CNRS Nantes University UFIP UFIP
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***  IMMUNE SYSTEM 10-OCT-19 6UMT  ***

elNémo ID: 210507044136130653

Job options:

ID        	=	 210507044136130653
JOBID     	=	 IMMUNE SYSTEM 10-OCT-19 6UMT
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    IMMUNE SYSTEM                           10-OCT-19   6UMT              
TITLE     HIGH-AFFINITY HUMAN PD-1 PD-L2 COMPLEX                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROGRAMMED CELL DEATH PROTEIN 1;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 33-150;                                       
COMPND   5 SYNONYM: HPD-1;                                                      
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PROGRAMMED CELL DEATH 1 LIGAND 2;                          
COMPND  10 CHAIN: B;                                                            
COMPND  11 SYNONYM: PROGRAMMED DEATH LIGAND 2,BUTYROPHILIN B7-DC,B7-DC;         
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PDCD1, PD1;                                                    
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F;                               
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: PDCD1LG2, B7DC, CD273, PDCD1L2, PDL2;                          
SOURCE  15 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  16 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  18 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F                                
KEYWDS    PD-1, PD-L2, IMMUNE CHECKPOINT, IMMUNE SYSTEM                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.TANG,P.S.KIM                                                        
REVDAT   2   18-DEC-19 6UMT    1       JRNL                                     
REVDAT   1   27-NOV-19 6UMT    0                                                
JRNL        AUTH   S.TANG,P.S.KIM                                               
JRNL        TITL   A HIGH-AFFINITY HUMAN PD-1/PD-L2 COMPLEX INFORMS AVENUES FOR 
JRNL        TITL 2 SMALL-MOLECULE IMMUNE CHECKPOINT DRUG DISCOVERY.             
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 116 24500 2019              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   31727844                                                     
JRNL        DOI    10.1073/PNAS.1916916116                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.99 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
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) : 1.99                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.51                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 17743                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.201                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1774                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 37.5080 -  4.6666    0.99     1343   149  0.1928 0.1928        
REMARK   3     2  4.6666 -  3.7051    1.00     1282   143  0.1528 0.1855        
REMARK   3     3  3.7051 -  3.2371    1.00     1261   139  0.1892 0.2142        
REMARK   3     4  3.2371 -  2.9412    1.00     1238   138  0.2030 0.2477        
REMARK   3     5  2.9412 -  2.7305    1.00     1244   139  0.2237 0.2390        
REMARK   3     6  2.7305 -  2.5695    1.00     1243   138  0.2136 0.2682        
REMARK   3     7  2.5695 -  2.4409    1.00     1230   136  0.2209 0.2560        
REMARK   3     8  2.4409 -  2.3346    1.00     1234   137  0.2075 0.2666        
REMARK   3     9  2.3346 -  2.2448    0.99     1221   136  0.2260 0.2638        
REMARK   3    10  2.2448 -  2.1673    1.00     1224   136  0.2341 0.2588        
REMARK   3    11  2.1673 -  2.0996    0.98     1200   133  0.2527 0.3290        
REMARK   3    12  2.0996 -  2.0395    0.95     1159   129  0.2655 0.3018        
REMARK   3    13  2.0395 -  1.9860    0.90     1090   121  0.2965 0.3448        
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)     : 0.230            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.580           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 35.84                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 50.76                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.014           1687                                  
REMARK   3   ANGLE     :  1.910           2298                                  
REMARK   3   CHIRALITY :  0.111            265                                  
REMARK   3   PLANARITY :  0.011            297                                  
REMARK   3   DIHEDRAL  : 12.800            613                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 6UMT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-OCT-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000244862.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-JUL-19                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL12-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : LIQUID NITROGEN-COOLED DOUBLE      
REMARK 200                                   CRYSTAL SI(111)                    
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17793                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.986                              
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     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 8.500                              
REMARK 200  R MERGE                    (I) : 0.14600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 5.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.76100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 3RRQ & 3BP5                              
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM MAGNESIUM ACETATE, 10% W/V        
REMARK 280  PEG8000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       20.64550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       44.85050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.89900            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       44.85050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       20.64550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.89900            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1860 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10860 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    14                                                      
REMARK 465     GLY A    15                                                      
REMARK 465     TRP A    16                                                      
REMARK 465     SER A    17                                                      
REMARK 465     CYS A    18                                                      
REMARK 465     ILE A    19                                                      
REMARK 465     ILE A    20                                                      
REMARK 465     LEU A    21                                                      
REMARK 465     PHE A    22                                                      
REMARK 465     LEU A    23                                                      
REMARK 465     VAL A    24                                                      
REMARK 465     ALA A    25                                                      
REMARK 465     THR A    26                                                      
REMARK 465     ALA A    27                                                      
REMARK 465     THR A    28                                                      
REMARK 465     GLY A    29                                                      
REMARK 465     VAL A    30                                                      
REMARK 465     HIS A    31                                                      
REMARK 465     SER A    32                                                      
REMARK 465     ASP A    85                                                      
REMARK 465     ARG A    86                                                      
REMARK 465     SER A    87                                                      
REMARK 465     GLN A    88                                                      
REMARK 465     PRO A    89                                                      
REMARK 465     GLY A    90                                                      
REMARK 465     GLN A    91                                                      
REMARK 465     ASP A    92                                                      
REMARK 465     GLU A   150                                                      
REMARK 465     PRO A   151                                                      
REMARK 465     GLU A   152                                                      
REMARK 465     ALA A   153                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ILE B     2                                                      
REMARK 465     PHE B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     LEU B     5                                                      
REMARK 465     LEU B     6                                                      
REMARK 465     MET B     7                                                      
REMARK 465     LEU B     8                                                      
REMARK 465     SER B     9                                                      
REMARK 465     LEU B    10                                                      
REMARK 465     GLU B    11                                                      
REMARK 465     LEU B    12                                                      
REMARK 465     GLN B    13                                                      
REMARK 465     LEU B    14                                                      
REMARK 465     HIS B    15                                                      
REMARK 465     GLN B    16                                                      
REMARK 465     ILE B    17                                                      
REMARK 465     ALA B    18                                                      
REMARK 465     ALA B    19                                                      
REMARK 465     ASP B    65                                                      
REMARK 465     THR B    66                                                      
REMARK 465     SER B    67                                                      
REMARK 465     SER B   122                                                      
REMARK 465     TYR B   123                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 131    CE   NZ                                             
REMARK 470     LYS A 135    CE   NZ                                             
REMARK 470     ARG A 148    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B  45    CG   OD1  OD2                                       
REMARK 470     SER B  48    OG                                                  
REMARK 470     HIS B  49    CG   ND1  CD2  CE1  NE2                             
REMARK 470     VAL B  50    CG1  CG2                                            
REMARK 470     ASN B  51    CG   OD1  ND2                                       
REMARK 470     LEU B  52    CG   CD1  CD2                                       
REMARK 470     GLU B  63    CG   CD   OE1  OE2                                  
REMARK 470     ASP B  64    CG   OD1  OD2                                       
REMARK 470     ARG B  70    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 118    CD   CE   NZ                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B   211     O    HOH B   244              1.47            
REMARK 500   O    HOH A   313     O    HOH A   316              1.63            
REMARK 500   O    HOH A   301     O    HOH A   354              2.00            
REMARK 500   ND1  HIS A   107     O    HOH A   301              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CB   SER A    60     OE2  GLU A   141     3445     1.68            
REMARK 500   OG   SER A    60     OE2  GLU A   141     3445     1.79            
REMARK 500   O    HOH A   358     O    HOH B   215     3555     2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU B  52   N   -  CA  -  C   ANGL. DEV. =  23.9 DEGREES          
REMARK 500    HIS B  69   N   -  CA  -  C   ANGL. DEV. =  17.8 DEGREES          
REMARK 500    ARG B  70   C   -  N   -  CA  ANGL. DEV. = -18.1 DEGREES          
REMARK 500    ARG B  70   N   -  CA  -  C   ANGL. DEV. = -22.6 DEGREES          
REMARK 500    GLU B  71   CA  -  C   -  N   ANGL. DEV. = -13.5 DEGREES          
REMARK 500    ARG B  72   C   -  N   -  CA  ANGL. DEV. =  15.9 DEGREES          
REMARK 500    ARG B  72   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG B  72   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG B  72   N   -  CA  -  C   ANGL. DEV. =  23.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 SER A   62     PHE A   63                 -108.27                    
REMARK 500 LEU B   52     GLY B   53                  115.70                    
REMARK 500 ARG B   70     GLU B   71                 -126.89                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    VAL B  50         10.79                                           
REMARK 500    GLU B  71         15.49                                           
