Welcome to PDBbind-CN database

Browse entries in the PDBbind-CN Database

HEADER    RNA BINDING PROTEIN/RNA                 11-FEB-19   6NY5              
TITLE     CRYSTAL STRUCTURE OF THE PUM-HD DOMAIN OF S. POMBE PUF1 IN COMPLEX    
TITLE    2 WITH RNA                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUMILIO DOMAIN-CONTAINING PROTEIN C56F2.08C;               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: PUM-HD DOMAIN (UNP RESIDUES 109-485);                      
COMPND   5 SYNONYM: PUF1;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: RNA (5'-R(P*UP*UP*AP*AP*UP*AP*AP*CP*UP*UP*AP*AP*U)-3');    
COMPND   9 CHAIN: C;                                                            
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SCHIZOSACCHAROMYCES POMBE;                      
SOURCE   3 ORGANISM_COMMON: FISSION YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4896;                                                
SOURCE   5 GENE: SPBC56F2.08C;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: SCHIZOSACCHAROMYCES POMBE;                      
SOURCE  11 ORGANISM_COMMON: FISSION YEAST;                                      
SOURCE  12 ORGANISM_TAXID: 4896                                                 
KEYWDS    PUF PROTEIN, RNA BINDING PROTEIN-RNA COMPLEX                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.QIU,T.M.T.HALL                                                      
REVDAT   2   15-JAN-20 6NY5    1       JRNL                                     
REVDAT   1   03-JUL-19 6NY5    0                                                
JRNL        AUTH   C.QIU,R.C.DUTCHER,D.F.PORTER,Y.ARAVA,M.WICKENS,T.M.T.HALL    
JRNL        TITL   DISTINCT RNA-BINDING MODULES IN A SINGLE PUF PROTEIN         
JRNL        TITL 2 COOPERATE TO DETERMINE RNA SPECIFICITY.                      
JRNL        REF    NUCLEIC ACIDS RES.            V.  47  8770 2019              
JRNL        REFN                   ESSN 1362-4962                               
JRNL        PMID   31294800                                                     
JRNL        DOI    10.1093/NAR/GKZ583                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.14_3260                                     
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.76                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 27506                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.215                           
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.263                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.080                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1948                            
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 32.7605 -  7.2103    0.99     1985   144  0.1708 0.2196        
REMARK   3     2  7.2103 -  5.7330    0.99     1891   148  0.2161 0.2621        
REMARK   3     3  5.7330 -  5.0112    0.98     1835   139  0.2101 0.2558        
REMARK   3     4  5.0112 -  4.5544    0.96     1810   136  0.1786 0.2311        
REMARK   3     5  4.5544 -  4.2287    0.97     1799   132  0.1786 0.2124        
REMARK   3     6  4.2287 -  3.9798    0.96     1795   131  0.1952 0.2240        
REMARK   3     7  3.9798 -  3.7808    0.96     1782   145  0.2230 0.2509        
REMARK   3     8  3.7808 -  3.6164    0.97     1791   137  0.2395 0.2931        
REMARK   3     9  3.6164 -  3.4774    0.97     1788   136  0.2461 0.3482        
REMARK   3    10  3.4774 -  3.3575    0.98     1811   143  0.2733 0.3398        
REMARK   3    11  3.3575 -  3.2526    0.98     1811   133  0.2893 0.4269        
REMARK   3    12  3.2526 -  3.1597    0.99     1824   141  0.2735 0.3574        
REMARK   3    13  3.1597 -  3.0766    1.00     1822   141  0.2847 0.3110        
REMARK   3    14  3.0766 -  3.0016    0.99     1814   142  0.2873 0.3534        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.380            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.610           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 93.13                          
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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN 'A' AND RESID 97 THROUGH 482)                   
REMARK   3    ORIGIN FOR THE GROUP (A):  56.3664  68.8622  55.1365              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4674 T22:   0.4644                                     
REMARK   3      T33:   0.7526 T12:  -0.1022                                     
REMARK   3      T13:  -0.0045 T23:   0.0189                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7695 L22:   0.8657                                     
REMARK   3      L33:   2.8723 L12:  -1.2645                                     
REMARK   3      L13:   2.1169 L23:  -0.6557                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0405 S12:   0.0121 S13:  -0.1065                       
REMARK   3      S21:  -0.0534 S22:  -0.0356 S23:   0.2065                       
REMARK   3      S31:   0.2096 S32:  -0.3383 S33:   0.1131                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN 'B' AND RESID 97 THROUGH 478)                   
REMARK   3    ORIGIN FOR THE GROUP (A): 111.7514  56.3073  37.2712              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3994 T22:   0.7021                                     
REMARK   3      T33:   0.4508 T12:   0.0417                                     
REMARK   3      T13:   0.0080 T23:  -0.0808                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6503 L22:   2.4500                                     
REMARK   3      L33:   3.4951 L12:  -0.7481                                     
REMARK   3      L13:   1.1083 L23:  -0.0365                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2115 S12:   0.4968 S13:  -0.1811                       
REMARK   3      S21:  -0.3451 S22:  -0.2273 S23:   0.1232                       
REMARK   3      S31:   0.0701 S32:   0.1858 S33:   0.0413                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN 'C' AND RESID -1 THROUGH 12)                    
REMARK   3    ORIGIN FOR THE GROUP (A):  84.5815  57.3195  51.0845              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7750 T22:   1.0049                                     
REMARK   3      T33:   0.7961 T12:   0.0098                                     
REMARK   3      T13:   0.0995 T23:   0.0141                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4458 L22:   0.5432                                     
REMARK   3      L33:   1.3217 L12:  -1.0074                                     
REMARK   3      L13:   0.1093 L23:   0.3927                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0553 S12:   1.5431 S13:   0.0208                       
REMARK   3      S21:  -0.5856 S22:   0.0874 S23:   0.0997                       
REMARK   3      S31:  -0.0722 S32:   0.7848 S33:  -0.1642                       
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 6NY5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-FEB-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000239620.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-MAR-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944+                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28120                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 8.100                              
REMARK 200  R MERGE                    (I) : 0.06200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: AUTOSOL                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.71                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4 M MAGNESIUM SULFATE, 0.1 M MES, PH   
REMARK 280  5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   -X+1/2,Y,-Z+3/4                                         
REMARK 290       6555   X,-Y+1/2,-Z+1/4                                         
REMARK 290       7555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X,-Y,Z                                                 
REMARK 290      11555   -Y+1/2,X,Z+3/4                                          
REMARK 290      12555   Y,-X+1/2,Z+1/4                                          
REMARK 290      13555   -X,Y+1/2,-Z+1/4                                         
REMARK 290      14555   X+1/2,-Y,-Z+3/4                                         
REMARK 290      15555   Y,X,-Z                                                  
REMARK 290      16555   -Y+1/2,-X+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       79.83850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       79.83850            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      107.76500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       79.83850            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       53.88250            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       79.83850            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      161.64750            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       79.83850            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      161.64750            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       79.83850            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       53.88250            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000       79.83850            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       79.83850            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      107.76500            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       79.83850            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       79.83850            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      107.76500            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       79.83850            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000      161.64750            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       79.83850            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       53.88250            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       79.83850            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       53.88250            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       79.83850            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      161.64750            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       79.83850            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       79.83850            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      107.76500            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 37020 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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     LYS A   483                                                      
REMARK 465     SER A   484                                                      
REMARK 465     ILE A   485                                                      
REMARK 465     PRO B   154                                                      
REMARK 465     VAL B   155                                                      
REMARK 465     GLU B   156                                                      
REMARK 465     THR B   157                                                      
REMARK 465     LEU B   158                                                      
REMARK 465     ARG B   159                                                      
REMARK 465     SER B   160                                                      
REMARK 465     ARG B   161                                                      
REMARK 465     GLN B   162                                                      
REMARK 465     PRO B   442                                                      
REMARK 465     SER B   443                                                      
REMARK 465     ILE B   444                                                      
REMARK 465     GLY B   479                                                      
REMARK 465     MET B   480                                                      
REMARK 465     THR B   481                                                      
REMARK 465     SER B   482                                                      
REMARK 465     LYS B   483                                                      
REMARK 465     SER B   484                                                      
REMARK 465     ILE B   485                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 114       56.74   -101.33                                   
REMARK 500    GLN A 124       10.54    -68.91                                   
REMARK 500    GLU A 126     -126.61     61.35                                   
REMARK 500    MET A 127     -179.50     61.47                                   
REMARK 500    ASN A 144       94.87    -62.58                                   
REMARK 500    LYS A 146       94.20    -67.86                                   
REMARK 500    LYS A 289      165.23     66.70                                   
REMARK 500    SER A 362       14.29     57.59                                   
REMARK 500    GLU A 401       75.60   -118.97                                   
REMARK 500    PHE A 414       77.35   -105.15                                   
REMARK 500    VAL A 430      -44.40   -133.25                                   
REMARK 500    SER A 443        7.56   -159.57                                   
REMARK 500    PRO A 467       45.82    -84.52                                   
REMARK 500    MET A 480      -79.09     55.21                                   
REMARK 500    SER B 114       55.85   -103.90                                   
REMARK 500    ASN B 144       95.32    -69.96                                   
REMARK 500    LYS B 289      168.27     66.13                                   
REMARK 500    ASP B 360      -70.58    -89.38                                   
REMARK 500    GLU B 401       78.59   -117.42                                   
REMARK 500    PHE B 414       73.37   -103.36                                   
REMARK 500    LYS B 417       31.88   -151.03                                   
REMARK 500    VAL B 430      -42.75   -134.94                                   
REMARK 500    PRO B 467       46.35    -89.25                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 605        DISTANCE =  5.83 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 101  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   C C   7   O2                                                     
REMARK 620 2   A C  10   OP1  71.2                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 101                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6NWW   RELATED DB: PDB                                   
DBREF  6NY5 A  109   485  UNP    O60059   YG58_SCHPO     109    485             
DBREF  6NY5 B  109   485  UNP    O60059   YG58_SCHPO     109    485             
DBREF  6NY5 C   -1    12  PDB    6NY5     6NY5            -1     12             
SEQADV 6NY5 SER A   97  UNP  O60059              EXPRESSION TAG                 
SEQADV 6NY5 GLU A   98  UNP  O60059              EXPRESSION TAG                 
SEQADV 6NY5 PHE A   99  UNP  O60059              EXPRESSION TAG                 
SEQADV 6NY5 GLU A  100  UNP  O60059              EXPRESSION TAG                 
SEQADV 6NY5 LEU A  101  UNP  O60059              EXPRESSION TAG                 
SEQADV 6NY5 ARG A  102  UNP  O60059              EXPRESSION TAG                 
SEQADV 6NY5 ARG A  103  UNP  O60059              EXPRESSION TAG                 
SEQADV 6NY5 GLN A  104  UNP  O60059              EXPRESSION TAG                 
SEQADV 6NY5 ALA A  105  UNP  O60059              EXPRESSION TAG                 
SEQADV 6NY5 CYS A  106  UNP  O60059              EXPRESSION TAG                 
SEQADV 6NY5 GLY A  107  UNP  O60059              EXPRESSION TAG                 
SEQADV 6NY5 ARG A  108  UNP  O60059              EXPRESSION TAG                 
SEQADV 6NY5 SER B   97  UNP  O60059              EXPRESSION TAG                 
SEQADV 6NY5 GLU B   98  UNP  O60059              EXPRESSION TAG                 
SEQADV 6NY5 PHE B   99  UNP  O60059              EXPRESSION TAG                 
SEQADV 6NY5 GLU B  100  UNP  O60059              EXPRESSION TAG                 
SEQADV 6NY5 LEU B  101  UNP  O60059              EXPRESSION TAG                 
SEQADV 6NY5 ARG B  102  UNP  O60059              EXPRESSION TAG                 
SEQADV 6NY5 ARG B  103  UNP  O60059              EXPRESSION TAG                 
SEQADV 6NY5 GLN B  104  UNP  O60059              EXPRESSION TAG                 
SEQADV 6NY5 ALA B  105  UNP  O60059              EXPRESSION TAG                 
SEQADV 6NY5 CYS B  106  UNP  O60059              EXPRESSION TAG                 
SEQADV 6NY5 GLY B  107  UNP  O60059              EXPRESSION TAG                 
SEQADV 6NY5 ARG B  108  UNP  O60059              EXPRESSION TAG                 
SEQRES   1 A  389  SER GLU PHE GLU LEU ARG ARG GLN ALA CYS GLY ARG SER          
SEQRES   2 A  389  GLN LEU LEU LYS SER ARG VAL ASP ILE LEU GLU VAL ALA          
SEQRES   3 A  389  ARG GLN PHE GLU MET ARG ILE ASN LEU ASP ILE VAL ASP          
SEQRES   4 A  389  SER MET ILE ALA SER ALA ILE GLU ASN ASN LYS VAL ALA          
SEQRES   5 A  389  THR GLU ILE LEU PRO PRO VAL GLU THR LEU ARG SER ARG          
SEQRES   6 A  389  GLN PHE GLU ALA SER LYS LEU ARG GLU ILE ARG LYS ASN          
SEQRES   7 A  389  ILE ASP SER GLY PHE TYR THR GLN GLU GLU ILE GLU VAL          
SEQRES   8 A  389  ILE ALA ARG SER MET LEU ASP ASP VAL ALA GLU LEU SER          
SEQRES   9 A  389  SER ASP TYR LEU GLY ASN THR VAL VAL GLN LYS PHE PHE          
SEQRES  10 A  389  GLU TYR CYS SER ASP PRO ILE LYS GLU ALA MET LEU GLU          
SEQRES  11 A  389  ARG ILE ALA PRO TYR LEU ALA ALA ILE GLY ILE HIS LYS          
SEQRES  12 A  389  ASN GLY THR TRP ALA ALA GLN LYS ILE ILE ASP VAL ALA          
SEQRES  13 A  389  SER THR GLU LYS GLN MET ASP LEU ILE VAL LYS HIS LEU          
SEQRES  14 A  389  ARG PRO TYR THR ALA LEU LEU TYR PHE ASP GLN PHE GLY          
SEQRES  15 A  389  ASN TYR VAL ALA GLN CYS CYS LEU ARG PHE LYS TYR PRO          
SEQRES  16 A  389  LYS ASN THR PHE LEU PHE GLU VAL MET ALA ARG HIS CYS          
SEQRES  17 A  389  CYS GLU ILE GLY GLN SER ARG PHE GLY ALA ARG ALA ILE          
SEQRES  18 A  389  ARG ALA CYS LEU GLU ASN GLU ASN ALA THR PHE GLU GLN          
SEQRES  19 A  389  GLN ALA LEU VAL VAL ALA SER ILE ILE ILE ASN SER HIS          
SEQRES  20 A  389  LEU LEU ALA THR ASN SER ASN GLY MET LEU LEU LEU THR          
SEQRES  21 A  389  TRP LEU LEU ASP ASN SER PHE PHE ARG ASN ARG HIS ARG          
SEQRES  22 A  389  LEU LEU ALA ILE HIS LEU ALA THR HIS LEU HIS THR THR          
SEQRES  23 A  389  CYS THR HIS LYS LEU ALA SER THR LEU ILE PHE LYS LEU          
SEQRES  24 A  389  ILE ASN ASN LYS GLN GLU PRO GLU SER ARG ASN LEU LEU          
SEQRES  25 A  389  LEU LYS ASN LEU PHE PHE SER GLU LYS ASP ASN VAL LEU          
SEQRES  26 A  389  THR TYR ILE LEU GLN ASP GLN ALA VAL GLY PRO SER PHE          
SEQRES  27 A  389  ILE HIS LYS VAL ILE THR TYR PRO SER ILE GLY ARG GLU          
SEQRES  28 A  389  PHE LEU ALA GLN PHE HIS LEU VAL ILE LYS ARG VAL LEU          
SEQRES  29 A  389  ILE ASN ILE HIS ALA GLN PRO ASN ALA VAL TYR CYS ARG          
SEQRES  30 A  389  LEU MET GLU GLU VAL GLY MET THR SER LYS SER ILE              
SEQRES   1 B  389  SER GLU PHE GLU LEU ARG ARG GLN ALA CYS GLY ARG SER          
SEQRES   2 B  389  GLN LEU LEU LYS SER ARG VAL ASP ILE LEU GLU VAL ALA          
SEQRES   3 B  389  ARG GLN PHE GLU MET ARG ILE ASN LEU ASP ILE VAL ASP          
SEQRES   4 B  389  SER MET ILE ALA SER ALA ILE GLU ASN ASN LYS VAL ALA          
SEQRES   5 B  389  THR GLU ILE LEU PRO PRO VAL GLU THR LEU ARG SER ARG          
SEQRES   6 B  389  GLN PHE GLU ALA SER LYS LEU ARG GLU ILE ARG LYS ASN          
SEQRES   7 B  389  ILE ASP SER GLY PHE TYR THR GLN GLU GLU ILE GLU VAL          
SEQRES   8 B  389  ILE ALA ARG SER MET LEU ASP ASP VAL ALA GLU LEU SER          
SEQRES   9 B  389  SER ASP TYR LEU GLY ASN THR VAL VAL GLN LYS PHE PHE          
SEQRES  10 B  389  GLU TYR CYS SER ASP PRO ILE LYS GLU ALA MET LEU GLU          
SEQRES  11 B  389  ARG ILE ALA PRO TYR LEU ALA ALA ILE GLY ILE HIS LYS          
SEQRES  12 B  389  ASN GLY THR TRP ALA ALA GLN LYS ILE ILE ASP VAL ALA          
SEQRES  13 B  389  SER THR GLU LYS GLN MET ASP LEU ILE VAL LYS HIS LEU          
SEQRES  14 B  389  ARG PRO TYR THR ALA LEU LEU TYR PHE ASP GLN PHE GLY          
SEQRES  15 B  389  ASN TYR VAL ALA GLN CYS CYS LEU ARG PHE LYS TYR PRO          
SEQRES  16 B  389  LYS ASN THR PHE LEU PHE GLU VAL MET ALA ARG HIS CYS          
SEQRES  17 B  389  CYS GLU ILE GLY GLN SER ARG PHE GLY ALA ARG ALA ILE          
SEQRES  18 B  389  ARG ALA CYS LEU GLU ASN GLU ASN ALA THR PHE GLU GLN          
SEQRES  19 B  389  GLN ALA LEU VAL VAL ALA SER ILE ILE ILE ASN SER HIS          
SEQRES  20 B  389  LEU LEU ALA THR ASN SER ASN GLY MET LEU LEU LEU THR          
SEQRES  21 B  389  TRP LEU LEU ASP ASN SER PHE PHE ARG ASN ARG HIS ARG          
SEQRES  22 B  389  LEU LEU ALA ILE HIS LEU ALA THR HIS LEU HIS THR THR          
SEQRES  23 B  389  CYS THR HIS LYS LEU ALA SER THR LEU ILE PHE LYS LEU          
SEQRES  24 B  389  ILE ASN ASN LYS GLN GLU PRO GLU SER ARG ASN LEU LEU          
SEQRES  25 B  389  LEU LYS ASN LEU PHE PHE SER GLU LYS ASP ASN VAL LEU          
SEQRES  26 B  389  THR TYR ILE LEU GLN ASP GLN ALA VAL GLY PRO SER PHE          
SEQRES  27 B  389  ILE HIS LYS VAL ILE THR TYR PRO SER ILE GLY ARG GLU          
SEQRES  28 B  389  PHE LEU ALA GLN PHE HIS LEU VAL ILE LYS ARG VAL LEU          
SEQRES  29 B  389  ILE ASN ILE HIS ALA GLN PRO ASN ALA VAL TYR CYS ARG          
SEQRES  30 B  389  LEU MET GLU GLU VAL GLY MET THR SER LYS SER ILE              
SEQRES   1 C   13    U   U   A   A   U   A   A   C   U   U   A   A   U          
HET    SO4  A 501       5                                                       
HET    SO4  A 502       5                                                       
HET    SO4  A 503       5                                                       
HET    SO4  B 501       5                                                       
HET    SO4  B 502       5                                                       
HET     MG  C 101       1                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   4  SO4    5(O4 S 2-)                                                   
FORMUL   9   MG    MG 2+                                                        
FORMUL  10  HOH   *25(H2 O)                                                     
HELIX    1 AA1 SER A   97  ALA A  105  1                                   9    
HELIX    2 AA2 SER A  109  SER A  114  1                                   6    
HELIX    3 AA3 SER A  114  GLN A  124  1                                  11    
HELIX    4 AA4 ASN A  130  ASN A  144  1                                  15    
HELIX    5 AA5 SER A  160  SER A  177  1                                  18    
HELIX    6 AA6 THR A  181  MET A  192  1                                  12    
HELIX    7 AA7 ASP A  195  SER A  200  1                                   6    
HELIX    8 AA8 LEU A  204  CYS A  216  1                                  13    
HELIX    9 AA9 SER A  217  ALA A  229  1                                  13    
HELIX   10 AB1 TYR A  231  ILE A  237  1                                   7    
HELIX   11 AB2 ASN A  240  VAL A  251  1                                  12    
HELIX   12 AB3 THR A  254  ARG A  266  1                                  13    
HELIX   13 AB4 TYR A  268  ASP A  275  1                                   8    
HELIX   14 AB5 PHE A  277  CYS A  285  1                                   9    
HELIX   15 AB6 LEU A  286  LYS A  289  5                                   4    
HELIX   16 AB7 ASN A  293  HIS A  303  1                                  11    
HELIX   17 AB8 HIS A  303  GLN A  309  1                                   7    
HELIX   18 AB9 SER A  310  ASN A  323  1                                  14    
HELIX   19 AC1 THR A  327  ILE A  340  1                                  14    
HELIX   20 AC2 ASN A  341  ALA A  346  1                                   6    
HELIX   21 AC3 ASN A  348  ASP A  360  1                                  13    
HELIX   22 AC4 ASN A  366  ALA A  376  1                                  11    
HELIX   23 AC5 HIS A  378  CYS A  383  1                                   6    
HELIX   24 AC6 LEU A  387  ASN A  398  1                                  12    
HELIX   25 AC7 GLU A  401  PHE A  414  1                                  14    
HELIX   26 AC8 SER A  415  LYS A  417  5                                   3    
HELIX   27 AC9 ASP A  418  ASP A  427  1                                  10    
HELIX   28 AD1 VAL A  430  THR A  440  1                                  11    
HELIX   29 AD2 ARG A  446  HIS A  464  1                                  19    
HELIX   30 AD3 TYR A  471  GLU A  477  1                                   7    
HELIX   31 AD4 GLU B   98  ALA B  105  1                                   8    
HELIX   32 AD5 SER B  109  SER B  114  1                                   6    
HELIX   33 AD6 SER B  114  PHE B  125  1                                  12    
HELIX   34 AD7 ASN B  130  ASN B  144  1                                  15    
HELIX   35 AD8 GLU B  164  SER B  177  1                                  14    
HELIX   36 AD9 THR B  181  SER B  191  1                                  11    
HELIX   37 AE1 ASP B  195  SER B  201  1                                   7    
HELIX   38 AE2 LEU B  204  CYS B  216  1                                  13    
HELIX   39 AE3 SER B  217  ILE B  237  1                                  21    
HELIX   40 AE4 ASN B  240  VAL B  251  1                                  12    
HELIX   41 AE5 THR B  254  ARG B  266  1                                  13    
HELIX   42 AE6 TYR B  268  PHE B  274  1                                   7    
HELIX   43 AE7 PHE B  277  CYS B  285  1                                   9    
HELIX   44 AE8 LEU B  286  LYS B  289  5                                   4    
HELIX   45 AE9 ASN B  293  HIS B  303  1                                  11    
HELIX   46 AF1 HIS B  303  GLN B  309  1                                   7    
HELIX   47 AF2 SER B  310  GLU B  322  1                                  13    
HELIX   48 AF3 THR B  327  ASN B  341  1                                  15    
HELIX   49 AF4 ASN B  341  ALA B  346  1                                   6    
HELIX   50 AF5 ASN B  348  ASP B  360  1                                  13    
HELIX   51 AF6 ASN B  366  ALA B  376  1                                  11    
HELIX   52 AF7 HIS B  378  CYS B  383  1                                   6    
HELIX   53 AF8 LEU B  387  ASN B  398  1                                  12    
HELIX   54 AF9 GLU B  401  PHE B  414  1                                  14    
HELIX   55 AG1 ASP B  418  ASP B  427  1                                  10    
HELIX   56 AG2 VAL B  430  THR B  440  1                                  11    
HELIX   57 AG3 ARG B  446  HIS B  464  1                                  19    
HELIX   58 AG4 TYR B  471  VAL B  478  1                                   8    
SSBOND   1 CYS A  106    CYS A  305                          1555   1555  2.03  
SSBOND   2 CYS B  106    CYS B  305                          1555   1555  2.03  
LINK         O2    C C   7                MG    MG C 101     1555   1555  2.40  
LINK         OP1   A C  10                MG    MG C 101     1555   1555  2.31  
CISPEP   1 TYR A  290    PRO A  291          0         1.58                     
CISPEP   2 TYR B  290    PRO B  291          0         5.72                     
SITE     1 AC1  3 ARG A 102  SER A 310  ARG A 311                               
SITE     1 AC2  2 THR A 254  GLU A 255                                          
SITE     1 AC3  4 ARG A 103  ARG A 108  SER A 109  ARG A 302                    
SITE     1 AC4  5 ARG B 103  SER B 109  LEU B 112  ARG B 302                    
SITE     2 AC4  5 HIS B 303                                                     
SITE     1 AC5  2 THR B 254  GLU B 255                                          
SITE     1 AC6  2   C C   7    A C  10                                          
CRYST1  159.677  159.677  215.530  90.00  90.00  90.00 I 41 2 2     32          
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      0.006263  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006263  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004640        0.00000                         
ATOM      1  N   SER A  97      68.863  81.988  48.505  1.00130.64           N  
ANISOU    1  N   SER A  97    14865  15754  19018  -1457  -1319   2760       N  
ATOM      2  CA  SER A  97      69.014  80.577  48.847  1.00123.65           C  
ANISOU    2  CA  SER A  97    14012  15003  17967  -1333  -1079   2546       C  
ATOM      3  C   SER A  97      67.899  79.731  48.236  1.00118.23           C  
ANISOU    3  C   SER A  97    13383  14419  17120  -1202   -920   2321       C  
ATOM      4  O   SER A  97      66.928  80.260  47.696  1.00117.81           O  
ANISOU    4  O   SER A  97    13354  14316  17091  -1199   -990   2297       O  
ATOM      5  CB  SER A  97      69.043  80.394  50.369  1.00117.14           C  
ANISOU    5  CB  SER A  97    13318  13939  17251  -1307  -1111   2332       C  
ATOM      6  OG  SER A  97      67.972  81.078  50.995  1.00110.42           O  
ANISOU    6  OG  SER A  97    12597  12824  16533  -1284  -1258   2159       O  
ATOM      7  N   GLU A  98      68.057  78.407  48.314  1.00115.60           N  
ANISOU    7  N   GLU A  98    13074  14220  16629  -1094   -725   2159       N  
ATOM      8  CA  GLU A  98      67.011  77.509  47.838  1.00121.19           C  
ANISOU    8  CA  GLU A  98    13850  14990  17207   -980   -602   1930       C  
ATOM      9  C   GLU A  98      65.763  77.606  48.707  1.00115.20           C  
ANISOU    9  C   GLU A  98    13230  13984  16558   -969   -648   1684       C  
ATOM     10  O   GLU A  98      64.654  77.325  48.236  1.00112.59           O  
ANISOU   10  O   GLU A  98    12936  13668  16174   -918   -614   1542       O  
ATOM     11  CB  GLU A  98      67.533  76.073  47.808  1.00132.85           C  
ANISOU   11  CB  GLU A  98    15339  16626  18512   -869   -428   1815       C  
ATOM     12  CG  GLU A  98      66.726  75.118  46.946  1.00138.45           C  
ANISOU   12  CG  GLU A  98    16086  17457  19063   -750   -331   1643       C  
ATOM     13  CD  GLU A  98      67.168  73.677  47.118  1.00140.82           C  
ANISOU   13  CD  GLU A  98    16443  17836  19226   -633   -207   1488       C  
ATOM     14  OE1 GLU A  98      67.623  73.323  48.227  1.00139.73           O  
ANISOU   14  OE1 GLU A  98    16367  17572  19152   -651   -184   1425       O  
ATOM     15  OE2 GLU A  98      67.079  72.905  46.141  1.00141.71           O  
ANISOU   15  OE2 GLU A  98    16544  18134  19166   -508   -149   1425       O  
ATOM     16  N   PHE A  99      65.929  77.993  49.975  1.00104.99           N  
ANISOU   16  N   PHE A  99    12003  12487  15404  -1004   -728   1632       N  
ATOM     17  CA  PHE A  99      64.785  78.226  50.851  1.00 93.14           C  
ANISOU   17  CA  PHE A  99    10607  10792  13989   -970   -784   1420       C  
ATOM     18  C   PHE A  99      63.947  79.397  50.353  1.00 94.60           C  
ANISOU   18  C   PHE A  99    10788  10898  14257   -990   -946   1464       C  
ATOM     19  O   PHE A  99      62.711  79.345  50.386  1.00 92.29           O  
ANISOU   19  O   PHE A  99    10543  10571  13950   -931   -940   1292       O  
ATOM     20  CB  PHE A  99      65.277  78.478  52.279  1.00 91.59           C  
ANISOU   20  CB  PHE A  99    10473  10424  13904   -975   -855   1370       C  
ATOM     21  CG  PHE A  99      64.187  78.474  53.323  1.00101.99           C  
ANISOU   21  CG  PHE A  99    11886  11607  15259   -899   -874   1136       C  
ATOM     22  CD1 PHE A  99      64.442  78.946  54.602  1.00106.06           C  
ANISOU   22  CD1 PHE A  99    12460  11966  15872   -869   -980   1075       C  
ATOM     23  CD2 PHE A  99      62.920  77.989  53.038  1.00107.43           C  
ANISOU   23  CD2 PHE A  99    12592  12351  15874   -848   -791    983       C  
ATOM     24  CE1 PHE A  99      63.453  78.945  55.571  1.00109.86           C  
ANISOU   24  CE1 PHE A  99    13008  12379  16354   -769   -991    868       C  
ATOM     25  CE2 PHE A  99      61.927  77.987  54.002  1.00111.27           C  
ANISOU   25  CE2 PHE A  99    13132  12769  16376   -774   -801    796       C  
ATOM     26  CZ  PHE A  99      62.195  78.465  55.271  1.00112.76           C  
ANISOU   26  CZ  PHE A  99    13372  12833  16639   -725   -894    740       C  
ATOM     27  N   GLU A 100      64.605  80.461  49.882  1.00101.24           N  
ANISOU   27  N   GLU A 100    11565  11714  15187  -1076  -1103   1709       N  
ATOM     28  CA  GLU A 100      63.888  81.639  49.404  1.00112.94           C  
ANISOU   28  CA  GLU A 100    13055  13095  16763  -1098  -1290   1772       C  
ATOM     29  C   GLU A 100      62.942  81.293  48.260  1.00110.76           C  
ANISOU   29  C   GLU A 100    12749  12978  16359  -1047  -1195   1724       C  
ATOM     30  O   GLU A 100      61.866  81.892  48.141  1.00120.91           O  
ANISOU   30  O   GLU A 100    14079  14175  17687  -1007  -1296   1633       O  
ATOM     31  CB  GLU A 100      64.889  82.711  48.961  1.00127.64           C  
ANISOU   31  CB  GLU A 100    14835  14922  18739  -1230  -1474   2099       C  
ATOM     32  CG  GLU A 100      65.740  83.303  50.086  1.00138.71           C  
ANISOU   32  CG  GLU A 100    16275  16116  20311  -1293  -1642   2154       C  
ATOM     33  CD  GLU A 100      66.849  84.214  49.570  1.00149.12           C  
ANISOU   33  CD  GLU A 100    17484  17432  21745  -1460  -1818   2525       C  
ATOM     34  OE1 GLU A 100      66.829  84.559  48.367  1.00152.78           O  
ANISOU   34  OE1 GLU A 100    17848  18038  22165  -1522  -1831   2747       O  
ATOM     35  OE2 GLU A 100      67.749  84.573  50.362  1.00150.72           O  
ANISOU   35  OE2 GLU A 100    17687  17500  22077  -1534  -1947   2609       O  
ATOM     36  N   LEU A 101      63.317  80.326  47.416  1.00102.91           N  
ANISOU   36  N   LEU A 101    11682  12222  15199  -1028  -1015   1768       N  
ATOM     37  CA  LEU A 101      62.478  79.974  46.273  1.00 99.90           C  
ANISOU   37  CA  LEU A 101    11272  11999  14688   -968   -943   1719       C  
ATOM     38  C   LEU A 101      61.231  79.211  46.698  1.00 97.80           C  
ANISOU   38  C   LEU A 101    11091  11683  14386   -887   -860   1415       C  
ATOM     39  O   LEU A 101      60.174  79.355  46.073  1.00 98.71           O  
ANISOU   39  O   LEU A 101    11208  11830  14469   -848   -882   1338       O  
ATOM     40  CB  LEU A 101      63.278  79.151  45.265  1.00103.15           C  
ANISOU   40  CB  LEU A 101    11585  12692  14915   -935   -799   1835       C  
ATOM     41  CG  LEU A 101      64.535  79.795  44.681  1.00107.73           C  
ANISOU   41  CG  LEU A 101    12030  13414  15487  -1013   -851   2179       C  
ATOM     42  CD1 LEU A 101      65.099  78.910  43.586  1.00110.43           C  
ANISOU   42  CD1 LEU A 101    12268  14097  15595   -920   -697   2251       C  
ATOM     43  CD2 LEU A 101      64.239  81.193  44.151  1.00104.46           C  
ANISOU   43  CD2 LEU A 101    11576  12928  15187  -1100  -1043   2389       C  
ATOM     44  N   ARG A 102      61.332  78.397  47.749  1.00 94.26           N  
ANISOU   44  N   ARG A 102    10704  11169  13942   -869   -771   1258       N  
ATOM     45  CA  ARG A 102      60.173  77.635  48.202  1.00 91.65           C  
ANISOU   45  CA  ARG A 102    10431  10809  13583   -817   -697   1012       C  
ATOM     46  C   ARG A 102      59.123  78.545  48.829  1.00 91.83           C  
ANISOU   46  C   ARG A 102    10489  10696  13709   -794   -820    915       C  
ATOM     47  O   ARG A 102      57.920  78.345  48.625  1.00 87.25           O  
ANISOU   47  O   ARG A 102     9907  10151  13094   -754   -802    777       O  
ATOM     48  CB  ARG A 102      60.617  76.552  49.182  1.00 90.52           C  
ANISOU   48  CB  ARG A 102    10337  10637  13419   -812   -580    908       C  
ATOM     49  CG  ARG A 102      61.481  75.483  48.539  1.00 90.44           C  
ANISOU   49  CG  ARG A 102    10308  10771  13283   -792   -462    949       C  
ATOM     50  CD  ARG A 102      61.691  74.307  49.470  1.00 86.40           C  
ANISOU   50  CD  ARG A 102     9865  10210  12752   -779   -361    819       C  
ATOM     51  NE  ARG A 102      61.927  73.070  48.731  1.00 84.99           N  
ANISOU   51  NE  ARG A 102     9701  10151  12441   -725   -272    764       N  
ATOM     52  CZ  ARG A 102      63.133  72.568  48.478  1.00 88.86           C  
ANISOU   52  CZ  ARG A 102    10177  10741  12843   -679   -222    839       C  
ATOM     53  NH1 ARG A 102      64.225  73.195  48.908  1.00 89.13           N  
ANISOU   53  NH1 ARG A 102    10169  10778  12919   -709   -240    994       N  
ATOM     54  NH2 ARG A 102      63.248  71.439  47.794  1.00 88.19           N  
ANISOU   54  NH2 ARG A 102    10123  10759  12628   -593   -170    755       N  
ATOM     55  N   ARG A 103      59.559  79.561  49.582  1.00 95.76           N  
ANISOU   55  N   ARG A 103    11014  11042  14328   -806   -963    980       N  
ATOM     56  CA  ARG A 103      58.611  80.494  50.183  1.00 99.37           C  
ANISOU   56  CA  ARG A 103    11514  11375  14869   -740  -1112    872       C  
ATOM     57  C   ARG A 103      58.011  81.430  49.148  1.00104.33           C  
ANISOU   57  C   ARG A 103    12119  12005  15517   -733  -1245    947       C  
ATOM     58  O   ARG A 103      56.862  81.860  49.297  1.00103.07           O  
ANISOU   58  O   ARG A 103    11978  11819  15365   -650  -1317    811       O  
ATOM     59  CB  ARG A 103      59.279  81.311  51.284  1.00103.24           C  
ANISOU   59  CB  ARG A 103    12060  11681  15484   -731  -1267    899       C  
ATOM     60  CG  ARG A 103      59.779  80.465  52.429  1.00119.46           C  
ANISOU   60  CG  ARG A 103    14142  13730  17516   -717  -1148    808       C  
ATOM     61  CD  ARG A 103      60.473  81.308  53.482  1.00133.96           C  
ANISOU   61  CD  ARG A 103    16037  15387  19476   -694  -1323    827       C  
ATOM     62  NE  ARG A 103      59.523  82.188  54.173  1.00140.79           N  
ANISOU   62  NE  ARG A 103    16959  16146  20389   -562  -1493    671       N  
ATOM     63  CZ  ARG A 103      59.820  83.404  54.627  1.00142.02           C  
ANISOU   63  CZ  ARG A 103    17179  16106  20678   -520  -1757    694       C  
ATOM     64  NH1 ARG A 103      61.041  83.882  54.474  1.00148.63           N  
ANISOU   64  NH1 ARG A 103    18019  16825  21629   -635  -1879    891       N  
ATOM     65  NH2 ARG A 103      58.903  84.145  55.246  1.00137.03           N  
ANISOU   65  NH2 ARG A 103    16605  15397  20062   -356  -1919    520       N  
ATOM     66  N   GLN A 104      58.779  81.779  48.116  1.00107.95           N  
ANISOU   66  N   GLN A 104    12527  12514  15975   -811  -1282   1175       N  
ATOM     67  CA  GLN A 104      58.251  82.649  47.073  1.00108.37           C  
ANISOU   67  CA  GLN A 104    12556  12581  16041   -809  -1407   1276       C  
ATOM     68  C   GLN A 104      57.180  81.939  46.254  1.00100.68           C  
ANISOU   68  C   GLN A 104    11548  11774  14933   -751  -1281   1145       C  
ATOM     69  O   GLN A 104      56.212  82.573  45.820  1.00 97.69           O  
ANISOU   69  O   GLN A 104    11174  11381  14564   -700  -1380   1100       O  
ATOM     70  CB  GLN A 104      59.398  83.144  46.186  1.00111.42           C  
ANISOU   70  CB  GLN A 104    12870  13019  16445   -916  -1467   1592       C  
ATOM     71  CG  GLN A 104      59.160  84.498  45.531  1.00118.79           C  
ANISOU   71  CG  GLN A 104    13802  13858  17474   -946  -1697   1765       C  
ATOM     72  CD  GLN A 104      58.751  84.384  44.074  1.00128.97           C  
ANISOU   72  CD  GLN A 104    15014  15356  18635   -935  -1633   1862       C  
ATOM     73  OE1 GLN A 104      59.261  83.533  43.341  1.00136.58           O  
ANISOU   73  OE1 GLN A 104    15892  16552  19451   -943  -1457   1939       O  
ATOM     74  NE2 GLN A 104      57.832  85.243  43.644  1.00127.57           N  
ANISOU   74  NE2 GLN A 104    14867  15103  18500   -892  -1787   1850       N  
ATOM     75  N   ALA A 105      57.327  80.631  46.053  1.00 98.15           N  
ANISOU   75  N   ALA A 105    11199  11600  14492   -753  -1083   1073       N  
ATOM     76  CA  ALA A 105      56.316  79.806  45.405  1.00 95.20           C  
ANISOU   76  CA  ALA A 105    10804  11360  14006   -704   -981    923       C  
ATOM     77  C   ALA A 105      55.239  79.322  46.369  1.00 90.98           C  
ANISOU   77  C   ALA A 105    10300  10780  13488   -665   -939    688       C  
ATOM     78  O   ALA A 105      54.348  78.569  45.958  1.00 78.47           O  
ANISOU   78  O   ALA A 105     8691   9293  11831   -646   -866    561       O  
ATOM     79  CB  ALA A 105      56.975  78.601  44.727  1.00 96.20           C  
ANISOU   79  CB  ALA A 105    10901  11650  14002   -709   -828    946       C  
ATOM     80  N   CYS A 106      55.308  79.723  47.639  1.00 97.15           N  
ANISOU   80  N   CYS A 106    11124  11432  14358   -650   -991    636       N  
ATOM     81  CA  CYS A 106      54.306  79.372  48.632  1.00102.83           C  
ANISOU   81  CA  CYS A 106    11845  12150  15075   -597   -953    444       C  
ATOM     82  C   CYS A 106      53.558  80.578  49.172  1.00108.61           C  
ANISOU   82  C   CYS A 106    12594  12804  15869   -497  -1118    376       C  
ATOM     83  O   CYS A 106      52.439  80.419  49.664  1.00107.49           O  
ANISOU   83  O   CYS A 106    12418  12733  15690   -426  -1097    223       O  
ATOM     84  CB  CYS A 106      54.960  78.633  49.812  1.00 99.28           C  
ANISOU   84  CB  CYS A 106    11428  11659  14636   -622   -856    408       C  
ATOM     85  SG  CYS A 106      55.113  76.847  49.604  1.00 94.13           S  
ANISOU   85  SG  CYS A 106    10764  11106  13894   -694   -657    363       S  
ATOM     86  N   GLY A 107      54.141  81.768  49.089  1.00117.40           N  
ANISOU   86  N   GLY A 107    13754  13780  17073   -484  -1297    491       N  
ATOM     87  CA  GLY A 107      53.576  82.914  49.753  1.00118.41           C  
ANISOU   87  CA  GLY A 107    13928  13795  17269   -362  -1494    407       C  
ATOM     88  C   GLY A 107      53.803  82.806  51.252  1.00119.43           C  
ANISOU   88  C   GLY A 107    14095  13864  17420   -294  -1492    297       C  
ATOM     89  O   GLY A 107      54.473  81.902  51.756  1.00117.10           O  
ANISOU   89  O   GLY A 107    13794  13596  17102   -361  -1344    311       O  
ATOM     90  N   ARG A 108      53.218  83.758  51.968  1.00124.75           N  
ANISOU   90  N   ARG A 108    14812  14461  18126   -135  -1673    177       N  
ATOM     91  CA  ARG A 108      53.339  83.762  53.414  1.00129.32           C  
ANISOU   91  CA  ARG A 108    15425  15008  18702    -24  -1694     53       C  
ATOM     92  C   ARG A 108      52.477  82.656  54.017  1.00123.24           C  
ANISOU   92  C   ARG A 108    14563  14465  17796     15  -1474    -81       C  
ATOM     93  O   ARG A 108      51.508  82.185  53.413  1.00125.76           O  
ANISOU   93  O   ARG A 108    14797  14945  18039     -1  -1372   -119       O  
ATOM     94  CB  ARG A 108      52.971  85.138  53.970  1.00133.81           C  
ANISOU   94  CB  ARG A 108    16075  15436  19330    172  -1984    -54       C  
ATOM     95  CG  ARG A 108      53.792  86.245  53.319  1.00137.72           C  
ANISOU   95  CG  ARG A 108    16662  15680  19987    100  -2237    114       C  
ATOM     96  CD  ARG A 108      53.512  87.620  53.894  1.00142.78           C  
ANISOU   96  CD  ARG A 108    17414  16125  20712    297  -2579      3       C  
ATOM     97  NE  ARG A 108      54.324  88.642  53.237  1.00142.80           N  
ANISOU   97  NE  ARG A 108    17500  15865  20894    187  -2842    205       N  
ATOM     98  CZ  ARG A 108      55.589  88.909  53.549  1.00137.33           C  
ANISOU   98  CZ  ARG A 108    16860  14980  20337     70  -2958    351       C  
ATOM     99  NH1 ARG A 108      56.200  88.223  54.506  1.00131.78           N  
ANISOU   99  NH1 ARG A 108    16149  14316  19605     65  -2827    296       N  
ATOM    100  NH2 ARG A 108      56.249  89.858  52.899  1.00136.28           N  
ANISOU  100  NH2 ARG A 108    16782  14625  20374    -51  -3211    568       N  
ATOM    101  N   SER A 109      52.854  82.235  55.222  1.00110.66           N  
ANISOU  101  N   SER A 109    12980  12887  16178     58  -1409   -137       N  
ATOM    102  CA  SER A 109      52.317  81.007  55.790  1.00 98.01           C  
ANISOU  102  CA  SER A 109    11286  11490  14465     36  -1182   -194       C  
ATOM    103  C   SER A 109      50.809  81.090  55.978  1.00 98.86           C  
ANISOU  103  C   SER A 109    11289  11807  14466    170  -1171   -324       C  
ATOM    104  O   SER A 109      50.273  82.110  56.420  1.00101.82           O  
ANISOU  104  O   SER A 109    11679  12187  14820    376  -1340   -438       O  
ATOM    105  CB  SER A 109      52.990  80.707  57.128  1.00 89.15           C  
ANISOU  105  CB  SER A 109    10196  10348  13329     86  -1143   -224       C  
ATOM    106  OG  SER A 109      52.282  79.701  57.829  1.00 81.76           O  
ANISOU  106  OG  SER A 109     9159   9629  12277     96   -959   -274       O  
ATOM    107  N   GLN A 110      50.123  79.999  55.631  1.00105.53           N  
ANISOU  107  N   GLN A 110    12025  12829  15243     59   -986   -306       N  
ATOM    108  CA  GLN A 110      48.696  79.896  55.901  1.00113.73           C  
ANISOU  108  CA  GLN A 110    12926  14115  16173    158   -946   -400       C  
ATOM    109  C   GLN A 110      48.408  79.743  57.390  1.00115.82           C  
ANISOU  109  C   GLN A 110    13125  14545  16337    302   -897   -471       C  
ATOM    110  O   GLN A 110      47.260  79.919  57.810  1.00121.94           O  
ANISOU  110  O   GLN A 110    13774  15560  16999    448   -895   -555       O  
ATOM    111  CB  GLN A 110      48.101  78.719  55.121  1.00115.26           C  
ANISOU  111  CB  GLN A 110    13018  14431  16343    -31   -786   -340       C  
ATOM    112  CG  GLN A 110      48.229  78.836  53.605  1.00113.64           C  
ANISOU  112  CG  GLN A 110    12858  14119  16201   -136   -832   -288       C  
ATOM    113  CD  GLN A 110      47.211  79.783  52.989  1.00118.67           C  
ANISOU  113  CD  GLN A 110    13452  14827  16812    -12   -960   -362       C  
ATOM    114  OE1 GLN A 110      46.379  80.368  53.686  1.00123.13           O  
ANISOU  114  OE1 GLN A 110    13950  15526  17306    168  -1022   -466       O  
ATOM    115  NE2 GLN A 110      47.275  79.939  51.673  1.00119.16           N  
ANISOU  115  NE2 GLN A 110    13547  14817  16914    -86  -1005   -312       N  
ATOM    116  N   LEU A 111      49.426  79.421  58.193  1.00112.52           N  
ANISOU  116  N   LEU A 111    12779  14030  15943    278   -855   -435       N  
ATOM    117  CA  LEU A 111      49.237  79.323  59.636  1.00112.19           C  
ANISOU  117  CA  LEU A 111    12681  14154  15792    437   -815   -498       C  
ATOM    118  C   LEU A 111      49.038  80.697  60.265  1.00119.71           C  
ANISOU  118  C   LEU A 111    13683  15097  16703    740  -1034   -653       C  
ATOM    119  O   LEU A 111      48.264  80.835  61.220  1.00127.58           O  
ANISOU  119  O   LEU A 111    14577  16347  17550    953  -1026   -750       O  
ATOM    120  CB  LEU A 111      50.436  78.609  60.269  1.00104.89           C  
ANISOU  120  CB  LEU A 111    11833  13112  14907    331   -723   -418       C  
ATOM    121  CG  LEU A 111      50.466  78.349  61.778  1.00 98.88           C  
ANISOU  121  CG  LEU A 111    11027  12510  14034    472   -661   -455       C  
ATOM    122  CD1 LEU A 111      50.194  76.883  62.089  1.00 94.03           C  
ANISOU  122  CD1 LEU A 111    10299  12066  13363    296   -432   -334       C  
ATOM    123  CD2 LEU A 111      51.794  78.789  62.374  1.00 99.23           C  
ANISOU  123  CD2 LEU A 111    11225  12330  14149    531   -763   -475       C  
ATOM    124  N   LEU A 112      49.714  81.723  59.740  1.00119.85           N  
ANISOU  124  N   LEU A 112    13853  14837  16847    771  -1245   -673       N  
ATOM    125  CA  LEU A 112      49.584  83.065  60.298  1.00130.66           C  
ANISOU  125  CA  LEU A 112    15303  16138  18205   1061  -1509   -831       C  
ATOM    126  C   LEU A 112      48.194  83.636  60.047  1.00134.44           C  
ANISOU  126  C   LEU A 112    15688  16817  18577   1253  -1584   -951       C  
ATOM    127  O   LEU A 112      47.546  84.148  60.969  1.00131.27           O  
ANISOU  127  O   LEU A 112    15242  16597  18036   1551  -1673  -1111       O  
ATOM    128  CB  LEU A 112      50.650  83.984  59.704  1.00137.06           C  
ANISOU  128  CB  LEU A 112    16294  16578  19205   1000  -1740   -780       C  
ATOM    129  CG  LEU A 112      52.094  83.510  59.850  1.00142.64           C  
ANISOU  129  CG  LEU A 112    17082  17092  20022    809  -1684   -648       C  
ATOM    130  CD1 LEU A 112      53.050  84.536  59.259  1.00147.06           C  
ANISOU  130  CD1 LEU A 112    17788  17319  20769    750  -1939   -572       C  
ATOM    131  CD2 LEU A 112      52.423  83.225  61.306  1.00142.39           C  
ANISOU  131  CD2 LEU A 112    17053  17140  19908    949  -1646   -731       C  
ATOM    132  N   LYS A 113      47.725  83.567  58.800  1.00144.26           N  
ANISOU  132  N   LYS A 113    16896  18048  19869   1107  -1557   -884       N  
ATOM    133  CA  LYS A 113      46.412  84.110  58.466  1.00153.75           C  
ANISOU  133  CA  LYS A 113    18007  19437  20975   1281  -1632   -993       C  
ATOM    134  C   LYS A 113      45.311  83.364  59.210  1.00164.84           C  
ANISOU  134  C   LYS A 113    19193  21258  22181   1371  -1441  -1035       C  
ATOM    135  O   LYS A 113      44.522  83.962  59.951  1.00167.94           O  
ANISOU  135  O   LYS A 113    19516  21871  22424   1677  -1531  -1188       O  
ATOM    136  CB  LYS A 113      46.176  84.037  56.953  1.00152.07           C  
ANISOU  136  CB  LYS A 113    17790  19141  20849   1083  -1616   -895       C  
ATOM    137  CG  LYS A 113      47.370  84.413  56.087  1.00148.58           C  
ANISOU  137  CG  LYS A 113    17515  18348  20592    908  -1725   -769       C  
ATOM    138  CD  LYS A 113      46.966  84.560  54.621  1.00142.06           C  
ANISOU  138  CD  LYS A 113    16677  17486  19813    791  -1746   -697       C  
ATOM    139  CE  LYS A 113      46.159  85.832  54.386  1.00137.33           C  
ANISOU  139  CE  LYS A 113    16113  16867  19198   1026  -1994   -820       C  
ATOM    140  NZ  LYS A 113      45.951  86.113  52.935  1.00130.52           N  
ANISOU  140  NZ  LYS A 113    15267  15927  18397    914  -2046   -729       N  
ATOM    141  N   SER A 114      45.258  82.050  59.035  1.00169.69           N  
ANISOU  141  N   SER A 114    19691  21993  22788   1112  -1189   -893       N  
ATOM    142  CA  SER A 114      44.139  81.241  59.516  1.00177.15           C  
ANISOU  142  CA  SER A 114    20400  23335  23574   1120  -1006   -871       C  
ATOM    143  C   SER A 114      44.497  80.515  60.814  1.00170.96           C  
ANISOU  143  C   SER A 114    19556  22698  22704   1132   -864   -822       C  
ATOM    144  O   SER A 114      44.414  79.292  60.916  1.00175.13           O  
ANISOU  144  O   SER A 114    19974  23344  23224    908   -662   -676       O  
ATOM    145  CB  SER A 114      43.708  80.257  58.431  1.00186.05           C  
ANISOU  145  CB  SER A 114    21434  24496  24762    820   -860   -739       C  
ATOM    146  OG  SER A 114      44.829  79.724  57.746  1.00188.24           O  
ANISOU  146  OG  SER A 114    21857  24468  25198    565   -819   -630       O  
ATOM    147  N   ARG A 115      44.897  81.293  61.825  1.00162.79           N  
ANISOU  147  N   ARG A 115    18602  21648  21603   1407   -993   -947       N  
ATOM    148  CA  ARG A 115      45.116  80.714  63.148  1.00150.14           C  
ANISOU  148  CA  ARG A 115    16926  20241  19879   1479   -869   -918       C  
ATOM    149  C   ARG A 115      43.815  80.196  63.747  1.00143.70           C  
ANISOU  149  C   ARG A 115    15829  19923  18849   1571   -717   -882       C  
ATOM    150  O   ARG A 115      43.820  79.186  64.462  1.00139.76           O  
ANISOU  150  O   ARG A 115    15206  19621  18278   1459   -526   -743       O  
ATOM    151  CB  ARG A 115      45.750  81.742  64.084  1.00148.05           C  
ANISOU  151  CB  ARG A 115    16809  19867  19577   1795  -1073  -1088       C  
ATOM    152  CG  ARG A 115      45.974  81.233  65.499  1.00150.20           C  
ANISOU  152  CG  ARG A 115    17007  20364  19698   1917   -960  -1075       C  
ATOM    153  CD  ARG A 115      46.460  82.330  66.433  1.00156.03           C  
ANISOU  153  CD  ARG A 115    17886  21021  20377   2284  -1198  -1283       C  
ATOM    154  NE  ARG A 115      45.385  83.244  66.818  1.00161.49           N  
ANISOU  154  NE  ARG A 115    18489  21996  20874   2682  -1346  -1479       N  
ATOM    155  CZ  ARG A 115      45.126  84.399  66.214  1.00160.51           C  
ANISOU  155  CZ  ARG A 115    18480  21697  20809   2853  -1609  -1638       C  
ATOM    156  NH1 ARG A 115      45.871  84.798  65.192  1.00160.09           N  
ANISOU  156  NH1 ARG A 115    18624  21193  21009   2641  -1747  -1600       N  
ATOM    157  NH2 ARG A 115      44.126  85.161  66.635  1.00157.64           N  
ANISOU  157  NH2 ARG A 115    18030  21624  20243   3247  -1741  -1828       N  
ATOM    158  N   VAL A 116      42.697  80.865  63.461  1.00141.80           N  
ANISOU  158  N   VAL A 116    15474  19901  18501   1768   -802   -987       N  
ATOM    159  CA  VAL A 116      41.414  80.412  63.983  1.00140.40           C  
ANISOU  159  CA  VAL A 116    14994  20243  18107   1856   -660   -934       C  
ATOM    160  C   VAL A 116      40.829  79.299  63.118  1.00149.99           C  
ANISOU  160  C   VAL A 116    16055  21533  19404   1482   -487   -733       C  
ATOM    161  O   VAL A 116      40.115  78.428  63.627  1.00153.71           O  
ANISOU  161  O   VAL A 116    16276  22371  19758   1393   -313   -579       O  
ATOM    162  CB  VAL A 116      40.438  81.594  64.109  1.00129.93           C  
ANISOU  162  CB  VAL A 116    13596  19163  16609   2261   -832  -1143       C  
ATOM    163  CG1 VAL A 116      39.308  81.257  65.074  1.00129.31           C  
ANISOU  163  CG1 VAL A 116    13193  19696  16244   2457   -694  -1102       C  
ATOM    164  CG2 VAL A 116      41.180  82.841  64.561  1.00127.40           C  
ANISOU  164  CG2 VAL A 116    13521  18586  16298   2591  -1097  -1371       C  
ATOM    165  N   ASP A 117      41.112  79.301  61.809  1.00146.72           N  
ANISOU  165  N   ASP A 117    15777  20784  19186   1259   -543   -720       N  
ATOM    166  CA  ASP A 117      40.605  78.236  60.944  1.00152.03           C  
ANISOU  166  CA  ASP A 117    16328  21492  19945    916   -413   -554       C  
ATOM    167  C   ASP A 117      41.265  76.898  61.263  1.00149.46           C  
ANISOU  167  C   ASP A 117    16007  21081  19701    614   -248   -361       C  
ATOM    168  O   ASP A 117      40.622  75.846  61.169  1.00154.75           O  
ANISOU  168  O   ASP A 117    16495  21932  20373    383   -123   -195       O  
ATOM    169  CB  ASP A 117      40.817  78.594  59.470  1.00153.50           C  
ANISOU  169  CB  ASP A 117    16672  21349  20301    790   -525   -603       C  
ATOM    170  CG  ASP A 117      39.909  79.719  58.994  1.00153.32           C  
ANISOU  170  CG  ASP A 117    16607  21446  20202   1038   -677   -758       C  
ATOM    171  OD1 ASP A 117      39.022  80.150  59.761  1.00155.38           O  
ANISOU  171  OD1 ASP A 117    16695  22073  20271   1306   -689   -833       O  
ATOM    172  OD2 ASP A 117      40.083  80.168  57.842  1.00151.27           O  
ANISOU  172  OD2 ASP A 117    16481  20930  20064    976   -787   -801       O  
ATOM    173  N   ILE A 118      42.551  76.917  61.626  1.00139.44           N  
ANISOU  173  N   ILE A 118    14946  19524  18511    606   -264   -375       N  
ATOM    174  CA  ILE A 118      43.223  75.693  62.061  1.00127.22           C  
ANISOU  174  CA  ILE A 118    13414  17902  17023    363   -120   -207       C  
ATOM    175  C   ILE A 118      42.582  75.163  63.335  1.00126.35           C  
ANISOU  175  C   ILE A 118    13071  18205  16733    430     11    -96       C  
ATOM    176  O   ILE A 118      42.344  73.956  63.478  1.00123.22           O  
ANISOU  176  O   ILE A 118    12552  17906  16360    174    142    105       O  
ATOM    177  CB  ILE A 118      44.730  75.950  62.247  1.00117.46           C  
ANISOU  177  CB  ILE A 118    12437  16306  15887    383   -176   -259       C  
ATOM    178  CG1 ILE A 118      45.454  75.848  60.906  1.00121.23           C  
ANISOU  178  CG1 ILE A 118    13097  16409  16557    177   -232   -254       C  
ATOM    179  CG2 ILE A 118      45.329  74.984  63.257  1.00110.67           C  
ANISOU  179  CG2 ILE A 118    11566  15482  15002    287    -41   -129       C  
ATOM    180  CD1 ILE A 118      46.945  76.042  61.016  1.00124.18           C  
ANISOU  180  CD1 ILE A 118    13694  16458  17030    170   -280   -272       C  
ATOM    181  N   LEU A 119      42.289  76.059  64.280  1.00124.23           N  
ANISOU  181  N   LEU A 119    12736  18190  16275    786    -38   -218       N  
ATOM    182  CA  LEU A 119      41.557  75.667  65.476  1.00128.89           C  
ANISOU  182  CA  LEU A 119    13066  19260  16648    900     87   -109       C  
ATOM    183  C   LEU A 119      40.195  75.082  65.125  1.00133.60           C  
ANISOU  183  C   LEU A 119    13366  20209  17186    750    176     44       C  
ATOM    184  O   LEU A 119      39.713  74.177  65.816  1.00135.73           O  
ANISOU  184  O   LEU A 119    13409  20796  17365    627    322    263       O  
ATOM    185  CB  LEU A 119      41.405  76.875  66.400  1.00134.14           C  
ANISOU  185  CB  LEU A 119    13718  20149  17099   1370    -19   -315       C  
ATOM    186  CG  LEU A 119      42.717  77.384  67.004  1.00137.01           C  
ANISOU  186  CG  LEU A 119    14341  20215  17503   1528   -116   -446       C  
ATOM    187  CD1 LEU A 119      42.548  78.789  67.566  1.00142.36           C  
ANISOU  187  CD1 LEU A 119    15067  21001  18020   2003   -311   -711       C  
ATOM    188  CD2 LEU A 119      43.234  76.431  68.073  1.00136.62           C  
ANISOU  188  CD2 LEU A 119    14239  20279  17390   1440     45   -279       C  
ATOM    189  N   GLU A 120      39.566  75.573  64.052  1.00135.70           N  
ANISOU  189  N   GLU A 120    13625  20427  17509    745     83    -50       N  
ATOM    190  CA  GLU A 120      38.299  75.002  63.603  1.00139.98           C  
ANISOU  190  CA  GLU A 120    13891  21273  18022    574    149     94       C  
ATOM    191  C   GLU A 120      38.485  73.574  63.106  1.00130.60           C  
ANISOU  191  C   GLU A 120    12698  19899  17027    117    236    325       C  
ATOM    192  O   GLU A 120      37.733  72.669  63.488  1.00130.66           O  
ANISOU  192  O   GLU A 120    12445  20211  16987    -67    341    556       O  
ATOM    193  CB  GLU A 120      37.686  75.868  62.501  1.00148.59           C  
ANISOU  193  CB  GLU A 120    15007  22308  19142    676     13    -76       C  
ATOM    194  CG  GLU A 120      37.269  77.259  62.936  1.00158.49           C  
ANISOU  194  CG  GLU A 120    16240  23779  20199   1139   -106   -306       C  
ATOM    195  CD  GLU A 120      36.751  78.097  61.782  1.00163.58           C  
ANISOU  195  CD  GLU A 120    16943  24313  20896   1222   -257   -466       C  
ATOM    196  OE1 GLU A 120      36.656  77.566  60.654  1.00164.28           O  
ANISOU  196  OE1 GLU A 120    17062  24199  21158    921   -251   -391       O  
ATOM    197  OE2 GLU A 120      36.441  79.286  62.001  1.00166.27           O  
ANISOU  197  OE2 GLU A 120    17307  24766  21101   1604   -396   -674       O  
ATOM    198  N   VAL A 121      39.478  73.355  62.240  1.00118.12           N  
ANISOU  198  N   VAL A 121    11396  17822  15660    -65    177    274       N  
ATOM    199  CA  VAL A 121      39.702  72.024  61.685  1.00108.36           C  
ANISOU  199  CA  VAL A 121    10191  16371  14608   -462    221    453       C  
ATOM    200  C   VAL A 121      40.072  71.045  62.789  1.00108.98           C  
ANISOU  200  C   VAL A 121    10210  16536  14661   -589    340    658       C  
ATOM    201  O   VAL A 121      39.714  69.862  62.730  1.00115.17           O  
ANISOU  201  O   VAL A 121    10879  17351  15530   -896    384    877       O  
ATOM    202  CB  VAL A 121      40.791  72.067  60.591  1.00 98.22           C  
ANISOU  202  CB  VAL A 121     9224  14577  13520   -564    132    335       C  
ATOM    203  CG1 VAL A 121      40.989  70.685  59.974  1.00 93.15           C  
ANISOU  203  CG1 VAL A 121     8626  13715  13053   -932    146    486       C  
ATOM    204  CG2 VAL A 121      40.458  73.103  59.527  1.00 94.98           C  
ANISOU  204  CG2 VAL A 121     8873  14090  13123   -426     10    151       C  
ATOM    205  N   ALA A 122      40.782  71.518  63.816  1.00104.22           N  
ANISOU  205  N   ALA A 122     9684  15967  13946   -357    374    596       N  
ATOM    206  CA  ALA A 122      41.200  70.630  64.895  1.00104.10           C  
ANISOU  206  CA  ALA A 122     9625  16033  13895   -456    487    789       C  
ATOM    207  C   ALA A 122      40.000  70.057  65.638  1.00110.66           C  
ANISOU  207  C   ALA A 122    10094  17372  14579   -521    592   1032       C  
ATOM    208  O   ALA A 122      40.008  68.885  66.033  1.00113.26           O  
ANISOU  208  O   ALA A 122    10341  17729  14965   -791    665   1289       O  
ATOM    209  CB  ALA A 122      42.125  71.371  65.859  1.00104.40           C  
ANISOU  209  CB  ALA A 122     9804  16043  13820   -152    488    651       C  
ATOM    210  N   ARG A 123      38.958  70.867  65.835  1.00114.16           N  
ANISOU  210  N   ARG A 123    10311  18234  14831   -275    590    969       N  
ATOM    211  CA  ARG A 123      37.781  70.396  66.558  1.00127.32           C  
ANISOU  211  CA  ARG A 123    11591  20458  16328   -313    697   1218       C  
ATOM    212  C   ARG A 123      37.111  69.248  65.815  1.00131.39           C  
ANISOU  212  C   ARG A 123    11966  20932  17023   -753    693   1462       C  
ATOM    213  O   ARG A 123      36.906  68.161  66.369  1.00136.00           O  
ANISOU  213  O   ARG A 123    12388  21658  17629  -1013    769   1769       O  
ATOM    214  CB  ARG A 123      36.793  71.545  66.770  1.00135.75           C  
ANISOU  214  CB  ARG A 123    12450  21982  17149     67    676   1069       C  
ATOM    215  CG  ARG A 123      37.376  72.805  67.397  1.00138.81           C  
ANISOU  215  CG  ARG A 123    12997  22376  17369    537    617    781       C  
ATOM    216  CD  ARG A 123      36.451  73.984  67.145  1.00144.44           C  
ANISOU  216  CD  ARG A 123    13591  23376  17913    884    527    571       C  
ATOM    217  NE  ARG A 123      36.003  73.992  65.755  1.00149.23           N  
ANISOU  217  NE  ARG A 123    14236  23762  18704    676    443    528       N  
ATOM    218  CZ  ARG A 123      35.138  74.860  65.237  1.00151.43           C  
ANISOU  218  CZ  ARG A 123    14420  24225  18892    890    354    369       C  
ATOM    219  NH1 ARG A 123      34.600  75.809  65.992  1.00152.17           N  
ANISOU  219  NH1 ARG A 123    14376  24734  18707   1336    326    226       N  
ATOM    220  NH2 ARG A 123      34.802  74.767  63.957  1.00151.50           N  
ANISOU  220  NH2 ARG A 123    14474  24009  19079    675    283    345       N  
ATOM    221  N   GLN A 124      36.782  69.466  64.546  1.00131.07           N  
ANISOU  221  N   GLN A 124    11997  20680  17122   -846    585   1335       N  
ATOM    222  CA  GLN A 124      36.049  68.499  63.732  1.00136.50           C  
ANISOU  222  CA  GLN A 124    12555  21326  17982  -1230    540   1522       C  
ATOM    223  C   GLN A 124      36.865  67.244  63.402  1.00130.25           C  
ANISOU  223  C   GLN A 124    11970  20077  17442  -1601    501   1655       C  
ATOM    224  O   GLN A 124      36.433  66.436  62.568  1.00130.33           O  
ANISOU  224  O   GLN A 124    11951  19932  17636  -1919    412   1761       O  
ATOM    225  CB  GLN A 124      35.562  69.187  62.455  1.00139.39           C  
ANISOU  225  CB  GLN A 124    12972  21579  18411  -1173    424   1307       C  
ATOM    226  CG  GLN A 124      34.367  70.110  62.688  1.00140.90           C  
ANISOU  226  CG  GLN A 124    12870  22295  18370   -894    444   1253       C  
ATOM    227  CD  GLN A 124      34.416  71.368  61.839  1.00136.47           C  
ANISOU  227  CD  GLN A 124    12483  21576  17792   -615    334    923       C  
ATOM    228  OE1 GLN A 124      33.504  71.642  61.059  1.00137.39           O  
ANISOU  228  OE1 GLN A 124    12472  21820  17911   -621    270    875       O  
ATOM    229  NE2 GLN A 124      35.482  72.149  61.999  1.00129.79           N  
ANISOU  229  NE2 GLN A 124    11926  20454  16933   -372    300    706       N  
ATOM    230  N   PHE A 125      38.022  67.063  64.041  1.00126.67           N  
ANISOU  230  N   PHE A 125    11726  19405  16997  -1552    547   1642       N  
ATOM    231  CA  PHE A 125      38.798  65.838  63.911  1.00126.11           C  
ANISOU  231  CA  PHE A 125    11837  18947  17133  -1867    513   1779       C  
ATOM    232  C   PHE A 125      38.340  64.746  64.868  1.00133.19           C  
ANISOU  232  C   PHE A 125    12495  20099  18013  -2109    581   2150       C  
ATOM    233  O   PHE A 125      38.844  63.623  64.779  1.00134.17           O  
ANISOU  233  O   PHE A 125    12748  19910  18320  -2398    526   2297       O  
ATOM    234  CB  PHE A 125      40.279  66.115  64.161  1.00119.10           C  
ANISOU  234  CB  PHE A 125    11275  17716  16262  -1708    528   1607       C  
ATOM    235  CG  PHE A 125      41.024  66.596  62.954  1.00112.85           C  
ANISOU  235  CG  PHE A 125    10781  16496  15600  -1654    422   1336       C  
ATOM    236  CD1 PHE A 125      40.824  66.006  61.716  1.00115.08           C  
ANISOU  236  CD1 PHE A 125    11140  16518  16069  -1892    306   1323       C  
ATOM    237  CD2 PHE A 125      41.943  67.622  63.059  1.00105.74           C  
ANISOU  237  CD2 PHE A 125    10080  15461  14635  -1366    425   1106       C  
ATOM    238  CE1 PHE A 125      41.516  66.447  60.605  1.00110.59           C  
ANISOU  238  CE1 PHE A 125    10825  15603  15593  -1825    219   1092       C  
ATOM    239  CE2 PHE A 125      42.637  68.066  61.956  1.00104.73           C  
ANISOU  239  CE2 PHE A 125    10200  14973  14620  -1330    331    899       C  
ATOM    240  CZ  PHE A 125      42.424  67.478  60.725  1.00104.95           C  
ANISOU  240  CZ  PHE A 125    10287  14783  14807  -1552    239    896       C  
ATOM    241  N   GLU A 126      37.406  65.046  65.769  1.00135.89           N  
ANISOU  241  N   GLU A 126    12489  21008  18134  -1989    689   2312       N  
ATOM    242  CA  GLU A 126      37.015  64.158  66.869  1.00138.47           C  
ANISOU  242  CA  GLU A 126    12555  21665  18391  -2166    780   2695       C  
ATOM    243  C   GLU A 126      38.262  63.953  67.728  1.00134.11           C  
ANISOU  243  C   GLU A 126    12226  20920  17812  -2074    846   2687       C  
ATOM    244  O   GLU A 126      38.871  64.949  68.149  1.00127.81           O  
ANISOU  244  O   GLU A 126    11552  20155  16854  -1702    902   2440       O  
ATOM    245  CB  GLU A 126      36.383  62.880  66.339  1.00144.15           C  
ANISOU  245  CB  GLU A 126    13156  22273  19342  -2644    673   2991       C  
ATOM    246  CG  GLU A 126      35.514  62.160  67.356  1.00154.82           C  
ANISOU  246  CG  GLU A 126    14239  24017  20567  -2770    735   3362       C  
ATOM    247  CD  GLU A 126      35.131  60.766  66.906  1.00162.08           C  
ANISOU  247  CD  GLU A 126    15251  24606  21725  -3186    569   3578       C  
ATOM    248  OE1 GLU A 126      35.422  60.422  65.739  1.00162.72           O  
ANISOU  248  OE1 GLU A 126    15542  24222  22060  -3373    410   3436       O  
ATOM    249  OE2 GLU A 126      34.547  60.015  67.713  1.00163.40           O  
ANISOU  249  OE2 GLU A 126    15284  24980  21821  -3310    581   3885       O  
ATOM    250  N   MET A 127      38.669  62.708  68.007  1.00137.34           N  
ANISOU  250  N   MET A 127    12695  21114  18374  -2393    823   2943       N  
ATOM    251  CA  MET A 127      39.858  62.394  68.797  1.00138.50           C  
ANISOU  251  CA  MET A 127    13055  21060  18508  -2331    877   2954       C  
ATOM    252  C   MET A 127      39.745  62.945  70.215  1.00142.78           C  
ANISOU  252  C   MET A 127    13388  22124  18739  -2026   1046   3036       C  
ATOM    253  O   MET A 127      38.729  63.548  70.576  1.00146.91           O  
ANISOU  253  O   MET A 127    13594  23178  19047  -1855   1120   3087       O  
ATOM    254  CB  MET A 127      41.125  62.930  68.114  1.00135.35           C  
ANISOU  254  CB  MET A 127    13068  20151  18209  -2163    812   2578       C  
ATOM    255  CG  MET A 127      41.324  62.463  66.667  1.00133.68           C  
ANISOU  255  CG  MET A 127    13078  19447  18269  -2400    646   2459       C  
ATOM    256  SD  MET A 127      42.604  63.362  65.742  1.00124.22           S  
ANISOU  256  SD  MET A 127    12280  17785  17133  -2155    584   2026       S  
ATOM    257  CE  MET A 127      44.055  63.095  66.751  1.00118.34           C  
ANISOU  257  CE  MET A 127    11756  16854  16352  -2051    655   2029       C  
ATOM    258  N   ARG A 128      40.776  62.732  71.035  1.00144.21           N  
ANISOU  258  N   ARG A 128    13738  22179  18878  -1937   1103   3046       N  
ATOM    259  CA  ARG A 128      40.796  63.210  72.412  1.00148.26           C  
ANISOU  259  CA  ARG A 128    14085  23161  19088  -1623   1251   3106       C  
ATOM    260  C   ARG A 128      41.522  64.544  72.545  1.00150.62           C  
ANISOU  260  C   ARG A 128    14585  23398  19246  -1167   1255   2697       C  
ATOM    261  O   ARG A 128      41.982  64.890  73.638  1.00154.12           O  
ANISOU  261  O   ARG A 128    15022  24051  19485   -891   1338   2670       O  
ATOM    262  CB  ARG A 128      41.423  62.157  73.334  1.00144.55           C  
ANISOU  262  CB  ARG A 128    13651  22633  18639  -1794   1305   3390       C  
ATOM    263  CG  ARG A 128      42.864  61.744  73.013  1.00136.86           C  
ANISOU  263  CG  ARG A 128    13099  21027  17873  -1870   1226   3230       C  
ATOM    264  CD  ARG A 128      43.885  62.566  73.798  1.00129.16           C  
ANISOU  264  CD  ARG A 128    12295  20056  16723  -1473   1294   2985       C  
ATOM    265  NE  ARG A 128      45.002  61.770  74.291  1.00125.47           N  
ANISOU  265  NE  ARG A 128    12047  19285  16342  -1574   1296   3070       N  
ATOM    266  CZ  ARG A 128      45.938  62.233  75.114  1.00118.72           C  
ANISOU  266  CZ  ARG A 128    11329  18431  15349  -1283   1351   2925       C  
ATOM    267  NH1 ARG A 128      45.888  63.488  75.539  1.00115.16           N  
ANISOU  267  NH1 ARG A 128    10827  18252  14676   -875   1390   2683       N  
ATOM    268  NH2 ARG A 128      46.921  61.438  75.519  1.00114.31           N  
ANISOU  268  NH2 ARG A 128    10962  17593  14875  -1393   1348   3016       N  
ATOM    269  N   ILE A 129      41.593  65.311  71.458  1.00143.79           N  
ANISOU  269  N   ILE A 129    13887  22263  18485  -1083   1151   2388       N  
ATOM    270  CA  ILE A 129      42.463  66.480  71.377  1.00136.02           C  
ANISOU  270  CA  ILE A 129    13160  21070  17454   -730   1101   2010       C  
ATOM    271  C   ILE A 129      42.121  67.474  72.478  1.00127.68           C  
ANISOU  271  C   ILE A 129    11928  20513  16070   -287   1168   1918       C  
ATOM    272  O   ILE A 129      40.963  67.880  72.637  1.00129.20           O  
ANISOU  272  O   ILE A 129    11825  21184  16082   -154   1203   1966       O  
ATOM    273  CB  ILE A 129      42.351  67.124  69.993  1.00135.23           C  
ANISOU  273  CB  ILE A 129    13202  20675  17505   -738    976   1757       C  
ATOM    274  CG1 ILE A 129      42.850  66.153  68.924  1.00139.10           C  
ANISOU  274  CG1 ILE A 129    13899  20656  18295  -1122    896   1809       C  
ATOM    275  CG2 ILE A 129      43.115  68.438  69.946  1.00130.04           C  
ANISOU  275  CG2 ILE A 129    12769  19849  16790   -372    903   1400       C  
ATOM    276  CD1 ILE A 129      42.280  66.427  67.558  1.00143.37           C  
ANISOU  276  CD1 ILE A 129    14457  21048  18968  -1222    792   1686       C  
ATOM    277  N   ASN A 130      43.131  67.853  73.258  1.00117.18           N  
ANISOU  277  N   ASN A 130    10776  19091  14655    -41   1175   1779       N  
ATOM    278  CA  ASN A 130      43.044  69.034  74.108  1.00110.36           C  
ANISOU  278  CA  ASN A 130     9851  18568  13512    449   1170   1568       C  
ATOM    279  C   ASN A 130      43.188  70.265  73.224  1.00108.89           C  
ANISOU  279  C   ASN A 130     9856  18118  13397    656   1011   1202       C  
ATOM    280  O   ASN A 130      44.288  70.578  72.758  1.00104.34           O  
ANISOU  280  O   ASN A 130     9598  17050  12996    650    910   1007       O  
ATOM    281  CB  ASN A 130      44.125  68.994  75.185  1.00108.22           C  
ANISOU  281  CB  ASN A 130     9728  18239  13153    624   1201   1535       C  
ATOM    282  CG  ASN A 130      44.011  70.138  76.183  1.00111.62           C  
ANISOU  282  CG  ASN A 130    10087  19050  13274   1156   1176   1320       C  
ATOM    283  OD1 ASN A 130      43.777  71.291  75.811  1.00112.36           O  
ANISOU  283  OD1 ASN A 130    10235  19137  13320   1436   1050   1031       O  
ATOM    284  ND2 ASN A 130      44.184  69.821  77.464  1.00112.39           N  
ANISOU  284  ND2 ASN A 130    10073  19477  13155   1312   1279   1456       N  
ATOM    285  N   LEU A 131      42.076  70.965  72.988  1.00113.74           N  
ANISOU  285  N   LEU A 131    10268  19074  13874    837    982   1126       N  
ATOM    286  CA  LEU A 131      42.080  72.062  72.026  1.00119.41           C  
ANISOU  286  CA  LEU A 131    11154  19535  14680    988    819    817       C  
ATOM    287  C   LEU A 131      42.961  73.218  72.482  1.00121.11           C  
ANISOU  287  C   LEU A 131    11608  19578  14830   1381    683    499       C  
ATOM    288  O   LEU A 131      43.503  73.949  71.644  1.00120.13           O  
ANISOU  288  O   LEU A 131    11733  19038  14874   1410    527    273       O  
ATOM    289  CB  LEU A 131      40.649  72.543  71.776  1.00122.37           C  
ANISOU  289  CB  LEU A 131    11242  20354  14897   1124    815    810       C  
ATOM    290  CG  LEU A 131      39.748  71.555  71.024  1.00122.75           C  
ANISOU  290  CG  LEU A 131    11080  20490  15068    710    892   1085       C  
ATOM    291  CD1 LEU A 131      38.320  72.076  70.888  1.00125.43           C  
ANISOU  291  CD1 LEU A 131    11106  21332  15221    878    893   1081       C  
ATOM    292  CD2 LEU A 131      40.335  71.215  69.661  1.00117.39           C  
ANISOU  292  CD2 LEU A 131    10670  19205  14726    371    803   1030       C  
ATOM    293  N   ASP A 132      43.126  73.396  73.795  1.00119.09           N  
ANISOU  293  N   ASP A 132    11280  19635  14335   1682    725    488       N  
ATOM    294  CA  ASP A 132      43.927  74.512  74.283  1.00115.55           C  
ANISOU  294  CA  ASP A 132    11056  19025  13824   2073    560    175       C  
ATOM    295  C   ASP A 132      45.415  74.268  74.062  1.00108.00           C  
ANISOU  295  C   ASP A 132    10427  17494  13114   1884    507    131       C  
ATOM    296  O   ASP A 132      46.183  75.226  73.911  1.00108.39           O  
ANISOU  296  O   ASP A 132    10723  17218  13243   2074    320   -130       O  
ATOM    297  CB  ASP A 132      43.629  74.757  75.763  1.00121.25           C  
ANISOU  297  CB  ASP A 132    11595  20283  14193   2482    610    162       C  
ATOM    298  CG  ASP A 132      43.653  76.229  76.126  1.00122.26           C  
ANISOU  298  CG  ASP A 132    11829  20461  14162   3012    389   -211       C  
ATOM    299  OD1 ASP A 132      44.586  76.933  75.684  1.00122.95           O  
ANISOU  299  OD1 ASP A 132    12234  20034  14446   3052    191   -445       O  
ATOM    300  OD2 ASP A 132      42.732  76.681  76.843  1.00120.06           O  
ANISOU  300  OD2 ASP A 132    11313  20741  13563   3393    397   -265       O  
ATOM    301  N   ILE A 133      45.837  73.002  74.030  1.00102.17           N  
ANISOU  301  N   ILE A 133     9692  16625  12502   1511    654    390       N  
ATOM    302  CA  ILE A 133      47.239  72.690  73.767  1.00 98.51           C  
ANISOU  302  CA  ILE A 133     9523  15642  12264   1328    613    359       C  
ATOM    303  C   ILE A 133      47.606  73.045  72.330  1.00 97.08           C  
ANISOU  303  C   ILE A 133     9546  14992  12349   1143    489    237       C  
ATOM    304  O   ILE A 133      48.694  73.573  72.064  1.00 89.27           O  
ANISOU  304  O   ILE A 133     8809  13613  11495   1184    362     75       O  
ATOM    305  CB  ILE A 133      47.525  71.208  74.079  1.00 96.37           C  
ANISOU  305  CB  ILE A 133     9203  15361  12051    994    784    666       C  
ATOM    306  CG1 ILE A 133      47.449  70.951  75.583  1.00 98.75           C  
ANISOU  306  CG1 ILE A 133     9347  16081  12091   1205    892    780       C  
ATOM    307  CG2 ILE A 133      48.889  70.797  73.557  1.00 94.93           C  
ANISOU  307  CG2 ILE A 133     9317  14635  12119    773    741    637       C  
ATOM    308  CD1 ILE A 133      47.881  69.556  75.975  1.00 98.11           C  
ANISOU  308  CD1 ILE A 133     9256  15946  12075    897   1032   1077       C  
ATOM    309  N   VAL A 134      46.704  72.770  71.383  1.00 98.22           N  
ANISOU  309  N   VAL A 134     9570  15186  12563    939    518    322       N  
ATOM    310  CA  VAL A 134      46.970  73.081  69.981  1.00 98.88           C  
ANISOU  310  CA  VAL A 134     9825  14871  12874    774    408    220       C  
ATOM    311  C   VAL A 134      47.228  74.573  69.796  1.00109.76           C  
ANISOU  311  C   VAL A 134    11348  16112  14245   1085    207    -65       C  
ATOM    312  O   VAL A 134      48.171  74.970  69.102  1.00112.47           O  
ANISOU  312  O   VAL A 134    11924  16037  14772   1019     91   -166       O  
ATOM    313  CB  VAL A 134      45.806  72.597  69.095  1.00 90.72           C  
ANISOU  313  CB  VAL A 134     8610  13978  11882    550    461    346       C  
ATOM    314  CG1 VAL A 134      46.018  73.030  67.646  1.00 74.05           C  
ANISOU  314  CG1 VAL A 134     6667  11498   9972    431    340    223       C  
ATOM    315  CG2 VAL A 134      45.645  71.086  69.198  1.00 93.90           C  
ANISOU  315  CG2 VAL A 134     8903  14433  12341    202    610    638       C  
ATOM    316  N   ASP A 135      46.400  75.422  70.414  1.00114.41           N  
ANISOU  316  N   ASP A 135    11798  17055  14619   1435    148   -190       N  
ATOM    317  CA  ASP A 135      46.566  76.863  70.233  1.00115.49           C  
ANISOU  317  CA  ASP A 135    12083  17041  14757   1743    -86   -468       C  
ATOM    318  C   ASP A 135      47.881  77.347  70.830  1.00115.77           C  
ANISOU  318  C   ASP A 135    12354  16787  14847   1885   -213   -598       C  
ATOM    319  O   ASP A 135      48.537  78.232  70.267  1.00114.87           O  
ANISOU  319  O   ASP A 135    12451  16307  14886   1932   -416   -753       O  
ATOM    320  CB  ASP A 135      45.386  77.620  70.845  1.00117.78           C  
ANISOU  320  CB  ASP A 135    12174  17798  14779   2130   -137   -591       C  
ATOM    321  CG  ASP A 135      45.350  79.089  70.430  1.00121.45           C  
ANISOU  321  CG  ASP A 135    12792  18083  15269   2424   -412   -875       C  
ATOM    322  OD1 ASP A 135      45.299  79.375  69.212  1.00119.72           O  
ANISOU  322  OD1 ASP A 135    12667  17587  15236   2252   -494   -897       O  
ATOM    323  OD2 ASP A 135      45.376  79.961  71.325  1.00124.63           O  
ANISOU  323  OD2 ASP A 135    13230  18619  15507   2835   -563  -1077       O  
ATOM    324  N   SER A 136      48.288  76.773  71.965  1.00118.72           N  
ANISOU  324  N   SER A 136    12686  17319  15101   1944   -105   -521       N  
ATOM    325  CA  SER A 136      49.562  77.153  72.566  1.00118.97           C  
ANISOU  325  CA  SER A 136    12934  17083  15187   2066   -223   -636       C  
ATOM    326  C   SER A 136      50.742  76.694  71.719  1.00109.31           C  
ANISOU  326  C   SER A 136    11912  15377  14242   1717   -221   -554       C  
ATOM    327  O   SER A 136      51.827  77.282  71.804  1.00108.44           O  
ANISOU  327  O   SER A 136    12006  14954  14244   1784   -380   -670       O  
ATOM    328  CB  SER A 136      49.660  76.587  73.982  1.00128.53           C  
ANISOU  328  CB  SER A 136    14036  18614  16184   2217    -94   -561       C  
ATOM    329  OG  SER A 136      49.325  75.212  73.999  1.00134.95           O  
ANISOU  329  OG  SER A 136    14687  19604  16984   1910    158   -273       O  
ATOM    330  N   MET A 137      50.556  75.652  70.902  1.00102.18           N  
ANISOU  330  N   MET A 137    10953  14421  13450   1355    -58   -355       N  
ATOM    331  CA  MET A 137      51.591  75.274  69.944  1.00 99.09           C  
ANISOU  331  CA  MET A 137    10744  13604  13301   1060    -69   -296       C  
ATOM    332  C   MET A 137      51.663  76.267  68.792  1.00 99.88           C  
ANISOU  332  C   MET A 137    10959  13443  13549   1058   -251   -420       C  
ATOM    333  O   MET A 137      52.757  76.643  68.358  1.00100.24           O  
ANISOU  333  O   MET A 137    11187  13145  13753    994   -365   -459       O  
ATOM    334  CB  MET A 137      51.345  73.861  69.414  1.00 96.40           C  
ANISOU  334  CB  MET A 137    10322  13281  13025    710    125    -71       C  
ATOM    335  CG  MET A 137      51.764  72.755  70.365  1.00 95.02           C  
ANISOU  335  CG  MET A 137    10116  13198  12789    624    277     87       C  
ATOM    336  SD  MET A 137      51.508  71.106  69.686  1.00 94.34           S  
ANISOU  336  SD  MET A 137     9971  13060  12813    208    439    343       S  
ATOM    337  CE  MET A 137      51.949  70.097  71.101  1.00 98.40           C  
ANISOU  337  CE  MET A 137    10446  13724  13216    200    575    511       C  
ATOM    338  N   ILE A 138      50.506  76.694  68.279  1.00 99.18           N  
ANISOU  338  N   ILE A 138    10753  13526  13406   1122   -282   -464       N  
ATOM    339  CA  ILE A 138      50.477  77.748  67.269  1.00 97.72           C  
ANISOU  339  CA  ILE A 138    10672  13119  13339   1160   -475   -585       C  
ATOM    340  C   ILE A 138      51.061  79.036  67.830  1.00105.11           C  
ANISOU  340  C   ILE A 138    11754  13905  14276   1456   -723   -780       C  
ATOM    341  O   ILE A 138      51.674  79.824  67.098  1.00105.98           O  
ANISOU  341  O   ILE A 138    12022  13692  14554   1422   -910   -835       O  
ATOM    342  CB  ILE A 138      49.039  77.956  66.760  1.00 91.00           C  
ANISOU  342  CB  ILE A 138     9651  12525  12399   1212   -462   -605       C  
ATOM    343  CG1 ILE A 138      48.408  76.613  66.393  1.00 96.02           C  
ANISOU  343  CG1 ILE A 138    10123  13332  13028    923   -235   -403       C  
ATOM    344  CG2 ILE A 138      49.028  78.876  65.553  1.00 87.16           C  
ANISOU  344  CG2 ILE A 138     9275  11787  12053   1196   -641   -692       C  
ATOM    345  CD1 ILE A 138      46.902  76.663  66.277  1.00101.71           C  
ANISOU  345  CD1 ILE A 138    10615  14418  13612    997   -192   -397       C  
ATOM    346  N   ALA A 139      50.887  79.271  69.132  1.00107.72           N  
ANISOU  346  N   ALA A 139    12033  14471  14423   1750   -747   -878       N  
ATOM    347  CA  ALA A 139      51.508  80.424  69.774  1.00117.82           C  
ANISOU  347  CA  ALA A 139    13469  15590  15707   2045  -1012  -1079       C  
ATOM    348  C   ALA A 139      53.026  80.297  69.772  1.00119.60           C  
ANISOU  348  C   ALA A 139    13878  15448  16116   1879  -1063  -1028       C  
ATOM    349  O   ALA A 139      53.735  81.207  69.326  1.00121.87           O  
ANISOU  349  O   ALA A 139    14333  15398  16573   1886  -1303  -1103       O  
ATOM    350  CB  ALA A 139      50.980  80.578  71.200  1.00126.93           C  
ANISOU  350  CB  ALA A 139    14514  17122  16591   2419  -1010  -1197       C  
ATOM    351  N   SER A 140      53.544  79.169  70.269  1.00121.73           N  
ANISOU  351  N   SER A 140    14112  15783  16357   1724   -850   -887       N  
ATOM    352  CA  SER A 140      54.988  78.964  70.261  1.00115.66           C  
ANISOU  352  CA  SER A 140    13499  14698  15749   1567   -882   -831       C  
ATOM    353  C   SER A 140      55.534  78.897  68.839  1.00107.86           C  
ANISOU  353  C   SER A 140    12593  13404  14983   1257   -895   -720       C  
ATOM    354  O   SER A 140      56.693  79.260  68.600  1.00111.20           O  
ANISOU  354  O   SER A 140    13155  13531  15564   1178  -1023   -709       O  
ATOM    355  CB  SER A 140      55.345  77.694  71.033  1.00117.72           C  
ANISOU  355  CB  SER A 140    13699  15106  15921   1466   -644   -695       C  
ATOM    356  OG  SER A 140      56.728  77.657  71.346  1.00121.31           O  
ANISOU  356  OG  SER A 140    14301  15308  16484   1416   -706   -689       O  
ATOM    357  N   ALA A 141      54.713  78.450  67.884  1.00 98.50           N  
ANISOU  357  N   ALA A 141    11311  12307  13805   1089   -772   -633       N  
ATOM    358  CA  ALA A 141      55.144  78.410  66.490  1.00 94.24           C  
ANISOU  358  CA  ALA A 141    10838  11523  13446    832   -787   -537       C  
ATOM    359  C   ALA A 141      55.367  79.811  65.941  1.00113.65           C  
ANISOU  359  C   ALA A 141    13405  13753  16025    927  -1066   -632       C  
ATOM    360  O   ALA A 141      56.271  80.032  65.126  1.00116.88           O  
ANISOU  360  O   ALA A 141    13908  13904  16599    758  -1142   -549       O  
ATOM    361  CB  ALA A 141      54.112  77.671  65.640  1.00 77.47           C  
ANISOU  361  CB  ALA A 141     8586   9559  11289    667   -621   -449       C  
ATOM    362  N   ILE A 142      54.552  80.767  66.376  1.00124.62           N  
ANISOU  362  N   ILE A 142    14778  15245  17329   1203  -1231   -796       N  
ATOM    363  CA  ILE A 142      54.645  82.122  65.853  1.00130.40           C  
ANISOU  363  CA  ILE A 142    15622  15743  18182   1302  -1531   -887       C  
ATOM    364  C   ILE A 142      55.629  82.977  66.653  1.00133.26           C  
ANISOU  364  C   ILE A 142    16133  15880  18621   1461  -1791   -987       C  
ATOM    365  O   ILE A 142      56.303  83.839  66.079  1.00129.96           O  
ANISOU  365  O   ILE A 142    15837  15154  18389   1397  -2030   -964       O  
ATOM    366  CB  ILE A 142      53.242  82.750  65.811  1.00129.39           C  
ANISOU  366  CB  ILE A 142    15414  15819  17928   1534  -1612  -1027       C  
ATOM    367  CG1 ILE A 142      52.348  81.953  64.855  1.00122.91           C  
ANISOU  367  CG1 ILE A 142    14451  15178  17072   1335  -1385   -911       C  
ATOM    368  CG2 ILE A 142      53.313  84.206  65.385  1.00133.93           C  
ANISOU  368  CG2 ILE A 142    16126  16133  18627   1672  -1964  -1138       C  
ATOM    369  CD1 ILE A 142      50.906  82.403  64.832  1.00121.98           C  
ANISOU  369  CD1 ILE A 142    14216  15321  16809   1547  -1422  -1030       C  
ATOM    370  N   GLU A 143      55.749  82.743  67.962  1.00137.06           N  
ANISOU  370  N   GLU A 143    16602  16507  18967   1658  -1761  -1082       N  
ATOM    371  CA  GLU A 143      56.709  83.500  68.761  1.00148.43           C  
ANISOU  371  CA  GLU A 143    18187  17730  20481   1814  -2021  -1189       C  
ATOM    372  C   GLU A 143      58.134  83.247  68.287  1.00160.73           C  
ANISOU  372  C   GLU A 143    19829  18997  22245   1520  -2022  -1017       C  
ATOM    373  O   GLU A 143      58.851  84.177  67.902  1.00164.06           O  
ANISOU  373  O   GLU A 143    20370  19108  22858   1476  -2298  -1007       O  
ATOM    374  CB  GLU A 143      56.572  83.147  70.244  1.00148.81           C  
ANISOU  374  CB  GLU A 143    18189  18034  20318   2080  -1950  -1310       C  
ATOM    375  CG  GLU A 143      57.760  83.624  71.076  1.00151.87           C  
ANISOU  375  CG  GLU A 143    18722  18195  20788   2185  -2169  -1391       C  
ATOM    376  CD  GLU A 143      57.499  83.592  72.570  1.00156.07           C  
ANISOU  376  CD  GLU A 143    19226  18986  21088   2545  -2179  -1567       C  
ATOM    377  OE1 GLU A 143      56.732  82.719  73.027  1.00157.51           O  
ANISOU  377  OE1 GLU A 143    19247  19548  21050   2599  -1899  -1526       O  
ATOM    378  OE2 GLU A 143      58.063  84.447  73.288  1.00157.03           O  
ANISOU  378  OE2 GLU A 143    19481  18937  21247   2776  -2482  -1737       O  
ATOM    379  N   ASN A 144      58.564  81.985  68.316  1.00168.46           N  
ANISOU  379  N   ASN A 144    20742  20081  23186   1318  -1727   -871       N  
ATOM    380  CA  ASN A 144      59.903  81.624  67.867  1.00166.19           C  
ANISOU  380  CA  ASN A 144    20511  19575  23058   1059  -1697   -707       C  
ATOM    381  C   ASN A 144      60.064  81.948  66.388  1.00161.74           C  
ANISOU  381  C   ASN A 144    19957  18841  22657    826  -1749   -566       C  
ATOM    382  O   ASN A 144      59.689  81.149  65.525  1.00163.57           O  
ANISOU  382  O   ASN A 144    20109  19182  22860    646  -1527   -452       O  
ATOM    383  CB  ASN A 144      60.177  80.142  68.132  1.00167.59           C  
ANISOU  383  CB  ASN A 144    20617  19919  23142    915  -1372   -593       C  
ATOM    384  CG  ASN A 144      60.164  79.802  69.611  1.00171.66           C  
ANISOU  384  CG  ASN A 144    21121  20604  23498   1130  -1320   -696       C  
ATOM    385  OD1 ASN A 144      61.196  79.853  70.282  1.00171.84           O  
ANISOU  385  OD1 ASN A 144    21218  20510  23563   1163  -1397   -710       O  
ATOM    386  ND2 ASN A 144      58.990  79.454  70.128  1.00173.91           N  
ANISOU  386  ND2 ASN A 144    21297  21189  23592   1280  -1190   -757       N  
ATOM    387  N   ASN A 145      60.609  83.127  66.089  1.00149.76           N  
ANISOU  387  N   ASN A 145    18536  17056  21310    832  -2058   -566       N  
ATOM    388  CA  ASN A 145      60.749  83.585  64.717  1.00139.49           C  
ANISOU  388  CA  ASN A 145    17238  15605  20158    630  -2139   -414       C  
ATOM    389  C   ASN A 145      62.181  83.531  64.208  1.00134.97           C  
ANISOU  389  C   ASN A 145    16686  14852  19747    388  -2172   -207       C  
ATOM    390  O   ASN A 145      62.409  83.819  63.028  1.00138.45           O  
ANISOU  390  O   ASN A 145    17105  15207  20294    204  -2212    -39       O  
ATOM    391  CB  ASN A 145      60.209  85.017  64.581  1.00134.37           C  
ANISOU  391  CB  ASN A 145    16671  14791  19595    792  -2487   -524       C  
ATOM    392  CG  ASN A 145      58.764  85.052  64.112  1.00130.43           C  
ANISOU  392  CG  ASN A 145    16108  14475  18977    894  -2412   -611       C  
ATOM    393  OD1 ASN A 145      58.171  84.015  63.809  1.00128.17           O  
ANISOU  393  OD1 ASN A 145    15708  14428  18562    813  -2106   -569       O  
ATOM    394  ND2 ASN A 145      58.188  86.249  64.059  1.00129.31           N  
ANISOU  394  ND2 ASN A 145    16039  14211  18881   1076  -2713   -734       N  
ATOM    395  N   LYS A 146      63.145  83.173  65.057  1.00120.97           N  
ANISOU  395  N   LYS A 146    14939  13045  17981    391  -2154   -204       N  
ATOM    396  CA  LYS A 146      64.541  83.036  64.639  1.00107.61           C  
ANISOU  396  CA  LYS A 146    13239  11228  16419    169  -2165      0       C  
ATOM    397  C   LYS A 146      64.660  81.846  63.694  1.00 97.72           C  
ANISOU  397  C   LYS A 146    11890  10146  15093    -30  -1841    158       C  
ATOM    398  O   LYS A 146      64.814  80.702  64.127  1.00101.99           O  
ANISOU  398  O   LYS A 146    12402  10832  15516    -35  -1597    142       O  
ATOM    399  CB  LYS A 146      65.451  82.872  65.851  1.00104.36           C  
ANISOU  399  CB  LYS A 146    12875  10767  16011    249  -2214    -61       C  
ATOM    400  CG  LYS A 146      65.394  84.028  66.838  1.00110.41           C  
ANISOU  400  CG  LYS A 146    13751  11356  16844    476  -2566   -244       C  
ATOM    401  CD  LYS A 146      66.032  85.296  66.275  1.00110.10           C  
ANISOU  401  CD  LYS A 146    13769  11014  17051    365  -2935   -129       C  
ATOM    402  CE  LYS A 146      67.537  85.141  66.100  1.00 98.77           C  
ANISOU  402  CE  LYS A 146    12299   9476  15753    135  -2959     89       C  
ATOM    403  NZ  LYS A 146      68.154  86.374  65.536  1.00 87.76           N  
ANISOU  403  NZ  LYS A 146    10936   7796  14611     -8  -3331    249       N  
ATOM    404  N   VAL A 147      64.585  82.111  62.394  1.00 87.28           N  
ANISOU  404  N   VAL A 147    10523   8804  13835   -182  -1853    308       N  
ATOM    405  CA  VAL A 147      64.685  81.082  61.367  1.00 78.26           C  
ANISOU  405  CA  VAL A 147     9298   7820  12619   -343  -1587    444       C  
ATOM    406  C   VAL A 147      65.904  81.380  60.512  1.00 82.00           C  
ANISOU  406  C   VAL A 147     9725   8224  13206   -531  -1660    687       C  
ATOM    407  O   VAL A 147      66.088  82.515  60.060  1.00 90.66           O  
ANISOU  407  O   VAL A 147    10829   9172  14445   -586  -1907    792       O  
ATOM    408  CB  VAL A 147      63.420  81.014  60.496  1.00 70.90           C  
ANISOU  408  CB  VAL A 147     8327   6993  11618   -337  -1507    408       C  
ATOM    409  CG1 VAL A 147      63.611  80.004  59.378  1.00 57.63           C  
ANISOU  409  CG1 VAL A 147     6573   5456   9868   -489  -1276    540       C  
ATOM    410  CG2 VAL A 147      62.218  80.648  61.349  1.00 84.43           C  
ANISOU  410  CG2 VAL A 147    10049   8827  13204   -162  -1417    198       C  
ATOM    411  N   ALA A 148      66.725  80.362  60.284  1.00 78.44           N  
ANISOU  411  N   ALA A 148     9220   7894  12689   -625  -1456    788       N  
ATOM    412  CA  ALA A 148      67.947  80.536  59.518  1.00 76.06           C  
ANISOU  412  CA  ALA A 148     8844   7597  12461   -786  -1496   1033       C  
ATOM    413  C   ALA A 148      67.674  80.408  58.025  1.00 74.27           C  
ANISOU  413  C   ALA A 148     8534   7501  12186   -885  -1405   1177       C  
ATOM    414  O   ALA A 148      66.871  79.579  57.590  1.00 67.76           O  
ANISOU  414  O   ALA A 148     7704   6811  11232   -847  -1211   1087       O  
ATOM    415  CB  ALA A 148      68.997  79.514  59.953  1.00 75.12           C  
ANISOU  415  CB  ALA A 148     8699   7574  12270   -805  -1328   1066       C  
ATOM    416  N   THR A 149      68.353  81.247  57.243  1.00 80.57           N  
ANISOU  416  N   THR A 149     9260   8262  13092  -1014  -1562   1414       N  
ATOM    417  CA  THR A 149      68.240  81.209  55.790  1.00 80.97           C  
ANISOU  417  CA  THR A 149     9214   8464  13087  -1103  -1489   1587       C  
ATOM    418  C   THR A 149      69.102  80.103  55.191  1.00 71.17           C  
ANISOU  418  C   THR A 149     7874   7465  11702  -1142  -1258   1701       C  
ATOM    419  O   THR A 149      68.687  79.436  54.236  1.00 66.59           O  
ANISOU  419  O   THR A 149     7252   7063  10985  -1124  -1093   1701       O  
ATOM    420  CB  THR A 149      68.630  82.576  55.214  1.00 93.61           C  
ANISOU  420  CB  THR A 149    10765   9945  14857  -1230  -1762   1830       C  
ATOM    421  OG1 THR A 149      67.570  83.516  55.444  1.00 98.16           O  
ANISOU  421  OG1 THR A 149    11443  10323  15531  -1161  -1966   1702       O  
ATOM    422  CG2 THR A 149      68.946  82.495  53.723  1.00 97.35           C  
ANISOU  422  CG2 THR A 149    11096  10634  15258  -1340  -1675   2089       C  
ATOM    423  N   GLU A 150      70.291  79.887  55.747  1.00 71.31           N  
ANISOU  423  N   GLU A 150     7856   7496  11741  -1177  -1256   1782       N  
ATOM    424  CA  GLU A 150      71.271  78.957  55.208  1.00 82.83           C  
ANISOU  424  CA  GLU A 150     9211   9196  13064  -1195  -1072   1905       C  
ATOM    425  C   GLU A 150      71.806  78.081  56.333  1.00 84.05           C  
ANISOU  425  C   GLU A 150     9429   9335  13173  -1117   -969   1761       C  
ATOM    426  O   GLU A 150      71.472  78.261  57.507  1.00 82.88           O  
ANISOU  426  O   GLU A 150     9389   9002  13099  -1061  -1043   1592       O  
ATOM    427  CB  GLU A 150      72.426  79.703  54.528  1.00 99.30           C  
ANISOU  427  CB  GLU A 150    11136  11376  15219  -1340  -1192   2244       C  
ATOM    428  CG  GLU A 150      73.238  80.577  55.480  1.00105.26           C  
ANISOU  428  CG  GLU A 150    11893  11932  16171  -1427  -1424   2335       C  
ATOM    429  CD  GLU A 150      73.997  81.681  54.768  1.00108.65           C  
ANISOU  429  CD  GLU A 150    12171  12377  16735  -1615  -1630   2696       C  
ATOM    430  OE1 GLU A 150      74.333  81.495  53.578  1.00111.84           O  
ANISOU  430  OE1 GLU A 150    12419  13051  17024  -1668  -1523   2919       O  
ATOM    431  OE2 GLU A 150      74.271  82.726  55.402  1.00102.87           O  
ANISOU  431  OE2 GLU A 150    11472  11394  16221  -1706  -1912   2763       O  
ATOM    432  N   ILE A 151      72.657  77.128  55.964  1.00 79.64           N  
ANISOU  432  N   ILE A 151     8797   8987  12475  -1096   -803   1828       N  
ATOM    433  CA  ILE A 151      73.352  76.266  56.913  1.00 68.09           C  
ANISOU  433  CA  ILE A 151     7379   7532  10959  -1026   -708   1728       C  
ATOM    434  C   ILE A 151      74.845  76.403  56.646  1.00 80.26           C  
ANISOU  434  C   ILE A 151     8770   9229  12495  -1092   -734   1970       C  
ATOM    435  O   ILE A 151      75.303  76.154  55.523  1.00 83.92           O  
ANISOU  435  O   ILE A 151     9103   9943  12841  -1102   -651   2135       O  
ATOM    436  CB  ILE A 151      72.902  74.801  56.792  1.00 57.13           C  
ANISOU  436  CB  ILE A 151     6066   6249   9392   -905   -485   1545       C  
ATOM    437  CG1 ILE A 151      71.552  74.582  57.477  1.00 54.45           C  
ANISOU  437  CG1 ILE A 151     5867   5747   9073   -850   -465   1311       C  
ATOM    438  CG2 ILE A 151      73.932  73.885  57.381  1.00 48.29           C  
ANISOU  438  CG2 ILE A 151     4953   5203   8190   -840   -389   1522       C  
ATOM    439  CD1 ILE A 151      71.018  73.166  57.319  1.00 54.92           C  
ANISOU  439  CD1 ILE A 151     6000   5880   8988   -767   -283   1157       C  
ATOM    440  N   LEU A 152      75.601  76.803  57.671  1.00 89.09           N  
ANISOU  440  N   LEU A 152     9895  10224  13729  -1127   -853   1994       N  
ATOM    441  CA  LEU A 152      77.018  77.087  57.498  1.00 89.72           C  
ANISOU  441  CA  LEU A 152     9811  10443  13835  -1216   -913   2248       C  
ATOM    442  C   LEU A 152      77.867  76.058  58.227  1.00 90.07           C  
ANISOU  442  C   LEU A 152     9873  10576  13773  -1114   -783   2158       C  
ATOM    443  O   LEU A 152      77.670  75.831  59.431  1.00 84.95           O  
ANISOU  443  O   LEU A 152     9364   9744  13169  -1045   -799   1957       O  
ATOM    444  CB  LEU A 152      77.351  78.496  58.004  1.00101.00           C  
ANISOU  444  CB  LEU A 152    11212  11652  15510  -1362  -1209   2390       C  
ATOM    445  CG  LEU A 152      76.853  79.645  57.120  1.00108.90           C  
ANISOU  445  CG  LEU A 152    12154  12590  16631  -1495  -1382   2574       C  
ATOM    446  CD1 LEU A 152      77.380  80.990  57.604  1.00117.45           C  
ANISOU  446  CD1 LEU A 152    13208  13443  17974  -1652  -1716   2743       C  
ATOM    447  CD2 LEU A 152      77.216  79.417  55.656  1.00107.49           C  
ANISOU  447  CD2 LEU A 152    11788  12744  16311  -1546  -1254   2826       C  
ATOM    448  N   PRO A 153      78.814  75.427  57.537  1.00 91.04           N  
ANISOU  448  N   PRO A 153     9854  10996  13742  -1084   -658   2301       N  
ATOM    449  CA  PRO A 153      79.659  74.407  58.166  1.00 87.95           C  
ANISOU  449  CA  PRO A 153     9480  10702  13234   -967   -538   2214       C  
ATOM    450  C   PRO A 153      80.635  75.027  59.148  1.00 77.09           C  
ANISOU  450  C   PRO A 153     8055   9228  12008  -1049   -695   2307       C  
ATOM    451  O   PRO A 153      80.858  76.246  59.127  1.00 79.30           O  
ANISOU  451  O   PRO A 153     8248   9409  12474  -1213   -907   2495       O  
ATOM    452  CB  PRO A 153      80.397  73.786  56.971  1.00 93.58           C  
ANISOU  452  CB  PRO A 153    10023  11797  13737   -903   -398   2372       C  
ATOM    453  CG  PRO A 153      80.464  74.900  55.977  1.00 96.44           C  
ANISOU  453  CG  PRO A 153    10204  12267  14172  -1061   -511   2664       C  
ATOM    454  CD  PRO A 153      79.142  75.612  56.113  1.00 95.43           C  
ANISOU  454  CD  PRO A 153    10219  11839  14200  -1133   -619   2551       C  
ATOM    455  N   PRO A 154      81.238  74.226  60.026  1.00 72.04           N  
ANISOU  455  N   PRO A 154     7475   8597  11301   -940   -620   2182       N  
ATOM    456  CA  PRO A 154      82.323  74.752  60.862  1.00 73.13           C  
ANISOU  456  CA  PRO A 154     7538   8686  11561  -1011   -767   2288       C  
ATOM    457  C   PRO A 154      83.517  75.135  60.002  1.00 76.45           C  
ANISOU  457  C   PRO A 154     7689   9399  11960  -1120   -804   2626       C  
ATOM    458  O   PRO A 154      83.849  74.451  59.030  1.00 77.80           O  
ANISOU  458  O   PRO A 154     7743   9889  11927  -1042   -636   2712       O  
ATOM    459  CB  PRO A 154      82.650  73.587  61.808  1.00 63.26           C  
ANISOU  459  CB  PRO A 154     6409   7437  10190   -838   -631   2074       C  
ATOM    460  CG  PRO A 154      82.153  72.370  61.106  1.00 69.94           C  
ANISOU  460  CG  PRO A 154     7319   8435  10819   -693   -407   1952       C  
ATOM    461  CD  PRO A 154      80.952  72.810  60.314  1.00 73.58           C  
ANISOU  461  CD  PRO A 154     7814   8828  11317   -754   -418   1943       C  
ATOM    462  N   VAL A 155      84.146  76.259  60.355  1.00 75.32           N  
ANISOU  462  N   VAL A 155     7439   9152  12027  -1298  -1042   2825       N  
ATOM    463  CA  VAL A 155      85.269  76.759  59.570  1.00 85.81           C  
ANISOU  463  CA  VAL A 155     8478  10761  13364  -1446  -1107   3202       C  
ATOM    464  C   VAL A 155      86.379  75.723  59.563  1.00 85.35           C  
ANISOU  464  C   VAL A 155     8299  11038  13092  -1311   -927   3230       C  
ATOM    465  O   VAL A 155      86.759  75.189  60.613  1.00 85.46           O  
ANISOU  465  O   VAL A 155     8416  10960  13095  -1208   -907   3048       O  
ATOM    466  CB  VAL A 155      85.764  78.101  60.129  1.00 91.58           C  
ANISOU  466  CB  VAL A 155     9138  11266  14392  -1673  -1436   3397       C  
ATOM    467  CG1 VAL A 155      86.708  78.758  59.144  1.00 91.97           C  
ANISOU  467  CG1 VAL A 155     8869  11602  14475  -1877  -1523   3848       C  
ATOM    468  CG2 VAL A 155      84.590  79.017  60.442  1.00 95.75           C  
ANISOU  468  CG2 VAL A 155     9857  11397  15126  -1737  -1637   3267       C  
ATOM    469  N   GLU A 156      86.899  75.424  58.375  1.00 81.03           N  
ANISOU  469  N   GLU A 156     7530  10902  12354  -1288   -797   3452       N  
ATOM    470  CA  GLU A 156      87.946  74.422  58.262  1.00 79.09           C  
ANISOU  470  CA  GLU A 156     7159  11020  11871  -1120   -628   3472       C  
ATOM    471  C   GLU A 156      89.304  75.054  58.533  1.00 79.29           C  
ANISOU  471  C   GLU A 156     6926  11205  11996  -1276   -772   3781       C  
ATOM    472  O   GLU A 156      89.583  76.178  58.106  1.00 83.98           O  
ANISOU  472  O   GLU A 156     7324  11827  12756  -1522   -951   4114       O  
ATOM    473  CB  GLU A 156      87.929  73.758  56.883  1.00 84.91           C  
ANISOU  473  CB  GLU A 156     7767  12173  12322   -972   -429   3549       C  
ATOM    474  CG  GLU A 156      88.258  74.670  55.719  1.00101.80           C  
ANISOU  474  CG  GLU A 156     9610  14600  14468  -1147   -494   3959       C  
ATOM    475  CD  GLU A 156      88.797  73.911  54.513  1.00111.10           C  
ANISOU  475  CD  GLU A 156    10578  16334  15302   -949   -294   4081       C  
ATOM    476  OE1 GLU A 156      89.542  72.922  54.709  1.00104.93           O  
ANISOU  476  OE1 GLU A 156     9769  15789  14310   -730   -165   3972       O  
ATOM    477  OE2 GLU A 156      88.479  74.310  53.369  1.00117.97           O  
ANISOU  477  OE2 GLU A 156    11311  17414  16100   -994   -274   4281       O  
ATOM    478  N   THR A 157      90.137  74.332  59.272  1.00 73.03           N  
ANISOU  478  N   THR A 157     6135  10500  11113  -1144   -710   3676       N  
ATOM    479  CA  THR A 157      91.483  74.764  59.603  1.00 80.90           C  
ANISOU  479  CA  THR A 157     6884  11675  12180  -1265   -830   3942       C  
ATOM    480  C   THR A 157      92.483  73.956  58.783  1.00 89.12           C  
ANISOU  480  C   THR A 157     7667  13288  12908  -1099   -634   4099       C  
ATOM    481  O   THR A 157      92.113  73.091  57.985  1.00 92.11           O  
ANISOU  481  O   THR A 157     8083  13892  13024   -879   -427   3981       O  
ATOM    482  CB  THR A 157      91.743  74.622  61.106  1.00 72.65           C  
ANISOU  482  CB  THR A 157     6017  10322  11266  -1228   -927   3712       C  
ATOM    483  OG1 THR A 157      91.607  73.251  61.495  1.00 68.39           O  
ANISOU  483  OG1 THR A 157     5667   9819  10499   -934   -708   3382       O  
ATOM    484  CG2 THR A 157      90.758  75.468  61.900  1.00 66.74           C  
ANISOU  484  CG2 THR A 157     5506   9050  10800  -1356  -1135   3553       C  
ATOM    485  N   LEU A 158      93.766  74.247  58.982  1.00 89.80           N  
ANISOU  485  N   LEU A 158     7484  13620  13016  -1192   -715   4365       N  
ATOM    486  CA  LEU A 158      94.826  73.549  58.268  1.00100.17           C  
ANISOU  486  CA  LEU A 158     8514  15525  14020  -1021   -545   4536       C  
ATOM    487  C   LEU A 158      95.366  72.423  59.138  1.00107.88           C  
ANISOU  487  C   LEU A 158     9622  16525  14844   -755   -435   4243       C  
ATOM    488  O   LEU A 158      95.665  72.628  60.320  1.00111.17           O  
ANISOU  488  O   LEU A 158    10136  16655  15447   -830   -568   4149       O  
ATOM    489  CB  LEU A 158      95.950  74.504  57.860  1.00104.36           C  
ANISOU  489  CB  LEU A 158     8622  16392  14637  -1280   -687   5048       C  
ATOM    490  CG  LEU A 158      95.528  75.737  57.053  1.00109.76           C  
ANISOU  490  CG  LEU A 158     9204  17010  15488  -1571   -840   5375       C  
ATOM    491  CD1 LEU A 158      96.495  76.884  57.286  1.00112.25           C  
ANISOU  491  CD1 LEU A 158     9444  17247  15958  -1830  -1094   5693       C  
ATOM    492  CD2 LEU A 158      95.401  75.446  55.569  1.00111.56           C  
ANISOU  492  CD2 LEU A 158     9308  17688  15394  -1429   -650   5518       C  
ATOM    493  N   ARG A 159      95.474  71.234  58.549  1.00117.89           N  
ANISOU  493  N   ARG A 159    10903  18123  15768   -430   -210   4090       N  
ATOM    494  CA  ARG A 159      95.892  70.027  59.246  1.00116.91           C  
ANISOU  494  CA  ARG A 159    10933  18021  15466   -135    -99   3790       C  
ATOM    495  C   ARG A 159      96.891  69.269  58.385  1.00123.69           C  
ANISOU  495  C   ARG A 159    11526  19512  15958    129     56   3908       C  
ATOM    496  O   ARG A 159      96.769  69.245  57.157  1.00132.13           O  
ANISOU  496  O   ARG A 159    12432  20937  16834    203    147   4054       O  
ATOM    497  CB  ARG A 159      94.690  69.117  59.562  1.00115.28           C  
ANISOU  497  CB  ARG A 159    11143  17441  15217     57     -5   3353       C  
ATOM    498  CG  ARG A 159      93.468  69.845  60.116  1.00120.98           C  
ANISOU  498  CG  ARG A 159    12109  17618  16241   -164   -125   3238       C  
ATOM    499  CD  ARG A 159      92.232  68.956  60.130  1.00127.70           C  
ANISOU  499  CD  ARG A 159    13301  18202  17016     12    -13   2878       C  
ATOM    500  NE  ARG A 159      91.924  68.425  58.804  1.00137.60           N  
ANISOU  500  NE  ARG A 159    14499  19754  18027    173    120   2886       N  
ATOM    501  CZ  ARG A 159      90.912  67.603  58.538  1.00138.45           C  
ANISOU  501  CZ  ARG A 159    14861  19705  18040    333    209   2610       C  
ATOM    502  NH1 ARG A 159      90.094  67.212  59.508  1.00135.52           N  
ANISOU  502  NH1 ARG A 159    14800  18897  17793    337    193   2330       N  
ATOM    503  NH2 ARG A 159      90.716  67.174  57.297  1.00139.44           N  
ANISOU  503  NH2 ARG A 159    14918  20122  17940    490    303   2623       N  
ATOM    504  N   SER A 160      97.886  68.663  59.028  1.00113.07           N  
ANISOU  504  N   SER A 160    10131  18328  14501    291     80   3844       N  
ATOM    505  CA  SER A 160      98.681  67.624  58.377  1.00108.94           C  
ANISOU  505  CA  SER A 160     9459  18349  13583    655    240   3816       C  
ATOM    506  C   SER A 160      97.809  66.374  58.360  1.00115.37           C  
ANISOU  506  C   SER A 160    10659  18942  14233    973    353   3370       C  
ATOM    507  O   SER A 160      97.838  65.553  59.279  1.00114.57           O  
ANISOU  507  O   SER A 160    10814  18595  14120   1138    362   3072       O  
ATOM    508  CB  SER A 160     100.002  67.399  59.102  1.00103.80           C  
ANISOU  508  CB  SER A 160     8637  17927  12876    727    214   3884       C  
ATOM    509  OG  SER A 160      99.814  67.327  60.503  1.00106.59           O  
ANISOU  509  OG  SER A 160     9273  17766  13459    657    120   3644       O  
ATOM    510  N   ARG A 161      97.019  66.238  57.290  1.00121.98           N  
ANISOU  510  N   ARG A 161    11535  19863  14947   1052    425   3339       N  
ATOM    511  CA  ARG A 161      95.899  65.299  57.283  1.00108.31           C  
ANISOU  511  CA  ARG A 161    10197  17795  13163   1247    479   2943       C  
ATOM    512  C   ARG A 161      96.347  63.850  57.440  1.00104.57           C  
ANISOU  512  C   ARG A 161     9877  17447  12407   1662    553   2644       C  
ATOM    513  O   ARG A 161      95.593  63.026  57.969  1.00105.34           O  
ANISOU  513  O   ARG A 161    10344  17139  12540   1776    550   2303       O  
ATOM    514  CB  ARG A 161      95.094  65.470  55.994  1.00113.03           C  
ANISOU  514  CB  ARG A 161    10757  18527  13661   1262    528   2998       C  
ATOM    515  CG  ARG A 161      94.688  66.907  55.710  1.00120.35           C  
ANISOU  515  CG  ARG A 161    11516  19365  14845    871    444   3317       C  
ATOM    516  CD  ARG A 161      94.194  67.073  54.284  1.00132.72           C  
ANISOU  516  CD  ARG A 161    12958  21224  16247    924    507   3440       C  
ATOM    517  NE  ARG A 161      94.095  68.480  53.904  1.00140.82           N  
ANISOU  517  NE  ARG A 161    13747  22276  17481    562    419   3826       N  
ATOM    518  CZ  ARG A 161      93.798  68.906  52.680  1.00142.17           C  
ANISOU  518  CZ  ARG A 161    13739  22737  17541    540    454   4037       C  
ATOM    519  NH1 ARG A 161      93.569  68.034  51.708  1.00141.75           N  
ANISOU  519  NH1 ARG A 161    13713  22985  17160    875    578   3882       N  
ATOM    520  NH2 ARG A 161      93.731  70.207  52.428  1.00142.90           N  
ANISOU  520  NH2 ARG A 161    13632  22811  17853    189    347   4403       N  
ATOM    521  N   GLN A 162      97.560  63.516  56.999  1.00104.57           N  
ANISOU  521  N   GLN A 162     9599  18007  12125   1893    607   2773       N  
ATOM    522  CA  GLN A 162      98.005  62.129  57.064  1.00 99.32           C  
ANISOU  522  CA  GLN A 162     9085  17484  11170   2329    656   2478       C  
ATOM    523  C   GLN A 162      98.526  61.745  58.445  1.00 98.04           C  
ANISOU  523  C   GLN A 162     9074  17059  11118   2340    608   2334       C  
ATOM    524  O   GLN A 162      98.367  60.590  58.855  1.00 95.74           O  
ANISOU  524  O   GLN A 162     9086  16569  10723   2612    608   2000       O  
ATOM    525  CB  GLN A 162      99.065  61.875  55.998  1.00101.20           C  
ANISOU  525  CB  GLN A 162     8963  18471  11019   2629    734   2649       C  
ATOM    526  CG  GLN A 162      98.453  61.678  54.634  1.00105.12           C  
ANISOU  526  CG  GLN A 162     9435  19208  11297   2805    789   2624       C  
ATOM    527  CD  GLN A 162      99.480  61.623  53.540  1.00111.37           C  
ANISOU  527  CD  GLN A 162     9816  20803  11699   3079    869   2852       C  
ATOM    528  OE1 GLN A 162     100.528  62.264  53.626  1.00112.63           O  
ANISOU  528  OE1 GLN A 162     9595  21362  11838   2958    885   3197       O  
ATOM    529  NE2 GLN A 162      99.186  60.861  52.493  1.00115.91           N  
ANISOU  529  NE2 GLN A 162    10451  21639  11953   3457    910   2668       N  
ATOM    530  N   PHE A 163      99.161  62.678  59.166  1.00102.91           N  
ANISOU  530  N   PHE A 163     9488  17668  11944   2054    548   2582       N  
ATOM    531  CA  PHE A 163      99.443  62.442  60.581  1.00 97.12           C  
ANISOU  531  CA  PHE A 163     8939  16593  11369   2019    486   2431       C  
ATOM    532  C   PHE A 163      98.154  62.393  61.388  1.00 96.81           C  
ANISOU  532  C   PHE A 163     9302  15886  11594   1863    439   2186       C  
ATOM    533  O   PHE A 163      98.063  61.650  62.373  1.00 92.04           O  
ANISOU  533  O   PHE A 163     8976  14976  11021   1977    422   1933       O  
ATOM    534  CB  PHE A 163     100.374  63.526  61.140  1.00 84.26           C  
ANISOU  534  CB  PHE A 163     7000  15094   9923   1737    402   2754       C  
ATOM    535  CG  PHE A 163     100.820  63.280  62.566  1.00 90.28           C  
ANISOU  535  CG  PHE A 163     7914  15577  10810   1737    334   2606       C  
ATOM    536  CD1 PHE A 163     100.046  63.705  63.642  1.00 90.88           C  
ANISOU  536  CD1 PHE A 163     8254  15075  11203   1503    241   2485       C  
ATOM    537  CD2 PHE A 163     102.023  62.641  62.831  1.00 98.37           C  
ANISOU  537  CD2 PHE A 163     8809  16947  11622   1990    360   2591       C  
ATOM    538  CE1 PHE A 163     100.454  63.480  64.952  1.00 88.80           C  
ANISOU  538  CE1 PHE A 163     8125  14578  11035   1523    179   2350       C  
ATOM    539  CE2 PHE A 163     102.441  62.417  64.138  1.00 98.53           C  
ANISOU  539  CE2 PHE A 163     8968  16718  11751   1998    295   2458       C  
ATOM    540  CZ  PHE A 163     101.655  62.837  65.198  1.00 95.41           C  
ANISOU  540  CZ  PHE A 163     8839  15746  11669   1764    205   2339       C  
ATOM    541  N   GLU A 164      97.153  63.179  60.984  1.00 93.49           N  
ANISOU  541  N   GLU A 164     8908  15257  11358   1608    416   2270       N  
ATOM    542  CA  GLU A 164      95.859  63.147  61.653  1.00 84.69           C  
ANISOU  542  CA  GLU A 164     8146  13564  10468   1475    379   2051       C  
ATOM    543  C   GLU A 164      95.109  61.861  61.341  1.00 82.57           C  
ANISOU  543  C   GLU A 164     8183  13156  10032   1748    442   1734       C  
ATOM    544  O   GLU A 164      94.438  61.299  62.216  1.00 82.84           O  
ANISOU  544  O   GLU A 164     8535  12768  10171   1759    421   1498       O  
ATOM    545  CB  GLU A 164      95.034  64.361  61.239  1.00 87.22           C  
ANISOU  545  CB  GLU A 164     8389  13738  11013   1150    328   2234       C  
ATOM    546  CG  GLU A 164      93.872  64.656  62.156  1.00 99.19           C  
ANISOU  546  CG  GLU A 164    10195  14691  12801    961    264   2069       C  
ATOM    547  CD  GLU A 164      92.919  65.673  61.568  1.00108.63           C  
ANISOU  547  CD  GLU A 164    11351  15755  14169    710    219   2199       C  
ATOM    548  OE1 GLU A 164      92.618  65.573  60.356  1.00116.73           O  
ANISOU  548  OE1 GLU A 164    12294  17007  15053    774    284   2258       O  
ATOM    549  OE2 GLU A 164      92.468  66.568  62.317  1.00106.16           O  
ANISOU  549  OE2 GLU A 164    11096  15117  14125    468    109   2231       O  
ATOM    550  N   ALA A 165      95.210  61.381  60.098  1.00 80.81           N  
ANISOU  550  N   ALA A 165     7866  13291   9548   1974    503   1733       N  
ATOM    551  CA  ALA A 165      94.523  60.153  59.714  1.00 71.09           C  
ANISOU  551  CA  ALA A 165     6927  11923   8161   2246    521   1428       C  
ATOM    552  C   ALA A 165      95.054  58.957  60.495  1.00 70.44           C  
ANISOU  552  C   ALA A 165     7053  11749   7961   2520    501   1189       C  
ATOM    553  O   ALA A 165      94.278  58.154  61.025  1.00 69.40           O  
ANISOU  553  O   ALA A 165     7265  11206   7897   2571    464    940       O  
ATOM    554  CB  ALA A 165      94.666  59.922  58.212  1.00 67.48           C  
ANISOU  554  CB  ALA A 165     6301  11919   7419   2474    569   1474       C  
ATOM    555  N   SER A 166      96.380  58.819  60.573  1.00 65.75           N  
ANISOU  555  N   SER A 166     6247  11545   7190   2697    517   1278       N  
ATOM    556  CA  SER A 166      96.956  57.720  61.341  1.00 78.63           C  
ANISOU  556  CA  SER A 166     8069  13100   8707   2966    489   1060       C  
ATOM    557  C   SER A 166      96.491  57.767  62.788  1.00 79.65           C  
ANISOU  557  C   SER A 166     8446  12704   9112   2757    443    969       C  
ATOM    558  O   SER A 166      96.191  56.728  63.387  1.00 88.04           O  
ANISOU  558  O   SER A 166     9824  13468  10158   2914    406    724       O  
ATOM    559  CB  SER A 166      98.481  57.769  61.282  1.00 93.76           C  
ANISOU  559  CB  SER A 166     9671  15539  10415   3145    515   1209       C  
ATOM    560  OG  SER A 166      98.963  58.985  61.825  1.00104.17           O  
ANISOU  560  OG  SER A 166    10728  16913  11939   2817    509   1494       O  
ATOM    561  N   LYS A 167      96.422  58.967  63.367  1.00 77.92           N  
ANISOU  561  N   LYS A 167     8089  12372   9146   2411    431   1168       N  
ATOM    562  CA  LYS A 167      96.012  59.091  64.762  1.00 91.63           C  
ANISOU  562  CA  LYS A 167    10037  13658  11122   2237    384   1085       C  
ATOM    563  C   LYS A 167      94.589  58.584  64.954  1.00 85.20           C  
ANISOU  563  C   LYS A 167     9564  12390  10416   2186    377    885       C  
ATOM    564  O   LYS A 167      94.318  57.798  65.871  1.00 73.39           O  
ANISOU  564  O   LYS A 167     8339  10592   8954   2260    353    707       O  
ATOM    565  CB  LYS A 167      96.146  60.549  65.212  1.00104.83           C  
ANISOU  565  CB  LYS A 167    11493  15298  13038   1895    339   1325       C  
ATOM    566  CG  LYS A 167      95.885  60.803  66.690  1.00110.59           C  
ANISOU  566  CG  LYS A 167    12398  15631  13992   1746    276   1249       C  
ATOM    567  CD  LYS A 167      95.952  62.298  66.981  1.00113.41           C  
ANISOU  567  CD  LYS A 167    12551  15948  14593   1424    189   1471       C  
ATOM    568  CE  LYS A 167      95.574  62.628  68.416  1.00110.47           C  
ANISOU  568  CE  LYS A 167    12359  15183  14433   1299    110   1374       C  
ATOM    569  NZ  LYS A 167      95.479  64.103  68.613  1.00106.98           N  
ANISOU  569  NZ  LYS A 167    11756  14652  14240   1001    -15   1558       N  
ATOM    570  N   LEU A 168      93.675  58.994  64.070  1.00 84.26           N  
ANISOU  570  N   LEU A 168     9427  12241  10347   2062    394    927       N  
ATOM    571  CA  LEU A 168      92.274  58.598  64.184  1.00 76.01           C  
ANISOU  571  CA  LEU A 168     8670  10795   9417   1985    383    766       C  
ATOM    572  C   LEU A 168      92.089  57.107  63.922  1.00 83.24           C  
ANISOU  572  C   LEU A 168     9842  11629  10157   2277    362    527       C  
ATOM    573  O   LEU A 168      91.284  56.451  64.595  1.00 86.88           O  
ANISOU  573  O   LEU A 168    10586  11709  10713   2250    328    378       O  
ATOM    574  CB  LEU A 168      91.433  59.419  63.211  1.00 73.22           C  
ANISOU  574  CB  LEU A 168     8208  10473   9141   1801    399    876       C  
ATOM    575  CG  LEU A 168      91.420  60.931  63.435  1.00 66.29           C  
ANISOU  575  CG  LEU A 168     7117   9598   8473   1491    378   1106       C  
ATOM    576  CD1 LEU A 168      90.745  61.624  62.266  1.00 64.92           C  
ANISOU  576  CD1 LEU A 168     6819   9525   8322   1365    391   1223       C  
ATOM    577  CD2 LEU A 168      90.704  61.270  64.734  1.00 56.65           C  
ANISOU  577  CD2 LEU A 168     6075   7960   7490   1301    336   1040       C  
ATOM    578  N   ARG A 169      92.808  56.558  62.936  1.00 78.85           N  
ANISOU  578  N   ARG A 169     9188  11432   9340   2562    366    494       N  
ATOM    579  CA  ARG A 169      92.728  55.125  62.667  1.00 70.71           C  
ANISOU  579  CA  ARG A 169     8412  10320   8133   2878    302    247       C  
ATOM    580  C   ARG A 169      93.094  54.311  63.899  1.00 77.36           C  
ANISOU  580  C   ARG A 169     9473  10922   8999   2976    254    121       C  
ATOM    581  O   ARG A 169      92.433  53.315  64.213  1.00 87.21           O  
ANISOU  581  O   ARG A 169    11034  11824  10278   3047    176    -60       O  
ATOM    582  CB  ARG A 169      93.641  54.747  61.499  1.00 74.51           C  
ANISOU  582  CB  ARG A 169     8720  11295   8296   3220    306    230       C  
ATOM    583  CG  ARG A 169      93.195  55.274  60.151  1.00 62.14           C  
ANISOU  583  CG  ARG A 169     6984   9971   6656   3194    340    317       C  
ATOM    584  CD  ARG A 169      93.981  54.639  59.022  1.00 68.65           C  
ANISOU  584  CD  ARG A 169     7693  11269   7122   3608    327    244       C  
ATOM    585  NE  ARG A 169      93.492  55.084  57.721  1.00 99.20           N  
ANISOU  585  NE  ARG A 169    11415  15372  10903   3605    356    317       N  
ATOM    586  CZ  ARG A 169      94.055  56.048  56.999  1.00100.49           C  
ANISOU  586  CZ  ARG A 169    11201  16011  10970   3547    447    585       C  
ATOM    587  NH1 ARG A 169      95.144  56.661  57.442  1.00 97.95           N  
ANISOU  587  NH1 ARG A 169    10602  15978  10636   3478    506    807       N  
ATOM    588  NH2 ARG A 169      93.537  56.388  55.826  1.00100.90           N  
ANISOU  588  NH2 ARG A 169    11144  16256  10938   3554    469    644       N  
ATOM    589  N   GLU A 170      94.145  54.719  64.612  1.00 59.00           N  
ANISOU  589  N   GLU A 170     6983   8771   6664   2974    286    229       N  
ATOM    590  CA  GLU A 170      94.565  53.964  65.785  1.00 76.57           C  
ANISOU  590  CA  GLU A 170     9403  10796   8893   3085    242    116       C  
ATOM    591  C   GLU A 170      93.572  54.123  66.933  1.00 84.03           C  
ANISOU  591  C   GLU A 170    10554  11275  10100   2815    234    107       C  
ATOM    592  O   GLU A 170      93.323  53.170  67.681  1.00 91.26           O  
ANISOU  592  O   GLU A 170    11745  11899  11032   2899    177    -27       O  
ATOM    593  CB  GLU A 170      95.965  54.400  66.205  1.00 80.30           C  
ANISOU  593  CB  GLU A 170     9624  11606   9282   3157    273    237       C  
ATOM    594  CG  GLU A 170      96.821  53.264  66.717  1.00 98.14           C  
ANISOU  594  CG  GLU A 170    12028  13894  11366   3484    219     79       C  
ATOM    595  CD  GLU A 170      97.971  53.754  67.565  1.00114.90           C  
ANISOU  595  CD  GLU A 170    13955  16211  13491   3469    242    195       C  
ATOM    596  OE1 GLU A 170      98.245  54.973  67.535  1.00118.57           O  
ANISOU  596  OE1 GLU A 170    14131  16858  14062   3234    287    411       O  
ATOM    597  OE2 GLU A 170      98.584  52.929  68.276  1.00120.64           O  
ANISOU  597  OE2 GLU A 170    14823  16889  14124   3685    197     74       O  
ATOM    598  N   ILE A 171      92.992  55.317  67.084  1.00 81.03           N  
ANISOU  598  N   ILE A 171    10041  10830   9917   2501    280    256       N  
ATOM    599  CA  ILE A 171      91.991  55.538  68.126  1.00 78.49           C  
ANISOU  599  CA  ILE A 171     9889  10117   9818   2268    276    248       C  
ATOM    600  C   ILE A 171      90.788  54.631  67.904  1.00 79.12           C  
ANISOU  600  C   ILE A 171    10245   9891   9926   2272    239    115       C  
ATOM    601  O   ILE A 171      90.307  53.966  68.828  1.00 74.68           O  
ANISOU  601  O   ILE A 171     9914   9030   9433   2254    207     45       O  
ATOM    602  CB  ILE A 171      91.572  57.019  68.170  1.00 74.43           C  
ANISOU  602  CB  ILE A 171     9177   9612   9490   1968    307    414       C  
ATOM    603  CG1 ILE A 171      92.727  57.897  68.651  1.00 77.68           C  
ANISOU  603  CG1 ILE A 171     9347  10245   9924   1927    300    553       C  
ATOM    604  CG2 ILE A 171      90.357  57.210  69.067  1.00 67.42           C  
ANISOU  604  CG2 ILE A 171     8464   8357   8797   1765    303    385       C  
ATOM    605  CD1 ILE A 171      92.413  59.379  68.605  1.00 78.83           C  
ANISOU  605  CD1 ILE A 171     9298  10394  10259   1644    284    720       C  
ATOM    606  N   ARG A 172      90.279  54.595  66.674  1.00 84.93           N  
ANISOU  606  N   ARG A 172    10953  10706  10612   2289    233     93       N  
ATOM    607  CA  ARG A 172      89.155  53.712  66.389  1.00 79.87           C  
ANISOU  607  CA  ARG A 172    10567   9775  10005   2290    170    -34       C  
ATOM    608  C   ARG A 172      89.570  52.251  66.512  1.00 83.64           C  
ANISOU  608  C   ARG A 172    11285  10148  10344   2573     67   -203       C  
ATOM    609  O   ARG A 172      88.807  51.426  67.029  1.00 87.49           O  
ANISOU  609  O   ARG A 172    12033  10289  10920   2531     -8   -277       O  
ATOM    610  CB  ARG A 172      88.591  54.014  65.001  1.00 62.10           C  
ANISOU  610  CB  ARG A 172     8225   7652   7717   2270    173    -31       C  
ATOM    611  CG  ARG A 172      87.393  53.168  64.615  1.00 76.44           C  
ANISOU  611  CG  ARG A 172    10288   9172   9583   2254     87   -158       C  
ATOM    612  CD  ARG A 172      87.006  53.461  63.182  1.00 92.48           C  
ANISOU  612  CD  ARG A 172    12213  11383  11543   2283     84   -169       C  
ATOM    613  NE  ARG A 172      88.166  53.389  62.299  1.00 98.65           N  
ANISOU  613  NE  ARG A 172    12832  12573  12078   2567     90   -186       N  
ATOM    614  CZ  ARG A 172      88.130  53.635  60.995  1.00 98.19           C  
ANISOU  614  CZ  ARG A 172    12638  12781  11890   2663     96   -183       C  
ATOM    615  NH1 ARG A 172      86.987  53.986  60.417  1.00 92.83           N  
ANISOU  615  NH1 ARG A 172    11976  11976  11319   2488     93   -172       N  
ATOM    616  NH2 ARG A 172      89.239  53.539  60.274  1.00103.72           N  
ANISOU  616  NH2 ARG A 172    13170  13901  12338   2944    108   -183       N  
ATOM    617  N   LYS A 173      90.789  51.921  66.077  1.00 76.63           N  
ANISOU  617  N   LYS A 173    10309   9566   9242   2862     50   -253       N  
ATOM    618  CA  LYS A 173      91.259  50.542  66.160  1.00 73.24           C  
ANISOU  618  CA  LYS A 173    10114   9049   8666   3172    -73   -433       C  
ATOM    619  C   LYS A 173      91.354  50.072  67.607  1.00 85.24           C  
ANISOU  619  C   LYS A 173    11815  10291  10281   3127    -99   -435       C  
ATOM    620  O   LYS A 173      90.981  48.936  67.923  1.00 98.58           O  
ANISOU  620  O   LYS A 173    13798  11674  11985   3216   -224   -551       O  
ATOM    621  CB  LYS A 173      92.611  50.406  65.459  1.00 74.87           C  
ANISOU  621  CB  LYS A 173    10147   9702   8599   3510    -73   -475       C  
ATOM    622  CG  LYS A 173      93.244  49.025  65.595  1.00 91.32           C  
ANISOU  622  CG  LYS A 173    12464  11724  10508   3878   -215   -676       C  
ATOM    623  CD  LYS A 173      94.632  48.986  64.975  1.00103.12           C  
ANISOU  623  CD  LYS A 173    13744  13725  11711   4227   -197   -705       C  
ATOM    624  CE  LYS A 173      95.307  47.644  65.208  1.00110.24           C  
ANISOU  624  CE  LYS A 173    14887  14563  12435   4617   -351   -917       C  
ATOM    625  NZ  LYS A 173      95.461  47.362  66.662  1.00117.39           N  
ANISOU  625  NZ  LYS A 173    15952  15176  13477   4517   -363   -893       N  
ATOM    626  N   ASN A 174      91.840  50.933  68.504  1.00 81.40           N  
ANISOU  626  N   ASN A 174    11163   9900   9866   2989      2   -301       N  
ATOM    627  CA  ASN A 174      91.998  50.540  69.902  1.00 85.53           C  
ANISOU  627  CA  ASN A 174    11837  10203  10457   2968    -14   -299       C  
ATOM    628  C   ASN A 174      90.669  50.500  70.647  1.00 82.88           C  
ANISOU  628  C   ASN A 174    11673   9489  10330   2700    -15   -251       C  
ATOM    629  O   ASN A 174      90.522  49.723  71.595  1.00 84.00           O  
ANISOU  629  O   ASN A 174    12027   9382  10506   2720    -69   -273       O  
ATOM    630  CB  ASN A 174      92.977  51.483  70.606  1.00 92.65           C  
ANISOU  630  CB  ASN A 174    12501  11341  11359   2928     73   -186       C  
ATOM    631  CG  ASN A 174      94.425  51.111  70.357  1.00104.15           C  
ANISOU  631  CG  ASN A 174    13856  13121  12596   3239     50   -239       C  
ATOM    632  OD1 ASN A 174      94.851  50.002  70.676  1.00118.84           O  
ANISOU  632  OD1 ASN A 174    15917  14892  14344   3482    -34   -365       O  
ATOM    633  ND2 ASN A 174      95.186  52.031  69.769  1.00 98.17           N  
ANISOU  633  ND2 ASN A 174    12779  12750  11771   3235    116   -131       N  
ATOM    634  N   ILE A 175      89.696  51.319  70.241  1.00 81.16           N  
ANISOU  634  N   ILE A 175    11356   9240  10242   2454     43   -173       N  
ATOM    635  CA  ILE A 175      88.372  51.259  70.855  1.00 70.89           C  
ANISOU  635  CA  ILE A 175    10194   7624   9117   2215     44   -123       C  
ATOM    636  C   ILE A 175      87.672  49.967  70.468  1.00 81.77           C  
ANISOU  636  C   ILE A 175    11840   8734  10495   2275    -87   -218       C  
ATOM    637  O   ILE A 175      87.061  49.291  71.307  1.00 84.45           O  
ANISOU  637  O   ILE A 175    12374   8792  10923   2190   -138   -187       O  
ATOM    638  CB  ILE A 175      87.534  52.481  70.443  1.00 64.34           C  
ANISOU  638  CB  ILE A 175     9181   6852   8412   1964    128    -28       C  
ATOM    639  CG1 ILE A 175      88.060  53.751  71.105  1.00 65.13           C  
ANISOU  639  CG1 ILE A 175     9062   7121   8564   1864    213     76       C  
ATOM    640  CG2 ILE A 175      86.080  52.266  70.827  1.00 52.71           C  
ANISOU  640  CG2 ILE A 175     7848   5092   7089   1751    118      9       C  
ATOM    641  CD1 ILE A 175      87.413  55.010  70.572  1.00 56.87           C  
ANISOU  641  CD1 ILE A 175     7829   6152   7628   1653    264    162       C  
ATOM    642  N   ASP A 176      87.738  49.612  69.185  1.00 89.17           N  
ANISOU  642  N   ASP A 176    12788   9757  11335   2421   -158   -324       N  
ATOM    643  CA  ASP A 176      87.107  48.388  68.719  1.00 86.79           C  
ANISOU  643  CA  ASP A 176    12751   9185  11041   2495   -328   -436       C  
ATOM    644  C   ASP A 176      87.758  47.160  69.339  1.00 86.52           C  
ANISOU  644  C   ASP A 176    12956   8988  10932   2717   -464   -523       C  
ATOM    645  O   ASP A 176      87.089  46.140  69.537  1.00 90.84           O  
ANISOU  645  O   ASP A 176    13761   9193  11560   2685   -619   -553       O  
ATOM    646  CB  ASP A 176      87.163  48.332  67.192  1.00 92.06           C  
ANISOU  646  CB  ASP A 176    13366  10024  11588   2657   -386   -555       C  
