N  
ATOM   3112  CA  GLY A 253     131.500 176.677 302.709  1.00110.48           C  
ANISOU 3112  CA  GLY A 253     5997  17330  18652     33  -1203   1114       C  
ATOM   3113  C   GLY A 253     130.618 176.886 301.488  1.00106.80           C  
ANISOU 3113  C   GLY A 253     5752  16668  18161    -66   -945   1186       C  
ATOM   3114  O   GLY A 253     131.019 176.606 300.356  1.00 97.54           O  
ANISOU 3114  O   GLY A 253     4445  15676  16938     -5   -823   1039       O  
ATOM   3115  N   ASP A 256     132.358 174.678 294.962  1.00100.73           N  
ANISOU 3115  N   ASP A 256     4387  16712  17175    473   -300    441       N  
ATOM   3116  CA  ASP A 256     133.465 173.759 295.203  1.00112.91           C  
ANISOU 3116  CA  ASP A 256     5614  18531  18754    777   -468    237       C  
ATOM   3117  C   ASP A 256     133.333 172.496 294.354  1.00112.63           C  
ANISOU 3117  C   ASP A 256     5624  18473  18697   1131   -465    192       C  
ATOM   3118  O   ASP A 256     133.054 172.562 293.156  1.00110.11           O  
ANISOU 3118  O   ASP A 256     5366  18121  18348   1077   -286    177       O  
ATOM   3119  CB  ASP A 256     133.539 173.400 296.680  1.00104.79           C  
ANISOU 3119  CB  ASP A 256     4593  17473  17750    921   -713    305       C  
ATOM   3120  N   GLN A 257     133.553 171.342 294.984  1.00117.49           N  
ANISOU 3120  N   GLN A 257     6214  19100  19326   1505   -669    169       N  
ATOM   3121  CA  GLN A 257     133.329 170.048 294.355  1.00118.23           C  
ANISOU 3121  CA  GLN A 257     6405  19115  19402   1868   -692    156       C  
ATOM   3122  C   GLN A 257     132.128 169.309 294.921  1.00115.40           C  
ANISOU 3122  C   GLN A 257     6427  18399  19022   2018   -760    404       C  
ATOM   3123  O   GLN A 257     131.467 168.575 294.183  1.00112.72           O  
ANISOU 3123  O   GLN A 257     6279  17880  18669   2160   -690    467       O  
ATOM   3124  CB  GLN A 257     134.573 169.160 294.494  1.00123.76           C  
ANISOU 3124  CB  GLN A 257     6884  19981  20157   2202   -858    -55       C  
ATOM   3125  N   SER A 258     131.833 169.492 296.213  1.00116.28           N  
ANISOU 3125  N   SER A 258     6645  18381  19157   1976   -893    536       N  
ATOM   3126  CA  SER A 258     130.623 168.919 296.798  1.00114.07           C  
ANISOU 3126  CA  SER A 258     6730  17699  18912   2055   -938    767       C  
ATOM   3127  C   SER A 258     129.382 169.683 296.351  1.00110.13           C  
ANISOU 3127  C   SER A 258     6499  16903  18442   1721   -748    935       C  
ATOM   3128  O   SER A 258     128.325 169.083 296.118  1.00106.08           O  
ANISOU 3128  O   SER A 258     6257  16085  17962   1783   -704   1065       O  
ATOM   3129  CB  SER A 258     130.734 168.912 298.324  1.00 99.46           C  
ANISOU 3129  CB  SER A 258     4903  15794  17094   2117  -1143    843       C  
ATOM   3130  OG  SER A 258     131.104 170.189 298.820  1.00 99.76           O  
ANISOU 3130  OG  SER A 258     4796  15966  17142   1792  -1133    827       O  
ATOM   3131  N   LYS A 259     129.491 171.004 296.225  1.00111.35           N  
ANISOU 3131  N   LYS A 259     6582  17143  18584   1373   -637    926       N  
ATOM   3132  CA  LYS A 259     128.397 171.840 295.753  1.00108.47           C  
ANISOU 3132  CA  LYS A 259     6462  16530  18222   1080   -458   1064       C  
ATOM   3133  C   LYS A 259     128.326 171.931 294.230  1.00110.96           C  
ANISOU 3133  C   LYS A 259     6763  16919  18476   1035   -268    983       C  
ATOM   3134  O   LYS A 259     127.494 172.682 293.709  1.00110.72           O  
ANISOU 3134  O   LYS A 259     6920  16723  18426    811   -116   1074       O  
ATOM   3135  CB  LYS A 259     128.513 173.247 296.355  1.00106.98           C  
ANISOU 3135  CB  LYS A 259     6241  16367  18038    746   -428   1106       C  
ATOM   3136  N   GLN A 260     129.166 171.187 293.501  1.00112.80           N  
ANISOU 3136  N   GLN A 260     6785  17395  18677   1260   -278    813       N  
ATOM   3137  CA  GLN A 260     129.092 171.179 292.044  1.00 93.00           C  
ANISOU 3137  CA  GLN A 260     4270  14945  16120   1244   -107    739       C  
ATOM   3138  C   GLN A 260     127.831 170.508 291.523  1.00 90.25           C  
ANISOU 3138  C   GLN A 260     4226  14284  15780   1328    -53    874       C  
ATOM   3139  O   GLN A 260     127.555 170.595 290.322  1.00 89.55           O  
ANISOU 3139  O   GLN A 260     4180  14198  15648   1286     93    843       O  
ATOM   3140  CB  GLN A 260     130.320 170.484 291.451  1.00103.95           C  
ANISOU 3140  CB  GLN A 260     5346  16659  17490   1492   -144    516       C  
ATOM   3141  N   GLN A 261     127.070 169.838 292.392  1.00 88.88           N  
ANISOU 3141  N   GLN A 261     4254  13846  15669   1440   -166   1015       N  
ATOM   3142  CA  GLN A 261     125.819 169.209 291.985  1.00102.69           C  
ANISOU 3142  CA  GLN A 261     6278  15292  17449   1485   -115   1136       C  
ATOM   3143  C   GLN A 261     124.661 170.199 291.950  1.00100.00           C  
ANISOU 3143  C   GLN A 261     6165  14728  17102   1187      3   1275       C  
ATOM   3144  O   GLN A 261     123.719 170.012 291.169  1.00 99.78           O  
ANISOU 3144  O   GLN A 261     6307  14542  17063   1161    101   1326       O  
ATOM   3145  CB  GLN A 261     125.490 168.040 292.925  1.00101.96           C  
ANISOU 3145  CB  GLN A 261     6299  15000  17440   1726   -277   1222       C  
ATOM   3146  CG  GLN A 261     124.010 167.609 292.983  1.00 98.32           C  
ANISOU 3146  CG  GLN A 261     6137  14169  17050   1679   -241   1388       C  
ATOM   3147  CD  GLN A 261     123.518 166.904 291.724  1.00 83.46           C  