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 A 373        DISTANCE =  5.99 ANGSTROMS                       
REMARK 525    HOH B 251        DISTANCE =  6.50 ANGSTROMS                       
REMARK 525    HOH B 252        DISTANCE =  8.39 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 A 201  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  46   OE1                                                    
REMARK 620 2 GLU A  46   OE2  58.4                                              
REMARK 620 3 GLU A 146   OE1  91.7  78.6                                        
REMARK 620 4 GLU A 146   OE2 129.4  75.6  57.2                                  
REMARK 620 5 ASP B  37   OD2  67.0 119.7  79.7 131.4                            
REMARK 620 6 HIS B  88   NE2  64.8 118.4  81.4 133.9   2.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 201                  
DBREF  6UMT A   33   150  UNP    Q15116   PDCD1_HUMAN     33    150             
DBREF  6UMT B    1   123  UNP    Q9BQ51   PD1L2_HUMAN      1    123             
SEQADV 6UMT MET A   14  UNP  Q15116              EXPRESSION TAG                 
SEQADV 6UMT GLY A   15  UNP  Q15116              EXPRESSION TAG                 
SEQADV 6UMT TRP A   16  UNP  Q15116              EXPRESSION TAG                 
SEQADV 6UMT SER A   17  UNP  Q15116              EXPRESSION TAG                 
SEQADV 6UMT CYS A   18  UNP  Q15116              EXPRESSION TAG                 
SEQADV 6UMT ILE A   19  UNP  Q15116              EXPRESSION TAG                 
SEQADV 6UMT ILE A   20  UNP  Q15116              EXPRESSION TAG                 
SEQADV 6UMT LEU A   21  UNP  Q15116              EXPRESSION TAG                 
SEQADV 6UMT PHE A   22  UNP  Q15116              EXPRESSION TAG                 
SEQADV 6UMT LEU A   23  UNP  Q15116              EXPRESSION TAG                 
SEQADV 6UMT VAL A   24  UNP  Q15116              EXPRESSION TAG                 
SEQADV 6UMT ALA A   25  UNP  Q15116              EXPRESSION TAG                 
SEQADV 6UMT THR A   26  UNP  Q15116              EXPRESSION TAG                 
SEQADV 6UMT ALA A   27  UNP  Q15116              EXPRESSION TAG                 
SEQADV 6UMT THR A   28  UNP  Q15116              EXPRESSION TAG                 
SEQADV 6UMT GLY A   29  UNP  Q15116              EXPRESSION TAG                 
SEQADV 6UMT VAL A   30  UNP  Q15116              EXPRESSION TAG                 
SEQADV 6UMT HIS A   31  UNP  Q15116              EXPRESSION TAG                 
SEQADV 6UMT SER A   32  UNP  Q15116              EXPRESSION TAG                 
SEQADV 6UMT SER A   49  UNP  Q15116    ASN    49 CONFLICT                       
SEQADV 6UMT SER A   58  UNP  Q15116    ASN    58 CONFLICT                       
SEQADV 6UMT GLY A   74  UNP  Q15116    ASN    74 ENGINEERED MUTATION            
SEQADV 6UMT PRO A   76  UNP  Q15116    THR    76 ENGINEERED MUTATION            
SEQADV 6UMT SER A   93  UNP  Q15116    CYS    93 CONFLICT                       
SEQADV 6UMT ASP A  116  UNP  Q15116    ASN   116 CONFLICT                       
SEQADV 6UMT VAL A  132  UNP  Q15116    ALA   132 ENGINEERED MUTATION            
SEQADV 6UMT PRO A  151  UNP  Q15116              EXPRESSION TAG                 
SEQADV 6UMT GLU A  152  UNP  Q15116              EXPRESSION TAG                 
SEQADV 6UMT ALA A  153  UNP  Q15116              EXPRESSION TAG                 
SEQADV 6UMT ASP B   37  UNP  Q9BQ51    ASN    37 CONFLICT                       
SEQADV 6UMT ASP B   64  UNP  Q9BQ51    ASN    64 CONFLICT                       
SEQRES   1 A  140  MET GLY TRP SER CYS ILE ILE LEU PHE LEU VAL ALA THR          
SEQRES   2 A  140  ALA THR GLY VAL HIS SER ASN PRO PRO THR PHE SER PRO          
SEQRES   3 A  140  ALA LEU LEU VAL VAL THR GLU GLY ASP SER ALA THR PHE          
SEQRES   4 A  140  THR CYS SER PHE SER SER THR SER GLU SER PHE VAL LEU          
SEQRES   5 A  140  ASN TRP TYR ARG MET SER PRO SER GLY GLN PRO ASP LYS          
SEQRES   6 A  140  LEU ALA ALA PHE PRO GLU ASP ARG SER GLN PRO GLY GLN          
SEQRES   7 A  140  ASP SER ARG PHE ARG VAL THR GLN LEU PRO ASN GLY ARG          
SEQRES   8 A  140  ASP PHE HIS MET SER VAL VAL ARG ALA ARG ARG ASP ASP          
SEQRES   9 A  140  SER GLY THR TYR LEU CYS GLY ALA ILE SER LEU ALA PRO          
SEQRES  10 A  140  LYS VAL GLN ILE LYS GLU SER LEU ARG ALA GLU LEU ARG          
SEQRES  11 A  140  VAL THR GLU ARG ARG ALA GLU PRO GLU ALA                      
SEQRES   1 B  123  MET ILE PHE LEU LEU LEU MET LEU SER LEU GLU LEU GLN          
SEQRES   2 B  123  LEU HIS GLN ILE ALA ALA LEU PHE THR VAL THR VAL PRO          
SEQRES   3 B  123  LYS GLU LEU TYR ILE ILE GLU HIS GLY SER ASP VAL THR          
SEQRES   4 B  123  LEU GLU CYS ASN PHE ASP THR GLY SER HIS VAL ASN LEU          
SEQRES   5 B  123  GLY ALA ILE THR ALA SER LEU GLN LYS VAL GLU ASP ASP          
SEQRES   6 B  123  THR SER PRO HIS ARG GLU ARG ALA THR LEU LEU GLU GLU          
SEQRES   7 B  123  GLN LEU PRO LEU GLY LYS ALA SER PHE HIS ILE PRO GLN          
SEQRES   8 B  123  VAL GLN VAL ARG ASP GLU GLY GLN TYR GLN CYS ILE ILE          
SEQRES   9 B  123  ILE TYR GLY VAL ALA TRP ASP TYR LYS TYR LEU THR LEU          
SEQRES  10 B  123  LYS VAL LYS ALA SER TYR                                      
HET     MG  A 201       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  HOH   *125(H2 O)                                                    
HELIX    1 AA1 ARG A  114  SER A  118  5                                   5    
HELIX    2 AA2 GLU B   77  LEU B   82  5                                   6    
HELIX    3 AA3 GLN B   93  GLU B   97  5                                   5    
SHEET    1 AA1 4 THR A  36  SER A  38  0                                        
SHEET    2 AA1 4 ALA A  50  SER A  55 -1  O  THR A  53   N  SER A  38           
SHEET    3 AA1 4 ASP A 105  VAL A 110 -1  O  MET A 108   N  PHE A  52           
SHEET    4 AA1 4 PHE A  95  GLN A  99 -1  N  ARG A  96   O  SER A 109           
SHEET    1 AA2 5 LEU A  41  THR A  45  0                                        
SHEET    2 AA2 5 ALA A 140  THR A 145  1  O  GLU A 141   N  LEU A  42           
SHEET    3 AA2 5 GLY A 119  SER A 127 -1  N  GLY A 119   O  LEU A 142           
SHEET    4 AA2 5 LEU A  65  MET A  70 -1  N  TYR A  68   O  LEU A 122           
SHEET    5 AA2 5 PRO A  76  PHE A  82 -1  O  ASP A  77   N  ARG A  69           
SHEET    1 AA3 4 LEU A  41  THR A  45  0                                        
SHEET    2 AA3 4 ALA A 140  THR A 145  1  O  GLU A 141   N  LEU A  42           
SHEET    3 AA3 4 GLY A 119  SER A 127 -1  N  GLY A 119   O  LEU A 142           
SHEET    4 AA3 4 GLN A 133  GLU A 136 -1  O  LYS A 135   N  ALA A 125           
SHEET    1 AA4 4 THR B  22  THR B  24  0                                        
SHEET    2 AA4 4 VAL B  38  ASP B  45 -1  O  ASN B  43   N  THR B  24           
SHEET    3 AA4 4 LYS B  84  ILE B  89 -1  O  ALA B  85   N  CYS B  42           
SHEET    4 AA4 4 THR B  74  LEU B  75 -1  N  THR B  74   O  HIS B  88           
SHEET    1 AA5 4 LEU B  29  GLU B  33  0                                        
SHEET    2 AA5 4 ALA B 109  LYS B 120  1  O  LYS B 118   N  TYR B  30           
SHEET    3 AA5 4 GLY B  98  TYR B 106 -1  N  TYR B 106   O  ALA B 109           
SHEET    4 AA5 4 ILE B  55  LYS B  61 -1  N  SER B  58   O  ILE B 103           
SSBOND   1 CYS A   54    CYS A  123                          1555   1555  2.04  
SSBOND   2 CYS B   42    CYS B  102                          1555   1555  2.07  
LINK         OE1 GLU A  46                MG    MG A 201     1555   1555  2.11  
LINK         OE2 GLU A  46                MG    MG A 201     1555   1555  2.43  
LINK         OE1 GLU A 146                MG    MG A 201     1555   1555  2.51  
LINK         OE2 GLU A 146                MG    MG A 201     1555   1555  1.99  
LINK         OD2 ASP B  37                MG    MG A 201     1555   3545  1.99  
LINK         NE2 HIS B  88                MG    MG A 201     1555   3545  2.01  
CISPEP   1 SER A   38    PRO A   39          0         0.57                     
CISPEP   2 PHE A   82    PRO A   83          0       -12.83                     
CISPEP   3 ALA A  129    PRO A  130          0         2.34                     
SITE     1 AC1  4 GLU A  46  GLU A 146  ASP B  37  HIS B  88                    
CRYST1   41.291   67.798   89.701  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.024218  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014750  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011148        0.00000                         
ATOM      1  N   ASN A  33     -24.027  -9.539  19.170  1.00111.31           N  
ANISOU    1  N   ASN A  33    12657  14221  15414  -1189  -1298  -4138       N  
ATOM      2  CA  ASN A  33     -23.199 -10.217  20.160  1.00108.34           C  
ANISOU    2  CA  ASN A  33    12515  13486  15165  -1354   -857  -3959       C  
ATOM      3  C   ASN A  33     -21.841  -9.544  20.469  1.00 99.06           C  
ANISOU    3  C   ASN A  33    11702  12421  13515  -1050   -713  -3465       C  
ATOM      4  O   ASN A  33     -21.189  -9.931  21.441  1.00101.06           O  
ANISOU    4  O   ASN A  33    12153  12425  13822  -1086   -350  -3162       O  
ATOM      5  CB  ASN A  33     -22.990 -11.673  19.738  1.00117.04           C  
ANISOU    5  CB  ASN A  33    13811  14236  16424  -1494   -767  -4198       C  
ATOM      6  CG  ASN A  33     -24.293 -12.464  19.739  1.00126.13           C  
ANISOU    6  CG  ASN A  33    14633  15208  18082  -1793   -735  -4454       C  
ATOM      7  OD1 ASN A  33     -25.348 -11.936  20.099  1.00128.87           O  
ANISOU    7  OD1 ASN A  33    14584  15691  18689  -1896   -755  -4480       O  
ATOM      8  ND2 ASN A  33     -24.230 -13.727  19.323  1.00130.65           N  
ANISOU    8  ND2 ASN A  33    15361  15477  18804  -1918   -674  -4657       N  
ATOM      9  N   PRO A  34     -21.406  -8.542  19.665  1.00 83.38           N  
ANISOU    9  N   PRO A  34     9812  10792  11076   -746   -988  -3389       N  
ATOM     10  CA  PRO A  34     -20.437  -7.630  20.294  1.00 70.58           C  
ANISOU   10  CA  PRO A  34     8364   9278   9176   -553   -802  -2919       C  
ATOM     11  C   PRO A  34     -21.072  -6.991  21.522  1.00 57.90           C  
ANISOU   11  C   PRO A  34     6522   7668   7811   -674   -635  -2704       C  
ATOM     12  O   PRO A  34     -22.283  -6.799  21.518  1.00 57.97           O  
ANISOU   12  O   PRO A  34     6198   7745   8083   -806   -767  -2918       O  
ATOM     13  CB  PRO A  34     -20.177  -6.572  19.220  1.00 71.52           C  
ANISOU   13  CB  PRO A  34     8581   9745   8847   -265  -1094  -2905       C  
ATOM     14  CG  PRO A  34     -20.529  -7.209  17.951  1.00 75.86           C  
ANISOU   14  CG  PRO A  34     9187  10337   9300   -230  -1392  -3325       C  
ATOM     15  CD  PRO A  34     -21.520  -8.309  18.213  1.00 81.93           C  
ANISOU   15  CD  PRO A  34     9694  10865  10569   -546  -1405  -3685       C  
ATOM     16  N   PRO A  35     -20.283  -6.644  22.545  1.00 49.94           N  
ANISOU   16  N   PRO A  35     5665   6595   6714   -610   -366  -2322       N  
ATOM     17  CA  PRO A  35     -20.963  -6.060  23.705  1.00 46.59           C  
ANISOU   17  CA  PRO A  35     5050   6163   6489   -715   -199  -2154       C  
ATOM     18  C   PRO A  35     -21.633  -4.748  23.352  1.00 47.38           C  
ANISOU   18  C   PRO A  35     4920   6581   6503   -599   -450  -2180       C  
ATOM     19  O   PRO A  35     -21.251  -4.083  22.386  1.00 41.97           O  
ANISOU   19  O   PRO A  35     4329   6117   5500   -383   -706  -2188       O  
ATOM     20  CB  PRO A  35     -19.832  -5.808  24.717  1.00 41.10           C  
ANISOU   20  CB  PRO A  35     4615   5394   5608   -589     39  -1769       C  
ATOM     21  CG  PRO A  35     -18.623  -6.495  24.148  1.00 40.77           C  
ANISOU   21  CG  PRO A  35     4843   5271   5375   -457     29  -1764       C  
ATOM     22  CD  PRO A  35     -18.821  -6.534  22.664  1.00 43.69           C  
ANISOU   22  CD  PRO A  35     5171   5801   5628   -408   -251  -2054       C  
ATOM     23  N   THR A  36     -22.653  -4.389  24.121  1.00 49.01           N  
ANISOU   23  N   THR A  36     4845   6786   6990   -727   -350  -2192       N  
ATOM     24  CA  THR A  36     -23.241  -3.073  23.972  1.00 48.00           C  
ANISOU   24  CA  THR A  36     4516   6929   6791   -572   -557  -2174       C  
ATOM     25  C   THR A  36     -22.754  -2.242  25.152  1.00 42.96           C  
ANISOU   25  C   THR A  36     4003   6277   6041   -501   -306  -1810       C  
ATOM     26  O   THR A  36     -22.334  -2.781  26.167  1.00 39.95           O  
ANISOU   26  O   THR A  36     3776   5686   5717   -606     13  -1640       O  
ATOM     27  CB  THR A  36     -24.757  -3.132  23.911  1.00 51.22           C  
ANISOU   27  CB  THR A  36     4462   7389   7610   -717   -665  -2501       C  
ATOM     28  OG1 THR A  36     -25.245  -3.728  25.112  1.00 56.97           O  
ANISOU   28  OG1 THR A  36     5059   7872   8715   -994   -241  -2467       O  
ATOM     29  CG2 THR A  36     -25.219  -3.968  22.694  1.00 54.62           C  
ANISOU   29  CG2 THR A  36     4758   7844   8152   -780   -988  -2933       C  
ATOM     30  N   PHE A  37     -22.799  -0.928  25.006  1.00 42.88           N  