ATOM    647  CG  ASP A 176      86.378  49.461  66.536  1.00 99.08           C  
ANISOU  647  CG  ASP A 176    14049  11032  12565   2425   -274   -463       C  
ATOM    648  OD1 ASP A 176      85.506  50.056  67.206  1.00 99.87           O  
ANISOU  648  OD1 ASP A 176    14113  10991  12843   2133   -195   -336       O  
ATOM    649  OD2 ASP A 176      86.623  49.747  65.344  1.00104.82           O  
ANISOU  649  OD2 ASP A 176    14648  12008  13171   2551   -270   -516       O  
ATOM    650  N   SER A 177      89.043  47.242  69.678  1.00 83.98           N  
ANISOU  650  N   SER A 177    12549   8895  10465   2928   -421   -550       N  
ATOM    651  CA  SER A 177      89.754  46.129  70.294  1.00 91.24           C  
ANISOU  651  CA  SER A 177    13686   9683  11298   3163   -549   -637       C  
ATOM    652  C   SER A 177      89.575  46.064  71.806  1.00 94.74           C  
ANISOU  652  C   SER A 177    14212   9925  11860   2999   -506   -508       C  
ATOM    653  O   SER A 177      90.107  45.143  72.436  1.00104.17           O  
ANISOU  653  O   SER A 177    15598  10983  12999   3169   -612   -555       O  
ATOM    654  CB  SER A 177      91.247  46.208  69.961  1.00 92.91           C  
ANISOU  654  CB  SER A 177    13757  10266  11279   3491   -526   -727       C  
ATOM    655  OG  SER A 177      91.461  46.102  68.566  1.00 99.80           O  
ANISOU  655  OG  SER A 177    14567  11353  11999   3700   -581   -853       O  
ATOM    656  N   GLY A 178      88.850  47.010  72.403  1.00 91.05           N  
ANISOU  656  N   GLY A 178    13607   9448  11540   2696   -362   -350       N  
ATOM    657  CA  GLY A 178      88.698  47.024  73.846  1.00 91.27           C  
ANISOU  657  CA  GLY A 178    13686   9344  11648   2570   -311   -227       C  
ATOM    658  C   GLY A 178      89.965  47.320  74.613  1.00 96.15           C  
ANISOU  658  C   GLY A 178    14207  10167  12157   2733   -248   -233       C  
ATOM    659  O   GLY A 178      89.975  47.203  75.842  1.00 86.94           O  
ANISOU  659  O   GLY A 178    13105   8901  11026   2685   -224   -152       O  
ATOM    660  N   PHE A 179      91.038  47.704  73.921  1.00105.91           N  
ANISOU  660  N   PHE A 179    15276  11711  13255   2927   -222   -316       N  
ATOM    661  CA  PHE A 179      92.301  48.058  74.558  1.00108.48           C  
ANISOU  661  CA  PHE A 179    15472  12268  13477   3075   -169   -315       C  
ATOM    662  C   PHE A 179      92.223  49.359  75.351  1.00 99.99           C  
ANISOU  662  C   PHE A 179    14183  11301  12508   2858    -34   -185       C  
ATOM    663  O   PHE A 179      93.207  49.718  76.009  1.00101.83           O  
ANISOU  663  O   PHE A 179    14307  11701  12683   2949     -3   -173       O  
ATOM    664  CB  PHE A 179      93.405  48.165  73.498  1.00113.57           C  
ANISOU  664  CB  PHE A 179    15953  13257  13940   3323   -178   -408       C  
ATOM    665  CG  PHE A 179      93.812  46.844  72.904  1.00127.03           C  
ANISOU  665  CG  PHE A 179    17871  14904  15488   3641   -334   -576       C  
ATOM    666  CD1 PHE A 179      94.574  46.794  71.748  1.00134.41           C  
ANISOU  666  CD1 PHE A 179    18681  16155  16233   3895   -359   -678       C  
ATOM    667  CD2 PHE A 179      93.426  45.653  73.497  1.00133.66           C  
ANISOU  667  CD2 PHE A 179    19036  15382  16365   3696   -474   -626       C  
ATOM    668  CE1 PHE A 179      94.947  45.577  71.198  1.00138.45           C  
ANISOU  668  CE1 PHE A 179    19401  16621  16583   4232   -528   -861       C  
ATOM    669  CE2 PHE A 179      93.795  44.436  72.953  1.00135.18           C  
ANISOU  669  CE2 PHE A 179    19450  15487  16424   4003   -660   -796       C  
ATOM    670  CZ  PHE A 179      94.556  44.398  71.803  1.00136.89           C  
ANISOU  670  CZ  PHE A 179    19553  16019  16441   4288   -692   -932       C  
ATOM    671  N   TYR A 180      91.097  50.068  75.311  1.00 84.83           N  
ANISOU  671  N   TYR A 180    12205   9291  10737   2590     27    -99       N  
ATOM    672  CA  TYR A 180      90.953  51.352  75.980  1.00 80.07           C  
ANISOU  672  CA  TYR A 180    11410   8779  10233   2406    122      0       C  
ATOM    673  C   TYR A 180      90.029  51.220  77.184  1.00 83.03           C  
ANISOU  673  C   TYR A 180    11914   8929  10705   2264    143     74       C  
ATOM    674  O   TYR A 180      89.010  50.522  77.127  1.00 85.33           O  
ANISOU  674  O   TYR A 180    12372   9000  11050   2174    112    100       O  
ATOM    675  CB  TYR A 180      90.393  52.417  75.029  1.00 83.64           C  
ANISOU  675  CB  TYR A 180    11669   9341  10770   2227    173     44       C  
ATOM    676  CG  TYR A 180      91.429  53.121  74.172  1.00 89.61           C  
ANISOU  676  CG  TYR A 180    12183  10415  11451   2307    187     46       C  
ATOM    677  CD1 TYR A 180      92.754  53.223  74.576  1.00 84.92           C  
ANISOU  677  CD1 TYR A 180    11483  10020  10762   2463    178     42       C  
ATOM    678  CD2 TYR A 180      91.076  53.681  72.950  1.00 85.98           C  
ANISOU  678  CD2 TYR A 180    11585  10073  11011   2220    207     73       C  
ATOM    679  CE1 TYR A 180      93.697  53.862  73.783  1.00 80.28           C  
ANISOU  679  CE1 TYR A 180    10643   9757  10104   2518    190     83       C  
ATOM    680  CE2 TYR A 180      92.008  54.324  72.157  1.00 84.40           C  
ANISOU  680  CE2 TYR A 180    11141  10194  10735   2280    222    116       C  
ATOM    681  CZ  TYR A 180      93.316  54.408  72.575  1.00 86.55           C  
ANISOU  681  CZ  TYR A 180    11295  10674  10915   2423    213    130       C  
ATOM    682  OH  TYR A 180      94.240  55.047  71.777  1.00 93.75           O  
ANISOU  682  OH  TYR A 180    11934  11937  11750   2465    227    210       O  
ATOM    683  N   THR A 181      90.403  51.885  78.273  1.00 77.02           N  
ANISOU  683  N   THR A 181    11067   8240   9957   2252    184    115       N  
ATOM    684  CA  THR A 181      89.505  52.145  79.384  1.00 74.82           C  
ANISOU  684  CA  THR A 181    10830   7843   9754   2116    225    196       C  
ATOM    685  C   THR A 181      88.530  53.253  78.990  1.00 74.13           C  
ANISOU  685  C   THR A 181    10597   7783   9786   1904    275    241       C  
ATOM    686  O   THR A 181      88.828  54.092  78.136  1.00 81.73           O  
ANISOU  686  O   THR A 181    11390   8885  10779   1863    278    221       O  
ATOM    687  CB  THR A 181      90.304  52.563  80.625  1.00 84.34           C  
ANISOU  687  CB  THR A 181    11984   9145  10918   2214    233    196       C  
ATOM    688  OG1 THR A 181      91.398  51.660  80.820  1.00 91.51           O  
ANISOU  688  OG1 THR A 181    12992  10072  11706   2433    182    140       O  
ATOM    689  CG2 THR A 181      89.437  52.549  81.876  1.00 91.11           C  
ANISOU  689  CG2 THR A 181    12918   9900  11800   2142    269    276       C  
ATOM    690  N   GLN A 182      87.342  53.246  79.606  1.00 69.83           N  
ANISOU  690  N   GLN A 182    10112   7120   9301   1770    310    316       N  
ATOM    691  CA  GLN A 182      86.438  54.383  79.440  1.00 66.59           C  
ANISOU  691  CA  GLN A 182     9560   6753   8990   1599    352    348       C  
ATOM    692  C   GLN A 182      87.114  55.679  79.856  1.00 76.10           C  
ANISOU  692  C   GLN A 182    10586   8112  10215   1626    341    316       C  
ATOM    693  O   GLN A 182      86.850  56.735  79.272  1.00 80.17           O  
ANISOU  693  O   GLN A 182    10956   8690  10815   1519    333    314       O  
ATOM    694  CB  GLN A 182      85.152  54.180  80.244  1.00 48.65           C  
ANISOU  694  CB  GLN A 182     7356   4386   6745   1491    395    441       C  
ATOM    695  CG  GLN A 182      84.020  55.137  79.900  1.00 47.78           C  
ANISOU  695  CG  GLN A 182     7124   4306   6725   1323    431    469       C  
ATOM    696  CD  GLN A 182      83.244  55.604  81.128  1.00 76.13           C  
ANISOU  696  CD  GLN A 182    10678   7947  10301   1303    476    529       C  
ATOM    697  OE1 GLN A 182      83.822  55.840  82.194  1.00 77.93           O  
ANISOU  697  OE1 GLN A 182    10898   8248  10465   1428    470    511       O  
ATOM    698  NE2 GLN A 182      81.927  55.722  80.987  1.00 76.56           N  
ANISOU  698  NE2 GLN A 182    10705   7984  10400   1161    516    599       N  
ATOM    699  N   GLU A 183      87.995  55.621  80.854  1.00 84.55           N  
ANISOU  699  N   GLU A 183    11672   9234  11221   1766    319    293       N  
ATOM    700  CA  GLU A 183      88.721  56.822  81.249  1.00 91.34           C  
ANISOU  700  CA  GLU A 183    12369  10219  12115   1792    269    256       C  
ATOM    701  C   GLU A 183      89.752  57.206  80.193  1.00 85.09           C  
ANISOU  701  C   GLU A 183    11436   9554  11339   1801    227    239       C  
ATOM    702  O   GLU A 183      89.928  58.393  79.891  1.00 77.87           O  
ANISOU  702  O   GLU A 183    10351   8719  10518   1712    176    251       O  
ATOM    703  CB  GLU A 183      89.385  56.609  82.609  1.00 98.73           C  
ANISOU  703  CB  GLU A 183    13361  11180  12971   1950    247    232       C  
ATOM    704  CG  GLU A 183      90.204  57.786  83.095  1.00106.28           C  
ANISOU  704  CG  GLU A 183    14164  12245  13970   1989    159    183       C  
ATOM    705  CD  GLU A 183      90.930  57.486  84.387  1.00123.96           C  
ANISOU  705  CD  GLU A 183    16466  14517  16117   2166    130    146       C  
ATOM    706  OE1 GLU A 183      90.401  56.697  85.199  1.00132.13           O  
ANISOU  706  OE1 GLU A 183    17648  15490  17067   2232    187    173       O  
ATOM    707  OE2 GLU A 183      92.032  58.035  84.590  1.00132.70           O  
ANISOU  707  OE2 GLU A 183    17466  15718  17236   2234     43    103       O  
ATOM    708  N   GLU A 184      90.431  56.214  79.611  1.00 83.62           N  
ANISOU  708  N   GLU A 184    11313   9399  11059   1913    235    221       N  
ATOM    709  CA  GLU A 184      91.413  56.501  78.571  1.00 79.18           C  
ANISOU  709  CA  GLU A 184    10593   9018  10475   1947    208    222       C  
ATOM    710  C   GLU A 184      90.753  57.137  77.350  1.00 79.97           C  
ANISOU  710  C   GLU A 184    10581   9147  10656   1785    223    264       C  
ATOM    711  O   GLU A 184      91.337  58.018  76.708  1.00 73.59           O  
ANISOU  711  O   GLU A 184     9569   8503   9887   1730    190    314       O  
ATOM    712  CB  GLU A 184      92.151  55.220  78.182  1.00 71.31           C  
ANISOU  712  CB  GLU A 184     9704   8059   9330   2143    208    171       C  
ATOM    713  CG  GLU A 184      93.076  54.677  79.255  1.00 69.51           C  
ANISOU  713  CG  GLU A 184     9552   7848   9009   2326    181    132       C  
ATOM    714  CD  GLU A 184      93.736  53.375  78.847  1.00 86.82           C  
ANISOU  714  CD  GLU A 184    11875  10061  11052   2542    160     68       C  
ATOM    715  OE1 GLU A 184      93.197  52.690  77.955  1.00 97.32           O  
ANISOU  715  OE1 GLU A 184    13308  11310  12357   2548    158     41       O  
ATOM    716  OE2 GLU A 184      94.800  53.037  79.409  1.00 97.64           O  
ANISOU  716  OE2 GLU A 184    13248  11525  12326   2721    130     31       O  
ATOM    717  N   ILE A 185      89.533  56.704  77.020  1.00 81.19           N  
ANISOU  717  N   ILE A 185    10860   9150  10840   1699    263    262       N  
ATOM    718  CA  ILE A 185      88.791  57.306  75.914  1.00 70.19           C  
ANISOU  718  CA  ILE A 185     9372   7772   9524   1547    277    297       C  
ATOM    719  C   ILE A 185      88.457  58.760  76.226  1.00 69.78           C  
ANISOU  719  C   ILE A 185     9171   7737   9605   1397    245    342       C  
ATOM    720  O   ILE A 185      88.649  59.654  75.391  1.00 70.80           O  
ANISOU  720  O   ILE A 185     9130   7974   9797   1305    214    395       O  
ATOM    721  CB  ILE A 185      87.518  56.491  75.619  1.00 57.59           C  
ANISOU  721  CB  ILE A 185     7946   5996   7939   1484    312    284       C  
ATOM    722  CG1 ILE A 185      87.870  55.096  75.093  1.00 54.62           C  
ANISOU  722  CG1 ILE A 185     7725   5580   7448   1636    293    227       C  
ATOM    723  CG2 ILE A 185      86.610  57.235  74.651  1.00 56.08           C  
ANISOU  723  CG2 ILE A 185     7658   5811   7839   1316    325    317       C  
ATOM    724  CD1 ILE A 185      86.651  54.272  74.711  1.00 48.43           C  
ANISOU  724  CD1 ILE A 185     7108   4597   6696   1557    286    221       C  
ATOM    725  N   GLU A 186      87.952  59.016  77.436  1.00 60.42           N  
ANISOU  725  N   GLU A 186     8050   6449   8458   1385    238    325       N  
ATOM    726  CA  GLU A 186      87.571  60.370  77.824  1.00 63.69           C  
ANISOU  726  CA  GLU A 186     8353   6856   8989   1282    176    335       C  
ATOM    727  C   GLU A 186      88.771  61.307  77.874  1.00 69.30           C  
ANISOU  727  C   GLU A 186     8895   7684   9753   1290     70    357       C  
ATOM    728  O   GLU A 186      88.623  62.513  77.638  1.00 67.84           O  
ANISOU  728  O   GLU A 186     8584   7502   9691   1173    -19    389       O  
ATOM    729  CB  GLU A 186      86.861  60.339  79.178  1.00 68.60           C  
ANISOU  729  CB  GLU A 186     9080   7388   9597   1325    186    298       C  
ATOM    730  CG  GLU A 186      85.504  59.656  79.141  1.00 71.32           C  
ANISOU  730  CG  GLU A 186     9542   7635   9920   1265    275    320       C  
ATOM    731  CD  GLU A 186      84.790  59.675  80.476  1.00 79.24           C  
ANISOU  731  CD  GLU A 186    10611   8613  10886   1315    295    314       C  
ATOM    732  OE1 GLU A 186      85.372  60.170  81.464  1.00 84.89           O  
ANISOU  732  OE1 GLU A 186    11300   9374  11579   1423    235    269       O  
ATOM    733  OE2 GLU A 186      83.646  59.185  80.537  1.00 81.57           O  
ANISOU  733  OE2 GLU A 186    10971   8857  11163   1252    365    361       O  
ATOM    734  N   VAL A 187      89.957  60.787  78.193  1.00 66.48           N  
ANISOU  734  N   VAL A 187     8532   7417   9310   1423     60    347       N  
ATOM    735  CA  VAL A 187      91.148  61.629  78.169  1.00 71.45           C  
ANISOU  735  CA  VAL A 187     8976   8179   9993   1413    -49    393       C  
ATOM    736  C   VAL A 187      91.448  62.063  76.743  1.00 76.03           C  
ANISOU  736  C   VAL A 187     9377   8901  10609   1302    -55    500       C  
ATOM    737  O   VAL A 187      91.746  63.237  76.485  1.00 79.07           O  
ANISOU  737  O   VAL A 187     9588   9333  11122   1172   -167    584       O  
ATOM    738  CB  VAL A 187      92.342  60.896  78.809  1.00 70.27           C  
ANISOU  738  CB  VAL A 187     8852   8121   9727   1592    -50    361       C  
ATOM    739  CG1 VAL A 187      93.627  61.677  78.593  1.00 63.46           C  
ANISOU  739  CG1 VAL A 187     7763   7433   8914   1566   -160    438       C  
ATOM    740  CG2 VAL A 187      92.099  60.685  80.290  1.00 72.70           C  
ANISOU  740  CG2 VAL A 187     9308   8308  10008   1695    -64    275       C  
ATOM    741  N   ILE A 188      91.350  61.127  75.793  1.00 74.39           N  
ANISOU  741  N   ILE A 188     9214   8762  10289   1356     48    502       N  
ATOM    742  CA  ILE A 188      91.575  61.448  74.386  1.00 68.34           C  
ANISOU  742  CA  ILE A 188     8278   8169   9518   1282     57    603       C  
ATOM    743  C   ILE A 188      90.517  62.421  73.884  1.00 70.92           C  
ANISOU  743  C   ILE A 188     8558   8399   9990   1084     29    653       C  
ATOM    744  O   ILE A 188      90.828  63.397  73.190  1.00 71.21           O  
ANISOU  744  O   ILE A 188     8397   8548  10112    955    -39    778       O  
ATOM    745  CB  ILE A 188      91.592  60.159  73.546  1.00 64.47           C  
ANISOU  745  CB  ILE A 188     7882   7757   8859   1427    155    555       C  
ATOM    746  CG1 ILE A 188      92.716  59.229  74.008  1.00 67.78           C  
ANISOU  746  CG1 ILE A 188     8344   8282   9126   1648    162    500       C  
ATOM    747  CG2 ILE A 188      91.756  60.490  72.086  1.00 61.25           C  
ANISOU  747  CG2 ILE A 188     7294   7559   8419   1378    171    654       C  
ATOM    748  CD1 ILE A 188      92.683  57.862  73.358  1.00 60.15           C  
ANISOU  748  CD1 ILE A 188     7525   7337   7991   1832    219    412       C  
ATOM    749  N   ALA A 189      89.250  62.171  74.224  1.00 68.23           N  
ANISOU  749  N   ALA A 189     8388   7858   9678   1053     73    571       N  
ATOM    750  CA  ALA A 189      88.179  63.062  73.788  1.00 68.15           C  
ANISOU  750  CA  ALA A 189     8343   7758   9793    887     46    602       C  
ATOM    751  C   ALA A 189      88.356  64.466  74.353  1.00 72.30           C  
ANISOU  751  C   ALA A 189     8756   8239  10475    785   -104    642       C  
ATOM    752  O   ALA A 189      88.147  65.457  73.645  1.00 87.82           O  
ANISOU  752  O   ALA A 189    10595  10218  12554    640   -179    731       O  
ATOM    753  CB  ALA A 189      86.818  62.488  74.188  1.00 69.51           C  
ANISOU  753  CB  ALA A 189     8704   7752   9953    886    119    513       C  
ATOM    754  N   ARG A 190      88.739  64.576  75.627  1.00 70.50           N  
ANISOU  754  N   ARG A 190     8579   7948  10259    866   -170    576       N  
ATOM    755  CA  ARG A 190      88.896  65.902  76.216  1.00 74.47           C  
ANISOU  755  CA  ARG A 190     8999   8380  10917    793   -354    586       C  
ATOM    756  C   ARG A 190      90.030  66.671  75.548  1.00 71.66           C  
ANISOU  756  C   ARG A 190     8422   8157  10649    686   -474    738       C  
ATOM    757  O   ARG A 190      89.977  67.904  75.473  1.00 79.17           O  
ANISOU  757  O   ARG A 190     9276   9037  11769    552   -648    800       O  
ATOM    758  CB  ARG A 190      89.112  65.788  77.732  1.00 77.86           C  
ANISOU  758  CB  ARG A 190     9533   8732  11317    935   -406    469       C  
ATOM    759  CG  ARG A 190      88.714  67.041  78.523  1.00 85.76           C  
ANISOU  759  CG  ARG A 190    10532   9597  12455    910   -598    406       C  
ATOM    760  CD  ARG A 190      88.910  66.886  80.029  1.00 96.21           C  
ANISOU  760  CD  ARG A 190    11960  10876  13718   1087   -648    277       C  
ATOM    761  NE  ARG A 190      88.333  65.645  80.546  1.00109.69           N  
ANISOU  761  NE  ARG A 190    13826  12597  15255   1216   -454    216       N  
ATOM    762  CZ  ARG A 190      89.039  64.652  81.082  1.00118.98           C  
ANISOU  762  CZ  ARG A 190    15065  13836  16306   1345   -374    200       C  
ATOM    763  NH1 ARG A 190      90.361  64.743  81.170  1.00119.25           N  
ANISOU  763  NH1 ARG A 190    15010  13947  16354   1377   -456    228       N  
ATOM    764  NH2 ARG A 190      88.425  63.561  81.527  1.00118.14           N  
ANISOU  764  NH2 ARG A 190    15107  13717  16065   1437   -221    171       N  
ATOM    765  N   SER A 191      91.040  65.963  75.032  1.00 66.85           N  
ANISOU  765  N   SER A 191     7725   7750   9925    746   -396    811       N  
ATOM    766  CA  SER A 191      92.163  66.582  74.333  1.00 62.77           C  
ANISOU  766  CA  SER A 191     6960   7428   9460    648   -487    994       C  
ATOM    767  C   SER A 191      91.803  67.049  72.935  1.00 65.89           C  
ANISOU  767  C   SER A 191     7220   7920   9894    497   -468   1143       C  
ATOM    768  O   SER A 191      92.583  67.784  72.319  1.00 66.90           O  
ANISOU  768  O   SER A 191     7118   8207  10095    370   -565   1339       O  
ATOM    769  CB  SER A 191      93.340  65.608  74.235  1.00 61.52           C  
ANISOU  769  CB  SER A 191     6740   7506   9128    801   -396   1017       C  
ATOM    770  OG  SER A 191      93.167  64.699  73.159  1.00 71.65           O  
ANISOU  770  OG  SER A 191     8034   8940  10249    876   -233   1028       O  
ATOM    771  N   MET A 192      90.646  66.640  72.425  1.00 70.78           N  
ANISOU  771  N   MET A 192     7968   8459  10468    502   -352   1071       N  
ATOM    772  CA  MET A 192      90.237  66.954  71.066  1.00 71.05           C  
ANISOU  772  CA  MET A 192     7892   8592  10510    387   -316   1194       C  
ATOM    773  C   MET A 192      89.014  67.858  71.029  1.00 73.83           C  
ANISOU  773  C   MET A 192     8304   8728  11019    247   -395   1172       C  
ATOM    774  O   MET A 192      88.347  67.948  69.996  1.00 75.17           O  
ANISOU  774  O   MET A 192     8446   8935  11182    176   -340   1225       O  
ATOM    775  CB  MET A 192      89.979  65.663  70.289  1.00 63.97           C  
ANISOU  775  CB  MET A 192     7079   7816   9412    527   -128   1129       C  
ATOM    776  CG  MET A 192      91.234  64.823  70.137  1.00 68.29           C  
ANISOU  776  CG  MET A 192     7547   8616   9785    691    -67   1155       C  
ATOM    777  SD  MET A 192      91.187  63.690  68.736  1.00 83.05           S  
ANISOU  777  SD  MET A 192     9418  10714  11423    846     84   1139       S  
ATOM    778  CE  MET A 192      90.344  62.284  69.407  1.00 80.24           C  
ANISOU  778  CE  MET A 192     9400  10107  10980   1011    170    891       C  
ATOM    779  N   LEU A 193      88.705  68.535  72.137  1.00 76.63           N  
ANISOU  779  N   LEU A 193     8741   8871  11505    228   -532   1084       N  
ATOM    780  CA  LEU A 193      87.508  69.369  72.174  1.00 76.88           C  
ANISOU  780  CA  LEU A 193     8842   8706  11664    137   -616   1036       C  
ATOM    781  C   LEU A 193      87.603  70.525  71.191  1.00 74.73           C  
ANISOU  781  C   LEU A 193     8394   8461  11540    -59   -756   1226       C  
ATOM    782  O   LEU A 193      86.582  70.965  70.650  1.00 71.15           O  
ANISOU  782  O   LEU A 193     7972   7921  11142   -134   -764   1223       O  
ATOM    783  CB  LEU A 193      87.267  69.898  73.586  1.00 74.36           C  
ANISOU  783  CB  LEU A 193     8634   8187  11431    201   -761    893       C  
ATOM    784  CG  LEU A 193      86.918  68.871  74.656  1.00 66.43           C  
ANISOU  784  CG  LEU A 193     7813   7142  10286    388   -631    715       C  
ATOM    785  CD1 LEU A 193      86.829  69.558  76.002  1.00 67.03           C  
ANISOU  785  CD1 LEU A 193     7961   7070  10436    466   -801    591       C  
ATOM    786  CD2 LEU A 193      85.609  68.189  74.309  1.00 66.58           C  
ANISOU  786  CD2 LEU A 193     7953   7127  10216    409   -460    644       C  
ATOM    787  N   ASP A 194      88.814  71.031  70.949  1.00 80.73           N  
ANISOU  787  N   ASP A 194     8959   9350  12366   -150   -873   1411       N  
ATOM    788  CA  ASP A 194      89.009  72.068  69.945  1.00 82.36           C  
ANISOU  788  CA  ASP A 194     8971   9615  12707   -357  -1005   1648       C  
ATOM    789  C   ASP A 194      88.776  71.556  68.530  1.00 76.54           C  
ANISOU  789  C   ASP A 194     8146   9104  11833   -373   -820   1760       C  
ATOM    790  O   ASP A 194      88.714  72.366  67.598  1.00 65.03           O  
ANISOU  790  O   ASP A 194     6540   7702  10465   -538   -902   1958       O  
ATOM    791  CB  ASP A 194      90.427  72.643  70.044  1.00 88.91           C  
ANISOU  791  CB  ASP A 194     9584  10564  13632   -462  -1172   1854       C  
ATOM    792  CG  ASP A 194      90.790  73.079  71.451  1.00 91.90           C  
ANISOU  792  CG  ASP A 194    10048  10735  14136   -423  -1372   1731       C  
ATOM    793  OD1 ASP A 194      91.513  72.324  72.137  1.00 96.35           O  
ANISOU  793  OD1 ASP A 194    10632  11388  14587   -283  -1298   1651       O  
ATOM    794  OD2 ASP A 194      90.352  74.171  71.872  1.00 91.61           O  
ANISOU  794  OD2 ASP A 194    10063  10443  14303   -514  -1617   1704       O  
ATOM    795  N   ASP A 195      88.637  70.240  68.353  1.00 78.81           N  
ANISOU  795  N   ASP A 195     8527   9513  11905   -200   -592   1637       N  
ATOM    796  CA  ASP A 195      88.641  69.627  67.038  1.00 78.17           C  
ANISOU  796  CA  ASP A 195     8357   9683  11660   -165   -432   1724       C  
ATOM    797  C   ASP A 195      87.407  68.794  66.718  1.00 80.15           C  
ANISOU  797  C   ASP A 195     8803   9844  11806    -69   -277   1542       C  
ATOM    798  O   ASP A 195      87.225  68.429  65.552  1.00 80.47           O  
ANISOU  798  O   ASP A 195     8784  10060  11731    -46   -178   1599       O  
ATOM    799  CB  ASP A 195      89.888  68.743  66.880  1.00 77.80           C  
ANISOU  799  CB  ASP A 195     8201   9933  11427    -22   -331   1774       C  
ATOM    800  CG  ASP A 195      91.176  69.532  67.002  1.00 91.26           C  
ANISOU  800  CG  ASP A 195     9659  11794  13220   -135   -476   2002       C  
ATOM    801  OD1 ASP A 195      91.298  70.568  66.316  1.00 99.33           O  
ANISOU  801  OD1 ASP A 195    10490  12884  14365   -331   -592   2237       O  
ATOM    802  OD2 ASP A 195      92.068  69.118  67.772  1.00 97.65           O  
ANISOU  802  OD2 ASP A 195    10459  12661  13981    -35   -483   1960       O  
ATOM    803  N   VAL A 196      86.552  68.492  67.699  1.00 79.65           N  
ANISOU  803  N   VAL A 196     8957   9531  11774    -11   -264   1336       N  
ATOM    804  CA  VAL A 196      85.478  67.531  67.458  1.00 73.97           C  
ANISOU  804  CA  VAL A 196     8412   8744  10949     76   -119   1182       C  
ATOM    805  C   VAL A 196      84.455  68.077  66.474  1.00 76.20           C  
ANISOU  805  C   VAL A 196     8668   8999  11286    -37   -124   1227       C  
ATOM    806  O   VAL A 196      83.847  67.309  65.717  1.00 82.89           O  
ANISOU  806  O   VAL A 196     9578   9893  12024     18     -9   1170       O  
ATOM    807  CB  VAL A 196      84.808  67.112  68.780  1.00 70.07           C  
ANISOU  807  CB  VAL A 196     8125   8026  10472    150   -104    995       C  
ATOM    808  CG1 VAL A 196      85.706  66.156  69.545  1.00 80.82           C  
ANISOU  808  CG1 VAL A 196     9549   9439  11722    302    -50    931       C  
ATOM    809  CG2 VAL A 196      84.470  68.330  69.626  1.00 63.94           C  
ANISOU  809  CG2 VAL A 196     7349   7075   9872     63   -266    982       C  
ATOM    810  N   ALA A 197      84.241  69.394  66.460  1.00 69.78           N  
ANISOU  810  N   ALA A 197     7771   8096  10646   -189   -275   1325       N  
ATOM    811  CA  ALA A 197      83.258  69.964  65.546  1.00 69.81           C  
ANISOU  811  CA  ALA A 197     7754   8068  10705   -292   -291   1369       C  
ATOM    812  C   ALA A 197      83.683  69.767  64.096  1.00 68.83           C  
ANISOU  812  C   ALA A 197     7472   8210  10469   -306   -217   1528       C  
ATOM    813  O   ALA A 197      82.881  69.351  63.252  1.00 64.16           O  
ANISOU  813  O   ALA A 197     6924   7655   9798   -280   -125   1483       O  
ATOM    814  CB  ALA A 197      83.051  71.448  65.851  1.00 71.38           C  
ANISOU  814  CB  ALA A 197     7902   8103  11117   -438   -504   1446       C  
ATOM    815  N   GLU A 198      84.951  70.055  63.792  1.00 72.33           N  
ANISOU  815  N   GLU A 198     7721   8866  10896   -336   -260   1721       N  
ATOM    816  CA  GLU A 198      85.437  69.907  62.426  1.00 67.89           C  
ANISOU  816  CA  GLU A 198     6975   8622  10197   -326   -188   1896       C  
ATOM    817  C   GLU A 198      85.616  68.443  62.052  1.00 71.76           C  
ANISOU  817  C   GLU A 198     7537   9286  10442   -102    -13   1762       C  
ATOM    818  O   GLU A 198      85.416  68.074  60.890  1.00 88.15           O  
ANISOU  818  O   GLU A 198     9559  11557  12377    -36     68   1793       O  
ATOM    819  CB  GLU A 198      86.749  70.668  62.256  1.00 65.27           C  
ANISOU  819  CB  GLU A 198     6383   8501   9914   -432   -292   2173       C  
ATOM    820  CG  GLU A 198      87.209  70.792  60.824  1.00 74.16           C  
ANISOU  820  CG  GLU A 198     7270   9993  10912   -451   -239   2415       C  
ATOM    821  CD  GLU A 198      88.530  71.521  60.703  1.00 84.81           C  
ANISOU  821  CD  GLU A 198     8332  11580  12310   -575   -344   2728       C  
ATOM    822  OE1 GLU A 198      88.839  72.340  61.594  1.00 91.06           O  
ANISOU  822  OE1 GLU A 198     9114  12164  13319   -725   -523   2786       O  
ATOM    823  OE2 GLU A 198      89.263  71.267  59.723  1.00100.04           O  
ANISOU  823  OE2 GLU A 198    10039  13917  14055   -514   -257   2918       O  
ATOM    824  N   LEU A 199      85.975  67.597  63.021  1.00 56.61           N  
ANISOU  824  N   LEU A 199     5750   7290   8468     30     28   1604       N  
ATOM    825  CA  LEU A 199      86.162  66.176  62.756  1.00 55.67           C  
ANISOU  825  CA  LEU A 199     5731   7291   8132    254    156   1461       C  
ATOM    826  C   LEU A 199      84.841  65.447  62.559  1.00 62.55           C  
ANISOU  826  C   LEU A 199     6820   7971   8977    302    217   1267       C  
ATOM    827  O   LEU A 199      84.834  64.336  62.018  1.00 63.01           O  
ANISOU  827  O   LEU A 199     6959   8119   8862    475    289   1158       O  
ATOM    828  CB  LEU A 199      86.927  65.518  63.907  1.00 52.91           C  
ANISOU  828  CB  LEU A 199     5467   6890   7747    372    162   1362       C  
ATOM    829  CG  LEU A 199      88.433  65.748  64.054  1.00 57.29           C  
ANISOU  829  CG  LEU A 199     5817   7697   8253    404    129   1516       C  
ATOM    830  CD1 LEU A 199      88.903  65.188  65.384  1.00 54.68           C  
ANISOU  830  CD1 LEU A 199     5619   7230   7926    501    120   1383       C  
ATOM    831  CD2 LEU A 199      89.233  65.154  62.901  1.00 65.41           C  
ANISOU  831  CD2 LEU A 199     6687   9121   9044    571    210   1598       C  
ATOM    832  N   SER A 200      83.728  66.031  63.006  1.00 62.21           N  
ANISOU  832  N   SER A 200     6871   7668   9098    161    173   1217       N  
ATOM    833  CA  SER A 200      82.448  65.343  62.894  1.00 61.77           C  
ANISOU  833  CA  SER A 200     7003   7439   9027    185    225   1052       C  
ATOM    834  C   SER A 200      82.066  65.080  61.448  1.00 56.79           C  
ANISOU  834  C   SER A 200     6326   6963   8287    226    265   1068       C  
ATOM    835  O   SER A 200      81.340  64.120  61.174  1.00 59.50           O  
ANISOU  835  O   SER A 200     6822   7224   8560    307    306    921       O  
ATOM    836  CB  SER A 200      81.348  66.152  63.582  1.00 61.39           C  
ANISOU  836  CB  SER A 200     7022   7146   9159     37    167   1017       C  
ATOM    837  OG  SER A 200      81.662  66.370  64.944  1.00 60.73           O  
ANISOU  837  OG  SER A 200     6988   6930   9155     33    121    981       O  
ATOM    838  N   SER A 201      82.542  65.903  60.518  1.00 51.28           N  
ANISOU  838  N   SER A 201     5419   6492   7573    170    241   1254       N  
ATOM    839  CA  SER A 201      82.237  65.735  59.105  1.00 56.66           C  
ANISOU  839  CA  SER A 201     6034   7365   8130    226    279   1285       C  
ATOM    840  C   SER A 201      83.358  65.052  58.332  1.00 54.18           C  
ANISOU  840  C   SER A 201     5606   7398   7582    431    331   1329       C  
ATOM    841  O   SER A 201      83.259  64.925  57.110  1.00 58.67           O  
ANISOU  841  O   SER A 201     6094   8190   8011    516    359   1364       O  
ATOM    842  CB  SER A 201      81.919  67.094  58.477  1.00 54.94           C  
ANISOU  842  CB  SER A 201     5652   7196   8028     41    218   1479       C  
ATOM    843  OG  SER A 201      80.715  67.621  59.010  1.00 60.74           O  
ANISOU  843  OG  SER A 201     6507   7630   8942    -99    167   1399       O  
ATOM    844  N   ASP A 202      84.410  64.602  59.010  1.00 55.21           N  
ANISOU  844  N   ASP A 202     5725   7602   7650    535    342   1320       N  
ATOM    845  CA  ASP A 202      85.527  63.953  58.341  1.00 61.16           C  
ANISOU  845  CA  ASP A 202     6359   8719   8161    762    387   1354       C  
ATOM    846  C   ASP A 202      85.180  62.501  58.028  1.00 65.49           C  
ANISOU  846  C   ASP A 202     7121   9222   8538   1010    414   1101       C  
ATOM    847  O   ASP A 202      84.365  61.876  58.712  1.00 64.74           O  
ANISOU  847  O   ASP A 202     7272   8791   8533    992    395    916       O  
ATOM    848  CB  ASP A 202      86.786  64.025  59.211  1.00 61.97           C  
ANISOU  848  CB  ASP A 202     6366   8917   8262    785    376   1436       C  
ATOM    849  CG  ASP A 202      88.030  63.547  58.483  1.00 73.17           C  
ANISOU  849  CG  ASP A 202     7599  10783   9420   1014    422   1516       C  
ATOM    850  OD1 ASP A 202      88.379  64.164  57.449  1.00 85.09           O  
ANISOU  850  OD1 ASP A 202     8858  12630  10844    992    437   1729       O  
ATOM    851  OD2 ASP A 202      88.664  62.573  58.944  1.00 67.87           O  
ANISOU  851  OD2 ASP A 202     7021  10146   8621   1224    440   1378       O  
ATOM    852  N   TYR A 203      85.794  61.970  56.966  1.00 75.02           N  
ANISOU  852  N   TYR A 203     8228  10782   9493   1248    441   1103       N  
ATOM    853  CA  TYR A 203      85.534  60.582  56.590  1.00 78.02           C  
ANISOU  853  CA  TYR A 203     8821  11119   9704   1516    423    847       C  
ATOM    854  C   TYR A 203      85.918  59.629  57.707  1.00 71.26           C  
ANISOU  854  C   TYR A 203     8165  10055   8855   1624    398    686       C  
ATOM    855  O   TYR A 203      85.237  58.622  57.939  1.00 66.35           O  
ANISOU  855  O   TYR A 203     7810   9154   8247   1702    345    471       O  
ATOM    856  CB  TYR A 203      86.286  60.209  55.314  1.00 86.59           C  
ANISOU  856  CB  TYR A 203     9747  12668  10484   1807    443    868       C  
ATOM    857  CG  TYR A 203      86.321  58.711  55.073  1.00100.30           C  
ANISOU  857  CG  TYR A 203    11712  14371  12028   2143    384    583       C  
ATOM    858  CD1 TYR A 203      85.185  58.032  54.647  1.00104.42           C  
ANISOU  858  CD1 TYR A 203    12468  14637  12571   2187    310    374       C  
ATOM    859  CD2 TYR A 203      87.489  57.978  55.262  1.00105.43           C  
ANISOU  859  CD2 TYR A 203    12344  15238  12477   2421    379    522       C  
ATOM    860  CE1 TYR A 203      85.205  56.666  54.424  1.00104.17           C  
ANISOU  860  CE1 TYR A 203    12663  14533  12386   2489    210    111       C  
ATOM    861  CE2 TYR A 203      87.516  56.608  55.038  1.00111.61           C  
ANISOU  861  CE2 TYR A 203    13358  15962  13088   2748    289    247       C  
ATOM    862  CZ  TYR A 203      86.370  55.960  54.619  1.00108.35           C  
ANISOU  862  CZ  TYR A 203    13189  15260  12718   2775    194     42       C  
ATOM    863  OH  TYR A 203      86.384  54.603  54.393  1.00115.33           O  
ANISOU  863  OH  TYR A 203    14321  16046  13455   3093     60   -234       O  
ATOM    864  N   LEU A 204      87.020  59.918  58.394  1.00 72.36           N  
ANISOU  864  N   LEU A 204     8176  10330   8987   1626    421    798       N  
ATOM    865  CA  LEU A 204      87.440  59.149  59.554  1.00 72.95           C  
ANISOU  865  CA  LEU A 204     8424  10214   9081   1710    399    672       C  
ATOM    866  C   LEU A 204      86.939  59.743  60.858  1.00 67.70           C  
ANISOU  866  C   LEU A 204     7838   9206   8679   1442    392    707       C  
ATOM    867  O   LEU A 204      86.523  59.000  61.747  1.00 66.33           O  
ANISOU  867  O   LEU A 204     7901   8732   8570   1456    367    560       O  
ATOM    868  CB  LEU A 204      88.966  59.054  59.603  1.00 74.14           C  
ANISOU  868  CB  LEU A 204     8389  10726   9054   1896    423    756       C  
ATOM    869  CG  LEU A 204      89.581  58.093  58.593  1.00 80.83           C  
ANISOU  869  CG  LEU A 204     9219  11903   9589   2266    416    647       C  
ATOM    870  CD1 LEU A 204      91.105  58.220  58.571  1.00 81.60           C  
ANISOU  870  CD1 LEU A 204     9060  12441   9503   2429    454    783       C  
ATOM    871  CD2 LEU A 204      89.141  56.672  58.887  1.00 84.13           C  
ANISOU  871  CD2 LEU A 204     9984  12023   9959   2470    336    353       C  
ATOM    872  N   GLY A 205      86.964  61.071  60.982  1.00 63.44           N  
ANISOU  872  N   GLY A 205     7106   8711   8287   1209    398    906       N  
ATOM    873  CA  GLY A 205      86.602  61.697  62.241  1.00 64.46           C  
ANISOU  873  CA  GLY A 205     7299   8552   8643    999    370    926       C  
ATOM    874  C   GLY A 205      85.176  61.394  62.655  1.00 66.70           C  
ANISOU  874  C   GLY A 205     7814   8477   9051    903    362    784       C  
ATOM    875  O   GLY A 205      84.893  61.205  63.840  1.00 75.65           O  
ANISOU  875  O   GLY A 205     9090   9367  10285    854    351    713       O  
ATOM    876  N   ASN A 206      84.261  61.318  61.681  1.00 59.58           N  
ANISOU  876  N   ASN A 206     6943   7562   8132    882    367    749       N  
ATOM    877  CA  ASN A 206      82.860  61.070  62.004  1.00 61.66           C  
ANISOU  877  CA  ASN A 206     7395   7516   8517    772    355    638       C  
ATOM    878  C   ASN A 206      82.691  59.725  62.701  1.00 60.91           C  
ANISOU  878  C   ASN A 206     7543   7217   8384    889    342    472       C  
ATOM    879  O   ASN A 206      81.862  59.589  63.607  1.00 63.09           O  
ANISOU  879  O   ASN A 206     7953   7235   8782    777    338    428       O  
ATOM    880  CB  ASN A 206      81.999  61.153  60.737  1.00 63.65           C  
ANISOU  880  CB  ASN A 206     7626   7818   8740    750    352    626       C  
ATOM    881  CG  ASN A 206      81.818  59.811  60.050  1.00 64.51           C  
ANISOU  881  CG  ASN A 206     7892   7921   8698    951    327    459       C  
ATOM    882  OD1 ASN A 206      80.935  59.034  60.418  1.00 55.92           O  
ANISOU  882  OD1 ASN A 206     7010   6567   7671    927    292    332       O  
ATOM    883  ND2 ASN A 206      82.633  59.544  59.028  1.00 71.23           N  
ANISOU  883  ND2 ASN A 206     8641   9074   9349   1154    329    465       N  
ATOM    884  N   THR A 207      83.484  58.724  62.311  1.00 59.08           N  
ANISOU  884  N   THR A 207     7365   7109   7976   1124    326    390       N  
ATOM    885  CA  THR A 207      83.416  57.436  62.992  1.00 68.28           C  
ANISOU  885  CA  THR A 207     8772   8060   9113   1238    284    245       C  
ATOM    886  C   THR A 207      83.980  57.515  64.407  1.00 72.94           C  
ANISOU  886  C   THR A 207     9387   8562   9764   1209    303    279       C  
ATOM    887  O   THR A 207      83.494  56.815  65.303  1.00 73.52           O  
ANISOU  887  O   THR A 207     9651   8384   9899   1184    281    215       O  
ATOM    888  CB  THR A 207      84.145  56.366  62.174  1.00 75.80           C  
ANISOU  888  CB  THR A 207     9786   9165   9850   1533    232    127       C  
ATOM    889  OG1 THR A 207      85.505  56.760  61.953  1.00 76.80           O  
ANISOU  889  OG1 THR A 207     9709   9635   9836   1671    273    211       O  
ATOM    890  CG2 THR A 207      83.459  56.163  60.834  1.00 82.63           C  
ANISOU  890  CG2 THR A 207    10662  10084  10650   1584    190     59       C  
ATOM    891  N   VAL A 208      84.982  58.369  64.635  1.00 73.97           N  
ANISOU  891  N   VAL A 208     9322   8899   9883   1202    335    394       N  
ATOM    892  CA  VAL A 208      85.580  58.490  65.963  1.00 71.71           C  
ANISOU  892  CA  VAL A 208     9052   8544   9649   1190    339    417       C  
ATOM    893  C   VAL A 208      84.691  59.316  66.885  1.00 73.58           C  
ANISOU  893  C   VAL A 208     9302   8577  10077    970    344    462       C  
ATOM    894  O   VAL A 208      84.497  58.966  68.055  1.00 71.98           O  
ANISOU  894  O   VAL A 208     9229   8198   9921    962    343    421       O  
ATOM    895  CB  VAL A 208      86.993  59.091  65.860  1.00 64.69           C  
ANISOU  895  CB  VAL A 208     7940   7954   8687   1260    346    527       C  
ATOM    896  CG1 VAL A 208      87.519  59.437  67.240  1.00 59.75           C  
ANISOU  896  CG1 VAL A 208     7313   7246   8146   1216    332    556       C  
ATOM    897  CG2 VAL A 208      87.935  58.127  65.155  1.00 58.88           C  
ANISOU  897  CG2 VAL A 208     7201   7447   7725   1534    343    462       C  
ATOM    898  N   VAL A 209      84.155  60.429  66.377  1.00 71.42           N  
ANISOU  898  N   VAL A 209     8892   8342   9902    808    342    549       N  
ATOM    899  CA  VAL A 209      83.208  61.231  67.146  1.00 63.27           C  
ANISOU  899  CA  VAL A 209     7876   7131   9033    632    330    569       C  
ATOM    900  C   VAL A 209      81.987  60.405  67.535  1.00 65.42           C  
ANISOU  900  C   VAL A 209     8346   7181   9331    604    351    476       C  
ATOM    901  O   VAL A 209      81.436  60.565  68.631  1.00 63.24           O  
ANISOU  901  O   VAL A 209     8131   6765   9130    540    355    466       O  
ATOM    902  CB  VAL A 209      82.829  62.496  66.353  1.00 55.04           C  
ANISOU  902  CB  VAL A 209     6666   6166   8081    485    303    671       C  
ATOM    903  CG1 VAL A 209      81.746  63.283  67.070  1.00 43.54           C  
ANISOU  903  CG1 VAL A 209     5241   4527   6775    340    275    662       C  
ATOM    904  CG2 VAL A 209      84.060  63.369  66.181  1.00 45.20           C  
ANISOU  904  CG2 VAL A 209     5213   5121   6840    475    260    807       C  
ATOM    905  N   GLN A 210      81.546  59.506  66.655  1.00 63.25           N  
ANISOU  905  N   GLN A 210     8162   6881   8988    654    352    413       N  
ATOM    906  CA  GLN A 210      80.455  58.609  67.017  1.00 55.91           C  
ANISOU  906  CA  GLN A 210     7415   5733   8093    611    346    349       C  
ATOM    907  C   GLN A 210      80.821  57.797  68.247  1.00 62.26           C  
ANISOU  907  C   GLN A 210     8358   6423   8875    684    345    324       C  
ATOM    908  O   GLN A 210      80.124  57.840  69.268  1.00 65.53           O  
ANISOU  908  O   GLN A 210     8825   6713   9361    593    364    351       O  
ATOM    909  CB  GLN A 210      80.120  57.681  65.855  1.00 54.27           C  
ANISOU  909  CB  GLN A 210     7300   5506   7816    681    305    272       C  
ATOM    910  CG  GLN A 210      79.241  58.301  64.806  1.00 59.10           C  
ANISOU  910  CG  GLN A 210     7823   6159   8472    573    305    289       C  
ATOM    911  CD  GLN A 210      78.822  57.294  63.765  1.00 61.11           C  
ANISOU  911  CD  GLN A 210     8194   6363   8661    653    240    190       C  
ATOM    912  OE1 GLN A 210      78.002  56.408  64.031  1.00 62.24           O  
ANISOU  912  OE1 GLN A 210     8501   6291   8856    605    188    140       O  
ATOM    913  NE2 GLN A 210      79.421  57.390  62.582  1.00 52.82           N  
ANISOU  913  NE2 GLN A 210     7058   5521   7492    784    228    168       N  
ATOM    914  N   LYS A 211      81.934  57.062  68.168  1.00 61.86           N  
ANISOU  914  N   LYS A 211     8358   6437   8709    864    322    279       N  
ATOM    915  CA  LYS A 211      82.381  56.251  69.295  1.00 62.25           C  
ANISOU  915  CA  LYS A 211     8546   6381   8726    952    311    256       C  
ATOM    916  C   LYS A 211      82.481  57.081  70.573  1.00 56.98           C  
ANISOU  916  C   LYS A 211     7808   5717   8126    882    352    320       C  
ATOM    917  O   LYS A 211      82.124  56.606  71.656  1.00 61.59           O  
ANISOU  917  O   LYS A 211     8504   6169   8727    868    360    331       O  
ATOM    918  CB  LYS A 211      83.725  55.598  68.960  1.00 65.82           C  
ANISOU  918  CB  LYS A 211     9018   6959   9031   1181    278    196       C  
ATOM    919  CG  LYS A 211      83.709  54.719  67.708  1.00 72.56           C  
ANISOU  919  CG  LYS A 211     9956   7828   9786   1313    212    101       C  
ATOM    920  CD  LYS A 211      82.860  53.478  67.916  1.00 79.63           C  
ANISOU  920  CD  LYS A 211    11100   8436  10719   1301    128     38       C  
ATOM    921  CE  LYS A 211      82.668  52.703  66.628  1.00 84.12           C  
ANISOU  921  CE  LYS A 211    11762   8987  11213   1422     27    -76       C  
ATOM    922  NZ  LYS A 211      81.594  51.686  66.814  1.00 88.18           N  
ANISOU  922  NZ  LYS A 211    12499   9182  11822   1331    -81   -104       N  
ATOM    923  N   PHE A 212      82.933  58.334  70.462  1.00 51.77           N  
ANISOU  923  N   PHE A 212     6961   5206   7502    839    361    368       N  
ATOM    924  CA  PHE A 212      83.096  59.169  71.650  1.00 63.33           C  
ANISOU  924  CA  PHE A 212     8367   6666   9031    801    361    403       C  
ATOM    925  C   PHE A 212      81.771  59.360  72.372  1.00 64.35           C  
ANISOU  925  C   PHE A 212     8551   6662   9237    686    383    412       C  
ATOM    926  O   PHE A 212      81.713  59.298  73.603  1.00 73.85           O  
ANISOU  926  O   PHE A 212     9807   7817  10437    717    392    413       O  
ATOM    927  CB  PHE A 212      83.690  60.528  71.275  1.00 66.97           C  
ANISOU  927  CB  PHE A 212     8622   7274   9550    747    323    463       C  
ATOM    928  CG  PHE A 212      85.172  60.496  71.046  1.00 66.60           C  
ANISOU  928  CG  PHE A 212     8479   7402   9425    861    301    489       C  
ATOM    929  CD1 PHE A 212      85.893  59.330  71.254  1.00 64.60           C  
ANISOU  929  CD1 PHE A 212     8333   7167   9046   1031    318    433       C  
ATOM    930  CD2 PHE A 212      85.846  61.631  70.629  1.00 60.70           C  
ANISOU  930  CD2 PHE A 212     7526   6805   8730    797    251    583       C  
ATOM    931  CE1 PHE A 212      87.250  59.290  71.038  1.00 60.55           C  
ANISOU  931  CE1 PHE A 212     7713   6849   8442   1154    302    457       C  
ATOM    932  CE2 PHE A 212      87.205  61.597  70.415  1.00 52.97           C  
ANISOU  932  CE2 PHE A 212     6427   6024   7674    892    233    635       C  
ATOM    933  CZ  PHE A 212      87.907  60.423  70.622  1.00 59.82           C  
ANISOU  933  CZ  PHE A 212     7393   6938   8397   1081    267    565       C  
ATOM    934  N   PHE A 213      80.695  59.599  71.626  1.00 59.23           N  
ANISOU  934  N   PHE A 213     7881   5979   8645    568    392    422       N  
ATOM    935  CA  PHE A 213      79.387  59.723  72.251  1.00 54.06           C  
ANISOU  935  CA  PHE A 213     7259   5237   8045    468    418    440       C  
ATOM    936  C   PHE A 213      78.814  58.375  72.672  1.00 61.18           C  
ANISOU  936  C   PHE A 213     8322   6014   8910    467    441    454       C  
ATOM    937  O   PHE A 213      77.904  58.335  73.507  1.00 74.32           O  
ANISOU  937  O   PHE A 213    10004   7641  10592    406    472    500       O  
ATOM    938  CB  PHE A 213      78.418  60.439  71.306  1.00 51.96           C  
ANISOU  938  CB  PHE A 213     6907   4985   7852    343    413    450       C  
ATOM    939  CG  PHE A 213      78.596  61.936  71.262  1.00 49.12           C  
ANISOU  939  CG  PHE A 213     6397   4703   7562    308    368    463       C  
ATOM    940  CD1 PHE A 213      77.765  62.770  71.992  1.00 46.46           C  
ANISOU  940  CD1 PHE A 213     6022   4350   7280    268    352    457       C  
ATOM    941  CD2 PHE A 213      79.594  62.509  70.489  1.00 55.15           C  
ANISOU  941  CD2 PHE A 213     7056   5565   8334    323    324    489       C  
ATOM    942  CE1 PHE A 213      77.923  64.150  71.947  1.00 50.87           C  
ANISOU  942  CE1 PHE A 213     6468   4943   7918    245    267    457       C  
ATOM    943  CE2 PHE A 213      79.760  63.886  70.444  1.00 55.45           C  
ANISOU  943  CE2 PHE A 213     6963   5643   8460    267    248    524       C  
ATOM    944  CZ  PHE A 213      78.925  64.707  71.174  1.00 53.87           C  
ANISOU  944  CZ  PHE A 213     6754   5381   8333    230    207    498       C  
ATOM    945  N   GLU A 214      79.323  57.270  72.124  1.00 56.55           N  
ANISOU  945  N   GLU A 214     7848   5370   8269    539    412    423       N  
ATOM    946  CA  GLU A 214      78.832  55.967  72.549  1.00 72.39           C  
ANISOU  946  CA  GLU A 214    10023   7219  10262    526    394    451       C  
ATOM    947  C   GLU A 214      79.469  55.527  73.859  1.00 83.77           C  
ANISOU  947  C   GLU A 214    11540   8642  11648    623    406    479       C  
ATOM    948  O   GLU A 214      78.843  54.794  74.633  1.00 90.95           O  
ANISOU  948  O   GLU A 214    12545   9450  12563    573    410    556       O  
ATOM    949  CB  GLU A 214      79.100  54.904  71.480  1.00 78.46           C  
ANISOU  949  CB  GLU A 214    10916   7901  10996    591    316    386       C  
ATOM    950  CG  GLU A 214      78.534  55.198  70.104  1.00 81.68           C  
ANISOU  950  CG  GLU A 214    11264   8335  11436    526    293    346       C  
ATOM    951  CD  GLU A 214      78.750  54.045  69.133  1.00 88.22           C  
ANISOU  951  CD  GLU A 214    12237   9069  12214    627    189    259       C  
ATOM    952  OE1 GLU A 214      77.947  53.084  69.161  1.00 90.81           O  
ANISOU  952  OE1 GLU A 214    12711   9198  12594    553    112    272       O  
ATOM    953  OE2 GLU A 214      79.733  54.083  68.362  1.00 89.65           O  
ANISOU  953  OE2 GLU A 214    12384   9380  12298    789    170    181       O  
ATOM    954  N   TYR A 215      80.696  55.963  74.127  1.00 79.26           N  
ANISOU  954  N   TYR A 215    10916   8177  11023    755    408    434       N  
ATOM    955  CA  TYR A 215      81.469  55.412  75.228  1.00 76.38           C  
ANISOU  955  CA  TYR A 215    10636   7794  10589    878    406    442       C  
ATOM    956  C   TYR A 215      81.793  56.403  76.338  1.00 71.27           C  
ANISOU  956  C   TYR A 215     9885   7255   9938    913    437    453       C  
ATOM    957  O   TYR A 215      81.917  55.986  77.489  1.00 87.14           O  
ANISOU  957  O   TYR A 215    11967   9243  11898    977    451    486       O  
ATOM    958  CB  TYR A 215      82.771  54.788  74.696  1.00 77.66           C  
ANISOU  958  CB  TYR A 215    10855   7984  10667   1048    356    367       C  
ATOM    959  CG  TYR A 215      82.533  53.589  73.794  1.00 89.57           C  
ANISOU  959  CG  TYR A 215    12517   9359  12156   1074    286    327       C  
ATOM    960  CD1 TYR A 215      81.874  52.464  74.269  1.00 95.45           C  
ANISOU  960  CD1 TYR A 215    13444   9900  12922   1031    239    376       C  
ATOM    961  CD2 TYR A 215      82.978  53.574  72.480  1.00 93.44           C  
ANISOU  961  CD2 TYR A 215    12969   9930  12603   1150    249    248       C  
ATOM    962  CE1 TYR A 215      81.656  51.365  73.464  1.00 98.55           C  
ANISOU  962  CE1 TYR A 215    13997  10133  13316   1057    130    330       C  
ATOM    963  CE2 TYR A 215      82.762  52.473  71.666  1.00 95.09           C  
ANISOU  963  CE2 TYR A 215    13333  10011  12784   1209    155    183       C  
ATOM    964  CZ  TYR A 215      82.104  51.373  72.166  1.00 98.08           C  
ANISOU  964  CZ  TYR A 215    13912  10147  13206   1161     83    215       C  
ATOM    965  OH  TYR A 215      81.887  50.276  71.366  1.00104.01           O  
ANISOU  965  OH  TYR A 215    14837  10734  13949   1220    -54    140       O  
ATOM    966  N   CYS A 216      81.915  57.693  76.047  1.00 54.66           N  
ANISOU  966  N   CYS A 216     7623   5259   7886    878    430    428       N  
ATOM    967  CA  CYS A 216      82.178  58.646  77.115  1.00 57.46           C  
ANISOU  967  CA  CYS A 216     7897   5687   8248    924    418    418       C  
ATOM    968  C   CYS A 216      80.948  58.842  77.997  1.00 66.36           C  
ANISOU  968  C   CYS A 216     9032   6803   9380    873    457    458       C  
ATOM    969  O   CYS A 216      79.803  58.713  77.554  1.00 71.04           O  
ANISOU  969  O   CYS A 216     9625   7360  10008    755    490    500       O  
ATOM    970  CB  CYS A 216      82.625  59.987  76.545  1.00 58.09           C  
ANISOU  970  CB  CYS A 216     7814   5853   8403    889    359    392       C  
ATOM    971  SG  CYS A 216      84.191  59.909  75.676  1.00 69.38           S  
ANISOU  971  SG  CYS A 216     9175   7383   9802    962    319    384       S  
ATOM    972  N   SER A 217      81.201  59.150  79.266  1.00 69.31           N  
ANISOU  972  N   SER A 217     9401   7231   9704    978    450    446       N  
ATOM    973  CA  SER A 217      80.122  59.415  80.200  1.00 74.01           C  
ANISOU  973  CA  SER A 217     9976   7878  10265    977    487    482       C  
ATOM    974  C   SER A 217      79.454  60.748  79.870  1.00 77.03           C  
ANISOU  974  C   SER A 217    10234   8313  10722    925    444    432       C  
ATOM    975  O   SER A 217      79.934  61.535  79.048  1.00 79.62           O  
ANISOU  975  O   SER A 217    10491   8624  11136    885    373    380       O  
ATOM    976  CB  SER A 217      80.643  59.412  81.635  1.00 81.18           C  
ANISOU  976  CB  SER A 217    10912   8857  11077   1143    479    467       C  
ATOM    977  OG  SER A 217      81.633  60.409  81.814  1.00 92.59           O  
ANISOU  977  OG  SER A 217    12289  10337  12553   1235    381    363       O  
ATOM    978  N   ASP A 218      78.334  61.003  80.540  1.00 74.59           N  
ANISOU  978  N   ASP A 218     9889   8081  10368    933    479    458       N  
ATOM    979  CA  ASP A 218      77.502  62.148  80.180  1.00 70.55           C  
ANISOU  979  CA  ASP A 218     9274   7615   9917    892    436    409       C  
ATOM    980  C   ASP A 218      78.194  63.501  80.312  1.00 72.22           C  
ANISOU  980  C   ASP A 218     9420   7829  10190    978    294    290       C  
ATOM    981  O   ASP A 218      77.901  64.387  79.489  1.00 71.85           O  
ANISOU  981  O   ASP A 218     9305   7750  10244    899    225    256       O  
ATOM    982  CB  ASP A 218      76.211  62.126  81.004  1.00 67.90           C  
ANISOU  982  CB  ASP A 218     8900   7411   9488    926    501    459       C  
ATOM    983  CG  ASP A 218      75.269  61.025  80.569  1.00 81.25           C  
ANISOU  983  CG  ASP A 218    10616   9083  11171    770    607    602       C  
ATOM    984  OD1 ASP A 218      75.397  60.551  79.417  1.00 84.92           O  
ANISOU  984  OD1 ASP A 218    11124   9419  11725    634    606    619       O  
ATOM    985  OD2 ASP A 218      74.390  60.645  81.371  1.00 86.45           O  
ANISOU  985  OD2 ASP A 218    11245   9870  11733    786    680    701       O  
ATOM    986  N   PRO A 219      79.067  63.753  81.293  1.00 72.74           N  
ANISOU  986  N   PRO A 219     9505   7922  10212   1131    226    228       N  
ATOM    987  CA  PRO A 219      79.705  65.078  81.334  1.00 73.35           C  
ANISOU  987  CA  PRO A 219     9521   7967  10381   1186     47    122       C  
ATOM    988  C   PRO A 219      80.603  65.337  80.142  1.00 69.00           C  
ANISOU  988  C   PRO A 219     8926   7330   9962   1055    -14    150       C  
ATOM    989  O   PRO A 219      80.682  66.477  79.673  1.00 57.69           O  
ANISOU  989  O   PRO A 219     7420   5852   8648   1005   -154    116       O  
ATOM    990  CB  PRO A 219      80.499  65.050  82.648  1.00 68.01           C  
ANISOU  990  CB  PRO A 219     8885   7338   9620   1377     -8     60       C  
ATOM    991  CG  PRO A 219      79.833  64.024  83.467  1.00 73.07           C  
ANISOU  991  CG  PRO A 219     9584   8079  10100   1448    144    126       C  
ATOM    992  CD  PRO A 219      79.389  62.971  82.499  1.00 69.99           C  
ANISOU  992  CD  PRO A 219     9227   7637   9730   1268    283    251       C  
ATOM    993  N   ILE A 220      81.284  64.313  79.633  1.00 72.43           N  
ANISOU  993  N   ILE A 220     9400   7752  10370   1007     75    218       N  
ATOM    994  CA  ILE A 220      82.168  64.523  78.495  1.00 74.34           C  
ANISOU  994  CA  ILE A 220     9574   7973  10700    909     29    258       C  
ATOM    995  C   ILE A 220      81.357  64.637  77.211  1.00 70.65           C  
ANISOU  995  C   ILE A 220     9066   7486  10293    759     70    306       C  
ATOM    996  O   ILE A 220      81.695  65.425  76.318  1.00 69.62           O  
ANISOU  996  O   ILE A 220     8837   7354  10261    668    -12    337       O  
ATOM    997  CB  ILE A 220      83.224  63.403  78.417  1.00 79.11           C  
ANISOU  997  CB  ILE A 220    10230   8603  11226    960     97    293       C  
ATOM    998  CG1 ILE A 220      84.374  63.669  79.397  1.00 77.14           C  
ANISOU  998  CG1 ILE A 220     9968   8382  10959   1086      6    249       C  
ATOM    999  CG2 ILE A 220      83.773  63.275  77.003  1.00 83.20           C  
ANISOU  999  CG2 ILE A 220    10680   9151  11782    866    107    353       C  
ATOM   1000  CD1 ILE A 220      84.044  63.392  80.851  1.00 80.35           C  
ANISOU 1000  CD1 ILE A 220    10466   8796  11269   1232     26    194       C  
ATOM   1001  N   LYS A 221      80.266  63.874  77.101  1.00 61.05           N  
ANISOU 1001  N   LYS A 221     7916   6260   9021    722    186    327       N  
ATOM   1002  CA  LYS A 221      79.357  64.078  75.979  1.00 53.93           C  
ANISOU 1002  CA  LYS A 221     6973   5341   8177    590    211    356       C  
ATOM   1003  C   LYS A 221      78.860  65.516  75.952  1.00 65.32           C  
ANISOU 1003  C   LYS A 221     8327   6778   9713    564     95    316       C  
ATOM   1004  O   LYS A 221      78.923  66.190  74.917  1.00 71.51           O  
ANISOU 1004  O   LYS A 221     9035   7547  10589    464     34    345       O  
ATOM   1005  CB  LYS A 221      78.181  63.107  76.052  1.00 43.04           C  
ANISOU 1005  CB  LYS A 221     5667   3949   6735    550    327    390       C  
ATOM   1006  CG  LYS A 221      78.597  61.655  76.076  1.00 57.81           C  
ANISOU 1006  CG  LYS A 221     7651   5782   8532    571    402    430       C  
ATOM   1007  CD  LYS A 221      77.528  60.779  75.466  1.00 59.41           C  
ANISOU 1007  CD  LYS A 221     7908   5932   8732    462    468    483       C  
ATOM   1008  CE  LYS A 221      76.170  60.971  76.100  1.00 58.94           C  
ANISOU 1008  CE  LYS A 221     7817   5915   8661    418    509    520       C  
ATOM   1009  NZ  LYS A 221      75.238  59.977  75.500  1.00 48.29           N  
ANISOU 1009  NZ  LYS A 221     6521   4503   7325    291    555    593       N  
ATOM   1010  N   GLU A 222      78.390  66.013  77.097  1.00 64.73           N  
ANISOU 1010  N   GLU A 222     8264   6723   9607    671     48    249       N  
ATOM   1011  CA  GLU A 222      77.945  67.398  77.171  1.00 60.47           C  
ANISOU 1011  CA  GLU A 222     7662   6162   9150    688   -100    183       C  
ATOM   1012  C   GLU A 222      79.073  68.374  76.855  1.00 65.53           C  
ANISOU 1012  C   GLU A 222     8243   6735   9919    659   -280    182       C  
ATOM   1013  O   GLU A 222      78.820  69.465  76.331  1.00 72.86           O  
ANISOU 1013  O   GLU A 222     9114   7606  10963    596   -417    175       O  
ATOM   1014  CB  GLU A 222      77.359  67.679  78.552  1.00 64.14           C  
ANISOU 1014  CB  GLU A 222     8155   6692   9524    864   -130     91       C  
ATOM   1015  CG  GLU A 222      75.999  67.043  78.761  1.00 81.38           C  
ANISOU 1015  CG  GLU A 222    10346   8976  11599    867     19    122       C  
ATOM   1016  CD  GLU A 222      75.707  66.757  80.214  1.00 86.69           C  
ANISOU 1016  CD  GLU A 222    11045   9775  12119   1052     59     89       C  
ATOM   1017  OE1 GLU A 222      76.434  67.286  81.080  1.00 90.69           O  
ANISOU 1017  OE1 GLU A 222    11568  10281  12607   1207    -59     -1       O  
ATOM   1018  OE2 GLU A 222      74.754  65.999  80.489  1.00 85.55           O  
ANISOU 1018  OE2 GLU A 222    10895   9741  11870   1040    201    165       O  
ATOM   1019  N   ALA A 223      80.320  68.005  77.155  1.00 64.95           N  
ANISOU 1019  N   ALA A 223     8176   6671   9833    694   -292    204       N  
ATOM   1020  CA  ALA A 223      81.440  68.884  76.839  1.00 71.57           C  
ANISOU 1020  CA  ALA A 223     8930   7466  10799    640   -467    240       C  
ATOM   1021  C   ALA A 223      81.721  68.895  75.343  1.00 76.14           C  
ANISOU 1021  C   ALA A 223     9418   8070  11443    471   -436    369       C  
ATOM   1022  O   ALA A 223      82.020  69.949  74.766  1.00 79.81           O  
ANISOU 1022  O   ALA A 223     9787   8493  12044    369   -594    431       O  
ATOM   1023  CB  ALA A 223      82.681  68.454  77.618  1.00 65.51           C  
ANISOU 1023  CB  ALA A 223     8177   6729   9985    735   -485    231       C  
ATOM   1024  N   MET A 224      81.635  67.729  74.703  1.00 66.14           N  
ANISOU 1024  N   MET A 224     8180   6873  10077    446   -251    416       N  
ATOM   1025  CA  MET A 224      81.759  67.669  73.252  1.00 62.74           C  
ANISOU 1025  CA  MET A 224     7667   6498   9672    323   -209    521       C  
ATOM   1026  C   MET A 224      80.576  68.350  72.578  1.00 60.89           C  
ANISOU 1026  C   MET A 224     7411   6216   9509    227   -236    523       C  
ATOM   1027  O   MET A 224      80.745  69.084  71.596  1.00 64.02           O  
ANISOU 1027  O   MET A 224     7703   6629   9993    115   -312    616       O  
ATOM   1028  CB  MET A 224      81.852  66.213  72.798  1.00 56.42           C  
ANISOU 1028  CB  MET A 224     6933   5767   8737    360    -34    531       C  
ATOM   1029  CG  MET A 224      83.112  65.501  73.227  1.00 47.86           C  
ANISOU 1029  CG  MET A 224     5862   4749   7573    462    -10    538       C  
ATOM   1030  SD  MET A 224      83.192  63.840  72.553  1.00 54.86           S  
ANISOU 1030  SD  MET A 224     6846   5690   8310    527    146    532       S  
ATOM   1031  CE  MET A 224      81.814  63.044  73.377  1.00 54.78           C  
ANISOU 1031  CE  MET A 224     7008   5547   8260    546    230    458       C  
ATOM   1032  N   LEU A 225      79.367  68.112  73.090  1.00 57.09           N  
ANISOU 1032  N   LEU A 225     7015   5694   8983    271   -174    438       N  
ATOM   1033  CA  LEU A 225      78.178  68.661  72.454  1.00 56.91           C  
ANISOU 1033  CA  LEU A 225     6970   5643   9010    195   -187    432       C  
ATOM   1034  C   LEU A 225      78.186  70.182  72.494  1.00 58.39           C  
ANISOU 1034  C   LEU A 225     7094   5756   9336    168   -398    424       C  
ATOM   1035  O   LEU A 225      77.694  70.829  71.562  1.00 63.39           O  
ANISOU 1035  O   LEU A 225     7672   6368  10046     69   -451    471       O  
ATOM   1036  CB  LEU A 225      76.920  68.104  73.125  1.00 42.29           C  
ANISOU 1036  CB  LEU A 225     5198   3798   7072    256    -85    356       C  
ATOM   1037  CG  LEU A 225      75.583  68.505  72.506  1.00 54.55           C  
ANISOU 1037  CG  LEU A 225     6724   5348   8652    190    -76    345       C  
ATOM   1038  CD1 LEU A 225      75.483  67.943  71.105  1.00 51.34           C  
ANISOU 1038  CD1 LEU A 225     6295   4961   8249     68      9    421       C  
ATOM   1039  CD2 LEU A 225      74.430  68.013  73.349  1.00 60.69           C  
ANISOU 1039  CD2 LEU A 225     7548   6176   9337    259     15    294       C  
ATOM   1040  N   GLU A 226      78.761  70.771  73.546  1.00 62.96           N  
ANISOU 1040  N   GLU A 226     7687   6282   9954    260   -543    364       N  
ATOM   1041  CA  GLU A 226      78.821  72.226  73.636  1.00 72.76           C  
ANISOU 1041  CA  GLU A 226     8889   7412  11346    242   -796    346       C  
ATOM   1042  C   GLU A 226      79.671  72.820  72.523  1.00 71.35           C  
ANISOU 1042  C   GLU A 226     8593   7219  11298     70   -900    513       C  
ATOM   1043  O   GLU A 226      79.478  73.982  72.147  1.00 76.83           O  
ANISOU 1043  O   GLU A 226     9247   7811  12136     -4  -1098    547       O  
ATOM   1044  CB  GLU A 226      79.360  72.649  75.004  1.00 83.21           C  
ANISOU 1044  CB  GLU A 226    10260   8675  12681    391   -952    237       C  
ATOM   1045  CG  GLU A 226      78.281  72.801  76.067  1.00 97.77           C  
ANISOU 1045  CG  GLU A 226    12189  10523  14436    577   -966     67       C  
ATOM   1046  CD  GLU A 226      78.835  72.743  77.477  1.00111.81           C  
ANISOU 1046  CD  GLU A 226    14025  12307  16150    764  -1038    -44       C  
ATOM   1047  OE1 GLU A 226      80.016  73.103  77.666  1.00122.00           O  
ANISOU 1047  OE1 GLU A 226    15291  13530  17533    742  -1188    -17       O  
ATOM   1048  OE2 GLU A 226      78.091  72.336  78.394  1.00119.74           O  
ANISOU 1048  OE2 GLU A 226    15087  13403  17005    932   -947   -147       O  
ATOM   1049  N   ARG A 227      80.609  72.045  71.980  1.00 61.37           N  
ANISOU 1049  N   ARG A 227     7268   6069   9981     15   -779    627       N  
ATOM   1050  CA  ARG A 227      81.412  72.499  70.855  1.00 68.62           C  
ANISOU 1050  CA  ARG A 227     8041   7046  10984   -141   -844    818       C  
ATOM   1051  C   ARG A 227      80.784  72.175  69.506  1.00 73.17           C  
ANISOU 1051  C   ARG A 227     8576   7714  11513   -227   -708    898       C  
ATOM   1052  O   ARG A 227      81.129  72.817  68.509  1.00 86.28           O  
ANISOU 1052  O   ARG A 227    10109   9421  13253   -360   -786   1063       O  
ATOM   1053  CB  ARG A 227      82.810  71.874  70.898  1.00 66.77           C  
ANISOU 1053  CB  ARG A 227     7734   6943  10692   -130   -791    908       C  
ATOM   1054  CG  ARG A 227      83.571  72.042  72.198  1.00 58.98           C  
ANISOU 1054  CG  ARG A 227     6782   5890   9737    -38   -912    833       C  
ATOM   1055  CD  ARG A 227      84.036  73.477  72.423  1.00 64.73           C  
ANISOU 1055  CD  ARG A 227     7437   6485  10673   -130  -1219    896       C  
ATOM   1056  NE  ARG A 227      85.385  73.513  72.984  1.00 80.57           N  
ANISOU 1056  NE  ARG A 227     9372   8527  12715   -124  -1320    953       N  
ATOM   1057  CZ  ARG A 227      85.686  73.200  74.243  1.00 95.76           C  
ANISOU 1057  CZ  ARG A 227    11390  10408  14588     32  -1343    805       C  
ATOM   1058  NH1 ARG A 227      84.736  72.809  75.087  1.00 96.84           N  
ANISOU 1058  NH1 ARG A 227    11687  10483  14625    196  -1261    606       N  
ATOM   1059  NH2 ARG A 227      86.944  73.267  74.657  1.00101.43           N  
ANISOU 1059  NH2 ARG A 227    12026  11168  15346     24  -1445    868       N  
ATOM   1060  N   ILE A 228      79.877  71.203  69.454  1.00 66.93           N  
ANISOU 1060  N   ILE A 228     7881   6954  10596   -160   -519    798       N  
ATOM   1061  CA  ILE A 228      79.348  70.677  68.199  1.00 58.94           C  
ANISOU 1061  CA  ILE A 228     6843   6036   9516   -218   -384    851       C  
ATOM   1062  C   ILE A 228      77.979  71.271  67.888  1.00 67.69           C  
ANISOU 1062  C   ILE A 228     7980   7060  10679   -260   -419    800       C  
ATOM   1063  O   ILE A 228      77.654  71.522  66.723  1.00 73.44           O  
ANISOU 1063  O   ILE A 228     8642   7837  11424   -349   -411    885       O  
ATOM   1064  CB  ILE A 228      79.286  69.139  68.256  1.00 48.92           C  
ANISOU 1064  CB  ILE A 228     5664   4838   8084   -126   -184    781       C  
ATOM   1065  CG1 ILE A 228      80.701  68.553  68.248  1.00 43.56           C  
ANISOU 1065  CG1 ILE A 228     4937   4278   7335    -75   -151    846       C  
ATOM   1066  CG2 ILE A 228      78.397  68.567  67.151  1.00 42.27           C  
ANISOU 1066  CG2 ILE A 228     4839   4042   7180   -162    -72    779       C  
ATOM   1067  CD1 ILE A 228      80.733  67.043  68.365  1.00 46.26           C  
ANISOU 1067  CD1 ILE A 228     5390   4660   7526     36      6    767       C  
ATOM   1068  N   ALA A 229      77.179  71.516  68.928  1.00 65.93           N  
ANISOU 1068  N   ALA A 229     7846   6734  10469   -180   -461    663       N  
ATOM   1069  CA  ALA A 229      75.787  71.935  68.755  1.00 64.06           C  
ANISOU 1069  CA  ALA A 229     7639   6451  10251   -185   -474    593       C  
ATOM   1070  C   ALA A 229      75.596  73.079  67.763  1.00 68.98           C  
ANISOU 1070  C   ALA A 229     8181   7031  10996   -296   -618    684       C  
ATOM   1071  O   ALA A 229      74.706  72.972  66.905  1.00 77.85           O  
ANISOU 1071  O   ALA A 229     9294   8190  12096   -344   -548    692       O  
ATOM   1072  CB  ALA A 229      75.188  72.286  70.126  1.00 61.47           C  
ANISOU 1072  CB  ALA A 229     7385   6056   9913    -50   -545    445       C  
ATOM   1073  N   PRO A 230      76.369  74.172  67.795  1.00 63.66           N  
ANISOU 1073  N   PRO A 230     7450   6278  10461   -351   -831    767       N  
ATOM   1074  CA  PRO A 230      76.160  75.235  66.797  1.00 64.96           C  
ANISOU 1074  CA  PRO A 230     7539   6394  10749   -474   -978    885       C  
ATOM   1075  C   PRO A 230      76.399  74.794  65.361  1.00 67.27           C  
ANISOU 1075  C   PRO A 230     7730   6841  10987   -585   -848   1049       C  
ATOM   1076  O   PRO A 230      76.028  75.534  64.441  1.00 76.23           O  
ANISOU 1076  O   PRO A 230     8805   7963  12194   -680   -932   1149       O  
ATOM   1077  CB  PRO A 230      77.165  76.319  67.213  1.00 60.78           C  
ANISOU 1077  CB  PRO A 230     6965   5744  10386   -527  -1245    971       C  
ATOM   1078  CG  PRO A 230      77.453  76.040  68.640  1.00 63.10           C  
ANISOU 1078  CG  PRO A 230     7347   5984  10644   -381  -1266    815       C  
ATOM   1079  CD  PRO A 230      77.403  74.555  68.772  1.00 63.97           C  
ANISOU 1079  CD  PRO A 230     7491   6247  10566   -309   -977    761       C  
ATOM   1080  N   TYR A 231      77.002  73.627  65.135  1.00 67.09           N  
ANISOU 1080  N   TYR A 231     7690   6971  10832   -558   -659   1075       N  
ATOM   1081  CA  TYR A 231      77.211  73.114  63.788  1.00 67.57           C  
ANISOU 1081  CA  TYR A 231     7660   7209  10803   -611   -536   1199       C  
ATOM   1082  C   TYR A 231      76.481  71.806  63.529  1.00 69.26           C  
ANISOU 1082  C   TYR A 231     7962   7490  10864   -530   -329   1074       C  
ATOM   1083  O   TYR A 231      76.632  71.234  62.442  1.00 62.73           O  
ANISOU 1083  O   TYR A 231     7083   6814   9938   -533   -230   1138       O  
ATOM   1084  CB  TYR A 231      78.707  72.919  63.518  1.00 61.21           C  
ANISOU 1084  CB  TYR A 231     6732   6561   9965   -635   -529   1362       C  
ATOM   1085  CG  TYR A 231      79.526  74.116  63.912  1.00 76.02           C  
ANISOU 1085  CG  TYR A 231     8518   8357  12010   -734   -754   1498       C  
ATOM   1086  CD1 TYR A 231      80.246  74.128  65.098  1.00 77.43           C  
ANISOU 1086  CD1 TYR A 231     8732   8456  12231   -684   -830   1442       C  
ATOM   1087  CD2 TYR A 231      79.546  75.253  63.119  1.00 92.15           C  
ANISOU 1087  CD2 TYR A 231    10447  10386  14181   -881   -915   1688       C  
ATOM   1088  CE1 TYR A 231      80.989  75.228  65.465  1.00 85.05           C  
ANISOU 1088  CE1 TYR A 231     9621   9324  13370   -781  -1071   1561       C  
ATOM   1089  CE2 TYR A 231      80.282  76.359  63.478  1.00 98.98           C  
ANISOU 1089  CE2 TYR A 231    11236  11144  15229   -993  -1161   1828       C  
ATOM   1090  CZ  TYR A 231      81.002  76.343  64.651  1.00100.68           C  
ANISOU 1090  CZ  TYR A 231    11489  11272  15492   -944  -1246   1759       C  
ATOM   1091  OH  TYR A 231      81.737  77.450  65.010  1.00113.74           O  
ANISOU 1091  OH  TYR A 231    13072  12799  17346  -1063  -1525   1895       O  
ATOM   1092  N   LEU A 232      75.698  71.319  64.495  1.00 68.00           N  
ANISOU 1092  N   LEU A 232     7928   7230  10677   -453   -277    906       N  
ATOM   1093  CA  LEU A 232      75.027  70.033  64.344  1.00 58.83           C  
ANISOU 1093  CA  LEU A 232     6853   6105   9394   -401   -110    810       C  
ATOM   1094  C   LEU A 232      74.202  69.984  63.065  1.00 63.35           C  
ANISOU 1094  C   LEU A 232     7395   6733   9941   -455    -71    831       C  
ATOM   1095  O   LEU A 232      74.227  68.983  62.340  1.00 64.72           O  
ANISOU 1095  O   LEU A 232     7589   6992  10011   -426     32    819       O  
ATOM   1096  CB  LEU A 232      74.149  69.771  65.564  1.00 52.27           C  
ANISOU 1096  CB  LEU A 232     6127   5175   8559   -341    -85    673       C  
ATOM   1097  CG  LEU A 232      73.620  68.355  65.774  1.00 54.07           C  
ANISOU 1097  CG  LEU A 232     6451   5412   8680   -301     62    598       C  
ATOM   1098  CD1 LEU A 232      74.753  67.337  65.743  1.00 46.74           C  
ANISOU 1098  CD1 LEU A 232     5555   4534   7668   -246    129    621       C  
ATOM   1099  CD2 LEU A 232      72.873  68.304  67.099  1.00 50.94           C  
ANISOU 1099  CD2 LEU A 232     6116   4959   8278   -247     73    512       C  
ATOM   1100  N   ALA A 233      73.475  71.064  62.764  1.00 63.88           N  
ANISOU 1100  N   ALA A 233     7422   6748  10103   -518   -170    852       N  
ATOM   1101  CA  ALA A 233      72.702  71.115  61.528  1.00 60.37           C  
ANISOU 1101  CA  ALA A 233     6940   6361   9636   -566   -145    877       C  
ATOM   1102  C   ALA A 233      73.608  70.999  60.309  1.00 60.53           C  
ANISOU 1102  C   ALA A 233     6859   6545   9594   -587   -122   1020       C  
ATOM   1103  O   ALA A 233      73.312  70.241  59.377  1.00 57.76           O  
ANISOU 1103  O   ALA A 233     6513   6293   9138   -558    -33    999       O  
ATOM   1104  CB  ALA A 233      71.883  72.404  61.473  1.00 63.01           C  
ANISOU 1104  CB  ALA A 233     7247   6607  10086   -618   -280    884       C  
ATOM   1105  N   ALA A 234      74.718  71.743  60.301  1.00 58.42           N  
ANISOU 1105  N   ALA A 234     6490   6325   9383   -629   -212   1171       N  
ATOM   1106  CA  ALA A 234      75.687  71.624  59.215  1.00 50.34           C  
ANISOU 1106  CA  ALA A 234     5335   5518   8274   -636   -181   1338       C  
ATOM   1107  C   ALA A 234      76.202  70.199  59.093  1.00 56.48           C  
ANISOU 1107  C   ALA A 234     6157   6424   8881   -509    -36   1262       C  
ATOM   1108  O   ALA A 234      76.172  69.607  58.008  1.00 57.50           O  
ANISOU 1108  O   ALA A 234     6254   6714   8877   -448     37   1271       O  
ATOM   1109  CB  ALA A 234      76.844  72.595  59.438  1.00 46.69           C  
ANISOU 1109  CB  ALA A 234     4743   5084   7912   -719   -311   1531       C  
ATOM   1110  N   ILE A 235      76.685  69.637  60.203  1.00 59.86           N  
ANISOU 1110  N   ILE A 235     6665   6778   9302   -448    -10   1177       N  
ATOM   1111  CA  ILE A 235      77.092  68.235  60.230  1.00 60.15           C  
ANISOU 1111  CA  ILE A 235     6781   6887   9189   -314    102   1081       C  
ATOM   1112  C   ILE A 235      75.943  67.336  59.789  1.00 60.90           C  
ANISOU 1112  C   ILE A 235     6996   6922   9220   -275    168    935       C  
ATOM   1113  O   ILE A 235      76.143  66.352  59.067  1.00 43.63           O  
ANISOU 1113  O   ILE A 235     4841   4841   6896   -168    224    887       O  
ATOM   1114  CB  ILE A 235      77.598  67.879  61.642  1.00 58.68           C  
ANISOU 1114  CB  ILE A 235     6679   6589   9029   -269    103   1009       C  
ATOM   1115  CG1 ILE A 235      78.760  68.798  62.018  1.00 56.39           C  
ANISOU 1115  CG1 ILE A 235     6258   6355   8811   -317     11   1156       C  
ATOM   1116  CG2 ILE A 235      77.998  66.418  61.740  1.00 43.29           C  
ANISOU 1116  CG2 ILE A 235     4832   4681   6935   -128    197    908       C  
ATOM   1117  CD1 ILE A 235      79.008  68.897  63.502  1.00 57.71           C  
ANISOU 1117  CD1 ILE A 235     6504   6371   9054   -298    -35   1083       C  
ATOM   1118  N   GLY A 236      74.717  67.688  60.184  1.00 56.77           N  
ANISOU 1118  N   GLY A 236     6536   6237   8796   -352    145    865       N  
ATOM   1119  CA  GLY A 236      73.571  66.843  59.899  1.00 57.23           C  
ANISOU 1119  CA  GLY A 236     6699   6226   8818   -342    192    741       C  
ATOM   1120  C   GLY A 236      73.312  66.626  58.422  1.00 57.33           C  
ANISOU 1120  C   GLY A 236     6670   6365   8747   -317    202    752       C  
ATOM   1121  O   GLY A 236      72.871  65.546  58.025  1.00 52.03           O  
ANISOU 1121  O   GLY A 236     6094   5673   8001   -258    230    645       O  
ATOM   1122  N   ILE A 237      73.575  67.638  57.590  1.00 57.91           N  
ANISOU 1122  N   ILE A 237     6604   6568   8832   -359    162    886       N  
ATOM   1123  CA  ILE A 237      73.330  67.534  56.151  1.00 59.74           C  
ANISOU 1123  CA  ILE A 237     6778   6954   8967   -321    170    910       C  
ATOM   1124  C   ILE A 237      74.563  67.104  55.370  1.00 61.42           C  
ANISOU 1124  C   ILE A 237     6905   7417   9014   -191    203    986       C  
ATOM   1125  O   ILE A 237      74.496  67.005  54.137  1.00 65.68           O  
ANISOU 1125  O   ILE A 237     7381   8137   9437   -123    212   1013       O  
ATOM   1126  CB  ILE A 237      72.784  68.857  55.572  1.00 53.04           C  
ANISOU 1126  CB  ILE A 237     5821   6125   8207   -434    105   1027       C  
ATOM   1127  CG1 ILE A 237      73.870  69.938  55.566  1.00 54.37           C  
ANISOU 1127  CG1 ILE A 237     5837   6397   8425   -494     45   1241       C  
ATOM   1128  CG2 ILE A 237      71.538  69.302  56.323  1.00 50.19           C  
ANISOU 1128  CG2 ILE A 237     5536   5549   7985   -526     66    936       C  
ATOM   1129  CD1 ILE A 237      73.454  71.226  54.880  1.00 51.58           C  
ANISOU 1129  CD1 ILE A 237     5376   6062   8159   -606    -46   1388       C  
ATOM   1130  N   HIS A 238      75.681  66.844  56.041  1.00 56.68           N  
ANISOU 1130  N   HIS A 238     6291   6861   8383   -136    222   1020       N  
ATOM   1131  CA  HIS A 238      76.858  66.295  55.382  1.00 58.14           C  
ANISOU 1131  CA  HIS A 238     6393   7313   8383     23    259   1073       C  
ATOM   1132  C   HIS A 238      76.721  64.783  55.223  1.00 65.21           C  
ANISOU 1132  C   HIS A 238     7454   8181   9143    202    286    867       C  
ATOM   1133  O   HIS A 238      76.244  64.094  56.127  1.00 63.60           O  
ANISOU 1133  O   HIS A 238     7420   7737   9008    188    282    727       O  
ATOM   1134  CB  HIS A 238      78.112  66.638  56.184  1.00 53.72           C  
ANISOU 1134  CB  HIS A 238     5746   6816   7850     10    255   1192       C  
ATOM   1135  CG  HIS A 238      79.394  66.404  55.448  1.00 56.29           C  
ANISOU 1135  CG  HIS A 238     5914   7487   7988    152    289   1311       C  
ATOM   1136  ND1 HIS A 238      79.938  65.148  55.291  1.00 61.88           N  
ANISOU 1136  ND1 HIS A 238     6696   8309   8508    376    335   1179       N  
ATOM   1137  CD2 HIS A 238      80.255  67.264  54.855  1.00 61.83           C  
ANISOU 1137  CD2 HIS A 238     6377   8461   8653    108    276   1562       C  
ATOM   1138  CE1 HIS A 238      81.072  65.242  54.621  1.00 66.25           C  
ANISOU 1138  CE1 HIS A 238     7056   9220   8896    489    361   1329       C  
ATOM   1139  NE2 HIS A 238      81.288  66.515  54.344  1.00 65.13           N  
ANISOU 1139  NE2 HIS A 238     6710   9191   8844    316    333   1579       N  
ATOM   1140  N   LYS A 239      77.141  64.271  54.060  1.00 66.72           N  
ANISOU 1140  N   LYS A 239     7592   8624   9135    381    298    855       N  
ATOM   1141  CA  LYS A 239      76.975  62.848  53.761  1.00 68.29           C  
ANISOU 1141  CA  LYS A 239     7962   8782   9203    577    277    641       C  
ATOM   1142  C   LYS A 239      77.713  61.979  54.768  1.00 70.17           C  
ANISOU 1142  C   LYS A 239     8318   8922   9421    670    280    555       C  
ATOM   1143  O   LYS A 239      77.254  60.880  55.108  1.00 75.10           O  
ANISOU 1143  O   LYS A 239     9149   9334  10053    732    234    375       O  
ATOM   1144  CB  LYS A 239      77.465  62.538  52.343  1.00 69.60           C  
ANISOU 1144  CB  LYS A 239     8032   9287   9126    803    276    641       C  
ATOM   1145  CG  LYS A 239      77.115  61.132  51.854  1.00 68.12           C  
ANISOU 1145  CG  LYS A 239     8042   9032   8810   1022    204    390       C  
ATOM   1146  CD  LYS A 239      77.695  60.857  50.469  1.00 76.33           C  
ANISOU 1146  CD  LYS A 239     8975  10453   9572   1299    195    377       C  
ATOM   1147  CE  LYS A 239      76.717  60.118  49.557  1.00 85.96           C  
ANISOU 1147  CE  LYS A 239    10340  11591  10728   1420     96    169       C  
ATOM   1148  NZ  LYS A 239      76.208  58.846  50.140  1.00 89.46           N  
ANISOU 1148  NZ  LYS A 239    11067  11679  11246   1464    -17    -74       N  
ATOM   1149  N   ASN A 240      78.868  62.446  55.240  1.00 65.53           N  
ANISOU 1149  N   ASN A 240     7599   8486   8813    677    319    693       N  
ATOM   1150  CA  ASN A 240      79.601  61.779  56.309  1.00 67.71           C  
ANISOU 1150  CA  ASN A 240     7970   8670   9085    748    324    631       C  
ATOM   1151  C   ASN A 240      79.102  62.204  57.681  1.00 75.34           C  
ANISOU 1151  C   ASN A 240     9014   9342  10269    543    324    641       C  
ATOM   1152  O   ASN A 240      78.836  61.358  58.540  1.00 78.61           O  
ANISOU 1152  O   ASN A 240     9610   9534  10723    562    310    516       O  
ATOM   1153  CB  ASN A 240      81.094  62.093  56.206  1.00 70.61           C  
ANISOU 1153  CB  ASN A 240     8144   9358   9325    853    359    777       C  
ATOM   1154  CG  ASN A 240      81.747  61.443  55.021  1.00 69.80           C  
ANISOU 1154  CG  ASN A 240     7974   9592   8956   1127    364    742       C  
ATOM   1155  OD1 ASN A 240      82.365  62.123  54.195  1.00 65.14           O  
ANISOU 1155  OD1 ASN A 240     7145   9350   8254   1157    398    925       O  
ATOM   1156  ND2 ASN A 240      81.626  60.125  54.923  1.00 69.67           N  
ANISOU 1156  ND2 ASN A 240     8161   9483   8826   1340    316    515       N  
ATOM   1157  N   GLY A 241      78.990  63.514  57.897  1.00 76.81           N  
ANISOU 1157  N   GLY A 241     9062   9534  10590    360    324    796       N  
ATOM   1158  CA  GLY A 241      78.680  64.020  59.217  1.00 75.16           C  
ANISOU 1158  CA  GLY A 241     8903   9095  10558    212    309    803       C  
ATOM   1159  C   GLY A 241      77.308  63.616  59.710  1.00 69.38           C  
ANISOU 1159  C   GLY A 241     8340   8097   9922    134    304    672       C  
ATOM   1160  O   GLY A 241      77.066  63.587  60.918  1.00 72.98           O  
ANISOU 1160  O   GLY A 241     8878   8379  10470     77    304    637       O  
ATOM   1161  N   THR A 242      76.393  63.291  58.797  1.00 59.55           N  
ANISOU 1161  N   THR A 242     7137   6839   8649    135    295    607       N  
ATOM   1162  CA  THR A 242      75.052  62.942  59.239  1.00 62.68           C  
ANISOU 1162  CA  THR A 242     7664   7008   9144     38    284    510       C  
ATOM   1163  C   THR A 242      75.085  61.710  60.134  1.00 61.83           C  
ANISOU 1163  C   THR A 242     7731   6738   9023     95    284    409       C  
ATOM   1164  O   THR A 242      74.289  61.609  61.072  1.00 58.86           O  
ANISOU 1164  O   THR A 242     7427   6190   8746     -7    289    390       O  
ATOM   1165  CB  THR A 242      74.122  62.748  58.031  1.00 65.01           C  
ANISOU 1165  CB  THR A 242     7969   7324   9407     34    258    457       C  
ATOM   1166  OG1 THR A 242      72.759  62.719  58.478  1.00 57.46           O  
ANISOU 1166  OG1 THR A 242     7084   6178   8570   -100    246    407       O  
ATOM   1167  CG2 THR A 242      74.423  61.452  57.286  1.00 66.92           C  
ANISOU 1167  CG2 THR A 242     8317   7605   9504    211    224    338       C  
ATOM   1168  N   TRP A 243      76.034  60.795  59.901  1.00 63.60           N  
ANISOU 1168  N   TRP A 243     8014   7032   9119    266    273    356       N  
ATOM   1169  CA  TRP A 243      76.167  59.630  60.772  1.00 67.73           C  
ANISOU 1169  CA  TRP A 243     8713   7388   9634    325    252    273       C  
ATOM   1170  C   TRP A 243      76.530  60.043  62.190  1.00 68.89           C  
ANISOU 1170  C   TRP A 243     8847   7472   9856    263    295    337       C  
ATOM   1171  O   TRP A 243      76.074  59.427  63.160  1.00 82.13           O  
ANISOU 1171  O   TRP A 243    10647   8971  11586    219    292    308       O  
ATOM   1172  CB  TRP A 243      77.220  58.670  60.221  1.00 63.81           C  
ANISOU 1172  CB  TRP A 243     8276   6997   8970    557    215    195       C  
ATOM   1173  CG  TRP A 243      76.871  58.080  58.899  1.00 65.10           C  
ANISOU 1173  CG  TRP A 243     8487   7212   9038    668    146     95       C  
ATOM   1174  CD1 TRP A 243      77.136  58.611  57.670  1.00 74.00           C  
ANISOU 1174  CD1 TRP A 243     9470   8591  10055    750    158    124       C  
ATOM   1175  CD2 TRP A 243      76.192  56.843  58.665  1.00 70.40           C  
ANISOU 1175  CD2 TRP A 243     9362   7676   9711    716     35    -48       C  
ATOM   1176  NE1 TRP A 243      76.665  57.779  56.683  1.00 78.79           N  
ANISOU 1176  NE1 TRP A 243    10183   9175  10579    872     66    -14       N  
ATOM   1177  CE2 TRP A 243      76.079  56.687  57.267  1.00 77.08           C  
ANISOU 1177  CE2 TRP A 243    10187   8660  10441    848    -24   -128       C  
ATOM   1178  CE3 TRP A 243      75.669  55.851  59.500  1.00 59.32           C  
ANISOU 1178  CE3 TRP A 243     8154   5985   8399    656    -36   -102       C  
ATOM   1179  CZ2 TRP A 243      75.461  55.579  56.686  1.00 69.77           C  
ANISOU 1179  CZ2 TRP A 243     9442   7569   9498    930   -171   -286       C  
ATOM   1180  CZ3 TRP A 243      75.055  54.754  58.920  1.00 59.43           C  
ANISOU 1180  CZ3 TRP A 243     8342   5826   8413    708   -185   -231       C  
ATOM   1181  CH2 TRP A 243      74.957  54.627  57.527  1.00 63.63           C  
ANISOU 1181  CH2 TRP A 243     8862   6476   8837    849   -260   -335       C  
ATOM   1182  N   ALA A 244      77.358  61.076  62.330  1.00 59.10           N  
ANISOU 1182  N   ALA A 244     7454   6381   8619    259    322    432       N  
ATOM   1183  CA  ALA A 244      77.719  61.568  63.652  1.00 59.28           C  
ANISOU 1183  CA  ALA A 244     7462   6346   8714    214    337    478       C  
ATOM   1184  C   ALA A 244      76.588  62.383  64.272  1.00 59.02           C  
ANISOU 1184  C   ALA A 244     7411   6199   8815     60    337    499       C  
ATOM   1185  O   ALA A 244      76.349  62.295  65.480  1.00 59.15           O  
ANISOU 1185  O   ALA A 244     7489   6110   8875     39    348    485       O  
ATOM   1186  CB  ALA A 244      79.003  62.398  63.567  1.00 43.67           C  
ANISOU 1186  CB  ALA A 244     5325   4557   6712    253    331    578       C  
ATOM   1187  N   ALA A 245      75.881  63.178  63.466  1.00 56.70           N  
ANISOU 1187  N   ALA A 245     7029   5943   8572    -29    320    531       N  
ATOM   1188  CA  ALA A 245      74.800  63.990  64.013  1.00 52.00           C  
ANISOU 1188  CA  ALA A 245     6411   5260   8087   -144    307    537       C  
ATOM   1189  C   ALA A 245      73.648  63.123  64.500  1.00 53.23           C  
ANISOU 1189  C   ALA A 245     6682   5287   8254   -185    337    474       C  
ATOM   1190  O   ALA A 245      73.080  63.380  65.568  1.00 57.86           O  
ANISOU 1190  O   ALA A 245     7280   5818   8888   -222    348    475       O  
ATOM   1191  CB  ALA A 245      74.314  64.997  62.973  1.00 53.51           C  
ANISOU 1191  CB  ALA A 245     6488   5520   8324   -220    272    586       C  
ATOM   1192  N   GLN A 246      73.288  62.091  63.734  1.00 51.84           N  
ANISOU 1192  N   GLN A 246     6588   5077   8033   -174    334    428       N  
ATOM   1193  CA  GLN A 246      72.206  61.208  64.159  1.00 54.41           C  
ANISOU 1193  CA  GLN A 246     7014   5271   8388   -243    337    400       C  
ATOM   1194  C   GLN A 246      72.603  60.382  65.374  1.00 64.12           C  
ANISOU 1194  C   GLN A 246     8348   6416   9599   -204    355    408       C  
ATOM   1195  O   GLN A 246      71.766  60.106  66.241  1.00 70.04           O  
ANISOU 1195  O   GLN A 246     9126   7099  10386   -280    376    443       O  
ATOM   1196  CB  GLN A 246      71.779  60.293  63.012  1.00 49.54           C  
ANISOU 1196  CB  GLN A 246     6471   4607   7743   -241    287    342       C  
ATOM   1197  CG  GLN A 246      71.235  61.020  61.800  1.00 57.10           C  
ANISOU 1197  CG  GLN A 246     7331   5652   8711   -279    270    335       C  
ATOM   1198  CD  GLN A 246      70.891  60.068  60.681  1.00 67.55           C  
ANISOU 1198  CD  GLN A 246     8738   6933   9993   -245    201    255       C  
ATOM   1199  OE1 GLN A 246      70.428  58.951  60.926  1.00 71.81           O  
ANISOU 1199  OE1 GLN A 246     9408   7320  10556   -272    148    216       O  
ATOM   1200  NE2 GLN A 246      71.103  60.503  59.444  1.00 65.03           N  
ANISOU 1200  NE2 GLN A 246     8346   6748   9613   -183    185    237       N  
ATOM   1201  N   LYS A 247      73.869  59.967  65.450  1.00 63.06           N  
ANISOU 1201  N   LYS A 247     8260   6305   9393    -79    349    389       N  
ATOM   1202  CA  LYS A 247      74.341  59.259  66.634  1.00 58.03           C  
ANISOU 1202  CA  LYS A 247     7722   5595   8734    -27    363    400       C  
ATOM   1203  C   LYS A 247      74.213  60.136  67.870  1.00 55.96           C  
ANISOU 1203  C   LYS A 247     7386   5367   8508    -57    407    449       C  
ATOM   1204  O   LYS A 247      73.610  59.731  68.867  1.00 56.91           O  
ANISOU 1204  O   LYS A 247     7554   5430   8640    -96    432    485       O  
ATOM   1205  CB  LYS A 247      75.789  58.805  66.443  1.00 51.80           C  
ANISOU 1205  CB  LYS A 247     6975   4857   7852    134    345    364       C  
ATOM   1206  CG  LYS A 247      76.178  57.662  67.363  1.00 55.78           C  
ANISOU 1206  CG  LYS A 247     7630   5244   8319    202    331    354       C  
ATOM   1207  CD  LYS A 247      75.260  56.474  67.124  1.00 66.40           C  
ANISOU 1207  CD  LYS A 247     9121   6413   9694    139    268    338       C  
ATOM   1208  CE  LYS A 247      75.690  55.243  67.891  1.00 75.23           C  
ANISOU 1208  CE  LYS A 247    10412   7390  10783    208    221    339       C  
ATOM   1209  NZ  LYS A 247      74.721  54.120  67.706  1.00 85.45           N  
ANISOU 1209  NZ  LYS A 247    11847   8479  12140    110    124    352       N  
ATOM   1210  N   ILE A 248      74.757  61.357  67.803  1.00 54.85           N  
ANISOU 1210  N   ILE A 248     7126   5330   8386    -34    400    457       N  
ATOM   1211  CA  ILE A 248      74.688  62.303  68.916  1.00 54.00           C  
ANISOU 1211  CA  ILE A 248     6956   5248   8315    -32    401    474       C  
ATOM   1212  C   ILE A 248      73.256  62.457  69.413  1.00 60.96           C  
ANISOU 1212  C   ILE A 248     7823   6110   9228   -110    425    485       C  
ATOM   1213  O   ILE A 248      73.001  62.480  70.624  1.00 66.53           O  
ANISOU 1213  O   ILE A 248     8538   6828   9912    -77    449    497       O  
ATOM   1214  CB  ILE A 248      75.280  63.659  68.492  1.00 51.37           C  
ANISOU 1214  CB  ILE A 248     6496   4992   8032    -31    342    488       C  
ATOM   1215  CG1 ILE A 248      76.800  63.568  68.342  1.00 52.32           C  
ANISOU 1215  CG1 ILE A 248     6596   5174   8109     52    322    508       C  
ATOM   1216  CG2 ILE A 248      74.892  64.742  69.481  1.00 53.21           C  
ANISOU 1216  CG2 ILE A 248     6677   5221   8319    -27    299    476       C  
ATOM   1217  CD1 ILE A 248      77.423  64.797  67.683  1.00 50.98           C  
ANISOU 1217  CD1 ILE A 248     6280   5092   7996     17    251    570       C  
ATOM   1218  N   ILE A 249      72.299  62.556  68.492  1.00 63.05           N  
ANISOU 1218  N   ILE A 249     8054   6373   9529   -202    421    484       N  
ATOM   1219  CA  ILE A 249      70.908  62.740  68.889  1.00 60.21           C  
ANISOU 1219  CA  ILE A 249     7653   6032   9191   -275    444    503       C  
ATOM   1220  C   ILE A 249      70.325  61.439  69.427  1.00 62.90           C  
ANISOU 1220  C   ILE A 249     8075   6318   9505   -327    486    558       C  
ATOM   1221  O   ILE A 249      69.593  61.440  70.424  1.00 73.87           O  
ANISOU 1221  O   ILE A 249     9431   7766  10872   -340    525    610       O  
ATOM   1222  CB  ILE A 249      70.096  63.290  67.703  1.00 55.69           C  
ANISOU 1222  CB  ILE A 249     7011   5481   8669   -357    417    487       C  
ATOM   1223  CG1 ILE A 249      70.667  64.649  67.286  1.00 56.99           C  
ANISOU 1223  CG1 ILE A 249     7090   5692   8872   -319    357    467       C  
ATOM   1224  CG2 ILE A 249      68.620  63.394  68.069  1.00 43.57           C  
ANISOU 1224  CG2 ILE A 249     5420   3990   7145   -428    442    510       C  
ATOM   1225  CD1 ILE A 249      70.153  65.168  65.967  1.00 55.57           C  
ANISOU 1225  CD1 ILE A 249     6848   5534   8731   -386    323    465       C  
ATOM   1226  N   ASP A 250      70.651  60.308  68.793  1.00 61.32           N  
ANISOU 1226  N   ASP A 250     7983   6015   9301   -349    462    557       N  
ATOM   1227  CA  ASP A 250      70.105  59.019  69.214  1.00 67.14           C  
ANISOU 1227  CA  ASP A 250     8813   6656  10041   -422    460    626       C  
ATOM   1228  C   ASP A 250      70.621  58.572  70.572  1.00 69.50           C  
ANISOU 1228  C   ASP A 250     9166   6953  10288   -358    495    684       C  
ATOM   1229  O   ASP A 250      69.957  57.770  71.237  1.00 75.91           O  
ANISOU 1229  O   ASP A 250    10011   7731  11102   -437    506    790       O  
ATOM   1230  CB  ASP A 250      70.424  57.947  68.177  1.00 73.30           C  
ANISOU 1230  CB  ASP A 250     9721   7298  10833   -428    381    582       C  
ATOM   1231  CG  ASP A 250      69.576  58.080  66.935  1.00 80.87           C  
ANISOU 1231  CG  ASP A 250    10641   8247  11841   -515    337    546       C  
ATOM   1232  OD1 ASP A 250      68.450  58.618  67.046  1.00 90.32           O  
ANISOU 1232  OD1 ASP A 250    11730   9509  13077   -620    366    592       O  
ATOM   1233  OD2 ASP A 250      70.034  57.658  65.851  1.00 74.59           O  
ANISOU 1233  OD2 ASP A 250     9915   7398  11029   -459    269    465       O  
ATOM   1234  N   VAL A 251      71.790  59.058  70.989  1.00 67.65           N  
ANISOU 1234  N   VAL A 251     8935   6760  10009   -223    506    633       N  
ATOM   1235  CA  VAL A 251      72.368  58.725  72.285  1.00 57.83           C  
ANISOU 1235  CA  VAL A 251     7739   5528   8706   -138    536    673       C  
ATOM   1236  C   VAL A 251      72.223  59.878  73.278  1.00 61.72           C  
ANISOU 1236  C   VAL A 251     8119   6164   9167    -69    573    667       C  
ATOM   1237  O   VAL A 251      72.822  59.851  74.359  1.00 66.66           O  
ANISOU 1237  O   VAL A 251     8769   6827   9733     36    590    675       O  
ATOM   1238  CB  VAL A 251      73.835  58.285  72.124  1.00 58.59           C  
ANISOU 1238  CB  VAL A 251     7932   5565   8764    -16    503    613       C  
ATOM   1239  CG1 VAL A 251      74.352  57.569  73.366  1.00 77.04           C  
ANISOU 1239  CG1 VAL A 251    10356   7874  11040     59    521    665       C  
ATOM   1240  CG2 VAL A 251      73.947  57.338  70.948  1.00 58.07           C  
ANISOU 1240  CG2 VAL A 251     7967   5381   8714    -41    440    578       C  
ATOM   1241  N   ALA A 252      71.427  60.891  72.941  1.00 57.03           N  
ANISOU 1241  N   ALA A 252     7411   5652   8608   -106    569    640       N  
ATOM   1242  CA  ALA A 252      71.152  61.971  73.880  1.00 55.88           C  
ANISOU 1242  CA  ALA A 252     7171   5637   8425    -14    573    613       C  
ATOM   1243  C   ALA A 252      70.420  61.423  75.099  1.00 70.90           C  
ANISOU 1243  C   ALA A 252     9056   7640  10241      1    641    711       C  
ATOM   1244  O   ALA A 252      69.240  61.068  75.015  1.00 80.40           O  
ANISOU 1244  O   ALA A 252    10205   8900  11442   -105    681    798       O  
ATOM   1245  CB  ALA A 252      70.332  63.075  73.208  1.00 48.49           C  
ANISOU 1245  CB  ALA A 252     6128   4756   7540    -51    537    563       C  
ATOM   1246  N   SER A 253      71.111  61.344  76.235  1.00 73.62           N  
ANISOU 1246  N   SER A 253     9435   8028  10509    131    654    712       N  
ATOM   1247  CA  SER A 253      70.568  60.700  77.425  1.00 79.74           C  
ANISOU 1247  CA  SER A 253    10196   8920  11181    157    725    833       C  
ATOM   1248  C   SER A 253      70.115  61.677  78.504  1.00 80.08           C  
ANISOU 1248  C   SER A 253    10128   9182  11119    319    736    795       C  
ATOM   1249  O   SER A 253      69.165  61.375  79.235  1.00 81.64           O  
ANISOU 1249  O   SER A 253    10244   9556  11219    320    807    914       O  
ATOM   1250  CB  SER A 253      71.608  59.743  78.015  1.00 77.70           C  
ANISOU 1250  CB  SER A 253    10063   8573  10885    207    733    876       C  
ATOM   1251  OG  SER A 253      72.846  60.405  78.204  1.00 76.93           O  
ANISOU 1251  OG  SER A 253     9998   8449  10785    353    678    746       O  
ATOM   1252  N   THR A 254      70.756  62.833  78.625  1.00 78.39           N  
ANISOU 1252  N   THR A 254     9901   8970  10915    464    652    640       N  
ATOM   1253  CA  THR A 254      70.417  63.794  79.662  1.00 75.10           C  
ANISOU 1253  CA  THR A 254     9403   8740  10392    663    620    564       C  
ATOM   1254  C   THR A 254      69.514  64.891  79.111  1.00 75.85           C  
ANISOU 1254  C   THR A 254     9401   8897  10523    672    561    480       C  
ATOM   1255  O   THR A 254      69.366  65.067  77.900  1.00 80.82           O  
ANISOU 1255  O   THR A 254    10031   9403  11274    528    532    466       O  
ATOM   1256  CB  THR A 254      71.678  64.415  80.257  1.00 73.51           C  
ANISOU 1256  CB  THR A 254     9261   8483  10188    834    518    435       C  
ATOM   1257  OG1 THR A 254      72.162  65.432  79.375  1.00 70.36           O  
ANISOU 1257  OG1 THR A 254     8862   7946   9924    810    389    315       O  
ATOM   1258  CG2 THR A 254      72.747  63.355  80.435  1.00 71.14           C  
ANISOU 1258  CG2 THR A 254     9069   8073   9887    802    560    500       C  
ATOM   1259  N   GLU A 255      68.904  65.638  80.032  1.00 71.28           N  
ANISOU 1259  N   GLU A 255     8738   8525   9821    867    535    417       N  
ATOM   1260  CA  GLU A 255      68.085  66.774  79.630  1.00 76.57           C  
ANISOU 1260  CA  GLU A 255     9325   9257  10509    926    451    310       C  
ATOM   1261  C   GLU A 255      68.953  67.917  79.126  1.00 75.10           C  
ANISOU 1261  C   GLU A 255     9202   8874  10459    974    265    146       C  
ATOM   1262  O   GLU A 255      68.512  68.715  78.290  1.00 76.06           O  
ANISOU 1262  O   GLU A 255     9292   8937  10670    930    181     84       O  
ATOM   1263  CB  GLU A 255      67.211  67.235  80.800  1.00 84.88           C  
ANISOU 1263  CB  GLU A 255    10271  10614  11365   1166    459    275       C  
ATOM   1264  CG  GLU A 255      66.081  68.179  80.404  1.00 92.65           C  
ANISOU 1264  CG  GLU A 255    11152  11717  12334   1230    400    192       C  
ATOM   1265  CD  GLU A 255      65.427  68.862  81.595  1.00102.99           C  
ANISOU 1265  CD  GLU A 255    12366  13334  13430   1549    361     98       C  
ATOM   1266  OE1 GLU A 255      65.340  68.237  82.673  1.00109.28           O  
ANISOU 1266  OE1 GLU A 255    13114  14357  14049   1658    467    192       O  
ATOM   1267  OE2 GLU A 255      64.987  70.025  81.446  1.00105.36           O  
ANISOU 1267  OE2 GLU A 255    12640  13662  13729   1707    215    -70       O  
ATOM   1268  N   LYS A 256      70.190  68.008  79.613  1.00 71.57           N  
ANISOU 1268  N   LYS A 256     8836   8324  10034   1054    191     90       N  
ATOM   1269  CA  LYS A 256      71.082  69.061  79.145  1.00 77.11           C  
ANISOU 1269  CA  LYS A 256     9581   8836  10882   1068     -3    -28       C  
ATOM   1270  C   LYS A 256      71.474  68.843  77.689  1.00 79.63           C  
ANISOU 1270  C   LYS A 256     9916   8979  11359    827     13     48       C  
ATOM   1271  O   LYS A 256      71.683  69.812  76.948  1.00 77.26           O  
ANISOU 1271  O   LYS A 256     9605   8563  11187    784   -131     -5       O  
ATOM   1272  CB  LYS A 256      72.315  69.124  80.047  1.00 70.63           C  
ANISOU 1272  CB  LYS A 256     8827   7966  10044   1200    -85    -87       C  
ATOM   1273  CG  LYS A 256      73.272  70.253  79.742  1.00 71.73           C  
ANISOU 1273  CG  LYS A 256     8996   7920  10340   1215   -317   -190       C  
ATOM   1274  CD  LYS A 256      74.464  70.182  80.669  1.00 80.41           C  
ANISOU 1274  CD  LYS A 256    10150   8985  11416   1336   -390   -237       C  
ATOM   1275  CE  LYS A 256      75.735  70.650  79.989  1.00 90.10           C  
ANISOU 1275  CE  LYS A 256    11392  10015  12825   1214   -535   -224       C  
ATOM   1276  NZ  LYS A 256      76.940  70.165  80.723  1.00 92.08           N  
ANISOU 1276  NZ  LYS A 256    11687  10255  13043   1280   -538   -223       N  
ATOM   1277  N   GLN A 257      71.549  67.580  77.261  1.00 75.01           N  
ANISOU 1277  N   GLN A 257     9357   8381  10761    678    172    173       N  
ATOM   1278  CA  GLN A 257      71.901  67.252  75.884  1.00 67.22           C  
ANISOU 1278  CA  GLN A 257     8386   7265   9889    486    193    235       C  
ATOM   1279  C   GLN A 257      70.744  67.509  74.927  1.00 69.37           C  
ANISOU 1279  C   GLN A 257     8597   7557  10203    379    210    251       C  
ATOM   1280  O   GLN A 257      70.947  68.060  73.839  1.00 74.49           O  
ANISOU 1280  O   GLN A 257     9230   8115  10959    288    139    244       O  
ATOM   1281  CB  GLN A 257      72.347  65.792  75.796  1.00 62.18           C  
ANISOU 1281  CB  GLN A 257     7817   6596   9213    404    322    335       C  
ATOM   1282  CG  GLN A 257      73.652  65.505  76.515  1.00 63.09           C  
ANISOU 1282  CG  GLN A 257     7997   6675   9300    497    300    321       C  
ATOM   1283  CD  GLN A 257      73.999  64.023  76.541  1.00 77.23           C  
ANISOU 1283  CD  GLN A 257     9872   8433  11039    445    413    411       C  
ATOM   1284  OE1 GLN A 257      73.632  63.269  75.641  1.00 89.08           O  
ANISOU 1284  OE1 GLN A 257    11398   9881  12569    314    468    471       O  
ATOM   1285  NE2 GLN A 257      74.709  63.600  77.580  1.00 76.84           N  
ANISOU 1285  NE2 GLN A 257     9876   8404  10914    558    426    412       N  
ATOM   1286  N   MET A 258      69.525  67.111  75.303  1.00 63.14           N  
ANISOU 1286  N   MET A 258     7760   6904   9324    383    303    289       N  
ATOM   1287  CA  MET A 258      68.385  67.348  74.422  1.00 64.83           C  
ANISOU 1287  CA  MET A 258     7906   7152   9574    285    316    303       C  
ATOM   1288  C   MET A 258      68.122  68.835  74.254  1.00 67.25           C  
ANISOU 1288  C   MET A 258     8168   7456   9929    381    164    186       C  
ATOM   1289  O   MET A 258      67.828  69.299  73.147  1.00 72.30           O  
ANISOU 1289  O   MET A 258     8784   8027  10660    282    116    181       O  
ATOM   1290  CB  MET A 258      67.133  66.643  74.946  1.00 65.84           C  
ANISOU 1290  CB  MET A 258     7965   7458   9592    269    437    389       C  
ATOM   1291  CG  MET A 258      67.241  65.125  74.988  1.00 68.83           C  
ANISOU 1291  CG  MET A 258     8396   7805   9952    136    556    530       C  
ATOM   1292  SD  MET A 258      65.745  64.316  75.593  1.00 69.12           S  
ANISOU 1292  SD  MET A 258     8322   8059   9881     72    677    688       S  
ATOM   1293  CE  MET A 258      66.310  62.620  75.696  1.00 62.46           C  
ANISOU 1293  CE  MET A 258     7594   7081   9057    -74    744    844       C  
ATOM   1294  N   ASP A 259      68.229  69.601  75.340  1.00 70.55           N  
ANISOU 1294  N   ASP A 259     8581   7939  10284    586     68     85       N  
ATOM   1295  CA  ASP A 259      67.957  71.031  75.249  1.00 76.37           C  
ANISOU 1295  CA  ASP A 259     9298   8647  11074    701   -119    -43       C  
ATOM   1296  C   ASP A 259      68.981  71.731  74.368  1.00 72.69           C  
ANISOU 1296  C   ASP A 259     8876   7960  10781    604   -270    -51       C  
ATOM   1297  O   ASP A 259      68.635  72.646  73.613  1.00 73.25           O  
ANISOU 1297  O   ASP A 259     8927   7960  10946    573   -394    -84       O  
ATOM   1298  CB  ASP A 259      67.922  71.651  76.645  1.00 87.46           C  
ANISOU 1298  CB  ASP A 259    10704  10162  12364    974   -220   -169       C  
ATOM   1299  CG  ASP A 259      66.747  71.157  77.465  1.00 93.07           C  
ANISOU 1299  CG  ASP A 259    11328  11156  12878   1091    -80   -145       C  
ATOM   1300  OD1 ASP A 259      65.674  70.907  76.873  1.00 96.34           O  
ANISOU 1300  OD1 ASP A 259    11661  11670  13272    993     14    -80       O  
ATOM   1301  OD2 ASP A 259      66.893  71.024  78.698  1.00 98.52           O  
ANISOU 1301  OD2 ASP A 259    12018  11989  13428   1283    -67   -181       O  
ATOM   1302  N   LEU A 260      70.244  71.305  74.438  1.00 69.29           N  
ANISOU 1302  N   LEU A 260     8497   7436  10394    554   -264     -3       N  
ATOM   1303  CA  LEU A 260      71.262  71.863  73.553  1.00 67.03           C  
ANISOU 1303  CA  LEU A 260     8220   6987  10261    439   -387     36       C  
ATOM   1304  C   LEU A 260      70.948  71.559  72.094  1.00 65.72           C  
ANISOU 1304  C   LEU A 260     8018   6801  10153    250   -306    134       C  
ATOM   1305  O   LEU A 260      71.050  72.440  71.231  1.00 59.12           O  
ANISOU 1305  O   LEU A 260     7151   5880   9430    177   -433    155       O  
ATOM   1306  CB  LEU A 260      72.635  71.308  73.921  1.00 63.44           C  
ANISOU 1306  CB  LEU A 260     7805   6488   9811    430   -367     81       C  
ATOM   1307  CG  LEU A 260      73.473  72.111  74.904  1.00 60.38           C  
ANISOU 1307  CG  LEU A 260     7446   6035   9461    570   -557     -5       C  
ATOM   1308  CD1 LEU A 260      74.755  71.356  75.192  1.00 62.51           C  
ANISOU 1308  CD1 LEU A 260     7743   6294   9716    549   -498     54       C  
ATOM   1309  CD2 LEU A 260      73.762  73.496  74.347  1.00 57.82           C  
ANISOU 1309  CD2 LEU A 260     7099   5565   9306    527   -808    -19       C  
ATOM   1310  N   ILE A 261      70.569  70.313  71.802  1.00 60.38           N  
ANISOU 1310  N   ILE A 261     7348   6195   9400    170   -113    198       N  
ATOM   1311  CA  ILE A 261      70.246  69.931  70.432  1.00 52.06           C  
ANISOU 1311  CA  ILE A 261     6268   5127   8384     14    -46    270       C  
ATOM   1312  C   ILE A 261      69.044  70.717  69.926  1.00 57.08           C  
ANISOU 1312  C   ILE A 261     6850   5788   9048      3   -101    234       C  
ATOM   1313  O   ILE A 261      69.085  71.310  68.843  1.00 64.09           O  
ANISOU 1313  O   ILE A 261     7708   6622  10022    -81   -172    266       O  
ATOM   1314  CB  ILE A 261      70.013  68.413  70.345  1.00 54.10           C  
ANISOU 1314  CB  ILE A 261     6565   5430   8563    -51    130    327       C  
ATOM   1315  CG1 ILE A 261      71.313  67.664  70.652  1.00 53.58           C  
ANISOU 1315  CG1 ILE A 261     6562   5324   8473    -32    165    360       C  
ATOM   1316  CG2 ILE A 261      69.469  68.029  68.978  1.00 60.49           C  
ANISOU 1316  CG2 ILE A 261     7354   6230   9400   -183    177    371       C  
ATOM   1317  CD1 ILE A 261      71.164  66.167  70.644  1.00 52.44           C  
ANISOU 1317  CD1 ILE A 261     6481   5184   8260    -79    296    409       C  
ATOM   1318  N   VAL A 262      67.958  70.740  70.703  1.00 58.95           N  
ANISOU 1318  N   VAL A 262     7064   6133   9204     97    -69    175       N  
ATOM   1319  CA  VAL A 262      66.773  71.495  70.301  1.00 55.73           C  
ANISOU 1319  CA  VAL A 262     6596   5774   8805    115   -124    127       C  
ATOM   1320  C   VAL A 262      67.111  72.969  70.131  1.00 57.47           C  
ANISOU 1320  C   VAL A 262     6824   5884   9129    181   -347     60       C  
ATOM   1321  O   VAL A 262      66.625  73.629  69.206  1.00 61.88           O  
ANISOU 1321  O   VAL A 262     7352   6402   9756    125   -422     64       O  
ATOM   1322  CB  VAL A 262      65.632  71.295  71.317  1.00 53.52           C  
ANISOU 1322  CB  VAL A 262     6265   5679   8390    240    -55     82       C  
ATOM   1323  CG1 VAL A 262      64.465  72.209  70.986  1.00 52.33           C  
ANISOU 1323  CG1 VAL A 262     6048   5600   8236    301   -135     12       C  
ATOM   1324  CG2 VAL A 262      65.171  69.847  71.333  1.00 57.29           C  
ANISOU 1324  CG2 VAL A 262     6724   6248   8795    124    140    190       C  
ATOM   1325  N   LYS A 263      67.953  73.509  71.015  1.00 64.39           N  
ANISOU 1325  N   LYS A 263     7744   6695  10027    298   -475      4       N  
ATOM   1326  CA  LYS A 263      68.280  74.929  70.944  1.00 68.79           C  
ANISOU 1326  CA  LYS A 263     8320   7112  10704    358   -735    -57       C  
ATOM   1327  C   LYS A 263      68.997  75.252  69.637  1.00 72.77           C  
ANISOU 1327  C   LYS A 263     8807   7488  11355    165   -799     70       C  
ATOM   1328  O   LYS A 263      68.603  76.170  68.908  1.00 72.01           O  
ANISOU 1328  O   LYS A 263     8693   7319  11348    129   -938     76       O  
ATOM   1329  CB  LYS A 263      69.126  75.330  72.158  1.00 59.95           C  
ANISOU 1329  CB  LYS A 263     7256   5935   9587    511   -875   -141       C  
ATOM   1330  CG  LYS A 263      69.523  76.804  72.235  1.00 70.04           C  
ANISOU 1330  CG  LYS A 263     8573   7031  11010    581  -1199   -213       C  
ATOM   1331  CD  LYS A 263      70.143  77.122  73.594  1.00 80.23           C  
ANISOU 1331  CD  LYS A 263     9923   8287  12272    777  -1344   -335       C  
ATOM   1332  CE  LYS A 263      70.374  78.611  73.785  1.00 89.00           C  
ANISOU 1332  CE  LYS A 263    11091   9196  13529    877  -1715   -439       C  
ATOM   1333  NZ  LYS A 263      71.461  79.106  72.902  1.00 99.21           N  
ANISOU 1333  NZ  LYS A 263    12373  10286  15037    651  -1866   -281       N  
ATOM   1334  N   HIS A 264      70.025  74.473  69.304  1.00 63.18           N  
ANISOU 1334  N   HIS A 264     7588   6268  10148     50   -694    181       N  
ATOM   1335  CA  HIS A 264      70.896  74.768  68.177  1.00 60.26           C  
ANISOU 1335  CA  HIS A 264     7178   5829   9889   -108   -752    322       C  
ATOM   1336  C   HIS A 264      70.436  74.133  66.873  1.00 62.72           C  
ANISOU 1336  C   HIS A 264     7445   6219  10166   -235   -599    408       C  
ATOM   1337  O   HIS A 264      71.107  74.302  65.848  1.00 73.28           O  
ANISOU 1337  O   HIS A 264     8730   7551  11562   -352   -624    538       O  
ATOM   1338  CB  HIS A 264      72.321  74.320  68.499  1.00 61.22           C  
ANISOU 1338  CB  HIS A 264     7301   5940  10020   -135   -735    393       C  
ATOM   1339  CG  HIS A 264      73.019  75.211  69.476  1.00 75.36           C  
ANISOU 1339  CG  HIS A 264     9120   7617  11895    -49   -953    341       C  
ATOM   1340  ND1 HIS A 264      72.945  75.020  70.840  1.00 75.84           N  
ANISOU 1340  ND1 HIS A 264     9244   7692  11878    121   -957    205       N  
ATOM   1341  CD2 HIS A 264      73.786  76.311  69.291  1.00 75.08           C  
ANISOU 1341  CD2 HIS A 264     9058   7450  12020   -109  -1197    411       C  
ATOM   1342  CE1 HIS A 264      73.647  75.957  71.451  1.00 75.86           C  
ANISOU 1342  CE1 HIS A 264     9268   7569  11986    179  -1199    168       C  
ATOM   1343  NE2 HIS A 264      74.166  76.754  70.534  1.00 77.12           N  
ANISOU 1343  NE2 HIS A 264     9374   7624  12302     28  -1357    296       N  
ATOM   1344  N   LEU A 265      69.320  73.408  66.879  1.00 46.13           N  
ANISOU 1344  N   LEU A 265     5353   4207   7967   -214   -451    348       N  
ATOM   1345  CA  LEU A 265      68.750  72.909  65.636  1.00 53.48           C  
ANISOU 1345  CA  LEU A 265     6250   5196   8876   -321   -345    404       C  
ATOM   1346  C   LEU A 265      67.537  73.703  65.179  1.00 62.90           C  
ANISOU 1346  C   LEU A 265     7410   6391  10097   -314   -419    359       C  
ATOM   1347  O   LEU A 265      67.284  73.786  63.974  1.00 63.02           O  
ANISOU 1347  O   LEU A 265     7387   6421  10136   -406   -410    422       O  
ATOM   1348  CB  LEU A 265      68.349  71.439  65.779  1.00 53.24           C  
ANISOU 1348  CB  LEU A 265     6248   5246   8734   -334   -148    389       C  
ATOM   1349  CG  LEU A 265      69.422  70.372  65.580  1.00 48.98           C  
ANISOU 1349  CG  LEU A 265     5743   4715   8153   -370    -52    450       C  
ATOM   1350  CD1 LEU A 265      68.737  69.039  65.347  1.00 45.67           C  
ANISOU 1350  CD1 LEU A 265     5360   4337   7656   -409     90    438       C  
ATOM   1351  CD2 LEU A 265      70.364  70.710  64.439  1.00 47.59           C  
ANISOU 1351  CD2 LEU A 265     5518   4543   8020   -435   -100    550       C  
ATOM   1352  N   ARG A 266      66.798  74.297  66.114  1.00 70.49           N  
ANISOU 1352  N   ARG A 266     8384   7355  11043   -186   -498    246       N  
ATOM   1353  CA  ARG A 266      65.531  74.945  65.786  1.00 79.02           C  
ANISOU 1353  CA  ARG A 266     9432   8470  12123   -147   -556    183       C  
ATOM   1354  C   ARG A 266      65.635  75.970  64.658  1.00 81.23           C  
ANISOU 1354  C   ARG A 266     9693   8653  12520   -222   -710    247       C  
ATOM   1355  O   ARG A 266      64.763  75.950  63.771  1.00 78.65           O  
ANISOU 1355  O   ARG A 266     9328   8379  12179   -273   -669    257       O  
ATOM   1356  CB  ARG A 266      64.932  75.579  67.051  1.00 88.01           C  
ANISOU 1356  CB  ARG A 266    10586   9642  13213     54   -655     40       C  
ATOM   1357  CG  ARG A 266      63.555  76.200  66.843  1.00100.63           C  
ANISOU 1357  CG  ARG A 266    12142  11315  14779    136   -710    -44       C  
ATOM   1358  CD  ARG A 266      63.104  76.984  68.068  1.00112.55           C  
ANISOU 1358  CD  ARG A 266    13667  12868  16227    383   -850   -201       C  
ATOM   1359  NE  ARG A 266      62.731  76.123  69.187  1.00115.71           N  
ANISOU 1359  NE  ARG A 266    14034  13463  16469    487   -688   -237       N  
ATOM   1360  CZ  ARG A 266      61.481  75.786  69.494  1.00115.70           C  
ANISOU 1360  CZ  ARG A 266    13945  13685  16332    564   -577   -271       C  
ATOM   1361  NH1 ARG A 266      60.468  76.226  68.757  1.00117.40           N  
ANISOU 1361  NH1 ARG A 266    14104  13952  16550    560   -609   -296       N  
ATOM   1362  NH2 ARG A 266      61.245  75.001  70.538  1.00106.52           N  
ANISOU 1362  NH2 ARG A 266    12738  12710  15025    643   -434   -264       N  
ATOM   1363  N   PRO A 267      66.635  76.862  64.610  1.00 78.28           N  
ANISOU 1363  N   PRO A 267     9337   8141  12265   -245   -896    308       N  
ATOM   1364  CA  PRO A 267      66.710  77.800  63.476  1.00 74.63           C  
ANISOU 1364  CA  PRO A 267     8844   7597  11917   -342  -1044    413       C  
ATOM   1365  C   PRO A 267      66.891  77.126  62.130  1.00 72.93           C  
ANISOU 1365  C   PRO A 267     8567   7474  11669   -490   -893    552       C  
ATOM   1366  O   PRO A 267      66.548  77.728  61.105  1.00 80.51           O  
ANISOU 1366  O   PRO A 267     9489   8422  12677   -554   -966    625       O  
ATOM   1367  CB  PRO A 267      67.923  78.673  63.821  1.00 73.66           C  
ANISOU 1367  CB  PRO A 267     8740   7317  11930   -365  -1263    489       C  
ATOM   1368  CG  PRO A 267      68.066  78.563  65.285  1.00 72.40           C  
ANISOU 1368  CG  PRO A 267     8643   7134  11732   -211  -1293    343       C  
ATOM   1369  CD  PRO A 267      67.677  77.157  65.612  1.00 74.43           C  
ANISOU 1369  CD  PRO A 267     8892   7562  11825   -184  -1009    292       C  
ATOM   1370  N   TYR A 268      67.418  75.903  62.091  1.00 61.92           N  
ANISOU 1370  N   TYR A 268     7165   6174  10187   -528   -701    585       N  
ATOM   1371  CA  TYR A 268      67.682  75.217  60.834  1.00 59.08           C  
ANISOU 1371  CA  TYR A 268     6756   5916   9777   -627   -577    694       C  
ATOM   1372  C   TYR A 268      66.700  74.086  60.571  1.00 61.84           C  
ANISOU 1372  C   TYR A 268     7121   6360  10016   -619   -400    608       C  
ATOM   1373  O   TYR A 268      66.889  73.327  59.612  1.00 69.05           O  
ANISOU 1373  O   TYR A 268     8013   7355  10867   -669   -300    661       O  
ATOM   1374  CB  TYR A 268      69.111  74.670  60.816  1.00 48.98           C  
ANISOU 1374  CB  TYR A 268     5457   4676   8476   -663   -523    799       C  
ATOM   1375  CG  TYR A 268      70.161  75.641  61.299  1.00 55.46           C  
ANISOU 1375  CG  TYR A 268     6257   5402   9415   -684   -700    890       C  
ATOM   1376  CD1 TYR A 268      70.819  76.481  60.413  1.00 57.31           C  
ANISOU 1376  CD1 TYR A 268     6404   5637   9734   -788   -825   1079       C  
ATOM   1377  CD2 TYR A 268      70.518  75.695  62.639  1.00 59.86           C  
ANISOU 1377  CD2 TYR A 268     6873   5876   9996   -605   -753    800       C  
ATOM   1378  CE1 TYR A 268      71.791  77.361  60.851  1.00 56.47           C  
ANISOU 1378  CE1 TYR A 268     6269   5430   9757   -835  -1015   1185       C  
ATOM   1379  CE2 TYR A 268      71.486  76.573  63.086  1.00 58.95           C  
ANISOU 1379  CE2 TYR A 268     6741   5656  10000   -628   -944    876       C  
ATOM   1380  CZ  TYR A 268      72.119  77.404  62.190  1.00 54.27           C  
ANISOU 1380  CZ  TYR A 268     6062   5046   9514   -755  -1082   1072       C  
ATOM   1381  OH  TYR A 268      73.086  78.275  62.637  1.00 55.31           O  
ANISOU 1381  OH  TYR A 268     6169   5059   9787   -804  -1298   1168       O  
ATOM   1382  N   THR A 269      65.661  73.953  61.401  1.00 56.12           N  
ANISOU 1382  N   THR A 269     6424   5637   9260   -550   -374    481       N  
ATOM   1383  CA  THR A 269      64.757  72.811  61.295  1.00 62.45           C  
ANISOU 1383  CA  THR A 269     7231   6523   9974   -567   -222    425       C  
ATOM   1384  C   THR A 269      64.139  72.721  59.906  1.00 67.01           C  
ANISOU 1384  C   THR A 269     7769   7151  10541   -636   -203    453       C  
ATOM   1385  O   THR A 269      64.151  71.654  59.278  1.00 63.04           O  
ANISOU 1385  O   THR A 269     7279   6693   9982   -683   -103    463       O  
ATOM   1386  CB  THR A 269      63.670  72.904  62.366  1.00 60.98           C  
ANISOU 1386  CB  THR A 269     7040   6376   9754   -484   -214    321       C  
ATOM   1387  OG1 THR A 269      64.278  72.932  63.662  1.00 61.96           O  
ANISOU 1387  OG1 THR A 269     7201   6473   9866   -398   -229    290       O  
ATOM   1388  CG2 THR A 269      62.727  71.708  62.280  1.00 52.12           C  
ANISOU 1388  CG2 THR A 269     5901   5343   8559   -537    -72    302       C  
ATOM   1389  N   ALA A 270      63.598  73.837  59.405  1.00 65.11           N  
ANISOU 1389  N   ALA A 270     7489   6894  10354   -629   -319    458       N  
ATOM   1390  CA  ALA A 270      63.025  73.833  58.063  1.00 69.26           C  
ANISOU 1390  CA  ALA A 270     7975   7476  10864   -684   -311    487       C  
ATOM   1391  C   ALA A 270      64.056  73.393  57.029  1.00 71.77           C  
ANISOU 1391  C   ALA A 270     8280   7837  11151   -736   -270    598       C  
ATOM   1392  O   ALA A 270      63.759  72.570  56.153  1.00 67.72           O  
ANISOU 1392  O   ALA A 270     7764   7399  10569   -758   -192    585       O  
ATOM   1393  CB  ALA A 270      62.472  75.216  57.726  1.00 65.67           C  
ANISOU 1393  CB  ALA A 270     7489   6982  10480   -660   -467    494       C  
ATOM   1394  N   LEU A 271      65.284  73.907  57.134  1.00 67.01           N  
ANISOU 1394  N   LEU A 271     7664   7205  10590   -745   -332    705       N  
ATOM   1395  CA  LEU A 271      66.329  73.520  56.195  1.00 67.71           C  
ANISOU 1395  CA  LEU A 271     7712   7391  10624   -773   -288    828       C  
ATOM   1396  C   LEU A 271      66.632  72.031  56.276  1.00 70.94           C  
ANISOU 1396  C   LEU A 271     8172   7854  10927   -738   -147    761       C  
ATOM   1397  O   LEU A 271      66.922  71.402  55.252  1.00 73.07           O  
ANISOU 1397  O   LEU A 271     8423   8235  11105   -721    -93    790       O  
ATOM   1398  CB  LEU A 271      67.592  74.335  56.457  1.00 68.79           C  
ANISOU 1398  CB  LEU A 271     7805   7499  10833   -801   -387    973       C  
ATOM   1399  CG  LEU A 271      67.456  75.806  56.067  1.00 69.89           C  
ANISOU 1399  CG  LEU A 271     7893   7575  11088   -855   -566   1085       C  
ATOM   1400  CD1 LEU A 271      68.586  76.632  56.652  1.00 69.63           C  
ANISOU 1400  CD1 LEU A 271     7833   7456  11166   -898   -707   1211       C  
ATOM   1401  CD2 LEU A 271      67.395  75.954  54.553  1.00 66.67           C  
ANISOU 1401  CD2 LEU A 271     7401   7305  10626   -897   -555   1215       C  
ATOM   1402  N   LEU A 272      66.562  71.450  57.477  1.00 64.42           N  
ANISOU 1402  N   LEU A 272     7415   6954  10106   -713   -100    671       N  
ATOM   1403  CA  LEU A 272      66.848  70.026  57.624  1.00 57.53           C  
ANISOU 1403  CA  LEU A 272     6610   6100   9150   -684      6    615       C  
ATOM   1404  C   LEU A 272      65.823  69.177  56.882  1.00 62.42           C  
ANISOU 1404  C   LEU A 272     7256   6742   9720   -700     48    536       C  
ATOM   1405  O   LEU A 272      66.183  68.204  56.208  1.00 64.54           O  
ANISOU 1405  O   LEU A 272     7562   7053   9907   -665     84    515       O  
ATOM   1406  CB  LEU A 272      66.884  69.652  59.103  1.00 52.40           C  
ANISOU 1406  CB  LEU A 272     6022   5368   8520   -662     38    556       C  
ATOM   1407  CG  LEU A 272      68.068  70.178  59.917  1.00 48.27           C  
ANISOU 1407  CG  LEU A 272     5492   4814   8032   -630     -4    613       C  
ATOM   1408  CD1 LEU A 272      67.900  69.820  61.395  1.00 45.03           C  
ANISOU 1408  CD1 LEU A 272     5144   4340   7625   -590     27    540       C  
ATOM   1409  CD2 LEU A 272      69.384  69.649  59.378  1.00 44.19           C  
ANISOU 1409  CD2 LEU A 272     4965   4373   7452   -605     31    687       C  
ATOM   1410  N   TYR A 273      64.540  69.536  56.986  1.00 62.89           N  
ANISOU 1410  N   TYR A 273     7296   6778   9823   -739     26    484       N  
ATOM   1411  CA  TYR A 273      63.498  68.781  56.298  1.00 59.56           C  
ANISOU 1411  CA  TYR A 273     6887   6372   9371   -772     45    416       C  
ATOM   1412  C   TYR A 273      63.697  68.790  54.788  1.00 58.74           C  
ANISOU 1412  C   TYR A 273     6757   6354   9209   -748     20    438       C  
ATOM   1413  O   TYR A 273      63.299  67.840  54.106  1.00 58.04           O  
ANISOU 1413  O   TYR A 273     6708   6275   9070   -742     26    371       O  
ATOM   1414  CB  TYR A 273      62.121  69.349  56.637  1.00 64.92           C  
ANISOU 1414  CB  TYR A 273     7517   7051  10100   -810     20    374       C  
ATOM   1415  CG  TYR A 273      61.533  68.843  57.935  1.00 67.66           C  
ANISOU 1415  CG  TYR A 273     7878   7370  10459   -830     67    339       C  
ATOM   1416  CD1 TYR A 273      60.612  67.805  57.945  1.00 63.54           C  
ANISOU 1416  CD1 TYR A 273     7365   6848   9929   -900     99    307       C  
ATOM   1417  CD2 TYR A 273      61.882  69.419  59.149  1.00 68.05           C  
ANISOU 1417  CD2 TYR A 273     7925   7404  10527   -779     65    348       C  
ATOM   1418  CE1 TYR A 273      60.069  67.347  59.125  1.00 61.75           C  
ANISOU 1418  CE1 TYR A 273     7126   6631   9706   -931    145    317       C  
ATOM   1419  CE2 TYR A 273      61.343  68.968  60.336  1.00 62.14           C  
ANISOU 1419  CE2 TYR A 273     7172   6674   9763   -778    115    331       C  
ATOM   1420  CZ  TYR A 273      60.437  67.931  60.318  1.00 60.69           C  
ANISOU 1420  CZ  TYR A 273     6979   6515   9564   -860    164    330       C  
ATOM   1421  OH  TYR A 273      59.891  67.473  61.498  1.00 60.48           O  
ANISOU 1421  OH  TYR A 273     6925   6541   9515   -873    218    354       O  
ATOM   1422  N   PHE A 274      64.300  69.850  54.244  1.00 55.88           N  
ANISOU 1422  N   PHE A 274     6324   6058   8851   -731    -23    540       N  
ATOM   1423  CA  PHE A 274      64.526  69.897  52.805  1.00 55.43           C  
ANISOU 1423  CA  PHE A 274     6220   6128   8714   -695    -38    588       C  
ATOM   1424  C   PHE A 274      65.642  68.960  52.367  1.00 62.13           C  
ANISOU 1424  C   PHE A 274     7094   7066   9445   -608      7    597       C  
ATOM   1425  O   PHE A 274      65.730  68.646  51.175  1.00 73.60           O  
ANISOU 1425  O   PHE A 274     8524   8648  10791   -538      2    595       O  
ATOM   1426  CB  PHE A 274      64.872  71.317  52.355  1.00 59.35           C  
ANISOU 1426  CB  PHE A 274     6619   6681   9251   -718   -107    736       C  
ATOM   1427  CG  PHE A 274      63.776  72.315  52.578  1.00 64.45           C  
ANISOU 1427  CG  PHE A 274     7244   7249   9995   -767   -182    715       C  
ATOM   1428  CD1 PHE A 274      62.448  71.935  52.535  1.00 64.30           C  
ANISOU 1428  CD1 PHE A 274     7249   7204   9978   -778   -170    588       C  
ATOM   1429  CD2 PHE A 274      64.081  73.641  52.844  1.00 70.16           C  
ANISOU 1429  CD2 PHE A 274     7923   7922  10812   -797   -285    824       C  
ATOM   1430  CE1 PHE A 274      61.442  72.859  52.748  1.00 67.11           C  
ANISOU 1430  CE1 PHE A 274     7576   7517  10404   -795   -240    561       C  
ATOM   1431  CE2 PHE A 274      63.082  74.568  53.058  1.00 71.73           C  
ANISOU 1431  CE2 PHE A 274     8118   8044  11093   -808   -377    784       C  
ATOM   1432  CZ  PHE A 274      61.760  74.176  53.010  1.00 72.97           C  
ANISOU 1432  CZ  PHE A 274     8289   8207  11227   -796   -345    648       C  
ATOM   1433  N   ASP A 275      66.490  68.509  53.292  1.00 54.79           N  
ANISOU 1433  N   ASP A 275     6212   6088   8519   -588     43    599       N  
ATOM   1434  CA  ASP A 275      67.732  67.842  52.928  1.00 60.47           C  
ANISOU 1434  CA  ASP A 275     6936   6921   9120   -483     76    628       C  
ATOM   1435  C   ASP A 275      67.558  66.329  52.927  1.00 64.73           C  
ANISOU 1435  C   ASP A 275     7604   7400   9592   -412     90    476       C  
ATOM   1436  O   ASP A 275      66.802  65.768  53.726  1.00 68.26           O  
ANISOU 1436  O   ASP A 275     8139   7683  10114   -476     89    388       O  
ATOM   1437  CB  ASP A 275      68.866  68.247  53.878  1.00 64.19           C  
ANISOU 1437  CB  ASP A 275     7378   7381   9629   -492     90    724       C  
ATOM   1438  CG  ASP A 275      70.221  67.682  53.456  1.00 76.75           C  
ANISOU 1438  CG  ASP A 275     8939   9138  11083   -373    125    776       C  
ATOM   1439  OD1 ASP A 275      70.550  66.535  53.830  1.00 81.54           O  
ANISOU 1439  OD1 ASP A 275     9649   9704  11629   -290    156    671       O  
ATOM   1440  OD2 ASP A 275      70.950  68.385  52.721  1.00 78.08           O  
ANISOU 1440  OD2 ASP A 275     8973   9493  11199   -358    115    933       O  
ATOM   1441  N   GLN A 276      68.273  65.672  52.006  1.00 64.89           N  
ANISOU 1441  N   GLN A 276     7629   7563   9462   -268     88    453       N  
ATOM   1442  CA  GLN A 276      68.171  64.223  51.877  1.00 66.51           C  
ANISOU 1442  CA  GLN A 276     7976   7694   9600   -172     56    294       C  
ATOM   1443  C   GLN A 276      68.666  63.505  53.125  1.00 71.83           C  
ANISOU 1443  C   GLN A 276     8753   8222  10318   -179     77    261       C  
ATOM   1444  O   GLN A 276      68.218  62.391  53.419  1.00 80.92           O  
ANISOU 1444  O   GLN A 276    10043   9213  11491   -177     30    145       O  
ATOM   1445  CB  GLN A 276      68.965  63.741  50.668  1.00 69.99           C  
ANISOU 1445  CB  GLN A 276     8398   8350   9844     34     36    265       C  
ATOM   1446  CG  GLN A 276      70.409  64.192  50.660  1.00 75.86           C  
ANISOU 1446  CG  GLN A 276     9026   9309  10486    124     95    406       C  
ATOM   1447  CD  GLN A 276      71.165  63.648  49.471  1.00 79.67           C  
ANISOU 1447  CD  GLN A 276     9473  10060  10738    363     81    374       C  
ATOM   1448  OE1 GLN A 276      70.814  62.596  48.930  1.00 79.88           O  
ANISOU 1448  OE1 GLN A 276     9625  10048  10679    502      8    192       O  
ATOM   1449  NE2 GLN A 276      72.208  64.358  49.054  1.00 81.38           N  
ANISOU 1449  NE2 GLN A 276     9513  10561  10847    422    136    556       N  
ATOM   1450  N   PHE A 277      69.605  64.104  53.853  1.00 62.62           N  
ANISOU 1450  N   PHE A 277     7523   7102   9167   -189    130    371       N  
ATOM   1451  CA  PHE A 277      70.068  63.536  55.112  1.00 60.36           C  
ANISOU 1451  CA  PHE A 277     7326   6686   8922   -195    154    349       C  
ATOM   1452  C   PHE A 277      69.523  64.270  56.324  1.00 62.15           C  
ANISOU 1452  C   PHE A 277     7531   6787   9295   -343    179    399       C  
ATOM   1453  O   PHE A 277      69.155  63.631  57.310  1.00 60.82           O  
ANISOU 1453  O   PHE A 277     7457   6471   9180   -387    187    351       O  
ATOM   1454  CB  PHE A 277      71.596  63.534  55.169  1.00 61.83           C  
ANISOU 1454  CB  PHE A 277     7464   7022   9006    -72    185    414       C  
ATOM   1455  CG  PHE A 277      72.250  62.987  53.936  1.00 62.86           C  
ANISOU 1455  CG  PHE A 277     7576   7354   8953    117    166    380       C  
ATOM   1456  CD1 PHE A 277      72.048  61.670  53.560  1.00 66.41           C  
ANISOU 1456  CD1 PHE A 277     8178   7734   9323    245    104    213       C  
ATOM   1457  CD2 PHE A 277      73.073  63.781  53.159  1.00 57.45           C  
ANISOU 1457  CD2 PHE A 277     6719   6940   8171    176    195    519       C  
ATOM   1458  CE1 PHE A 277      72.652  61.156  52.430  1.00 63.41           C  
ANISOU 1458  CE1 PHE A 277     7786   7558   8748    465     70    154       C  
ATOM   1459  CE2 PHE A 277      73.681  63.271  52.027  1.00 54.50           C  
ANISOU 1459  CE2 PHE A 277     6307   6808   7592    382    185    492       C  
ATOM   1460  CZ  PHE A 277      73.473  61.955  51.667  1.00 53.46           C  
ANISOU 1460  CZ  PHE A 277     6336   6613   7362    546    123    292       C  
ATOM   1461  N   GLY A 278      69.449  65.602  56.261  1.00 62.53           N  
ANISOU 1461  N   GLY A 278     7458   6897   9402   -410    176    499       N  
ATOM   1462  CA  GLY A 278      68.979  66.373  57.399  1.00 60.48           C  
ANISOU 1462  CA  GLY A 278     7182   6535   9263   -505    174    524       C  
ATOM   1463  C   GLY A 278      67.583  65.994  57.855  1.00 59.80           C  
ANISOU 1463  C   GLY A 278     7151   6335   9235   -580    177    444       C  
ATOM   1464  O   GLY A 278      67.261  66.111  59.042  1.00 64.26           O  
ANISOU 1464  O   GLY A 278     7733   6827   9857   -616    194    438       O  
ATOM   1465  N   ASN A 279      66.734  65.529  56.932  1.00 55.21           N  
ANISOU 1465  N   ASN A 279     6585   5758   8633   -599    156    388       N  
ATOM   1466  CA  ASN A 279      65.374  65.189  57.333  1.00 55.75           C  
ANISOU 1466  CA  ASN A 279     6677   5743   8763   -691    151    338       C  
ATOM   1467  C   ASN A 279      65.362  63.975  58.251  1.00 62.61           C  
ANISOU 1467  C   ASN A 279     7650   6500   9639   -711    169    310       C  
ATOM   1468  O   ASN A 279      64.454  63.830  59.076  1.00 61.19           O  
ANISOU 1468  O   ASN A 279     7461   6274   9513   -796    185    322       O  
ATOM   1469  CB  ASN A 279      64.487  64.960  56.106  1.00 51.99           C  
ANISOU 1469  CB  ASN A 279     6190   5292   8272   -714    104    286       C  
ATOM   1470  CG  ASN A 279      64.712  63.613  55.452  1.00 53.61           C  
ANISOU 1470  CG  ASN A 279     6503   5450   8415   -659     60    207       C  
ATOM   1471  OD1 ASN A 279      64.057  62.629  55.797  1.00 57.92           O  
ANISOU 1471  OD1 ASN A 279     7129   5875   9005   -724     25    162       O  