ANISOU 3147  CD  GLN A 261     4325  12229  15158   1773   -141   1360       C  
ATOM   3148  OE1 GLN A 261     123.944 167.211 290.612  1.00 93.79           O  
ANISOU 3148  OE1 GLN A 261     5520  13729  16387   1749    -35   1250       O  
ATOM   3149  NE2 GLN A 261     122.610 165.952 291.901  1.00 82.60           N  
ANISOU 3149  NE2 GLN A 261     4398  11848  15139   1875   -175   1461       N  
ATOM   3150  N   LEU A 262     124.716 171.256 292.766  1.00 97.62           N  
ANISOU 3150  N   LEU A 262     5866  14422  16805    975     -9   1331       N  
ATOM   3151  CA  LEU A 262     123.583 172.168 292.885  1.00 80.08           C  
ANISOU 3151  CA  LEU A 262     3880  11974  14574    738     84   1474       C  
ATOM   3152  C   LEU A 262     123.162 172.716 291.528  1.00 92.57           C  
ANISOU 3152  C   LEU A 262     5526  13577  16068    626    264   1441       C  
ATOM   3153  O   LEU A 262     122.014 172.545 291.111  1.00 90.76           O  
ANISOU 3153  O   LEU A 262     5505  13150  15829    615    325   1524       O  
ATOM   3154  CB  LEU A 262     123.909 173.308 293.849  1.00 80.27           C  
ANISOU 3154  CB  LEU A 262     3864  12030  14605    536     53   1520       C  
ATOM   3155  CG  LEU A 262     123.295 173.089 295.231  1.00 90.39           C  
ANISOU 3155  CG  LEU A 262     5292  13076  15975    553    -76   1673       C  
ATOM   3156  CD1 LEU A 262     124.234 172.259 296.098  1.00 93.09           C  
ANISOU 3156  CD1 LEU A 262     5457  13536  16376    760   -264   1612       C  
ATOM   3157  CD2 LEU A 262     122.942 174.406 295.893  1.00 78.02           C  
ANISOU 3157  CD2 LEU A 262     3822  11420  14403    304    -41   1783       C  
ATOM   3158  N   ARG A 263     124.085 173.365 290.814  1.00 80.63           N  
ANISOU 3158  N   ARG A 263     3826  12318  14493    545    350   1314       N  
ATOM   3159  CA  ARG A 263     123.736 173.875 289.493  1.00 79.84           C  
ANISOU 3159  CA  ARG A 263     3785  12239  14311    457    520   1283       C  
ATOM   3160  C   ARG A 263     123.308 172.753 288.554  1.00 79.50           C  
ANISOU 3160  C   ARG A 263     3794  12148  14264    656    537   1250       C  
ATOM   3161  O   ARG A 263     122.448 172.966 287.695  1.00111.56           O  
ANISOU 3161  O   ARG A 263     8008  16105  18273    606    644   1287       O  
ATOM   3162  CB  ARG A 263     124.899 174.659 288.890  1.00101.97           C  
ANISOU 3162  CB  ARG A 263     6352  15329  17063    340    614   1144       C  
ATOM   3163  CG  ARG A 263     124.515 175.448 287.640  1.00101.14           C  
ANISOU 3163  CG  ARG A 263     6330  15224  16875    209    803   1137       C  
ATOM   3164  CD  ARG A 263     123.919 176.814 287.979  1.00 79.77           C  
ANISOU 3164  CD  ARG A 263     3789  12384  14135    -39    886   1255       C  
ATOM   3165  NE  ARG A 263     122.657 177.074 287.288  1.00 77.35           N  
ANISOU 3165  NE  ARG A 263     3735  11881  13772    -50    981   1352       N  
ATOM   3166  CZ  ARG A 263     122.549 177.369 285.994  1.00 84.13           C  
ANISOU 3166  CZ  ARG A 263     4607  12797  14561    -65   1124   1306       C  
ATOM   3167  NH1 ARG A 263     123.629 177.429 285.228  1.00 86.43           N  
ANISOU 3167  NH1 ARG A 263     4678  13327  14833    -80   1201   1167       N  
ATOM   3168  NH2 ARG A 263     121.355 177.594 285.462  1.00 81.81           N  
ANISOU 3168  NH2 ARG A 263     4535  12332  14216    -58   1191   1394       N  
ATOM   3169  N   ASN A 264     123.877 171.553 288.700  1.00 81.15           N  
ANISOU 3169  N   ASN A 264     3878  12432  14524    895    428   1183       N  
ATOM   3170  CA  ASN A 264     123.376 170.422 287.921  1.00 80.85           C  
ANISOU 3170  CA  ASN A 264     3914  12307  14499   1088    435   1173       C  
ATOM   3171  C   ASN A 264     122.009 169.976 288.423  1.00 82.02           C  
ANISOU 3171  C   ASN A 264     4315  12143  14704   1078    397   1326       C  
ATOM   3172  O   ASN A 264     121.162 169.535 287.636  1.00 77.38           O  
ANISOU 3172  O   ASN A 264     3850  11442  14110   1109    458   1349       O  
ATOM   3173  CB  ASN A 264     124.371 169.261 287.958  1.00 83.53           C  
ANISOU 3173  CB  ASN A 264     4061  12802  14874   1375    329   1064       C  
ATOM   3174  N   ALA A 265     121.773 170.087 289.732  1.00 77.89           N  
ANISOU 3174  N   ALA A 265     3860  11490  14245   1028    299   1427       N  
ATOM   3175  CA  ALA A 265     120.457 169.791 290.283  1.00 86.11           C  
ANISOU 3175  CA  ALA A 265     5128  12244  15346    984    276   1575       C  
ATOM   3176  C   ALA A 265     119.498 170.962 290.114  1.00 73.47           C  
ANISOU 3176  C   ALA A 265     3693  10550  13673    753    386   1655       C  
ATOM   3177  O   ALA A 265     118.294 170.753 289.939  1.00 71.76           O  
ANISOU 3177  O   ALA A 265     3646  10161  13460    719    421   1733       O  
ATOM   3178  CB  ALA A 265     120.576 169.414 291.760  1.00 86.77           C  
ANISOU 3178  CB  ALA A 265     5221  12215  15531   1041    127   1658       C  
ATOM   3179  N   ARG A 266     120.006 172.192 290.163  1.00 73.63           N  
ANISOU 3179  N   ARG A 266     3659  10690  13626    601    439   1634       N  
ATOM   3180  CA  ARG A 266     119.147 173.345 289.925  1.00 71.74           C  
ANISOU 3180  CA  ARG A 266     3581  10369  13308    419    548   1709       C  
ATOM   3181  C   ARG A 266     118.668 173.389 288.481  1.00 85.13           C  
ANISOU 3181  C   ARG A 266     5324  12104  14919    429    672   1653       C  
ATOM   3182  O   ARG A 266     117.564 173.871 288.218  1.00 83.61           O  
ANISOU 3182  O   ARG A 266     5302  11798  14669    354    738   1725       O  