ANISOU   30  N   PHE A  37     3965   6475   5852   -298   -465  -1702       N  
ATOM     31  CA  PHE A  37     -22.126  -0.050  25.939  1.00 42.42           C  
ANISOU   31  CA  PHE A  37     4075   6413   5630   -202   -289  -1391       C  
ATOM     32  C   PHE A  37     -22.893   1.261  25.947  1.00 43.95           C  
ANISOU   32  C   PHE A  37     4087   6775   5837    -57   -425  -1388       C  
ATOM     33  O   PHE A  37     -23.025   1.900  24.898  1.00 43.18           O  
ANISOU   33  O   PHE A  37     3989   6838   5580    128   -724  -1452       O  
ATOM     34  CB  PHE A  37     -20.673   0.141  25.507  1.00 42.11           C  
ANISOU   34  CB  PHE A  37     4355   6392   5252    -63   -327  -1214       C  
ATOM     35  CG  PHE A  37     -19.811   0.814  26.536  1.00 41.18           C  
ANISOU   35  CG  PHE A  37     4397   6235   5015     -4   -154   -952       C  
ATOM     36  CD1 PHE A  37     -19.221   2.030  26.261  1.00 42.27           C  
ANISOU   36  CD1 PHE A  37     4629   6481   4950    150   -239   -820       C  
ATOM     37  CD2 PHE A  37     -19.587   0.220  27.768  1.00 39.97           C  
ANISOU   37  CD2 PHE A  37     4326   5917   4945    -94     90   -852       C  
ATOM     38  CE1 PHE A  37     -18.391   2.647  27.184  1.00 39.97           C  
ANISOU   38  CE1 PHE A  37     4453   6149   4585    185   -114   -641       C  
ATOM     39  CE2 PHE A  37     -18.790   0.825  28.704  1.00 39.54           C  
ANISOU   39  CE2 PHE A  37     4422   5847   4755     -9    179   -662       C  
ATOM     40  CZ  PHE A  37     -18.181   2.046  28.408  1.00 39.80           C  
ANISOU   40  CZ  PHE A  37     4487   6004   4630    118     61   -581       C  
ATOM     41  N   SER A  38     -23.442   1.646  27.100  1.00 40.45           N  
ANISOU   41  N   SER A  38     3518   6284   5567   -112   -201  -1320       N  
ATOM     42  CA  SER A  38     -24.375   2.769  27.105  1.00 42.21           C  
ANISOU   42  CA  SER A  38     3507   6648   5881     31   -322  -1378       C  
ATOM     43  C   SER A  38     -24.207   3.590  28.388  1.00 44.20           C  
ANISOU   43  C   SER A  38     3858   6843   6092     71    -62  -1170       C  
ATOM     44  O   SER A  38     -23.717   3.063  29.391  1.00 42.91           O  
ANISOU   44  O   SER A  38     3867   6531   5906    -53    229  -1042       O  
ATOM     45  CB  SER A  38     -25.818   2.250  26.963  1.00 50.60           C  
ANISOU   45  CB  SER A  38     4116   7750   7359    -93   -360  -1699       C  
ATOM     46  OG  SER A  38     -26.193   1.570  28.143  1.00 51.89           O  
ANISOU   46  OG  SER A  38     4187   7736   7794   -340     64  -1692       O  
ATOM     47  N   PRO A  39     -24.609   4.877  28.364  1.00 42.13           N  
ANISOU   47  N   PRO A  39     3528   6683   5798    273   -180  -1144       N  
ATOM     48  CA  PRO A  39     -25.211   5.580  27.221  1.00 42.61           C  
ANISOU   48  CA  PRO A  39     3445   6902   5841    496   -547  -1267       C  
ATOM     49  C   PRO A  39     -24.159   6.005  26.227  1.00 41.21           C  
ANISOU   49  C   PRO A  39     3616   6748   5293    648   -752  -1117       C  
ATOM     50  O   PRO A  39     -22.966   6.034  26.577  1.00 36.56           O  
ANISOU   50  O   PRO A  39     3314   6062   4514    586   -589   -919       O  
ATOM     51  CB  PRO A  39     -25.884   6.792  27.873  1.00 46.77           C  
ANISOU   51  CB  PRO A  39     3852   7454   6464    665   -493  -1239       C  
ATOM     52  CG  PRO A  39     -25.040   7.075  29.062  1.00 42.57           C  
ANISOU   52  CG  PRO A  39     3592   6784   5798    588   -179  -1020       C  
ATOM     53  CD  PRO A  39     -24.573   5.719  29.574  1.00 42.15           C  
ANISOU   53  CD  PRO A  39     3613   6626   5775    324     53  -1004       C  
ATOM     54  N   ALA A  40     -24.571   6.315  25.007  1.00 42.34           N  
ANISOU   54  N   ALA A  40     3740   7017   5330    854  -1096  -1221       N  
ATOM     55  CA  ALA A  40     -23.631   6.754  23.977  1.00 40.44           C  
ANISOU   55  CA  ALA A  40     3882   6782   4703   1015  -1234  -1063       C  
ATOM     56  C   ALA A  40     -22.950   8.050  24.389  1.00 43.29           C  
ANISOU   56  C   ALA A  40     4504   7037   4906   1125  -1089   -793       C  
ATOM     57  O   ALA A  40     -21.808   8.304  23.985  1.00 40.87           O  
ANISOU   57  O   ALA A  40     4518   6657   4352   1126  -1001   -615       O  
ATOM     58  CB  ALA A  40     -24.360   6.931  22.585  1.00 41.32           C  
ANISOU   58  CB  ALA A  40     3983   7050   4666   1292  -1663  -1228       C  
ATOM     59  N   LEU A  41     -23.659   8.869  25.171  1.00 43.52           N  
ANISOU   59  N   LEU A  41     4381   7045   5109   1209  -1043   -791       N  
ATOM     60  CA  LEU A  41     -23.142  10.151  25.660  1.00 39.16           C  
ANISOU   60  CA  LEU A  41     4059   6358   4462   1305   -908   -583       C  
ATOM     61  C   LEU A  41     -23.457  10.291  27.152  1.00 38.91           C  
ANISOU   61  C   LEU A  41     3854   6267   4662   1189   -666   -613       C  
ATOM     62  O   LEU A  41     -24.600  10.380  27.538  1.00 39.67           O  
ANISOU   62  O   LEU A  41     3664   6426   4984   1260   -685   -758       O  
ATOM     63  CB  LEU A  41     -23.756  11.330  24.892  1.00 38.46           C  
ANISOU   63  CB  LEU A  41     4078   6270   4264   1656  -1144   -540       C  
ATOM     64  CG  LEU A  41     -23.569  12.725  25.539  1.00 39.47           C  
ANISOU   64  CG  LEU A  41     4385   6217   4396   1769   -999   -380       C  
ATOM     65  CD1 LEU A  41     -22.083  13.004  25.798  1.00 37.63           C  
ANISOU   65  CD1 LEU A  41     4466   5809   4024   1575   -744   -188       C  
ATOM     66  CD2 LEU A  41     -24.107  13.816  24.629  1.00 42.71           C  
ANISOU   66  CD2 LEU A  41     4987   6584   4658   2157  -1239   -304       C  
ATOM     67  N   LEU A  42     -22.431  10.308  27.976  1.00 36.39           N  
ANISOU   67  N   LEU A  42     3711   5835   4280   1029   -440   -495       N  
ATOM     68  CA  LEU A  42     -22.585  10.372  29.435  1.00 38.27           C  
ANISOU   68  CA  LEU A  42     3882   6014   4643    937   -206   -517       C  
ATOM     69  C   LEU A  42     -21.992  11.678  29.943  1.00 36.30           C  
ANISOU   69  C   LEU A  42     3859   5627   4308   1020   -140   -412       C  
ATOM     70  O   LEU A  42     -20.832  11.976  29.667  1.00 36.38           O  
ANISOU   70  O   LEU A  42     4090   5552   4180    965   -138   -305       O  
ATOM     71  CB  LEU A  42     -21.878   9.183  30.087  1.00 35.67           C  
ANISOU   71  CB  LEU A  42     3598   5665   4290    711    -42   -506       C  
ATOM     72  CG  LEU A  42     -21.882   9.100  31.625  1.00 38.22           C  
ANISOU   72  CG  LEU A  42     3964   5918   4638    640    207   -504       C  
ATOM     73  CD1 LEU A  42     -23.306   9.093  32.109  1.00 39.82           C  
ANISOU   73  CD1 LEU A  42     3913   6159   5059    669    340   -626       C  
ATOM     74  CD2 LEU A  42     -21.099   7.841  32.101  1.00 38.25           C  
ANISOU   74  CD2 LEU A  42     4087   5884   4564    480    317   -463       C  
ATOM     75  N   VAL A  43     -22.774  12.474  30.652  1.00 36.07           N  
ANISOU   75  N   VAL A  43     3759   5559   4388   1144    -70   -467       N  
ATOM     76  CA  VAL A  43     -22.306  13.784  31.082  1.00 34.96           C  
ANISOU   76  CA  VAL A  43     3841   5251   4191   1233    -22   -404       C  
ATOM     77  C   VAL A  43     -22.431  13.835  32.595  1.00 38.56           C  
ANISOU   77  C   VAL A  43     4295   5671   4684   1178    191   -488       C  
ATOM     78  O   VAL A  43     -23.509  13.615  33.130  1.00 41.78           O  
ANISOU   78  O   VAL A  43     4501   6149   5225   1233    305   -591       O  
ATOM     79  CB  VAL A  43     -23.109  14.943  30.444  1.00 40.48           C  
ANISOU   79  CB  VAL A  43     4551   5888   4941   1519   -154   -392       C  
ATOM     80  CG1 VAL A  43     -22.628  16.281  30.961  1.00 42.09           C  
ANISOU   80  CG1 VAL A  43     5013   5859   5122   1586    -64   -342       C  
ATOM     81  CG2 VAL A  43     -23.057  14.897  28.893  1.00 49.38           C  
ANISOU   81  CG2 VAL A  43     5760   7054   5947   1638   -385   -297       C  
ATOM     82  N  AVAL A  44     -21.318  14.134  33.267  0.42 35.68           N  
ANISOU   82  N  AVAL A  44     4155   5200   4203   1079    247   -464       N  
ATOM     83  N  BVAL A  44     -21.316  14.072  33.280  0.58 35.37           N  
ANISOU   83  N  BVAL A  44     4111   5167   4162   1073    250   -465       N  
ATOM     84  CA AVAL A  44     -21.217  14.103  34.730  0.42 36.28           C  
ANISOU   84  CA AVAL A  44     4322   5249   4215   1047    409   -550       C  
ATOM     85  CA BVAL A  44     -21.332  14.226  34.738  0.58 36.42           C  
ANISOU   85  CA BVAL A  44     4334   5259   4245   1068    414   -556       C  
ATOM     86  C  AVAL A  44     -20.440  15.329  35.240  0.42 36.32           C  
ANISOU   86  C  AVAL A  44     4553   5078   4168   1075    384   -598       C  
ATOM     87  C  BVAL A  44     -20.605  15.488  35.171  0.58 36.63           C  
ANISOU   87  C  BVAL A  44     4583   5106   4229   1104    386   -599       C  
ATOM     88  O  AVAL A  44     -19.559  15.832  34.545  0.42 35.50           O  
ANISOU   88  O  AVAL A  44     4537   4873   4079   1014    279   -544       O  
ATOM     89  O  BVAL A  44     -19.922  16.151  34.390  0.58 36.08           O  
ANISOU   89  O  BVAL A  44     4601   4918   4188   1079    284   -538       O  
ATOM     90  CB AVAL A  44     -20.505  12.809  35.201  0.42 34.79           C  
ANISOU   90  CB AVAL A  44     4180   5136   3901    888    448   -527       C  
ATOM     91  CB BVAL A  44     -20.682  13.028  35.471  0.58 34.57           C  
ANISOU   91  CB BVAL A  44     4169   5093   3874    919    484   -551       C  
ATOM     92  CG1AVAL A  44     -20.607  12.646  36.701  0.42 33.77           C  
ANISOU   92  CG1AVAL A  44     4201   4991   3638    913    623   -596       C  
ATOM     93  CG1BVAL A  44     -21.524  11.767  35.297  0.58 35.02           C  
ANISOU   93  CG1BVAL A  44     4033   5264   4010    857    594   -536       C  
ATOM     94  CG2AVAL A  44     -21.054  11.565  34.460  0.42 31.56           C  
ANISOU   94  CG2AVAL A  44     3570   4844   3576    811    455   -487       C  
ATOM     95  CG2BVAL A  44     -19.221  12.801  34.983  0.58 27.21           C  
ANISOU   95  CG2BVAL A  44     3335   4141   2864    801    324   -498       C  
ATOM     96  N   THR A  45     -20.768  15.811  36.435  1.00 34.64           N  
ANISOU   96  N   THR A  45     4440   4813   3909   1156    506   -717       N  
ATOM     97  CA  THR A  45     -20.067  16.938  37.036  1.00 36.77           C  
ANISOU   97  CA  THR A  45     4925   4904   4143   1172    468   -826       C  
ATOM     98  C   THR A  45     -18.768  16.431  37.670  1.00 36.40           C  
ANISOU   98  C   THR A  45     4999   4887   3946   1028    370   -891       C  
ATOM     99  O   THR A  45     -18.772  15.336  38.250  1.00 33.44           O  
ANISOU   99  O   THR A  45     4636   4652   3418   1012    414   -875       O  
ATOM    100  CB  THR A  45     -20.967  17.609  38.085  1.00 41.43           C  
ANISOU  100  CB  THR A  45     5593   5436   4711   1347    632   -965       C  
ATOM    101  OG1 THR A  45     -22.164  18.071  37.437  1.00 45.84           O  
ANISOU  101  OG1 THR A  45     5982   5982   5455   1518    688   -927       O  
ATOM    102  CG2 THR A  45     -20.263  18.784  38.730  1.00 44.32           C  
ANISOU  102  CG2 THR A  45     6199   5594   5046   1361    576  -1128       C  
ATOM    103  N   GLU A  46     -17.671  17.189  37.556  1.00 36.77           N  
ANISOU  103  N   GLU A  46     5126   4790   4055    932    243   -974       N  
ATOM    104  CA  GLU A  46     -16.377  16.733  38.083  1.00 37.14           C  
ANISOU  104  CA  GLU A  46     5209   4887   4016    816     89  -1085       C  
ATOM    105  C   GLU A  46     -16.540  16.439  39.577  1.00 33.91           C  
ANISOU  105  C   GLU A  46     4985   4553   3347    942     88  -1229       C  
ATOM    106  O   GLU A  46     -17.203  17.173  40.282  1.00 35.69           O  
ANISOU  106  O   GLU A  46     5349   4697   3515   1064    187  -1336       O  
ATOM    107  CB  GLU A  46     -15.248  17.762  37.839  1.00 39.17           C  
ANISOU  107  CB  GLU A  46     5470   4949   4462    671    -17  -1225       C  
ATOM    108  CG  GLU A  46     -15.494  19.109  38.450  1.00 38.50           C  
ANISOU  108  CG  GLU A  46     5546   4642   4441    728     13  -1404       C  
ATOM    109  CD  GLU A  46     -14.355  20.145  38.300  1.00 40.05           C  
ANISOU  109  CD  GLU A  46     5742   4592   4884    535    -60  -1590       C  
ATOM    110  OE1 GLU A  46     -13.161  19.822  37.993  1.00 38.37           O  
ANISOU  110  OE1 GLU A  46     5370   4411   4797    344   -165  -1654       O  
ATOM    111  OE2 GLU A  46     -14.689  21.330  38.582  1.00 42.07           O  
ANISOU  111  OE2 GLU A  46     6151   4599   5236    577      5  -1707       O  
ATOM    112  N   GLY A  47     -15.983  15.325  40.039  1.00 33.51           N  
ANISOU  112  N   GLY A  47     4973   4649   3110    947     -4  -1218       N  
ATOM    113  CA  GLY A  47     -16.123  14.964  41.449  1.00 37.77           C  