ATOM   1472  ND2 ASN A 279      65.633  63.563  54.500  1.00 53.65           N  
ANISOU 1472  ND2 ASN A 279     6509   5558   8316   -532     46    195       N  
ATOM   1473  N   TYR A 280      66.365  63.104  58.138  1.00 66.78           N  
ANISOU 1473  N   TYR A 280     8269   6999  10104   -627    162    286       N  
ATOM   1474  CA  TYR A 280      66.512  62.024  59.107  1.00 60.91           C  
ANISOU 1474  CA  TYR A 280     7635   6135   9373   -639    167    278       C  
ATOM   1475  C   TYR A 280      67.094  62.533  60.419  1.00 61.90           C  
ANISOU 1475  C   TYR A 280     7735   6272   9512   -626    231    338       C  
ATOM   1476  O   TYR A 280      66.765  62.004  61.486  1.00 59.35           O  
ANISOU 1476  O   TYR A 280     7455   5878   9218   -675    253    364       O  
ATOM   1477  CB  TYR A 280      67.384  60.914  58.520  1.00 49.31           C  
ANISOU 1477  CB  TYR A 280     6286   4625   7825   -523    114    211       C  
ATOM   1478  CG  TYR A 280      66.707  60.138  57.413  1.00 50.73           C  
ANISOU 1478  CG  TYR A 280     6531   4750   7996   -523     15    123       C  
ATOM   1479  CD1 TYR A 280      66.850  60.512  56.079  1.00 56.28           C  
ANISOU 1479  CD1 TYR A 280     7184   5579   8620   -432    -14     76       C  
ATOM   1480  CD2 TYR A 280      65.924  59.030  57.699  1.00 51.91           C  
ANISOU 1480  CD2 TYR A 280     6787   4722   8215   -615    -66     97       C  
ATOM   1481  CE1 TYR A 280      66.225  59.799  55.064  1.00 62.16           C  
ANISOU 1481  CE1 TYR A 280     7994   6274   9348   -409   -123    -24       C  
ATOM   1482  CE2 TYR A 280      65.304  58.311  56.697  1.00 62.77           C  
ANISOU 1482  CE2 TYR A 280     8231   6021   9598   -616   -193      6       C  
ATOM   1483  CZ  TYR A 280      65.456  58.696  55.384  1.00 67.52           C  
ANISOU 1483  CZ  TYR A 280     8792   6749  10112   -501   -222    -69       C  
ATOM   1484  OH  TYR A 280      64.832  57.969  54.398  1.00 76.19           O  
ANISOU 1484  OH  TYR A 280     9966   7770  11211   -483   -366   -178       O  
ATOM   1485  N   VAL A 281      67.947  63.559  60.354  1.00 58.43           N  
ANISOU 1485  N   VAL A 281     7220   5926   9055   -564    248    373       N  
ATOM   1486  CA  VAL A 281      68.455  64.196  61.564  1.00 51.03           C  
ANISOU 1486  CA  VAL A 281     6254   4993   8142   -546    277    416       C  
ATOM   1487  C   VAL A 281      67.312  64.813  62.360  1.00 55.50           C  
ANISOU 1487  C   VAL A 281     6766   5556   8767   -612    287    423       C  
ATOM   1488  O   VAL A 281      67.248  64.677  63.587  1.00 61.31           O  
ANISOU 1488  O   VAL A 281     7519   6272   9504   -602    318    436       O  
ATOM   1489  CB  VAL A 281      69.526  65.242  61.201  1.00 48.22           C  
ANISOU 1489  CB  VAL A 281     5816   4727   7779   -492    255    467       C  
ATOM   1490  CG1 VAL A 281      69.939  66.038  62.427  1.00 41.00           C  
ANISOU 1490  CG1 VAL A 281     4872   3794   6911   -476    245    496       C  
ATOM   1491  CG2 VAL A 281      70.731  64.562  60.569  1.00 54.25           C  
ANISOU 1491  CG2 VAL A 281     6610   5549   8452   -398    261    471       C  
ATOM   1492  N   ALA A 282      66.386  65.492  61.678  1.00 53.87           N  
ANISOU 1492  N   ALA A 282     6485   5390   8593   -662    259    415       N  
ATOM   1493  CA  ALA A 282      65.243  66.071  62.379  1.00 55.37           C  
ANISOU 1493  CA  ALA A 282     6612   5610   8816   -696    263    411       C  
ATOM   1494  C   ALA A 282      64.368  64.986  62.994  1.00 57.76           C  
ANISOU 1494  C   ALA A 282     6943   5895   9110   -764    308    425       C  
ATOM   1495  O   ALA A 282      63.880  65.135  64.119  1.00 64.35           O  
ANISOU 1495  O   ALA A 282     7737   6780   9931   -755    342    449       O  
ATOM   1496  CB  ALA A 282      64.425  66.947  61.430  1.00 51.66           C  
ANISOU 1496  CB  ALA A 282     6061   5190   8376   -726    216    395       C  
ATOM   1497  N   GLN A 283      64.164  63.880  62.275  1.00 55.14           N  
ANISOU 1497  N   GLN A 283     6674   5496   8779   -829    294    419       N  
ATOM   1498  CA  GLN A 283      63.333  62.804  62.805  1.00 55.26           C  
ANISOU 1498  CA  GLN A 283     6714   5470   8811   -929    306    465       C  
ATOM   1499  C   GLN A 283      63.956  62.178  64.047  1.00 64.11           C  
ANISOU 1499  C   GLN A 283     7900   6553   9907   -901    347    518       C  
ATOM   1500  O   GLN A 283      63.234  61.699  64.930  1.00 73.29           O  
ANISOU 1500  O   GLN A 283     9033   7742  11072   -972    378    599       O  
ATOM   1501  CB  GLN A 283      63.105  61.744  61.730  1.00 44.57           C  
ANISOU 1501  CB  GLN A 283     5442   4011   7483   -995    233    434       C  
ATOM   1502  CG  GLN A 283      62.288  62.227  60.553  1.00 44.60           C  
ANISOU 1502  CG  GLN A 283     5377   4062   7507  -1032    189    387       C  
ATOM   1503  CD  GLN A 283      62.129  61.167  59.480  1.00 69.24           C  
ANISOU 1503  CD  GLN A 283     8591   7073  10644  -1067     92    331       C  
ATOM   1504  OE1 GLN A 283      61.763  60.021  59.764  1.00 60.80           O  
ANISOU 1504  OE1 GLN A 283     7597   5886   9620  -1157     35    361       O  
ATOM   1505  NE2 GLN A 283      62.442  61.534  58.242  1.00 70.42           N  
ANISOU 1505  NE2 GLN A 283     8742   7260  10754   -988     53    255       N  
ATOM   1506  N   CYS A 284      65.289  62.182  64.139  1.00 60.73           N  
ANISOU 1506  N   CYS A 284     7545   6083   9445   -797    350    488       N  
ATOM   1507  CA  CYS A 284      65.956  61.622  65.310  1.00 56.30           C  
ANISOU 1507  CA  CYS A 284     7051   5487   8854   -754    386    531       C  
ATOM   1508  C   CYS A 284      65.523  62.322  66.586  1.00 61.13           C  
ANISOU 1508  C   CYS A 284     7571   6213   9442   -727    442    575       C  
ATOM   1509  O   CYS A 284      65.554  61.719  67.666  1.00 67.56           O  
ANISOU 1509  O   CYS A 284     8414   7032  10225   -725    481    643       O  
ATOM   1510  CB  CYS A 284      67.472  61.716  65.153  1.00 43.04           C  
ANISOU 1510  CB  CYS A 284     5435   3781   7136   -632    377    486       C  
ATOM   1511  SG  CYS A 284      68.155  60.549  63.974  1.00 69.65           S  
ANISOU 1511  SG  CYS A 284     8936   7047  10482   -598    311    429       S  
ATOM   1512  N   CYS A 285      65.112  63.585  66.482  1.00 54.21           N  
ANISOU 1512  N   CYS A 285     6590   5436   8571   -689    435    537       N  
ATOM   1513  CA  CYS A 285      64.664  64.334  67.644  1.00 55.14           C  
ANISOU 1513  CA  CYS A 285     6623   5680   8647   -617    463    547       C  
ATOM   1514  C   CYS A 285      63.269  63.937  68.101  1.00 64.14           C  
ANISOU 1514  C   CYS A 285     7673   6935   9761   -695    508    624       C  
ATOM   1515  O   CYS A 285      62.850  64.366  69.181  1.00 71.44           O  
ANISOU 1515  O   CYS A 285     8519   8009  10616   -613    544    645       O  
ATOM   1516  CB  CYS A 285      64.706  65.829  67.345  1.00 50.47           C  
ANISOU 1516  CB  CYS A 285     5967   5133   8077   -532    400    468       C  
ATOM   1517  SG  CYS A 285      66.379  66.448  67.111  1.00 65.99           S  
ANISOU 1517  SG  CYS A 285     7994   7005  10075   -450    335    428       S  
ATOM   1518  N   LEU A 286      62.544  63.132  67.319  1.00 58.78           N  
ANISOU 1518  N   LEU A 286     6996   6208   9129   -843    498    670       N  
ATOM   1519  CA  LEU A 286      61.250  62.645  67.788  1.00 63.62           C  
ANISOU 1519  CA  LEU A 286     7505   6942   9727   -948    535    783       C  
ATOM   1520  C   LEU A 286      61.399  61.816  69.057  1.00 74.74           C  
ANISOU 1520  C   LEU A 286     8928   8388  11082   -958    591    910       C  
ATOM   1521  O   LEU A 286      60.477  61.773  69.878  1.00 83.59           O  
ANISOU 1521  O   LEU A 286     9917   9700  12142   -981    646   1022       O  
ATOM   1522  CB  LEU A 286      60.561  61.831  66.693  1.00 60.81           C  
ANISOU 1522  CB  LEU A 286     7165   6487   9453  -1122    479    814       C  
ATOM   1523  CG  LEU A 286      60.108  62.586  65.441  1.00 61.53           C  
ANISOU 1523  CG  LEU A 286     7211   6583   9582  -1127    429    713       C  
ATOM   1524  CD1 LEU A 286      59.897  61.598  64.310  1.00 55.13           C  
ANISOU 1524  CD1 LEU A 286     6479   5617   8850  -1260    349    710       C  
ATOM   1525  CD2 LEU A 286      58.834  63.388  65.691  1.00 59.33           C  
ANISOU 1525  CD2 LEU A 286     6756   6518   9270  -1123    458    734       C  
ATOM   1526  N   ARG A 287      62.553  61.162  69.236  1.00 73.58           N  
ANISOU 1526  N   ARG A 287     8927   8084  10944   -930    579    904       N  
ATOM   1527  CA  ARG A 287      62.843  60.420  70.462  1.00 69.42           C  
ANISOU 1527  CA  ARG A 287     8431   7582  10363   -920    626   1022       C  
ATOM   1528  C   ARG A 287      62.651  61.260  71.718  1.00 73.98           C  
ANISOU 1528  C   ARG A 287     8891   8396  10823   -771    700   1036       C  
ATOM   1529  O   ARG A 287      62.317  60.719  72.779  1.00 75.06           O  
ANISOU 1529  O   ARG A 287     8975   8656  10887   -784    758   1181       O  
ATOM   1530  CB  ARG A 287      64.283  59.914  70.434  1.00 74.41           C  
ANISOU 1530  CB  ARG A 287     9238   8029  11007   -851    595    965       C  
ATOM   1531  CG  ARG A 287      64.505  58.525  69.899  1.00 88.57           C  
ANISOU 1531  CG  ARG A 287    11174   9608  12871   -971    523   1014       C  
ATOM   1532  CD  ARG A 287      65.946  58.100  70.179  1.00 93.72           C  
ANISOU 1532  CD  ARG A 287    11979  10137  13495   -853    508    961       C  
ATOM   1533  NE  ARG A 287      66.317  58.323  71.576  1.00 89.25           N  
ANISOU 1533  NE  ARG A 287    11382   9687  12842   -752    584   1019       N  
ATOM   1534  CZ  ARG A 287      67.088  59.321  72.002  1.00 84.38           C  
ANISOU 1534  CZ  ARG A 287    10738   9156  12168   -587    617    922       C  
ATOM   1535  NH1 ARG A 287      67.583  60.198  71.143  1.00 91.22           N  
ANISOU 1535  NH1 ARG A 287    11593  10004  13062   -526    584    790       N  
ATOM   1536  NH2 ARG A 287      67.360  59.446  73.291  1.00 78.92           N  
ANISOU 1536  NH2 ARG A 287    10024   8570  11391   -486    671    968       N  
ATOM   1537  N   PHE A 288      62.875  62.577  71.628  1.00 66.90           N  
ANISOU 1537  N   PHE A 288     7954   7565   9900   -619    681    891       N  
ATOM   1538  CA  PHE A 288      62.865  63.425  72.818  1.00 69.56           C  
ANISOU 1538  CA  PHE A 288     8212   8097  10119   -427    711    857       C  
ATOM   1539  C   PHE A 288      61.503  63.461  73.503  1.00 77.41           C  
ANISOU 1539  C   PHE A 288     9028   9372  11012   -424    776    966       C  
ATOM   1540  O   PHE A 288      61.425  63.839  74.679  1.00 78.94           O  
ANISOU 1540  O   PHE A 288     9151   9773  11071   -254    814    975       O  
ATOM   1541  CB  PHE A 288      63.301  64.853  72.467  1.00 64.31           C  
ANISOU 1541  CB  PHE A 288     7550   7408   9475   -279    629    678       C  
ATOM   1542  CG  PHE A 288      64.730  64.966  71.997  1.00 66.24           C  
ANISOU 1542  CG  PHE A 288     7930   7442   9795   -257    568    597       C  
ATOM   1543  CD1 PHE A 288      65.236  66.189  71.584  1.00 63.67           C  
ANISOU 1543  CD1 PHE A 288     7611   7064   9519   -167    471    475       C  
ATOM   1544  CD2 PHE A 288      65.566  63.862  71.970  1.00 69.16           C  
ANISOU 1544  CD2 PHE A 288     8413   7678  10186   -325    596    656       C  
ATOM   1545  CE1 PHE A 288      66.549  66.307  71.155  1.00 61.44           C  
ANISOU 1545  CE1 PHE A 288     7417   6627   9300   -161    417    436       C  
ATOM   1546  CE2 PHE A 288      66.879  63.973  71.540  1.00 65.34           C  
ANISOU 1546  CE2 PHE A 288     8027   7049   9750   -288    547    590       C  
ATOM   1547  CZ  PHE A 288      67.371  65.197  71.134  1.00 59.31           C  
ANISOU 1547  CZ  PHE A 288     7240   6263   9030   -213    464    491       C  
ATOM   1548  N   LYS A 289      60.437  63.088  72.793  1.00 77.37           N  
ANISOU 1548  N   LYS A 289     8939   9402  11057   -594    782   1049       N  
ATOM   1549  CA  LYS A 289      59.083  63.009  73.332  1.00 77.81           C  
ANISOU 1549  CA  LYS A 289     8795   9751  11019   -624    846   1188       C  
ATOM   1550  C   LYS A 289      58.514  64.369  73.710  1.00 77.14           C  
ANISOU 1550  C   LYS A 289     8578   9917  10816   -398    841   1064       C  
ATOM   1551  O   LYS A 289      59.241  65.364  73.801  1.00 74.49           O  
ANISOU 1551  O   LYS A 289     8319   9517  10469   -206    777    880       O  
ATOM   1552  CB  LYS A 289      59.025  62.073  74.545  1.00 78.42           C  
ANISOU 1552  CB  LYS A 289     8826   9969  11003   -653    928   1397       C  
ATOM   1553  CG  LYS A 289      59.326  60.616  74.226  1.00 81.96           C  
ANISOU 1553  CG  LYS A 289     9391  10179  11571   -895    906   1554       C  
ATOM   1554  CD  LYS A 289      58.968  59.720  75.400  1.00 87.26           C  
ANISOU 1554  CD  LYS A 289     9974  11030  12153   -960    979   1817       C  
ATOM   1555  CE  LYS A 289      59.063  58.252  75.026  1.00 91.85           C  
ANISOU 1555  CE  LYS A 289    10668  11354  12878  -1227    916   1992       C  
ATOM   1556  NZ  LYS A 289      58.187  57.416  75.898  1.00 94.98           N  
ANISOU 1556  NZ  LYS A 289    10903  11964  13220  -1379    966   2317       N  
ATOM   1557  N   TYR A 290      57.204  64.409  73.914  1.00 81.36           N  
ANISOU 1557  N   TYR A 290     8911  10736  11264   -418    891   1167       N  
ATOM   1558  CA  TYR A 290      56.558  65.633  74.351  1.00 84.93           C  
ANISOU 1558  CA  TYR A 290     9228  11467  11575   -170    878   1048       C  
ATOM   1559  C   TYR A 290      57.110  66.034  75.716  1.00 87.77           C  
ANISOU 1559  C   TYR A 290     9590  11989  11770     99    898    999       C  
ATOM   1560  O   TYR A 290      57.330  65.171  76.574  1.00103.78           O  
ANISOU 1560  O   TYR A 290    11602  14101  13727     63    981   1165       O  
ATOM   1561  CB  TYR A 290      55.042  65.428  74.414  1.00 90.97           C  
ANISOU 1561  CB  TYR A 290     9749  12564  12253   -241    945   1203       C  
ATOM   1562  CG  TYR A 290      54.263  66.637  74.871  1.00100.75           C  
ANISOU 1562  CG  TYR A 290    10830  14135  13317     45    929   1079       C  
ATOM   1563  CD1 TYR A 290      53.837  67.601  73.965  1.00 99.49           C  
ANISOU 1563  CD1 TYR A 290    10669  13924  13210    107    836    904       C  
ATOM   1564  CD2 TYR A 290      53.949  66.812  76.211  1.00108.89           C  
ANISOU 1564  CD2 TYR A 290    11715  15545  14115    277    998   1133       C  
ATOM   1565  CE1 TYR A 290      53.125  68.710  74.388  1.00101.51           C  
ANISOU 1565  CE1 TYR A 290    10796  14473  13301    396    797    772       C  
ATOM   1566  CE2 TYR A 290      53.239  67.912  76.642  1.00112.23           C  
ANISOU 1566  CE2 TYR A 290    12000  16289  14355    584    965    995       C  
ATOM   1567  CZ  TYR A 290      52.829  68.857  75.729  1.00108.92           C  
ANISOU 1567  CZ  TYR A 290    11595  15788  14002    644    857    809       C  
ATOM   1568  OH  TYR A 290      52.119  69.949  76.169  1.00114.38           O  
ANISOU 1568  OH  TYR A 290    12162  16790  14505    975    801    656       O  
ATOM   1569  N   PRO A 291      57.359  67.329  75.954  1.00 77.57           N  
ANISOU 1569  N   PRO A 291     8327  10730  10416    377    802    774       N  
ATOM   1570  CA  PRO A 291      57.127  68.445  75.039  1.00 76.85           C  
ANISOU 1570  CA  PRO A 291     8261  10537  10403    443    680    583       C  
ATOM   1571  C   PRO A 291      58.374  68.904  74.289  1.00 77.59           C  
ANISOU 1571  C   PRO A 291     8566  10242  10673    411    559    437       C  
ATOM   1572  O   PRO A 291      58.338  69.949  73.638  1.00 80.41           O  
ANISOU 1572  O   PRO A 291     8958  10500  11096    486    433    285       O  
ATOM   1573  CB  PRO A 291      56.658  69.546  75.981  1.00 74.25           C  
ANISOU 1573  CB  PRO A 291     7834  10501   9878    798    621    441       C  
ATOM   1574  CG  PRO A 291      57.456  69.292  77.229  1.00 66.71           C  
ANISOU 1574  CG  PRO A 291     6927   9610   8810    951    651    454       C  
ATOM   1575  CD  PRO A 291      57.725  67.804  77.297  1.00 69.88           C  
ANISOU 1575  CD  PRO A 291     7340   9951   9261    677    795    701       C  
ATOM   1576  N   LYS A 292      59.465  68.144  74.383  1.00 78.10           N  
ANISOU 1576  N   LYS A 292     8761  10104  10809    303    589    497       N  
ATOM   1577  CA  LYS A 292      60.723  68.613  73.812  1.00 79.63           C  
ANISOU 1577  CA  LYS A 292     9124   9988  11142    299    479    377       C  
ATOM   1578  C   LYS A 292      60.734  68.510  72.288  1.00 75.09           C  
ANISOU 1578  C   LYS A 292     8597   9203  10729     89    449    382       C  
ATOM   1579  O   LYS A 292      61.348  69.349  71.617  1.00 70.05           O  
ANISOU 1579  O   LYS A 292     8036   8390  10190    115    332    274       O  
ATOM   1580  CB  LYS A 292      61.888  67.833  74.419  1.00 78.00           C  
ANISOU 1580  CB  LYS A 292     9028   9669  10940    277    523    434       C  
ATOM   1581  CG  LYS A 292      62.031  68.039  75.917  1.00 80.33           C  
ANISOU 1581  CG  LYS A 292     9290  10160  11070    513    534    408       C  
ATOM   1582  CD  LYS A 292      63.484  67.980  76.352  1.00 84.76           C  
ANISOU 1582  CD  LYS A 292     9995  10540  11671    571    485    357       C  
ATOM   1583  CE  LYS A 292      63.653  68.440  77.797  1.00 91.14           C  
ANISOU 1583  CE  LYS A 292    10780  11535  12315    852    455    282       C  
ATOM   1584  NZ  LYS A 292      63.221  69.850  78.018  1.00 95.72           N  
ANISOU 1584  NZ  LYS A 292    11319  12207  12844   1096    303     92       N  
ATOM   1585  N   ASN A 293      60.057  67.508  71.725  1.00 69.98           N  
ANISOU 1585  N   ASN A 293     7902   8576  10110   -116    538    515       N  
ATOM   1586  CA  ASN A 293      60.020  67.327  70.279  1.00 66.80           C  
ANISOU 1586  CA  ASN A 293     7545   7994   9840   -294    506    511       C  
ATOM   1587  C   ASN A 293      59.018  68.244  69.597  1.00 73.52           C  
ANISOU 1587  C   ASN A 293     8301   8934  10700   -264    448    439       C  
ATOM   1588  O   ASN A 293      58.824  68.126  68.382  1.00 78.33           O  
ANISOU 1588  O   ASN A 293     8929   9430  11403   -401    422    438       O  
ATOM   1589  CB  ASN A 293      59.686  65.873  69.933  1.00 67.89           C  
ANISOU 1589  CB  ASN A 293     7687   8091  10018   -518    583    664       C  
ATOM   1590  CG  ASN A 293      58.327  65.439  70.462  1.00 71.07           C  
ANISOU 1590  CG  ASN A 293     7920   8745  10339   -574    656    796       C  
ATOM   1591  OD1 ASN A 293      57.597  66.225  71.072  1.00 60.69           O  
ANISOU 1591  OD1 ASN A 293     6472   7674   8913   -423    666    764       O  
ATOM   1592  ND2 ASN A 293      57.988  64.175  70.242  1.00 79.56           N  
ANISOU 1592  ND2 ASN A 293     8995   9769  11466   -787    692    950       N  
ATOM   1593  N   THR A 294      58.371  69.138  70.348  1.00 74.16           N  
ANISOU 1593  N   THR A 294     8282   9222  10672    -67    418    370       N  
ATOM   1594  CA  THR A 294      57.319  69.973  69.779  1.00 74.17           C  
ANISOU 1594  CA  THR A 294     8186   9331  10662    -16    360    299       C  
ATOM   1595  C   THR A 294      57.864  70.927  68.724  1.00 65.61           C  
ANISOU 1595  C   THR A 294     7203   8021   9704    -10    221    184       C  
ATOM   1596  O   THR A 294      57.143  71.288  67.784  1.00 67.77           O  
ANISOU 1596  O   THR A 294     7430   8300  10019    -62    183    161       O  
ATOM   1597  CB  THR A 294      56.604  70.739  70.898  1.00 81.53           C  
ANISOU 1597  CB  THR A 294     9000  10550  11426    247    340    229       C  
ATOM   1598  OG1 THR A 294      55.991  69.805  71.796  1.00 84.27           O  
ANISOU 1598  OG1 THR A 294     9216  11160  11643    220    484    382       O  
ATOM   1599  CG2 THR A 294      55.528  71.664  70.342  1.00 83.23           C  
ANISOU 1599  CG2 THR A 294     9119  10885  11618    337    262    137       C  
ATOM   1600  N   PHE A 295      59.138  71.319  68.834  1.00 61.34           N  
ANISOU 1600  N   PHE A 295     6790   7289   9228     40    143    131       N  
ATOM   1601  CA  PHE A 295      59.707  72.226  67.842  1.00 64.02           C  
ANISOU 1601  CA  PHE A 295     7206   7427   9692     24      4     68       C  
ATOM   1602  C   PHE A 295      59.637  71.633  66.440  1.00 63.99           C  
ANISOU 1602  C   PHE A 295     7212   7327   9773   -188     51    141       C  
ATOM   1603  O   PHE A 295      59.512  72.374  65.459  1.00 67.19           O  
ANISOU 1603  O   PHE A 295     7622   7659  10248   -208    -42    109       O  
ATOM   1604  CB  PHE A 295      61.148  72.582  68.217  1.00 67.32           C  
ANISOU 1604  CB  PHE A 295     7736   7672  10169     76    -82     42       C  
ATOM   1605  CG  PHE A 295      62.160  71.550  67.815  1.00 70.88           C  
ANISOU 1605  CG  PHE A 295     8258   8002  10672    -85      9    140       C  
ATOM   1606  CD1 PHE A 295      62.905  71.706  66.659  1.00 65.32           C  
ANISOU 1606  CD1 PHE A 295     7602   7145  10073   -196    -41    175       C  
ATOM   1607  CD2 PHE A 295      62.368  70.425  68.594  1.00 78.64           C  
ANISOU 1607  CD2 PHE A 295     9253   9041  11585   -109    136    203       C  
ATOM   1608  CE1 PHE A 295      63.837  70.759  66.286  1.00 68.65           C  
ANISOU 1608  CE1 PHE A 295     8082   7488  10515   -303     35    249       C  
ATOM   1609  CE2 PHE A 295      63.300  69.473  68.226  1.00 76.71           C  
ANISOU 1609  CE2 PHE A 295     9086   8679  11381   -228    198    275       C  
ATOM   1610  CZ  PHE A 295      64.033  69.639  67.069  1.00 72.18           C  
ANISOU 1610  CZ  PHE A 295     8558   7970  10897   -312    148    287       C  
ATOM   1611  N   LEU A 296      59.686  70.302  66.328  1.00 56.46           N  
ANISOU 1611  N   LEU A 296     6267   6373   8812   -336    177    238       N  
ATOM   1612  CA  LEU A 296      59.546  69.665  65.023  1.00 52.54           C  
ANISOU 1612  CA  LEU A 296     5787   5795   8380   -507    202    285       C  
ATOM   1613  C   LEU A 296      58.171  69.921  64.427  1.00 60.43           C  
ANISOU 1613  C   LEU A 296     6679   6911   9369   -540    192    270       C  
ATOM   1614  O   LEU A 296      58.035  70.087  63.210  1.00 68.60           O  
ANISOU 1614  O   LEU A 296     7724   7879  10462   -612    150    257       O  
ATOM   1615  CB  LEU A 296      59.780  68.163  65.137  1.00 52.93           C  
ANISOU 1615  CB  LEU A 296     5881   5806   8425   -637    300    375       C  
ATOM   1616  CG  LEU A 296      61.207  67.717  65.394  1.00 62.04           C  
ANISOU 1616  CG  LEU A 296     7153   6826   9595   -625    310    390       C  
ATOM   1617  CD1 LEU A 296      61.203  66.219  65.649  1.00 65.90           C  
ANISOU 1617  CD1 LEU A 296     7686   7283  10071   -735    386    476       C  
ATOM   1618  CD2 LEU A 296      62.110  68.096  64.228  1.00 63.41           C  
ANISOU 1618  CD2 LEU A 296     7388   6872   9831   -642    246    363       C  
ATOM   1619  N   PHE A 297      57.136  69.934  65.264  1.00 64.63           N  
ANISOU 1619  N   PHE A 297     7096   7645   9814   -480    234    279       N  
ATOM   1620  CA  PHE A 297      55.783  70.106  64.752  1.00 72.15           C  
ANISOU 1620  CA  PHE A 297     7924   8743  10746   -511    231    275       C  
ATOM   1621  C   PHE A 297      55.436  71.573  64.550  1.00 77.39           C  
ANISOU 1621  C   PHE A 297     8562   9444  11400   -343    113    155       C  
ATOM   1622  O   PHE A 297      54.670  71.902  63.635  1.00 76.05           O  
ANISOU 1622  O   PHE A 297     8340   9301  11254   -379     73    130       O  
ATOM   1623  CB  PHE A 297      54.788  69.423  65.687  1.00 69.30           C  
ANISOU 1623  CB  PHE A 297     7420   8625  10286   -530    330    369       C  
ATOM   1624  CG  PHE A 297      55.014  67.948  65.812  1.00 66.97           C  
ANISOU 1624  CG  PHE A 297     7155   8267  10024   -722    414    508       C  
ATOM   1625  CD1 PHE A 297      55.930  67.451  66.724  1.00 62.82           C  
ANISOU 1625  CD1 PHE A 297     6708   7687   9473   -695    460    554       C  
ATOM   1626  CD2 PHE A 297      54.326  67.059  65.003  1.00 65.65           C  
ANISOU 1626  CD2 PHE A 297     6949   8074   9921   -926    422    588       C  
ATOM   1627  CE1 PHE A 297      56.155  66.097  66.831  1.00 59.03           C  
ANISOU 1627  CE1 PHE A 297     6275   7124   9032   -865    512    682       C  
ATOM   1628  CE2 PHE A 297      54.543  65.699  65.109  1.00 63.21           C  
ANISOU 1628  CE2 PHE A 297     6690   7667   9660  -1102    455    712       C  
ATOM   1629  CZ  PHE A 297      55.459  65.219  66.024  1.00 61.72           C  
ANISOU 1629  CZ  PHE A 297     6586   7418   9445  -1070    500    761       C  
ATOM   1630  N   GLU A 298      55.993  72.464  65.373  1.00 73.82           N  
ANISOU 1630  N   GLU A 298     8155   8977  10917   -154     35     74       N  
ATOM   1631  CA  GLU A 298      55.836  73.892  65.123  1.00 78.03           C  
ANISOU 1631  CA  GLU A 298     8703   9475  11470      6   -129    -46       C  
ATOM   1632  C   GLU A 298      56.364  74.259  63.741  1.00 82.08           C  
ANISOU 1632  C   GLU A 298     9296   9775  12114   -111   -211    -32       C  
ATOM   1633  O   GLU A 298      55.676  74.922  62.956  1.00 88.64           O  
ANISOU 1633  O   GLU A 298    10094  10619  12967    -94   -289    -72       O  
ATOM   1634  CB  GLU A 298      56.548  74.701  66.209  1.00 82.67           C  
ANISOU 1634  CB  GLU A 298     9358  10022  12030    215   -239   -136       C  
ATOM   1635  CG  GLU A 298      55.947  74.541  67.598  1.00 90.91           C  
ANISOU 1635  CG  GLU A 298    10307  11326  12906    394   -177   -168       C  
ATOM   1636  CD  GLU A 298      56.780  75.206  68.682  1.00 94.83           C  
ANISOU 1636  CD  GLU A 298    10890  11768  13374    606   -292   -268       C  
ATOM   1637  OE1 GLU A 298      57.720  75.960  68.338  1.00 93.97           O  
ANISOU 1637  OE1 GLU A 298    10906  11407  13391    613   -453   -318       O  
ATOM   1638  OE2 GLU A 298      56.493  74.972  69.879  1.00 94.07           O  
ANISOU 1638  OE2 GLU A 298    10726  11891  13125    763   -231   -284       O  
ATOM   1639  N   VAL A 299      57.581  73.813  63.420  1.00 76.30           N  
ANISOU 1639  N   VAL A 299     8661   8872  11457   -222   -190     34       N  
ATOM   1640  CA  VAL A 299      58.173  74.123  62.122  1.00 66.28           C  
ANISOU 1640  CA  VAL A 299     7448   7450  10287   -323   -255     74       C  
ATOM   1641  C   VAL A 299      57.386  73.460  60.999  1.00 69.76           C  
ANISOU 1641  C   VAL A 299     7836   7945  10724   -455   -183    109       C  
ATOM   1642  O   VAL A 299      57.182  74.052  59.932  1.00 75.71           O  
ANISOU 1642  O   VAL A 299     8585   8661  11521   -478   -258    108       O  
ATOM   1643  CB  VAL A 299      59.648  73.696  62.100  1.00 60.20           C  
ANISOU 1643  CB  VAL A 299     6765   6543   9565   -391   -234    144       C  
ATOM   1644  CG1 VAL A 299      60.250  73.937  60.720  1.00 62.25           C  
ANISOU 1644  CG1 VAL A 299     7049   6706   9896   -488   -282    213       C  
ATOM   1645  CG2 VAL A 299      60.420  74.434  63.176  1.00 60.26           C  
ANISOU 1645  CG2 VAL A 299     6822   6484   9591   -263   -334    104       C  
ATOM   1646  N   MET A 300      56.934  72.223  61.216  1.00 67.03           N  
ANISOU 1646  N   MET A 300     7454   7682  10332   -547    -53    147       N  
ATOM   1647  CA  MET A 300      56.131  71.553  60.201  1.00 73.74           C  
ANISOU 1647  CA  MET A 300     8257   8571  11188   -673    -14    169       C  
ATOM   1648  C   MET A 300      54.812  72.273  59.956  1.00 80.97           C  
ANISOU 1648  C   MET A 300     9066   9623  12078   -617    -63    116       C  
ATOM   1649  O   MET A 300      54.298  72.251  58.834  1.00 74.71           O  
ANISOU 1649  O   MET A 300     8249   8829  11309   -684    -88    111       O  
ATOM   1650  CB  MET A 300      55.876  70.101  60.601  1.00 73.04           C  
ANISOU 1650  CB  MET A 300     8154   8520  11078   -793     95    233       C  
ATOM   1651  CG  MET A 300      57.005  69.167  60.230  1.00 66.92           C  
ANISOU 1651  CG  MET A 300     7497   7592  10337   -875    123    273       C  
ATOM   1652  SD  MET A 300      56.566  67.438  60.441  1.00 52.00           S  
ANISOU 1652  SD  MET A 300     5612   5693   8451  -1034    191    346       S  
ATOM   1653  CE  MET A 300      56.416  67.359  62.220  1.00 48.85           C  
ANISOU 1653  CE  MET A 300     5153   5419   7989   -978    267    406       C  
ATOM   1654  N   ALA A 301      54.246  72.916  60.979  1.00 82.50           N  
ANISOU 1654  N   ALA A 301     9190   9950  12206   -471    -84     66       N  
ATOM   1655  CA  ALA A 301      52.979  73.611  60.782  1.00 75.31           C  
ANISOU 1655  CA  ALA A 301     8169   9195  11250   -386   -136      4       C  
ATOM   1656  C   ALA A 301      53.184  74.952  60.089  1.00 80.61           C  
ANISOU 1656  C   ALA A 301     8900   9752  11974   -285   -295    -67       C  
ATOM   1657  O   ALA A 301      52.468  75.283  59.139  1.00 88.38           O  
ANISOU 1657  O   ALA A 301     9844  10765  12973   -305   -341    -87       O  
ATOM   1658  CB  ALA A 301      52.264  73.801  62.119  1.00 64.41           C  
ANISOU 1658  CB  ALA A 301     6679   8044   9750   -230   -106    -29       C  
ATOM   1659  N   ARG A 302      54.163  75.733  60.549  1.00 75.33           N  
ANISOU 1659  N   ARG A 302     8330   8946  11345   -183   -396    -95       N  
ATOM   1660  CA  ARG A 302      54.385  77.052  59.969  1.00 78.47           C  
ANISOU 1660  CA  ARG A 302     8790   9211  11814   -101   -583   -137       C  
ATOM   1661  C   ARG A 302      54.846  76.949  58.521  1.00 78.84           C  
ANISOU 1661  C   ARG A 302     8875   9137  11943   -259   -590    -47       C  
ATOM   1662  O   ARG A 302      54.349  77.675  57.653  1.00 89.22           O  
ANISOU 1662  O   ARG A 302    10179  10437  13285   -240   -689    -59       O  
ATOM   1663  CB  ARG A 302      55.405  77.824  60.803  1.00 86.76           C  
ANISOU 1663  CB  ARG A 302     9937  10117  12911     14   -714   -167       C  
ATOM   1664  CG  ARG A 302      55.845  79.139  60.190  1.00100.41           C  
ANISOU 1664  CG  ARG A 302    11746  11655  14752     55   -940   -168       C  
ATOM   1665  CD  ARG A 302      56.899  79.813  61.055  1.00117.23           C  
ANISOU 1665  CD  ARG A 302    13972  13622  16948    145  -1092   -189       C  
ATOM   1666  NE  ARG A 302      56.322  80.792  61.972  1.00130.38           N  
ANISOU 1666  NE  ARG A 302    15658  15308  18572    398  -1272   -350       N  
ATOM   1667  CZ  ARG A 302      56.062  82.056  61.653  1.00136.55           C  
ANISOU 1667  CZ  ARG A 302    16494  15966  19425    508  -1522   -412       C  
ATOM   1668  NH1 ARG A 302      56.323  82.502  60.429  1.00134.63           N  
ANISOU 1668  NH1 ARG A 302    16279  15577  19299    365  -1608   -297       N  
ATOM   1669  NH2 ARG A 302      55.538  82.874  62.557  1.00140.48           N  
ANISOU 1669  NH2 ARG A 302    17020  16491  19865    778  -1697   -587       N  
ATOM   1670  N   HIS A 303      55.783  76.050  58.237  1.00 70.85           N  
ANISOU 1670  N   HIS A 303     7907   8058  10956   -395   -490     42       N  
ATOM   1671  CA  HIS A 303      56.345  75.896  56.901  1.00 69.04           C  
ANISOU 1671  CA  HIS A 303     7707   7755  10772   -513   -491    130       C  
ATOM   1672  C   HIS A 303      55.813  74.641  56.223  1.00 75.39           C  
ANISOU 1672  C   HIS A 303     8471   8644  11529   -626   -360    139       C  
ATOM   1673  O   HIS A 303      56.534  73.954  55.496  1.00 77.94           O  
ANISOU 1673  O   HIS A 303     8833   8927  11855   -710   -310    199       O  
ATOM   1674  CB  HIS A 303      57.868  75.871  56.962  1.00 69.06           C  
ANISOU 1674  CB  HIS A 303     7781   7636  10824   -554   -502    220       C  
ATOM   1675  CG  HIS A 303      58.446  76.986  57.773  1.00 83.40           C  
ANISOU 1675  CG  HIS A 303     9642   9343  12704   -458   -652    211       C  
ATOM   1676  ND1 HIS A 303      58.714  78.230  57.245  1.00 89.42           N  
ANISOU 1676  ND1 HIS A 303    10427   9998  13552   -439   -836    260       N  
ATOM   1677  CD2 HIS A 303      58.793  77.049  59.080  1.00 88.30           C  
ANISOU 1677  CD2 HIS A 303    10295   9937  13318   -371   -668    157       C  
ATOM   1678  CE1 HIS A 303      59.208  79.010  58.190  1.00 91.44           C  
ANISOU 1678  CE1 HIS A 303    10734  10143  13866   -350   -978    229       C  
ATOM   1679  NE2 HIS A 303      59.267  78.317  59.313  1.00 89.51           N  
ANISOU 1679  NE2 HIS A 303    10496   9954  13559   -296   -875    157       N  
ATOM   1680  N   CYS A 304      54.537  74.333  56.464  1.00 75.92           N  
ANISOU 1680  N   CYS A 304     8455   8841  11550   -619   -320     79       N  
ATOM   1681  CA  CYS A 304      53.936  73.143  55.875  1.00 69.84           C  
ANISOU 1681  CA  CYS A 304     7646   8131  10757   -740   -233     89       C  
ATOM   1682  C   CYS A 304      53.968  73.201  54.357  1.00 68.45           C  
ANISOU 1682  C   CYS A 304     7487   7925  10595   -786   -276    102       C  
ATOM   1683  O   CYS A 304      54.139  72.170  53.700  1.00 73.43           O  
ANISOU 1683  O   CYS A 304     8145   8537  11217   -874   -230    116       O  
ATOM   1684  CB  CYS A 304      52.502  72.980  56.379  1.00 69.66           C  
ANISOU 1684  CB  CYS A 304     7501   8279  10690   -731   -204     47       C  
ATOM   1685  SG  CYS A 304      51.641  71.532  55.754  1.00 75.43           S  
ANISOU 1685  SG  CYS A 304     8170   9069  11423   -908   -140     74       S  
ATOM   1686  N   CYS A 305      53.830  74.398  53.786  1.00 70.63           N  
ANISOU 1686  N   CYS A 305     7755   8194  10888   -714   -379     98       N  
ATOM   1687  CA  CYS A 305      53.843  74.535  52.335  1.00 78.90           C  
ANISOU 1687  CA  CYS A 305     8806   9241  11932   -743   -421    126       C  
ATOM   1688  C   CYS A 305      55.211  74.208  51.752  1.00 71.15           C  
ANISOU 1688  C   CYS A 305     7894   8192  10948   -778   -399    215       C  
ATOM   1689  O   CYS A 305      55.332  73.349  50.871  1.00 71.05           O  
ANISOU 1689  O   CYS A 305     7894   8211  10892   -820   -358    215       O  
ATOM   1690  CB  CYS A 305      53.424  75.946  51.936  1.00 92.44           C  
ANISOU 1690  CB  CYS A 305    10499  10954  13669   -657   -551    124       C  
ATOM   1691  SG  CYS A 305      53.290  76.132  50.155  1.00 98.68           S  
ANISOU 1691  SG  CYS A 305    11277  11781  14435   -682   -598    172       S  
ATOM   1692  N   GLU A 306      56.250  74.903  52.217  1.00 64.38           N  
ANISOU 1692  N   GLU A 306     7076   7256  10131   -747   -441    288       N  
ATOM   1693  CA  GLU A 306      57.590  74.679  51.686  1.00 62.41           C  
ANISOU 1693  CA  GLU A 306     6862   6984   9868   -774   -420    395       C  
ATOM   1694  C   GLU A 306      58.040  73.244  51.925  1.00 68.78           C  
ANISOU 1694  C   GLU A 306     7709   7797  10626   -809   -304    363       C  
ATOM   1695  O   GLU A 306      58.569  72.587  51.021  1.00 83.23           O  
ANISOU 1695  O   GLU A 306     9555   9675  12394   -812   -271    390       O  
ATOM   1696  CB  GLU A 306      58.571  75.666  52.318  1.00 61.40           C  
ANISOU 1696  CB  GLU A 306     6756   6763   9812   -754   -502    486       C  
ATOM   1697  CG  GLU A 306      58.164  77.136  52.230  1.00 66.41           C  
ANISOU 1697  CG  GLU A 306     7376   7339  10518   -712   -666    512       C  
ATOM   1698  CD  GLU A 306      57.296  77.579  53.396  1.00 80.86           C  
ANISOU 1698  CD  GLU A 306     9216   9130  12376   -629   -719    381       C  
ATOM   1699  OE1 GLU A 306      56.353  76.843  53.759  1.00 89.41           O  
ANISOU 1699  OE1 GLU A 306    10269  10302  13402   -615   -625    272       O  
ATOM   1700  OE2 GLU A 306      57.574  78.648  53.975  1.00 86.69           O  
ANISOU 1700  OE2 GLU A 306     9988   9760  13190   -570   -868    392       O  
ATOM   1701  N   ILE A 307      57.820  72.733  53.138  1.00 61.24           N  
ANISOU 1701  N   ILE A 307     6774   6806   9689   -820   -252    305       N  
ATOM   1702  CA  ILE A 307      58.280  71.390  53.472  1.00 62.31           C  
ANISOU 1702  CA  ILE A 307     6963   6918   9792   -857   -165    287       C  
ATOM   1703  C   ILE A 307      57.469  70.342  52.718  1.00 64.25           C  
ANISOU 1703  C   ILE A 307     7210   7197  10005   -906   -148    222       C  
ATOM   1704  O   ILE A 307      58.027  69.415  52.119  1.00 62.01           O  
ANISOU 1704  O   ILE A 307     6984   6900   9677   -905   -133    211       O  
ATOM   1705  CB  ILE A 307      58.216  71.169  54.992  1.00 58.92           C  
ANISOU 1705  CB  ILE A 307     6546   6452   9387   -857   -120    265       C  
ATOM   1706  CG1 ILE A 307      59.155  72.136  55.709  1.00 53.81           C  
ANISOU 1706  CG1 ILE A 307     5916   5753   8776   -796   -163    313       C  
ATOM   1707  CG2 ILE A 307      58.599  69.751  55.328  1.00 57.83           C  
ANISOU 1707  CG2 ILE A 307     6472   6276   9226   -905    -46    257       C  
ATOM   1708  CD1 ILE A 307      58.996  72.136  57.213  1.00 51.93           C  
ANISOU 1708  CD1 ILE A 307     5682   5505   8544   -757   -139    276       C  
ATOM   1709  N   GLY A 308      56.141  70.480  52.726  1.00 63.75           N  
ANISOU 1709  N   GLY A 308     7082   7181   9960   -937   -169    171       N  
ATOM   1710  CA  GLY A 308      55.272  69.500  52.093  1.00 60.58           C  
ANISOU 1710  CA  GLY A 308     6671   6799   9550  -1004   -180    113       C  
ATOM   1711  C   GLY A 308      55.430  69.408  50.590  1.00 69.96           C  
ANISOU 1711  C   GLY A 308     7880   8014  10688   -968   -231     90       C  
ATOM   1712  O   GLY A 308      55.001  68.417  49.989  1.00 72.20           O  
ANISOU 1712  O   GLY A 308     8190   8283  10959  -1005   -264     27       O  
ATOM   1713  N   GLN A 309      56.037  70.412  49.965  1.00 72.39           N  
ANISOU 1713  N   GLN A 309     8174   8366  10966   -894   -254    147       N  
ATOM   1714  CA  GLN A 309      56.276  70.380  48.530  1.00 75.27           C  
ANISOU 1714  CA  GLN A 309     8541   8802  11254   -838   -292    149       C  
ATOM   1715  C   GLN A 309      57.620  69.764  48.157  1.00 79.82           C  
ANISOU 1715  C   GLN A 309     9179   9394  11753   -774   -263    182       C  
ATOM   1716  O   GLN A 309      57.897  69.597  46.963  1.00 82.62           O  
ANISOU 1716  O   GLN A 309     9533   9847  12012   -696   -290    179       O  
ATOM   1717  CB  GLN A 309      56.167  71.793  47.952  1.00 73.01           C  
ANISOU 1717  CB  GLN A 309     8189   8583  10968   -797   -342    226       C  
ATOM   1718  CG  GLN A 309      54.752  72.344  47.972  1.00 78.97           C  
ANISOU 1718  CG  GLN A 309     8881   9358  11766   -819   -390    166       C  
ATOM   1719  CD  GLN A 309      54.618  73.647  47.218  1.00 84.70           C  
ANISOU 1719  CD  GLN A 309     9560  10135  12485   -767   -465    236       C  
ATOM   1720  OE1 GLN A 309      54.976  73.735  46.045  1.00 87.91           O  
ANISOU 1720  OE1 GLN A 309     9959  10621  12822   -726   -487    288       O  
ATOM   1721  NE2 GLN A 309      54.080  74.662  47.880  1.00 90.03           N  
ANISOU 1721  NE2 GLN A 309    10205  10776  13226   -755   -517    237       N  
ATOM   1722  N   SER A 310      58.454  69.411  49.133  1.00 70.54           N  
ANISOU 1722  N   SER A 310     8052   8148  10600   -786   -211    211       N  
ATOM   1723  CA  SER A 310      59.777  68.873  48.856  1.00 64.83           C  
ANISOU 1723  CA  SER A 310     7377   7461   9794   -708   -183    245       C  
ATOM   1724  C   SER A 310      59.768  67.353  48.930  1.00 60.41           C  
ANISOU 1724  C   SER A 310     6919   6827   9208   -696   -191    129       C  
ATOM   1725  O   SER A 310      59.019  66.756  49.706  1.00 63.59           O  
ANISOU 1725  O   SER A 310     7356   7114   9691   -789   -196     72       O  
ATOM   1726  CB  SER A 310      60.810  69.417  49.838  1.00 62.06           C  
ANISOU 1726  CB  SER A 310     7020   7077   9482   -716   -139    349       C  
ATOM   1727  OG  SER A 310      60.741  68.706  51.058  1.00 60.76           O  
ANISOU 1727  OG  SER A 310     6920   6794   9374   -765   -102    295       O  
ATOM   1728  N   ARG A 311      60.634  66.733  48.124  1.00 55.66           N  
ANISOU 1728  N   ARG A 311     6361   6302   8486   -573   -204    104       N  
ATOM   1729  CA  ARG A 311      60.687  65.275  48.067  1.00 62.59           C  
ANISOU 1729  CA  ARG A 311     7360   7089   9333   -529   -255    -25       C  
ATOM   1730  C   ARG A 311      60.989  64.678  49.436  1.00 66.82           C  
ANISOU 1730  C   ARG A 311     7967   7470   9951   -604   -219    -18       C  
ATOM   1731  O   ARG A 311      60.438  63.634  49.802  1.00 69.91           O  
ANISOU 1731  O   ARG A 311     8446   7715  10402   -667   -277    -98       O  
ATOM   1732  CB  ARG A 311      61.726  64.821  47.036  1.00 60.28           C  
ANISOU 1732  CB  ARG A 311     7097   6940   8867   -331   -278    -57       C  
ATOM   1733  CG  ARG A 311      62.155  63.361  47.165  1.00 66.37           C  
ANISOU 1733  CG  ARG A 311     8017   7603   9597   -243   -345   -189       C  
ATOM   1734  CD  ARG A 311      62.921  62.882  45.939  1.00 73.50           C  
ANISOU 1734  CD  ARG A 311     8946   8683  10297      1   -399   -266       C  
ATOM   1735  NE  ARG A 311      63.271  61.462  46.017  1.00 83.22           N  
ANISOU 1735  NE  ARG A 311    10343   9787  11488    114   -503   -423       N  
ATOM   1736  CZ  ARG A 311      62.425  60.466  45.768  1.00 84.63           C  
ANISOU 1736  CZ  ARG A 311    10648   9784  11724    100   -661   -585       C  
ATOM   1737  NH1 ARG A 311      61.163  60.725  45.448  1.00 87.10           N  
ANISOU 1737  NH1 ARG A 311    10922  10041  12132    -31   -714   -607       N  
ATOM   1738  NH2 ARG A 311      62.835  59.207  45.852  1.00 80.06           N  
ANISOU 1738  NH2 ARG A 311    10235   9067  11115    213   -786   -722       N  
ATOM   1739  N   PHE A 312      61.836  65.343  50.218  1.00 61.49           N  
ANISOU 1739  N   PHE A 312     7254   6821   9288   -607   -137     90       N  
ATOM   1740  CA  PHE A 312      62.246  64.798  51.504  1.00 59.84           C  
ANISOU 1740  CA  PHE A 312     7112   6489   9135   -652    -97    100       C  
ATOM   1741  C   PHE A 312      61.396  65.308  52.657  1.00 58.24           C  
ANISOU 1741  C   PHE A 312     6862   6214   9052   -788    -62    142       C  
ATOM   1742  O   PHE A 312      61.039  64.532  53.550  1.00 67.82           O  
ANISOU 1742  O   PHE A 312     8130   7318  10322   -862    -58    125       O  
ATOM   1743  CB  PHE A 312      63.717  65.115  51.744  1.00 64.63           C  
ANISOU 1743  CB  PHE A 312     7707   7173   9676   -560    -41    180       C  
ATOM   1744  CG  PHE A 312      64.601  64.634  50.643  1.00 74.83           C  
ANISOU 1744  CG  PHE A 312     9019   8597  10818   -395    -65    150       C  
ATOM   1745  CD1 PHE A 312      65.274  65.528  49.834  1.00 75.64           C  
ANISOU 1745  CD1 PHE A 312     9006   8902  10830   -321    -41    256       C  
ATOM   1746  CD2 PHE A 312      64.718  63.278  50.385  1.00 78.49           C  
ANISOU 1746  CD2 PHE A 312     9610   8991  11220   -305   -130     19       C  
ATOM   1747  CE1 PHE A 312      66.077  65.077  48.809  1.00 75.53           C  
ANISOU 1747  CE1 PHE A 312     8985   9069  10644   -143    -54    238       C  
ATOM   1748  CE2 PHE A 312      65.516  62.820  49.361  1.00 74.66           C  
ANISOU 1748  CE2 PHE A 312     9144   8657  10568   -106   -165    -33       C  
ATOM   1749  CZ  PHE A 312      66.197  63.721  48.571  1.00 70.52           C  
ANISOU 1749  CZ  PHE A 312     8483   8383   9928    -17   -114     78       C  
ATOM   1750  N   GLY A 313      61.054  66.592  52.652  1.00 53.12           N  
ANISOU 1750  N   GLY A 313     6112   5637   8434   -810    -47    202       N  
ATOM   1751  CA  GLY A 313      60.244  67.127  53.732  1.00 61.89           C  
ANISOU 1751  CA  GLY A 313     7172   6714   9629   -891    -25    221       C  
ATOM   1752  C   GLY A 313      58.866  66.498  53.801  1.00 70.34           C  
ANISOU 1752  C   GLY A 313     8228   7757  10742   -986    -49    168       C  
ATOM   1753  O   GLY A 313      58.377  66.173  54.886  1.00 78.73           O  
ANISOU 1753  O   GLY A 313     9279   8787  11849  -1055    -17    187       O  
ATOM   1754  N   ALA A 314      58.220  66.318  52.646  1.00 66.63           N  
ANISOU 1754  N   ALA A 314     7745   7318  10255   -991   -110    114       N  
ATOM   1755  CA  ALA A 314      56.896  65.704  52.639  1.00 67.31           C  
ANISOU 1755  CA  ALA A 314     7802   7379  10393  -1099   -153     74       C  
ATOM   1756  C   ALA A 314      56.952  64.285  53.180  1.00 67.54           C  
ANISOU 1756  C   ALA A 314     7922   7280  10459  -1174   -178     66       C  
ATOM   1757  O   ALA A 314      56.105  63.883  53.986  1.00 71.19           O  
ANISOU 1757  O   ALA A 314     8339   7723  10985  -1296   -173    111       O  
ATOM   1758  CB  ALA A 314      56.312  65.715  51.228  1.00 76.44           C  
ANISOU 1758  CB  ALA A 314     8942   8582  11521  -1077   -234      5       C  
ATOM   1759  N   ARG A 315      57.954  63.515  52.757  1.00 68.69           N  
ANISOU 1759  N   ARG A 315     8191   7350  10559  -1096   -213     21       N  
ATOM   1760  CA  ARG A 315      58.115  62.169  53.289  1.00 64.14           C  
ANISOU 1760  CA  ARG A 315     7727   6620  10023  -1153   -263     13       C  
ATOM   1761  C   ARG A 315      58.518  62.187  54.758  1.00 64.38           C  
ANISOU 1761  C   ARG A 315     7754   6628  10081  -1194   -169    108       C  
ATOM   1762  O   ARG A 315      58.163  61.268  55.505  1.00 70.41           O  
ANISOU 1762  O   ARG A 315     8555   7290  10908  -1304   -196    154       O  
ATOM   1763  CB  ARG A 315      59.126  61.400  52.441  1.00 58.82           C  
ANISOU 1763  CB  ARG A 315     7191   5888   9271  -1011   -340    -82       C  
ATOM   1764  CG  ARG A 315      58.554  60.976  51.093  1.00 65.05           C  
ANISOU 1764  CG  ARG A 315     8011   6667  10037   -974   -476   -197       C  
ATOM   1765  CD  ARG A 315      59.631  60.579  50.100  1.00 76.13           C  
ANISOU 1765  CD  ARG A 315     9515   8106  11305   -760   -533   -301       C  
ATOM   1766  NE  ARG A 315      59.056  60.078  48.854  1.00 85.14           N  
ANISOU 1766  NE  ARG A 315    10701   9234  12415   -699   -686   -433       N  
ATOM   1767  CZ  ARG A 315      58.551  60.846  47.893  1.00 80.81           C  
ANISOU 1767  CZ  ARG A 315    10056   8833  11815   -660   -684   -453       C  
ATOM   1768  NH1 ARG A 315      58.528  62.164  48.027  1.00 77.88           N  
ANISOU 1768  NH1 ARG A 315     9544   8616  11430   -685   -548   -342       N  
ATOM   1769  NH2 ARG A 315      58.056  60.291  46.796  1.00 79.82           N  
ANISOU 1769  NH2 ARG A 315     9985   8689  11655   -589   -838   -588       N  
ATOM   1770  N   ALA A 316      59.234  63.225  55.195  1.00 62.49           N  
ANISOU 1770  N   ALA A 316     7465   6478   9798  -1111    -73    148       N  
ATOM   1771  CA  ALA A 316      59.562  63.348  56.612  1.00 63.38           C  
ANISOU 1771  CA  ALA A 316     7568   6586   9928  -1129      8    224       C  
ATOM   1772  C   ALA A 316      58.330  63.702  57.437  1.00 67.06           C  
ANISOU 1772  C   ALA A 316     7913   7127  10439  -1229     44    284       C  
ATOM   1773  O   ALA A 316      58.155  63.188  58.548  1.00 73.17           O  
ANISOU 1773  O   ALA A 316     8682   7888  11232  -1292     81    356       O  
ATOM   1774  CB  ALA A 316      60.665  64.388  56.812  1.00 53.46           C  
ANISOU 1774  CB  ALA A 316     6294   5393   8624  -1011     66    242       C  
ATOM   1775  N   ILE A 317      57.473  64.589  56.921  1.00 63.77           N  
ANISOU 1775  N   ILE A 317     7389   6816  10024  -1232     33    263       N  
ATOM   1776  CA  ILE A 317      56.198  64.866  57.581  1.00 68.06           C  
ANISOU 1776  CA  ILE A 317     7799   7471  10589  -1307     57    311       C  
ATOM   1777  C   ILE A 317      55.406  63.579  57.766  1.00 71.08           C  
ANISOU 1777  C   ILE A 317     8176   7803  11027  -1469     19    369       C  
ATOM   1778  O   ILE A 317      54.885  63.299  58.853  1.00 71.09           O  
ANISOU 1778  O   ILE A 317     8101   7875  11035  -1543     67    470       O  
ATOM   1779  CB  ILE A 317      55.388  65.909  56.788  1.00 67.84           C  
ANISOU 1779  CB  ILE A 317     7671   7552  10553  -1274     27    262       C  
ATOM   1780  CG1 ILE A 317      56.019  67.295  56.911  1.00 65.11           C  
ANISOU 1780  CG1 ILE A 317     7312   7251  10173  -1135     43    241       C  
ATOM   1781  CG2 ILE A 317      53.921  65.906  57.226  1.00 66.38           C  
ANISOU 1781  CG2 ILE A 317     7338   7502  10381  -1360     34    304       C  
ATOM   1782  CD1 ILE A 317      55.246  68.370  56.191  1.00 60.38           C  
ANISOU 1782  CD1 ILE A 317     6628   6742   9570  -1093     -5    200       C  
ATOM   1783  N   ARG A 318      55.293  62.782  56.701  1.00 71.48           N  
ANISOU 1783  N   ARG A 318     8304   7739  11117  -1525    -85    315       N  
ATOM   1784  CA  ARG A 318      54.559  61.525  56.792  1.00 73.45           C  
ANISOU 1784  CA  ARG A 318     8564   7895  11449  -1698   -172    375       C  
ATOM   1785  C   ARG A 318      55.176  60.601  57.838  1.00 75.39           C  
ANISOU 1785  C   ARG A 318     8897   8031  11717  -1746   -156    465       C  
ATOM   1786  O   ARG A 318      54.459  59.892  58.555  1.00 70.57           O  
ANISOU 1786  O   ARG A 318     8229   7419  11167  -1908   -175    597       O  
ATOM   1787  CB  ARG A 318      54.524  60.853  55.420  1.00 69.76           C  
ANISOU 1787  CB  ARG A 318     8200   7291  11014  -1704   -322    264       C  
ATOM   1788  CG  ARG A 318      53.693  59.584  55.349  1.00 70.94           C  
ANISOU 1788  CG  ARG A 318     8371   7305  11277  -1896   -469    314       C  
ATOM   1789  CD  ARG A 318      53.906  58.906  54.011  1.00 78.94           C  
ANISOU 1789  CD  ARG A 318     9530   8158  12306  -1843   -644    163       C  
ATOM   1790  NE  ARG A 318      55.314  58.573  53.829  1.00 89.63           N  
ANISOU 1790  NE  ARG A 318    11061   9406  13590  -1673   -652     75       N  
ATOM   1791  CZ  ARG A 318      55.839  58.096  52.707  1.00 97.13           C  
ANISOU 1791  CZ  ARG A 318    12149  10260  14495  -1540   -781    -78       C  
ATOM   1792  NH1 ARG A 318      55.074  57.878  51.645  1.00 91.14           N  
ANISOU 1792  NH1 ARG A 318    11388   9475  13764  -1560   -925   -171       N  
ATOM   1793  NH2 ARG A 318      57.137  57.831  52.652  1.00105.85           N  
ANISOU 1793  NH2 ARG A 318    13388  11316  15514  -1369   -771   -143       N  
ATOM   1794  N   ALA A 319      56.507  60.611  57.953  1.00 73.03           N  
ANISOU 1794  N   ALA A 319     8726   7655  11366  -1612   -122    413       N  
ATOM   1795  CA  ALA A 319      57.166  59.786  58.960  1.00 64.52           C  
ANISOU 1795  CA  ALA A 319     7740   6475  10300  -1635   -106    492       C  
ATOM   1796  C   ALA A 319      56.907  60.318  60.366  1.00 72.68           C  
ANISOU 1796  C   ALA A 319     8647   7668  11299  -1650     26    615       C  
ATOM   1797  O   ALA A 319      56.647  59.539  61.292  1.00 88.69           O  
ANISOU 1797  O   ALA A 319    10665   9675  13358  -1762     31    750       O  
ATOM   1798  CB  ALA A 319      58.667  59.715  58.680  1.00 52.39           C  
ANISOU 1798  CB  ALA A 319     6356   4847   8702  -1468   -104    397       C  
ATOM   1799  N   CYS A 320      56.969  61.642  60.542  1.00 63.84           N  
ANISOU 1799  N   CYS A 320     7433   6712  10113  -1529    117    575       N  
ATOM   1800  CA  CYS A 320      56.721  62.232  61.855  1.00 65.82           C  
ANISOU 1800  CA  CYS A 320     7567   7132  10308  -1492    222    658       C  
ATOM   1801  C   CYS A 320      55.297  61.971  62.329  1.00 69.76           C  
ANISOU 1801  C   CYS A 320     7898   7786  10821  -1631    235    784       C  
ATOM   1802  O   CYS A 320      55.072  61.686  63.510  1.00 72.11           O  
ANISOU 1802  O   CYS A 320     8124   8193  11082  -1663    300    916       O  
ATOM   1803  CB  CYS A 320      56.994  63.731  61.811  1.00 71.68           C  
ANISOU 1803  CB  CYS A 320     8257   7988  10991  -1326    264    567       C  
ATOM   1804  SG  CYS A 320      58.731  64.152  61.862  1.00 86.03           S  
ANISOU 1804  SG  CYS A 320    10213   9695  12781  -1172    275    495       S  
ATOM   1805  N   LEU A 321      54.322  62.074  61.425  1.00 70.95           N  
ANISOU 1805  N   LEU A 321     7971   7975  11013  -1711    174    759       N  
ATOM   1806  CA  LEU A 321      52.935  61.845  61.807  1.00 72.19           C  
ANISOU 1806  CA  LEU A 321     7939   8309  11181  -1852    181    893       C  
ATOM   1807  C   LEU A 321      52.692  60.392  62.189  1.00 79.39           C  
ANISOU 1807  C   LEU A 321     8874   9112  12179  -2065    121   1061       C  
ATOM   1808  O   LEU A 321      51.842  60.111  63.040  1.00 88.13           O  
ANISOU 1808  O   LEU A 321     9813  10400  13271  -2178    164   1246       O  
ATOM   1809  CB  LEU A 321      52.005  62.248  60.666  1.00 70.95           C  
ANISOU 1809  CB  LEU A 321     7701   8200  11057  -1890    113    818       C  
ATOM   1810  CG  LEU A 321      51.890  63.739  60.371  1.00 66.11           C  
ANISOU 1810  CG  LEU A 321     7020   7733  10364  -1705    156    692       C  
ATOM   1811  CD1 LEU A 321      51.111  63.947  59.090  1.00 60.77           C  
ANISOU 1811  CD1 LEU A 321     6302   7056   9730  -1751     71    615       C  
ATOM   1812  CD2 LEU A 321      51.224  64.461  61.531  1.00 68.96           C  
ANISOU 1812  CD2 LEU A 321     7198   8381  10624  -1621    252    761       C  
ATOM   1813  N   GLU A 322      53.411  59.462  61.567  1.00 80.40           N  
ANISOU 1813  N   GLU A 322     9203   8956  12391  -2115      8   1010       N  
ATOM   1814  CA  GLU A 322      53.290  58.046  61.882  1.00 82.33           C  
ANISOU 1814  CA  GLU A 322     9512   9033  12738  -2312    -95   1160       C  
ATOM   1815  C   GLU A 322      54.189  57.616  63.032  1.00 82.29           C  
ANISOU 1815  C   GLU A 322     9591   8982  12695  -2271    -29   1252       C  
ATOM   1816  O   GLU A 322      54.150  56.445  63.423  1.00 87.11           O  
ANISOU 1816  O   GLU A 322    10263   9446  13390  -2433   -119   1399       O  
ATOM   1817  CB  GLU A 322      53.610  57.194  60.649  1.00 84.51           C  
ANISOU 1817  CB  GLU A 322     9983   9009  13119  -2356   -289   1036       C  
ATOM   1818  CG  GLU A 322      52.465  57.053  59.664  1.00 86.56           C  
ANISOU 1818  CG  GLU A 322    10159   9264  13463  -2492   -417   1018       C  
ATOM   1819  CD  GLU A 322      52.920  56.488  58.335  1.00 90.16           C  
ANISOU 1819  CD  GLU A 322    10819   9460  13977  -2443   -601    830       C  
ATOM   1820  OE1 GLU A 322      54.142  56.291  58.166  1.00 92.14           O  
ANISOU 1820  OE1 GLU A 322    11258   9568  14182  -2285   -611    712       O  
ATOM   1821  OE2 GLU A 322      52.058  56.224  57.467  1.00 93.24           O  
ANISOU 1821  OE2 GLU A 322    11174   9805  14447  -2549   -743    797       O  
ATOM   1822  N   ASN A 323      54.995  58.522  63.574  1.00 77.57           N  
ANISOU 1822  N   ASN A 323     9002   8491  11981  -2065    106   1173       N  
ATOM   1823  CA  ASN A 323      55.910  58.166  64.644  1.00 75.27           C  
ANISOU 1823  CA  ASN A 323     8795   8161  11643  -2004    167   1240       C  
ATOM   1824  C   ASN A 323      55.166  58.005  65.962  1.00 79.63           C  
ANISOU 1824  C   ASN A 323     9169   8940  12147  -2092    256   1472       C  
ATOM   1825  O   ASN A 323      54.201  58.718  66.248  1.00 83.12           O  
ANISOU 1825  O   ASN A 323     9398   9659  12523  -2086    332   1526       O  
ATOM   1826  CB  ASN A 323      56.999  59.222  64.799  1.00 73.14           C  
ANISOU 1826  CB  ASN A 323     8582   7936  11273  -1760    261   1084       C  
ATOM   1827  CG  ASN A 323      58.104  58.769  65.715  1.00 79.56           C  
ANISOU 1827  CG  ASN A 323     9514   8666  12047  -1686    299   1121       C  
ATOM   1828  OD1 ASN A 323      58.083  59.045  66.914  1.00 80.64           O  
ANISOU 1828  OD1 ASN A 323     9565   8972  12104  -1633    400   1215       O  
ATOM   1829  ND2 ASN A 323      59.075  58.054  65.161  1.00 84.94           N  
ANISOU 1829  ND2 ASN A 323    10394   9106  12774  -1662    213   1040       N  
ATOM   1830  N   GLU A 324      55.640  57.061  66.777  1.00 82.96           N  
ANISOU 1830  N   GLU A 324     9672   9262  12585  -2158    244   1614       N  
ATOM   1831  CA  GLU A 324      54.970  56.730  68.028  1.00 89.44           C  
ANISOU 1831  CA  GLU A 324    10322  10305  13355  -2259    321   1877       C  
ATOM   1832  C   GLU A 324      55.077  57.832  69.077  1.00 80.95           C  
ANISOU 1832  C   GLU A 324     9111   9550  12097  -2040    497   1861       C  
ATOM   1833  O   GLU A 324      54.347  57.782  70.072  1.00 78.24           O  
ANISOU 1833  O   GLU A 324     8572   9490  11667  -2081    581   2068       O  
ATOM   1834  CB  GLU A 324      55.536  55.420  68.587  1.00 95.49           C  
ANISOU 1834  CB  GLU A 324    11236  10855  14191  -2379    244   2036       C  
ATOM   1835  CG  GLU A 324      57.039  55.440  68.819  1.00 98.98           C  
ANISOU 1835  CG  GLU A 324    11894  11129  14586  -2181    267   1884       C  
ATOM   1836  CD  GLU A 324      57.532  54.248  69.622  1.00104.25           C  
ANISOU 1836  CD  GLU A 324    12680  11639  15290  -2272    213   2063       C  
ATOM   1837  OE1 GLU A 324      56.698  53.412  70.034  1.00106.50           O  
ANISOU 1837  OE1 GLU A 324    12875  11945  15645  -2504    154   2329       O  
ATOM   1838  OE2 GLU A 324      58.759  54.150  69.841  1.00103.38           O  
ANISOU 1838  OE2 GLU A 324    12747  11391  15142  -2115    222   1952       O  
ATOM   1839  N   ASN A 325      55.949  58.821  68.879  1.00 73.41           N  
ANISOU 1839  N   ASN A 325     8246   8568  11077  -1806    539   1628       N  
ATOM   1840  CA  ASN A 325      56.174  59.881  69.854  1.00 75.11           C  
ANISOU 1840  CA  ASN A 325     8371   9034  11133  -1574    660   1577       C  
ATOM   1841  C   ASN A 325      55.427  61.164  69.515  1.00 76.27           C  
ANISOU 1841  C   ASN A 325     8367   9397  11214  -1453    687   1456       C  
ATOM   1842  O   ASN A 325      55.664  62.195  70.154  1.00 80.21           O  
ANISOU 1842  O   ASN A 325     8821  10062  11593  -1226    743   1356       O  
ATOM   1843  CB  ASN A 325      57.669  60.182  69.975  1.00 76.43           C  
ANISOU 1843  CB  ASN A 325     8732   9025  11282  -1397    661   1414       C  
ATOM   1844  CG  ASN A 325      58.466  58.993  70.451  1.00 83.78           C  
ANISOU 1844  CG  ASN A 325     9813   9770  12252  -1469    638   1520       C  
ATOM   1845  OD1 ASN A 325      58.406  58.618  71.621  1.00 91.01           O  
ANISOU 1845  OD1 ASN A 325    10669  10822  13088  -1465    704   1682       O  
ATOM   1846  ND2 ASN A 325      59.233  58.396  69.544  1.00 83.39           N  
ANISOU 1846  ND2 ASN A 325     9958   9419  12307  -1516    540   1426       N  
ATOM   1847  N   ALA A 326      54.545  61.130  68.523  1.00 71.13           N  
ANISOU 1847  N   ALA A 326     7648   8734  10643  -1586    627   1450       N  
ATOM   1848  CA  ALA A 326      53.761  62.296  68.142  1.00 76.42           C  
ANISOU 1848  CA  ALA A 326     8177   9603  11255  -1475    639   1340       C  
ATOM   1849  C   ALA A 326      52.409  62.241  68.847  1.00 90.02           C  
ANISOU 1849  C   ALA A 326     9632  11689  12883  -1528    705   1527       C  
ATOM   1850  O   ALA A 326      51.597  61.346  68.575  1.00 92.87           O  
ANISOU 1850  O   ALA A 326     9902  12061  13324  -1770    670   1705       O  
ATOM   1851  CB  ALA A 326      53.582  62.351  66.626  1.00 73.99           C  
ANISOU 1851  CB  ALA A 326     7939   9102  11070  -1567    539   1221       C  
ATOM   1852  N   THR A 327      52.174  63.188  69.757  1.00 90.75           N  
ANISOU 1852  N   THR A 327     9592  12087  12802  -1295    785   1491       N  
ATOM   1853  CA  THR A 327      50.906  63.259  70.468  1.00 88.87           C  
ANISOU 1853  CA  THR A 327     9070  12268  12428  -1289    859   1659       C  
ATOM   1854  C   THR A 327      49.779  63.613  69.501  1.00 95.10           C  
ANISOU 1854  C   THR A 327     9724  13152  13259  -1366    811   1626       C  
ATOM   1855  O   THR A 327      50.010  64.100  68.390  1.00 94.58           O  
ANISOU 1855  O   THR A 327     9784  12860  13292  -1352    729   1434       O  
ATOM   1856  CB  THR A 327      50.969  64.294  71.597  1.00 83.17           C  
ANISOU 1856  CB  THR A 327     8257  11857  11487   -955    931   1573       C  
ATOM   1857  OG1 THR A 327      51.156  65.606  71.052  1.00 74.59           O  
ANISOU 1857  OG1 THR A 327     7243  10710  10389   -733    863   1296       O  
ATOM   1858  CG2 THR A 327      52.129  63.991  72.529  1.00 85.10           C  
ANISOU 1858  CG2 THR A 327     8643  12001  11689   -864    968   1586       C  
ATOM   1859  N   PHE A 328      48.541  63.358  69.932  1.00105.44           N  
ANISOU 1859  N   PHE A 328    10757  14820  14483  -1448    865   1832       N  
ATOM   1860  CA  PHE A 328      47.398  63.657  69.072  1.00114.75           C  
ANISOU 1860  CA  PHE A 328    11782  16125  15694  -1524    821   1817       C  
ATOM   1861  C   PHE A 328      47.320  65.145  68.759  1.00112.72           C  
ANISOU 1861  C   PHE A 328    11531  15957  15339  -1221    801   1540       C  
ATOM   1862  O   PHE A 328      46.919  65.534  67.656  1.00123.26           O  
ANISOU 1862  O   PHE A 328    12884  17191  16758  -1257    724   1418       O  
ATOM   1863  CB  PHE A 328      46.101  63.174  69.719  1.00123.32           C  
ANISOU 1863  CB  PHE A 328    12532  17643  16680  -1649    890   2111       C  
ATOM   1864  CG  PHE A 328      46.036  61.687  69.907  1.00133.73           C  
ANISOU 1864  CG  PHE A 328    13832  18850  18131  -1998    868   2419       C  
ATOM   1865  CD1 PHE A 328      45.931  60.841  68.813  1.00134.12           C  
ANISOU 1865  CD1 PHE A 328    13988  18554  18416  -2300    731   2455       C  
ATOM   1866  CD2 PHE A 328      46.084  61.134  71.175  1.00138.96           C  
ANISOU 1866  CD2 PHE A 328    14376  19743  18680  -2015    963   2674       C  
ATOM   1867  CE1 PHE A 328      45.873  59.470  68.983  1.00135.99           C  
ANISOU 1867  CE1 PHE A 328    14229  18647  18793  -2621    666   2734       C  
ATOM   1868  CE2 PHE A 328      46.026  59.765  71.351  1.00139.88           C  
ANISOU 1868  CE2 PHE A 328    14484  19731  18933  -2350    917   2979       C  
ATOM   1869  CZ  PHE A 328      45.920  58.932  70.254  1.00138.11           C  
ANISOU 1869  CZ  PHE A 328    14382  19131  18965  -2658    756   3006       C  
ATOM   1870  N   GLU A 329      47.711  65.992  69.712  1.00103.56           N  
ANISOU 1870  N   GLU A 329    10369  14971  14007   -913    849   1433       N  
ATOM   1871  CA  GLU A 329      47.725  67.428  69.460  1.00 99.60           C  
ANISOU 1871  CA  GLU A 329     9908  14503  13431   -614    788   1162       C  
ATOM   1872  C   GLU A 329      48.752  67.783  68.390  1.00 98.27           C  
ANISOU 1872  C   GLU A 329    10021  13876  13440   -639    681    962       C  
ATOM   1873  O   GLU A 329      48.490  68.619  67.518  1.00100.45           O  
ANISOU 1873  O   GLU A 329    10325  14087  13753   -565    598    802       O  
ATOM   1874  CB  GLU A 329      48.008  68.187  70.759  1.00103.85           C  
ANISOU 1874  CB  GLU A 329    10409  15291  13757   -271    825   1082       C  
ATOM   1875  CG  GLU A 329      46.898  68.114  71.814  1.00111.57           C  
ANISOU 1875  CG  GLU A 329    11070  16824  14496   -154    930   1251       C  
ATOM   1876  CD  GLU A 329      46.852  66.785  72.558  1.00117.00           C  
ANISOU 1876  CD  GLU A 329    11648  17637  15170   -384   1046   1574       C  
ATOM   1877  OE1 GLU A 329      47.930  66.248  72.894  1.00117.98           O  
ANISOU 1877  OE1 GLU A 329    11960  17501  15367   -448   1056   1602       O  
ATOM   1878  OE2 GLU A 329      45.737  66.284  72.818  1.00119.71           O  
ANISOU 1878  OE2 GLU A 329    11708  18349  15428   -502   1119   1815       O  
ATOM   1879  N   GLN A 330      49.927  67.149  68.438  1.00 90.64           N  
ANISOU 1879  N   GLN A 330     9254  12610  12575   -738    682    983       N  
ATOM   1880  CA  GLN A 330      50.943  67.388  67.418  1.00 81.71           C  
ANISOU 1880  CA  GLN A 330     8363  11087  11595   -770    593    828       C  
ATOM   1881  C   GLN A 330      50.483  66.889  66.053  1.00 81.99           C  
ANISOU 1881  C   GLN A 330     8413  10965  11773   -998    538    846       C  
ATOM   1882  O   GLN A 330      50.699  67.558  65.036  1.00 89.22           O  
ANISOU 1882  O   GLN A 330     9423  11720  12756   -956    458    696       O  
ATOM   1883  CB  GLN A 330      52.263  66.725  67.826  1.00 77.51           C  
ANISOU 1883  CB  GLN A 330     8015  10317  11117   -815    613    859       C  
ATOM   1884  CG  GLN A 330      52.966  67.371  69.021  1.00 73.76           C  
ANISOU 1884  CG  GLN A 330     7575   9929  10521   -564    634    790       C  
ATOM   1885  CD  GLN A 330      54.084  66.508  69.587  1.00 73.07           C  
ANISOU 1885  CD  GLN A 330     7626   9671  10466   -629    674    867       C  
ATOM   1886  OE1 GLN A 330      54.139  65.300  69.341  1.00 70.64           O  
ANISOU 1886  OE1 GLN A 330     7353   9243  10243   -857    700   1011       O  
ATOM   1887  NE2 GLN A 330      54.994  67.130  70.334  1.00 71.73           N  
ANISOU 1887  NE2 GLN A 330     7545   9474  10236   -421    658    762       N  
ATOM   1888  N   GLN A 331      49.851  65.714  66.010  1.00 79.11           N  
ANISOU 1888  N   GLN A 331     7956  10643  11459  -1240    564   1036       N  
ATOM   1889  CA  GLN A 331      49.285  65.215  64.760  1.00 83.16           C  
ANISOU 1889  CA  GLN A 331     8469  11026  12103  -1448    488   1047       C  
ATOM   1890  C   GLN A 331      48.213  66.155  64.227  1.00 92.79           C  
ANISOU 1890  C   GLN A 331     9534  12451  13270  -1358    461    961       C  
ATOM   1891  O   GLN A 331      48.230  66.532  63.050  1.00 98.10           O  
ANISOU 1891  O   GLN A 331    10290  12963  14020  -1365    380    830       O  
ATOM   1892  CB  GLN A 331      48.714  63.810  64.967  1.00 78.50           C  
ANISOU 1892  CB  GLN A 331     7790  10454  11583  -1728    489   1286       C  
ATOM   1893  CG  GLN A 331      49.763  62.718  65.095  1.00 75.85           C  
ANISOU 1893  CG  GLN A 331     7655   9818  11347  -1854    462   1350       C  
ATOM   1894  CD  GLN A 331      49.185  61.417  65.622  1.00 81.14           C  
ANISOU 1894  CD  GLN A 331     8223  10534  12073  -2113    453   1624       C  
ATOM   1895  OE1 GLN A 331      48.527  60.671  64.894  1.00 76.93           O  
ANISOU 1895  OE1 GLN A 331     7658   9904  11667  -2342    349   1706       O  
ATOM   1896  NE2 GLN A 331      49.455  61.125  66.889  1.00 89.63           N  
ANISOU 1896  NE2 GLN A 331     9250  11746  13060  -2082    543   1776       N  
ATOM   1897  N   ALA A 332      47.270  66.549  65.088  1.00 93.29           N  
ANISOU 1897  N   ALA A 332     9366  12895  13185  -1253    527   1035       N  
ATOM   1898  CA  ALA A 332      46.176  67.411  64.651  1.00 96.96           C  
ANISOU 1898  CA  ALA A 332     9666  13592  13582  -1148    498    956       C  
ATOM   1899  C   ALA A 332      46.688  68.760  64.160  1.00 90.34           C  
ANISOU 1899  C   ALA A 332     8970  12627  12728   -901    424    705       C  
ATOM   1900  O   ALA A 332      46.175  69.303  63.175  1.00 86.16           O  
ANISOU 1900  O   ALA A 332     8428  12074  12235   -887    351    604       O  
ATOM   1901  CB  ALA A 332      45.176  67.603  65.789  1.00105.44           C  
ANISOU 1901  CB  ALA A 332    10458  15142  14463  -1031    588   1079       C  
ATOM   1902  N   LEU A 333      47.693  69.318  64.841  1.00 87.10           N  
ANISOU 1902  N   LEU A 333     8694  12132  12270   -710    426    612       N  
ATOM   1903  CA  LEU A 333      48.260  70.596  64.423  1.00 80.86           C  
ANISOU 1903  CA  LEU A 333     8045  11188  11489   -499    324    401       C  
ATOM   1904  C   LEU A 333      48.809  70.515  63.004  1.00 79.80           C  
ANISOU 1904  C   LEU A 333     8078  10724  11520   -644    249    344       C  
ATOM   1905  O   LEU A 333      48.527  71.380  62.165  1.00 76.53           O  
ANISOU 1905  O   LEU A 333     7680  10270  11126   -567    160    230       O  
ATOM   1906  CB  LEU A 333      49.359  71.023  65.394  1.00 81.86           C  
ANISOU 1906  CB  LEU A 333     8297  11238  11569   -318    320    337       C  
ATOM   1907  CG  LEU A 333      50.244  72.186  64.940  1.00 79.28           C  
ANISOU 1907  CG  LEU A 333     8153  10663  11304   -163    186    158       C  
ATOM   1908  CD1 LEU A 333      49.411  73.442  64.710  1.00 84.94           C  
ANISOU 1908  CD1 LEU A 333     8800  11519  11955     49     77     18       C  
ATOM   1909  CD2 LEU A 333      51.363  72.450  65.936  1.00 71.66           C  
ANISOU 1909  CD2 LEU A 333     7306   9610  10311    -20    171    115       C  
ATOM   1910  N   VAL A 334      49.594  69.473  62.718  1.00 80.45           N  
ANISOU 1910  N   VAL A 334     8282  10581  11705   -837    276    422       N  
ATOM   1911  CA  VAL A 334      50.225  69.352  61.408  1.00 84.01           C  
ANISOU 1911  CA  VAL A 334     8889  10751  12279   -938    208    365       C  
ATOM   1912  C   VAL A 334      49.213  68.932  60.346  1.00 92.02           C  
ANISOU 1912  C   VAL A 334     9819  11798  13345  -1089    173    385       C  
ATOM   1913  O   VAL A 334      49.241  69.436  59.217  1.00 94.62           O  
ANISOU 1913  O   VAL A 334    10208  12023  13719  -1072     98    294       O  
ATOM   1914  CB  VAL A 334      51.416  68.381  61.485  1.00 80.48           C  
ANISOU 1914  CB  VAL A 334     8601  10076  11900  -1049    236    420       C  
ATOM   1915  CG1 VAL A 334      52.080  68.255  60.135  1.00 80.00           C  
ANISOU 1915  CG1 VAL A 334     8684   9779  11932  -1114    168    358       C  
ATOM   1916  CG2 VAL A 334      52.418  68.875  62.505  1.00 85.33           C  
ANISOU 1916  CG2 VAL A 334     9293  10663  12465   -891    260    391       C  
ATOM   1917  N   VAL A 335      48.300  68.016  60.685  1.00 90.56           N  
ANISOU 1917  N   VAL A 335     9488  11766  13156  -1244    215    519       N  
ATOM   1918  CA  VAL A 335      47.317  67.562  59.702  1.00 84.68           C  
ANISOU 1918  CA  VAL A 335     8657  11045  12474  -1404    159    543       C  
ATOM   1919  C   VAL A 335      46.366  68.693  59.325  1.00 85.95           C  
ANISOU 1919  C   VAL A 335     8687  11405  12565  -1262    126    449       C  
ATOM   1920  O   VAL A 335      46.016  68.861  58.149  1.00 84.90           O  
ANISOU 1920  O   VAL A 335     8572  11200  12485  -1301     50    377       O  
ATOM   1921  CB  VAL A 335      46.559  66.328  60.225  1.00 80.30           C  
ANISOU 1921  CB  VAL A 335     7958  10605  11947  -1627    189    740       C  
ATOM   1922  CG1 VAL A 335      45.386  66.004  59.319  1.00 77.90           C  
ANISOU 1922  CG1 VAL A 335     7526  10369  11704  -1782    114    767       C  
ATOM   1923  CG2 VAL A 335      47.493  65.136  60.294  1.00 81.52           C  
ANISOU 1923  CG2 VAL A 335     8282  10491  12201  -1782    173    812       C  
ATOM   1924  N   ALA A 336      45.937  69.490  60.309  1.00 88.93           N  
ANISOU 1924  N   ALA A 336     8936  12044  12812  -1073    172    438       N  
ATOM   1925  CA  ALA A 336      45.115  70.657  60.004  1.00 92.11           C  
ANISOU 1925  CA  ALA A 336     9236  12625  13135   -890    120    323       C  
ATOM   1926  C   ALA A 336      45.881  71.662  59.156  1.00 94.67           C  
ANISOU 1926  C   ALA A 336     9752  12709  13510   -761     21    162       C  
ATOM   1927  O   ALA A 336      45.297  72.336  58.298  1.00 96.89           O  
ANISOU 1927  O   ALA A 336    10006  13014  13793   -703    -56     78       O  
ATOM   1928  CB  ALA A 336      44.625  71.313  61.293  1.00 91.52           C  
ANISOU 1928  CB  ALA A 336     9007  12878  12889   -662    169    320       C  
ATOM   1929  N   SER A 337      47.190  71.781  59.384  1.00 94.31           N  
ANISOU 1929  N   SER A 337     9890  12438  13504   -720     17    136       N  
ATOM   1930  CA  SER A 337      47.999  72.643  58.533  1.00 96.27           C  
ANISOU 1930  CA  SER A 337    10305  12458  13815   -641    -81     33       C  
ATOM   1931  C   SER A 337      48.088  72.086  57.116  1.00 91.41           C  
ANISOU 1931  C   SER A 337     9754  11683  13292   -810   -111     45       C  
ATOM   1932  O   SER A 337      48.132  72.853  56.146  1.00 92.48           O  
ANISOU 1932  O   SER A 337     9943  11743  13453   -753   -197    -23       O  
ATOM   1933  CB  SER A 337      49.388  72.822  59.145  1.00100.53           C  
ANISOU 1933  CB  SER A 337    10999  12820  14377   -578    -79     28       C  
ATOM   1934  OG  SER A 337      50.161  73.755  58.412  1.00107.05           O  
ANISOU 1934  OG  SER A 337    11958  13454  15263   -506   -186    -37       O  
ATOM   1935  N   ILE A 338      48.092  70.759  56.975  1.00 85.13           N  
ANISOU 1935  N   ILE A 338     8959  10840  12546  -1008    -59    130       N  
ATOM   1936  CA  ILE A 338      48.067  70.148  55.648  1.00 86.55           C  
ANISOU 1936  CA  ILE A 338     9197  10890  12799  -1142   -110    118       C  
ATOM   1937  C   ILE A 338      46.763  70.483  54.932  1.00 89.91           C  
ANISOU 1937  C   ILE A 338     9486  11466  13209  -1148   -164     80       C  
ATOM   1938  O   ILE A 338      46.750  70.738  53.720  1.00 89.19           O  
ANISOU 1938  O   ILE A 338     9449  11296  13145  -1143   -236     17       O  
ATOM   1939  CB  ILE A 338      48.291  68.625  55.756  1.00 81.89           C  
ANISOU 1939  CB  ILE A 338     8646  10199  12270  -1337    -83    205       C  
ATOM   1940  CG1 ILE A 338      49.730  68.322  56.183  1.00 74.40           C  
ANISOU 1940  CG1 ILE A 338     7861   9072  11335  -1313    -46    220       C  
ATOM   1941  CG2 ILE A 338      47.973  67.925  54.440  1.00 82.02           C  
ANISOU 1941  CG2 ILE A 338     8699  10115  12352  -1459   -168    173       C  
ATOM   1942  CD1 ILE A 338      50.033  66.842  56.301  1.00 68.76           C  
ANISOU 1942  CD1 ILE A 338     7215   8229  10682  -1479    -44    293       C  
ATOM   1943  N   ILE A 339      45.649  70.506  55.667  1.00 88.44           N  
ANISOU 1943  N   ILE A 339     9111  11527  12967  -1144   -129    123       N  
ATOM   1944  CA  ILE A 339      44.354  70.746  55.036  1.00 87.73           C  
ANISOU 1944  CA  ILE A 339     8867  11608  12857  -1156   -179     96       C  
ATOM   1945  C   ILE A 339      44.260  72.177  54.519  1.00 93.61           C  
ANISOU 1945  C   ILE A 339     9640  12373  13554   -945   -250    -30       C  
ATOM   1946  O   ILE A 339      43.865  72.411  53.366  1.00 97.52           O  
ANISOU 1946  O   ILE A 339    10142  12837  14073   -956   -324    -87       O  
ATOM   1947  CB  ILE A 339      43.214  70.409  56.015  1.00 86.01           C  
ANISOU 1947  CB  ILE A 339     8409  11699  12573  -1198   -117    199       C  
ATOM   1948  CG1 ILE A 339      42.958  68.900  56.029  1.00 89.91           C  
ANISOU 1948  CG1 ILE A 339     8852  12153  13157  -1478   -106    345       C  
ATOM   1949  CG2 ILE A 339      41.945  71.155  55.655  1.00 82.93           C  
ANISOU 1949  CG2 ILE A 339     7841  11556  12112  -1101   -160    143       C  
ATOM   1950  CD1 ILE A 339      42.066  68.437  57.153  1.00 93.44           C  
ANISOU 1950  CD1 ILE A 339     9058  12902  13542  -1554    -31    512       C  
ATOM   1951  N   ILE A 340      44.634  73.158  55.350  1.00 89.59           N  
ANISOU 1951  N   ILE A 340     9158  11903  12980   -745   -249    -75       N  
ATOM   1952  CA  ILE A 340      44.599  74.554  54.917  1.00 85.89           C  
ANISOU 1952  CA  ILE A 340     8738  11411  12484   -543   -355   -188       C  
ATOM   1953  C   ILE A 340      45.696  74.905  53.924  1.00 79.67           C  
ANISOU 1953  C   ILE A 340     8145  10347  11779   -560   -423   -206       C  
ATOM   1954  O   ILE A 340      45.744  76.046  53.444  1.00 78.94           O  
ANISOU 1954  O   ILE A 340     8106  10200  11686   -423   -532   -268       O  
ATOM   1955  CB  ILE A 340      44.678  75.510  56.124  1.00 86.21           C  
ANISOU 1955  CB  ILE A 340     8766  11554  12437   -307   -378   -246       C  
ATOM   1956  CG1 ILE A 340      46.088  75.528  56.708  1.00 82.05           C  
ANISOU 1956  CG1 ILE A 340     8405  10815  11956   -294   -367   -226       C  
ATOM   1957  CG2 ILE A 340      43.684  75.122  57.218  1.00 89.81           C  
ANISOU 1957  CG2 ILE A 340     9008  12342  12775   -266   -290   -206       C  
ATOM   1958  CD1 ILE A 340      46.344  76.722  57.547  1.00 83.77           C  
ANISOU 1958  CD1 ILE A 340     8669  11040  12119    -40   -461   -320       C  
ATOM   1959  N   ASN A 341      46.584  73.969  53.602  1.00 78.49           N  
ANISOU 1959  N   ASN A 341     8096  10033  11693   -714   -373   -143       N  
ATOM   1960  CA  ASN A 341      47.565  74.153  52.541  1.00 81.53           C  
ANISOU 1960  CA  ASN A 341     8628  10219  12130   -735   -423   -138       C  
ATOM   1961  C   ASN A 341      47.312  73.214  51.375  1.00 91.88           C  
ANISOU 1961  C   ASN A 341     9940  11503  13466   -874   -423   -132       C  
ATOM   1962  O   ASN A 341      48.179  73.072  50.506  1.00 97.14           O  
ANISOU 1962  O   ASN A 341    10717  12039  14152   -894   -444   -118       O  
ATOM   1963  CB  ASN A 341      48.981  73.938  53.075  1.00 75.70           C  
ANISOU 1963  CB  ASN A 341     8017   9323  11424   -748   -382    -86       C  
ATOM   1964  CG  ASN A 341      49.434  75.053  53.992  1.00 73.72           C  
ANISOU 1964  CG  ASN A 341     7802   9045  11164   -592   -432   -106       C  
ATOM   1965  OD1 ASN A 341      49.934  76.091  53.549  1.00 79.03           O  
ANISOU 1965  OD1 ASN A 341     8546   9615  11866   -510   -536   -111       O  
ATOM   1966  ND2 ASN A 341      49.243  74.851  55.282  1.00 66.19           N  
ANISOU 1966  ND2 ASN A 341     6795   8186  10169   -548   -374   -112       N  
ATOM   1967  N   SER A 342      46.137  72.578  51.336  1.00 90.86           N  
ANISOU 1967  N   SER A 342     9681  11510  13331   -960   -414   -140       N  
ATOM   1968  CA  SER A 342      45.869  71.536  50.352  1.00 89.45           C  
ANISOU 1968  CA  SER A 342     9511  11285  13190  -1101   -443   -146       C  
ATOM   1969  C   SER A 342      45.877  72.080  48.934  1.00 90.45           C  
ANISOU 1969  C   SER A 342     9688  11378  13301  -1036   -525   -205       C  
ATOM   1970  O   SER A 342      46.280  71.376  48.000  1.00 92.60           O  
ANISOU 1970  O   SER A 342    10041  11556  13586  -1090   -558   -222       O  
ATOM   1971  CB  SER A 342      44.525  70.873  50.655  1.00 87.11           C  
ANISOU 1971  CB  SER A 342     9042  11152  12905  -1219   -441   -123       C  
ATOM   1972  OG  SER A 342      43.497  71.841  50.779  1.00 81.65           O  
ANISOU 1972  OG  SER A 342     8207  10662  12154  -1108   -461   -160       O  
ATOM   1973  N   HIS A 343      45.431  73.323  48.748  1.00 86.53           N  
ANISOU 1973  N   HIS A 343     9146  10964  12768   -903   -573   -238       N  
ATOM   1974  CA  HIS A 343      45.428  73.907  47.416  1.00 85.30           C  
ANISOU 1974  CA  HIS A 343     9031  10787  12591   -838   -654   -271       C  
ATOM   1975  C   HIS A 343      46.837  74.135  46.892  1.00 87.32           C  
ANISOU 1975  C   HIS A 343     9432  10900  12845   -802   -656   -218       C  
ATOM   1976  O   HIS A 343      47.030  74.200  45.672  1.00 82.40           O  
ANISOU 1976  O   HIS A 343     8847  10269  12191   -777   -704   -220       O  
ATOM   1977  CB  HIS A 343      44.640  75.214  47.424  1.00 81.01           C  
ANISOU 1977  CB  HIS A 343     8416  10349  12014   -698   -722   -311       C  
ATOM   1978  CG  HIS A 343      45.279  76.300  48.228  1.00 77.43           C  
ANISOU 1978  CG  HIS A 343     8023   9832  11564   -573   -744   -288       C  
ATOM   1979  ND1 HIS A 343      45.128  76.401  49.594  1.00 77.70           N  
ANISOU 1979  ND1 HIS A 343     8008   9926  11587   -527   -703   -299       N  
ATOM   1980  CD2 HIS A 343      46.067  77.337  47.858  1.00 77.27           C  
ANISOU 1980  CD2 HIS A 343     8106   9694  11561   -484   -824   -249       C  
ATOM   1981  CE1 HIS A 343      45.798  77.453  50.031  1.00 79.84           C  
ANISOU 1981  CE1 HIS A 343     8365  10100  11871   -401   -770   -295       C  
ATOM   1982  NE2 HIS A 343      46.376  78.038  48.997  1.00 77.33           N  
ANISOU 1982  NE2 HIS A 343     8139   9661  11584   -389   -850   -254       N  
ATOM   1983  N   LEU A 344      47.823  74.241  47.785  1.00 88.19           N  
ANISOU 1983  N   LEU A 344     9609  10922  12978   -793   -607   -162       N  
ATOM   1984  CA  LEU A 344      49.224  74.372  47.406  1.00 78.43           C  
ANISOU 1984  CA  LEU A 344     8484   9575  11740   -775   -601    -88       C  
ATOM   1985  C   LEU A 344      49.929  73.025  47.331  1.00 70.57           C  
ANISOU 1985  C   LEU A 344     7553   8521  10741   -859   -536    -83       C  
ATOM   1986  O   LEU A 344      50.761  72.807  46.441  1.00 62.68           O  
ANISOU 1986  O   LEU A 344     6617   7498   9699   -835   -543    -52       O  
ATOM   1987  CB  LEU A 344      49.951  75.277  48.398  1.00 72.34           C  
ANISOU 1987  CB  LEU A 344     7752   8730  11004   -714   -608    -33       C  
ATOM   1988  CG  LEU A 344      49.436  76.713  48.394  1.00 71.12           C  
ANISOU 1988  CG  LEU A 344     7571   8590  10860   -601   -720    -44       C  
ATOM   1989  CD1 LEU A 344      49.789  77.439  49.695  1.00 64.27           C  
ANISOU 1989  CD1 LEU A 344     6731   7658  10030   -525   -753    -44       C  
ATOM   1990  CD2 LEU A 344      49.970  77.446  47.173  1.00 66.87           C  
ANISOU 1990  CD2 LEU A 344     7077   8012  10318   -574   -802     42       C  
ATOM   1991  N   LEU A 345      49.612  72.117  48.255  1.00 70.80           N  
ANISOU 1991  N   LEU A 345     7561   8538  10801   -945   -482   -105       N  
ATOM   1992  CA  LEU A 345      50.214  70.791  48.216  1.00 76.09           C  
ANISOU 1992  CA  LEU A 345     8307   9126  11478  -1022   -452   -108       C  
ATOM   1993  C   LEU A 345      49.765  70.008  46.987  1.00 80.36           C  
ANISOU 1993  C   LEU A 345     8861   9676  11997  -1048   -522   -179       C  
ATOM   1994  O   LEU A 345      50.549  69.236  46.424  1.00 78.53           O  
ANISOU 1994  O   LEU A 345     8726   9379  11734  -1031   -538   -200       O  
ATOM   1995  CB  LEU A 345      49.878  70.033  49.500  1.00 73.67           C  
ANISOU 1995  CB  LEU A 345     7968   8804  11220  -1122   -397    -90       C  
ATOM   1996  CG  LEU A 345      50.440  70.675  50.775  1.00 69.77           C  
ANISOU 1996  CG  LEU A 345     7477   8303  10730  -1071   -331    -36       C  
ATOM   1997  CD1 LEU A 345      49.978  69.940  52.025  1.00 69.46           C  
ANISOU 1997  CD1 LEU A 345     7379   8298  10715  -1158   -272     -3       C  
ATOM   1998  CD2 LEU A 345      51.954  70.727  50.722  1.00 65.76           C  
ANISOU 1998  CD2 LEU A 345     7088   7686  10211  -1022   -308      5       C  
ATOM   1999  N   ALA A 346      48.526  70.216  46.538  1.00 85.07           N  
ANISOU 1999  N   ALA A 346     9362  10361  12600  -1068   -579   -228       N  
ATOM   2000  CA  ALA A 346      47.985  69.443  45.428  1.00 78.25           C  
ANISOU 2000  CA  ALA A 346     8507   9501  11725  -1096   -670   -311       C  
ATOM   2001  C   ALA A 346      48.650  69.755  44.093  1.00 83.28           C  
ANISOU 2001  C   ALA A 346     9212  10161  12269   -965   -711   -336       C  
ATOM   2002  O   ALA A 346      48.341  69.083  43.104  1.00 87.20           O  
ANISOU 2002  O   ALA A 346     9735  10663  12735   -949   -799   -423       O  
ATOM   2003  CB  ALA A 346      46.478  69.676  45.315  1.00 62.37           C  
ANISOU 2003  CB  ALA A 346     6356   7600   9741  -1147   -721   -348       C  
ATOM   2004  N   THR A 347      49.553  70.732  44.033  1.00 81.06           N  
ANISOU 2004  N   THR A 347     8956   9905  11941   -869   -663   -253       N  
ATOM   2005  CA  THR A 347      50.142  71.135  42.763  1.00 83.54           C  
ANISOU 2005  CA  THR A 347     9299  10293  12151   -747   -695   -231       C  
ATOM   2006  C   THR A 347      51.439  70.402  42.430  1.00 92.28           C  
ANISOU 2006  C   THR A 347    10500  11380  13183   -685   -670   -217       C  
ATOM   2007  O   THR A 347      52.019  70.660  41.370  1.00103.90           O  
ANISOU 2007  O   THR A 347    11978  12958  14540   -567   -686   -183       O  
ATOM   2008  CB  THR A 347      50.393  72.644  42.749  1.00 75.98           C  
ANISOU 2008  CB  THR A 347     8300   9383  11186   -689   -685   -114       C  
ATOM   2009  OG1 THR A 347      51.430  72.966  43.682  1.00 81.59           O  
ANISOU 2009  OG1 THR A 347     9047  10020  11934   -703   -623    -15       O  
ATOM   2010  CG2 THR A 347      49.128  73.383  43.135  1.00 70.95           C  
ANISOU 2010  CG2 THR A 347     7578   8771  10607   -712   -723   -149       C  
ATOM   2011  N   ASN A 348      51.912  69.504  43.291  1.00 88.62           N  
ANISOU 2011  N   ASN A 348    10100  10805  12766   -746   -633   -235       N  
ATOM   2012  CA  ASN A 348      53.064  68.682  42.946  1.00 88.93           C  
ANISOU 2012  CA  ASN A 348    10234  10834  12723   -663   -627   -251       C  
ATOM   2013  C   ASN A 348      52.910  67.320  43.609  1.00 80.90           C  
ANISOU 2013  C   ASN A 348     9296   9664  11777   -749   -660   -342       C  
ATOM   2014  O   ASN A 348      52.067  67.126  44.489  1.00 80.34           O  
ANISOU 2014  O   ASN A 348     9188   9514  11822   -892   -659   -344       O  
ATOM   2015  CB  ASN A 348      54.390  69.357  43.336  1.00 97.54           C  
ANISOU 2015  CB  ASN A 348    11326  11958  13778   -614   -537   -107       C  
ATOM   2016  CG  ASN A 348      54.773  69.120  44.780  1.00104.76           C  
ANISOU 2016  CG  ASN A 348    12274  12743  14789   -707   -471    -73       C  
ATOM   2017  OD1 ASN A 348      55.420  68.129  45.105  1.00109.82           O  
ANISOU 2017  OD1 ASN A 348    12996  13315  15417   -698   -458   -110       O  
ATOM   2018  ND2 ASN A 348      54.394  70.046  45.653  1.00105.79           N  
ANISOU 2018  ND2 ASN A 348    12345  12845  15005   -775   -439     -8       N  
ATOM   2019  N   SER A 349      53.730  66.367  43.160  1.00 77.29           N  
ANISOU 2019  N   SER A 349     8943   9181  11242   -651   -702   -408       N  
ATOM   2020  CA  SER A 349      53.530  64.979  43.568  1.00 81.06           C  
ANISOU 2020  CA  SER A 349     9520   9486  11791   -721   -788   -508       C  
ATOM   2021  C   SER A 349      53.868  64.762  45.037  1.00 78.28           C  
ANISOU 2021  C   SER A 349     9187   9015  11540   -844   -703   -425       C  
ATOM   2022  O   SER A 349      53.303  63.864  45.673  1.00 82.05           O  
ANISOU 2022  O   SER A 349     9700   9349  12126   -979   -763   -451       O  
ATOM   2023  CB  SER A 349      54.361  64.047  42.685  1.00 86.94           C  
ANISOU 2023  CB  SER A 349    10389  10233  12410   -541   -880   -624       C  
ATOM   2024  OG  SER A 349      55.705  64.488  42.594  1.00 88.66           O  
ANISOU 2024  OG  SER A 349    10608  10578  12501   -397   -776   -542       O  
ATOM   2025  N   ASN A 350      54.772  65.570  45.593  1.00 71.69           N  
ANISOU 2025  N   ASN A 350     8326   8239  10675   -806   -578   -312       N  
ATOM   2026  CA  ASN A 350      55.168  65.391  46.986  1.00 75.74           C  
ANISOU 2026  CA  ASN A 350     8860   8653  11266   -895   -500   -240       C  
ATOM   2027  C   ASN A 350      54.061  65.839  47.934  1.00 79.62           C  
ANISOU 2027  C   ASN A 350     9251   9134  11868  -1045   -465   -189       C  
ATOM   2028  O   ASN A 350      53.721  65.130  48.889  1.00 76.85           O  
ANISOU 2028  O   ASN A 350     8912   8690  11598  -1163   -462   -170       O  
ATOM   2029  CB  ASN A 350      56.461  66.155  47.262  1.00 72.32           C  
ANISOU 2029  CB  ASN A 350     8421   8288  10770   -805   -399   -140       C  
ATOM   2030  CG  ASN A 350      57.602  65.695  46.380  1.00 71.47           C  
ANISOU 2030  CG  ASN A 350     8382   8247  10526   -641   -419   -171       C  
ATOM   2031  OD1 ASN A 350      57.840  64.497  46.223  1.00 75.68           O  
ANISOU 2031  OD1 ASN A 350     9024   8699  11032   -594   -489   -272       O  
ATOM   2032  ND2 ASN A 350      58.306  66.649  45.784  1.00 66.23           N  
ANISOU 2032  ND2 ASN A 350     7650   7743   9771   -545   -374    -77       N  
ATOM   2033  N   GLY A 351      53.494  67.023  47.691  1.00 81.30           N  
ANISOU 2033  N   GLY A 351     9359   9459  12074  -1029   -444   -157       N  
ATOM   2034  CA  GLY A 351      52.368  67.468  48.492  1.00 78.74           C  
ANISOU 2034  CA  GLY A 351     8925   9169  11823  -1128   -422   -129       C  
ATOM   2035  C   GLY A 351      51.139  66.604  48.283  1.00 84.84           C  
ANISOU 2035  C   GLY A 351     9657   9923  12653  -1246   -505   -183       C  
ATOM   2036  O   GLY A 351      50.359  66.382  49.211  1.00 94.42           O  
ANISOU 2036  O   GLY A 351    10791  11151  13934  -1365   -484   -137       O  
ATOM   2037  N   MET A 352      50.948  66.101  47.060  1.00 79.14           N  
ANISOU 2037  N   MET A 352     8980   9186  11903  -1213   -610   -275       N  
ATOM   2038  CA  MET A 352      49.821  65.213  46.803  1.00 85.06           C  
ANISOU 2038  CA  MET A 352     9701   9893  12727  -1338   -726   -329       C  
ATOM   2039  C   MET A 352      49.975  63.909  47.572  1.00 86.98           C  
ANISOU 2039  C   MET A 352    10018   9973  13056  -1466   -769   -304       C  
ATOM   2040  O   MET A 352      48.976  63.288  47.951  1.00 84.42           O  
ANISOU 2040  O   MET A 352     9626   9618  12832  -1637   -836   -269       O  
ATOM   2041  CB  MET A 352      49.697  64.948  45.300  1.00 90.37           C  
ANISOU 2041  CB  MET A 352    10425  10571  13339  -1244   -854   -453       C  
ATOM   2042  CG  MET A 352      48.433  64.190  44.914  1.00 96.79           C  
ANISOU 2042  CG  MET A 352    11195  11341  14239  -1372  -1005   -517       C  
ATOM   2043  SD  MET A 352      46.914  65.097  45.277  1.00 98.33           S  
ANISOU 2043  SD  MET A 352    11169  11709  14484  -1482   -963   -451       S  
ATOM   2044  CE  MET A 352      46.917  66.297  43.948  1.00 93.42           C  
ANISOU 2044  CE  MET A 352    10527  11235  13735  -1285   -964   -524       C  
ATOM   2045  N   LEU A 353      51.219  63.486  47.815  1.00 87.19           N  
ANISOU 2045  N   LEU A 353    10178   9904  13047  -1391   -740   -305       N  
ATOM   2046  CA  LEU A 353      51.462  62.314  48.649  1.00 88.68           C  
ANISOU 2046  CA  LEU A 353    10450   9926  13317  -1502   -779   -267       C  
ATOM   2047  C   LEU A 353      50.924  62.522  50.059  1.00 87.77           C  
ANISOU 2047  C   LEU A 353    10215   9863  13272  -1650   -674   -122       C  
ATOM   2048  O   LEU A 353      50.380  61.593  50.668  1.00 94.72           O  
ANISOU 2048  O   LEU A 353    11082  10655  14252  -1822   -737    -51       O  
ATOM   2049  CB  LEU A 353      52.958  62.003  48.682  1.00 91.15           C  
ANISOU 2049  CB  LEU A 353    10915  10164  13555  -1360   -748   -297       C  
ATOM   2050  CG  LEU A 353      53.497  61.146  49.829  1.00106.53           C  
ANISOU 2050  CG  LEU A 353    12945  11968  15564  -1439   -732   -227       C  
ATOM   2051  CD1 LEU A 353      52.852  59.762  49.847  1.00118.91           C  
ANISOU 2051  CD1 LEU A 353    14585  13342  17252  -1591   -915   -244       C  
ATOM   2052  CD2 LEU A 353      55.006  61.034  49.722  1.00111.52           C  
ANISOU 2052  CD2 LEU A 353    13705  12571  16094  -1260   -692   -269       C  
ATOM   2053  N   LEU A 354      51.067  63.736  50.596  1.00 80.80           N  
ANISOU 2053  N   LEU A 354     9240   9127  12333  -1579   -530    -68       N  
ATOM   2054  CA  LEU A 354      50.533  64.025  51.923  1.00 74.51           C  
ANISOU 2054  CA  LEU A 354     8318   8426  11568  -1668   -433     51       C  
ATOM   2055  C   LEU A 354      49.009  64.004  51.923  1.00 82.49           C  
ANISOU 2055  C   LEU A 354     9159   9555  12628  -1800   -476     91       C  
ATOM   2056  O   LEU A 354      48.388  63.508  52.871  1.00 86.76           O  
ANISOU 2056  O   LEU A 354     9601  10143  13220  -1944   -456    210       O  
ATOM   2057  CB  LEU A 354      51.043  65.378  52.409  1.00 67.49           C  
ANISOU 2057  CB  LEU A 354     7388   7652  10604  -1526   -312     67       C  
ATOM   2058  CG  LEU A 354      52.426  65.414  53.055  1.00 67.40           C  
ANISOU 2058  CG  LEU A 354     7486   7561  10561  -1444   -239     92       C  
ATOM   2059  CD1 LEU A 354      52.728  66.825  53.545  1.00 71.19           C  
ANISOU 2059  CD1 LEU A 354     7911   8145  10994  -1322   -164    108       C  
ATOM   2060  CD2 LEU A 354      52.531  64.405  54.190  1.00 56.66           C  
ANISOU 2060  CD2 LEU A 354     6152   6131   9247  -1552   -212    177       C  
ATOM   2061  N   LEU A 355      48.389  64.539  50.869  1.00 82.29           N  
ANISOU 2061  N   LEU A 355     9083   9603  12581  -1753   -535      7       N  
ATOM   2062  CA  LEU A 355      46.932  64.554  50.802  1.00 82.17           C  
ANISOU 2062  CA  LEU A 355     8892   9721  12606  -1870   -582     40       C  
ATOM   2063  C   LEU A 355      46.372  63.153  50.576  1.00 81.03           C  
ANISOU 2063  C   LEU A 355     8762   9446  12578  -2071   -731     69       C  
ATOM   2064  O   LEU A 355      45.350  62.786  51.168  1.00 84.83           O  
ANISOU 2064  O   LEU A 355     9084  10023  13124  -2244   -747    189       O  
ATOM   2065  CB  LEU A 355      46.472  65.514  49.705  1.00 83.38           C  
ANISOU 2065  CB  LEU A 355     9000   9979  12703  -1753   -615    -64       C  
ATOM   2066  CG  LEU A 355      46.853  66.984  49.906  1.00 79.81           C  
ANISOU 2066  CG  LEU A 355     8522   9641  12159  -1572   -511    -77       C  
ATOM   2067  CD1 LEU A 355      46.543  67.795  48.660  1.00 81.01           C  
ANISOU 2067  CD1 LEU A 355     8664   9852  12262  -1462   -571   -169       C  
ATOM   2068  CD2 LEU A 355      46.146  67.575  51.119  1.00 76.81           C  
ANISOU 2068  CD2 LEU A 355     7979   9447  11760  -1577   -424      4       C  
ATOM   2069  N   THR A 356      47.028  62.354  49.727  1.00 81.63           N  
ANISOU 2069  N   THR A 356     9023   9312  12681  -2045   -858    -33       N  
ATOM   2070  CA  THR A 356      46.595  60.971  49.536  1.00 86.31           C  
ANISOU 2070  CA  THR A 356     9668   9724  13403  -2228  -1047    -18       C  
ATOM   2071  C   THR A 356      46.776  60.161  50.816  1.00 89.08           C  
ANISOU 2071  C   THR A 356    10022   9991  13834  -2389  -1022    148       C  
ATOM   2072  O   THR A 356      45.973  59.271  51.121  1.00 86.31           O  
ANISOU 2072  O   THR A 356     9602   9581  13611  -2617  -1142    264       O  
ATOM   2073  CB  THR A 356      47.368  60.326  48.384  1.00 81.88           C  
ANISOU 2073  CB  THR A 356     9326   8958  12826  -2107  -1204   -194       C  
ATOM   2074  OG1 THR A 356      47.253  61.141  47.212  1.00 87.00           O  
ANISOU 2074  OG1 THR A 356     9960   9720  13376  -1941  -1209   -327       O  
ATOM   2075  CG2 THR A 356      46.812  58.944  48.077  1.00 79.18           C  
ANISOU 2075  CG2 THR A 356     9051   8400  12633  -2283  -1458   -207       C  
ATOM   2076  N   TRP A 357      47.831  60.457  51.578  1.00 84.56           N  
ANISOU 2076  N   TRP A 357     9522   9415  13191  -2280   -876    177       N  
ATOM   2077  CA  TRP A 357      48.018  59.807  52.869  1.00 82.97           C  
ANISOU 2077  CA  TRP A 357     9313   9169  13044  -2411   -829    345       C  
ATOM   2078  C   TRP A 357      46.892  60.168  53.829  1.00 89.01           C  
ANISOU 2078  C   TRP A 357     9821  10183  13817  -2548   -732    528       C  
ATOM   2079  O   TRP A 357      46.380  59.305  54.551  1.00 93.56           O  
ANISOU 2079  O   TRP A 357    10322  10742  14486  -2761   -781    708       O  
ATOM   2080  CB  TRP A 357      49.376  60.199  53.453  1.00 74.30           C  
ANISOU 2080  CB  TRP A 357     8333   8047  11852  -2239   -686    322       C  
ATOM   2081  CG  TRP A 357      49.645  59.628  54.811  1.00 72.60           C  
ANISOU 2081  CG  TRP A 357     8112   7805  11669  -2341   -622    489       C  
ATOM   2082  CD1 TRP A 357      50.247  58.440  55.093  1.00 75.96           C  
ANISOU 2082  CD1 TRP A 357     8696   7998  12168  -2417   -722    528       C  
ATOM   2083  CD2 TRP A 357      49.324  60.226  56.073  1.00 70.97           C  
ANISOU 2083  CD2 TRP A 357     7735   7822  11408  -2357   -455    635       C  
ATOM   2084  NE1 TRP A 357      50.318  58.256  56.453  1.00 78.00           N  
ANISOU 2084  NE1 TRP A 357     8890   8321  12428  -2497   -617    708       N  
ATOM   2085  CE2 TRP A 357      49.758  59.339  57.077  1.00 74.13           C  
ANISOU 2085  CE2 TRP A 357     8193   8124  11851  -2454   -448    774       C  
ATOM   2086  CE3 TRP A 357      48.706  61.422  56.452  1.00 70.84           C  
ANISOU 2086  CE3 TRP A 357     7528   8086  11301  -2275   -324    654       C  
ATOM   2087  CZ2 TRP A 357      49.596  59.611  58.434  1.00 72.85           C  
ANISOU 2087  CZ2 TRP A 357     7892   8157  11631  -2471   -301    937       C  
ATOM   2088  CZ3 TRP A 357      48.548  61.689  57.798  1.00 74.27           C  
ANISOU 2088  CZ3 TRP A 357     7834   8711  11676  -2274   -191    795       C  
ATOM   2089  CH2 TRP A 357      48.993  60.789  58.773  1.00 75.96           C  
ANISOU 2089  CH2 TRP A 357     8096   8844  11921  -2371   -174    939       C  
ATOM   2090  N   LEU A 358      46.490  61.441  53.843  1.00 87.61           N  
ANISOU 2090  N   LEU A 358     9500  10253  13535  -2421   -605    494       N  
ATOM   2091  CA  LEU A 358      45.429  61.876  54.745  1.00 85.35           C  
ANISOU 2091  CA  LEU A 358     8956  10255  13216  -2494   -508    645       C  
ATOM   2092  C   LEU A 358      44.105  61.200  54.413  1.00 94.61           C  
ANISOU 2092  C   LEU A 358     9969  11484  14494  -2726   -640    745       C  
ATOM   2093  O   LEU A 358      43.371  60.784  55.317  1.00104.88           O  
ANISOU 2093  O   LEU A 358    11083  12942  15824  -2897   -614    957       O  
ATOM   2094  CB  LEU A 358      45.289  63.398  54.689  1.00 73.95           C  
ANISOU 2094  CB  LEU A 358     7423   9035  11640  -2273   -389    548       C  
ATOM   2095  CG  LEU A 358      44.083  64.004  55.413  1.00 71.74           C  
ANISOU 2095  CG  LEU A 358     6868   9100  11291  -2282   -308    654       C  
ATOM   2096  CD1 LEU A 358      44.052  63.589  56.875  1.00 71.49           C  
ANISOU 2096  CD1 LEU A 358     6728   9205  11231  -2355   -207    851       C  
ATOM   2097  CD2 LEU A 358      44.097  65.517  55.287  1.00 68.91           C  
ANISOU 2097  CD2 LEU A 358     6477   8898  10808  -2027   -233    522       C  
ATOM   2098  N   LEU A 359      43.785  61.072  53.124  1.00 90.60           N  
ANISOU 2098  N   LEU A 359     9519  10864  14041  -2735   -790    608       N  
ATOM   2099  CA  LEU A 359      42.505  60.484  52.747  1.00 90.59           C  
ANISOU 2099  CA  LEU A 359     9359  10912  14149  -2957   -939    692       C  
ATOM   2100  C   LEU A 359      42.468  58.991  53.054  1.00101.97           C  
ANISOU 2100  C   LEU A 359    10858  12125  15761  -3224  -1106    844       C  
ATOM   2101  O   LEU A 359      41.451  58.478  53.536  1.00108.12           O  
ANISOU 2101  O   LEU A 359    11431  13023  16628  -3468  -1162   1057       O  
ATOM   2102  CB  LEU A 359      42.227  60.745  51.268  1.00 86.57           C  
ANISOU 2102  CB  LEU A 359     8914  10332  13647  -2875  -1070    488       C  
ATOM   2103  CG  LEU A 359      41.848  62.182  50.894  1.00 88.25           C  
ANISOU 2103  CG  LEU A 359     9013  10798  13721  -2671   -950    383       C  
ATOM   2104  CD1 LEU A 359      41.510  62.284  49.414  1.00 92.93           C  
ANISOU 2104  CD1 LEU A 359     9663  11319  14328  -2615  -1099    205       C  
ATOM   2105  CD2 LEU A 359      40.690  62.692  51.741  1.00 88.04           C  
ANISOU 2105  CD2 LEU A 359     8684  11118  13648  -2736   -847    540       C  
ATOM   2106  N   ASP A 360      43.565  58.279  52.790  1.00108.47           N  
ANISOU 2106  N   ASP A 360    11955  12627  16632  -3181  -1201    749       N  
ATOM   2107  CA  ASP A 360      43.661  56.850  53.070  1.00115.66           C  
ANISOU 2107  CA  ASP A 360    12968  13267  17711  -3409  -1393    873       C  
ATOM   2108  C   ASP A 360      44.039  56.555  54.515  1.00123.50           C  
ANISOU 2108  C   ASP A 360    13919  14312  18696  -3492  -1261   1099       C  
ATOM   2109  O   ASP A 360      44.337  55.399  54.840  1.00132.38           O  
ANISOU 2109  O   ASP A 360    15164  15184  19950  -3655  -1411   1206       O  
ATOM   2110  CB  ASP A 360      44.673  56.187  52.129  1.00116.01           C  
ANISOU 2110  CB  ASP A 360    13334  12952  17793  -3287  -1576    650       C  
ATOM   2111  CG  ASP A 360      44.399  56.492  50.669  1.00123.78           C  
ANISOU 2111  CG  ASP A 360    14372  13905  18755  -3163  -1702    415       C  
ATOM   2112  OD1 ASP A 360      43.371  57.137  50.378  1.00128.95           O  
ANISOU 2112  OD1 ASP A 360    14820  14784  19392  -3203  -1668    433       O  
ATOM   2113  OD2 ASP A 360      45.209  56.079  49.810  1.00126.69           O  
ANISOU 2113  OD2 ASP A 360    14983  14044  19109  -3008  -1838    210       O  
ATOM   2114  N   ASN A 361      44.028  57.567  55.382  1.00123.39           N  
ANISOU 2114  N   ASN A 361    13742  14612  18528  -3371  -1004   1167       N  
ATOM   2115  CA  ASN A 361      44.403  57.368  56.776  1.00126.23           C  
ANISOU 2115  CA  ASN A 361    14053  15059  18849  -3412   -866   1369       C  
ATOM   2116  C   ASN A 361      43.226  56.879  57.611  1.00133.40           C  
ANISOU 2116  C   ASN A 361    14680  16188  19820  -3688   -875   1689       C  
ATOM   2117  O   ASN A 361      43.401  56.029  58.490  1.00140.69           O  
ANISOU 2117  O   ASN A 361    15605  17043  20808  -3854   -898   1910       O  
ATOM   2118  CB  ASN A 361      44.973  58.665  57.341  1.00123.47           C  
ANISOU 2118  CB  ASN A 361    13671  14940  18301  -3132   -614   1281       C  
ATOM   2119  CG  ASN A 361      44.868  58.743  58.837  1.00123.79           C  
ANISOU 2119  CG  ASN A 361    13548  15227  18261  -3159   -449   1506       C  
ATOM   2120  OD1 ASN A 361      43.890  59.263  59.366  1.00128.48           O  
ANISOU 2120  OD1 ASN A 361    13869  16174  18774  -3177   -351   1633       O  
ATOM   2121  ND2 ASN A 361      45.880  58.241  59.534  1.00118.93           N  
ANISOU 2121  ND2 ASN A 361    13090  14453  17646  -3138   -416   1553       N  
ATOM   2122  N   SER A 362      42.028  57.409  57.359  1.00132.87           N  
ANISOU 2122  N   SER A 362    14355  16405  19725  -3739   -857   1733       N  
ATOM   2123  CA  SER A 362      40.784  56.953  57.981  1.00139.48           C  
ANISOU 2123  CA  SER A 362    14880  17497  20619  -4015   -883   2051       C  
ATOM   2124  C   SER A 362      40.816  57.023  59.508  1.00136.67           C  
ANISOU 2124  C   SER A 362    14348  17435  20146  -4021   -684   2310       C  
ATOM   2125  O   SER A 362      39.958  56.442  60.181  1.00127.03           O  
ANISOU 2125  O   SER A 362    12949  16410  18908  -4179   -683   2567       O  
ATOM   2126  CB  SER A 362      40.440  55.527  57.517  1.00140.12           C  
ANISOU 2126  CB  SER A 362    15093  17263  20882  -4257  -1149   2124       C  
ATOM   2127  OG  SER A 362      41.447  54.594  57.865  1.00135.95           O  
ANISOU 2127  OG  SER A 362    14833  16400  20420  -4279  -1227   2141       O  
ATOM   2128  N   PHE A 363      41.795  57.735  60.062  1.00134.64           N  
ANISOU 2128  N   PHE A 363    14210  17217  19730  -3743   -499   2181       N  
ATOM   2129  CA  PHE A 363      41.859  57.985  61.495  1.00126.73           C  
ANISOU 2129  CA  PHE A 363    13046  16532  18575  -3676   -298   2378       C  
ATOM   2130  C   PHE A 363      41.345  59.365  61.873  1.00115.16           C  
ANISOU 2130  C   PHE A 363    11360  15515  16880  -3410   -102   2301       C  
ATOM   2131  O   PHE A 363      40.821  59.541  62.978  1.00107.59           O  
ANISOU 2131  O   PHE A 363    10142  14954  15782  -3393     36   2515       O  
ATOM   2132  CB  PHE A 363      43.301  57.818  61.993  1.00125.04           C  
ANISOU 2132  CB  PHE A 363    13107  16068  18334  -3537   -242   2293       C  
ATOM   2133  CG  PHE A 363      43.470  58.063  63.462  1.00126.26           C  
ANISOU 2133  CG  PHE A 363    13123  16527  18323  -3441    -46   2471       C  
ATOM   2134  CD1 PHE A 363      43.816  59.318  63.937  1.00123.45           C  
ANISOU 2134  CD1 PHE A 363    12739  16410  17757  -3108    138   2308       C  
ATOM   2135  CD2 PHE A 363      43.277  57.036  64.370  1.00130.61           C  
ANISOU 2135  CD2 PHE A 363    13574  17123  18929  -3680    -65   2807       C  
ATOM   2136  CE1 PHE A 363      43.969  59.542  65.288  1.00126.79           C  
ANISOU 2136  CE1 PHE A 363    13039  17121  18013  -2990    300   2451       C  
ATOM   2137  CE2 PHE A 363      43.428  57.252  65.723  1.00131.80           C  
ANISOU 2137  CE2 PHE A 363    13589  17583  18906  -3573    118   2976       C  
ATOM   2138  CZ  PHE A 363      43.774  58.507  66.185  1.00130.83           C  
ANISOU 2138  CZ  PHE A 363    13442  17709  18560  -3215    302   2785       C  
ATOM   2139  N   PHE A 364      41.475  60.340  60.977  1.00112.51           N  
ANISOU 2139  N   PHE A 364    11120  15132  16497  -3191   -100   2005       N  
ATOM   2140  CA  PHE A 364      40.944  61.680  61.185  1.00114.48           C  
ANISOU 2140  CA  PHE A 364    11189  15761  16549  -2927     35   1900       C  
ATOM   2141  C   PHE A 364      39.545  61.742  60.588  1.00124.26           C  
ANISOU 2141  C   PHE A 364    12172  17228  17812  -3054    -35   1965       C  
ATOM   2142  O   PHE A 364      39.376  61.561  59.378  1.00128.18           O  
ANISOU 2142  O   PHE A 364    12771  17491  18441  -3143   -184   1836       O  
ATOM   2143  CB  PHE A 364      41.852  62.722  60.534  1.00109.63           C  
ANISOU 2143  CB  PHE A 364    10817  14955  15881  -2636     53   1570       C  
ATOM   2144  CG  PHE A 364      43.211  62.815  61.160  1.00104.88           C  
ANISOU 2144  CG  PHE A 364    10436  14176  15239  -2488    127   1502       C  
ATOM   2145  CD1 PHE A 364      43.452  63.693  62.202  1.00107.11           C  
ANISOU 2145  CD1 PHE A 364    10650  14707  15339  -2239    270   1480       C  
ATOM   2146  CD2 PHE A 364      44.249  62.018  60.705  1.00 97.58           C  
ANISOU 2146  CD2 PHE A 364     9784  12842  14449  -2582     39   1451       C  
ATOM   2147  CE1 PHE A 364      44.703  63.773  62.778  1.00107.63           C  
ANISOU 2147  CE1 PHE A 364    10914  14606  15376  -2110    325   1418       C  
ATOM   2148  CE2 PHE A 364      45.497  62.093  61.275  1.00 96.71           C  
ANISOU 2148  CE2 PHE A 364     9861  12585  14298  -2447    106   1394       C  
ATOM   2149  CZ  PHE A 364      45.726  62.971  62.314  1.00103.48           C  
ANISOU 2149  CZ  PHE A 364    10645  13683  14990  -2223    250   1383       C  
ATOM   2150  N   ARG A 365      38.546  61.993  61.430  1.00127.89           N  
ANISOU 2150  N   ARG A 365    12292  18169  18132  -3047     69   2164       N  
ATOM   2151  CA  ARG A 365      37.173  62.033  60.950  1.00133.17           C  
ANISOU 2151  CA  ARG A 365    12678  19107  18812  -3172      9   2254       C  
ATOM   2152  C   ARG A 365      36.915  63.309  60.154  1.00125.61           C  
ANISOU 2152  C   ARG A 365    11741  18231  17754  -2890     18   1954       C  
ATOM   2153  O   ARG A 365      37.517  64.358  60.403  1.00126.81           O  
ANISOU 2153  O   ARG A 365    12007  18416  17760  -2564    114   1749       O  
ATOM   2154  CB  ARG A 365      36.187  61.934  62.115  1.00141.48           C  
ANISOU 2154  CB  ARG A 365    13328  20710  19717  -3229    128   2575       C  
ATOM   2155  CG  ARG A 365      34.789  61.496  61.691  1.00148.83           C  
ANISOU 2155  CG  ARG A 365    13986  21855  20709  -3465     33   2755       C  
ATOM   2156  CD  ARG A 365      33.722  61.931  62.688  1.00152.65           C  
ANISOU 2156  CD  ARG A 365    14123  22948  20928  -3316    183   2929       C  
ATOM   2157  NE  ARG A 365      32.381  61.820  62.116  1.00153.30           N  
ANISOU 2157  NE  ARG A 365    14018  23208  21020  -3420     98   2988       N  
ATOM   2158  CZ  ARG A 365      31.297  62.398  62.627  1.00149.57           C  
ANISOU 2158  CZ  ARG A 365    13239  23275  20316  -3257    199   3074       C  
ATOM   2159  NH1 ARG A 365      31.392  63.131  63.728  1.00154.15           N  
ANISOU 2159  NH1 ARG A 365    13673  24273  20625  -2959    382   3094       N  
ATOM   2160  NH2 ARG A 365      30.120  62.245  62.035  1.00141.55           N  
ANISOU 2160  NH2 ARG A 365    12067  22386  19330  -3373    108   3128       N  
ATOM   2161  N   ASN A 366      36.005  63.201  59.181  1.00122.05           N  
ANISOU 2161  N   ASN A 366    11183  17798  17394  -3026   -105   1937       N  
ATOM   2162  CA  ASN A 366      35.604  64.317  58.320  1.00116.33           C  
ANISOU 2162  CA  ASN A 366    10458  17153  16591  -2795   -123   1679       C  
ATOM   2163  C   ASN A 366      36.772  64.853  57.500  1.00110.89           C  
ANISOU 2163  C   ASN A 366    10141  16051  15941  -2608   -163   1374       C  
ATOM   2164  O   ASN A 366      36.807  66.036  57.155  1.00107.36           O  
ANISOU 2164  O   ASN A 366     9738  15673  15380  -2329   -133   1160       O  
ATOM   2165  CB  ASN A 366      34.966  65.451  59.127  1.00114.78           C  
ANISOU 2165  CB  ASN A 366    10009  17467  16134  -2497     26   1667       C  
ATOM   2166  CG  ASN A 366      33.854  64.967  60.030  1.00113.46           C  
ANISOU 2166  CG  ASN A 366     9438  17789  15884  -2649     92   1995       C  
ATOM   2167  OD1 ASN A 366      33.173  63.987  59.726  1.00118.99           O  
ANISOU 2167  OD1 ASN A 366     9987  18488  16737  -2994     -9   2214       O  
ATOM   2168  ND2 ASN A 366      33.670  65.649  61.157  1.00106.16           N  
ANISOU 2168  ND2 ASN A 366     8328  17297  14712  -2387    249   2040       N  
ATOM   2169  N   ARG A 367      37.741  63.989  57.188  1.00111.55           N  
ANISOU 2169  N   ARG A 367    10487  15715  16181  -2755   -240   1363       N  
ATOM   2170  CA  ARG A 367      38.870  64.406  56.362  1.00102.23           C  
ANISOU 2170  CA  ARG A 367     9635  14175  15031  -2593   -279   1104       C  
ATOM   2171  C   ARG A 367      38.402  64.806  54.970  1.00105.05           C  
ANISOU 2171  C   ARG A 367    10027  14458  15430  -2558   -398    924       C  
ATOM   2172  O   ARG A 367      38.779  65.864  54.454  1.00 98.88           O  
ANISOU 2172  O   ARG A 367     9359  13643  14568  -2313   -375    721       O  
ATOM   2173  CB  ARG A 367      39.901  63.280  56.283  1.00 95.99           C  
ANISOU 2173  CB  ARG A 367     9092  12991  14387  -2756   -353   1138       C  
ATOM   2174  CG  ARG A 367      39.268  61.901  56.236  1.00 99.62           C  
ANISOU 2174  CG  ARG A 367     9462  13372  15017  -3106   -494   1349       C  
ATOM   2175  CD  ARG A 367      40.270  60.804  55.944  1.00103.16           C  
ANISOU 2175  CD  ARG A 367    10194  13383  15618  -3234   -620   1332       C  
ATOM   2176  NE  ARG A 367      39.663  59.488  56.124  1.00112.56           N  
ANISOU 2176  NE  ARG A 367    11295  14494  16981  -3579   -774   1570       N  
ATOM   2177  CZ  ARG A 367      38.888  58.889  55.224  1.00117.01           C  
ANISOU 2177  CZ  ARG A 367    11817  14948  17693  -3778   -984   1576       C  
ATOM   2178  NH1 ARG A 367      38.620  59.487  54.069  1.00123.04           N  
ANISOU 2178  NH1 ARG A 367    12620  15694  18436  -3650  -1045   1347       N  
ATOM   2179  NH2 ARG A 367      38.377  57.690  55.478  1.00111.58           N  
ANISOU 2179  NH2 ARG A 367    11050  14166  17181  -4110  -1148   1819       N  
ATOM   2180  N   HIS A 368      37.562  63.971  54.351  1.00113.89           N  
ANISOU 2180  N   HIS A 368    11046  15549  16679  -2806   -540   1007       N  
ATOM   2181  CA  HIS A 368      37.079  64.260  53.005  1.00116.95           C  
ANISOU 2181  CA  HIS A 368    11462  15868  17106  -2779   -668    837       C  
ATOM   2182  C   HIS A 368      36.217  65.516  52.984  1.00119.34           C  
ANISOU 2182  C   HIS A 368    11563  16530  17253  -2571   -591    766       C  
ATOM   2183  O   HIS A 368      36.347  66.351  52.082  1.00118.35           O  
ANISOU 2183  O   HIS A 368    11547  16339  17081  -2382   -622    560       O  
ATOM   2184  CB  HIS A 368      36.298  63.064  52.463  1.00118.51           C  
ANISOU 2184  CB  HIS A 368    11576  15970  17484  -3099   -861    953       C  
ATOM   2185  CG  HIS A 368      36.154  63.060  50.973  1.00118.54           C  
ANISOU 2185  CG  HIS A 368    11706  15776  17556  -3079  -1031    749       C  
ATOM   2186  ND1 HIS A 368      36.794  62.143  50.166  1.00118.47           N  
ANISOU 2186  ND1 HIS A 368    11948  15378  17687  -3173  -1209    657       N  
ATOM   2187  CD2 HIS A 368      35.449  63.864  50.142  1.00119.13           C  
ANISOU 2187  CD2 HIS A 368    11695  16004  17567  -2953  -1060    612       C  
ATOM   2188  CE1 HIS A 368      36.486  62.379  48.904  1.00117.64           C  
ANISOU 2188  CE1 HIS A 368    11898  15207  17592  -3102  -1334    474       C  
ATOM   2189  NE2 HIS A 368      35.671  63.418  48.861  1.00118.21           N  
ANISOU 2189  NE2 HIS A 368    11768  15598  17547  -2979  -1243    450       N  
ATOM   2190  N   ARG A 369      35.331  65.667  53.969  1.00124.28           N  
ANISOU 2190  N   ARG A 369    11888  17549  17782  -2589   -497    941       N  
ATOM   2191  CA  ARG A 369      34.485  66.854  54.025  1.00122.02           C  
ANISOU 2191  CA  ARG A 369    11402  17632  17326  -2356   -434    864       C  
ATOM   2192  C   ARG A 369      35.319  68.108  54.273  1.00115.49           C  
ANISOU 2192  C   ARG A 369    10747  16773  16359  -2005   -342    672       C  
ATOM   2193  O   ARG A 369      35.203  69.097  53.540  1.00110.97           O  
ANISOU 2193  O   ARG A 369    10236  16198  15730  -1800   -382    482       O  
ATOM   2194  CB  ARG A 369      33.416  66.678  55.107  1.00122.92           C  
ANISOU 2194  CB  ARG A 369    11142  18220  17343  -2430   -348   1108       C  
ATOM   2195  CG  ARG A 369      32.742  67.964  55.556  1.00124.80           C  
ANISOU 2195  CG  ARG A 369    11181  18888  17348  -2106   -252   1027       C  
ATOM   2196  CD  ARG A 369      32.144  67.801  56.943  1.00132.73           C  
ANISOU 2196  CD  ARG A 369    11866  20360  18204  -2106   -120   1270       C  
ATOM   2197  NE  ARG A 369      32.129  69.059  57.682  1.00139.29           N  
ANISOU 2197  NE  ARG A 369    12641  21495  18788  -1702    -13   1140       N  
ATOM   2198  CZ  ARG A 369      32.128  69.146  59.009  1.00145.35           C  
ANISOU 2198  CZ  ARG A 369    13250  22592  19384  -1576    120   1270       C  
ATOM   2199  NH1 ARG A 369      32.148  68.045  59.749  1.00147.85           N  
ANISOU 2199  NH1 ARG A 369    13440  22982  19753  -1845    178   1561       N  
ATOM   2200  NH2 ARG A 369      32.112  70.335  59.598  1.00146.73           N  
ANISOU 2200  NH2 ARG A 369    13399  23018  19333  -1171    178   1108       N  
ATOM   2201  N   LEU A 370      36.182  68.077  55.295  1.00109.83           N  
ANISOU 2201  N   LEU A 370    10117  16017  15596  -1939   -238    726       N  
ATOM   2202  CA  LEU A 370      36.988  69.250  55.627  1.00 99.95           C  
ANISOU 2202  CA  LEU A 370     9024  14725  14227  -1621   -177    557       C  
ATOM   2203  C   LEU A 370      37.948  69.609  54.502  1.00 94.43           C  
ANISOU 2203  C   LEU A 370     8629  13637  13614  -1557   -260    367       C  
ATOM   2204  O   LEU A 370      38.257  70.789  54.299  1.00 89.27           O  
ANISOU 2204  O   LEU A 370     8072  12961  12883  -1304   -271    209       O  
ATOM   2205  CB  LEU A 370      37.766  69.006  56.920  1.00 93.46           C  
ANISOU 2205  CB  LEU A 370     8241  13916  13355  -1589    -65    659       C  
ATOM   2206  CG  LEU A 370      36.988  69.170  58.226  1.00 89.98           C  
ANISOU 2206  CG  LEU A 370     7507  13941  12740  -1495     45    803       C  
ATOM   2207  CD1 LEU A 370      37.740  68.542  59.388  1.00 89.78           C  
ANISOU 2207  CD1 LEU A 370     7519  13893  12700  -1552    143    952       C  
ATOM   2208  CD2 LEU A 370      36.714  70.640  58.498  1.00 92.21           C  
ANISOU 2208  CD2 LEU A 370     7743  14458  12833  -1113     58    622       C  
ATOM   2209  N   LEU A 371      38.430  68.608  53.765  1.00 91.27           N  
ANISOU 2209  N   LEU A 371     8378  12935  13366  -1774   -332    387       N  
ATOM   2210  CA  LEU A 371      39.334  68.881  52.654  1.00 89.40           C  
ANISOU 2210  CA  LEU A 371     8404  12380  13185  -1704   -404    225       C  
ATOM   2211  C   LEU A 371      38.607  69.581  51.513  1.00 91.00           C  
ANISOU 2211  C   LEU A 371     8566  12645  13365  -1615   -493     98       C  
ATOM   2212  O   LEU A 371      39.144  70.515  50.904  1.00 91.72           O  
ANISOU 2212  O   LEU A 371     8802  12628  13419  -1431   -517    -35       O  
ATOM   2213  CB  LEU A 371      39.962  67.577  52.174  1.00 83.34           C  
ANISOU 2213  CB  LEU A 371     7794  11313  12560  -1924   -474    265       C  
ATOM   2214  CG  LEU A 371      41.235  67.675  51.346  1.00 76.39           C  
ANISOU 2214  CG  LEU A 371     7192  10124  11707  -1836   -512    135       C  
ATOM   2215  CD1 LEU A 371      42.375  68.203  52.196  1.00 71.50           C  
ANISOU 2215  CD1 LEU A 371     6692   9444  11031  -1692   -405    135       C  
ATOM   2216  CD2 LEU A 371      41.558  66.304  50.798  1.00 81.88           C  
ANISOU 2216  CD2 LEU A 371     8007  10574  12528  -2034   -617    155       C  
ATOM   2217  N   ALA A 372      37.380  69.148  51.216  1.00 88.15           N  
ANISOU 2217  N   ALA A 372     8000  12463  13031  -1752   -550    154       N  
ATOM   2218  CA  ALA A 372      36.624  69.757  50.127  1.00 81.06           C  
ANISOU 2218  CA  ALA A 372     7053  11638  12110  -1671   -641     34       C  
ATOM   2219  C   ALA A 372      36.180  71.173  50.477  1.00 86.87           C  
ANISOU 2219  C   ALA A 372     7691  12621  12694  -1393   -596    -45       C  
ATOM   2220  O   ALA A 372      36.131  72.043  49.599  1.00 87.28           O  
ANISOU 2220  O   ALA A 372     7820  12630  12712  -1235   -662   -182       O  
ATOM   2221  CB  ALA A 372      35.418  68.887  49.776  1.00 78.42           C  
ANISOU 2221  CB  ALA A 372     6509  11436  11851  -1901   -728    122       C  
ATOM   2222  N   ILE A 373      35.853  71.425  51.751  1.00 87.12           N  
ANISOU 2222  N   ILE A 373     7558  12919  12625  -1314   -497     38       N  
ATOM   2223  CA  ILE A 373      35.421  72.761  52.166  1.00 81.79           C  
ANISOU 2223  CA  ILE A 373     6800  12486  11792  -1011   -481    -59       C  
ATOM   2224  C   ILE A 373      36.515  73.783  51.895  1.00 80.65           C  
ANISOU 2224  C   ILE A 373     6924  12082  11638   -796   -516   -205       C  
ATOM   2225  O   ILE A 373      36.251  74.893  51.417  1.00 71.42           O  
ANISOU 2225  O   ILE A 373     5784  10943  10408   -584   -592   -333       O  
ATOM   2226  CB  ILE A 373      35.020  72.769  53.652  1.00 80.43           C  
ANISOU 2226  CB  ILE A 373     6416  12652  11491   -936   -370     52       C  
ATOM   2227  CG1 ILE A 373      33.759  71.944  53.892  1.00 81.30           C  
ANISOU 2227  CG1 ILE A 373     6201  13099  11590  -1133   -344    227       C  
ATOM   2228  CG2 ILE A 373      34.828  74.199  54.147  1.00 76.54           C  
ANISOU 2228  CG2 ILE A 373     5902  12353  10828   -563   -380    -91       C  
ATOM   2229  CD1 ILE A 373      33.299  71.970  55.335  1.00 80.64           C  
ANISOU 2229  CD1 ILE A 373     5871  13423  11347  -1042   -225    362       C  
ATOM   2230  N   HIS A 374      37.761  73.431  52.217  1.00 87.89           N  
ANISOU 2230  N   HIS A 374     8033  12741  12619   -853   -473   -172       N  
ATOM   2231  CA  HIS A 374      38.859  74.359  51.978  1.00 90.85           C  
ANISOU 2231  CA  HIS A 374     8646  12872  13000   -682   -515   -275       C  
ATOM   2232  C   HIS A 374      39.158  74.496  50.492  1.00 88.45           C  
ANISOU 2232  C   HIS A 374     8489  12349  12770   -720   -608   -342       C  
ATOM   2233  O   HIS A 374      39.404  75.604  50.000  1.00 84.38           O  
ANISOU 2233  O   HIS A 374     8075  11755  12229   -544   -686   -430       O  
ATOM   2234  CB  HIS A 374      40.108  73.910  52.729  1.00 90.91           C  
ANISOU 2234  CB  HIS A 374     8800  12691  13051   -737   -442   -212       C  
ATOM   2235  CG  HIS A 374      41.308  74.749  52.430  1.00 91.73           C  
ANISOU 2235  CG  HIS A 374     9135  12536  13183   -608   -495   -284       C  
ATOM   2236  ND1 HIS A 374      41.550  75.953  53.057  1.00 93.92           N  
ANISOU 2236  ND1 HIS A 374     9457  12833  13395   -368   -541   -357       N  
ATOM   2237  CD2 HIS A 374      42.322  74.571  51.551  1.00 89.91           C  
ANISOU 2237  CD2 HIS A 374     9092  12034  13036   -683   -525   -284       C  
ATOM   2238  CE1 HIS A 374      42.667  76.475  52.583  1.00 91.81           C  
ANISOU 2238  CE1 HIS A 374     9392  12299  13192   -333   -602   -378       C  
ATOM   2239  NE2 HIS A 374      43.155  75.657  51.669  1.00 88.77           N  
ANISOU 2239  NE2 HIS A 374     9085  11758  12886   -519   -579   -327       N  
ATOM   2240  N   LEU A 375      39.138  73.381  49.761  1.00 86.73           N  
ANISOU 2240  N   LEU A 375     8285  12030  12638   -939   -618   -299       N  
ATOM   2241  CA  LEU A 375      39.485  73.399  48.347  1.00 81.48           C  
ANISOU 2241  CA  LEU A 375     7758  11180  12020   -957   -702   -364       C  
ATOM   2242  C   LEU A 375      38.425  74.075  47.485  1.00 83.73           C  
ANISOU 2242  C   LEU A 375     7943  11610  12259   -864   -790   -445       C  
ATOM   2243  O   LEU A 375      38.709  74.396  46.326  1.00 82.59           O  
ANISOU 2243  O   LEU A 375     7913  11344  12122   -820   -864   -503       O  
ATOM   2244  CB  LEU A 375      39.728  71.968  47.863  1.00 76.84           C  
ANISOU 2244  CB  LEU A 375     7219  10450  11527  -1185   -716   -320       C  
ATOM   2245  CG  LEU A 375      41.090  71.374  48.238  1.00 70.22           C  
ANISOU 2245  CG  LEU A 375     6558   9389  10735  -1241   -662   -273       C  
ATOM   2246  CD1 LEU A 375      41.065  69.853  48.188  1.00 67.84           C  
ANISOU 2246  CD1 LEU A 375     6263   8988  10524  -1467   -688   -218       C  
ATOM   2247  CD2 LEU A 375      42.177  71.924  47.332  1.00 65.63           C  
ANISOU 2247  CD2 LEU A 375     6170   8627  10138  -1127   -694   -330       C  
ATOM   2248  N   ALA A 376      37.224  74.312  48.022  1.00 80.68           N  
ANISOU 2248  N   ALA A 376     7340  11505  11811   -821   -783   -444       N  
ATOM   2249  CA  ALA A 376      36.171  74.937  47.228  1.00 78.04           C  
ANISOU 2249  CA  ALA A 376     6901  11326  11426   -723   -870   -526       C  
ATOM   2250  C   ALA A 376      36.439  76.419  46.993  1.00 89.85           C  
ANISOU 2250  C   ALA A 376     8506  12777  12855   -459   -936   -619       C  
ATOM   2251  O   ALA A 376      35.928  76.993  46.024  1.00 95.91           O  
ANISOU 2251  O   ALA A 376     9272  13571  13598   -373  -1029   -692       O  
ATOM   2252  CB  ALA A 376      34.815  74.744  47.906  1.00 66.95           C  
ANISOU 2252  CB  ALA A 376     5207  10273   9959   -744   -843   -485       C  
ATOM   2253  N   THR A 377      37.227  77.055  47.858  1.00 90.64           N  
ANISOU 2253  N   THR A 377     8707  12799  12934   -331   -909   -616       N  
ATOM   2254  CA  THR A 377      37.574  78.462  47.710  1.00 84.96           C  
ANISOU 2254  CA  THR A 377     8114  11987  12180    -96  -1010   -690       C  
ATOM   2255  C   THR A 377      38.867  78.668  46.934  1.00 82.84           C  
ANISOU 2255  C   THR A 377     8076  11410  11989   -135  -1049   -654       C  
ATOM   2256  O   THR A 377      39.361  79.799  46.865  1.00 81.23           O  
ANISOU 2256  O   THR A 377     7996  11082  11787     21  -1146   -674       O  
ATOM   2257  CB  THR A 377      37.685  79.124  49.084  1.00 85.65           C  
ANISOU 2257  CB  THR A 377     8185  12158  12202     88  -1001   -717       C  
ATOM   2258  OG1 THR A 377      38.511  78.319  49.936  1.00 94.93           O  
ANISOU 2258  OG1 THR A 377     9397  13255  13416    -42   -886   -631       O  
ATOM   2259  CG2 THR A 377      36.311  79.260  49.711  1.00 77.19           C  
ANISOU 2259  CG2 THR A 377     6868  11455  11007    211   -989   -766       C  
ATOM   2260  N   HIS A 378      39.426  77.607  46.360  1.00 84.47           N  
ANISOU 2260  N   HIS A 378     8339  11500  12258   -332   -990   -594       N  
ATOM   2261  CA  HIS A 378      40.642  77.673  45.559  1.00 85.22           C  
ANISOU 2261  CA  HIS A 378     8618  11362  12398   -364  -1011   -545       C  
ATOM   2262  C   HIS A 378      40.477  76.858  44.288  1.00 86.50           C  
ANISOU 2262  C   HIS A 378     8783  11513  12569   -479  -1025   -553       C  
ATOM   2263  O   HIS A 378      41.391  76.149  43.858  1.00 87.70           O  
ANISOU 2263  O   HIS A 378     9039  11533  12750   -572   -992   -511       O  
ATOM   2264  CB  HIS A 378      41.852  77.186  46.352  1.00 84.34           C  
ANISOU 2264  CB  HIS A 378     8606  11105  12332   -441   -926   -473       C  
ATOM   2265  CG  HIS A 378      42.104  77.959  47.608  1.00 87.13           C  
ANISOU 2265  CG  HIS A 378     8973  11458  12676   -316   -928   -477       C  
ATOM   2266  ND1 HIS A 378      42.802  79.147  47.624  1.00 88.25           N  
ANISOU 2266  ND1 HIS A 378     9237  11459  12834   -181  -1026   -467       N  
ATOM   2267  CD2 HIS A 378      41.753  77.710  48.892  1.00 87.24           C  
ANISOU 2267  CD2 HIS A 378     8891  11597  12659   -296   -860   -486       C  
ATOM   2268  CE1 HIS A 378      42.870  79.597  48.864  1.00 88.01           C  
ANISOU 2268  CE1 HIS A 378     9201  11450  12789    -71  -1032   -497       C  
ATOM   2269  NE2 HIS A 378      42.241  78.745  49.653  1.00 88.56           N  
ANISOU 2269  NE2 HIS A 378     9135  11700  12816   -127   -921   -511       N  
ATOM   2270  N   LEU A 379      39.299  76.942  43.668  1.00 87.00           N  
ANISOU 2270  N   LEU A 379     8731  11728  12599   -454  -1086   -620       N  
ATOM   2271  CA  LEU A 379      39.034  76.163  42.466  1.00 80.39           C  
ANISOU 2271  CA  LEU A 379     7890  10889  11765   -545  -1125   -651       C  
ATOM   2272  C   LEU A 379      39.707  76.740  41.228  1.00 80.49           C  
ANISOU 2272  C   LEU A 379     8036  10805  11742   -454  -1188   -638       C  
ATOM   2273  O   LEU A 379      39.881  76.011  40.244  1.00 78.11           O  
ANISOU 2273  O   LEU A 379     7775  10476  11429   -507  -1212   -659       O  
ATOM   2274  CB  LEU A 379      37.525  76.050  42.227  1.00 69.67           C  
ANISOU 2274  CB  LEU A 379     6349   9737  10385   -555  -1178   -722       C  
ATOM   2275  CG  LEU A 379      36.718  75.259  43.263  1.00 70.46           C  
ANISOU 2275  CG  LEU A 379     6269   9988  10515   -686  -1121   -699       C  
ATOM   2276  CD1 LEU A 379      35.221  75.350  42.975  1.00 70.26           C  
ANISOU 2276  CD1 LEU A 379     6037  10204  10454   -675  -1184   -753       C  
ATOM   2277  CD2 LEU A 379      37.168  73.808  43.339  1.00 69.79           C  
ANISOU 2277  CD2 LEU A 379     6222   9781  10515   -904  -1090   -651       C  
ATOM   2278  N   HIS A 380      40.088  78.023  41.252  1.00 78.51           N  
ANISOU 2278  N   HIS A 380     7851  10508  11471   -312  -1232   -598       N  
ATOM   2279  CA  HIS A 380      40.785  78.613  40.111  1.00 75.88           C  
ANISOU 2279  CA  HIS A 380     7627  10101  11103   -242  -1292   -535       C  
ATOM   2280  C   HIS A 380      42.075  77.865  39.812  1.00 78.50           C  
ANISOU 2280  C   HIS A 380     8063  10324  11437   -323  -1225   -457       C  
ATOM   2281  O   HIS A 380      42.328  77.467  38.670  1.00 74.85           O  
ANISOU 2281  O   HIS A 380     7635   9888  10918   -315  -1244   -454       O  
ATOM   2282  CB  HIS A 380      41.096  80.088  40.369  1.00 75.21           C  
ANISOU 2282  CB  HIS A 380     7605   9943  11029   -110  -1374   -470       C  
ATOM   2283  CG  HIS A 380      39.925  80.889  40.839  1.00 82.35           C  
ANISOU 2283  CG  HIS A 380     8422  10948  11918     14  -1453   -562       C  
ATOM   2284  ND1 HIS A 380      39.469  80.848  42.138  1.00 87.86           N  
ANISOU 2284  ND1 HIS A 380     9044  11710  12628     36  -1415   -625       N  
ATOM   2285  CD2 HIS A 380      39.127  81.766  40.185  1.00 86.52           C  
ANISOU 2285  CD2 HIS A 380     8924  11545  12404    145  -1573   -604       C  
ATOM   2286  CE1 HIS A 380      38.433  81.659  42.262  1.00 91.92           C  
ANISOU 2286  CE1 HIS A 380     9483  12344  13099    190  -1508   -710       C  
ATOM   2287  NE2 HIS A 380      38.205  82.228  41.091  1.00 86.71           N  
ANISOU 2287  NE2 HIS A 380     8858  11675  12412    255  -1609   -704       N  
ATOM   2288  N   THR A 381      42.910  77.670  40.832  1.00 83.17           N  
ANISOU 2288  N   THR A 381     8705  10815  12082   -378  -1151   -402       N  
ATOM   2289  CA  THR A 381      44.230  77.103  40.596  1.00 82.99           C  
ANISOU 2289  CA  THR A 381     8781  10700  12051   -427  -1091   -321       C  
ATOM   2290  C   THR A 381      44.182  75.583  40.486  1.00 82.44           C  
ANISOU 2290  C   THR A 381     8707  10635  11980   -531  -1042   -396       C  
ATOM   2291  O   THR A 381      44.871  75.001  39.641  1.00 85.10           O  
ANISOU 2291  O   THR A 381     9109  10964  12262   -520  -1040   -385       O  
ATOM   2292  CB  THR A 381      45.189  77.540  41.703  1.00 83.01           C  
ANISOU 2292  CB  THR A 381     8843  10584  12112   -438  -1048   -232       C  
ATOM   2293  OG1 THR A 381      44.509  77.524  42.964  1.00 89.85           O  
ANISOU 2293  OG1 THR A 381     9646  11467  13024   -453  -1023   -299       O  
ATOM   2294  CG2 THR A 381      45.694  78.947  41.427  1.00 75.36           C  
ANISOU 2294  CG2 THR A 381     7926   9558  11151   -347  -1137   -117       C  
ATOM   2295  N   THR A 382      43.365  74.926  41.311  1.00 81.88           N  
ANISOU 2295  N   THR A 382     8557  10589  11965   -625  -1018   -465       N  
ATOM   2296  CA  THR A 382      43.342  73.466  41.311  1.00 86.52           C  
ANISOU 2296  CA  THR A 382     9153  11138  12581   -747  -1004   -517       C  