ATOM   3183  CB  ARG A 266     119.889 174.630 290.295  1.00 85.77           C  
ANISOU 3183  CB  ARG A 266     5278  12260  15050    257    582   1702       C  
ATOM   3184  CG  ARG A 266     119.126 175.915 290.062  1.00 70.87           C  
ANISOU 3184  CG  ARG A 266     3550  10295  13081     90    699   1784       C  
ATOM   3185  CD  ARG A 266     119.636 176.986 290.995  1.00 71.40           C  
ANISOU 3185  CD  ARG A 266     3582  10383  13162    -68    685   1837       C  
ATOM   3186  NE  ARG A 266     119.979 178.217 290.298  1.00 93.44           N  
ANISOU 3186  NE  ARG A 266     6346  13283  15875   -224    827   1807       N  
ATOM   3187  CZ  ARG A 266     120.624 179.228 290.868  1.00 94.46           C  
ANISOU 3187  CZ  ARG A 266     6408  13475  16009   -396    845   1824       C  
ATOM   3188  NH1 ARG A 266     120.992 179.137 292.140  1.00 95.26           N  
ANISOU 3188  NH1 ARG A 266     6455  13551  16187   -418    715   1866       N  
ATOM   3189  NH2 ARG A 266     120.901 180.322 290.168  1.00 93.13           N  
ANISOU 3189  NH2 ARG A 266     6225  13392  15770   -553    994   1801       N  
ATOM   3190  N   LYS A 267     119.468 172.865 287.545  1.00 86.52           N  
ANISOU 3190  N   LYS A 267     5343  12448  15081    537    698   1525       N  
ATOM   3191  CA  LYS A 267     119.105 172.900 286.130  1.00 72.47           C  
ANISOU 3191  CA  LYS A 267     3593  10716  13225    556    814   1468       C  
ATOM   3192  C   LYS A 267     117.749 172.252 285.878  1.00 84.49           C  
ANISOU 3192  C   LYS A 267     5288  12062  14754    601    809   1532       C  
ATOM   3193  O   LYS A 267     116.936 172.779 285.111  1.00 83.02           O  
ANISOU 3193  O   LYS A 267     5209  11850  14484    542    900   1547       O  
ATOM   3194  CB  LYS A 267     120.184 172.209 285.294  1.00 74.67           C  
ANISOU 3194  CB  LYS A 267     3669  11192  13510    703    824   1327       C  
ATOM   3195  CG  LYS A 267     121.334 173.104 284.855  1.00 76.35           C  
ANISOU 3195  CG  LYS A 267     3704  11634  13670    617    908   1230       C  
ATOM   3196  CD  LYS A 267     122.457 172.275 284.238  1.00 89.33           C  
ANISOU 3196  CD  LYS A 267     5122  13490  15331    795    895   1086       C  
ATOM   3197  CE  LYS A 267     123.742 173.083 284.078  1.00 91.43           C  
ANISOU 3197  CE  LYS A 267     5159  14014  15567    696    959    979       C  
ATOM   3198  NZ  LYS A 267     124.829 172.305 283.409  1.00 94.13           N  
ANISOU 3198  NZ  LYS A 267     5261  14587  15917    883    956    824       N  
ATOM   3199  N   VAL A 268     117.485 171.109 286.514  1.00 84.88           N  
ANISOU 3199  N   VAL A 268     5351  11994  14904    707    704   1571       N  
ATOM   3200  CA  VAL A 268     116.218 170.415 286.300  1.00 83.68           C  
ANISOU 3200  CA  VAL A 268     5331  11687  14778    729    703   1626       C  
ATOM   3201  C   VAL A 268     115.091 171.089 287.077  1.00 67.76           C  
ANISOU 3201  C   VAL A 268     3484   9525  12736    587    704   1749       C  
ATOM   3202  O   VAL A 268     114.005 171.326 286.535  1.00 66.53           O  
ANISOU 3202  O   VAL A 268     3437   9331  12511    535    765   1771       O  
ATOM   3203  CB  VAL A 268     116.360 168.920 286.656  1.00 84.72           C  
ANISOU 3203  CB  VAL A 268     5407  11732  15049    894    604   1630       C  
ATOM   3204  CG1 VAL A 268     117.357 168.720 287.786  1.00 72.09           C  
ANISOU 3204  CG1 VAL A 268     3712  10149  13529    961    496   1641       C  
ATOM   3205  CG2 VAL A 268     115.007 168.315 287.012  1.00 69.62           C  
ANISOU 3205  CG2 VAL A 268     3627   9616  13208    856    582   1730       C  
ATOM   3206  N   CYS A 269     115.336 171.424 288.348  1.00 67.62           N  
ANISOU 3206  N   CYS A 269     3482   9441  12769    533    636   1827       N  
ATOM   3207  CA  CYS A 269     114.347 172.149 289.145  1.00 65.95           C  
ANISOU 3207  CA  CYS A 269     3426   9101  12530    412    641   1949       C  
ATOM   3208  C   CYS A 269     113.964 173.464 288.479  1.00 64.99           C  
ANISOU 3208  C   CYS A 269     3380   9048  12265    314    754   1948       C  
ATOM   3209  O   CYS A 269     112.787 173.841 288.440  1.00 63.62           O  
ANISOU 3209  O   CYS A 269     3339   8807  12027    267    794   2011       O  
ATOM   3210  CB  CYS A 269     114.892 172.409 290.550  1.00107.37           C  
ANISOU 3210  CB  CYS A 269     8655  14288  17853    378    554   2026       C  
ATOM   3211  SG  CYS A 269     115.463 170.944 291.445  1.00108.40           S  
ANISOU 3211  SG  CYS A 269     8689  14338  18161    523    408   2038       S  
ATOM   3212  N   ILE A 270     114.962 174.182 287.962  1.00 65.92           N  
ANISOU 3212  N   ILE A 270     3402   9309  12337    289    810   1876       N  
ATOM   3213  CA  ILE A 270     114.714 175.406 287.205  1.00 72.49           C  
ANISOU 3213  CA  ILE A 270     4290  10201  13050    209    932   1876       C  
ATOM   3214  C   ILE A 270     113.944 175.098 285.921  1.00 71.30           C  
ANISOU 3214  C   ILE A 270     4181  10084  12827    269   1001   1822       C  
ATOM   3215  O   ILE A 270     113.089 175.882 285.489  1.00 63.94           O  
ANISOU 3215  O   ILE A 270     3355   9141  11800    233   1078   1864       O  
ATOM   3216  CB  ILE A 270     116.052 176.120 286.918  1.00 75.37           C  
ANISOU 3216  CB  ILE A 270     4512  10720  13406    154    985   1807       C  
ATOM   3217  CG1 ILE A 270     116.221 177.377 287.772  1.00 75.38           C  
ANISOU 3217  CG1 ILE A 270     4555  10688  13397     13   1007   1899       C  
ATOM   3218  CG2 ILE A 270     116.198 176.442 285.461  1.00 76.64           C  