ANISOU  113  CA  GLY A  47     5781   5249   3320   1110      8  -1316       C  
ATOM    114  C   GLY A  47     -17.164  13.870  41.684  1.00 40.08           C  
ANISOU  114  C   GLY A  47     6137   5634   3458   1185    277  -1123       C  
ATOM    115  O   GLY A  47     -17.059  13.117  42.652  1.00 45.08           O  
ANISOU  115  O   GLY A  47     7024   6323   3782   1302    306  -1114       O  
ATOM    116  N   ASP A  48     -18.159  13.780  40.804  1.00 34.50           N  
ANISOU  116  N   ASP A  48     5210   4928   2969   1124    473   -980       N  
ATOM    117  CA  ASP A  48     -19.192  12.736  40.854  1.00 35.42           C  
ANISOU  117  CA  ASP A  48     5286   5111   3062   1128    753   -833       C  
ATOM    118  C   ASP A  48     -18.742  11.428  40.192  1.00 38.54           C  
ANISOU  118  C   ASP A  48     5587   5571   3484   1015    689   -686       C  
ATOM    119  O   ASP A  48     -17.794  11.428  39.395  1.00 35.78           O  
ANISOU  119  O   ASP A  48     5124   5237   3232    934    449   -682       O  
ATOM    120  CB  ASP A  48     -20.477  13.224  40.160  1.00 37.20           C  
ANISOU  120  CB  ASP A  48     5246   5325   3563   1127    930   -811       C  
ATOM    121  CG  ASP A  48     -21.252  14.265  40.987  1.00 46.36           C  
ANISOU  121  CG  ASP A  48     6505   6417   4694   1282   1109   -947       C  
ATOM    122  OD1 ASP A  48     -21.051  14.335  42.208  1.00 48.98           O  
ANISOU  122  OD1 ASP A  48     7142   6725   4742   1381   1193  -1035       O  
ATOM    123  OD2 ASP A  48     -22.073  15.008  40.414  1.00 52.93           O  
ANISOU  123  OD2 ASP A  48     7129   7215   5766   1341   1158   -975       O  
ATOM    124  N   SER A  49     -19.431  10.318  40.466  1.00 32.69           N  
ANISOU  124  N   SER A  49     4887   4844   2689    998    941   -574       N  
ATOM    125  CA  SER A  49     -19.084   9.069  39.765  1.00 31.28           C  
ANISOU  125  CA  SER A  49     4624   4688   2574    888    896   -451       C  
ATOM    126  C   SER A  49     -19.742   9.092  38.380  1.00 32.87           C  
ANISOU  126  C   SER A  49     4455   4928   3105    760    888   -433       C  
ATOM    127  O   SER A  49     -20.806   9.666  38.207  1.00 34.32           O  
ANISOU  127  O   SER A  49     4463   5122   3456    772   1017   -482       O  
ATOM    128  CB  SER A  49     -19.533   7.822  40.557  1.00 33.21           C  
ANISOU  128  CB  SER A  49     5094   4870   2656    899   1194   -335       C  
ATOM    129  OG  SER A  49     -19.073   7.830  41.924  1.00 35.52           O  
ANISOU  129  OG  SER A  49     5816   5123   2557   1084   1217   -339       O  
ATOM    130  N   ALA A  50     -19.101   8.457  37.415  1.00 35.34           N  
ANISOU  130  N   ALA A  50     4665   5271   3493    672    720   -383       N  
ATOM    131  CA  ALA A  50     -19.630   8.328  36.067  1.00 36.08           C  
ANISOU  131  CA  ALA A  50     4474   5413   3823    582    668   -378       C  
ATOM    132  C   ALA A  50     -19.755   6.854  35.794  1.00 36.46           C  
ANISOU  132  C   ALA A  50     4496   5444   3914    475    758   -326       C  
ATOM    133  O   ALA A  50     -18.745   6.164  35.806  1.00 38.85           O  
ANISOU  133  O   ALA A  50     4939   5722   4099    474    664   -276       O  
ATOM    134  CB  ALA A  50     -18.676   8.986  35.051  1.00 34.05           C  
ANISOU  134  CB  ALA A  50     4166   5179   3591    577    413   -380       C  
ATOM    135  N   THR A  51     -20.957   6.374  35.498  1.00 33.68           N  
ANISOU  135  N   THR A  51     3937   5093   3766    388    925   -365       N  
ATOM    136  CA  THR A  51     -21.147   4.951  35.318  1.00 34.30           C  
ANISOU  136  CA  THR A  51     4003   5100   3928    252   1054   -343       C  
ATOM    137  C   THR A  51     -21.693   4.597  33.930  1.00 38.22           C  
ANISOU  137  C   THR A  51     4188   5665   4668    152    914   -450       C  
ATOM    138  O   THR A  51     -22.772   5.027  33.536  1.00 37.82           O  
ANISOU  138  O   THR A  51     3852   5687   4831    145    914   -567       O  
ATOM    139  CB  THR A  51     -22.070   4.393  36.412  1.00 40.09           C  
ANISOU  139  CB  THR A  51     4808   5718   4707    187   1460   -324       C  
ATOM    140  OG1 THR A  51     -21.456   4.623  37.686  1.00 38.42           O  
ANISOU  140  OG1 THR A  51     4979   5445   4172    326   1554   -223       O  
ATOM    141  CG2 THR A  51     -22.268   2.904  36.231  1.00 44.07           C  
ANISOU  141  CG2 THR A  51     5327   6080   5337     16   1639   -300       C  
ATOM    142  N   PHE A  52     -20.900   3.841  33.168  1.00 37.06           N  
ANISOU  142  N   PHE A  52     4101   5505   4475    111    763   -431       N  
ATOM    143  CA  PHE A  52     -21.390   3.213  31.950  1.00 39.21           C  
ANISOU  143  CA  PHE A  52     4149   5816   4932     13    647   -558       C  
ATOM    144  C   PHE A  52     -21.939   1.820  32.235  1.00 41.84           C  
ANISOU  144  C   PHE A  52     4460   5992   5447   -171    888   -609       C  
ATOM    145  O   PHE A  52     -21.616   1.231  33.245  1.00 45.01           O  
ANISOU  145  O   PHE A  52     5114   6236   5753   -192   1125   -485       O  
ATOM    146  CB  PHE A  52     -20.281   3.086  30.937  1.00 35.29           C  
ANISOU  146  CB  PHE A  52     3750   5368   4290     65    408   -535       C  
ATOM    147  CG  PHE A  52     -19.824   4.378  30.340  1.00 38.05           C  
ANISOU  147  CG  PHE A  52     4108   5833   4516    201    209   -500       C  
ATOM    148  CD1 PHE A  52     -18.606   4.943  30.725  1.00 36.80           C  
ANISOU  148  CD1 PHE A  52     4132   5658   4191    270    185   -394       C  
ATOM    149  CD2 PHE A  52     -20.556   4.982  29.322  1.00 36.63           C  
ANISOU  149  CD2 PHE A  52     3765   5760   4394    267     37   -585       C  
ATOM    150  CE1 PHE A  52     -18.144   6.108  30.127  1.00 36.62           C  
ANISOU  150  CE1 PHE A  52     4133   5685   4097    351     65   -360       C  
ATOM    151  CE2 PHE A  52     -20.112   6.148  28.716  1.00 37.09           C  
ANISOU  151  CE2 PHE A  52     3912   5868   4314    403   -102   -514       C  
ATOM    152  CZ  PHE A  52     -18.896   6.713  29.108  1.00 36.59           C  
ANISOU  152  CZ  PHE A  52     4036   5748   4118    419    -53   -394       C  
ATOM    153  N   THR A  53     -22.748   1.276  31.333  1.00 39.44           N  
ANISOU  153  N   THR A  53     3879   5708   5397   -297    821   -800       N  
ATOM    154  CA  THR A  53     -23.129  -0.114  31.453  1.00 35.98           C  
ANISOU  154  CA  THR A  53     3431   5072   5169   -511   1045   -874       C  
ATOM    155  C   THR A  53     -22.712  -0.899  30.219  1.00 38.09           C  
ANISOU  155  C   THR A  53     3685   5337   5451   -553    804  -1002       C  
ATOM    156  O   THR A  53     -23.034  -0.500  29.090  1.00 41.35           O  
ANISOU  156  O   THR A  53     3880   5930   5903   -502    498  -1175       O  
ATOM    157  CB  THR A  53     -24.658  -0.264  31.662  1.00 41.97           C  
ANISOU  157  CB  THR A  53     3813   5802   6333   -697   1266  -1071       C  
ATOM    158  OG1 THR A  53     -25.048   0.459  32.838  1.00 42.98           O  
ANISOU  158  OG1 THR A  53     3977   5926   6428   -642   1545   -957       O  
ATOM    159  CG2 THR A  53     -25.014  -1.723  31.818  1.00 43.33           C  
ANISOU  159  CG2 THR A  53     3994   5703   6767   -968   1562  -1150       C  
ATOM    160  N   CYS A  54     -21.967  -1.986  30.437  1.00 39.25           N  
ANISOU  160  N   CYS A  54     4109   5276   5530   -603    932   -916       N  
ATOM    161  CA ACYS A  54     -21.571  -2.912  29.378  0.99 42.45           C  
ANISOU  161  CA ACYS A  54     4541   5624   5963   -649    771  -1055       C  
ATOM    162  CA BCYS A  54     -21.592  -2.892  29.365  0.01 42.20           C  
ANISOU  162  CA BCYS A  54     4502   5598   5935   -649    767  -1059       C  
ATOM    163  C   CYS A  54     -22.428  -4.162  29.455  1.00 47.40           C  
ANISOU  163  C   CYS A  54     5072   5992   6945   -921   1009  -1224       C  
ATOM    164  O   CYS A  54     -22.680  -4.677  30.538  1.00 49.13           O  
ANISOU  164  O   CYS A  54     5437   5968   7261  -1034   1389  -1098       O  
ATOM    165  CB ACYS A  54     -20.083  -3.283  29.482  0.99 43.81           C  
ANISOU  165  CB ACYS A  54     5068   5723   5853   -488    737   -875       C  
ATOM    166  CB BCYS A  54     -20.100  -3.223  29.426  0.01 41.78           C  
ANISOU  166  CB BCYS A  54     4797   5483   5596   -485    720   -882       C  
ATOM    167  SG ACYS A  54     -19.492  -4.434  28.153  0.99 51.80           S  
ANISOU  167  SG ACYS A  54     6149   6654   6877   -504    573  -1060       S  
ATOM    168  SG BCYS A  54     -19.491  -4.198  28.028  0.01 51.66           S  
ANISOU  168  SG BCYS A  54     6099   6696   6832   -482    525  -1066       S  
ATOM    169  N  ASER A  55     -22.887  -4.644  28.302  0.55 46.27           N  
ANISOU  169  N  ASER A  55     4706   5883   6990  -1029    800  -1524       N  
ATOM    170  N  BSER A  55     -22.862  -4.658  28.301  0.45 46.12           N  
ANISOU  170  N  BSER A  55     4696   5861   6967  -1027    800  -1521       N  
ATOM    171  CA ASER A  55     -23.718  -5.838  28.244  0.55 47.01           C  
ANISOU  171  CA ASER A  55     4658   5712   7491  -1331   1000  -1760       C  
ATOM    172  CA BSER A  55     -23.709  -5.836  28.244  0.45 47.03           C  
ANISOU  172  CA BSER A  55     4663   5714   7491  -1329    999  -1758       C  
ATOM    173  C  ASER A  55     -23.086  -6.877  27.331  0.55 46.64           C  
ANISOU  173  C  ASER A  55     4787   5528   7407  -1346    853  -1905       C  
ATOM    174  C  BSER A  55     -23.106  -6.885  27.321  0.45 46.61           C  
ANISOU  174  C  BSER A  55     4777   5523   7410  -1350    852  -1911       C  
ATOM    175  O  ASER A  55     -22.757  -6.576  26.176  0.55 43.82           O  
ANISOU  175  O  ASER A  55     4385   5398   6868  -1198    471  -2053       O  
ATOM    176  O  BSER A  55     -22.812  -6.600  26.155  0.45 44.13           O  
ANISOU  176  O  BSER A  55     4408   5434   6924  -1209    469  -2070       O  
ATOM    177  CB ASER A  55     -25.117  -5.493  27.743  0.55 49.65           C  
ANISOU  177  CB ASER A  55     4460   6207   8197  -1481    862  -2106       C  
ATOM    178  CB BSER A  55     -25.109  -5.458  27.768  0.45 49.61           C  
ANISOU  178  CB BSER A  55     4458   6207   8185  -1475    865  -2096       C  
ATOM    179  OG ASER A  55     -25.628  -4.354  28.408  0.55 49.97           O  
ANISOU  179  OG ASER A  55     4323   6429   8233  -1391    931  -1992       O  
ATOM    180  OG BSER A  55     -25.938  -6.599  27.686  0.45 54.16           O  
ANISOU  180  OG BSER A  55     4827   6518   9233  -1814   1062  -2384       O  
ATOM    181  N   PHE A  56     -22.928  -8.095  27.842  1.00 47.19           N  
ANISOU  181  N   PHE A  56     5097   5204   7630  -1505   1179  -1858       N  
ATOM    182  CA  PHE A  56     -22.288  -9.167  27.092  1.00 48.37           C  
ANISOU  182  CA  PHE A  56     5459   5160   7759  -1504   1091  -1990       C  
ATOM    183  C   PHE A  56     -22.551 -10.508  27.737  1.00 54.27           C  
ANISOU  183  C   PHE A  56     6407   5399   8815  -1754   1519  -1985       C  
ATOM    184  O   PHE A  56     -22.617 -10.614  28.958  1.00 57.38           O  
ANISOU  184  O   PHE A  56     7007   5574   9220  -1791   1912  -1702       O  
ATOM    185  CB  PHE A  56     -20.765  -8.963  27.002  1.00 47.95           C  
ANISOU  185  CB  PHE A  56     5764   5200   7254  -1162    953  -1737       C  
ATOM    186  CG  PHE A  56     -20.063 -10.061  26.251  1.00 52.72           C  
ANISOU  186  CG  PHE A  56     6591   5604   7836  -1121    892  -1877       C  
ATOM    187  CD1 PHE A  56     -20.131 -10.121  24.858  1.00 53.31           C  
ANISOU  187  CD1 PHE A  56     6526   5850   7881  -1108    568  -2208       C  
ATOM    188  CD2 PHE A  56     -19.369 -11.049  26.923  1.00 55.03           C  
ANISOU  188  CD2 PHE A  56     7266   5524   8118  -1064   1153  -1692       C  
ATOM    189  CE1 PHE A  56     -19.516 -11.143  24.153  1.00 53.34           C  
ANISOU  189  CE1 PHE A  56     6747   5661   7860  -1063    533  -2371       C  
ATOM    190  CE2 PHE A  56     -18.747 -12.081  26.223  1.00 54.15           C  
ANISOU  190  CE2 PHE A  56     7360   5202   8013  -1004   1108  -1843       C  
ATOM    191  CZ  PHE A  56     -18.820 -12.128  24.834  1.00 53.49           C  
ANISOU  191  CZ  PHE A  56     7113   5295   7915  -1016    811  -2194       C  
ATOM    192  N   SER A  57     -22.674 -11.540  26.917  1.00 54.77           N  
ANISOU  192  N   SER A  57     6463   5247   9102  -1911   1458  -2295       N  
ATOM    193  CA  SER A  57     -22.829 -12.886  27.431  1.00 63.73           C  
ANISOU  193  CA  SER A  57     7850   5826  10539  -2148   1879  -2293       C  
ATOM    194  C   SER A  57     -22.294 -13.895  26.421  1.00 71.20           C  
ANISOU  194  C   SER A  57     8967   6581  11506  -2129   1702  -2552       C  
ATOM    195  O   SER A  57     -22.499 -13.749  25.210  1.00 72.55           O  
ANISOU  195  O   SER A  57     8875   7001  11689  -2134   1303  -2927       O  