ATOM   2297  C   THR A 382      42.779  72.918  40.003  1.00 92.18           C  
ANISOU 2297  C   THR A 382     9862  11908  13256   -734  -1101   -610       C  
ATOM   2298  O   THR A 382      43.374  72.026  39.386  1.00 87.74           O  
ANISOU 2298  O   THR A 382     9387  11283  12666   -739  -1128   -647       O  
ATOM   2299  CB  THR A 382      42.540  72.952  42.509  1.00 80.38           C  
ANISOU 2299  CB  THR A 382     8269  10394  11879   -870   -968   -527       C  
ATOM   2300  OG1 THR A 382      41.414  73.808  42.743  1.00 85.52           O  
ANISOU 2300  OG1 THR A 382     8787  11193  12516   -814   -994   -550       O  
ATOM   2301  CG2 THR A 382      43.412  72.924  43.752  1.00 69.58           C  
ANISOU 2301  CG2 THR A 382     6951   8941  10546   -899   -870   -449       C  
ATOM   2302  N   CYS A 383      41.641  73.449  39.553  1.00 92.14           N  
ANISOU 2302  N   CYS A 383     9754  12021  13232   -696  -1167   -662       N  
ATOM   2303  CA  CYS A 383      41.004  72.925  38.351  1.00 91.04           C  
ANISOU 2303  CA  CYS A 383     9597  11938  13056   -682  -1274   -763       C  
ATOM   2304  C   CYS A 383      41.733  73.304  37.068  1.00 86.36           C  
ANISOU 2304  C   CYS A 383     9099  11366  12347   -530  -1308   -756       C  
ATOM   2305  O   CYS A 383      41.399  72.762  36.008  1.00 90.34           O  
ANISOU 2305  O   CYS A 383     9612  11914  12797   -488  -1402   -853       O  
ATOM   2306  CB  CYS A 383      39.555  73.397  38.286  1.00 94.30           C  
ANISOU 2306  CB  CYS A 383     9857  12493  13479   -681  -1334   -817       C  
ATOM   2307  SG  CYS A 383      38.568  72.858  39.695  1.00 97.94           S  
ANISOU 2307  SG  CYS A 383    10155  13013  14046   -856  -1296   -801       S  
ATOM   2308  N   THR A 384      42.710  74.207  37.128  1.00 82.66           N  
ANISOU 2308  N   THR A 384     8692  10881  11835   -445  -1246   -635       N  
ATOM   2309  CA  THR A 384      43.528  74.536  35.970  1.00 80.69           C  
ANISOU 2309  CA  THR A 384     8510  10686  11463   -313  -1262   -577       C  
ATOM   2310  C   THR A 384      44.906  73.893  36.024  1.00 79.10           C  
ANISOU 2310  C   THR A 384     8405  10426  11223   -306  -1198   -522       C  
ATOM   2311  O   THR A 384      45.674  74.029  35.066  1.00 80.68           O  
ANISOU 2311  O   THR A 384     8643  10714  11298   -187  -1201   -462       O  
ATOM   2312  CB  THR A 384      43.684  76.053  35.832  1.00 81.78           C  
ANISOU 2312  CB  THR A 384     8634  10862  11577   -228  -1267   -441       C  
ATOM   2313  OG1 THR A 384      44.098  76.609  37.085  1.00 81.04           O  
ANISOU 2313  OG1 THR A 384     8553  10662  11577   -286  -1210   -355       O  
ATOM   2314  CG2 THR A 384      42.365  76.683  35.423  1.00 85.62           C  
ANISOU 2314  CG2 THR A 384     9036  11438  12057   -179  -1354   -512       C  
ATOM   2315  N   HIS A 385      45.238  73.207  37.116  1.00 72.09           N  
ANISOU 2315  N   HIS A 385     7547   9417  10426   -419  -1139   -531       N  
ATOM   2316  CA  HIS A 385      46.509  72.516  37.261  1.00 77.43           C  
ANISOU 2316  CA  HIS A 385     8315  10034  11070   -409  -1082   -494       C  
ATOM   2317  C   HIS A 385      46.352  71.055  36.857  1.00 81.13           C  
ANISOU 2317  C   HIS A 385     8840  10462  11525   -419  -1157   -650       C  
ATOM   2318  O   HIS A 385      45.300  70.444  37.067  1.00 80.21           O  
ANISOU 2318  O   HIS A 385     8685  10296  11496   -521  -1230   -757       O  
ATOM   2319  CB  HIS A 385      47.028  72.620  38.699  1.00 84.80           C  
ANISOU 2319  CB  HIS A 385     9264  10848  12108   -513   -988   -413       C  
ATOM   2320  CG  HIS A 385      48.437  72.141  38.871  1.00 86.38           C  
ANISOU 2320  CG  HIS A 385     9551  11002  12267   -487   -923   -350       C  
ATOM   2321  ND1 HIS A 385      48.764  70.807  38.989  1.00 85.47           N  
ANISOU 2321  ND1 HIS A 385     9509  10813  12153   -513   -935   -444       N  
ATOM   2322  CD2 HIS A 385      49.608  72.820  38.915  1.00 82.62           C  
ANISOU 2322  CD2 HIS A 385     9095  10550  11747   -435   -862   -198       C  
ATOM   2323  CE1 HIS A 385      50.073  70.686  39.114  1.00 84.03           C  
ANISOU 2323  CE1 HIS A 385     9387  10625  11915   -458   -870   -365       C  
ATOM   2324  NE2 HIS A 385      50.609  71.893  39.073  1.00 84.68           N  
ANISOU 2324  NE2 HIS A 385     9428  10776  11969   -419   -820   -208       N  
ATOM   2325  N   LYS A 386      47.416  70.501  36.268  1.00 80.48           N  
ANISOU 2325  N   LYS A 386     8843  10405  11330   -305  -1156   -657       N  
ATOM   2326  CA  LYS A 386      47.348  69.143  35.737  1.00 78.39           C  
ANISOU 2326  CA  LYS A 386     8658  10093  11033   -264  -1269   -829       C  
ATOM   2327  C   LYS A 386      47.119  68.123  36.846  1.00 83.63           C  
ANISOU 2327  C   LYS A 386     9363  10555  11856   -441  -1290   -884       C  
ATOM   2328  O   LYS A 386      46.258  67.243  36.731  1.00 87.54           O  
ANISOU 2328  O   LYS A 386     9867  10964  12429   -521  -1424  -1013       O  
ATOM   2329  CB  LYS A 386      48.628  68.822  34.964  1.00 79.02           C  
ANISOU 2329  CB  LYS A 386     8817  10274  10933    -66  -1258   -824       C  
ATOM   2330  CG  LYS A 386      48.684  67.399  34.441  1.00 88.90           C  
ANISOU 2330  CG  LYS A 386    10179  11461  12138     22  -1404  -1027       C  
ATOM   2331  CD  LYS A 386      49.771  67.221  33.395  1.00102.03           C  
ANISOU 2331  CD  LYS A 386    11892  13313  13564    291  -1411  -1044       C  
ATOM   2332  CE  LYS A 386      49.659  65.849  32.737  1.00115.58           C  
ANISOU 2332  CE  LYS A 386    13730  14965  15219    427  -1608  -1293       C  
ATOM   2333  NZ  LYS A 386      50.603  65.675  31.597  1.00121.52           N  
ANISOU 2333  NZ  LYS A 386    14516  15960  15696    746  -1631  -1339       N  
ATOM   2334  N   LEU A 387      47.881  68.226  37.933  1.00 84.64           N  
ANISOU 2334  N   LEU A 387     9513  10606  12040   -513  -1171   -774       N  
ATOM   2335  CA  LEU A 387      47.789  67.255  39.015  1.00 86.62           C  
ANISOU 2335  CA  LEU A 387     9805  10679  12428   -673  -1182   -797       C  
ATOM   2336  C   LEU A 387      46.689  67.583  40.018  1.00 89.69           C  
ANISOU 2336  C   LEU A 387    10075  11043  12959   -860  -1149   -744       C  
ATOM   2337  O   LEU A 387      46.001  66.674  40.495  1.00 89.59           O  
ANISOU 2337  O   LEU A 387    10050  10928  13061  -1012  -1224   -784       O  
ATOM   2338  CB  LEU A 387      49.139  67.146  39.727  1.00 80.96           C  
ANISOU 2338  CB  LEU A 387     9165   9906  11690   -646  -1072   -710       C  
ATOM   2339  CG  LEU A 387      49.252  66.096  40.831  1.00 74.12           C  
ANISOU 2339  CG  LEU A 387     8361   8855  10945   -790  -1080   -720       C  
ATOM   2340  CD1 LEU A 387      48.654  64.769  40.399  1.00 69.40           C  
ANISOU 2340  CD1 LEU A 387     7835   8131  10403   -836  -1268   -869       C  
ATOM   2341  CD2 LEU A 387      50.712  65.921  41.180  1.00 72.50           C  
ANISOU 2341  CD2 LEU A 387     8249   8622  10675   -702   -996   -667       C  
ATOM   2342  N   ALA A 388      46.507  68.863  40.350  1.00 91.87           N  
ANISOU 2342  N   ALA A 388    10261  11420  13228   -844  -1054   -646       N  
ATOM   2343  CA  ALA A 388      45.528  69.230  41.369  1.00 98.32           C  
ANISOU 2343  CA  ALA A 388    10956  12255  14145   -974  -1016   -601       C  
ATOM   2344  C   ALA A 388      44.106  68.913  40.919  1.00102.69           C  
ANISOU 2344  C   ALA A 388    11409  12867  14743  -1048  -1128   -684       C  
ATOM   2345  O   ALA A 388      43.274  68.483  41.727  1.00 95.93           O  
ANISOU 2345  O   ALA A 388    10456  12008  13985  -1203  -1136   -662       O  
ATOM   2346  CB  ALA A 388      45.664  70.712  41.715  1.00 98.46           C  
ANISOU 2346  CB  ALA A 388    10919  12358  14132   -895   -931   -509       C  
ATOM   2347  N   SER A 389      43.809  69.124  39.634  1.00109.96           N  
ANISOU 2347  N   SER A 389    12334  13861  15585   -939  -1217   -766       N  
ATOM   2348  CA  SER A 389      42.478  68.828  39.114  1.00107.47           C  
ANISOU 2348  CA  SER A 389    11922  13603  15309  -1002  -1341   -854       C  
ATOM   2349  C   SER A 389      42.137  67.353  39.253  1.00102.93           C  
ANISOU 2349  C   SER A 389    11376  12891  14842  -1158  -1465   -917       C  
ATOM   2350  O   SER A 389      40.960  67.000  39.394  1.00100.52           O  
ANISOU 2350  O   SER A 389    10951  12615  14628  -1301  -1550   -931       O  
ATOM   2351  CB  SER A 389      42.389  69.258  37.653  1.00110.87           C  
ANISOU 2351  CB  SER A 389    12377  14131  15619   -832  -1421   -937       C  
ATOM   2352  OG  SER A 389      43.467  68.714  36.912  1.00113.69           O  
ANISOU 2352  OG  SER A 389    12878  14437  15882   -707  -1453   -986       O  
ATOM   2353  N   THR A 390      43.148  66.482  39.203  1.00101.37           N  
ANISOU 2353  N   THR A 390    11335  12545  14637  -1133  -1494   -950       N  
ATOM   2354  CA  THR A 390      42.927  65.059  39.435  1.00102.60           C  
ANISOU 2354  CA  THR A 390    11547  12523  14915  -1285  -1640  -1000       C  
ATOM   2355  C   THR A 390      42.280  64.823  40.792  1.00101.00           C  
ANISOU 2355  C   THR A 390    11219  12299  14856  -1523  -1586   -865       C  
ATOM   2356  O   THR A 390      41.328  64.041  40.911  1.00 96.66           O  
ANISOU 2356  O   THR A 390    10595  11699  14433  -1709  -1722   -863       O  
ATOM   2357  CB  THR A 390      44.256  64.306  39.333  1.00102.95           C  
ANISOU 2357  CB  THR A 390    11786  12419  14912  -1186  -1661  -1047       C  
ATOM   2358  OG1 THR A 390      44.600  64.129  37.953  1.00103.02           O  
ANISOU 2358  OG1 THR A 390    11897  12457  14790   -976  -1779  -1200       O  
ATOM   2359  CG2 THR A 390      44.178  62.948  40.023  1.00100.88           C  
ANISOU 2359  CG2 THR A 390    11590  11935  14803  -1372  -1782  -1045       C  
ATOM   2360  N   LEU A 391      42.770  65.510  41.825  1.00100.29           N  
ANISOU 2360  N   LEU A 391    11093  12266  14747  -1518  -1396   -742       N  
ATOM   2361  CA  LEU A 391      42.214  65.335  43.161  1.00100.10           C  
ANISOU 2361  CA  LEU A 391    10939  12270  14823  -1708  -1326   -605       C  
ATOM   2362  C   LEU A 391      40.805  65.910  43.255  1.00 94.63           C  
ANISOU 2362  C   LEU A 391    10025  11782  14149  -1777  -1328   -570       C  
ATOM   2363  O   LEU A 391      39.897  65.262  43.790  1.00 96.56           O  
ANISOU 2363  O   LEU A 391    10134  12055  14498  -1979  -1386   -491       O  
ATOM   2364  CB  LEU A 391      43.137  65.980  44.193  1.00 98.90           C  
ANISOU 2364  CB  LEU A 391    10815  12139  14624  -1643  -1137   -507       C  
ATOM   2365  CG  LEU A 391      42.570  66.100  45.606  1.00 97.58           C  
ANISOU 2365  CG  LEU A 391    10491  12075  14509  -1774  -1034   -366       C  
ATOM   2366  CD1 LEU A 391      42.254  64.730  46.186  1.00 95.49           C  
ANISOU 2366  CD1 LEU A 391    10211  11697  14375  -2005  -1117   -286       C  
ATOM   2367  CD2 LEU A 391      43.555  66.847  46.485  1.00 96.23           C  
ANISOU 2367  CD2 LEU A 391    10371  11917  14276  -1663   -872   -306       C  
ATOM   2368  N   ILE A 392      40.606  67.129  42.747  1.00 87.90           N  
ANISOU 2368  N   ILE A 392     9124  11082  13193  -1610  -1274   -614       N  
ATOM   2369  CA  ILE A 392      39.280  67.743  42.780  1.00 93.22           C  
ANISOU 2369  CA  ILE A 392     9590  11968  13862  -1635  -1283   -600       C  
ATOM   2370  C   ILE A 392      38.271  66.846  42.079  1.00101.26           C  
ANISOU 2370  C   ILE A 392    10536  12973  14965  -1779  -1466   -654       C  
ATOM   2371  O   ILE A 392      37.135  66.683  42.539  1.00102.97           O  
ANISOU 2371  O   ILE A 392    10550  13331  15244  -1927  -1493   -581       O  
ATOM   2372  CB  ILE A 392      39.321  69.146  42.145  1.00 91.75           C  
ANISOU 2372  CB  ILE A 392     9406  11902  13554  -1413  -1238   -658       C  
ATOM   2373  CG1 ILE A 392      40.315  70.045  42.884  1.00 88.34           C  
ANISOU 2373  CG1 ILE A 392     9046  11455  13064  -1291  -1094   -593       C  
ATOM   2374  CG2 ILE A 392      37.931  69.771  42.137  1.00 85.69           C  
ANISOU 2374  CG2 ILE A 392     8430  11358  12770  -1411  -1262   -663       C  
ATOM   2375  CD1 ILE A 392      39.967  70.297  44.334  1.00 89.33           C  
ANISOU 2375  CD1 ILE A 392     9044  11688  13210  -1345   -990   -495       C  
ATOM   2376  N   PHE A 393      38.676  66.244  40.960  1.00105.52           N  
ANISOU 2376  N   PHE A 393    11232  13356  15503  -1728  -1608   -781       N  
ATOM   2377  CA  PHE A 393      37.807  65.302  40.262  1.00115.49           C  
ANISOU 2377  CA  PHE A 393    12459  14560  16863  -1859  -1827   -853       C  
ATOM   2378  C   PHE A 393      37.472  64.108  41.148  1.00107.97           C  
ANISOU 2378  C   PHE A 393    11453  13491  16080  -2137  -1906   -737       C  
ATOM   2379  O   PHE A 393      36.318  63.666  41.198  1.00104.97           O  
ANISOU 2379  O   PHE A 393    10904  13174  15807  -2328  -2026   -685       O  
ATOM   2380  CB  PHE A 393      38.478  64.851  38.962  1.00121.76           C  
ANISOU 2380  CB  PHE A 393    13461  15202  17600  -1706  -1973  -1029       C  
ATOM   2381  CG  PHE A 393      37.610  63.989  38.090  1.00123.30           C  
ANISOU 2381  CG  PHE A 393    13643  15325  17880  -1793  -2234  -1145       C  
ATOM   2382  CD1 PHE A 393      36.515  64.526  37.433  1.00124.52           C  
ANISOU 2382  CD1 PHE A 393    13650  15653  18010  -1772  -2295  -1196       C  
ATOM   2383  CD2 PHE A 393      37.901  62.647  37.912  1.00124.72           C  
ANISOU 2383  CD2 PHE A 393    13969  15252  18169  -1885  -2441  -1212       C  
ATOM   2384  CE1 PHE A 393      35.721  63.738  36.623  1.00130.40           C  
ANISOU 2384  CE1 PHE A 393    14380  16326  18839  -1852  -2554  -1308       C  
ATOM   2385  CE2 PHE A 393      37.113  61.855  37.103  1.00128.38           C  
ANISOU 2385  CE2 PHE A 393    14433  15621  18724  -1962  -2720  -1330       C  
ATOM   2386  CZ  PHE A 393      36.020  62.401  36.459  1.00132.81           C  
ANISOU 2386  CZ  PHE A 393    14836  16363  19263  -1951  -2775  -1376       C  
ATOM   2387  N   LYS A 394      38.465  63.583  41.870  1.00108.05           N  
ANISOU 2387  N   LYS A 394    11594  13339  16120  -2171  -1847   -674       N  
ATOM   2388  CA  LYS A 394      38.207  62.456  42.759  1.00106.78           C  
ANISOU 2388  CA  LYS A 394    11390  13057  16123  -2440  -1925   -535       C  
ATOM   2389  C   LYS A 394      37.279  62.849  43.901  1.00100.79           C  
ANISOU 2389  C   LYS A 394    10357  12547  15390  -2595  -1793   -333       C  
ATOM   2390  O   LYS A 394      36.464  62.033  44.348  1.00100.96           O  
ANISOU 2390  O   LYS A 394    10236  12570  15552  -2857  -1902   -196       O  
ATOM   2391  CB  LYS A 394      39.528  61.898  43.300  1.00109.34           C  
ANISOU 2391  CB  LYS A 394    11922  13169  16454  -2412  -1877   -515       C  
ATOM   2392  CG  LYS A 394      39.367  60.868  44.411  1.00113.71           C  
ANISOU 2392  CG  LYS A 394    12430  13610  17163  -2682  -1922   -331       C  
ATOM   2393  CD  LYS A 394      40.489  59.838  44.394  1.00117.37           C  
ANISOU 2393  CD  LYS A 394    13156  13761  17679  -2669  -2031   -387       C  
ATOM   2394  CE  LYS A 394      40.213  58.711  45.383  1.00123.10           C  
ANISOU 2394  CE  LYS A 394    13844  14343  18586  -2965  -2129   -193       C  
ATOM   2395  NZ  LYS A 394      41.097  57.528  45.170  1.00123.59           N  
ANISOU 2395  NZ  LYS A 394    14176  14054  18730  -2965  -2326   -276       N  
ATOM   2396  N   LEU A 395      37.366  64.098  44.366  1.00 92.83           N  
ANISOU 2396  N   LEU A 395     9264  11762  14245  -2430  -1577   -309       N  
ATOM   2397  CA  LEU A 395      36.533  64.531  45.483  1.00 94.86           C  
ANISOU 2397  CA  LEU A 395     9259  12297  14485  -2517  -1448   -137       C  
ATOM   2398  C   LEU A 395      35.062  64.626  45.094  1.00104.11           C  
ANISOU 2398  C   LEU A 395    10185  13686  15684  -2614  -1543   -117       C  
ATOM   2399  O   LEU A 395      34.186  64.504  45.958  1.00107.96           O  
ANISOU 2399  O   LEU A 395    10421  14400  16198  -2768  -1500     61       O  
ATOM   2400  CB  LEU A 395      37.035  65.873  46.014  1.00 90.06           C  
ANISOU 2400  CB  LEU A 395     8653  11846  13720  -2275  -1236   -155       C  
ATOM   2401  CG  LEU A 395      38.352  65.839  46.794  1.00 85.39           C  
ANISOU 2401  CG  LEU A 395     8230  11110  13105  -2212  -1113   -116       C  
ATOM   2402  CD1 LEU A 395      39.131  67.130  46.603  1.00 83.86           C  
ANISOU 2402  CD1 LEU A 395     8144  10939  12779  -1941  -1001   -215       C  
ATOM   2403  CD2 LEU A 395      38.089  65.590  48.270  1.00 77.12           C  
ANISOU 2403  CD2 LEU A 395     7023  10207  12071  -2337  -1002     78       C  
ATOM   2404  N   ILE A 396      34.769  64.836  43.815  1.00111.94           N  
ANISOU 2404  N   ILE A 396    11232  14641  16659  -2521  -1671   -286       N  
ATOM   2405  CA  ILE A 396      33.381  64.903  43.365  1.00113.86           C  
ANISOU 2405  CA  ILE A 396    11246  15085  16931  -2609  -1778   -280       C  
ATOM   2406  C   ILE A 396      32.839  63.522  43.022  1.00117.35           C  
ANISOU 2406  C   ILE A 396    11664  15357  17567  -2894  -2028   -235       C  
ATOM   2407  O   ILE A 396      31.708  63.186  43.384  1.00113.34           O  
ANISOU 2407  O   ILE A 396    10894  15026  17142  -3110  -2091    -85       O  
ATOM   2408  CB  ILE A 396      33.263  65.864  42.168  1.00106.97           C  
ANISOU 2408  CB  ILE A 396    10432  14271  15939  -2361  -1803   -479       C  
ATOM   2409  CG1 ILE A 396      33.615  67.290  42.595  1.00102.67           C  
ANISOU 2409  CG1 ILE A 396     9880  13901  15228  -2108  -1592   -492       C  
ATOM   2410  CG2 ILE A 396      31.853  65.815  41.598  1.00108.87           C  
ANISOU 2410  CG2 ILE A 396    10453  14694  16219  -2454  -1942   -492       C  
ATOM   2411  CD1 ILE A 396      33.747  68.250  41.440  1.00100.51           C  
ANISOU 2411  CD1 ILE A 396     9709  13640  14842  -1860  -1616   -661       C  
ATOM   2412  N   ASN A 397      33.639  62.709  42.327  1.00133.81           N  
ANISOU 2412  N   ASN A 397    14014  17103  19724  -2892  -2188   -359       N  
ATOM   2413  CA  ASN A 397      33.201  61.382  41.908  1.00153.89           C  
ANISOU 2413  CA  ASN A 397    16583  19424  22465  -3138  -2481   -351       C  
ATOM   2414  C   ASN A 397      32.871  60.467  43.077  1.00155.57           C  
ANISOU 2414  C   ASN A 397    16657  19612  22841  -3466  -2513    -82       C  
ATOM   2415  O   ASN A 397      32.098  59.518  42.902  1.00167.26           O  
ANISOU 2415  O   ASN A 397    18049  20996  24507  -3735  -2761     -1       O  
ATOM   2416  CB  ASN A 397      34.273  60.728  41.042  1.00170.60           C  
ANISOU 2416  CB  ASN A 397    19037  21188  24595  -3012  -2641   -554       C  
ATOM   2417  CG  ASN A 397      34.251  61.229  39.617  1.00183.22           C  
ANISOU 2417  CG  ASN A 397    20735  22801  26081  -2766  -2729   -803       C  
ATOM   2418  OD1 ASN A 397      33.710  62.297  39.326  1.00186.03           O  
ANISOU 2418  OD1 ASN A 397    20950  23417  26317  -2636  -2611   -832       O  
ATOM   2419  ND2 ASN A 397      34.842  60.457  38.715  1.00189.04           N  
ANISOU 2419  ND2 ASN A 397    21717  23266  26843  -2680  -2947   -988       N  
ATOM   2420  N   ASN A 398      33.442  60.714  44.253  1.00145.80           N  
ANISOU 2420  N   ASN A 398    15399  18455  21545  -3455  -2285     67       N  
ATOM   2421  CA  ASN A 398      33.148  59.900  45.426  1.00141.24           C  
ANISOU 2421  CA  ASN A 398    14672  17894  21098  -3755  -2292    352       C  
ATOM   2422  C   ASN A 398      31.678  60.027  45.807  1.00139.84           C  
ANISOU 2422  C   ASN A 398    14109  18069  20954  -3956  -2295    557       C  
ATOM   2423  O   ASN A 398      31.254  61.063  46.331  1.00131.39           O  
ANISOU 2423  O   ASN A 398    12828  17375  19720  -3822  -2069    610       O  
ATOM   2424  CB  ASN A 398      34.051  60.307  46.597  1.00135.56           C  
ANISOU 2424  CB  ASN A 398    13997  17242  20267  -3650  -2024    452       C  
ATOM   2425  CG  ASN A 398      33.994  59.327  47.755  1.00134.30           C  
ANISOU 2425  CG  ASN A 398    13745  17042  20239  -3942  -2044    740       C  
ATOM   2426  OD1 ASN A 398      32.925  59.043  48.293  1.00134.51           O  
ANISOU 2426  OD1 ASN A 398    13476  17296  20337  -4186  -2073    981       O  
ATOM   2427  ND2 ASN A 398      35.152  58.806  48.146  1.00135.28           N  
ANISOU 2427  ND2 ASN A 398    14114  16895  20392  -3919  -2030    734       N  
ATOM   2428  N   LYS A 399      30.898  58.974  45.548  1.00146.70           N  
ANISOU 2428  N   LYS A 399    14897  18824  22019  -4254  -2556    664       N  
ATOM   2429  CA  LYS A 399      29.472  59.007  45.857  1.00153.45           C  
ANISOU 2429  CA  LYS A 399    15433  20022  22848  -4387  -2519    843       C  
ATOM   2430  C   LYS A 399      29.215  58.948  47.358  1.00160.36           C  
ANISOU 2430  C   LYS A 399    16106  21173  23650  -4480  -2290   1148       C  
ATOM   2431  O   LYS A 399      28.220  59.504  47.836  1.00165.01           O  
ANISOU 2431  O   LYS A 399    16378  22186  24131  -4474  -2152   1285       O  
ATOM   2432  CB  LYS A 399      28.754  57.853  45.154  1.00151.90           C  
ANISOU 2432  CB  LYS A 399    15304  19599  22812  -4585  -2806    839       C  
ATOM   2433  CG  LYS A 399      28.887  57.860  43.636  1.00146.59           C  
ANISOU 2433  CG  LYS A 399    14821  18682  22193  -4474  -3056    527       C  
ATOM   2434  CD  LYS A 399      28.054  56.755  43.001  1.00143.28           C  
ANISOU 2434  CD  LYS A 399    14440  18076  21924  -4664  -3345    534       C  
ATOM   2435  CE  LYS A 399      28.136  56.797  41.483  1.00136.54           C  
ANISOU 2435  CE  LYS A 399    13766  17016  21097  -4518  -3597    209       C  
ATOM   2436  NZ  LYS A 399      27.206  55.819  40.848  1.00135.82           N  
ANISOU 2436  NZ  LYS A 399    13682  16779  21144  -4692  -3885    212       N  
ATOM   2437  N   GLN A 400      30.094  58.285  48.114  1.00161.80           N  
ANISOU 2437  N   GLN A 400    16464  21138  23874  -4541  -2250   1254       N  
ATOM   2438  CA  GLN A 400      29.897  58.135  49.552  1.00161.99           C  
ANISOU 2438  CA  GLN A 400    16314  21411  23826  -4623  -2050   1551       C  
ATOM   2439  C   GLN A 400      30.121  59.432  50.321  1.00152.85           C  
ANISOU 2439  C   GLN A 400    14975  20641  22462  -4404  -1758   1568       C  
ATOM   2440  O   GLN A 400      29.811  59.483  51.517  1.00149.67           O  
ANISOU 2440  O   GLN A 400    14378  20535  21953  -4423  -1578   1802       O  
ATOM   2441  CB  GLN A 400      30.816  57.035  50.098  1.00164.89           C  
ANISOU 2441  CB  GLN A 400    16937  21417  24296  -4738  -2112   1648       C  
ATOM   2442  CG  GLN A 400      30.575  55.645  49.499  1.00170.34           C  
ANISOU 2442  CG  GLN A 400    17808  21725  25187  -4949  -2422   1663       C  
ATOM   2443  CD  GLN A 400      31.150  55.480  48.100  1.00171.25           C  
ANISOU 2443  CD  GLN A 400    18215  21458  25395  -4852  -2659   1334       C  
ATOM   2444  OE1 GLN A 400      31.673  56.428  47.514  1.00170.27           O  
ANISOU 2444  OE1 GLN A 400    18141  21364  25188  -4641  -2594   1105       O  
ATOM   2445  NE2 GLN A 400      31.045  54.271  47.556  1.00172.05           N  
ANISOU 2445  NE2 GLN A 400    18505  21205  25661  -4993  -2951   1314       N  
ATOM   2446  N   GLU A 401      30.645  60.475  49.672  1.00147.49           N  
ANISOU 2446  N   GLU A 401    14352  19971  21718  -4185  -1723   1331       N  
ATOM   2447  CA  GLU A 401      30.800  61.802  50.264  1.00139.97           C  
ANISOU 2447  CA  GLU A 401    13285  19364  20533  -3893  -1458   1284       C  
ATOM   2448  C   GLU A 401      29.972  62.773  49.429  1.00140.61           C  
ANISOU 2448  C   GLU A 401    13240  19677  20508  -3709  -1464   1109       C  
ATOM   2449  O   GLU A 401      30.521  63.550  48.633  1.00132.64           O  
ANISOU 2449  O   GLU A 401    12452  18528  19415  -3438  -1444    833       O  
ATOM   2450  CB  GLU A 401      32.268  62.222  50.322  1.00129.93           C  
ANISOU 2450  CB  GLU A 401    12360  17826  19182  -3636  -1341   1090       C  
ATOM   2451  CG  GLU A 401      33.174  61.225  51.039  1.00124.64           C  
ANISOU 2451  CG  GLU A 401    11852  16886  18620  -3798  -1354   1231       C  
ATOM   2452  CD  GLU A 401      32.998  61.242  52.549  1.00118.44           C  
ANISOU 2452  CD  GLU A 401    10835  16419  17746  -3855  -1166   1508       C  
ATOM   2453  OE1 GLU A 401      32.445  62.231  53.075  1.00115.93           O  
ANISOU 2453  OE1 GLU A 401    10287  16523  17238  -3672   -990   1530       O  
ATOM   2454  OE2 GLU A 401      33.409  60.262  53.207  1.00113.67           O  
ANISOU 2454  OE2 GLU A 401    10282  15654  17255  -4066  -1205   1702       O  
ATOM   2455  N   PRO A 402      28.642  62.757  49.583  1.00152.13           N  
ANISOU 2455  N   PRO A 402    14333  21506  21962  -3852  -1494   1279       N  
ATOM   2456  CA  PRO A 402      27.791  63.577  48.712  1.00154.63           C  
ANISOU 2456  CA  PRO A 402    14528  22029  22194  -3695  -1532   1112       C  
ATOM   2457  C   PRO A 402      27.817  65.047  49.093  1.00153.57           C  
ANISOU 2457  C   PRO A 402    14339  22213  21795  -3305  -1306    983       C  
ATOM   2458  O   PRO A 402      27.758  65.920  48.222  1.00162.62           O  
ANISOU 2458  O   PRO A 402    15583  23346  22859  -3064  -1325    740       O  
ATOM   2459  CB  PRO A 402      26.401  62.966  48.916  1.00156.52           C  
ANISOU 2459  CB  PRO A 402    14472  22519  22480  -3919  -1597   1328       C  
ATOM   2460  CG  PRO A 402      26.434  62.464  50.322  1.00158.49           C  
ANISOU 2460  CG  PRO A 402    14635  22905  22680  -4009  -1441   1604       C  
ATOM   2461  CD  PRO A 402      27.857  62.028  50.596  1.00157.28           C  
ANISOU 2461  CD  PRO A 402    14780  22368  22610  -4039  -1435   1578       C  
ATOM   2462  N   GLU A 403      27.902  65.330  50.396  1.00143.31           N  
ANISOU 2462  N   GLU A 403    12891  21199  20361  -3231  -1111   1144       N  
ATOM   2463  CA  GLU A 403      27.964  66.714  50.848  1.00129.84           C  
ANISOU 2463  CA  GLU A 403    11153  19774  18405  -2838   -929   1008       C  
ATOM   2464  C   GLU A 403      29.187  67.430  50.288  1.00115.02           C  
ANISOU 2464  C   GLU A 403     9672  17532  16499  -2573   -909    726       C  
ATOM   2465  O   GLU A 403      29.144  68.644  50.062  1.00103.05           O  
ANISOU 2465  O   GLU A 403     8190  16133  14830  -2256   -857    540       O  
ATOM   2466  CB  GLU A 403      27.957  66.758  52.377  1.00134.53           C  
ANISOU 2466  CB  GLU A 403    11545  20709  18862  -2801   -743   1226       C  
ATOM   2467  CG  GLU A 403      27.869  68.156  52.971  1.00140.17           C  
ANISOU 2467  CG  GLU A 403    12187  21766  19306  -2379   -586   1092       C  
ATOM   2468  CD  GLU A 403      28.248  68.185  54.442  1.00143.49           C  
ANISOU 2468  CD  GLU A 403    12519  22413  19589  -2292   -412   1249       C  
ATOM   2469  OE1 GLU A 403      27.992  67.180  55.141  1.00146.49           O  
ANISOU 2469  OE1 GLU A 403    12704  22923  20031  -2577   -388   1548       O  
ATOM   2470  OE2 GLU A 403      28.821  69.200  54.895  1.00139.75           O  
ANISOU 2470  OE2 GLU A 403    12176  21972  18950  -1942   -316   1078       O  
ATOM   2471  N   SER A 404      30.273  66.695  50.033  1.00117.20           N  
ANISOU 2471  N   SER A 404    10243  17367  16919  -2698   -965    699       N  
ATOM   2472  CA  SER A 404      31.491  67.319  49.522  1.00115.72           C  
ANISOU 2472  CA  SER A 404    10407  16861  16701  -2465   -941    468       C  
ATOM   2473  C   SER A 404      31.348  67.679  48.049  1.00112.66           C  
ANISOU 2473  C   SER A 404    10147  16318  16340  -2378  -1077    254       C  
ATOM   2474  O   SER A 404      31.738  68.775  47.627  1.00108.62           O  
ANISOU 2474  O   SER A 404     9771  15780  15720  -2101  -1038     76       O  
ATOM   2475  CB  SER A 404      32.688  66.390  49.732  1.00117.80           C  
ANISOU 2475  CB  SER A 404    10923  16747  17089  -2608   -955    513       C  
ATOM   2476  OG  SER A 404      32.604  65.246  48.897  1.00122.24           O  
ANISOU 2476  OG  SER A 404    11568  17039  17840  -2862  -1151    522       O  
ATOM   2477  N   ARG A 405      30.794  66.766  47.246  1.00116.77           N  
ANISOU 2477  N   ARG A 405    10629  16728  17008  -2613  -1256    274       N  
ATOM   2478  CA  ARG A 405      30.640  67.041  45.821  1.00119.15           C  
ANISOU 2478  CA  ARG A 405    11050  16896  17326  -2523  -1395     68       C  
ATOM   2479  C   ARG A 405      29.605  68.131  45.568  1.00115.92           C  
ANISOU 2479  C   ARG A 405    10432  16833  16779  -2337  -1369     -1       C  
ATOM   2480  O   ARG A 405      29.666  68.812  44.539  1.00116.33           O  
ANISOU 2480  O   ARG A 405    10609  16814  16779  -2151  -1425   -191       O  
ATOM   2481  CB  ARG A 405      30.265  65.761  45.068  1.00123.26           C  
ANISOU 2481  CB  ARG A 405    11581  17212  18041  -2810  -1625     93       C  
ATOM   2482  CG  ARG A 405      28.795  65.367  45.153  1.00124.39           C  
ANISOU 2482  CG  ARG A 405    11378  17637  18247  -3029  -1722    243       C  
ATOM   2483  CD  ARG A 405      28.368  64.608  43.905  1.00124.22           C  
ANISOU 2483  CD  ARG A 405    11416  17405  18379  -3183  -1992    144       C  
ATOM   2484  NE  ARG A 405      27.012  64.077  44.012  1.00132.33           N  
ANISOU 2484  NE  ARG A 405    12109  18667  19505  -3449  -2116    319       N  
ATOM   2485  CZ  ARG A 405      25.912  64.771  43.736  1.00142.94           C  
ANISOU 2485  CZ  ARG A 405    13197  20357  20755  -3369  -2108    299       C  
ATOM   2486  NH1 ARG A 405      26.006  66.028  43.325  1.00145.94           N  
ANISOU 2486  NH1 ARG A 405    13640  20863  20948  -3026  -1994    103       N  
ATOM   2487  NH2 ARG A 405      24.718  64.205  43.860  1.00147.99           N  
ANISOU 2487  NH2 ARG A 405    13515  21218  21495  -3638  -2229    485       N  
ATOM   2488  N   ASN A 406      28.657  68.316  46.491  1.00115.42           N  
ANISOU 2488  N   ASN A 406    10048  17165  16641  -2368  -1285    155       N  
ATOM   2489  CA  ASN A 406      27.678  69.388  46.336  1.00113.15           C  
ANISOU 2489  CA  ASN A 406     9556  17235  16199  -2152  -1260     80       C  
ATOM   2490  C   ASN A 406      28.312  70.750  46.577  1.00106.61           C  
ANISOU 2490  C   ASN A 406     8881  16425  15201  -1782  -1141    -72       C  
ATOM   2491  O   ASN A 406      28.042  71.708  45.842  1.00106.17           O  
ANISOU 2491  O   ASN A 406     8866  16415  15059  -1556  -1185   -239       O  
ATOM   2492  CB  ASN A 406      26.498  69.179  47.286  1.00116.07           C  
ANISOU 2492  CB  ASN A 406     9517  18072  16514  -2267  -1203    300       C  
ATOM   2493  CG  ASN A 406      25.648  67.983  46.909  1.00110.49           C  
ANISOU 2493  CG  ASN A 406     8614  17382  15984  -2638  -1363    459       C  
ATOM   2494  OD1 ASN A 406      25.663  67.530  45.764  1.00100.74           O  
ANISOU 2494  OD1 ASN A 406     7524  15868  14885  -2745  -1542    346       O  
ATOM   2495  ND2 ASN A 406      24.887  67.473  47.873  1.00113.06           N  
ANISOU 2495  ND2 ASN A 406     8601  18052  16307  -2833  -1313    732       N  
ATOM   2496  N   LEU A 407      29.146  70.863  47.612  1.00102.47           N  
ANISOU 2496  N   LEU A 407     8442  15860  14632  -1717  -1009    -11       N  
ATOM   2497  CA  LEU A 407      29.836  72.123  47.861  1.00102.48           C  
ANISOU 2497  CA  LEU A 407     8611  15826  14499  -1384   -934   -152       C  
ATOM   2498  C   LEU A 407      30.841  72.427  46.760  1.00101.67           C  
ANISOU 2498  C   LEU A 407     8845  15327  14456  -1305  -1006   -314       C  
ATOM   2499  O   LEU A 407      31.025  73.589  46.379  1.00107.86           O  
ANISOU 2499  O   LEU A 407     9739  16092  15151  -1044  -1023   -454       O  
ATOM   2500  CB  LEU A 407      30.533  72.086  49.218  1.00101.81           C  
ANISOU 2500  CB  LEU A 407     8546  15773  14365  -1346   -795    -50       C  
ATOM   2501  CG  LEU A 407      31.129  73.424  49.661  1.00101.09           C  
ANISOU 2501  CG  LEU A 407     8594  15681  14134   -995   -742   -187       C  
ATOM   2502  CD1 LEU A 407      30.043  74.476  49.847  1.00101.72           C  
ANISOU 2502  CD1 LEU A 407     8462  16147  14039   -727   -756   -266       C  
ATOM   2503  CD2 LEU A 407      31.928  73.241  50.935  1.00102.66           C  
ANISOU 2503  CD2 LEU A 407     8839  15864  14303   -980   -623    -94       C  
ATOM   2504  N   LEU A 408      31.500  71.395  46.237  1.00 94.67           N  
ANISOU 2504  N   LEU A 408     8122  14134  13716  -1521  -1061   -290       N  
ATOM   2505  CA  LEU A 408      32.465  71.610  45.166  1.00 90.10           C  
ANISOU 2505  CA  LEU A 408     7835  13230  13169  -1438  -1123   -426       C  
ATOM   2506  C   LEU A 408      31.782  72.106  43.898  1.00 88.80           C  
ANISOU 2506  C   LEU A 408     7654  13113  12974  -1342  -1241   -557       C  
ATOM   2507  O   LEU A 408      32.283  73.021  43.235  1.00 89.36           O  
ANISOU 2507  O   LEU A 408     7889  13082  12982  -1137  -1259   -667       O  
ATOM   2508  CB  LEU A 408      33.238  70.322  44.893  1.00 87.78           C  
ANISOU 2508  CB  LEU A 408     7701  12636  13015  -1661  -1172   -385       C  
ATOM   2509  CG  LEU A 408      34.354  70.031  45.892  1.00 88.38           C  
ANISOU 2509  CG  LEU A 408     7904  12567  13109  -1688  -1059   -301       C  
ATOM   2510  CD1 LEU A 408      34.791  68.586  45.780  1.00 93.83           C  
ANISOU 2510  CD1 LEU A 408     8689  13018  13944  -1937  -1132   -238       C  
ATOM   2511  CD2 LEU A 408      35.527  70.975  45.667  1.00 82.98           C  
ANISOU 2511  CD2 LEU A 408     7454  11718  12355  -1460  -1007   -397       C  
ATOM   2512  N   LEU A 409      30.629  71.528  43.555  1.00 85.79           N  
ANISOU 2512  N   LEU A 409     7065  12893  12638  -1493  -1332   -530       N  
ATOM   2513  CA  LEU A 409      29.967  71.886  42.306  1.00 85.45           C  
ANISOU 2513  CA  LEU A 409     7007  12890  12572  -1414  -1458   -658       C  
ATOM   2514  C   LEU A 409      29.270  73.240  42.389  1.00 87.02           C  
ANISOU 2514  C   LEU A 409     7085  13358  12621  -1151  -1428   -726       C  
ATOM   2515  O   LEU A 409      29.233  73.971  41.393  1.00 89.15           O  
ANISOU 2515  O   LEU A 409     7454  13583  12837   -982  -1501   -853       O  
ATOM   2516  CB  LEU A 409      28.969  70.796  41.913  1.00 86.57           C  
ANISOU 2516  CB  LEU A 409     6966  13101  12827  -1673  -1591   -610       C  
ATOM   2517  CG  LEU A 409      29.594  69.496  41.393  1.00 88.34           C  
ANISOU 2517  CG  LEU A 409     7363  12995  13207  -1890  -1708   -609       C  
ATOM   2518  CD1 LEU A 409      28.539  68.414  41.222  1.00 86.58           C  
ANISOU 2518  CD1 LEU A 409     6938  12838  13123  -2175  -1868   -531       C  
ATOM   2519  CD2 LEU A 409      30.358  69.722  40.095  1.00 89.41           C  
ANISOU 2519  CD2 LEU A 409     7770  12888  13314  -1733  -1788   -787       C  
ATOM   2520  N   LYS A 410      28.717  73.593  43.551  1.00 85.75           N  
ANISOU 2520  N   LYS A 410     6714  13488  12380  -1095  -1333   -644       N  
ATOM   2521  CA  LYS A 410      28.079  74.898  43.692  1.00 85.36           C  
ANISOU 2521  CA  LYS A 410     6565  13694  12174   -804  -1325   -730       C  
ATOM   2522  C   LYS A 410      29.088  76.019  43.476  1.00 86.33           C  
ANISOU 2522  C   LYS A 410     6966  13595  12242   -549  -1322   -839       C  
ATOM   2523  O   LYS A 410      28.827  76.973  42.735  1.00 90.80           O  
ANISOU 2523  O   LYS A 410     7587  14173  12740   -345  -1404   -954       O  
ATOM   2524  CB  LYS A 410      27.418  75.020  45.067  1.00 91.51           C  
ANISOU 2524  CB  LYS A 410     7073  14844  12851   -758  -1221   -625       C  
ATOM   2525  CG  LYS A 410      26.921  76.423  45.388  1.00100.85           C  
ANISOU 2525  CG  LYS A 410     8190  16279  13852   -395  -1221   -739       C  
ATOM   2526  CD  LYS A 410      26.352  76.515  46.795  1.00112.13           C  
ANISOU 2526  CD  LYS A 410     9352  18105  15147   -309  -1114   -643       C  
ATOM   2527  CE  LYS A 410      25.973  77.947  47.138  1.00119.51           C  
ANISOU 2527  CE  LYS A 410    10263  19258  15888    104  -1143   -792       C  
ATOM   2528  NZ  LYS A 410      25.390  78.063  48.502  1.00126.12           N  
ANISOU 2528  NZ  LYS A 410    10827  20536  16556    242  -1043   -717       N  
ATOM   2529  N   ASN A 411      30.259  75.913  44.105  1.00 84.30           N  
ANISOU 2529  N   ASN A 411     6885  13126  12021   -567  -1242   -789       N  
ATOM   2530  CA  ASN A 411      31.289  76.924  43.914  1.00 87.04           C  
ANISOU 2530  CA  ASN A 411     7488  13244  12339   -364  -1256   -860       C  
ATOM   2531  C   ASN A 411      31.917  76.855  42.530  1.00 81.11           C  
ANISOU 2531  C   ASN A 411     6946  12226  11647   -398  -1336   -909       C  
ATOM   2532  O   ASN A 411      32.477  77.854  42.068  1.00 75.03           O  
ANISOU 2532  O   ASN A 411     6343  11323  10841   -220  -1384   -958       O  
ATOM   2533  CB  ASN A 411      32.366  76.784  44.990  1.00 90.18           C  
ANISOU 2533  CB  ASN A 411     7999  13505  12762   -385  -1153   -787       C  
ATOM   2534  CG  ASN A 411      31.877  77.213  46.354  1.00 96.35           C  
ANISOU 2534  CG  ASN A 411     8611  14561  13439   -248  -1085   -765       C  
ATOM   2535  OD1 ASN A 411      32.054  78.362  46.752  1.00 96.62           O  
ANISOU 2535  OD1 ASN A 411     8715  14609  13389     14  -1118   -843       O  
ATOM   2536  ND2 ASN A 411      31.244  76.294  47.074  1.00104.10           N  
ANISOU 2536  ND2 ASN A 411     9363  15770  14420   -416  -1007   -654       N  
ATOM   2537  N   LEU A 412      31.822  75.709  41.856  1.00 81.26           N  
ANISOU 2537  N   LEU A 412     6952  12173  11750   -614  -1367   -891       N  
ATOM   2538  CA  LEU A 412      32.430  75.558  40.538  1.00 82.79           C  
ANISOU 2538  CA  LEU A 412     7335  12151  11972   -620  -1444   -946       C  
ATOM   2539  C   LEU A 412      31.651  76.318  39.470  1.00 85.36           C  
ANISOU 2539  C   LEU A 412     7623  12585  12226   -468  -1553  -1043       C  
ATOM   2540  O   LEU A 412      32.233  77.073  38.683  1.00 83.20           O  
ANISOU 2540  O   LEU A 412     7513  12191  11908   -321  -1595  -1075       O  
ATOM   2541  CB  LEU A 412      32.524  74.073  40.179  1.00 83.96           C  
ANISOU 2541  CB  LEU A 412     7489  12186  12224   -865  -1479   -925       C  
ATOM   2542  CG  LEU A 412      33.337  73.689  38.941  1.00 86.31           C  
ANISOU 2542  CG  LEU A 412     7995  12264  12534   -859  -1552   -986       C  
ATOM   2543  CD1 LEU A 412      34.752  74.211  39.058  1.00 86.47           C  
ANISOU 2543  CD1 LEU A 412     8226  12106  12523   -752  -1473   -946       C  
ATOM   2544  CD2 LEU A 412      33.343  72.179  38.749  1.00 87.79           C  
ANISOU 2544  CD2 LEU A 412     8190  12335  12831  -1084  -1621   -986       C  
ATOM   2545  N   PHE A 413      30.332  76.140  39.433  1.00 87.82           N  
ANISOU 2545  N   PHE A 413     7707  13139  12523   -504  -1602  -1074       N  
ATOM   2546  CA  PHE A 413      29.514  76.673  38.353  1.00 87.95           C  
ANISOU 2546  CA  PHE A 413     7674  13265  12478   -383  -1717  -1173       C  
ATOM   2547  C   PHE A 413      28.775  77.949  38.727  1.00 99.00           C  
ANISOU 2547  C   PHE A 413     8968  14881  13766   -143  -1729  -1218       C  
ATOM   2548  O   PHE A 413      28.617  78.836  37.881  1.00108.19           O  
ANISOU 2548  O   PHE A 413    10205  16039  14865     40  -1816  -1291       O  
ATOM   2549  CB  PHE A 413      28.515  75.611  37.890  1.00 88.42           C  
ANISOU 2549  CB  PHE A 413     7555  13442  12600   -576  -1800  -1192       C  
ATOM   2550  CG  PHE A 413      29.168  74.412  37.261  1.00 99.10           C  
ANISOU 2550  CG  PHE A 413     9043  14555  14054   -763  -1852  -1194       C  
ATOM   2551  CD1 PHE A 413      29.553  74.436  35.926  1.00101.66           C  
ANISOU 2551  CD1 PHE A 413     9533  14743  14349   -680  -1948  -1288       C  
ATOM   2552  CD2 PHE A 413      29.406  73.264  37.999  1.00100.62           C  
ANISOU 2552  CD2 PHE A 413     9203  14668  14361  -1002  -1819  -1103       C  
ATOM   2553  CE1 PHE A 413      30.160  73.339  35.344  1.00 92.39           C  
ANISOU 2553  CE1 PHE A 413     8490  13367  13246   -805  -2015  -1316       C  
ATOM   2554  CE2 PHE A 413      30.011  72.160  37.419  1.00 96.99           C  
ANISOU 2554  CE2 PHE A 413     8889  13971  13993  -1146  -1899  -1127       C  
ATOM   2555  CZ  PHE A 413      30.390  72.200  36.089  1.00 91.16           C  
ANISOU 2555  CZ  PHE A 413     8318  13108  13212  -1033  -2000  -1246       C  
ATOM   2556  N   PHE A 414      28.334  78.078  39.978  1.00 99.77           N  
ANISOU 2556  N   PHE A 414     8900  15178  13829   -120  -1654  -1175       N  
ATOM   2557  CA  PHE A 414      27.550  79.234  40.411  1.00100.96           C  
ANISOU 2557  CA  PHE A 414     8934  15572  13853    142  -1682  -1240       C  
ATOM   2558  C   PHE A 414      28.450  80.142  41.251  1.00100.13           C  
ANISOU 2558  C   PHE A 414     8995  15337  13713    325  -1645  -1236       C  
ATOM   2559  O   PHE A 414      28.386  80.172  42.481  1.00107.55           O  
ANISOU 2559  O   PHE A 414     9835  16419  14611    367  -1567  -1202       O  
ATOM   2560  CB  PHE A 414      26.315  78.778  41.179  1.00103.98           C  
ANISOU 2560  CB  PHE A 414     8980  16337  14189     80  -1641  -1202       C  
ATOM   2561  CG  PHE A 414      25.592  77.634  40.528  1.00111.65           C  
ANISOU 2561  CG  PHE A 414     9788  17388  15245   -182  -1685  -1164       C  
ATOM   2562  CD1 PHE A 414      25.295  77.663  39.175  1.00113.84           C  
ANISOU 2562  CD1 PHE A 414    10124  17589  15540   -175  -1808  -1256       C  
ATOM   2563  CD2 PHE A 414      25.222  76.521  41.264  1.00117.66           C  
ANISOU 2563  CD2 PHE A 414    10341  18291  16074   -440  -1622  -1029       C  
ATOM   2564  CE1 PHE A 414      24.637  76.605  38.571  1.00115.71           C  
ANISOU 2564  CE1 PHE A 414    10223  17876  15864   -410  -1883  -1238       C  
ATOM   2565  CE2 PHE A 414      24.563  75.462  40.668  1.00120.18           C  
ANISOU 2565  CE2 PHE A 414    10518  18648  16497   -700  -1704   -987       C  
ATOM   2566  CZ  PHE A 414      24.270  75.502  39.322  1.00118.53           C  
ANISOU 2566  CZ  PHE A 414    10379  18348  16310   -680  -1841  -1103       C  
ATOM   2567  N   SER A 415      29.306  80.893  40.560  1.00 98.87           N  
ANISOU 2567  N   SER A 415     9087  14909  13569    434  -1715  -1261       N  
ATOM   2568  CA  SER A 415      30.195  81.866  41.178  1.00 67.14           C  
ANISOU 2568  CA  SER A 415     5251  10718   9540    605  -1731  -1256       C  
ATOM   2569  C   SER A 415      29.825  83.275  40.731  1.00 80.58           C  
ANISOU 2569  C   SER A 415     7025  12424  11169    890  -1888  -1347       C  
ATOM   2570  O   SER A 415      29.119  83.468  39.737  1.00 87.66           O  
ANISOU 2570  O   SER A 415     7876  13402  12029    938  -1971  -1400       O  
ATOM   2571  CB  SER A 415      31.660  81.574  40.835  1.00 72.32           C  
ANISOU 2571  CB  SER A 415     6145  11039  10296    470  -1695  -1166       C  
ATOM   2572  OG  SER A 415      31.891  81.609  39.437  1.00 88.38           O  
ANISOU 2572  OG  SER A 415     8289  12948  12346    443  -1765  -1161       O  
ATOM   2573  N   GLU A 416      30.312  84.259  41.486  1.00 82.35           N  
ANISOU 2573  N   GLU A 416     7370  12544  11373   1085  -1948  -1369       N  
ATOM   2574  CA  GLU A 416      30.014  85.661  41.213  1.00 82.72           C  
ANISOU 2574  CA  GLU A 416     7511  12555  11363   1373  -2136  -1456       C  
ATOM   2575  C   GLU A 416      30.483  86.050  39.815  1.00 78.62           C  
ANISOU 2575  C   GLU A 416     7167  11806  10898   1340  -2235  -1401       C  
ATOM   2576  O   GLU A 416      31.677  85.979  39.507  1.00 72.09           O  
ANISOU 2576  O   GLU A 416     6520  10711  10161   1215  -2218  -1284       O  
ATOM   2577  CB  GLU A 416      30.679  86.548  42.268  1.00 89.38           C  
ANISOU 2577  CB  GLU A 416     8497  13251  12212   1557  -2212  -1479       C  
ATOM   2578  CG  GLU A 416      30.701  88.026  41.920  1.00 98.28           C  
ANISOU 2578  CG  GLU A 416     9799  14212  13329   1825  -2455  -1543       C  
ATOM   2579  CD  GLU A 416      29.338  88.666  42.030  1.00107.48           C  
ANISOU 2579  CD  GLU A 416    10820  15666  14352   2111  -2566  -1708       C  
ATOM   2580  OE1 GLU A 416      28.581  88.281  42.945  1.00113.09           O  
ANISOU 2580  OE1 GLU A 416    11313  16703  14954   2188  -2473  -1784       O  
ATOM   2581  OE2 GLU A 416      29.022  89.549  41.204  1.00111.13           O  
ANISOU 2581  OE2 GLU A 416    11374  16047  14801   2265  -2747  -1750       O  
ATOM   2582  N   LYS A 417      29.531  86.450  38.969  1.00 83.90           N  
ANISOU 2582  N   LYS A 417     7768  12611  11499   1457  -2336  -1476       N  
ATOM   2583  CA  LYS A 417      29.794  86.848  37.584  1.00 79.79           C  
ANISOU 2583  CA  LYS A 417     7383  11934  10998   1454  -2436  -1423       C  
ATOM   2584  C   LYS A 417      30.584  85.787  36.821  1.00 75.38           C  
ANISOU 2584  C   LYS A 417     6872  11264  10505   1187  -2316  -1309       C  
ATOM   2585  O   LYS A 417      31.284  86.104  35.855  1.00 80.79           O  
ANISOU 2585  O   LYS A 417     7709  11775  11212   1169  -2372  -1213       O  
ATOM   2586  CB  LYS A 417      30.511  88.201  37.522  1.00 69.53           C  
ANISOU 2586  CB  LYS A 417     6317  10364   9737   1623  -2615  -1372       C  
ATOM   2587  CG  LYS A 417      29.733  89.267  36.775  1.00 71.20           C  
ANISOU 2587  CG  LYS A 417     6558  10610   9883   1854  -2815  -1440       C  
ATOM   2588  CD  LYS A 417      28.516  89.716  37.562  1.00 83.48           C  
ANISOU 2588  CD  LYS A 417     7965  12420  11332   2106  -2885  -1627       C  
ATOM   2589  CE  LYS A 417      27.691  90.722  36.768  1.00 96.28           C  
ANISOU 2589  CE  LYS A 417     9615  14086  12882   2347  -3090  -1707       C  
ATOM   2590  NZ  LYS A 417      26.667  91.416  37.607  1.00101.00           N  
ANISOU 2590  NZ  LYS A 417    10112  14900  13365   2664  -3204  -1896       N  
ATOM   2591  N   ASP A 418      30.484  84.531  37.264  1.00 69.36           N  
ANISOU 2591  N   ASP A 418     5977  10610   9767    990  -2163  -1312       N  
ATOM   2592  CA  ASP A 418      31.082  83.374  36.603  1.00 76.04           C  
ANISOU 2592  CA  ASP A 418     6852  11376  10665    758  -2068  -1244       C  
ATOM   2593  C   ASP A 418      32.605  83.409  36.597  1.00 83.22           C  
ANISOU 2593  C   ASP A 418     7965  12015  11638    681  -2027  -1112       C  
ATOM   2594  O   ASP A 418      33.226  82.833  35.704  1.00 91.98           O  
ANISOU 2594  O   ASP A 418     9147  13044  12757    575  -1998  -1051       O  
ATOM   2595  CB  ASP A 418      30.574  83.222  35.167  1.00 86.31           C  
ANISOU 2595  CB  ASP A 418     8132  12742  11918    764  -2140  -1280       C  
ATOM   2596  CG  ASP A 418      29.118  82.845  35.109  1.00 95.40           C  
ANISOU 2596  CG  ASP A 418     9055  14169  13023    773  -2165  -1399       C  
ATOM   2597  OD1 ASP A 418      28.722  81.953  35.889  1.00109.54           O  
ANISOU 2597  OD1 ASP A 418    10689  16083  14849    629  -2077  -1412       O  
ATOM   2598  OD2 ASP A 418      28.376  83.437  34.294  1.00 89.23           O  
ANISOU 2598  OD2 ASP A 418     8242  13488  12172    916  -2276  -1464       O  
ATOM   2599  N   ASN A 419      33.239  84.039  37.591  1.00 78.42           N  
ANISOU 2599  N   ASN A 419     7445  11284  11069    743  -2030  -1068       N  
ATOM   2600  CA  ASN A 419      34.685  84.221  37.494  1.00 76.02           C  
ANISOU 2600  CA  ASN A 419     7327  10729  10827    678  -2016   -926       C  
ATOM   2601  C   ASN A 419      35.438  82.917  37.726  1.00 64.51           C  
ANISOU 2601  C   ASN A 419     5869   9227   9416    463  -1858   -875       C  
ATOM   2602  O   ASN A 419      36.534  82.736  37.184  1.00 64.27           O  
ANISOU 2602  O   ASN A 419     5958   9056   9407    388  -1830   -761       O  
ATOM   2603  CB  ASN A 419      35.179  85.277  38.482  1.00 78.70           C  
ANISOU 2603  CB  ASN A 419     7770  10923  11211    802  -2096   -898       C  
ATOM   2604  CG  ASN A 419      35.013  84.850  39.916  1.00 73.83           C  
ANISOU 2604  CG  ASN A 419     7065  10384  10602    789  -2003   -967       C  
ATOM   2605  OD1 ASN A 419      35.869  84.145  40.461  1.00 61.55           O  
ANISOU 2605  OD1 ASN A 419     5545   8740   9100    642  -1885   -899       O  
ATOM   2606  ND2 ASN A 419      33.919  85.272  40.543  1.00 77.99           N  
ANISOU 2606  ND2 ASN A 419     7471  11101  11062    958  -2056  -1096       N  
ATOM   2607  N   VAL A 420      34.891  82.009  38.537  1.00 61.81           N  
ANISOU 2607  N   VAL A 420     5388   9012   9084    367  -1760   -943       N  
ATOM   2608  CA  VAL A 420      35.592  80.755  38.801  1.00 67.21           C  
ANISOU 2608  CA  VAL A 420     6086   9629   9822    166  -1634   -895       C  
ATOM   2609  C   VAL A 420      35.583  79.886  37.557  1.00 73.46           C  
ANISOU 2609  C   VAL A 420     6883  10431  10598     69  -1639   -907       C  
ATOM   2610  O   VAL A 420      36.607  79.310  37.171  1.00 82.62           O  
ANISOU 2610  O   VAL A 420     8153  11466  11774    -13  -1593   -844       O  
ATOM   2611  CB  VAL A 420      34.968  80.009  39.996  1.00 61.13           C  
ANISOU 2611  CB  VAL A 420     5158   8996   9072     75  -1545   -934       C  
ATOM   2612  CG1 VAL A 420      35.626  78.629  40.161  1.00 60.33           C  
ANISOU 2612  CG1 VAL A 420     5080   8806   9036   -144  -1442   -883       C  
ATOM   2613  CG2 VAL A 420      35.055  80.832  41.259  1.00 61.10           C  
ANISOU 2613  CG2 VAL A 420     5154   9003   9058    205  -1541   -935       C  
ATOM   2614  N   LEU A 421      34.418  79.767  36.916  1.00 74.64           N  
ANISOU 2614  N   LEU A 421     6911  10744  10706     97  -1706  -1000       N  
ATOM   2615  CA  LEU A 421      34.344  78.985  35.692  1.00 74.54           C  
ANISOU 2615  CA  LEU A 421     6909  10743  10670     36  -1743  -1039       C  
ATOM   2616  C   LEU A 421      35.066  79.690  34.552  1.00 73.15           C  
ANISOU 2616  C   LEU A 421     6875  10493  10425    158  -1798   -976       C  
ATOM   2617  O   LEU A 421      35.694  79.030  33.716  1.00 74.66           O  
ANISOU 2617  O   LEU A 421     7141  10642  10585    122  -1792   -961       O  
ATOM   2618  CB  LEU A 421      32.884  78.717  35.330  1.00 81.98           C  
ANISOU 2618  CB  LEU A 421     7674  11883  11590     33  -1816  -1152       C  
ATOM   2619  CG  LEU A 421      32.631  77.710  34.207  1.00 80.19           C  
ANISOU 2619  CG  LEU A 421     7438  11673  11357    -47  -1882  -1225       C  
ATOM   2620  CD1 LEU A 421      33.307  76.380  34.520  1.00 78.47           C  
ANISOU 2620  CD1 LEU A 421     7270  11327  11218   -234  -1830  -1208       C  
ATOM   2621  CD2 LEU A 421      31.148  77.518  33.999  1.00 86.50           C  
ANISOU 2621  CD2 LEU A 421     8040  12673  12152    -65  -1965  -1325       C  
ATOM   2622  N   THR A 422      35.005  81.025  34.516  1.00 62.63           N  
ANISOU 2622  N   THR A 422     5582   9152   9063    312  -1865   -930       N  
ATOM   2623  CA  THR A 422      35.716  81.775  33.484  1.00 62.68           C  
ANISOU 2623  CA  THR A 422     5711   9093   9011    410  -1925   -821       C  
ATOM   2624  C   THR A 422      37.202  81.457  33.510  1.00 75.86           C  
ANISOU 2624  C   THR A 422     7501  10624  10699    332  -1843   -682       C  
ATOM   2625  O   THR A 422      37.805  81.167  32.474  1.00 80.76           O  
ANISOU 2625  O   THR A 422     8173  11265  11245    345  -1840   -621       O  
ATOM   2626  CB  THR A 422      35.496  83.279  33.662  1.00 63.21           C  
ANISOU 2626  CB  THR A 422     5817   9120   9078    565  -2035   -772       C  
ATOM   2627  OG1 THR A 422      34.096  83.578  33.588  1.00 76.82           O  
ANISOU 2627  OG1 THR A 422     7422  11003  10765    667  -2114   -911       O  
ATOM   2628  CG2 THR A 422      36.222  84.048  32.571  1.00 77.14           C  
ANISOU 2628  CG2 THR A 422     7695  10822  10793    639  -2109   -614       C  
ATOM   2629  N   TYR A 423      37.807  81.489  34.697  1.00 79.04           N  
ANISOU 2629  N   TYR A 423     7938  10909  11184    265  -1777   -634       N  
ATOM   2630  CA  TYR A 423      39.241  81.251  34.798  1.00 79.39           C  
ANISOU 2630  CA  TYR A 423     8088  10830  11248    195  -1703   -496       C  
ATOM   2631  C   TYR A 423      39.603  79.850  34.314  1.00 75.53           C  
ANISOU 2631  C   TYR A 423     7598  10380  10720    105  -1625   -543       C  
ATOM   2632  O   TYR A 423      40.606  79.665  33.613  1.00 78.71           O  
ANISOU 2632  O   TYR A 423     8070  10774  11060    119  -1598   -443       O  
ATOM   2633  CB  TYR A 423      39.705  81.471  36.241  1.00 70.53           C  
ANISOU 2633  CB  TYR A 423     6994   9582  10223    145  -1655   -464       C  
ATOM   2634  CG  TYR A 423      41.199  81.346  36.399  1.00 66.78           C  
ANISOU 2634  CG  TYR A 423     6620   8979   9774     78  -1590   -312       C  
ATOM   2635  CD1 TYR A 423      42.035  82.434  36.173  1.00 61.72           C  
ANISOU 2635  CD1 TYR A 423     6063   8239   9149    124  -1662   -134       C  
ATOM   2636  CD2 TYR A 423      41.778  80.131  36.747  1.00 63.28           C  
ANISOU 2636  CD2 TYR A 423     6185   8517   9342    -37  -1472   -334       C  
ATOM   2637  CE1 TYR A 423      43.402  82.316  36.301  1.00 65.60           C  
ANISOU 2637  CE1 TYR A 423     6621   8642   9661     53  -1604     22       C  
ATOM   2638  CE2 TYR A 423      43.141  80.004  36.875  1.00 60.41           C  
ANISOU 2638  CE2 TYR A 423     5902   8062   8989    -84  -1412   -200       C  
ATOM   2639  CZ  TYR A 423      43.949  81.097  36.651  1.00 66.76           C  
ANISOU 2639  CZ  TYR A 423     6768   8797   9803    -41  -1471    -19       C  
ATOM   2640  OH  TYR A 423      45.309  80.966  36.780  1.00 72.27           O  
ANISOU 2640  OH  TYR A 423     7522   9430  10509    -96  -1412    131       O  
ATOM   2641  N   ILE A 424      38.783  78.856  34.660  1.00 77.19           N  
ANISOU 2641  N   ILE A 424     7724  10643  10963     22  -1604   -690       N  
ATOM   2642  CA  ILE A 424      39.078  77.473  34.296  1.00 83.22           C  
ANISOU 2642  CA  ILE A 424     8505  11401  11715    -65  -1572   -755       C  
ATOM   2643  C   ILE A 424      38.977  77.278  32.786  1.00 93.32           C  
ANISOU 2643  C   ILE A 424     9801  12780  12875     36  -1648   -798       C  
ATOM   2644  O   ILE A 424      39.876  76.710  32.155  1.00 95.33           O  
ANISOU 2644  O   ILE A 424    10134  13030  13058     66  -1629   -773       O  
ATOM   2645  CB  ILE A 424      38.146  76.520  35.064  1.00 74.86           C  
ANISOU 2645  CB  ILE A 424     7342  10360  10743   -202  -1565   -872       C  
ATOM   2646  CG1 ILE A 424      38.325  76.724  36.570  1.00 69.50           C  
ANISOU 2646  CG1 ILE A 424     6640   9617  10150   -275  -1478   -815       C  
ATOM   2647  CG2 ILE A 424      38.404  75.074  34.679  1.00 70.63           C  
ANISOU 2647  CG2 ILE A 424     6844   9776  10217   -295  -1581   -947       C  
ATOM   2648  CD1 ILE A 424      37.322  75.988  37.409  1.00 59.64           C  
ANISOU 2648  CD1 ILE A 424     5251   8438   8973   -404  -1466   -883       C  
ATOM   2649  N   LEU A 425      37.886  77.756  32.182  1.00 97.10           N  
ANISOU 2649  N   LEU A 425    10205  13373  13317    112  -1739   -869       N  
ATOM   2650  CA  LEU A 425      37.685  77.619  30.742  1.00 91.61           C  
ANISOU 2650  CA  LEU A 425     9517  12792  12497    227  -1823   -922       C  
ATOM   2651  C   LEU A 425      38.543  78.577  29.927  1.00 89.09           C  
ANISOU 2651  C   LEU A 425     9271  12516  12064    365  -1821   -754       C  
ATOM   2652  O   LEU A 425      38.606  78.431  28.702  1.00 86.49           O  
ANISOU 2652  O   LEU A 425     8955  12308  11601    481  -1872   -769       O  
ATOM   2653  CB  LEU A 425      36.209  77.832  30.390  1.00 86.50           C  
ANISOU 2653  CB  LEU A 425     8757  12262  11849    263  -1925  -1049       C  
ATOM   2654  CG  LEU A 425      35.246  76.768  30.921  1.00 78.63           C  
ANISOU 2654  CG  LEU A 425     7653  11272  10950    116  -1956  -1197       C  
ATOM   2655  CD1 LEU A 425      33.793  77.133  30.645  1.00 77.71           C  
ANISOU 2655  CD1 LEU A 425     7396  11301  10828    154  -2052  -1296       C  
ATOM   2656  CD2 LEU A 425      35.585  75.401  30.344  1.00 68.24           C  
ANISOU 2656  CD2 LEU A 425     6394   9911   9623     65  -2003  -1294       C  
ATOM   2657  N   GLN A 426      39.177  79.566  30.560  1.00 85.45           N  
ANISOU 2657  N   GLN A 426     8850  11966  11652    357  -1780   -585       N  
ATOM   2658  CA  GLN A 426      40.159  80.380  29.857  1.00 77.23           C  
ANISOU 2658  CA  GLN A 426     7868  10953  10523    443  -1782   -374       C  
ATOM   2659  C   GLN A 426      41.485  79.647  29.742  1.00 84.34           C  
ANISOU 2659  C   GLN A 426     8824  11854  11368    417  -1689   -289       C  
ATOM   2660  O   GLN A 426      42.261  79.914  28.819  1.00 89.38           O  
ANISOU 2660  O   GLN A 426     9478  12606  11875    507  -1684   -136       O  
ATOM   2661  CB  GLN A 426      40.364  81.714  30.578  1.00 76.70           C  
ANISOU 2661  CB  GLN A 426     7830  10762  10550    433  -1815   -219       C  
ATOM   2662  CG  GLN A 426      39.318  82.773  30.275  1.00 78.43           C  
ANISOU 2662  CG  GLN A 426     8020  11012  10769    534  -1942   -240       C  
ATOM   2663  CD  GLN A 426      39.451  83.990  31.172  1.00 83.11           C  
ANISOU 2663  CD  GLN A 426     8661  11442  11476    536  -2011   -136       C  
ATOM   2664  OE1 GLN A 426      39.986  83.900  32.284  1.00 76.51           O  
ANISOU 2664  OE1 GLN A 426     7857  10475  10740    451  -1956   -119       O  
ATOM   2665  NE2 GLN A 426      38.945  85.135  30.703  1.00 63.89           N  
ANISOU 2665  NE2 GLN A 426     6241   9006   9027    647  -2151    -78       N  
ATOM   2666  N   ASP A 427      41.760  78.738  30.674  1.00 78.19           N  
ANISOU 2666  N   ASP A 427     8063  10968  10676    302  -1616   -372       N  
ATOM   2667  CA  ASP A 427      42.944  77.903  30.591  1.00 73.52           C  
ANISOU 2667  CA  ASP A 427     7526  10381  10026    294  -1537   -330       C  
ATOM   2668  C   ASP A 427      42.851  77.009  29.362  1.00 86.33           C  
ANISOU 2668  C   ASP A 427     9152  12158  11491    415  -1583   -452       C  
ATOM   2669  O   ASP A 427      41.761  76.682  28.886  1.00 88.71           O  
ANISOU 2669  O   ASP A 427     9417  12508  11781    448  -1672   -623       O  
ATOM   2670  CB  ASP A 427      43.090  77.072  31.868  1.00 71.74           C  
ANISOU 2670  CB  ASP A 427     7325   9999   9935    148  -1470   -415       C  
ATOM   2671  CG  ASP A 427      44.181  76.030  31.770  1.00 77.65           C  
ANISOU 2671  CG  ASP A 427     8136  10745  10621    154  -1409   -419       C  
ATOM   2672  OD1 ASP A 427      45.360  76.412  31.617  1.00 81.19           O  
ANISOU 2672  OD1 ASP A 427     8612  11235  11003    197  -1349   -240       O  
ATOM   2673  OD2 ASP A 427      43.863  74.828  31.857  1.00 82.01           O  
ANISOU 2673  OD2 ASP A 427     8709  11257  11196    117  -1435   -594       O  
ATOM   2674  N   GLN A 428      44.012  76.635  28.829  1.00 91.74           N  
ANISOU 2674  N   GLN A 428     9875  12939  12043    501  -1533   -366       N  
ATOM   2675  CA  GLN A 428      44.065  75.836  27.613  1.00 87.10           C  
ANISOU 2675  CA  GLN A 428     9299  12526  11268    671  -1589   -484       C  
ATOM   2676  C   GLN A 428      44.299  74.360  27.910  1.00 90.21           C  
ANISOU 2676  C   GLN A 428     9762  12835  11681    653  -1602   -681       C  
ATOM   2677  O   GLN A 428      43.526  73.503  27.470  1.00100.91           O  
ANISOU 2677  O   GLN A 428    11132  14183  13025    691  -1718   -906       O  
ATOM   2678  CB  GLN A 428      45.164  76.361  26.684  1.00 85.09           C  
ANISOU 2678  CB  GLN A 428     9025  12498  10808    828  -1540   -262       C  
ATOM   2679  CG  GLN A 428      44.822  77.657  25.979  1.00 94.87           C  
ANISOU 2679  CG  GLN A 428    10200  13859  11985    888  -1578    -82       C  
ATOM   2680  CD  GLN A 428      43.635  77.527  25.047  1.00100.94           C  
ANISOU 2680  CD  GLN A 428    10946  14732  12675   1005  -1694   -264       C  
ATOM   2681  OE1 GLN A 428      42.488  77.557  25.484  1.00106.55           O  
ANISOU 2681  OE1 GLN A 428    11647  15310  13526    917  -1758   -418       O  
ATOM   2682  NE2 GLN A 428      43.907  77.369  23.755  1.00103.15           N  
ANISOU 2682  NE2 GLN A 428    11204  15275  12715   1216  -1722   -247       N  
ATOM   2683  N   ALA A 429      45.350  74.048  28.668  1.00 76.84           N  
ANISOU 2683  N   ALA A 429     8113  11059  10025    590  -1506   -599       N  
ATOM   2684  CA  ALA A 429      45.854  72.683  28.699  1.00 74.84           C  
ANISOU 2684  CA  ALA A 429     7940  10762   9733    634  -1531   -756       C  
ATOM   2685  C   ALA A 429      45.108  71.774  29.668  1.00 86.50           C  
ANISOU 2685  C   ALA A 429     9456  11996  11415    451  -1586   -935       C  
ATOM   2686  O   ALA A 429      45.216  70.549  29.538  1.00 96.51           O  
ANISOU 2686  O   ALA A 429    10803  13198  12669    488  -1673  -1109       O  
ATOM   2687  CB  ALA A 429      47.345  72.693  29.039  1.00 71.91           C  
ANISOU 2687  CB  ALA A 429     7596  10431   9297    663  -1408   -588       C  
ATOM   2688  N   VAL A 430      44.355  72.325  30.623  1.00 88.54           N  
ANISOU 2688  N   VAL A 430     9658  12130  11854    266  -1554   -892       N  
ATOM   2689  CA  VAL A 430      43.761  71.514  31.686  1.00 85.87           C  
ANISOU 2689  CA  VAL A 430     9327  11596  11704     73  -1580  -1000       C  
ATOM   2690  C   VAL A 430      42.290  71.851  31.902  1.00 86.49           C  
ANISOU 2690  C   VAL A 430     9303  11665  11894    -33  -1642  -1061       C  
ATOM   2691  O   VAL A 430      41.453  70.953  32.057  1.00 83.63           O  
ANISOU 2691  O   VAL A 430     8922  11224  11628   -138  -1746  -1202       O  
ATOM   2692  CB  VAL A 430      44.546  71.685  33.000  1.00 69.23           C  
ANISOU 2692  CB  VAL A 430     7241   9363   9701    -52  -1444   -864       C  
ATOM   2693  CG1 VAL A 430      43.749  71.124  34.167  1.00 69.34           C  
ANISOU 2693  CG1 VAL A 430     7223   9221   9903   -258  -1455   -928       C  
ATOM   2694  CG2 VAL A 430      45.894  71.002  32.904  1.00 59.33           C  
ANISOU 2694  CG2 VAL A 430     6085   8101   8357     31  -1402   -845       C  
ATOM   2695  N   GLY A 431      41.975  73.145  31.929  1.00 82.04           N  
ANISOU 2695  N   GLY A 431     8668  11181  11322     -9  -1595   -946       N  
ATOM   2696  CA  GLY A 431      40.649  73.624  32.245  1.00 84.97           C  
ANISOU 2696  CA  GLY A 431     8930  11572  11781    -83  -1639   -989       C  
ATOM   2697  C   GLY A 431      39.520  72.937  31.500  1.00 89.24           C  
ANISOU 2697  C   GLY A 431     9422  12165  12320    -81  -1785  -1168       C  
ATOM   2698  O   GLY A 431      38.733  72.185  32.087  1.00 87.56           O  
ANISOU 2698  O   GLY A 431     9151  11883  12234   -237  -1838  -1253       O  
ATOM   2699  N   PRO A 432      39.415  73.182  30.189  1.00 92.89           N  
ANISOU 2699  N   PRO A 432     9895  12760  12637     91  -1864  -1215       N  
ATOM   2700  CA  PRO A 432      38.272  72.631  29.440  1.00 98.22           C  
ANISOU 2700  CA  PRO A 432    10518  13490  13311    104  -2024  -1394       C  
ATOM   2701  C   PRO A 432      38.201  71.114  29.474  1.00100.34           C  
ANISOU 2701  C   PRO A 432    10840  13631  13652     16  -2142  -1551       C  
ATOM   2702  O   PRO A 432      37.098  70.554  29.514  1.00106.11           O  
ANISOU 2702  O   PRO A 432    11496  14332  14489   -100  -2270  -1665       O  
ATOM   2703  CB  PRO A 432      38.498  73.164  28.019  1.00 99.37           C  
ANISOU 2703  CB  PRO A 432    10693  13810  13254    341  -2070  -1395       C  
ATOM   2704  CG  PRO A 432      39.382  74.362  28.188  1.00 93.80           C  
ANISOU 2704  CG  PRO A 432    10003  13152  12484    404  -1930  -1171       C  
ATOM   2705  CD  PRO A 432      40.268  74.036  29.345  1.00 88.24           C  
ANISOU 2705  CD  PRO A 432     9350  12297  11880    274  -1816  -1087       C  
ATOM   2706  N   SER A 433      39.350  70.432  29.467  1.00 98.49           N  
ANISOU 2706  N   SER A 433    10733  13318  13370     66  -2119  -1554       N  
ATOM   2707  CA  SER A 433      39.347  68.977  29.581  1.00104.56           C  
ANISOU 2707  CA  SER A 433    11579  13923  14225    -14  -2258  -1703       C  
ATOM   2708  C   SER A 433      38.754  68.524  30.909  1.00101.11           C  
ANISOU 2708  C   SER A 433    11072  13329  14014   -297  -2244  -1661       C  
ATOM   2709  O   SER A 433      38.088  67.484  30.973  1.00106.88           O  
ANISOU 2709  O   SER A 433    11799  13941  14870   -431  -2413  -1772       O  
ATOM   2710  CB  SER A 433      40.768  68.431  29.431  1.00117.34           C  
ANISOU 2710  CB  SER A 433    13347  15500  15735    117  -2222  -1703       C  
ATOM   2711  OG  SER A 433      41.488  69.130  28.431  1.00125.85           O  
ANISOU 2711  OG  SER A 433    14447  16785  16585    369  -2164  -1651       O  
ATOM   2712  N   PHE A 434      38.984  69.293  31.978  1.00 91.53           N  
ANISOU 2712  N   PHE A 434     9801  12121  12854   -389  -2059  -1491       N  
ATOM   2713  CA  PHE A 434      38.449  68.938  33.289  1.00 87.85           C  
ANISOU 2713  CA  PHE A 434     9248  11559  12572   -633  -2024  -1428       C  
ATOM   2714  C   PHE A 434      36.932  69.086  33.324  1.00 80.57           C  
ANISOU 2714  C   PHE A 434     8150  10732  11731   -745  -2107  -1461       C  
ATOM   2715  O   PHE A 434      36.220  68.187  33.786  1.00 73.37           O  
ANISOU 2715  O   PHE A 434     7167   9744  10964   -946  -2208  -1483       O  
ATOM   2716  CB  PHE A 434      39.108  69.802  34.368  1.00 90.91           C  
ANISOU 2716  CB  PHE A 434     9622  11954  12966   -654  -1816  -1258       C  
ATOM   2717  CG  PHE A 434      38.468  69.681  35.732  1.00 87.04           C  
ANISOU 2717  CG  PHE A 434     9011  11439  12623   -862  -1757  -1178       C  
ATOM   2718  CD1 PHE A 434      38.782  68.627  36.574  1.00 80.41           C  
ANISOU 2718  CD1 PHE A 434     8210  10447  11896  -1027  -1759  -1150       C  
ATOM   2719  CD2 PHE A 434      37.562  70.637  36.174  1.00 83.39           C  
ANISOU 2719  CD2 PHE A 434     8390  11125  12169   -873  -1704  -1125       C  
ATOM   2720  CE1 PHE A 434      38.199  68.525  37.828  1.00 79.42           C  
ANISOU 2720  CE1 PHE A 434     7953  10339  11884  -1211  -1696  -1050       C  
ATOM   2721  CE2 PHE A 434      36.976  70.536  37.424  1.00 78.95           C  
ANISOU 2721  CE2 PHE A 434     7696  10596  11707  -1032  -1642  -1046       C  
ATOM   2722  CZ  PHE A 434      37.296  69.480  38.252  1.00 76.10           C  
ANISOU 2722  CZ  PHE A 434     7360  10104  11452  -1206  -1631   -998       C  
ATOM   2723  N   ILE A 435      36.421  70.219  32.837  1.00 90.98           N  
ANISOU 2723  N   ILE A 435     9387  12223  12960   -621  -2076  -1450       N  
ATOM   2724  CA  ILE A 435      34.982  70.468  32.883  1.00 99.51           C  
ANISOU 2724  CA  ILE A 435    10283  13430  14097   -701  -2144  -1478       C  
ATOM   2725  C   ILE A 435      34.228  69.434  32.056  1.00110.27           C  
ANISOU 2725  C   ILE A 435    11629  14760  15510   -760  -2368  -1631       C  
ATOM   2726  O   ILE A 435      33.178  68.932  32.474  1.00109.11           O  
ANISOU 2726  O   ILE A 435    11333  14631  15494   -952  -2455  -1632       O  
ATOM   2727  CB  ILE A 435      34.674  71.903  32.418  1.00 91.53           C  
ANISOU 2727  CB  ILE A 435     9218  12594  12965   -520  -2089  -1451       C  
ATOM   2728  CG1 ILE A 435      35.267  72.917  33.403  1.00 91.64           C  
ANISOU 2728  CG1 ILE A 435     9239  12612  12969   -489  -1912  -1304       C  
ATOM   2729  CG2 ILE A 435      33.174  72.100  32.236  1.00 83.96           C  
ANISOU 2729  CG2 ILE A 435     8073  11791  12037   -560  -2184  -1513       C  
ATOM   2730  CD1 ILE A 435      34.652  72.870  34.789  1.00 88.82           C  
ANISOU 2730  CD1 ILE A 435     8738  12286  12723   -649  -1843  -1238       C  
ATOM   2731  N   HIS A 436      34.747  69.094  30.874  1.00125.97           N  
ANISOU 2731  N   HIS A 436    13760  16711  17391   -592  -2477  -1755       N  
ATOM   2732  CA  HIS A 436      34.082  68.090  30.051  1.00136.45           C  
ANISOU 2732  CA  HIS A 436    15097  17983  18765   -622  -2728  -1928       C  
ATOM   2733  C   HIS A 436      34.077  66.731  30.741  1.00136.33           C  
ANISOU 2733  C   HIS A 436    15114  17746  18939   -858  -2847  -1939       C  
ATOM   2734  O   HIS A 436      33.079  66.003  30.687  1.00144.44           O  
ANISOU 2734  O   HIS A 436    16050  18726  20107  -1030  -3041  -1996       O  
ATOM   2735  CB  HIS A 436      34.751  67.992  28.680  1.00146.98           C  
ANISOU 2735  CB  HIS A 436    16590  19341  19915   -348  -2821  -2069       C  
ATOM   2736  CG  HIS A 436      34.183  66.912  27.812  1.00157.44           C  
ANISOU 2736  CG  HIS A 436    17958  20583  21278   -341  -3111  -2279       C  
ATOM   2737  ND1 HIS A 436      34.634  65.610  27.852  1.00160.20           N  
ANISOU 2737  ND1 HIS A 436    18449  20709  21712   -395  -3279  -2383       N  
ATOM   2738  CD2 HIS A 436      33.194  66.939  26.888  1.00161.09           C  
ANISOU 2738  CD2 HIS A 436    18350  21142  21713   -280  -3288  -2412       C  
ATOM   2739  CE1 HIS A 436      33.948  64.882  26.989  1.00163.45           C  
ANISOU 2739  CE1 HIS A 436    18882  21070  22153   -367  -3563  -2577       C  
ATOM   2740  NE2 HIS A 436      33.068  65.665  26.391  1.00163.27           N  
ANISOU 2740  NE2 HIS A 436    18726  21246  22062   -301  -3568  -2597       N  
ATOM   2741  N   LYS A 437      35.181  66.374  31.400  1.00128.73           N  
ANISOU 2741  N   LYS A 437    14277  16643  17990   -878  -2746  -1870       N  
ATOM   2742  CA  LYS A 437      35.232  65.106  32.120  1.00123.07           C  
ANISOU 2742  CA  LYS A 437    13603  15700  17457  -1104  -2860  -1858       C  
ATOM   2743  C   LYS A 437      34.257  65.100  33.293  1.00120.75           C  
ANISOU 2743  C   LYS A 437    13095  15449  17337  -1396  -2809  -1697       C  
ATOM   2744  O   LYS A 437      33.667  64.060  33.612  1.00124.29           O  
ANISOU 2744  O   LYS A 437    13495  15763  17966  -1632  -2987  -1686       O  
ATOM   2745  CB  LYS A 437      36.658  64.835  32.598  1.00117.23           C  
ANISOU 2745  CB  LYS A 437    13040  14828  16676  -1039  -2743  -1812       C  
ATOM   2746  CG  LYS A 437      36.938  63.381  32.919  1.00113.28           C  
ANISOU 2746  CG  LYS A 437    12663  14055  16322  -1182  -2929  -1864       C  
ATOM   2747  CD  LYS A 437      38.345  63.192  33.452  1.00106.32           C  
ANISOU 2747  CD  LYS A 437    11942  13069  15387  -1105  -2794  -1813       C  
ATOM   2748  CE  LYS A 437      38.604  61.738  33.800  1.00108.13           C  
ANISOU 2748  CE  LYS A 437    12307  13007  15769  -1241  -2999  -1865       C  
ATOM   2749  NZ  LYS A 437      39.806  61.585  34.659  1.00110.64           N  
ANISOU 2749  NZ  LYS A 437    12735  13232  16071  -1230  -2839  -1769       N  
ATOM   2750  N   VAL A 438      34.072  66.253  33.941  1.00113.06           N  
ANISOU 2750  N   VAL A 438    11984  14669  16305  -1375  -2582  -1565       N  
ATOM   2751  CA  VAL A 438      33.117  66.351  35.044  1.00104.25           C  
ANISOU 2751  CA  VAL A 438    10636  13667  15306  -1601  -2518  -1412       C  
ATOM   2752  C   VAL A 438      31.693  66.161  34.537  1.00108.17           C  
ANISOU 2752  C   VAL A 438    10946  14281  15871  -1706  -2697  -1463       C  
ATOM   2753  O   VAL A 438      30.874  65.491  35.178  1.00110.20           O  
ANISOU 2753  O   VAL A 438    11036  14548  16286  -1970  -2779  -1362       O  
ATOM   2754  CB  VAL A 438      33.284  67.698  35.772  1.00 90.52           C  
ANISOU 2754  CB  VAL A 438     8816  12117  13462  -1489  -2262  -1298       C  
ATOM   2755  CG1 VAL A 438      32.099  67.965  36.687  1.00 79.47           C  
ANISOU 2755  CG1 VAL A 438     7143  10926  12125  -1645  -2210  -1177       C  
ATOM   2756  CG2 VAL A 438      34.578  67.712  36.559  1.00 91.47           C  
ANISOU 2756  CG2 VAL A 438     9080  12109  13564  -1463  -2102  -1214       C  
ATOM   2757  N   ILE A 439      31.378  66.745  33.379  1.00104.92           N  
ANISOU 2757  N   ILE A 439    10548  13974  15340  -1508  -2764  -1602       N  
ATOM   2758  CA  ILE A 439      30.035  66.634  32.817  1.00109.31           C  
ANISOU 2758  CA  ILE A 439    10928  14656  15949  -1583  -2940  -1665       C  
ATOM   2759  C   ILE A 439      29.741  65.196  32.415  1.00123.97           C  
ANISOU 2759  C   ILE A 439    12834  16296  17973  -1768  -3235  -1748       C  
ATOM   2760  O   ILE A 439      28.711  64.625  32.793  1.00132.17           O  
ANISOU 2760  O   ILE A 439    13679  17365  19175  -2028  -3365  -1671       O  
ATOM   2761  CB  ILE A 439      29.879  67.577  31.613  1.00107.38           C  
ANISOU 2761  CB  ILE A 439    10716  14557  15525  -1302  -2951  -1802       C  
ATOM   2762  CG1 ILE A 439      29.913  69.038  32.043  1.00 96.95           C  
ANISOU 2762  CG1 ILE A 439     9318  13445  14072  -1150  -2713  -1707       C  
ATOM   2763  CG2 ILE A 439      28.586  67.277  30.860  1.00117.05           C  
ANISOU 2763  CG2 ILE A 439    11793  15874  16804  -1366  -3177  -1905       C  
ATOM   2764  CD1 ILE A 439      29.902  69.968  30.859  1.00 93.33           C  
ANISOU 2764  CD1 ILE A 439     8920  13102  13441   -875  -2729  -1815       C  
ATOM   2765  N   THR A 440      30.630  64.596  31.624  1.00128.44           N  
ANISOU 2765  N   THR A 440    13654  16649  18498  -1628  -3364  -1905       N  
ATOM   2766  CA  THR A 440      30.408  63.256  31.088  1.00131.59           C  
ANISOU 2766  CA  THR A 440    14146  16810  19044  -1746  -3698  -2034       C  
ATOM   2767  C   THR A 440      30.775  62.197  32.130  1.00129.66           C  
ANISOU 2767  C   THR A 440    13946  16324  18993  -2012  -3747  -1906       C  
ATOM   2768  O   THR A 440      31.666  61.368  31.948  1.00128.82           O  
ANISOU 2768  O   THR A 440    14074  15962  18910  -1959  -3870  -2000       O  
ATOM   2769  CB  THR A 440      31.190  63.067  29.794  1.00136.08           C  
ANISOU 2769  CB  THR A 440    14966  17281  19457  -1436  -3831  -2275       C  
ATOM   2770  OG1 THR A 440      32.585  63.296  30.033  1.00135.74           O  
ANISOU 2770  OG1 THR A 440    15104  17187  19283  -1264  -3634  -2249       O  
ATOM   2771  CG2 THR A 440      30.694  64.040  28.726  1.00133.95           C  
ANISOU 2771  CG2 THR A 440    14633  17256  19006  -1198  -3813  -2384       C  
ATOM   2772  N   TYR A 441      30.060  62.248  33.249  1.00137.45           N  
ANISOU 2772  N   TYR A 441    14697  17420  20109  -2287  -3650  -1680       N  
ATOM   2773  CA  TYR A 441      30.208  61.266  34.312  1.00151.36           C  
ANISOU 2773  CA  TYR A 441    16450  18992  22067  -2581  -3699  -1509       C  
ATOM   2774  C   TYR A 441      28.833  60.959  34.894  1.00166.69           C  
ANISOU 2774  C   TYR A 441    18078  21065  24190  -2920  -3793  -1320       C  
ATOM   2775  O   TYR A 441      28.176  61.853  35.442  1.00165.48           O  
ANISOU 2775  O   TYR A 441    17673  21236  23966  -2937  -3582  -1184       O  
ATOM   2776  CB  TYR A 441      31.164  61.771  35.393  1.00148.49           C  
ANISOU 2776  CB  TYR A 441    16128  18672  21622  -2532  -3379  -1362       C  
ATOM   2777  CG  TYR A 441      31.596  60.695  36.357  1.00154.94           C  
ANISOU 2777  CG  TYR A 441    17007  19251  22614  -2778  -3438  -1216       C  
ATOM   2778  CD1 TYR A 441      32.538  59.743  35.987  1.00158.52           C  
ANISOU 2778  CD1 TYR A 441    17747  19372  23112  -2722  -3618  -1347       C  
ATOM   2779  CD2 TYR A 441      31.060  60.624  37.636  1.00159.36           C  
ANISOU 2779  CD2 TYR A 441    17335  19936  23279  -3048  -3321   -946       C  
ATOM   2780  CE1 TYR A 441      32.934  58.749  36.864  1.00162.03           C  
ANISOU 2780  CE1 TYR A 441    18262  19581  23721  -2943  -3690  -1213       C  
ATOM   2781  CE2 TYR A 441      31.450  59.635  38.521  1.00163.30           C  
ANISOU 2781  CE2 TYR A 441    17888  20222  23936  -3279  -3378   -791       C  
ATOM   2782  CZ  TYR A 441      32.387  58.700  38.130  1.00164.14           C  
ANISOU 2782  CZ  TYR A 441    18297  19965  24103  -3232  -3568   -925       C  
ATOM   2783  OH  TYR A 441      32.778  57.717  39.009  1.00165.17           O  
ANISOU 2783  OH  TYR A 441    18495  19868  24395  -3456  -3641   -770       O  
ATOM   2784  N   PRO A 442      28.359  59.714  34.788  1.00177.56           N  
ANISOU 2784  N   PRO A 442    19456  22209  25799  -3188  -4124  -1302       N  
ATOM   2785  CA  PRO A 442      26.990  59.407  35.226  1.00186.62           C  
ANISOU 2785  CA  PRO A 442    20276  23508  27124  -3529  -4242  -1101       C  
ATOM   2786  C   PRO A 442      26.844  59.382  36.739  1.00193.88           C  
ANISOU 2786  C   PRO A 442    20979  24577  28112  -3782  -4033   -767       C  
ATOM   2787  O   PRO A 442      26.787  58.306  37.344  1.00202.61           O  
ANISOU 2787  O   PRO A 442    22133  25506  29345  -4022  -4103   -598       O  
ATOM   2788  CB  PRO A 442      26.733  58.026  34.613  1.00187.73           C  
ANISOU 2788  CB  PRO A 442    20585  23310  27436  -3681  -4616  -1178       C  
ATOM   2789  CG  PRO A 442      28.090  57.406  34.531  1.00185.19           C  
ANISOU 2789  CG  PRO A 442    20612  22627  27126  -3555  -4697  -1310       C  
ATOM   2790  CD  PRO A 442      29.046  58.532  34.235  1.00180.36           C  
ANISOU 2790  CD  PRO A 442    20111  22153  26265  -3184  -4432  -1465       C  
ATOM   2791  N   SER A 443      26.778  60.561  37.360  1.00188.93           N  
ANISOU 2791  N   SER A 443    20185  24302  27297  -3640  -3683   -675       N  
ATOM   2792  CA  SER A 443      26.617  60.659  38.807  1.00181.76           C  
ANISOU 2792  CA  SER A 443    19053  23601  26405  -3823  -3462   -372       C  
ATOM   2793  C   SER A 443      26.077  62.025  39.212  1.00171.49           C  
ANISOU 2793  C   SER A 443    17506  22756  24895  -3643  -3168   -321       C  
ATOM   2794  O   SER A 443      26.003  62.339  40.404  1.00169.04           O  
ANISOU 2794  O   SER A 443    17015  22680  24534  -3701  -2946   -106       O  
ATOM   2795  CB  SER A 443      27.949  60.396  39.518  1.00179.76           C  
ANISOU 2795  CB  SER A 443    19041  23123  26135  -3774  -3323   -334       C  
ATOM   2796  OG  SER A 443      28.405  59.073  39.294  1.00180.96           O  
ANISOU 2796  OG  SER A 443    19409  22861  26488  -3949  -3607   -360       O  
ATOM   2797  N   ILE A 444      25.693  62.841  38.232  1.00165.38           N  
ANISOU 2797  N   ILE A 444    16729  22115  23993  -3408  -3179   -522       N  
ATOM   2798  CA  ILE A 444      25.290  64.219  38.490  1.00150.69           C  
ANISOU 2798  CA  ILE A 444    14694  20642  21921  -3177  -2929   -522       C  
ATOM   2799  C   ILE A 444      23.775  64.323  38.592  1.00139.24           C  
ANISOU 2799  C   ILE A 444    12856  19551  20499  -3329  -2992   -399       C  
ATOM   2800  O   ILE A 444      23.238  64.813  39.591  1.00141.74           O  
ANISOU 2800  O   ILE A 444    12895  20224  20734  -3352  -2805   -213       O  
ATOM   2801  CB  ILE A 444      25.824  65.158  37.394  1.00144.17           C  
ANISOU 2801  CB  ILE A 444    14095  19762  20920  -2809  -2890   -794       C  
ATOM   2802  CG1 ILE A 444      27.352  65.163  37.399  1.00134.45           C  
ANISOU 2802  CG1 ILE A 444    13204  18245  19635  -2649  -2792   -877       C  
ATOM   2803  CG2 ILE A 444      25.267  66.565  37.570  1.00145.72           C  
ANISOU 2803  CG2 ILE A 444    14113  20333  20921  -2577  -2694   -802       C  
ATOM   2804  CD1 ILE A 444      27.947  65.999  36.302  1.00130.79           C  
ANISOU 2804  CD1 ILE A 444    12955  17733  19005  -2313  -2765  -1101       C  
ATOM   2805  N   GLY A 445      23.082  63.866  37.559  1.00128.13           N  
ANISOU 2805  N   GLY A 445    11419  18071  19192  -3416  -3261   -507       N  
ATOM   2806  CA  GLY A 445      21.654  64.016  37.428  1.00125.44           C  
ANISOU 2806  CA  GLY A 445    10724  18069  18870  -3531  -3347   -428       C  
ATOM   2807  C   GLY A 445      21.339  64.646  36.096  1.00124.05           C  
ANISOU 2807  C   GLY A 445    10630  17913  18591  -3278  -3449   -701       C  
ATOM   2808  O   GLY A 445      22.163  64.641  35.175  1.00126.62           O  
ANISOU 2808  O   GLY A 445    11283  17944  18881  -3088  -3525   -931       O  
ATOM   2809  N   ARG A 446      20.137  65.201  35.984  1.00123.72           N  
ANISOU 2809  N   ARG A 446    10277  18247  18484  -3261  -3449   -669       N  
ATOM   2810  CA  ARG A 446      19.746  65.821  34.726  1.00124.56           C  
ANISOU 2810  CA  ARG A 446    10441  18399  18488  -3021  -3552   -917       C  
ATOM   2811  C   ARG A 446      19.196  67.223  34.954  1.00122.65           C  
ANISOU 2811  C   ARG A 446    10010  18579  18012  -2745  -3330   -931       C  
ATOM   2812  O   ARG A 446      19.335  68.095  34.091  1.00121.43           O  
ANISOU 2812  O   ARG A 446    10002  18432  17706  -2434  -3310  -1142       O  
ATOM   2813  CB  ARG A 446      18.733  64.941  33.990  1.00133.18           C  
ANISOU 2813  CB  ARG A 446    11379  19457  19765  -3271  -3890   -931       C  
ATOM   2814  CG  ARG A 446      19.306  63.591  33.579  1.00138.78           C  
ANISOU 2814  CG  ARG A 446    12332  19694  20703  -3489  -4174   -979       C  
ATOM   2815  CD  ARG A 446      18.370  62.822  32.662  1.00147.92           C  
ANISOU 2815  CD  ARG A 446    13479  20782  21944  -3621  -4448  -1064       C  
ATOM   2816  NE  ARG A 446      19.037  61.657  32.088  1.00150.09           N  
ANISOU 2816  NE  ARG A 446    14102  20579  22346  -3697  -4687  -1182       N  
ATOM   2817  CZ  ARG A 446      18.446  60.759  31.306  1.00152.65           C  
ANISOU 2817  CZ  ARG A 446    14501  20730  22769  -3817  -4964  -1262       C  
ATOM   2818  NH1 ARG A 446      17.164  60.886  30.990  1.00155.54           N  
ANISOU 2818  NH1 ARG A 446    14607  21364  23129  -3897  -5033  -1234       N  
ATOM   2819  NH2 ARG A 446      19.144  59.735  30.833  1.00151.42           N  
ANISOU 2819  NH2 ARG A 446    14682  20133  22717  -3837  -5184  -1381       N  
ATOM   2820  N   GLU A 447      18.574  67.452  36.111  1.00125.15           N  
ANISOU 2820  N   GLU A 447    10004  19258  18290  -2839  -3172   -704       N  
ATOM   2821  CA  GLU A 447      18.164  68.807  36.462  1.00125.50           C  
ANISOU 2821  CA  GLU A 447     9897  19692  18094  -2532  -2962   -732       C  
ATOM   2822  C   GLU A 447      19.381  69.698  36.669  1.00125.90           C  
ANISOU 2822  C   GLU A 447    10259  19585  17994  -2221  -2756   -842       C  
ATOM   2823  O   GLU A 447      19.423  70.835  36.186  1.00123.90           O  
ANISOU 2823  O   GLU A 447    10097  19411  17569  -1891  -2694  -1005       O  
ATOM   2824  CB  GLU A 447      17.288  68.790  37.716  1.00129.24           C  
ANISOU 2824  CB  GLU A 447     9952  20617  18537  -2678  -2841   -462       C  
ATOM   2825  CG  GLU A 447      17.026  70.171  38.300  1.00132.55           C  
ANISOU 2825  CG  GLU A 447    10244  21429  18689  -2320  -2615   -495       C  
ATOM   2826  CD  GLU A 447      15.602  70.654  38.068  1.00138.11           C  
ANISOU 2826  CD  GLU A 447    10658  22520  19298  -2218  -2646   -489       C  
ATOM   2827  OE1 GLU A 447      14.743  69.830  37.685  1.00141.07           O  
ANISOU 2827  OE1 GLU A 447    10905  22865  19830  -2460  -2804   -400       O  
ATOM   2828  OE2 GLU A 447      15.345  71.861  38.264  1.00138.14           O  
ANISOU 2828  OE2 GLU A 447    10606  22806  19074  -1871  -2517   -582       O  
ATOM   2829  N   PHE A 448      20.388  69.189  37.382  1.00134.36           N  
ANISOU 2829  N   PHE A 448    11495  20420  19137  -2330  -2666   -744       N  
ATOM   2830  CA  PHE A 448      21.618  69.948  37.572  1.00142.05           C  
ANISOU 2830  CA  PHE A 448    12767  21215  19991  -2067  -2492   -835       C  
ATOM   2831  C   PHE A 448      22.451  69.989  36.298  1.00137.48           C  
ANISOU 2831  C   PHE A 448    12540  20282  19414  -1924  -2597  -1051       C  
ATOM   2832  O   PHE A 448      23.122  70.990  36.030  1.00143.30           O  
ANISOU 2832  O   PHE A 448    13472  20966  20009  -1634  -2493  -1163       O  
ATOM   2833  CB  PHE A 448      22.442  69.346  38.710  1.00153.28           C  
ANISOU 2833  CB  PHE A 448    14250  22502  21487  -2229  -2370   -664       C  
ATOM   2834  CG  PHE A 448      21.799  69.467  40.059  1.00163.59           C  
ANISOU 2834  CG  PHE A 448    15227  24191  22738  -2305  -2222   -443       C  
ATOM   2835  CD1 PHE A 448      20.756  70.354  40.273  1.00166.58           C  
ANISOU 2835  CD1 PHE A 448    15322  25011  22958  -2133  -2161   -440       C  
ATOM   2836  CD2 PHE A 448      22.247  68.698  41.120  1.00167.89           C  
ANISOU 2836  CD2 PHE A 448    15742  24675  23372  -2524  -2146   -238       C  
ATOM   2837  CE1 PHE A 448      20.167  70.465  41.516  1.00169.46           C  
ANISOU 2837  CE1 PHE A 448    15368  25781  23239  -2166  -2022   -239       C  
ATOM   2838  CE2 PHE A 448      21.663  68.805  42.366  1.00171.03           C  
ANISOU 2838  CE2 PHE A 448    15823  25467  23694  -2575  -2003    -21       C  
ATOM   2839  CZ  PHE A 448      20.621  69.690  42.564  1.00170.46           C  
ANISOU 2839  CZ  PHE A 448    15457  25864  23447  -2388  -1938    -22       C  
ATOM   2840  N   LEU A 449      22.418  68.916  35.506  1.00133.76           N  
ANISOU 2840  N   LEU A 449    12149  19577  19097  -2115  -2819  -1106       N  
ATOM   2841  CA  LEU A 449      23.261  68.844  34.317  1.00121.76           C  
ANISOU 2841  CA  LEU A 449    10957  17747  17557  -1962  -2923  -1309       C  
ATOM   2842  C   LEU A 449      22.914  69.943  33.321  1.00115.86           C  
ANISOU 2842  C   LEU A 449    10235  17143  16642  -1660  -2933  -1477       C  
ATOM   2843  O   LEU A 449      23.808  70.545  32.715  1.00115.61           O  
ANISOU 2843  O   LEU A 449    10457  16973  16496  -1418  -2879  -1589       O  
ATOM   2844  CB  LEU A 449      23.129  67.466  33.672  1.00118.59           C  
ANISOU 2844  CB  LEU A 449    10614  17097  17347  -2201  -3202  -1357       C  
ATOM   2845  CG  LEU A 449      24.178  67.109  32.623  1.00114.34           C  
ANISOU 2845  CG  LEU A 449    10430  16222  16791  -2056  -3316  -1552       C  
ATOM   2846  CD1 LEU A 449      25.376  66.443  33.277  1.00109.19           C  
ANISOU 2846  CD1 LEU A 449     9982  15294  16210  -2144  -3250  -1481       C  
ATOM   2847  CD2 LEU A 449      23.564  66.205  31.564  1.00120.46           C  
ANISOU 2847  CD2 LEU A 449    11212  16874  17684  -2161  -3646  -1690       C  
ATOM   2848  N   ALA A 450      21.620  70.223  33.140  1.00113.10           N  
ANISOU 2848  N   ALA A 450     9615  17086  16273  -1673  -3007  -1480       N  
ATOM   2849  CA  ALA A 450      21.219  71.326  32.272  1.00108.19           C  
ANISOU 2849  CA  ALA A 450     9001  16620  15485  -1378  -3015  -1628       C  
ATOM   2850  C   ALA A 450      21.601  72.671  32.868  1.00112.62           C  
ANISOU 2850  C   ALA A 450     9602  17314  15876  -1112  -2792  -1602       C  
ATOM   2851  O   ALA A 450      21.910  73.611  32.127  1.00116.85           O  
ANISOU 2851  O   ALA A 450    10296  17823  16277   -838  -2780  -1717       O  
ATOM   2852  CB  ALA A 450      19.715  71.277  32.011  1.00104.88           C  
ANISOU 2852  CB  ALA A 450     8263  16500  15085  -1458  -3150  -1632       C  
ATOM   2853  N   GLN A 451      21.577  72.785  34.197  1.00109.04           N  
ANISOU 2853  N   GLN A 451     9006  17000  15424  -1182  -2634  -1446       N  
ATOM   2854  CA  GLN A 451      21.996  74.023  34.843  1.00102.69           C  
ANISOU 2854  CA  GLN A 451     8259  16287  14469   -922  -2455  -1435       C  
ATOM   2855  C   GLN A 451      23.480  74.282  34.611  1.00 93.21           C  
ANISOU 2855  C   GLN A 451     7412  14754  13250   -806  -2386  -1474       C  
ATOM   2856  O   GLN A 451      23.886  75.425  34.373  1.00 89.00           O  
ANISOU 2856  O   GLN A 451     7018  14204  12594   -540  -2335  -1532       O  
ATOM   2857  CB  GLN A 451      21.675  73.963  36.339  1.00105.90           C  
ANISOU 2857  CB  GLN A 451     8435  16928  14874  -1017  -2314  -1267       C  
ATOM   2858  CG  GLN A 451      21.482  75.317  37.014  1.00112.11           C  
ANISOU 2858  CG  GLN A 451     9158  17959  15481   -714  -2190  -1285       C  
ATOM   2859  CD  GLN A 451      20.248  76.056  36.526  1.00124.74           C  
ANISOU 2859  CD  GLN A 451    10551  19880  16963   -533  -2270  -1376       C  
ATOM   2860  OE1 GLN A 451      20.350  77.064  35.826  1.00129.09           O  
ANISOU 2860  OE1 GLN A 451    11253  20384  17409   -261  -2311  -1512       O  
ATOM   2861  NE2 GLN A 451      19.074  75.559  36.902  1.00130.82           N  
ANISOU 2861  NE2 GLN A 451    10967  20990  17749   -686  -2299  -1285       N  
ATOM   2862  N   PHE A 452      24.304  73.229  34.667  1.00 90.40           N  
ANISOU 2862  N   PHE A 452     7200  14131  13017  -1002  -2400  -1431       N  
ATOM   2863  CA  PHE A 452      25.723  73.392  34.368  1.00 94.48           C  
ANISOU 2863  CA  PHE A 452     8032  14358  13508   -895  -2342  -1463       C  
ATOM   2864  C   PHE A 452      25.938  73.725  32.898  1.00103.52           C  
ANISOU 2864  C   PHE A 452     9346  15412  14574   -716  -2453  -1607       C  
ATOM   2865  O   PHE A 452      26.787  74.559  32.560  1.00110.26           O  
ANISOU 2865  O   PHE A 452    10391  16174  15328   -512  -2388  -1622       O  
ATOM   2866  CB  PHE A 452      26.508  72.128  34.736  1.00 95.39           C  
ANISOU 2866  CB  PHE A 452     8255  14226  13762  -1128  -2348  -1398       C  
ATOM   2867  CG  PHE A 452      26.409  71.734  36.188  1.00100.07           C  
ANISOU 2867  CG  PHE A 452     8696  14899  14429  -1313  -2234  -1231       C  
ATOM   2868  CD1 PHE A 452      26.027  72.651  37.155  1.00102.66           C  
ANISOU 2868  CD1 PHE A 452     8866  15476  14663  -1201  -2092  -1159       C  
ATOM   2869  CD2 PHE A 452      26.742  70.448  36.588  1.00 99.48           C  
ANISOU 2869  CD2 PHE A 452     8646  14645  14506  -1579  -2279  -1149       C  
ATOM   2870  CE1 PHE A 452      25.946  72.283  38.487  1.00100.16           C  
ANISOU 2870  CE1 PHE A 452     8399  15269  14388  -1347  -1981  -1000       C  
ATOM   2871  CE2 PHE A 452      26.669  70.075  37.920  1.00 94.65           C  
ANISOU 2871  CE2 PHE A 452     7890  14119  13955  -1750  -2172   -972       C  
ATOM   2872  CZ  PHE A 452      26.271  70.994  38.870  1.00 94.28           C  
ANISOU 2872  CZ  PHE A 452     7667  14357  13796  -1631  -2013   -894       C  
ATOM   2873  N   HIS A 453      25.177  73.076  32.012  1.00104.80           N  
ANISOU 2873  N   HIS A 453     9434  15606  14781   -793  -2633  -1701       N  
ATOM   2874  CA  HIS A 453      25.306  73.334  30.583  1.00 99.94           C  
ANISOU 2874  CA  HIS A 453     8962  14938  14073   -609  -2750  -1844       C  
ATOM   2875  C   HIS A 453      25.049  74.802  30.261  1.00 99.40           C  
ANISOU 2875  C   HIS A 453     8886  15034  13846   -335  -2695  -1867       C  
ATOM   2876  O   HIS A 453      25.735  75.387  29.415  1.00104.31           O  
ANISOU 2876  O   HIS A 453     9698  15574  14360   -138  -2696  -1907       O  
ATOM   2877  CB  HIS A 453      24.342  72.434  29.806  1.00 99.94           C  
ANISOU 2877  CB  HIS A 453     8846  14976  14152   -735  -2973  -1950       C  
ATOM   2878  CG  HIS A 453      24.843  71.036  29.600  1.00106.28           C  
ANISOU 2878  CG  HIS A 453     9767  15525  15087   -923  -3105  -1986       C  
ATOM   2879  ND1 HIS A 453      24.171  70.112  28.826  1.00107.73           N  
ANISOU 2879  ND1 HIS A 453     9906  15666  15362  -1033  -3355  -2100       N  
ATOM   2880  CD2 HIS A 453      25.946  70.403  30.067  1.00106.13           C  
ANISOU 2880  CD2 HIS A 453     9921  15274  15130  -1006  -3047  -1933       C  
ATOM   2881  CE1 HIS A 453      24.839  68.972  28.825  1.00108.98           C  
ANISOU 2881  CE1 HIS A 453    10214  15560  15633  -1169  -3458  -2123       C  
ATOM   2882  NE2 HIS A 453      25.920  69.122  29.570  1.00107.35           N  
ANISOU 2882  NE2 HIS A 453    10139  15243  15405  -1152  -3267  -2022       N  
ATOM   2883  N   LEU A 454      24.075  75.419  30.937  1.00 91.00           N  
ANISOU 2883  N   LEU A 454     7601  14214  12760   -312  -2655  -1831       N  
ATOM   2884  CA  LEU A 454      23.742  76.811  30.650  1.00 89.91           C  
ANISOU 2884  CA  LEU A 454     7460  14223  12479    -39  -2639  -1867       C  
ATOM   2885  C   LEU A 454      24.920  77.731  30.941  1.00 95.67           C  
ANISOU 2885  C   LEU A 454     8409  14796  13145    123  -2520  -1799       C  
ATOM   2886  O   LEU A 454      25.226  78.635  30.154  1.00103.86           O  
ANISOU 2886  O   LEU A 454     9585  15797  14080    333  -2553  -1825       O  
ATOM   2887  CB  LEU A 454      22.522  77.250  31.463  1.00 84.58           C  
ANISOU 2887  CB  LEU A 454     6500  13856  11779    -23  -2618  -1847       C  
ATOM   2888  CG  LEU A 454      21.147  77.037  30.825  1.00106.43           C  
ANISOU 2888  CG  LEU A 454     9039  16863  14538    -44  -2763  -1933       C  
ATOM   2889  CD1 LEU A 454      20.062  77.716  31.655  1.00112.67           C  
ANISOU 2889  CD1 LEU A 454     9554  18000  15255     46  -2720  -1907       C  
ATOM   2890  CD2 LEU A 454      21.110  77.491  29.367  1.00110.14           C  
ANISOU 2890  CD2 LEU A 454     9645  17285  14917    147  -2889  -2062       C  
ATOM   2891  N   VAL A 455      25.592  77.513  32.073  1.00 94.51           N  
ANISOU 2891  N   VAL A 455     8292  14556  13061     18  -2392  -1698       N  
ATOM   2892  CA  VAL A 455      26.641  78.431  32.503  1.00 87.89           C  
ANISOU 2892  CA  VAL A 455     7637  13580  12178    158  -2294  -1625       C  
ATOM   2893  C   VAL A 455      27.875  78.289  31.620  1.00 87.34           C  
ANISOU 2893  C   VAL A 455     7816  13277  12093    185  -2299  -1605       C  
ATOM   2894  O   VAL A 455      28.486  79.286  31.217  1.00 89.19           O  
ANISOU 2894  O   VAL A 455     8196  13440  12251    360  -2297  -1564       O  
ATOM   2895  CB  VAL A 455      26.956  78.199  33.990  1.00 78.92           C  
ANISOU 2895  CB  VAL A 455     6446  12434  11108     45  -2164  -1531       C  
ATOM   2896  CG1 VAL A 455      27.998  79.184  34.475  1.00 81.53           C  
ANISOU 2896  CG1 VAL A 455     6960  12615  11403    193  -2090  -1466       C  
ATOM   2897  CG2 VAL A 455      25.687  78.335  34.809  1.00 75.52           C  
ANISOU 2897  CG2 VAL A 455     5736  12301  10656     45  -2157  -1539       C  
ATOM   2898  N   ILE A 456      28.248  77.054  31.290  1.00 81.84           N  
ANISOU 2898  N   ILE A 456     7163  12470  11463     20  -2321  -1627       N  
ATOM   2899  CA  ILE A 456      29.386  76.828  30.404  1.00 79.85           C  
ANISOU 2899  CA  ILE A 456     7125  12050  11166     74  -2330  -1621       C  
ATOM   2900  C   ILE A 456      29.136  77.454  29.035  1.00 81.16           C  
ANISOU 2900  C   ILE A 456     7337  12296  11203    273  -2433  -1683       C  
ATOM   2901  O   ILE A 456      30.034  78.065  28.443  1.00 77.52           O  
ANISOU 2901  O   ILE A 456     7030  11772  10652    413  -2409  -1614       O  
ATOM   2902  CB  ILE A 456      29.672  75.321  30.298  1.00 78.15           C  
ANISOU 2902  CB  ILE A 456     6940  11714  11038   -112  -2375  -1669       C  
ATOM   2903  CG1 ILE A 456      30.053  74.770  31.665  1.00 71.15           C  
ANISOU 2903  CG1 ILE A 456     6029  10736  10271   -301  -2265  -1577       C  
ATOM   2904  CG2 ILE A 456      30.777  75.051  29.303  1.00 77.16           C  
ANISOU 2904  CG2 ILE A 456     7019  11468  10830     -9  -2398  -1688       C  
ATOM   2905  CD1 ILE A 456      29.790  73.307  31.794  1.00 73.79           C  
ANISOU 2905  CD1 ILE A 456     6315  10992  10731   -527  -2352  -1619       C  
ATOM   2906  N   LYS A 457      27.917  77.312  28.508  1.00 83.57           N  
ANISOU 2906  N   LYS A 457     7497  12759  11497    284  -2552  -1797       N  
ATOM   2907  CA  LYS A 457      27.571  77.994  27.264  1.00 89.40           C  
ANISOU 2907  CA  LYS A 457     8265  13598  12104    489  -2652  -1856       C  
ATOM   2908  C   LYS A 457      27.715  79.505  27.405  1.00 93.22           C  
ANISOU 2908  C   LYS A 457     8796  14112  12511    675  -2607  -1760       C  
ATOM   2909  O   LYS A 457      28.223  80.173  26.499  1.00 99.29           O  
ANISOU 2909  O   LYS A 457     9690  14864  13172    838  -2636  -1711       O  
ATOM   2910  CB  LYS A 457      26.148  77.629  26.841  1.00 90.76           C  
ANISOU 2910  CB  LYS A 457     8250  13945  12291    461  -2790  -1993       C  
ATOM   2911  CG  LYS A 457      25.718  78.175  25.481  1.00 84.28           C  
ANISOU 2911  CG  LYS A 457     7453  13237  11332    670  -2910  -2076       C  
ATOM   2912  CD  LYS A 457      24.324  77.667  25.135  1.00 85.75           C  
ANISOU 2912  CD  LYS A 457     7441  13588  11552    613  -3057  -2218       C  
ATOM   2913  CE  LYS A 457      23.862  78.095  23.755  1.00 80.27           C  
ANISOU 2913  CE  LYS A 457     6768  13011  10719    821  -3190  -2319       C  
ATOM   2914  NZ  LYS A 457      22.538  77.488  23.442  1.00 82.41           N  
ANISOU 2914  NZ  LYS A 457     6841  13432  11041    741  -3349  -2461       N  
ATOM   2915  N   ARG A 458      27.284  80.061  28.540  1.00 90.42           N  
ANISOU 2915  N   ARG A 458     8345  13805  12207    662  -2552  -1727       N  
ATOM   2916  CA  ARG A 458      27.382  81.505  28.736  1.00 90.14           C  
ANISOU 2916  CA  ARG A 458     8370  13766  12112    852  -2554  -1657       C  
ATOM   2917  C   ARG A 458      28.837  81.956  28.845  1.00 86.92           C  
ANISOU 2917  C   ARG A 458     8169  13149  11707    873  -2483  -1504       C  
ATOM   2918  O   ARG A 458      29.193  83.047  28.383  1.00 89.40           O  
ANISOU 2918  O   ARG A 458     8593  13415  11959   1029  -2533  -1418       O  
ATOM   2919  CB  ARG A 458      26.609  81.922  29.989  1.00 89.35           C  
ANISOU 2919  CB  ARG A 458     8120  13780  12050    863  -2526  -1681       C  
ATOM   2920  CG  ARG A 458      26.519  83.435  30.189  1.00 88.22           C  
ANISOU 2920  CG  ARG A 458     8040  13636  11846   1097  -2582  -1653       C  
ATOM   2921  CD  ARG A 458      26.621  83.840  31.659  1.00 83.56           C  
ANISOU 2921  CD  ARG A 458     7418  13032  11298   1114  -2516  -1625       C  
ATOM   2922  NE  ARG A 458      25.376  83.661  32.405  1.00 88.17           N  
ANISOU 2922  NE  ARG A 458     7756  13882  11863   1126  -2512  -1722       N  
ATOM   2923  CZ  ARG A 458      25.121  82.634  33.214  1.00 87.43           C  
ANISOU 2923  CZ  ARG A 458     7499  13891  11829    931  -2413  -1715       C  
ATOM   2924  NH1 ARG A 458      26.034  81.690  33.408  1.00 81.56           N  
ANISOU 2924  NH1 ARG A 458     6836  12975  11177    717  -2320  -1638       N  
ATOM   2925  NH2 ARG A 458      23.955  82.562  33.847  1.00 83.38           N  
ANISOU 2925  NH2 ARG A 458     6732  13669  11278    955  -2412  -1773       N  
ATOM   2926  N   VAL A 459      29.690  81.137  29.461  1.00 69.81           N  
ANISOU 2926  N   VAL A 459     6052  10857   9617    709  -2378  -1453       N  
ATOM   2927  CA  VAL A 459      31.073  81.548  29.681  1.00 73.49           C  
ANISOU 2927  CA  VAL A 459     6689  11141  10093    715  -2306  -1298       C  
ATOM   2928  C   VAL A 459      31.845  81.537  28.367  1.00 75.81           C  
ANISOU 2928  C   VAL A 459     7105  11413  10288    788  -2335  -1230       C  
ATOM   2929  O   VAL A 459      32.536  82.506  28.027  1.00 68.37           O  
ANISOU 2929  O   VAL A 459     6270  10409   9300    889  -2351  -1082       O  
ATOM   2930  CB  VAL A 459      31.737  80.651  30.746  1.00 76.81           C  
ANISOU 2930  CB  VAL A 459     7119  11450  10615    531  -2186  -1269       C  
ATOM   2931  CG1 VAL A 459      33.252  80.729  30.652  1.00 65.95           C  
ANISOU 2931  CG1 VAL A 459     5914   9910   9235    518  -2117  -1123       C  
ATOM   2932  CG2 VAL A 459      31.275  81.052  32.143  1.00 67.00           C  
ANISOU 2932  CG2 VAL A 459     5785  10232   9439    513  -2144  -1275       C  
ATOM   2933  N   LEU A 460      31.722  80.448  27.602  1.00 84.56           N  
ANISOU 2933  N   LEU A 460     8190  12580  11357    744  -2358  -1330       N  
ATOM   2934  CA  LEU A 460      32.449  80.324  26.341  1.00 76.99           C  
ANISOU 2934  CA  LEU A 460     7332  11650  10271    844  -2383  -1283       C  
ATOM   2935  C   LEU A 460      32.028  81.389  25.335  1.00 72.17           C  
ANISOU 2935  C   LEU A 460     6726  11154   9541   1035  -2478  -1241       C  
ATOM   2936  O   LEU A 460      32.848  81.841  24.529  1.00 70.87           O  
ANISOU 2936  O   LEU A 460     6652  11009   9267   1138  -2475  -1096       O  
ATOM   2937  CB  LEU A 460      32.222  78.935  25.760  1.00 70.35           C  
ANISOU 2937  CB  LEU A 460     6466  10852   9411    792  -2432  -1447       C  
ATOM   2938  CG  LEU A 460      32.654  77.750  26.614  1.00 74.90           C  
ANISOU 2938  CG  LEU A 460     7054  11299  10105    604  -2370  -1488       C  
ATOM   2939  CD1 LEU A 460      31.939  76.506  26.124  1.00 78.41           C  
ANISOU 2939  CD1 LEU A 460     7443  11775  10573    542  -2492  -1682       C  
ATOM   2940  CD2 LEU A 460      34.158  77.569  26.538  1.00 68.59           C  
ANISOU 2940  CD2 LEU A 460     6395  10411   9254    624  -2278  -1365       C  
ATOM   2941  N   ILE A 461      30.758  81.794  25.359  1.00 71.59           N  
ANISOU 2941  N   ILE A 461     6546  11177   9480   1087  -2564  -1351       N  
ATOM   2942  CA  ILE A 461      30.317  82.908  24.527  1.00 76.12           C  
ANISOU 2942  CA  ILE A 461     7130  11841   9950   1274  -2664  -1307       C  
ATOM   2943  C   ILE A 461      30.955  84.211  24.998  1.00 85.54           C  
ANISOU 2943  C   ILE A 461     8421  12907  11172   1328  -2658  -1108       C  
ATOM   2944  O   ILE A 461      31.497  84.982  24.196  1.00 89.47           O  
ANISOU 2944  O   ILE A 461     9007  13405  11584   1436  -2702   -944       O  
ATOM   2945  CB  ILE A 461      28.781  82.994  24.531  1.00 73.90           C  
ANISOU 2945  CB  ILE A 461     6700  11702   9677   1321  -2762  -1486       C  
ATOM   2946  CG1 ILE A 461      28.204  81.889  23.655  1.00 78.22           C  
ANISOU 2946  CG1 ILE A 461     7172  12373  10173   1303  -2826  -1655       C  
ATOM   2947  CG2 ILE A 461      28.308  84.360  24.053  1.00 74.87           C  
ANISOU 2947  CG2 ILE A 461     6844  11879   9725   1519  -2866  -1431       C  
ATOM   2948  CD1 ILE A 461      26.813  81.497  24.013  1.00 76.02           C  
ANISOU 2948  CD1 ILE A 461     6710  12216   9960   1242  -2893  -1828       C  
ATOM   2949  N   ASN A 462      30.903  84.474  26.308  1.00 82.42           N  
ANISOU 2949  N   ASN A 462     8010  12405  10900   1255  -2618  -1110       N  
ATOM   2950  CA  ASN A 462      31.474  85.701  26.853  1.00 86.42           C  
ANISOU 2950  CA  ASN A 462     8621  12757  11456   1309  -2652   -946       C  
ATOM   2951  C   ASN A 462      32.997  85.695  26.829  1.00 90.28           C  
ANISOU 2951  C   ASN A 462     9235  13106  11961   1228  -2575   -732       C  
ATOM   2952  O   ASN A 462      33.613  86.764  26.901  1.00 91.58           O  
ANISOU 2952  O   ASN A 462     9500  13142  12154   1271  -2638   -545       O  
ATOM   2953  CB  ASN A 462      30.953  85.924  28.272  1.00 84.25           C  
ANISOU 2953  CB  ASN A 462     8290  12437  11286   1288  -2643  -1039       C  
ATOM   2954  CG  ASN A 462      29.465  86.213  28.294  1.00 91.14           C  
ANISOU 2954  CG  ASN A 462     9027  13480  12121   1410  -2735  -1215       C  
ATOM   2955  OD1 ASN A 462      28.930  86.805  27.357  1.00 92.63           O  
ANISOU 2955  OD1 ASN A 462     9221  13749  12226   1554  -2849  -1227       O  
ATOM   2956  ND2 ASN A 462      28.787  85.792  29.356  1.00 92.75           N  
ANISOU 2956  ND2 ASN A 462     9097  13766  12376   1358  -2684  -1341       N  
ATOM   2957  N   ILE A 463      33.608  84.514  26.730  1.00 89.43           N  
ANISOU 2957  N   ILE A 463     9121  13020  11840   1112  -2459   -752       N  
ATOM   2958  CA  ILE A 463      35.036  84.407  26.462  1.00 90.02           C  
ANISOU 2958  CA  ILE A 463     9288  13028  11885   1064  -2385   -553       C  
ATOM   2959  C   ILE A 463      35.330  84.712  24.994  1.00 99.63           C  
ANISOU 2959  C   ILE A 463    10532  14384  12941   1189  -2435   -427       C  
ATOM   2960  O   ILE A 463      36.419  85.199  24.662  1.00106.47           O  
ANISOU 2960  O   ILE A 463    11463  15225  13768   1191  -2416   -180       O  
ATOM   2961  CB  ILE A 463      35.510  82.996  26.866  1.00 85.23           C  
ANISOU 2961  CB  ILE A 463     8667  12411  11306    929  -2260   -646       C  
ATOM   2962  CG1 ILE A 463      35.847  82.925  28.344  1.00 91.19           C  
ANISOU 2962  CG1 ILE A 463     9435  13002  12211    797  -2185   -639       C  
ATOM   2963  CG2 ILE A 463      36.705  82.547  26.070  1.00 84.74           C  
ANISOU 2963  CG2 ILE A 463     8665  12400  11134    944  -2199   -515       C  
ATOM   2964  CD1 ILE A 463      36.295  81.542  28.742  1.00 94.92           C  
ANISOU 2964  CD1 ILE A 463     9901  13451  12715    664  -2077   -720       C  
ATOM   2965  N   HIS A 464      34.353  84.480  24.105  1.00 98.62           N  
ANISOU 2965  N   HIS A 464    10339  14420  12711   1297  -2506   -576       N  
ATOM   2966  CA  HIS A 464      34.553  84.436  22.649  1.00 87.60           C  
ANISOU 2966  CA  HIS A 464     8948  13209  11128   1432  -2541   -509       C  
ATOM   2967  C   HIS A 464      35.514  83.301  22.294  1.00 88.44           C  
ANISOU 2967  C   HIS A 464     9072  13385  11147   1404  -2438   -508       C  
ATOM   2968  O   HIS A 464      36.457  83.467  21.517  1.00 89.77           O  
ANISOU 2968  O   HIS A 464     9271  13662  11177   1479  -2407   -313       O  
ATOM   2969  CB  HIS A 464      35.038  85.780  22.088  1.00 80.65           C  
ANISOU 2969  CB  HIS A 464     8125  12328  10191   1520  -2608   -222       C  
ATOM   2970  CG  HIS A 464      34.957  85.886  20.593  1.00 91.12           C  
ANISOU 2970  CG  HIS A 464     9432  13883  11309   1687  -2661   -157       C  
ATOM   2971  ND1 HIS A 464      33.825  85.556  19.879  1.00 97.65           N  
ANISOU 2971  ND1 HIS A 464    10198  14860  12045   1807  -2739   -379       N  
ATOM   2972  CD2 HIS A 464      35.873  86.284  19.678  1.00 96.67           C  
ANISOU 2972  CD2 HIS A 464    10153  14713  11863   1759  -2649    116       C  
ATOM   2973  CE1 HIS A 464      34.046  85.751  18.590  1.00100.16           C  
ANISOU 2973  CE1 HIS A 464    10511  15380  12163   1962  -2773   -261       C  
ATOM   2974  NE2 HIS A 464      35.282  86.193  18.441  1.00 96.74           N  
ANISOU 2974  NE2 HIS A 464    10120  14952  11685   1937  -2713     48       N  
ATOM   2975  N   ALA A 465      35.267  82.137  22.897  1.00 87.56           N  
ANISOU 2975  N   ALA A 465     8935  13221  11115   1299  -2395   -721       N  
ATOM   2976  CA  ALA A 465      36.078  80.951  22.659  1.00 86.23           C  
ANISOU 2976  CA  ALA A 465     8797  13089  10878   1283  -2328   -770       C  
ATOM   2977  C   ALA A 465      35.754  80.345  21.298  1.00104.11           C  
ANISOU 2977  C   ALA A 465    11043  15560  12952   1456  -2410   -904       C  
ATOM   2978  O   ALA A 465      34.594  80.033  21.005  1.00 95.53           O  
ANISOU 2978  O   ALA A 465     9901  14518  11877   1485  -2515  -1114       O  
ATOM   2979  CB  ALA A 465      35.833  79.922  23.760  1.00 70.02           C  
ANISOU 2979  CB  ALA A 465     6729  10886   8989   1108  -2289   -948       C  
ATOM   2980  N   GLN A 466      36.788  80.173  20.468  1.00113.22           N  
ANISOU 2980  N   GLN A 466    12236  16863  13922   1583  -2369   -783       N  
ATOM   2981  CA  GLN A 466      36.641  79.579  19.150  1.00112.55           C  
ANISOU 2981  CA  GLN A 466    12142  17003  13619   1792  -2448   -909       C  
ATOM   2982  C   GLN A 466      36.447  78.067  19.262  1.00114.98           C  
ANISOU 2982  C   GLN A 466    12476  17252  13959   1768  -2503  -1204       C  
ATOM   2983  O   GLN A 466      36.890  77.448  20.233  1.00113.78           O  
ANISOU 2983  O   GLN A 466    12359  16923  13948   1609  -2438  -1233       O  
ATOM   2984  CB  GLN A 466      37.863  79.892  18.289  1.00109.64           C  
ANISOU 2984  CB  GLN A 466    11787  16853  13019   1955  -2379   -664       C  
ATOM   2985  CG  GLN A 466      38.094  81.381  18.066  1.00114.75           C  
ANISOU 2985  CG  GLN A 466    12409  17555  13637   1967  -2358   -333       C  
ATOM   2986  CD  GLN A 466      36.821  82.118  17.673  1.00119.49           C  
ANISOU 2986  CD  GLN A 466    12977  18169  14256   2023  -2480   -400       C  
ATOM   2987  OE1 GLN A 466      36.225  81.840  16.631  1.00127.92           O  
ANISOU 2987  OE1 GLN A 466    14017  19428  15160   2202  -2568   -540       O  
ATOM   2988  NE2 GLN A 466      36.396  83.058  18.511  1.00108.66           N  
ANISOU 2988  NE2 GLN A 466    11612  16600  13076   1889  -2499   -314       N  
ATOM   2989  N   PRO A 467      35.769  77.444  18.275  1.00117.03           N  
ANISOU 2989  N   PRO A 467    12725  17643  14099   1924  -2645  -1428       N  
ATOM   2990  CA  PRO A 467      35.496  76.002  18.317  1.00117.06           C  
ANISOU 2990  CA  PRO A 467    12766  17559  14154   1901  -2756  -1721       C  
ATOM   2991  C   PRO A 467      36.644  75.145  17.784  1.00117.73           C  
ANISOU 2991  C   PRO A 467    12935  17741  14056   2070  -2748  -1757       C  
ATOM   2992  O   PRO A 467      36.439  74.206  17.008  1.00118.76           O  
ANISOU 2992  O   PRO A 467    13106  17941  14075   2233  -2903  -1999       O  
ATOM   2993  CB  PRO A 467      34.244  75.874  17.449  1.00112.04           C  
ANISOU 2993  CB  PRO A 467    12080  17024  13467   2010  -2939  -1934       C  
ATOM   2994  CG  PRO A 467      34.420  76.939  16.428  1.00113.95           C  
ANISOU 2994  CG  PRO A 467    12296  17516  13482   2229  -2911  -1758       C  
ATOM   2995  CD  PRO A 467      35.093  78.091  17.135  1.00115.10           C  
ANISOU 2995  CD  PRO A 467    12434  17607  13691   2117  -2738  -1430       C  
ATOM   2996  N   ASN A 468      37.867  75.456  18.208  1.00112.25           N  
ANISOU 2996  N   ASN A 468    12267  17056  13327   2045  -2582  -1525       N  
ATOM   2997  CA  ASN A 468      39.029  74.681  17.792  1.00105.90           C  
ANISOU 2997  CA  ASN A 468    11528  16372  12338   2216  -2557  -1542       C  
ATOM   2998  C   ASN A 468      39.178  73.424  18.639  1.00 98.30           C  
ANISOU 2998  C   ASN A 468    10648  15157  11544   2078  -2603  -1743       C  
ATOM   2999  O   ASN A 468      38.224  72.995  19.296  1.00 99.34           O  
ANISOU 2999  O   ASN A 468    10777  15061  11908   1878  -2694  -1904       O  
ATOM   3000  CB  ASN A 468      40.293  75.538  17.865  1.00104.26           C  
ANISOU 3000  CB  ASN A 468    11291  16305  12019   2242  -2368  -1188       C  
ATOM   3001  CG  ASN A 468      40.387  76.327  19.153  1.00 95.09           C  
ANISOU 3001  CG  ASN A 468    10111  14909  11109   1955  -2245   -984       C  
ATOM   3002  OD1 ASN A 468      40.007  75.847  20.222  1.00 85.75           O  
ANISOU 3002  OD1 ASN A 468     8959  13461  10162   1745  -2251  -1110       O  
ATOM   3003  ND2 ASN A 468      40.886  77.555  19.054  1.00 93.70           N  
ANISOU 3003  ND2 ASN A 468     9885  14834  10885   1949  -2149   -660       N  
ATOM   3004  N   ALA A 469      40.377  72.833  18.635  1.00 90.49           N  
ANISOU 3004  N   ALA A 469     9723  14223  10436   2184  -2545  -1718       N  
ATOM   3005  CA  ALA A 469      40.598  71.571  19.332  1.00 84.43           C  
ANISOU 3005  CA  ALA A 469     9055  13221   9805   2090  -2614  -1914       C  
ATOM   3006  C   ALA A 469      40.320  71.671  20.822  1.00 88.38           C  
ANISOU 3006  C   ALA A 469     9543  13415  10623   1737  -2529  -1840       C  
ATOM   3007  O   ALA A 469      40.022  70.653  21.455  1.00 93.21           O  
ANISOU 3007  O   ALA A 469    10215  13790  11410   1595  -2629  -2019       O  
ATOM   3008  CB  ALA A 469      42.031  71.092  19.112  1.00 83.52           C  
ANISOU 3008  CB  ALA A 469     9000  13248   9487   2284  -2542  -1863       C  
ATOM   3009  N   VAL A 470      40.401  72.871  21.393  1.00 88.82           N  
ANISOU 3009  N   VAL A 470     9524  13471  10754   1600  -2366  -1579       N  
ATOM   3010  CA  VAL A 470      40.226  73.025  22.831  1.00 92.53           C  
ANISOU 3010  CA  VAL A 470     9979  13686  11491   1305  -2278  -1505       C  
ATOM   3011  C   VAL A 470      38.751  72.989  23.206  1.00 90.54           C  
ANISOU 3011  C   VAL A 470     9665  13307  11431   1141  -2384  -1644       C  
ATOM   3012  O   VAL A 470      38.353  72.313  24.162  1.00 86.84           O  
ANISOU 3012  O   VAL A 470     9198  12631  11166    933  -2411  -1731       O  
ATOM   3013  CB  VAL A 470      40.893  74.326  23.305  1.00 91.69           C  
ANISOU 3013  CB  VAL A 470     9827  13618  11392   1245  -2100  -1190       C  
ATOM   3014  CG1 VAL A 470      40.823  74.432  24.811  1.00 75.87           C  
ANISOU 3014  CG1 VAL A 470     7821  11368   9639    982  -2015  -1133       C  
ATOM   3015  CG2 VAL A 470      42.331  74.379  22.824  1.00101.63           C  
ANISOU 3015  CG2 VAL A 470    11114  15055  12447   1407  -2003  -1023       C  
ATOM   3016  N   TYR A 471      37.921  73.708  22.454  1.00 94.99           N  
ANISOU 3016  N   TYR A 471    10157  14013  11922   1233  -2445  -1651       N  
ATOM   3017  CA  TYR A 471      36.535  73.942  22.824  1.00 97.39           C  
ANISOU 3017  CA  TYR A 471    10369  14248  12387   1090  -2520  -1736       C  
ATOM   3018  C   TYR A 471      35.530  73.182  21.974  1.00107.48           C  
ANISOU 3018  C   TYR A 471    11628  15571  13638   1163  -2733  -1991       C  
ATOM   3019  O   TYR A 471      34.330  73.274  22.245  1.00101.36           O  
ANISOU 3019  O   TYR A 471    10756  14761  12995   1039  -2809  -2068       O  
ATOM   3020  CB  TYR A 471      36.218  75.438  22.748  1.00 97.18           C  
ANISOU 3020  CB  TYR A 471    10270  14325  12328   1125  -2448  -1553       C  
ATOM   3021  CG  TYR A 471      37.089  76.301  23.632  1.00102.53           C  
ANISOU 3021  CG  TYR A 471    10964  14928  13063   1039  -2280  -1302       C  
ATOM   3022  CD1 TYR A 471      37.005  76.209  25.013  1.00104.88           C  
ANISOU 3022  CD1 TYR A 471    11246  15038  13564    826  -2210  -1281       C  
ATOM   3023  CD2 TYR A 471      37.983  77.214  23.087  1.00 96.53           C  
ANISOU 3023  CD2 TYR A 471    10228  14292  12156   1169  -2206  -1074       C  
ATOM   3024  CE1 TYR A 471      37.788  76.992  25.827  1.00103.03           C  
ANISOU 3024  CE1 TYR A 471    11036  14725  13386    760  -2082  -1073       C  
ATOM   3025  CE2 TYR A 471      38.772  78.005  23.895  1.00 92.77           C  
ANISOU 3025  CE2 TYR A 471     9769  13725  11755   1075  -2087   -843       C  
ATOM   3026  CZ  TYR A 471      38.669  77.889  25.267  1.00 99.90           C  
ANISOU 3026  CZ  TYR A 471    10672  14423  12863    878  -2031   -859       C  
ATOM   3027  OH  TYR A 471      39.445  78.668  26.093  1.00102.57           O  
ANISOU 3027  OH  TYR A 471    11035  14657  13279    796  -1936   -649       O  
ATOM   3028  N   CYS A 472      35.972  72.450  20.949  1.00120.40           N  
ANISOU 3028  N   CYS A 472    13348  17299  15100   1374  -2843  -2129       N  
ATOM   3029  CA  CYS A 472      35.015  71.814  20.050  1.00129.85           C  
ANISOU 3029  CA  CYS A 472    14535  18540  16260   1471  -3075  -2382       C  
ATOM   3030  C   CYS A 472      34.154  70.805  20.798  1.00125.63           C  
ANISOU 3030  C   CYS A 472    13979  17770  15987   1217  -3221  -2547       C  
ATOM   3031  O   CYS A 472      32.920  70.873  20.759  1.00125.79           O  
ANISOU 3031  O   CYS A 472    13892  17791  16111   1119  -3334  -2631       O  
ATOM   3032  CB  CYS A 472      35.739  71.141  18.883  1.00142.76           C  
ANISOU 3032  CB  CYS A 472    16280  20315  17648   1775  -3183  -2520       C  
ATOM   3033  SG  CYS A 472      34.618  70.405  17.659  1.00153.89           S  
ANISOU 3033  SG  CYS A 472    17695  21788  18987   1945  -3504  -2852       S  
ATOM   3034  N   ARG A 473      34.794  69.870  21.501  1.00121.29           N  
ANISOU 3034  N   ARG A 473    13516  17024  15544   1100  -3224  -2575       N  
ATOM   3035  CA  ARG A 473      34.060  68.818  22.196  1.00116.45           C  
ANISOU 3035  CA  ARG A 473    12886  16176  15183    845  -3384  -2701       C  
ATOM   3036  C   ARG A 473      33.053  69.405  23.179  1.00105.32           C  
ANISOU 3036  C   ARG A 473    11303  14741  13971    575  -3299  -2578       C  
ATOM   3037  O   ARG A 473      31.878  69.016  23.193  1.00 97.88           O  
ANISOU 3037  O   ARG A 473    10258  13766  13167    434  -3464  -2681       O  
ATOM   3038  CB  ARG A 473      35.051  67.889  22.902  1.00119.12           C  
ANISOU 3038  CB  ARG A 473    13352  16310  15597    765  -3365  -2698       C  
ATOM   3039  CG  ARG A 473      34.420  66.675  23.551  1.00125.90           C  
ANISOU 3039  CG  ARG A 473    14217  16905  16715    503  -3564  -2812       C  
ATOM   3040  CD  ARG A 473      35.469  65.724  24.109  1.00133.30           C  
ANISOU 3040  CD  ARG A 473    15309  17637  17703    469  -3573  -2826       C  
ATOM   3041  NE  ARG A 473      36.398  65.256  23.084  1.00144.72           N  
ANISOU 3041  NE  ARG A 473    16924  19142  18919    802  -3673  -2984       N  
ATOM   3042  CZ  ARG A 473      37.269  64.266  23.259  1.00154.30           C  
ANISOU 3042  CZ  ARG A 473    18300  20191  20135    856  -3759  -3073       C  
ATOM   3043  NH1 ARG A 473      37.323  63.626  24.419  1.00156.69           N  
ANISOU 3043  NH1 ARG A 473    18625  20236  20675    577  -3761  -3008       N  
ATOM   3044  NH2 ARG A 473      38.077  63.904  22.271  1.00157.75           N  
ANISOU 3044  NH2 ARG A 473    18873  20739  20326   1206  -3851  -3227       N  
ATOM   3045  N   LEU A 474      33.492  70.372  23.987  1.00105.23           N  
ANISOU 3045  N   LEU A 474    11250  14766  13967    518  -3055  -2359       N  
ATOM   3046  CA  LEU A 474      32.639  70.928  25.031  1.00106.39           C  
ANISOU 3046  CA  LEU A 474    11238  14907  14278    299  -2966  -2248       C  
ATOM   3047  C   LEU A 474      31.522  71.790  24.447  1.00107.87           C  
ANISOU 3047  C   LEU A 474    11294  15282  14410    378  -3016  -2275       C  
ATOM   3048  O   LEU A 474      30.406  71.811  24.982  1.00107.42           O  
ANISOU 3048  O   LEU A 474    11078  15248  14488    212  -3058  -2285       O  
ATOM   3049  CB  LEU A 474      33.495  71.735  26.011  1.00106.19           C  
ANISOU 3049  CB  LEU A 474    11229  14858  14259    259  -2722  -2032       C  
ATOM   3050  CG  LEU A 474      32.830  72.497  27.165  1.00 93.19           C  
ANISOU 3050  CG  LEU A 474     9438  13234  12737    100  -2605  -1906       C  
ATOM   3051  CD1 LEU A 474      32.383  71.553  28.272  1.00 97.00           C  
ANISOU 3051  CD1 LEU A 474     9844  13589  13424   -171  -2629  -1912       C  
ATOM   3052  CD2 LEU A 474      33.755  73.578  27.704  1.00 69.61           C  
ANISOU 3052  CD2 LEU A 474     6502  10252   9695    165  -2408  -1717       C  
ATOM   3053  N   MET A 475      31.801  72.513  23.358  1.00107.63           N  
ANISOU 3053  N   MET A 475    11314  15409  14172    636  -3012  -2275       N  
ATOM   3054  CA  MET A 475      30.805  73.427  22.801  1.00105.60           C  
ANISOU 3054  CA  MET A 475    10944  15328  13850    731  -3053  -2287       C  
ATOM   3055  C   MET A 475      29.599  72.671  22.267  1.00108.98           C  
ANISOU 3055  C   MET A 475    11285  15781  14341    685  -3284  -2496       C  
ATOM   3056  O   MET A 475      28.461  73.138  22.386  1.00112.42           O  
ANISOU 3056  O   MET A 475    11565  16317  14832    629  -3322  -2508       O  
ATOM   3057  CB  MET A 475      31.428  74.280  21.697  1.00104.36           C  
ANISOU 3057  CB  MET A 475    10867  15334  13453   1013  -3013  -2221       C  
ATOM   3058  CG  MET A 475      32.022  75.592  22.180  1.00104.96           C  
ANISOU 3058  CG  MET A 475    10949  15437  13492   1042  -2822  -1977       C  
ATOM   3059  SD  MET A 475      32.897  76.478  20.875  1.00106.09           S  
ANISOU 3059  SD  MET A 475    11176  15772  13360   1337  -2785  -1838       S  
ATOM   3060  CE  MET A 475      31.550  76.873  19.759  1.00107.42           C  
ANISOU 3060  CE  MET A 475    11257  16128  13431   1493  -2954  -1979       C  
ATOM   3061  N   GLU A 476      29.828  71.501  21.670  1.00112.61           N  
ANISOU 3061  N   GLU A 476    11841  16151  14793    718  -3459  -2666       N  
ATOM   3062  CA  GLU A 476      28.719  70.676  21.210  1.00115.35           C  
ANISOU 3062  CA  GLU A 476    12116  16477  15233    647  -3719  -2868       C  
ATOM   3063  C   GLU A 476      27.870  70.178  22.374  1.00117.36           C  
ANISOU 3063  C   GLU A 476    12217  16622  15753    306  -3750  -2826       C  
ATOM   3064  O   GLU A 476      26.667  69.947  22.208  1.00120.36           O  
ANISOU 3064  O   GLU A 476    12449  17056  16228    203  -3915  -2912       O  
ATOM   3065  CB  GLU A 476      29.257  69.500  20.400  1.00115.78           C  
ANISOU 3065  CB  GLU A 476    12338  16423  15231    770  -3928  -3068       C  
ATOM   3066  CG  GLU A 476      29.898  69.902  19.091  1.00117.26           C  
ANISOU 3066  CG  GLU A 476    12639  16791  15123   1139  -3935  -3132       C  
ATOM   3067  CD  GLU A 476      30.631  68.750  18.441  1.00120.40           C  
ANISOU 3067  CD  GLU A 476    13215  17095  15436   1301  -4117  -3326       C  
ATOM   3068  OE1 GLU A 476      30.442  67.603  18.897  1.00122.03           O  
ANISOU 3068  OE1 GLU A 476    13462  17063  15840   1116  -4295  -3444       O  
ATOM   3069  OE2 GLU A 476      31.398  68.990  17.484  1.00120.04           O  
ANISOU 3069  OE2 GLU A 476    13266  17222  15121   1621  -4091  -3354       O  
ATOM   3070  N   GLU A 477      28.473  70.021  23.556  1.00114.41           N  
ANISOU 3070  N   GLU A 477    11859  16118  15494    129  -3592  -2679       N  
ATOM   3071  CA  GLU A 477      27.763  69.463  24.700  1.00115.23           C  
ANISOU 3071  CA  GLU A 477    11811  16137  15835   -197  -3614  -2610       C  
ATOM   3072  C   GLU A 477      26.694  70.399  25.245  1.00120.66           C  
ANISOU 3072  C   GLU A 477    12265  17030  16551   -269  -3516  -2507       C  
ATOM   3073  O   GLU A 477      25.844  69.960  26.025  1.00132.61           O  
ANISOU 3073  O   GLU A 477    13595  18554  18235   -521  -3561  -2454       O  
ATOM   3074  CB  GLU A 477      28.757  69.120  25.813  1.00112.07           C  
ANISOU 3074  CB  GLU A 477    11496  15567  15519   -333  -3456  -2472       C  
ATOM   3075  CG  GLU A 477      28.298  68.033  26.774  1.00116.20           C  
ANISOU 3075  CG  GLU A 477    11929  15935  16287   -665  -3552  -2429       C  
ATOM   3076  CD  GLU A 477      28.593  66.635  26.263  1.00122.36           C  
ANISOU 3076  CD  GLU A 477    12863  16475  17153   -711  -3817  -2586       C  
ATOM   3077  OE1 GLU A 477      29.401  66.508  25.318  1.00124.22           O  
ANISOU 3077  OE1 GLU A 477    13297  16669  17232   -456  -3876  -2724       O  
ATOM   3078  OE2 GLU A 477      28.025  65.665  26.807  1.00125.36           O  
ANISOU 3078  OE2 GLU A 477    13165  16715  17752   -992  -3978  -2566       O  
ATOM   3079  N   VAL A 478      26.714  71.671  24.860  1.00118.42           N  
ANISOU 3079  N   VAL A 478    11976  16919  16100    -48  -3394  -2468       N  
ATOM   3080  CA  VAL A 478      25.833  72.654  25.477  1.00114.82           C  
ANISOU 3080  CA  VAL A 478    11323  16651  15652    -72  -3291  -2374       C  
ATOM   3081  C   VAL A 478      25.032  73.390  24.408  1.00113.29           C  
ANISOU 3081  C   VAL A 478    11069  16652  15325    132  -3388  -2473       C  
ATOM   3082  O   VAL A 478      24.273  74.320  24.708  1.00111.01           O  
ANISOU 3082  O   VAL A 478    10631  16541  15005    178  -3329  -2424       O  
ATOM   3083  CB  VAL A 478      26.639  73.638  26.345  1.00106.17           C  
ANISOU 3083  CB  VAL A 478    10284  15550  14507    -13  -3047  -2203       C  
ATOM   3084  CG1 VAL A 478      27.318  72.908  27.498  1.00101.02           C  
ANISOU 3084  CG1 VAL A 478     9667  14727  13991   -223  -2951  -2105       C  
ATOM   3085  CG2 VAL A 478      27.657  74.397  25.506  1.00102.46           C  
ANISOU 3085  CG2 VAL A 478    10008  15065  13856    245  -2984  -2182       C  
ATOM   3086  N   GLY A 479      25.181  72.970  23.157  1.00116.09           N  
ANISOU 3086  N   GLY A 479    11537  16984  15589    274  -3548  -2622       N  
ATOM   3087  CA  GLY A 479      24.573  73.672  22.044  1.00126.12           C  
ANISOU 3087  CA  GLY A 479    12777  18436  16706    500  -3636  -2713       C  
ATOM   3088  C   GLY A 479      25.629  74.196  21.095  1.00134.27           C  
ANISOU 3088  C   GLY A 479    14012  19480  17526    777  -3582  -2701       C  
ATOM   3089  O   GLY A 479      26.368  73.406  20.501  1.00142.42           O  
ANISOU 3089  O   GLY A 479    15192  20416  18506    843  -3659  -2787       O  
ATOM   3090  N   MET A 480      25.715  75.521  20.949  1.00131.39           N  
ANISOU 3090  N   MET A 480    13650  19239  17032    948  -3462  -2586       N  
ATOM   3091  CA  MET A 480      26.794  76.160  20.200  1.00131.57           C  
ANISOU 3091  CA  MET A 480    13839  19290  16861   1180  -3382  -2496       C  
ATOM   3092  C   MET A 480      26.918  75.635  18.774  1.00139.63           C  
ANISOU 3092  C   MET A 480    14944  20390  17717   1381  -3540  -2648       C  
ATOM   3093  O   MET A 480      26.479  76.287  17.821  1.00147.90           O  
ANISOU 3093  O   MET A 480    15972  21608  18614   1583  -3605  -2678       O  
ATOM   3094  CB  MET A 480      28.129  75.963  20.920  1.00127.14           C  
ANISOU 3094  CB  MET A 480    13403  18569  16334   1103  -3222  -2355       C  
ATOM   3095  CG  MET A 480      28.229  76.616  22.285  1.00121.49           C  
ANISOU 3095  CG  MET A 480    12637  17779  15744    956  -3057  -2192       C  
ATOM   3096  SD  MET A 480      29.109  78.189  22.250  1.00114.67           S  
ANISOU 3096  SD  MET A 480    11869  16942  14756   1126  -2909  -1955       S  
ATOM   3097  CE  MET A 480      29.254  78.496  24.003  1.00117.70           C  
ANISOU 3097  CE  MET A 480    12209  17190  15321    928  -2763  -1836       C  
ATOM   3098  N   THR A 481      27.539  74.463  18.624  1.00134.60           N  
ANISOU 3098  N   THR A 481    14408  19636  17098   1350  -3611  -2751       N  
ATOM   3099  CA  THR A 481      27.785  73.869  17.316  1.00128.71           C  
ANISOU 3099  CA  THR A 481    13761  18966  16177   1578  -3773  -2919       C  
ATOM   3100  C   THR A 481      27.239  72.447  17.255  1.00129.91           C  
ANISOU 3100  C   THR A 481    13909  18980  16471   1454  -4015  -3159       C  
ATOM   3101  O   THR A 481      26.522  72.011  18.161  1.00135.89           O  
ANISOU 3101  O   THR A 481    14554  19614  17463   1175  -4057  -3169       O  
ATOM   3102  CB  THR A 481      29.285  73.886  16.998  1.00115.78           C  
ANISOU 3102  CB  THR A 481    12283  17345  14365   1747  -3650  -2812       C  
ATOM   3103  OG1 THR A 481      30.012  73.245  18.056  1.00 97.71           O  
ANISOU 3103  OG1 THR A 481    10050  14847  12228   1549  -3560  -2756       O  
ATOM   3104  CG2 THR A 481      29.784  75.317  16.841  1.00118.43           C  
ANISOU 3104  CG2 THR A 481    12617  17827  14552   1878  -3462  -2559       C  
ATOM   3105  N   SER A 482      27.565  71.720  16.191  1.00126.01           N  
ANISOU 3105  N   SER A 482    13533  18512  15834   1665  -4192  -3346       N  
ATOM   3106  CA  SER A 482      27.102  70.346  16.027  1.00115.60           C  
ANISOU 3106  CA  SER A 482    12243  17029  14651   1574  -4479  -3594       C  
ATOM   3107  C   SER A 482      28.107  69.522  15.225  1.00114.85           C  
ANISOU 3107  C   SER A 482    12347  16907  14383   1826  -4598  -3750       C  
ATOM   3108  O   SER A 482      28.332  68.346  15.511  1.00113.38           O  
ANISOU 3108  O   SER A 482    12252  16496  14330   1724  -4762  -3884       O  
ATOM   3109  CB  SER A 482      25.732  70.326  15.347  1.00108.96           C  
ANISOU 3109  CB  SER A 482    11279  16286  13837   1591  -4708  -3764       C  
ATOM   3110  OG  SER A 482      25.673  71.286  14.307  1.00 98.58           O  
ANISOU 3110  OG  SER A 482     9960  15235  12259   1895  -4664  -3754       O  
TER    3111      SER A 482                                                      
ATOM   3112  N   SER B  97     116.169  39.829  45.527  1.00102.85           N  
ANISOU 3112  N   SER B  97    13301  12710  13068    840   -911  -1432       N  
ATOM   3113  CA  SER B  97     115.349  41.023  45.702  1.00 98.36           C  
ANISOU 3113  CA  SER B  97    12544  12285  12542    620   -760  -1320       C  
ATOM   3114  C   SER B  97     114.462  41.255  44.494  1.00 99.02           C  
ANISOU 3114  C   SER B  97    12553  12436  12634    569   -775  -1405       C  
ATOM   3115  O   SER B  97     114.562  40.544  43.495  1.00107.44           O  
ANISOU 3115  O   SER B  97    13710  13453  13657    713   -897  -1555       O  
ATOM   3116  CB  SER B  97     116.224  42.254  45.933  1.00 95.84           C  
ANISOU 3116  CB  SER B  97    12026  12234  12156    689   -617  -1250       C  
ATOM   3117  OG  SER B  97     115.430  43.426  46.023  1.00 97.60           O  
ANISOU 3117  OG  SER B  97    12094  12580  12409    504   -489  -1158       O  
ATOM   3118  N   GLU B  98     113.586  42.256  44.590  1.00 87.36           N  
ANISOU 3118  N   GLU B  98    10920  11070  11202    383   -662  -1318       N  
ATOM   3119  CA  GLU B  98     112.864  42.686  43.402  1.00 84.56           C  
ANISOU 3119  CA  GLU B  98    10466  10827  10834    367   -672  -1395       C  
ATOM   3120  C   GLU B  98     113.810  43.330  42.402  1.00 90.32           C  
ANISOU 3120  C   GLU B  98    11095  11798  11423    589   -622  -1463       C  
ATOM   3121  O   GLU B  98     113.595  43.231  41.190  1.00 99.40           O  
ANISOU 3121  O   GLU B  98    12247  13008  12512    681   -684  -1580       O  
ATOM   3122  CB  GLU B  98     111.742  43.654  43.777  1.00 82.77           C  