ANISOU 3218  CG2 ILE A 270     4633  11001  13485    167   1108   1722       C  
ATOM   3219  CD1 ILE A 270     117.452 178.201 287.416  1.00 77.39           C  
ANISOU 3219  CD1 ILE A 270     4663  11106  13635    -86   1084   1829       C  
ATOM   3220  N   ALA A 271     114.230 173.953 285.295  1.00 73.09           N  
ANISOU 3220  N   ALA A 271     4316  10357  13098    376    973   1733       N  
ATOM   3221  CA  ALA A 271     113.559 173.565 284.057  1.00 74.77           C  
ANISOU 3221  CA  ALA A 271     4548  10609  13254    437   1029   1675       C  
ATOM   3222  C   ALA A 271     112.239 172.847 284.298  1.00 64.60           C  
ANISOU 3222  C   ALA A 271     3354   9210  11982    448    982   1724       C  
ATOM   3223  O   ALA A 271     111.328 172.956 283.470  1.00 64.05           O  
ANISOU 3223  O   ALA A 271     3334   9171  11831    454   1035   1704       O  
ATOM   3224  CB  ALA A 271     114.472 172.675 283.215  1.00 78.13           C  
ANISOU 3224  CB  ALA A 271     4824  11139  13723    554   1030   1560       C  
ATOM   3225  N   LEU A 272     112.123 172.109 285.406  1.00 73.11           N  
ANISOU 3225  N   LEU A 272     4442  10169  13169    449    886   1787       N  
ATOM   3226  CA  LEU A 272     110.840 171.531 285.798  1.00 72.62           C  
ANISOU 3226  CA  LEU A 272     4460  10000  13132    424    852   1849       C  
ATOM   3227  C   LEU A 272     109.774 172.611 285.931  1.00 72.08           C  
ANISOU 3227  C   LEU A 272     4516   9933  12938    340    902   1911       C  
ATOM   3228  O   LEU A 272     108.636 172.437 285.479  1.00 61.85           O  
ANISOU 3228  O   LEU A 272     3260   8659  11583    331    924   1902       O  
ATOM   3229  CB  LEU A 272     110.992 170.775 287.124  1.00 72.66           C  
ANISOU 3229  CB  LEU A 272     4459   9862  13287    425    752   1932       C  
ATOM   3230  CG  LEU A 272     110.061 169.652 287.609  1.00 72.87           C  
ANISOU 3230  CG  LEU A 272     4502   9755  13429    418    701   1992       C  
ATOM   3231  CD1 LEU A 272     110.104 169.571 289.133  1.00 63.82           C  
ANISOU 3231  CD1 LEU A 272     3396   8462  12389    381    626   2112       C  
ATOM   3232  CD2 LEU A 272     108.623 169.768 287.121  1.00 63.15           C  
ANISOU 3232  CD2 LEU A 272     3338   8553  12104    350    751   1994       C  
ATOM   3233  N   ALA A 273     110.130 173.738 286.550  1.00 61.85           N  
ANISOU 3233  N   ALA A 273     3272   8627  11603    285    921   1974       N  
ATOM   3234  CA  ALA A 273     109.175 174.811 286.794  1.00 60.70           C  
ANISOU 3234  CA  ALA A 273     3244   8471  11350    232    969   2055       C  
ATOM   3235  C   ALA A 273     108.606 175.405 285.514  1.00 60.53           C  
ANISOU 3235  C   ALA A 273     3239   8563  11195    260   1065   2001       C  
ATOM   3236  O   ALA A 273     107.638 176.168 285.588  1.00 69.61           O  
ANISOU 3236  O   ALA A 273     4475   9724  12249    248   1106   2064       O  
ATOM   3237  CB  ALA A 273     109.831 175.914 287.626  1.00 60.56           C  
ANISOU 3237  CB  ALA A 273     3259   8415  11335    174    980   2139       C  
ATOM   3238  N   PHE A 274     109.174 175.081 284.350  1.00 71.76           N  
ANISOU 3238  N   PHE A 274     4576  10078  12610    313   1102   1893       N  
ATOM   3239  CA  PHE A 274     108.636 175.571 283.086  1.00 71.20           C  
ANISOU 3239  CA  PHE A 274     4515  10114  12425    354   1192   1843       C  
ATOM   3240  C   PHE A 274     107.342 174.876 282.685  1.00 61.08           C  
ANISOU 3240  C   PHE A 274     3240   8867  11102    382   1168   1807       C  
ATOM   3241  O   PHE A 274     106.803 175.181 281.616  1.00 65.14           O  
ANISOU 3241  O   PHE A 274     3747   9482  11520    429   1230   1757       O  
ATOM   3242  CB  PHE A 274     109.682 175.421 281.976  1.00 71.61           C  
ANISOU 3242  CB  PHE A 274     4465  10254  12488    405   1245   1741       C  
ATOM   3243  CG  PHE A 274     110.620 176.591 281.869  1.00 62.89           C  
ANISOU 3243  CG  PHE A 274     3352   9183  11359    364   1331   1767       C  
ATOM   3244  CD1 PHE A 274     111.639 176.765 282.792  1.00 69.67           C  
ANISOU 3244  CD1 PHE A 274     4170  10005  12296    302   1295   1797       C  
ATOM   3245  CD2 PHE A 274     110.479 177.522 280.851  1.00 63.07           C  
ANISOU 3245  CD2 PHE A 274     3397   9280  11288    383   1455   1767       C  
ATOM   3246  CE1 PHE A 274     112.500 177.846 282.703  1.00 69.89           C  
ANISOU 3246  CE1 PHE A 274     4169  10078  12307    236   1383   1817       C  
ATOM   3247  CE2 PHE A 274     111.338 178.603 280.754  1.00 63.71           C  
ANISOU 3247  CE2 PHE A 274     3463   9386  11357    324   1554   1803       C  
ATOM   3248  CZ  PHE A 274     112.348 178.766 281.682  1.00 69.71           C  
ANISOU 3248  CZ  PHE A 274     4173  10118  12196    238   1519   1824       C  
ATOM   3249  N   LEU A 275     106.832 173.963 283.512  1.00 60.92           N  
ANISOU 3249  N   LEU A 275     3220   8771  11156    349   1085   1835       N  
ATOM   3250  CA  LEU A 275     105.567 173.292 283.249  1.00 76.77           C  
ANISOU 3250  CA  LEU A 275     5211  10824  13134    342   1064   1803       C  
ATOM   3251  C   LEU A 275     104.391 173.927 283.984  1.00 75.87           C  
ANISOU 3251  C   LEU A 275     5178  10714  12935    295   1066   1884       C  
ATOM   3252  O   LEU A 275     103.241 173.710 283.581  1.00 60.24           O  
ANISOU 3252  O   LEU A 275     3171   8833  10884    292   1072   1844       O  
ATOM   3253  CB  LEU A 275     105.669 171.804 283.626  1.00 77.90           C  