ATOM    196  CB  SER A  57     -24.298 -13.167  27.764  1.00 68.64           C  
ANISOU  196  CB  SER A  57     8099   6250  11730  -2592   2191  -2530       C  
ATOM    197  OG  SER A  57     -24.534 -14.557  27.873  1.00 78.93           O  
ANISOU  197  OG  SER A  57     9591   7002  13395  -2873   2543  -2647       O  
ATOM    198  N   SER A  58     -21.588 -14.902  26.927  1.00 73.98           N  
ANISOU  198  N   SER A  58     9798   6487  11823  -2063   1989  -2348       N  
ATOM    199  CA  SER A  58     -21.089 -15.994  26.099  1.00 79.23           C  
ANISOU  199  CA  SER A  58    10678   6876  12549  -2044   1902  -2588       C  
ATOM    200  C   SER A  58     -21.439 -17.315  26.751  1.00 87.23           C  
ANISOU  200  C   SER A  58    11995   7205  13944  -2313   2401  -2561       C  
ATOM    201  O   SER A  58     -21.133 -17.551  27.921  1.00 86.40           O  
ANISOU  201  O   SER A  58    12282   6804  13742  -2219   2780  -2141       O  
ATOM    202  CB  SER A  58     -19.575 -15.903  25.883  1.00 76.07           C  
ANISOU  202  CB  SER A  58    10618   6615  11669  -1576   1701  -2367       C  
ATOM    203  OG  SER A  58     -19.115 -17.077  25.231  1.00 78.99           O  
ANISOU  203  OG  SER A  58    11243   6641  12130  -1549   1704  -2583       O  
ATOM    204  N   THR A  59     -22.082 -18.183  25.987  1.00 93.91           N  
ANISOU  204  N   THR A  59    12655   7925  15103  -2548   2333  -2921       N  
ATOM    205  CA  THR A  59     -22.535 -19.440  26.546  1.00104.73           C  
ANISOU  205  CA  THR A  59    14226   8803  16762  -2751   2750  -2828       C  
ATOM    206  C   THR A  59     -21.433 -20.491  26.426  1.00108.87           C  
ANISOU  206  C   THR A  59    15299   8944  17121  -2500   2791  -2713       C  
ATOM    207  O   THR A  59     -21.514 -21.565  27.024  1.00113.78           O  
ANISOU  207  O   THR A  59    16241   9103  17886  -2570   3157  -2540       O  
ATOM    208  CB  THR A  59     -23.845 -19.923  25.856  1.00111.67           C  
ANISOU  208  CB  THR A  59    14615   9721  18095  -3124   2675  -3272       C  
ATOM    209  OG1 THR A  59     -23.725 -19.805  24.431  1.00110.72           O  
ANISOU  209  OG1 THR A  59    14272   9905  17893  -3047   2126  -3697       O  
ATOM    210  CG2 THR A  59     -25.025 -19.076  26.309  1.00111.67           C  
ANISOU  210  CG2 THR A  59    14111  10000  18317  -3340   2773  -3308       C  
ATOM    211  N   SER A  60     -20.368 -20.119  25.742  1.00105.90           N  
ANISOU  211  N   SER A  60    15046   8775  16417  -2167   2444  -2780       N  
ATOM    212  CA  SER A  60     -19.374 -21.076  25.319  1.00108.06           C  
ANISOU  212  CA  SER A  60    15719   8778  16561  -1902   2388  -2794       C  
ATOM    213  C   SER A  60     -17.946 -20.659  25.648  1.00103.18           C  
ANISOU  213  C   SER A  60    15460   8223  15519  -1403   2326  -2495       C  
ATOM    214  O   SER A  60     -17.034 -21.457  25.544  1.00105.57           O  
ANISOU  214  O   SER A  60    16118   8287  15707  -1109   2327  -2423       O  
ATOM    215  CB  SER A  60     -19.519 -21.353  23.828  1.00110.78           C  
ANISOU  215  CB  SER A  60    15824   9308  16959  -1964   1999  -3305       C  
ATOM    216  OG  SER A  60     -19.036 -20.278  23.081  1.00105.77           O  
ANISOU  216  OG  SER A  60    15004   9180  16003  -1749   1626  -3450       O  
ATOM    217  N   GLU A  61     -17.732 -19.423  26.087  1.00101.10           N  
ANISOU  217  N   GLU A  61    15056   8364  14993  -1256   2228  -2276       N  
ATOM    218  CA  GLU A  61     -16.380 -18.983  26.441  1.00 99.80           C  
ANISOU  218  CA  GLU A  61    15101   8438  14381   -737   2074  -1939       C  
ATOM    219  C   GLU A  61     -16.329 -18.195  27.763  1.00110.21           C  
ANISOU  219  C   GLU A  61    16494   9894  15488   -613   2196  -1484       C  
ATOM    220  O   GLU A  61     -17.288 -17.552  28.110  1.00105.37           O  
ANISOU  220  O   GLU A  61    15623   9428  14984   -894   2287  -1470       O  
ATOM    221  CB  GLU A  61     -15.745 -18.199  25.285  1.00 88.19           C  
ANISOU  221  CB  GLU A  61    13328   7535  12644   -533   1648  -2152       C  
ATOM    222  CG  GLU A  61     -15.563 -18.990  23.998  1.00 88.07           C  
ANISOU  222  CG  GLU A  61    13343   7401  12718   -543   1520  -2582       C  
ATOM    223  CD  GLU A  61     -15.206 -18.134  22.787  1.00 81.58           C  
ANISOU  223  CD  GLU A  61    12233   7146  11616   -409   1157  -2812       C  
ATOM    224  OE1 GLU A  61     -15.937 -17.199  22.472  1.00 78.07           O  
ANISOU  224  OE1 GLU A  61    11450   7080  11134   -587    980  -2905       O  
ATOM    225  OE2 GLU A  61     -14.193 -18.404  22.143  1.00 79.38           O  
ANISOU  225  OE2 GLU A  61    12090   6921  11150   -107   1073  -2897       O  
ATOM    226  N   SER A  62     -15.219 -18.284  28.492  1.00125.02           N  
ANISOU  226  N   SER A  62    18722  11712  17068   -171   2184  -1149       N  
ATOM    227  CA  SER A  62     -15.046 -17.641  29.791  1.00129.26           C  
ANISOU  227  CA  SER A  62    19419  12347  17347     16   2262   -739       C  
ATOM    228  C   SER A  62     -15.107 -16.138  29.693  1.00124.89           C  
ANISOU  228  C   SER A  62    18419  12425  16608      8   1993   -742       C  
ATOM    229  O   SER A  62     -15.732 -15.486  30.530  1.00127.79           O  
ANISOU  229  O   SER A  62    18744  12881  16928   -112   2130   -561       O  
ATOM    230  CB  SER A  62     -13.707 -18.050  30.419  1.00135.84           C  
ANISOU  230  CB  SER A  62    20679  13045  17889    566   2173   -466       C  
ATOM    231  OG  SER A  62     -12.551 -17.631  29.699  1.00136.69           O  
ANISOU  231  OG  SER A  62    20556  13552  17829    896   1791   -596       O  
ATOM    232  N   PHE A  63     -14.458 -15.574  28.685  1.00102.45           N  
ANISOU  232  N   PHE A  63    15274   9998  13655    142   1648   -941       N  
ATOM    233  CA  PHE A  63     -13.242 -14.818  28.870  1.00 79.01           C  
ANISOU  233  CA  PHE A  63    12253   7389  10377    537   1386   -795       C  
ATOM    234  C   PHE A  63     -13.602 -13.572  29.706  1.00 64.66           C  
ANISOU  234  C   PHE A  63    10280   5883   8405    492   1354   -596       C  
ATOM    235  O   PHE A  63     -14.740 -13.234  29.854  1.00 61.43           O  
ANISOU  235  O   PHE A  63     9730   5483   8128    171   1496   -622       O  
ATOM    236  CB  PHE A  63     -12.700 -14.368  27.512  1.00 71.68           C  
ANISOU  236  CB  PHE A  63    10997   6833   9406    586   1124  -1072       C  
ATOM    237  CG  PHE A  63     -11.889 -15.407  26.766  1.00 72.16           C  
ANISOU  237  CG  PHE A  63    11220   6682   9514    791   1107  -1248       C  
ATOM    238  CD1 PHE A  63     -10.580 -15.687  27.120  1.00 70.20           C  
ANISOU  238  CD1 PHE A  63    11126   6406   9142   1226   1031  -1124       C  
ATOM    239  CD2 PHE A  63     -12.410 -16.057  25.675  1.00 69.52           C  
ANISOU  239  CD2 PHE A  63    10855   6206   9352    574   1137  -1578       C  
ATOM    240  CE1 PHE A  63      -9.830 -16.614  26.421  1.00 68.61           C  
ANISOU  240  CE1 PHE A  63    11049   6018   9001   1444   1031  -1304       C  
ATOM    241  CE2 PHE A  63     -11.666 -16.984  24.981  1.00 68.87           C  
ANISOU  241  CE2 PHE A  63    10939   5928   9300    777   1135  -1762       C  
ATOM    242  CZ  PHE A  63     -10.376 -17.259  25.352  1.00 68.06           C  
ANISOU  242  CZ  PHE A  63    10989   5785   9085   1215   1102  -1616       C  
ATOM    243  N   VAL A  64     -12.598 -12.935  30.267  1.00 56.73           N  
ANISOU  243  N   VAL A  64     9293   5116   7147    829   1163   -427       N  
ATOM    244  CA  VAL A  64     -12.707 -11.657  30.951  1.00 48.70           C  
ANISOU  244  CA  VAL A  64     8115   4430   5958    837   1068   -289       C  
ATOM    245  C   VAL A  64     -13.228 -10.536  30.047  1.00 44.29           C  
ANISOU  245  C   VAL A  64     7102   4266   5459    590    941   -474       C  
ATOM    246  O   VAL A  64     -13.023 -10.556  28.861  1.00 42.88           O  
ANISOU  246  O   VAL A  64     6730   4219   5344    547    826   -690       O  
ATOM    247  CB  VAL A  64     -11.309 -11.250  31.437  1.00 48.17           C  
ANISOU  247  CB  VAL A  64     8077   4563   5664   1259    807   -187       C  
ATOM    248  CG1 VAL A  64     -11.286  -9.875  32.026  1.00 40.43           C  
ANISOU  248  CG1 VAL A  64     6905   3933   4525   1269    667   -110       C  
ATOM    249  CG2 VAL A  64     -10.763 -12.254  32.413  1.00 52.29           C  
ANISOU  249  CG2 VAL A  64     9080   4725   6063   1597    860     14       C  
ATOM    250  N   LEU A  65     -13.931  -9.578  30.638  1.00 38.97           N  
ANISOU  250  N   LEU A  65     6309   3757   4739    458    976   -382       N  
ATOM    251  CA  LEU A  65     -14.485  -8.458  29.913  1.00 36.70           C  
ANISOU  251  CA  LEU A  65     5644   3811   4490    274    852   -520       C  
ATOM    252  C   LEU A  65     -13.665  -7.212  30.233  1.00 35.26           C  
ANISOU  252  C   LEU A  65     5342   3954   4103    467    653   -426       C  
ATOM    253  O   LEU A  65     -13.419  -6.944  31.392  1.00 35.04           O  
ANISOU  253  O   LEU A  65     5476   3902   3936    608    670   -251       O  
ATOM    254  CB  LEU A  65     -15.953  -8.259  30.306  1.00 42.15           C  
ANISOU  254  CB  LEU A  65     6242   4432   5341    -19   1053   -526       C  
ATOM    255  CG  LEU A  65     -16.781  -7.263  29.499  1.00 46.09           C  
ANISOU  255  CG  LEU A  65     6352   5231   5929   -199    917   -701       C  
ATOM    256  CD1 LEU A  65     -17.018  -7.821  28.091  1.00 50.52           C  
ANISOU  256  CD1 LEU A  65     6769   5795   6630   -316    793   -988       C  
ATOM    257  CD2 LEU A  65     -18.118  -6.981  30.199  1.00 49.53           C  
ANISOU  257  CD2 LEU A  65     6673   5611   6537   -422   1135   -684       C  
ATOM    258  N   ASN A  66     -13.269  -6.442  29.222  1.00 34.31           N  
ANISOU  258  N   ASN A  66     4965   4115   3957    469    480   -552       N  
ATOM    259  CA  ASN A  66     -12.354  -5.314  29.436  1.00 34.33           C  
ANISOU  259  CA  ASN A  66     4839   4375   3828    622    326   -495       C  
ATOM    260  C   ASN A  66     -12.989  -3.969  29.200  1.00 34.62           C  
ANISOU  260  C   ASN A  66     4666   4641   3846    481    279   -504       C  
ATOM    261  O   ASN A  66     -13.823  -3.813  28.315  1.00 34.81           O  
ANISOU  261  O   ASN A  66     4572   4723   3932    323    279   -611       O  
ATOM    262  CB  ASN A  66     -11.123  -5.394  28.516  1.00 36.02           C  
ANISOU  262  CB  ASN A  66     4949   4704   4034    768    230   -607       C  
ATOM    263  CG  ASN A  66     -10.152  -6.502  28.893  1.00 37.61           C  
ANISOU  263  CG  ASN A  66     5319   4723   4247   1016    219   -596       C  
ATOM    264  OD1 ASN A  66     -10.355  -7.237  29.860  1.00 38.67           O  
ANISOU  264  OD1 ASN A  66     5714   4621   4357   1103    272   -476       O  
ATOM    265  ND2 ASN A  66      -9.086  -6.631  28.104  1.00 36.88           N  
ANISOU  265  ND2 ASN A  66     5099   4727   4188   1153    175   -719       N  
ATOM    266  N   TRP A  67     -12.559  -2.981  29.971  1.00 31.20           N  
ANISOU  266  N   TRP A  67     4196   4333   3325    567    207   -415       N  
ATOM    267  CA  TRP A  67     -13.016  -1.624  29.765  1.00 29.46           C  
ANISOU  267  CA  TRP A  67     3806   4298   3090    470    164   -417       C  
ATOM    268  C   TRP A  67     -11.857  -0.754  29.256  1.00 31.37           C  
ANISOU  268  C   TRP A  67     3907   4708   3306    545     66   -455       C  
ATOM    269  O   TRP A  67     -10.777  -0.796  29.848  1.00 30.79           O  
ANISOU  269  O   TRP A  67     3831   4642   3224    689     -6   -454       O  
ATOM    270  CB  TRP A  67     -13.580  -1.100  31.086  1.00 31.97           C  
ANISOU  270  CB  TRP A  67     4207   4587   3354    473    210   -312       C  
ATOM    271  CG  TRP A  67     -14.127   0.260  31.040  1.00 30.78           C  
ANISOU  271  CG  TRP A  67     3913   4579   3202    400    181   -315       C  
ATOM    272  CD1 TRP A  67     -14.596   0.919  29.956  1.00 30.81           C  
ANISOU  272  CD1 TRP A  67     3757   4693   3255    314    141   -377       C  
ATOM    273  CD2 TRP A  67     -14.258   1.152  32.150  1.00 31.04           C  
ANISOU  273  CD2 TRP A  67     3996   4641   3158    447    181   -257       C  
ATOM    274  NE1 TRP A  67     -14.995   2.177  30.312  1.00 32.30           N  
ANISOU  274  NE1 TRP A  67     3886   4959   3427    309    123   -346       N  
ATOM    275  CE2 TRP A  67     -14.794   2.341  31.661  1.00 30.40           C  
ANISOU  275  CE2 TRP A  67     3760   4670   3122    375    154   -287       C  
ATOM    276  CE3 TRP A  67     -13.981   1.047  33.511  1.00 37.57           C  
ANISOU  276  CE3 TRP A  67     5025   5400   3848    573    191   -188       C  
ATOM    277  CZ2 TRP A  67     -15.068   3.424  32.484  1.00 36.15           C  
ANISOU  277  CZ2 TRP A  67     4503   5428   3805    404    157   -266       C  
ATOM    278  CZ3 TRP A  67     -14.259   2.134  34.335  1.00 39.10           C  
ANISOU  278  CZ3 TRP A  67     5243   5650   3962    600    184   -181       C  