ANISOU 3122  CB  GLU B  98    10092  10676  10683    146   -566  -1286       C  
ATOM   3123  CG  GLU B  98     110.754  43.903  42.649  1.00 90.21           C  
ANISOU 3123  CG  GLU B  98    10955  11683  11639    105   -618  -1367       C  
ATOM   3124  CD  GLU B  98     109.879  45.117  42.884  1.00 97.98           C  
ANISOU 3124  CD  GLU B  98    11760  12807  12661    -35   -498  -1270       C  
ATOM   3125  OE1 GLU B  98     110.267  45.985  43.693  1.00103.58           O  
ANISOU 3125  OE1 GLU B  98    12401  13608  13347    -50   -364  -1156       O  
ATOM   3126  OE2 GLU B  98     108.795  45.196  42.266  1.00 98.30           O  
ANISOU 3126  OE2 GLU B  98    11733  12862  12754   -120   -555  -1315       O  
ATOM   3127  N   PHE B  99     114.872  43.970  42.891  1.00 91.66           N  
ANISOU 3127  N   PHE B  99    11179  12113  11535    671   -516  -1388       N  
ATOM   3128  CA  PHE B  99     115.867  44.552  41.998  1.00 88.59           C  
ANISOU 3128  CA  PHE B  99    10677  11970  11014    863   -452  -1430       C  
ATOM   3129  C   PHE B  99     116.557  43.469  41.178  1.00 91.58           C  
ANISOU 3129  C   PHE B  99    11168  12324  11305   1113   -561  -1591       C  
ATOM   3130  O   PHE B  99     116.669  43.582  39.953  1.00102.28           O  
ANISOU 3130  O   PHE B  99    12492  13819  12550   1250   -562  -1685       O  
ATOM   3131  CB  PHE B  99     116.880  45.359  42.811  1.00 87.02           C  
ANISOU 3131  CB  PHE B  99    10360  11910  10796    871   -339  -1311       C  
ATOM   3132  CG  PHE B  99     117.771  46.235  41.981  1.00 96.21           C  
ANISOU 3132  CG  PHE B  99    11360  13353  11842    989   -240  -1304       C  
ATOM   3133  CD1 PHE B  99     117.475  46.501  40.655  1.00105.92           C  
ANISOU 3133  CD1 PHE B  99    12556  14709  12981   1056   -225  -1372       C  
ATOM   3134  CD2 PHE B  99     118.905  46.800  42.533  1.00101.86           C  
ANISOU 3134  CD2 PHE B  99    11957  14210  12534   1024   -166  -1221       C  
ATOM   3135  CE1 PHE B  99     118.301  47.305  39.894  1.00112.18           C  
ANISOU 3135  CE1 PHE B  99    13206  15765  13653   1150   -119  -1343       C  
ATOM   3136  CE2 PHE B  99     119.728  47.608  41.778  1.00108.10           C  
ANISOU 3136  CE2 PHE B  99    12583  15265  13224   1100    -67  -1194       C  
ATOM   3137  CZ  PHE B  99     119.428  47.859  40.458  1.00112.22           C  
ANISOU 3137  CZ  PHE B  99    13079  15912  13647   1161    -33  -1247       C  
ATOM   3138  N   GLU B 100     117.017  42.402  41.840  1.00 89.94           N  
ANISOU 3138  N   GLU B 100    11110  11934  11131   1192   -660  -1626       N  
ATOM   3139  CA  GLU B 100     117.686  41.311  41.134  1.00100.24           C  
ANISOU 3139  CA  GLU B 100    12548  13191  12348   1463   -781  -1792       C  
ATOM   3140  C   GLU B 100     116.823  40.766  40.008  1.00102.73           C  
ANISOU 3140  C   GLU B 100    12981  13413  12638   1485   -901  -1935       C  
ATOM   3141  O   GLU B 100     117.335  40.414  38.940  1.00112.87           O  
ANISOU 3141  O   GLU B 100    14303  14794  13788   1733   -943  -2081       O  
ATOM   3142  CB  GLU B 100     118.029  40.179  42.101  1.00118.85           C  
ANISOU 3142  CB  GLU B 100    15101  15291  14765   1512   -905  -1803       C  
ATOM   3143  CG  GLU B 100     119.116  40.490  43.100  1.00136.47           C  
ANISOU 3143  CG  GLU B 100    17245  17616  16992   1575   -834  -1705       C  
ATOM   3144  CD  GLU B 100     119.348  39.342  44.061  1.00149.16           C  
ANISOU 3144  CD  GLU B 100    19082  18942  18652   1623   -977  -1710       C  
ATOM   3145  OE1 GLU B 100     118.823  38.236  43.808  1.00152.71           O  
ANISOU 3145  OE1 GLU B 100    19766  19129  19126   1643  -1136  -1806       O  
ATOM   3146  OE2 GLU B 100     120.039  39.549  45.079  1.00152.01           O  
ANISOU 3146  OE2 GLU B 100    19402  19329  19025   1633   -944  -1614       O  
ATOM   3147  N   LEU B 101     115.511  40.679  40.228  1.00 99.73           N  
ANISOU 3147  N   LEU B 101    12658  12854  12382   1232   -960  -1900       N  
ATOM   3148  CA  LEU B 101     114.649  40.072  39.222  1.00104.22           C  
ANISOU 3148  CA  LEU B 101    13347  13305  12946   1232  -1113  -2043       C  
ATOM   3149  C   LEU B 101     114.464  40.993  38.021  1.00106.28           C  
ANISOU 3149  C   LEU B 101    13466  13824  13093   1294  -1040  -2084       C  
ATOM   3150  O   LEU B 101     114.513  40.538  36.872  1.00118.90           O  
ANISOU 3150  O   LEU B 101    15160  15441  14576   1478  -1142  -2246       O  
ATOM   3151  CB  LEU B 101     113.301  39.697  39.838  1.00104.62           C  
ANISOU 3151  CB  LEU B 101    13466  13107  13177    923  -1201  -1983       C  
ATOM   3152  CG  LEU B 101     113.346  38.725  41.021  1.00100.80           C  
ANISOU 3152  CG  LEU B 101    13160  12338  12802    827  -1279  -1923       C  
ATOM   3153  CD1 LEU B 101     111.945  38.236  41.347  1.00 99.16           C  
ANISOU 3153  CD1 LEU B 101    13020  11897  12759    520  -1379  -1881       C  
ATOM   3154  CD2 LEU B 101     114.286  37.557  40.752  1.00 95.49           C  
ANISOU 3154  CD2 LEU B 101    12718  11518  12048   1102  -1432  -2068       C  
ATOM   3155  N   ARG B 102     114.261  42.290  38.261  1.00 97.19           N  
ANISOU 3155  N   ARG B 102    12109  12864  11956   1156   -873  -1940       N  
ATOM   3156  CA  ARG B 102     114.123  43.224  37.149  1.00 94.14           C  
ANISOU 3156  CA  ARG B 102    11606  12713  11448   1216   -803  -1957       C  
ATOM   3157  C   ARG B 102     115.464  43.531  36.492  1.00100.78           C  
ANISOU 3157  C   ARG B 102    12384  13806  12102   1477   -697  -1985       C  
ATOM   3158  O   ARG B 102     115.510  43.800  35.287  1.00102.33           O  
ANISOU 3158  O   ARG B 102    12571  14162  12146   1615   -688  -2061       O  
ATOM   3159  CB  ARG B 102     113.448  44.509  37.623  1.00 81.81           C  
ANISOU 3159  CB  ARG B 102     9873  11249   9962    993   -677  -1796       C  
ATOM   3160  CG  ARG B 102     112.104  44.271  38.277  1.00 80.82           C  
ANISOU 3160  CG  ARG B 102     9766  10926  10015    741   -753  -1759       C  
ATOM   3161  CD  ARG B 102     111.346  45.572  38.503  1.00 96.59           C  
ANISOU 3161  CD  ARG B 102    11596  13047  12057    578   -641  -1635       C  
ATOM   3162  NE  ARG B 102     110.153  45.372  39.325  1.00102.79           N  
ANISOU 3162  NE  ARG B 102    12361  13679  13015    343   -676  -1580       N  
ATOM   3163  CZ  ARG B 102     108.967  45.001  38.853  1.00106.34           C  
ANISOU 3163  CZ  ARG B 102    12813  14049  13544    239   -802  -1650       C  
ATOM   3164  NH1 ARG B 102     108.799  44.796  37.550  1.00108.55           N  
ANISOU 3164  NH1 ARG B 102    13140  14368  13736    361   -923  -1789       N  
ATOM   3165  NH2 ARG B 102     107.944  44.843  39.683  1.00105.98           N  
ANISOU 3165  NH2 ARG B 102    12714  13896  13658     14   -807  -1579       N  
ATOM   3166  N   ARG B 103     116.557  43.493  37.255  1.00104.34           N  
ANISOU 3166  N   ARG B 103    12783  14308  12554   1549   -617  -1922       N  
ATOM   3167  CA  ARG B 103     117.880  43.652  36.659  1.00107.86           C  
ANISOU 3167  CA  ARG B 103    13142  15007  12831   1802   -519  -1953       C  
ATOM   3168  C   ARG B 103     118.184  42.516  35.689  1.00108.43           C  
ANISOU 3168  C   ARG B 103    13380  15045  12773   2089   -644  -2163       C  
ATOM   3169  O   ARG B 103     118.827  42.729  34.653  1.00106.11           O  
ANISOU 3169  O   ARG B 103    13030  14994  12292   2305   -569  -2224       O  
ATOM   3170  CB  ARG B 103     118.942  43.735  37.761  1.00115.63           C  
ANISOU 3170  CB  ARG B 103    14031  16036  13867   1817   -442  -1854       C  
ATOM   3171  CG  ARG B 103     120.377  43.628  37.274  1.00128.86           C  
ANISOU 3171  CG  ARG B 103    15605  17962  15393   2098   -365  -1903       C  
ATOM   3172  CD  ARG B 103     120.749  44.781  36.370  1.00137.25           C  
ANISOU 3172  CD  ARG B 103    16477  19352  16319   2112   -192  -1829       C  
ATOM   3173  NE  ARG B 103     122.119  44.656  35.892  1.00143.41           N  
ANISOU 3173  NE  ARG B 103    17130  20406  16954   2374    -99  -1866       N  
ATOM   3174  CZ  ARG B 103     122.659  45.454  34.981  1.00146.39           C  
ANISOU 3174  CZ  ARG B 103    17345  21099  17176   2437     62  -1814       C  
ATOM   3175  NH1 ARG B 103     121.941  46.438  34.456  1.00143.05           N  
ANISOU 3175  NH1 ARG B 103    16899  20732  16722   2263    129  -1723       N  
ATOM   3176  NH2 ARG B 103     123.917  45.276  34.601  1.00152.35           N  
ANISOU 3176  NH2 ARG B 103    17959  22122  17804   2676    157  -1844       N  
ATOM   3177  N   GLN B 104     117.722  41.301  36.002  1.00117.74           N  
ANISOU 3177  N   GLN B 104    14778  15918  14040   2097   -838  -2273       N  
ATOM   3178  CA  GLN B 104     117.922  40.176  35.094  1.00124.46           C  
ANISOU 3178  CA  GLN B 104    15833  16688  14769   2373   -994  -2492       C  
ATOM   3179  C   GLN B 104     117.090  40.324  33.827  1.00116.46           C  
ANISOU 3179  C   GLN B 104    14880  15712  13657   2388  -1060  -2596       C  
ATOM   3180  O   GLN B 104     117.514  39.879  32.755  1.00116.69           O  
ANISOU 3180  O   GLN B 104    15007  15835  13496   2674  -1107  -2761       O  
ATOM   3181  CB  GLN B 104     117.583  38.856  35.793  1.00135.25           C  
ANISOU 3181  CB  GLN B 104    17449  17673  16267   2344  -1209  -2571       C  
ATOM   3182  CG  GLN B 104     118.602  38.402  36.832  1.00140.20           C  
ANISOU 3182  CG  GLN B 104    18088  18249  16934   2448  -1193  -2526       C  
ATOM   3183  CD  GLN B 104     118.131  37.198  37.633  1.00145.42           C  
ANISOU 3183  CD  GLN B 104    19016  18502  17736   2362  -1402  -2561       C  
ATOM   3184  OE1 GLN B 104     116.948  36.858  37.633  1.00153.96           O  
ANISOU 3184  OE1 GLN B 104    20225  19343  18928   2136  -1528  -2570       O  
ATOM   3185  NE2 GLN B 104     119.061  36.550  38.327  1.00142.29           N  
ANISOU 3185  NE2 GLN B 104    18701  18026  17337   2535  -1445  -2572       N  
ATOM   3186  N   ALA B 105     115.913  40.938  33.926  1.00109.38           N  
ANISOU 3186  N   ALA B 105    13931  14755  12874   2104  -1070  -2511       N  
ATOM   3187  CA  ALA B 105     115.034  41.125  32.780  1.00107.74           C  
ANISOU 3187  CA  ALA B 105    13774  14577  12586   2102  -1156  -2604       C  
ATOM   3188  C   ALA B 105     115.289  42.431  32.037  1.00105.15           C  
ANISOU 3188  C   ALA B 105    13265  14585  12101   2144   -966  -2514       C  
ATOM   3189  O   ALA B 105     114.574  42.730  31.076  1.00103.49           O  
ANISOU 3189  O   ALA B 105    13091  14425  11807   2148  -1027  -2573       O  
ATOM   3190  CB  ALA B 105     113.568  41.061  33.225  1.00106.39           C  
ANISOU 3190  CB  ALA B 105    13629  14172  12624   1785  -1286  -2568       C  
ATOM   3191  N   CYS B 106     116.281  43.217  32.459  1.00104.58           N  
ANISOU 3191  N   CYS B 106    13009  14736  11989   2165   -751  -2368       N  
ATOM   3192  CA  CYS B 106     116.607  44.471  31.795  1.00100.34           C  
ANISOU 3192  CA  CYS B 106    12313  14508  11306   2182   -566  -2258       C  
ATOM   3193  C   CYS B 106     117.957  44.455  31.100  1.00 88.72           C  
ANISOU 3193  C   CYS B 106    10784  13315   9610   2471   -431  -2292       C  
ATOM   3194  O   CYS B 106     118.164  45.240  30.168  1.00 82.98           O  
ANISOU 3194  O   CYS B 106     9988  12838   8701   2539   -310  -2247       O  
ATOM   3195  CB  CYS B 106     116.584  45.635  32.799  1.00 98.19           C  
ANISOU 3195  CB  CYS B 106    11849  14289  11169   1923   -416  -2032       C  
ATOM   3196  SG  CYS B 106     114.931  46.265  33.191  1.00103.47           S  
ANISOU 3196  SG  CYS B 106    12511  14787  12016   1612   -493  -1956       S  
ATOM   3197  N   GLY B 107     118.865  43.589  31.518  1.00 85.37           N  
ANISOU 3197  N   GLY B 107    10386  12865   9187   2647   -448  -2365       N  
ATOM   3198  CA  GLY B 107     120.179  43.584  30.932  1.00 91.25           C  
ANISOU 3198  CA  GLY B 107    11033  13909   9728   2930   -304  -2392       C  
ATOM   3199  C   GLY B 107     121.028  44.695  31.513  1.00110.18           C  
ANISOU 3199  C   GLY B 107    13155  16551  12158   2802    -79  -2172       C  
ATOM   3200  O   GLY B 107     120.675  45.359  32.491  1.00115.18           O  
ANISOU 3200  O   GLY B 107    13702  17086  12974   2521    -55  -2017       O  
ATOM   3201  N   ARG B 108     122.182  44.884  30.883  1.00123.97           N  
ANISOU 3201  N   ARG B 108    14761  18628  13715   3020     84  -2163       N  
ATOM   3202  CA  ARG B 108     123.077  45.956  31.283  1.00129.72           C  
ANISOU 3202  CA  ARG B 108    15211  19618  14457   2897    295  -1953       C  
ATOM   3203  C   ARG B 108     122.393  47.307  31.102  1.00123.77           C  
ANISOU 3203  C   ARG B 108    14401  18907  13720   2613    381  -1773       C  
ATOM   3204  O   ARG B 108     121.475  47.466  30.292  1.00112.37           O  
ANISOU 3204  O   ARG B 108    13096  17408  12191   2599    325  -1818       O  
ATOM   3205  CB  ARG B 108     124.376  45.883  30.480  1.00139.73           C  
ANISOU 3205  CB  ARG B 108    16325  21267  15501   3184    464  -1978       C  
ATOM   3206  CG  ARG B 108     125.121  44.554  30.643  1.00143.91           C  
ANISOU 3206  CG  ARG B 108    16908  21773  16000   3515    376  -2170       C  
ATOM   3207  CD  ARG B 108     126.229  44.393  29.611  1.00149.22           C  
ANISOU 3207  CD  ARG B 108    17453  22840  16405   3858    539  -2234       C  
ATOM   3208  NE  ARG B 108     125.731  44.067  28.275  1.00149.53           N  
ANISOU 3208  NE  ARG B 108    17693  22917  16204   4066    511  -2384       N  
ATOM   3209  CZ  ARG B 108     125.864  42.875  27.695  1.00147.17           C  
ANISOU 3209  CZ  ARG B 108    17590  22570  15760   4434    391  -2633       C  
ATOM   3210  NH1 ARG B 108     126.496  41.891  28.322  1.00151.67           N  
ANISOU 3210  NH1 ARG B 108    18184  23031  16414   4615    283  -2735       N  
ATOM   3211  NH2 ARG B 108     125.381  42.670  26.476  1.00140.21           N  
ANISOU 3211  NH2 ARG B 108    16906  21686  14681   4558    336  -2726       N  
ATOM   3212  N   SER B 109     122.835  48.281  31.892  1.00126.49           N  
ANISOU 3212  N   SER B 109    14552  19331  14176   2390    496  -1572       N  
ATOM   3213  CA  SER B 109     122.200  49.592  31.896  1.00118.70           C  
ANISOU 3213  CA  SER B 109    13533  18341  13228   2115    556  -1395       C  
ATOM   3214  C   SER B 109     122.393  50.295  30.561  1.00105.75           C  
ANISOU 3214  C   SER B 109    11861  16972  11348   2184    697  -1334       C  
ATOM   3215  O   SER B 109     123.518  50.422  30.067  1.00 97.32           O  
ANISOU 3215  O   SER B 109    10638  16208  10132   2312    859  -1286       O  
ATOM   3216  CB  SER B 109     122.771  50.453  33.020  1.00118.42           C  
ANISOU 3216  CB  SER B 109    13314  18333  13348   1885    636  -1206       C  
ATOM   3217  OG  SER B 109     122.349  51.797  32.876  1.00117.74           O  
ANISOU 3217  OG  SER B 109    13199  18278  13260   1655    708  -1031       O  
ATOM   3218  N   GLN B 110     121.283  50.769  29.989  1.00 97.65           N  
ANISOU 3218  N   GLN B 110    10977  15845  10279   2098    636  -1327       N  
ATOM   3219  CA  GLN B 110     121.357  51.558  28.767  1.00 97.50           C  
ANISOU 3219  CA  GLN B 110    10962  16056  10028   2136    760  -1242       C  
ATOM   3220  C   GLN B 110     122.157  52.842  28.960  1.00100.91           C  
ANISOU 3220  C   GLN B 110    11198  16690  10452   1941    952   -987       C  
ATOM   3221  O   GLN B 110     122.628  53.421  27.976  1.00105.73           O  
ANISOU 3221  O   GLN B 110    11767  17558  10847   1989   1105   -888       O  
ATOM   3222  CB  GLN B 110     119.947  51.881  28.270  1.00102.63           C  
ANISOU 3222  CB  GLN B 110    11803  16529  10664   2064    626  -1276       C  
ATOM   3223  CG  GLN B 110     119.174  50.678  27.742  1.00113.72           C  
ANISOU 3223  CG  GLN B 110    13407  17776  12025   2261    433  -1526       C  
ATOM   3224  CD  GLN B 110     119.640  50.221  26.368  1.00124.52           C  
ANISOU 3224  CD  GLN B 110    14856  19368  13089   2562    483  -1639       C  
ATOM   3225  OE1 GLN B 110     120.532  50.821  25.764  1.00130.58           O  
ANISOU 3225  OE1 GLN B 110    15517  20435  13664   2623    687  -1516       O  
ATOM   3226  NE2 GLN B 110     119.027  49.154  25.865  1.00125.45           N  
ANISOU 3226  NE2 GLN B 110    15169  19342  13155   2747    294  -1871       N  
ATOM   3227  N   LEU B 111     122.319  53.300  30.205  1.00105.73           N  
ANISOU 3227  N   LEU B 111    11702  17186  11287   1717    943   -876       N  
ATOM   3228  CA  LEU B 111     123.192  54.438  30.473  1.00106.35           C  
ANISOU 3228  CA  LEU B 111    11590  17440  11378   1523   1101   -644       C  
ATOM   3229  C   LEU B 111     124.658  54.075  30.289  1.00109.42           C  
ANISOU 3229  C   LEU B 111    11756  18143  11677   1663   1254   -627       C  
ATOM   3230  O   LEU B 111     125.458  54.922  29.878  1.00131.29           O  
ANISOU 3230  O   LEU B 111    14366  21169  14348   1568   1428   -444       O  
ATOM   3231  CB  LEU B 111     122.957  54.963  31.887  1.00102.43           C  
ANISOU 3231  CB  LEU B 111    11062  16721  11138   1268   1022   -556       C  
ATOM   3232  CG  LEU B 111     123.724  56.232  32.263  1.00100.23           C  
ANISOU 3232  CG  LEU B 111    10623  16561  10900   1024   1137   -318       C  
ATOM   3233  CD1 LEU B 111     122.848  57.462  32.113  1.00 92.88           C  
ANISOU 3233  CD1 LEU B 111     9827  15495   9970    821   1111   -183       C  
ATOM   3234  CD2 LEU B 111     124.282  56.130  33.674  1.00101.17           C  
ANISOU 3234  CD2 LEU B 111    10619  16590  11232    912   1086   -296       C  
ATOM   3235  N   LEU B 112     125.032  52.830  30.589  1.00 98.31           N  
ANISOU 3235  N   LEU B 112    10330  16722  10302   1886   1191   -809       N  
ATOM   3236  CA  LEU B 112     126.406  52.400  30.356  1.00102.11           C  
ANISOU 3236  CA  LEU B 112    10589  17523  10684   2074   1330   -818       C  
ATOM   3237  C   LEU B 112     126.697  52.285  28.865  1.00107.17           C  
ANISOU 3237  C   LEU B 112    11240  18458  11022   2303   1474   -851       C  
ATOM   3238  O   LEU B 112     127.733  52.759  28.383  1.00103.02           O  
ANISOU 3238  O   LEU B 112    10492  18285  10366   2314   1682   -717       O  
ATOM   3239  CB  LEU B 112     126.665  51.064  31.045  1.00104.89           C  
ANISOU 3239  CB  LEU B 112    10959  17756  11137   2288   1199  -1019       C  
ATOM   3240  CG  LEU B 112     126.395  50.987  32.541  1.00108.75           C  
ANISOU 3240  CG  LEU B 112    11467  17954  11901   2104   1051  -1006       C  
ATOM   3241  CD1 LEU B 112     126.794  49.612  33.055  1.00114.16           C  
ANISOU 3241  CD1 LEU B 112    12182  18555  12640   2356    935  -1196       C  
ATOM   3242  CD2 LEU B 112     127.137  52.087  33.281  1.00107.56           C  
ANISOU 3242  CD2 LEU B 112    11083  17920  11867   1839   1143   -785       C  
ATOM   3243  N   LYS B 113     125.792  51.648  28.121  1.00111.29           N  
ANISOU 3243  N   LYS B 113    12016  18846  11421   2486   1365  -1026       N  
ATOM   3244  CA  LYS B 113     126.005  51.434  26.695  1.00118.82           C  
ANISOU 3244  CA  LYS B 113    13024  20061  12060   2745   1479  -1088       C  
ATOM   3245  C   LYS B 113     126.012  52.755  25.934  1.00122.28           C  
ANISOU 3245  C   LYS B 113    13425  20691  12345   2561   1651   -852       C  
ATOM   3246  O   LYS B 113     126.997  53.108  25.274  1.00125.78           O  
ANISOU 3246  O   LYS B 113    13712  21445  12635   2596   1847   -722       O  
ATOM   3247  CB  LYS B 113     124.924  50.503  26.135  1.00118.56           C  
ANISOU 3247  CB  LYS B 113    13302  19794  11950   2950   1277  -1334       C  
ATOM   3248  CG  LYS B 113     124.688  49.214  26.916  1.00118.57           C  
ANISOU 3248  CG  LYS B 113    13407  19522  12124   3083   1066  -1557       C  
ATOM   3249  CD  LYS B 113     123.684  48.328  26.183  1.00121.64           C  
ANISOU 3249  CD  LYS B 113    14102  19708  12410   3278    869  -1793       C  
ATOM   3250  CE  LYS B 113     124.213  47.917  24.810  1.00128.69           C  
ANISOU 3250  CE  LYS B 113    15049  20891  12956   3633    970  -1909       C  
ATOM   3251  NZ  LYS B 113     123.313  46.974  24.080  1.00127.89           N  
ANISOU 3251  NZ  LYS B 113    15263  20585  12743   3849    749  -2165       N  
ATOM   3252  N   SER B 114     124.916  53.500  26.020  1.00115.89           N  
ANISOU 3252  N   SER B 114    12783  19638  11613   2336   1546   -776       N  
ATOM   3253  CA  SER B 114     124.691  54.660  25.160  1.00109.36           C  
ANISOU 3253  CA  SER B 114    12011  18929  10611   2202   1660   -582       C  
ATOM   3254  C   SER B 114     124.930  55.963  25.921  1.00 93.36           C  
ANISOU 3254  C   SER B 114     9850  16868   8756   1830   1725   -313       C  
ATOM   3255  O   SER B 114     124.074  56.844  25.992  1.00 78.11           O  
ANISOU 3255  O   SER B 114     8060  14740   6878   1629   1647   -209       O  
ATOM   3256  CB  SER B 114     123.285  54.603  24.574  1.00108.81           C  
ANISOU 3256  CB  SER B 114    12242  18625  10475   2252   1479   -695       C  
ATOM   3257  OG  SER B 114     122.365  54.111  25.529  1.00100.73           O  
ANISOU 3257  OG  SER B 114    11314  17245   9715   2181   1249   -831       O  
ATOM   3258  N   ARG B 115     126.134  56.076  26.488  1.00 94.35           N  
ANISOU 3258  N   ARG B 115     9697  17188   8962   1752   1858   -206       N  
ATOM   3259  CA  ARG B 115     126.540  57.335  27.103  1.00 95.36           C  
ANISOU 3259  CA  ARG B 115     9687  17320   9226   1399   1928     58       C  
ATOM   3260  C   ARG B 115     126.594  58.451  26.064  1.00101.05           C  
ANISOU 3260  C   ARG B 115    10455  18210   9729   1272   2083    285       C  
ATOM   3261  O   ARG B 115     126.225  59.596  26.351  1.00 98.02           O  
ANISOU 3261  O   ARG B 115    10144  17669   9430    985   2049    470       O  
ATOM   3262  CB  ARG B 115     127.893  57.164  27.803  1.00 92.79           C  
ANISOU 3262  CB  ARG B 115     9032  17210   9014   1358   2033    116       C  
ATOM   3263  CG  ARG B 115     128.467  58.440  28.415  1.00100.78           C  
ANISOU 3263  CG  ARG B 115     9878  18250  10165    982   2097    389       C  
ATOM   3264  CD  ARG B 115     129.687  58.145  29.282  1.00115.40           C  
ANISOU 3264  CD  ARG B 115    11405  20268  12173    950   2139    407       C  
ATOM   3265  NE  ARG B 115     130.337  59.366  29.756  1.00131.23           N  
ANISOU 3265  NE  ARG B 115    13251  22306  14304    580   2186    669       N  
ATOM   3266  CZ  ARG B 115     131.257  59.406  30.718  1.00135.72           C  
ANISOU 3266  CZ  ARG B 115    13592  22897  15078    452   2145    712       C  
ATOM   3267  NH1 ARG B 115     131.644  58.288  31.319  1.00130.12           N  
ANISOU 3267  NH1 ARG B 115    12787  22191  14463    676   2064    518       N  
ATOM   3268  NH2 ARG B 115     131.792  60.566  31.082  1.00138.33           N  
ANISOU 3268  NH2 ARG B 115    13808  23234  15517    101   2167    948       N  
ATOM   3269  N   VAL B 116     127.024  58.131  24.842  1.00105.82           N  
ANISOU 3269  N   VAL B 116    11045  19125  10036   1497   2249    271       N  
ATOM   3270  CA  VAL B 116     127.079  59.151  23.801  1.00105.62           C  
ANISOU 3270  CA  VAL B 116    11106  19223   9802   1377   2382    496       C  
ATOM   3271  C   VAL B 116     125.708  59.383  23.174  1.00101.91           C  
ANISOU 3271  C   VAL B 116    10974  18555   9193   1439   2253    438       C  
ATOM   3272  O   VAL B 116     125.399  60.506  22.756  1.00 99.19           O  
ANISOU 3272  O   VAL B 116    10753  18171   8762   1246   2285    648       O  
ATOM   3273  CB  VAL B 116     128.123  58.783  22.735  1.00107.89           C  
ANISOU 3273  CB  VAL B 116    11304  19772   9919   1546   2538    516       C  
ATOM   3274  CG1 VAL B 116     128.513  60.018  21.933  1.00101.15           C  
ANISOU 3274  CG1 VAL B 116    10461  19050   8923   1322   2705    815       C  
ATOM   3275  CG2 VAL B 116     129.341  58.152  23.389  1.00115.50           C  
ANISOU 3275  CG2 VAL B 116    11971  20861  11054   1585   2578    470       C  
ATOM   3276  N   ASP B 117     124.867  58.347  23.085  1.00100.65           N  
ANISOU 3276  N   ASP B 117    10985  18223   9033   1694   2072    156       N  
ATOM   3277  CA  ASP B 117     123.516  58.552  22.569  1.00 99.44           C  
ANISOU 3277  CA  ASP B 117    11140  17833   8810   1733   1895     85       C  
ATOM   3278  C   ASP B 117     122.698  59.421  23.514  1.00 96.55           C  
ANISOU 3278  C   ASP B 117    10849  17129   8707   1444   1735    178       C  
ATOM   3279  O   ASP B 117     121.983  60.328  23.069  1.00 90.44           O  
ANISOU 3279  O   ASP B 117    10261  16248   7854   1344   1683    294       O  
ATOM   3280  CB  ASP B 117     122.819  57.210  22.342  1.00106.58           C  
ANISOU 3280  CB  ASP B 117    12189  18618   9688   2041   1716   -241       C  
ATOM   3281  CG  ASP B 117     123.451  56.400  21.222  1.00128.01           C  
ANISOU 3281  CG  ASP B 117    14908  21644  12086   2377   1847   -357       C  
ATOM   3282  OD1 ASP B 117     124.346  56.928  20.525  1.00138.88           O  
ANISOU 3282  OD1 ASP B 117    16190  23290  13289   2354   2064   -168       O  
ATOM   3283  OD2 ASP B 117     123.054  55.228  21.043  1.00133.70           O  
ANISOU 3283  OD2 ASP B 117    15743  22278  12780   2643   1701   -632       O  
ATOM   3284  N   ILE B 118     122.797  59.157  24.822  1.00 97.39           N  
ANISOU 3284  N   ILE B 118    10824  17068   9112   1327   1651    126       N  
ATOM   3285  CA  ILE B 118     122.069  59.948  25.812  1.00 91.48           C  
ANISOU 3285  CA  ILE B 118    10138  16011   8608   1074   1508    201       C  
ATOM   3286  C   ILE B 118     122.490  61.407  25.740  1.00 94.41           C  
ANISOU 3286  C   ILE B 118    10496  16431   8946    801   1617    501       C  
ATOM   3287  O   ILE B 118     121.649  62.315  25.792  1.00 96.34           O  
ANISOU 3287  O   ILE B 118    10918  16463   9222    669   1511    587       O  
ATOM   3288  CB  ILE B 118     122.289  59.365  27.219  1.00 88.51           C  
ANISOU 3288  CB  ILE B 118     9615  15492   8522   1012   1428    103       C  
ATOM   3289  CG1 ILE B 118     121.326  58.209  27.466  1.00 89.12           C  
ANISOU 3289  CG1 ILE B 118     9808  15364   8689   1196   1239   -168       C  
ATOM   3290  CG2 ILE B 118     122.123  60.437  28.291  1.00 82.39           C  
ANISOU 3290  CG2 ILE B 118     8829  14510   7964    711   1370    261       C  
ATOM   3291  CD1 ILE B 118     121.501  57.561  28.807  1.00 86.56           C  
ANISOU 3291  CD1 ILE B 118     9373  14892   8623   1150   1161   -260       C  
ATOM   3292  N   LEU B 119     123.797  61.657  25.620  1.00 95.01           N  
ANISOU 3292  N   LEU B 119    10356  16784   8958    712   1823    665       N  
ATOM   3293  CA  LEU B 119     124.278  63.028  25.501  1.00 98.61           C  
ANISOU 3293  CA  LEU B 119    10798  17291   9380    422   1930    969       C  
ATOM   3294  C   LEU B 119     123.698  63.707  24.267  1.00107.53           C  
ANISOU 3294  C   LEU B 119    12175  18442  10241    456   1957   1081       C  
ATOM   3295  O   LEU B 119     123.385  64.904  24.298  1.00114.98           O  
ANISOU 3295  O   LEU B 119    13261  19229  11198    233   1915   1278       O  
ATOM   3296  CB  LEU B 119     125.808  63.047  25.465  1.00 90.57           C  
ANISOU 3296  CB  LEU B 119     9470  16618   8325    333   2159   1119       C  
ATOM   3297  CG  LEU B 119     126.535  62.754  26.779  1.00 83.65           C  
ANISOU 3297  CG  LEU B 119     8339  15717   7729    217   2126   1086       C  
ATOM   3298  CD1 LEU B 119     128.010  62.465  26.539  1.00 87.69           C  
ANISOU 3298  CD1 LEU B 119     8514  16638   8168    231   2352   1173       C  
ATOM   3299  CD2 LEU B 119     126.364  63.913  27.750  1.00 85.47           C  
ANISOU 3299  CD2 LEU B 119     8620  15678   8179   -127   2011   1250       C  
ATOM   3300  N   GLU B 120     123.529  62.955  23.176  1.00105.43           N  
ANISOU 3300  N   GLU B 120    11986  18351   9720    746   2008    951       N  
ATOM   3301  CA  GLU B 120     122.960  63.531  21.961  1.00102.63           C  
ANISOU 3301  CA  GLU B 120    11888  18024   9084    810   2020   1044       C  
ATOM   3302  C   GLU B 120     121.480  63.842  22.140  1.00 84.67           C  
ANISOU 3302  C   GLU B 120     9881  15390   6900    823   1756    946       C  
ATOM   3303  O   GLU B 120     121.018  64.928  21.773  1.00 71.52           O  
ANISOU 3303  O   GLU B 120     8413  13610   5152    699   1716   1121       O  
ATOM   3304  CB  GLU B 120     123.168  62.583  20.783  1.00112.90           C  
ANISOU 3304  CB  GLU B 120    13213  19607  10078   1144   2127    905       C  
ATOM   3305  CG  GLU B 120     124.601  62.473  20.314  1.00116.74           C  
ANISOU 3305  CG  GLU B 120    13455  20512  10391   1156   2427   1044       C  
ATOM   3306  CD  GLU B 120     124.738  61.554  19.118  1.00113.62           C  
ANISOU 3306  CD  GLU B 120    13137  20284   9748   1501   2476    874       C  
ATOM   3307  OE1 GLU B 120     123.696  61.090  18.607  1.00108.74           O  
ANISOU 3307  OE1 GLU B 120    12765  19562   8990   1731   2319    683       O  
ATOM   3308  OE2 GLU B 120     125.884  61.291  18.694  1.00113.14           O  
ANISOU 3308  OE2 GLU B 120    12898  20439   9652   1541   2648    922       O  
ATOM   3309  N   VAL B 121     120.719  62.892  22.693  1.00 79.37           N  
ANISOU 3309  N   VAL B 121     9218  14541   6396    976   1573    671       N  
ATOM   3310  CA  VAL B 121     119.299  63.129  22.950  1.00 79.75           C  
ANISOU 3310  CA  VAL B 121     9469  14274   6558    986   1326    569       C  
ATOM   3311  C   VAL B 121     119.114  64.373  23.811  1.00 82.63           C  
ANISOU 3311  C   VAL B 121     9867  14418   7112    701   1270    756       C  
ATOM   3312  O   VAL B 121     118.296  65.247  23.498  1.00 63.63           O  
ANISOU 3312  O   VAL B 121     7674  11853   4649    666   1160    836       O  
ATOM   3313  CB  VAL B 121     118.655  61.891  23.601  1.00 71.18           C  
ANISOU 3313  CB  VAL B 121     8334  13044   5666   1136   1161    271       C  
ATOM   3314  CG1 VAL B 121     117.197  62.160  23.915  1.00 60.47           C  
ANISOU 3314  CG1 VAL B 121     7138  11394   4442   1128    922    178       C  
ATOM   3315  CG2 VAL B 121     118.786  60.680  22.687  1.00 73.68           C  
ANISOU 3315  CG2 VAL B 121     8668  13544   5782   1431   1182     72       C  
ATOM   3316  N   ALA B 122     119.885  64.481  24.898  1.00 76.38           N  
ANISOU 3316  N   ALA B 122     8877  13610   6536    510   1332    824       N  
ATOM   3317  CA  ALA B 122     119.820  65.667  25.747  1.00 74.64           C  
ANISOU 3317  CA  ALA B 122     8698  13176   6484    240   1273    998       C  
ATOM   3318  C   ALA B 122     120.170  66.928  24.966  1.00 83.22           C  
ANISOU 3318  C   ALA B 122     9921  14319   7380     81   1365   1284       C  
ATOM   3319  O   ALA B 122     119.539  67.977  25.147  1.00 82.44           O  
ANISOU 3319  O   ALA B 122    10018  13985   7321    -37   1244   1391       O  
ATOM   3320  CB  ALA B 122     120.747  65.499  26.949  1.00 70.17           C  
ANISOU 3320  CB  ALA B 122     7890  12623   6149     72   1329   1021       C  
ATOM   3321  N   ARG B 123     121.176  66.847  24.091  1.00 88.20           N  
ANISOU 3321  N   ARG B 123    10456  15260   7795     83   1582   1416       N  
ATOM   3322  CA  ARG B 123     121.461  67.959  23.192  1.00 91.04           C  
ANISOU 3322  CA  ARG B 123    10968  15691   7931    -55   1683   1698       C  
ATOM   3323  C   ARG B 123     120.308  68.175  22.216  1.00 94.81           C  
ANISOU 3323  C   ARG B 123    11759  16067   8198    136   1559   1651       C  
ATOM   3324  O   ARG B 123     119.814  69.299  22.063  1.00 99.35           O  
ANISOU 3324  O   ARG B 123    12569  16446   8733     18   1466   1813       O  
ATOM   3325  CB  ARG B 123     122.777  67.704  22.447  1.00 95.88           C  
ANISOU 3325  CB  ARG B 123    11382  16706   8342    -72   1967   1839       C  
ATOM   3326  CG  ARG B 123     123.120  68.708  21.340  1.00106.92           C  
ANISOU 3326  CG  ARG B 123    12936  18235   9454   -195   2113   2142       C  
ATOM   3327  CD  ARG B 123     123.871  69.937  21.844  1.00105.66           C  
ANISOU 3327  CD  ARG B 123    12728  18007   9410   -601   2173   2457       C  
ATOM   3328  NE  ARG B 123     122.991  70.933  22.444  1.00105.23           N  
ANISOU 3328  NE  ARG B 123    12934  17539   9509   -747   1935   2507       N  
ATOM   3329  CZ  ARG B 123     123.050  71.306  23.719  1.00106.27           C  
ANISOU 3329  CZ  ARG B 123    12996  17437   9946   -948   1809   2500       C  
ATOM   3330  NH1 ARG B 123     123.957  70.771  24.527  1.00 94.55           N  
ANISOU 3330  NH1 ARG B 123    11186  16088   8649  -1041   1890   2454       N  
ATOM   3331  NH2 ARG B 123     122.206  72.218  24.183  1.00110.27           N  
ANISOU 3331  NH2 ARG B 123    13765  17575  10556  -1037   1594   2534       N  
ATOM   3332  N   GLN B 124     119.838  67.097  21.577  1.00 92.59           N  
ANISOU 3332  N   GLN B 124    11498  15896   7786    443   1528   1417       N  
ATOM   3333  CA  GLN B 124     118.782  67.173  20.566  1.00104.97           C  
ANISOU 3333  CA  GLN B 124    13345  17402   9135    653   1398   1348       C  
ATOM   3334  C   GLN B 124     117.429  67.607  21.128  1.00107.08           C  
ANISOU 3334  C   GLN B 124    13784  17320   9583    662   1122   1248       C  
ATOM   3335  O   GLN B 124     116.484  67.749  20.346  1.00109.45           O  
ANISOU 3335  O   GLN B 124    14311  17553   9723    832    983   1191       O  
ATOM   3336  CB  GLN B 124     118.637  65.821  19.854  1.00110.54           C  
ANISOU 3336  CB  GLN B 124    14018  18296   9685    974   1405   1091       C  
ATOM   3337  CG  GLN B 124     119.826  65.461  18.975  1.00117.34           C  
ANISOU 3337  CG  GLN B 124    14772  19538  10272   1047   1679   1185       C  
ATOM   3338  CD  GLN B 124     119.773  64.038  18.457  1.00124.22           C  
ANISOU 3338  CD  GLN B 124    15602  20573  11023   1377   1672    899       C  
ATOM   3339  OE1 GLN B 124     118.701  63.498  18.188  1.00125.00           O  
ANISOU 3339  OE1 GLN B 124    15860  20528  11108   1580   1456    673       O  
ATOM   3340  NE2 GLN B 124     120.940  63.417  18.331  1.00128.26           N  
ANISOU 3340  NE2 GLN B 124    15894  21387  11453   1436   1897    903       N  
ATOM   3341  N   PHE B 125     117.302  67.817  22.443  1.00103.77           N  
ANISOU 3341  N   PHE B 125    13260  16690   9477    501   1037   1221       N  
ATOM   3342  CA  PHE B 125     116.068  68.376  22.987  1.00 97.15           C  
ANISOU 3342  CA  PHE B 125    12579  15543   8792    508    800   1155       C  
ATOM   3343  C   PHE B 125     115.852  69.817  22.547  1.00 92.92           C  
ANISOU 3343  C   PHE B 125    12308  14871   8127    396    753   1398       C  
ATOM   3344  O   PHE B 125     114.728  70.321  22.652  1.00 97.29           O  
ANISOU 3344  O   PHE B 125    13041  15201   8726    475    547   1342       O  
ATOM   3345  CB  PHE B 125     116.072  68.308  24.519  1.00 92.00           C  
ANISOU 3345  CB  PHE B 125    11764  14715   8477    365    744   1085       C  
ATOM   3346  CG  PHE B 125     115.677  66.965  25.079  1.00 82.38           C  
ANISOU 3346  CG  PHE B 125    10372  13505   7422    513    683    802       C  
ATOM   3347  CD1 PHE B 125     114.620  66.251  24.535  1.00 79.08           C  
ANISOU 3347  CD1 PHE B 125    10026  13072   6950    748    543    590       C  
ATOM   3348  CD2 PHE B 125     116.368  66.412  26.144  1.00 72.41           C  
ANISOU 3348  CD2 PHE B 125     8885  12259   6368    410    753    754       C  
ATOM   3349  CE1 PHE B 125     114.255  65.018  25.052  1.00 69.58           C  
ANISOU 3349  CE1 PHE B 125     8679  11854   5905    853    478    346       C  
ATOM   3350  CE2 PHE B 125     116.012  65.174  26.659  1.00 61.80           C  
ANISOU 3350  CE2 PHE B 125     7411  10902   5166    536    693    512       C  
ATOM   3351  CZ  PHE B 125     114.955  64.480  26.110  1.00 56.02           C  
ANISOU 3351  CZ  PHE B 125     6759  10142   4385    747    558    313       C  
ATOM   3352  N   GLU B 126     116.900  70.480  22.056  1.00 92.75           N  
ANISOU 3352  N   GLU B 126    12312  14983   7945    217    937   1670       N  
ATOM   3353  CA  GLU B 126     116.849  71.896  21.700  1.00 93.06           C  
ANISOU 3353  CA  GLU B 126    12618  14871   7868     62    901   1940       C  
ATOM   3354  C   GLU B 126     116.331  72.733  22.864  1.00 96.27           C  
ANISOU 3354  C   GLU B 126    13105  14937   8536    -76    720   1951       C  
ATOM   3355  O   GLU B 126     115.526  73.651  22.694  1.00105.38           O  
ANISOU 3355  O   GLU B 126    14535  15863   9643    -43    550   2014       O  
ATOM   3356  CB  GLU B 126     116.010  72.122  20.443  1.00 97.10           C  
ANISOU 3356  CB  GLU B 126    13419  15384   8092    283    804   1943       C  
ATOM   3357  CG  GLU B 126     116.600  71.503  19.186  1.00 98.60           C  
ANISOU 3357  CG  GLU B 126    13591  15911   7962    412    995   1976       C  
ATOM   3358  CD  GLU B 126     115.975  72.055  17.924  1.00 94.35           C  
ANISOU 3358  CD  GLU B 126    13390  15359   7098    565    916   2070       C  
ATOM   3359  OE1 GLU B 126     114.905  72.692  18.020  1.00 97.21           O  
ANISOU 3359  OE1 GLU B 126    13977  15454   7507    635    676   2038       O  
ATOM   3360  OE2 GLU B 126     116.560  71.870  16.838  1.00104.73           O  
ANISOU 3360  OE2 GLU B 126    14752  16939   8102    628   1094   2177       O  
ATOM   3361  N   MET B 127     116.789  72.399  24.067  1.00 89.69           N  
ANISOU 3361  N   MET B 127    12038  14070   7971   -208    747   1880       N  
ATOM   3362  CA  MET B 127     116.447  73.152  25.264  1.00 94.57           C  
ANISOU 3362  CA  MET B 127    12717  14385   8829   -342    595   1887       C  
ATOM   3363  C   MET B 127     117.679  73.731  25.944  1.00 92.04           C  
ANISOU 3363  C   MET B 127    12292  14057   8624   -674    703   2094       C  
ATOM   3364  O   MET B 127     117.589  74.187  27.091  1.00 86.17           O  
ANISOU 3364  O   MET B 127    11555  13086   8099   -795    591   2075       O  
ATOM   3365  CB  MET B 127     115.657  72.273  26.234  1.00106.76           C  
ANISOU 3365  CB  MET B 127    14111  15849  10605   -184    479   1589       C  
ATOM   3366  CG  MET B 127     114.354  71.756  25.656  1.00116.17           C  
ANISOU 3366  CG  MET B 127    15391  17027  11721    114    339   1382       C  
ATOM   3367  SD  MET B 127     113.618  70.481  26.692  1.00125.02           S  
ANISOU 3367  SD  MET B 127    16276  18124  13102    260    257   1054       S  
ATOM   3368  CE  MET B 127     113.465  71.348  28.254  1.00121.03           C  
ANISOU 3368  CE  MET B 127    15793  17336  12856     96    161   1088       C  
ATOM   3369  N   ARG B 128     118.826  73.721  25.262  1.00 93.66           N  
ANISOU 3369  N   ARG B 128    12392  14513   8681   -821    916   2289       N  
ATOM   3370  CA  ARG B 128     120.038  74.380  25.742  1.00 89.25           C  
ANISOU 3370  CA  ARG B 128    11729  13968   8212  -1169   1017   2524       C  
ATOM   3371  C   ARG B 128     120.530  73.754  27.043  1.00 76.35           C  
ANISOU 3371  C   ARG B 128     9807  12344   6857  -1243   1017   2381       C  
ATOM   3372  O   ARG B 128     120.902  74.455  27.986  1.00 78.73           O  
ANISOU 3372  O   ARG B 128    10115  12458   7339  -1479    939   2471       O  
ATOM   3373  CB  ARG B 128     119.809  75.883  25.913  1.00 90.94           C  
ANISOU 3373  CB  ARG B 128    12260  13856   8438  -1375    868   2738       C  
ATOM   3374  CG  ARG B 128     119.567  76.618  24.615  1.00 97.99           C  
ANISOU 3374  CG  ARG B 128    13449  14744   9038  -1359    886   2945       C  
ATOM   3375  CD  ARG B 128     119.057  78.022  24.885  1.00104.93           C  
ANISOU 3375  CD  ARG B 128    14694  15227   9946  -1487    674   3093       C  
ATOM   3376  NE  ARG B 128     117.625  78.035  25.180  1.00106.07           N  
ANISOU 3376  NE  ARG B 128    15027  15131  10144  -1194    437   2860       N  
ATOM   3377  CZ  ARG B 128     117.035  78.918  25.979  1.00106.80           C  
ANISOU 3377  CZ  ARG B 128    15340  14865  10376  -1223    216   2846       C  
ATOM   3378  NH1 ARG B 128     117.749  79.874  26.554  1.00109.78           N  
ANISOU 3378  NH1 ARG B 128    15809  15050  10852  -1542    180   3048       N  
ATOM   3379  NH2 ARG B 128     115.729  78.853  26.196  1.00104.69           N  
ANISOU 3379  NH2 ARG B 128    15199  14434  10145   -931     23   2626       N  
ATOM   3380  N   ILE B 129     120.526  72.426  27.091  1.00 68.92           N  
ANISOU 3380  N   ILE B 129     8636  11607   5944  -1032   1088   2154       N  
ATOM   3381  CA  ILE B 129     120.967  71.690  28.269  1.00 72.63           C  
ANISOU 3381  CA  ILE B 129     8842  12098   6655  -1063   1087   2005       C  
ATOM   3382  C   ILE B 129     122.487  71.622  28.287  1.00 78.15           C  
ANISOU 3382  C   ILE B 129     9270  13059   7366  -1281   1280   2171       C  
ATOM   3383  O   ILE B 129     123.114  71.175  27.319  1.00 86.79           O  
ANISOU 3383  O   ILE B 129    10237  14468   8272  -1224   1474   2235       O  
ATOM   3384  CB  ILE B 129     120.350  70.286  28.282  1.00 80.01           C  
ANISOU 3384  CB  ILE B 129     9663  13126   7610   -754   1072   1706       C  
ATOM   3385  CG1 ILE B 129     118.836  70.379  28.452  1.00 98.09           C  
ANISOU 3385  CG1 ILE B 129    12173  15158   9938   -573    867   1542       C  
ATOM   3386  CG2 ILE B 129     120.959  69.445  29.382  1.00 81.47           C  
ANISOU 3386  CG2 ILE B 129     9577  13368   8008   -780   1096   1577       C  
ATOM   3387  CD1 ILE B 129     118.078  69.416  27.583  1.00114.71           C  
ANISOU 3387  CD1 ILE B 129    14299  17381  11905   -280    858   1353       C  
ATOM   3388  N   ASN B 130     123.084  72.055  29.396  1.00 74.14           N  
ANISOU 3388  N   ASN B 130     8663  12434   7074  -1519   1223   2233       N  
ATOM   3389  CA  ASN B 130     124.532  71.997  29.556  1.00 75.48           C  
ANISOU 3389  CA  ASN B 130     8535  12850   7294  -1742   1378   2379       C  
ATOM   3390  C   ASN B 130     125.000  70.545  29.559  1.00 82.35           C  
ANISOU 3390  C   ASN B 130     9097  14021   8172  -1524   1506   2186       C  
ATOM   3391  O   ASN B 130     124.654  69.775  30.461  1.00 85.78           O  
ANISOU 3391  O   ASN B 130     9462  14359   8769  -1385   1404   1958       O  
ATOM   3392  CB  ASN B 130     124.935  72.698  30.854  1.00 74.23           C  
ANISOU 3392  CB  ASN B 130     8356  12464   7384  -2014   1236   2440       C  
ATOM   3393  CG  ASN B 130     126.439  72.849  31.001  1.00 86.51           C  
ANISOU 3393  CG  ASN B 130     9608  14258   9003  -2297   1368   2626       C  
ATOM   3394  OD1 ASN B 130     127.201  71.911  30.764  1.00 98.65           O  
ANISOU 3394  OD1 ASN B 130    10833  16136  10512  -2203   1537   2574       O  
ATOM   3395  ND2 ASN B 130     126.875  74.043  31.390  1.00 87.73           N  
ANISOU 3395  ND2 ASN B 130     9854  14233   9248  -2642   1280   2843       N  
ATOM   3396  N   LEU B 131     125.809  70.177  28.560  1.00 82.83           N  
ANISOU 3396  N   LEU B 131     8980  14445   8046  -1491   1731   2282       N  
ATOM   3397  CA  LEU B 131     126.232  68.786  28.419  1.00 83.15           C  
ANISOU 3397  CA  LEU B 131     8762  14776   8056  -1237   1851   2089       C  
ATOM   3398  C   LEU B 131     127.308  68.385  29.420  1.00 88.33           C  
ANISOU 3398  C   LEU B 131     9086  15553   8921  -1349   1875   2067       C  
ATOM   3399  O   LEU B 131     127.381  67.207  29.791  1.00 79.57           O  
ANISOU 3399  O   LEU B 131     7824  14535   7875  -1121   1871   1842       O  
ATOM   3400  CB  LEU B 131     126.734  68.524  27.001  1.00 87.96           C  
ANISOU 3400  CB  LEU B 131     9299  15752   8370  -1124   2089   2186       C  
ATOM   3401  CG  LEU B 131     125.667  68.296  25.933  1.00 91.45           C  
ANISOU 3401  CG  LEU B 131    10018  16156   8572   -858   2067   2091       C  
ATOM   3402  CD1 LEU B 131     126.345  68.070  24.602  1.00 98.16           C  
ANISOU 3402  CD1 LEU B 131    10781  17399   9115   -760   2322   2204       C  
ATOM   3403  CD2 LEU B 131     124.770  67.120  26.292  1.00 85.48           C  
ANISOU 3403  CD2 LEU B 131     9305  15280   7893   -543   1924   1751       C  
ATOM   3404  N   ASP B 132     128.161  69.322  29.851  1.00 95.61           N  
ANISOU 3404  N   ASP B 132     9900  16476   9952  -1697   1887   2296       N  
ATOM   3405  CA  ASP B 132     129.163  68.989  30.862  1.00 91.73           C  
ANISOU 3405  CA  ASP B 132     9094  16087   9672  -1810   1875   2269       C  
ATOM   3406  C   ASP B 132     128.510  68.567  32.169  1.00 83.90           C  
ANISOU 3406  C   ASP B 132     8189  14791   8900  -1714   1649   2038       C  
ATOM   3407  O   ASP B 132     129.000  67.661  32.851  1.00 85.06           O  
ANISOU 3407  O   ASP B 132     8112  15043   9165  -1603   1638   1888       O  
ATOM   3408  CB  ASP B 132     130.104  70.167  31.114  1.00 97.26           C  
ANISOU 3408  CB  ASP B 132     9689  16802  10464  -2234   1887   2560       C  
ATOM   3409  CG  ASP B 132     131.197  69.828  32.124  1.00106.16           C  
ANISOU 3409  CG  ASP B 132    10464  18063  11809  -2352   1862   2534       C  
ATOM   3410  OD1 ASP B 132     131.981  68.892  31.868  1.00113.12           O  
ANISOU 3410  OD1 ASP B 132    11023  19306  12650  -2190   2019   2465       O  
ATOM   3411  OD2 ASP B 132     131.254  70.478  33.191  1.00107.14           O  
ANISOU 3411  OD2 ASP B 132    10647  17923  12140  -2582   1668   2566       O  
ATOM   3412  N   ILE B 133     127.418  69.231  32.547  1.00 81.82           N  
ANISOU 3412  N   ILE B 133     8250  14154   8684  -1751   1469   2014       N  
ATOM   3413  CA  ILE B 133     126.697  68.838  33.750  1.00 79.72           C  
ANISOU 3413  CA  ILE B 133     8080  13612   8598  -1646   1275   1800       C  
ATOM   3414  C   ILE B 133     126.100  67.449  33.573  1.00 80.25           C  
ANISOU 3414  C   ILE B 133     8122  13753   8617  -1290   1298   1540       C  
ATOM   3415  O   ILE B 133     126.187  66.601  34.470  1.00 83.40           O  
ANISOU 3415  O   ILE B 133     8410  14125   9152  -1183   1234   1370       O  
ATOM   3416  CB  ILE B 133     125.617  69.882  34.091  1.00 69.92           C  
ANISOU 3416  CB  ILE B 133     7191  11986   7391  -1732   1095   1831       C  
ATOM   3417  CG1 ILE B 133     126.252  71.242  34.373  1.00 69.85           C  
ANISOU 3417  CG1 ILE B 133     7235  11859   7447  -2096   1036   2078       C  
ATOM   3418  CG2 ILE B 133     124.811  69.432  35.294  1.00 58.64           C  
ANISOU 3418  CG2 ILE B 133     5853  10305   6121  -1598    924   1608       C  
ATOM   3419  CD1 ILE B 133     125.263  72.285  34.839  1.00 62.41           C  
ANISOU 3419  CD1 ILE B 133     6649  10515   6547  -2162    835   2093       C  
ATOM   3420  N   VAL B 134     125.498  67.192  32.410  1.00 65.42           N  
ANISOU 3420  N   VAL B 134     6361  11959   6538  -1106   1378   1509       N  
ATOM   3421  CA  VAL B 134     124.867  65.902  32.157  1.00 71.59           C  
ANISOU 3421  CA  VAL B 134     7149  12785   7267   -780   1375   1262       C  
ATOM   3422  C   VAL B 134     125.908  64.793  32.130  1.00 87.63           C  
ANISOU 3422  C   VAL B 134     8886  15115   9294   -649   1498   1179       C  
ATOM   3423  O   VAL B 134     125.708  63.719  32.708  1.00 99.91           O  
ANISOU 3423  O   VAL B 134    10394  16626  10940   -464   1431    968       O  
ATOM   3424  CB  VAL B 134     124.067  65.954  30.844  1.00 72.46           C  
ANISOU 3424  CB  VAL B 134     7455  12930   7148   -624   1418   1258       C  
ATOM   3425  CG1 VAL B 134     123.507  64.578  30.493  1.00 68.15           C  
ANISOU 3425  CG1 VAL B 134     6910  12442   6541   -299   1405   1000       C  
ATOM   3426  CG2 VAL B 134     122.960  66.979  30.947  1.00 58.58           C  
ANISOU 3426  CG2 VAL B 134     5991  10862   5407   -710   1269   1311       C  
ATOM   3427  N   ASP B 135     127.035  65.033  31.462  1.00 84.50           N  
ANISOU 3427  N   ASP B 135     8286  15031   8788   -738   1680   1346       N  
ATOM   3428  CA  ASP B 135     128.039  63.986  31.338  1.00 85.96           C  
ANISOU 3428  CA  ASP B 135     8178  15538   8945   -573   1808   1262       C  
ATOM   3429  C   ASP B 135     128.675  63.671  32.685  1.00 85.05           C  
ANISOU 3429  C   ASP B 135     7872  15373   9072   -648   1711   1202       C  
ATOM   3430  O   ASP B 135     128.904  62.499  33.008  1.00 89.55           O  
ANISOU 3430  O   ASP B 135     8323  16020   9680   -418   1697   1012       O  
ATOM   3431  CB  ASP B 135     129.098  64.398  30.319  1.00 95.55           C  
ANISOU 3431  CB  ASP B 135     9195  17130   9981   -661   2043   1474       C  
ATOM   3432  CG  ASP B 135     129.968  63.243  29.896  1.00104.00           C  
ANISOU 3432  CG  ASP B 135     9993  18569  10954   -399   2198   1359       C  
ATOM   3433  OD1 ASP B 135     129.408  62.233  29.416  1.00100.92           O  
ANISOU 3433  OD1 ASP B 135     9711  18187  10446    -73   2188   1144       O  
ATOM   3434  OD2 ASP B 135     131.204  63.342  30.046  1.00111.81           O  
ANISOU 3434  OD2 ASP B 135    10692  19786  12004   -508   2293   1465       O  
ATOM   3435  N   SER B 136     128.957  64.699  33.491  1.00 77.33           N  
ANISOU 3435  N   SER B 136     6885  14247   8251   -960   1625   1358       N  
ATOM   3436  CA  SER B 136     129.531  64.455  34.810  1.00 78.43           C  
ANISOU 3436  CA  SER B 136     6868  14322   8611  -1032   1508   1299       C  
ATOM   3437  C   SER B 136     128.592  63.635  35.682  1.00 82.60           C  
ANISOU 3437  C   SER B 136     7567  14575   9242   -837   1342   1059       C  
ATOM   3438  O   SER B 136     129.054  62.869  36.535  1.00 79.81           O  
ANISOU 3438  O   SER B 136     7075  14239   9009   -750   1278    941       O  
ATOM   3439  CB  SER B 136     129.878  65.775  35.502  1.00 81.82           C  
ANISOU 3439  CB  SER B 136     7313  14598   9178  -1406   1413   1499       C  
ATOM   3440  OG  SER B 136     128.782  66.671  35.504  1.00 86.70           O  
ANISOU 3440  OG  SER B 136     8269  14892   9782  -1506   1306   1546       O  
ATOM   3441  N   MET B 137     127.275  63.781  35.485  1.00 91.19           N  
ANISOU 3441  N   MET B 137     8949  15415  10284   -769   1268    990       N  
ATOM   3442  CA  MET B 137     126.325  62.938  36.205  1.00 84.53           C  
ANISOU 3442  CA  MET B 137     8252  14340   9525   -586   1134    772       C  
ATOM   3443  C   MET B 137     126.388  61.499  35.713  1.00 82.07           C  
ANISOU 3443  C   MET B 137     7860  14190   9133   -281   1194    586       C  
ATOM   3444  O   MET B 137     126.365  60.559  36.517  1.00 81.65           O  
ANISOU 3444  O   MET B 137     7783  14057   9185   -154   1111    431       O  
ATOM   3445  CB  MET B 137     124.905  63.487  36.064  1.00 75.95           C  
ANISOU 3445  CB  MET B 137     7463  12982   8411   -592   1045    752       C  
ATOM   3446  CG  MET B 137     124.651  64.799  36.797  1.00 74.15           C  
ANISOU 3446  CG  MET B 137     7374  12517   8283   -843    936    883       C  
ATOM   3447  SD  MET B 137     122.957  65.387  36.584  1.00 67.75           S  
ANISOU 3447  SD  MET B 137     6895  11419   7428   -790    832    839       S  
ATOM   3448  CE  MET B 137     123.032  66.964  37.417  1.00 74.09           C  
ANISOU 3448  CE  MET B 137     7837  11984   8330  -1077    714   1007       C  
ATOM   3449  N   ILE B 138     126.454  61.307  34.394  1.00 75.69           N  
ANISOU 3449  N   ILE B 138     7036  13596   8127   -153   1330    599       N  
ATOM   3450  CA  ILE B 138     126.684  59.971  33.857  1.00 77.45           C  
ANISOU 3450  CA  ILE B 138     7179  13996   8252    150   1389    423       C  
ATOM   3451  C   ILE B 138     128.022  59.431  34.338  1.00 84.47           C  
ANISOU 3451  C   ILE B 138     7778  15110   9208    192   1442    416       C  
ATOM   3452  O   ILE B 138     128.166  58.226  34.573  1.00 85.01           O  
ANISOU 3452  O   ILE B 138     7805  15199   9295    431   1402    232       O  
ATOM   3453  CB  ILE B 138     126.600  59.985  32.318  1.00 78.24           C  
ANISOU 3453  CB  ILE B 138     7321  14308   8097    280   1532    452       C  
ATOM   3454  CG1 ILE B 138     125.325  60.693  31.867  1.00 78.34           C  
ANISOU 3454  CG1 ILE B 138     7614  14102   8049    216   1461    485       C  
ATOM   3455  CG2 ILE B 138     126.624  58.569  31.774  1.00 79.59           C  
ANISOU 3455  CG2 ILE B 138     7481  14602   8159    624   1552    232       C  
ATOM   3456  CD1 ILE B 138     125.348  61.116  30.424  1.00 83.56           C  
ANISOU 3456  CD1 ILE B 138     8330  14964   8454    262   1600    588       C  
ATOM   3457  N   ALA B 139     129.016  60.308  34.503  1.00 87.66           N  
ANISOU 3457  N   ALA B 139     7976  15677   9654    -40   1517    614       N  
ATOM   3458  CA  ALA B 139     130.294  59.883  35.065  1.00 91.23           C  
ANISOU 3458  CA  ALA B 139     8122  16347  10196    -20   1544    614       C  
ATOM   3459  C   ALA B 139     130.124  59.402  36.498  1.00 97.16           C  
ANISOU 3459  C   ALA B 139     8920  16843  11152    -10   1348    489       C  
ATOM   3460  O   ALA B 139     130.539  58.290  36.847  1.00103.19           O  
ANISOU 3460  O   ALA B 139     9587  17674  11946    217   1314    334       O  
ATOM   3461  CB  ALA B 139     131.306  61.027  35.001  1.00 92.23           C  
ANISOU 3461  CB  ALA B 139     8019  16674  10349   -325   1640    868       C  
ATOM   3462  N   SER B 140     129.512  60.231  37.346  1.00 98.08           N  
ANISOU 3462  N   SER B 140     9205  16662  11397   -240   1215    553       N  
ATOM   3463  CA  SER B 140     129.301  59.835  38.733  1.00 91.85           C  
ANISOU 3463  CA  SER B 140     8488  15629  10780   -234   1037    447       C  
ATOM   3464  C   SER B 140     128.343  58.658  38.831  1.00 84.44           C  
ANISOU 3464  C   SER B 140     7745  14514   9824     24    968    233       C  
ATOM   3465  O   SER B 140     128.449  57.846  39.760  1.00 94.73           O  
ANISOU 3465  O   SER B 140     9052  15716  11226    130    862    116       O  
ATOM   3466  CB  SER B 140     128.779  61.019  39.546  1.00 96.46           C  
ANISOU 3466  CB  SER B 140     9238  15938  11475   -512    918    555       C  
ATOM   3467  OG  SER B 140     128.903  60.767  40.934  1.00103.10           O  
ANISOU 3467  OG  SER B 140    10096  16610  12469   -534    762    487       O  
ATOM   3468  N   ALA B 141     127.406  58.544  37.884  1.00 77.67           N  
ANISOU 3468  N   ALA B 141     7057  13612   8842    121   1017    186       N  
ATOM   3469  CA  ALA B 141     126.526  57.381  37.856  1.00 77.23           C  
ANISOU 3469  CA  ALA B 141     7171  13404   8770    351    947    -15       C  
ATOM   3470  C   ALA B 141     127.317  56.101  37.624  1.00 93.02           C  
ANISOU 3470  C   ALA B 141     9033  15588  10721    621    977   -151       C  
ATOM   3471  O   ALA B 141     127.038  55.067  38.244  1.00 95.79           O  
ANISOU 3471  O   ALA B 141     9475  15781  11139    768    868   -303       O  
ATOM   3472  CB  ALA B 141     125.457  57.556  36.778  1.00 71.77           C  
ANISOU 3472  CB  ALA B 141     6661  12662   7947    399    982    -37       C  
ATOM   3473  N   ILE B 142     128.314  56.152  36.738  1.00101.37           N  
ANISOU 3473  N   ILE B 142     9878  16984  11655    695   1126    -95       N  
ATOM   3474  CA  ILE B 142     129.166  54.992  36.500  1.00100.84           C  
ANISOU 3474  CA  ILE B 142     9661  17126  11529    982   1162   -226       C  
ATOM   3475  C   ILE B 142     130.211  54.846  37.605  1.00103.45           C  
ANISOU 3475  C   ILE B 142     9783  17517  12007    950   1100   -206       C  
ATOM   3476  O   ILE B 142     130.578  53.723  37.969  1.00111.97           O  
ANISOU 3476  O   ILE B 142    10837  18599  13109   1189   1029   -358       O  
ATOM   3477  CB  ILE B 142     129.816  55.096  35.109  1.00101.76           C  
ANISOU 3477  CB  ILE B 142     9618  17613  11434   1100   1363   -177       C  
ATOM   3478  CG1 ILE B 142     128.742  55.206  34.027  1.00100.32           C  
ANISOU 3478  CG1 ILE B 142     9673  17354  11091   1150   1397   -209       C  
ATOM   3479  CG2 ILE B 142     130.700  53.891  34.824  1.00104.52           C  
ANISOU 3479  CG2 ILE B 142     9813  18198  11703   1441   1404   -330       C  
ATOM   3480  CD1 ILE B 142     129.303  55.353  32.629  1.00103.59           C  
ANISOU 3480  CD1 ILE B 142     9971  18126  11264   1270   1601   -152       C  
ATOM   3481  N   GLU B 143     130.694  55.961  38.161  1.00107.63           N  
ANISOU 3481  N   GLU B 143    10176  18080  12637    661   1103    -26       N  
ATOM   3482  CA  GLU B 143     131.676  55.898  39.242  1.00118.82           C  
ANISOU 3482  CA  GLU B 143    11395  19551  14201    612   1017     -5       C  
ATOM   3483  C   GLU B 143     131.098  55.203  40.469  1.00132.92           C  
ANISOU 3483  C   GLU B 143    13388  21004  16112    676    820   -136       C  
ATOM   3484  O   GLU B 143     131.636  54.197  40.943  1.00142.36           O  
ANISOU 3484  O   GLU B 143    14520  22230  17339    891    746   -257       O  
ATOM   3485  CB  GLU B 143     132.154  57.306  39.601  1.00121.31           C  
ANISOU 3485  CB  GLU B 143    11574  19912  14605    254   1027    212       C  
ATOM   3486  CG  GLU B 143     133.019  57.363  40.855  1.00127.88           C  
ANISOU 3486  CG  GLU B 143    12241  20741  15606    163    890    232       C  
ATOM   3487  CD  GLU B 143     133.707  58.705  41.030  1.00135.48           C  
ANISOU 3487  CD  GLU B 143    13020  21809  16648   -187    903    447       C  
ATOM   3488  OE1 GLU B 143     133.021  59.683  41.402  1.00135.59           O  
ANISOU 3488  OE1 GLU B 143    13238  21566  16713   -437    831    539       O  
ATOM   3489  OE2 GLU B 143     134.932  58.780  40.791  1.00139.27           O  
ANISOU 3489  OE2 GLU B 143    13150  22628  17138   -211    980    524       O  
ATOM   3490  N   ASN B 144     129.999  55.735  41.002  1.00136.83           N  
ANISOU 3490  N   ASN B 144    14136  21184  16669    501    736   -109       N  
ATOM   3491  CA  ASN B 144     129.340  55.154  42.171  1.00134.85           C  
ANISOU 3491  CA  ASN B 144    14097  20618  16521    536    572   -210       C  
ATOM   3492  C   ASN B 144     128.693  53.834  41.770  1.00135.25           C  
ANISOU 3492  C   ASN B 144    14314  20571  16505    806    553   -389       C  
ATOM   3493  O   ASN B 144     127.572  53.803  41.258  1.00132.71           O  
ANISOU 3493  O   ASN B 144    14187  20104  16134    804    568   -428       O  
ATOM   3494  CB  ASN B 144     128.315  56.130  42.737  1.00131.36           C  
ANISOU 3494  CB  ASN B 144    13863  19908  16141    293    516   -129       C  
ATOM   3495  CG  ASN B 144     128.954  57.395  43.280  1.00130.96           C  
ANISOU 3495  CG  ASN B 144    13695  19897  16167     26    490     33       C  
ATOM   3496  OD1 ASN B 144     128.542  58.505  42.943  1.00132.61           O  
ANISOU 3496  OD1 ASN B 144    13966  20061  16358   -171    528    150       O  
ATOM   3497  ND2 ASN B 144     129.956  57.233  44.139  1.00129.28           N  
ANISOU 3497  ND2 ASN B 144    13326  19752  16041     19    403     38       N  
ATOM   3498  N   ASN B 145     129.410  52.734  41.998  1.00141.73           N  
ANISOU 3498  N   ASN B 145    15060  21464  17327   1043    502   -504       N  
ATOM   3499  CA  ASN B 145     128.927  51.400  41.671  1.00142.90           C  
ANISOU 3499  CA  ASN B 145    15379  21499  17417   1309    454   -682       C  
ATOM   3500  C   ASN B 145     128.333  50.667  42.866  1.00142.58           C  
ANISOU 3500  C   ASN B 145    15566  21128  17480   1324    288   -755       C  
ATOM   3501  O   ASN B 145     127.785  49.574  42.689  1.00146.68           O  
ANISOU 3501  O   ASN B 145    16271  21491  17970   1500    225   -891       O  
ATOM   3502  CB  ASN B 145     130.062  50.558  41.077  1.00146.78           C  
ANISOU 3502  CB  ASN B 145    15679  22269  17820   1608    498   -777       C  
ATOM   3503  CG  ASN B 145     129.898  50.330  39.591  1.00149.02           C  
ANISOU 3503  CG  ASN B 145    15961  22728  17931   1771    627   -840       C  
ATOM   3504  OD1 ASN B 145     128.826  50.563  39.035  1.00153.51           O  
ANISOU 3504  OD1 ASN B 145    16715  23161  18453   1691    648   -843       O  
ATOM   3505  ND2 ASN B 145     130.961  49.876  38.937  1.00145.61           N  
ANISOU 3505  ND2 ASN B 145    15318  22614  17396   2015    712   -894       N  
ATOM   3506  N   LYS B 146     128.431  51.233  44.070  1.00139.28           N  
ANISOU 3506  N   LYS B 146    15152  20595  17173   1142    212   -666       N  
ATOM   3507  CA  LYS B 146     127.880  50.594  45.258  1.00128.96           C  
ANISOU 3507  CA  LYS B 146    14069  18986  15945   1146     70   -714       C  
ATOM   3508  C   LYS B 146     126.367  50.467  45.147  1.00114.29           C  
ANISOU 3508  C   LYS B 146    12465  16874  14086   1064     70   -741       C  
ATOM   3509  O   LYS B 146     125.641  51.448  45.332  1.00115.37           O  
ANISOU 3509  O   LYS B 146    12652  16931  14251    849    105   -650       O  
ATOM   3510  CB  LYS B 146     128.254  51.379  46.519  1.00132.64           C  
ANISOU 3510  CB  LYS B 146    14497  19397  16503    961     -4   -606       C  
ATOM   3511  CG  LYS B 146     129.749  51.475  46.781  1.00136.56           C  
ANISOU 3511  CG  LYS B 146    14727  20134  17025   1024    -39   -580       C  
ATOM   3512  CD  LYS B 146     130.040  52.289  48.033  1.00133.22           C  
ANISOU 3512  CD  LYS B 146    14296  19629  16691    825   -141   -483       C  
ATOM   3513  CE  LYS B 146     131.528  52.319  48.337  1.00133.86           C  
ANISOU 3513  CE  LYS B 146    14096  19951  16813    886   -205   -465       C  
ATOM   3514  NZ  LYS B 146     131.837  53.116  49.556  1.00134.50           N  
ANISOU 3514  NZ  LYS B 146    14181  19945  16979    692   -335   -382       N  
ATOM   3515  N   VAL B 147     125.885  49.268  44.834  1.00 94.44           N  
ANISOU 3515  N   VAL B 147    10109  14230  11543   1237     20   -870       N  
ATOM   3516  CA  VAL B 147     124.458  48.977  44.751  1.00 83.44           C  
ANISOU 3516  CA  VAL B 147     8940  12597  10166   1161      0   -906       C  
ATOM   3517  C   VAL B 147     124.143  47.837  45.707  1.00 87.91           C  
ANISOU 3517  C   VAL B 147     9715  12900  10789   1224   -130   -967       C  
ATOM   3518  O   VAL B 147     124.777  46.776  45.649  1.00 92.85           O  
ANISOU 3518  O   VAL B 147    10373  13517  11389   1444   -207  -1065       O  
ATOM   3519  CB  VAL B 147     124.027  48.628  43.317  1.00 77.42           C  
ANISOU 3519  CB  VAL B 147     8197  11910   9310   1275     50  -1000       C  
ATOM   3520  CG1 VAL B 147     122.725  47.863  43.335  1.00 67.23           C  
ANISOU 3520  CG1 VAL B 147     7142  10349   8054   1251    -28  -1077       C  
ATOM   3521  CG2 VAL B 147     123.865  49.898  42.510  1.00 82.09           C  
ANISOU 3521  CG2 VAL B 147     8663  12678   9848   1141    176   -906       C  
ATOM   3522  N   ALA B 148     123.159  48.055  46.575  1.00 85.28           N  
ANISOU 3522  N   ALA B 148     9528  12351  10522   1040   -152   -905       N  
ATOM   3523  CA  ALA B 148     122.870  47.114  47.642  1.00 93.82           C  
ANISOU 3523  CA  ALA B 148    10811  13183  11653   1056   -259   -921       C  
ATOM   3524  C   ALA B 148     121.958  45.996  47.159  1.00 97.06           C  
ANISOU 3524  C   ALA B 148    11408  13402  12067   1107   -313  -1018       C  
ATOM   3525  O   ALA B 148     121.049  46.214  46.352  1.00 88.97           O  
ANISOU 3525  O   ALA B 148    10389  12377  11038   1031   -265  -1041       O  
ATOM   3526  CB  ALA B 148     122.230  47.835  48.826  1.00 97.90           C  
ANISOU 3526  CB  ALA B 148    11402  13574  12222    841   -243   -805       C  
ATOM   3527  N   THR B 149     122.215  44.790  47.662  1.00106.02           N  
ANISOU 3527  N   THR B 149    12707  14363  13212   1236   -434  -1076       N  
ATOM   3528  CA  THR B 149     121.344  43.658  47.371  1.00119.77           C  
ANISOU 3528  CA  THR B 149    14663  15871  14973   1253   -516  -1157       C  
ATOM   3529  C   THR B 149     120.021  43.793  48.115  1.00107.62           C  
ANISOU 3529  C   THR B 149    13250  14132  13510    995   -494  -1064       C  
ATOM   3530  O   THR B 149     118.948  43.824  47.500  1.00102.44           O  
ANISOU 3530  O   THR B 149    12612  13428  12881    882   -468  -1086       O  
ATOM   3531  CB  THR B 149     122.045  42.349  47.746  1.00142.50           C  
ANISOU 3531  CB  THR B 149    17709  18599  17837   1468   -666  -1235       C  
ATOM   3532  OG1 THR B 149     123.174  42.142  46.887  1.00150.66           O  
ANISOU 3532  OG1 THR B 149    18612  19841  18791   1741   -679  -1345       O  
ATOM   3533  CG2 THR B 149     121.093  41.172  47.601  1.00148.60           C  
ANISOU 3533  CG2 THR B 149    18744  19074  18645   1441   -774  -1299       C  
ATOM   3534  N   GLU B 150     120.082  43.888  49.441  1.00103.09           N  
ANISOU 3534  N   GLU B 150    12752  13456  12962    907   -503   -960       N  
ATOM   3535  CA  GLU B 150     118.915  44.074  50.289  1.00 95.50           C  
ANISOU 3535  CA  GLU B 150    11892  12342  12053    676   -456   -856       C  
ATOM   3536  C   GLU B 150     119.141  45.288  51.180  1.00 93.92           C  
ANISOU 3536  C   GLU B 150    11594  12252  11837    579   -372   -743       C  
ATOM   3537  O   GLU B 150     120.190  45.937  51.135  1.00 94.15           O  
ANISOU 3537  O   GLU B 150    11483  12457  11832    666   -367   -743       O  
ATOM   3538  CB  GLU B 150     118.648  42.835  51.152  1.00 98.10           C  
ANISOU 3538  CB  GLU B 150    12479  12389  12406    662   -558   -832       C  
ATOM   3539  CG  GLU B 150     118.627  41.543  50.383  1.00104.43           C  
ANISOU 3539  CG  GLU B 150    13422  13038  13217    785   -685   -952       C  
ATOM   3540  CD  GLU B 150     117.487  41.477  49.394  1.00109.39           C  
ANISOU 3540  CD  GLU B 150    14026  13642  13894    665   -663  -1006       C  
ATOM   3541  OE1 GLU B 150     116.409  42.041  49.684  1.00108.91           O  
ANISOU 3541  OE1 GLU B 150    13918  13579  13885    440   -568   -919       O  
ATOM   3542  OE2 GLU B 150     117.674  40.863  48.323  1.00112.21           O  
ANISOU 3542  OE2 GLU B 150    14412  13993  14232    813   -749  -1143       O  
ATOM   3543  N   ILE B 151     118.154  45.581  52.017  1.00 95.18           N  
ANISOU 3543  N   ILE B 151    11832  12311  12022    396   -309   -648       N  
ATOM   3544  CA  ILE B 151     118.261  46.622  53.031  1.00 96.42           C  
ANISOU 3544  CA  ILE B 151    11960  12526  12150    314   -248   -548       C  
ATOM   3545  C   ILE B 151     118.420  45.938  54.384  1.00112.01           C  
ANISOU 3545  C   ILE B 151    14139  14323  14096    316   -308   -480       C  
ATOM   3546  O   ILE B 151     117.586  45.108  54.769  1.00116.00           O  
ANISOU 3546  O   ILE B 151    14806  14647  14621    232   -307   -443       O  
ATOM   3547  CB  ILE B 151     117.045  47.559  53.001  1.00 85.75           C  
ANISOU 3547  CB  ILE B 151    10546  11219  10818    144   -123   -496       C  
ATOM   3548  CG1 ILE B 151     117.149  48.519  51.817  1.00 72.68           C  
ANISOU 3548  CG1 ILE B 151     8696   9757   9163    160    -77   -543       C  
ATOM   3549  CG2 ILE B 151     116.939  48.328  54.274  1.00 89.21           C  
ANISOU 3549  CG2 ILE B 151    11038  11645  11213     69    -74   -398       C  
ATOM   3550  CD1 ILE B 151     115.963  49.436  51.683  1.00 63.39           C  
ANISOU 3550  CD1 ILE B 151     7460   8622   8002     28     25   -506       C  
ATOM   3551  N   LEU B 152     119.519  46.276  55.113  1.00118.87           N  
ANISOU 3551  N   LEU B 152    15004  15245  14916    406   -369   -457       N  
ATOM   3552  CA  LEU B 152     119.831  45.551  56.346  1.00132.65           C  
ANISOU 3552  CA  LEU B 152    16963  16823  16615    448   -455   -401       C  
ATOM   3553  C   LEU B 152     119.469  46.372  57.574  1.00133.92           C  
ANISOU 3553  C   LEU B 152    17195  16971  16717    336   -393   -296       C  
ATOM   3554  O   LEU B 152     119.912  47.524  57.693  1.00135.42           O  
ANISOU 3554  O   LEU B 152    17260  17307  16888    327   -377   -291       O  
ATOM   3555  CB  LEU B 152     121.309  45.183  56.394  1.00140.23           C  
ANISOU 3555  CB  LEU B 152    17894  17834  17552    657   -599   -459       C  
ATOM   3556  CG  LEU B 152     121.782  44.112  55.411  1.00141.88           C  
ANISOU 3556  CG  LEU B 152    18096  18023  17788    831   -685   -571       C  
ATOM   3557  CD1 LEU B 152     123.227  43.724  55.702  1.00142.76           C  
ANISOU 3557  CD1 LEU B 152    18188  18188  17867   1059   -831   -619       C  
ATOM   3558  CD2 LEU B 152     120.862  42.900  55.458  1.00139.41           C  
ANISOU 3558  CD2 LEU B 152    18024  17451  17495    783   -713   -565       C  
ATOM   3559  N   PRO B 153     118.688  45.812  58.517  1.00130.92           N  
ANISOU 3559  N   PRO B 153    17028  16418  16299    250   -360   -208       N  
ATOM   3560  CA  PRO B 153     118.314  46.491  59.763  1.00121.98           C  
ANISOU 3560  CA  PRO B 153    15997  15272  15079    170   -294   -109       C  
ATOM   3561  C   PRO B 153     119.470  46.604  60.752  1.00118.45           C  
ANISOU 3561  C   PRO B 153    15649  14812  14545    292   -425    -94       C  
ATOM   3562  O   PRO B 153     119.216  46.741  61.949  1.00118.84           O  
ANISOU 3562  O   PRO B 153    15873  14788  14493    259   -405     -9       O  
ATOM   3563  CB  PRO B 153     117.210  45.592  60.331  1.00121.89           C  
ANISOU 3563  CB  PRO B 153    16180  15083  15049     52   -219    -16       C  
ATOM   3564  CG  PRO B 153     117.528  44.245  59.787  1.00125.01           C  
ANISOU 3564  CG  PRO B 153    16665  15333  15501    120   -336    -60       C  
ATOM   3565  CD  PRO B 153     118.034  44.496  58.395  1.00128.45           C  
ANISOU 3565  CD  PRO B 153    16876  15911  16020    209   -376   -193       C  
ATOM   3566  N   PHE B 163     114.270  52.225  78.838  1.00144.35           N  
ANISOU 3566  N   PHE B 163    22107  18009  14728    859    536    839       N  
ATOM   3567  CA  PHE B 163     113.482  53.091  77.967  1.00143.05           C  
ANISOU 3567  CA  PHE B 163    21644  17991  14718    810    687    752       C  
ATOM   3568  C   PHE B 163     112.177  52.417  77.557  1.00138.06           C  
ANISOU 3568  C   PHE B 163    20831  17464  14162    648   1017    889       C  
ATOM   3569  O   PHE B 163     111.920  52.205  76.370  1.00135.21           O  
ANISOU 3569  O   PHE B 163    20170  17126  14075    507   1050    868       O  
ATOM   3570  CB  PHE B 163     114.284  53.481  76.724  1.00142.94           C  
ANISOU 3570  CB  PHE B 163    21363  17938  15009    754    466    610       C  
ATOM   3571  CG  PHE B 163     115.440  54.394  77.013  1.00150.33           C  
ANISOU 3571  CG  PHE B 163    22408  18809  15903    882    159    464       C  
ATOM   3572  CD1 PHE B 163     115.350  55.354  78.008  1.00157.60           C  
ANISOU 3572  CD1 PHE B 163    23564  19749  16567   1043    131    400       C  
ATOM   3573  CD2 PHE B 163     116.616  54.292  76.290  1.00151.31           C  
ANISOU 3573  CD2 PHE B 163    22393  18856  16240    841   -107    389       C  
ATOM   3574  CE1 PHE B 163     116.413  56.195  78.275  1.00161.18           C  
ANISOU 3574  CE1 PHE B 163    24123  20124  16993   1138   -178    264       C  
ATOM   3575  CE2 PHE B 163     117.682  55.130  76.553  1.00154.47           C  
ANISOU 3575  CE2 PHE B 163    22866  19207  16619    928   -396    265       C  
ATOM   3576  CZ  PHE B 163     117.580  56.082  77.548  1.00159.11           C  
ANISOU 3576  CZ  PHE B 163    23698  19791  16964   1065   -442    202       C  
ATOM   3577  N   GLU B 164     111.357  52.087  78.552  1.00131.84           N  
ANISOU 3577  N   GLU B 164    20224  16747  13121    667   1257   1032       N  
ATOM   3578  CA  GLU B 164     110.072  51.454  78.310  1.00129.02           C  
ANISOU 3578  CA  GLU B 164    19697  16510  12816    497   1583   1183       C  
ATOM   3579  C   GLU B 164     109.054  52.484  77.826  1.00112.22           C  
ANISOU 3579  C   GLU B 164    17299  14599  10742    529   1778   1092       C  
ATOM   3580  O   GLU B 164     109.343  53.677  77.700  1.00103.76           O  
ANISOU 3580  O   GLU B 164    16208  13561   9656    686   1659    918       O  
ATOM   3581  CB  GLU B 164     109.583  50.746  79.571  1.00145.44           C  
ANISOU 3581  CB  GLU B 164    22061  18606  14595    497   1783   1387       C  
ATOM   3582  CG  GLU B 164     110.181  49.366  79.761  1.00157.73           C  
ANISOU 3582  CG  GLU B 164    23811  19949  16170    379   1668   1538       C  
ATOM   3583  CD  GLU B 164     110.388  49.013  81.218  1.00169.15           C  
ANISOU 3583  CD  GLU B 164    25681  21339  17249    491   1690   1672       C  
ATOM   3584  OE1 GLU B 164     109.713  49.617  82.078  1.00174.24           O  
ANISOU 3584  OE1 GLU B 164    26433  22153  17617    606   1904   1703       O  
ATOM   3585  OE2 GLU B 164     111.225  48.129  81.502  1.00172.19           O  
ANISOU 3585  OE2 GLU B 164    26301  21515  17608    482   1491   1744       O  
ATOM   3586  N   ALA B 165     107.834  52.007  77.564  1.00105.69           N  
ANISOU 3586  N   ALA B 165    16264  13915   9977    376   2072   1216       N  
ATOM   3587  CA  ALA B 165     106.804  52.855  76.972  1.00102.93           C  
ANISOU 3587  CA  ALA B 165    15612  13783   9716    397   2253   1134       C  
ATOM   3588  C   ALA B 165     106.485  54.052  77.856  1.00103.32           C  
ANISOU 3588  C   ALA B 165    15802  13976   9479    659   2343   1046       C  
ATOM   3589  O   ALA B 165     106.304  55.170  77.360  1.00 92.15           O  
ANISOU 3589  O   ALA B 165    14246  12642   8126    784   2303    880       O  
ATOM   3590  CB  ALA B 165     105.539  52.037  76.710  1.00106.44           C  
ANISOU 3590  CB  ALA B 165    15820  14371  10253    180   2555   1303       C  
ATOM   3591  N   SER B 166     106.413  53.838  79.169  1.00120.51           N  
ANISOU 3591  N   SER B 166    18281  16178  11328    759   2458   1153       N  
ATOM   3592  CA  SER B 166     106.054  54.928  80.068  1.00121.75           C  
ANISOU 3592  CA  SER B 166    18599  16480  11178   1033   2557   1066       C  
ATOM   3593  C   SER B 166     107.092  56.045  80.032  1.00111.28           C  
ANISOU 3593  C   SER B 166    17435  15013   9834   1232   2222    840       C  
ATOM   3594  O   SER B 166     106.738  57.231  80.010  1.00103.08           O  
ANISOU 3594  O   SER B 166    16365  14073   8728   1422   2235    687       O  
ATOM   3595  CB  SER B 166     105.882  54.389  81.485  1.00128.95           C  
ANISOU 3595  CB  SER B 166    19838  17434  11723   1099   2728   1234       C  
ATOM   3596  OG  SER B 166     107.045  53.692  81.890  1.00132.66           O  
ANISOU 3596  OG  SER B 166    20602  17655  12146   1062   2475   1285       O  
ATOM   3597  N   LYS B 167     108.378  55.686  79.995  1.00106.38           N  
ANISOU 3597  N   LYS B 167    16977  14158   9283   1188   1908    815       N  
ATOM   3598  CA  LYS B 167     109.422  56.702  80.093  1.00103.45           C  
ANISOU 3598  CA  LYS B 167    16775  13652   8878   1353   1579    621       C  
ATOM   3599  C   LYS B 167     109.482  57.554  78.830  1.00107.96           C  
ANISOU 3599  C   LYS B 167    17056  14222   9741   1318   1460    463       C  
ATOM   3600  O   LYS B 167     109.647  58.777  78.909  1.00116.64           O  
ANISOU 3600  O   LYS B 167    18235  15309  10773   1486   1332    298       O  
ATOM   3601  CB  LYS B 167     110.768  56.034  80.387  1.00 97.39           C  
ANISOU 3601  CB  LYS B 167    16221  12665   8119   1310   1281    646       C  
ATOM   3602  CG  LYS B 167     111.836  56.983  80.919  1.00111.38           C  
ANISOU 3602  CG  LYS B 167    18247  14308   9763   1494    950    477       C  
ATOM   3603  CD  LYS B 167     112.977  56.224  81.606  1.00122.98           C  
ANISOU 3603  CD  LYS B 167    19986  15605  11134   1501    707    532       C  
ATOM   3604  CE  LYS B 167     114.009  57.181  82.214  1.00121.95           C  
ANISOU 3604  CE  LYS B 167    20111  15358  10867   1678    362    362       C  
ATOM   3605  NZ  LYS B 167     115.140  56.480  82.905  1.00110.10           N  
ANISOU 3605  NZ  LYS B 167    18863  13701   9267   1707     99    404       N  
ATOM   3606  N   LEU B 168     109.326  56.929  77.660  1.00 95.83           N  
ANISOU 3606  N   LEU B 168    15202  12690   8517   1103   1496    512       N  
ATOM   3607  CA  LEU B 168     109.317  57.669  76.400  1.00 79.86           C  
ANISOU 3607  CA  LEU B 168    12902  10679   6763   1061   1405    382       C  
ATOM   3608  C   LEU B 168     108.133  58.628  76.319  1.00 86.00           C  
ANISOU 3608  C   LEU B 168    13559  11643   7473   1193   1611    313       C  
ATOM   3609  O   LEU B 168     108.282  59.768  75.860  1.00 80.54           O  
ANISOU 3609  O   LEU B 168    12836  10927   6839   1294   1474    159       O  
ATOM   3610  CB  LEU B 168     109.280  56.691  75.226  1.00 67.07           C  
ANISOU 3610  CB  LEU B 168    10990   9041   5453    820   1427    458       C  
ATOM   3611  CG  LEU B 168     110.520  55.839  74.983  1.00 60.58           C  
ANISOU 3611  CG  LEU B 168    10227   8033   4758    709   1186    488       C  
ATOM   3612  CD1 LEU B 168     110.231  54.819  73.913  1.00 58.09           C  
ANISOU 3612  CD1 LEU B 168     9648   7719   4706    498   1257    565       C  
ATOM   3613  CD2 LEU B 168     111.672  56.730  74.560  1.00 61.26           C  
ANISOU 3613  CD2 LEU B 168    10326   8012   4938    769    877    331       C  
ATOM   3614  N   ARG B 169     106.947  58.178  76.744  1.00 96.59           N  
ANISOU 3614  N   ARG B 169    14827  13175   8697   1192   1939    431       N  
ATOM   3615  CA  ARG B 169     105.765  59.034  76.685  1.00 94.18           C  
ANISOU 3615  CA  ARG B 169    14377  13083   8325   1340   2152    366       C  
ATOM   3616  C   ARG B 169     105.963  60.301  77.505  1.00 85.99           C  
ANISOU 3616  C   ARG B 169    13627  12026   7020   1639   2053    213       C  
ATOM   3617  O   ARG B 169     105.589  61.394  77.067  1.00 79.49           O  
ANISOU 3617  O   ARG B 169    12723  11249   6229   1783   2023     69       O  
ATOM   3618  CB  ARG B 169     104.526  58.271  77.163  1.00107.04           C  
ANISOU 3618  CB  ARG B 169    15882  14943   9846   1284   2530    537       C  
ATOM   3619  CG  ARG B 169     103.953  57.312  76.124  1.00118.24           C  
ANISOU 3619  CG  ARG B 169    16937  16422  11566   1003   2649    651       C  
ATOM   3620  CD  ARG B 169     102.561  56.793  76.486  1.00127.04           C  
ANISOU 3620  CD  ARG B 169    17860  17807  12602    942   3032    803       C  
ATOM   3621  NE  ARG B 169     102.022  55.933  75.431  1.00135.39           N  
ANISOU 3621  NE  ARG B 169    18568  18904  13970    661   3104    893       N  
ATOM   3622  CZ  ARG B 169     101.215  56.352  74.458  1.00136.80           C  
ANISOU 3622  CZ  ARG B 169    18398  19232  14348    644   3167    819       C  
ATOM   3623  NH1 ARG B 169     100.840  57.625  74.408  1.00142.82           N  
ANISOU 3623  NH1 ARG B 169    19117  20117  15032    903   3174    659       N  
ATOM   3624  NH2 ARG B 169     100.779  55.501  73.535  1.00127.16           N  
ANISOU 3624  NH2 ARG B 169    16887  18028  13400    380   3204    900       N  
ATOM   3625  N   GLU B 170     106.571  60.179  78.688  1.00 88.99           N  
ANISOU 3625  N   GLU B 170    14365  12319   7129   1744   1978    235       N  
ATOM   3626  CA  GLU B 170     106.816  61.364  79.502  1.00 93.87           C  
ANISOU 3626  CA  GLU B 170    15295  12893   7480   2032   1848     76       C  
ATOM   3627  C   GLU B 170     107.786  62.316  78.813  1.00 94.93           C  
ANISOU 3627  C   GLU B 170    15463  12817   7790   2040   1481   -101       C  
ATOM   3628  O   GLU B 170     107.622  63.540  78.889  1.00100.03           O  
ANISOU 3628  O   GLU B 170    16216  13448   8344   2245   1396   -261       O  
ATOM   3629  CB  GLU B 170     107.343  60.964  80.876  1.00 99.69           C  
ANISOU 3629  CB  GLU B 170    16421  13565   7892   2131   1812    137       C  
ATOM   3630  CG  GLU B 170     106.832  61.861  81.983  1.00114.14           C  
ANISOU 3630  CG  GLU B 170    18532  15498   9336   2462   1909     41       C  
ATOM   3631  CD  GLU B 170     107.758  61.899  83.174  1.00128.84           C  
ANISOU 3631  CD  GLU B 170    20846  17205  10904   2598   1697     12       C  
ATOM   3632  OE1 GLU B 170     108.683  61.061  83.231  1.00134.15           O  
ANISOU 3632  OE1 GLU B 170    21593  17722  11656   2428   1525    101       O  
ATOM   3633  OE2 GLU B 170     107.558  62.762  84.056  1.00134.49           O  
ANISOU 3633  OE2 GLU B 170    21844  17952  11303   2889   1691   -108       O  
ATOM   3634  N   ILE B 171     108.797  61.776  78.129  1.00 93.70           N  
ANISOU 3634  N   ILE B 171    15218  12498   7885   1819   1260    -70       N  
ATOM   3635  CA  ILE B 171     109.725  62.622  77.384  1.00 86.86           C  
ANISOU 3635  CA  ILE B 171    14338  11456   7210   1783    932   -210       C  
ATOM   3636  C   ILE B 171     108.980  63.381  76.297  1.00 90.56           C  
ANISOU 3636  C   ILE B 171    14543  12005   7862   1788   1005   -286       C  
ATOM   3637  O   ILE B 171     109.148  64.594  76.132  1.00 95.66           O  
ANISOU 3637  O   ILE B 171    15286  12563   8496   1910    833   -432       O  
ATOM   3638  CB  ILE B 171     110.866  61.783  76.785  1.00 76.47           C  
ANISOU 3638  CB  ILE B 171    12919  10004   6133   1547    730   -146       C  
ATOM   3639  CG1 ILE B 171     111.761  61.218  77.883  1.00 67.89           C  
ANISOU 3639  CG1 ILE B 171    12131   8807   4858   1579    582   -102       C  
ATOM   3640  CG2 ILE B 171     111.695  62.633  75.832  1.00 70.40           C  
ANISOU 3640  CG2 ILE B 171    12054   9103   5593   1474    447   -266       C  
ATOM   3641  CD1 ILE B 171     112.903  60.390  77.348  1.00 66.26           C  
ANISOU 3641  CD1 ILE B 171    11824   8480   4872   1387    376    -50       C  
ATOM   3642  N   ARG B 172     108.146  62.672  75.536  1.00 89.28           N  
ANISOU 3642  N   ARG B 172    14055  11996   7870   1655   1243   -186       N  
ATOM   3643  CA  ARG B 172     107.371  63.329  74.491  1.00 92.07           C  
ANISOU 3643  CA  ARG B 172    14149  12440   8392   1670   1314   -253       C  
ATOM   3644  C   ARG B 172     106.336  64.268  75.096  1.00 99.40           C  
ANISOU 3644  C   ARG B 172    15171  13508   9088   1955   1472   -341       C  
ATOM   3645  O   ARG B 172     106.065  65.342  74.545  1.00 95.34           O  
ANISOU 3645  O   ARG B 172    14622  12976   8626   2074   1392   -468       O  
ATOM   3646  CB  ARG B 172     106.701  62.283  73.602  1.00 88.82           C  
ANISOU 3646  CB  ARG B 172    13376  12165   8206   1462   1518   -128       C  
ATOM   3647  CG  ARG B 172     105.869  62.871  72.479  1.00 98.72           C  
ANISOU 3647  CG  ARG B 172    14345  13525   9637   1475   1585   -192       C  
ATOM   3648  CD  ARG B 172     105.162  61.777  71.708  1.00103.59           C  
ANISOU 3648  CD  ARG B 172    14624  14280  10457   1269   1777    -72       C  
ATOM   3649  NE  ARG B 172     104.359  60.944  72.595  1.00107.83           N  
ANISOU 3649  NE  ARG B 172    15149  14981  10839   1262   2059     59       N  
ATOM   3650  CZ  ARG B 172     103.563  59.966  72.181  1.00106.37           C  
ANISOU 3650  CZ  ARG B 172    14694  14935  10788   1084   2263    181       C  
ATOM   3651  NH1 ARG B 172     103.470  59.689  70.887  1.00108.12           N  
ANISOU 3651  NH1 ARG B 172    14642  15145  11292    920   2202    172       N  
ATOM   3652  NH2 ARG B 172     102.863  59.264  73.061  1.00103.56           N  
ANISOU 3652  NH2 ARG B 172    14345  14725  10276   1063   2521    315       N  
ATOM   3653  N   LYS B 173     105.760  63.885  76.238  1.00105.03           N  
ANISOU 3653  N   LYS B 173    16017  14360   9529   2080   1696   -275       N  
ATOM   3654  CA  LYS B 173     104.795  64.749  76.912  1.00111.89           C  
ANISOU 3654  CA  LYS B 173    16987  15387  10140   2389   1863   -365       C  
ATOM   3655  C   LYS B 173     105.445  66.050  77.360  1.00116.77           C  
ANISOU 3655  C   LYS B 173    17958  15810  10597   2617   1578   -554       C  
ATOM   3656  O   LYS B 173     104.888  67.134  77.152  1.00123.31           O  
ANISOU 3656  O   LYS B 173    18801  16668  11383   2832   1565   -693       O  
ATOM   3657  CB  LYS B 173     104.173  64.007  78.098  1.00113.82           C  
ANISOU 3657  CB  LYS B 173    17321  15823  10101   2463   2163   -238       C  
ATOM   3658  CG  LYS B 173     103.209  64.820  78.954  1.00118.94           C  
ANISOU 3658  CG  LYS B 173    18095  16668  10428   2816   2364   -325       C  
ATOM   3659  CD  LYS B 173     102.638  63.959  80.085  1.00120.67           C  
ANISOU 3659  CD  LYS B 173    18382  17096  10370   2848   2688   -162       C  
ATOM   3660  CE  LYS B 173     101.813  64.769  81.082  1.00123.15           C  
ANISOU 3660  CE  LYS B 173    18815  17578  10400   3179   2834   -251       C  
ATOM   3661  NZ  LYS B 173     102.623  65.793  81.794  1.00124.31           N  
ANISOU 3661  NZ  LYS B 173    19377  17487  10370   3406   2515   -431       N  
ATOM   3662  N   ASN B 174     106.635  65.966  77.958  1.00117.18           N  
ANISOU 3662  N   ASN B 174    18303  15651  10568   2574   1325   -567       N  
ATOM   3663  CA  ASN B 174     107.291  67.167  78.468  1.00114.68           C  
ANISOU 3663  CA  ASN B 174    18347  15132  10094   2770   1027   -745       C  
ATOM   3664  C   ASN B 174     107.862  68.026  77.351  1.00106.60           C  
ANISOU 3664  C   ASN B 174    17245  13918   9341   2669    742   -848       C  
ATOM   3665  O   ASN B 174     108.007  69.243  77.519  1.00110.21           O  
ANISOU 3665  O   ASN B 174    17940  14233   9701   2851    540  -1009       O  
ATOM   3666  CB  ASN B 174     108.395  66.790  79.452  1.00111.25           C  
ANISOU 3666  CB  ASN B 174    18233  14540   9496   2743    825   -726       C  
ATOM   3667  CG  ASN B 174     107.857  66.464  80.819  1.00106.61           C  
ANISOU 3667  CG  ASN B 174    17888  14095   8523   2960   1042   -685       C  
ATOM   3668  OD1 ASN B 174     107.087  67.236  81.392  1.00108.78           O  
ANISOU 3668  OD1 ASN B 174    18315  14472   8545   3256   1160   -789       O  
ATOM   3669  ND2 ASN B 174     108.265  65.321  81.360  1.00102.63           N  
ANISOU 3669  ND2 ASN B 174    17436  13602   7957   2829   1096   -533       N  
ATOM   3670  N   ILE B 175     108.209  67.422  76.217  1.00 99.47           N  
ANISOU 3670  N   ILE B 175    16033  12999   8764   2383    714   -757       N  
ATOM   3671  CA  ILE B 175     108.676  68.216  75.092  1.00 96.87           C  
ANISOU 3671  CA  ILE B 175    15608  12516   8680   2280    482   -832       C  
ATOM   3672  C   ILE B 175     107.516  68.981  74.471  1.00103.19           C  
ANISOU 3672  C   ILE B 175    16268  13430   9509   2440    623   -903       C  
ATOM   3673  O   ILE B 175     107.629  70.177  74.173  1.00105.18           O  
ANISOU 3673  O   ILE B 175    16660  13535   9768   2547    425  -1032       O  
ATOM   3674  CB  ILE B 175     109.388  67.315  74.070  1.00 86.32           C  
ANISOU 3674  CB  ILE B 175    13989  11152   7657   1953    425   -716       C  
ATOM   3675  CG1 ILE B 175     110.747  66.882  74.619  1.00 88.49           C  
ANISOU 3675  CG1 ILE B 175    14437  11268   7916   1831    187   -689       C  
ATOM   3676  CG2 ILE B 175     109.550  68.043  72.749  1.00 80.86           C  
ANISOU 3676  CG2 ILE B 175    13131  10378   7217   1850    283   -764       C  
ATOM   3677  CD1 ILE B 175     111.432  65.834  73.785  1.00 89.81           C  
ANISOU 3677  CD1 ILE B 175    14341  11435   8347   1554    159   -574       C  
ATOM   3678  N   ASP B 176     106.377  68.313  74.288  1.00111.02           N  
ANISOU 3678  N   ASP B 176    16988  14680  10514   2459    955   -821       N  
ATOM   3679  CA  ASP B 176     105.201  68.986  73.752  1.00117.91           C  
ANISOU 3679  CA  ASP B 176    17701  15696  11403   2637   1099   -890       C  
ATOM   3680  C   ASP B 176     104.636  70.019  74.717  1.00127.84           C  
ANISOU 3680  C   ASP B 176    19250  16975  12347   3015   1119  -1035       C  
ATOM   3681  O   ASP B 176     103.964  70.956  74.278  1.00131.40           O  
ANISOU 3681  O   ASP B 176    19677  17448  12802   3210   1110  -1146       O  
ATOM   3682  CB  ASP B 176     104.122  67.962  73.397  1.00114.75           C  
ANISOU 3682  CB  ASP B 176    16919  15586  11094   2552   1444   -762       C  
ATOM   3683  CG  ASP B 176     104.551  67.026  72.281  1.00105.92           C  
ANISOU 3683  CG  ASP B 176    15510  14441  10295   2210   1412   -644       C  
ATOM   3684  OD1 ASP B 176     105.479  67.385  71.525  1.00102.09           O  
ANISOU 3684  OD1 ASP B 176    15054  13753   9982   2076   1149   -679       O  
ATOM   3685  OD2 ASP B 176     103.955  65.936  72.157  1.00102.39           O  
ANISOU 3685  OD2 ASP B 176    14808  14176   9920   2075   1649   -517       O  
ATOM   3686  N   SER B 177     104.899  69.878  76.012  1.00130.54           N  
ANISOU 3686  N   SER B 177    19884  17306  12408   3141   1135  -1044       N  
ATOM   3687  CA  SER B 177     104.410  70.817  77.011  1.00133.85           C  
ANISOU 3687  CA  SER B 177    20618  17747  12492   3525   1152  -1193       C  
ATOM   3688  C   SER B 177     105.312  72.029  77.193  1.00123.76           C  
ANISOU 3688  C   SER B 177    19734  16138  11150   3628    753  -1363       C  
ATOM   3689  O   SER B 177     105.042  72.856  78.069  1.00135.83           O  
ANISOU 3689  O   SER B 177    21591  17634  12386   3959    710  -1509       O  
ATOM   3690  CB  SER B 177     104.253  70.117  78.362  1.00141.91           C  
ANISOU 3690  CB  SER B 177    21803  18915  13203   3631   1357  -1124       C  
ATOM   3691  OG  SER B 177     103.288  69.082  78.308  1.00149.26           O  
ANISOU 3691  OG  SER B 177    22391  20161  14158   3554   1747   -963       O  
ATOM   3692  N   GLY B 178     106.385  72.141  76.417  1.00109.04           N  
ANISOU 3692  N   GLY B 178    17853  14032   9545   3353    457  -1347       N  
ATOM   3693  CA  GLY B 178     107.370  73.179  76.655  1.00103.83           C  
ANISOU 3693  CA  GLY B 178    17564  13047   8840   3384     60  -1481       C  
ATOM   3694  C   GLY B 178     108.071  73.122  77.997  1.00107.84           C  
ANISOU 3694  C   GLY B 178    18450  13447   9077   3475    -81  -1528       C  
ATOM   3695  O   GLY B 178     108.781  74.069  78.345  1.00112.56           O  
ANISOU 3695  O   GLY B 178    19395  13777   9596   3542   -420  -1663       O  
ATOM   3696  N   PHE B 179     107.891  72.042  78.763  1.00105.34           N  
ANISOU 3696  N   PHE B 179    18092  13322   8610   3474    156  -1417       N  
ATOM   3697  CA  PHE B 179     108.487  71.897  80.087  1.00105.70           C  
ANISOU 3697  CA  PHE B 179    18505  13290   8365   3581     44  -1449       C  
ATOM   3698  C   PHE B 179     110.000  71.749  80.041  1.00109.55           C  
ANISOU 3698  C   PHE B 179    19098  13522   9003   3314   -326  -1432       C  
ATOM   3699  O   PHE B 179     110.629  71.748  81.103  1.00124.30           O  
ANISOU 3699  O   PHE B 179    21297  15286  10644   3399   -496  -1480       O  
ATOM   3700  CB  PHE B 179     107.867  70.683  80.793  1.00109.56           C  
ANISOU 3700  CB  PHE B 179    18887  14060   8680   3611    417  -1297       C  
ATOM   3701  CG  PHE B 179     108.127  70.616  82.277  1.00118.47           C  
ANISOU 3701  CG  PHE B 179    20293  15146   9573   3744    365  -1289       C  
ATOM   3702  CD1 PHE B 179     107.430  71.433  83.155  1.00125.16           C  
ANISOU 3702  CD1 PHE B 179    21288  16025  10243   4043    414  -1375       C  
ATOM   3703  CD2 PHE B 179     109.035  69.700  82.797  1.00111.69           C  
ANISOU 3703  CD2 PHE B 179    19548  14226   8662   3585    273  -1192       C  
ATOM   3704  CE1 PHE B 179     107.655  71.359  84.522  1.00124.26           C  
ANISOU 3704  CE1 PHE B 179    21437  15878   9898   4177    373  -1369       C  
ATOM   3705  CE2 PHE B 179     109.260  69.622  84.161  1.00112.65           C  
ANISOU 3705  CE2 PHE B 179    19930  14311   8562   3718    225  -1184       C  
ATOM   3706  CZ  PHE B 179     108.569  70.452  85.022  1.00121.04           C  
ANISOU 3706  CZ  PHE B 179    21143  15404   9443   4012    280  -1274       C  
ATOM   3707  N   TYR B 180     110.594  71.629  78.855  1.00103.69           N  
ANISOU 3707  N   TYR B 180    18081  12692   8624   3007   -456  -1368       N  
ATOM   3708  CA  TYR B 180     112.023  71.399  78.708  1.00 97.75           C  
ANISOU 3708  CA  TYR B 180    17349  11748   8045   2737   -776  -1334       C  
ATOM   3709  C   TYR B 180     112.690  72.599  78.051  1.00 91.44           C  
ANISOU 3709  C   TYR B 180    16636  10690   7417   2643  -1127  -1442       C  
ATOM   3710  O   TYR B 180     112.094  73.263  77.198  1.00 93.22           O  
ANISOU 3710  O   TYR B 180    16746  10911   7762   2669  -1078  -1476       O  
ATOM   3711  CB  TYR B 180     112.299  70.151  77.865  1.00 99.92           C  
ANISOU 3711  CB  TYR B 180    17219  12145   8600   2435   -636  -1152       C  
ATOM   3712  CG  TYR B 180     112.343  68.865  78.653  1.00106.06           C  
ANISOU 3712  CG  TYR B 180    18000  13054   9242   2423   -466  -1029       C  
ATOM   3713  CD1 TYR B 180     112.971  68.806  79.889  1.00106.15           C  
ANISOU 3713  CD1 TYR B 180    18359  12973   8999   2532   -634  -1070       C  
ATOM   3714  CD2 TYR B 180     111.764  67.704  78.156  1.00108.15           C  
ANISOU 3714  CD2 TYR B 180    17941  13521   9631   2297   -155   -870       C  
ATOM   3715  CE1 TYR B 180     113.016  67.628  80.613  1.00104.57           C  
ANISOU 3715  CE1 TYR B 180    18191  12880   8662   2525   -487   -946       C  
ATOM   3716  CE2 TYR B 180     111.807  66.521  78.871  1.00106.75           C  
ANISOU 3716  CE2 TYR B 180    17795  13436   9328   2272    -11   -745       C  
ATOM   3717  CZ  TYR B 180     112.432  66.490  80.098  1.00102.90           C  
ANISOU 3717  CZ  TYR B 180    17663  12855   8580   2390   -173   -778       C  
ATOM   3718  OH  TYR B 180     112.470  65.313  80.804  1.00 99.32           O  
ANISOU 3718  OH  TYR B 180    17265  12481   7990   2370    -35   -641       O  
ATOM   3719  N   THR B 181     113.922  72.875  78.465  1.00 91.45           N  
ANISOU 3719  N   THR B 181    16844  10475   7426   2530  -1491  -1491       N  
ATOM   3720  CA  THR B 181     114.814  73.756  77.732  1.00 71.38           C  
ANISOU 3720  CA  THR B 181    14309   7696   5117   2321  -1837  -1537       C  
ATOM   3721  C   THR B 181     115.413  73.004  76.553  1.00 88.28           C  
ANISOU 3721  C   THR B 181    16019   9911   7611   1976  -1801  -1381       C  
ATOM   3722  O   THR B 181     115.455  71.772  76.531  1.00 90.30           O  
ANISOU 3722  O   THR B 181    16049  10345   7916   1890  -1607  -1258       O  
ATOM   3723  CB  THR B 181     115.942  74.259  78.633  1.00 88.86           C  
ANISOU 3723  CB  THR B 181    16871   9672   7222   2304  -2247  -1639       C  
ATOM   3724  OG1 THR B 181     115.414  74.581  79.924  1.00 98.70           O  
ANISOU 3724  OG1 THR B 181    18519  10900   8083   2650  -2235  -1767       O  
ATOM   3725  CG2 THR B 181     116.608  75.490  78.042  1.00 85.32           C  
ANISOU 3725  CG2 THR B 181    16522   8948   6949   2147  -2608  -1716       C  
ATOM   3726  N   GLN B 182     115.882  73.761  75.560  1.00 84.98           N  
ANISOU 3726  N   GLN B 182    15505   9351   7432   1781  -1991  -1384       N  
ATOM   3727  CA  GLN B 182     116.589  73.132  74.452  1.00 92.47           C  
ANISOU 3727  CA  GLN B 182    16068  10366   8700   1459  -1987  -1246       C  
ATOM   3728  C   GLN B 182     117.829  72.400  74.949  1.00 93.87           C  
ANISOU 3728  C   GLN B 182    16215  10532   8919   1299  -2170  -1200       C  
ATOM   3729  O   GLN B 182     118.147  71.306  74.471  1.00 78.98           O  
ANISOU 3729  O   GLN B 182    14022   8800   7188   1149  -2040  -1079       O  
ATOM   3730  CB  GLN B 182     116.958  74.172  73.394  1.00 98.97           C  
ANISOU 3730  CB  GLN B 182    16839  11027   9739   1276  -2182  -1252       C  
ATOM   3731  CG  GLN B 182     117.324  73.555  72.053  1.00100.31           C  
ANISOU 3731  CG  GLN B 182    16579  11323  10211   1000  -2076  -1107       C  
ATOM   3732  CD  GLN B 182     118.536  74.194  71.410  1.00102.40           C  
ANISOU 3732  CD  GLN B 182    16786  11428  10693    705  -2380  -1073       C  
ATOM   3733  OE1 GLN B 182     119.454  74.641  72.098  1.00114.40           O  
ANISOU 3733  OE1 GLN B 182    18506  12783  12178    636  -2689  -1129       O  
ATOM   3734  NE2 GLN B 182     118.558  74.219  70.083  1.00 92.42           N  
ANISOU 3734  NE2 GLN B 182    15238  10224   9651    521  -2295   -976       N  
ATOM   3735  N   GLU B 183     118.528  72.979  75.931  1.00105.15           N  
ANISOU 3735  N   GLU B 183    17971  11776  10204   1349  -2486  -1304       N  
ATOM   3736  CA  GLU B 183     119.699  72.316  76.497  1.00110.88           C  
ANISOU 3736  CA  GLU B 183    18685  12493  10950   1228  -2688  -1274       C  
ATOM   3737  C   GLU B 183     119.309  71.083  77.303  1.00 97.58           C  
ANISOU 3737  C   GLU B 183    17019  10984   9075   1391  -2455  -1221       C  
ATOM   3738  O   GLU B 183     120.062  70.102  77.337  1.00 89.16           O  
ANISOU 3738  O   GLU B 183    15784   9994   8098   1270  -2487  -1136       O  
ATOM   3739  CB  GLU B 183     120.491  73.296  77.365  1.00127.91           C  
ANISOU 3739  CB  GLU B 183    21207  14401  12993   1246  -3109  -1410       C  
ATOM   3740  CG  GLU B 183     121.303  74.325  76.579  1.00140.21           C  
ANISOU 3740  CG  GLU B 183    22705  15770  14797    977  -3415  -1423       C  
ATOM   3741  CD  GLU B 183     120.445  75.368  75.872  1.00142.97           C  
ANISOU 3741  CD  GLU B 183    23128  16020  15174   1027  -3341  -1462       C  
ATOM   3742  OE1 GLU B 183     119.250  75.503  76.215  1.00142.06           O  
ANISOU 3742  OE1 GLU B 183    23185  15949  14844   1319  -3118  -1526       O  
ATOM   3743  OE2 GLU B 183     120.968  76.046  74.962  1.00140.38           O  
ANISOU 3743  OE2 GLU B 183    22681  15578  15080    777  -3504  -1423       O  
ATOM   3744  N   GLU B 184     118.143  71.114  77.952  1.00 93.95           N  
ANISOU 3744  N   GLU B 184    16760  10590   8345   1668  -2218  -1264       N  
ATOM   3745  CA  GLU B 184     117.670  69.940  78.678  1.00 85.49           C  
ANISOU 3745  CA  GLU B 184    15703   9693   7086   1803  -1960  -1187       C  
ATOM   3746  C   GLU B 184     117.321  68.811  77.717  1.00 84.65           C  
ANISOU 3746  C   GLU B 184    15184   9784   7196   1651  -1657  -1027       C  
ATOM   3747  O   GLU B 184     117.611  67.641  77.992  1.00 84.79           O  
ANISOU 3747  O   GLU B 184    15118   9891   7206   1606  -1578   -926       O  
ATOM   3748  CB  GLU B 184     116.470  70.318  79.551  1.00 89.38           C  
ANISOU 3748  CB  GLU B 184    16485  10236   7238   2130  -1757  -1264       C  
ATOM   3749  CG  GLU B 184     116.818  71.309  80.666  1.00103.48           C  
ANISOU 3749  CG  GLU B 184    18738  11824   8756   2325  -2062  -1435       C  
ATOM   3750  CD  GLU B 184     115.610  71.787  81.459  1.00109.36           C  
ANISOU 3750  CD  GLU B 184    19767  12632   9152   2682  -1856  -1530       C  
ATOM   3751  OE1 GLU B 184     114.479  71.712  80.936  1.00106.67           O  
ANISOU 3751  OE1 GLU B 184    19237  12461   8832   2762  -1518  -1487       O  
ATOM   3752  OE2 GLU B 184     115.799  72.253  82.604  1.00112.59           O  
ANISOU 3752  OE2 GLU B 184    20492  12927   9358   2863  -2010  -1614       O  
ATOM   3753  N   ILE B 185     116.716  69.143  76.574  1.00 80.09           N  
ANISOU 3753  N   ILE B 185    14362   9261   6808   1575  -1507  -1005       N  
ATOM   3754  CA  ILE B 185     116.456  68.131  75.554  1.00 72.49           C  
ANISOU 3754  CA  ILE B 185    13010   8465   6070   1415  -1264   -869       C  
ATOM   3755  C   ILE B 185     117.768  67.564  75.030  1.00 74.44           C  
ANISOU 3755  C   ILE B 185    13052   8681   6552   1172  -1461   -805       C  
ATOM   3756  O   ILE B 185     117.892  66.354  74.801  1.00 76.59           O  
ANISOU 3756  O   ILE B 185    13127   9067   6908   1092  -1327   -699       O  
ATOM   3757  CB  ILE B 185     115.598  68.719  74.417  1.00 73.20           C  
ANISOU 3757  CB  ILE B 185    12902   8605   6307   1394  -1108   -875       C  
ATOM   3758  CG1 ILE B 185     114.209  69.097  74.927  1.00 76.51           C  
ANISOU 3758  CG1 ILE B 185    13467   9109   6496   1661   -869   -930       C  
ATOM   3759  CG2 ILE B 185     115.452  67.723  73.275  1.00 68.25           C  
ANISOU 3759  CG2 ILE B 185    11879   8129   5925   1212   -909   -749       C  
ATOM   3760  CD1 ILE B 185     113.281  69.575  73.835  1.00 72.67           C  
ANISOU 3760  CD1 ILE B 185    12771   8694   6145   1667   -708   -935       C  
ATOM   3761  N   GLU B 186     118.775  68.422  74.846  1.00 69.77           N  
ANISOU 3761  N   GLU B 186    12505   7935   6067   1052  -1787   -869       N  
ATOM   3762  CA  GLU B 186     120.035  67.955  74.278  1.00 65.65           C  
ANISOU 3762  CA  GLU B 186    11744   7418   5781    821  -1967   -810       C  
ATOM   3763  C   GLU B 186     120.774  67.019  75.224  1.00 71.72           C  
ANISOU 3763  C   GLU B 186    12602   8201   6448    861  -2075   -786       C  
ATOM   3764  O   GLU B 186     121.468  66.103  74.764  1.00 69.13           O  
ANISOU 3764  O   GLU B 186    12026   7956   6286    736  -2084   -707       O  
ATOM   3765  CB  GLU B 186     120.912  69.145  73.895  1.00 65.68           C  
ANISOU 3765  CB  GLU B 186    11767   7265   5923    663  -2287   -871       C  
ATOM   3766  CG  GLU B 186     120.354  69.928  72.717  1.00 76.93           C  
ANISOU 3766  CG  GLU B 186    13053   8680   7499    578  -2190   -860       C  
ATOM   3767  CD  GLU B 186     121.225  71.094  72.312  1.00 93.51           C  
ANISOU 3767  CD  GLU B 186    15182  10610   9737    389  -2503   -895       C  
ATOM   3768  OE1 GLU B 186     122.263  71.327  72.965  1.00102.99           O  
ANISOU 3768  OE1 GLU B 186    16499  11704  10928    316  -2807   -937       O  
ATOM   3769  OE2 GLU B 186     120.875  71.768  71.325  1.00 99.14           O  
ANISOU 3769  OE2 GLU B 186    15799  11295  10573    303  -2451   -874       O  
ATOM   3770  N   VAL B 187     120.635  67.223  76.537  1.00 78.00           N  
ANISOU 3770  N   VAL B 187    13760   8917   6959   1054  -2161   -857       N  
ATOM   3771  CA  VAL B 187     121.248  66.312  77.500  1.00 80.23           C  
ANISOU 3771  CA  VAL B 187    14167   9208   7108   1121  -2258   -830       C  
ATOM   3772  C   VAL B 187     120.585  64.941  77.427  1.00 71.73           C  
ANISOU 3772  C   VAL B 187    12965   8288   6002   1163  -1927   -701       C  
ATOM   3773  O   VAL B 187     121.260  63.903  77.465  1.00 62.61           O  
ANISOU 3773  O   VAL B 187    11705   7171   4913   1110  -1975   -628       O  
ATOM   3774  CB  VAL B 187     121.167  66.917  78.914  1.00 88.79           C  
ANISOU 3774  CB  VAL B 187    15703  10171   7861   1335  -2419   -940       C  
ATOM   3775  CG1 VAL B 187     121.646  65.925  79.965  1.00 68.46           C  
ANISOU 3775  CG1 VAL B 187    13295   7612   5104   1436  -2489   -900       C  
ATOM   3776  CG2 VAL B 187     121.972  68.207  78.981  1.00 95.19           C  
ANISOU 3776  CG2 VAL B 187    16645  10795   8727   1260  -2805  -1069       C  
ATOM   3777  N   ILE B 188     119.254  64.920  77.308  1.00 71.13           N  
ANISOU 3777  N   ILE B 188    12894   8298   5833   1259  -1599   -672       N  
ATOM   3778  CA  ILE B 188     118.526  63.665  77.135  1.00 68.98           C  
ANISOU 3778  CA  ILE B 188    12480   8169   5561   1259  -1276   -540       C  
ATOM   3779  C   ILE B 188     118.967  62.975  75.849  1.00 66.99           C  
ANISOU 3779  C   ILE B 188    11844   7978   5630   1051  -1247   -464       C  
ATOM   3780  O   ILE B 188     119.258  61.773  75.833  1.00 58.47           O  
ANISOU 3780  O   ILE B 188    10678   6942   4597   1010  -1198   -372       O  
ATOM   3781  CB  ILE B 188     117.008  63.924  77.133  1.00 61.45           C  
ANISOU 3781  CB  ILE B 188    11549   7317   4481   1378   -942   -531       C  
ATOM   3782  CG1 ILE B 188     116.553  64.532  78.460  1.00 67.19           C  
ANISOU 3782  CG1 ILE B 188    12667   8008   4853   1622   -945   -607       C  
ATOM   3783  CG2 ILE B 188     116.247  62.640  76.871  1.00 60.51           C  
ANISOU 3783  CG2 ILE B 188    11255   7342   4396   1331   -620   -385       C  
ATOM   3784  CD1 ILE B 188     115.109  65.005  78.460  1.00 64.71           C  
ANISOU 3784  CD1 ILE B 188    12366   7811   4411   1771   -642   -626       C  
ATOM   3785  N   ALA B 189     119.023  63.734  74.750  1.00 66.96           N  
ANISOU 3785  N   ALA B 189    11627   7975   5841    930  -1283   -504       N  
ATOM   3786  CA  ALA B 189     119.368  63.151  73.457  1.00 66.64           C  
ANISOU 3786  CA  ALA B 189    11225   8011   6086    751  -1235   -439       C  
ATOM   3787  C   ALA B 189     120.762  62.538  73.484  1.00 70.54           C  
ANISOU 3787  C   ALA B 189    11632   8482   6687    668  -1473   -421       C  
ATOM   3788  O   ALA B 189     120.950  61.372  73.114  1.00 64.37           O  
ANISOU 3788  O   ALA B 189    10688   7770   6000    628  -1389   -343       O  
ATOM   3789  CB  ALA B 189     119.261  64.211  72.361  1.00 63.04           C  
ANISOU 3789  CB  ALA B 189    10603   7547   5804    646  -1259   -483       C  
ATOM   3790  N   ARG B 190     121.752  63.311  73.934  1.00 76.94           N  
ANISOU 3790  N   ARG B 190    12554   9196   7485    648  -1785   -497       N  
ATOM   3791  CA  ARG B 190     123.124  62.821  73.989  1.00 73.43           C  
ANISOU 3791  CA  ARG B 190    12002   8750   7147    578  -2036   -490       C  
ATOM   3792  C   ARG B 190     123.264  61.598  74.885  1.00 75.75           C  
ANISOU 3792  C   ARG B 190    12441   9051   7292    705  -2024   -439       C  
ATOM   3793  O   ARG B 190     124.187  60.800  74.691  1.00 80.41           O  
ANISOU 3793  O   ARG B 190    12876   9680   7997    670  -2143   -408       O  
ATOM   3794  CB  ARG B 190     124.055  63.944  74.459  1.00 65.63           C  
ANISOU 3794  CB  ARG B 190    11136   7649   6151    531  -2388   -585       C  
ATOM   3795  CG  ARG B 190     125.483  63.811  73.961  1.00 86.16           C  
ANISOU 3795  CG  ARG B 190    13468  10293   8974    376  -2637   -579       C  
ATOM   3796  CD  ARG B 190     126.359  64.953  74.443  1.00106.66           C  
ANISOU 3796  CD  ARG B 190    16181  12771  11574    297  -2997   -667       C  
ATOM   3797  NE  ARG B 190     125.697  66.250  74.329  1.00119.42           N  
ANISOU 3797  NE  ARG B 190    17956  14271  13147    267  -2989   -724       N  
ATOM   3798  CZ  ARG B 190     126.336  67.416  74.319  1.00130.58           C  
ANISOU 3798  CZ  ARG B 190    19415  15566  14632    130  -3271   -785       C  
ATOM   3799  NH1 ARG B 190     127.659  67.451  74.417  1.00135.08           N  
ANISOU 3799  NH1 ARG B 190    19849  16143  15331     -6  -3575   -794       N  
ATOM   3800  NH2 ARG B 190     125.654  68.549  74.212  1.00131.51           N  
ANISOU 3800  NH2 ARG B 190    19714  15557  14697    129  -3258   -837       N  
ATOM   3801  N   SER B 191     122.361  61.426  75.847  1.00 75.64           N  
ANISOU 3801  N   SER B 191    12719   9004   7016    861  -1876   -425       N  
ATOM   3802  CA  SER B 191     122.379  60.255  76.712  1.00 80.75           C  
ANISOU 3802  CA  SER B 191    13539   9646   7496    976  -1838   -352       C  
ATOM   3803  C   SER B 191     121.699  59.046  76.089  1.00 86.74           C  
ANISOU 3803  C   SER B 191    14131  10488   8339    937  -1546   -234       C  
ATOM   3804  O   SER B 191     121.693  57.978  76.710  1.00 91.00           O  
ANISOU 3804  O   SER B 191    14811  11007   8758   1011  -1504   -153       O  
ATOM   3805  CB  SER B 191     121.698  60.572  78.043  1.00 90.85           C  
ANISOU 3805  CB  SER B 191    15217  10869   8435   1156  -1788   -372       C  
ATOM   3806  OG  SER B 191     120.292  60.541  77.886  1.00 97.33           O  
ANISOU 3806  OG  SER B 191    16041  11763   9176   1190  -1433   -320       O  
ATOM   3807  N   MET B 192     121.116  59.191  74.896  1.00 89.15           N  
ANISOU 3807  N   MET B 192    14164  10870   8838    822  -1357   -219       N  
ATOM   3808  CA  MET B 192     120.427  58.099  74.218  1.00 78.33           C  
ANISOU 3808  CA  MET B 192    12629   9570   7564    769  -1098   -120       C  
ATOM   3809  C   MET B 192     121.005  57.822  72.837  1.00 71.93           C  
ANISOU 3809  C   MET B 192    11465   8818   7045    636  -1135   -124       C  
ATOM   3810  O   MET B 192     120.335  57.203  72.004  1.00 74.92           O  
ANISOU 3810  O   MET B 192    11673   9257   7537    572   -925    -71       O  
ATOM   3811  CB  MET B 192     118.929  58.389  74.117  1.00 76.58           C  
ANISOU 3811  CB  MET B 192    12422   9408   7265    780   -789    -91       C  
ATOM   3812  CG  MET B 192     118.301  58.753  75.448  1.00 98.64           C  
ANISOU 3812  CG  MET B 192    15552  12176   9750    932   -722    -92       C  
ATOM   3813  SD  MET B 192     116.573  59.213  75.290  1.00110.36           S  
ANISOU 3813  SD  MET B 192    17002  13775  11154    968   -363    -73       S  
ATOM   3814  CE  MET B 192     115.859  57.654  74.807  1.00112.81           C  
ANISOU 3814  CE  MET B 192    17142  14157  11564    854    -92     84       C  
ATOM   3815  N   LEU B 193     122.244  58.256  72.587  1.00 65.44           N  
ANISOU 3815  N   LEU B 193    10531   7992   6342    593  -1400   -187       N  
ATOM   3816  CA  LEU B 193     122.882  58.011  71.296  1.00 53.33           C  
ANISOU 3816  CA  LEU B 193     8655   6542   5065    482  -1431   -190       C  
ATOM   3817  C   LEU B 193     123.040  56.520  71.024  1.00 63.07           C  
ANISOU 3817  C   LEU B 193     9812   7796   6356    516  -1368   -126       C  
ATOM   3818  O   LEU B 193     122.859  56.068  69.887  1.00 75.54           O  
ANISOU 3818  O   LEU B 193    11155   9447   8100    449  -1244   -109       O  
ATOM   3819  CB  LEU B 193     124.240  58.712  71.250  1.00 53.79           C  
ANISOU 3819  CB  LEU B 193     8609   6609   5220    430  -1731   -255       C  
ATOM   3820  CG  LEU B 193     124.148  60.242  71.282  1.00 59.87           C  
ANISOU 3820  CG  LEU B 193     9433   7336   5978    358  -1817   -318       C  
ATOM   3821  CD1 LEU B 193     125.517  60.903  71.439  1.00 54.93           C  
ANISOU 3821  CD1 LEU B 193     8738   6699   5434    284  -2146   -373       C  
ATOM   3822  CD2 LEU B 193     123.452  60.733  70.027  1.00 57.92           C  
ANISOU 3822  CD2 LEU B 193     8980   7155   5873    249  -1623   -305       C  
ATOM   3823  N   ASP B 194     123.375  55.737  72.054  1.00 67.40           N  
ANISOU 3823  N   ASP B 194    10581   8269   6759    630  -1464    -94       N  
ATOM   3824  CA  ASP B 194     123.518  54.296  71.880  1.00 75.26           C  
ANISOU 3824  CA  ASP B 194    11557   9245   7791    677  -1428    -32       C  
ATOM   3825  C   ASP B 194     122.211  53.606  71.525  1.00 76.01           C  
ANISOU 3825  C   ASP B 194    11673   9329   7879    632  -1131     49       C  
ATOM   3826  O   ASP B 194     122.244  52.462  71.061  1.00 92.38           O  
ANISOU 3826  O   ASP B 194    13688  11381  10033    636  -1089     92       O  
ATOM   3827  CB  ASP B 194     124.100  53.667  73.145  1.00 84.17           C  
ANISOU 3827  CB  ASP B 194    12967  10275   8740    817  -1606     -6       C  
ATOM   3828  CG  ASP B 194     125.464  54.217  73.489  1.00 94.51           C  
ANISOU 3828  CG  ASP B 194    14231  11602  10075    862  -1933    -90       C  
ATOM   3829  OD1 ASP B 194     125.552  55.085  74.382  1.00100.57           O  
ANISOU 3829  OD1 ASP B 194    15190  12326  10696    891  -2055   -131       O  
ATOM   3830  OD2 ASP B 194     126.450  53.772  72.865  1.00 98.40           O  
ANISOU 3830  OD2 ASP B 194    14494  12161  10733    874  -2073   -120       O  
ATOM   3831  N   ASP B 195     121.071  54.266  71.725  1.00 81.91           N  
ANISOU 3831  N   ASP B 195    12497  10091   8534    593   -936     66       N  
ATOM   3832  CA  ASP B 195     119.775  53.675  71.437  1.00 80.63           C  
ANISOU 3832  CA  ASP B 195    12328   9939   8368    535   -654    147       C  
ATOM   3833  C   ASP B 195     119.003  54.383  70.331  1.00 69.96           C  
ANISOU 3833  C   ASP B 195    10734   8688   7159    434   -494    109       C  
ATOM   3834  O   ASP B 195     118.001  53.834  69.859  1.00 59.90           O  
ANISOU 3834  O   ASP B 195     9387   7441   5933    368   -283    165       O  
ATOM   3835  CB  ASP B 195     118.914  53.643  72.714  1.00 84.47           C  
ANISOU 3835  CB  ASP B 195    13116  10384   8597    596   -519    222       C  
ATOM   3836  CG  ASP B 195     119.483  52.717  73.782  1.00 88.01           C  
ANISOU 3836  CG  ASP B 195    13837  10720   8883    691   -641    291       C  
ATOM   3837  OD1 ASP B 195     119.753  51.538  73.468  1.00 85.88           O  
ANISOU 3837  OD1 ASP B 195    13545  10389   8697    675   -664    348       O  
ATOM   3838  OD2 ASP B 195     119.668  53.169  74.934  1.00 90.97           O  
ANISOU 3838  OD2 ASP B 195    14467  11057   9039    796   -727    284       O  
ATOM   3839  N   VAL B 196     119.454  55.555  69.877  1.00 66.45           N  
ANISOU 3839  N   VAL B 196    10165   8292   6789    412   -601     22       N  
ATOM   3840  CA  VAL B 196     118.617  56.387  69.018  1.00 64.95           C  
ANISOU 3840  CA  VAL B 196     9812   8180   6684    342   -454     -9       C  
ATOM   3841  C   VAL B 196     118.350  55.722  67.666  1.00 64.41           C  
ANISOU 3841  C   VAL B 196     9485   8176   6814    253   -346      6       C  
ATOM   3842  O   VAL B 196     117.327  56.000  67.029  1.00 63.94           O  
ANISOU 3842  O   VAL B 196     9315   8176   6803    203   -173      8       O  
ATOM   3843  CB  VAL B 196     119.243  57.790  68.871  1.00 61.08           C  
ANISOU 3843  CB  VAL B 196     9288   7697   6223    330   -621    -95       C  
ATOM   3844  CG1 VAL B 196     120.451  57.765  67.943  1.00 57.06           C  
ANISOU 3844  CG1 VAL B 196     8546   7229   5904    257   -789   -125       C  
ATOM   3845  CG2 VAL B 196     118.199  58.800  68.404  1.00 63.51           C  
ANISOU 3845  CG2 VAL B 196     9548   8048   6536    308   -475   -123       C  
ATOM   3846  N   ALA B 197     119.226  54.820  67.215  1.00 65.10           N  
ANISOU 3846  N   ALA B 197     9477   8253   7007    250   -452      9       N  
ATOM   3847  CA  ALA B 197     118.950  54.113  65.965  1.00 59.33           C  
ANISOU 3847  CA  ALA B 197     8535   7571   6438    188   -357     12       C  
ATOM   3848  C   ALA B 197     117.849  53.074  66.148  1.00 60.14           C  
ANISOU 3848  C   ALA B 197     8722   7622   6505    160   -177     88       C  
ATOM   3849  O   ALA B 197     116.934  52.982  65.320  1.00 72.61           O  
ANISOU 3849  O   ALA B 197    10164   9252   8172     86    -27     92       O  
ATOM   3850  CB  ALA B 197     120.221  53.458  65.425  1.00 58.19           C  
ANISOU 3850  CB  ALA B 197     8269   7439   6403    223   -524    -20       C  
ATOM   3851  N   GLU B 198     117.921  52.281  67.223  1.00 57.77           N  
ANISOU 3851  N   GLU B 198     8653   7222   6077    210   -199    156       N  
ATOM   3852  CA  GLU B 198     116.861  51.316  67.506  1.00 65.66           C  
ANISOU 3852  CA  GLU B 198     9752   8164   7032    154    -23    255       C  
ATOM   3853  C   GLU B 198     115.525  52.014  67.730  1.00 69.82           C  
ANISOU 3853  C   GLU B 198    10268   8770   7489    102    195    285       C  
ATOM   3854  O   GLU B 198     114.475  51.520  67.299  1.00 71.40           O  
ANISOU 3854  O   GLU B 198    10382   8997   7751      5    367    334       O  
ATOM   3855  CB  GLU B 198     117.225  50.470  68.728  1.00 78.50           C  
ANISOU 3855  CB  GLU B 198    11664   9662   8501    220    -92    338       C  
ATOM   3856  CG  GLU B 198     118.136  49.288  68.443  1.00103.64           C  
ANISOU 3856  CG  GLU B 198    14875  12742  11762    266   -254    339       C  
ATOM   3857  CD  GLU B 198     118.113  48.246  69.554  1.00128.14           C  
ANISOU 3857  CD  GLU B 198    18285  15690  14710    304   -272    454       C  
ATOM   3858  OE1 GLU B 198     117.029  48.003  70.130  1.00135.49           O  
ANISOU 3858  OE1 GLU B 198    19347  16596  15538    221    -80    566       O  
ATOM   3859  OE2 GLU B 198     119.185  47.679  69.861  1.00135.91           O  
ANISOU 3859  OE2 GLU B 198    19380  16588  15672    419   -478    440       O  
ATOM   3860  N   LEU B 199     115.543  53.170  68.398  1.00 67.65           N  
ANISOU 3860  N   LEU B 199    10077   8539   7088    173    180    248       N  
ATOM   3861  CA  LEU B 199     114.298  53.868  68.697  1.00 66.81           C  
ANISOU 3861  CA  LEU B 199     9974   8520   6892    170    383    264       C  
ATOM   3862  C   LEU B 199     113.634  54.423  67.446  1.00 66.27           C  
ANISOU 3862  C   LEU B 199     9638   8554   6986    105    471    207       C  
ATOM   3863  O   LEU B 199     112.406  54.563  67.417  1.00 73.20           O  
ANISOU 3863  O   LEU B 199    10450   9518   7845     76    670    237       O  
ATOM   3864  CB  LEU B 199     114.543  55.001  69.690  1.00 63.68           C  
ANISOU 3864  CB  LEU B 199     9762   8125   6309    292    316    217       C  
ATOM   3865  CG  LEU B 199     114.785  54.579  71.129  1.00 69.82           C  
ANISOU 3865  CG  LEU B 199    10844   8826   6859    377    289    284       C  
ATOM   3866  CD1 LEU B 199     115.420  55.723  71.890  1.00 69.43           C  
ANISOU 3866  CD1 LEU B 199    10966   8751   6664    501    122    197       C  
ATOM   3867  CD2 LEU B 199     113.471  54.150  71.767  1.00 76.22           C  
ANISOU 3867  CD2 LEU B 199    11736   9695   7530    360    563    395       C  
ATOM   3868  N   SER B 200     114.416  54.750  66.413  1.00 54.97           N  
ANISOU 3868  N   SER B 200     8046   7132   5709     86    330    129       N  
ATOM   3869  CA  SER B 200     113.843  55.365  65.219  1.00 57.35           C  
ANISOU 3869  CA  SER B 200     8121   7526   6143     38    395     75       C  
ATOM   3870  C   SER B 200     112.746  54.503  64.601  1.00 56.43           C  
ANISOU 3870  C   SER B 200     7868   7453   6119    -54    564    121       C  
ATOM   3871  O   SER B 200     111.825  55.033  63.973  1.00 58.34           O  
ANISOU 3871  O   SER B 200     7961   7789   6415    -75    672     95       O  
ATOM   3872  CB  SER B 200     114.942  55.645  64.198  1.00 57.10           C  
ANISOU 3872  CB  SER B 200     7946   7500   6249     20    226      9       C  
ATOM   3873  OG  SER B 200     115.948  56.479  64.746  1.00 57.05           O  
ANISOU 3873  OG  SER B 200     8040   7458   6177     74     58    -29       O  
ATOM   3874  N   SER B 201     112.808  53.188  64.790  1.00 52.37           N  
ANISOU 3874  N   SER B 201     7412   6861   5623   -109    574    190       N  
ATOM   3875  CA  SER B 201     111.798  52.275  64.275  1.00 59.13           C  
ANISOU 3875  CA  SER B 201     8162   7730   6573   -224    709    241       C  
ATOM   3876  C   SER B 201     110.762  51.876  65.319  1.00 65.42           C  
ANISOU 3876  C   SER B 201     9069   8539   7249   -270    895    355       C  
ATOM   3877  O   SER B 201     109.838  51.118  65.005  1.00 70.71           O  
ANISOU 3877  O   SER B 201     9647   9224   7998   -395   1015    416       O  
ATOM   3878  CB  SER B 201     112.474  51.025  63.714  1.00 67.04           C  
ANISOU 3878  CB  SER B 201     9168   8620   7683   -267    593    246       C  
ATOM   3879  OG  SER B 201     113.217  51.351  62.554  1.00 82.97           O  
ANISOU 3879  OG  SER B 201    11029  10674   9820   -234    469    144       O  
ATOM   3880  N   ASP B 202     110.888  52.361  66.545  1.00 64.00           N  
ANISOU 3880  N   ASP B 202     9083   8359   6877   -178    921    388       N  
ATOM   3881  CA  ASP B 202     109.962  51.989  67.599  1.00 67.30           C  
ANISOU 3881  CA  ASP B 202     9617   8807   7148   -210   1116    508       C  
ATOM   3882  C   ASP B 202     108.661  52.772  67.449  1.00 67.26           C  
ANISOU 3882  C   ASP B 202     9438   8984   7135   -208   1317    495       C  
ATOM   3883  O   ASP B 202     108.661  53.933  67.030  1.00 67.41           O  
ANISOU 3883  O   ASP B 202     9364   9079   7168   -111   1280    386       O  
ATOM   3884  CB  ASP B 202     110.601  52.247  68.962  1.00 68.94           C  
ANISOU 3884  CB  ASP B 202    10114   8956   7124    -84   1062    538       C  
ATOM   3885  CG  ASP B 202     109.799  51.677  70.093  1.00 75.67           C  
ANISOU 3885  CG  ASP B 202    11124   9828   7798   -118   1261    686       C  
ATOM   3886  OD1 ASP B 202     109.597  50.444  70.104  1.00 76.55           O  
ANISOU 3886  OD1 ASP B 202    11272   9855   7957   -254   1305    802       O  
ATOM   3887  OD2 ASP B 202     109.366  52.461  70.962  1.00 78.35           O  
ANISOU 3887  OD2 ASP B 202    11561  10265   7944     -7   1373    688       O  
ATOM   3888  N   TYR B 203     107.540  52.122  67.789  1.00 67.62           N  
ANISOU 3888  N   TYR B 203     9433   9099   7159   -318   1528    611       N  
ATOM   3889  CA  TYR B 203     106.240  52.767  67.603  1.00 68.21           C  
ANISOU 3889  CA  TYR B 203     9298   9377   7243   -314   1727    600       C  
ATOM   3890  C   TYR B 203     106.114  54.028  68.449  1.00 66.27           C  
ANISOU 3890  C   TYR B 203     9159   9232   6788   -108   1787    545       C  
ATOM   3891  O   TYR B 203     105.442  54.985  68.040  1.00 62.34           O  
ANISOU 3891  O   TYR B 203     8500   8875   6312    -21   1851    461       O  
ATOM   3892  CB  TYR B 203     105.100  51.785  67.900  1.00 75.00           C  
ANISOU 3892  CB  TYR B 203    10071  10308   8117   -491   1947    753       C  
ATOM   3893  CG  TYR B 203     104.789  51.551  69.361  1.00 95.58           C  
ANISOU 3893  CG  TYR B 203    12883  12953  10481   -468   2123    892       C  
ATOM   3894  CD1 TYR B 203     103.663  52.111  69.951  1.00103.37           C  
ANISOU 3894  CD1 TYR B 203    13772  14165  11337   -410   2374    931       C  
ATOM   3895  CD2 TYR B 203     105.609  50.748  70.144  1.00109.67           C  
ANISOU 3895  CD2 TYR B 203    14959  14556  12152   -491   2042    987       C  
ATOM   3896  CE1 TYR B 203     103.370  51.885  71.293  1.00120.20           C  
ANISOU 3896  CE1 TYR B 203    16099  16352  13221   -381   2556   1067       C  
ATOM   3897  CE2 TYR B 203     105.327  50.518  71.485  1.00117.63           C  
ANISOU 3897  CE2 TYR B 203    16182  15598  12915   -467   2205   1125       C  
ATOM   3898  CZ  TYR B 203     104.208  51.087  72.056  1.00118.11           C  
ANISOU 3898  CZ  TYR B 203    16145  15894  12837   -416   2471   1169       C  
ATOM   3899  OH  TYR B 203     103.927  50.859  73.388  1.00108.39           O  
ANISOU 3899  OH  TYR B 203    15131  14716  11337   -382   2651   1313       O  
ATOM   3900  N   LEU B 204     106.765  54.055  69.613  1.00 67.32           N  
ANISOU 3900  N   LEU B 204     9581   9286   6711    -12   1749    582       N  
ATOM   3901  CA  LEU B 204     106.904  55.263  70.417  1.00 65.78           C  
ANISOU 3901  CA  LEU B 204     9550   9137   6306    204   1738    503       C  
ATOM   3902  C   LEU B 204     108.221  55.991  70.188  1.00 74.15           C  
ANISOU 3902  C   LEU B 204    10730  10057   7387    298   1455    377       C  
ATOM   3903  O   LEU B 204     108.234  57.223  70.128  1.00 75.34           O  
ANISOU 3903  O   LEU B 204    10893  10242   7491    437   1397    263       O  
ATOM   3904  CB  LEU B 204     106.770  54.935  71.904  1.00 65.98           C  
ANISOU 3904  CB  LEU B 204     9838   9173   6057    268   1866    614       C  
ATOM   3905  CG  LEU B 204     105.350  54.961  72.461  1.00 84.40           C  
ANISOU 3905  CG  LEU B 204    12078  11726   8262    283   2187    701       C  
ATOM   3906  CD1 LEU B 204     105.323  54.433  73.885  1.00 87.41           C  
ANISOU 3906  CD1 LEU B 204    12738  12106   8366    316   2315    840       C  
ATOM   3907  CD2 LEU B 204     104.798  56.376  72.402  1.00 89.12           C  
ANISOU 3907  CD2 LEU B 204    12599  12474   8789    492   2236    561       C  
ATOM   3908  N   GLY B 205     109.332  55.261  70.072  1.00 71.10           N  
ANISOU 3908  N   GLY B 205    10432   9513   7069    227   1270    398       N  
ATOM   3909  CA  GLY B 205     110.622  55.915  69.926  1.00 69.67           C  
ANISOU 3909  CA  GLY B 205    10341   9223   6908    301   1004    292       C  
ATOM   3910  C   GLY B 205     110.675  56.829  68.717  1.00 68.06           C  
ANISOU 3910  C   GLY B 205     9927   9058   6876    297    923    178       C  
ATOM   3911  O   GLY B 205     111.262  57.913  68.772  1.00 67.38           O  
ANISOU 3911  O   GLY B 205     9917   8935   6751    389    774     84       O  
ATOM   3912  N   ASN B 206     110.041  56.413  67.615  1.00 68.83           N  
ANISOU 3912  N   ASN B 206     9772   9222   7159    186   1013    189       N  
ATOM   3913  CA  ASN B 206     110.074  57.199  66.386  1.00 60.23           C  
ANISOU 3913  CA  ASN B 206     8489   8168   6226    179    938     94       C  
ATOM   3914  C   ASN B 206     109.495  58.593  66.597  1.00 59.59           C  
ANISOU 3914  C   ASN B 206     8439   8158   6046    318    976     18       C  
ATOM   3915  O   ASN B 206     109.986  59.566  66.016  1.00 58.10           O  
ANISOU 3915  O   ASN B 206     8234   7933   5910    354    833    -66       O  
ATOM   3916  CB  ASN B 206     109.333  56.449  65.277  1.00 55.45           C  
ANISOU 3916  CB  ASN B 206     7632   7631   5806     50   1037    121       C  
ATOM   3917  CG  ASN B 206     107.852  56.783  65.227  1.00 63.73           C  
ANISOU 3917  CG  ASN B 206     8541   8835   6840     71   1245    128       C  
ATOM   3918  OD1 ASN B 206     107.442  57.751  64.583  1.00 70.96           O  
ANISOU 3918  OD1 ASN B 206     9341   9823   7797    138   1239     48       O  
ATOM   3919  ND2 ASN B 206     107.039  55.963  65.880  1.00 70.14           N  
ANISOU 3919  ND2 ASN B 206     9351   9704   7594      9   1427    231       N  
ATOM   3920  N   THR B 207     108.461  58.718  67.435  1.00 62.79           N  
ANISOU 3920  N   THR B 207     8896   8663   6297    403   1169     50       N  
ATOM   3921  CA  THR B 207     107.926  60.045  67.721  1.00 71.66           C  
ANISOU 3921  CA  THR B 207    10080   9848   7302    579   1196    -37       C  
ATOM   3922  C   THR B 207     108.898  60.857  68.566  1.00 70.16           C  
ANISOU 3922  C   THR B 207    10177   9526   6952    699   1010   -101       C  
ATOM   3923  O   THR B 207     108.963  62.084  68.428  1.00 70.33           O  
ANISOU 3923  O   THR B 207    10267   9514   6942    810    906   -201       O  
ATOM   3924  CB  THR B 207     106.571  59.940  68.425  1.00 76.08           C  
ANISOU 3924  CB  THR B 207    10603  10579   7724    662   1466     10       C  
ATOM   3925  OG1 THR B 207     106.717  59.228  69.658  1.00 78.95           O  
ANISOU 3925  OG1 THR B 207    11164  10925   7908    665   1547    104       O  
ATOM   3926  CG2 THR B 207     105.576  59.193  67.547  1.00 76.20           C  
ANISOU 3926  CG2 THR B 207    10306  10728   7917    524   1627     68       C  
ATOM   3927  N   VAL B 208     109.668  60.188  69.427  1.00 69.57           N  
ANISOU 3927  N   VAL B 208    10288   9364   6781    674    944    -45       N  
ATOM   3928  CA  VAL B 208     110.645  60.881  70.259  1.00 66.13           C  
ANISOU 3928  CA  VAL B 208    10127   8800   6199    776    737   -108       C  
ATOM   3929  C   VAL B 208     111.852  61.310  69.436  1.00 59.36           C  
ANISOU 3929  C   VAL B 208     9217   7826   5512    688    473   -168       C  
ATOM   3930  O   VAL B 208     112.309  62.454  69.540  1.00 55.47           O  
ANISOU 3930  O   VAL B 208     8848   7252   4977    757    303   -258       O  
ATOM   3931  CB  VAL B 208     111.055  59.991  71.447  1.00 63.76           C  
ANISOU 3931  CB  VAL B 208    10042   8453   5731    788    744    -25       C  
ATOM   3932  CG1 VAL B 208     112.233  60.599  72.194  1.00 53.56           C  
ANISOU 3932  CG1 VAL B 208     9013   7016   4320    871    477    -97       C  
ATOM   3933  CG2 VAL B 208     109.872  59.790  72.387  1.00 59.80           C  
ANISOU 3933  CG2 VAL B 208     9626   8080   5014    892   1014     38       C  
ATOM   3934  N   VAL B 209     112.387  60.409  68.608  1.00 55.06           N  
ANISOU 3934  N   VAL B 209     8492   7271   5158    534    433   -118       N  
ATOM   3935  CA  VAL B 209     113.525  60.774  67.770  1.00 51.94           C  
ANISOU 3935  CA  VAL B 209     8008   6805   4922    447    212   -163       C  
ATOM   3936  C   VAL B 209     113.153  61.927  66.846  1.00 58.90           C  
ANISOU 3936  C   VAL B 209     8782   7709   5889    453    196   -230       C  
ATOM   3937  O   VAL B 209     113.967  62.822  66.585  1.00 58.42           O  
ANISOU 3937  O   VAL B 209     8763   7567   5869    430      1   -282       O  
ATOM   3938  CB  VAL B 209     114.027  59.550  66.987  1.00 49.35           C  
ANISOU 3938  CB  VAL B 209     7495   6490   4767    316    206   -104       C  
ATOM   3939  CG1 VAL B 209     115.188  59.940  66.077  1.00 53.95           C  
ANISOU 3939  CG1 VAL B 209     7954   7041   5505    236      7   -145       C  
ATOM   3940  CG2 VAL B 209     114.443  58.459  67.946  1.00 46.90           C  
ANISOU 3940  CG2 VAL B 209     7332   6126   4360    327    192    -38       C  
ATOM   3941  N   GLN B 210     111.913  61.931  66.349  1.00 62.88           N  
ANISOU 3941  N   GLN B 210     9149   8320   6421    479    392   -224       N  
ATOM   3942  CA  GLN B 210     111.417  63.073  65.588  1.00 60.74           C  
ANISOU 3942  CA  GLN B 210     8814   8068   6198    524    379   -290       C  
ATOM   3943  C   GLN B 210     111.550  64.364  66.387  1.00 71.38           C  
ANISOU 3943  C   GLN B 210    10417   9318   7384    665    259   -369       C  
ATOM   3944  O   GLN B 210     112.201  65.318  65.940  1.00 67.06           O  
ANISOU 3944  O   GLN B 210     9919   8669   6891    635     72   -416       O  
ATOM   3945  CB  GLN B 210     109.962  62.844  65.183  1.00 54.67           C  
ANISOU 3945  CB  GLN B 210     7875   7446   5450    567    609   -278       C  
ATOM   3946  CG  GLN B 210     109.757  61.938  63.987  1.00 46.10           C  
ANISOU 3946  CG  GLN B 210     6520   6434   4560    424    675   -232       C  
ATOM   3947  CD  GLN B 210     108.293  61.875  63.558  1.00 55.27           C  