ANISOU 3253  CB  LEU A 275     5283  10885  13430    325    988   1791       C  
ATOM   3254  CG  LEU A 275     106.268 170.791 282.635  1.00 62.82           C  
ANISOU 3254  CG  LEU A 275     3262   9004  11601    395    986   1697       C  
ATOM   3255  CD1 LEU A 275     107.642 171.208 282.143  1.00 63.23           C  
ANISOU 3255  CD1 LEU A 275     3286   9084  11655    467   1021   1657       C  
ATOM   3256  CD2 LEU A 275     106.330 169.395 283.251  1.00 63.62           C  
ANISOU 3256  CD2 LEU A 275     3303   8981  11888    381    915   1729       C  
ATOM   3257  N   SER A 276     104.653 174.712 285.037  1.00 75.58           N  
ANISOU 3257  N   SER A 276     5225  10589  12903    265   1064   1995       N  
ATOM   3258  CA  SER A 276     103.574 175.355 285.784  1.00 75.91           C  
ANISOU 3258  CA  SER A 276     5342  10635  12866    241   1073   2088       C  
ATOM   3259  C   SER A 276     102.822 176.358 284.924  1.00 80.05           C  
ANISOU 3259  C   SER A 276     5887  11298  13232    304   1155   2078       C  
ATOM   3260  O   SER A 276     101.617 176.560 285.112  1.00 82.58           O  
ANISOU 3260  O   SER A 276     6218  11694  13463    311   1162   2102       O  
ATOM   3261  CB  SER A 276     104.129 176.045 287.033  1.00 72.66           C  
ANISOU 3261  CB  SER A 276     5012  10094  12501    209   1060   2220       C  
ATOM   3262  OG  SER A 276     104.704 177.304 286.717  1.00 58.01           O  
ANISOU 3262  OG  SER A 276     3198   8257  10588    237   1134   2263       O  
ATOM   3263  N   SER A 277     103.516 177.005 283.988  1.00 58.88           N  
ANISOU 3263  N   SER A 277     3200   8657  10513    358   1223   2047       N  
ATOM   3264  CA  SER A 277     102.834 177.857 283.025  1.00 59.05           C  
ANISOU 3264  CA  SER A 277     3231   8809  10396    442   1308   2040       C  
ATOM   3265  C   SER A 277     101.901 177.058 282.130  1.00 59.64           C  
ANISOU 3265  C   SER A 277     3217   9022  10422    473   1286   1914       C  
ATOM   3266  O   SER A 277     100.964 177.626 281.557  1.00 59.88           O  
ANISOU 3266  O   SER A 277     3242   9182  10329    548   1333   1909       O  
ATOM   3267  CB  SER A 277     103.858 178.604 282.177  1.00 59.42           C  
ANISOU 3267  CB  SER A 277     3282   8860  10434    484   1399   2039       C  
ATOM   3268  OG  SER A 277     103.223 179.256 281.096  1.00 89.44           O  
ANISOU 3268  OG  SER A 277     7085  12788  14112    584   1486   2027       O  
ATOM   3269  N   SER A 278     102.135 175.752 282.006  1.00 68.06           N  
ANISOU 3269  N   SER A 278     4202  10070  11587    426   1218   1820       N  
ATOM   3270  CA  SER A 278     101.356 174.875 281.145  1.00 69.26           C  
ANISOU 3270  CA  SER A 278     4247  10349  11718    436   1196   1698       C  
ATOM   3271  C   SER A 278     100.491 173.906 281.944  1.00 69.81           C  
ANISOU 3271  C   SER A 278     4270  10416  11837    339   1125   1694       C  
ATOM   3272  O   SER A 278     100.178 172.812 281.470  1.00 70.80           O  
ANISOU 3272  O   SER A 278     4289  10595  12016    302   1091   1605       O  
ATOM   3273  CB  SER A 278     102.277 174.099 280.210  1.00 61.57           C  
ANISOU 3273  CB  SER A 278     3200   9369  10826    466   1194   1605       C  
ATOM   3274  OG  SER A 278     101.525 173.230 279.384  1.00 62.49           O  
ANISOU 3274  OG  SER A 278     3204   9605  10935    473   1173   1496       O  
ATOM   3275  N   VAL A 279     100.101 174.290 283.156  1.00 60.45           N  
ANISOU 3275  N   VAL A 279     3157   9169  10644    291   1110   1799       N  
ATOM   3276  CA  VAL A 279      99.293 173.424 284.001  1.00 82.63           C  
ANISOU 3276  CA  VAL A 279     5924  11969  13503    185   1057   1812       C  
ATOM   3277  C   VAL A 279      97.846 173.895 284.123  1.00 84.39           C  
ANISOU 3277  C   VAL A 279     6119  12354  13591    183   1078   1807       C  
ATOM   3278  O   VAL A 279      96.970 173.068 284.424  1.00 91.85           O  
ANISOU 3278  O   VAL A 279     6978  13365  14556     83   1049   1767       O  
ATOM   3279  CB  VAL A 279      99.925 173.257 285.401  1.00 79.94           C  
ANISOU 3279  CB  VAL A 279     5666  11428  13279    126   1018   1935       C  
ATOM   3280  CG1 VAL A 279      99.520 174.402 286.336  1.00 79.38           C  
ANISOU 3280  CG1 VAL A 279     5699  11338  13125    144   1044   2059       C  
ATOM   3281  CG2 VAL A 279      99.560 171.901 285.993  1.00 78.94           C  
ANISOU 3281  CG2 VAL A 279     5472  11243  13278     12    964   1935       C  
ATOM   3282  N   ASN A 280      97.557 175.180 283.886  1.00 78.63           N  
ANISOU 3282  N   ASN A 280     5448  11699  12730    289   1135   1852       N  
ATOM   3283  CA  ASN A 280      96.168 175.634 283.971  1.00 73.35           C  
ANISOU 3283  CA  ASN A 280     4735  11203  11931    318   1155   1851       C  
ATOM   3284  C   ASN A 280      95.299 175.066 282.857  1.00 74.85           C  
ANISOU 3284  C   ASN A 280     4769  11599  12073    321   1148   1690       C  
ATOM   3285  O   ASN A 280      94.186 174.598 283.155  1.00 63.42           O  
ANISOU 3285  O   ASN A 280     3219  10277  10599    246   1128   1642       O  
ATOM   3286  CB  ASN A 280      96.115 177.162 283.988  1.00 71.41           C  
ANISOU 3286  CB  ASN A 280     4593  10979  11561    457   1225   1971       C  
ATOM   3287  CG  ASN A 280      96.935 177.754 285.097  1.00 69.70           C  
ANISOU 3287  CG  ASN A 280     4514  10567  11400    442   1236   2134       C  
ATOM   3288  OD1 ASN A 280      97.691 177.050 285.770  1.00 70.78           O  
ANISOU 3288  OD1 ASN A 280     4673  10546  11674    343   1184   2147       O  