ATOM    279  CH2 TRP A  67     -14.789   3.304  33.816  1.00 35.93           C  
ANISOU  279  CH2 TRP A  67     4657   5345   3650    504    175   -228       C  
ATOM    280  N   TYR A  68     -12.092   0.033  28.195  1.00 32.47           N  
ANISOU  280  N   TYR A  68     3934   4965   3439    458     68   -494       N  
ATOM    281  CA  TYR A  68     -11.053   0.818  27.488  1.00 31.87           C  
ANISOU  281  CA  TYR A  68     3751   5001   3359    483     77   -522       C  
ATOM    282  C   TYR A  68     -11.368   2.284  27.359  1.00 31.80           C  
ANISOU  282  C   TYR A  68     3691   5066   3327    412     82   -469       C  
ATOM    283  O   TYR A  68     -12.529   2.676  27.178  1.00 34.10           O  
ANISOU  283  O   TYR A  68     4016   5366   3575    362     59   -437       O  
ATOM    284  CB  TYR A  68     -10.824   0.310  26.034  1.00 31.12           C  
ANISOU  284  CB  TYR A  68     3677   4932   3215    485    147   -604       C  
ATOM    285  CG  TYR A  68     -10.124  -0.996  26.010  1.00 31.06           C  
ANISOU  285  CG  TYR A  68     3703   4844   3256    585    169   -682       C  
ATOM    286  CD1 TYR A  68      -8.733  -1.067  26.222  1.00 28.94           C  
ANISOU  286  CD1 TYR A  68     3318   4601   3075    704    191   -725       C  
ATOM    287  CD2 TYR A  68     -10.824  -2.170  25.840  1.00 31.06           C  
ANISOU  287  CD2 TYR A  68     3827   4717   3256    570    163   -739       C  
ATOM    288  CE1 TYR A  68      -8.089  -2.276  26.238  1.00 28.27           C  
ANISOU  288  CE1 TYR A  68     3267   4430   3046    851    193   -801       C  
ATOM    289  CE2 TYR A  68     -10.171  -3.401  25.833  1.00 30.90           C  
ANISOU  289  CE2 TYR A  68     3881   4572   3289    687    193   -808       C  
ATOM    290  CZ  TYR A  68      -8.803  -3.439  26.046  1.00 36.07           C  
ANISOU  290  CZ  TYR A  68     4440   5264   4000    851    201   -828       C  
ATOM    291  OH  TYR A  68      -8.150  -4.656  26.061  1.00 38.03           O  
ANISOU  291  OH  TYR A  68     4762   5378   4309   1020    215   -900       O  
ATOM    292  N   ARG A  69     -10.317   3.088  27.402  1.00 30.18           N  
ANISOU  292  N   ARG A  69     3387   4897   3184    413    117   -480       N  
ATOM    293  CA  ARG A  69     -10.379   4.472  26.952  1.00 29.68           C  
ANISOU  293  CA  ARG A  69     3313   4849   3115    338    188   -429       C  
ATOM    294  C   ARG A  69      -9.518   4.606  25.689  1.00 34.40           C  
ANISOU  294  C   ARG A  69     3900   5467   3704    316    367   -445       C  
ATOM    295  O   ARG A  69      -8.414   4.044  25.619  1.00 34.43           O  
ANISOU  295  O   ARG A  69     3780   5489   3813    343    433   -535       O  
ATOM    296  CB  ARG A  69      -9.907   5.431  28.044  1.00 31.56           C  
ANISOU  296  CB  ARG A  69     3459   5064   3468    309    140   -449       C  
ATOM    297  CG  ARG A  69      -9.783   6.861  27.573  1.00 32.21           C  
ANISOU  297  CG  ARG A  69     3547   5097   3596    214    258   -406       C  
ATOM    298  CD  ARG A  69      -9.533   7.841  28.706  1.00 33.39           C  
ANISOU  298  CD  ARG A  69     3626   5193   3867    171    185   -466       C  
ATOM    299  NE  ARG A  69      -9.475   9.212  28.219  1.00 36.21           N  
ANISOU  299  NE  ARG A  69     4027   5439   4292     67    333   -418       N  
ATOM    300  CZ  ARG A  69      -9.163  10.246  28.984  1.00 37.74           C  
ANISOU  300  CZ  ARG A  69     4167   5541   4630     -6    311   -498       C  
ATOM    301  NH1 ARG A  69      -8.866  10.038  30.260  1.00 38.48           N  
ANISOU  301  NH1 ARG A  69     4163   5683   4776     37    112   -644       N  
ATOM    302  NH2 ARG A  69      -9.107  11.469  28.476  1.00 42.52           N  
ANISOU  302  NH2 ARG A  69     4853   5987   5316   -110    487   -441       N  
ATOM    303  N   MET A  70     -10.048   5.287  24.671  1.00 32.95           N  
ANISOU  303  N   MET A  70     3867   5275   3376    299    454   -360       N  
ATOM    304  CA  MET A  70      -9.328   5.482  23.416  1.00 35.38           C  
ANISOU  304  CA  MET A  70     4257   5580   3604    293    688   -341       C  
ATOM    305  C   MET A  70      -8.472   6.749  23.422  1.00 42.54           C  
ANISOU  305  C   MET A  70     5109   6400   4656    178    911   -292       C  
ATOM    306  O   MET A  70      -8.955   7.844  23.711  1.00 47.21           O  
ANISOU  306  O   MET A  70     5776   6908   5253    138    894   -202       O  
ATOM    307  CB  MET A  70     -10.323   5.537  22.245  1.00 40.35           C  
ANISOU  307  CB  MET A  70     5159   6234   3938    381    659   -270       C  
ATOM    308  CG  MET A  70     -11.330   4.408  22.281  1.00 41.35           C  
ANISOU  308  CG  MET A  70     5295   6424   3992    447    420   -365       C  
ATOM    309  SD  MET A  70     -10.548   2.775  22.405  1.00 54.68           S  
ANISOU  309  SD  MET A  70     6876   8119   5782    460    446   -523       S  
ATOM    310  CE  MET A  70      -9.805   2.752  20.772  1.00 43.48           C  
ANISOU  310  CE  MET A  70     5649   6733   4138    527    692   -543       C  
ATOM    311  N   SER A  71      -7.195   6.587  23.106  1.00 43.34           N  
ANISOU  311  N   SER A  71     5057   6500   4911    120   1141   -375       N  
ATOM    312  CA  SER A  71      -6.247   7.690  22.992  1.00 53.52           C  
ANISOU  312  CA  SER A  71     6243   7679   6414    -40   1431   -371       C  
ATOM    313  C   SER A  71      -6.567   8.617  21.806  1.00 66.57           C  
ANISOU  313  C   SER A  71     8248   9206   7841    -61   1719   -173       C  
ATOM    314  O   SER A  71      -7.451   8.318  20.978  1.00 59.66           O  
ANISOU  314  O   SER A  71     7686   8372   6610     90   1653    -64       O  
ATOM    315  CB  SER A  71      -4.834   7.130  22.839  1.00 52.34           C  
ANISOU  315  CB  SER A  71     5792   7577   6517    -83   1633   -544       C  
ATOM    316  OG  SER A  71      -4.674   6.627  21.526  1.00 59.64           O  
ANISOU  316  OG  SER A  71     6909   8523   7229    -19   1904   -497       O  
ATOM    317  N   PRO A  72      -5.854   9.755  21.722  1.00 85.13           N  
ANISOU  317  N   PRO A  72    10565  11384  10397   -239   2035   -136       N  
ATOM    318  CA  PRO A  72      -5.928  10.573  20.502  1.00 91.13           C  
ANISOU  318  CA  PRO A  72    11721  11975  10928   -247   2412     81       C  
ATOM    319  C   PRO A  72      -5.691   9.766  19.231  1.00 90.80           C  
ANISOU  319  C   PRO A  72    11890  12020  10591   -128   2638    115       C  
ATOM    320  O   PRO A  72      -6.525   9.773  18.325  1.00 95.85           O  
ANISOU  320  O   PRO A  72    12964  12663  10790     60   2601    276       O  
ATOM    321  CB  PRO A  72      -4.796  11.586  20.698  1.00 98.04           C  
ANISOU  321  CB  PRO A  72    12398  12640  12211   -525   2807     33       C  
ATOM    322  CG  PRO A  72      -4.708  11.739  22.182  1.00 95.56           C  
ANISOU  322  CG  PRO A  72    11699  12362  12246   -615   2464   -167       C  
ATOM    323  CD  PRO A  72      -4.993  10.379  22.747  1.00 88.12           C  
ANISOU  323  CD  PRO A  72    10576  11685  11220   -438   2055   -300       C  
ATOM    324  N   SER A  73      -4.565   9.059  19.193  1.00 83.78           N  
ANISOU  324  N   SER A  73    10685  11210   9939   -205   2838    -65       N  
ATOM    325  CA  SER A  73      -4.163   8.283  18.024  1.00 78.73           C  
ANISOU  325  CA  SER A  73    10215  10641   9058    -99   3119    -75       C  
ATOM    326  C   SER A  73      -5.060   7.068  17.802  1.00 72.65           C  
ANISOU  326  C   SER A  73     9599  10053   7950    143   2724   -129       C  
ATOM    327  O   SER A  73      -4.904   6.347  16.821  1.00 76.70           O  
ANISOU  327  O   SER A  73    10310  10631   8200    269   2882   -164       O  
ATOM    328  CB  SER A  73      -2.701   7.842  18.154  1.00 80.04           C  
ANISOU  328  CB  SER A  73     9920  10844   9646   -228   3418   -297       C  
ATOM    329  OG  SER A  73      -2.503   6.917  19.209  1.00 79.23           O  
ANISOU  329  OG  SER A  73     9394  10900   9808   -172   3026   -525       O  
ATOM    330  N   GLY A  74      -5.998   6.840  18.712  1.00 63.68           N  
ANISOU  330  N   GLY A  74     8376   8982   6836    195   2241   -156       N  
ATOM    331  CA  GLY A  74      -6.962   5.771  18.545  1.00 58.59           C  
ANISOU  331  CA  GLY A  74     7860   8467   5936    373   1884   -221       C  
ATOM    332  C   GLY A  74      -6.554   4.437  19.146  1.00 55.08           C  
ANISOU  332  C   GLY A  74     7116   8116   5697    402   1725   -430       C  
ATOM    333  O   GLY A  74      -7.182   3.421  18.845  1.00 53.62           O  
ANISOU  333  O   GLY A  74     7049   7995   5330    523   1520   -514       O  
ATOM    334  N   GLN A  75      -5.515   4.431  19.989  1.00 50.13           N  
ANISOU  334  N   GLN A  75     6112   7481   5455    306   1800   -532       N  
ATOM    335  CA  GLN A  75      -5.137   3.235  20.725  1.00 40.00           C  
ANISOU  335  CA  GLN A  75     4572   6260   4365    387   1600   -706       C  
ATOM    336  C   GLN A  75      -5.999   2.984  21.970  1.00 36.89           C  
ANISOU  336  C   GLN A  75     4130   5867   4020    409   1194   -694       C  
ATOM    337  O   GLN A  75      -6.241   3.875  22.804  1.00 32.69           O  
ANISOU  337  O   GLN A  75     3522   5304   3593    322   1088   -630       O  
ATOM    338  CB  GLN A  75      -3.654   3.295  21.149  1.00 37.80           C  
ANISOU  338  CB  GLN A  75     3888   5994   4479    336   1785   -855       C  
ATOM    339  CG  GLN A  75      -2.682   3.317  19.972  1.00 44.26           C  
ANISOU  339  CG  GLN A  75     4693   6811   5314    316   2263   -908       C  
ATOM    340  CD  GLN A  75      -2.576   1.971  19.248  1.00 43.08           C  
ANISOU  340  CD  GLN A  75     4658   6715   4995    508   2302  -1021       C  
ATOM    341  OE1 GLN A  75      -3.222   0.976  19.626  1.00 41.84           O  
ANISOU  341  OE1 GLN A  75     4587   6571   4739    641   1965  -1065       O  
ATOM    342  NE2 GLN A  75      -1.768   1.940  18.211  1.00 46.53           N  
ANISOU  342  NE2 GLN A  75     5116   7155   5408    515   2751  -1076       N  
ATOM    343  N   PRO A  76      -6.422   1.736  22.147  1.00 30.84           N  
ANISOU  343  N   PRO A  76     3281   5135   3301     54   1119  -1031       N  
ATOM    344  CA  PRO A  76      -7.232   1.459  23.333  1.00 30.42           C  
ANISOU  344  CA  PRO A  76     3141   5108   3309    121    781   -933       C  
ATOM    345  C   PRO A  76      -6.357   1.294  24.577  1.00 35.24           C  
ANISOU  345  C   PRO A  76     3458   5690   4240    151    679   -982       C  
ATOM    346  O   PRO A  76      -5.406   0.521  24.557  1.00 37.77           O  
ANISOU  346  O   PRO A  76     3591   5966   4793    196    728  -1132       O  
ATOM    347  CB  PRO A  76      -7.946   0.154  22.962  1.00 31.30           C  
ANISOU  347  CB  PRO A  76     3327   5215   3350    194    650   -986       C  
ATOM    348  CG  PRO A  76      -6.932  -0.540  22.084  1.00 33.08           C  
ANISOU  348  CG  PRO A  76     3512   5402   3656    197    886  -1172       C  
ATOM    349  CD  PRO A  76      -6.275   0.554  21.276  1.00 32.29           C  
ANISOU  349  CD  PRO A  76     3521   5302   3444     98   1207  -1181       C  
ATOM    350  N   ASP A  77      -6.668   2.024  25.650  1.00 34.03           N  
ANISOU  350  N   ASP A  77     3276   5553   4100    142    519   -874       N  
ATOM    351  CA  ASP A  77      -5.895   1.902  26.904  1.00 39.25           C  
ANISOU  351  CA  ASP A  77     3721   6186   5006    193    347   -924       C  
ATOM    352  C   ASP A  77      -6.736   1.173  27.933  1.00 32.62           C  
ANISOU  352  C   ASP A  77     2972   5332   4090    278     84   -818       C  
ATOM    353  O   ASP A  77      -7.847   1.613  28.260  1.00 29.72           O  
ANISOU  353  O   ASP A  77     2760   4992   3541    246     36   -690       O  
ATOM    354  CB  ASP A  77      -5.489   3.270  27.443  1.00 44.76           C  
ANISOU  354  CB  ASP A  77     4346   6890   5771    112    372   -918       C  
ATOM    355  CG  ASP A  77      -4.729   3.177  28.779  1.00 56.00           C  
ANISOU  355  CG  ASP A  77     5576   8287   7414    182    118   -996       C  
ATOM    356  OD1 ASP A  77      -3.911   2.250  28.952  1.00 58.46           O  
ANISOU  356  OD1 ASP A  77     5712   8554   7946    282     11  -1119       O  
ATOM    357  OD2 ASP A  77      -4.958   4.027  29.673  1.00 59.65           O  
ANISOU  357  OD2 ASP A  77     6079   8761   7824    155     -3   -945       O  
ATOM    358  N   LYS A  78      -6.225   0.054  28.436  1.00 32.49           N  
ANISOU  358  N   LYS A  78     2871   5247   4228    389    -65   -874       N  
ATOM    359  CA  LYS A  78      -7.050  -0.806  29.285  1.00 33.85           C  
ANISOU  359  CA  LYS A  78     3199   5358   4305    457   -246   -756       C  
ATOM    360  C   LYS A  78      -7.209  -0.178  30.657  1.00 32.61           C  
ANISOU  360  C   LYS A  78     3126   5201   4065    467   -413   -660       C  
ATOM    361  O   LYS A  78      -6.217   0.020  31.342  1.00 30.01           O  