ANISOU 3947  CD  GLN B 210     7502   7745   5754    465    869   -234       C  
ATOM   3948  OE1 GLN B 210     107.747  62.858  63.064  1.00 48.51           O  
ANISOU 3948  OE1 GLN B 210     6606   6922   4902    558    861   -296       O  
ATOM   3949  NE2 GLN B 210     107.659  60.716  63.736  1.00 45.53           N  
ANISOU 3949  NE2 GLN B 210     6158   6597   4546    391   1032   -162       N  
ATOM   3950  N   LYS B 211     110.941  64.406  67.581  1.00 48.93           N  
ANISOU 3950  N   LYS B 211     7753   6504   4335    818    363   -383       N  
ATOM   3951  CA  LYS B 211     111.038  65.593  68.427  1.00 53.50           C  
ANISOU 3951  CA  LYS B 211     8614   6981   4733    983    240   -475       C  
ATOM   3952  C   LYS B 211     112.490  65.965  68.713  1.00 58.78           C  
ANISOU 3952  C   LYS B 211     9448   7475   5411    904    -51   -501       C  
ATOM   3953  O   LYS B 211     112.817  67.154  68.814  1.00 56.21           O  
ANISOU 3953  O   LYS B 211     9296   7020   5042    958   -236   -583       O  
ATOM   3954  CB  LYS B 211     110.279  65.373  69.738  1.00 63.96           C  
ANISOU 3954  CB  LYS B 211    10111   8383   5809   1162    409   -474       C  
ATOM   3955  CG  LYS B 211     108.789  65.064  69.600  1.00 64.03           C  
ANISOU 3955  CG  LYS B 211     9942   8594   5792   1245    709   -444       C  
ATOM   3956  CD  LYS B 211     107.990  66.305  69.227  1.00 71.76           C  
ANISOU 3956  CD  LYS B 211    10923   9599   6742   1419    718   -548       C  
ATOM   3957  CE  LYS B 211     106.581  65.946  68.765  1.00 78.33           C  
ANISOU 3957  CE  LYS B 211    11485  10656   7622   1463    990   -517       C  
ATOM   3958  NZ  LYS B 211     105.879  65.073  69.751  1.00 85.06           N  
ANISOU 3958  NZ  LYS B 211    12326  11671   8320   1508   1245   -437       N  
ATOM   3959  N   PHE B 212     113.375  64.970  68.836  1.00 61.60           N  
ANISOU 3959  N   PHE B 212     9753   7821   5829    777   -108   -434       N  
ATOM   3960  CA  PHE B 212     114.793  65.254  69.048  1.00 64.39           C  
ANISOU 3960  CA  PHE B 212    10208   8040   6217    691   -391   -456       C  
ATOM   3961  C   PHE B 212     115.379  66.060  67.896  1.00 71.39           C  
ANISOU 3961  C   PHE B 212    10963   8869   7292    556   -545   -475       C  
ATOM   3962  O   PHE B 212     116.168  66.985  68.117  1.00 71.59           O  
ANISOU 3962  O   PHE B 212    11135   8759   7307    525   -784   -525       O  
ATOM   3963  CB  PHE B 212     115.575  63.953  69.231  1.00 63.20           C  
ANISOU 3963  CB  PHE B 212     9979   7915   6119    596   -411   -380       C  
ATOM   3964  CG  PHE B 212     115.493  63.382  70.618  1.00 61.31           C  
ANISOU 3964  CG  PHE B 212     9972   7662   5660    714   -377   -362       C  
ATOM   3965  CD1 PHE B 212     114.819  64.057  71.622  1.00 61.98           C  
ANISOU 3965  CD1 PHE B 212    10314   7726   5509    896   -331   -418       C  
ATOM   3966  CD2 PHE B 212     116.095  62.171  70.918  1.00 58.28           C  
ANISOU 3966  CD2 PHE B 212     9567   7285   5292    662   -394   -289       C  
ATOM   3967  CE1 PHE B 212     114.744  63.533  72.898  1.00 65.57           C  
ANISOU 3967  CE1 PHE B 212    10998   8180   5737   1010   -288   -392       C  
ATOM   3968  CE2 PHE B 212     116.027  61.643  72.193  1.00 62.05           C  
ANISOU 3968  CE2 PHE B 212    10284   7741   5551    771   -367   -258       C  
ATOM   3969  CZ  PHE B 212     115.349  62.327  73.185  1.00 64.88           C  
ANISOU 3969  CZ  PHE B 212    10895   8090   5665    940   -308   -305       C  
ATOM   3970  N   PHE B 213     115.009  65.724  66.658  1.00 73.24           N  
ANISOU 3970  N   PHE B 213    10932   9202   7695    466   -418   -429       N  
ATOM   3971  CA  PHE B 213     115.541  66.448  65.511  1.00 64.51           C  
ANISOU 3971  CA  PHE B 213     9702   8057   6751    335   -541   -428       C  
ATOM   3972  C   PHE B 213     114.835  67.777  65.282  1.00 67.39           C  
ANISOU 3972  C   PHE B 213    10189   8349   7066    424   -565   -489       C  
ATOM   3973  O   PHE B 213     115.427  68.685  64.687  1.00 67.96           O  
ANISOU 3973  O   PHE B 213    10279   8322   7220    324   -734   -493       O  
ATOM   3974  CB  PHE B 213     115.459  65.581  64.253  1.00 58.32           C  
ANISOU 3974  CB  PHE B 213     8611   7403   6144    222   -411   -362       C  
ATOM   3975  CG  PHE B 213     116.574  64.581  64.138  1.00 54.05           C  
ANISOU 3975  CG  PHE B 213     7941   6897   5698    106   -478   -313       C  
ATOM   3976  CD1 PHE B 213     117.703  64.870  63.391  1.00 60.26           C  
ANISOU 3976  CD1 PHE B 213     8602   7677   6618    -38   -631   -290       C  
ATOM   3977  CD2 PHE B 213     116.490  63.351  64.766  1.00 52.38           C  
ANISOU 3977  CD2 PHE B 213     7733   6731   5439    148   -388   -283       C  
ATOM   3978  CE1 PHE B 213     118.739  63.953  63.285  1.00 58.95           C  
ANISOU 3978  CE1 PHE B 213     8298   7566   6534   -113   -692   -255       C  
ATOM   3979  CE2 PHE B 213     117.520  62.429  64.660  1.00 56.95           C  
ANISOU 3979  CE2 PHE B 213     8208   7333   6099     74   -466   -247       C  
ATOM   3980  CZ  PHE B 213     118.646  62.731  63.917  1.00 54.71           C  
ANISOU 3980  CZ  PHE B 213     7781   7061   5948    -44   -618   -241       C  
ATOM   3981  N   GLU B 214     113.597  67.926  65.754  1.00 48.17           N  
ANISOU 3981  N   GLU B 214     7844   5961   4496    613   -404   -533       N  
ATOM   3982  CA  GLU B 214     112.910  69.198  65.573  1.00 78.12           C  
ANISOU 3982  CA  GLU B 214    11771   9681   8230    740   -440   -605       C  
ATOM   3983  C   GLU B 214     113.473  70.281  66.490  1.00 85.15           C  
ANISOU 3983  C   GLU B 214    12995  10371   8986    810   -679   -686       C  
ATOM   3984  O   GLU B 214     113.427  71.466  66.139  1.00 91.51           O  
ANISOU 3984  O   GLU B 214    13934  11042   9795    836   -817   -734       O  
ATOM   3985  CB  GLU B 214     111.408  69.023  65.807  1.00 76.10           C  
ANISOU 3985  CB  GLU B 214    11480   9567   7868    943   -192   -635       C  
ATOM   3986  CG  GLU B 214     110.757  68.034  64.848  1.00 81.91           C  
ANISOU 3986  CG  GLU B 214    11889  10486   8748    865     18   -564       C  
ATOM   3987  CD  GLU B 214     109.247  67.944  64.997  1.00 96.74           C  
ANISOU 3987  CD  GLU B 214    13689  12521  10545   1045    252   -591       C  
ATOM   3988  OE1 GLU B 214     108.767  67.138  65.823  1.00101.15           O  
ANISOU 3988  OE1 GLU B 214    14236  13190  11005   1098    423   -562       O  
ATOM   3989  OE2 GLU B 214     108.536  68.668  64.265  1.00102.11           O  
ANISOU 3989  OE2 GLU B 214    14312  13224  11262   1129    265   -632       O  
ATOM   3990  N   TYR B 215     114.032  69.904  67.647  1.00 82.52           N  
ANISOU 3990  N   TYR B 215    12821  10001   8533    837   -751   -701       N  
ATOM   3991  CA  TYR B 215     114.372  70.867  68.692  1.00 80.62           C  
ANISOU 3991  CA  TYR B 215    12934   9578   8121    950   -966   -799       C  
ATOM   3992  C   TYR B 215     115.849  70.929  69.055  1.00 72.77           C  
ANISOU 3992  C   TYR B 215    12023   8450   7177    778  -1250   -791       C  
ATOM   3993  O   TYR B 215     116.285  71.948  69.595  1.00 63.15           O  
ANISOU 3993  O   TYR B 215    11078   7038   5877    806  -1497   -872       O  
ATOM   3994  CB  TYR B 215     113.565  70.572  69.970  1.00 78.43           C  
ANISOU 3994  CB  TYR B 215    12847   9369   7585   1202   -816   -853       C  
ATOM   3995  CG  TYR B 215     112.071  70.766  69.815  1.00 83.68           C  
ANISOU 3995  CG  TYR B 215    13465  10164   8164   1411   -563   -886       C  
ATOM   3996  CD1 TYR B 215     111.206  69.681  69.842  1.00 91.47           C  
ANISOU 3996  CD1 TYR B 215    14242  11375   9135   1450   -259   -816       C  
ATOM   3997  CD2 TYR B 215     111.525  72.033  69.640  1.00 84.83           C  
ANISOU 3997  CD2 TYR B 215    13774  10209   8250   1570   -640   -985       C  
ATOM   3998  CE1 TYR B 215     109.838  69.847  69.696  1.00 94.54           C  
ANISOU 3998  CE1 TYR B 215    14547  11912   9460   1632    -29   -843       C  
ATOM   3999  CE2 TYR B 215     110.155  72.210  69.494  1.00 88.51           C  
ANISOU 3999  CE2 TYR B 215    14172  10818   8640   1786   -415  -1023       C  
ATOM   4000  CZ  TYR B 215     109.318  71.112  69.526  1.00 90.80           C  
ANISOU 4000  CZ  TYR B 215    14216  11359   8925   1812   -106   -951       C  
ATOM   4001  OH  TYR B 215     107.957  71.277  69.386  1.00 90.49           O  
ANISOU 4001  OH  TYR B 215    14072  11490   8823   2017    117   -985       O  
ATOM   4002  N   CYS B 216     116.631  69.888  68.791  1.00 68.03           N  
ANISOU 4002  N   CYS B 216    11199   7943   6708    609  -1238   -704       N  
ATOM   4003  CA  CYS B 216     118.044  69.959  69.133  1.00 66.76           C  
ANISOU 4003  CA  CYS B 216    11083   7680   6603    456  -1516   -700       C  
ATOM   4004  C   CYS B 216     118.796  70.843  68.151  1.00 60.26           C  
ANISOU 4004  C   CYS B 216    10167   6759   5968    241  -1706   -674       C  
ATOM   4005  O   CYS B 216     118.363  71.066  67.020  1.00 68.00           O  
ANISOU 4005  O   CYS B 216    10982   7789   7068    179  -1593   -629       O  
ATOM   4006  CB  CYS B 216     118.674  68.568  69.176  1.00 68.18           C  
ANISOU 4006  CB  CYS B 216    11055   7994   6855    373  -1455   -621       C  
ATOM   4007  SG  CYS B 216     118.083  67.567  70.562  1.00 78.21           S  
ANISOU 4007  SG  CYS B 216    12507   9329   7880    589  -1302   -631       S  
ATOM   4008  N   SER B 217     119.924  71.371  68.610  1.00 69.16           N  
ANISOU 4008  N   SER B 217    11413   7748   7117    121  -2007   -699       N  
ATOM   4009  CA  SER B 217     120.778  72.157  67.743  1.00 70.72           C  
ANISOU 4009  CA  SER B 217    11508   7861   7502   -127  -2197   -651       C  
ATOM   4010  C   SER B 217     121.535  71.240  66.787  1.00 71.65           C  
ANISOU 4010  C   SER B 217    11229   8169   7827   -322  -2115   -536       C  
ATOM   4011  O   SER B 217     121.612  70.023  66.979  1.00 69.32           O  
ANISOU 4011  O   SER B 217    10784   8027   7529   -268  -1984   -510       O  
ATOM   4012  CB  SER B 217     121.746  72.998  68.569  1.00 77.40           C  
ANISOU 4012  CB  SER B 217    12592   8502   8314   -214  -2559   -713       C  
ATOM   4013  OG  SER B 217     122.568  72.165  69.365  1.00 86.27           O  
ANISOU 4013  OG  SER B 217    13672   9692   9414   -222  -2655   -718       O  
ATOM   4014  N   ASP B 218     122.103  71.849  65.748  1.00 81.69           N  
ANISOU 4014  N   ASP B 218    12347   9423   9269   -545  -2195   -463       N  
ATOM   4015  CA  ASP B 218     122.741  71.079  64.682  1.00 85.07           C  
ANISOU 4015  CA  ASP B 218    12392  10051   9881   -709  -2090   -356       C  
ATOM   4016  C   ASP B 218     123.844  70.134  65.156  1.00 83.42           C  
ANISOU 4016  C   ASP B 218    12017   9955   9724   -763  -2179   -341       C  
ATOM   4017  O   ASP B 218     123.914  69.011  64.625  1.00 82.71           O  
ANISOU 4017  O   ASP B 218    11667  10056   9701   -745  -2002   -293       O  
ATOM   4018  CB  ASP B 218     123.281  72.038  63.612  1.00 85.96           C  
ANISOU 4018  CB  ASP B 218    12402  10115  10142   -954  -2188   -271       C  
ATOM   4019  CG  ASP B 218     122.176  72.679  62.781  1.00 88.24           C  
ANISOU 4019  CG  ASP B 218    12768  10351  10406   -894  -2045   -258       C  
ATOM   4020  OD1 ASP B 218     121.064  72.110  62.696  1.00 86.47           O  
ANISOU 4020  OD1 ASP B 218    12538  10212  10103   -692  -1815   -292       O  
ATOM   4021  OD2 ASP B 218     122.427  73.760  62.206  1.00 87.98           O  
ANISOU 4021  OD2 ASP B 218    12803  10191  10436  -1055  -2172   -207       O  
ATOM   4022  N   PRO B 219     124.728  70.497  66.098  1.00 75.45           N  
ANISOU 4022  N   PRO B 219    11139   8837   8690   -819  -2458   -385       N  
ATOM   4023  CA  PRO B 219     125.770  69.535  66.504  1.00 71.40           C  
ANISOU 4023  CA  PRO B 219    10446   8453   8231   -846  -2546   -373       C  
ATOM   4024  C   PRO B 219     125.213  68.272  67.131  1.00 77.09           C  
ANISOU 4024  C   PRO B 219    11208   9260   8825   -614  -2374   -404       C  
ATOM   4025  O   PRO B 219     125.816  67.199  66.992  1.00 75.68           O  
ANISOU 4025  O   PRO B 219    10804   9234   8715   -612  -2337   -369       O  
ATOM   4026  CB  PRO B 219     126.615  70.332  67.506  1.00 65.67           C  
ANISOU 4026  CB  PRO B 219     9922   7558   7472   -926  -2903   -434       C  
ATOM   4027  CG  PRO B 219     126.346  71.756  67.188  1.00 65.43           C  
ANISOU 4027  CG  PRO B 219    10070   7334   7456  -1046  -3013   -438       C  
ATOM   4028  CD  PRO B 219     124.920  71.802  66.757  1.00 66.56           C  
ANISOU 4028  CD  PRO B 219    10319   7467   7503   -874  -2736   -448       C  
ATOM   4029  N   ILE B 220     124.077  68.368  67.822  1.00 77.00           N  
ANISOU 4029  N   ILE B 220    11479   9154   8622   -417  -2266   -466       N  
ATOM   4030  CA  ILE B 220     123.466  67.183  68.413  1.00 71.44           C  
ANISOU 4030  CA  ILE B 220    10824   8529   7791   -221  -2081   -473       C  
ATOM   4031  C   ILE B 220     122.688  66.407  67.356  1.00 74.27           C  
ANISOU 4031  C   ILE B 220    10953   9037   8230   -205  -1774   -409       C  
ATOM   4032  O   ILE B 220     122.693  65.171  67.353  1.00 74.87           O  
ANISOU 4032  O   ILE B 220    10909   9222   8314   -147  -1652   -375       O  
ATOM   4033  CB  ILE B 220     122.590  67.587  69.618  1.00 69.28           C  
ANISOU 4033  CB  ILE B 220    10931   8123   7267    -18  -2078   -556       C  
ATOM   4034  CG1 ILE B 220     123.453  67.775  70.873  1.00 69.01           C  
ANISOU 4034  CG1 ILE B 220    11123   7977   7120     17  -2373   -621       C  
ATOM   4035  CG2 ILE B 220     121.532  66.539  69.912  1.00 64.42           C  
ANISOU 4035  CG2 ILE B 220    10343   7606   6529    160  -1788   -533       C  
ATOM   4036  CD1 ILE B 220     124.317  69.021  70.878  1.00 65.50           C  
ANISOU 4036  CD1 ILE B 220    10749   7386   6753   -147  -2695   -664       C  
ATOM   4037  N   LYS B 221     122.036  67.116  66.426  1.00 69.48           N  
ANISOU 4037  N   LYS B 221    10292   8424   7683   -256  -1667   -394       N  
ATOM   4038  CA  LYS B 221     121.445  66.450  65.268  1.00 62.15           C  
ANISOU 4038  CA  LYS B 221     9119   7641   6854   -269  -1419   -336       C  
ATOM   4039  C   LYS B 221     122.501  65.688  64.480  1.00 65.05           C  
ANISOU 4039  C   LYS B 221     9177   8149   7389   -397  -1440   -275       C  
ATOM   4040  O   LYS B 221     122.255  64.567  64.018  1.00 66.64           O  
ANISOU 4040  O   LYS B 221     9219   8473   7630   -350  -1270   -247       O  
ATOM   4041  CB  LYS B 221     120.745  67.463  64.359  1.00 60.77           C  
ANISOU 4041  CB  LYS B 221     8943   7429   6719   -312  -1353   -330       C  
ATOM   4042  CG  LYS B 221     119.616  68.228  65.018  1.00 64.23           C  
ANISOU 4042  CG  LYS B 221     9665   7748   6992   -150  -1315   -401       C  
ATOM   4043  CD  LYS B 221     118.589  68.676  63.995  1.00 60.69           C  
ANISOU 4043  CD  LYS B 221     9149   7329   6580   -124  -1154   -388       C  
ATOM   4044  CE  LYS B 221     119.197  69.548  62.914  1.00 62.96           C  
ANISOU 4044  CE  LYS B 221     9342   7575   7006   -311  -1270   -337       C  
ATOM   4045  NZ  LYS B 221     118.140  70.100  62.021  1.00 60.82           N  
ANISOU 4045  NZ  LYS B 221     9064   7306   6740   -255  -1142   -333       N  
ATOM   4046  N   GLU B 222     123.683  66.283  64.311  1.00 62.88           N  
ANISOU 4046  N   GLU B 222     8814   7864   7215   -558  -1651   -256       N  
ATOM   4047  CA  GLU B 222     124.755  65.579  63.619  1.00 72.08           C  
ANISOU 4047  CA  GLU B 222     9666   9194   8528   -657  -1671   -203       C  
ATOM   4048  C   GLU B 222     125.251  64.387  64.425  1.00 78.20           C  
ANISOU 4048  C   GLU B 222    10431  10019   9262   -540  -1715   -227       C  
ATOM   4049  O   GLU B 222     125.627  63.361  63.845  1.00 79.49           O  
ANISOU 4049  O   GLU B 222    10369  10330   9505   -518  -1630   -199       O  
ATOM   4050  CB  GLU B 222     125.897  66.544  63.307  1.00 77.92           C  
ANISOU 4050  CB  GLU B 222    10293   9928   9385   -874  -1884   -166       C  
ATOM   4051  CG  GLU B 222     125.577  67.473  62.151  1.00 82.86           C  
ANISOU 4051  CG  GLU B 222    10851  10547  10083  -1015  -1809   -105       C  
ATOM   4052  CD  GLU B 222     126.309  68.788  62.229  1.00 89.73           C  
ANISOU 4052  CD  GLU B 222    11784  11297  11011  -1225  -2048    -77       C  
ATOM   4053  OE1 GLU B 222     127.301  68.877  62.983  1.00 94.34           O  
ANISOU 4053  OE1 GLU B 222    12365  11857  11622  -1297  -2277    -95       O  
ATOM   4054  OE2 GLU B 222     125.879  69.739  61.546  1.00 87.01           O  
ANISOU 4054  OE2 GLU B 222    11503  10871  10684  -1320  -2021    -35       O  
ATOM   4055  N   ALA B 223     125.249  64.491  65.755  1.00 82.65           N  
ANISOU 4055  N   ALA B 223    11260  10457   9688   -448  -1854   -281       N  
ATOM   4056  CA  ALA B 223     125.636  63.348  66.573  1.00 72.22           C  
ANISOU 4056  CA  ALA B 223     9976   9164   8302   -318  -1898   -296       C  
ATOM   4057  C   ALA B 223     124.609  62.227  66.470  1.00 66.68           C  
ANISOU 4057  C   ALA B 223     9303   8499   7534   -179  -1638   -276       C  
ATOM   4058  O   ALA B 223     124.974  61.053  66.339  1.00 61.14           O  
ANISOU 4058  O   ALA B 223     8480   7880   6871   -121  -1603   -255       O  
ATOM   4059  CB  ALA B 223     125.825  63.779  68.026  1.00 56.72           C  
ANISOU 4059  CB  ALA B 223     8321   7052   6179   -245  -2110   -356       C  
ATOM   4060  N   MET B 224     123.320  62.565  66.527  1.00 62.72           N  
ANISOU 4060  N   MET B 224     8957   7936   6936   -125  -1464   -283       N  
ATOM   4061  CA  MET B 224     122.290  61.548  66.349  1.00 60.89           C  
ANISOU 4061  CA  MET B 224     8722   7748   6664    -32  -1214   -253       C  
ATOM   4062  C   MET B 224     122.369  60.926  64.959  1.00 67.91           C  
ANISOU 4062  C   MET B 224     9313   8768   7722    -99  -1091   -217       C  
ATOM   4063  O   MET B 224     122.322  59.698  64.818  1.00 63.73           O  
ANISOU 4063  O   MET B 224     8717   8286   7212    -43  -1004   -195       O  
ATOM   4064  CB  MET B 224     120.908  62.153  66.594  1.00 49.72           C  
ANISOU 4064  CB  MET B 224     7483   6278   5131     32  -1054   -270       C  
ATOM   4065  CG  MET B 224     120.657  62.525  68.039  1.00 48.54           C  
ANISOU 4065  CG  MET B 224     7654   6016   4770    151  -1127   -309       C  
ATOM   4066  SD  MET B 224     118.984  63.121  68.356  1.00 57.83           S  
ANISOU 4066  SD  MET B 224     9010   7171   5790    271   -906   -333       S  
ATOM   4067  CE  MET B 224     118.998  64.663  67.446  1.00 60.79           C  
ANISOU 4067  CE  MET B 224     9330   7499   6268    181   -998   -378       C  
ATOM   4068  N   LEU B 225     122.518  61.759  63.925  1.00 72.84           N  
ANISOU 4068  N   LEU B 225     9777   9441   8458   -217  -1092   -210       N  
ATOM   4069  CA  LEU B 225     122.527  61.265  62.553  1.00 65.61           C  
ANISOU 4069  CA  LEU B 225     8597   8656   7675   -267   -966   -180       C  
ATOM   4070  C   LEU B 225     123.730  60.374  62.277  1.00 63.99           C  
ANISOU 4070  C   LEU B 225     8195   8558   7559   -267  -1051   -171       C  
ATOM   4071  O   LEU B 225     123.640  59.442  61.468  1.00 70.94           O  
ANISOU 4071  O   LEU B 225     8922   9531   8501   -231   -934   -163       O  
ATOM   4072  CB  LEU B 225     122.513  62.444  61.583  1.00 67.74           C  
ANISOU 4072  CB  LEU B 225     8768   8949   8020   -394   -967   -162       C  
ATOM   4073  CG  LEU B 225     122.470  62.102  60.096  1.00 56.32           C  
ANISOU 4073  CG  LEU B 225     7072   7643   6684   -442   -833   -130       C  
ATOM   4074  CD1 LEU B 225     121.164  61.404  59.765  1.00 51.87           C  
ANISOU 4074  CD1 LEU B 225     6535   7086   6089   -350   -630   -143       C  
ATOM   4075  CD2 LEU B 225     122.635  63.356  59.280  1.00 55.02           C  
ANISOU 4075  CD2 LEU B 225     6846   7486   6575   -580   -868    -93       C  
ATOM   4076  N   GLU B 226     124.860  60.647  62.928  1.00 64.30           N  
ANISOU 4076  N   GLU B 226     8235   8590   7606   -295  -1264   -180       N  
ATOM   4077  CA  GLU B 226     126.041  59.814  62.745  1.00 68.49           C  
ANISOU 4077  CA  GLU B 226     8564   9240   8217   -266  -1359   -180       C  
ATOM   4078  C   GLU B 226     125.796  58.386  63.218  1.00 64.97           C  
ANISOU 4078  C   GLU B 226     8209   8766   7709   -101  -1306   -193       C  
ATOM   4079  O   GLU B 226     126.402  57.447  62.692  1.00 70.39           O  
ANISOU 4079  O   GLU B 226     8722   9558   8466    -36  -1304   -199       O  
ATOM   4080  CB  GLU B 226     127.221  60.443  63.483  1.00 86.20           C  
ANISOU 4080  CB  GLU B 226    10800  11474  10476   -330  -1622   -192       C  
ATOM   4081  CG  GLU B 226     128.591  59.984  63.026  1.00104.26           C  
ANISOU 4081  CG  GLU B 226    12786  13942  12887   -345  -1732   -185       C  
ATOM   4082  CD  GLU B 226     129.700  60.833  63.622  1.00117.83           C  
ANISOU 4082  CD  GLU B 226    14457  15664  14648   -461  -1998   -189       C  
ATOM   4083  OE1 GLU B 226     129.558  62.076  63.627  1.00121.18           O  
ANISOU 4083  OE1 GLU B 226    14953  16007  15082   -620  -2057   -172       O  
ATOM   4084  OE2 GLU B 226     130.700  60.258  64.106  1.00121.40           O  
ANISOU 4084  OE2 GLU B 226    14811  16189  15126   -389  -2165   -213       O  
ATOM   4085  N   ARG B 227     124.910  58.200  64.200  1.00 71.32           N  
ANISOU 4085  N   ARG B 227     9293   9430   8374    -26  -1260   -195       N  
ATOM   4086  CA  ARG B 227     124.539  56.872  64.677  1.00 61.05           C  
ANISOU 4086  CA  ARG B 227     8118   8075   7004    104  -1194   -185       C  
ATOM   4087  C   ARG B 227     123.372  56.270  63.909  1.00 54.40           C  
ANISOU 4087  C   ARG B 227     7249   7238   6184    104   -957   -164       C  
ATOM   4088  O   ARG B 227     123.193  55.047  63.950  1.00 65.30           O  
ANISOU 4088  O   ARG B 227     8671   8587   7554    183   -906   -150       O  
ATOM   4089  CB  ARG B 227     124.159  56.915  66.161  1.00 67.82           C  
ANISOU 4089  CB  ARG B 227     9296   8791   7682    178  -1248   -179       C  
ATOM   4090  CG  ARG B 227     125.171  57.558  67.092  1.00 73.56           C  
ANISOU 4090  CG  ARG B 227    10110   9483   8357    186  -1507   -211       C  
ATOM   4091  CD  ARG B 227     126.373  56.660  67.303  1.00 85.14           C  
ANISOU 4091  CD  ARG B 227    11491  10995   9865    272  -1684   -221       C  
ATOM   4092  NE  ARG B 227     126.970  56.892  68.615  1.00103.37           N  
ANISOU 4092  NE  ARG B 227    14007  13220  12051    337  -1914   -245       N  
ATOM   4093  CZ  ARG B 227     126.760  56.115  69.673  1.00114.89           C  
ANISOU 4093  CZ  ARG B 227    15734  14572  13347    474  -1941   -226       C  
ATOM   4094  NH1 ARG B 227     125.982  55.046  69.570  1.00120.03           N  
ANISOU 4094  NH1 ARG B 227    16469  15182  13955    538  -1753   -174       N  
ATOM   4095  NH2 ARG B 227     127.337  56.399  70.832  1.00115.41           N  
ANISOU 4095  NH2 ARG B 227    15993  14567  13289    538  -2168   -254       N  
ATOM   4096  N   ILE B 228     122.575  57.092  63.233  1.00 61.91           N  
ANISOU 4096  N   ILE B 228     8144   8215   7164     19   -830   -162       N  
ATOM   4097  CA  ILE B 228     121.376  56.635  62.543  1.00 64.11           C  
ANISOU 4097  CA  ILE B 228     8394   8501   7463     12   -621   -148       C  
ATOM   4098  C   ILE B 228     121.642  56.361  61.067  1.00 65.18           C  
ANISOU 4098  C   ILE B 228     8275   8758   7734    -23   -571   -162       C  
ATOM   4099  O   ILE B 228     121.087  55.416  60.506  1.00 63.68           O  
ANISOU 4099  O   ILE B 228     8046   8572   7576      6   -462   -164       O  
ATOM   4100  CB  ILE B 228     120.234  57.660  62.722  1.00 55.23           C  
ANISOU 4100  CB  ILE B 228     7373   7339   6273    -26   -513   -145       C  
ATOM   4101  CG1 ILE B 228     119.741  57.663  64.180  1.00 56.92           C  
ANISOU 4101  CG1 ILE B 228     7857   7448   6320     44   -509   -131       C  
ATOM   4102  CG2 ILE B 228     119.084  57.373  61.764  1.00 41.33           C  
ANISOU 4102  CG2 ILE B 228     5512   5625   4568    -52   -320   -139       C  
ATOM   4103  CD1 ILE B 228     118.627  58.666  64.444  1.00 57.79           C  
ANISOU 4103  CD1 ILE B 228     8075   7537   6346     49   -402   -141       C  
ATOM   4104  N   ALA B 229     122.507  57.162  60.434  1.00 60.29           N  
ANISOU 4104  N   ALA B 229     7485   8235   7187    -89   -653   -169       N  
ATOM   4105  CA  ALA B 229     122.749  57.084  58.990  1.00 57.78           C  
ANISOU 4105  CA  ALA B 229     6930   8055   6971   -122   -588   -175       C  
ATOM   4106  C   ALA B 229     122.897  55.663  58.455  1.00 55.72           C  
ANISOU 4106  C   ALA B 229     6589   7836   6747    -21   -547   -202       C  
ATOM   4107  O   ALA B 229     122.181  55.312  57.503  1.00 54.69           O  
ANISOU 4107  O   ALA B 229     6397   7736   6647    -21   -422   -215       O  
ATOM   4108  CB  ALA B 229     123.985  57.922  58.625  1.00 52.83           C  
ANISOU 4108  CB  ALA B 229     6127   7540   6406   -205   -708   -160       C  
ATOM   4109  N   PRO B 230     123.768  54.803  59.000  1.00 55.51           N  
ANISOU 4109  N   PRO B 230     6575   7802   6714     78   -661   -218       N  
ATOM   4110  CA  PRO B 230     123.889  53.441  58.449  1.00 60.73           C  
ANISOU 4110  CA  PRO B 230     7190   8479   7405    196   -636   -254       C  
ATOM   4111  C   PRO B 230     122.598  52.639  58.481  1.00 60.37           C  
ANISOU 4111  C   PRO B 230     7306   8301   7331    205   -517   -250       C  
ATOM   4112  O   PRO B 230     122.541  51.567  57.862  1.00 71.84           O  
ANISOU 4112  O   PRO B 230     8736   9746   8817    282   -496   -286       O  
ATOM   4113  CB  PRO B 230     124.960  52.792  59.339  1.00 67.10           C  
ANISOU 4113  CB  PRO B 230     8044   9262   8188    312   -806   -267       C  
ATOM   4114  CG  PRO B 230     125.709  53.934  59.933  1.00 64.56           C  
ANISOU 4114  CG  PRO B 230     7677   8991   7863    236   -927   -247       C  
ATOM   4115  CD  PRO B 230     124.699  55.010  60.124  1.00 58.14           C  
ANISOU 4115  CD  PRO B 230     6975   8104   7010    103   -838   -213       C  
ATOM   4116  N   TYR B 231     121.571  53.108  59.185  1.00 52.98           N  
ANISOU 4116  N   TYR B 231     6529   7265   6335    131   -444   -210       N  
ATOM   4117  CA  TYR B 231     120.284  52.431  59.219  1.00 51.98           C  
ANISOU 4117  CA  TYR B 231     6519   7039   6192    108   -318   -191       C  
ATOM   4118  C   TYR B 231     119.157  53.246  58.611  1.00 53.69           C  
ANISOU 4118  C   TYR B 231     6674   7299   6428     14   -180   -187       C  
ATOM   4119  O   TYR B 231     118.011  52.781  58.617  1.00 54.52           O  
ANISOU 4119  O   TYR B 231     6840   7346   6531    -22    -70   -170       O  
ATOM   4120  CB  TYR B 231     119.920  52.052  60.660  1.00 45.64           C  
ANISOU 4120  CB  TYR B 231     5962   6094   5284    123   -327   -137       C  
ATOM   4121  CG  TYR B 231     121.009  51.279  61.361  1.00 62.21           C  
ANISOU 4121  CG  TYR B 231     8154   8134   7348    233   -485   -137       C  
ATOM   4122  CD1 TYR B 231     121.902  51.910  62.216  1.00 64.79           C  
ANISOU 4122  CD1 TYR B 231     8527   8475   7617    268   -623   -135       C  
ATOM   4123  CD2 TYR B 231     121.146  49.913  61.163  1.00 68.41           C  
ANISOU 4123  CD2 TYR B 231     8993   8840   8158    309   -518   -146       C  
ATOM   4124  CE1 TYR B 231     122.900  51.201  62.851  1.00 71.46           C  
ANISOU 4124  CE1 TYR B 231     9448   9274   8429    385   -786   -141       C  
ATOM   4125  CE2 TYR B 231     122.137  49.196  61.796  1.00 80.77           C  
ANISOU 4125  CE2 TYR B 231    10655  10348   9687    436   -677   -150       C  
ATOM   4126  CZ  TYR B 231     123.012  49.843  62.638  1.00 84.22           C  
ANISOU 4126  CZ  TYR B 231    11116  10818  10066    478   -809   -148       C  
ATOM   4127  OH  TYR B 231     124.001  49.125  63.270  1.00 98.72           O  
ANISOU 4127  OH  TYR B 231    13041  12603  11864    620   -985   -157       O  
ATOM   4128  N   LEU B 232     119.453  54.428  58.063  1.00 46.43           N  
ANISOU 4128  N   LEU B 232     5631   6480   5531    -31   -190   -198       N  
ATOM   4129  CA  LEU B 232     118.399  55.317  57.586  1.00 49.09           C  
ANISOU 4129  CA  LEU B 232     5937   6843   5870    -98    -82   -194       C  
ATOM   4130  C   LEU B 232     117.534  54.647  56.520  1.00 54.52           C  
ANISOU 4130  C   LEU B 232     6538   7560   6618   -106     19   -220       C  
ATOM   4131  O   LEU B 232     116.303  54.753  56.557  1.00 57.31           O  
ANISOU 4131  O   LEU B 232     6923   7889   6964   -142    121   -211       O  
ATOM   4132  CB  LEU B 232     119.022  56.610  57.063  1.00 49.34           C  
ANISOU 4132  CB  LEU B 232     5866   6960   5920   -146   -135   -193       C  
ATOM   4133  CG  LEU B 232     118.083  57.791  56.833  1.00 49.68           C  
ANISOU 4133  CG  LEU B 232     5933   7000   5941   -195    -67   -185       C  
ATOM   4134  CD1 LEU B 232     117.231  58.046  58.065  1.00 48.79           C  
ANISOU 4134  CD1 LEU B 232     6008   6789   5740   -171    -28   -174       C  
ATOM   4135  CD2 LEU B 232     118.899  59.029  56.464  1.00 48.33           C  
ANISOU 4135  CD2 LEU B 232     5704   6875   5785   -260   -154   -166       C  
ATOM   4136  N   ALA B 233     118.153  53.937  55.574  1.00 53.98           N  
ANISOU 4136  N   ALA B 233     6355   7550   6605    -64    -15   -259       N  
ATOM   4137  CA  ALA B 233     117.371  53.237  54.559  1.00 54.59           C  
ANISOU 4137  CA  ALA B 233     6373   7638   6732    -64     51   -299       C  
ATOM   4138  C   ALA B 233     116.477  52.176  55.187  1.00 57.95           C  
ANISOU 4138  C   ALA B 233     6927   7931   7159    -83     90   -284       C  
ATOM   4139  O   ALA B 233     115.310  52.030  54.803  1.00 58.31           O  
ANISOU 4139  O   ALA B 233     6953   7965   7236   -141    170   -289       O  
ATOM   4140  CB  ALA B 233     118.293  52.609  53.512  1.00 59.68           C  
ANISOU 4140  CB  ALA B 233     6900   8365   7410     17     -3   -355       C  
ATOM   4141  N   ALA B 234     117.003  51.429  56.160  1.00 58.78           N  
ANISOU 4141  N   ALA B 234     7165   7936   7231    -43     28   -258       N  
ATOM   4142  CA  ALA B 234     116.188  50.425  56.834  1.00 58.30           C  
ANISOU 4142  CA  ALA B 234     7252   7736   7163    -84     67   -217       C  
ATOM   4143  C   ALA B 234     115.059  51.075  57.620  1.00 62.04           C  
ANISOU 4143  C   ALA B 234     7781   8203   7589   -170    187   -154       C  
ATOM   4144  O   ALA B 234     113.915  50.603  57.584  1.00 67.39           O  
ANISOU 4144  O   ALA B 234     8464   8844   8296   -252    279   -128       O  
ATOM   4145  CB  ALA B 234     117.063  49.562  57.738  1.00 41.44           C  
ANISOU 4145  CB  ALA B 234     5273   5489   4982     -9    -37   -193       C  
ATOM   4146  N   ILE B 235     115.361  52.165  58.332  1.00 56.61           N  
ANISOU 4146  N   ILE B 235     7128   7555   6826   -150    184   -132       N  
ATOM   4147  CA  ILE B 235     114.313  52.908  59.023  1.00 50.27           C  
ANISOU 4147  CA  ILE B 235     6373   6767   5959   -192    300    -91       C  
ATOM   4148  C   ILE B 235     113.338  53.489  58.006  1.00 54.02           C  
ANISOU 4148  C   ILE B 235     6689   7338   6500   -234    386   -126       C  
ATOM   4149  O   ILE B 235     112.121  53.521  58.238  1.00 51.66           O  
ANISOU 4149  O   ILE B 235     6377   7059   6194   -279    507    -99       O  
ATOM   4150  CB  ILE B 235     114.941  54.000  59.917  1.00 41.83           C  
ANISOU 4150  CB  ILE B 235     5398   5704   4790   -141    243    -83       C  
ATOM   4151  CG1 ILE B 235     115.888  53.380  60.939  1.00 44.55           C  
ANISOU 4151  CG1 ILE B 235     5905   5957   5065    -89    137    -52       C  
ATOM   4152  CG2 ILE B 235     113.885  54.765  60.680  1.00 40.67           C  
ANISOU 4152  CG2 ILE B 235     5327   5574   4553   -143    361    -55       C  
ATOM   4153  CD1 ILE B 235     116.872  54.370  61.528  1.00 42.15           C  
ANISOU 4153  CD1 ILE B 235     5656   5662   4696    -41     12    -70       C  
ATOM   4154  N   GLY B 236     113.851  53.906  56.844  1.00 49.71           N  
ANISOU 4154  N   GLY B 236     6009   6863   6013   -215    326   -183       N  
ATOM   4155  CA  GLY B 236     113.015  54.540  55.839  1.00 50.38           C  
ANISOU 4155  CA  GLY B 236     5961   7037   6144   -236    384   -217       C  
ATOM   4156  C   GLY B 236     111.903  53.655  55.315  1.00 48.63           C  
ANISOU 4156  C   GLY B 236     5670   6812   5994   -293    451   -228       C  
ATOM   4157  O   GLY B 236     110.817  54.144  54.998  1.00 50.59           O  
ANISOU 4157  O   GLY B 236     5836   7125   6262   -315    526   -238       O  
ATOM   4158  N   ILE B 237     112.149  52.344  55.211  1.00 44.00           N  
ANISOU 4158  N   ILE B 237     5121   6145   5452   -314    410   -232       N  
ATOM   4159  CA  ILE B 237     111.110  51.425  54.760  1.00 52.47           C  
ANISOU 4159  CA  ILE B 237     6146   7187   6604   -395    448   -241       C  
ATOM   4160  C   ILE B 237     110.264  50.880  55.906  1.00 56.59           C  
ANISOU 4160  C   ILE B 237     6754   7640   7106   -485    542   -154       C  
ATOM   4161  O   ILE B 237     109.347  50.087  55.655  1.00 51.19           O  
ANISOU 4161  O   ILE B 237     6028   6924   6498   -589    576   -142       O  
ATOM   4162  CB  ILE B 237     111.693  50.236  53.960  1.00 58.52           C  
ANISOU 4162  CB  ILE B 237     6928   7878   7429   -376    341   -297       C  
ATOM   4163  CG1 ILE B 237     112.462  49.285  54.870  1.00 59.58           C  
ANISOU 4163  CG1 ILE B 237     7235   7874   7530   -354    283   -255       C  
ATOM   4164  CG2 ILE B 237     112.588  50.717  52.823  1.00 63.08           C  
ANISOU 4164  CG2 ILE B 237     7412   8551   8003   -276    269   -374       C  
ATOM   4165  CD1 ILE B 237     112.970  48.064  54.147  1.00 62.28           C  
ANISOU 4165  CD1 ILE B 237     7619   8121   7922   -309    169   -319       C  
ATOM   4166  N   HIS B 238     110.531  51.278  57.152  1.00 52.51           N  
ANISOU 4166  N   HIS B 238     6361   7103   6486   -457    585    -89       N  
ATOM   4167  CA  HIS B 238     109.753  50.775  58.278  1.00 52.32           C  
ANISOU 4167  CA  HIS B 238     6431   7032   6417   -537    695      9       C  
ATOM   4168  C   HIS B 238     108.471  51.579  58.459  1.00 59.53           C  
ANISOU 4168  C   HIS B 238     7226   8078   7314   -565    846     28       C  
ATOM   4169  O   HIS B 238     108.480  52.815  58.411  1.00 42.15           O  
ANISOU 4169  O   HIS B 238     4981   5971   5062   -473    860    -13       O  
ATOM   4170  CB  HIS B 238     110.577  50.794  59.568  1.00 58.14           C  
ANISOU 4170  CB  HIS B 238     7373   7694   7024   -474    672     68       C  
ATOM   4171  CG  HIS B 238     109.950  50.030  60.701  1.00 57.64           C  
ANISOU 4171  CG  HIS B 238     7447   7559   6894   -557    776    186       C  
ATOM   4172  ND1 HIS B 238     108.930  50.544  61.474  1.00 55.78           N  
ANISOU 4172  ND1 HIS B 238     7199   7417   6579   -586    947    250       N  
ATOM   4173  CD2 HIS B 238     110.188  48.785  61.178  1.00 59.14           C  
ANISOU 4173  CD2 HIS B 238     7796   7596   7077   -615    739    258       C  
ATOM   4174  CE1 HIS B 238     108.569  49.651  62.379  1.00 60.75           C  
ANISOU 4174  CE1 HIS B 238     7962   7968   7151   -673   1026    368       C  
ATOM   4175  NE2 HIS B 238     109.318  48.575  62.222  1.00 59.55           N  
ANISOU 4175  NE2 HIS B 238     7929   7651   7044   -699    894    379       N  
ATOM   4176  N   LYS B 239     107.367  50.851  58.674  1.00 44.40           N  
ANISOU 4176  N   LYS B 239     5259   6166   5443   -693    953     93       N  
ATOM   4177  CA  LYS B 239     106.053  51.469  58.842  1.00 52.14           C  
ANISOU 4177  CA  LYS B 239     6088   7302   6420   -720   1108    114       C  
ATOM   4178  C   LYS B 239     106.086  52.597  59.868  1.00 66.20           C  
ANISOU 4178  C   LYS B 239     7952   9159   8042   -591   1195    132       C  
ATOM   4179  O   LYS B 239     105.569  53.690  59.610  1.00 71.72           O  
ANISOU 4179  O   LYS B 239     8542   9986   8724   -502   1237     76       O  
ATOM   4180  CB  LYS B 239     105.026  50.403  59.239  1.00 61.49           C  
ANISOU 4180  CB  LYS B 239     7230   8475   7659   -901   1221    217       C  
ATOM   4181  CG  LYS B 239     103.596  50.918  59.362  1.00 76.88           C  
ANISOU 4181  CG  LYS B 239     8970  10620   9623   -937   1392    242       C  
ATOM   4182  CD  LYS B 239     102.631  49.871  59.935  1.00 85.25           C  
ANISOU 4182  CD  LYS B 239     9984  11684  10724  -1145   1526    375       C  
ATOM   4183  CE  LYS B 239     103.007  49.437  61.342  1.00 90.09           C  
ANISOU 4183  CE  LYS B 239    10836  12212  11184  -1165   1617    508       C  
ATOM   4184  NZ  LYS B 239     102.027  48.465  61.907  1.00 90.12           N  
ANISOU 4184  NZ  LYS B 239    10795  12229  11219  -1389   1768    663       N  
ATOM   4185  N   ASN B 240     106.694  52.356  61.034  1.00 68.44           N  
ANISOU 4185  N   ASN B 240     8449   9357   8197   -566   1207    202       N  
ATOM   4186  CA  ASN B 240     106.874  53.423  62.014  1.00 63.28           C  
ANISOU 4186  CA  ASN B 240     7917   8751   7375   -426   1253    201       C  
ATOM   4187  C   ASN B 240     108.096  54.272  61.691  1.00 64.25           C  
ANISOU 4187  C   ASN B 240     8115   8821   7477   -310   1080    112       C  
ATOM   4188  O   ASN B 240     108.025  55.506  61.693  1.00 64.52           O  
ANISOU 4188  O   ASN B 240     8140   8920   7454   -201   1074     54       O  
ATOM   4189  CB  ASN B 240     107.020  52.847  63.421  1.00 54.57           C  
ANISOU 4189  CB  ASN B 240     7030   7582   6123   -439   1326    312       C  
ATOM   4190  CG  ASN B 240     105.742  52.254  63.944  1.00 57.22           C  
ANISOU 4190  CG  ASN B 240     7296   8005   6441   -553   1537    424       C  
ATOM   4191  OD1 ASN B 240     105.689  51.080  64.298  1.00 61.45           O  
ANISOU 4191  OD1 ASN B 240     7912   8446   6990   -689   1566    530       O  
ATOM   4192  ND2 ASN B 240     104.693  53.062  63.988  1.00 66.55           N  
ANISOU 4192  ND2 ASN B 240     8322   9370   7593   -499   1685    404       N  
ATOM   4193  N   GLY B 241     109.226  53.619  61.412  1.00 63.89           N  
ANISOU 4193  N   GLY B 241     8141   8658   7479   -332    932    103       N  
ATOM   4194  CA  GLY B 241     110.474  54.343  61.246  1.00 62.53           C  
ANISOU 4194  CA  GLY B 241     8027   8448   7283   -243    774     40       C  
ATOM   4195  C   GLY B 241     110.464  55.348  60.113  1.00 61.72           C  
ANISOU 4195  C   GLY B 241     7772   8423   7254   -212    727    -43       C  
ATOM   4196  O   GLY B 241     111.199  56.338  60.154  1.00 64.51           O  
ANISOU 4196  O   GLY B 241     8177   8771   7565   -146    632    -80       O  
ATOM   4197  N   THR B 242     109.636  55.119  59.089  1.00 58.79           N  
ANISOU 4197  N   THR B 242     7223   8120   6993   -266    779    -67       N  
ATOM   4198  CA  THR B 242     109.636  56.023  57.946  1.00 53.86           C  
ANISOU 4198  CA  THR B 242     6474   7564   6427   -230    726   -137       C  
ATOM   4199  C   THR B 242     109.268  57.446  58.350  1.00 53.79           C  
ANISOU 4199  C   THR B 242     6507   7603   6328   -135    754   -159       C  
ATOM   4200  O   THR B 242     109.772  58.404  57.753  1.00 53.48           O  
ANISOU 4200  O   THR B 242     6462   7565   6293    -94    663   -200       O  
ATOM   4201  CB  THR B 242     108.698  55.509  56.855  1.00 55.78           C  
ANISOU 4201  CB  THR B 242     6534   7873   6788   -292    769   -164       C  
ATOM   4202  OG1 THR B 242     108.922  56.255  55.651  1.00 59.62           O  
ANISOU 4202  OG1 THR B 242     6926   8409   7317   -253    693   -227       O  
ATOM   4203  CG2 THR B 242     107.232  55.615  57.280  1.00 58.45           C  
ANISOU 4203  CG2 THR B 242     6791   8300   7116   -306    918   -139       C  
ATOM   4204  N   TRP B 243     108.421  57.607  59.374  1.00 48.87           N  
ANISOU 4204  N   TRP B 243     5941   7015   5612    -94    877   -128       N  
ATOM   4205  CA  TRP B 243     108.084  58.945  59.851  1.00 46.97           C  
ANISOU 4205  CA  TRP B 243     5776   6807   5264     33    894   -163       C  
ATOM   4206  C   TRP B 243     109.311  59.644  60.424  1.00 54.27           C  
ANISOU 4206  C   TRP B 243     6896   7624   6102     81    753   -177       C  
ATOM   4207  O   TRP B 243     109.476  60.861  60.261  1.00 49.62           O  
ANISOU 4207  O   TRP B 243     6364   7015   5476    155    675   -225       O  
ATOM   4208  CB  TRP B 243     106.996  58.873  60.916  1.00 51.84           C  
ANISOU 4208  CB  TRP B 243     6419   7503   5776     86   1069   -127       C  
ATOM   4209  CG  TRP B 243     105.683  58.307  60.477  1.00 44.10           C  
ANISOU 4209  CG  TRP B 243     5221   6653   4882     30   1214   -108       C  
ATOM   4210  CD1 TRP B 243     105.312  56.994  60.495  1.00 47.75           C  
ANISOU 4210  CD1 TRP B 243     5599   7125   5419   -116   1293    -37       C  
ATOM   4211  CD2 TRP B 243     104.542  59.038  60.010  1.00 44.72           C  
ANISOU 4211  CD2 TRP B 243     5140   6870   4981    115   1287   -158       C  
ATOM   4212  NE1 TRP B 243     104.019  56.859  60.053  1.00 55.47           N  
ANISOU 4212  NE1 TRP B 243     6357   8245   6475   -150   1408    -38       N  
ATOM   4213  CE2 TRP B 243     103.522  58.098  59.748  1.00 60.10           C  
ANISOU 4213  CE2 TRP B 243     6882   8925   7029      2   1408   -115       C  
ATOM   4214  CE3 TRP B 243     104.285  60.395  59.783  1.00 44.75           C  
ANISOU 4214  CE3 TRP B 243     5163   6909   4932    278   1245   -235       C  
ATOM   4215  CZ2 TRP B 243     102.268  58.469  59.265  1.00 59.31           C  
ANISOU 4215  CZ2 TRP B 243     6563   8991   6981     51   1490   -151       C  
ATOM   4216  CZ3 TRP B 243     103.038  60.764  59.306  1.00 45.68           C  
ANISOU 4216  CZ3 TRP B 243     5087   7180   5090    351   1327   -274       C  
ATOM   4217  CH2 TRP B 243     102.046  59.804  59.050  1.00 63.28           C  
ANISOU 4217  CH2 TRP B 243     7081   9539   7423    240   1449   -233       C  
ATOM   4218  N   ALA B 244     110.174  58.889  61.112  1.00 55.45           N  
ANISOU 4218  N   ALA B 244     7156   7693   6217     39    704   -135       N  
ATOM   4219  CA  ALA B 244     111.394  59.467  61.660  1.00 55.24           C  
ANISOU 4219  CA  ALA B 244     7295   7573   6123     71    546   -150       C  
ATOM   4220  C   ALA B 244     112.414  59.744  60.565  1.00 51.65           C  
ANISOU 4220  C   ALA B 244     6744   7100   5782     11    400   -176       C  
ATOM   4221  O   ALA B 244     113.100  60.774  60.588  1.00 47.14           O  
ANISOU 4221  O   ALA B 244     6244   6481   5185     26    275   -201       O  
ATOM   4222  CB  ALA B 244     111.989  58.532  62.713  1.00 53.81           C  
ANISOU 4222  CB  ALA B 244     7255   7323   5869     59    526    -98       C  
ATOM   4223  N   ALA B 245     112.535  58.831  59.602  1.00 49.69           N  
ANISOU 4223  N   ALA B 245     6338   6889   5654    -62    413   -167       N  
ATOM   4224  CA  ALA B 245     113.547  58.990  58.568  1.00 52.66           C  
ANISOU 4224  CA  ALA B 245     6613   7277   6119   -108    297   -184       C  
ATOM   4225  C   ALA B 245     113.227  60.177  57.668  1.00 50.38           C  
ANISOU 4225  C   ALA B 245     6261   7028   5854   -102    284   -211       C  
ATOM   4226  O   ALA B 245     114.125  60.943  57.299  1.00 46.93           O  
ANISOU 4226  O   ALA B 245     5827   6574   5429   -133    172   -210       O  
ATOM   4227  CB  ALA B 245     113.672  57.699  57.763  1.00 52.64           C  
ANISOU 4227  CB  ALA B 245     6481   7305   6215   -154    318   -182       C  
ATOM   4228  N   GLN B 246     111.952  60.362  57.321  1.00 43.72           N  
ANISOU 4228  N   GLN B 246     5358   6237   5015    -66    391   -230       N  
ATOM   4229  CA  GLN B 246     111.593  61.520  56.511  1.00 45.17           C  
ANISOU 4229  CA  GLN B 246     5512   6445   5207    -36    364   -255       C  
ATOM   4230  C   GLN B 246     111.746  62.809  57.303  1.00 62.03           C  
ANISOU 4230  C   GLN B 246     7828   8498   7242     27    294   -266       C  
ATOM   4231  O   GLN B 246     112.163  63.834  56.753  1.00 57.68           O  
ANISOU 4231  O   GLN B 246     7313   7907   6697     12    195   -267       O  
ATOM   4232  CB  GLN B 246     110.170  61.378  55.983  1.00 47.32           C  
ANISOU 4232  CB  GLN B 246     5667   6804   5510      7    479   -281       C  
ATOM   4233  CG  GLN B 246     109.989  60.149  55.121  1.00 55.14           C  
ANISOU 4233  CG  GLN B 246     6495   7854   6602    -63    518   -281       C  
ATOM   4234  CD  GLN B 246     108.573  59.979  54.646  1.00 64.11           C  
ANISOU 4234  CD  GLN B 246     7500   9078   7781    -38    610   -309       C  
ATOM   4235  OE1 GLN B 246     107.886  60.958  54.345  1.00 68.53           O  
ANISOU 4235  OE1 GLN B 246     8045   9678   8316     43    613   -337       O  
ATOM   4236  NE2 GLN B 246     108.118  58.734  54.583  1.00 38.46           N  
ANISOU 4236  NE2 GLN B 246     4158   5855   4599   -106    671   -301       N  
ATOM   4237  N   LYS B 247     111.421  62.773  58.600  1.00 70.00           N  
ANISOU 4237  N   LYS B 247     8973   9473   8151     96    337   -272       N  
ATOM   4238  CA  LYS B 247     111.616  63.947  59.445  1.00 65.18           C  
ANISOU 4238  CA  LYS B 247     8572   8767   7427    173    249   -299       C  
ATOM   4239  C   LYS B 247     113.092  64.307  59.553  1.00 62.62           C  
ANISOU 4239  C   LYS B 247     8329   8346   7117     83     67   -281       C  
ATOM   4240  O   LYS B 247     113.457  65.488  59.517  1.00 64.35           O  
ANISOU 4240  O   LYS B 247     8665   8476   7311     83    -60   -297       O  
ATOM   4241  CB  LYS B 247     111.028  63.698  60.832  1.00 67.71           C  
ANISOU 4241  CB  LYS B 247     9026   9088   7614    276    342   -308       C  
ATOM   4242  CG  LYS B 247     110.727  64.971  61.597  1.00 73.29           C  
ANISOU 4242  CG  LYS B 247     9945   9721   8180    418    290   -364       C  
ATOM   4243  CD  LYS B 247     109.689  65.787  60.852  1.00 78.58           C  
ANISOU 4243  CD  LYS B 247    10551  10441   8865    514    339   -407       C  
ATOM   4244  CE  LYS B 247     109.259  66.998  61.638  1.00 82.96           C  
ANISOU 4244  CE  LYS B 247    11331  10923   9267    697    296   -477       C  
ATOM   4245  NZ  LYS B 247     110.349  68.002  61.680  1.00 87.04           N  
ANISOU 4245  NZ  LYS B 247    12045  11256   9768    651     65   -494       N  
ATOM   4246  N   ILE B 248     113.955  63.299  59.688  1.00 55.38           N  
ANISOU 4246  N   ILE B 248     7351   7444   6247      5     41   -248       N  
ATOM   4247  CA  ILE B 248     115.389  63.551  59.786  1.00 51.37           C  
ANISOU 4247  CA  ILE B 248     6872   6879   5766    -81   -133   -230       C  
ATOM   4248  C   ILE B 248     115.893  64.236  58.530  1.00 54.77           C  
ANISOU 4248  C   ILE B 248     7188   7333   6292   -178   -200   -208       C  
ATOM   4249  O   ILE B 248     116.652  65.210  58.593  1.00 51.69           O  
ANISOU 4249  O   ILE B 248     6875   6866   5900   -244   -347   -197       O  
ATOM   4250  CB  ILE B 248     116.138  62.235  60.037  1.00 48.10           C  
ANISOU 4250  CB  ILE B 248     6386   6501   5390   -116   -138   -205       C  
ATOM   4251  CG1 ILE B 248     115.900  61.776  61.467  1.00 46.84           C  
ANISOU 4251  CG1 ILE B 248     6404   6285   5108    -34   -117   -209       C  
ATOM   4252  CG2 ILE B 248     117.628  62.405  59.739  1.00 44.65           C  
ANISOU 4252  CG2 ILE B 248     5877   6065   5023   -213   -302   -185       C  
ATOM   4253  CD1 ILE B 248     116.330  60.368  61.702  1.00 58.18           C  
ANISOU 4253  CD1 ILE B 248     7795   7742   6570    -45    -99   -178       C  
ATOM   4254  N   ILE B 249     115.481  63.731  57.368  1.00 66.95           N  
ANISOU 4254  N   ILE B 249     8551   8976   7911   -196    -98   -197       N  
ATOM   4255  CA  ILE B 249     115.918  64.303  56.101  1.00 64.63           C  
ANISOU 4255  CA  ILE B 249     8149   8722   7685   -280   -139   -164       C  
ATOM   4256  C   ILE B 249     115.308  65.681  55.898  1.00 63.67           C  
ANISOU 4256  C   ILE B 249     8153   8522   7519   -252   -178   -171       C  
ATOM   4257  O   ILE B 249     115.977  66.604  55.416  1.00 62.45           O  
ANISOU 4257  O   ILE B 249     8027   8320   7383   -346   -285   -128       O  
ATOM   4258  CB  ILE B 249     115.558  63.351  54.950  1.00 56.95           C  
ANISOU 4258  CB  ILE B 249     6983   7876   6781   -279    -27   -164       C  
ATOM   4259  CG1 ILE B 249     116.259  62.004  55.153  1.00 53.39           C  
ANISOU 4259  CG1 ILE B 249     6439   7476   6370   -292    -16   -165       C  
ATOM   4260  CG2 ILE B 249     115.907  63.982  53.615  1.00 54.76           C  
ANISOU 4260  CG2 ILE B 249     6613   7652   6542   -348    -51   -126       C  
ATOM   4261  CD1 ILE B 249     115.728  60.900  54.263  1.00 45.21           C  
ANISOU 4261  CD1 ILE B 249     5263   6528   5386   -265     86   -187       C  
ATOM   4262  N   ASP B 250     114.036  65.847  56.277  1.00 59.64           N  
ANISOU 4262  N   ASP B 250     7719   7995   6945   -121    -95   -220       N  
ATOM   4263  CA  ASP B 250     113.352  67.113  56.041  1.00 61.89           C  
ANISOU 4263  CA  ASP B 250     8126   8206   7181    -51   -134   -240       C  
ATOM   4264  C   ASP B 250     113.966  68.254  56.844  1.00 63.80           C  
ANISOU 4264  C   ASP B 250     8601   8282   7359    -66   -299   -244       C  
ATOM   4265  O   ASP B 250     113.920  69.407  56.400  1.00 60.53           O  
ANISOU 4265  O   ASP B 250     8298   7770   6929    -73   -394   -234       O  
ATOM   4266  CB  ASP B 250     111.860  66.978  56.354  1.00 68.03           C  
ANISOU 4266  CB  ASP B 250     8908   9035   7905    116     -3   -300       C  
ATOM   4267  CG  ASP B 250     111.086  66.287  55.234  1.00 84.86           C  
ANISOU 4267  CG  ASP B 250    10827  11304  10113    122    112   -300       C  
ATOM   4268  OD1 ASP B 250     111.545  66.330  54.068  1.00 94.26           O  
ANISOU 4268  OD1 ASP B 250    11925  12525  11366     37     74   -262       O  
ATOM   4269  OD2 ASP B 250     110.020  65.701  55.515  1.00 91.95           O  
ANISOU 4269  OD2 ASP B 250    11650  12285  11002    208    238   -335       O  
ATOM   4270  N   VAL B 251     114.553  67.963  58.007  1.00 68.32           N  
ANISOU 4270  N   VAL B 251     9266   8806   7887    -73   -354   -260       N  
ATOM   4271  CA  VAL B 251     115.187  68.996  58.823  1.00 67.05           C  
ANISOU 4271  CA  VAL B 251     9338   8477   7663    -94   -541   -276       C  
ATOM   4272  C   VAL B 251     116.706  68.978  58.686  1.00 66.10           C  
ANISOU 4272  C   VAL B 251     9153   8336   7627   -292   -688   -214       C  
ATOM   4273  O   VAL B 251     117.402  69.609  59.486  1.00 74.81           O  
ANISOU 4273  O   VAL B 251    10424   9308   8693   -338   -864   -227       O  
ATOM   4274  CB  VAL B 251     114.772  68.892  60.303  1.00 59.26           C  
ANISOU 4274  CB  VAL B 251     8541   7437   6540     57   -532   -347       C  
ATOM   4275  CG1 VAL B 251     113.255  68.908  60.438  1.00 48.65           C  
ANISOU 4275  CG1 VAL B 251     7220   6153   5113    256   -364   -402       C  
ATOM   4276  CG2 VAL B 251     115.380  67.663  60.973  1.00 67.05           C  
ANISOU 4276  CG2 VAL B 251     9450   8494   7532     19   -499   -329       C  
ATOM   4277  N   ALA B 252     117.238  68.267  57.693  1.00 62.32           N  
ANISOU 4277  N   ALA B 252     8428   7994   7256   -404   -625   -151       N  
ATOM   4278  CA  ALA B 252     118.676  68.292  57.465  1.00 64.03           C  
ANISOU 4278  CA  ALA B 252     8540   8231   7557   -586   -749    -87       C  
ATOM   4279  C   ALA B 252     119.072  69.691  57.020  1.00 67.69           C  
ANISOU 4279  C   ALA B 252     9108   8571   8038   -718   -894    -35       C  
ATOM   4280  O   ALA B 252     118.752  70.109  55.905  1.00 84.64           O  
ANISOU 4280  O   ALA B 252    11202  10744  10212   -756   -840     16       O  
ATOM   4281  CB  ALA B 252     119.092  67.240  56.436  1.00 61.23           C  
ANISOU 4281  CB  ALA B 252     7902   8068   7294   -641   -632    -40       C  
ATOM   4282  N   SER B 253     119.749  70.425  57.895  1.00 62.38           N  
ANISOU 4282  N   SER B 253     8605   7749   7346   -791  -1093    -44       N  
ATOM   4283  CA  SER B 253     120.015  71.839  57.678  1.00 71.97           C  
ANISOU 4283  CA  SER B 253     9991   8789   8567   -914  -1263     -3       C  
ATOM   4284  C   SER B 253     121.451  72.137  57.281  1.00 75.97           C  
ANISOU 4284  C   SER B 253    10358   9319   9187  -1185  -1398    102       C  
ATOM   4285  O   SER B 253     121.687  73.092  56.534  1.00 88.49           O  
ANISOU 4285  O   SER B 253    11982  10828  10811  -1340  -1469    190       O  
ATOM   4286  CB  SER B 253     119.668  72.634  58.942  1.00 92.05           C  
ANISOU 4286  CB  SER B 253    12869  11110  10996   -806  -1421    -98       C  
ATOM   4287  OG  SER B 253     120.257  72.050  60.095  1.00100.70           O  
ANISOU 4287  OG  SER B 253    13986  12213  12063   -784  -1498   -150       O  
ATOM   4288  N   THR B 254     122.413  71.355  57.748  1.00 75.71           N  
ANISOU 4288  N   THR B 254    10160   9398   9208  -1245  -1437    104       N  
ATOM   4289  CA  THR B 254     123.814  71.626  57.477  1.00 85.01           C  
ANISOU 4289  CA  THR B 254    11171  10627  10501  -1499  -1573    199       C  
ATOM   4290  C   THR B 254     124.324  70.766  56.326  1.00 81.44           C  
ANISOU 4290  C   THR B 254    10363  10445  10134  -1562  -1401    281       C  
ATOM   4291  O   THR B 254     123.673  69.816  55.883  1.00 77.58           O  
ANISOU 4291  O   THR B 254     9770  10088   9618  -1402  -1203    247       O  
ATOM   4292  CB  THR B 254     124.661  71.380  58.724  1.00 87.49           C  
ANISOU 4292  CB  THR B 254    11516  10906  10822  -1519  -1759    143       C  
ATOM   4293  OG1 THR B 254     124.876  69.974  58.879  1.00 87.67           O  
ANISOU 4293  OG1 THR B 254    11329  11126  10856  -1401  -1638    110       O  
ATOM   4294  CG2 THR B 254     123.940  71.905  59.945  1.00 93.79           C  
ANISOU 4294  CG2 THR B 254    12677  11471  11487  -1365  -1877     28       C  
ATOM   4295  N   GLU B 255     125.521  71.117  55.848  1.00 85.09           N  
ANISOU 4295  N   GLU B 255    10639  10993  10700  -1802  -1484    391       N  
ATOM   4296  CA  GLU B 255     126.175  70.320  54.818  1.00 84.63           C  
ANISOU 4296  CA  GLU B 255    10228  11215  10711  -1853  -1330    466       C  
ATOM   4297  C   GLU B 255     126.625  68.972  55.362  1.00 84.82           C  
ANISOU 4297  C   GLU B 255    10074  11401  10752  -1713  -1295    388       C  
ATOM   4298  O   GLU B 255     126.551  67.962  54.653  1.00 81.09           O  
ANISOU 4298  O   GLU B 255     9405  11125  10282  -1603  -1116    381       O  
ATOM   4299  CB  GLU B 255     127.363  71.092  54.231  1.00 95.97           C  
ANISOU 4299  CB  GLU B 255    11494  12721  12247  -2155  -1421    614       C  
ATOM   4300  CG  GLU B 255     127.970  70.445  52.989  1.00110.12           C  
ANISOU 4300  CG  GLU B 255    12931  14824  14085  -2203  -1231    707       C  
ATOM   4301  CD  GLU B 255     129.313  71.035  52.586  1.00124.53           C  
ANISOU 4301  CD  GLU B 255    14524  16776  16018  -2506  -1312    858       C  
ATOM   4302  OE1 GLU B 255     129.519  72.254  52.768  1.00130.92           O  
ANISOU 4302  OE1 GLU B 255    15490  17394  16861  -2735  -1480    940       O  
ATOM   4303  OE2 GLU B 255     130.164  70.274  52.079  1.00127.68           O  
ANISOU 4303  OE2 GLU B 255    14578  17469  16467  -2515  -1209    897       O  
ATOM   4304  N   LYS B 256     127.077  68.935  56.618  1.00 87.55           N  
ANISOU 4304  N   LYS B 256    10512  11653  11099  -1702  -1479    324       N  
ATOM   4305  CA  LYS B 256     127.517  67.679  57.214  1.00 86.69           C  
ANISOU 4305  CA  LYS B 256    10271  11671  10996  -1558  -1473    253       C  
ATOM   4306  C   LYS B 256     126.366  66.688  57.340  1.00 78.40           C  
ANISOU 4306  C   LYS B 256     9325  10610   9853  -1304  -1298    166       C  
ATOM   4307  O   LYS B 256     126.576  65.475  57.220  1.00 75.33           O  
ANISOU 4307  O   LYS B 256     8775  10370   9476  -1182  -1208    136       O  
ATOM   4308  CB  LYS B 256     128.156  67.961  58.575  1.00 98.25           C  
ANISOU 4308  CB  LYS B 256    11862  13010  12460  -1594  -1730    202       C  
ATOM   4309  CG  LYS B 256     128.824  66.772  59.238  1.00106.42           C  
ANISOU 4309  CG  LYS B 256    12762  14168  13505  -1464  -1774    143       C  
ATOM   4310  CD  LYS B 256     129.364  67.162  60.604  1.00117.85           C  
ANISOU 4310  CD  LYS B 256    14378  15469  14930  -1492  -2050     88       C  
ATOM   4311  CE  LYS B 256     129.210  66.031  61.608  1.00121.49           C  
ANISOU 4311  CE  LYS B 256    14939  15922  15301  -1255  -2062     -6       C  
ATOM   4312  NZ  LYS B 256     129.296  66.531  63.009  1.00120.43           N  
ANISOU 4312  NZ  LYS B 256    15091  15586  15080  -1233  -2303    -76       N  
ATOM   4313  N   GLN B 257     125.145  67.188  57.558  1.00 73.16           N  
ANISOU 4313  N   GLN B 257     8922   9774   9100  -1224  -1252    127       N  
ATOM   4314  CA  GLN B 257     123.982  66.315  57.695  1.00 66.97           C  
ANISOU 4314  CA  GLN B 257     8223   8986   8237  -1012  -1084     57       C  
ATOM   4315  C   GLN B 257     123.582  65.722  56.354  1.00 70.65           C  
ANISOU 4315  C   GLN B 257     8500   9609   8735   -980   -882     87       C  
ATOM   4316  O   GLN B 257     123.364  64.511  56.240  1.00 73.90           O  
ANISOU 4316  O   GLN B 257     8819  10117   9143   -853   -769     47       O  
ATOM   4317  CB  GLN B 257     122.807  67.088  58.302  1.00 67.00           C  
ANISOU 4317  CB  GLN B 257     8530   8791   8136   -929  -1091      6       C  
ATOM   4318  CG  GLN B 257     123.009  67.527  59.750  1.00 66.14           C  
ANISOU 4318  CG  GLN B 257     8661   8517   7951   -900  -1278    -52       C  
ATOM   4319  CD  GLN B 257     121.872  68.391  60.272  1.00 69.96           C  
ANISOU 4319  CD  GLN B 257     9445   8820   8318   -797  -1280   -108       C  
ATOM   4320  OE1 GLN B 257     120.726  68.260  59.835  1.00 67.02           O  
ANISOU 4320  OE1 GLN B 257     9092   8469   7903   -683  -1106   -124       O  
ATOM   4321  NE2 GLN B 257     122.188  69.285  61.209  1.00 68.38           N  
ANISOU 4321  NE2 GLN B 257     9476   8445   8061   -825  -1490   -145       N  
ATOM   4322  N   MET B 258     123.468  66.567  55.326  1.00 70.48           N  
ANISOU 4322  N   MET B 258     8442   9602   8736  -1090   -845    157       N  
ATOM   4323  CA  MET B 258     123.085  66.072  54.009  1.00 68.35           C  
ANISOU 4323  CA  MET B 258     8012   9480   8477  -1052   -666    182       C  
ATOM   4324  C   MET B 258     124.084  65.051  53.482  1.00 70.66           C  
ANISOU 4324  C   MET B 258     8026   9993   8828  -1050   -615    198       C  
ATOM   4325  O   MET B 258     123.688  63.988  52.991  1.00 75.17           O  
ANISOU 4325  O   MET B 258     8512  10662   9388   -916   -486    152       O  
ATOM   4326  CB  MET B 258     122.930  67.234  53.033  1.00 61.72           C  
ANISOU 4326  CB  MET B 258     7202   8613   7637  -1180   -659    270       C  
ATOM   4327  CG  MET B 258     121.835  68.197  53.419  1.00 59.32           C  
ANISOU 4327  CG  MET B 258     7178   8096   7266  -1134   -703    241       C  
ATOM   4328  SD  MET B 258     121.706  69.544  52.237  1.00 67.55           S  
ANISOU 4328  SD  MET B 258     8284   9082   8299  -1277   -716    355       S  
ATOM   4329  CE  MET B 258     120.462  70.571  53.026  1.00 53.16           C  
ANISOU 4329  CE  MET B 258     6820   6988   6392  -1159   -806    281       C  
ATOM   4330  N   ASP B 259     125.382  65.344  53.588  1.00 67.85           N  
ANISOU 4330  N   ASP B 259     7524   9718   8537  -1190   -725    258       N  
ATOM   4331  CA  ASP B 259     126.376  64.399  53.091  1.00 68.25           C  
ANISOU 4331  CA  ASP B 259     7289  10005   8637  -1161   -675    266       C  
ATOM   4332  C   ASP B 259     126.248  63.054  53.790  1.00 67.32           C  
ANISOU 4332  C   ASP B 259     7185   9890   8502   -959   -667    161       C  
ATOM   4333  O   ASP B 259     126.352  62.002  53.149  1.00 68.77           O  
ANISOU 4333  O   ASP B 259     7223  10221   8687   -836   -560    128       O  
ATOM   4334  CB  ASP B 259     127.782  64.965  53.266  1.00 73.58           C  
ANISOU 4334  CB  ASP B 259     7789  10773   9394  -1348   -813    345       C  
ATOM   4335  CG  ASP B 259     128.031  66.163  52.385  1.00 91.05           C  
ANISOU 4335  CG  ASP B 259     9952  13013  11631  -1573   -799    476       C  
ATOM   4336  OD1 ASP B 259     127.478  66.195  51.265  1.00 98.22           O  
ANISOU 4336  OD1 ASP B 259    10840  13986  12493  -1549   -639    514       O  
ATOM   4337  OD2 ASP B 259     128.783  67.067  52.805  1.00101.14           O  
ANISOU 4337  OD2 ASP B 259    11221  14238  12969  -1780   -959    546       O  
ATOM   4338  N   LEU B 260     125.999  63.067  55.101  1.00 70.22           N  
ANISOU 4338  N   LEU B 260     7755  10086   8840   -916   -783    109       N  
ATOM   4339  CA  LEU B 260     125.828  61.818  55.837  1.00 71.66           C  
ANISOU 4339  CA  LEU B 260     7993  10244   8991   -735   -780     27       C  
ATOM   4340  C   LEU B 260     124.630  61.038  55.324  1.00 65.60           C  
ANISOU 4340  C   LEU B 260     7289   9456   8179   -605   -607    -16       C  
ATOM   4341  O   LEU B 260     124.680  59.806  55.209  1.00 59.78           O  
ANISOU 4341  O   LEU B 260     6491   8778   7444   -474   -557    -62       O  
ATOM   4342  CB  LEU B 260     125.660  62.101  57.325  1.00 73.77           C  
ANISOU 4342  CB  LEU B 260     8501  10324   9203   -717   -922     -8       C  
ATOM   4343  CG  LEU B 260     126.929  62.122  58.159  1.00 70.32           C  
ANISOU 4343  CG  LEU B 260     8003   9913   8803   -756  -1125    -10       C  
ATOM   4344  CD1 LEU B 260     126.559  62.479  59.580  1.00 68.60           C  
ANISOU 4344  CD1 LEU B 260     8077   9490   8497   -721  -1256    -52       C  
ATOM   4345  CD2 LEU B 260     127.614  60.774  58.085  1.00 67.96           C  
ANISOU 4345  CD2 LEU B 260     7532   9756   8533   -618  -1116    -43       C  
ATOM   4346  N   ILE B 261     123.535  61.739  55.032  1.00 60.89           N  
ANISOU 4346  N   ILE B 261     6822   8767   7545   -635   -532     -7       N  
ATOM   4347  CA  ILE B 261     122.346  61.083  54.504  1.00 55.59           C  
ANISOU 4347  CA  ILE B 261     6190   8087   6845   -532   -381    -47       C  
ATOM   4348  C   ILE B 261     122.616  60.543  53.106  1.00 56.37           C  
ANISOU 4348  C   ILE B 261     6083   8358   6977   -511   -283    -40       C  
ATOM   4349  O   ILE B 261     122.318  59.381  52.806  1.00 62.84           O  
ANISOU 4349  O   ILE B 261     6867   9213   7795   -396   -214    -95       O  
ATOM   4350  CB  ILE B 261     121.156  62.058  54.522  1.00 54.56           C  
ANISOU 4350  CB  ILE B 261     6226   7838   6668   -556   -341    -42       C  
ATOM   4351  CG1 ILE B 261     120.795  62.416  55.966  1.00 54.07           C  
ANISOU 4351  CG1 ILE B 261     6385   7614   6544   -527   -419    -68       C  
ATOM   4352  CG2 ILE B 261     119.966  61.462  53.795  1.00 52.35           C  
ANISOU 4352  CG2 ILE B 261     5934   7581   6377   -471   -196    -78       C  
ATOM   4353  CD1 ILE B 261     119.698  63.455  56.084  1.00 57.00           C  
ANISOU 4353  CD1 ILE B 261     6925   7874   6859   -519   -394    -75       C  
ATOM   4354  N   VAL B 262     123.208  61.372  52.237  1.00 53.09           N  
ANISOU 4354  N   VAL B 262     5542   8048   6582   -624   -281     29       N  
ATOM   4355  CA  VAL B 262     123.522  60.942  50.873  1.00 48.60           C  
ANISOU 4355  CA  VAL B 262     4782   7667   6016   -595   -178     41       C  
ATOM   4356  C   VAL B 262     124.476  59.753  50.886  1.00 51.96           C  
ANISOU 4356  C   VAL B 262     5047   8229   6468   -487   -188     -4       C  
ATOM   4357  O   VAL B 262     124.327  58.814  50.094  1.00 50.89           O  
ANISOU 4357  O   VAL B 262     4838   8184   6313   -363   -103    -57       O  
ATOM   4358  CB  VAL B 262     124.106  62.112  50.058  1.00 50.23           C  
ANISOU 4358  CB  VAL B 262     4890   7968   6228   -757   -173    149       C  
ATOM   4359  CG1 VAL B 262     124.612  61.613  48.713  1.00 43.11           C  
ANISOU 4359  CG1 VAL B 262     3776   7297   5306   -714    -58    167       C  
ATOM   4360  CG2 VAL B 262     123.077  63.212  49.864  1.00 52.67           C  
ANISOU 4360  CG2 VAL B 262     5380   8134   6499   -826   -164    185       C  
ATOM   4361  N   LYS B 263     125.473  59.775  51.779  1.00 54.86           N  
ANISOU 4361  N   LYS B 263     5364   8606   6873   -518   -310      8       N  
ATOM   4362  CA  LYS B 263     126.504  58.738  51.781  1.00 57.28           C  
ANISOU 4362  CA  LYS B 263     5497   9061   7206   -399   -339    -33       C  
ATOM   4363  C   LYS B 263     125.931  57.377  52.151  1.00 59.47           C  
ANISOU 4363  C   LYS B 263     5896   9242   7458   -210   -326   -131       C  
ATOM   4364  O   LYS B 263     126.326  56.351  51.580  1.00 65.09           O  
ANISOU 4364  O   LYS B 263     6497  10068   8166    -63   -291   -187       O  
ATOM   4365  CB  LYS B 263     127.632  59.110  52.748  1.00 57.65           C  
ANISOU 4365  CB  LYS B 263     5473   9128   7303   -474   -500     -2       C  
ATOM   4366  CG  LYS B 263     128.716  58.036  52.900  1.00 61.53           C  
ANISOU 4366  CG  LYS B 263     5787   9770   7822   -322   -557    -54       C  
ATOM   4367  CD  LYS B 263     129.902  58.536  53.721  1.00 73.27           C  
ANISOU 4367  CD  LYS B 263     7154  11313   9370   -416   -730    -17       C  
ATOM   4368  CE  LYS B 263     131.082  57.563  53.680  1.00 78.71           C  
ANISOU 4368  CE  LYS B 263     7605  12208  10093   -254   -783    -64       C  
ATOM   4369  NZ  LYS B 263     130.789  56.271  54.366  1.00 75.52           N  
ANISOU 4369  NZ  LYS B 263     7370  11676   9647    -23   -835   -164       N  
ATOM   4370  N   HIS B 264     125.015  57.345  53.112  1.00 50.95           N  
ANISOU 4370  N   HIS B 264     5050   7953   6355   -210   -356   -151       N  
ATOM   4371  CA  HIS B 264     124.490  56.096  53.633  1.00 49.43           C  
ANISOU 4371  CA  HIS B 264     4994   7645   6141    -69   -356   -218       C  
ATOM   4372  C   HIS B 264     123.156  55.714  53.013  1.00 51.62           C  
ANISOU 4372  C   HIS B 264     5364   7850   6398    -45   -234   -249       C  
ATOM   4373  O   HIS B 264     122.599  54.672  53.371  1.00 60.77           O  
ANISOU 4373  O   HIS B 264     6643   8901   7547     41   -227   -294       O  
ATOM   4374  CB  HIS B 264     124.363  56.176  55.159  1.00 59.10           C  
ANISOU 4374  CB  HIS B 264     6415   8702   7339    -81   -459   -210       C  
ATOM   4375  CG  HIS B 264     125.671  56.053  55.880  1.00 65.60           C  
ANISOU 4375  CG  HIS B 264     7167   9577   8180    -48   -613   -209       C  
ATOM   4376  ND1 HIS B 264     126.458  57.142  56.188  1.00 68.84           N  
ANISOU 4376  ND1 HIS B 264     7498  10040   8618   -172   -715   -162       N  
ATOM   4377  CD2 HIS B 264     126.337  54.967  56.338  1.00 63.65           C  
ANISOU 4377  CD2 HIS B 264     6916   9335   7932     98   -699   -251       C  
ATOM   4378  CE1 HIS B 264     127.550  56.734  56.811  1.00 67.83           C  
ANISOU 4378  CE1 HIS B 264     7298   9965   8511   -108   -858   -179       C  
ATOM   4379  NE2 HIS B 264     127.501  55.418  56.915  1.00 67.14           N  
ANISOU 4379  NE2 HIS B 264     7257   9851   8401     69   -850   -234       N  
ATOM   4380  N   LEU B 265     122.624  56.530  52.105  1.00 50.05           N  
ANISOU 4380  N   LEU B 265     5120   7704   6194   -124   -151   -222       N  
ATOM   4381  CA  LEU B 265     121.430  56.157  51.359  1.00 51.67           C  
ANISOU 4381  CA  LEU B 265     5374   7873   6386    -93    -52   -260       C  
ATOM   4382  C   LEU B 265     121.735  55.728  49.937  1.00 61.19           C  
ANISOU 4382  C   LEU B 265     6430   9235   7583    -24      6   -294       C  
ATOM   4383  O   LEU B 265     120.974  54.943  49.360  1.00 65.14           O  
ANISOU 4383  O   LEU B 265     6970   9703   8076     47     49   -358       O  
ATOM   4384  CB  LEU B 265     120.436  57.320  51.305  1.00 45.60           C  
ANISOU 4384  CB  LEU B 265     4684   7043   5600   -195     -7   -220       C  
ATOM   4385  CG  LEU B 265     119.520  57.536  52.509  1.00 53.70           C  
ANISOU 4385  CG  LEU B 265     5891   7903   6608   -217    -15   -216       C  
ATOM   4386  CD1 LEU B 265     118.348  58.426  52.113  1.00 37.21           C  
ANISOU 4386  CD1 LEU B 265     3853   5785   4501   -259     49   -205       C  
ATOM   4387  CD2 LEU B 265     119.055  56.223  53.122  1.00 49.06           C  
ANISOU 4387  CD2 LEU B 265     5392   7226   6025   -143     -3   -258       C  
ATOM   4388  N   ARG B 266     122.827  56.234  49.365  1.00 63.09           N  
ANISOU 4388  N   ARG B 266     6501   9650   7819    -47      7   -253       N  
ATOM   4389  CA  ARG B 266     123.133  55.983  47.959  1.00 56.67           C  
ANISOU 4389  CA  ARG B 266     5546   9017   6968     23     84   -274       C  
ATOM   4390  C   ARG B 266     123.118  54.503  47.596  1.00 57.07           C  
ANISOU 4390  C   ARG B 266     5605   9072   7005    209     83   -385       C  
ATOM   4391  O   ARG B 266     122.442  54.144  46.619  1.00 62.52           O  
ANISOU 4391  O   ARG B 266     6320   9777   7658    268    138   -438       O  
ATOM   4392  CB  ARG B 266     124.470  56.652  47.604  1.00 63.21           C  
ANISOU 4392  CB  ARG B 266     6168  10055   7796    -36     90   -197       C  
ATOM   4393  CG  ARG B 266     124.816  56.564  46.117  1.00 95.16           C  
ANISOU 4393  CG  ARG B 266    10062  14320  11774     28    197   -197       C  
ATOM   4394  CD  ARG B 266     126.216  57.087  45.813  1.00111.49           C  
ANISOU 4394  CD  ARG B 266    11888  16628  13843    -31    221   -111       C  
ATOM   4395  NE  ARG B 266     126.323  58.539  45.953  1.00112.47           N  
ANISOU 4395  NE  ARG B 266    12005  16738  13990   -265    212     25       N  
ATOM   4396  CZ  ARG B 266     126.190  59.402  44.949  1.00106.65           C  
ANISOU 4396  CZ  ARG B 266    11236  16090  13195   -368    301    117       C  
ATOM   4397  NH1 ARG B 266     125.933  58.964  43.724  1.00100.33           N  
ANISOU 4397  NH1 ARG B 266    10403  15417  12301   -248    413     82       N  
ATOM   4398  NH2 ARG B 266     126.310  60.706  45.172  1.00106.24           N  
ANISOU 4398  NH2 ARG B 266    11210  15985  13170   -588    267    243       N  
ATOM   4399  N   PRO B 267     123.782  53.601  48.326  1.00 56.39           N  
ANISOU 4399  N   PRO B 267     5526   8956   6944    315      4   -430       N  
ATOM   4400  CA  PRO B 267     123.719  52.180  47.942  1.00 56.09           C  
ANISOU 4400  CA  PRO B 267     5536   8888   6889    503    -16   -542       C  
ATOM   4401  C   PRO B 267     122.311  51.622  47.921  1.00 57.84           C  
ANISOU 4401  C   PRO B 267     5947   8910   7120    487    -10   -590       C  
ATOM   4402  O   PRO B 267     122.060  50.638  47.216  1.00 64.73           O  
ANISOU 4402  O   PRO B 267     6862   9762   7971    611    -18   -684       O  
ATOM   4403  CB  PRO B 267     124.574  51.485  49.012  1.00 58.76           C  
ANISOU 4403  CB  PRO B 267     5893   9176   7255    596   -127   -560       C  
ATOM   4404  CG  PRO B 267     125.468  52.555  49.544  1.00 59.03           C  
ANISOU 4404  CG  PRO B 267     5789   9324   7314    484   -152   -469       C  
ATOM   4405  CD  PRO B 267     124.622  53.793  49.524  1.00 61.06           C  
ANISOU 4405  CD  PRO B 267     6100   9525   7574    283    -92   -388       C  
ATOM   4406  N   TYR B 268     121.382  52.218  48.662  1.00 56.46           N  
ANISOU 4406  N   TYR B 268     5883   8595   6974    341      0   -533       N  
ATOM   4407  CA  TYR B 268     120.031  51.690  48.774  1.00 54.40           C  
ANISOU 4407  CA  TYR B 268     5771   8163   6736    306     10   -565       C  
ATOM   4408  C   TYR B 268     119.015  52.494  47.976  1.00 57.28           C  
ANISOU 4408  C   TYR B 268     6111   8562   7090    219     84   -552       C  
ATOM   4409  O   TYR B 268     117.812  52.226  48.087  1.00 55.31           O  
ANISOU 4409  O   TYR B 268     5950   8194   6869    169     96   -570       O  
ATOM   4410  CB  TYR B 268     119.611  51.628  50.243  1.00 51.64           C  
ANISOU 4410  CB  TYR B 268     5566   7642   6414    230    -20   -515       C  
ATOM   4411  CG  TYR B 268     120.610  50.960  51.159  1.00 52.46           C  
ANISOU 4411  CG  TYR B 268     5717   7700   6516    315   -111   -516       C  
ATOM   4412  CD1 TYR B 268     121.637  51.683  51.745  1.00 54.34           C  
ANISOU 4412  CD1 TYR B 268     5881   8021   6745    302   -154   -466       C  
ATOM   4413  CD2 TYR B 268     120.505  49.608  51.461  1.00 55.72           C  
ANISOU 4413  CD2 TYR B 268     6262   7972   6939    403   -172   -564       C  
ATOM   4414  CE1 TYR B 268     122.546  51.074  52.594  1.00 59.15           C  
ANISOU 4414  CE1 TYR B 268     6529   8595   7351    393   -257   -472       C  
ATOM   4415  CE2 TYR B 268     121.408  48.990  52.306  1.00 58.95           C  
ANISOU 4415  CE2 TYR B 268     6733   8327   7336    501   -271   -564       C  
ATOM   4416  CZ  TYR B 268     122.427  49.727  52.872  1.00 64.65           C  
ANISOU 4416  CZ  TYR B 268     7363   9154   8046    504   -314   -521       C  
ATOM   4417  OH  TYR B 268     123.330  49.122  53.722  1.00 70.39           O  
ANISOU 4417  OH  TYR B 268     8147   9838   8761    614   -432   -526       O  
ATOM   4418  N   THR B 269     119.463  53.459  47.164  1.00 59.18           N  
ANISOU 4418  N   THR B 269     6231   8965   7290    199    129   -515       N  
ATOM   4419  CA  THR B 269     118.520  54.347  46.489  1.00 60.16           C  
ANISOU 4419  CA  THR B 269     6355   9108   7394    124    183   -491       C  
ATOM   4420  C   THR B 269     117.571  53.574  45.579  1.00 61.42           C  
ANISOU 4420  C   THR B 269     6550   9240   7548    185    183   -582       C  
ATOM   4421  O   THR B 269     116.367  53.854  45.546  1.00 56.59           O  
ANISOU 4421  O   THR B 269     5985   8556   6959    123    194   -584       O  
ATOM   4422  CB  THR B 269     119.267  55.419  45.698  1.00 53.96           C  
ANISOU 4422  CB  THR B 269     5454   8495   6553     93    226   -423       C  
ATOM   4423  OG1 THR B 269     120.091  56.183  46.587  1.00 63.48           O  
ANISOU 4423  OG1 THR B 269     6632   9709   7781      6    201   -338       O  
ATOM   4424  CG2 THR B 269     118.278  56.359  45.043  1.00 43.94           C  
ANISOU 4424  CG2 THR B 269     4218   7222   5254     30    262   -393       C  
ATOM   4425  N   ALA B 270     118.083  52.588  44.843  1.00 72.11           N  
ANISOU 4425  N   ALA B 270     7880  10649   8871    316    159   -666       N  
ATOM   4426  CA  ALA B 270     117.203  51.785  43.998  1.00 70.56           C  
ANISOU 4426  CA  ALA B 270     7739  10401   8668    374    127   -767       C  
ATOM   4427  C   ALA B 270     116.182  51.033  44.840  1.00 67.27           C  
ANISOU 4427  C   ALA B 270     7438   9778   8342    303     78   -791       C  
ATOM   4428  O   ALA B 270     114.977  51.075  44.564  1.00 66.99           O  
ANISOU 4428  O   ALA B 270     7426   9688   8341    237     73   -812       O  
ATOM   4429  CB  ALA B 270     118.024  50.816  43.148  1.00 77.13           C  
ANISOU 4429  CB  ALA B 270     8554  11315   9436    554     97   -866       C  
ATOM   4430  N   LEU B 271     116.647  50.355  45.892  1.00 60.52           N  
ANISOU 4430  N   LEU B 271     6651   8817   7527    311     42   -778       N  
ATOM   4431  CA  LEU B 271     115.744  49.575  46.728  1.00 58.48           C  
ANISOU 4431  CA  LEU B 271     6513   8363   7344    231      7   -779       C  
ATOM   4432  C   LEU B 271     114.691  50.452  47.395  1.00 59.57           C  
ANISOU 4432  C   LEU B 271     6644   8472   7519     81     73   -698       C  
ATOM   4433  O   LEU B 271     113.578  49.988  47.669  1.00 65.77           O  
ANISOU 4433  O   LEU B 271     7476   9150   8364     -7     72   -702       O  
ATOM   4434  CB  LEU B 271     116.553  48.814  47.771  1.00 60.32           C  
ANISOU 4434  CB  LEU B 271     6838   8494   7588    278    -44   -761       C  
ATOM   4435  CG  LEU B 271     117.429  47.720  47.163  1.00 67.46           C  
ANISOU 4435  CG  LEU B 271     7775   9397   8462    457   -128   -861       C  
ATOM   4436  CD1 LEU B 271     118.435  47.224  48.181  1.00 74.74           C  
ANISOU 4436  CD1 LEU B 271     8760  10258   9380    533   -184   -836       C  
ATOM   4437  CD2 LEU B 271     116.579  46.573  46.641  1.00 71.35           C  
ANISOU 4437  CD2 LEU B 271     8387   9733   8991    462   -205   -952       C  
ATOM   4438  N   LEU B 272     115.018  51.720  47.656  1.00 49.91           N  
ANISOU 4438  N   LEU B 272     5359   7344   6260     51    129   -626       N  
ATOM   4439  CA  LEU B 272     114.033  52.631  48.231  1.00 43.34           C  
ANISOU 4439  CA  LEU B 272     4529   6494   5445    -51    188   -566       C  
ATOM   4440  C   LEU B 272     112.922  52.950  47.238  1.00 54.14           C  
ANISOU 4440  C   LEU B 272     5836   7910   6825    -69    201   -606       C  
ATOM   4441  O   LEU B 272     111.746  52.997  47.618  1.00 58.16           O  
ANISOU 4441  O   LEU B 272     6345   8374   7381   -140    230   -596       O  
ATOM   4442  CB  LEU B 272     114.715  53.915  48.704  1.00 38.18           C  
ANISOU 4442  CB  LEU B 272     3857   5904   4745    -67    213   -491       C  
ATOM   4443  CG  LEU B 272     115.579  53.807  49.962  1.00 41.81           C  
ANISOU 4443  CG  LEU B 272     4386   6304   5196    -71    187   -443       C  
ATOM   4444  CD1 LEU B 272     116.290  55.119  50.252  1.00 36.81           C  
ANISOU 4444  CD1 LEU B 272     3728   5733   4524   -100    183   -381       C  
ATOM   4445  CD2 LEU B 272     114.723  53.392  51.151  1.00 40.10           C  
ANISOU 4445  CD2 LEU B 272     4278   5957   4999   -125    214   -415       C  
ATOM   4446  N   TYR B 273     113.268  53.164  45.960  1.00 60.13           N  
ANISOU 4446  N   TYR B 273     6535   8777   7535      1    181   -650       N  
ATOM   4447  CA  TYR B 273     112.241  53.446  44.957  1.00 50.32           C  
ANISOU 4447  CA  TYR B 273     5248   7581   6291      2    171   -695       C  
ATOM   4448  C   TYR B 273     111.234  52.307  44.848  1.00 47.18           C  
ANISOU 4448  C   TYR B 273     4867   7088   5970    -33    119   -769       C  
ATOM   4449  O   TYR B 273     110.066  52.542  44.524  1.00 49.90           O  
ANISOU 4449  O   TYR B 273     5163   7444   6353    -75    110   -790       O  
ATOM   4450  CB  TYR B 273     112.870  53.720  43.584  1.00 51.80           C  
ANISOU 4450  CB  TYR B 273     5396   7899   6387     97    157   -729       C  
ATOM   4451  CG  TYR B 273     113.312  55.155  43.390  1.00 49.06           C  
ANISOU 4451  CG  TYR B 273     5018   7652   5971     85    206   -641       C  
ATOM   4452  CD1 TYR B 273     114.563  55.574  43.810  1.00 46.30           C  
ANISOU 4452  CD1 TYR B 273     4652   7349   5590     76    237   -570       C  
ATOM   4453  CD2 TYR B 273     112.455  56.101  42.840  1.00 46.96           C  
ANISOU 4453  CD2 TYR B 273     4745   7421   5679     74    208   -624       C  
ATOM   4454  CE1 TYR B 273     114.971  56.881  43.656  1.00 44.72           C  
ANISOU 4454  CE1 TYR B 273     4437   7217   5338     32    267   -478       C  
ATOM   4455  CE2 TYR B 273     112.849  57.420  42.688  1.00 48.75           C  
ANISOU 4455  CE2 TYR B 273     4978   7703   5841     53    238   -534       C  
ATOM   4456  CZ  TYR B 273     114.114  57.804  43.101  1.00 51.31           C  
ANISOU 4456  CZ  TYR B 273     5294   8061   6141     19    268   -457       C  
ATOM   4457  OH  TYR B 273     114.536  59.112  42.962  1.00 52.44           O  
ANISOU 4457  OH  TYR B 273     5454   8239   6230    -33    284   -356       O  
ATOM   4458  N   PHE B 274     111.660  51.077  45.129  1.00 39.13           N  
ANISOU 4458  N   PHE B 274     3918   5968   4982    -19     71   -807       N  
ATOM   4459  CA  PHE B 274     110.777  49.922  45.062  1.00 40.15           C  
ANISOU 4459  CA  PHE B 274     4087   5974   5194    -79      2   -868       C  
ATOM   4460  C   PHE B 274     109.815  49.828  46.240  1.00 47.64           C  
ANISOU 4460  C   PHE B 274     5038   6834   6229   -228     53   -794       C  
ATOM   4461  O   PHE B 274     108.864  49.043  46.175  1.00 49.49           O  
ANISOU 4461  O   PHE B 274     5272   6985   6548   -323      8   -824       O  
ATOM   4462  CB  PHE B 274     111.605  48.638  44.989  1.00 62.16           C  
ANISOU 4462  CB  PHE B 274     6985   8657   7976     -3    -81   -932       C  
ATOM   4463  CG  PHE B 274     112.349  48.469  43.697  1.00 69.68           C  
ANISOU 4463  CG  PHE B 274     7933   9702   8838    160   -135  -1031       C  
ATOM   4464  CD1 PHE B 274     113.500  47.702  43.641  1.00 85.95           C  
ANISOU 4464  CD1 PHE B 274    10065  11741  10852    296   -179  -1079       C  
ATOM   4465  CD2 PHE B 274     111.904  49.084  42.540  1.00 65.71           C  
ANISOU 4465  CD2 PHE B 274     7360   9322   8285    196   -140  -1076       C  
ATOM   4466  CE1 PHE B 274     114.186  47.548  42.450  1.00 86.64           C  
ANISOU 4466  CE1 PHE B 274    10139  11942  10838    468   -209  -1173       C  
ATOM   4467  CE2 PHE B 274     112.586  48.932  41.352  1.00 65.19           C  
ANISOU 4467  CE2 PHE B 274     7301   9357   8110    355   -174  -1160       C  
ATOM   4468  CZ  PHE B 274     113.727  48.165  41.306  1.00 75.47           C  
ANISOU 4468  CZ  PHE B 274     8661  10653   9360    493   -200  -1210       C  
ATOM   4469  N   ASP B 275     110.025  50.599  47.303  1.00 55.48           N  
ANISOU 4469  N   ASP B 275     6034   7848   7198   -254    145   -698       N  
ATOM   4470  CA  ASP B 275     109.308  50.413  48.558  1.00 61.13           C  
ANISOU 4470  CA  ASP B 275     6776   8488   7962   -371    212   -620       C  
ATOM   4471  C   ASP B 275     108.154  51.399  48.695  1.00 59.14           C  
ANISOU 4471  C   ASP B 275     6410   8333   7726   -418    292   -589       C  
ATOM   4472  O   ASP B 275     108.258  52.554  48.268  1.00 64.69           O  
ANISOU 4472  O   ASP B 275     7063   9143   8375   -345    309   -594       O  
ATOM   4473  CB  ASP B 275     110.269  50.560  49.738  1.00 59.45           C  
ANISOU 4473  CB  ASP B 275     6665   8230   7693   -346    251   -544       C  
ATOM   4474  CG  ASP B 275     109.608  50.282  51.062  1.00 66.32           C  
ANISOU 4474  CG  ASP B 275     7593   9021   8582   -451    327   -456       C  
ATOM   4475  OD1 ASP B 275     109.000  51.212  51.632  1.00 73.54           O  
ANISOU 4475  OD1 ASP B 275     8460  10009   9472   -473    421   -407       O  
ATOM   4476  OD2 ASP B 275     109.684  49.131  51.526  1.00 71.15           O  
ANISOU 4476  OD2 ASP B 275     8311   9498   9226   -504    294   -436       O  
ATOM   4477  N   GLN B 276     107.052  50.929  49.301  1.00 52.31           N  
ANISOU 4477  N   GLN B 276     5508   7433   6934   -539    340   -552       N  
ATOM   4478  CA  GLN B 276     105.885  51.788  49.510  1.00 56.42           C  
ANISOU 4478  CA  GLN B 276     5899   8068   7472   -565    425   -527       C  
ATOM   4479  C   GLN B 276     106.215  53.033  50.331  1.00 56.37           C  
ANISOU 4479  C   GLN B 276     5928   8120   7368   -485    514   -470       C  
ATOM   4480  O   GLN B 276     105.631  54.097  50.095  1.00 58.61           O  
ANISOU 4480  O   GLN B 276     6129   8509   7629   -424    544   -483       O  
ATOM   4481  CB  GLN B 276     104.762  51.007  50.184  1.00 66.09           C  
ANISOU 4481  CB  GLN B 276     7064   9264   8785   -721    486   -476       C  
ATOM   4482  CG  GLN B 276     105.184  50.304  51.461  1.00 79.77           C  
ANISOU 4482  CG  GLN B 276     8940  10876  10494   -793    547   -380       C  
ATOM   4483  CD  GLN B 276     104.025  49.643  52.190  1.00 83.77           C  
ANISOU 4483  CD  GLN B 276     9381  11375  11074   -968    638   -299       C  
ATOM   4484  OE1 GLN B 276     102.887  50.110  52.125  1.00 91.76           O  
ANISOU 4484  OE1 GLN B 276    10210  12524  12130  -1006    710   -295       O  
ATOM   4485  NE2 GLN B 276     104.307  48.531  52.866  1.00 68.44           N  
ANISOU 4485  NE2 GLN B 276     7582   9276   9146  -1075    633   -229       N  
ATOM   4486  N   PHE B 277     107.129  52.930  51.296  1.00 52.97           N  
ANISOU 4486  N   PHE B 277     5635   7612   6877   -475    539   -413       N  
ATOM   4487  CA  PHE B 277     107.539  54.096  52.071  1.00 47.86           C  
ANISOU 4487  CA  PHE B 277     5051   6999   6135   -400    591   -371       C  
ATOM   4488  C   PHE B 277     108.885  54.650  51.643  1.00 55.20           C  
ANISOU 4488  C   PHE B 277     6043   7922   7007   -321    511   -389       C  
ATOM   4489  O   PHE B 277     109.075  55.869  51.667  1.00 65.00           O  
ANISOU 4489  O   PHE B 277     7297   9209   8190   -261    514   -380       O  
ATOM   4490  CB  PHE B 277     107.605  53.763  53.567  1.00 56.71           C  
ANISOU 4490  CB  PHE B 277     6286   8053   7208   -439    669   -290       C  
ATOM   4491  CG  PHE B 277     106.401  53.032  54.082  1.00 61.23           C  
ANISOU 4491  CG  PHE B 277     6800   8632   7833   -548    765   -244       C  
ATOM   4492  CD1 PHE B 277     105.140  53.601  54.001  1.00 58.50           C  
ANISOU 4492  CD1 PHE B 277     6303   8413   7510   -550    851   -250       C  
ATOM   4493  CD2 PHE B 277     106.537  51.788  54.680  1.00 55.20           C  
ANISOU 4493  CD2 PHE B 277     6130   7751   7092   -649    771   -186       C  
ATOM   4494  CE1 PHE B 277     104.032  52.930  54.477  1.00 57.35           C  
ANISOU 4494  CE1 PHE B 277     6067   8302   7420   -670    951   -195       C  
ATOM   4495  CE2 PHE B 277     105.436  51.116  55.163  1.00 43.73           C  
ANISOU 4495  CE2 PHE B 277     4621   6306   5690   -783    867   -121       C  
ATOM   4496  CZ  PHE B 277     104.181  51.689  55.065  1.00 54.10           C  
ANISOU 4496  CZ  PHE B 277     5750   7770   7034   -802    965   -123       C  
ATOM   4497  N   GLY B 278     109.818  53.781  51.245  1.00 50.40           N  
ANISOU 4497  N   GLY B 278     5473   7260   6417   -318    437   -412       N  
ATOM   4498  CA  GLY B 278     111.157  54.237  50.911  1.00 50.06           C  
ANISOU 4498  CA  GLY B 278     5458   7240   6323   -251    377   -417       C  
ATOM   4499  C   GLY B 278     111.203  55.212  49.750  1.00 55.98           C  
ANISOU 4499  C   GLY B 278     6128   8093   7050   -207    356   -446       C  
ATOM   4500  O   GLY B 278     112.053  56.105  49.722  1.00 66.33           O  
ANISOU 4500  O   GLY B 278     7457   9438   8309   -181    336   -415       O  
ATOM   4501  N   ASN B 279     110.301  55.061  48.775  1.00 47.35           N  
ANISOU 4501  N   ASN B 279     4952   7045   5993   -205    349   -498       N  
ATOM   4502  CA  ASN B 279     110.318  55.979  47.642  1.00 49.28           C  
ANISOU 4502  CA  ASN B 279     5145   7383   6198   -154    323   -517       C  
ATOM   4503  C   ASN B 279     109.978  57.396  48.079  1.00 53.55           C  
ANISOU 4503  C   ASN B 279     5711   7941   6694   -139    355   -469       C  
ATOM   4504  O   ASN B 279     110.478  58.361  47.489  1.00 52.97           O  
ANISOU 4504  O   ASN B 279     5652   7907   6565   -110    328   -446       O  
ATOM   4505  CB  ASN B 279     109.372  55.499  46.534  1.00 49.86           C  
ANISOU 4505  CB  ASN B 279     5138   7496   6311   -143    287   -591       C  
ATOM   4506  CG  ASN B 279     107.920  55.826  46.808  1.00 52.56           C  
ANISOU 4506  CG  ASN B 279     5414   7856   6699   -168    320   -597       C  
ATOM   4507  OD1 ASN B 279     107.433  56.899  46.445  1.00 47.22           O  
ANISOU 4507  OD1 ASN B 279     4710   7243   5988   -116    319   -594       O  
ATOM   4508  ND2 ASN B 279     107.208  54.884  47.410  1.00 63.01           N  
ANISOU 4508  ND2 ASN B 279     6708   9131   8102   -247    344   -602       N  
ATOM   4509  N   TYR B 280     109.154  57.542  49.120  1.00 48.05           N  
ANISOU 4509  N   TYR B 280     5032   7212   6013   -155    412   -450       N  
ATOM   4510  CA  TYR B 280     108.928  58.864  49.693  1.00 42.87           C  
ANISOU 4510  CA  TYR B 280     4436   6554   5300   -112    432   -417       C  
ATOM   4511  C   TYR B 280     110.148  59.344  50.463  1.00 47.79           C  
ANISOU 4511  C   TYR B 280     5176   7114   5868   -125    406   -365       C  
ATOM   4512  O   TYR B 280     110.438  60.546  50.476  1.00 53.82           O  
ANISOU 4512  O   TYR B 280     6008   7862   6578   -100    371   -339       O  
ATOM   4513  CB  TYR B 280     107.696  58.849  50.593  1.00 37.47           C  
ANISOU 4513  CB  TYR B 280     3728   5880   4630   -101    514   -419       C  
ATOM   4514  CG  TYR B 280     106.385  58.732  49.841  1.00 55.96           C  
ANISOU 4514  CG  TYR B 280     5926   8307   7028    -81    525   -468       C  
ATOM   4515  CD1 TYR B 280     105.797  57.490  49.611  1.00 38.68           C  
ANISOU 4515  CD1 TYR B 280     3633   6134   4929   -160    538   -494       C  
ATOM   4516  CD2 TYR B 280     105.736  59.863  49.358  1.00 41.04           C  
ANISOU 4516  CD2 TYR B 280     4013   6474   5106     16    503   -491       C  
ATOM   4517  CE1 TYR B 280     104.597  57.380  48.935  1.00 39.53           C  
ANISOU 4517  CE1 TYR B 280     3593   6327   5100   -155    527   -543       C  
ATOM   4518  CE2 TYR B 280     104.544  59.763  48.682  1.00 42.93           C  
ANISOU 4518  CE2 TYR B 280     4108   6804   5399     47    495   -543       C  
ATOM   4519  CZ  TYR B 280     103.976  58.522  48.468  1.00 46.08           C  
ANISOU 4519  CZ  TYR B 280     4380   7233   5895    -45    506   -570       C  
ATOM   4520  OH  TYR B 280     102.783  58.439  47.779  1.00 49.94           O  
ANISOU 4520  OH  TYR B 280     4707   7819   6449    -25    477   -625       O  
ATOM   4521  N   VAL B 281     110.872  58.425  51.106  1.00 45.08           N  
ANISOU 4521  N   VAL B 281     4865   6724   5538   -166    406   -350       N  
ATOM   4522  CA  VAL B 281     112.116  58.798  51.768  1.00 42.46           C  
ANISOU 4522  CA  VAL B 281     4622   6346   5164   -179    356   -309       C  
ATOM   4523  C   VAL B 281     113.125  59.297  50.744  1.00 46.27           C  
ANISOU 4523  C   VAL B 281     5059   6884   5640   -191    294   -295       C  
ATOM   4524  O   VAL B 281     113.795  60.315  50.958  1.00 55.68           O  
ANISOU 4524  O   VAL B 281     6306   8055   6793   -214    245   -253       O  
ATOM   4525  CB  VAL B 281     112.659  57.612  52.591  1.00 46.87           C  
ANISOU 4525  CB  VAL B 281     5221   6849   5737   -199    353   -300       C  
ATOM   4526  CG1 VAL B 281     114.037  57.923  53.153  1.00 40.91           C  
ANISOU 4526  CG1 VAL B 281     4529   6066   4949   -206    275   -268       C  
ATOM   4527  CG2 VAL B 281     111.693  57.273  53.732  1.00 45.57           C  
ANISOU 4527  CG2 VAL B 281     5125   6633   5555   -204    431   -285       C  
ATOM   4528  N   ALA B 282     113.231  58.606  49.606  1.00 55.70           N  
ANISOU 4528  N   ALA B 282     6155   8148   6862   -180    294   -329       N  
ATOM   4529  CA  ALA B 282     114.098  59.076  48.529  1.00 56.84           C  
ANISOU 4529  CA  ALA B 282     6242   8377   6979   -184    263   -307       C  
ATOM   4530  C   ALA B 282     113.719  60.488  48.095  1.00 57.07           C  
ANISOU 4530  C   ALA B 282     6309   8409   6964   -194    252   -268       C  
ATOM   4531  O   ALA B 282     114.581  61.365  47.975  1.00 58.68           O  
ANISOU 4531  O   ALA B 282     6537   8622   7137   -244    216   -203       O  
ATOM   4532  CB  ALA B 282     114.032  58.117  47.342  1.00 54.09           C  
ANISOU 4532  CB  ALA B 282     5805   8106   6642   -139    271   -366       C  
ATOM   4533  N   GLN B 283     112.425  60.731  47.872  1.00 54.29           N  
ANISOU 4533  N   GLN B 283     5965   8048   6614   -148    273   -303       N  
ATOM   4534  CA  GLN B 283     111.998  62.052  47.420  1.00 55.13           C  
ANISOU 4534  CA  GLN B 283     6130   8145   6673   -127    246   -273       C  
ATOM   4535  C   GLN B 283     112.336  63.137  48.436  1.00 53.46           C  
ANISOU 4535  C   GLN B 283     6049   7833   6429   -154    208   -223       C  
ATOM   4536  O   GLN B 283     112.604  64.283  48.054  1.00 56.75           O  
ANISOU 4536  O   GLN B 283     6543   8216   6802   -175    155   -170       O  
ATOM   4537  CB  GLN B 283     110.501  62.055  47.144  1.00 44.52           C  
ANISOU 4537  CB  GLN B 283     4755   6817   5342    -49    265   -332       C  
ATOM   4538  CG  GLN B 283     110.101  61.118  46.061  1.00 38.37           C  
ANISOU 4538  CG  GLN B 283     3865   6121   4591    -27    268   -389       C  
ATOM   4539  CD  GLN B 283     108.615  61.110  45.860  1.00 46.47           C  
ANISOU 4539  CD  GLN B 283     4834   7173   5647     36    270   -449       C  
ATOM   4540  OE1 GLN B 283     107.981  62.172  45.770  1.00 42.24           O  
ANISOU 4540  OE1 GLN B 283     4341   6632   5075    102    248   -442       O  
ATOM   4541  NE2 GLN B 283     108.030  59.911  45.848  1.00 46.74           N  
ANISOU 4541  NE2 GLN B 283     4773   7231   5754     16    288   -509       N  
ATOM   4542  N   CYS B 284     112.331  62.805  49.729  1.00 50.47           N  
ANISOU 4542  N   CYS B 284     5720   7394   6064   -155    223   -237       N  
ATOM   4543  CA  CYS B 284     112.718  63.795  50.727  1.00 64.00           C  
ANISOU 4543  CA  CYS B 284     7580   9002   7734   -170    166   -204       C  
ATOM   4544  C   CYS B 284     114.104  64.361  50.464  1.00 64.55           C  
ANISOU 4544  C   CYS B 284     7668   9058   7799   -275     85   -133       C  
ATOM   4545  O   CYS B 284     114.387  65.492  50.872  1.00 69.63           O  
ANISOU 4545  O   CYS B 284     8445   9603   8408   -309      5    -97       O  
ATOM   4546  CB  CYS B 284     112.662  63.195  52.131  1.00 59.44           C  
ANISOU 4546  CB  CYS B 284     7057   8377   7152   -153    194   -227       C  
ATOM   4547  SG  CYS B 284     110.996  62.944  52.739  1.00 56.19           S  
ANISOU 4547  SG  CYS B 284     6647   7979   6725    -45    299   -282       S  
ATOM   4548  N   CYS B 285     114.963  63.613  49.774  1.00 47.80           N  
ANISOU 4548  N   CYS B 285     5415   7037   5711   -328    101   -114       N  
ATOM   4549  CA  CYS B 285     116.303  64.094  49.487  1.00 46.14           C  
ANISOU 4549  CA  CYS B 285     5173   6855   5502   -438     42    -37       C  
ATOM   4550  C   CYS B 285     116.336  65.128  48.375  1.00 50.77           C  
ANISOU 4550  C   CYS B 285     5778   7460   6053   -488     26     32       C  
ATOM   4551  O   CYS B 285     117.390  65.730  48.148  1.00 58.25           O  
ANISOU 4551  O   CYS B 285     6708   8424   6999   -609    -22    120       O  
ATOM   4552  CB  CYS B 285     117.213  62.926  49.128  1.00 47.65           C  
ANISOU 4552  CB  CYS B 285     5203   7172   5728   -446     76    -45       C  
ATOM   4553  SG  CYS B 285     117.508  61.836  50.528  1.00 53.81           S  
ANISOU 4553  SG  CYS B 285     6000   7902   6542   -406     57    -97       S  
ATOM   4554  N   LEU B 286     115.216  65.356  47.686  1.00 46.95           N  
ANISOU 4554  N   LEU B 286     5327   6976   5538   -404     58      4       N  
ATOM   4555  CA  LEU B 286     115.200  66.388  46.658  1.00 52.45           C  
ANISOU 4555  CA  LEU B 286     6078   7669   6181   -440     30     78       C  
ATOM   4556  C   LEU B 286     115.432  67.765  47.264  1.00 63.08           C  
ANISOU 4556  C   LEU B 286     7607   8854   7507   -514    -75    142       C  
ATOM   4557  O   LEU B 286     115.932  68.666  46.581  1.00 70.38           O  
ANISOU 4557  O   LEU B 286     8588   9756   8400   -614   -120    244       O  
ATOM   4558  CB  LEU B 286     113.873  66.353  45.901  1.00 56.65           C  
ANISOU 4558  CB  LEU B 286     6620   8223   6681   -310     59     21       C  
ATOM   4559  CG  LEU B 286     113.613  65.106  45.055  1.00 48.02           C  
ANISOU 4559  CG  LEU B 286     5371   7274   5600   -248    132    -42       C  
ATOM   4560  CD1 LEU B 286     112.134  64.987  44.753  1.00 38.07           C  
ANISOU 4560  CD1 LEU B 286     4114   6012   4338   -122    136   -125       C  
ATOM   4561  CD2 LEU B 286     114.437  65.136  43.780  1.00 50.91           C  
ANISOU 4561  CD2 LEU B 286     5674   7760   5909   -299    156     29       C  
ATOM   4562  N   ARG B 287     115.079  67.937  48.544  1.00 62.56           N  
ANISOU 4562  N   ARG B 287     7652   8669   7451   -467   -120     85       N  
ATOM   4563  CA  ARG B 287     115.322  69.190  49.255  1.00 54.60           C  
ANISOU 4563  CA  ARG B 287     6846   7481   6417   -521   -244    122       C  
ATOM   4564  C   ARG B 287     116.772  69.639  49.160  1.00 56.08           C  
ANISOU 4564  C   ARG B 287     7016   7659   6634   -726   -321    232       C  
ATOM   4565  O   ARG B 287     117.051  70.844  49.156  1.00 54.01           O  
ANISOU 4565  O   ARG B 287     6916   7255   6351   -822   -435    304       O  
ATOM   4566  CB  ARG B 287     114.959  69.034  50.732  1.00 73.14           C  
ANISOU 4566  CB  ARG B 287     9292   9740   8758   -435   -267     36       C  
ATOM   4567  CG  ARG B 287     113.570  69.480  51.140  1.00 89.54           C  
ANISOU 4567  CG  ARG B 287    11500  11742  10779   -253   -255    -45       C  
ATOM   4568  CD  ARG B 287     113.478  69.591  52.658  1.00 93.24           C  
ANISOU 4568  CD  ARG B 287    12107  12109  11209   -189   -294   -107       C  
ATOM   4569  NE  ARG B 287     114.534  70.444  53.202  1.00 99.86           N  
ANISOU 4569  NE  ARG B 287    13103  12801  12039   -313   -450    -60       N  
ATOM   4570  CZ  ARG B 287     115.631  69.995  53.808  1.00104.27           C  
ANISOU 4570  CZ  ARG B 287    13615  13370  12635   -431   -496    -37       C  
ATOM   4571  NH1 ARG B 287     115.830  68.693  53.954  1.00100.52           N  
ANISOU 4571  NH1 ARG B 287    12961  13033  12199   -426   -395    -55       N  
ATOM   4572  NH2 ARG B 287     116.535  70.851  54.264  1.00111.19           N  
ANISOU 4572  NH2 ARG B 287    14630  14108  13511   -555   -661      3       N  
ATOM   4573  N   PHE B 288     117.710  68.687  49.096  1.00 58.03           N  
ANISOU 4573  N   PHE B 288     7065   8053   6932   -797   -269    248       N  
ATOM   4574  CA  PHE B 288     119.126  69.020  49.205  1.00 62.86           C  
ANISOU 4574  CA  PHE B 288     7615   8683   7585   -990   -344    343       C  
ATOM   4575  C   PHE B 288     119.596  69.917  48.068  1.00 63.36           C  
ANISOU 4575  C   PHE B 288     7677   8769   7629  -1140   -355    481       C  
ATOM   4576  O   PHE B 288     120.640  70.568  48.201  1.00 68.83           O  
ANISOU 4576  O   PHE B 288     8364   9432   8358  -1336   -443    582       O  
ATOM   4577  CB  PHE B 288     119.978  67.744  49.229  1.00 61.88           C  
ANISOU 4577  CB  PHE B 288     7254   8746   7513   -994   -275    324       C  
ATOM   4578  CG  PHE B 288     119.712  66.843  50.408  1.00 60.69           C  
ANISOU 4578  CG  PHE B 288     7120   8562   7379   -877   -278    214       C  
ATOM   4579  CD1 PHE B 288     118.864  67.235  51.433  1.00 57.61           C  
ANISOU 4579  CD1 PHE B 288     6933   8003   6953   -794   -330    149       C  
ATOM   4580  CD2 PHE B 288     120.321  65.602  50.490  1.00 59.73           C  
ANISOU 4580  CD2 PHE B 288     6822   8577   7294   -839   -228    180       C  
ATOM   4581  CE1 PHE B 288     118.615  66.402  52.506  1.00 49.93           C  
ANISOU 4581  CE1 PHE B 288     5985   7009   5977   -694   -317     67       C  
ATOM   4582  CE2 PHE B 288     120.082  64.765  51.568  1.00 57.04           C  
ANISOU 4582  CE2 PHE B 288     6524   8190   6959   -740   -236     97       C  
ATOM   4583  CZ  PHE B 288     119.228  65.167  52.576  1.00 55.32           C  
ANISOU 4583  CZ  PHE B 288     6507   7812   6699   -677   -273     48       C  
ATOM   4584  N   LYS B 289     118.855  69.950  46.956  1.00 58.59           N  
ANISOU 4584  N   LYS B 289     7076   8219   6966  -1060   -272    494       N  
ATOM   4585  CA  LYS B 289     119.181  70.738  45.770  1.00 68.10           C  
ANISOU 4585  CA  LYS B 289     8300   9453   8123  -1181   -263    635       C  
ATOM   4586  C   LYS B 289     120.453  70.246  45.085  1.00 73.10           C  
ANISOU 4586  C   LYS B 289     8688  10313   8775  -1319   -177    732       C  
ATOM   4587  O   LYS B 289     121.192  69.419  45.634  1.00 76.62           O  
ANISOU 4587  O   LYS B 289     8960  10868   9284  -1330   -157    690       O  
ATOM   4588  CB  LYS B 289     119.312  72.230  46.118  1.00 58.75           C  
ANISOU 4588  CB  LYS B 289     7358   8032   6931  -1319   -420    725       C  
ATOM   4589  CG  LYS B 289     118.075  72.839  46.760  1.00 60.94           C  
ANISOU 4589  CG  LYS B 289     7894   8090   7170  -1153   -510    625       C  
ATOM   4590  CD  LYS B 289     118.191  74.353  46.863  1.00 73.80           C  
ANISOU 4590  CD  LYS B 289     9796   9470   8774  -1274   -677    719       C  
ATOM   4591  CE  LYS B 289     116.883  74.990  47.322  1.00 94.62           C  
ANISOU 4591  CE  LYS B 289    12693  11907  11350  -1058   -758    612       C  
ATOM   4592  NZ  LYS B 289     116.803  76.430  46.929  1.00107.35           N  
ANISOU 4592  NZ  LYS B 289    14590  13287  12910  -1132   -906    714       N  
ATOM   4593  N   TYR B 290     120.700  70.736  43.875  1.00 62.13           N  
ANISOU 4593  N   TYR B 290     7284   9004   7319  -1407   -122    862       N  
ATOM   4594  CA  TYR B 290     121.953  70.445  43.197  1.00 69.34           C  
ANISOU 4594  CA  TYR B 290     7962  10151   8233  -1550    -28    977       C  
ATOM   4595  C   TYR B 290     123.113  71.085  43.958  1.00 74.08           C  
ANISOU 4595  C   TYR B 290     8522  10699   8926  -1796   -135   1078       C  
ATOM   4596  O   TYR B 290     123.027  72.256  44.351  1.00 73.56           O  
ANISOU 4596  O   TYR B 290     8671  10405   8875  -1933   -276   1148       O  
ATOM   4597  CB  TYR B 290     121.921  70.963  41.756  1.00 77.66           C  
ANISOU 4597  CB  TYR B 290     9042  11293   9171  -1601     58   1116       C  
ATOM   4598  CG  TYR B 290     123.169  70.642  40.956  1.00 83.44           C  
ANISOU 4598  CG  TYR B 290     9516  12310   9878  -1728    190   1241       C  
ATOM   4599  CD1 TYR B 290     123.314  69.418  40.313  1.00 76.96           C  
ANISOU 4599  CD1 TYR B 290     8486  11748   9006  -1562    339   1161       C  
ATOM   4600  CD2 TYR B 290     124.207  71.565  40.853  1.00 82.81           C  
ANISOU 4600  CD2 TYR B 290     9396  12244   9823  -2014    164   1439       C  
ATOM   4601  CE1 TYR B 290     124.456  69.124  39.594  1.00 74.83           C  
ANISOU 4601  CE1 TYR B 290     7971  11764   8699  -1645    472   1266       C  
ATOM   4602  CE2 TYR B 290     125.351  71.279  40.134  1.00 79.40           C  
ANISOU 4602  CE2 TYR B 290     8694  12108   9366  -2130    304   1561       C  
ATOM   4603  CZ  TYR B 290     125.471  70.058  39.504  1.00 81.72           C  
ANISOU 4603  CZ  TYR B 290     8777  12677   9595  -1929    466   1470       C  
ATOM   4604  OH  TYR B 290     126.609  69.770  38.781  1.00 87.77           O  
ANISOU 4604  OH  TYR B 290     9265  13764  10319  -2012    619   1584       O  
ATOM   4605  N   PRO B 291     124.232  70.369  44.147  1.00 72.74           N  
ANISOU 4605  N   PRO B 291     8083  10737   8820  -1857    -88   1086       N  
ATOM   4606  CA  PRO B 291     124.527  69.042  43.595  1.00 74.09           C  
ANISOU 4606  CA  PRO B 291     8001  11184   8966  -1702     68   1016       C  
ATOM   4607  C   PRO B 291     124.261  67.858  44.518  1.00 71.18           C  
ANISOU 4607  C   PRO B 291     7585  10809   8652  -1506     50    831       C  
ATOM   4608  O   PRO B 291     124.570  66.725  44.152  1.00 68.68           O  
ANISOU 4608  O   PRO B 291     7079  10695   8323  -1373    153    764       O  
ATOM   4609  CB  PRO B 291     126.020  69.134  43.303  1.00 71.74           C  
ANISOU 4609  CB  PRO B 291     7437  11114   8708  -1900    113   1155       C  
ATOM   4610  CG  PRO B 291     126.539  70.032  44.392  1.00 66.20           C  
ANISOU 4610  CG  PRO B 291     6813  10224   8115  -2119    -74   1212       C  
ATOM   4611  CD  PRO B 291     125.414  70.962  44.794  1.00 60.81           C  
ANISOU 4611  CD  PRO B 291     6490   9208   7407  -2109   -200   1188       C  
ATOM   4612  N   LYS B 292     123.698  68.101  45.697  1.00 72.59           N  
ANISOU 4612  N   LYS B 292     7947  10755   8879  -1479    -79    750       N  
ATOM   4613  CA  LYS B 292     123.601  67.016  46.663  1.00 68.71           C  
ANISOU 4613  CA  LYS B 292     7413  10259   8435  -1327   -100    605       C  
ATOM   4614  C   LYS B 292     122.501  66.022  46.303  1.00 71.87           C  
ANISOU 4614  C   LYS B 292     7843  10679   8786  -1099     -1    479       C  
ATOM   4615  O   LYS B 292     122.664  64.817  46.536  1.00 67.27           O  
ANISOU 4615  O   LYS B 292     7147  10187   8225   -973     38    385       O  
ATOM   4616  CB  LYS B 292     123.395  67.594  48.062  1.00 61.34           C  
ANISOU 4616  CB  LYS B 292     6673   9088   7547  -1370   -261    565       C  
ATOM   4617  CG  LYS B 292     124.504  68.553  48.487  1.00 68.48           C  
ANISOU 4617  CG  LYS B 292     7557   9950   8513  -1611   -397    678       C  
ATOM   4618  CD  LYS B 292     124.944  68.294  49.926  1.00 78.55           C  
ANISOU 4618  CD  LYS B 292     8859  11138   9849  -1605   -538    601       C  
ATOM   4619  CE  LYS B 292     126.295  68.934  50.247  1.00 81.97           C  
ANISOU 4619  CE  LYS B 292     9177  11603  10366  -1848   -674    703       C  
ATOM   4620  NZ  LYS B 292     126.312  70.411  50.054  1.00 88.30           N  
ANISOU 4620  NZ  LYS B 292    10148  12233  11170  -2067   -781    823       N  
ATOM   4621  N   ASN B 293     121.399  66.486  45.709  1.00 72.45           N  
ANISOU 4621  N   ASN B 293     8065  10666   8796  -1044     26    475       N  
ATOM   4622  CA  ASN B 293     120.325  65.579  45.315  1.00 65.93           C  
ANISOU 4622  CA  ASN B 293     7252   9864   7935   -850    102    358       C  
ATOM   4623  C   ASN B 293     120.613  64.846  44.013  1.00 67.25           C  
ANISOU 4623  C   ASN B 293     7260  10247   8043   -782    219    360       C  
ATOM   4624  O   ASN B 293     119.745  64.101  43.545  1.00 70.64           O  
ANISOU 4624  O   ASN B 293     7703  10696   8442   -632    265    262       O  
ATOM   4625  CB  ASN B 293     119.002  66.331  45.166  1.00 61.08           C  
ANISOU 4625  CB  ASN B 293     6836   9095   7277   -795     74    341       C  
ATOM   4626  CG  ASN B 293     119.062  67.411  44.112  1.00 57.97           C  
ANISOU 4626  CG  ASN B 293     6508   8707   6811   -884     75    465       C  
ATOM   4627  OD1 ASN B 293     120.096  67.624  43.484  1.00 59.15           O  
ANISOU 4627  OD1 ASN B 293     6550   8984   6942  -1010    113    578       O  
ATOM   4628  ND2 ASN B 293     117.942  68.088  43.895  1.00 59.90           N  
ANISOU 4628  ND2 ASN B 293     6926   8822   7009   -814     37    450       N  
ATOM   4629  N   THR B 294     121.792  65.053  43.415  1.00 64.33           N  
ANISOU 4629  N   THR B 294     6741  10047   7654   -889    265    467       N  
ATOM   4630  CA  THR B 294     122.092  64.441  42.123  1.00 59.76           C  
ANISOU 4630  CA  THR B 294     6024   9693   6988   -806    388    472       C  
ATOM   4631  C   THR B 294     122.040  62.921  42.190  1.00 59.97           C  
ANISOU 4631  C   THR B 294     5954   9804   7029   -613    424    320       C  
ATOM   4632  O   THR B 294     121.622  62.275  41.223  1.00 59.00           O  
ANISOU 4632  O   THR B 294     5818   9774   6826   -475    491    255       O  
ATOM   4633  CB  THR B 294     123.465  64.904  41.625  1.00 63.95           C  
ANISOU 4633  CB  THR B 294     6379  10421   7498   -960    446    622       C  
ATOM   4634  OG1 THR B 294     123.463  66.328  41.460  1.00 67.89           O  
ANISOU 4634  OG1 THR B 294     6998  10817   7979  -1159    404    778       O  
ATOM   4635  CG2 THR B 294     123.812  64.248  40.296  1.00 67.29           C  
ANISOU 4635  CG2 THR B 294     6657  11105   7804   -846    592    623       C  
ATOM   4636  N   PHE B 295     122.435  62.331  43.324  1.00 62.87           N  
ANISOU 4636  N   PHE B 295     6278  10121   7489   -597    364    258       N  
ATOM   4637  CA  PHE B 295     122.452  60.875  43.423  1.00 63.19           C  
ANISOU 4637  CA  PHE B 295     6253  10215   7542   -418    381    123       C  
ATOM   4638  C   PHE B 295     121.087  60.273  43.105  1.00 65.86           C  
ANISOU 4638  C   PHE B 295     6722  10448   7855   -289    387     10       C  
ATOM   4639  O   PHE B 295     121.009  59.157  42.579  1.00 69.44           O  
ANISOU 4639  O   PHE B 295     7133  10972   8279   -140    417    -90       O  
ATOM   4640  CB  PHE B 295     122.926  60.441  44.815  1.00 58.36           C  
ANISOU 4640  CB  PHE B 295     5630   9516   7026   -424    293     84       C  
ATOM   4641  CG  PHE B 295     121.860  60.501  45.871  1.00 59.64           C  
ANISOU 4641  CG  PHE B 295     5985   9441   7235   -425    222     31       C  
ATOM   4642  CD1 PHE B 295     121.555  61.699  46.500  1.00 57.00           C  
ANISOU 4642  CD1 PHE B 295     5774   8965   6917   -555    160    100       C  
ATOM   4643  CD2 PHE B 295     121.152  59.361  46.224  1.00 54.42           C  
ANISOU 4643  CD2 PHE B 295     5388   8698   6591   -293    218    -84       C  
ATOM   4644  CE1 PHE B 295     120.572  61.756  47.468  1.00 51.16           C  
ANISOU 4644  CE1 PHE B 295     5203   8035   6200   -530    113     47       C  
ATOM   4645  CE2 PHE B 295     120.163  59.413  47.186  1.00 50.69           C  
ANISOU 4645  CE2 PHE B 295     5072   8037   6151   -300    178   -118       C  
ATOM   4646  CZ  PHE B 295     119.871  60.614  47.810  1.00 45.92           C  
ANISOU 4646  CZ  PHE B 295     4575   7323   5551   -406    134    -55       C  
ATOM   4647  N   LEU B 296     120.005  60.998  43.399  1.00 62.27           N  
ANISOU 4647  N   LEU B 296     6422   9827   7412   -339    347     21       N  
ATOM   4648  CA  LEU B 296     118.673  60.501  43.076  1.00 59.24           C  
ANISOU 4648  CA  LEU B 296     6128   9364   7016   -233    347    -78       C  
ATOM   4649  C   LEU B 296     118.499  60.325  41.574  1.00 54.74           C  
ANISOU 4649  C   LEU B 296     5526   8929   6343   -152    402    -94       C  
ATOM   4650  O   LEU B 296     117.905  59.339  41.122  1.00 50.24           O  
ANISOU 4650  O   LEU B 296     4962   8365   5760    -29    400   -208       O  
ATOM   4651  CB  LEU B 296     117.611  61.456  43.616  1.00 55.71           C  
ANISOU 4651  CB  LEU B 296     5826   8750   6590   -287    300    -56       C  
ATOM   4652  CG  LEU B 296     117.417  61.488  45.126  1.00 50.44           C  
ANISOU 4652  CG  LEU B 296     5232   7934   6001   -323    248    -74       C  
ATOM   4653  CD1 LEU B 296     116.480  62.620  45.473  1.00 58.32           C  
ANISOU 4653  CD1 LEU B 296     6370   8800   6989   -352    211    -46       C  
ATOM   4654  CD2 LEU B 296     116.876  60.156  45.622  1.00 42.61           C  
ANISOU 4654  CD2 LEU B 296     4232   6900   5058   -232    255   -183       C  
ATOM   4655  N   PHE B 297     119.010  61.275  40.785  1.00 55.71           N  
ANISOU 4655  N   PHE B 297     5629   9154   6384   -224    445     23       N  
ATOM   4656  CA  PHE B 297     118.835  61.224  39.339  1.00 59.20           C  
ANISOU 4656  CA  PHE B 297     6066   9729   6698   -143    501     23       C  
ATOM   4657  C   PHE B 297     119.839  60.297  38.673  1.00 64.88           C  
ANISOU 4657  C   PHE B 297     6640  10660   7350    -42    579    -13       C  
ATOM   4658  O   PHE B 297     119.535  59.713  37.628  1.00 74.44           O  
ANISOU 4658  O   PHE B 297     7863  11962   8459     96    607    -88       O  
ATOM   4659  CB  PHE B 297     118.936  62.630  38.753  1.00 54.14           C  
ANISOU 4659  CB  PHE B 297     5489   9103   5977   -262    520    179       C  
ATOM   4660  CG  PHE B 297     117.911  63.568  39.294  1.00 54.24           C  
ANISOU 4660  CG  PHE B 297     5665   8908   6034   -317    433    200       C  
ATOM   4661  CD1 PHE B 297     118.136  64.248  40.475  1.00 59.95           C  
ANISOU 4661  CD1 PHE B 297     6434   9494   6851   -440    375    254       C  
ATOM   4662  CD2 PHE B 297     116.708  63.745  38.642  1.00 51.97           C  
ANISOU 4662  CD2 PHE B 297     5488   8566   5690   -223    397    151       C  
ATOM   4663  CE1 PHE B 297     117.184  65.104  40.989  1.00 59.82           C  
ANISOU 4663  CE1 PHE B 297     6579   9291   6860   -456    296    257       C  
ATOM   4664  CE2 PHE B 297     115.751  64.597  39.153  1.00 53.82           C  
ANISOU 4664  CE2 PHE B 297     5861   8627   5963   -240    317    158       C  
ATOM   4665  CZ  PHE B 297     115.989  65.274  40.330  1.00 51.83           C  
ANISOU 4665  CZ  PHE B 297     5661   8239   5793   -348    272    209       C  
ATOM   4666  N   GLU B 298     121.031  60.149  39.254  1.00 63.24           N  
ANISOU 4666  N   GLU B 298     6297  10539   7193    -93    604     31       N  
ATOM   4667  CA  GLU B 298     121.971  59.153  38.754  1.00 61.83           C  
ANISOU 4667  CA  GLU B 298     5968  10566   6960     44    671    -27       C  
ATOM   4668  C   GLU B 298     121.354  57.763  38.828  1.00 63.99           C  
ANISOU 4668  C   GLU B 298     6302  10757   7255    231    616   -214       C  
ATOM   4669  O   GLU B 298     121.383  57.001  37.854  1.00 63.43           O  
ANISOU 4669  O   GLU B 298     6219  10801   7080    398    651   -303       O  
ATOM   4670  CB  GLU B 298     123.274  59.210  39.559  1.00 65.94           C  
ANISOU 4670  CB  GLU B 298     6320  11177   7557    -36    678     39       C  
ATOM   4671  CG  GLU B 298     124.018  60.544  39.489  1.00 73.02           C  
ANISOU 4671  CG  GLU B 298     7138  12160   8448   -254    720    232       C  
ATOM   4672  CD  GLU B 298     125.166  60.623  40.489  1.00 81.62           C  
ANISOU 4672  CD  GLU B 298     8067  13298   9646   -356    681    284       C  
ATOM   4673  OE1 GLU B 298     125.483  59.587  41.111  1.00 81.89           O  
ANISOU 4673  OE1 GLU B 298     8041  13334   9739   -225    638    169       O  
ATOM   4674  OE2 GLU B 298     125.730  61.724  40.678  1.00 84.87           O  
ANISOU 4674  OE2 GLU B 298     8429  13729  10090   -571    675    438       O  
ATOM   4675  N   VAL B 299     120.755  57.434  39.978  1.00 64.20           N  
ANISOU 4675  N   VAL B 299     6411  10573   7409    200    524   -271       N  
ATOM   4676  CA  VAL B 299     120.140  56.125  40.166  1.00 56.69           C  
ANISOU 4676  CA  VAL B 299     5532   9510   6496    335    461   -427       C  
ATOM   4677  C   VAL B 299     118.932  55.959  39.258  1.00 56.81           C  
ANISOU 4677  C   VAL B 299     5654   9475   6455    396    438   -503       C  
ATOM   4678  O   VAL B 299     118.718  54.891  38.673  1.00 62.81           O  
ANISOU 4678  O   VAL B 299     6447  10242   7177    543    407   -631       O  
ATOM   4679  CB  VAL B 299     119.770  55.932  41.646  1.00 47.03           C  
ANISOU 4679  CB  VAL B 299     4376   8083   5410    258    386   -437       C  
ATOM   4680  CG1 VAL B 299     119.012  54.628  41.845  1.00 50.35           C  
ANISOU 4680  CG1 VAL B 299     4891   8364   5876    358    319   -574       C  
ATOM   4681  CG2 VAL B 299     121.023  55.955  42.490  1.00 41.69           C  
ANISOU 4681  CG2 VAL B 299     3599   7464   4779    227    381   -383       C  
ATOM   4682  N   MET B 300     118.123  57.009  39.123  1.00 56.93           N  
ANISOU 4682  N   MET B 300     5733   9432   6464    294    434   -432       N  
ATOM   4683  CA  MET B 300     116.963  56.930  38.244  1.00 62.72           C  
ANISOU 4683  CA  MET B 300     6555  10132   7146    355    395   -503       C  
ATOM   4684  C   MET B 300     117.381  56.750  36.789  1.00 64.90           C  
ANISOU 4684  C   MET B 300     6812  10594   7254    482    443   -527       C  
ATOM   4685  O   MET B 300     116.729  56.021  36.036  1.00 60.77           O  
ANISOU 4685  O   MET B 300     6350  10060   6679    602    388   -651       O  
ATOM   4686  CB  MET B 300     116.103  58.181  38.405  1.00 53.74           C  
ANISOU 4686  CB  MET B 300     5486   8909   6026    245    376   -418       C  
ATOM   4687  CG  MET B 300     115.163  58.130  39.591  1.00 40.82           C  
ANISOU 4687  CG  MET B 300     3896   7087   4527    181    317   -449       C  
ATOM   4688  SD  MET B 300     114.012  59.507  39.570  1.00 52.20           S  
ANISOU 4688  SD  MET B 300     5422   8448   5964    124    284   -386       S  
ATOM   4689  CE  MET B 300     115.163  60.866  39.700  1.00 45.77           C  
ANISOU 4689  CE  MET B 300     4618   7679   5095      9    334   -212       C  
ATOM   4690  N   ALA B 301     118.467  57.396  36.370  1.00 63.34           N  
ANISOU 4690  N   ALA B 301     6530  10574   6962    454    545   -409       N  
ATOM   4691  CA  ALA B 301     118.892  57.257  34.983  1.00 55.84           C  
ANISOU 4691  CA  ALA B 301     5563   9829   5825    583    616   -419       C  
ATOM   4692  C   ALA B 301     119.497  55.880  34.731  1.00 57.32           C  
ANISOU 4692  C   ALA B 301     5698  10106   5973    776    621   -562       C  
ATOM   4693  O   ALA B 301     119.156  55.211  33.750  1.00 62.95           O  
ANISOU 4693  O   ALA B 301     6483  10867   6569    943    595   -682       O  
ATOM   4694  CB  ALA B 301     119.879  58.364  34.619  1.00 52.76           C  
ANISOU 4694  CB  ALA B 301     5085   9618   5344    475    740   -229       C  
ATOM   4695  N   ARG B 302     120.385  55.432  35.621  1.00 56.48           N  
ANISOU 4695  N   ARG B 302     5486  10014   5961    771    636   -562       N  
ATOM   4696  CA  ARG B 302     121.075  54.163  35.409  1.00 62.15           C  
ANISOU 4696  CA  ARG B 302     6158  10821   6635    979    635   -696       C  
ATOM   4697  C   ARG B 302     120.112  52.984  35.471  1.00 67.82           C  
ANISOU 4697  C   ARG B 302     7030  11333   7404   1090    495   -880       C  
ATOM   4698  O   ARG B 302     120.212  52.051  34.668  1.00 75.35           O  
ANISOU 4698  O   ARG B 302     8034  12343   8251   1297    470  -1020       O  
ATOM   4699  CB  ARG B 302     122.182  53.993  36.447  1.00 47.92           C  
ANISOU 4699  CB  ARG B 302     4212   9061   4934    949    655   -652       C  
ATOM   4700  CG  ARG B 302     122.953  52.702  36.330  1.00 49.82           C  
ANISOU 4700  CG  ARG B 302     4406   9387   5136   1188    642   -791       C  
ATOM   4701  CD  ARG B 302     123.959  52.581  37.456  1.00 74.42           C  
ANISOU 4701  CD  ARG B 302     7384  12526   8366   1155    634   -747       C  
ATOM   4702  NE  ARG B 302     125.181  51.903  37.043  1.00 95.85           N  
ANISOU 4702  NE  ARG B 302     9945  15483  10992   1375    695   -805       N  
ATOM   4703  CZ  ARG B 302     126.227  51.706  37.839  1.00113.38           C  
ANISOU 4703  CZ  ARG B 302    12010  17783  13287   1400    687   -782       C  
ATOM   4704  NH1 ARG B 302     126.192  52.112  39.105  1.00115.54           N  
ANISOU 4704  NH1 ARG B 302    12285  17897  13719   1213    613   -705       N  
ATOM   4705  NH2 ARG B 302     127.302  51.087  37.374  1.00120.19           N  
ANISOU 4705  NH2 ARG B 302    12716  18893  14057   1631    746   -846       N  
ATOM   4706  N   HIS B 303     119.180  53.000  36.417  1.00 68.84           N  
ANISOU 4706  N   HIS B 303     7240  11225   7692    954    402   -883       N  
ATOM   4707  CA  HIS B 303     118.233  51.906  36.592  1.00 67.56           C  
ANISOU 4707  CA  HIS B 303     7210  10855   7605   1006    269  -1033       C  
ATOM   4708  C   HIS B 303     116.824  52.334  36.190  1.00 67.06           C  
ANISOU 4708  C   HIS B 303     7234  10690   7555    923    206  -1046       C  
ATOM   4709  O   HIS B 303     115.833  51.919  36.793  1.00 73.64           O  
ANISOU 4709  O   HIS B 303     8135  11329   8518    844    112  -1095       O  
ATOM   4710  CB  HIS B 303     118.260  51.393  38.029  1.00 69.15           C  
ANISOU 4710  CB  HIS B 303     7426  10875   7973    927    214  -1030       C  
ATOM   4711  CG  HIS B 303     119.640  51.118  38.543  1.00 81.00           C  
ANISOU 4711  CG  HIS B 303     8827  12478   9472   1000    259  -1004       C  
ATOM   4712  ND1 HIS B 303     120.337  49.969  38.236  1.00 85.56           N  
ANISOU 4712  ND1 HIS B 303     9417  13096   9995   1214    223  -1127       N  
ATOM   4713  CD2 HIS B 303     120.438  51.830  39.375  1.00 82.22           C  
ANISOU 4713  CD2 HIS B 303     8867  12696   9677    898    317   -879       C  
ATOM   4714  CE1 HIS B 303     121.514  49.997  38.837  1.00 86.09           C  
ANISOU 4714  CE1 HIS B 303     9361  13269  10079   1248    266  -1074       C  
ATOM   4715  NE2 HIS B 303     121.599  51.114  39.537  1.00 81.79           N  
ANISOU 4715  NE2 HIS B 303     8734  12738   9602   1046    319   -923       N  
ATOM   4716  N   CYS B 304     116.729  53.169  35.151  1.00 62.58           N  
ANISOU 4716  N   CYS B 304     6661  10265   6851    942    259   -996       N  
ATOM   4717  CA  CYS B 304     115.429  53.586  34.635  1.00 61.46           C  
ANISOU 4717  CA  CYS B 304     6599  10051   6703    900    184  -1018       C  
ATOM   4718  C   CYS B 304     114.600  52.397  34.169  1.00 62.13           C  
ANISOU 4718  C   CYS B 304     6784  10022   6802    999     39  -1202       C  
ATOM   4719  O   CYS B 304     113.369  52.421  34.272  1.00 68.28           O  
ANISOU 4719  O   CYS B 304     7601  10672   7671    920    -61  -1240       O  
ATOM   4720  CB  CYS B 304     115.621  54.587  33.491  1.00 63.96           C  
ANISOU 4720  CB  CYS B 304     6919  10546   6835    937    258   -933       C  
ATOM   4721  SG  CYS B 304     114.097  55.161  32.716  1.00 69.79           S  
ANISOU 4721  SG  CYS B 304     7761  11219   7535    927    148   -962       S  
ATOM   4722  N   CYS B 305     115.248  51.350  33.659  1.00 72.63           N  
ANISOU 4722  N   CYS B 305     8153  11395   8046   1173     16  -1322       N  
ATOM   4723  CA  CYS B 305     114.516  50.154  33.256  1.00 85.82           C  
ANISOU 4723  CA  CYS B 305     9947  12925   9738   1260   -150  -1507       C  
ATOM   4724  C   CYS B 305     113.890  49.461  34.461  1.00 89.65           C  
ANISOU 4724  C   CYS B 305    10453  13168  10443   1120   -242  -1532       C  
ATOM   4725  O   CYS B 305     112.688  49.172  34.470  1.00 97.08           O  
ANISOU 4725  O   CYS B 305    11441  13964  11481   1031   -365  -1593       O  
ATOM   4726  CB  CYS B 305     115.443  49.195  32.504  1.00 99.20           C  
ANISOU 4726  CB  CYS B 305    11702  14710  11279   1506   -157  -1636       C  
ATOM   4727  SG  CYS B 305     114.611  47.732  31.821  1.00110.28           S  
ANISOU 4727  SG  CYS B 305    13305  15923  12675   1636   -394  -1884       S  
ATOM   4728  N   GLU B 306     114.689  49.193  35.495  1.00 86.42           N  
ANISOU 4728  N   GLU B 306    10004  12720  10112   1093   -183  -1478       N  
ATOM   4729  CA  GLU B 306     114.183  48.427  36.630  1.00 69.79           C  
ANISOU 4729  CA  GLU B 306     7947  10384   8188    974   -264  -1494       C  
ATOM   4730  C   GLU B 306     113.224  49.259  37.475  1.00 65.96           C  
ANISOU 4730  C   GLU B 306     7397   9829   7835    754   -234  -1379       C  
ATOM   4731  O   GLU B 306     112.141  48.791  37.844  1.00 73.17           O  
ANISOU 4731  O   GLU B 306     8345  10583   8872    639   -324  -1414       O  
ATOM   4732  CB  GLU B 306     115.345  47.909  37.474  1.00 56.86           C  
ANISOU 4732  CB  GLU B 306     6302   8728   6574   1033   -223  -1471       C  
ATOM   4733  CG  GLU B 306     116.325  47.033  36.711  1.00 61.18           C  
ANISOU 4733  CG  GLU B 306     6904   9354   6989   1287   -252  -1597       C  
ATOM   4734  CD  GLU B 306     117.431  47.834  36.048  1.00 77.35           C  
ANISOU 4734  CD  GLU B 306     8820  11694   8875   1407   -103  -1536       C  
ATOM   4735  OE1 GLU B 306     117.147  48.948  35.563  1.00 82.54           O  
ANISOU 4735  OE1 GLU B 306     9406  12480   9475   1325    -22  -1444       O  
ATOM   4736  OE2 GLU B 306     118.584  47.348  36.007  1.00 85.15           O  
ANISOU 4736  OE2 GLU B 306     9773  12786   9792   1583    -68  -1574       O  
ATOM   4737  N   ILE B 307     113.600  50.500  37.786  1.00 62.26           N  
ANISOU 4737  N   ILE B 307     6833   9482   7340    693   -109  -1240       N  
ATOM   4738  CA  ILE B 307     112.748  51.343  38.620  1.00 60.94           C  
ANISOU 4738  CA  ILE B 307     6619   9255   7279    521    -78  -1140       C  
ATOM   4739  C   ILE B 307     111.457  51.687  37.890  1.00 64.75           C  
ANISOU 4739  C   ILE B 307     7100   9737   7765    493   -147  -1182       C  
ATOM   4740  O   ILE B 307     110.373  51.705  38.489  1.00 69.16           O  
ANISOU 4740  O   ILE B 307     7634  10199   8446    373   -181  -1174       O  
ATOM   4741  CB  ILE B 307     113.507  52.612  39.053  1.00 52.36           C  
ANISOU 4741  CB  ILE B 307     5462   8279   6153    476     44   -993       C  
ATOM   4742  CG1 ILE B 307     114.695  52.237  39.947  1.00 46.11           C  
ANISOU 4742  CG1 ILE B 307     4654   7479   5387    486     87   -954       C  
ATOM   4743  CG2 ILE B 307     112.570  53.581  39.759  1.00 46.32           C  
ANISOU 4743  CG2 ILE B 307     4675   7458   5468    340     65   -909       C  
ATOM   4744  CD1 ILE B 307     115.611  53.399  40.295  1.00 40.42           C  
ANISOU 4744  CD1 ILE B 307     3857   6873   4628    436    183   -820       C  
ATOM   4745  N   GLY B 308     111.547  51.949  36.585  1.00 61.48           N  
ANISOU 4745  N   GLY B 308     6706   9445   7208    610   -168  -1229       N  
ATOM   4746  CA  GLY B 308     110.379  52.333  35.813  1.00 58.34           C  
ANISOU 4746  CA  GLY B 308     6311   9061   6795    607   -252  -1272       C  
ATOM   4747  C   GLY B 308     109.326  51.251  35.710  1.00 63.61           C  
ANISOU 4747  C   GLY B 308     7007   9593   7569    572   -407  -1405       C  
ATOM   4748  O   GLY B 308     108.161  51.555  35.433  1.00 63.97           O  
ANISOU 4748  O   GLY B 308     7012   9630   7663    523   -486  -1430       O  
ATOM   4749  N   GLN B 309     109.700  49.997  35.934  1.00 69.54           N  
ANISOU 4749  N   GLN B 309     7826  10233   8363    593   -464  -1489       N  
ATOM   4750  CA  GLN B 309     108.754  48.897  35.833  1.00 79.58           C  
ANISOU 4750  CA  GLN B 309     9145  11348   9744    535   -629  -1611       C  
ATOM   4751  C   GLN B 309     108.092  48.555  37.162  1.00 77.24           C  
ANISOU 4751  C   GLN B 309     8797  10904   9647    333   -619  -1547       C  
ATOM   4752  O   GLN B 309     107.256  47.647  37.203  1.00 75.91           O  
ANISOU 4752  O   GLN B 309     8653  10595   9594    236   -750  -1622       O  
ATOM   4753  CB  GLN B 309     109.452  47.664  35.259  1.00 97.18           C  
ANISOU 4753  CB  GLN B 309    11517  13507  11899    679   -726  -1749       C  
ATOM   4754  CG  GLN B 309     109.972  47.898  33.850  1.00113.05           C  
ANISOU 4754  CG  GLN B 309    13586  15678  13691    894   -740  -1829       C  
ATOM   4755  CD  GLN B 309     110.410  46.630  33.164  1.00122.96           C  
ANISOU 4755  CD  GLN B 309    14999  16856  14863   1063   -869  -2002       C  
ATOM   4756  OE1 GLN B 309     109.645  45.671  33.064  1.00125.39           O  
ANISOU 4756  OE1 GLN B 309    15398  16981  15265   1010  -1054  -2122       O  
ATOM   4757  NE2 GLN B 309     111.651  46.612  32.688  1.00124.83           N  
ANISOU 4757  NE2 GLN B 309    15272  17234  14924   1269   -778  -2019       N  
ATOM   4758  N   SER B 310     108.425  49.265  38.238  1.00 79.56           N  
ANISOU 4758  N   SER B 310     9026  11225   9978    261   -471  -1407       N  
ATOM   4759  CA  SER B 310     107.836  49.015  39.545  1.00 83.39           C  
ANISOU 4759  CA  SER B 310     9471  11594  10620     84   -435  -1333       C  
ATOM   4760  C   SER B 310     106.661  49.952  39.791  1.00 74.78           C  
ANISOU 4760  C   SER B 310     8244  10573   9596    -15   -398  -1274       C  
ATOM   4761  O   SER B 310     106.622  51.077  39.281  1.00 66.57           O  
ANISOU 4761  O   SER B 310     7155   9667   8472     59   -359  -1246       O  
ATOM   4762  CB  SER B 310     108.859  49.200  40.662  1.00 87.54           C  
ANISOU 4762  CB  SER B 310    10022  12103  11136     80   -309  -1226       C  
ATOM   4763  OG  SER B 310     108.987  50.573  40.977  1.00 88.06           O  
ANISOU 4763  OG  SER B 310    10009  12293  11158     77   -191  -1121       O  
ATOM   4764  N   ARG B 311     105.715  49.485  40.612  1.00 72.00           N  
ANISOU 4764  N   ARG B 311     7833  10131   9393   -179   -405  -1247       N  
ATOM   4765  CA  ARG B 311     104.510  50.268  40.863  1.00 71.81           C  
ANISOU 4765  CA  ARG B 311     7654  10193   9440   -257   -370  -1204       C  
ATOM   4766  C   ARG B 311     104.847  51.580  41.561  1.00 73.38           C  
ANISOU 4766  C   ARG B 311     7820  10486   9577   -213   -217  -1090       C  
ATOM   4767  O   ARG B 311     104.229  52.616  41.288  1.00 69.45           O  
ANISOU 4767  O   ARG B 311     7236  10098   9055   -168   -203  -1077       O  
ATOM   4768  CB  ARG B 311     103.514  49.460  41.699  1.00 75.58           C  
ANISOU 4768  CB  ARG B 311     8057  10577  10084   -455   -379  -1178       C  
ATOM   4769  CG  ARG B 311     102.163  50.155  41.849  1.00 93.74           C  
ANISOU 4769  CG  ARG B 311    10156  12997  12465   -522   -352  -1153       C  
ATOM   4770  CD  ARG B 311     101.211  49.467  42.827  1.00 98.88           C  
ANISOU 4770  CD  ARG B 311    10699  13595  13274   -735   -312  -1092       C  
ATOM   4771  NE  ARG B 311      99.864  50.027  42.719  1.00 93.05           N  
ANISOU 4771  NE  ARG B 311     9733  13005  12618   -777   -314  -1097       N  
ATOM   4772  CZ  ARG B 311      99.470  51.148  43.314  1.00 84.72           C  