ATOM   3289  ND2 ASN A 280      96.803 179.059 285.294  1.00 68.13           N  
ANISOU 3289  ND2 ASN A 280     4405  10383  11099    549   1305   2271       N  
ATOM   3290  N   PRO A 281      95.705 175.091 281.579  1.00 76.07           N  
ANISOU 3290  N   PRO A 281     4884  11805  12214    401   1167   1602       N  
ATOM   3291  CA  PRO A 281      94.805 174.578 280.531  1.00 79.13           C  
ANISOU 3291  CA  PRO A 281     5109  12394  12561    411   1155   1452       C  
ATOM   3292  C   PRO A 281      94.389 173.129 280.731  1.00 65.28           C  
ANISOU 3292  C   PRO A 281     3219  10672  10911    237   1097   1359       C  
ATOM   3293  O   PRO A 281      93.268 172.764 280.355  1.00 66.67           O  
ANISOU 3293  O   PRO A 281     3246  11035  11052    193   1085   1259       O  
ATOM   3294  CB  PRO A 281      95.626 174.765 279.247  1.00 80.19           C  
ANISOU 3294  CB  PRO A 281     5250  12521  12696    522   1187   1399       C  
ATOM   3295  CG  PRO A 281      96.539 175.897 279.556  1.00 63.08           C  
ANISOU 3295  CG  PRO A 281     3250  10219  10499    606   1244   1536       C  
ATOM   3296  CD  PRO A 281      96.910 175.712 280.994  1.00 62.15           C  
ANISOU 3296  CD  PRO A 281     3214   9940  10461    495   1211   1639       C  
ATOM   3297  N   LEU A 282      95.247 172.287 281.313  1.00 64.84           N  
ANISOU 3297  N   LEU A 282     3203  10441  10991    133   1066   1402       N  
ATOM   3298  CA  LEU A 282      94.837 170.911 281.577  1.00 65.99           C  
ANISOU 3298  CA  LEU A 282     3229  10602  11241    -45   1024   1352       C  
ATOM   3299  C   LEU A 282      93.851 170.846 282.734  1.00 76.03           C  
ANISOU 3299  C   LEU A 282     4487  11911  12490   -168   1021   1397       C  
ATOM   3300  O   LEU A 282      92.903 170.053 282.707  1.00 77.97           O  
ANISOU 3300  O   LEU A 282     4587  12288  12750   -317   1010   1315       O  
ATOM   3301  CB  LEU A 282      96.055 170.033 281.862  1.00 65.66           C  
ANISOU 3301  CB  LEU A 282     3236  10342  11369    -93    996   1413       C  
ATOM   3302  CG  LEU A 282      96.967 169.686 280.684  1.00 65.92           C  
ANISOU 3302  CG  LEU A 282     3234  10353  11459     -3    998   1352       C  
ATOM   3303  CD1 LEU A 282      97.651 168.350 280.925  1.00 66.57           C  
ANISOU 3303  CD1 LEU A 282     3278  10272  11744    -93    962   1389       C  
ATOM   3304  CD2 LEU A 282      96.196 169.664 279.374  1.00 83.31           C  
ANISOU 3304  CD2 LEU A 282     5295  12784  13575     36   1011   1210       C  
ATOM   3305  N   LEU A 283      94.059 171.672 283.761  1.00 75.25           N  
ANISOU 3305  N   LEU A 283     4531  11702  12357   -119   1036   1529       N  
ATOM   3306  CA  LEU A 283      93.111 171.723 284.866  1.00 77.46           C  
ANISOU 3306  CA  LEU A 283     4803  12025  12603   -211   1043   1584       C  
ATOM   3307  C   LEU A 283      91.763 172.264 284.412  1.00 81.49           C  
ANISOU 3307  C   LEU A 283     5195  12795  12972   -167   1071   1499       C  
ATOM   3308  O   LEU A 283      90.726 171.894 284.973  1.00 85.00           O  
ANISOU 3308  O   LEU A 283     5544  13351  13401   -288   1078   1475       O  
ATOM   3309  CB  LEU A 283      93.675 172.572 286.006  1.00 63.82           C  
ANISOU 3309  CB  LEU A 283     3253  10122  10873   -144   1053   1757       C  
ATOM   3310  CG  LEU A 283      94.584 171.893 287.037  1.00 63.19           C  
ANISOU 3310  CG  LEU A 283     3263   9791  10956   -234   1019   1866       C  
ATOM   3311  CD1 LEU A 283      95.416 170.779 286.422  1.00 63.64           C  
ANISOU 3311  CD1 LEU A 283     3272   9752  11158   -287    984   1807       C  
ATOM   3312  CD2 LEU A 283      95.491 172.925 287.680  1.00 61.61           C  
ANISOU 3312  CD2 LEU A 283     3230   9423  10757   -120   1025   2008       C  
ATOM   3313  N   TYR A 284      91.753 173.129 283.397  1.00 66.39           N  
ANISOU 3313  N   TYR A 284     3282  10980  10962      9   1091   1461       N  
ATOM   3314  CA  TYR A 284      90.484 173.557 282.826  1.00 67.80           C  
ANISOU 3314  CA  TYR A 284     3328  11407  11025     77   1108   1385       C  
ATOM   3315  C   TYR A 284      89.915 172.491 281.905  1.00 69.65           C  
ANISOU 3315  C   TYR A 284     3357  11787  11319    -36   1080   1211       C  
ATOM   3316  O   TYR A 284      88.692 172.368 281.788  1.00 84.59           O  
ANISOU 3316  O   TYR A 284     5092  13877  13170    -80   1080   1144       O  
ATOM   3317  CB  TYR A 284      90.648 174.873 282.068  1.00 67.26           C  
ANISOU 3317  CB  TYR A 284     3341  11386  10828    317   1145   1436       C  
ATOM   3318  CG  TYR A 284      91.266 175.996 282.873  1.00 65.63           C  
ANISOU 3318  CG  TYR A 284     3335  11035  10565    423   1184   1621       C  
ATOM   3319  CD1 TYR A 284      91.383 175.921 284.257  1.00 64.86           C  
ANISOU 3319  CD1 TYR A 284     3319  10811  10513    329   1179   1733       C  
ATOM   3320  CD2 TYR A 284      91.729 177.139 282.242  1.00 65.04           C  
ANISOU 3320  CD2 TYR A 284     3366  10951  10395    613   1233   1696       C  
ATOM   3321  CE1 TYR A 284      91.952 176.946 284.981  1.00 63.53           C  
ANISOU 3321  CE1 TYR A 284     3322  10509  10307    421   1214   1910       C  
ATOM   3322  CE2 TYR A 284      92.294 178.168 282.957  1.00 63.80           C  
ANISOU 3322  CE2 TYR A 284     3381  10665  10195    692   1279   1875       C  
ATOM   3323  CZ  TYR A 284      92.402 178.068 284.322  1.00 63.04           C  
ANISOU 3323  CZ  TYR A 284     3354  10444  10156    596   1265   1979       C  
ATOM   3324  OH  TYR A 284      92.968 179.103 285.024  1.00 61.96           O  