ANISOU  361  O   LYS A  78     2687   4851   3864    534   -572   -730       O  
ATOM    362  CB  LYS A  78      -6.411  -2.184  29.403  1.00 33.16           C  
ANISOU  362  CB  LYS A  78     3048   5153   4398    589   -358   -828       C  
ATOM    363  CG  LYS A  78      -7.229  -3.242  30.122  1.00 31.84           C  
ANISOU  363  CG  LYS A  78     3086   4866   4145    647   -481   -699       C  
ATOM    364  CD  LYS A  78      -6.474  -4.570  30.085  1.00 32.89           C  
ANISOU  364  CD  LYS A  78     3156   4848   4491    794   -584   -780       C  
ATOM    365  CE  LYS A  78      -7.005  -5.641  31.017  1.00 33.31           C  
ANISOU  365  CE  LYS A  78     3450   4718   4488    875   -726   -633       C  
ATOM    366  NZ  LYS A  78      -6.195  -6.917  30.919  1.00 33.02           N  
ANISOU  366  NZ  LYS A  78     3352   4499   4694   1045   -844   -716       N  
ATOM    367  N   LEU A  79      -8.437   0.118  31.059  1.00 32.65           N  
ANISOU  367  N   LEU A  79     3312   5218   3874    407   -384   -532       N  
ATOM    368  CA  LEU A  79      -8.678   0.740  32.377  1.00 33.94           C  
ANISOU  368  CA  LEU A  79     3605   5375   3916    406   -492   -454       C  
ATOM    369  C   LEU A  79      -8.924  -0.274  33.483  1.00 31.65           C  
ANISOU  369  C   LEU A  79     3529   4962   3534    490   -628   -357       C  
ATOM    370  O   LEU A  79      -8.418  -0.148  34.601  1.00 31.04           O  
ANISOU  370  O   LEU A  79     3565   4844   3383    566   -818   -339       O  
ATOM    371  CB  LEU A  79      -9.898   1.660  32.324  1.00 30.79           C  
ANISOU  371  CB  LEU A  79     3291   5029   3380    298   -348   -384       C  
ATOM    372  CG  LEU A  79      -9.903   2.724  31.243  1.00 30.97           C  
ANISOU  372  CG  LEU A  79     3204   5133   3430    224   -214   -429       C  
ATOM    373  CD1 LEU A  79     -11.303   3.320  31.137  1.00 32.39           C  
ANISOU  373  CD1 LEU A  79     3471   5326   3510    166   -127   -360       C  
ATOM    374  CD2 LEU A  79      -8.840   3.789  31.495  1.00 34.87           C  
ANISOU  374  CD2 LEU A  79     3590   5654   4006    201   -237   -504       C  
ATOM    375  N   ALA A  80      -9.795  -1.232  33.195  1.00 34.83           N  
ANISOU  375  N   ALA A  80     4027   5287   3919    469   -523   -293       N  
ATOM    376  CA  ALA A  80     -10.134  -2.232  34.190  1.00 40.96           C  
ANISOU  376  CA  ALA A  80     5062   5899   4602    523   -578   -175       C  
ATOM    377  C   ALA A  80     -10.776  -3.367  33.470  1.00 39.77           C  
ANISOU  377  C   ALA A  80     4905   5650   4555    491   -453   -173       C  
ATOM    378  O   ALA A  80     -10.981  -3.297  32.252  1.00 37.25           O  
ANISOU  378  O   ALA A  80     4395   5414   4343    436   -359   -275       O  
ATOM    379  CB  ALA A  80     -11.075  -1.667  35.252  1.00 42.76           C  
ANISOU  379  CB  ALA A  80     5526   6106   4614    444   -478    -70       C  
ATOM    380  N   ALA A  81     -11.136  -4.390  34.231  1.00 39.22           N  
ANISOU  380  N   ALA A  81     5080   5386   4436    518   -444    -60       N  
ATOM    381  CA  ALA A  81     -11.687  -5.618  33.665  1.00 41.75           C  
ANISOU  381  CA  ALA A  81     5408   5558   4897    485   -330    -70       C  
ATOM    382  C   ALA A  81     -12.448  -6.422  34.713  1.00 44.08           C  
ANISOU  382  C   ALA A  81     6036   5614   5098    443   -207     90       C  
ATOM    383  O   ALA A  81     -12.228  -6.265  35.907  1.00 42.96           O  
ANISOU  383  O   ALA A  81     6181   5398   4743    500   -273    225       O  
ATOM    384  CB  ALA A  81     -10.589  -6.460  33.080  1.00 37.41           C  
ANISOU  384  CB  ALA A  81     4746   4947   4521    628   -485   -155       C  
ATOM    385  N   PHE A  82     -13.322  -7.304  34.255  1.00 44.49           N  
ANISOU  385  N   PHE A  82     6073   5526   5305    339    -21     64       N  
ATOM    386  CA  PHE A  82     -13.965  -8.242  35.162  1.00 48.69           C  
ANISOU  386  CA  PHE A  82     6931   5770   5798    281    155    213       C  
ATOM    387  C   PHE A  82     -13.919  -9.645  34.599  1.00 49.91           C  
ANISOU  387  C   PHE A  82     7081   5704   6180    301    171    175       C  
ATOM    388  O   PHE A  82     -14.190  -9.841  33.411  1.00 51.73           O  
ANISOU  388  O   PHE A  82     7018   6009   6628    243    194    -10       O  
ATOM    389  CB  PHE A  82     -15.417  -7.847  35.426  1.00 49.60           C  
ANISOU  389  CB  PHE A  82     7043   5868   5933     64    482    205       C  
ATOM    390  CG  PHE A  82     -16.100  -8.707  36.469  1.00 55.78           C  
ANISOU  390  CG  PHE A  82     8203   6329   6663    -34    763    364       C  
ATOM    391  CD1 PHE A  82     -16.133  -8.310  37.798  1.00 58.59           C  
ANISOU  391  CD1 PHE A  82     8950   6613   6700    -31    863    537       C  
ATOM    392  CD2 PHE A  82     -16.690  -9.915  36.124  1.00 57.19           C  
ANISOU  392  CD2 PHE A  82     8379   6255   7096   -137    948    333       C  
ATOM    393  CE1 PHE A  82     -16.756  -9.094  38.761  1.00 63.12           C  
ANISOU  393  CE1 PHE A  82     9945   6861   7176   -133   1182    701       C  
ATOM    394  CE2 PHE A  82     -17.307 -10.707  37.092  1.00 60.47           C  
ANISOU  394  CE2 PHE A  82     9175   6329   7470   -251   1269    493       C  
ATOM    395  CZ  PHE A  82     -17.342 -10.292  38.400  1.00 64.04           C  
ANISOU  395  CZ  PHE A  82    10052   6708   7573   -251   1404    687       C  
ATOM    396  N   PRO A  83     -13.547 -10.620  35.434  1.00 50.73           N  
ANISOU  396  N   PRO A  83     7539   5519   6217    399    137    346       N  
ATOM    397  CA  PRO A  83     -12.933 -10.360  36.747  1.00 59.78           C  
ANISOU  397  CA  PRO A  83     9070   6597   7045    538    -15    549       C  
ATOM    398  C   PRO A  83     -11.414 -10.265  36.604  1.00 71.30           C  
ANISOU  398  C   PRO A  83    10422   8151   8519    801   -437    500       C  
ATOM    399  O   PRO A  83     -10.824 -11.071  35.880  1.00 70.44           O  
ANISOU  399  O   PRO A  83    10150   7959   8655    908   -555    407       O  
ATOM    400  CB  PRO A  83     -13.336 -11.579  37.573  1.00 55.89           C  
ANISOU  400  CB  PRO A  83     9045   5698   6492    523    154    756       C  
ATOM    401  CG  PRO A  83     -13.416 -12.704  36.555  1.00 54.35           C  
ANISOU  401  CG  PRO A  83     8641   5346   6662    501    203    634       C  
ATOM    402  CD  PRO A  83     -13.806 -12.056  35.213  1.00 50.88           C  
ANISOU  402  CD  PRO A  83     7664   5219   6449    375    250    358       C  
ATOM    403  N   GLU A  84     -10.796  -9.240  37.163  1.00 79.84           N  
ANISOU  403  N   GLU A  84    11520   9415   9402    890   -647    509       N  
ATOM    404  CA  GLU A  84      -9.342  -9.165  37.219  1.00 88.54           C  
ANISOU  404  CA  GLU A  84    12514  10566  10563   1141  -1061    443       C  
ATOM    405  C   GLU A  84      -9.012  -8.145  38.305  1.00 96.11           C  
ANISOU  405  C   GLU A  84    13673  11632  11214   1200  -1253    504       C  
ATOM    406  O   GLU A  84      -9.846  -7.331  38.624  1.00 93.91           O  
ANISOU  406  O   GLU A  84    13474  11462  10745   1028  -1025    536       O  
ATOM    407  CB  GLU A  84      -8.794  -8.768  35.834  1.00 84.53           C  
ANISOU  407  CB  GLU A  84    11464  10289  10363   1127  -1077    189       C  
ATOM    408  CG  GLU A  84      -7.375  -9.199  35.485  1.00 83.91           C  
ANISOU  408  CG  GLU A  84    11162  10177  10544   1360  -1385     53       C  
ATOM    409  CD  GLU A  84      -6.919  -8.727  34.103  1.00 78.72           C  
ANISOU  409  CD  GLU A  84    10019   9740  10152   1300  -1284   -201       C  
ATOM    410  OE1 GLU A  84      -7.648  -8.910  33.136  1.00 73.30           O  
ANISOU  410  OE1 GLU A  84     9226   9100   9526   1146  -1017   -267       O  
ATOM    411  OE2 GLU A  84      -5.822  -8.178  33.992  1.00 77.18           O  
ANISOU  411  OE2 GLU A  84     9566   9657  10103   1405  -1468   -345       O  
ATOM    412  N   SER A  93      -8.138   2.009  43.366  1.00 62.38           N  
ANISOU  412  N   SER A  93     9731   8513   5459    921  -1892   -158       N  
ATOM    413  CA  SER A  93      -8.283   2.182  41.930  1.00 59.24           C  
ANISOU  413  CA  SER A  93     8804   8223   5482    800  -1655   -210       C  
ATOM    414  C   SER A  93      -9.359   3.245  41.598  1.00 53.79           C  
ANISOU  414  C   SER A  93     8004   7623   4809    593  -1249   -236       C  
ATOM    415  O   SER A  93     -10.355   3.408  42.297  1.00 56.10           O  
ANISOU  415  O   SER A  93     8612   7862   4840    515  -1000   -162       O  
ATOM    416  CB  SER A  93      -8.603   0.834  41.254  1.00 63.81           C  
ANISOU  416  CB  SER A  93     9362   8701   6180    824  -1522    -61       C  
ATOM    417  OG  SER A  93      -8.517   0.910  39.826  1.00 63.73           O  
ANISOU  417  OG  SER A  93     8872   8793   6549    747  -1377   -140       O  
ATOM    418  N   ARG A  94      -9.109   3.992  40.535  1.00 47.65           N  
ANISOU  418  N   ARG A  94     6787   6963   4355    515  -1183   -353       N  
ATOM    419  CA  ARG A  94      -9.997   5.038  40.074  1.00 42.51           C  
ANISOU  419  CA  ARG A  94     5999   6379   3775    360   -870   -382       C  
ATOM    420  C   ARG A  94     -11.170   4.474  39.284  1.00 38.15           C  
ANISOU  420  C   ARG A  94     5386   5806   3303    279   -550   -264       C  
ATOM    421  O   ARG A  94     -12.161   5.167  39.059  1.00 36.16           O  
ANISOU  421  O   ARG A  94     5078   5574   3089    177   -299   -272       O  
ATOM    422  CB  ARG A  94      -9.238   6.017  39.169  1.00 46.10           C  
ANISOU  422  CB  ARG A  94     6060   6925   4530    313   -918   -528       C  
ATOM    423  CG  ARG A  94      -8.134   6.831  39.814  1.00 50.00           C  
ANISOU  423  CG  ARG A  94     6502   7435   5059    348  -1200   -710       C  
ATOM    424  CD  ARG A  94      -7.832   8.045  38.925  1.00 49.21           C  
ANISOU  424  CD  ARG A  94     6068   7382   5249    229  -1067   -829       C  
ATOM    425  NE  ARG A  94      -9.059   8.832  38.797  1.00 48.07           N  
ANISOU  425  NE  ARG A  94     6008   7234   5023    126   -767   -763       N  
ATOM    426  CZ  ARG A  94      -9.591   9.248  37.649  1.00 45.03           C  
ANISOU  426  CZ  ARG A  94     5453   6860   4796     51   -528   -705       C  
ATOM    427  NH1 ARG A  94      -8.978   8.974  36.508  1.00 43.52           N  
ANISOU  427  NH1 ARG A  94     5035   6692   4809     43   -507   -702       N  
ATOM    428  NH2 ARG A  94     -10.754   9.925  37.653  1.00 38.80           N  
ANISOU  428  NH2 ARG A  94     4743   6046   3955     -3   -314   -661       N  
ATOM    429  N   PHE A  95     -10.991   3.245  38.797  1.00 34.87           N  
ANISOU  429  N   PHE A  95     4941   5344   2965    336   -596   -188       N  
ATOM    430  CA  PHE A  95     -11.919   2.562  37.902  1.00 36.87           C  
ANISOU  430  CA  PHE A  95     5087   5572   3350    270   -363   -120       C  
ATOM    431  C   PHE A  95     -12.497   1.332  38.539  1.00 45.78           C  
ANISOU  431  C   PHE A  95     6511   6544   4341    280   -267      8       C  
ATOM    432  O   PHE A  95     -11.806   0.608  39.261  1.00 52.15           O  
ANISOU  432  O   PHE A  95     7561   7254   4998    394   -465     73       O  
ATOM    433  CB  PHE A  95     -11.207   2.223  36.594  1.00 38.04           C  
ANISOU  433  CB  PHE A  95     4930   5782   3743    305   -453   -175       C  
ATOM    434  CG  PHE A  95     -10.579   3.417  35.987  1.00 37.70           C  
ANISOU  434  CG  PHE A  95     4647   5850   3827    276   -489   -287       C  
ATOM    435  CD1 PHE A  95     -11.371   4.420  35.468  1.00 35.57           C  
ANISOU  435  CD1 PHE A  95     4291   5631   3592    182   -309   -299       C  
ATOM    436  CD2 PHE A  95      -9.220   3.606  36.044  1.00 40.96           C  
ANISOU  436  CD2 PHE A  95     4933   6288   4343    342   -702   -389       C  
ATOM    437  CE1 PHE A  95     -10.807   5.564  34.972  1.00 36.44           C  
ANISOU  437  CE1 PHE A  95     4242   5799   3803    146   -312   -378       C  
ATOM    438  CE2 PHE A  95      -8.657   4.743  35.525  1.00 43.71           C  
ANISOU  438  CE2 PHE A  95     5068   6702   4836    281   -673   -499       C  
ATOM    439  CZ  PHE A  95      -9.456   5.726  35.000  1.00 37.86           C  
ANISOU  439  CZ  PHE A  95     4300   5995   4090    178   -465   -476       C  
ATOM    440  N   ARG A  96     -13.797   1.131  38.335  1.00 45.58           N  
ANISOU  440  N   ARG A  96     6476   6465   4376    162     39     38       N  
ATOM    441  CA  ARG A  96     -14.455   0.018  38.978  1.00 45.36           C  
ANISOU  441  CA  ARG A  96     6737   6249   4248    126    222    154       C  
ATOM    442  C   ARG A  96     -15.410  -0.696  38.041  1.00 41.36           C  
ANISOU  442  C   ARG A  96     6013   5688   4013     28    430    132       C  
ATOM    443  O   ARG A  96     -16.194  -0.061  37.315  1.00 38.73           O  
ANISOU  443  O   ARG A  96     5398   5442   3875    -52    548     30       O  
ATOM    444  CB  ARG A  96     -15.188   0.486  40.220  1.00 47.55           C  