ANISOU 4772  CZ  ARG B 311     8565  12091  11534   -717   -178  -1029       C  
ATOM   4773  NH1 ARG B 311     100.327  51.843  44.050  1.00 82.45           N  
ANISOU 4773  NH1 ARG B 311     8386  11800  11139   -629    -41   -950       N  
ATOM   4774  NH2 ARG B 311      98.229  51.586  43.157  1.00 77.73           N  
ANISOU 4774  NH2 ARG B 311     7459  11351  10724   -732   -195  -1048       N  
ATOM   4775  N   PHE B 312     105.834  51.558  42.454  1.00 72.29           N  
ANISOU 4775  N   PHE B 312     7763  10296   9408   -216   -122  -1015       N  
ATOM   4776  CA  PHE B 312     106.184  52.740  43.228  1.00 59.97           C  
ANISOU 4776  CA  PHE B 312     6196   8796   7795   -190      1   -912       C  
ATOM   4777  C   PHE B 312     107.278  53.566  42.566  1.00 60.02           C  
ANISOU 4777  C   PHE B 312     6260   8878   7668    -67     13   -898       C  
ATOM   4778  O   PHE B 312     107.171  54.797  42.504  1.00 59.18           O  
ANISOU 4778  O   PHE B 312     6134   8846   7507    -26     53   -848       O  
ATOM   4779  CB  PHE B 312     106.626  52.333  44.634  1.00 53.77           C  
ANISOU 4779  CB  PHE B 312     5469   7917   7046   -269     86   -833       C  
ATOM   4780  CG  PHE B 312     105.579  51.587  45.405  1.00 56.12           C  
ANISOU 4780  CG  PHE B 312     5713   8149   7462   -412    105   -812       C  
ATOM   4781  CD1 PHE B 312     105.788  50.276  45.799  1.00 59.40           C  
ANISOU 4781  CD1 PHE B 312     6211   8422   7936   -499     68   -815       C  
ATOM   4782  CD2 PHE B 312     104.382  52.198  45.735  1.00 64.42           C  
ANISOU 4782  CD2 PHE B 312     6630   9284   8562   -458    162   -784       C  
ATOM   4783  CE1 PHE B 312     104.821  49.589  46.516  1.00 65.17           C  
ANISOU 4783  CE1 PHE B 312     6896   9090   8775   -661     94   -772       C  
ATOM   4784  CE2 PHE B 312     103.411  51.519  46.450  1.00 68.81           C  
ANISOU 4784  CE2 PHE B 312     7109   9810   9226   -606    201   -749       C  
ATOM   4785  CZ  PHE B 312     103.630  50.212  46.842  1.00 67.23           C  
ANISOU 4785  CZ  PHE B 312     6996   9462   9087   -724    170   -734       C  
ATOM   4786  N   GLY B 313     108.329  52.908  42.071  1.00 59.34           N  
ANISOU 4786  N   GLY B 313     6246   8775   7525     -7    -20   -936       N  
ATOM   4787  CA  GLY B 313     109.442  53.641  41.489  1.00 61.98           C  
ANISOU 4787  CA  GLY B 313     6611   9206   7733     90     14   -904       C  
ATOM   4788  C   GLY B 313     109.027  54.508  40.318  1.00 62.84           C  
ANISOU 4788  C   GLY B 313     6697   9422   7757    160    -17   -920       C  
ATOM   4789  O   GLY B 313     109.459  55.657  40.202  1.00 60.95           O  
ANISOU 4789  O   GLY B 313     6468   9252   7438    184     35   -839       O  
ATOM   4790  N   ALA B 314     108.175  53.973  39.439  1.00 66.40           N  
ANISOU 4790  N   ALA B 314     7132   9876   8220    189   -119  -1021       N  
ATOM   4791  CA  ALA B 314     107.697  54.758  38.306  1.00 69.90           C  
ANISOU 4791  CA  ALA B 314     7569  10417   8573    269   -169  -1041       C  
ATOM   4792  C   ALA B 314     106.945  55.994  38.776  1.00 58.78           C  
ANISOU 4792  C   ALA B 314     6114   9031   7190    242   -134   -965       C  
ATOM   4793  O   ALA B 314     107.157  57.096  38.254  1.00 56.35           O  
ANISOU 4793  O   ALA B 314     5847   8789   6776    304   -119   -907       O  
ATOM   4794  CB  ALA B 314     106.815  53.896  37.404  1.00 80.26           C  
ANISOU 4794  CB  ALA B 314     8871  11715   9911    297   -313  -1176       C  
ATOM   4795  N   ARG B 315     106.072  55.836  39.772  1.00 55.42           N  
ANISOU 4795  N   ARG B 315     5612   8549   6895    155   -117   -960       N  
ATOM   4796  CA  ARG B 315     105.372  56.992  40.317  1.00 52.45           C  
ANISOU 4796  CA  ARG B 315     5194   8200   6534    160    -77   -899       C  
ATOM   4797  C   ARG B 315     106.322  57.933  41.046  1.00 51.65           C  
ANISOU 4797  C   ARG B 315     5175   8079   6372    158     20   -789       C  
ATOM   4798  O   ARG B 315     106.126  59.155  41.014  1.00 54.56           O  
ANISOU 4798  O   ARG B 315     5577   8467   6684    210     26   -738       O  
ATOM   4799  CB  ARG B 315     104.249  56.528  41.239  1.00 50.73           C  
ANISOU 4799  CB  ARG B 315     4859   7957   6460     74    -59   -918       C  
ATOM   4800  CG  ARG B 315     103.063  55.996  40.467  1.00 57.55           C  
ANISOU 4800  CG  ARG B 315     5610   8862   7394     70   -177  -1017       C  
ATOM   4801  CD  ARG B 315     102.217  55.048  41.284  1.00 62.94           C  
ANISOU 4801  CD  ARG B 315     6172   9509   8234    -70   -161  -1032       C  
ATOM   4802  NE  ARG B 315     101.044  54.632  40.526  1.00 66.63           N  
ANISOU 4802  NE  ARG B 315     6506  10028   8782    -90   -292  -1124       N  
ATOM   4803  CZ  ARG B 315     101.040  53.647  39.633  1.00 69.63           C  
ANISOU 4803  CZ  ARG B 315     6913  10360   9181   -118   -430  -1220       C  
ATOM   4804  NH1 ARG B 315     102.148  52.960  39.392  1.00 67.39           N  
ANISOU 4804  NH1 ARG B 315     6784   9985   8836   -108   -441  -1238       N  
ATOM   4805  NH2 ARG B 315      99.923  53.344  38.983  1.00 73.32           N  
ANISOU 4805  NH2 ARG B 315     7252  10876   9730   -144   -568  -1307       N  
ATOM   4806  N   ALA B 316     107.361  57.393  41.690  1.00 44.55           N  
ANISOU 4806  N   ALA B 316     4318   7129   5480    103     78   -754       N  
ATOM   4807  CA  ALA B 316     108.345  58.252  42.338  1.00 53.23           C  
ANISOU 4807  CA  ALA B 316     5489   8210   6526     89    144   -655       C  
ATOM   4808  C   ALA B 316     109.217  58.976  41.318  1.00 61.03           C  
ANISOU 4808  C   ALA B 316     6532   9266   7392    137    134   -609       C  
ATOM   4809  O   ALA B 316     109.662  60.101  41.577  1.00 62.80           O  
ANISOU 4809  O   ALA B 316     6817   9479   7566    122    158   -520       O  
ATOM   4810  CB  ALA B 316     109.211  57.436  43.299  1.00 48.84           C  
ANISOU 4810  CB  ALA B 316     4952   7592   6013     26    190   -636       C  
ATOM   4811  N   ILE B 317     109.477  58.351  40.165  1.00 61.14           N  
ANISOU 4811  N   ILE B 317     6536   9346   7347    191     97   -666       N  
ATOM   4812  CA  ILE B 317     110.203  59.033  39.095  1.00 57.66           C  
ANISOU 4812  CA  ILE B 317     6143   8997   6769    240    104   -612       C  
ATOM   4813  C   ILE B 317     109.392  60.216  38.581  1.00 60.49           C  
ANISOU 4813  C   ILE B 317     6550   9363   7071    281     60   -577       C  
ATOM   4814  O   ILE B 317     109.915  61.327  38.424  1.00 64.21           O  
ANISOU 4814  O   ILE B 317     7094   9841   7461    264     84   -469       O  
ATOM   4815  CB  ILE B 317     110.550  58.049  37.961  1.00 52.57           C  
ANISOU 4815  CB  ILE B 317     5490   8433   6052    321     75   -697       C  
ATOM   4816  CG1 ILE B 317     111.636  57.072  38.403  1.00 50.29           C  
ANISOU 4816  CG1 ILE B 317     5175   8145   5787    311    120   -715       C  
ATOM   4817  CG2 ILE B 317     110.987  58.792  36.704  1.00 50.59           C  
ANISOU 4817  CG2 ILE B 317     5292   8297   5633    387     86   -643       C  
ATOM   4818  CD1 ILE B 317     111.948  56.032  37.364  1.00 40.86           C  
ANISOU 4818  CD1 ILE B 317     3990   7018   4517    422     84   -821       C  
ATOM   4819  N   ARG B 318     108.103  59.994  38.303  1.00 54.43           N  
ANISOU 4819  N   ARG B 318     5743   8589   6349    333    -17   -665       N  
ATOM   4820  CA  ARG B 318     107.232  61.096  37.908  1.00 51.96           C  
ANISOU 4820  CA  ARG B 318     5471   8280   5992    400    -76   -644       C  
ATOM   4821  C   ARG B 318     107.313  62.235  38.912  1.00 56.79           C  
ANISOU 4821  C   ARG B 318     6141   8815   6621    365    -33   -549       C  
ATOM   4822  O   ARG B 318     107.474  63.401  38.530  1.00 54.05           O  
ANISOU 4822  O   ARG B 318     5905   8451   6181    396    -55   -468       O  
ATOM   4823  CB  ARG B 318     105.786  60.604  37.762  1.00 48.79           C  
ANISOU 4823  CB  ARG B 318     4970   7891   5676    448   -165   -759       C  
ATOM   4824  CG  ARG B 318     104.870  61.590  37.053  1.00 47.80           C  
ANISOU 4824  CG  ARG B 318     4877   7796   5487    561   -258   -764       C  
ATOM   4825  CD  ARG B 318     103.458  61.629  37.633  1.00 66.00           C  
ANISOU 4825  CD  ARG B 318     7055  10106   7915    592   -303   -831       C  
ATOM   4826  NE  ARG B 318     102.731  60.369  37.461  1.00 84.96           N  
ANISOU 4826  NE  ARG B 318     9311  12545  10426    553   -361   -947       N  
ATOM   4827  CZ  ARG B 318     102.219  59.646  38.455  1.00 88.11           C  
ANISOU 4827  CZ  ARG B 318     9578  12927  10974    458   -314   -977       C  
ATOM   4828  NH1 ARG B 318     102.358  60.040  39.718  1.00 83.39           N  
ANISOU 4828  NH1 ARG B 318     8978  12287  10419    414   -198   -908       N  
ATOM   4829  NH2 ARG B 318     101.571  58.521  38.183  1.00 86.18           N  
ANISOU 4829  NH2 ARG B 318     9215  12700  10828    401   -388  -1073       N  
ATOM   4830  N   ALA B 319     107.246  61.904  40.206  1.00 56.96           N  
ANISOU 4830  N   ALA B 319     6113   8777   6750    301     21   -556       N  
ATOM   4831  CA  ALA B 319     107.281  62.920  41.253  1.00 50.51           C  
ANISOU 4831  CA  ALA B 319     5369   7880   5943    285     50   -488       C  
ATOM   4832  C   ALA B 319     108.607  63.671  41.258  1.00 60.71           C  
ANISOU 4832  C   ALA B 319     6775   9135   7158    218     74   -373       C  
ATOM   4833  O   ALA B 319     108.629  64.903  41.369  1.00 68.20           O  
ANISOU 4833  O   ALA B 319     7843  10016   8054    231     42   -303       O  
ATOM   4834  CB  ALA B 319     107.029  62.266  42.609  1.00 47.22           C  
ANISOU 4834  CB  ALA B 319     4885   7422   5633    232    113   -518       C  
ATOM   4835  N   CYS B 320     109.723  62.941  41.147  1.00 57.73           N  
ANISOU 4835  N   CYS B 320     6361   8800   6776    145    121   -353       N  
ATOM   4836  CA  CYS B 320     111.039  63.574  41.108  1.00 53.43           C  
ANISOU 4836  CA  CYS B 320     5878   8253   6170     62    147   -238       C  
ATOM   4837  C   CYS B 320     111.170  64.511  39.911  1.00 58.92           C  
ANISOU 4837  C   CYS B 320     6659   8985   6744     82    117   -159       C  
ATOM   4838  O   CYS B 320     111.720  65.612  40.034  1.00 65.22           O  
ANISOU 4838  O   CYS B 320     7560   9721   7497     11    105    -45       O  
ATOM   4839  CB  CYS B 320     112.134  62.507  41.062  1.00 53.37           C  
ANISOU 4839  CB  CYS B 320     5779   8324   6176     17    202   -248       C  
ATOM   4840  SG  CYS B 320     112.389  61.558  42.575  1.00 57.62           S  
ANISOU 4840  SG  CYS B 320     6265   8795   6834    -30    229   -295       S  
ATOM   4841  N   LEU B 321     110.674  64.090  38.743  1.00 53.17           N  
ANISOU 4841  N   LEU B 321     5905   8345   5952    172     95   -215       N  
ATOM   4842  CA  LEU B 321     110.833  64.912  37.549  1.00 52.65           C  
ANISOU 4842  CA  LEU B 321     5938   8323   5744    198     72   -130       C  
ATOM   4843  C   LEU B 321     109.970  66.165  37.620  1.00 56.05           C  
ANISOU 4843  C   LEU B 321     6504   8641   6151    248    -13    -93       C  
ATOM   4844  O   LEU B 321     110.353  67.212  37.084  1.00 54.90           O  
ANISOU 4844  O   LEU B 321     6495   8462   5901    216    -33     31       O  
ATOM   4845  CB  LEU B 321     110.498  64.098  36.299  1.00 46.26           C  
ANISOU 4845  CB  LEU B 321     5086   7636   4855    304     54   -214       C  
ATOM   4846  CG  LEU B 321     111.480  62.970  35.957  1.00 53.85           C  
ANISOU 4846  CG  LEU B 321     5951   8717   5792    292    130   -246       C  
ATOM   4847  CD1 LEU B 321     110.924  62.095  34.845  1.00 56.98           C  
ANISOU 4847  CD1 LEU B 321     6331   9201   6119    422     80   -368       C  
ATOM   4848  CD2 LEU B 321     112.875  63.485  35.600  1.00 51.76           C  
ANISOU 4848  CD2 LEU B 321     5701   8540   5426    206    223    -99       C  
ATOM   4849  N   GLU B 322     108.821  66.087  38.290  1.00 51.90           N  
ANISOU 4849  N   GLU B 322     5946   8057   5716    328    -61   -191       N  
ATOM   4850  CA  GLU B 322     107.960  67.248  38.485  1.00 51.98           C  
ANISOU 4850  CA  GLU B 322     6077   7965   5708    413   -144   -177       C  
ATOM   4851  C   GLU B 322     108.382  68.109  39.668  1.00 51.68           C  
ANISOU 4851  C   GLU B 322     6144   7787   5706    342   -138   -109       C  
ATOM   4852  O   GLU B 322     107.750  69.140  39.921  1.00 59.45           O  
ANISOU 4852  O   GLU B 322     7258   8664   6667    428   -214   -100       O  
ATOM   4853  CB  GLU B 322     106.508  66.793  38.649  1.00 54.11           C  
ANISOU 4853  CB  GLU B 322     6235   8269   6054    547   -192   -316       C  
ATOM   4854  CG  GLU B 322     105.798  66.597  37.320  1.00 76.12           C  
ANISOU 4854  CG  GLU B 322     9004  11147   8772    661   -276   -372       C  
ATOM   4855  CD  GLU B 322     104.545  65.756  37.434  1.00 86.25           C  
ANISOU 4855  CD  GLU B 322    10109  12502  10161    740   -317   -518       C  
ATOM   4856  OE1 GLU B 322     104.259  65.259  38.546  1.00 86.04           O  
ANISOU 4856  OE1 GLU B 322     9968  12463  10259    695   -256   -565       O  
ATOM   4857  OE2 GLU B 322     103.841  65.601  36.410  1.00 86.60           O  
ANISOU 4857  OE2 GLU B 322    10128  12616  10161    841   -414   -581       O  
ATOM   4858  N   ASN B 323     109.443  67.737  40.377  1.00 47.08           N  
ANISOU 4858  N   ASN B 323     5521   7197   5171    204    -67    -67       N  
ATOM   4859  CA  ASN B 323     109.824  68.452  41.582  1.00 54.43           C  
ANISOU 4859  CA  ASN B 323     6551   7991   6139    139    -81    -23       C  
ATOM   4860  C   ASN B 323     110.555  69.744  41.248  1.00 59.00           C  
ANISOU 4860  C   ASN B 323     7320   8463   6636     50   -142    120       C  
ATOM   4861  O   ASN B 323     111.381  69.789  40.333  1.00 56.01           O  
ANISOU 4861  O   ASN B 323     6937   8151   6192    -45   -115    220       O  
ATOM   4862  CB  ASN B 323     110.707  67.581  42.467  1.00 55.05           C  
ANISOU 4862  CB  ASN B 323     6522   8099   6296     26     -7    -32       C  
ATOM   4863  CG  ASN B 323     110.905  68.183  43.831  1.00 53.74           C  
ANISOU 4863  CG  ASN B 323     6458   7795   6167    -12    -36    -20       C  
ATOM   4864  OD1 ASN B 323     111.852  68.933  44.067  1.00 53.79           O  
ANISOU 4864  OD1 ASN B 323     6568   7718   6153   -130    -76     77       O  
ATOM   4865  ND2 ASN B 323     109.992  67.876  44.738  1.00 55.73           N  
ANISOU 4865  ND2 ASN B 323     6683   8026   6467     85    -19   -116       N  
ATOM   4866  N   GLU B 324     110.273  70.792  42.023  1.00 70.01           N  
ANISOU 4866  N   GLU B 324     8885   9686   8030     78   -223    133       N  
ATOM   4867  CA  GLU B 324     110.858  72.095  41.742  1.00 72.54           C  
ANISOU 4867  CA  GLU B 324     9423   9859   8278    -14   -309    271       C  
ATOM   4868  C   GLU B 324     112.358  72.148  41.999  1.00 69.46           C  
ANISOU 4868  C   GLU B 324     9017   9462   7913   -250   -281    390       C  
ATOM   4869  O   GLU B 324     112.995  73.128  41.600  1.00 78.79           O  
ANISOU 4869  O   GLU B 324    10350  10546   9041   -380   -341    532       O  
ATOM   4870  CB  GLU B 324     110.157  73.174  42.566  1.00 82.28           C  
ANISOU 4870  CB  GLU B 324    10868  10891   9503     98   -424    234       C  
ATOM   4871  CG  GLU B 324     110.212  72.931  44.055  1.00100.35           C  
ANISOU 4871  CG  GLU B 324    13135  13126  11867     99   -408    153       C  
ATOM   4872  CD  GLU B 324     109.793  74.146  44.857  1.00115.42           C  
ANISOU 4872  CD  GLU B 324    15298  14816  13740    195   -534    131       C  
ATOM   4873  OE1 GLU B 324     109.531  75.204  44.244  1.00121.44           O  
ANISOU 4873  OE1 GLU B 324    16265  15449  14429    247   -644    188       O  
ATOM   4874  OE2 GLU B 324     109.732  74.041  46.101  1.00117.83           O  
ANISOU 4874  OE2 GLU B 324    15619  15073  14080    231   -528     56       O  
ATOM   4875  N   ASN B 325     112.940  71.138  42.642  1.00 62.46           N  
ANISOU 4875  N   ASN B 325     7950   8675   7107   -314   -200    343       N  
ATOM   4876  CA  ASN B 325     114.368  71.146  42.926  1.00 65.65           C  
ANISOU 4876  CA  ASN B 325     8304   9097   7545   -524   -183    445       C  
ATOM   4877  C   ASN B 325     115.179  70.352  41.922  1.00 64.02           C  
ANISOU 4877  C   ASN B 325     7907   9104   7312   -597    -73    501       C  
ATOM   4878  O   ASN B 325     116.390  70.194  42.110  1.00 62.43           O  
ANISOU 4878  O   ASN B 325     7605   8970   7146   -755    -41    577       O  
ATOM   4879  CB  ASN B 325     114.645  70.600  44.323  1.00 67.46           C  
ANISOU 4879  CB  ASN B 325     8471   9295   7866   -540   -182    364       C  
ATOM   4880  CG  ASN B 325     114.028  71.441  45.389  1.00 65.98           C  
ANISOU 4880  CG  ASN B 325     8485   8904   7682   -472   -286    314       C  
ATOM   4881  OD1 ASN B 325     114.467  72.566  45.636  1.00 65.74           O  
ANISOU 4881  OD1 ASN B 325     8639   8708   7633   -571   -398    396       O  
ATOM   4882  ND2 ASN B 325     113.012  70.903  46.049  1.00 68.72           N  
ANISOU 4882  ND2 ASN B 325     8801   9260   8048   -302   -253    181       N  
ATOM   4883  N   ALA B 326     114.544  69.832  40.882  1.00 62.70           N  
ANISOU 4883  N   ALA B 326     7684   9057   7083   -473    -21    457       N  
ATOM   4884  CA  ALA B 326     115.245  69.109  39.835  1.00 55.20           C  
ANISOU 4884  CA  ALA B 326     6582   8315   6077   -503     83    498       C  
ATOM   4885  C   ALA B 326     115.676  70.107  38.767  1.00 56.37           C  
ANISOU 4885  C   ALA B 326     6843   8471   6104   -599     80    670       C  
ATOM   4886  O   ALA B 326     114.843  70.855  38.241  1.00 46.64           O  
ANISOU 4886  O   ALA B 326     5785   7140   4796   -521     10    690       O  
ATOM   4887  CB  ALA B 326     114.345  68.025  39.249  1.00 43.17           C  
ANISOU 4887  CB  ALA B 326     4965   6903   4535   -320    121    356       C  
ATOM   4888  N   THR B 327     116.974  70.144  38.470  1.00 57.91           N  
ANISOU 4888  N   THR B 327     6940   8784   6280   -770    154    800       N  
ATOM   4889  CA  THR B 327     117.457  71.042  37.431  1.00 62.18           C  
ANISOU 4889  CA  THR B 327     7575   9353   6697   -890    176    990       C  
ATOM   4890  C   THR B 327     117.112  70.480  36.057  1.00 62.21           C  
ANISOU 4890  C   THR B 327     7542   9540   6555   -747    262    971       C  
ATOM   4891  O   THR B 327     116.836  69.287  35.900  1.00 64.66           O  
ANISOU 4891  O   THR B 327     7710   9985   6874   -594    317    821       O  
ATOM   4892  CB  THR B 327     118.970  71.255  37.537  1.00 62.30           C  
ANISOU 4892  CB  THR B 327     7460   9470   6741  -1135    241   1148       C  
ATOM   4893  OG1 THR B 327     119.655  70.008  37.345  1.00 65.83           O  
ANISOU 4893  OG1 THR B 327     7640  10174   7197  -1086    373   1083       O  
ATOM   4894  CG2 THR B 327     119.343  71.833  38.899  1.00 59.04           C  
ANISOU 4894  CG2 THR B 327     7100   8865   6469  -1283    126   1161       C  
ATOM   4895  N   PHE B 328     117.118  71.361  35.052  1.00 55.96           N  
ANISOU 4895  N   PHE B 328     6906   8737   5619   -796    261   1126       N  
ATOM   4896  CA  PHE B 328     116.852  70.908  33.690  1.00 59.22           C  
ANISOU 4896  CA  PHE B 328     7312   9328   5861   -658    336   1120       C  
ATOM   4897  C   PHE B 328     117.733  69.720  33.326  1.00 60.16           C  
ANISOU 4897  C   PHE B 328     7175   9727   5955   -637    494   1078       C  
ATOM   4898  O   PHE B 328     117.250  68.719  32.785  1.00 63.08           O  
ANISOU 4898  O   PHE B 328     7481  10218   6270   -441    522    929       O  
ATOM   4899  CB  PHE B 328     117.060  72.047  32.687  1.00 70.29           C  
ANISOU 4899  CB  PHE B 328     8911  10702   7093   -760    339   1340       C  
ATOM   4900  CG  PHE B 328     116.152  73.225  32.898  1.00 80.66           C  
ANISOU 4900  CG  PHE B 328    10512  11729   8404   -739    167   1376       C  
ATOM   4901  CD1 PHE B 328     114.784  73.101  32.719  1.00 88.90           C  
ANISOU 4901  CD1 PHE B 328    11661  12692   9424   -493     58   1221       C  
ATOM   4902  CD2 PHE B 328     116.668  74.463  33.234  1.00 83.61           C  
ANISOU 4902  CD2 PHE B 328    11054  11917   8796   -961    102   1565       C  
ATOM   4903  CE1 PHE B 328     113.944  74.182  32.903  1.00 89.22           C  
ANISOU 4903  CE1 PHE B 328    11961  12484   9455   -438   -105   1244       C  
ATOM   4904  CE2 PHE B 328     115.834  75.549  33.416  1.00 85.72           C  
ANISOU 4904  CE2 PHE B 328    11615  11904   9051   -913    -72   1587       C  
ATOM   4905  CZ  PHE B 328     114.470  75.408  33.251  1.00 85.85           C  
ANISOU 4905  CZ  PHE B 328    11726  11856   9037   -635   -171   1423       C  
ATOM   4906  N   GLU B 329     119.028  69.806  33.646  1.00 55.67           N  
ANISOU 4906  N   GLU B 329     6460   9262   5432   -832    584   1200       N  
ATOM   4907  CA  GLU B 329     119.961  68.727  33.335  1.00 56.95           C  
ANISOU 4907  CA  GLU B 329     6366   9705   5568   -796    734   1164       C  
ATOM   4908  C   GLU B 329     119.549  67.421  34.001  1.00 57.97           C  
ANISOU 4908  C   GLU B 329     6374   9839   5811   -616    705    923       C  
ATOM   4909  O   GLU B 329     119.572  66.360  33.367  1.00 57.13           O  
ANISOU 4909  O   GLU B 329     6168   9909   5628   -446    778    811       O  
ATOM   4910  CB  GLU B 329     121.372  69.129  33.760  1.00 65.51           C  
ANISOU 4910  CB  GLU B 329     7290  10884   6717  -1046    808   1331       C  
ATOM   4911  CG  GLU B 329     121.954  70.285  32.963  1.00 74.22           C  
ANISOU 4911  CG  GLU B 329     8476  12029   7695  -1256    869   1596       C  
ATOM   4912  CD  GLU B 329     121.299  71.614  33.274  1.00 81.38           C  
ANISOU 4912  CD  GLU B 329     9675  12616   8628  -1378    709   1696       C  
ATOM   4913  OE1 GLU B 329     121.056  71.907  34.468  1.00 83.74           O  
ANISOU 4913  OE1 GLU B 329    10032  12690   9095  -1433    570   1629       O  
ATOM   4914  OE2 GLU B 329     121.028  72.367  32.315  1.00 87.99           O  
ANISOU 4914  OE2 GLU B 329    10703  13426   9305  -1404    718   1839       O  
ATOM   4915  N   GLN B 330     119.175  67.478  35.279  1.00 62.59           N  
ANISOU 4915  N   GLN B 330     6984  10226   6570   -649    596    844       N  
ATOM   4916  CA  GLN B 330     118.675  66.289  35.960  1.00 64.01           C  
ANISOU 4916  CA  GLN B 330     7083  10382   6857   -497    563    635       C  
ATOM   4917  C   GLN B 330     117.430  65.750  35.271  1.00 59.28           C  
ANISOU 4917  C   GLN B 330     6568   9766   6189   -291    522    494       C  
ATOM   4918  O   GLN B 330     117.314  64.543  35.026  1.00 54.67           O  
ANISOU 4918  O   GLN B 330     5890   9282   5600   -147    549    350       O  
ATOM   4919  CB  GLN B 330     118.386  66.620  37.420  1.00 66.55           C  
ANISOU 4919  CB  GLN B 330     7455  10487   7344   -571    457    598       C  
ATOM   4920  CG  GLN B 330     119.637  66.819  38.226  1.00 68.76           C  
ANISOU 4920  CG  GLN B 330     7618  10794   7713   -748    473    687       C  
ATOM   4921  CD  GLN B 330     119.379  67.530  39.521  1.00 65.95           C  
ANISOU 4921  CD  GLN B 330     7380  10203   7476   -842    351    689       C  
ATOM   4922  OE1 GLN B 330     118.321  68.131  39.710  1.00 66.68           O  
ANISOU 4922  OE1 GLN B 330     7658  10114   7565   -791    266    658       O  
ATOM   4923  NE2 GLN B 330     120.349  67.476  40.428  1.00 62.69           N  
ANISOU 4923  NE2 GLN B 330     6862   9797   7160   -965    332    718       N  
ATOM   4924  N   GLN B 331     116.482  66.633  34.955  1.00 54.55           N  
ANISOU 4924  N   GLN B 331     6154   9033   5541   -270    439    527       N  
ATOM   4925  CA  GLN B 331     115.316  66.214  34.188  1.00 58.30           C  
ANISOU 4925  CA  GLN B 331     6697   9510   5943    -81    383    404       C  
ATOM   4926  C   GLN B 331     115.739  65.609  32.857  1.00 65.51           C  
ANISOU 4926  C   GLN B 331     7567  10643   6683     15    472    401       C  
ATOM   4927  O   GLN B 331     115.313  64.505  32.497  1.00 73.59           O  
ANISOU 4927  O   GLN B 331     8535  11734   7692    171    458    238       O  
ATOM   4928  CB  GLN B 331     114.387  67.403  33.959  1.00 56.70           C  
ANISOU 4928  CB  GLN B 331     6700   9149   5692    -66    276    465       C  
ATOM   4929  CG  GLN B 331     113.668  67.872  35.201  1.00 57.84           C  
ANISOU 4929  CG  GLN B 331     6904   9085   5988    -83    176    415       C  
ATOM   4930  CD  GLN B 331     113.021  69.218  35.002  1.00 61.80           C  
ANISOU 4930  CD  GLN B 331     7625   9427   6429    -74     72    503       C  
ATOM   4931  OE1 GLN B 331     111.949  69.318  34.413  1.00 71.89           O  
ANISOU 4931  OE1 GLN B 331     8983  10683   7648     82     -8    435       O  
ATOM   4932  NE2 GLN B 331     113.684  70.268  35.465  1.00 68.86           N  
ANISOU 4932  NE2 GLN B 331     8626  10202   7336   -238     57    653       N  
ATOM   4933  N   ALA B 332     116.600  66.318  32.123  1.00 61.78           N  
ANISOU 4933  N   ALA B 332     7124  10282   6069    -82    563    585       N  
ATOM   4934  CA  ALA B 332     117.001  65.871  30.795  1.00 58.75           C  
ANISOU 4934  CA  ALA B 332     6719  10125   5478     23    664    600       C  
ATOM   4935  C   ALA B 332     117.705  64.522  30.848  1.00 59.01           C  
ANISOU 4935  C   ALA B 332     6553  10337   5531    115    753    475       C  
ATOM   4936  O   ALA B 332     117.545  63.695  29.944  1.00 63.77           O  
ANISOU 4936  O   ALA B 332     7156  11072   6002    298    775    364       O  
ATOM   4937  CB  ALA B 332     117.903  66.919  30.149  1.00 61.88           C  
ANISOU 4937  CB  ALA B 332     7163  10619   5729   -136    771    852       C  
ATOM   4938  N   LEU B 333     118.496  64.284  31.893  1.00 55.97           N  
ANISOU 4938  N   LEU B 333     6014   9950   5302      5    791    485       N  
ATOM   4939  CA  LEU B 333     119.203  63.014  32.010  1.00 58.48           C  
ANISOU 4939  CA  LEU B 333     6153  10424   5643    110    860    365       C  
ATOM   4940  C   LEU B 333     118.226  61.859  32.182  1.00 64.18           C  
ANISOU 4940  C   LEU B 333     6909  11046   6433    291    752    130       C  
ATOM   4941  O   LEU B 333     118.354  60.816  31.533  1.00 63.54           O  
ANISOU 4941  O   LEU B 333     6791  11090   6262    466    778      3       O  
ATOM   4942  CB  LEU B 333     120.181  63.073  33.182  1.00 63.49           C  
ANISOU 4942  CB  LEU B 333     6629  11052   6440    -45    890    425       C  
ATOM   4943  CG  LEU B 333     120.827  61.754  33.594  1.00 66.33           C  
ANISOU 4943  CG  LEU B 333     6818  11520   6864     74    922    286       C  
ATOM   4944  CD1 LEU B 333     121.594  61.144  32.427  1.00 69.55           C  
ANISOU 4944  CD1 LEU B 333     7124  12218   7083    224   1059    274       C  
ATOM   4945  CD2 LEU B 333     121.729  61.957  34.804  1.00 59.98           C  
ANISOU 4945  CD2 LEU B 333     5875  10693   6222    -86    922    354       C  
ATOM   4946  N   VAL B 334     117.239  62.027  33.058  1.00 70.21           N  
ANISOU 4946  N   VAL B 334     7745  11582   7351    249    629     70       N  
ATOM   4947  CA  VAL B 334     116.308  60.940  33.331  1.00 70.12           C  
ANISOU 4947  CA  VAL B 334     7744  11469   7427    375    528   -132       C  
ATOM   4948  C   VAL B 334     115.328  60.766  32.177  1.00 70.74           C  
ANISOU 4948  C   VAL B 334     7936  11564   7378    521    457   -220       C  
ATOM   4949  O   VAL B 334     114.975  59.638  31.819  1.00 65.84           O  
ANISOU 4949  O   VAL B 334     7311  10960   6747    660    404   -386       O  
ATOM   4950  CB  VAL B 334     115.591  61.193  34.669  1.00 66.60           C  
ANISOU 4950  CB  VAL B 334     7318  10808   7178    279    443   -152       C  
ATOM   4951  CG1 VAL B 334     114.652  60.045  35.008  1.00 56.95           C  
ANISOU 4951  CG1 VAL B 334     6090   9491   6059    373    353   -338       C  
ATOM   4952  CG2 VAL B 334     116.620  61.390  35.775  1.00 66.51           C  
ANISOU 4952  CG2 VAL B 334     7215  10785   7272    143    496    -67       C  
ATOM   4953  N   VAL B 335     114.891  61.872  31.568  1.00 70.13           N  
ANISOU 4953  N   VAL B 335     7978  11471   7198    495    436   -112       N  
ATOM   4954  CA  VAL B 335     113.947  61.788  30.457  1.00 64.91           C  
ANISOU 4954  CA  VAL B 335     7433  10826   6403    641    347   -192       C  
ATOM   4955  C   VAL B 335     114.604  61.143  29.244  1.00 66.52           C  
ANISOU 4955  C   VAL B 335     7639  11239   6396    781    423   -227       C  
ATOM   4956  O   VAL B 335     113.999  60.303  28.568  1.00 66.21           O  
ANISOU 4956  O   VAL B 335     7646  11217   6292    943    335   -391       O  
ATOM   4957  CB  VAL B 335     113.390  63.184  30.124  1.00 63.73           C  
ANISOU 4957  CB  VAL B 335     7431  10602   6182    593    298    -56       C  
ATOM   4958  CG1 VAL B 335     112.632  63.161  28.799  1.00 50.38           C  
ANISOU 4958  CG1 VAL B 335     5870   8967   4306    759    214   -115       C  
ATOM   4959  CG2 VAL B 335     112.496  63.678  31.254  1.00 49.01           C  
ANISOU 4959  CG2 VAL B 335     5578   8532   4513    523    198    -76       C  
ATOM   4960  N   ALA B 336     115.847  61.528  28.945  1.00 71.08           N  
ANISOU 4960  N   ALA B 336     8164  11985   6858    723    585    -75       N  
ATOM   4961  CA  ALA B 336     116.587  60.868  27.875  1.00 74.05           C  
ANISOU 4961  CA  ALA B 336     8516  12596   7022    875    689   -108       C  
ATOM   4962  C   ALA B 336     116.762  59.387  28.169  1.00 78.56           C  
ANISOU 4962  C   ALA B 336     8995  13184   7670   1010    662   -316       C  
ATOM   4963  O   ALA B 336     116.695  58.552  27.259  1.00 87.48           O  
ANISOU 4963  O   ALA B 336    10178  14413   8648   1211    641   -454       O  
ATOM   4964  CB  ALA B 336     117.948  61.535  27.678  1.00 72.77           C  
ANISOU 4964  CB  ALA B 336     8261  12633   6756    760    887    106       C  
ATOM   4965  N   SER B 337     116.991  59.039  29.436  1.00 70.78           N  
ANISOU 4965  N   SER B 337     7896  12090   6909    912    649   -344       N  
ATOM   4966  CA  SER B 337     117.062  57.628  29.787  1.00 65.14           C  
ANISOU 4966  CA  SER B 337     7128  11345   6278   1036    596   -538       C  
ATOM   4967  C   SER B 337     115.709  56.953  29.586  1.00 62.06           C  
ANISOU 4967  C   SER B 337     6856  10788   5936   1127    411   -723       C  
ATOM   4968  O   SER B 337     115.641  55.802  29.141  1.00 61.45           O  
ANISOU 4968  O   SER B 337     6815  10723   5810   1293    348   -897       O  
ATOM   4969  CB  SER B 337     117.554  57.468  31.225  1.00 65.50           C  
ANISOU 4969  CB  SER B 337     7050  11296   6544    905    611   -511       C  
ATOM   4970  OG  SER B 337     117.779  56.103  31.527  1.00 76.58           O  
ANISOU 4970  OG  SER B 337     8417  12675   8007   1033    568   -679       O  
ATOM   4971  N   ILE B 338     114.620  57.667  29.883  1.00 66.22           N  
ANISOU 4971  N   ILE B 338     7444  11162   6555   1025    314   -689       N  
ATOM   4972  CA  ILE B 338     113.282  57.132  29.643  1.00 66.73           C  
ANISOU 4972  CA  ILE B 338     7587  11094   6671   1092    135   -850       C  
ATOM   4973  C   ILE B 338     113.085  56.851  28.163  1.00 74.07           C  
ANISOU 4973  C   ILE B 338     8634  12140   7369   1279     84   -937       C  
ATOM   4974  O   ILE B 338     112.480  55.842  27.778  1.00 79.14           O  
ANISOU 4974  O   ILE B 338     9329  12725   8014   1393    -56  -1125       O  
ATOM   4975  CB  ILE B 338     112.216  58.109  30.176  1.00 65.06           C  
ANISOU 4975  CB  ILE B 338     7396  10744   6580    971     59   -782       C  
ATOM   4976  CG1 ILE B 338     112.241  58.153  31.709  1.00 50.46           C  
ANISOU 4976  CG1 ILE B 338     5451   8762   4961    816     85   -742       C  
ATOM   4977  CG2 ILE B 338     110.828  57.740  29.655  1.00 48.25           C  
ANISOU 4977  CG2 ILE B 338     5329   8536   4468   1051   -125   -929       C  
ATOM   4978  CD1 ILE B 338     111.235  59.106  32.291  1.00 45.11           C  
ANISOU 4978  CD1 ILE B 338     4791   7962   4388    726     23   -685       C  
ATOM   4979  N   ILE B 339     113.609  57.732  27.312  1.00 76.42           N  
ANISOU 4979  N   ILE B 339     8985  12597   7453   1308    189   -798       N  
ATOM   4980  CA  ILE B 339     113.398  57.611  25.873  1.00 70.61           C  
ANISOU 4980  CA  ILE B 339     8386  11981   6460   1493    146   -861       C  
ATOM   4981  C   ILE B 339     114.149  56.403  25.323  1.00 80.34           C  
ANISOU 4981  C   ILE B 339     9618  13343   7564   1681    187  -1003       C  
ATOM   4982  O   ILE B 339     113.569  55.550  24.635  1.00 92.06           O  
ANISOU 4982  O   ILE B 339    11209  14798   8973   1845     39  -1196       O  
ATOM   4983  CB  ILE B 339     113.810  58.918  25.172  1.00 63.43           C  
ANISOU 4983  CB  ILE B 339     7548  11205   5348   1457    267   -643       C  
ATOM   4984  CG1 ILE B 339     112.731  59.986  25.357  1.00 63.83           C  
ANISOU 4984  CG1 ILE B 339     7679  11100   5471   1361    149   -565       C  
ATOM   4985  CG2 ILE B 339     114.074  58.696  23.701  1.00 69.53           C  
ANISOU 4985  CG2 ILE B 339     8448  12171   5801   1662    299   -677       C  
ATOM   4986  CD1 ILE B 339     113.189  61.387  25.003  1.00 65.81           C  
ANISOU 4986  CD1 ILE B 339     8008  11416   5580   1266    262   -316       C  
ATOM   4987  N   ILE B 340     115.445  56.290  25.645  1.00 74.40           N  
ANISOU 4987  N   ILE B 340     8744  12732   6792   1667    372   -922       N  
ATOM   4988  CA  ILE B 340     116.217  55.144  25.168  1.00 83.50           C  
ANISOU 4988  CA  ILE B 340     9888  14020   7818   1879    416  -1065       C  
ATOM   4989  C   ILE B 340     115.848  53.835  25.852  1.00 82.09           C  
ANISOU 4989  C   ILE B 340     9709  13652   7832   1927    262  -1277       C  
ATOM   4990  O   ILE B 340     116.385  52.781  25.484  1.00 83.82           O  
ANISOU 4990  O   ILE B 340     9955  13938   7956   2128    258  -1427       O  
ATOM   4991  CB  ILE B 340     117.729  55.373  25.333  1.00 85.97           C  
ANISOU 4991  CB  ILE B 340    10038  14566   8063   1865    656   -921       C  
ATOM   4992  CG1 ILE B 340     118.127  55.263  26.797  1.00 93.04           C  
ANISOU 4992  CG1 ILE B 340    10771  15344   9235   1696    673   -880       C  
ATOM   4993  CG2 ILE B 340     118.139  56.744  24.819  1.00 79.66           C  
ANISOU 4993  CG2 ILE B 340     9227  13932   7110   1749    817   -670       C  
ATOM   4994  CD1 ILE B 340     119.595  55.167  26.982  1.00101.52           C  
ANISOU 4994  CD1 ILE B 340    11665  16644  10265   1723    864   -798       C  
ATOM   4995  N   ASN B 341     114.955  53.862  26.841  1.00 73.02           N  
ANISOU 4995  N   ASN B 341     8537  12266   6941   1755    137  -1291       N  
ATOM   4996  CA  ASN B 341     114.390  52.645  27.412  1.00 70.42           C  
ANISOU 4996  CA  ASN B 341     8236  11730   6790   1772    -31  -1479       C  
ATOM   4997  C   ASN B 341     112.929  52.458  27.041  1.00 78.12           C  
ANISOU 4997  C   ASN B 341     9319  12546   7816   1761   -250  -1601       C  
ATOM   4998  O   ASN B 341     112.291  51.533  27.551  1.00 87.76           O  
ANISOU 4998  O   ASN B 341    10559  13575   9210   1723   -403  -1736       O  
ATOM   4999  CB  ASN B 341     114.522  52.632  28.938  1.00 54.89           C  
ANISOU 4999  CB  ASN B 341     6145   9621   5088   1581      0  -1408       C  
ATOM   5000  CG  ASN B 341     115.946  52.404  29.410  1.00 61.64           C  
ANISOU 5000  CG  ASN B 341     6889  10600   5930   1619    156  -1350       C  
ATOM   5001  OD1 ASN B 341     116.422  51.268  29.471  1.00 65.65           O  
ANISOU 5001  OD1 ASN B 341     7418  11089   6437   1761    120  -1485       O  
ATOM   5002  ND2 ASN B 341     116.628  53.484  29.766  1.00 63.08           N  
ANISOU 5002  ND2 ASN B 341     6956  10902   6111   1494    315  -1150       N  
ATOM   5003  N   SER B 342     112.389  53.306  26.159  1.00 63.49           N  
ANISOU 5003  N   SER B 342     7538  10770   5817   1788   -277  -1551       N  
ATOM   5004  CA  SER B 342     110.952  53.301  25.904  1.00 67.55           C  
ANISOU 5004  CA  SER B 342     8116  11147   6404   1759   -492  -1646       C  
ATOM   5005  C   SER B 342     110.486  51.987  25.291  1.00 72.09           C  
ANISOU 5005  C   SER B 342     8807  11636   6949   1901   -697  -1891       C  
ATOM   5006  O   SER B 342     109.329  51.591  25.477  1.00 68.57           O  
ANISOU 5006  O   SER B 342     8364  11025   6664   1824   -897  -1998       O  
ATOM   5007  CB  SER B 342     110.585  54.477  24.998  1.00 81.42           C  
ANISOU 5007  CB  SER B 342     9946  13014   7974   1797   -487  -1542       C  
ATOM   5008  OG  SER B 342     111.397  54.501  23.836  1.00 95.17           O  
ANISOU 5008  OG  SER B 342    11795  14956   9409   1986   -394  -1535       O  
ATOM   5009  N   HIS B 343     111.362  51.300  24.555  1.00 74.65           N  
ANISOU 5009  N   HIS B 343     9225  12071   7066   2111   -655  -1986       N  
ATOM   5010  CA  HIS B 343     110.988  50.012  23.987  1.00 74.91           C  
ANISOU 5010  CA  HIS B 343     9403  11998   7062   2261   -868  -2233       C  
ATOM   5011  C   HIS B 343     110.844  48.940  25.055  1.00 84.08           C  
ANISOU 5011  C   HIS B 343    10525  12933   8489   2152   -961  -2326       C  
ATOM   5012  O   HIS B 343     110.155  47.941  24.827  1.00 81.83           O  
ANISOU 5012  O   HIS B 343    10350  12476   8265   2182  -1193  -2518       O  
ATOM   5013  CB  HIS B 343     112.006  49.580  22.934  1.00 73.35           C  
ANISOU 5013  CB  HIS B 343     9330  11991   6550   2549   -788  -2316       C  
ATOM   5014  CG  HIS B 343     113.377  49.326  23.475  1.00 75.55           C  
ANISOU 5014  CG  HIS B 343     9510  12379   6815   2602   -573  -2252       C  
ATOM   5015  ND1 HIS B 343     114.312  50.326  23.636  1.00 79.92           N  
ANISOU 5015  ND1 HIS B 343     9926  13149   7291   2553   -308  -2031       N  
ATOM   5016  CD2 HIS B 343     113.981  48.181  23.872  1.00 77.66           C  
ANISOU 5016  CD2 HIS B 343     9798  12571   7136   2707   -598  -2382       C  
ATOM   5017  CE1 HIS B 343     115.428  49.810  24.118  1.00 77.21           C  
ANISOU 5017  CE1 HIS B 343     9494  12879   6962   2622   -177  -2030       C  
ATOM   5018  NE2 HIS B 343     115.255  48.510  24.267  1.00 78.60           N  
ANISOU 5018  NE2 HIS B 343     9772  12881   7212   2732   -349  -2243       N  
ATOM   5019  N   LEU B 344     111.467  49.132  26.216  1.00 91.64           N  
ANISOU 5019  N   LEU B 344    11340  13875   9603   2017   -799  -2191       N  
ATOM   5020  CA  LEU B 344     111.297  48.225  27.342  1.00 78.37           C  
ANISOU 5020  CA  LEU B 344     9628  11973   8177   1890   -875  -2243       C  
ATOM   5021  C   LEU B 344     110.192  48.689  28.282  1.00 75.75           C  
ANISOU 5021  C   LEU B 344     9181  11499   8102   1621   -926  -2155       C  
ATOM   5022  O   LEU B 344     109.417  47.866  28.783  1.00 74.19           O  
ANISOU 5022  O   LEU B 344     9000  11093   8095   1506  -1086  -2246       O  
ATOM   5023  CB  LEU B 344     112.615  48.092  28.103  1.00 71.99           C  
ANISOU 5023  CB  LEU B 344     8740  11230   7381   1918   -686  -2158       C  
ATOM   5024  CG  LEU B 344     113.738  47.430  27.306  1.00 83.56           C  
ANISOU 5024  CG  LEU B 344    10296  12839   8614   2207   -636  -2267       C  
ATOM   5025  CD1 LEU B 344     115.104  47.728  27.918  1.00 84.98           C  
ANISOU 5025  CD1 LEU B 344    10332  13179   8776   2232   -407  -2133       C  
ATOM   5026  CD2 LEU B 344     113.503  45.934  27.209  1.00 91.21           C  
ANISOU 5026  CD2 LEU B 344    11438  13594   9623   2324   -853  -2497       C  
ATOM   5027  N   LEU B 345     110.098  49.999  28.525  1.00 74.12           N  
ANISOU 5027  N   LEU B 345     8862  11400   7899   1519   -793  -1977       N  
ATOM   5028  CA  LEU B 345     109.080  50.497  29.442  1.00 77.65           C  
ANISOU 5028  CA  LEU B 345     9194  11737   8571   1298   -824  -1896       C  
ATOM   5029  C   LEU B 345     107.677  50.302  28.887  1.00 84.97           C  
ANISOU 5029  C   LEU B 345    10145  12585   9554   1270  -1045  -2013       C  
ATOM   5030  O   LEU B 345     106.736  50.075  29.655  1.00 91.84           O  
ANISOU 5030  O   LEU B 345    10925  13323  10647   1097  -1127  -2019       O  
ATOM   5031  CB  LEU B 345     109.326  51.975  29.767  1.00 69.38           C  
ANISOU 5031  CB  LEU B 345     8055  10812   7496   1227   -650  -1693       C  
ATOM   5032  CG  LEU B 345     110.625  52.288  30.517  1.00 59.69           C  
ANISOU 5032  CG  LEU B 345     6764   9651   6262   1197   -445  -1556       C  
ATOM   5033  CD1 LEU B 345     110.836  53.787  30.726  1.00 51.60           C  
ANISOU 5033  CD1 LEU B 345     5680   8726   5200   1117   -306  -1361       C  
ATOM   5034  CD2 LEU B 345     110.639  51.544  31.837  1.00 56.34           C  
ANISOU 5034  CD2 LEU B 345     6285   9065   6056   1072   -448  -1566       C  
ATOM   5035  N   ALA B 346     107.519  50.367  27.566  1.00 84.51           N  
ANISOU 5035  N   ALA B 346    10201  12618   9292   1438  -1147  -2106       N  
ATOM   5036  CA  ALA B 346     106.202  50.241  26.960  1.00 83.74           C  
ANISOU 5036  CA  ALA B 346    10121  12463   9235   1424  -1381  -2223       C  
ATOM   5037  C   ALA B 346     105.586  48.862  27.151  1.00 82.02           C  
ANISOU 5037  C   ALA B 346     9935  12044   9184   1350  -1593  -2397       C  
ATOM   5038  O   ALA B 346     104.381  48.711  26.931  1.00 75.55           O  
ANISOU 5038  O   ALA B 346     9073  11156   8474   1269  -1795  -2480       O  
ATOM   5039  CB  ALA B 346     106.282  50.568  25.469  1.00 86.62           C  
ANISOU 5039  CB  ALA B 346    10633  12969   9310   1645  -1450  -2289       C  
ATOM   5040  N   THR B 347     106.367  47.869  27.574  1.00 83.63           N  
ANISOU 5040  N   THR B 347    10211  12147   9419   1369  -1563  -2448       N  
ATOM   5041  CA  THR B 347     105.888  46.498  27.679  1.00 87.37           C  
ANISOU 5041  CA  THR B 347    10767  12399  10028   1307  -1780  -2614       C  
ATOM   5042  C   THR B 347     105.126  46.207  28.968  1.00 94.43           C  
ANISOU 5042  C   THR B 347    11516  13130  11232   1021  -1797  -2543       C  
ATOM   5043  O   THR B 347     104.548  45.122  29.086  1.00100.89           O  
ANISOU 5043  O   THR B 347    12391  13750  12193    916  -1993  -2659       O  
ATOM   5044  CB  THR B 347     107.059  45.517  27.566  1.00 85.82           C  
ANISOU 5044  CB  THR B 347    10740  12148   9720   1477  -1758  -2706       C  
ATOM   5045  OG1 THR B 347     107.902  45.648  28.718  1.00 83.70           O  
ANISOU 5045  OG1 THR B 347    10383  11881   9538   1405  -1542  -2559       O  
ATOM   5046  CG2 THR B 347     107.875  45.808  26.311  1.00 81.41           C  
ANISOU 5046  CG2 THR B 347    10309  11790   8832   1774  -1704  -2766       C  
ATOM   5047  N   ASN B 348     105.116  47.122  29.940  1.00 98.65           N  
ANISOU 5047  N   ASN B 348    11879  13736  11867    891  -1600  -2356       N  
ATOM   5048  CA  ASN B 348     104.320  46.933  31.146  1.00100.20           C  
ANISOU 5048  CA  ASN B 348    11930  13811  12332    632  -1595  -2281       C  
ATOM   5049  C   ASN B 348     103.657  48.248  31.533  1.00 92.18           C  
ANISOU 5049  C   ASN B 348    10721  12932  11370    550  -1485  -2142       C  
ATOM   5050  O   ASN B 348     104.093  49.332  31.134  1.00 82.22           O  
ANISOU 5050  O   ASN B 348     9458  11831   9950    676  -1371  -2067       O  
ATOM   5051  CB  ASN B 348     105.153  46.394  32.319  1.00100.97           C  
ANISOU 5051  CB  ASN B 348    12052  13797  12514    559  -1458  -2200       C  
ATOM   5052  CG  ASN B 348     105.868  47.487  33.082  1.00100.33           C  
ANISOU 5052  CG  ASN B 348    11874  13849  12396    561  -1203  -2018       C  
ATOM   5053  OD1 ASN B 348     105.341  48.038  34.050  1.00100.34           O  
ANISOU 5053  OD1 ASN B 348    11734  13853  12537    400  -1110  -1896       O  
ATOM   5054  ND2 ASN B 348     107.082  47.803  32.654  1.00100.74           N  
ANISOU 5054  ND2 ASN B 348    12001  14018  12259    745  -1091  -2000       N  
ATOM   5055  N   SER B 349     102.595  48.131  32.339  1.00 89.90           N  
ANISOU 5055  N   SER B 349    10275  12577  11306    337  -1520  -2105       N  
ATOM   5056  CA  SER B 349     101.726  49.272  32.613  1.00 94.77           C  
ANISOU 5056  CA  SER B 349    10703  13322  11983    283  -1463  -2012       C  
ATOM   5057  C   SER B 349     102.448  50.382  33.366  1.00 90.74           C  
ANISOU 5057  C   SER B 349    10159  12905  11413    316  -1216  -1843       C  
ATOM   5058  O   SER B 349     102.166  51.564  33.137  1.00 88.91           O  
ANISOU 5058  O   SER B 349     9867  12801  11114    387  -1170  -1782       O  
ATOM   5059  CB  SER B 349     100.491  48.813  33.391  1.00102.34           C  
ANISOU 5059  CB  SER B 349    11478  14211  13195     49  -1530  -2005       C  
ATOM   5060  OG  SER B 349     100.844  48.012  34.506  1.00105.91           O  
ANISOU 5060  OG  SER B 349    11949  14520  13772   -107  -1440  -1943       O  
ATOM   5061  N   ASN B 350     103.375  50.031  34.260  1.00 84.09           N  
ANISOU 5061  N   ASN B 350     9368  11989  10593    271  -1074  -1770       N  
ATOM   5062  CA  ASN B 350     104.100  51.047  35.016  1.00 78.39           C  
ANISOU 5062  CA  ASN B 350     8622  11341   9821    288   -863  -1617       C  
ATOM   5063  C   ASN B 350     105.040  51.836  34.118  1.00 73.64           C  
ANISOU 5063  C   ASN B 350     8118  10864   8997    470   -806  -1593       C  
ATOM   5064  O   ASN B 350     105.042  53.072  34.142  1.00 69.60           O  
ANISOU 5064  O   ASN B 350     7571  10450   8423    503   -720  -1492       O  
ATOM   5065  CB  ASN B 350     104.863  50.392  36.162  1.00 76.54           C  
ANISOU 5065  CB  ASN B 350     8424  10995   9662    200   -756  -1556       C  
ATOM   5066  CG  ASN B 350     103.941  49.839  37.222  1.00 68.85           C  
ANISOU 5066  CG  ASN B 350     7349   9916   8894     -2   -763  -1527       C  
ATOM   5067  OD1 ASN B 350     103.000  50.518  37.662  1.00 48.67           O  
ANISOU 5067  OD1 ASN B 350     4646   7426   6422    -79   -725  -1470       O  
ATOM   5068  ND2 ASN B 350     104.175  48.586  37.612  1.00 68.26           N  
ANISOU 5068  ND2 ASN B 350     7358   9681   8897    -82   -816  -1565       N  
ATOM   5069  N   GLY B 351     105.855  51.140  33.325  1.00 74.22           N  
ANISOU 5069  N   GLY B 351     8322  10936   8942    592   -851  -1680       N  
ATOM   5070  CA  GLY B 351     106.675  51.831  32.345  1.00 71.35           C  
ANISOU 5070  CA  GLY B 351     8041  10719   8351    762   -792  -1655       C  
ATOM   5071  C   GLY B 351     105.846  52.685  31.406  1.00 75.14           C  
ANISOU 5071  C   GLY B 351     8517  11292   8741    830   -880  -1668       C  
ATOM   5072  O   GLY B 351     106.218  53.817  31.087  1.00 79.19           O  
ANISOU 5072  O   GLY B 351     9050  11918   9122    892   -785  -1560       O  
ATOM   5073  N   MET B 352     104.698  52.164  30.966  1.00 73.90           N  
ANISOU 5073  N   MET B 352     8336  11083   8660    811  -1075  -1794       N  
ATOM   5074  CA  MET B 352     103.829  52.942  30.093  1.00 75.26           C  
ANISOU 5074  CA  MET B 352     8498  11342   8755    888  -1188  -1817       C  
ATOM   5075  C   MET B 352     103.365  54.221  30.778  1.00 71.54           C  
ANISOU 5075  C   MET B 352     7913  10919   8349    829  -1090  -1675       C  
ATOM   5076  O   MET B 352     103.187  55.252  30.121  1.00 68.76           O  
ANISOU 5076  O   MET B 352     7603  10658   7864    933  -1105  -1628       O  
ATOM   5077  CB  MET B 352     102.631  52.095  29.660  1.00 80.66           C  
ANISOU 5077  CB  MET B 352     9141  11956   9550    848  -1433  -1981       C  
ATOM   5078  CG  MET B 352     101.750  52.759  28.610  1.00 84.07           C  
ANISOU 5078  CG  MET B 352     9575  12482   9884    960  -1593  -2035       C  
ATOM   5079  SD  MET B 352     102.661  53.119  27.089  1.00 82.71           S  
ANISOU 5079  SD  MET B 352     9643  12429   9355   1216  -1598  -2059       S  
ATOM   5080  CE  MET B 352     102.814  51.479  26.386  1.00 77.87           C  
ANISOU 5080  CE  MET B 352     9166  11717   8706   1275  -1787  -2281       C  
ATOM   5081  N   LEU B 353     103.180  54.177  32.098  1.00 76.77           N  
ANISOU 5081  N   LEU B 353     8455  11515   9200    676   -994  -1606       N  
ATOM   5082  CA  LEU B 353     102.781  55.376  32.826  1.00 80.00           C  
ANISOU 5082  CA  LEU B 353     8774  11962   9660    644   -899  -1484       C  
ATOM   5083  C   LEU B 353     103.810  56.486  32.653  1.00 78.11           C  
ANISOU 5083  C   LEU B 353     8650  11783   9247    725   -764  -1353       C  
ATOM   5084  O   LEU B 353     103.451  57.647  32.421  1.00 77.54           O  
ANISOU 5084  O   LEU B 353     8594  11760   9108    789   -769  -1286       O  
ATOM   5085  CB  LEU B 353     102.580  55.041  34.305  1.00 79.03           C  
ANISOU 5085  CB  LEU B 353     8530  11762   9736    479   -798  -1433       C  
ATOM   5086  CG  LEU B 353     102.615  56.184  35.318  1.00 89.20           C  
ANISOU 5086  CG  LEU B 353     9774  13068  11050    454   -651  -1297       C  
ATOM   5087  CD1 LEU B 353     101.517  57.208  35.031  1.00101.86           C  
ANISOU 5087  CD1 LEU B 353    11304  14748  12651    534   -722  -1296       C  
ATOM   5088  CD2 LEU B 353     102.483  55.628  36.722  1.00 87.76           C  
ANISOU 5088  CD2 LEU B 353     9498  12812  11036    302   -555  -1260       C  
ATOM   5089  N   LEU B 354     105.096  56.143  32.753  1.00 68.50           N  
ANISOU 5089  N   LEU B 354     7511  10560   7956    721   -650  -1311       N  
ATOM   5090  CA  LEU B 354     106.149  57.128  32.537  1.00 64.28           C  
ANISOU 5090  CA  LEU B 354     7066  10095   7261    768   -522  -1177       C  
ATOM   5091  C   LEU B 354     106.093  57.692  31.123  1.00 65.22           C  
ANISOU 5091  C   LEU B 354     7297  10312   7172    911   -592  -1182       C  
ATOM   5092  O   LEU B 354     106.194  58.911  30.928  1.00 66.10           O  
ANISOU 5092  O   LEU B 354     7469  10460   7187    936   -549  -1061       O  
ATOM   5093  CB  LEU B 354     107.510  56.488  32.802  1.00 63.42           C  
ANISOU 5093  CB  LEU B 354     6985   9993   7118    750   -405  -1153       C  
ATOM   5094  CG  LEU B 354     107.955  56.444  34.259  1.00 62.22           C  
ANISOU 5094  CG  LEU B 354     6766   9764   7112    620   -294  -1077       C  
ATOM   5095  CD1 LEU B 354     109.338  55.847  34.354  1.00 53.29           C  
ANISOU 5095  CD1 LEU B 354     5658   8663   5925    637   -201  -1061       C  
ATOM   5096  CD2 LEU B 354     107.923  57.844  34.855  1.00 69.66           C  
ANISOU 5096  CD2 LEU B 354     7705  10704   8059    568   -218   -934       C  
ATOM   5097  N   LEU B 355     105.927  56.817  30.124  1.00 57.28           N  
ANISOU 5097  N   LEU B 355     6342   9337   6084   1008   -710  -1320       N  
ATOM   5098  CA  LEU B 355     105.873  57.264  28.734  1.00 59.19           C  
ANISOU 5098  CA  LEU B 355     6712   9678   6098   1161   -784  -1333       C  
ATOM   5099  C   LEU B 355     104.638  58.115  28.474  1.00 65.22           C  
ANISOU 5099  C   LEU B 355     7463  10436   6880   1198   -917  -1332       C  
ATOM   5100  O   LEU B 355     104.711  59.131  27.773  1.00 67.99           O  
ANISOU 5100  O   LEU B 355     7927  10847   7057   1286   -915  -1241       O  
ATOM   5101  CB  LEU B 355     105.899  56.056  27.796  1.00 56.07           C  
ANISOU 5101  CB  LEU B 355     6388   9302   5613   1270   -905  -1507       C  
ATOM   5102  CG  LEU B 355     107.173  55.209  27.878  1.00 63.45           C  
ANISOU 5102  CG  LEU B 355     7357  10261   6491   1294   -785  -1525       C  
ATOM   5103  CD1 LEU B 355     107.031  53.888  27.124  1.00 66.49           C  
ANISOU 5103  CD1 LEU B 355     7823  10618   6823   1406   -940  -1730       C  
ATOM   5104  CD2 LEU B 355     108.365  56.001  27.369  1.00 64.50           C  
ANISOU 5104  CD2 LEU B 355     7564  10544   6400   1363   -605  -1378       C  
ATOM   5105  N   THR B 356     103.490  57.703  29.018  1.00 63.21           N  
ANISOU 5105  N   THR B 356     7070  10115   6831   1134  -1036  -1427       N  
ATOM   5106  CA  THR B 356     102.302  58.547  28.964  1.00 55.15           C  
ANISOU 5106  CA  THR B 356     5993   9106   5857   1176  -1150  -1424       C  
ATOM   5107  C   THR B 356     102.569  59.901  29.602  1.00 64.84           C  
ANISOU 5107  C   THR B 356     7248  10321   7067   1160  -1018  -1252       C  
ATOM   5108  O   THR B 356     102.210  60.941  29.037  1.00 65.95           O  
ANISOU 5108  O   THR B 356     7477  10489   7090   1268  -1081  -1198       O  
ATOM   5109  CB  THR B 356     101.132  57.850  29.655  1.00 58.57           C  
ANISOU 5109  CB  THR B 356     6223   9493   6539   1078  -1254  -1533       C  
ATOM   5110  OG1 THR B 356     100.920  56.564  29.060  1.00 65.21           O  
ANISOU 5110  OG1 THR B 356     7061  10312   7402   1071  -1399  -1693       O  
ATOM   5111  CG2 THR B 356      99.864  58.683  29.555  1.00 52.54           C  
ANISOU 5111  CG2 THR B 356     5366   8773   5823   1150  -1380  -1547       C  
ATOM   5112  N   TRP B 357     103.214  59.910  30.773  1.00 74.29           N  
ANISOU 5112  N   TRP B 357     8392  11464   8372   1032   -852  -1168       N  
ATOM   5113  CA  TRP B 357     103.570  61.178  31.401  1.00 73.33           C  
ANISOU 5113  CA  TRP B 357     8324  11309   8228   1010   -742  -1011       C  
ATOM   5114  C   TRP B 357     104.500  61.993  30.514  1.00 73.72           C  
ANISOU 5114  C   TRP B 357     8564  11400   8046   1069   -691   -888       C  
ATOM   5115  O   TRP B 357     104.372  63.220  30.428  1.00 89.92           O  
ANISOU 5115  O   TRP B 357    10718  13425  10024   1111   -700   -781       O  
ATOM   5116  CB  TRP B 357     104.208  60.946  32.773  1.00 65.37           C  
ANISOU 5116  CB  TRP B 357     7244  10237   7358    863   -587   -952       C  
ATOM   5117  CG  TRP B 357     104.670  62.237  33.374  1.00 57.68           C  
ANISOU 5117  CG  TRP B 357     6353   9214   6349    837   -495   -800       C  
ATOM   5118  CD1 TRP B 357     103.926  63.109  34.111  1.00 63.73           C  
ANISOU 5118  CD1 TRP B 357     7099   9925   7190    857   -513   -771       C  
ATOM   5119  CD2 TRP B 357     105.984  62.804  33.289  1.00 51.61           C  
ANISOU 5119  CD2 TRP B 357     5704   8444   5462    786   -382   -660       C  
ATOM   5120  NE1 TRP B 357     104.689  64.192  34.479  1.00 58.39           N  
ANISOU 5120  NE1 TRP B 357     6555   9187   6446    823   -437   -629       N  
ATOM   5121  CE2 TRP B 357     105.957  64.028  33.987  1.00 50.42           C  
ANISOU 5121  CE2 TRP B 357     5622   8210   5327    761   -357   -551       C  
ATOM   5122  CE3 TRP B 357     107.177  62.402  32.680  1.00 59.19           C  
ANISOU 5122  CE3 TRP B 357     6712   9476   6303    763   -302   -618       C  
ATOM   5123  CZ2 TRP B 357     107.075  64.849  34.098  1.00 56.49           C  
ANISOU 5123  CZ2 TRP B 357     6507   8945   6011    681   -269   -396       C  
ATOM   5124  CZ3 TRP B 357     108.287  63.220  32.791  1.00 59.67           C  
ANISOU 5124  CZ3 TRP B 357     6855   9537   6280    688   -193   -456       C  
ATOM   5125  CH2 TRP B 357     108.229  64.428  33.496  1.00 59.48           C  
ANISOU 5125  CH2 TRP B 357     6901   9411   6289    632   -185   -344       C  
ATOM   5126  N   LEU B 358     105.434  61.328  29.838  1.00 67.51           N  
ANISOU 5126  N   LEU B 358     7833  10680   7136   1079   -636   -898       N  
ATOM   5127  CA  LEU B 358     106.391  62.038  28.998  1.00 67.48           C  
ANISOU 5127  CA  LEU B 358     7988  10747   6904   1117   -556   -763       C  
ATOM   5128  C   LEU B 358     105.704  62.708  27.816  1.00 69.09           C  
ANISOU 5128  C   LEU B 358     8332  10987   6931   1265   -692   -761       C  
ATOM   5129  O   LEU B 358     106.007  63.861  27.488  1.00 70.95           O  
ANISOU 5129  O   LEU B 358     8711  11217   7031   1275   -657   -605       O  
ATOM   5130  CB  LEU B 358     107.473  61.072  28.521  1.00 63.52           C  
ANISOU 5130  CB  LEU B 358     7490  10343   6303   1127   -462   -795       C  
ATOM   5131  CG  LEU B 358     108.471  61.613  27.510  1.00 67.14           C  
ANISOU 5131  CG  LEU B 358     8084  10924   6501   1176   -360   -666       C  
ATOM   5132  CD1 LEU B 358     109.078  62.908  28.014  1.00 72.28           C  
ANISOU 5132  CD1 LEU B 358     8783  11539   7143   1053   -245   -450       C  
ATOM   5133  CD2 LEU B 358     109.545  60.573  27.308  1.00 74.72           C  
ANISOU 5133  CD2 LEU B 358     8997  11991   7400   1195   -249   -714       C  
ATOM   5134  N   LEU B 359     104.773  62.007  27.169  1.00 65.67           N  
ANISOU 5134  N   LEU B 359     7871  10582   6499   1374   -863   -929       N  
ATOM   5135  CA  LEU B 359     104.091  62.575  26.012  1.00 70.94           C  
ANISOU 5135  CA  LEU B 359     8677  11289   6989   1535  -1020   -943       C  
ATOM   5136  C   LEU B 359     103.192  63.740  26.411  1.00 76.39           C  
ANISOU 5136  C   LEU B 359     9377  11901   7747   1566  -1105   -883       C  
ATOM   5137  O   LEU B 359     103.222  64.803  25.780  1.00 80.56           O  
ANISOU 5137  O   LEU B 359    10088  12423   8099   1649  -1135   -765       O  
ATOM   5138  CB  LEU B 359     103.277  61.494  25.304  1.00 67.26           C  
ANISOU 5138  CB  LEU B 359     8164  10861   6530   1635  -1212  -1155       C  
ATOM   5139  CG  LEU B 359     104.057  60.494  24.462  1.00 63.65           C  
ANISOU 5139  CG  LEU B 359     7787  10487   5910   1693  -1185  -1233       C  
ATOM   5140  CD1 LEU B 359     103.105  59.527  23.784  1.00 57.59           C  
ANISOU 5140  CD1 LEU B 359     6998   9723   5159   1791  -1424  -1455       C  
ATOM   5141  CD2 LEU B 359     104.902  61.232  23.440  1.00 74.08           C  
ANISOU 5141  CD2 LEU B 359     9321  11908   6920   1787  -1092  -1091       C  
ATOM   5142  N   ASP B 360     102.381  63.556  27.457  1.00 72.05           N  
ANISOU 5142  N   ASP B 360     8641  11294   7442   1511  -1142   -959       N  
ATOM   5143  CA  ASP B 360     101.339  64.533  27.810  1.00 77.30           C  
ANISOU 5143  CA  ASP B 360     9286  11909   8177   1590  -1247   -946       C  
ATOM   5144  C   ASP B 360     101.867  65.597  28.768  1.00 87.73           C  
ANISOU 5144  C   ASP B 360    10672  13132   9531   1512  -1109   -784       C  
ATOM   5145  O   ASP B 360     102.019  66.764  28.394  1.00 76.10           O  
ANISOU 5145  O   ASP B 360     9394  11606   7913   1579  -1131   -658       O  
ATOM   5146  CB  ASP B 360     100.124  63.824  28.415  1.00 75.28           C  
ANISOU 5146  CB  ASP B 360     8777  11670   8155   1582  -1352  -1109       C  
ATOM   5147  CG  ASP B 360      99.669  62.623  27.597  1.00 87.91           C  
ANISOU 5147  CG  ASP B 360    10303  13340   9760   1612  -1500  -1279       C  
ATOM   5148  OD1 ASP B 360      99.095  61.689  28.198  1.00 92.85           O  
ANISOU 5148  OD1 ASP B 360    10717  13968  10593   1518  -1530  -1393       O  
ATOM   5149  OD2 ASP B 360      99.864  62.613  26.361  1.00 90.21           O  
ANISOU 5149  OD2 ASP B 360    10758  13677   9841   1725  -1593  -1297       O  
ATOM   5150  N   ASN B 361     102.129  65.203  30.016  1.00117.67           N  
ANISOU 5150  N   ASN B 361    14319  16882  13506   1372   -983   -787       N  
ATOM   5151  CA  ASN B 361     102.509  66.140  31.074  1.00119.68           C  
ANISOU 5151  CA  ASN B 361    14624  17034  13815   1303   -879   -665       C  
ATOM   5152  C   ASN B 361     104.019  66.365  31.042  1.00124.85           C  
ANISOU 5152  C   ASN B 361    15409  17665  14363   1173   -726   -511       C  
ATOM   5153  O   ASN B 361     104.768  65.953  31.928  1.00126.69           O  
ANISOU 5153  O   ASN B 361    15565  17877  14694   1032   -594   -485       O  
ATOM   5154  CB  ASN B 361     102.054  65.621  32.432  1.00111.14           C  
ANISOU 5154  CB  ASN B 361    13335  15932  12961   1225   -821   -739       C  
ATOM   5155  CG  ASN B 361     100.755  64.850  32.355  1.00114.25           C  
ANISOU 5155  CG  ASN B 361    13525  16404  13481   1290   -940   -905       C  
ATOM   5156  OD1 ASN B 361      99.795  65.290  31.718  1.00120.52           O  
ANISOU 5156  OD1 ASN B 361    14320  17236  14236   1443  -1095   -959       O  
ATOM   5157  ND2 ASN B 361     100.720  63.685  32.996  1.00111.24           N  
ANISOU 5157  ND2 ASN B 361    12966  16045  13255   1167   -879   -981       N  
ATOM   5158  N   SER B 362     104.462  67.042  29.986  1.00124.77           N  
ANISOU 5158  N   SER B 362    15596  17668  14144   1222   -748   -403       N  
ATOM   5159  CA  SER B 362     105.869  67.395  29.883  1.00121.54           C  
ANISOU 5159  CA  SER B 362    15297  17257  13626   1089   -600   -233       C  
ATOM   5160  C   SER B 362     106.027  68.552  28.910  1.00116.99           C  
ANISOU 5160  C   SER B 362    14970  16650  12832   1145   -649    -81       C  
ATOM   5161  O   SER B 362     105.269  68.686  27.945  1.00110.34           O  
ANISOU 5161  O   SER B 362    14215  15841  11868   1307   -785   -128       O  
ATOM   5162  CB  SER B 362     106.718  66.201  29.440  1.00129.45           C  
ANISOU 5162  CB  SER B 362    16208  18395  14583   1038   -496   -277       C  
ATOM   5163  OG  SER B 362     108.049  66.337  29.903  1.00136.81           O  
ANISOU 5163  OG  SER B 362    17136  19334  15512    877   -330   -143       O  
ATOM   5164  N   PHE B 363     107.030  69.384  29.187  1.00114.17           N  
ANISOU 5164  N   PHE B 363    14731  16223  12427   1000   -546    109       N  
ATOM   5165  CA  PHE B 363     107.342  70.570  28.403  1.00115.40           C  
ANISOU 5165  CA  PHE B 363    15144  16318  12383    997   -573    298       C  
ATOM   5166  C   PHE B 363     108.574  70.377  27.530  1.00 98.68           C  
ANISOU 5166  C   PHE B 363    13069  14341  10083    894   -422    438       C  
ATOM   5167  O   PHE B 363     109.130  71.356  27.022  1.00 93.83           O  
ANISOU 5167  O   PHE B 363    12655  13683   9313    818   -394    643       O  
ATOM   5168  CB  PHE B 363     107.538  71.771  29.330  1.00128.18           C  
ANISOU 5168  CB  PHE B 363    16890  17734  14078    891   -586    426       C  
ATOM   5169  CG  PHE B 363     108.837  71.745  30.104  1.00129.90           C  
ANISOU 5169  CG  PHE B 363    17037  17944  14375    650   -426    538       C  
ATOM   5170  CD1 PHE B 363     109.838  72.664  29.832  1.00128.82           C  
ANISOU 5170  CD1 PHE B 363    17067  17751  14129    480   -365    768       C  
ATOM   5171  CD2 PHE B 363     109.050  70.812  31.108  1.00127.71           C  
ANISOU 5171  CD2 PHE B 363    16527  17714  14283    586   -346    420       C  
ATOM   5172  CE1 PHE B 363     111.026  72.649  30.540  1.00127.87           C  
ANISOU 5172  CE1 PHE B 363    16855  17636  14092    251   -236    867       C  
ATOM   5173  CE2 PHE B 363     110.238  70.793  31.819  1.00122.56           C  
ANISOU 5173  CE2 PHE B 363    15806  17058  13701    380   -221    516       C  
ATOM   5174  CZ  PHE B 363     111.226  71.712  31.534  1.00123.61           C  
ANISOU 5174  CZ  PHE B 363    16081  17151  13735    213   -170    734       C  
ATOM   5175  N   PHE B 364     109.016  69.135  27.353  1.00 86.54           N  
ANISOU 5175  N   PHE B 364    11351  12973   8556    892   -324    335       N  
ATOM   5176  CA  PHE B 364     110.248  68.856  26.631  1.00 91.60           C  
ANISOU 5176  CA  PHE B 364    11990  13784   9031    813   -155    451       C  
ATOM   5177  C   PHE B 364     109.999  68.944  25.133  1.00 98.77           C  
ANISOU 5177  C   PHE B 364    13068  14798   9664    967   -201    478       C  
ATOM   5178  O   PHE B 364     109.185  68.192  24.587  1.00101.55           O  
ANISOU 5178  O   PHE B 364    13395  15207   9981   1150   -314    294       O  
ATOM   5179  CB  PHE B 364     110.783  67.480  27.015  1.00 97.90           C  
ANISOU 5179  CB  PHE B 364    12550  14714   9934    795    -51    312       C  
ATOM   5180  CG  PHE B 364     111.533  67.467  28.317  1.00105.02           C  
ANISOU 5180  CG  PHE B 364    13309  15558  11035    609     48    357       C  
ATOM   5181  CD1 PHE B 364     112.917  67.417  28.330  1.00106.56           C  
ANISOU 5181  CD1 PHE B 364    13428  15874  11185    466    223    489       C  
ATOM   5182  CD2 PHE B 364     110.858  67.514  29.526  1.00104.84           C  
ANISOU 5182  CD2 PHE B 364    13224  15375  11235    585    -34    268       C  
ATOM   5183  CE1 PHE B 364     113.613  67.412  29.520  1.00104.26           C  
ANISOU 5183  CE1 PHE B 364    13008  15532  11076    301    290    525       C  
ATOM   5184  CE2 PHE B 364     111.548  67.508  30.721  1.00103.58           C  
ANISOU 5184  CE2 PHE B 364    12957  15160  11238    427     43    306       C  
ATOM   5185  CZ  PHE B 364     112.927  67.456  30.717  1.00103.76           C  
ANISOU 5185  CZ  PHE B 364    12912  15290  11221    284    194    431       C  
ATOM   5186  N   ARG B 365     110.694  69.862  24.472  1.00 99.03           N  
ANISOU 5186  N   ARG B 365    13278  14851   9497    883   -120    711       N  
ATOM   5187  CA  ARG B 365     110.543  70.008  23.034  1.00100.55           C  
ANISOU 5187  CA  ARG B 365    13661  15150   9393   1026   -147    764       C  
ATOM   5188  C   ARG B 365     111.097  68.778  22.325  1.00 92.46           C  
ANISOU 5188  C   ARG B 365    12515  14377   8240   1115    -27    660       C  
ATOM   5189  O   ARG B 365     112.058  68.157  22.789  1.00 92.88           O  
ANISOU 5189  O   ARG B 365    12375  14543   8373   1006    142    660       O  
ATOM   5190  CB  ARG B 365     111.246  71.277  22.555  1.00113.90           C  
ANISOU 5190  CB  ARG B 365    15575  16803  10899    882    -65   1069       C  
ATOM   5191  CG  ARG B 365     110.984  71.613  21.100  1.00135.54           C  
ANISOU 5191  CG  ARG B 365    18567  19622  13311   1034   -109   1152       C  
ATOM   5192  CD  ARG B 365     109.488  71.767  20.821  1.00151.02           C  
ANISOU 5192  CD  ARG B 365    20664  21450  15268   1274   -383    993       C  
ATOM   5193  NE  ARG B 365     108.982  73.104  21.135  1.00155.76           N  
ANISOU 5193  NE  ARG B 365    21484  21799  15899   1243   -523   1125       N  
ATOM   5194  CZ  ARG B 365     107.725  73.495  20.937  1.00149.04           C  
ANISOU 5194  CZ  ARG B 365    20770  20818  15041   1451   -767   1025       C  
ATOM   5195  NH1 ARG B 365     106.836  72.652  20.428  1.00145.83           N  
ANISOU 5195  NH1 ARG B 365    20288  20513  14608   1680   -903    795       N  
ATOM   5196  NH2 ARG B 365     107.358  74.732  21.246  1.00144.76           N  
ANISOU 5196  NH2 ARG B 365    20443  20041  14518   1436   -890   1149       N  
ATOM   5197  N   ASN B 366     110.456  68.408  21.214  1.00 89.26           N  
ANISOU 5197  N   ASN B 366    12229  14052   7633   1335   -135    555       N  
ATOM   5198  CA  ASN B 366     110.849  67.282  20.361  1.00 88.81           C  
ANISOU 5198  CA  ASN B 366    12120  14221   7402   1474    -60    436       C  
ATOM   5199  C   ASN B 366     110.746  65.938  21.069  1.00 84.18           C  
ANISOU 5199  C   ASN B 366    11290  13655   7040   1506    -78    187       C  
ATOM   5200  O   ASN B 366     111.328  64.952  20.603  1.00 87.81           O  
ANISOU 5200  O   ASN B 366    11681  14289   7394   1593     15     93       O  
ATOM   5201  CB  ASN B 366     112.272  67.445  19.816  1.00 81.00           C  
ANISOU 5201  CB  ASN B 366    11138  13441   6196   1376    208    646       C  
ATOM   5202  CG  ASN B 366     112.485  68.765  19.127  1.00 78.30           C  
ANISOU 5202  CG  ASN B 366    11045  13078   5626   1303    249    927       C  
ATOM   5203  OD1 ASN B 366     113.341  69.550  19.534  1.00 83.77           O  
ANISOU 5203  OD1 ASN B 366    11723  13753   6352   1068    398   1163       O  
ATOM   5204  ND2 ASN B 366     111.713  69.021  18.072  1.00 81.81           N  
ANISOU 5204  ND2 ASN B 366    11732  13515   5835   1496    104    910       N  
ATOM   5205  N   ARG B 367     110.034  65.877  22.196  1.00 73.06           N  
ANISOU 5205  N   ARG B 367     9761  12069   5930   1443   -193     83       N  
ATOM   5206  CA  ARG B 367     109.895  64.610  22.905  1.00 67.46           C  
ANISOU 5206  CA  ARG B 367     8839  11357   5435   1454   -216   -134       C  
ATOM   5207  C   ARG B 367     109.158  63.592  22.044  1.00 67.67           C  
ANISOU 5207  C   ARG B 367     8900  11444   5369   1666   -374   -363       C  
ATOM   5208  O   ARG B 367     109.558  62.425  21.962  1.00 67.66           O  
ANISOU 5208  O   ARG B 367     8807  11529   5370   1721   -335   -505       O  
ATOM   5209  CB  ARG B 367     109.172  64.830  24.241  1.00 66.35           C  
ANISOU 5209  CB  ARG B 367     8582  11022   5606   1349   -305   -182       C  
ATOM   5210  CG  ARG B 367     107.745  65.370  24.109  1.00 68.91           C  
ANISOU 5210  CG  ARG B 367     8992  11223   5968   1455   -530   -249       C  
ATOM   5211  CD  ARG B 367     107.166  65.872  25.418  1.00 66.49           C  
ANISOU 5211  CD  ARG B 367     8591  10749   5923   1357   -576   -247       C  
ATOM   5212  NE  ARG B 367     105.824  66.417  25.223  1.00 75.80           N  
ANISOU 5212  NE  ARG B 367     9837  11842   7121   1489   -785   -312       N  
ATOM   5213  CZ  ARG B 367     105.564  67.653  24.805  1.00 88.32           C  
ANISOU 5213  CZ  ARG B 367    11624  13358   8577   1544   -853   -178       C  
ATOM   5214  NH1 ARG B 367     106.554  68.487  24.522  1.00 90.78           N  
ANISOU 5214  NH1 ARG B 367    12100  13663   8730   1448   -726     44       N  
ATOM   5215  NH2 ARG B 367     104.309  68.052  24.656  1.00 92.40           N  
ANISOU 5215  NH2 ARG B 367    12177  13810   9121   1694  -1057   -262       N  
ATOM   5216  N   HIS B 368     108.099  64.026  21.363  1.00 71.56           N  
ANISOU 5216  N   HIS B 368     9537  11886   5768   1796   -570   -405       N  
ATOM   5217  CA  HIS B 368     107.354  63.116  20.507  1.00 81.02           C  
ANISOU 5217  CA  HIS B 368    10779  13131   6874   1992   -756   -627       C  
ATOM   5218  C   HIS B 368     108.222  62.619  19.354  1.00 87.35           C  
ANISOU 5218  C   HIS B 368    11701  14128   7361   2121   -649   -626       C  
ATOM   5219  O   HIS B 368     108.279  61.413  19.081  1.00 86.05           O  
ANISOU 5219  O   HIS B 368    11492  14022   7180   2224   -692   -823       O  
ATOM   5220  CB  HIS B 368     106.091  63.810  19.999  1.00 85.32           C  
ANISOU 5220  CB  HIS B 368    11453  13596   7371   2111   -996   -655       C  
ATOM   5221  CG  HIS B 368     105.052  62.864  19.494  1.00 95.94           C  
ANISOU 5221  CG  HIS B 368    12773  14940   8740   2265  -1245   -914       C  
ATOM   5222  ND1 HIS B 368     103.894  62.593  20.189  1.00100.06           N  
ANISOU 5222  ND1 HIS B 368    13129  15349   9540   2239  -1431  -1062       N  
ATOM   5223  CD2 HIS B 368     104.989  62.135  18.355  1.00101.22           C  
ANISOU 5223  CD2 HIS B 368    13562  15710   9187   2443  -1349  -1053       C  
ATOM   5224  CE1 HIS B 368     103.167  61.727  19.506  1.00105.09           C  
ANISOU 5224  CE1 HIS B 368    13773  16012  10145   2369  -1647  -1276       C  
ATOM   5225  NE2 HIS B 368     103.807  61.436  18.387  1.00101.55           N  
ANISOU 5225  NE2 HIS B 368    13512  15682   9392   2503  -1613  -1283       N  
ATOM   5226  N   ARG B 369     108.934  63.534  18.690  1.00 85.24           N  
ANISOU 5226  N   ARG B 369    11592  13961   6834   2116   -501   -400       N  
ATOM   5227  CA  ARG B 369     109.796  63.144  17.579  1.00 92.01           C  
ANISOU 5227  CA  ARG B 369    12560  15039   7362   2247   -365   -376       C  
ATOM   5228  C   ARG B 369     110.919  62.223  18.044  1.00 85.16           C  
ANISOU 5228  C   ARG B 369    11504  14292   6561   2197   -160   -419       C  
ATOM   5229  O   ARG B 369     111.157  61.168  17.444  1.00 81.27           O  
ANISOU 5229  O   ARG B 369    11026  13920   5933   2371   -164   -591       O  
ATOM   5230  CB  ARG B 369     110.366  64.388  16.897  1.00106.42           C  
ANISOU 5230  CB  ARG B 369    14573  16948   8915   2205   -220    -84       C  
ATOM   5231  CG  ARG B 369     111.468  64.103  15.887  1.00118.34           C  
ANISOU 5231  CG  ARG B 369    16157  18726  10079   2301     -1     -3       C  
ATOM   5232  CD  ARG B 369     112.434  65.275  15.809  1.00133.12           C  
ANISOU 5232  CD  ARG B 369    18082  20678  11818   2115    242    342       C  
ATOM   5233  NE  ARG B 369     113.809  64.828  15.608  1.00146.30           N  
ANISOU 5233  NE  ARG B 369    19624  22612  13352   2090    535    423       N  
ATOM   5234  CZ  ARG B 369     114.881  65.577  15.846  1.00153.36           C  
ANISOU 5234  CZ  ARG B 369    20443  23603  14223   1870    784    702       C  
ATOM   5235  NH1 ARG B 369     114.740  66.817  16.297  1.00153.35           N  
ANISOU 5235  NH1 ARG B 369    20516  23425  14323   1650    762    925       N  
ATOM   5236  NH2 ARG B 369     116.096  65.084  15.639  1.00157.58           N  
ANISOU 5236  NH2 ARG B 369    20824  24411  14637   1872   1046    753       N  
ATOM   5237  N   LEU B 370     111.622  62.607  19.116  1.00 85.01           N  
ANISOU 5237  N   LEU B 370    11317  14236   6745   1975      6   -274       N  
ATOM   5238  CA  LEU B 370     112.748  61.802  19.584  1.00 81.22           C  
ANISOU 5238  CA  LEU B 370    10651  13882   6328   1934    198   -301       C  
ATOM   5239  C   LEU B 370     112.289  60.437  20.076  1.00 76.04           C  
ANISOU 5239  C   LEU B 370     9884  13137   5869   2018     56   -585       C  
ATOM   5240  O   LEU B 370     112.988  59.434  19.886  1.00 76.47           O  
ANISOU 5240  O   LEU B 370     9880  13318   5856   2129    138   -698       O  
ATOM   5241  CB  LEU B 370     113.502  62.539  20.690  1.00 85.93           C  
ANISOU 5241  CB  LEU B 370    11095  14435   7120   1671    361    -95       C  
ATOM   5242  CG  LEU B 370     114.475  63.631  20.246  1.00101.99           C  
ANISOU 5242  CG  LEU B 370    13184  16612   8956   1549    575    205       C  
ATOM   5243  CD1 LEU B 370     114.868  64.509  21.422  1.00101.27           C  
ANISOU 5243  CD1 LEU B 370    12984  16391   9102   1270    642    388       C  
ATOM   5244  CD2 LEU B 370     115.703  63.017  19.589  1.00115.15           C  
ANISOU 5244  CD2 LEU B 370    14771  18578  10402   1639    804    229       C  
ATOM   5245  N   LEU B 371     111.124  60.381  20.723  1.00 73.68           N  
ANISOU 5245  N   LEU B 371     9556  12624   5815   1967   -154   -698       N  
ATOM   5246  CA  LEU B 371     110.581  59.097  21.146  1.00 75.19           C  
ANISOU 5246  CA  LEU B 371     9660  12715   6195   2021   -307   -953       C  
ATOM   5247  C   LEU B 371     110.260  58.218  19.945  1.00 76.44           C  
ANISOU 5247  C   LEU B 371     9965  12947   6132   2264   -447  -1155       C  
ATOM   5248  O   LEU B 371     110.586  57.025  19.937  1.00 70.75           O  
ANISOU 5248  O   LEU B 371     9213  12244   5424   2356   -463  -1329       O  
ATOM   5249  CB  LEU B 371     109.335  59.315  22.001  1.00 80.87           C  
ANISOU 5249  CB  LEU B 371    10308  13220   7200   1909   -492  -1010       C  
ATOM   5250  CG  LEU B 371     108.836  58.146  22.844  1.00 77.79           C  
ANISOU 5250  CG  LEU B 371     9779  12696   7082   1864   -608  -1208       C  
ATOM   5251  CD1 LEU B 371     109.800  57.840  23.990  1.00 61.82           C  
ANISOU 5251  CD1 LEU B 371     7601  10658   5229   1723   -426  -1144       C  
ATOM   5252  CD2 LEU B 371     107.444  58.455  23.356  1.00 77.25           C  
ANISOU 5252  CD2 LEU B 371     9655  12471   7227   1793   -799  -1260       C  
ATOM   5253  N   ALA B 372     109.630  58.794  18.915  1.00 79.71           N  
ANISOU 5253  N   ALA B 372    10563  13394   6331   2382   -565  -1139       N  
ATOM   5254  CA  ALA B 372     109.314  58.025  17.715  1.00 82.09           C  
ANISOU 5254  CA  ALA B 372    11034  13767   6392   2627   -718  -1334       C  
ATOM   5255  C   ALA B 372     110.576  57.526  17.026  1.00 82.43           C  
ANISOU 5255  C   ALA B 372    11134  14032   6154   2777   -511  -1327       C  
ATOM   5256  O   ALA B 372     110.645  56.362  16.611  1.00 81.54           O  
ANISOU 5256  O   ALA B 372    11072  13942   5966   2951   -597  -1550       O  
ATOM   5257  CB  ALA B 372     108.483  58.869  16.752  1.00 69.24           C  
ANISOU 5257  CB  ALA B 372     9603  12145   4561   2729   -873  -1289       C  
ATOM   5258  N   ILE B 373     111.580  58.395  16.892  1.00 79.25           N  
ANISOU 5258  N   ILE B 373    10722  13797   5592   2714   -241  -1074       N  
ATOM   5259  CA  ILE B 373     112.822  58.009  16.227  1.00 79.65           C  
ANISOU 5259  CA  ILE B 373    10792  14108   5363   2858    -11  -1043       C  
ATOM   5260  C   ILE B 373     113.426  56.784  16.896  1.00 87.77           C  
ANISOU 5260  C   ILE B 373    11659  15135   6556   2891     35  -1210       C  
ATOM   5261  O   ILE B 373     113.812  55.817  16.230  1.00 94.88           O  
ANISOU 5261  O   ILE B 373    12635  16153   7264   3129     34  -1384       O  
ATOM   5262  CB  ILE B 373     113.805  59.193  16.203  1.00 80.44           C  
ANISOU 5262  CB  ILE B 373    10849  14377   5338   2710    282   -712       C  
ATOM   5263  CG1 ILE B 373     113.263  60.297  15.283  1.00 81.02           C  
ANISOU 5263  CG1 ILE B 373    11154  14463   5166   2735    228   -556       C  
ATOM   5264  CG2 ILE B 373     115.212  58.727  15.831  1.00 74.39           C  
ANISOU 5264  CG2 ILE B 373     9999  13903   4363   2814    561   -670       C  
ATOM   5265  CD1 ILE B 373     114.158  61.502  15.119  1.00 85.67           C  
ANISOU 5265  CD1 ILE B 373    11750  15198   5602   2577    494   -213       C  
ATOM   5266  N   HIS B 374     113.483  56.788  18.227  1.00 95.97           N  
ANISOU 5266  N   HIS B 374    12496  16027   7943   2672     57  -1171       N  
ATOM   5267  CA  HIS B 374     114.073  55.652  18.922  1.00 93.51           C  
ANISOU 5267  CA  HIS B 374    12044  15696   7789   2701     92  -1314       C  
ATOM   5268  C   HIS B 374     113.218  54.398  18.772  1.00 95.37           C  
ANISOU 5268  C   HIS B 374    12379  15760   8096   2846   -185  -1621       C  
ATOM   5269  O   HIS B 374     113.744  53.308  18.515  1.00 97.71           O  
ANISOU 5269  O   HIS B 374    12706  16113   8305   3034   -185  -1794       O  
ATOM   5270  CB  HIS B 374     114.286  55.976  20.396  1.00 77.93           C  
ANISOU 5270  CB  HIS B 374     9856  13595   6158   2433    164  -1195       C  
ATOM   5271  CG  HIS B 374     114.755  54.800  21.184  1.00 83.26           C  
ANISOU 5271  CG  HIS B 374    10411  14211   7013   2460    161  -1346       C  
ATOM   5272  ND1 HIS B 374     116.083  54.438  21.254  1.00 86.13           N  
ANISOU 5272  ND1 HIS B 374    10661  14771   7294   2537    371  -1310       N  
ATOM   5273  CD2 HIS B 374     114.071  53.869  21.888  1.00 80.62           C  
ANISOU 5273  CD2 HIS B 374    10062  13645   6924   2433    -33  -1533       C  
ATOM   5274  CE1 HIS B 374     116.199  53.347  21.990  1.00 85.61           C  
ANISOU 5274  CE1 HIS B 374    10531  14582   7414   2570    294  -1474       C  
ATOM   5275  NE2 HIS B 374     114.992  52.983  22.388  1.00 82.82           N  
ANISOU 5275  NE2 HIS B 374    10247  13961   7261   2496     52  -1603       N  
ATOM   5276  N   LEU B 375     111.899  54.530  18.924  1.00 92.37           N  
ANISOU 5276  N   LEU B 375    12049  15172   7877   2762   -431  -1695       N  
ATOM   5277  CA  LEU B 375     111.012  53.378  18.835  1.00 87.92           C  
ANISOU 5277  CA  LEU B 375    11561  14428   7417   2847   -715  -1971       C  
ATOM   5278  C   LEU B 375     110.913  52.816  17.421  1.00104.41           C  
ANISOU 5278  C   LEU B 375    13884  16613   9172   3139   -841  -2150       C  
ATOM   5279  O   LEU B 375     110.369  51.721  17.246  1.00116.40           O  
ANISOU 5279  O   LEU B 375    15492  17990  10743   3236  -1079  -2400       O  
ATOM   5280  CB  LEU B 375     109.622  53.764  19.339  1.00 80.65           C  
ANISOU 5280  CB  LEU B 375    10594  13299   6750   2672   -932  -1983       C  
ATOM   5281  CG  LEU B 375     109.474  53.856  20.862  1.00 77.34           C  
ANISOU 5281  CG  LEU B 375     9961  12724   6703   2411   -886  -1904       C  
ATOM   5282  CD1 LEU B 375     108.298  54.758  21.215  1.00 80.06           C  
ANISOU 5282  CD1 LEU B 375    10250  12959   7208   2263  -1006  -1828       C  
ATOM   5283  CD2 LEU B 375     109.337  52.489  21.525  1.00 66.17           C  
ANISOU 5283  CD2 LEU B 375     8497  11141   5506   2383  -1006  -2096       C  
ATOM   5284  N   ALA B 376     111.425  53.531  16.415  1.00101.88           N  
ANISOU 5284  N   ALA B 376    13680  16524   8506   3277   -692  -2025       N  
ATOM   5285  CA  ALA B 376     111.343  53.046  15.041  1.00102.36           C  
ANISOU 5285  CA  ALA B 376    13987  16693   8210   3576   -803  -2191       C  
ATOM   5286  C   ALA B 376     112.220  51.820  14.814  1.00103.39           C  
ANISOU 5286  C   ALA B 376    14160  16906   8215   3801   -747  -2377       C  
ATOM   5287  O   ALA B 376     111.925  51.004  13.932  1.00109.38           O  
ANISOU 5287  O   ALA B 376    15107  17607   8843   4013   -933  -2582       O  
ATOM   5288  CB  ALA B 376     111.723  54.162  14.068  1.00104.60           C  
ANISOU 5288  CB  ALA B 376    14390  17216   8138   3657   -628  -1980       C  
ATOM   5289  N   THR B 377     113.295  51.676  15.583  1.00 95.31           N  
ANISOU 5289  N   THR B 377    12950  15968   7297   3738   -503  -2282       N  
ATOM   5290  CA  THR B 377     114.168  50.515  15.490  1.00 96.16           C  
ANISOU 5290  CA  THR B 377    13074  16145   7317   3961   -447  -2454       C  
ATOM   5291  C   THR B 377     113.660  49.326  16.298  1.00 91.84           C  
ANISOU 5291  C   THR B 377    12521  15299   7074   3916   -693  -2685       C  
ATOM   5292  O   THR B 377     114.319  48.280  16.317  1.00 80.56           O  
ANISOU 5292  O   THR B 377    11124  13866   5620   4096   -687  -2837       O  
ATOM   5293  CB  THR B 377     115.590  50.881  15.941  1.00101.56           C  
ANISOU 5293  CB  THR B 377    13540  17069   7978   3923    -84  -2247       C  
ATOM   5294  OG1 THR B 377     115.541  51.566  17.200  1.00107.59           O  
ANISOU 5294  OG1 THR B 377    14082  17727   9070   3593     -9  -2057       O  
ATOM   5295  CG2 THR B 377     116.261  51.777  14.911  1.00 99.40           C  
ANISOU 5295  CG2 THR B 377    13282  17055   7431   3973    155  -2012       C  
ATOM   5296  N   HIS B 378     112.513  49.460  16.963  1.00 92.85           N  
ANISOU 5296  N   HIS B 378    12603  15164   7511   3670   -904  -2693       N  
ATOM   5297  CA  HIS B 378     111.907  48.391  17.751  1.00 89.95           C  
ANISOU 5297  CA  HIS B 378    12227  14496   7454   3574  -1142  -2879       C  
ATOM   5298  C   HIS B 378     110.446  48.205  17.369  1.00 86.35           C  
ANISOU 5298  C   HIS B 378    11894  13836   7080   3520  -1488  -3029       C  
ATOM   5299  O   HIS B 378     109.594  47.924  18.218  1.00 81.47           O  
ANISOU 5299  O   HIS B 378    11182  12978   6796   3291  -1656  -3064       O  
ATOM   5300  CB  HIS B 378     112.014  48.662  19.254  1.00 79.47           C  
ANISOU 5300  CB  HIS B 378    10653  13053   6491   3275  -1029  -2718       C  
ATOM   5301  CG  HIS B 378     113.414  48.828  19.759  1.00 72.44           C  
ANISOU 5301  CG  HIS B 378     9612  12346   5567   3298   -721  -2573       C  
ATOM   5302  ND1 HIS B 378     114.033  50.056  19.850  1.00 75.29           N  
ANISOU 5302  ND1 HIS B 378     9831  12920   5855   3197   -453  -2308       N  
ATOM   5303  CD2 HIS B 378     114.310  47.921  20.213  1.00 72.17           C  
ANISOU 5303  CD2 HIS B 378     9543  12310   5569   3406   -655  -2657       C  
ATOM   5304  CE1 HIS B 378     115.250  49.900  20.342  1.00 71.40           C  
ANISOU 5304  CE1 HIS B 378     9198  12564   5366   3229   -234  -2235       C  
ATOM   5305  NE2 HIS B 378     115.443  48.614  20.568  1.00 75.02           N  
ANISOU 5305  NE2 HIS B 378     9716  12902   5886   3370   -349  -2446       N  
ATOM   5306  N   LEU B 379     110.121  48.368  16.088  1.00 94.70           N  
ANISOU 5306  N   LEU B 379    13153  14996   7831   3726  -1601  -3115       N  
ATOM   5307  CA  LEU B 379     108.720  48.294  15.685  1.00104.07           C  
ANISOU 5307  CA  LEU B 379    14436  16013   9092   3673  -1943  -3249       C  
ATOM   5308  C   LEU B 379     108.192  46.862  15.705  1.00103.42           C  
ANISOU 5308  C   LEU B 379    14478  15675   9143   3713  -2263  -3544       C  
ATOM   5309  O   LEU B 379     106.998  46.651  15.946  1.00 86.25           O  
ANISOU 5309  O   LEU B 379    12270  13292   7208   3537  -2541  -3630       O  
ATOM   5310  CB  LEU B 379     108.545  48.924  14.303  1.00101.78           C  
ANISOU 5310  CB  LEU B 379    14331  15890   8452   3874  -1972  -3229       C  
ATOM   5311  CG  LEU B 379     108.727  50.443  14.262  1.00 87.22           C  
ANISOU 5311  CG  LEU B 379    12406  14254   6480   3798  -1743  -2948       C  
ATOM   5312  CD1 LEU B 379     108.594  50.942  12.847  1.00 80.99           C  
ANISOU 5312  CD1 LEU B 379    11812  13574   5385   3982  -1762  -2898       C  
ATOM   5313  CD2 LEU B 379     107.717  51.141  15.158  1.00 75.60           C  
ANISOU 5313  CD2 LEU B 379    10743  12624   5359   3497  -1834  -2832       C  
ATOM   5314  N   HIS B 380     109.061  45.871  15.481  1.00103.93           N  
ANISOU 5314  N   HIS B 380    14654  15717   9117   3907  -2214  -3655       N  
ATOM   5315  CA  HIS B 380     108.603  44.484  15.446  1.00100.28           C  
ANISOU 5315  CA  HIS B 380    14328  14957   8816   3926  -2511  -3888       C  
ATOM   5316  C   HIS B 380     108.097  44.034  16.812  1.00 93.69           C  
ANISOU 5316  C   HIS B 380    13367  13899   8332   3651  -2642  -3950       C  
ATOM   5317  O   HIS B 380     107.060  43.370  16.911  1.00 91.14           O  
ANISOU 5317  O   HIS B 380    13088  13314   8228   3506  -2956  -4088       O  
ATOM   5318  CB  HIS B 380     109.726  43.565  14.959  1.00107.62           C  
ANISOU 5318  CB  HIS B 380    15396  15909   9584   4207  -2411  -3963       C  
ATOM   5319  CG  HIS B 380     111.018  43.729  15.699  1.00119.19           C  
ANISOU 5319  CG  HIS B 380    16715  17554  11019   4247  -2079  -3840       C  
ATOM   5320  ND1 HIS B 380     111.380  42.914  16.751  1.00119.07           N  
ANISOU 5320  ND1 HIS B 380    16655  17377  11211   4184  -2096  -3914       N  
ATOM   5321  CD2 HIS B 380     112.032  44.612  15.542  1.00122.66           C  
ANISOU 5321  CD2 HIS B 380    17034  18316  11256   4333  -1728  -3639       C  
ATOM   5322  CE1 HIS B 380     112.564  43.285  17.206  1.00118.96           C  
ANISOU 5322  CE1 HIS B 380    16490  17587  11123   4247  -1773  -3774       C  
ATOM   5323  NE2 HIS B 380     112.980  44.315  16.492  1.00119.32           N  
ANISOU 5323  NE2 HIS B 380    16476  17932  10929   4323  -1543  -3600       N  
ATOM   5324  N   THR B 381     108.807  44.393  17.879  1.00 95.78           N  
ANISOU 5324  N   THR B 381    13418  14219   8754   3510  -2357  -3751       N  
ATOM   5325  CA  THR B 381     108.403  43.948  19.207  1.00 93.70           C  
ANISOU 5325  CA  THR B 381    13002  13707   8892   3210  -2413  -3712       C  
ATOM   5326  C   THR B 381     107.300  44.827  19.785  1.00 91.42           C  
ANISOU 5326  C   THR B 381    12500  13377   8857   2896  -2446  -3557       C  
ATOM   5327  O   THR B 381     106.371  44.316  20.422  1.00 85.46           O  
ANISOU 5327  O   THR B 381    11682  12388   8400   2663  -2646  -3610       O  
ATOM   5328  CB  THR B 381     109.613  43.921  20.139  1.00 94.19           C  
ANISOU 5328  CB  THR B 381    12937  13836   9014   3204  -2119  -3575       C  
ATOM   5329  OG1 THR B 381     110.440  45.059  19.871  1.00 97.15           O  
ANISOU 5329  OG1 THR B 381    13203  14529   9180   3289  -1803  -3375       O  
ATOM   5330  CG2 THR B 381     110.426  42.654  19.914  1.00 74.98           C  
ANISOU 5330  CG2 THR B 381    10705  11324   6461   3464  -2183  -3779       C  
ATOM   5331  N   THR B 382     107.381  46.145  19.564  1.00 95.35           N  
ANISOU 5331  N   THR B 382    12890  14101   9237   2890  -2253  -3363       N  
ATOM   5332  CA  THR B 382     106.396  47.064  20.134  1.00 97.85           C  
ANISOU 5332  CA  THR B 382    13007  14394   9777   2631  -2267  -3213       C  
ATOM   5333  C   THR B 382     105.029  46.881  19.491  1.00 92.00           C  
ANISOU 5333  C   THR B 382    12326  13549   9082   2601  -2611  -3368       C  
ATOM   5334  O   THR B 382     104.005  46.862  20.182  1.00 87.07           O  
ANISOU 5334  O   THR B 382    11538  12785   8757   2354  -2742  -3355       O  
ATOM   5335  CB  THR B 382     106.854  48.515  19.968  1.00100.29           C  
ANISOU 5335  CB  THR B 382    13235  14948   9924   2657  -2003  -2978       C  
ATOM   5336  OG1 THR B 382     107.494  48.673  18.694  1.00104.92           O  
ANISOU 5336  OG1 THR B 382    14016  15731  10120   2946  -1951  -3019       O  
ATOM   5337  CG2 THR B 382     107.809  48.922  21.084  1.00 93.42           C  
ANISOU 5337  CG2 THR B 382    12192  14130   9172   2532  -1694  -2774       C  
ATOM   5338  N   CYS B 383     104.992  46.769  18.164  1.00 93.48           N  
ANISOU 5338  N   CYS B 383    12735  13819   8966   2854  -2758  -3513       N  
ATOM   5339  CA  CYS B 383     103.723  46.639  17.466  1.00 92.25           C  
ANISOU 5339  CA  CYS B 383    12641  13580   8829   2845  -3108  -3669       C  
ATOM   5340  C   CYS B 383     103.141  45.237  17.559  1.00 92.16           C  
ANISOU 5340  C   CYS B 383    12713  13299   9003   2769  -3430  -3910       C  
ATOM   5341  O   CYS B 383     102.011  45.027  17.110  1.00 79.59           O  
ANISOU 5341  O   CYS B 383    11137  11614   7488   2710  -3752  -4046       O  
ATOM   5342  CB  CYS B 383     103.882  47.044  15.997  1.00 99.12           C  
ANISOU 5342  CB  CYS B 383    13745  14631   9284   3152  -3165  -3737       C  
ATOM   5343  SG  CYS B 383     104.566  48.711  15.721  1.00 94.76           S  
ANISOU 5343  SG  CYS B 383    13146  14385   8474   3239  -2806  -3438       S  
ATOM   5344  N   THR B 384     103.870  44.279  18.127  1.00 91.86           N  
ANISOU 5344  N   THR B 384    12733  13127   9042   2763  -3368  -3965       N  
ATOM   5345  CA  THR B 384     103.317  42.960  18.404  1.00 94.51           C  
ANISOU 5345  CA  THR B 384    13147  13163   9598   2637  -3666  -4160       C  
ATOM   5346  C   THR B 384     102.951  42.777  19.871  1.00 88.32           C  
ANISOU 5346  C   THR B 384    12119  12218   9219   2281  -3598  -4026       C  
ATOM   5347  O   THR B 384     102.399  41.732  20.231  1.00 91.19           O  
ANISOU 5347  O   THR B 384    12521  12319   9807   2112  -3836  -4149       O  
ATOM   5348  CB  THR B 384     104.293  41.857  17.970  1.00 96.47           C  
ANISOU 5348  CB  THR B 384    13679  13321   9654   2895  -3695  -4335       C  
ATOM   5349  OG1 THR B 384     105.610  42.144  18.457  1.00 99.86           O  
ANISOU 5349  OG1 THR B 384    14063  13906   9973   3010  -3335  -4196       O  
ATOM   5350  CG2 THR B 384     104.330  41.759  16.455  1.00 99.97           C  
ANISOU 5350  CG2 THR B 384    14340  13824   9821   3177  -3773  -4407       C  
ATOM   5351  N   HIS B 385     103.236  43.764  20.717  1.00 82.26           N  
ANISOU 5351  N   HIS B 385    11118  11595   8542   2160  -3286  -3777       N  
ATOM   5352  CA  HIS B 385     102.889  43.721  22.131  1.00 94.64           C  
ANISOU 5352  CA  HIS B 385    12453  13043  10464   1840  -3193  -3632       C  
ATOM   5353  C   HIS B 385     101.565  44.438  22.373  1.00 90.35           C  
ANISOU 5353  C   HIS B 385    11669  12535  10125   1617  -3284  -3555       C  
ATOM   5354  O   HIS B 385     101.301  45.492  21.786  1.00 82.48           O  
ANISOU 5354  O   HIS B 385    10622  11731   8985   1716  -3249  -3495       O  
ATOM   5355  CB  HIS B 385     103.986  44.361  22.984  1.00102.10           C  
ANISOU 5355  CB  HIS B 385    13289  14115  11388   1845  -2813  -3416       C  
ATOM   5356  CG  HIS B 385     103.816  44.137  24.454  1.00110.01           C  
ANISOU 5356  CG  HIS B 385    14111  14977  12711   1558  -2715  -3288       C  
ATOM   5357  ND1 HIS B 385     102.959  44.891  25.225  1.00112.17           N  
ANISOU 5357  ND1 HIS B 385    14131  15284  13203   1317  -2654  -3137       N  
ATOM   5358  CD2 HIS B 385     104.408  43.260  25.298  1.00113.42           C  
ANISOU 5358  CD2 HIS B 385    14591  15241  13262   1492  -2664  -3286       C  
ATOM   5359  CE1 HIS B 385     103.017  44.478  26.478  1.00109.89           C  
ANISOU 5359  CE1 HIS B 385    13744  14861  13148   1106  -2561  -3045       C  
ATOM   5360  NE2 HIS B 385     103.892  43.492  26.551  1.00111.43           N  
ANISOU 5360  NE2 HIS B 385    14123  14925  13289   1202  -2570  -3127       N  
ATOM   5361  N   LYS B 386     100.747  43.868  23.263  1.00 89.75           N  
ANISOU 5361  N   LYS B 386    11443  12279  10380   1320  -3395  -3548       N  
ATOM   5362  CA  LYS B 386      99.400  44.386  23.494  1.00 97.21           C  
ANISOU 5362  CA  LYS B 386    12134  13262  11539   1108  -3508  -3500       C  
ATOM   5363  C   LYS B 386      99.430  45.841  23.936  1.00 95.18           C  
ANISOU 5363  C   LYS B 386    11673  13229  11263   1112  -3235  -3283       C  
ATOM   5364  O   LYS B 386      98.678  46.675  23.418  1.00 97.81           O  
ANISOU 5364  O   LYS B 386    11909  13699  11556   1157  -3318  -3275       O  
ATOM   5365  CB  LYS B 386      98.680  43.531  24.538  1.00105.43           C  
ANISOU 5365  CB  LYS B 386    13026  14094  12937    769  -3601  -3487       C  
ATOM   5366  CG  LYS B 386      97.314  44.073  24.952  1.00110.98           C  
ANISOU 5366  CG  LYS B 386    13408  14874  13887    535  -3669  -3414       C  
ATOM   5367  CD  LYS B 386      96.531  43.048  25.767  1.00115.72           C  
ANISOU 5367  CD  LYS B 386    13884  15265  14819    190  -3808  -3426       C  
ATOM   5368  CE  LYS B 386      95.109  43.517  26.056  1.00114.60           C  
ANISOU 5368  CE  LYS B 386    13394  15232  14916    -29  -3897  -3374       C  
ATOM   5369  NZ  LYS B 386      94.284  42.447  26.689  1.00115.70           N  
ANISOU 5369  NZ  LYS B 386    13411  15177  15371   -384  -4063  -3392       N  
ATOM   5370  N   LEU B 387     100.287  46.166  24.898  1.00 91.63           N  
ANISOU 5370  N   LEU B 387    11169  12806  10840   1072  -2928  -3112       N  
ATOM   5371  CA  LEU B 387     100.289  47.517  25.439  1.00 91.13           C  
ANISOU 5371  CA  LEU B 387    10925  12917  10784   1051  -2687  -2908       C  
ATOM   5372  C   LEU B 387     101.199  48.453  24.655  1.00 89.08           C  
ANISOU 5372  C   LEU B 387    10801  12840  10206   1309  -2533  -2845       C  
ATOM   5373  O   LEU B 387     100.854  49.623  24.456  1.00 97.70           O  
ANISOU 5373  O   LEU B 387    11812  14075  11233   1354  -2477  -2745       O  
ATOM   5374  CB  LEU B 387     100.700  47.490  26.911  1.00 96.61           C  
ANISOU 5374  CB  LEU B 387    11489  13551  11669    864  -2446  -2746       C  
ATOM   5375  CG  LEU B 387     100.562  48.821  27.653  1.00104.15           C  
ANISOU 5375  CG  LEU B 387    12252  14648  12673    810  -2223  -2546       C  
ATOM   5376  CD1 LEU B 387      99.214  49.483  27.359  1.00109.94           C  
ANISOU 5376  CD1 LEU B 387    12813  15470  13490    772  -2370  -2562       C  
ATOM   5377  CD2 LEU B 387     100.746  48.608  29.140  1.00 99.29           C  
ANISOU 5377  CD2 LEU B 387    11512  13947  12268    605  -2041  -2419       C  
ATOM   5378  N   ALA B 388     102.349  47.962  24.193  1.00 79.59           N  
ANISOU 5378  N   ALA B 388     9805  11640   8796   1483  -2463  -2898       N  
ATOM   5379  CA  ALA B 388     103.278  48.832  23.481  1.00 79.31           C  
ANISOU 5379  CA  ALA B 388     9879  11799   8454   1706  -2285  -2814       C  
ATOM   5380  C   ALA B 388     102.705  49.304  22.147  1.00 90.08           C  
ANISOU 5380  C   ALA B 388    11355  13270   9600   1881  -2465  -2898       C  
ATOM   5381  O   ALA B 388     102.960  50.443  21.735  1.00 93.95           O  
ANISOU 5381  O   ALA B 388    11863  13926   9908   1983  -2333  -2767       O  
ATOM   5382  CB  ALA B 388     104.615  48.121  23.277  1.00 72.66           C  
ANISOU 5382  CB  ALA B 388     9205  10963   7441   1867  -2170  -2863       C  
ATOM   5383  N   SER B 389     101.914  48.464  21.469  1.00 94.12           N  
ANISOU 5383  N   SER B 389    11954  13679  10128   1910  -2780  -3111       N  
ATOM   5384  CA  SER B 389     101.331  48.876  20.193  1.00 93.63           C  
ANISOU 5384  CA  SER B 389    12011  13713   9852   2087  -2982  -3204       C  
ATOM   5385  C   SER B 389     100.422  50.083  20.358  1.00 88.76           C  
ANISOU 5385  C   SER B 389    11213  13190   9322   2011  -2988  -3076       C  
ATOM   5386  O   SER B 389     100.311  50.906  19.440  1.00 86.47           O  
ANISOU 5386  O   SER B 389    11027  13034   8794   2187  -3025  -3051       O  
ATOM   5387  CB  SER B 389     100.548  47.729  19.554  1.00 94.81           C  
ANISOU 5387  CB  SER B 389    12267  13710  10045   2098  -3356  -3465       C  
ATOM   5388  OG  SER B 389      99.610  47.175  20.459  1.00 92.53           O  
ANISOU 5388  OG  SER B 389    11770  13258  10128   1812  -3492  -3492       O  
ATOM   5389  N   THR B 390      99.760  50.203  21.513  1.00 85.89           N  
ANISOU 5389  N   THR B 390    10592  12759   9283   1765  -2953  -2995       N  
ATOM   5390  CA  THR B 390      98.897  51.356  21.752  1.00 87.64           C  
ANISOU 5390  CA  THR B 390    10632  13074   9592   1717  -2951  -2881       C  
ATOM   5391  C   THR B 390      99.696  52.651  21.728  1.00 83.38           C  
ANISOU 5391  C   THR B 390    10156  12674   8852   1831  -2684  -2675       C  
ATOM   5392  O   THR B 390      99.205  53.684  21.256  1.00 73.84           O  
ANISOU 5392  O   THR B 390     8952  11562   7541   1929  -2732  -2614       O  
ATOM   5393  CB  THR B 390      98.168  51.207  23.087  1.00 87.05           C  
ANISOU 5393  CB  THR B 390    10269  12922   9885   1446  -2916  -2823       C  
ATOM   5394  OG1 THR B 390      99.112  51.278  24.166  1.00 89.52           O  
ANISOU 5394  OG1 THR B 390    10545  13205  10263   1348  -2614  -2671       O  
ATOM   5395  CG2 THR B 390      97.423  49.885  23.148  1.00 83.99           C  
ANISOU 5395  CG2 THR B 390     9821  12384   9709   1290  -3173  -3003       C  
ATOM   5396  N   LEU B 391     100.934  52.612  22.231  1.00 78.69           N  
ANISOU 5396  N   LEU B 391     9612  12083   8201   1816  -2413  -2565       N  
ATOM   5397  CA  LEU B 391     101.775  53.802  22.219  1.00 75.30           C  
ANISOU 5397  CA  LEU B 391     9242  11777   7591   1890  -2161  -2360       C  
ATOM   5398  C   LEU B 391     102.277  54.104  20.812  1.00 79.18           C  
ANISOU 5398  C   LEU B 391     9979  12393   7711   2133  -2185  -2378       C  
ATOM   5399  O   LEU B 391     102.291  55.267  20.387  1.00 78.86           O  
ANISOU 5399  O   LEU B 391    10004  12451   7507   2215  -2126  -2242       O  
ATOM   5400  CB  LEU B 391     102.948  53.620  23.180  1.00 67.34           C  
ANISOU 5400  CB  LEU B 391     8192  10748   6647   1790  -1885  -2244       C  
ATOM   5401  CG  LEU B 391     104.048  54.676  23.053  1.00 64.59           C  
ANISOU 5401  CG  LEU B 391     7922  10529   6089   1858  -1626  -2043       C  
ATOM   5402  CD1 LEU B 391     103.487  56.041  23.397  1.00 61.02           C  
ANISOU 5402  CD1 LEU B 391     7398  10100   5688   1802  -1590  -1885       C  
ATOM   5403  CD2 LEU B 391     105.263  54.347  23.913  1.00 59.99           C  
ANISOU 5403  CD2 LEU B 391     7291   9939   5564   1774  -1386  -1957       C  
ATOM   5404  N   ILE B 392     102.691  53.069  20.078  1.00 81.22           N  
ANISOU 5404  N   ILE B 392    10394  12644   7821   2260  -2275  -2543       N  
ATOM   5405  CA  ILE B 392     103.152  53.259  18.706  1.00 85.55           C  
ANISOU 5405  CA  ILE B 392    11190  13327   7990   2512  -2296  -2575       C  
ATOM   5406  C   ILE B 392     102.048  53.885  17.859  1.00 89.45           C  
ANISOU 5406  C   ILE B 392    11747  13853   8387   2610  -2540  -2619       C  
ATOM   5407  O   ILE B 392     102.313  54.702  16.970  1.00 97.85           O  
ANISOU 5407  O   ILE B 392    12980  15047   9152   2775  -2495  -2529       O  
ATOM   5408  CB  ILE B 392     103.635  51.920  18.115  1.00 86.05           C  
ANISOU 5408  CB  ILE B 392    11413  13356   7927   2651  -2392  -2787       C  
ATOM   5409  CG1 ILE B 392     104.782  51.339  18.952  1.00 84.42           C  
ANISOU 5409  CG1 ILE B 392    11147  13125   7803   2585  -2151  -2740       C  
ATOM   5410  CG2 ILE B 392     104.065  52.095  16.659  1.00 82.85           C  
ANISOU 5410  CG2 ILE B 392    11274  13108   7098   2937  -2414  -2832       C  
ATOM   5411  CD1 ILE B 392     106.002  52.235  19.057  1.00 82.36           C  
ANISOU 5411  CD1 ILE B 392    10879  13042   7371   2619  -1807  -2510       C  
ATOM   5412  N   PHE B 393     100.791  53.523  18.126  1.00 82.02           N  
ANISOU 5412  N   PHE B 393    10665  12802   7697   2506  -2804  -2749       N  
ATOM   5413  CA  PHE B 393      99.694  54.139  17.390  1.00 80.28           C  
ANISOU 5413  CA  PHE B 393    10471  12623   7410   2604  -3054  -2794       C  
ATOM   5414  C   PHE B 393      99.501  55.593  17.802  1.00 90.65           C  
ANISOU 5414  C   PHE B 393    11698  14000   8746   2573  -2916  -2572       C  
ATOM   5415  O   PHE B 393      99.200  56.446  16.961  1.00 97.20           O  
ANISOU 5415  O   PHE B 393    12666  14910   9357   2735  -3004  -2525       O  
ATOM   5416  CB  PHE B 393      98.397  53.360  17.592  1.00 79.43           C  
ANISOU 5416  CB  PHE B 393    10194  12401   7584   2486  -3376  -2990       C  
ATOM   5417  CG  PHE B 393      97.200  54.038  16.994  1.00 91.88           C  
ANISOU 5417  CG  PHE B 393    11735  14032   9142   2574  -3638  -3031       C  
ATOM   5418  CD1 PHE B 393      97.081  54.172  15.616  1.00 98.74           C  
ANISOU 5418  CD1 PHE B 393    12857  14973   9689   2821  -3838  -3127       C  
ATOM   5419  CD2 PHE B 393      96.208  54.565  17.801  1.00 93.87           C  
ANISOU 5419  CD2 PHE B 393    11705  14278   9682   2431  -3684  -2976       C  
ATOM   5420  CE1 PHE B 393      95.989  54.809  15.059  1.00 97.28           C  
ANISOU 5420  CE1 PHE B 393    12644  14837   9478   2920  -4098  -3166       C  
ATOM   5421  CE2 PHE B 393      95.111  55.200  17.249  1.00 97.42           C  
ANISOU 5421  CE2 PHE B 393    12107  14793  10115   2538  -3934  -3020       C  
ATOM   5422  CZ  PHE B 393      95.002  55.323  15.878  1.00 95.54           C  
ANISOU 5422  CZ  PHE B 393    12125  14612   9563   2781  -4150  -3115       C  
ATOM   5423  N   LYS B 394      99.665  55.895  19.093  1.00 92.97           N  
ANISOU 5423  N   LYS B 394    11787  14247   9291   2376  -2711  -2436       N  
ATOM   5424  CA  LYS B 394      99.544  57.278  19.545  1.00 97.63           C  
ANISOU 5424  CA  LYS B 394    12322  14874   9900   2354  -2581  -2232       C  
ATOM   5425  C   LYS B 394     100.582  58.172  18.885  1.00 94.59           C  
ANISOU 5425  C   LYS B 394    12173  14585   9182   2482  -2389  -2053       C  
ATOM   5426  O   LYS B 394     100.347  59.374  18.714  1.00100.90           O  
ANISOU 5426  O   LYS B 394    13037  15412   9888   2541  -2379  -1912       O  
ATOM   5427  CB  LYS B 394      99.687  57.356  21.065  1.00102.42           C  
ANISOU 5427  CB  LYS B 394    12699  15410  10805   2131  -2382  -2127       C  
ATOM   5428  CG  LYS B 394      98.423  57.072  21.852  1.00104.17           C  
ANISOU 5428  CG  LYS B 394    12652  15571  11356   1998  -2536  -2218       C  
ATOM   5429  CD  LYS B 394      98.355  57.968  23.081  1.00102.33           C  
ANISOU 5429  CD  LYS B 394    12259  15323  11300   1881  -2347  -2051       C  
ATOM   5430  CE  LYS B 394      97.572  57.312  24.208  1.00100.10           C  
ANISOU 5430  CE  LYS B 394    11690  14981  11361   1687  -2375  -2117       C  
ATOM   5431  NZ  LYS B 394      98.358  56.228  24.873  1.00 91.77           N  
ANISOU 5431  NZ  LYS B 394    10615  13843  10411   1529  -2238  -2135       N  
ATOM   5432  N   LEU B 395     101.731  57.610  18.513  1.00 91.67           N  
ANISOU 5432  N   LEU B 395    11934  14267   8628   2526  -2234  -2051       N  
ATOM   5433  CA  LEU B 395     102.781  58.403  17.889  1.00 91.44           C  
ANISOU 5433  CA  LEU B 395    12103  14357   8283   2623  -2023  -1866       C  
ATOM   5434  C   LEU B 395     102.514  58.643  16.407  1.00 95.28           C  
ANISOU 5434  C   LEU B 395    12845  14935   8422   2862  -2189  -1914       C  
ATOM   5435  O   LEU B 395     102.970  59.652  15.857  1.00100.81           O  
ANISOU 5435  O   LEU B 395    13715  15720   8869   2936  -2070  -1726       O  
ATOM   5436  CB  LEU B 395     104.134  57.716  18.076  1.00 88.78           C  
ANISOU 5436  CB  LEU B 395    11776  14078   7879   2595  -1779  -1843       C  
ATOM   5437  CG  LEU B 395     104.685  57.652  19.499  1.00 84.86           C  
ANISOU 5437  CG  LEU B 395    11069  13513   7661   2374  -1570  -1745       C  
ATOM   5438  CD1 LEU B 395     105.483  56.373  19.669  1.00 87.07           C  
ANISOU 5438  CD1 LEU B 395    11324  13797   7963   2381  -1495  -1867       C  
ATOM   5439  CD2 LEU B 395     105.538  58.869  19.827  1.00 84.12           C  
ANISOU 5439  CD2 LEU B 395    10991  13480   7490   2294  -1310  -1473       C  
ATOM   5440  N   ILE B 396     101.790  57.741  15.750  1.00 95.87           N  
ANISOU 5440  N   ILE B 396    12965  14987   8474   2976  -2469  -2157       N  
ATOM   5441  CA  ILE B 396     101.438  57.920  14.345  1.00 92.55           C  
ANISOU 5441  CA  ILE B 396    12799  14647   7721   3218  -2667  -2227       C  
ATOM   5442  C   ILE B 396     100.163  58.734  14.194  1.00103.71           C  
ANISOU 5442  C   ILE B 396    14185  16019   9202   3258  -2916  -2226       C  
ATOM   5443  O   ILE B 396     100.107  59.674  13.398  1.00108.23           O  
ANISOU 5443  O   ILE B 396    14962  16657   9505   3408  -2945  -2111       O  
ATOM   5444  CB  ILE B 396     101.308  56.551  13.647  1.00 86.51           C  
ANISOU 5444  CB  ILE B 396    12126  13870   6872   3343  -2877  -2506       C  
ATOM   5445  CG1 ILE B 396     102.659  55.847  13.584  1.00 89.89           C  
ANISOU 5445  CG1 ILE B 396    12635  14370   7149   3382  -2626  -2504       C  
ATOM   5446  CG2 ILE B 396     100.733  56.718  12.255  1.00 89.27           C  
ANISOU 5446  CG2 ILE B 396    12720  14268   6929   3581  -3125  -2597       C  
ATOM   5447  CD1 ILE B 396     102.562  54.420  13.108  1.00 97.35           C  
ANISOU 5447  CD1 ILE B 396    13667  15261   8060   3492  -2833  -2792       C  
ATOM   5448  N   ASN B 397      99.127  58.386  14.959  1.00115.42           N  
ANISOU 5448  N   ASN B 397    15412  17400  11042   3130  -3098  -2348       N  
ATOM   5449  CA  ASN B 397      97.840  59.063  14.849  1.00134.57           C  
ANISOU 5449  CA  ASN B 397    17765  19808  13558   3185  -3355  -2376       C  
ATOM   5450  C   ASN B 397      97.934  60.553  15.151  1.00131.81           C  
ANISOU 5450  C   ASN B 397    17455  19468  13159   3193  -3204  -2126       C  
ATOM   5451  O   ASN B 397      97.071  61.319  14.707  1.00141.47           O  
ANISOU 5451  O   ASN B 397    18731  20699  14321   3328  -3409  -2120       O  
ATOM   5452  CB  ASN B 397      96.828  58.406  15.789  1.00156.72           C  
ANISOU 5452  CB  ASN B 397    20235  22529  16783   3009  -3511  -2523       C  
ATOM   5453  CG  ASN B 397      95.408  58.864  15.531  1.00175.49           C  
ANISOU 5453  CG  ASN B 397    22503  24921  19254   3094  -3827  -2608       C  
ATOM   5454  OD1 ASN B 397      95.053  59.228  14.409  1.00183.37           O  
ANISOU 5454  OD1 ASN B 397    23704  25971  19996   3310  -4036  -2652       O  
ATOM   5455  ND2 ASN B 397      94.586  58.857  16.576  1.00180.55           N  
ANISOU 5455  ND2 ASN B 397    22818  25528  20256   2934  -3860  -2628       N  
ATOM   5456  N   ASN B 398      98.957  60.983  15.890  1.00122.50           N  
ANISOU 5456  N   ASN B 398    16261  18277  12005   3057  -2872  -1926       N  
ATOM   5457  CA  ASN B 398      99.121  62.395  16.207  1.00119.12           C  
ANISOU 5457  CA  ASN B 398    15900  17828  11533   3046  -2736  -1685       C  
ATOM   5458  C   ASN B 398      99.415  63.177  14.936  1.00125.36           C  
ANISOU 5458  C   ASN B 398    17031  18685  11914   3244  -2765  -1567       C  
ATOM   5459  O   ASN B 398     100.498  63.050  14.354  1.00122.25           O  
ANISOU 5459  O   ASN B 398    16821  18375  11255   3270  -2578  -1478       O  
ATOM   5460  CB  ASN B 398     100.239  62.596  17.233  1.00116.73           C  
ANISOU 5460  CB  ASN B 398    15518  17496  11337   2842  -2390  -1506       C  
ATOM   5461  CG  ASN B 398     100.273  64.006  17.793  1.00115.03           C  
ANISOU 5461  CG  ASN B 398    15340  17214  11152   2793  -2284  -1282       C  
ATOM   5462  OD1 ASN B 398     100.354  64.984  17.051  1.00120.99           O  
ANISOU 5462  OD1 ASN B 398    16338  17978  11653   2911  -2308  -1141       O  
ATOM   5463  ND2 ASN B 398     100.222  64.115  19.113  1.00112.10           N  
ANISOU 5463  ND2 ASN B 398    14751  16764  11080   2621  -2173  -1247       N  
ATOM   5464  N   LYS B 399      98.449  63.992  14.506  1.00135.95           N  
ANISOU 5464  N   LYS B 399    18457  20002  13197   3394  -2998  -1561       N  
ATOM   5465  CA  LYS B 399      98.572  64.725  13.252  1.00142.25           C  
ANISOU 5465  CA  LYS B 399    19602  20850  13595   3601  -3072  -1456       C  
ATOM   5466  C   LYS B 399      99.546  65.891  13.357  1.00137.61           C  
ANISOU 5466  C   LYS B 399    19207  20239  12839   3531  -2795  -1142       C  
ATOM   5467  O   LYS B 399     100.145  66.283  12.349  1.00137.68           O  
ANISOU 5467  O   LYS B 399    19516  20319  12479   3637  -2730  -1008       O  
ATOM   5468  CB  LYS B 399      97.196  65.228  12.810  1.00144.87           C  
ANISOU 5468  CB  LYS B 399    19959  21152  13932   3793  -3432  -1554       C  
ATOM   5469  CG  LYS B 399      96.118  64.152  12.808  1.00146.50           C  
ANISOU 5469  CG  LYS B 399    19918  21359  14385   3806  -3707  -1849       C  
ATOM   5470  CD  LYS B 399      94.762  64.716  12.415  1.00151.04           C  
ANISOU 5470  CD  LYS B 399    20456  21871  15063   3942  -3984  -1912       C  
ATOM   5471  CE  LYS B 399      93.715  63.619  12.330  1.00154.73           C  
ANISOU 5471  CE  LYS B 399    20669  22332  15789   3915  -4231  -2184       C  
ATOM   5472  NZ  LYS B 399      92.424  64.132  11.796  1.00158.61           N  
ANISOU 5472  NZ  LYS B 399    21130  22786  16349   4062  -4497  -2250       N  
ATOM   5473  N   GLN B 400      99.721  66.451  14.554  1.00129.75           N  
ANISOU 5473  N   GLN B 400    18053  19145  12100   3348  -2635  -1017       N  
ATOM   5474  CA  GLN B 400     100.600  67.598  14.732  1.00128.01           C  
ANISOU 5474  CA  GLN B 400    18011  18873  11755   3252  -2403   -719       C  
ATOM   5475  C   GLN B 400     102.077  67.227  14.745  1.00114.51           C  
ANISOU 5475  C   GLN B 400    16323  17257   9931   3096  -2071   -590       C  
ATOM   5476  O   GLN B 400     102.922  68.126  14.787  1.00125.18           O  
ANISOU 5476  O   GLN B 400    17822  18586  11156   2992  -1868   -328       O  
ATOM   5477  CB  GLN B 400     100.256  68.337  16.030  1.00140.11           C  
ANISOU 5477  CB  GLN B 400    19381  20258  13597   3124  -2372   -648       C  
ATOM   5478  CG  GLN B 400      98.851  68.935  16.081  1.00155.88           C  
ANISOU 5478  CG  GLN B 400    21357  22173  15696   3297  -2672   -739       C  
ATOM   5479  CD  GLN B 400      97.769  67.908  16.367  1.00167.25           C  
ANISOU 5479  CD  GLN B 400    22489  23665  17393   3342  -2881  -1029       C  
ATOM   5480  OE1 GLN B 400      98.033  66.707  16.412  1.00174.08           O  
ANISOU 5480  OE1 GLN B 400    23201  24606  18337   3256  -2830  -1170       O  
ATOM   5481  NE2 GLN B 400      96.544  68.380  16.570  1.00168.72           N  
ANISOU 5481  NE2 GLN B 400    22581  23810  17715   3477  -3120  -1115       N  
ATOM   5482  N   GLU B 401     102.412  65.936  14.718  1.00 94.20           N  
ANISOU 5482  N   GLU B 401    13605  14785   7403   3078  -2019   -764       N  
ATOM   5483  CA  GLU B 401     103.799  65.475  14.697  1.00 96.18           C  
ANISOU 5483  CA  GLU B 401    13851  15153   7542   2970  -1715   -672       C  
ATOM   5484  C   GLU B 401     104.021  64.718  13.394  1.00105.94           C  
ANISOU 5484  C   GLU B 401    15259  16548   8445   3171  -1763   -785       C  
ATOM   5485  O   GLU B 401     104.032  63.477  13.377  1.00106.42           O  
ANISOU 5485  O   GLU B 401    15202  16659   8573   3211  -1807  -1008       O  
ATOM   5486  CB  GLU B 401     104.124  64.608  15.912  1.00 94.52           C  
ANISOU 5486  CB  GLU B 401    13331  14912   7671   2787  -1593   -774       C  
ATOM   5487  CG  GLU B 401     103.929  65.318  17.241  1.00 97.81           C  
ANISOU 5487  CG  GLU B 401    13586  15179   8399   2601  -1538   -672       C  
ATOM   5488  CD  GLU B 401     104.981  66.383  17.488  1.00106.43           C  
ANISOU 5488  CD  GLU B 401    14782  16258   9398   2453  -1290   -375       C  
ATOM   5489  OE1 GLU B 401     106.047  66.329  16.839  1.00110.74           O  
ANISOU 5489  OE1 GLU B 401    15439  16942   9696   2443  -1097   -252       O  
ATOM   5490  OE2 GLU B 401     104.747  67.267  18.339  1.00105.14           O  
ANISOU 5490  OE2 GLU B 401    14587  15952   9409   2345  -1289   -266       O  
ATOM   5491  N   PRO B 402     104.210  65.434  12.279  1.00106.96           N  
ANISOU 5491  N   PRO B 402    15691  16752   8198   3308  -1760   -635       N  
ATOM   5492  CA  PRO B 402     104.303  64.741  10.988  1.00110.11           C  
ANISOU 5492  CA  PRO B 402    16284  17305   8247   3538  -1835   -761       C  
ATOM   5493  C   PRO B 402     105.614  64.004  10.808  1.00116.40           C  
ANISOU 5493  C   PRO B 402    17051  18283   8894   3512  -1539   -739       C  
ATOM   5494  O   PRO B 402     105.617  62.890  10.270  1.00120.73           O  
ANISOU 5494  O   PRO B 402    17603  18903   9365   3655  -1611   -963       O  
ATOM   5495  CB  PRO B 402     104.137  65.882   9.977  1.00109.89           C  
ANISOU 5495  CB  PRO B 402    16580  17270   7903   3651  -1883   -560       C  
ATOM   5496  CG  PRO B 402     104.688  67.072  10.678  1.00106.29           C  
ANISOU 5496  CG  PRO B 402    16139  16750   7496   3452  -1682   -255       C  
ATOM   5497  CD  PRO B 402     104.383  66.890  12.141  1.00103.70           C  
ANISOU 5497  CD  PRO B 402    15482  16277   7641   3259  -1688   -339       C  
ATOM   5498  N   GLU B 403     106.730  64.590  11.253  1.00110.69           N  
ANISOU 5498  N   GLU B 403    16279  17617   8163   3323  -1210   -477       N  
ATOM   5499  CA  GLU B 403     108.018  63.924  11.102  1.00111.00           C  
ANISOU 5499  CA  GLU B 403    16254  17859   8063   3308   -915   -448       C  
ATOM   5500  C   GLU B 403     108.027  62.582  11.817  1.00106.84           C  
ANISOU 5500  C   GLU B 403    15474  17307   7814   3293   -951   -717       C  
ATOM   5501  O   GLU B 403     108.628  61.620  11.325  1.00103.23           O  
ANISOU 5501  O   GLU B 403    15028  17004   7190   3430   -869   -847       O  
ATOM   5502  CB  GLU B 403     109.144  64.821  11.622  1.00119.04           C  
ANISOU 5502  CB  GLU B 403    17207  18928   9095   3064   -582   -120       C  
ATOM   5503  CG  GLU B 403     110.551  64.317  11.311  1.00130.69           C  
ANISOU 5503  CG  GLU B 403    18619  20666  10370   3064   -251    -43       C  
ATOM   5504  CD  GLU B 403     111.605  64.898  12.243  1.00142.66           C  
ANISOU 5504  CD  GLU B 403    19938  22203  12062   2768     40    208       C  
ATOM   5505  OE1 GLU B 403     111.447  66.064  12.665  1.00148.21           O  
ANISOU 5505  OE1 GLU B 403    20691  22756  12864   2581     36    427       O  
ATOM   5506  OE2 GLU B 403     112.588  64.189  12.557  1.00144.26           O  
ANISOU 5506  OE2 GLU B 403    19940  22565  12307   2731    256    178       O  
ATOM   5507  N   SER B 404     107.351  62.496  12.965  1.00113.57           N  
ANISOU 5507  N   SER B 404    16111  17963   9076   3141  -1078   -804       N  
ATOM   5508  CA  SER B 404     107.214  61.218  13.654  1.00104.41           C  
ANISOU 5508  CA  SER B 404    14736  16747   8190   3116  -1148  -1055       C  
ATOM   5509  C   SER B 404     106.412  60.232  12.813  1.00 98.87           C  
ANISOU 5509  C   SER B 404    14147  16041   7380   3345  -1439  -1350       C  
ATOM   5510  O   SER B 404     106.876  59.124  12.522  1.00 89.59           O  
ANISOU 5510  O   SER B 404    12974  14942   6122   3455  -1417  -1521       O  
ATOM   5511  CB  SER B 404     106.554  61.432  15.015  1.00103.40           C  
ANISOU 5511  CB  SER B 404    14376  16416   8495   2906  -1226  -1065       C  
ATOM   5512  OG  SER B 404     107.245  62.416  15.762  1.00 99.90           O  
ANISOU 5512  OG  SER B 404    13865  15955   8138   2704   -992   -800       O  
ATOM   5513  N   ARG B 405     105.207  60.628  12.399  1.00 78.57           N  
ANISOU 5513  N   ARG B 405    11676  13377   4801   3432  -1732  -1418       N  
ATOM   5514  CA  ARG B 405     104.364  59.728  11.622  1.00 92.99           C  
ANISOU 5514  CA  ARG B 405    13601  15185   6546   3631  -2051  -1705       C  
ATOM   5515  C   ARG B 405     105.038  59.304  10.319  1.00100.26           C  
ANISOU 5515  C   ARG B 405    14746  16228   7121   3827  -1962  -1726       C  
ATOM   5516  O   ARG B 405     104.880  58.156   9.887  1.00102.54           O  
ANISOU 5516  O   ARG B 405    15050  16473   7437   3932  -2094  -1960       O  
ATOM   5517  CB  ARG B 405     103.014  60.392  11.351  1.00 95.68           C  
ANISOU 5517  CB  ARG B 405    13999  15425   6931   3691  -2366  -1740       C  
ATOM   5518  CG  ARG B 405     102.081  59.575  10.484  1.00111.82           C  
ANISOU 5518  CG  ARG B 405    16105  17384   8997   3833  -2677  -1992       C  
ATOM   5519  CD  ARG B 405     100.934  60.422   9.969  1.00130.41           C  
ANISOU 5519  CD  ARG B 405    18540  19658  11353   3910  -2923  -1965       C  
ATOM   5520  NE  ARG B 405     101.349  61.790   9.668  1.00152.49           N  
ANISOU 5520  NE  ARG B 405    21516  22505  13918   3932  -2757  -1675       N  
ATOM   5521  CZ  ARG B 405     102.086  62.139   8.618  1.00171.48           C  
ANISOU 5521  CZ  ARG B 405    24173  24995  15985   4033  -2590  -1528       C  
ATOM   5522  NH1 ARG B 405     102.498  61.219   7.755  1.00179.08           N  
ANISOU 5522  NH1 ARG B 405    25234  26017  16792   4151  -2562  -1653       N  
ATOM   5523  NH2 ARG B 405     102.409  63.411   8.424  1.00176.43           N  
ANISOU 5523  NH2 ARG B 405    24960  25642  16432   4014  -2452  -1250       N  
ATOM   5524  N   ASN B 406     105.816  60.196   9.699  1.00102.74           N  
ANISOU 5524  N   ASN B 406    15217  16666   7152   3852  -1720  -1468       N  
ATOM   5525  CA  ASN B 406     106.500  59.851   8.452  1.00104.67           C  
ANISOU 5525  CA  ASN B 406    15644  17025   7102   4016  -1593  -1457       C  
ATOM   5526  C   ASN B 406     107.599  58.818   8.678  1.00115.92           C  
ANISOU 5526  C   ASN B 406    16955  18563   8526   4032  -1374  -1538       C  
ATOM   5527  O   ASN B 406     107.670  57.810   7.964  1.00119.52           O  
ANISOU 5527  O   ASN B 406    17487  19021   8907   4202  -1448  -1732       O  
ATOM   5528  CB  ASN B 406     107.077  61.109   7.807  1.00100.52           C  
ANISOU 5528  CB  ASN B 406    15294  16607   6292   3998  -1373  -1137       C  
ATOM   5529  CG  ASN B 406     106.011  62.001   7.222  1.00106.03           C  
ANISOU 5529  CG  ASN B 406    16176  17184   6928   4056  -1616  -1083       C  
ATOM   5530  OD1 ASN B 406     104.907  61.547   6.913  1.00102.32           O  
ANISOU 5530  OD1 ASN B 406    15730  16588   6560   4167  -1941  -1308       O  
ATOM   5531  ND2 ASN B 406     106.321  63.285   7.090  1.00113.94           N  
ANISOU 5531  ND2 ASN B 406    17303  18213   7777   3972  -1468   -782       N  
ATOM   5532  N   LEU B 407     108.481  59.059   9.653  1.00115.70           N  
ANISOU 5532  N   LEU B 407    16752  18630   8580   3869  -1107  -1390       N  
ATOM   5533  CA  LEU B 407     109.548  58.100   9.924  1.00118.81           C  
ANISOU 5533  CA  LEU B 407    17015  19134   8993   3893   -899  -1464       C  
ATOM   5534  C   LEU B 407     108.993  56.780  10.442  1.00112.56           C  
ANISOU 5534  C   LEU B 407    16128  18191   8448   3935  -1139  -1787       C  
ATOM   5535  O   LEU B 407     109.535  55.714  10.126  1.00118.06           O  
ANISOU 5535  O   LEU B 407    16832  18916   9108   4067  -1102  -1940       O  
ATOM   5536  CB  LEU B 407     110.549  58.681  10.922  1.00120.99           C  
ANISOU 5536  CB  LEU B 407    17100  19536   9335   3693   -582  -1233       C  
ATOM   5537  CG  LEU B 407     111.848  57.883  11.078  1.00121.15           C  
ANISOU 5537  CG  LEU B 407    16977  19715   9341   3726   -314  -1251       C  
ATOM   5538  CD1 LEU B 407     112.618  57.847   9.760  1.00128.16           C  
ANISOU 5538  CD1 LEU B 407    18001  20773   9920   3890   -140  -1172       C  
ATOM   5539  CD2 LEU B 407     112.714  58.445  12.194  1.00116.15           C  
ANISOU 5539  CD2 LEU B 407    16119  19184   8828   3502    -42  -1039       C  
ATOM   5540  N   LEU B 408     107.918  56.830  11.231  1.00 99.54           N  
ANISOU 5540  N   LEU B 408    14391  16374   7055   3822  -1391  -1890       N  
ATOM   5541  CA  LEU B 408     107.304  55.599  11.713  1.00 90.51           C  
ANISOU 5541  CA  LEU B 408    13160  15066   6164   3822  -1640  -2184       C  
ATOM   5542  C   LEU B 408     106.655  54.810  10.586  1.00 83.98           C  
ANISOU 5542  C   LEU B 408    12511  14135   5264   4009  -1904  -2399       C  
ATOM   5543  O   LEU B 408     106.624  53.577  10.637  1.00 84.45           O  
ANISOU 5543  O   LEU B 408    12561  14092   5435   4064  -2028  -2626       O  
ATOM   5544  CB  LEU B 408     106.273  55.909  12.794  1.00 92.80           C  
ANISOU 5544  CB  LEU B 408    13258  15167   6834   3598  -1814  -2192       C  
ATOM   5545  CG  LEU B 408     106.842  56.135  14.190  1.00 88.51           C  
ANISOU 5545  CG  LEU B 408    12451  14571   6609   3336  -1573  -2033       C  
ATOM   5546  CD1 LEU B 408     105.803  56.790  15.063  1.00 90.03           C  
ANISOU 5546  CD1 LEU B 408    12483  14596   7130   3133  -1702  -1973       C  
ATOM   5547  CD2 LEU B 408     107.289  54.811  14.785  1.00 84.50           C  
ANISOU 5547  CD2 LEU B 408    11834  13998   6274   3317  -1558  -2211       C  
ATOM   5548  N   LEU B 409     106.131  55.489   9.569  1.00 86.21           N  
ANISOU 5548  N   LEU B 409    12967  14428   5361   4108  -2002  -2331       N  
ATOM   5549  CA  LEU B 409     105.506  54.769   8.467  1.00 91.54           C  
ANISOU 5549  CA  LEU B 409    13817  15009   5956   4290  -2260  -2534       C  
ATOM   5550  C   LEU B 409     106.532  54.181   7.504  1.00 95.45           C  
ANISOU 5550  C   LEU B 409    14466  15626   6173   4499  -2083  -2553       C  
ATOM   5551  O   LEU B 409     106.311  53.086   6.973  1.00 94.07           O  
ANISOU 5551  O   LEU B 409    14386  15353   6004   4640  -2269  -2783       O  
ATOM   5552  CB  LEU B 409     104.530  55.691   7.736  1.00 98.96           C  
ANISOU 5552  CB  LEU B 409    14886  15911   6805   4334  -2448  -2467       C  
ATOM   5553  CG  LEU B 409     103.213  55.920   8.484  1.00100.60           C  
ANISOU 5553  CG  LEU B 409    14937  15961   7326   4187  -2737  -2546       C  
ATOM   5554  CD1 LEU B 409     102.397  56.995   7.799  1.00 96.71           C  
ANISOU 5554  CD1 LEU B 409    14566  15456   6725   4248  -2878  -2441       C  
ATOM   5555  CD2 LEU B 409     102.420  54.624   8.566  1.00107.25           C  
ANISOU 5555  CD2 LEU B 409    15714  16627   8409   4180  -3046  -2846       C  
ATOM   5556  N   LYS B 410     107.655  54.871   7.276  1.00103.36           N  
ANISOU 5556  N   LYS B 410    15489  16840   6941   4516  -1731  -2312       N  
ATOM   5557  CA  LYS B 410     108.707  54.314   6.427  1.00109.20           C  
ANISOU 5557  CA  LYS B 410    16332  17731   7430   4712  -1533  -2320       C  
ATOM   5558  C   LYS B 410     109.252  53.015   7.008  1.00110.06           C  
ANISOU 5558  C   LYS B 410    16327  17796   7695   4751  -1516  -2512       C  
ATOM   5559  O   LYS B 410     109.332  51.995   6.314  1.00 97.08           O  
ANISOU 5559  O   LYS B 410    14807  16107   5971   4954  -1628  -2708       O  
ATOM   5560  CB  LYS B 410     109.843  55.324   6.243  1.00105.38           C  
ANISOU 5560  CB  LYS B 410    15830  17493   6715   4667  -1137  -2003       C  
ATOM   5561  CG  LYS B 410     111.122  54.698   5.683  1.00108.42           C  
ANISOU 5561  CG  LYS B 410    16222  18071   6902   4832   -876  -1999       C  
ATOM   5562  CD  LYS B 410     112.372  55.530   5.964  1.00120.38           C  
ANISOU 5562  CD  LYS B 410    17598  19828   8314   4703   -460  -1693       C  
ATOM   5563  CE  LYS B 410     113.631  54.763   5.554  1.00131.29           C  
ANISOU 5563  CE  LYS B 410    18925  21405   9556   4869   -219  -1720       C  
ATOM   5564  NZ  LYS B 410     114.885  55.566   5.652  1.00136.90           N  
ANISOU 5564  NZ  LYS B 410    19488  22376  10150   4744    188  -1415       N  
ATOM   5565  N   ASN B 411     109.640  53.040   8.287  1.00107.66           N  
ANISOU 5565  N   ASN B 411    15799  17497   7610   4566  -1384  -2457       N  
ATOM   5566  CA  ASN B 411     110.152  51.846   8.950  1.00103.95           C  
ANISOU 5566  CA  ASN B 411    15221  16968   7307   4590  -1374  -2628       C  
ATOM   5567  C   ASN B 411     109.088  50.768   9.118  1.00 95.96           C  
ANISOU 5567  C   ASN B 411    14261  15678   6522   4598  -1762  -2925       C  
ATOM   5568  O   ASN B 411     109.431  49.612   9.384  1.00 90.65           O  
ANISOU 5568  O   ASN B 411    13579  14915   5950   4668  -1811  -3099       O  
ATOM   5569  CB  ASN B 411     110.738  52.226  10.311  1.00109.97           C  
ANISOU 5569  CB  ASN B 411    15735  17794   8255   4375  -1154  -2489       C  
ATOM   5570  CG  ASN B 411     112.015  53.041  10.195  1.00118.24           C  
ANISOU 5570  CG  ASN B 411    16701  19118   9109   4358   -750  -2209       C  
ATOM   5571  OD1 ASN B 411     112.014  54.147   9.653  1.00123.59           O  
ANISOU 5571  OD1 ASN B 411    17448  19907   9606   4319   -641  -1994       O  
ATOM   5572  ND2 ASN B 411     113.109  52.508  10.736  1.00115.38           N  
ANISOU 5572  ND2 ASN B 411    16181  18858   8801   4371   -535  -2200       N  
ATOM   5573  N   LEU B 412     107.812  51.112   8.951  1.00 93.74           N  
ANISOU 5573  N   LEU B 412    14032  15255   6331   4525  -2045  -2979       N  
ATOM   5574  CA  LEU B 412     106.732  50.157   9.161  1.00103.81           C  
ANISOU 5574  CA  LEU B 412    15319  16267   7859   4479  -2420  -3237       C  
ATOM   5575  C   LEU B 412     106.424  49.346   7.905  1.00115.31           C  
ANISOU 5575  C   LEU B 412    17010  17635   9166   4709  -2638  -3425       C  
ATOM   5576  O   LEU B 412     106.343  48.116   7.965  1.00130.20           O  
ANISOU 5576  O   LEU B 412    18944  19352  11173   4758  -2811  -3639       O  
ATOM   5577  CB  LEU B 412     105.479  50.894   9.636  1.00106.23           C  
ANISOU 5577  CB  LEU B 412    15522  16475   8367   4280  -2628  -3207       C  
ATOM   5578  CG  LEU B 412     104.351  50.061  10.227  1.00113.40           C  
ANISOU 5578  CG  LEU B 412    16338  17129   9620   4131  -2975  -3424       C  
ATOM   5579  CD1 LEU B 412     104.897  49.211  11.355  1.00115.92           C  
ANISOU 5579  CD1 LEU B 412    16524  17369  10152   4014  -2899  -3499       C  
ATOM   5580  CD2 LEU B 412     103.254  50.976  10.738  1.00116.72           C  
ANISOU 5580  CD2 LEU B 412    16606  17517  10226   3944  -3116  -3349       C  
ATOM   5581  N   PHE B 413     106.254  50.015   6.765  1.00110.66           N  
ANISOU 5581  N   PHE B 413    16585  17148   8312   4851  -2639  -3345       N  
ATOM   5582  CA  PHE B 413     105.833  49.361   5.531  1.00119.82           C  
ANISOU 5582  CA  PHE B 413    17980  18226   9321   5070  -2872  -3521       C  
ATOM   5583  C   PHE B 413     106.957  49.190   4.518  1.00121.19           C  
ANISOU 5583  C   PHE B 413    18321  18588   9138   5342  -2641  -3477       C  
ATOM   5584  O   PHE B 413     107.048  48.140   3.871  1.00115.97           O  
ANISOU 5584  O   PHE B 413    17816  17845   8403   5541  -2779  -3672       O  
ATOM   5585  CB  PHE B 413     104.683  50.147   4.889  1.00120.70           C  
ANISOU 5585  CB  PHE B 413    18172  18295   9392   5057  -3095  -3495       C  
ATOM   5586  CG  PHE B 413     103.423  50.160   5.713  1.00118.18           C  
ANISOU 5586  CG  PHE B 413    17685  17785   9432   4822  -3381  -3579       C  
ATOM   5587  CD1 PHE B 413     102.554  49.079   5.694  1.00115.23           C  
ANISOU 5587  CD1 PHE B 413    17326  17180   9278   4791  -3730  -3829       C  
ATOM   5588  CD2 PHE B 413     103.127  51.234   6.540  1.00115.03           C  
ANISOU 5588  CD2 PHE B 413    17104  17440   9162   4625  -3296  -3402       C  
ATOM   5589  CE1 PHE B 413     101.398  49.081   6.461  1.00110.51           C  
ANISOU 5589  CE1 PHE B 413    16538  16426   9024   4553  -3977  -3894       C  
ATOM   5590  CE2 PHE B 413     101.977  51.240   7.312  1.00108.17           C  
ANISOU 5590  CE2 PHE B 413    16053  16419   8628   4417  -3547  -3477       C  
ATOM   5591  CZ  PHE B 413     101.111  50.163   7.271  1.00104.69           C  
ANISOU 5591  CZ  PHE B 413    15601  15767   8409   4374  -3879  -3719       C  
ATOM   5592  N   PHE B 414     107.826  50.188   4.374  1.00117.85           N  
ANISOU 5592  N   PHE B 414    17865  18415   8496   5350  -2292  -3219       N  
ATOM   5593  CA  PHE B 414     108.852  50.194   3.333  1.00110.37           C  
ANISOU 5593  CA  PHE B 414    17059  17684   7193   5592  -2053  -3142       C  
ATOM   5594  C   PHE B 414     110.194  49.843   3.969  1.00115.58           C  
ANISOU 5594  C   PHE B 414    17554  18496   7863   5595  -1729  -3072       C  
ATOM   5595  O   PHE B 414     111.077  50.684   4.137  1.00114.93           O  
ANISOU 5595  O   PHE B 414    17361  18643   7665   5524  -1386  -2822       O  
ATOM   5596  CB  PHE B 414     108.878  51.552   2.641  1.00107.81           C  
ANISOU 5596  CB  PHE B 414    16819  17533   6612   5584  -1895  -2890       C  
ATOM   5597  CG  PHE B 414     107.518  52.036   2.228  1.00138.75           C  