ANISOU 3324  OH  TYR A 284     3377  10177   9987    673   1312   2166       O  
ATOM   3325  N   ALA A 285      90.778 171.716 281.253  1.00 69.51           N  
ANISOU 3325  N   ALA A 285     3328  11680  11402    -83   1056   1150       N  
ATOM   3326  CA  ALA A 285      90.355 170.555 280.483  1.00 88.02           C  
ANISOU 3326  CA  ALA A 285     5480  14137  13827   -225   1026   1006       C  
ATOM   3327  C   ALA A 285      90.219 169.302 281.342  1.00 90.91           C  
ANISOU 3327  C   ALA A 285     5794  14443  14305   -495   1011   1008       C  
ATOM   3328  O   ALA A 285      90.013 168.211 280.798  1.00 91.78           O  
ANISOU 3328  O   ALA A 285     5758  14613  14500   -658    988    912       O  
ATOM   3329  CB  ALA A 285      91.333 170.295 279.332  1.00 86.19           C  
ANISOU 3329  CB  ALA A 285     5255  13852  13643   -137   1014    958       C  
ATOM   3330  N   CYS A 286      90.333 169.440 282.666  1.00 91.97           N  
ANISOU 3330  N   CYS A 286     6048  14452  14445   -554   1025   1131       N  
ATOM   3331  CA  CYS A 286      90.169 168.295 283.555  1.00 96.50           C  
ANISOU 3331  CA  CYS A 286     6593  14949  15122   -815   1020   1159       C  
ATOM   3332  C   CYS A 286      88.748 167.744 283.508  1.00 99.39           C  
ANISOU 3332  C   CYS A 286     6758  15528  15478  -1015   1038   1037       C  
ATOM   3333  O   CYS A 286      88.542 166.550 283.757  1.00103.43           O  
ANISOU 3333  O   CYS A 286     7198  16013  16087  -1285   1037   1007       O  
ATOM   3334  CB  CYS A 286      90.553 168.694 284.984  1.00 94.83           C  
ANISOU 3334  CB  CYS A 286     6559  14553  14919   -803   1033   1329       C  
ATOM   3335  SG  CYS A 286      90.344 167.419 286.256  1.00 96.70           S  
ANISOU 3335  SG  CYS A 286     6802  14653  15285  -1111   1041   1404       S  
ATOM   3336  N   ALA A 287      87.763 168.580 283.180  1.00 99.68           N  
ANISOU 3336  N   ALA A 287     6703  15761  15410   -895   1055    982       N  
ATOM   3337  CA  ALA A 287      86.367 168.146 283.120  1.00 99.79           C  
ANISOU 3337  CA  ALA A 287     6508  15976  15431  -1060   1068    890       C  
ATOM   3338  C   ALA A 287      86.122 167.217 281.932  1.00102.62           C  
ANISOU 3338  C   ALA A 287     6682  16432  15878  -1188   1030    758       C  
ATOM   3339  O   ALA A 287      85.378 166.239 282.038  1.00104.97           O  
ANISOU 3339  O   ALA A 287     6836  16794  16254  -1464   1031    701       O  
ATOM   3340  CB  ALA A 287      85.434 169.352 283.053  1.00 97.71           C  
ANISOU 3340  CB  ALA A 287     6198  15902  15025   -850   1082    922       C  
TER    3341      ALA A 287                                                      
HETATM 3342  C10 7Y9 A2001     117.021 175.089 281.698  1.00 74.49           C  
ANISOU 3342  C10 7Y9 A2001     5287  12340  10674   2710   2557  -1084       C  
HETATM 3343  C13 7Y9 A2001     119.673 174.528 281.574  1.00 92.94           C  
ANISOU 3343  C13 7Y9 A2001     7238  14674  13400   2820   2607  -1221       C  
HETATM 3344  C15 7Y9 A2001     118.258 179.706 282.323  1.00 81.51           C  
ANISOU 3344  C15 7Y9 A2001     5455  13040  12474   2222   2677  -1415       C  
HETATM 3345  C17 7Y9 A2001     117.081 179.806 283.042  1.00 76.95           C  
ANISOU 3345  C17 7Y9 A2001     4986  12517  11733   2195   2521  -1509       C  
HETATM 3346  C20 7Y9 A2001     121.963 174.839 280.912  1.00 90.83           C  
ANISOU 3346  C20 7Y9 A2001     6645  14365  13503   2817   2807  -1305       C  
HETATM 3347  C21 7Y9 A2001     115.457 181.430 283.666  1.00 85.76           C  
ANISOU 3347  C21 7Y9 A2001     6062  13536  12987   2002   2364  -1727       C  
HETATM 3348  C22 7Y9 A2001     114.432 180.789 284.605  1.00 85.93           C  
ANISOU 3348  C22 7Y9 A2001     6239  13795  12616   2057   2167  -1812       C  
HETATM 3349  C24 7Y9 A2001     112.123 180.678 285.243  1.00 86.96           C  
ANISOU 3349  C24 7Y9 A2001     6641  14113  12287   2029   1982  -1872       C  
HETATM 3350  C26 7Y9 A2001     110.686 181.157 285.049  1.00 69.96           C  
ANISOU 3350  C26 7Y9 A2001     4641  11888  10051   1958   1980  -1890       C  
HETATM 3351  C28 7Y9 A2001     113.745 179.317 286.368  1.00 88.47           C  
ANISOU 3351  C28 7Y9 A2001     6641  14684  12290   2185   1799  -1866       C  
HETATM 3352  O01 7Y9 A2001     116.773 180.967 283.763  1.00 77.73           O  
ANISOU 3352  O01 7Y9 A2001     4922  12587  12024   2075   2380  -1712       O  
HETATM 3353  O02 7Y9 A2001     123.293 174.404 280.907  1.00 91.86           O  
ANISOU 3353  O02 7Y9 A2001     6595  14522  13785   2898   2806  -1365       O  
HETATM 3354  O03 7Y9 A2001     109.852 180.041 285.029  1.00 69.03           O  
ANISOU 3354  O03 7Y9 A2001     4808  11946   9475   2054   1956  -1686       O  
HETATM 3355  N04 7Y9 A2001     103.811 182.349 285.022  1.00 61.90           N  
ANISOU 3355  N04 7Y9 A2001     4483  10812   8225   1699   1750  -1968       N  
HETATM 3356  N05 7Y9 A2001     103.566 180.147 285.844  1.00 60.13           N  
ANISOU 3356  N05 7Y9 A2001     4550  11163   7135   1882   1586  -1627       N  
HETATM 3357  C06 7Y9 A2001     117.841 176.141 280.948  1.00 75.92           C  
ANISOU 3357  C06 7Y9 A2001     5313  12408  11126   2584   2783  -1125       C  
HETATM 3358  C07 7Y9 A2001     117.632 177.468 281.669  1.00 76.10           C  
ANISOU 3358  C07 7Y9 A2001     5177  12435  11301   2442   2723  -1222       C  
HETATM 3359  C08 7Y9 A2001     119.312 175.700 280.928  1.00 92.64           C  
ANISOU 3359  C08 7Y9 A2001     7230  14548  13421   2662   2797  -1189       C  
HETATM 3360  C09 7Y9 A2001     117.281 176.250 279.538  1.00 89.66           C  
ANISOU 3360  C09 7Y9 A2001     7239  14039  12788   2521   3014   -994       C  
HETATM 3361  C11 7Y9 A2001     118.522 178.535 281.634  1.00 80.88           C  
ANISOU 3361  C11 7Y9 A2001     5525  12987  12218   2345   2789  -1279       C  
HETATM 3362  C12 7Y9 A2001     116.467 177.582 282.378  1.00 74.46           C  
ANISOU 3362  C12 7Y9 A2001     5082  12300  10911   2417   2569  -1259       C  
HETATM 3363  C14 7Y9 A2001     120.294 176.427 280.262  1.00 94.83           C  
ANISOU 3363  C14 7Y9 A2001     7328  14778  13925   2587   2986  -1179       C  
HETATM 3364  C16 7Y9 A2001     116.204 178.743 283.056  1.00 86.11           C  
ANISOU 3364  C16 7Y9 A2001     6405  13775  12537   2292   2478  -1415       C  
HETATM 3365  C18 7Y9 A2001     120.992 174.101 281.567  1.00 80.79           C  
ANISOU 3365  C18 7Y9 A2001     5513  13144  12040   2895   2609  -1285       C  
HETATM 3366  C19 7Y9 A2001     121.614 176.008 280.259  1.00 82.09           C  
ANISOU 3366  C19 7Y9 A2001     5546  13204  12442   2665   2992  -1231       C  
HETATM 3367  C23 7Y9 A2001     113.125 181.194 284.448  1.00 86.39           C  
ANISOU 3367  C23 7Y9 A2001     6435  13793  12596   1993   2162  -1820       C  
HETATM 3368  C25 7Y9 A2001     114.748 179.847 285.574  1.00 87.49           C  
ANISOU 3368  C25 7Y9 A2001     6416  14287  12541   2155   1986  -1851       C  
HETATM 3369  C27 7Y9 A2001     112.433 179.734 286.208  1.00 87.96           C  
ANISOU 3369  C27 7Y9 A2001     6731  14575  12116   2123   1798  -1880       C  
HETATM 3370  C29 7Y9 A2001     108.489 180.313 285.119  1.00 66.19           C  
ANISOU 3370  C29 7Y9 A2001     4599  11611   8939   2003   1902  -1713       C  
HETATM 3371  C30 7Y9 A2001     107.597 179.288 284.846  1.00 74.52           C  
ANISOU 3371  C30 7Y9 A2001     6027  12702   9587   2058   1895  -1421       C  
HETATM 3372  C31 7Y9 A2001     108.042 181.574 285.483  1.00 67.13           C  
ANISOU 3372  C31 7Y9 A2001     4544  11643   9319   1874   1817  -2003       C  
HETATM 3373  C32 7Y9 A2001     105.799 180.779 285.299  1.00 70.52           C  
ANISOU 3373  C32 7Y9 A2001     5490  12186   9120   1889   1776  -1746       C  
HETATM 3374  C33 7Y9 A2001     106.239 179.520 284.934  1.00 71.47           C  
ANISOU 3374  C33 7Y9 A2001     5822  12328   9004   1997   1834  -1422       C  
HETATM 3375  C34 7Y9 A2001     106.684 181.804 285.578  1.00 72.14           C  
ANISOU 3375  C34 7Y9 A2001     5324  12308   9778   1829   1755  -2046       C  
HETATM 3376  C35 7Y9 A2001     104.317 181.049 285.409  1.00 61.52           C  
ANISOU 3376  C35 7Y9 A2001     4529  11067   7780   1827   1703  -1778       C  
CONECT  581 1178                                                                
CONECT 1178  581                                                                
CONECT 3342 3357                                                                
CONECT 3343 3359 3365                                                           
CONECT 3344 3345 3361                                                           
CONECT 3345 3344 3352 3364                                                      
CONECT 3346 3353 3365 3366                                                      
CONECT 3347 3348 3352                                                           
CONECT 3348 3347 3367 3368                                                      
CONECT 3349 3350 3367 3369                                                      
CONECT 3350 3349 3354                                                           
CONECT 3351 3368 3369                                                           
CONECT 3352 3345 3347                                                           
CONECT 3353 3346                                                                
CONECT 3354 3350 3370                                                           
CONECT 3355 3376                                                                
CONECT 3356 3376                                                                
CONECT 3357 3342 3358 3359 3360                                                 
CONECT 3358 3357 3361 3362                                                      
CONECT 3359 3343 3357 3363                                                      
CONECT 3360 3357                                                                
CONECT 3361 3344 3358                                                           
CONECT 3362 3358 3364                                                           
CONECT 3363 3359 3366                                                           
CONECT 3364 3345 3362                                                           
CONECT 3365 3343 3346                                                           
CONECT 3366 3346 3363                                                           
CONECT 3367 3348 3349                                                           
CONECT 3368 3348 3351                                                           
CONECT 3369 3349 3351                                                           
CONECT 3370 3354 3371 3372                                                      
CONECT 3371 3370 3374                                                           
CONECT 3372 3370 3375                                                           
CONECT 3373 3374 3375 3376                                                      
CONECT 3374 3371 3373                                                           
CONECT 3375 3372 3373                                                           
CONECT 3376 3355 3356 3373                                                      
MASTER      442    0    1   25    5    0    4    6 3375    1   37   41          
END