ANISOU 5597  CG  PHE B 414    20855  21297  10566   5550  -2214  -2936       C  
ATOM   5598  CD1 PHE B 414     106.640  51.180   1.584  1.00136.66           C  
ANISOU 5598  CD1 PHE B 414    20746  20847  10333   5691  -2576  -3197       C  
ATOM   5599  CD2 PHE B 414     107.111  53.335   2.487  1.00138.25           C  
ANISOU 5599  CD2 PHE B 414    20747  21267  10514   5381  -2168  -2719       C  
ATOM   5600  CE1 PHE B 414     105.385  51.608   1.201  1.00144.03           C  
ANISOU 5600  CE1 PHE B 414    21763  21649  11314   5663  -2878  -3244       C  
ATOM   5601  CE2 PHE B 414     105.852  53.767   2.106  1.00142.07           C  
ANISOU 5601  CE2 PHE B 414    21326  21613  11040   5372  -2474  -2769       C  
ATOM   5602  CZ  PHE B 414     104.991  52.902   1.461  1.00146.25           C  
ANISOU 5602  CZ  PHE B 414    21986  21977  11607   5512  -2825  -3032       C  
ATOM   5603  N   SER B 415     110.347  48.565   4.314  1.00121.88           N  
ANISOU 5603  N   SER B 415    18341  19158   8809   5676  -1853  -3294       N  
ATOM   5604  CA  SER B 415     111.472  48.103   5.111  1.00123.64           C  
ANISOU 5604  CA  SER B 415    18388  19476   9115   5667  -1610  -3264       C  
ATOM   5605  C   SER B 415     112.571  47.526   4.221  1.00120.44           C  
ANISOU 5605  C   SER B 415    18077  19253   8432   5969  -1433  -3291       C  
ATOM   5606  O   SER B 415     112.516  47.599   2.993  1.00113.06           O  
ANISOU 5606  O   SER B 415    17342  18395   7219   6175  -1462  -3307       O  
ATOM   5607  CB  SER B 415     111.010  47.070   6.142  1.00125.98           C  
ANISOU 5607  CB  SER B 415    18612  19501   9756   5560  -1848  -3476       C  
ATOM   5608  OG  SER B 415     109.899  47.542   6.883  1.00121.57           O  
ANISOU 5608  OG  SER B 415    17967  18774   9448   5293  -2038  -3471       O  
ATOM   5609  N   GLU B 416     113.587  46.947   4.869  1.00138.84           N  
ANISOU 5609  N   GLU B 416    20254  21659  10840   6005  -1251  -3297       N  
ATOM   5610  CA  GLU B 416     114.726  46.376   4.152  1.00148.46           C  
ANISOU 5610  CA  GLU B 416    21516  23075  11817   6297  -1066  -3319       C  
ATOM   5611  C   GLU B 416     114.273  45.314   3.158  1.00145.02           C  
ANISOU 5611  C   GLU B 416    21364  22480  11257   6586  -1364  -3584       C  
ATOM   5612  O   GLU B 416     114.704  45.301   1.999  1.00156.39           O  
ANISOU 5612  O   GLU B 416    22951  24090  12381   6840  -1277  -3576       O  
ATOM   5613  CB  GLU B 416     115.728  45.793   5.154  1.00159.94           C  
ANISOU 5613  CB  GLU B 416    22754  24581  13436   6283   -898  -3321       C  
ATOM   5614  CG  GLU B 416     116.767  44.857   4.548  1.00177.17           C  
ANISOU 5614  CG  GLU B 416    24988  26897  15431   6619   -806  -3422       C  
ATOM   5615  CD  GLU B 416     117.949  45.596   3.941  1.00188.16           C  
ANISOU 5615  CD  GLU B 416    26263  28687  16544   6707   -404  -3186       C  
ATOM   5616  OE1 GLU B 416     118.284  46.694   4.433  1.00188.52           O  
ANISOU 5616  OE1 GLU B 416    26101  28900  16629   6460   -145  -2928       O  
ATOM   5617  OE2 GLU B 416     118.546  45.074   2.973  1.00194.23           O  
ANISOU 5617  OE2 GLU B 416    27146  29598  17054   7017   -350  -3256       O  
ATOM   5618  N   LYS B 417     113.392  44.412   3.597  1.00134.87           N  
ANISOU 5618  N   LYS B 417    20163  20861  10219   6541  -1723  -3819       N  
ATOM   5619  CA  LYS B 417     112.830  43.403   2.706  1.00138.75           C  
ANISOU 5619  CA  LYS B 417    20935  21155  10629   6778  -2052  -4076       C  
ATOM   5620  C   LYS B 417     111.436  42.995   3.158  1.00136.90           C  
ANISOU 5620  C   LYS B 417    20767  20557  10691   6583  -2460  -4248       C  
ATOM   5621  O   LYS B 417     111.038  41.840   2.968  1.00140.52           O  
ANISOU 5621  O   LYS B 417    21395  20766  11229   6697  -2763  -4489       O  
ATOM   5622  CB  LYS B 417     113.738  42.169   2.631  1.00144.14           C  
ANISOU 5622  CB  LYS B 417    21674  21833  11258   7052  -2040  -4229       C  
ATOM   5623  CG  LYS B 417     114.401  41.962   1.277  1.00150.44           C  
ANISOU 5623  CG  LYS B 417    22653  22839  11670   7424  -1940  -4256       C  
ATOM   5624  CD  LYS B 417     115.422  40.829   1.324  1.00152.05           C  
ANISOU 5624  CD  LYS B 417    22871  23077  11825   7699  -1891  -4382       C  
ATOM   5625  CE  LYS B 417     114.771  39.479   1.585  1.00148.94           C  
ANISOU 5625  CE  LYS B 417    22663  22290  11639   7756  -2303  -4670       C  
ATOM   5626  NZ  LYS B 417     113.898  39.047   0.455  1.00145.57           N  
ANISOU 5626  NZ  LYS B 417    22553  21687  11068   7931  -2632  -4857       N  
ATOM   5627  N   ASP B 418     110.692  43.928   3.757  1.00130.10           N  
ANISOU 5627  N   ASP B 418    19769  19664   9998   6284  -2475  -4124       N  
ATOM   5628  CA  ASP B 418     109.397  43.693   4.389  1.00134.37           C  
ANISOU 5628  CA  ASP B 418    20292  19900  10862   6039  -2818  -4248       C  
ATOM   5629  C   ASP B 418     109.502  42.817   5.627  1.00144.86           C  
ANISOU 5629  C   ASP B 418    21501  21029  12511   5893  -2890  -4349       C  
ATOM   5630  O   ASP B 418     108.498  42.263   6.078  1.00150.95           O  
ANISOU 5630  O   ASP B 418    22289  21510  13553   5721  -3208  -4496       O  
ATOM   5631  CB  ASP B 418     108.387  43.083   3.413  1.00140.19           C  
ANISOU 5631  CB  ASP B 418    21281  20426  11560   6161  -3206  -4460       C  
ATOM   5632  CG  ASP B 418     107.920  44.070   2.377  1.00148.96           C  
ANISOU 5632  CG  ASP B 418    22495  21675  12429   6228  -3208  -4361       C  
ATOM   5633  OD1 ASP B 418     108.760  44.849   1.878  1.00152.20           O  
ANISOU 5633  OD1 ASP B 418    22901  22374  12555   6349  -2887  -4173       O  
ATOM   5634  OD2 ASP B 418     106.715  44.064   2.058  1.00153.49           O  
ANISOU 5634  OD2 ASP B 418    23151  22066  13100   6153  -3534  -4466       O  
ATOM   5635  N   ASN B 419     110.704  42.681   6.191  1.00144.98           N  
ANISOU 5635  N   ASN B 419    21389  21195  12503   5948  -2600  -4266       N  
ATOM   5636  CA  ASN B 419     110.868  41.846   7.375  1.00140.51           C  
ANISOU 5636  CA  ASN B 419    20724  20437  12225   5825  -2661  -4356       C  
ATOM   5637  C   ASN B 419     110.170  42.457   8.586  1.00131.69           C  
ANISOU 5637  C   ASN B 419    19399  19227  11410   5456  -2686  -4269       C  
ATOM   5638  O   ASN B 419     109.605  41.731   9.412  1.00133.50           O  
ANISOU 5638  O   ASN B 419    19610  19181  11933   5284  -2908  -4395       O  
ATOM   5639  CB  ASN B 419     112.355  41.618   7.650  1.00142.75           C  
ANISOU 5639  CB  ASN B 419    20908  20931  12401   5993  -2340  -4278       C  
ATOM   5640  CG  ASN B 419     113.131  42.915   7.785  1.00142.33           C  
ANISOU 5640  CG  ASN B 419    20640  21231  12208   5925  -1937  -3998       C  
ATOM   5641  OD1 ASN B 419     112.673  43.974   7.355  1.00141.78           O  
ANISOU 5641  OD1 ASN B 419    20562  21276  12033   5833  -1883  -3862       O  
ATOM   5642  ND2 ASN B 419     114.315  42.836   8.381  1.00141.45           N  
ANISOU 5642  ND2 ASN B 419    20356  21287  12100   5966  -1661  -3905       N  
ATOM   5643  N   VAL B 420     110.185  43.787   8.702  1.00127.29           N  
ANISOU 5643  N   VAL B 420    18693  18888  10783   5327  -2468  -4050       N  
ATOM   5644  CA  VAL B 420     109.488  44.449   9.803  1.00121.62           C  
ANISOU 5644  CA  VAL B 420    17782  18100  10329   4997  -2497  -3965       C  
ATOM   5645  C   VAL B 420     107.989  44.193   9.708  1.00114.45           C  
ANISOU 5645  C   VAL B 420    16946  16926   9616   4850  -2892  -4112       C  
ATOM   5646  O   VAL B 420     107.339  43.808  10.688  1.00 93.42           O  
ANISOU 5646  O   VAL B 420    14180  14050   7267   4613  -3065  -4186       O  
ATOM   5647  CB  VAL B 420     109.797  45.957   9.806  1.00 93.23           C  
ANISOU 5647  CB  VAL B 420    14049  14787   6586   4916  -2202  -3694       C  
ATOM   5648  CG1 VAL B 420     109.058  46.652  10.942  1.00 89.47           C  
ANISOU 5648  CG1 VAL B 420    13382  14240   6373   4599  -2246  -3613       C  
ATOM   5649  CG2 VAL B 420     111.295  46.196   9.885  1.00 93.22           C  
ANISOU 5649  CG2 VAL B 420    13948  15059   6413   5032  -1808  -3534       C  
ATOM   5650  N   LEU B 421     107.416  44.409   8.521  1.00117.79           N  
ANISOU 5650  N   LEU B 421    17534  17362   9858   4981  -3042  -4151       N  
ATOM   5651  CA  LEU B 421     105.986  44.190   8.361  1.00119.18           C  
ANISOU 5651  CA  LEU B 421    17756  17306  10222   4845  -3423  -4286       C  
ATOM   5652  C   LEU B 421     105.637  42.709   8.440  1.00124.45           C  
ANISOU 5652  C   LEU B 421    18543  17668  11074   4850  -3723  -4528       C  
ATOM   5653  O   LEU B 421     104.564  42.353   8.941  1.00126.86           O  
ANISOU 5653  O   LEU B 421    18785  17742  11675   4613  -4003  -4622       O  
ATOM   5654  CB  LEU B 421     105.507  44.797   7.044  1.00101.60           C  
ANISOU 5654  CB  LEU B 421    15686  15175   7743   5003  -3508  -4266       C  
ATOM   5655  CG  LEU B 421     103.992  44.845   6.847  1.00102.38           C  
ANISOU 5655  CG  LEU B 421    15787  15087   8025   4855  -3878  -4366       C  
ATOM   5656  CD1 LEU B 421     103.298  45.425   8.068  1.00 98.70           C  
ANISOU 5656  CD1 LEU B 421    15051  14575   7874   4524  -3903  -4279       C  
ATOM   5657  CD2 LEU B 421     103.662  45.666   5.622  1.00104.72           C  
ANISOU 5657  CD2 LEU B 421    16225  15521   8045   5021  -3904  -4302       C  
ATOM   5658  N   THR B 422     106.534  41.835   7.977  1.00115.20           N  
ANISOU 5658  N   THR B 422    17538  16492   9740   5108  -3668  -4621       N  
ATOM   5659  CA  THR B 422     106.274  40.400   8.034  1.00114.38           C  
ANISOU 5659  CA  THR B 422    17583  16080   9796   5130  -3957  -4844       C  
ATOM   5660  C   THR B 422     106.156  39.918   9.475  1.00113.75           C  
ANISOU 5660  C   THR B 422    17345  15807  10070   4848  -3994  -4856       C  
ATOM   5661  O   THR B 422     105.213  39.198   9.825  1.00115.37           O  
ANISOU 5661  O   THR B 422    17571  15717  10547   4646  -4306  -4982       O  
ATOM   5662  CB  THR B 422     107.376  39.636   7.299  1.00115.21           C  
ANISOU 5662  CB  THR B 422    17888  16248   9638   5494  -3862  -4924       C  
ATOM   5663  OG1 THR B 422     107.429  40.071   5.932  1.00121.75           O  
ANISOU 5663  OG1 THR B 422    18874  17253  10134   5750  -3838  -4914       O  
ATOM   5664  CG2 THR B 422     107.115  38.138   7.351  1.00111.44           C  
ANISOU 5664  CG2 THR B 422    17596  15429   9319   5528  -4180  -5151       C  
ATOM   5665  N   TYR B 423     107.111  40.310  10.324  1.00112.97           N  
ANISOU 5665  N   TYR B 423    17082  15871   9970   4821  -3674  -4717       N  
ATOM   5666  CA  TYR B 423     107.080  39.917  11.731  1.00108.87           C  
ANISOU 5666  CA  TYR B 423    16416  15184   9766   4566  -3683  -4715       C  
ATOM   5667  C   TYR B 423     105.777  40.338  12.397  1.00112.77           C  
ANISOU 5667  C   TYR B 423    16746  15546  10556   4203  -3871  -4693       C  
ATOM   5668  O   TYR B 423     105.176  39.565  13.153  1.00113.72           O  
ANISOU 5668  O   TYR B 423    16841  15388  10978   3974  -4085  -4781       O  
ATOM   5669  CB  TYR B 423     108.282  40.518  12.462  1.00106.82           C  
ANISOU 5669  CB  TYR B 423    15984  15172   9430   4599  -3290  -4546       C  
ATOM   5670  CG  TYR B 423     108.506  39.994  13.869  1.00107.37           C  
ANISOU 5670  CG  TYR B 423    15939  15079   9779   4405  -3271  -4554       C  
ATOM   5671  CD1 TYR B 423     109.612  39.215  14.171  1.00109.63           C  
ANISOU 5671  CD1 TYR B 423    16280  15350  10026   4581  -3151  -4591       C  
ATOM   5672  CD2 TYR B 423     107.637  40.323  14.905  1.00101.60           C  
ANISOU 5672  CD2 TYR B 423    15034  14225   9344   4054  -3364  -4514       C  
ATOM   5673  CE1 TYR B 423     109.824  38.748  15.454  1.00108.83           C  
ANISOU 5673  CE1 TYR B 423    16091  15090  10171   4413  -3138  -4593       C  
ATOM   5674  CE2 TYR B 423     107.841  39.862  16.186  1.00 99.78           C  
ANISOU 5674  CE2 TYR B 423    14711  13843   9357   3875  -3342  -4514       C  
ATOM   5675  CZ  TYR B 423     108.936  39.077  16.457  1.00107.57           C  
ANISOU 5675  CZ  TYR B 423    15780  14797  10296   4056  -3231  -4554       C  
ATOM   5676  OH  TYR B 423     109.145  38.618  17.738  1.00116.73           O  
ANISOU 5676  OH  TYR B 423    16865  15792  11693   3886  -3217  -4550       O  
ATOM   5677  N   ILE B 424     105.333  41.570  12.140  1.00112.43           N  
ANISOU 5677  N   ILE B 424    16583  15703  10433   4144  -3792  -4563       N  
ATOM   5678  CA  ILE B 424     104.122  42.065  12.789  1.00110.60           C  
ANISOU 5678  CA  ILE B 424    16158  15388  10478   3819  -3952  -4527       C  
ATOM   5679  C   ILE B 424     102.919  41.232  12.370  1.00109.70           C  
ANISOU 5679  C   ILE B 424    16134  14998  10546   3713  -4355  -4698       C  
ATOM   5680  O   ILE B 424     102.165  40.728  13.211  1.00108.04           O  
ANISOU 5680  O   ILE B 424    15807  14572  10671   3422  -4539  -4743       O  
ATOM   5681  CB  ILE B 424     103.914  43.560  12.482  1.00108.69           C  
ANISOU 5681  CB  ILE B 424    15798  15414  10084   3824  -3801  -4353       C  
ATOM   5682  CG1 ILE B 424     105.124  44.375  12.948  1.00101.11           C  
ANISOU 5682  CG1 ILE B 424    14742  14719   8958   3893  -3398  -4166       C  
ATOM   5683  CG2 ILE B 424     102.632  44.070  13.125  1.00 88.74           C  
ANISOU 5683  CG2 ILE B 424    13055  12815   7847   3518  -3979  -4320       C  
ATOM   5684  CD1 ILE B 424     105.034  45.849  12.631  1.00 97.16           C  
ANISOU 5684  CD1 ILE B 424    14162  14469   8286   3902  -3234  -3971       C  
ATOM   5685  N   LEU B 425     102.740  41.050  11.060  1.00108.87           N  
ANISOU 5685  N   LEU B 425    16239  14899  10226   3941  -4495  -4790       N  
ATOM   5686  CA  LEU B 425     101.551  40.371  10.567  1.00100.84           C  
ANISOU 5686  CA  LEU B 425    15302  13645   9366   3842  -4884  -4945       C  
ATOM   5687  C   LEU B 425     101.588  38.870  10.814  1.00119.50           C  
ANISOU 5687  C   LEU B 425    17814  15694  11897   3798  -5091  -5109       C  
ATOM   5688  O   LEU B 425     100.538  38.222  10.743  1.00123.27           O  
ANISOU 5688  O   LEU B 425    18307  15936  12595   3613  -5418  -5218       O  
ATOM   5689  CB  LEU B 425     101.368  40.664   9.081  1.00111.67           C  
ANISOU 5689  CB  LEU B 425    16868  15119  10441   4113  -4975  -4994       C  
ATOM   5690  CG  LEU B 425     101.122  42.145   8.801  1.00109.31           C  
ANISOU 5690  CG  LEU B 425    16442  15087  10002   4126  -4828  -4828       C  
ATOM   5691  CD1 LEU B 425     101.121  42.435   7.303  1.00105.82           C  
ANISOU 5691  CD1 LEU B 425    16227  14757   9224   4426  -4880  -4862       C  
ATOM   5692  CD2 LEU B 425      99.830  42.601   9.462  1.00111.24           C  
ANISOU 5692  CD2 LEU B 425    16432  15266  10566   3799  -5006  -4791       C  
ATOM   5693  N   GLN B 426     102.759  38.299  11.103  1.00113.64           N  
ANISOU 5693  N   GLN B 426    17178  14941  11059   3959  -4914  -5121       N  
ATOM   5694  CA  GLN B 426     102.814  36.892  11.480  1.00117.67           C  
ANISOU 5694  CA  GLN B 426    17832  15130  11746   3904  -5108  -5258       C  
ATOM   5695  C   GLN B 426     102.377  36.661  12.920  1.00114.44           C  
ANISOU 5695  C   GLN B 426    17221  14544  11715   3514  -5142  -5203       C  
ATOM   5696  O   GLN B 426     102.033  35.528  13.273  1.00112.07           O  
ANISOU 5696  O   GLN B 426    17020  13930  11631   3366  -5372  -5302       O  
ATOM   5697  CB  GLN B 426     104.221  36.330  11.264  1.00126.09           C  
ANISOU 5697  CB  GLN B 426    19085  16248  12575   4242  -4922  -5294       C  
ATOM   5698  CG  GLN B 426     104.507  35.928   9.822  1.00136.86           C  
ANISOU 5698  CG  GLN B 426    20726  17645  13630   4614  -5018  -5419       C  
ATOM   5699  CD  GLN B 426     105.964  35.586   9.579  1.00143.41           C  
ANISOU 5699  CD  GLN B 426    21681  18613  14196   4973  -4778  -5422       C  
ATOM   5700  OE1 GLN B 426     106.856  36.099  10.256  1.00154.54           O  
ANISOU 5700  OE1 GLN B 426    22930  20221  15567   4988  -4455  -5287       O  
ATOM   5701  NE2 GLN B 426     106.214  34.722   8.601  1.00136.12           N  
ANISOU 5701  NE2 GLN B 426    21035  17595  13090   5270  -4938  -5578       N  
ATOM   5702  N   ASP B 427     102.380  37.698  13.752  1.00116.95           N  
ANISOU 5702  N   ASP B 427    17270  15052  12115   3344  -4921  -5042       N  
ATOM   5703  CA  ASP B 427     101.835  37.575  15.095  1.00121.84           C  
ANISOU 5703  CA  ASP B 427    17675  15522  13097   2959  -4959  -4980       C  
ATOM   5704  C   ASP B 427     100.331  37.329  15.029  1.00126.20           C  
ANISOU 5704  C   ASP B 427    18132  15897  13920   2660  -5286  -5027       C  
ATOM   5705  O   ASP B 427      99.664  37.691  14.058  1.00125.94           O  
ANISOU 5705  O   ASP B 427    18123  15940  13790   2735  -5429  -5069       O  
ATOM   5706  CB  ASP B 427     102.138  38.834  15.909  1.00122.59           C  
ANISOU 5706  CB  ASP B 427    17502  15884  13194   2871  -4659  -4801       C  
ATOM   5707  CG  ASP B 427     101.385  38.874  17.226  1.00126.42           C  
ANISOU 5707  CG  ASP B 427    17729  16250  14056   2463  -4710  -4727       C  
ATOM   5708  OD1 ASP B 427     101.651  38.014  18.091  1.00124.07           O  
ANISOU 5708  OD1 ASP B 427    17465  15734  13943   2326  -4730  -4747       O  
ATOM   5709  OD2 ASP B 427     100.521  39.759  17.393  1.00126.99           O  
ANISOU 5709  OD2 ASP B 427    17564  16446  14240   2286  -4730  -4642       O  
ATOM   5710  N   GLN B 428      99.797  36.694  16.073  1.00131.67           N  
ANISOU 5710  N   GLN B 428    18713  16357  14959   2313  -5401  -5012       N  
ATOM   5711  CA  GLN B 428      98.382  36.333  16.104  1.00130.48           C  
ANISOU 5711  CA  GLN B 428    18443  16035  15097   1990  -5700  -5042       C  
ATOM   5712  C   GLN B 428      97.525  37.369  16.834  1.00130.56           C  
ANISOU 5712  C   GLN B 428    18069  16216  15321   1702  -5629  -4896       C  
ATOM   5713  O   GLN B 428      96.591  37.929  16.252  1.00132.68           O  
ANISOU 5713  O   GLN B 428    18211  16594  15605   1664  -5757  -4896       O  
ATOM   5714  CB  GLN B 428      98.214  34.949  16.744  1.00126.09           C  
ANISOU 5714  CB  GLN B 428    17996  15113  14799   1756  -5883  -5097       C  
ATOM   5715  CG  GLN B 428      98.624  33.787  15.849  1.00123.50           C  
ANISOU 5715  CG  GLN B 428    18048  14563  14315   2001  -6078  -5268       C  
ATOM   5716  CD  GLN B 428      97.805  33.722  14.568  1.00127.96           C  
ANISOU 5716  CD  GLN B 428    18707  15122  14790   2090  -6347  -5387       C  
ATOM   5717  OE1 GLN B 428      98.279  34.092  13.492  1.00131.91           O  
ANISOU 5717  OE1 GLN B 428    19366  15787  14967   2454  -6301  -5452       O  
ATOM   5718  NE2 GLN B 428      96.564  33.257  14.682  1.00126.31           N  
ANISOU 5718  NE2 GLN B 428    18392  14733  14865   1752  -6624  -5407       N  
ATOM   5719  N   ALA B 429      97.840  37.643  18.102  1.00124.49           N  
ANISOU 5719  N   ALA B 429    17112  15477  14713   1519  -5427  -4772       N  
ATOM   5720  CA  ALA B 429      96.919  38.343  18.992  1.00121.05           C  
ANISOU 5720  CA  ALA B 429    16299  15139  14557   1189  -5393  -4637       C  
ATOM   5721  C   ALA B 429      96.975  39.865  18.899  1.00122.72           C  
ANISOU 5721  C   ALA B 429    16313  15696  14619   1319  -5190  -4530       C  
ATOM   5722  O   ALA B 429      96.070  40.525  19.420  1.00123.12           O  
ANISOU 5722  O   ALA B 429    16046  15853  14879   1095  -5192  -4431       O  
ATOM   5723  CB  ALA B 429      97.178  37.923  20.443  1.00110.37           C  
ANISOU 5723  CB  ALA B 429    14831  13646  13458    918  -5276  -4546       C  
ATOM   5724  N   VAL B 430      97.994  40.444  18.268  1.00117.17           N  
ANISOU 5724  N   VAL B 430    15781  15177  13563   1670  -5006  -4533       N  
ATOM   5725  CA  VAL B 430      98.176  41.894  18.318  1.00111.92           C  
ANISOU 5725  CA  VAL B 430    14949  14824  12752   1775  -4785  -4402       C  
ATOM   5726  C   VAL B 430      98.496  42.444  16.933  1.00109.83           C  
ANISOU 5726  C   VAL B 430    14885  14727  12117   2123  -4767  -4434       C  
ATOM   5727  O   VAL B 430      97.956  43.481  16.524  1.00102.86           O  
ANISOU 5727  O   VAL B 430    13889  14030  11164   2167  -4764  -4363       O  
ATOM   5728  CB  VAL B 430      99.283  42.272  19.326  1.00 98.93           C  
ANISOU 5728  CB  VAL B 430    13244  13277  11068   1790  -4465  -4289       C  
ATOM   5729  CG1 VAL B 430      99.695  43.732  19.168  1.00 96.16           C  
ANISOU 5729  CG1 VAL B 430    12790  13228  10520   1941  -4164  -4096       C  
ATOM   5730  CG2 VAL B 430      98.828  41.996  20.754  1.00 87.33           C  
ANISOU 5730  CG2 VAL B 430    11515  11668   9999   1415  -4387  -4151       C  
ATOM   5731  N   GLY B 431      99.365  41.741  16.206  1.00110.81           N  
ANISOU 5731  N   GLY B 431    15314  14783  12005   2378  -4754  -4535       N  
ATOM   5732  CA  GLY B 431      99.945  42.222  14.973  1.00104.74           C  
ANISOU 5732  CA  GLY B 431    14750  14192  10854   2730  -4666  -4543       C  
ATOM   5733  C   GLY B 431      98.958  42.742  13.948  1.00110.11           C  
ANISOU 5733  C   GLY B 431    15434  14937  11465   2785  -4859  -4566       C  
ATOM   5734  O   GLY B 431      98.880  43.948  13.692  1.00106.69           O  
ANISOU 5734  O   GLY B 431    14917  14729  10890   2864  -4737  -4446       O  
ATOM   5735  N   PRO B 432      98.192  41.838  13.328  1.00123.35           N  
ANISOU 5735  N   PRO B 432    17224  16408  13236   2749  -5174  -4718       N  
ATOM   5736  CA  PRO B 432      97.303  42.270  12.234  1.00121.35           C  
ANISOU 5736  CA  PRO B 432    17005  16213  12889   2840  -5375  -4759       C  
ATOM   5737  C   PRO B 432      96.274  43.303  12.662  1.00106.94           C  
ANISOU 5737  C   PRO B 432    14871  14515  11246   2644  -5405  -4646       C  
ATOM   5738  O   PRO B 432      95.970  44.221  11.889  1.00 97.23           O  
ANISOU 5738  O   PRO B 432    13658  13450   9836   2801  -5413  -4599       O  
ATOM   5739  CB  PRO B 432      96.647  40.958  11.780  1.00128.19           C  
ANISOU 5739  CB  PRO B 432    18011  16799  13898   2765  -5720  -4945       C  
ATOM   5740  CG  PRO B 432      97.584  39.881  12.232  1.00131.14           C  
ANISOU 5740  CG  PRO B 432    18549  16996  14282   2790  -5651  -5008       C  
ATOM   5741  CD  PRO B 432      98.173  40.379  13.519  1.00128.53           C  
ANISOU 5741  CD  PRO B 432    18014  16764  14059   2650  -5363  -4860       C  
ATOM   5742  N   SER B 433      95.730  43.182  13.877  1.00103.50           N  
ANISOU 5742  N   SER B 433    14152  14009  11162   2315  -5419  -4593       N  
ATOM   5743  CA  SER B 433      94.811  44.199  14.379  1.00118.54           C  
ANISOU 5743  CA  SER B 433    15734  16061  13247   2149  -5414  -4474       C  
ATOM   5744  C   SER B 433      95.460  45.575  14.368  1.00123.55           C  
ANISOU 5744  C   SER B 433    16352  16957  13635   2340  -5137  -4319       C  
ATOM   5745  O   SER B 433      94.817  46.571  14.027  1.00124.78           O  
ANISOU 5745  O   SER B 433    16402  17258  13751   2392  -5169  -4248       O  
ATOM   5746  CB  SER B 433      94.352  43.845  15.794  1.00120.69           C  
ANISOU 5746  CB  SER B 433    15705  16240  13911   1781  -5401  -4420       C  
ATOM   5747  OG  SER B 433      94.108  42.457  15.921  1.00128.65           O  
ANISOU 5747  OG  SER B 433    16792  16979  15111   1603  -5597  -4539       O  
ATOM   5748  N   PHE B 434      96.743  45.642  14.727  1.00120.09           N  
ANISOU 5748  N   PHE B 434    16024  16579  13025   2450  -4865  -4260       N  
ATOM   5749  CA  PHE B 434      97.452  46.917  14.753  1.00112.56           C  
ANISOU 5749  CA  PHE B 434    15066  15871  11832   2608  -4586  -4095       C  
ATOM   5750  C   PHE B 434      97.576  47.516  13.354  1.00120.12           C  
ANISOU 5750  C   PHE B 434    16253  16949  12436   2903  -4595  -4083       C  
ATOM   5751  O   PHE B 434      97.253  48.690  13.142  1.00122.01           O  
ANISOU 5751  O   PHE B 434    16429  17345  12583   2962  -4547  -3960       O  
ATOM   5752  CB  PHE B 434      98.829  46.726  15.391  1.00 98.22           C  
ANISOU 5752  CB  PHE B 434    13320  14092   9907   2655  -4300  -4044       C  
ATOM   5753  CG  PHE B 434      99.732  47.916  15.260  1.00 90.97           C  
ANISOU 5753  CG  PHE B 434    12447  13425   8694   2831  -4000  -3871       C  
ATOM   5754  CD1 PHE B 434      99.629  48.980  16.138  1.00 90.52           C  
ANISOU 5754  CD1 PHE B 434    12155  13478   8761   2691  -3811  -3671       C  
ATOM   5755  CD2 PHE B 434     100.687  47.970  14.256  1.00 94.64           C  
ANISOU 5755  CD2 PHE B 434    13173  13992   8794   3112  -3855  -3858       C  
ATOM   5756  CE1 PHE B 434     100.463  50.076  16.021  1.00 95.54           C  
ANISOU 5756  CE1 PHE B 434    12835  14298   9170   2809  -3501  -3459       C  
ATOM   5757  CE2 PHE B 434     101.521  49.062  14.131  1.00 97.98           C  
ANISOU 5757  CE2 PHE B 434    13630  14646   8951   3240  -3564  -3671       C  
ATOM   5758  CZ  PHE B 434     101.411  50.117  15.017  1.00 98.92           C  
ANISOU 5758  CZ  PHE B 434    13532  14856   9198   3082  -3401  -3476       C  
ATOM   5759  N   ILE B 435      98.043  46.723  12.382  1.00123.16           N  
ANISOU 5759  N   ILE B 435    16919  17259  12617   3100  -4659  -4206       N  
ATOM   5760  CA  ILE B 435      98.249  47.246  11.030  1.00121.30           C  
ANISOU 5760  CA  ILE B 435    16918  17144  12027   3390  -4646  -4189       C  
ATOM   5761  C   ILE B 435      96.923  47.661  10.404  1.00129.65           C  
ANISOU 5761  C   ILE B 435    17921  18185  13156   3370  -4923  -4224       C  
ATOM   5762  O   ILE B 435      96.845  48.672   9.695  1.00117.31           O  
ANISOU 5762  O   ILE B 435    16434  16769  11369   3533  -4877  -4126       O  
ATOM   5763  CB  ILE B 435      98.988  46.217  10.150  1.00108.39           C  
ANISOU 5763  CB  ILE B 435    15580  15428  10176   3611  -4668  -4326       C  
ATOM   5764  CG1 ILE B 435     100.407  45.973  10.667  1.00112.16           C  
ANISOU 5764  CG1 ILE B 435    16108  15974  10535   3685  -4355  -4268       C  
ATOM   5765  CG2 ILE B 435      99.044  46.693   8.703  1.00101.63           C  
ANISOU 5765  CG2 ILE B 435    14960  14685   8972   3898  -4690  -4320       C  
ATOM   5766  CD1 ILE B 435     101.311  47.188  10.573  1.00111.83           C  
ANISOU 5766  CD1 ILE B 435    16070  16206  10215   3817  -4008  -4055       C  
ATOM   5767  N   HIS B 436      95.861  46.891  10.651  1.00147.73           N  
ANISOU 5767  N   HIS B 436    20077  20295  15758   3166  -5213  -4357       N  
ATOM   5768  CA  HIS B 436      94.558  47.240  10.095  1.00154.47           C  
ANISOU 5768  CA  HIS B 436    20844  21144  16704   3139  -5484  -4397       C  
ATOM   5769  C   HIS B 436      94.055  48.563  10.652  1.00140.73           C  
ANISOU 5769  C   HIS B 436    18855  19568  15047   3067  -5390  -4229       C  
ATOM   5770  O   HIS B 436      93.483  49.377   9.917  1.00140.54           O  
ANISOU 5770  O   HIS B 436    18863  19635  14901   3200  -5482  -4193       O  
ATOM   5771  CB  HIS B 436      93.540  46.142  10.384  1.00171.72           C  
ANISOU 5771  CB  HIS B 436    22891  23119  19237   2888  -5789  -4549       C  
ATOM   5772  CG  HIS B 436      92.123  46.598  10.238  1.00181.35           C  
ANISOU 5772  CG  HIS B 436    23889  24369  20646   2777  -6025  -4555       C  
ATOM   5773  ND1 HIS B 436      91.250  46.665  11.302  1.00182.45           N  
ANISOU 5773  ND1 HIS B 436    23660  24505  21159   2473  -6071  -4506       N  
ATOM   5774  CD2 HIS B 436      91.434  47.033   9.157  1.00185.35           C  
ANISOU 5774  CD2 HIS B 436    24481  24927  21018   2941  -6218  -4599       C  
ATOM   5775  CE1 HIS B 436      90.080  47.112  10.881  1.00184.57           C  
ANISOU 5775  CE1 HIS B 436    23782  24830  21516   2458  -6280  -4521       C  
ATOM   5776  NE2 HIS B 436      90.165  47.342   9.583  1.00186.77           N  
ANISOU 5776  NE2 HIS B 436    24338  25134  21492   2740  -6383  -4582       N  
ATOM   5777  N   LYS B 437      94.235  48.781  11.956  1.00129.71           N  
ANISOU 5777  N   LYS B 437    17217  18203  13862   2864  -5219  -4129       N  
ATOM   5778  CA  LYS B 437      93.853  50.053  12.558  1.00122.02           C  
ANISOU 5778  CA  LYS B 437    16017  17385  12961   2817  -5110  -3964       C  
ATOM   5779  C   LYS B 437      94.634  51.200  11.930  1.00110.49           C  
ANISOU 5779  C   LYS B 437    14767  16093  11123   3078  -4903  -3817       C  
ATOM   5780  O   LYS B 437      94.052  52.079  11.287  1.00120.53           O  
ANISOU 5780  O   LYS B 437    16068  17440  12287   3203  -4987  -3763       O  
ATOM   5781  CB  LYS B 437      94.076  50.008  14.072  1.00125.99           C  
ANISOU 5781  CB  LYS B 437    16254  17889  13728   2573  -4941  -3887       C  
ATOM   5782  CG  LYS B 437      93.205  49.000  14.809  1.00135.01           C  
ANISOU 5782  CG  LYS B 437    17151  18876  15272   2271  -5123  -3989       C  
ATOM   5783  CD  LYS B 437      91.729  49.204  14.524  1.00143.47           C  
ANISOU 5783  CD  LYS B 437    18017  19958  16538   2191  -5379  -4026       C  
ATOM   5784  CE  LYS B 437      90.894  48.123  15.193  1.00147.21           C  
ANISOU 5784  CE  LYS B 437    18254  20282  17397   1866  -5549  -4109       C  
ATOM   5785  NZ  LYS B 437      89.432  48.362  15.030  1.00151.45           N  
ANISOU 5785  NZ  LYS B 437    18532  20868  18145   1765  -5772  -4127       N  
ATOM   5786  N   VAL B 438      95.963  51.178  12.077  1.00103.18           N  
ANISOU 5786  N   VAL B 438    13995  15223   9988   3159  -4630  -3746       N  
ATOM   5787  CA  VAL B 438      96.885  52.211  11.599  1.00105.83           C  
ANISOU 5787  CA  VAL B 438    14521  15726   9966   3363  -4378  -3572       C  
ATOM   5788  C   VAL B 438      96.437  52.829  10.279  1.00114.26           C  
ANISOU 5788  C   VAL B 438    15785  16839  10789   3579  -4504  -3556       C  
ATOM   5789  O   VAL B 438      96.512  54.049  10.095  1.00122.78           O  
ANISOU 5789  O   VAL B 438    16911  18036  11705   3668  -4392  -3382       O  
ATOM   5790  CB  VAL B 438      98.309  51.632  11.471  1.00 99.45           C  
ANISOU 5790  CB  VAL B 438    13905  14947   8935   3464  -4138  -3570       C  
ATOM   5791  CG1 VAL B 438      99.202  52.546  10.644  1.00 90.67           C  
ANISOU 5791  CG1 VAL B 438    13020  14008   7421   3686  -3902  -3400       C  
ATOM   5792  CG2 VAL B 438      98.918  51.419  12.850  1.00 94.73           C  
ANISOU 5792  CG2 VAL B 438    13120  14351   8522   3277  -3948  -3523       C  
ATOM   5793  N   ILE B 439      95.940  51.996   9.368  1.00115.65           N  
ANISOU 5793  N   ILE B 439    16088  16907  10946   3658  -4751  -3736       N  
ATOM   5794  CA  ILE B 439      95.555  52.458   8.039  1.00114.80           C  
ANISOU 5794  CA  ILE B 439    16197  16834  10589   3880  -4885  -3743       C  
ATOM   5795  C   ILE B 439      94.117  52.979   7.982  1.00121.86           C  
ANISOU 5795  C   ILE B 439    16919  17704  11680   3825  -5155  -3769       C  
ATOM   5796  O   ILE B 439      93.803  53.845   7.155  1.00115.62           O  
ANISOU 5796  O   ILE B 439    16262  16978  10690   3997  -5209  -3700       O  
ATOM   5797  CB  ILE B 439      95.794  51.316   7.033  1.00109.25           C  
ANISOU 5797  CB  ILE B 439    15738  16036   9738   4024  -5017  -3927       C  
ATOM   5798  CG1 ILE B 439      97.222  51.386   6.501  1.00100.14           C  
ANISOU 5798  CG1 ILE B 439    14840  14995   8215   4225  -4718  -3837       C  
ATOM   5799  CG2 ILE B 439      94.773  51.313   5.904  1.00119.00           C  
ANISOU 5799  CG2 ILE B 439    17082  17217  10914   4150  -5333  -4041       C  
ATOM   5800  CD1 ILE B 439      97.675  50.114   5.899  1.00102.43           C  
ANISOU 5800  CD1 ILE B 439    15318  15188   8413   4341  -4787  -4017       C  
ATOM   5801  N   THR B 440      93.242  52.499   8.862  1.00130.48           N  
ANISOU 5801  N   THR B 440    17707  18711  13157   3587  -5313  -3856       N  
ATOM   5802  CA  THR B 440      91.828  52.857   8.803  1.00136.16           C  
ANISOU 5802  CA  THR B 440    18225  19422  14089   3530  -5575  -3897       C  
ATOM   5803  C   THR B 440      91.514  53.958   9.819  1.00137.82           C  
ANISOU 5803  C   THR B 440    18171  19734  14459   3434  -5448  -3733       C  
ATOM   5804  O   THR B 440      90.788  53.772  10.796  1.00136.43           O  
ANISOU 5804  O   THR B 440    17664  19542  14633   3214  -5509  -3755       O  
ATOM   5805  CB  THR B 440      90.965  51.614   9.011  1.00131.47           C  
ANISOU 5805  CB  THR B 440    17456  18682  13815   3325  -5844  -4091       C  
ATOM   5806  OG1 THR B 440      91.282  51.002  10.267  1.00119.67           O  
ANISOU 5806  OG1 THR B 440    15755  17133  12579   3073  -5717  -4083       O  
ATOM   5807  CG2 THR B 440      91.236  50.607   7.904  1.00134.00           C  
ANISOU 5807  CG2 THR B 440    18075  18887  13950   3458  -5996  -4257       C  
ATOM   5808  N   TYR B 441      92.083  55.133   9.555  1.00140.39           N  
ANISOU 5808  N   TYR B 441    18661  20168  14514   3607  -5262  -3556       N  
ATOM   5809  CA  TYR B 441      91.744  56.347  10.298  1.00138.18           C  
ANISOU 5809  CA  TYR B 441    18200  19973  14330   3582  -5171  -3394       C  
ATOM   5810  C   TYR B 441      91.696  57.577   9.384  1.00133.01           C  
ANISOU 5810  C   TYR B 441    17781  19380  13378   3826  -5173  -3266       C  
ATOM   5811  O   TYR B 441      92.701  57.984   8.800  1.00127.25           O  
ANISOU 5811  O   TYR B 441    17346  18691  12311   3967  -4988  -3147       O  
ATOM   5812  CB  TYR B 441      92.725  56.572  11.455  1.00140.78           C  
ANISOU 5812  CB  TYR B 441    18446  20350  14693   3460  -4867  -3258       C  
ATOM   5813  CG  TYR B 441      92.548  55.598  12.604  1.00158.51           C  
ANISOU 5813  CG  TYR B 441    20394  22536  17295   3195  -4871  -3355       C  
ATOM   5814  CD1 TYR B 441      91.569  55.801  13.570  1.00165.33           C  
ANISOU 5814  CD1 TYR B 441    20897  23413  18506   3028  -4943  -3352       C  
ATOM   5815  CD2 TYR B 441      93.354  54.479  12.724  1.00171.14           C  
ANISOU 5815  CD2 TYR B 441    22078  24067  18882   3116  -4797  -3442       C  
ATOM   5816  CE1 TYR B 441      91.400  54.911  14.622  1.00171.87           C  
ANISOU 5816  CE1 TYR B 441    21455  24187  19658   2767  -4932  -3421       C  
ATOM   5817  CE2 TYR B 441      93.188  53.579  13.767  1.00178.40           C  
ANISOU 5817  CE2 TYR B 441    22751  24908  20125   2865  -4809  -3521       C  
ATOM   5818  CZ  TYR B 441      92.216  53.802  14.715  1.00179.41           C  
ANISOU 5818  CZ  TYR B 441    22522  25051  20594   2679  -4871  -3503       C  
ATOM   5819  OH  TYR B 441      92.067  52.905  15.752  1.00183.56           O  
ANISOU 5819  OH  TYR B 441    22808  25498  21436   2412  -4864  -3560       O  
ATOM   5820  N   GLY B 445      94.541  58.763   3.966  1.00105.15           N  
ANISOU 5820  N   GLY B 445    15852  16001   8098   4768  -4871  -2979       N  
ATOM   5821  CA  GLY B 445      94.515  59.185   2.575  1.00130.32           C  
ANISOU 5821  CA  GLY B 445    19359  19210  10946   5001  -4939  -2943       C  
ATOM   5822  C   GLY B 445      93.777  58.207   1.678  1.00138.29           C  
ANISOU 5822  C   GLY B 445    20432  20143  11971   5110  -5256  -3201       C  
ATOM   5823  O   GLY B 445      93.099  57.312   2.176  1.00149.47           O  
ANISOU 5823  O   GLY B 445    21618  21475  13698   4983  -5457  -3398       O  
ATOM   5824  N   ARG B 446      93.910  58.374   0.358  1.00140.47           N  
ANISOU 5824  N   ARG B 446    21022  20442  11908   5336  -5302  -3193       N  
ATOM   5825  CA  ARG B 446      93.284  57.479  -0.613  1.00148.99           C  
ANISOU 5825  CA  ARG B 446    22211  21447  12953   5469  -5605  -3433       C  
ATOM   5826  C   ARG B 446      94.309  56.970  -1.623  1.00148.93           C  
ANISOU 5826  C   ARG B 446    22517  21494  12574   5650  -5457  -3442       C  
ATOM   5827  O   ARG B 446      94.348  55.774  -1.935  1.00138.88           O  
ANISOU 5827  O   ARG B 446    21281  20158  11328   5687  -5578  -3652       O  
ATOM   5828  CB  ARG B 446      92.135  58.184  -1.341  1.00158.86           C  
ANISOU 5828  CB  ARG B 446    23528  22662  14169   5606  -5896  -3457       C  
ATOM   5829  CG  ARG B 446      91.453  57.349  -2.432  1.00164.58           C  
ANISOU 5829  CG  ARG B 446    24388  23310  14833   5758  -6231  -3699       C  
ATOM   5830  CD  ARG B 446      90.262  58.095  -3.022  1.00171.13           C  
ANISOU 5830  CD  ARG B 446    25243  24113  15666   5881  -6526  -3721       C  
ATOM   5831  NE  ARG B 446      89.314  58.475  -1.978  1.00172.83           N  
ANISOU 5831  NE  ARG B 446    25097  24306  16266   5704  -6643  -3725       N  
ATOM   5832  CZ  ARG B 446      88.134  57.896  -1.778  1.00172.02           C  
ANISOU 5832  CZ  ARG B 446    24742  24138  16480   5614  -6966  -3927       C  
ATOM   5833  NH1 ARG B 446      87.734  56.903  -2.561  1.00173.05           N  
ANISOU 5833  NH1 ARG B 446    24959  24197  16595   5678  -7229  -4147       N  
ATOM   5834  NH2 ARG B 446      87.352  58.319  -0.791  1.00168.31           N  
ANISOU 5834  NH2 ARG B 446    23928  23679  16342   5459  -7024  -3903       N  
ATOM   5835  N   GLU B 447      95.125  57.882  -2.157  1.00153.92           N  
ANISOU 5835  N   GLU B 447    23382  22242  12857   5766  -5197  -3210       N  
ATOM   5836  CA  GLU B 447      96.251  57.486  -2.998  1.00154.17           C  
ANISOU 5836  CA  GLU B 447    23677  22369  12531   5922  -4980  -3179       C  
ATOM   5837  C   GLU B 447      97.328  56.803  -2.163  1.00147.97           C  
ANISOU 5837  C   GLU B 447    22758  21639  11827   5791  -4697  -3166       C  
ATOM   5838  O   GLU B 447      97.855  55.749  -2.540  1.00133.72           O  
ANISOU 5838  O   GLU B 447    21036  19835   9935   5883  -4674  -3312       O  
ATOM   5839  CB  GLU B 447      96.815  58.720  -3.704  1.00153.09           C  
ANISOU 5839  CB  GLU B 447    23794  22353  12022   6036  -4760  -2903       C  
ATOM   5840  CG  GLU B 447      97.659  58.440  -4.929  1.00151.12           C  
ANISOU 5840  CG  GLU B 447    23855  22209  11354   6254  -4617  -2882       C  
ATOM   5841  CD  GLU B 447      97.808  59.665  -5.811  1.00149.77           C  
ANISOU 5841  CD  GLU B 447    23955  22118  10833   6374  -4519  -2643       C  
ATOM   5842  OE1 GLU B 447      98.710  60.487  -5.540  1.00148.67           O  
ANISOU 5842  OE1 GLU B 447    23845  22094  10550   6279  -4177  -2363       O  
ATOM   5843  OE2 GLU B 447      97.017  59.820  -6.763  1.00151.08           O  
ANISOU 5843  OE2 GLU B 447    24307  22226  10872   6552  -4788  -2728       O  
ATOM   5844  N   PHE B 448      97.661  57.401  -1.016  1.00153.37           N  
ANISOU 5844  N   PHE B 448    23237  22360  12676   5588  -4487  -2995       N  
ATOM   5845  CA  PHE B 448      98.612  56.800  -0.087  1.00149.47           C  
ANISOU 5845  CA  PHE B 448    22584  21913  12296   5448  -4233  -2984       C  
ATOM   5846  C   PHE B 448      98.082  55.494   0.493  1.00140.51           C  
ANISOU 5846  C   PHE B 448    21258  20636  11494   5353  -4462  -3260       C  
ATOM   5847  O   PHE B 448      98.860  54.570   0.758  1.00131.68           O  
ANISOU 5847  O   PHE B 448    20117  19527  10388   5340  -4330  -3341       O  
ATOM   5848  CB  PHE B 448      98.920  57.788   1.037  1.00151.26           C  
ANISOU 5848  CB  PHE B 448    22633  22192  12647   5248  -4007  -2750       C  
ATOM   5849  CG  PHE B 448     100.341  57.754   1.515  1.00158.83           C  
ANISOU 5849  CG  PHE B 448    23567  23287  13495   5177  -3608  -2595       C  
ATOM   5850  CD1 PHE B 448     101.173  56.694   1.203  1.00163.30           C  
ANISOU 5850  CD1 PHE B 448    24189  23905  13952   5266  -3490  -2709       C  
ATOM   5851  CD2 PHE B 448     100.829  58.765   2.328  1.00160.38           C  
ANISOU 5851  CD2 PHE B 448    23668  23553  13716   5020  -3362  -2341       C  
ATOM   5852  CE1 PHE B 448     102.476  56.661   1.663  1.00164.89           C  
ANISOU 5852  CE1 PHE B 448    24336  24247  14067   5206  -3121  -2569       C  
ATOM   5853  CE2 PHE B 448     102.131  58.734   2.795  1.00158.71           C  
ANISOU 5853  CE2 PHE B 448    23409  23474  13419   4940  -2997  -2197       C  
ATOM   5854  CZ  PHE B 448     102.954  57.680   2.462  1.00160.84           C  
ANISOU 5854  CZ  PHE B 448    23715  23815  13583   5034  -2873  -2312       C  
ATOM   5855  N   LEU B 449      96.764  55.399   0.694  1.00146.91           N  
ANISOU 5855  N   LEU B 449    21926  21314  12578   5281  -4804  -3401       N  
ATOM   5856  CA  LEU B 449      96.180  54.205   1.300  1.00147.00           C  
ANISOU 5856  CA  LEU B 449    21739  21181  12934   5142  -5030  -3641       C  
ATOM   5857  C   LEU B 449      96.370  52.979   0.415  1.00159.20           C  
ANISOU 5857  C   LEU B 449    23482  22655  14354   5299  -5165  -3856       C  
ATOM   5858  O   LEU B 449      96.586  51.868   0.915  1.00162.20           O  
ANISOU 5858  O   LEU B 449    23776  22941  14910   5208  -5195  -4003       O  
ATOM   5859  CB  LEU B 449      94.693  54.431   1.572  1.00138.85           C  
ANISOU 5859  CB  LEU B 449    20506  20049  12201   5035  -5364  -3730       C  
ATOM   5860  CG  LEU B 449      93.993  53.565   2.621  1.00129.32           C  
ANISOU 5860  CG  LEU B 449    18985  18717  11433   4786  -5541  -3890       C  
ATOM   5861  CD1 LEU B 449      94.234  54.150   3.992  1.00127.32           C  
ANISOU 5861  CD1 LEU B 449    18470  18519  11387   4577  -5324  -3732       C  
ATOM   5862  CD2 LEU B 449      92.500  53.459   2.331  1.00128.97           C  
ANISOU 5862  CD2 LEU B 449    18821  18580  11602   4754  -5934  -4039       C  
ATOM   5863  N   ALA B 450      96.276  53.155  -0.906  1.00170.41           N  
ANISOU 5863  N   ALA B 450    25179  24104  15466   5542  -5260  -3879       N  
ATOM   5864  CA  ALA B 450      96.467  52.025  -1.808  1.00176.82           C  
ANISOU 5864  CA  ALA B 450    26203  24847  16131   5723  -5396  -4085       C  
ATOM   5865  C   ALA B 450      97.928  51.599  -1.870  1.00177.60           C  
ANISOU 5865  C   ALA B 450    26423  25054  16003   5824  -5056  -4027       C  
ATOM   5866  O   ALA B 450      98.218  50.429  -2.143  1.00189.09           O  
ANISOU 5866  O   ALA B 450    27972  26428  17446   5914  -5135  -4214       O  
ATOM   5867  CB  ALA B 450      95.954  52.366  -3.207  1.00184.42           C  
ANISOU 5867  CB  ALA B 450    27434  25820  16816   5968  -5593  -4124       C  
ATOM   5868  N   GLN B 451      98.857  52.527  -1.626  1.00164.12           N  
ANISOU 5868  N   GLN B 451    24711  23528  14117   5812  -4684  -3769       N  
ATOM   5869  CA  GLN B 451     100.270  52.161  -1.587  1.00153.45           C  
ANISOU 5869  CA  GLN B 451    23420  22308  12576   5886  -4337  -3700       C  
ATOM   5870  C   GLN B 451     100.566  51.237  -0.414  1.00149.19           C  
ANISOU 5870  C   GLN B 451    22661  21679  12345   5711  -4301  -3804       C  
ATOM   5871  O   GLN B 451     101.340  50.282  -0.548  1.00149.26           O  
ANISOU 5871  O   GLN B 451    22744  21690  12279   5820  -4214  -3908       O  
ATOM   5872  CB  GLN B 451     101.138  53.415  -1.515  1.00145.72           C  
ANISOU 5872  CB  GLN B 451    22454  21542  11372   5864  -3954  -3382       C  
ATOM   5873  CG  GLN B 451     102.521  53.236  -2.104  1.00147.20           C  
ANISOU 5873  CG  GLN B 451    22792  21918  11221   6034  -3616  -3290       C  
ATOM   5874  CD  GLN B 451     102.489  52.984  -3.597  1.00156.41           C  
ANISOU 5874  CD  GLN B 451    24265  23116  12048   6327  -3723  -3378       C  
ATOM   5875  OE1 GLN B 451     102.754  51.874  -4.057  1.00158.42           O  
ANISOU 5875  OE1 GLN B 451    24624  23331  12238   6496  -3801  -3578       O  
ATOM   5876  NE2 GLN B 451     102.155  54.016  -4.363  1.00161.35           N  
ANISOU 5876  NE2 GLN B 451    25052  23804  12450   6397  -3737  -3229       N  
ATOM   5877  N   PHE B 452      99.967  51.512   0.746  1.00144.51           N  
ANISOU 5877  N   PHE B 452    21803  21010  12095   5450  -4365  -3775       N  
ATOM   5878  CA  PHE B 452     100.072  50.592   1.873  1.00141.65           C  
ANISOU 5878  CA  PHE B 452    21236  20532  12050   5265  -4381  -3890       C  
ATOM   5879  C   PHE B 452      99.291  49.309   1.607  1.00140.97           C  
ANISOU 5879  C   PHE B 452    21194  20224  12144   5276  -4752  -4177       C  
ATOM   5880  O   PHE B 452      99.712  48.223   2.022  1.00141.32           O  
ANISOU 5880  O   PHE B 452    21220  20168  12307   5246  -4755  -4307       O  
ATOM   5881  CB  PHE B 452      99.572  51.265   3.153  1.00140.63           C  
ANISOU 5881  CB  PHE B 452    20814  20387  12232   4986  -4360  -3779       C  
ATOM   5882  CG  PHE B 452     100.382  52.463   3.581  1.00133.98           C  
ANISOU 5882  CG  PHE B 452    19922  19736  11249   4943  -3999  -3496       C  
ATOM   5883  CD1 PHE B 452     101.723  52.580   3.242  1.00134.68           C  
ANISOU 5883  CD1 PHE B 452    20134  19994  11042   5070  -3657  -3364       C  
ATOM   5884  CD2 PHE B 452      99.792  53.479   4.319  1.00117.85           C  
ANISOU 5884  CD2 PHE B 452    17700  17704   9373   4773  -4006  -3357       C  
ATOM   5885  CE1 PHE B 452     102.458  53.686   3.639  1.00125.89           C  
ANISOU 5885  CE1 PHE B 452    18970  19051   9813   4999  -3331  -3091       C  
ATOM   5886  CE2 PHE B 452     100.519  54.587   4.712  1.00109.82           C  
ANISOU 5886  CE2 PHE B 452    16657  16839   8230   4725  -3695  -3092       C  
ATOM   5887  CZ  PHE B 452     101.854  54.690   4.374  1.00115.46           C  
ANISOU 5887  CZ  PHE B 452    17497  17714   8657   4824  -3357  -2954       C  
ATOM   5888  N   HIS B 453      98.146  49.418   0.924  1.00140.96           N  
ANISOU 5888  N   HIS B 453    21252  20134  12171   5314  -5077  -4276       N  
ATOM   5889  CA  HIS B 453      97.384  48.230   0.550  1.00141.33           C  
ANISOU 5889  CA  HIS B 453    21362  19969  12369   5323  -5447  -4541       C  
ATOM   5890  C   HIS B 453      98.242  47.253  -0.241  1.00141.51           C  
ANISOU 5890  C   HIS B 453    21653  19971  12145   5571  -5409  -4668       C  
ATOM   5891  O   HIS B 453      98.106  46.032  -0.096  1.00146.86           O  
ANISOU 5891  O   HIS B 453    22355  20460  12987   5536  -5601  -4866       O  
ATOM   5892  CB  HIS B 453      96.153  48.627  -0.269  1.00144.56           C  
ANISOU 5892  CB  HIS B 453    21828  20331  12770   5379  -5773  -4608       C  
ATOM   5893  CG  HIS B 453      94.999  49.107   0.555  1.00148.89           C  
ANISOU 5893  CG  HIS B 453    22073  20826  13671   5117  -5943  -4583       C  
ATOM   5894  ND1 HIS B 453      95.154  49.660   1.808  1.00147.46           N  
ANISOU 5894  ND1 HIS B 453    21623  20705  13699   4894  -5740  -4430       N  
ATOM   5895  CD2 HIS B 453      93.670  49.121   0.300  1.00151.85           C  
ANISOU 5895  CD2 HIS B 453    22360  21108  14227   5051  -6295  -4690       C  
ATOM   5896  CE1 HIS B 453      93.970  49.993   2.291  1.00145.55           C  
ANISOU 5896  CE1 HIS B 453    21139  20414  13750   4711  -5952  -4444       C  
ATOM   5897  NE2 HIS B 453      93.053  49.673   1.396  1.00150.51           N  
ANISOU 5897  NE2 HIS B 453    21860  20955  14372   4797  -6287  -4599       N  
ATOM   5898  N   LEU B 454      99.137  47.777  -1.082  1.00137.08           N  
ANISOU 5898  N   LEU B 454    21296  19601  11185   5822  -5160  -4547       N  
ATOM   5899  CA  LEU B 454      99.966  46.918  -1.921  1.00133.71           C  
ANISOU 5899  CA  LEU B 454    21125  19188  10492   6096  -5109  -4660       C  
ATOM   5900  C   LEU B 454     100.920  46.085  -1.078  1.00136.70           C  
ANISOU 5900  C   LEU B 454    21415  19542  10983   6043  -4919  -4690       C  
ATOM   5901  O   LEU B 454     101.066  44.878  -1.296  1.00126.83           O  
ANISOU 5901  O   LEU B 454    20290  18144   9758   6149  -5071  -4890       O  
ATOM   5902  CB  LEU B 454     100.740  47.765  -2.932  1.00139.33           C  
ANISOU 5902  CB  LEU B 454    22037  20144  10757   6349  -4843  -4489       C  
ATOM   5903  CG  LEU B 454     100.023  48.060  -4.255  1.00132.96           C  
ANISOU 5903  CG  LEU B 454    21473  19327   9718   6552  -5082  -4551       C  
ATOM   5904  CD1 LEU B 454     100.863  48.961  -5.155  1.00134.72           C  
ANISOU 5904  CD1 LEU B 454    21884  19804   9500   6768  -4776  -4346       C  
ATOM   5905  CD2 LEU B 454      99.673  46.764  -4.960  1.00136.92           C  
ANISOU 5905  CD2 LEU B 454    22171  19641  10212   6721  -5410  -4841       C  
ATOM   5906  N   VAL B 455     101.561  46.712  -0.090  1.00137.43           N  
ANISOU 5906  N   VAL B 455    21298  19767  11151   5883  -4601  -4494       N  
ATOM   5907  CA  VAL B 455     102.585  46.032   0.697  1.00137.31           C  
ANISOU 5907  CA  VAL B 455    21198  19762  11211   5855  -4383  -4499       C  
ATOM   5908  C   VAL B 455     101.963  44.981   1.614  1.00135.12           C  
ANISOU 5908  C   VAL B 455    20796  19211  11331   5641  -4645  -4683       C  
ATOM   5909  O   VAL B 455     102.529  43.898   1.804  1.00152.38           O  
ANISOU 5909  O   VAL B 455    23045  21295  13558   5710  -4650  -4809       O  
ATOM   5910  CB  VAL B 455     103.412  47.068   1.479  1.00133.54           C  
ANISOU 5910  CB  VAL B 455    20530  19508  10699   5735  -3979  -4230       C  
ATOM   5911  CG1 VAL B 455     104.544  46.398   2.223  1.00138.47           C  
ANISOU 5911  CG1 VAL B 455    21069  20169  11376   5735  -3741  -4230       C  
ATOM   5912  CG2 VAL B 455     103.962  48.122   0.526  1.00129.49           C  
ANISOU 5912  CG2 VAL B 455    20153  19249   9798   5914  -3735  -4031       C  
ATOM   5913  N   ILE B 456     100.790  45.274   2.189  1.00128.04           N  
ANISOU 5913  N   ILE B 456    19722  18191  10734   5379  -4868  -4695       N  
ATOM   5914  CA  ILE B 456     100.124  44.309   3.066  1.00126.33           C  
ANISOU 5914  CA  ILE B 456    19372  17719  10911   5135  -5118  -4849       C  
ATOM   5915  C   ILE B 456      99.772  43.040   2.307  1.00128.84           C  
ANISOU 5915  C   ILE B 456    19914  17814  11225   5264  -5443  -5098       C  
ATOM   5916  O   ILE B 456      99.891  41.927   2.838  1.00119.41           O  
ANISOU 5916  O   ILE B 456    18725  16422  10224   5181  -5547  -5227       O  
ATOM   5917  CB  ILE B 456      98.867  44.929   3.703  1.00126.19           C  
ANISOU 5917  CB  ILE B 456    19104  17645  11197   4843  -5296  -4805       C  
ATOM   5918  CG1 ILE B 456      99.214  46.171   4.512  1.00123.99           C  
ANISOU 5918  CG1 ILE B 456    18616  17567  10929   4721  -4989  -4562       C  
ATOM   5919  CG2 ILE B 456      98.132  43.905   4.563  1.00124.75           C  
ANISOU 5919  CG2 ILE B 456    18774  17202  11422   4566  -5554  -4951       C  
ATOM   5920  CD1 ILE B 456      98.005  46.789   5.149  1.00124.22           C  
ANISOU 5920  CD1 ILE B 456    18391  17556  11252   4463  -5156  -4519       C  
ATOM   5921  N   LYS B 457      99.310  43.185   1.064  1.00134.26           N  
ANISOU 5921  N   LYS B 457    20802  18517  11695   5466  -5624  -5168       N  
ATOM   5922  CA  LYS B 457      98.858  42.025   0.307  1.00138.57           C  
ANISOU 5922  CA  LYS B 457    21568  18839  12242   5583  -5973  -5412       C  
ATOM   5923  C   LYS B 457     100.015  41.073   0.020  1.00140.37           C  
ANISOU 5923  C   LYS B 457    22010  19045  12279   5835  -5853  -5500       C  
ATOM   5924  O   LYS B 457      99.843  39.849   0.056  1.00144.85           O  
ANISOU 5924  O   LYS B 457    22686  19364  12985   5827  -6098  -5691       O  
ATOM   5925  CB  LYS B 457      98.178  42.491  -0.983  1.00142.17           C  
ANISOU 5925  CB  LYS B 457    22200  19343  12476   5770  -6173  -5456       C  
ATOM   5926  CG  LYS B 457      97.423  41.413  -1.749  1.00144.01           C  
ANISOU 5926  CG  LYS B 457    22633  19330  12754   5845  -6601  -5711       C  
ATOM   5927  CD  LYS B 457      96.605  42.017  -2.883  1.00151.86           C  
ANISOU 5927  CD  LYS B 457    23752  20376  13571   5986  -6812  -5741       C  
ATOM   5928  CE  LYS B 457      95.847  40.941  -3.653  1.00165.75           C  
ANISOU 5928  CE  LYS B 457    25714  21888  15376   6058  -7254  -6001       C  
ATOM   5929  NZ  LYS B 457      94.953  41.486  -4.718  1.00171.01           N  
ANISOU 5929  NZ  LYS B 457    26490  22588  15899   6181  -7499  -6046       N  
ATOM   5930  N   ARG B 458     101.210  41.617  -0.233  1.00136.24           N  
ANISOU 5930  N   ARG B 458    21539  18780  11445   6051  -5475  -5355       N  
ATOM   5931  CA  ARG B 458     102.363  40.766  -0.511  1.00130.00           C  
ANISOU 5931  CA  ARG B 458    20924  18010  10462   6314  -5337  -5428       C  
ATOM   5932  C   ARG B 458     102.717  39.911   0.697  1.00147.39           C  
ANISOU 5932  C   ARG B 458    22998  20047  12957   6137  -5314  -5475       C  
ATOM   5933  O   ARG B 458     102.976  38.710   0.557  1.00148.58           O  
ANISOU 5933  O   ARG B 458    23317  20012  13124   6263  -5468  -5650       O  
ATOM   5934  CB  ARG B 458     103.565  41.615  -0.931  1.00129.61           C  
ANISOU 5934  CB  ARG B 458    20894  18305  10046   6538  -4905  -5231       C  
ATOM   5935  CG  ARG B 458     103.221  42.815  -1.791  1.00141.19           C  
ANISOU 5935  CG  ARG B 458    22415  19962  11267   6613  -4849  -5097       C  
ATOM   5936  CD  ARG B 458     104.394  43.256  -2.650  1.00143.55           C  
ANISOU 5936  CD  ARG B 458    22852  20556  11133   6919  -4508  -4970       C  
ATOM   5937  NE  ARG B 458     105.663  43.243  -1.927  1.00130.17           N  
ANISOU 5937  NE  ARG B 458    21010  19028   9420   6916  -4129  -4842       N  
ATOM   5938  CZ  ARG B 458     106.155  44.274  -1.250  1.00126.60           C  
ANISOU 5938  CZ  ARG B 458    20340  18780   8981   6749  -3796  -4594       C  
ATOM   5939  NH1 ARG B 458     105.479  45.410  -1.178  1.00125.85           N  
ANISOU 5939  NH1 ARG B 458    20161  18736   8918   6574  -3798  -4444       N  
ATOM   5940  NH2 ARG B 458     107.324  44.167  -0.637  1.00124.91           N  
ANISOU 5940  NH2 ARG B 458    19993  18714   8752   6760  -3472  -4496       N  
ATOM   5941  N   VAL B 459     102.719  40.512   1.890  1.00135.22           N  
ANISOU 5941  N   VAL B 459    21173  18561  11645   5849  -5136  -5321       N  
ATOM   5942  CA  VAL B 459     103.128  39.801   3.098  1.00133.24           C  
ANISOU 5942  CA  VAL B 459    20794  18174  11656   5678  -5079  -5340       C  
ATOM   5943  C   VAL B 459     102.115  38.718   3.463  1.00140.17           C  
ANISOU 5943  C   VAL B 459    21699  18689  12872   5466  -5486  -5531       C  
ATOM   5944  O   VAL B 459     102.492  37.597   3.820  1.00139.27           O  
ANISOU 5944  O   VAL B 459    21678  18379  12861   5487  -5567  -5647       O  
ATOM   5945  CB  VAL B 459     103.342  40.808   4.247  1.00125.12           C  
ANISOU 5945  CB  VAL B 459    19462  17307  10771   5429  -4790  -5122       C  
ATOM   5946  CG1 VAL B 459     103.407  40.100   5.590  1.00121.25           C  
ANISOU 5946  CG1 VAL B 459    18822  16626  10620   5181  -4811  -5154       C  
ATOM   5947  CG2 VAL B 459     104.614  41.626   4.010  1.00119.31           C  
ANISOU 5947  CG2 VAL B 459    18709  16909   9714   5633  -4359  -4933       C  
ATOM   5948  N   LEU B 460     100.816  39.026   3.366  1.00149.91           N  
ANISOU 5948  N   LEU B 460    22851  19827  14284   5257  -5754  -5559       N  
ATOM   5949  CA  LEU B 460      99.787  38.030   3.665  1.00147.11           C  
ANISOU 5949  CA  LEU B 460    22498  19139  14257   5022  -6145  -5723       C  
ATOM   5950  C   LEU B 460      99.884  36.815   2.748  1.00146.21           C  
ANISOU 5950  C   LEU B 460    22714  18821  14016   5264  -6405  -5941       C  
ATOM   5951  O   LEU B 460      99.560  35.696   3.166  1.00150.50           O  
ANISOU 5951  O   LEU B 460    23313  19069  14801   5116  -6648  -6070       O  
ATOM   5952  CB  LEU B 460      98.399  38.655   3.555  1.00146.48           C  
ANISOU 5952  CB  LEU B 460    22259  19046  14351   4796  -6375  -5709       C  
ATOM   5953  CG  LEU B 460      98.084  39.773   4.544  1.00135.59           C  
ANISOU 5953  CG  LEU B 460    20540  17824  13155   4525  -6186  -5512       C  
ATOM   5954  CD1 LEU B 460      96.883  40.578   4.074  1.00133.37           C  
ANISOU 5954  CD1 LEU B 460    20150  17605  12919   4439  -6377  -5490       C  
ATOM   5955  CD2 LEU B 460      97.828  39.178   5.915  1.00129.27           C  
ANISOU 5955  CD2 LEU B 460    19531  16837  12750   4170  -6227  -5508       C  
ATOM   5956  N   ILE B 461     100.316  37.010   1.501  1.00142.94           N  
ANISOU 5956  N   ILE B 461    22532  18555  13225   5634  -6365  -5979       N  
ATOM   5957  CA  ILE B 461     100.502  35.878   0.598  1.00141.53           C  
ANISOU 5957  CA  ILE B 461    22685  18200  12892   5909  -6598  -6188       C  
ATOM   5958  C   ILE B 461     101.666  35.014   1.065  1.00141.50           C  
ANISOU 5958  C   ILE B 461    22771  18138  12853   6051  -6439  -6219       C  
ATOM   5959  O   ILE B 461     101.539  33.791   1.200  1.00153.92           O  
ANISOU 5959  O   ILE B 461    24498  19412  14571   6032  -6697  -6381       O  
ATOM   5960  CB  ILE B 461     100.707  36.369  -0.846  1.00142.76           C  
ANISOU 5960  CB  ILE B 461    23059  18553  12629   6281  -6569  -6208       C  
ATOM   5961  CG1 ILE B 461      99.399  36.915  -1.423  1.00141.37           C  
ANISOU 5961  CG1 ILE B 461    22857  18347  12510   6163  -6845  -6237       C  
ATOM   5962  CG2 ILE B 461     101.256  35.245  -1.720  1.00144.65           C  
ANISOU 5962  CG2 ILE B 461    23646  18670  12646   6638  -6713  -6402       C  
ATOM   5963  CD1 ILE B 461      99.578  37.737  -2.687  1.00143.62           C  
ANISOU 5963  CD1 ILE B 461    23305  18875  12390   6481  -6752  -6193       C  
ATOM   5964  N   ASN B 462     102.817  35.639   1.325  1.00137.62           N  
ANISOU 5964  N   ASN B 462    22185  17930  12174   6191  -6020  -6060       N  
ATOM   5965  CA  ASN B 462     103.987  34.906   1.797  1.00139.36           C  
ANISOU 5965  CA  ASN B 462    22457  18137  12355   6342  -5842  -6075       C  
ATOM   5966  C   ASN B 462     103.801  34.341   3.200  1.00137.65           C  
ANISOU 5966  C   ASN B 462    22082  17686  12534   6003  -5901  -6069       C  
ATOM   5967  O   ASN B 462     104.505  33.396   3.570  1.00133.47           O  
ANISOU 5967  O   ASN B 462    21656  17024  12033   6106  -5895  -6139       O  
ATOM   5968  CB  ASN B 462     105.226  35.808   1.751  1.00131.44           C  
ANISOU 5968  CB  ASN B 462    21346  17525  11068   6542  -5368  -5886       C  
ATOM   5969  CG  ASN B 462     105.729  36.041   0.333  1.00140.70           C  
ANISOU 5969  CG  ASN B 462    22734  18917  11809   6947  -5285  -5907       C  
ATOM   5970  OD1 ASN B 462     105.588  35.180  -0.537  1.00146.88           O  
ANISOU 5970  OD1 ASN B 462    23796  19548  12465   7184  -5543  -6098       O  
ATOM   5971  ND2 ASN B 462     106.315  37.210   0.095  1.00133.66           N  
ANISOU 5971  ND2 ASN B 462    21721  18379  10683   7022  -4925  -5705       N  
ATOM   5972  N   ILE B 463     102.876  34.893   3.989  1.00148.33           N  
ANISOU 5972  N   ILE B 463    23188  18986  14183   5610  -5957  -5982       N  
ATOM   5973  CA  ILE B 463     102.587  34.319   5.300  1.00156.56           C  
ANISOU 5973  CA  ILE B 463    24088  19788  15609   5264  -6037  -5977       C  
ATOM   5974  C   ILE B 463     101.816  33.015   5.152  1.00160.94           C  
ANISOU 5974  C   ILE B 463    24838  19949  16362   5165  -6471  -6173       C  
ATOM   5975  O   ILE B 463     101.908  32.130   6.015  1.00161.69           O  
ANISOU 5975  O   ILE B 463    24945  19796  16693   5000  -6553  -6208       O  
ATOM   5976  CB  ILE B 463     101.819  35.336   6.171  1.00159.52           C  
ANISOU 5976  CB  ILE B 463    24128  20251  16232   4882  -5960  -5819       C  
ATOM   5977  CG1 ILE B 463     102.758  36.419   6.693  1.00162.53           C  
ANISOU 5977  CG1 ILE B 463    24314  20960  16481   4931  -5518  -5615       C  
ATOM   5978  CG2 ILE B 463     101.116  34.660   7.347  1.00157.08           C  
ANISOU 5978  CG2 ILE B 463    23686  19647  16350   4477  -6148  -5838       C  
ATOM   5979  CD1 ILE B 463     102.079  37.392   7.626  1.00163.31           C  
ANISOU 5979  CD1 ILE B 463    24093  21137  16820   4576  -5439  -5461       C  
ATOM   5980  N   HIS B 464     101.085  32.856   4.042  1.00161.41           N  
ANISOU 5980  N   HIS B 464    25070  19939  16318   5271  -6756  -6302       N  
ATOM   5981  CA  HIS B 464     100.070  31.813   3.892  1.00164.78           C  
ANISOU 5981  CA  HIS B 464    25633  20002  16975   5095  -7203  -6469       C  
ATOM   5982  C   HIS B 464      98.939  32.040   4.896  1.00164.13           C  
ANISOU 5982  C   HIS B 464    25251  19804  17307   4586  -7320  -6389       C  
ATOM   5983  O   HIS B 464      98.466  31.111   5.550  1.00168.30           O  
ANISOU 5983  O   HIS B 464    25784  20027  18135   4312  -7540  -6443       O  
ATOM   5984  CB  HIS B 464     100.672  30.408   4.034  1.00163.26           C  
ANISOU 5984  CB  HIS B 464    25703  19527  16804   5224  -7337  -6603       C  
ATOM   5985  CG  HIS B 464      99.771  29.305   3.577  1.00161.02           C  
ANISOU 5985  CG  HIS B 464    25639  18879  16664   5135  -7808  -6791       C  
ATOM   5986  ND1 HIS B 464      99.159  29.306   2.342  1.00164.01           N  
ANISOU 5986  ND1 HIS B 464    26190  19248  16880   5299  -8064  -6921       N  
ATOM   5987  CD2 HIS B 464      99.397  28.153   4.182  1.00159.88           C  
ANISOU 5987  CD2 HIS B 464    25581  18360  16804   4898  -8073  -6867       C  
ATOM   5988  CE1 HIS B 464      98.434  28.210   2.212  1.00167.00           C  
ANISOU 5988  CE1 HIS B 464    26742  19265  17445   5160  -8473  -7074       C  
ATOM   5989  NE2 HIS B 464      98.562  27.492   3.314  1.00168.21           N  
ANISOU 5989  NE2 HIS B 464    26849  19191  17872   4910  -8484  -7039       N  
ATOM   5990  N   ALA B 465      98.511  33.296   5.018  1.00161.57           N  
ANISOU 5990  N   ALA B 465    24661  19733  16994   4460  -7165  -6248       N  
ATOM   5991  CA  ALA B 465      97.559  33.686   6.052  1.00156.58           C  
ANISOU 5991  CA  ALA B 465    23696  19064  16733   4003  -7204  -6141       C  
ATOM   5992  C   ALA B 465      96.158  33.212   5.687  1.00158.00           C  
ANISOU 5992  C   ALA B 465    23865  19032  17134   3769  -7626  -6254       C  
ATOM   5993  O   ALA B 465      95.664  33.498   4.592  1.00145.31           O  
ANISOU 5993  O   ALA B 465    22358  17493  15361   3933  -7794  -6333       O  
ATOM   5994  CB  ALA B 465      97.585  35.201   6.246  1.00124.65           C  
ANISOU 5994  CB  ALA B 465    19389  15366  12606   3986  -6912  -5958       C  
ATOM   5995  N   GLN B 466      95.518  32.477   6.612  1.00177.42           N  
ANISOU 5995  N   GLN B 466    26201  21240  19972   3376  -7797  -6255       N  
ATOM   5996  CA  GLN B 466      94.145  32.028   6.453  1.00194.67           C  
ANISOU 5996  CA  GLN B 466    28310  23237  22421   3077  -8178  -6333       C  
ATOM   5997  C   GLN B 466      93.174  33.141   6.838  1.00197.00           C  
ANISOU 5997  C   GLN B 466    28210  23745  22894   2806  -8131  -6200       C  
ATOM   5998  O   GLN B 466      93.492  33.995   7.671  1.00199.86           O  
ANISOU 5998  O   GLN B 466    28329  24307  23301   2719  -7823  -6032       O  
ATOM   5999  CB  GLN B 466      93.877  30.793   7.308  1.00201.00           C  
ANISOU 5999  CB  GLN B 466    29131  23691  23550   2747  -8358  -6364       C  
ATOM   6000  CG  GLN B 466      94.775  29.618   6.997  1.00205.07           C  
ANISOU 6000  CG  GLN B 466    30042  23961  23916   3005  -8438  -6497       C  
ATOM   6001  CD  GLN B 466      94.850  29.331   5.511  1.00211.61           C  
ANISOU 6001  CD  GLN B 466    31200  24766  24437   3394  -8653  -6681       C  
ATOM   6002  OE1 GLN B 466      93.848  29.003   4.873  1.00213.95           O  
ANISOU 6002  OE1 GLN B 466    31541  24932  24816   3292  -9001  -6792       O  
ATOM   6003  NE2 GLN B 466      96.045  29.461   4.948  1.00214.33           N  
ANISOU 6003  NE2 GLN B 466    31769  25249  24419   3846  -8442  -6712       N  
ATOM   6004  N   PRO B 467      91.978  33.161   6.243  1.00195.95           N  
ANISOU 6004  N   PRO B 467    28006  23582  22865   2682  -8440  -6272       N  
ATOM   6005  CA  PRO B 467      91.023  34.245   6.497  1.00188.60           C  
ANISOU 6005  CA  PRO B 467    26701  22875  22082   2473  -8413  -6155       C  
ATOM   6006  C   PRO B 467      90.093  33.978   7.681  1.00182.65           C  
ANISOU 6006  C   PRO B 467    25594  22029  21777   1959  -8486  -6064       C  
ATOM   6007  O   PRO B 467      88.881  34.187   7.601  1.00184.29           O  
ANISOU 6007  O   PRO B 467    25561  22278  22184   1727  -8693  -6062       O  
ATOM   6008  CB  PRO B 467      90.249  34.323   5.180  1.00193.65           C  
ANISOU 6008  CB  PRO B 467    27463  23527  22587   2633  -8724  -6293       C  
ATOM   6009  CG  PRO B 467      90.201  32.890   4.731  1.00198.56           C  
ANISOU 6009  CG  PRO B 467    28388  23812  23242   2638  -9042  -6479       C  
ATOM   6010  CD  PRO B 467      91.512  32.269   5.162  1.00199.08           C  
ANISOU 6010  CD  PRO B 467    28684  23762  23195   2793  -8828  -6476       C  
ATOM   6011  N   ASN B 468      90.658  33.522   8.801  1.00180.73           N  
ANISOU 6011  N   ASN B 468    25306  21672  21690   1779  -8309  -5981       N  
ATOM   6012  CA  ASN B 468      89.853  33.269   9.993  1.00182.74           C  
ANISOU 6012  CA  ASN B 468    25226  21850  22357   1286  -8338  -5872       C  
ATOM   6013  C   ASN B 468      89.698  34.554  10.798  1.00178.39           C  
ANISOU 6013  C   ASN B 468    24288  21602  21890   1173  -8049  -5680       C  
ATOM   6014  O   ASN B 468      89.926  35.645  10.269  1.00170.58           O  
ANISOU 6014  O   ASN B 468    23279  20870  20664   1445  -7909  -5647       O  
ATOM   6015  CB  ASN B 468      90.472  32.173  10.865  1.00181.28           C  
ANISOU 6015  CB  ASN B 468    25178  21386  22314   1128  -8293  -5861       C  
ATOM   6016  CG  ASN B 468      89.430  31.432  11.697  1.00175.71           C  
ANISOU 6016  CG  ASN B 468    24247  20490  22024    611  -8476  -5810       C  
ATOM   6017  OD1 ASN B 468      89.378  31.561  12.927  1.00168.14           O  
ANISOU 6017  OD1 ASN B 468    23031  19556  21298    313  -8285  -5651       O  
ATOM   6018  ND2 ASN B 468      88.607  30.634  11.025  1.00174.85           N  
ANISOU 6018  ND2 ASN B 468    24240  20191  22006    500  -8846  -5942       N  
ATOM   6019  N   ALA B 469      89.329  34.438  12.077  1.00180.91           N  
ANISOU 6019  N   ALA B 469    24310  21891  22536    781  -7954  -5545       N  
ATOM   6020  CA  ALA B 469      88.985  35.616  12.867  1.00184.83           C  
ANISOU 6020  CA  ALA B 469    24406  22668  23152    643  -7721  -5367       C  
ATOM   6021  C   ALA B 469      90.131  36.614  12.969  1.00181.26           C  
ANISOU 6021  C   ALA B 469    24017  22427  22426    960  -7375  -5286       C  
ATOM   6022  O   ALA B 469      89.891  37.786  13.278  1.00176.93           O  
ANISOU 6022  O   ALA B 469    23200  22142  21886    962  -7205  -5163       O  
ATOM   6023  CB  ALA B 469      88.531  35.193  14.266  1.00185.34           C  
ANISOU 6023  CB  ALA B 469    24178  22646  23598    181  -7655  -5233       C  
ATOM   6024  N   VAL B 470      91.366  36.184  12.709  1.00180.23           N  
ANISOU 6024  N   VAL B 470    24231  22196  22051   1235  -7267  -5351       N  
ATOM   6025  CA  VAL B 470      92.503  37.089  12.823  1.00172.14           C  
ANISOU 6025  CA  VAL B 470    23259  21384  20764   1519  -6926  -5267       C  
ATOM   6026  C   VAL B 470      92.582  38.023  11.620  1.00171.27           C  
ANISOU 6026  C   VAL B 470    23253  21497  20323   1874  -6913  -5298       C  
ATOM   6027  O   VAL B 470      92.855  39.220  11.767  1.00165.05           O  
ANISOU 6027  O   VAL B 470    22331  20969  19414   1985  -6676  -5175       O  
ATOM   6028  CB  VAL B 470      93.802  36.281  12.999  1.00167.67           C  
ANISOU 6028  CB  VAL B 470    22997  20655  20056   1688  -6803  -5318       C  
ATOM   6029  CG1 VAL B 470      94.976  37.210  13.278  1.00162.84           C  
ANISOU 6029  CG1 VAL B 470    22385  20281  19206   1930  -6429  -5211       C  
ATOM   6030  CG2 VAL B 470      93.645  35.251  14.108  1.00164.27           C  
ANISOU 6030  CG2 VAL B 470    22508  19956  19951   1334  -6861  -5293       C  
ATOM   6031  N   TYR B 471      92.331  37.505  10.418  1.00179.21           N  
ANISOU 6031  N   TYR B 471    24510  22402  21178   2054  -7172  -5457       N  
ATOM   6032  CA  TYR B 471      92.583  38.241   9.185  1.00180.63           C  
ANISOU 6032  CA  TYR B 471    24869  22765  20998   2433  -7153  -5495       C  
ATOM   6033  C   TYR B 471      91.306  38.630   8.446  1.00179.46           C  
ANISOU 6033  C   TYR B 471    24606  22675  20905   2387  -7426  -5542       C  
ATOM   6034  O   TYR B 471      91.374  38.978   7.262  1.00176.76           O  
ANISOU 6034  O   TYR B 471    24470  22417  20273   2694  -7498  -5610       O  
ATOM   6035  CB  TYR B 471      93.483  37.416   8.259  1.00185.22           C  
ANISOU 6035  CB  TYR B 471    25872  23216  21288   2765  -7203  -5643       C  
ATOM   6036  CG  TYR B 471      94.849  37.099   8.832  1.00180.17           C  
ANISOU 6036  CG  TYR B 471    25362  22557  20537   2889  -6919  -5602       C  
ATOM   6037  CD1 TYR B 471      95.945  37.911   8.570  1.00177.72           C  
ANISOU 6037  CD1 TYR B 471    25135  22491  19901   3197  -6596  -5517       C  
ATOM   6038  CD2 TYR B 471      95.041  35.982   9.634  1.00181.77           C  
ANISOU 6038  CD2 TYR B 471    25604  22499  20961   2692  -6977  -5641       C  
ATOM   6039  CE1 TYR B 471      97.195  37.618   9.093  1.00179.82           C  
ANISOU 6039  CE1 TYR B 471    25495  22759  20069   3313  -6337  -5481       C  
ATOM   6040  CE2 TYR B 471      96.284  35.683  10.162  1.00182.96           C  
ANISOU 6040  CE2 TYR B 471    25872  22632  21012   2820  -6730  -5609       C  
ATOM   6041  CZ  TYR B 471      97.358  36.503   9.889  1.00181.06           C  
ANISOU 6041  CZ  TYR B 471    25688  22655  20452   3135  -6411  -5533       C  
ATOM   6042  OH  TYR B 471      98.595  36.204  10.414  1.00176.86           O  
ANISOU 6042  OH  TYR B 471    25248  22126  19825   3266  -6165  -5501       O  
ATOM   6043  N   CYS B 472      90.148  38.585   9.109  1.00182.01           N  
ANISOU 6043  N   CYS B 472    24601  22969  21587   2018  -7574  -5501       N  
ATOM   6044  CA  CYS B 472      88.893  38.929   8.444  1.00185.58           C  
ANISOU 6044  CA  CYS B 472    24913  23488  22110   1967  -7843  -5548       C  
ATOM   6045  C   CYS B 472      88.892  40.382   7.981  1.00182.35           C  
ANISOU 6045  C   CYS B 472    24436  23370  21477   2211  -7695  -5454       C  
ATOM   6046  O   CYS B 472      88.689  40.672   6.797  1.00186.27           O  
ANISOU 6046  O   CYS B 472    25115  23918  21740   2469  -7843  -5536       O  
ATOM   6047  CB  CYS B 472      87.710  38.667   9.379  1.00183.52           C  
ANISOU 6047  CB  CYS B 472    24257  23187  22284   1510  -7973  -5492       C  
ATOM   6048  SG  CYS B 472      87.251  36.932   9.570  1.00185.53           S  
ANISOU 6048  SG  CYS B 472    24599  23080  22814   1188  -8282  -5622       S  
ATOM   6049  N   ARG B 473      89.119  41.312   8.911  1.00171.20           N  
ANISOU 6049  N   ARG B 473    22777  22140  20131   2136  -7407  -5276       N  
ATOM   6050  CA  ARG B 473      88.997  42.730   8.590  1.00161.57           C  
ANISOU 6050  CA  ARG B 473    21468  21181  18740   2327  -7280  -5168       C  
ATOM   6051  C   ARG B 473      90.095  43.185   7.635  1.00159.18           C  
ANISOU 6051  C   ARG B 473    21526  20965  17991   2738  -7121  -5172       C  
ATOM   6052  O   ARG B 473      89.828  43.933   6.687  1.00156.76           O  
ANISOU 6052  O   ARG B 473    21314  20781  17466   2966  -7185  -5172       O  
ATOM   6053  CB  ARG B 473      89.032  43.561   9.874  1.00150.10           C  
ANISOU 6053  CB  ARG B 473    19680  19882  17469   2148  -7010  -4979       C  
ATOM   6054  CG  ARG B 473      88.002  43.163  10.923  1.00144.30           C  
ANISOU 6054  CG  ARG B 473    18557  19097  17173   1734  -7111  -4944       C  
ATOM   6055  CD  ARG B 473      87.977  44.156  12.081  1.00137.92           C  
ANISOU 6055  CD  ARG B 473    17417  18477  16509   1615  -6843  -4755       C  
ATOM   6056  NE  ARG B 473      89.324  44.495  12.538  1.00133.85           N  
ANISOU 6056  NE  ARG B 473    17048  18002  15806   1753  -6519  -4668       N  
ATOM   6057  CZ  ARG B 473      90.012  43.802  13.441  1.00129.74           C  
ANISOU 6057  CZ  ARG B 473    16535  17359  15399   1595  -6377  -4648       C  
ATOM   6058  NH1 ARG B 473      89.489  42.716  13.993  1.00129.68           N  
ANISOU 6058  NH1 ARG B 473    16417  17164  15692   1282  -6525  -4698       N  
ATOM   6059  NH2 ARG B 473      91.231  44.192  13.788  1.00125.29           N  
ANISOU 6059  NH2 ARG B 473    16098  16861  14645   1745  -6088  -4571       N  
ATOM   6060  N   LEU B 474      91.336  42.742   7.866  1.00154.93           N  
ANISOU 6060  N   LEU B 474    21187  20370  17307   2839  -6906  -5166       N  
ATOM   6061  CA  LEU B 474      92.464  43.254   7.091  1.00151.01           C  
ANISOU 6061  CA  LEU B 474    20983  20004  16390   3209  -6688  -5131       C  
ATOM   6062  C   LEU B 474      92.402  42.791   5.639  1.00146.08           C  
ANISOU 6062  C   LEU B 474    20686  19308  15507   3480  -6912  -5290       C  
ATOM   6063  O   LEU B 474      92.682  43.572   4.721  1.00141.60           O  
ANISOU 6063  O   LEU B 474    20286  18897  14618   3765  -6836  -5249       O  
ATOM   6064  CB  LEU B 474      93.786  42.826   7.735  1.00145.79           C  
ANISOU 6064  CB  LEU B 474    20423  19315  15657   3244  -6407  -5091       C  
ATOM   6065  CG  LEU B 474      95.084  43.240   7.028  1.00136.74           C  
ANISOU 6065  CG  LEU B 474    19551  18320  14083   3606  -6139  -5041       C  
ATOM   6066  CD1 LEU B 474      95.373  44.723   7.225  1.00128.43           C  
ANISOU 6066  CD1 LEU B 474    18378  17533  12887   3670  -5862  -4833       C  
ATOM   6067  CD2 LEU B 474      96.262  42.397   7.486  1.00133.91           C  
ANISOU 6067  CD2 LEU B 474    19322  17877  13681   3653  -5961  -5070       C  
ATOM   6068  N   MET B 475      92.045  41.524   5.411  1.00148.33           N  
ANISOU 6068  N   MET B 475    21082  19353  15926   3396  -7190  -5467       N  
ATOM   6069  CA  MET B 475      91.937  41.022   4.045  1.00160.91           C  
ANISOU 6069  CA  MET B 475    22992  20861  17286   3654  -7433  -5634       C  
ATOM   6070  C   MET B 475      90.853  41.755   3.263  1.00170.13           C  
ANISOU 6070  C   MET B 475    24094  22127  18422   3703  -7651  -5649       C  
ATOM   6071  O   MET B 475      90.985  41.943   2.049  1.00177.30           O  
ANISOU 6071  O   MET B 475    25269  23081  19016   4011  -7728  -5714       O  
ATOM   6072  CB  MET B 475      91.669  39.515   4.058  1.00164.98           C  
ANISOU 6072  CB  MET B 475    23621  21074  17990   3517  -7717  -5817       C  
ATOM   6073  CG  MET B 475      92.915  38.650   3.871  1.00160.45           C  
ANISOU 6073  CG  MET B 475    23363  20388  17213   3736  -7598  -5892       C  
ATOM   6074  SD  MET B 475      92.602  36.887   4.113  1.00159.62           S  
ANISOU 6074  SD  MET B 475    23382  19894  17374   3534  -7925  -6080       S  
ATOM   6075  CE  MET B 475      93.996  36.161   3.254  1.00154.98           C  
ANISOU 6075  CE  MET B 475    23250  19244  16390   3986  -7833  -6197       C  
ATOM   6076  N   GLU B 476      89.781  42.181   3.937  1.00170.27           N  
ANISOU 6076  N   GLU B 476    23756  22186  18754   3416  -7749  -5586       N  
ATOM   6077  CA  GLU B 476      88.744  42.954   3.262  1.00175.59           C  
ANISOU 6077  CA  GLU B 476    24339  22971  19407   3472  -7946  -5589       C  
ATOM   6078  C   GLU B 476      89.224  44.355   2.910  1.00172.44           C  
ANISOU 6078  C   GLU B 476    23996  22816  18707   3731  -7690  -5432       C  
ATOM   6079  O   GLU B 476      88.812  44.913   1.886  1.00177.05           O  
ANISOU 6079  O   GLU B 476    24708  23475  19088   3945  -7826  -5459       O  
ATOM   6080  CB  GLU B 476      87.496  43.032   4.141  1.00178.12           C  
ANISOU 6080  CB  GLU B 476    24231  23295  20151   3100  -8095  -5553       C  
ATOM   6081  CG  GLU B 476      86.846  41.692   4.424  1.00183.47           C  
ANISOU 6081  CG  GLU B 476    24835  23736  21140   2803  -8379  -5692       C  
ATOM   6082  CD  GLU B 476      85.886  41.753   5.593  1.00185.65           C  
ANISOU 6082  CD  GLU B 476    24650  24046  21843   2394  -8407  -5603       C  
ATOM   6083  OE1 GLU B 476      85.569  42.875   6.041  1.00184.21           O  
ANISOU 6083  OE1 GLU B 476    24204  24076  21710   2376  -8255  -5458       O  
ATOM   6084  OE2 GLU B 476      85.449  40.682   6.063  1.00188.44           O  
ANISOU 6084  OE2 GLU B 476    24907  24215  22477   2092  -8575  -5671       O  
ATOM   6085  N   GLU B 477      90.096  44.934   3.738  1.00161.05           N  
ANISOU 6085  N   GLU B 477    22474  21491  17228   3713  -7328  -5263       N  
ATOM   6086  CA  GLU B 477      90.519  46.314   3.539  1.00151.02           C  
ANISOU 6086  CA  GLU B 477    21231  20444  15704   3908  -7078  -5087       C  
ATOM   6087  C   GLU B 477      91.495  46.470   2.377  1.00149.68           C  
ANISOU 6087  C   GLU B 477    21456  20339  15077   4277  -6956  -5089       C  
ATOM   6088  O   GLU B 477      91.676  47.588   1.886  1.00151.15           O  
ANISOU 6088  O   GLU B 477    21723  20693  15014   4463  -6821  -4958       O  
ATOM   6089  CB  GLU B 477      91.147  46.851   4.826  1.00139.04           C  
ANISOU 6089  CB  GLU B 477    19501  19027  14302   3754  -6740  -4906       C  
ATOM   6090  CG  GLU B 477      91.065  48.360   4.986  1.00135.22           C  
ANISOU 6090  CG  GLU B 477    18903  18749  13726   3822  -6563  -4710       C  
ATOM   6091  CD  GLU B 477      89.694  48.816   5.441  1.00141.12           C  
ANISOU 6091  CD  GLU B 477    19313  19522  14785   3630  -6760  -4697       C  
ATOM   6092  OE1 GLU B 477      88.942  47.985   5.991  1.00143.50           O  
ANISOU 6092  OE1 GLU B 477    19394  19704  15424   3369  -6951  -4798       O  
ATOM   6093  OE2 GLU B 477      89.370  50.008   5.256  1.00143.56           O  
ANISOU 6093  OE2 GLU B 477    19575  19971  15000   3740  -6718  -4579       O  
ATOM   6094  N   VAL B 478      92.119  45.386   1.923  1.00145.02           N  
ANISOU 6094  N   VAL B 478    21113  19620  14367   4389  -6996  -5227       N  
ATOM   6095  CA  VAL B 478      93.123  45.478   0.867  1.00134.42           C  
ANISOU 6095  CA  VAL B 478    20126  18359  12587   4743  -6846  -5223       C  
ATOM   6096  C   VAL B 478      92.748  44.635  -0.354  1.00141.23           C  
ANISOU 6096  C   VAL B 478    21265  19083  13315   4932  -7170  -5439       C  
ATOM   6097  O   VAL B 478      91.719  43.957  -0.374  1.00139.02           O  
ANISOU 6097  O   VAL B 478    20903  18631  13287   4773  -7521  -5593       O  
ATOM   6098  CB  VAL B 478      94.516  45.072   1.397  1.00128.96           C  
ANISOU 6098  CB  VAL B 478    19509  17694  11796   4787  -6515  -5166       C  
ATOM   6099  CG1 VAL B 478      94.981  46.040   2.478  1.00118.63           C  
ANISOU 6099  CG1 VAL B 478    17965  16548  10560   4643  -6179  -4941       C  
ATOM   6100  CG2 VAL B 478      94.496  43.645   1.928  1.00124.04           C  
ANISOU 6100  CG2 VAL B 478    18871  16831  11425   4627  -6672  -5334       C  
TER    6101      VAL B 478                                                      
ATOM   6102  P     U C  -1      55.478  54.291  56.039  1.00164.44           P  
ANISOU 6102  P     U C  -1    20587  17059  24831    450  -1611    138       P  
ATOM   6103  OP1   U C  -1      54.250  54.954  55.533  1.00172.53           O  
ANISOU 6103  OP1   U C  -1    21611  18155  25788    436  -1770    186       O  
ATOM   6104  OP2   U C  -1      55.369  53.135  56.967  1.00164.77           O  
ANISOU 6104  OP2   U C  -1    20533  16901  25170    459  -1506     45       O  
ATOM   6105  O5'   U C  -1      56.347  53.829  54.786  1.00161.01           O  
ANISOU 6105  O5'   U C  -1    20134  16911  24133    468  -1621   -104       O  
ATOM   6106  C5'   U C  -1      56.416  54.622  53.605  1.00155.40           C  
ANISOU 6106  C5'   U C  -1    19463  16543  23039    462  -1706    -77       C  
ATOM   6107  C4'   U C  -1      57.766  54.504  52.941  1.00148.64           C  
ANISOU 6107  C4'   U C  -1    18621  15950  21906    477  -1625   -158       C  
ATOM   6108  O4'   U C  -1      58.286  53.165  53.165  1.00151.17           O  
ANISOU 6108  O4'   U C  -1    18858  16144  22435    515  -1558   -435       O  
ATOM   6109  C3'   U C  -1      57.771  54.717  51.429  1.00142.00           C  
ANISOU 6109  C3'   U C  -1    17745  15522  20686    502  -1730   -281       C  
ATOM   6110  O3'   U C  -1      59.012  55.307  51.039  1.00121.76           O  
ANISOU 6110  O3'   U C  -1    15241  13217  17806    489  -1631   -144       O  
ATOM   6111  C2'   U C  -1      57.690  53.289  50.893  1.00153.29           C  
ANISOU 6111  C2'   U C  -1    19034  16977  22232    558  -1783   -719       C  
ATOM   6112  O2'   U C  -1      58.195  53.122  49.584  1.00159.02           O  
ANISOU 6112  O2'   U C  -1    19696  18122  22604    607  -1831   -927       O  
ATOM   6113  C1'   U C  -1      58.520  52.525  51.923  1.00152.10           C  
ANISOU 6113  C1'   U C  -1    18887  16543  22362    559  -1629   -756       C  
ATOM   6114  N1    U C  -1      58.141  51.110  52.066  1.00145.92           N  
ANISOU 6114  N1    U C  -1    17976  15534  21934    596  -1660  -1093       N  
ATOM   6115  C2    U C  -1      58.982  50.137  51.554  1.00137.11           C  
ANISOU 6115  C2    U C  -1    16777  14521  20799    651  -1629  -1407       C  
ATOM   6116  O2    U C  -1      60.027  50.386  50.979  1.00121.47           O  
ANISOU 6116  O2    U C  -1    14822  12839  18492    674  -1575  -1422       O  
ATOM   6117  N3    U C  -1      58.547  48.847  51.737  1.00148.89           N  
ANISOU 6117  N3    U C  -1    18139  15745  22686    681  -1662  -1708       N  
ATOM   6118  C4    U C  -1      57.388  48.433  52.365  1.00154.82           C  
ANISOU 6118  C4    U C  -1    18832  16152  23839    651  -1714  -1708       C  
ATOM   6119  O4    U C  -1      57.136  47.228  52.449  1.00160.24           O  
ANISOU 6119  O4    U C  -1    19387  16603  24893    675  -1734  -1987       O  
ATOM   6120  C5    U C  -1      56.576  49.498  52.868  1.00151.14           C  
ANISOU 6120  C5    U C  -1    18458  15635  23334    595  -1740  -1370       C  
ATOM   6121  C6    U C  -1      56.973  50.764  52.706  1.00148.26           C  
ANISOU 6121  C6    U C  -1    18223  15514  22595    575  -1716  -1092       C  
ATOM   6122  P     U C   1      59.115  56.198  49.703  1.00 99.44           P  
ANISOU 6122  P     U C   1    12421  10843  14517    498  -1700    -28       P  
ATOM   6123  OP1   U C   1      58.020  57.198  49.694  1.00 89.96           O  
ANISOU 6123  OP1   U C   1    11271   9600  13309    478  -1806    222       O  
ATOM   6124  OP2   U C   1      59.314  55.289  48.542  1.00 98.49           O  
ANISOU 6124  OP2   U C   1    12175  11053  14194    572  -1764   -396       O  
ATOM   6125  O5'   U C   1      60.471  56.999  49.897  1.00 90.60           O  
ANISOU 6125  O5'   U C   1    11388   9826  13211    446  -1540    242       O  
ATOM   6126  C5'   U C   1      61.325  57.237  48.797  1.00 88.15           C  
ANISOU 6126  C5'   U C   1    11047   9946  12500    461  -1511    249       C  
ATOM   6127  C4'   U C   1      62.652  57.791  49.240  1.00 80.20           C  
ANISOU 6127  C4'   U C   1    10104   8947  11420    399  -1339    464       C  
ATOM   6128  O4'   U C   1      62.459  59.034  49.957  1.00 79.45           O  
ANISOU 6128  O4'   U C   1    10115   8639  11433    321  -1308    847       O  
ATOM   6129  C3'   U C   1      63.455  56.945  50.208  1.00 62.99           C  
ANISOU 6129  C3'   U C   1     7921   6528   9483    403  -1215    299       C  
ATOM   6130  O3'   U C   1      64.113  55.858  49.584  1.00 72.02           O  
ANISOU 6130  O3'   U C   1     8967   7887  10509    471  -1196    -40       O  
ATOM   6131  C2'   U C   1      64.407  57.971  50.811  1.00 70.62           C  
ANISOU 6131  C2'   U C   1     8970   7451  10412    321  -1074    622       C  
ATOM   6132  O2'   U C   1      65.482  58.240  49.928  1.00 80.38           O  
ANISOU 6132  O2'   U C   1    10175   9069  11297    307  -1000    665       O  
ATOM   6133  C1'   U C   1      63.519  59.216  50.874  1.00 75.95           C  
ANISOU 6133  C1'   U C   1     9717   8036  11106    268  -1151    946       C  
ATOM   6134  N1    U C   1      62.982  59.421  52.236  1.00 78.13           N  
ANISOU 6134  N1    U C   1    10048   7891  11747    246  -1142   1041       N  
ATOM   6135  C2    U C   1      63.606  60.393  52.994  1.00 81.32           C  
ANISOU 6135  C2    U C   1    10512   8167  12219    176  -1041   1300       C  
ATOM   6136  O2    U C   1      64.519  61.079  52.567  1.00 84.39           O  
ANISOU 6136  O2    U C   1    10913   8748  12405    120   -963   1463       O  
ATOM   6137  N3    U C   1      63.108  60.542  54.261  1.00 74.27           N  
ANISOU 6137  N3    U C   1     9648   6927  11643    176  -1038   1356       N  
ATOM   6138  C4    U C   1      62.081  59.818  54.829  1.00 70.13           C  
ANISOU 6138  C4    U C   1     9100   6179  11366    232  -1112   1212       C  
ATOM   6139  O4    U C   1      61.739  60.069  55.982  1.00 70.85           O  
ANISOU 6139  O4    U C   1     9208   6005  11708    233  -1093   1297       O  
ATOM   6140  C5    U C   1      61.498  58.821  53.986  1.00 70.38           C  
ANISOU 6140  C5    U C   1     9071   6330  11339    286  -1207    960       C  
ATOM   6141  C6    U C   1      61.963  58.655  52.747  1.00 70.17           C  
ANISOU 6141  C6    U C   1     9013   6642  11006    295  -1223    866       C  
ATOM   6142  P     A C   2      63.938  54.362  50.150  1.00 80.41           P  
ANISOU 6142  P     A C   2     9959   8675  11919    539  -1204   -409       P  
ATOM   6143  OP1   A C   2      64.644  53.454  49.210  1.00 81.56           O  
ANISOU 6143  OP1   A C   2     9992   9128  11868    615  -1206   -755       O  
ATOM   6144  OP2   A C   2      62.506  54.128  50.479  1.00 73.41           O  
ANISOU 6144  OP2   A C   2     9062   7517  11314    544  -1329   -456       O  
ATOM   6145  O5'   A C   2      64.768  54.359  51.508  1.00 77.14           O  
ANISOU 6145  O5'   A C   2     9608   7962  11738    509  -1040   -269       O  
ATOM   6146  C5'   A C   2      66.155  54.062  51.511  1.00 71.94           C  
ANISOU 6146  C5'   A C   2     8930   7449  10955    527   -908   -341       C  
ATOM   6147  C4'   A C   2      66.984  55.315  51.388  1.00 75.49           C  
ANISOU 6147  C4'   A C   2     9445   8105  11132    447   -816    -27       C  
ATOM   6148  O4'   A C   2      66.579  56.281  52.393  1.00 75.34           O  
ANISOU 6148  O4'   A C   2     9519   7809  11298    375   -793    289       O  
ATOM   6149  C3'   A C   2      68.477  55.148  51.613  1.00 76.94           C  
ANISOU 6149  C3'   A C   2     9611   8408  11215    450   -659    -56       C  
ATOM   6150  O3'   A C   2      69.147  54.659  50.466  1.00 80.89           O  
ANISOU 6150  O3'   A C   2    10023   9301  11410    501   -659   -276       O  
ATOM   6151  C2'   A C   2      68.912  56.549  52.024  1.00 79.72           C  
ANISOU 6151  C2'   A C   2    10043   8759  11488    342   -576    325       C  
ATOM   6152  O2'   A C   2      69.055  57.385  50.887  1.00 81.47           O  
ANISOU 6152  O2'   A C   2    10258   9337  11361    291   -600    485       O  
ATOM   6153  C1'   A C   2      67.699  57.026  52.824  1.00 76.57           C  
ANISOU 6153  C1'   A C   2     9712   8013  11368    314   -654    492       C  
ATOM   6154  N9    A C   2      67.868  56.843  54.281  1.00 71.60           N  
ANISOU 6154  N9    A C   2     9105   7046  11053    326   -572    526       N  
ATOM   6155  C8    A C   2      67.300  55.899  55.102  1.00 69.01           C  
ANISOU 6155  C8    A C   2     8754   6431  11037    398   -590    379       C  
ATOM   6156  N7    A C   2      67.643  56.017  56.360  1.00 65.95           N  
ANISOU 6156  N7    A C   2     8380   5831  10846    406   -495    483       N  
ATOM   6157  C5    A C   2      68.494  57.113  56.374  1.00 64.60           C  
ANISOU 6157  C5    A C   2     8244   5802  10500    329   -416    680       C  
ATOM   6158  C6    A C   2      69.201  57.761  57.407  1.00 59.50           C  
ANISOU 6158  C6    A C   2     7608   5068   9931    301   -308    830       C  
ATOM   6159  N6    A C   2      69.168  57.386  58.687  1.00 56.26           N  
ANISOU 6159  N6    A C   2     7175   4432   9768    367   -255    819       N  
ATOM   6160  N1    A C   2      69.956  58.827  57.076  1.00 59.27           N  
ANISOU 6160  N1    A C   2     7597   5208   9717    206   -253    996       N  
ATOM   6161  C2    A C   2      69.998  59.210  55.795  1.00 68.99           C  
ANISOU 6161  C2    A C   2     8836   6691  10685    149   -296   1045       C  
ATOM   6162  N3    A C   2      69.379  58.686  54.740  1.00 78.40           N  
ANISOU 6162  N3    A C   2    10018   8026  11743    182   -397    926       N  
ATOM   6163  C4    A C   2      68.637  57.627  55.102  1.00 68.62           C  
ANISOU 6163  C4    A C   2     8761   6602  10710    272   -458    724       C  
ATOM   6164  P     A C   3      70.470  53.761  50.615  1.00 80.42           P  
ANISOU 6164  P     A C   3     9897   9330  11329    567   -539   -513       P  
ATOM   6165  OP1   A C   3      70.823  53.289  49.253  1.00 89.78           O  
ANISOU 6165  OP1   A C   3    10975  10956  12183    632   -586   -770       O  
ATOM   6166  OP2   A C   3      70.260  52.766  51.702  1.00 82.21           O  
ANISOU 6166  OP2   A C   3    10119   9150  11966    632   -521   -671       O  
ATOM   6167  O5'   A C   3      71.590  54.791  51.089  1.00 82.74           O  
ANISOU 6167  O5'   A C   3    10243   9699  11495    475   -383   -209       O  
ATOM   6168  C5'   A C   3      71.982  55.883  50.267  1.00 89.53           C  
ANISOU 6168  C5'   A C   3    11108  10899  12011    391   -356     32       C  
ATOM   6169  C4'   A C   3      72.852  56.858  51.022  1.00 88.96           C  
ANISOU 6169  C4'   A C   3    11084  10755  11962    287   -216    323       C  
ATOM   6170  O4'   A C   3      72.090  57.446  52.106  1.00 86.14           O  
ANISOU 6170  O4'   A C   3    10816   9998  11916    238   -241    523       O  
ATOM   6171  C3'   A C   3      74.071  56.253  51.702  1.00 87.09           C  
ANISOU 6171  C3'   A C   3    10807  10495  11790    328    -80    174       C  
ATOM   6172  O3'   A C   3      75.172  56.120  50.826  1.00 94.58           O  
ANISOU 6172  O3'   A C   3    11670  11859  12408    337     -5     83       O  
ATOM   6173  C2'   A C   3      74.324  57.198  52.868  1.00 77.42           C  
ANISOU 6173  C2'   A C   3     9645   9014  10756    236      6    448       C  
ATOM   6174  O2'   A C   3      75.020  58.363  52.451  1.00 76.58           O  
ANISOU 6174  O2'   A C   3     9533   9128  10438    114     82    709       O  
ATOM   6175  C1'   A C   3      72.901  57.590  53.250  1.00 79.72           C  
ANISOU 6175  C1'   A C   3    10015   9006  11271    217   -116    581       C  
ATOM   6176  N9    A C   3      72.362  56.709  54.292  1.00 78.04           N  
ANISOU 6176  N9    A C   3     9812   8450  11389    307   -140    426       N  
ATOM   6177  C8    A C   3      71.649  55.547  54.128  1.00 80.17           C  
ANISOU 6177  C8    A C   3    10053   8621  11787    408   -227    173       C  
ATOM   6178  N7    A C   3      71.304  54.988  55.260  1.00 80.16           N  
ANISOU 6178  N7    A C   3    10058   8292  12108    467   -213    133       N  
ATOM   6179  C5    A C   3      71.832  55.845  56.218  1.00 73.94           C  
ANISOU 6179  C5    A C   3     9302   7414  11376    413   -117    353       C  
ATOM   6180  C6    A C   3      71.815  55.818  57.613  1.00 61.81           C  
ANISOU 6180  C6    A C   3     7770   5613  10102    451    -58    426       C  
ATOM   6181  N6    A C   3      71.222  54.852  58.311  1.00 72.46           N  
ANISOU 6181  N6    A C   3     9095   6718  11719    550    -78    322       N  
ATOM   6182  N1    A C   3      72.432  56.823  58.270  1.00 67.23           N  
ANISOU 6182  N1    A C   3     8469   6307  10770    387     24    611       N  
ATOM   6183  C2    A C   3      73.023  57.794  57.562  1.00 73.88           C  
ANISOU 6183  C2    A C   3     9322   7370  11378    277     50    736       C  
ATOM   6184  N3    A C   3      73.111  57.930  56.244  1.00 77.51           N  
ANISOU 6184  N3    A C   3     9782   8091  11578    228     13    727       N  
ATOM   6185  C4    A C   3      72.488  56.909  55.635  1.00 77.06           C  
ANISOU 6185  C4    A C   3     9711   8053  11516    309    -73    521       C  
ATOM   6186  P     U C   4      76.126  54.838  50.937  1.00 96.07           P  
ANISOU 6186  P     U C   4    11772  12130  12598    460     62   -274       P  
ATOM   6187  OP1   U C   4      77.219  55.028  49.947  1.00 93.15           O  
ANISOU 6187  OP1   U C   4    11313  12246  11836    445    140   -296       O  
ATOM   6188  OP2   U C   4      75.279  53.616  50.897  1.00 97.55           O  
ANISOU 6188  OP2   U C   4    11938  12138  12987    585    -56   -589       O  
ATOM   6189  O5'   U C   4      76.714  54.938  52.412  1.00 98.42           O  
ANISOU 6189  O5'   U C   4    12109  12116  13169    447    179   -182       O  
ATOM   6190  C5'   U C   4      78.111  54.836  52.644  1.00107.18           C  
ANISOU 6190  C5'   U C   4    13158  13396  14171    458    321   -235       C  
ATOM   6191  C4'   U C   4      78.749  56.195  52.790  1.00109.48           C  
ANISOU 6191  C4'   U C   4    13462  13790  14344    305    419     84       C  
ATOM   6192  O4'   U C   4      78.539  56.685  54.145  1.00106.62           O  
ANISOU 6192  O4'   U C   4    13161  13062  14287    268    450    243       O  
ATOM   6193  C3'   U C   4      80.257  56.219  52.566  1.00109.92           C  
ANISOU 6193  C3'   U C   4    13424  14168  14173    291    561     34       C  
ATOM   6194  O3'   U C   4      80.623  57.487  52.028  1.00 96.53           O  
ANISOU 6194  O3'   U C   4    11715  12686  12274    131    617    332       O  
ATOM   6195  C2'   U C   4      80.800  56.089  53.981  1.00111.24           C  
ANISOU 6195  C2'   U C   4    13596  14072  14597    323    650     18       C  
ATOM   6196  O2'   U C   4      82.121  56.555  54.149  1.00121.06           O  
ANISOU 6196  O2'   U C   4    14767  15520  15710    262    792     71       O  
ATOM   6197  C1'   U C   4      79.792  56.925  54.761  1.00103.09           C  
ANISOU 6197  C1'   U C   4    12659  12688  13821    245    591    261       C  
ATOM   6198  N1    U C   4      79.690  56.571  56.184  1.00 90.08           N  
ANISOU 6198  N1    U C   4    11030  10714  12483    324    615    219       N  
ATOM   6199  C2    U C   4      80.259  57.440  57.094  1.00 84.25           C  
ANISOU 6199  C2    U C   4    10276   9902  11833    251    702    373       C  
ATOM   6200  O2    U C   4      80.831  58.467  56.770  1.00 88.25           O  
ANISOU 6200  O2    U C   4    10756  10564  12210    113    760    539       O  
ATOM   6201  N3    U C   4      80.137  57.062  58.405  1.00 76.01           N  
ANISOU 6201  N3    U C   4     9230   8605  11044    350    720    326       N  
ATOM   6202  C4    U C   4      79.516  55.932  58.890  1.00 72.13           C  
ANISOU 6202  C4    U C   4     8754   7912  10739    503    671    182       C  
ATOM   6203  O4    U C   4      79.494  55.740  60.107  1.00 66.74           O  
ANISOU 6203  O4    U C   4     8054   7042  10262    586    706    193       O  
ATOM   6204  C5    U C   4      78.952  55.080  57.886  1.00 74.21           C  
ANISOU 6204  C5    U C   4     9037   8223  10938    554    584     30       C  
ATOM   6205  C6    U C   4      79.057  55.423  56.598  1.00 83.79           C  
ANISOU 6205  C6    U C   4    10248   9703  11886    469    554     34       C  
ATOM   6206  P     A C   5      80.971  57.613  50.467  1.00 89.35           P  
ANISOU 6206  P     A C   5    10721  12285  10941    108    621    347       P  
ATOM   6207  OP1   A C   5      79.747  58.062  49.754  1.00 93.83           O  
ANISOU 6207  OP1   A C   5    11344  12851  11455     77    491    505       O  
ATOM   6208  OP2   A C   5      81.626  56.338  50.070  1.00 91.15           O  
ANISOU 6208  OP2   A C   5    10857  12754  11023    259    636    -33       O  
ATOM   6209  O5'   A C   5      82.056  58.778  50.403  1.00 93.10           O  
ANISOU 6209  O5'   A C   5    11139  12956  11278    -56    770    637       O  
ATOM   6210  C5'   A C   5      81.671  60.145  50.431  1.00101.71           C  
ANISOU 6210  C5'   A C   5    12277  13927  12440   -220    774   1028       C  
ATOM   6211  C4'   A C   5      82.799  61.021  50.913  1.00112.40           C  
ANISOU 6211  C4'   A C   5    13571  15301  13836   -361    927   1212       C  
ATOM   6212  O4'   A C   5      83.492  60.347  51.995  1.00114.44           O  
ANISOU 6212  O4'   A C   5    13807  15412  14262   -283    990    960       O  
ATOM   6213  C3'   A C   5      83.900  61.318  49.904  1.00119.07           C  
ANISOU 6213  C3'   A C   5    14283  16631  14327   -433   1047   1310       C  
ATOM   6214  O3'   A C   5      83.577  62.364  49.002  1.00120.30           O  
ANISOU 6214  O3'   A C   5    14427  16946  14337   -559   1045   1681       O  
ATOM   6215  C2'   A C   5      85.093  61.620  50.801  1.00113.38           C  
ANISOU 6215  C2'   A C   5    13494  15845  13739   -509   1191   1297       C  
ATOM   6216  O2'   A C   5      84.991  62.922  51.361  1.00104.04           O  
ANISOU 6216  O2'   A C   5    12334  14391  12804   -682   1222   1612       O  
ATOM   6217  C1'   A C   5      84.877  60.609  51.919  1.00109.11           C  
ANISOU 6217  C1'   A C   5    13014  15003  13440   -352   1142    975       C  
ATOM   6218  N9    A C   5      85.583  59.332  51.687  1.00 99.97           N  
ANISOU 6218  N9    A C   5    11784  14099  12102   -193   1174    622       N  
ATOM   6219  C8    A C   5      85.057  58.122  51.290  1.00 91.22           C  
ANISOU 6219  C8    A C   5    10696  13036  10928    -18   1074    335       C  
ATOM   6220  N7    A C   5      85.945  57.161  51.201  1.00 89.18           N  
ANISOU 6220  N7    A C   5    10349  12994  10541    104   1130     41       N  
ATOM   6221  C5    A C   5      87.130  57.781  51.573  1.00 87.28           C  
ANISOU 6221  C5    A C   5    10026  12876  10260      3   1278    147       C  
ATOM   6222  C6    A C   5      88.443  57.307  51.689  1.00 80.62           C  
ANISOU 6222  C6    A C   5     9063  12281   9287     58   1396    -44       C  
ATOM   6223  N6    A C   5      88.788  56.044  51.430  1.00 82.82           N  
ANISOU 6223  N6    A C   5     9289  12722   9458    245   1379   -394       N  
ATOM   6224  N1    A C   5      89.394  58.185  52.080  1.00 78.76           N  
ANISOU 6224  N1    A C   5     8753  12116   9056    -84   1528    125       N  
ATOM   6225  C2    A C   5      89.040  59.450  52.339  1.00 87.23           C  
ANISOU 6225  C2    A C   5     9866  12997  10279   -269   1538    458       C  
ATOM   6226  N3    A C   5      87.839  60.015  52.268  1.00 85.73           N  
ANISOU 6226  N3    A C   5     9791  12554  10228   -331   1433    667       N  
ATOM   6227  C4    A C   5      86.922  59.115  51.874  1.00 88.61           C  
ANISOU 6227  C4    A C   5    10230  12880  10557   -186   1306    498       C  
ATOM   6228  P     A C   6      83.555  62.089  47.417  1.00114.81           P  
ANISOU 6228  P     A C   6    13645  16796  13181   -504   1025   1703       P  
ATOM   6229  OP1   A C   6      83.051  63.331  46.779  1.00116.93           O  
ANISOU 6229  OP1   A C   6    13922  17108  13398   -637   1017   2162       O  
ATOM   6230  OP2   A C   6      82.889  60.785  47.155  1.00106.64           O  
ANISOU 6230  OP2   A C   6    12639  15811  12069   -303    893   1316       O  
ATOM   6231  O5'   A C   6      85.089  61.918  47.028  1.00117.25           O  
ANISOU 6231  O5'   A C   6    13793  17539  13218   -529   1191   1634       O  
ATOM   6232  C5'   A C   6      85.906  63.049  46.772  1.00119.72           C  
ANISOU 6232  C5'   A C   6    14012  18011  13464   -716   1337   2000       C  
ATOM   6233  C4'   A C   6      87.149  63.028  47.623  1.00120.22           C  
ANISOU 6233  C4'   A C   6    14003  18015  13659   -775   1476   1880       C  
ATOM   6234  O4'   A C   6      87.044  61.973  48.610  1.00121.39           O  
ANISOU 6234  O4'   A C   6    14223  17893  14008   -623   1416   1476       O  
ATOM   6235  C3'   A C   6      88.449  62.723  46.902  1.00119.18           C  
ANISOU 6235  C3'   A C   6    13694  18422  13166   -772   1615   1801       C  
ATOM   6236  O3'   A C   6      88.984  63.853  46.240  1.00121.91           O  
ANISOU 6236  O3'   A C   6    13929  19012  13380   -960   1739   2222       O  
ATOM   6237  C2'   A C   6      89.334  62.197  48.026  1.00117.57           C  
ANISOU 6237  C2'   A C   6    13467  18048  13155   -734   1685   1503       C  
ATOM   6238  O2'   A C   6      89.843  63.272  48.803  1.00110.97           O  
ANISOU 6238  O2'   A C   6    12605  16964  12594   -926   1786   1740       O  
ATOM   6239  C1'   A C   6      88.320  61.429  48.875  1.00120.48           C  
ANISOU 6239  C1'   A C   6    13995  17983  13798   -584   1535   1243       C  
ATOM   6240  N9    A C   6      88.293  59.981  48.571  1.00119.98           N  
ANISOU 6240  N9    A C   6    13920  18101  13565   -361   1468    824       N  
ATOM   6241  C8    A C   6      87.263  59.263  48.011  1.00112.88           C  
ANISOU 6241  C8    A C   6    13085  17214  12590   -223   1320    668       C  
ATOM   6242  N7    A C   6      87.519  57.984  47.869  1.00108.81           N  
ANISOU 6242  N7    A C   6    12526  16844  11973    -36   1286    262       N  
ATOM   6243  C5    A C   6      88.805  57.838  48.373  1.00109.71           C  
ANISOU 6243  C5    A C   6    12548  17059  12078    -42   1423    155       C  
ATOM   6244  C6    A C   6      89.658  56.721  48.509  1.00103.50           C  
ANISOU 6244  C6    A C   6    11676  16435  11215    119   1461   -227       C  
ATOM   6245  N6    A C   6      89.336  55.480  48.136  1.00 95.15           N  
ANISOU 6245  N6    A C   6    10608  15444  10098    320   1361   -595       N  
ATOM   6246  N1    A C   6      90.880  56.921  49.054  1.00111.32           N  
ANISOU 6246  N1    A C   6    12578  17510  12209     69   1605   -232       N  
ATOM   6247  C2    A C   6      91.214  58.160  49.434  1.00118.49           C  
ANISOU 6247  C2    A C   6    13477  18334  13210   -138   1702    109       C  
ATOM   6248  N3    A C   6      90.502  59.284  49.361  1.00121.85           N  
ANISOU 6248  N3    A C   6    13974  18581  13744   -307   1678    478       N  
ATOM   6249  C4    A C   6      89.292  59.059  48.814  1.00117.17           C  
ANISOU 6249  C4    A C   6    13476  17917  13126   -244   1535    492       C  
ATOM   6250  P     C C   7      89.665  63.688  44.796  1.00133.94           P  
ANISOU 6250  P     C C   7    15274  21243  14374   -934   1826   2296       P  
ATOM   6251  OP1   C C   7      90.068  65.040  44.328  1.00136.17           O  
ANISOU 6251  OP1   C C   7    15458  21647  14635  -1159   1957   2823       O  
ATOM   6252  OP2   C C   7      88.747  62.879  43.949  1.00130.15           O  
ANISOU 6252  OP2   C C   7    14832  20993  13626   -742   1677   2113       O  
ATOM   6253  O5'   C C   7      90.988  62.845  45.097  1.00137.28           O  
ANISOU 6253  O5'   C C   7    15576  21907  14678   -863   1933   1923       O  
ATOM   6254  C5'   C C   7      91.987  63.337  45.984  1.00130.19           C  
ANISOU 6254  C5'   C C   7    14619  20835  14014  -1003   2069   1964       C  
ATOM   6255  C4'   C C   7      93.004  62.275  46.333  1.00122.25           C  
ANISOU 6255  C4'   C C   7    13528  20022  12899   -868   2124   1526       C  
ATOM   6256  O4'   C C   7      92.363  61.197  47.063  1.00123.11           O  
ANISOU 6256  O4'   C C   7    13776  19812  13189   -668   1985   1133       O  
ATOM   6257  C3'   C C   7      93.671  61.585  45.154  1.00119.60           C  
ANISOU 6257  C3'   C C   7    13030  20346  12065   -755   2175   1369       C  
ATOM   6258  O3'   C C   7      94.748  62.336  44.619  1.00121.83           O  
ANISOU 6258  O3'   C C   7    13124  21021  12147   -920   2356   1642       O  
ATOM   6259  C2'   C C   7      94.094  60.242  45.740  1.00121.58           C  
ANISOU 6259  C2'   C C   7    13286  20569  12338   -543   2138    835       C  
ATOM   6260  O2'   C C   7      95.303  60.373  46.475  1.00122.52           O  
ANISOU 6260  O2'   C C   7    13307  20684  12559   -612   2277    766       O  
ATOM   6261  C1'   C C   7      92.953  59.959  46.721  1.00122.30           C  
ANISOU 6261  C1'   C C   7    13590  20051  12829   -472   1986    724       C  
ATOM   6262  N1    C C   7      91.905  59.074  46.149  1.00119.18           N  
ANISOU 6262  N1    C C   7    13275  19682  12326   -286   1819    506       N  
ATOM   6263  C2    C C   7      92.108  57.687  46.070  1.00117.87           C  
ANISOU 6263  C2    C C   7    13075  19650  12059    -55   1761     30       C  
ATOM   6264  O2    C C   7      93.175  57.198  46.468  1.00123.18           O  
ANISOU 6264  O2    C C   7    13658  20436  12711      3   1851   -194       O  
ATOM   6265  N3    C C   7      91.137  56.895  45.556  1.00109.74           N  
ANISOU 6265  N3    C C   7    12102  18621  10974    105   1603   -189       N  
ATOM   6266  C4    C C   7      89.990  57.424  45.132  1.00106.49           C  
ANISOU 6266  C4    C C   7    11780  18106  10576     50   1504     47       C  
ATOM   6267  N4    C C   7      89.064  56.601  44.633  1.00105.50           N  
ANISOU 6267  N4    C C   7    11690  17995  10399    211   1345   -208       N  
ATOM   6268  C5    C C   7      89.749  58.827  45.204  1.00111.94           C  
ANISOU 6268  C5    C C   7    12515  18665  11352   -171   1559    545       C  
ATOM   6269  C6    C C   7      90.718  59.600  45.714  1.00116.20           C  
ANISOU 6269  C6    C C   7    12996  19180  11976   -333   1714    755       C  
ATOM   6270  P     U C   8      94.856  62.589  43.034  1.00125.97           P  
ANISOU 6270  P     U C   8    13493  22202  12169   -931   2409   1897       P  
ATOM   6271  OP1   U C   8      95.951  63.566  42.804  1.00127.11           O  
ANISOU 6271  OP1   U C   8    13453  22594  12248  -1153   2615   2256       O  
ATOM   6272  OP2   U C   8      93.495  62.890  42.518  1.00128.39           O  
ANISOU 6272  OP2   U C   8    13923  22390  12469   -907   2271   2117       O  
ATOM   6273  O5'   U C   8      95.305  61.175  42.452  1.00121.86           O  
ANISOU 6273  O5'   U C   8    12873  22168  11259   -673   2374   1392       O  
ATOM   6274  C5'   U C   8      96.384  60.458  43.040  1.00117.50           C  
ANISOU 6274  C5'   U C   8    12242  21678  10726   -598   2445   1021       C  
ATOM   6275  C4'   U C   8      96.328  58.983  42.727  1.00115.13           C  
ANISOU 6275  C4'   U C   8    11926  21601  10216   -311   2335    479       C  
ATOM   6276  O4'   U C   8      95.026  58.447  43.096  1.00116.03           O  
ANISOU 6276  O4'   U C   8    12241  21270  10573   -187   2142    306       O  
ATOM   6277  C3'   U C   8      96.546  58.617  41.261  1.00120.93           C  
ANISOU 6277  C3'   U C   8    12478  23070  10400   -197   2343    413       C  
ATOM   6278  O3'   U C   8      97.315  57.423  41.196  1.00114.36           O  
ANISOU 6278  O3'   U C   8    11537  22523   9394     12   2341    -99       O  
ATOM   6279  C2'   U C   8      95.132  58.356  40.751  1.00125.31           C  
ANISOU 6279  C2'   U C   8    13154  23532  10927    -85   2155    385       C  
ATOM   6280  O2'   U C   8      95.061  57.476  39.648  1.00117.38           O  
ANISOU 6280  O2'   U C   8    12021  23082   9498    131   2078     66       O  
ATOM   6281  C1'   U C   8      94.456  57.772  41.989  1.00129.61           C  
ANISOU 6281  C1'   U C   8    13915  23373  11959    -13   2028    116       C  
ATOM   6282  N1    U C   8      92.997  57.973  42.013  1.00141.06           N  
ANISOU 6282  N1    U C   8    15540  24458  13597    -11   1870    244       N  
ATOM   6283  C2    U C   8      92.190  56.855  42.101  1.00140.89           C  
ANISOU 6283  C2    U C   8    15605  24250  13676    197   1696   -174       C  
ATOM   6284  O2    U C   8      92.642  55.726  42.178  1.00141.55           O  
ANISOU 6284  O2    U C   8    15629  24429  13723    379   1668   -633       O  
ATOM   6285  N3    U C   8      90.837  57.108  42.105  1.00139.34           N  
ANISOU 6285  N3    U C   8    15559  23736  13649    184   1556    -35       N  
ATOM   6286  C4    U C   8      90.214  58.340  42.022  1.00138.32           C  
ANISOU 6286  C4    U C   8    15505  23461  13589      1   1567    469       C  
ATOM   6287  O4    U C   8      88.980  58.411  42.041  1.00132.22           O  
ANISOU 6287  O4    U C   8    14862  22409  12966     23   1426    526       O  
ATOM   6288  C5    U C   8      91.118  59.444  41.929  1.00143.13           C  
ANISOU 6288  C5    U C   8    16019  24259  14107   -204   1751    885       C  
ATOM   6289  C6    U C   8      92.439  59.228  41.922  1.00146.98           C  
ANISOU 6289  C6    U C   8    16355  25059  14433   -209   1894    762       C  
ATOM   6290  P     U C   9      98.893  57.506  41.455  1.00110.66           P  
ANISOU 6290  P     U C   9    10886  22334   8826    -54   2533   -145       P  
ATOM   6291  OP1   U C   9      99.278  58.933  41.307  1.00109.55           O  
ANISOU 6291  OP1   U C   9    10671  22277   8675   -342   2696    426       O  
ATOM   6292  OP2   U C   9      99.546  56.486  40.596  1.00105.45           O  
ANISOU 6292  OP2   U C   9    10037  22293   7737    168   2531   -555       O  
ATOM   6293  O5'   U C   9      99.055  57.139  43.002  1.00114.83           O  
ANISOU 6293  O5'   U C   9    11558  22230   9843    -34   2513   -371       O  
ATOM   6294  C5'   U C   9      98.523  55.936  43.534  1.00 96.30           C  
ANISOU 6294  C5'   U C   9     9335  19559   7695    199   2359   -821       C  
ATOM   6295  C4'   U C   9      99.365  55.404  44.669  1.00 94.20           C  
ANISOU 6295  C4'   U C   9     9067  19055   7670    269   2412  -1091       C  
ATOM   6296  O4'   U C   9     100.753  55.295  44.265  1.00 96.68           O  
ANISOU 6296  O4'   U C   9     9153  19909   7671    280   2559  -1201       O  
ATOM   6297  C3'   U C   9      99.426  56.252  45.924  1.00 91.40           C  
ANISOU 6297  C3'   U C   9     8813  18194   7719     84   2476   -832       C  
ATOM   6298  O3'   U C   9      98.272  56.119  46.732  1.00 91.51           O  
ANISOU 6298  O3'   U C   9     9046  17607   8117    120   2339   -833       O  
ATOM   6299  C2'   U C   9     100.697  55.747  46.600  1.00 91.05           C  
ANISOU 6299  C2'   U C   9     8653  18245   7696    165   2576  -1106       C  
ATOM   6300  O2'   U C   9     100.456  54.535  47.299  1.00 92.16           O  
ANISOU 6300  O2'   U C   9     8886  18088   8042    412   2467  -1507       O  
ATOM   6301  C1'   U C   9     101.591  55.452  45.393  1.00 94.85           C  
ANISOU 6301  C1'   U C   9     8908  19442   7686    222   2658  -1227       C  
ATOM   6302  N1    U C   9     102.566  56.546  45.162  1.00 96.83           N  
ANISOU 6302  N1    U C   9     8991  20014   7787    -18   2848   -894       N  
ATOM   6303  C2    U C   9     103.824  56.413  45.735  1.00 96.88           C  
ANISOU 6303  C2    U C   9     8860  20149   7801    -14   2971  -1054       C  
ATOM   6304  O2    U C   9     104.167  55.441  46.383  1.00 95.45           O  
ANISOU 6304  O2    U C   9     8693  19852   7722    191   2930  -1442       O  
ATOM   6305  N3    U C   9     104.689  57.455  45.515  1.00 98.89           N  
ANISOU 6305  N3    U C   9     8945  20680   7948   -255   3149   -738       N  
ATOM   6306  C4    U C   9     104.432  58.605  44.807  1.00100.90           C  
ANISOU 6306  C4    U C   9     9157  21071   8110   -497   3220   -258       C  
ATOM   6307  O4    U C   9     105.315  59.455  44.703  1.00102.81           O  
ANISOU 6307  O4    U C   9     9249  21484   8329   -704   3363     -2       O  
ATOM   6308  C5    U C   9     103.113  58.675  44.255  1.00100.70           C  
ANISOU 6308  C5    U C   9     9287  20903   8073   -472   3084   -102       C  
ATOM   6309  C6    U C   9     102.244  57.675  44.450  1.00 98.67           C  
ANISOU 6309  C6    U C   9     9194  20391   7905   -242   2905   -427       C  
ATOM   6310  P     A C  10      97.241  57.341  46.878  1.00 88.57           P  
ANISOU 6310  P     A C  10     8813  16876   7961    -99   2305   -373       P  
ATOM   6311  OP1   A C  10      95.889  56.799  46.594  1.00100.81           O  
ANISOU 6311  OP1   A C  10    10514  18217   9573     27   2124   -467       O  
ATOM   6312  OP2   A C  10      97.759  58.489  46.089  1.00 90.02           O  
ANISOU 6312  OP2   A C  10     8861  17431   7911   -323   2440     24       O  
ATOM   6313  O5'   A C  10      97.294  57.707  48.426  1.00 83.88           O  
ANISOU 6313  O5'   A C  10     8318  15732   7821   -169   2326   -329       O  
ATOM   6314  C5'   A C  10      98.519  58.060  49.048  1.00 83.94           C  
ANISOU 6314  C5'   A C  10     8198  15821   7873   -254   2473   -333       C  
ATOM   6315  C4'   A C  10      99.174  56.875  49.713  1.00 82.82           C  
ANISOU 6315  C4'   A C  10     8022  15681   7765    -25   2470   -763       C  
ATOM   6316  O4'   A C  10     100.606  56.970  49.530  1.00 92.36           O  
ANISOU 6316  O4'   A C  10     9022  17319   8753    -65   2626   -831       O  
ATOM   6317  C3'   A C  10      98.981  56.770  51.219  1.00 85.11           C  
ANISOU 6317  C3'   A C  10     8417  15461   8461     27   2437   -841       C  
ATOM   6318  O3'   A C  10      97.762  56.115  51.560  1.00 84.06           O  
ANISOU 6318  O3'   A C  10     8465  14937   8538    171   2280   -939       O  
ATOM   6319  C2'   A C  10     100.246  56.047  51.677  1.00 79.81           C  
ANISOU 6319  C2'   A C  10     7606  15007   7712    170   2525  -1151       C  
ATOM   6320  O2'   A C  10     100.140  54.651  51.437  1.00 79.95           O  
ANISOU 6320  O2'   A C  10     7642  15093   7642    443   2441  -1511       O  
ATOM   6321  C1'   A C  10     101.280  56.599  50.704  1.00 83.00           C  
ANISOU 6321  C1'   A C  10     7811  15957   7769     25   2665  -1044       C  
ATOM   6322  N9    A C  10     102.020  57.789  51.178  1.00 83.32           N  
ANISOU 6322  N9    A C  10     7743  15999   7914   -217   2802   -799       N  
ATOM   6323  C8    A C  10     101.729  59.107  50.916  1.00 84.12           C  
ANISOU 6323  C8    A C  10     7843  16024   8095   -491   2848   -394       C  
ATOM   6324  N7    A C  10     102.594  59.955  51.414  1.00 84.64           N  
ANISOU 6324  N7    A C  10     7775  16110   8275   -672   2975   -276       N  
ATOM   6325  C5    A C  10     103.534  59.140  52.031  1.00 84.11           C  
ANISOU 6325  C5    A C  10     7613  16177   8166   -499   3016   -629       C  
ATOM   6326  C6    A C  10     104.711  59.423  52.746  1.00 84.37           C  
ANISOU 6326  C6    A C  10     7477  16314   8266   -556   3137   -727       C  
ATOM   6327  N6    A C  10     105.164  60.658  52.969  1.00 85.35           N  
ANISOU 6327  N6    A C  10     7485  16400   8543   -826   3242   -481       N  
ATOM   6328  N1    A C  10     105.418  58.380  53.227  1.00 83.80           N  
ANISOU 6328  N1    A C  10     7345  16383   8113   -319   3143  -1097       N  
ATOM   6329  C2    A C  10     104.968  57.139  53.007  1.00 83.09           C  
ANISOU 6329  C2    A C  10     7360  16295   7916    -51   3037  -1347       C  
ATOM   6330  N3    A C  10     103.880  56.746  52.354  1.00 94.45           N  
ANISOU 6330  N3    A C  10     8952  17627   9308     19   2918  -1307       N  
ATOM   6331  C4    A C  10     103.199  57.806  51.884  1.00 85.95           C  
ANISOU 6331  C4    A C  10     7932  16445   8281   -215   2913   -941       C  
ATOM   6332  P     A C  11      97.256  56.010  53.083  1.00 81.10           P  
ANISOU 6332  P     A C  11     8215  14015   8584    237   2225   -967       P  
ATOM   6333  OP1   A C  11      95.860  55.512  53.081  1.00 80.12           O  
ANISOU 6333  OP1   A C  11     8264  13554   8625    334   2068   -985       O  
ATOM   6334  OP2   A C  11      97.547  57.286  53.790  1.00 78.91           O  
ANISOU 6334  OP2   A C  11     7906  13593   8482     20   2308   -706       O  
ATOM   6335  O5'   A C  11      98.157  54.845  53.676  1.00 78.37           O  
ANISOU 6335  O5'   A C  11     7787  13759   8230    476   2261  -1332       O  
ATOM   6336  C5'   A C  11      98.173  54.577  55.062  1.00 75.97           C  
ANISOU 6336  C5'   A C  11     7523  13124   8219    584   2255  -1409       C  
ATOM   6337  C4'   A C  11      99.562  54.260  55.544  1.00 75.10           C  
ANISOU 6337  C4'   A C  11     7251  13265   8020    674   2371  -1604       C  
ATOM   6338  O4'   A C  11     100.553  54.894  54.694  1.00 79.15           O  
ANISOU 6338  O4'   A C  11     7604  14232   8238    511   2489  -1543       O  
ATOM   6339  C3'   A C  11      99.874  54.780  56.929  1.00 71.97           C  
ANISOU 6339  C3'   A C  11     6827  12653   7864    649   2421  -1544       C  
ATOM   6340  O3'   A C  11      99.366  53.944  57.941  1.00 68.24           O  
ANISOU 6340  O3'   A C  11     6442  11855   7632    871   2348  -1662       O  
ATOM   6341  C2'   A C  11     101.390  54.908  56.916  1.00 72.32           C  
ANISOU 6341  C2'   A C  11     6667  13101   7712    629   2561  -1666       C  
ATOM   6342  O2'   A C  11     102.011  53.647  57.113  1.00 78.68           O  
ANISOU 6342  O2'   A C  11     7413  14042   8441    902   2567  -1977       O  
ATOM   6343  C1'   A C  11     101.631  55.365  55.479  1.00 80.15           C  
ANISOU 6343  C1'   A C  11     7592  14456   8403    455   2608  -1558       C  
ATOM   6344  N9    A C  11     101.652  56.834  55.380  1.00 85.93           N  
ANISOU 6344  N9    A C  11     8286  15176   9188    150   2673  -1239       N  
ATOM   6345  C8    A C  11     100.647  57.634  54.896  1.00 74.89           C  
ANISOU 6345  C8    A C  11     7000  13592   7864    -29   2615   -944       C  
ATOM   6346  N7    A C  11     100.935  58.910  54.930  1.00 75.68           N  
ANISOU 6346  N7    A C  11     7024  13693   8040   -287   2695   -688       N  
ATOM   6347  C5    A C  11     102.210  58.947  55.473  1.00 76.27           C  
ANISOU 6347  C5    A C  11     6919  13974   8085   -284   2813   -840       C  
ATOM   6348  C6    A C  11     103.066  60.012  55.764  1.00 77.40           C  
ANISOU 6348  C6    A C  11     6896  14206   8306   -503   2934   -721       C  
ATOM   6349  N6    A C  11     102.730  61.278  55.528  1.00 78.21           N  
ANISOU 6349  N6    A C  11     6995  14167   8556   -775   2957   -393       N  
ATOM   6350  N1    A C  11     104.274  59.730  56.300  1.00 77.86           N  
ANISOU 6350  N1    A C  11     6783  14495   8305   -432   3028   -953       N  
ATOM   6351  C2    A C  11     104.589  58.449  56.527  1.00 77.21           C  
ANISOU 6351  C2    A C  11     6705  14538   8091   -146   3001  -1266       C  
ATOM   6352  N3    A C  11     103.865  57.356  56.298  1.00 91.32           N  
ANISOU 6352  N3    A C  11     8642  16233   9822     80   2891  -1398       N  
ATOM   6353  C4    A C  11     102.671  57.678  55.761  1.00 95.32           C  
ANISOU 6353  C4    A C  11     9310  16516  10391    -10   2800  -1177       C  
ATOM   6354  P     U C  12      98.409  54.578  59.054  1.00 81.72           P  
ANISOU 6354  P     U C  12     8262  13123   9667    816   2289  -1465       P  
ATOM   6355  OP1   U C  12      97.319  53.605  59.330  1.00 94.17           O  
ANISOU 6355  OP1   U C  12     9983  14371  11426   1007   2171  -1518       O  
ATOM   6356  OP2   U C  12      98.034  55.942  58.587  1.00 66.11           O  
ANISOU 6356  OP2   U C  12     6307  11116   7694    524   2295  -1189       O  
ATOM   6357  O5'   U C  12      99.371  54.677  60.323  1.00 82.71           O  
ANISOU 6357  O5'   U C  12     8253  13299   9873    900   2376  -1561       O  
ATOM   6358  C5'   U C  12     100.671  54.090  60.280  1.00 70.24           C  
ANISOU 6358  C5'   U C  12     6518  12068   8104   1024   2468  -1787       C  
ATOM   6359  C4'   U C  12     101.205  53.765  61.650  1.00 79.78           C  
ANISOU 6359  C4'   U C  12     7641  13234   9437   1212   2505  -1902       C  
ATOM   6360  O4'   U C  12     102.345  54.618  61.948  1.00 84.80           O  
ANISOU 6360  O4'   U C  12     8093  14140   9986   1081   2617  -1927       O  
ATOM   6361  C3'   U C  12     100.223  53.937  62.807  1.00 90.53           C  
ANISOU 6361  C3'   U C  12     9100  14206  11090   1270   2432  -1776       C  
ATOM   6362  O3'   U C  12     100.426  52.890  63.754  1.00103.06           O  
ANISOU 6362  O3'   U C  12    10656  15744  12756   1572   2431  -1913       O  
ATOM   6363  C2'   U C  12     100.657  55.261  63.429  1.00 89.32           C  
ANISOU 6363  C2'   U C  12     8835  14105  10998   1076   2490  -1688       C  
ATOM   6364  O2'   U C  12     100.319  55.394  64.792  1.00100.55           O  
ANISOU 6364  O2'   U C  12    10245  15331  12630   1188   2462  -1670       O  
ATOM   6365  C1'   U C  12     102.168  55.213  63.216  1.00 79.48           C  
ANISOU 6365  C1'   U C  12     7391  13279   9529   1080   2610  -1867       C  
ATOM   6366  N1    U C  12     102.842  56.525  63.219  1.00 72.76           N  
ANISOU 6366  N1    U C  12     6396  12581   8668    817   2690  -1803       N  
ATOM   6367  C2    U C  12     104.177  56.593  63.602  1.00 77.67           C  
ANISOU 6367  C2    U C  12     6807  13525   9178    849   2794  -1979       C  
ATOM   6368  O2    U C  12     104.845  55.624  63.925  1.00 85.77           O  
ANISOU 6368  O2    U C  12     7898  14556  10135   1056   2723  -2076       O  
ATOM   6369  N3    U C  12     104.728  57.851  63.576  1.00 68.11           N  
ANISOU 6369  N3    U C  12     5453  12419   8005    580   2865  -1914       N  
ATOM   6370  C4    U C  12     104.103  59.032  63.231  1.00 68.20           C  
ANISOU 6370  C4    U C  12     5516  12228   8169    294   2843  -1679       C  
ATOM   6371  O4    U C  12     104.735  60.094  63.260  1.00 69.53           O  
ANISOU 6371  O4    U C  12     5527  12491   8399     66   2917  -1643       O  
ATOM   6372  C5    U C  12     102.732  58.881  62.855  1.00 66.88           C  
ANISOU 6372  C5    U C  12     5578  11741   8093    294   2732  -1499       C  
ATOM   6373  C6    U C  12     102.168  57.668  62.862  1.00 66.53           C  
ANISOU 6373  C6    U C  12     5670  11607   8001    544   2661  -1573       C  
TER    6374        U C  12                                                      
HETATM 6375  S   SO4 A 501      62.513  69.039  45.759  1.00120.31           S  
HETATM 6376  O1  SO4 A 501      63.808  69.597  45.372  1.00113.63           O  
HETATM 6377  O2  SO4 A 501      61.926  68.313  44.635  1.00119.90           O  
HETATM 6378  O3  SO4 A 501      62.709  68.116  46.875  1.00131.51           O  
HETATM 6379  O4  SO4 A 501      61.612  70.117  46.165  1.00120.74           O  
HETATM 6380  S   SO4 A 502      68.783  63.820  83.541  1.00128.04           S  
HETATM 6381  O1  SO4 A 502      68.820  65.020  82.709  1.00124.93           O  
HETATM 6382  O2  SO4 A 502      68.753  62.619  82.710  1.00121.07           O  
HETATM 6383  O3  SO4 A 502      67.581  63.853  84.372  1.00136.16           O  
HETATM 6384  O4  SO4 A 502      69.973  63.791  84.390  1.00126.20           O  
HETATM 6385  S   SO4 A 503      56.377  82.877  56.957  1.00166.30           S  
HETATM 6386  O1  SO4 A 503      57.514  82.363  56.202  1.00162.75           O  
HETATM 6387  O2  SO4 A 503      55.292  83.190  56.032  1.00164.18           O  
HETATM 6388  O3  SO4 A 503      55.941  81.868  57.917  1.00167.03           O  
HETATM 6389  O4  SO4 A 503      56.763  84.084  57.680  1.00168.86           O  
HETATM 6390  S   SO4 B 501     124.244  48.212  35.807  1.00121.06           S  
HETATM 6391  O1  SO4 B 501     124.437  47.863  34.403  1.00119.55           O  
HETATM 6392  O2  SO4 B 501     122.821  48.421  36.068  1.00122.12           O  
HETATM 6393  O3  SO4 B 501     124.722  47.117  36.648  1.00120.23           O  
HETATM 6394  O4  SO4 B 501     124.991  49.433  36.102  1.00115.21           O  
HETATM 6395  S   SO4 B 502     126.841  74.472  56.921  1.00129.85           S  
HETATM 6396  O1  SO4 B 502     128.168  74.628  56.326  1.00117.26           O  
HETATM 6397  O2  SO4 B 502     126.080  73.506  56.137  1.00134.07           O  
HETATM 6398  O3  SO4 B 502     126.974  73.987  58.293  1.00133.47           O  
HETATM 6399  O4  SO4 B 502     126.127  75.749  56.927  1.00127.05           O  
HETATM 6400 MG    MG C 101      94.317  55.172  47.078  1.00 87.29          MG  
HETATM 6401  O   HOH A 601      84.549  45.911  68.997  1.00 72.58           O  
HETATM 6402  O   HOH A 602      39.953  75.913  55.335  1.00 73.17           O  
HETATM 6403  O   HOH A 603      43.489  79.645  44.678  1.00 77.14           O  
HETATM 6404  O   HOH A 604      55.721  66.823  40.496  1.00 78.48           O  
HETATM 6405  O   HOH A 605      30.739  85.356  20.572  1.00 59.56           O  
HETATM 6406  O   HOH A 606      48.171  57.472  61.669  1.00 69.45           O  
HETATM 6407  O   HOH A 607      45.411  81.533  49.520  1.00 64.14           O  
HETATM 6408  O   HOH A 608      18.237  62.491  37.121  1.00 76.51           O  
HETATM 6409  O   HOH A 609      82.870  68.671  52.081  1.00 69.81           O  
HETATM 6410  O   HOH A 610      49.214  60.758  72.904  1.00 67.18           O  
HETATM 6411  O   HOH A 611      83.712  53.861  52.160  1.00 85.30           O  
HETATM 6412  O   HOH A 612      99.585  67.033  54.936  1.00 48.06           O  
HETATM 6413  O   HOH A 613      97.131  49.469  73.375  1.00 55.83           O  
HETATM 6414  O   HOH A 614      99.139  64.155  68.842  1.00 58.42           O  
HETATM 6415  O   HOH A 615      53.839  73.620  38.743  1.00 69.50           O  
HETATM 6416  O   HOH A 616      72.110  80.793  46.368  1.00 65.43           O  
HETATM 6417  O   HOH A 617      71.257  81.338  64.707  1.00 58.54           O  
HETATM 6418  O   HOH A 618      42.537  84.003  40.013  1.00 68.84           O  
HETATM 6419  O   HOH B 601     104.006  70.556  22.684  1.00 53.53           O  
HETATM 6420  O   HOH B 602      95.543  53.548  42.503  1.00 65.65           O  
HETATM 6421  O   HOH B 603     106.855  46.514  64.182  1.00 57.20           O  
HETATM 6422  O   HOH B 604     103.413  51.531  79.911  1.00 54.66           O  
HETATM 6423  O   HOH B 605     129.856  62.087  69.575  1.00 64.75           O  
HETATM 6424  O   HOH C 201      69.396  52.459  55.445  1.00 64.68           O  
HETATM 6425  O   HOH C 202     103.871  63.393  51.177  1.00 64.32           O  
CONECT   85 1691                                                                
CONECT 1691   85                                                                
CONECT 3196 4727                                                                
CONECT 4727 3196                                                                
CONECT 6264 6400                                                                
CONECT 6311 6400                                                                
CONECT 6375 6376 6377 6378 6379                                                 
CONECT 6376 6375                                                                
CONECT 6377 6375                                                                
CONECT 6378 6375                                                                
CONECT 6379 6375                                                                
CONECT 6380 6381 6382 6383 6384                                                 
CONECT 6381 6380                                                                
CONECT 6382 6380                                                                
CONECT 6383 6380                                                                
CONECT 6384 6380                                                                
CONECT 6385 6386 6387 6388 6389                                                 
CONECT 6386 6385                                                                
CONECT 6387 6385                                                                
CONECT 6388 6385                                                                
CONECT 6389 6385                                                                
CONECT 6390 6391 6392 6393 6394                                                 
CONECT 6391 6390                                                                
CONECT 6392 6390                                                                
CONECT 6393 6390                                                                
CONECT 6394 6390                                                                
CONECT 6395 6396 6397 6398 6399                                                 
CONECT 6396 6395                                                                
CONECT 6397 6395                                                                
CONECT 6398 6395                                                                
CONECT 6399 6395                                                                
CONECT 6400 6264 6311                                                           
MASTER      419    0    6   58    0    0    7    6 6422    3   32   61          
END

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Related entries of code: 6ny5

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
No similar entries are found!
Complexes with the same small molecule ligand
PDB Code	Check Database	Ligand Name
No complexes with the same small molecule ligand are found!

Entry Information

PDB ID	6ny5
Complex Type	Protein-Nucleic Acid
PDBbind Subset	general set
Protein Name	PUM-HD domain of S. pombe Puf1
Ligand Name	dual UAAU RNA motifs
EC.Number	E.C.-.-.-.-
Resolution	3(Å)
Affinity (Kd/Ki/IC50)	Kd=50.1nM
Release Year	2019
Protein/NA Sequence	Check fasta file
Primary Reference	(2019) Nucleic Acids Res. Vol. 47: pp. 8770-8784

Links to External Databases

RCSB PDB	The mother database
PDBsum	Enhanced annotations on PDB entries
Pubchem	Comprehensive collection of chemical and biological data
UniProtKB AC	UniProt accession number (AC): O60059
Entrez Gene ID	NCBI Entrez Gene ID: 2540913
ASD	Information of known allosteric effects of PDB entries

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