ANISOU  444  CB  ARG A  96     7338   6448   4282     49    463    186       C  
ATOM    445  CG  ARG A  96     -15.844  -0.632  40.971  1.00 54.24           C  
ANISOU  445  CG  ARG A  96     8553   7059   4995    -12    726    320       C  
ATOM    446  CD  ARG A  96     -16.399  -0.130  42.282  1.00 57.71           C  
ANISOU  446  CD  ARG A  96     9392   7414   5123    -82    988    347       C  
ATOM    447  NE  ARG A  96     -15.412   0.657  43.024  1.00 57.44           N  
ANISOU  447  NE  ARG A  96     9576   7472   4775     46    675    325       N  
ATOM    448  CZ  ARG A  96     -15.718   1.404  44.086  1.00 59.25           C  
ANISOU  448  CZ  ARG A  96    10125   7681   4707      6    831    291       C  
ATOM    449  NH1 ARG A  96     -16.974   1.466  44.508  1.00 59.90           N  
ANISOU  449  NH1 ARG A  96    10323   7651   4787   -161   1337    278       N  
ATOM    450  NH2 ARG A  96     -14.783   2.095  44.722  1.00 57.32           N  
ANISOU  450  NH2 ARG A  96    10065   7518   4196    126    494    236       N  
ATOM    451  N   VAL A  97     -15.324  -2.019  38.054  1.00 41.24           N  
ANISOU  451  N   VAL A  97     6136   5511   4022     50    437    215       N  
ATOM    452  CA  VAL A  97     -16.192  -2.869  37.233  1.00 42.09           C  
ANISOU  452  CA  VAL A  97     6059   5530   4405    -49    616    170       C  
ATOM    453  C   VAL A  97     -16.885  -3.879  38.095  1.00 42.31           C  
ANISOU  453  C   VAL A  97     6407   5288   4380   -141    901    283       C  
ATOM    454  O   VAL A  97     -16.224  -4.614  38.825  1.00 42.00           O  
ANISOU  454  O   VAL A  97     6731   5095   4133    -49    812    432       O  
ATOM    455  CB  VAL A  97     -15.419  -3.653  36.135  1.00 44.71           C  
ANISOU  455  CB  VAL A  97     6204   5884   4900     45    390    126       C  
ATOM    456  CG1 VAL A  97     -16.412  -4.406  35.254  1.00 42.83           C  
ANISOU  456  CG1 VAL A  97     5764   5565   4945    -69    554     31       C  
ATOM    457  CG2 VAL A  97     -14.603  -2.718  35.298  1.00 43.88           C  
ANISOU  457  CG2 VAL A  97     5838   6010   4824    125    166     27       C  
ATOM    458  N   THR A  98     -18.208  -3.924  38.008  1.00 42.14           N  
ANISOU  458  N   THR A  98     6256   5186   4570   -318   1242    204       N  
ATOM    459  CA  THR A  98     -18.983  -4.827  38.844  1.00 49.46           C  
ANISOU  459  CA  THR A  98     7480   5821   5490   -456   1623    295       C  
ATOM    460  C   THR A  98     -20.077  -5.496  38.016  1.00 52.20           C  
ANISOU  460  C   THR A  98     7489   6060   6284   -618   1840    143       C  
ATOM    461  O   THR A  98     -20.599  -4.901  37.074  1.00 54.32           O  
ANISOU  461  O   THR A  98     7319   6495   6824   -644   1762    -49       O  
ATOM    462  CB  THR A  98     -19.631  -4.080  40.028  1.00 58.99           C  
ANISOU  462  CB  THR A  98     8940   6979   6494   -557   1958    323       C  
ATOM    463  OG1 THR A  98     -20.489  -3.058  39.511  1.00 62.76           O  
ANISOU  463  OG1 THR A  98     8990   7613   7242   -639   2062    121       O  
ATOM    464  CG2 THR A  98     -18.575  -3.426  40.916  1.00 59.23           C  
ANISOU  464  CG2 THR A  98     9339   7102   6063   -398   1712    442       C  
ATOM    465  N   GLN A  99     -20.420  -6.728  38.362  1.00 53.29           N  
ANISOU  465  N   GLN A  99     7844   5900   6505   -719   2090    222       N  
ATOM    466  CA  GLN A  99     -21.403  -7.497  37.602  1.00 53.42           C  
ANISOU  466  CA  GLN A  99     7534   5774   6989   -885   2282     48       C  
ATOM    467  C   GLN A  99     -22.780  -7.377  38.229  1.00 55.44           C  
ANISOU  467  C   GLN A  99     7738   5854   7471  -1128   2810    -44       C  
ATOM    468  O   GLN A  99     -22.952  -7.666  39.397  1.00 57.95           O  
ANISOU  468  O   GLN A  99     8497   5942   7578  -1220   3183    118       O  
ATOM    469  CB  GLN A  99     -20.981  -8.964  37.522  1.00 56.06           C  
ANISOU  469  CB  GLN A  99     8092   5843   7366   -873   2271    154       C  
ATOM    470  CG  GLN A  99     -21.942  -9.864  36.745  1.00 59.38           C  
ANISOU  470  CG  GLN A  99     8186   6081   8293  -1056   2456    -52       C  
ATOM    471  CD  GLN A  99     -21.483 -11.304  36.736  1.00 64.04           C  
ANISOU  471  CD  GLN A  99     9038   6371   8923  -1041   2463     61       C  
ATOM    472  OE1 GLN A  99     -21.051 -11.827  37.765  1.00 68.35           O  
ANISOU  472  OE1 GLN A  99    10112   6676   9180  -1007   2604    326       O  
ATOM    473  NE2 GLN A  99     -21.558 -11.952  35.573  1.00 62.25           N  
ANISOU  473  NE2 GLN A  99     8480   6141   9033  -1049   2290   -142       N  
ATOM    474  N   LEU A 100     -23.765  -6.946  37.457  1.00 55.90           N  
ANISOU  474  N   LEU A 100     7269   6004   7965  -1224   2846   -317       N  
ATOM    475  CA  LEU A 100     -25.113  -6.745  38.005  1.00 58.90           C  
ANISOU  475  CA  LEU A 100     7493   6221   8666  -1453   3357   -468       C  
ATOM    476  C   LEU A 100     -25.831  -8.087  38.182  1.00 62.43           C  
ANISOU  476  C   LEU A 100     7979   6289   9454  -1686   3777   -508       C  
ATOM    477  O   LEU A 100     -25.315  -9.123  37.762  1.00 63.47           O  
ANISOU  477  O   LEU A 100     8222   6304   9589  -1652   3615   -436       O  
ATOM    478  CB  LEU A 100     -25.916  -5.798  37.109  1.00 61.88           C  
ANISOU  478  CB  LEU A 100     7258   6808   9444  -1440   3187   -771       C  
ATOM    479  CG  LEU A 100     -25.262  -4.440  36.827  1.00 63.14           C  
ANISOU  479  CG  LEU A 100     7370   7305   9315  -1222   2791   -736       C  
ATOM    480  CD1 LEU A 100     -26.349  -3.487  36.371  1.00 65.89           C  
ANISOU  480  CD1 LEU A 100     7214   7745  10077  -1244   2793  -1012       C  
ATOM    481  CD2 LEU A 100     -24.507  -3.876  38.044  1.00 63.96           C  
ANISOU  481  CD2 LEU A 100     7978   7438   8887  -1160   2904   -495       C  
ATOM    482  N   PRO A 101     -26.998  -8.089  38.852  1.00 66.52           N  
ANISOU  482  N   PRO A 101     8452   6627  10197  -1814   4163   -645       N  
ATOM    483  CA  PRO A 101     -27.619  -9.381  39.164  1.00 71.13           C  
ANISOU  483  CA  PRO A 101     9160   6854  11011  -1959   4495   -678       C  
ATOM    484  C   PRO A 101     -28.000 -10.246  37.963  1.00 74.24           C  
ANISOU  484  C   PRO A 101     9103   7180  11926  -2027   4335   -909       C  
ATOM    485  O   PRO A 101     -27.903 -11.467  38.073  1.00 77.58           O  
ANISOU  485  O   PRO A 101     9745   7331  12400  -2107   4498   -829       O  
ATOM    486  CB  PRO A 101     -28.874  -8.972  39.943  1.00 72.60           C  
ANISOU  486  CB  PRO A 101     9271   6918  11397  -2046   4872   -864       C  
ATOM    487  CG  PRO A 101     -28.472  -7.708  40.646  1.00 69.54           C  
ANISOU  487  CG  PRO A 101     9105   6730  10587  -1939   4821   -743       C  
ATOM    488  CD  PRO A 101     -27.603  -6.992  39.639  1.00 66.07           C  
ANISOU  488  CD  PRO A 101     8408   6638  10058  -1794   4325   -716       C  
ATOM    489  N   ASN A 102     -28.412  -9.654  36.845  1.00 72.16           N  
ANISOU  489  N   ASN A 102     8259   7146  12013  -1974   3988  -1194       N  
ATOM    490  CA  ASN A 102     -28.873 -10.474  35.718  1.00 74.37           C  
ANISOU  490  CA  ASN A 102     8131   7361  12767  -2016   3786  -1463       C  
ATOM    491  C   ASN A 102     -27.755 -11.252  35.028  1.00 72.75           C  
ANISOU  491  C   ASN A 102     8053   7146  12444  -1997   3527  -1340       C  
ATOM    492  O   ASN A 102     -28.008 -12.069  34.150  1.00 76.70           O  
ANISOU  492  O   ASN A 102     8301   7562  13278  -2029   3360  -1550       O  
ATOM    493  CB  ASN A 102     -29.622  -9.613  34.692  1.00 73.02           C  
ANISOU  493  CB  ASN A 102     7381   7429  12936  -1911   3398  -1800       C  
ATOM    494  CG  ASN A 102     -28.748  -8.569  34.030  1.00 67.03           C  
ANISOU  494  CG  ASN A 102     6538   7032  11899  -1741   2943  -1730       C  
ATOM    495  OD1 ASN A 102     -27.529  -8.716  33.929  1.00 65.91           O  
ANISOU  495  OD1 ASN A 102     6652   6982  11409  -1693   2809  -1509       O  
ATOM    496  ND2 ASN A 102     -29.376  -7.496  33.567  1.00 65.24           N  
ANISOU  496  ND2 ASN A 102     5980   6996  11814  -1616   2682  -1920       N  
ATOM    497  N   GLY A 103     -26.517 -10.982  35.423  1.00 68.04           N  
ANISOU  497  N   GLY A 103     7885   6653  11314  -1866   3410  -1016       N  
ATOM    498  CA  GLY A 103     -25.378 -11.725  34.914  1.00 66.51           C  
ANISOU  498  CA  GLY A 103     7927   6472  10871  -1695   3055   -877       C  
ATOM    499  C   GLY A 103     -24.757 -11.190  33.634  1.00 63.73           C  
ANISOU  499  C   GLY A 103     7303   6488  10424  -1467   2454  -1007       C  
ATOM    500  O   GLY A 103     -23.588 -11.472  33.355  1.00 65.17           O  
ANISOU  500  O   GLY A 103     7716   6751  10295  -1280   2165   -859       O  
ATOM    501  N   ARG A 104     -25.507 -10.424  32.845  1.00 61.46           N  
ANISOU  501  N   ARG A 104     6543   6405  10403  -1469   2266  -1287       N  
ATOM    502  CA  ARG A 104     -24.982 -10.018  31.532  1.00 57.81           C  
ANISOU  502  CA  ARG A 104     5889   6246   9831  -1266   1723  -1414       C  
ATOM    503  C   ARG A 104     -24.679  -8.532  31.439  1.00 49.81           C  
ANISOU  503  C   ARG A 104     4838   5564   8523  -1097   1491  -1347       C  
ATOM    504  O   ARG A 104     -23.992  -8.098  30.518  1.00 45.47           O  
ANISOU  504  O   ARG A 104     4270   5255   7753   -916   1100  -1362       O  
ATOM    505  CB  ARG A 104     -25.945 -10.422  30.421  1.00 61.80           C  
ANISOU  505  CB  ARG A 104     5941   6714  10826  -1348   1548  -1803       C  
ATOM    506  CG  ARG A 104     -27.335  -9.902  30.613  1.00 63.43           C  
ANISOU  506  CG  ARG A 104     5740   6868  11494  -1496   1721  -2044       C  
ATOM    507  CD  ARG A 104     -28.260 -10.382  29.518  1.00 68.74           C  
ANISOU  507  CD  ARG A 104     6012   7497  12610  -1509   1457  -2432       C  
ATOM    508  NE  ARG A 104     -29.649 -10.078  29.856  1.00 72.02           N  
ANISOU  508  NE  ARG A 104     6188   7812  13364  -1529   1629  -2601       N  
ATOM    509  CZ  ARG A 104     -30.163  -8.862  29.752  1.00 73.38           C  
ANISOU  509  CZ  ARG A 104     6194   8158  13530  -1395   1449  -2663       C  
ATOM    510  NH1 ARG A 104     -29.395  -7.868  29.311  1.00 71.31           N  
ANISOU  510  NH1 ARG A 104     5996   8189  12911  -1228   1106  -2547       N  
ATOM    511  NH2 ARG A 104     -31.430  -8.637  30.089  1.00 75.78           N  
ANISOU  511  NH2 ARG A 104     6273   8321  14198  -1422   1623  -2850       N  
ATOM    512  N   ASP A 105     -25.148  -7.763  32.418  1.00 49.77           N  
ANISOU  512  N   ASP A 105     4861   5547   8503  -1163   1771  -1269       N  
ATOM    513  CA  ASP A 105     -24.821  -6.340  32.496  1.00 50.67           C  
ANISOU  513  CA  ASP A 105     4984   5932   8337  -1012   1598  -1187       C  
ATOM    514  C   ASP A 105     -23.700  -6.076  33.526  1.00 49.16           C  
ANISOU  514  C   ASP A 105     5259   5773   7648   -932   1688   -863       C  
ATOM    515  O   ASP A 105     -23.596  -6.782  34.541  1.00 50.64           O  
ANISOU  515  O   ASP A 105     5765   5733   7742  -1028   2007   -704       O  
ATOM    516  CB  ASP A 105     -26.081  -5.509  32.845  1.00 54.34           C  
ANISOU  516  CB  ASP A 105     5135   6377   9135  -1108   1803  -1363       C  
ATOM    517  CG  ASP A 105     -27.136  -5.539  31.735  1.00 61.72           C  
ANISOU  517  CG  ASP A 105     5557   7321  10571  -1124   1569  -1719       C  
ATOM    518  OD1 ASP A 105     -26.763  -5.703  30.557  1.00 61.59           O  
ANISOU  518  OD1 ASP A 105     5475   7438  10487   -994   1138  -1801       O  
ATOM    519  OD2 ASP A 105     -28.346  -5.412  32.035  1.00 68.95           O  
ANISOU  519  OD2 ASP A 105     6194   8097  11906  -1233   1783  -1918       O  
ATOM    520  N   PHE A 106     -22.867  -5.072  33.238  1.00 46.08           N  
ANISOU  520  N   PHE A 106     4920   5643   6947   -754   1393   -779       N  
ATOM    521  CA  PHE A 106     -21.722  -4.683  34.075  1.00 40.92           C  
ANISOU  521  CA  PHE A 106     4637   5054   5855   -651   1371   -531       C  
ATOM    522  C   PHE A 106     -21.691  -3.186  34.224  1.00 43.39           C  
ANISOU  522  C   PHE A 106     4886   5568   6031   -578   1290   -530       C  
ATOM    523  O   PHE A 106     -21.726  -2.466  33.217  1.00 45.14           O  
ANISOU  523  O   PHE A 106     4866   5967   6317   -491   1031   -638       O  
ATOM    524  CB  PHE A 106     -20.381  -5.153  33.475  1.00 32.17           C  
ANISOU  524  CB  PHE A 106     3655   4030   4539   -497   1061   -444       C  
ATOM    525  CG  PHE A 106     -20.295  -6.618  33.342  1.00 38.54           C  
ANISOU  525  CG  PHE A 106     4551   4619   5475   -542   1121   -441       C  
ATOM    526  CD1 PHE A 106     -20.886  -7.256  32.262  1.00 38.88           C  
ANISOU  526  CD1 PHE A 106     4321   4622   5830   -599   1051   -654       C  
ATOM    527  CD2 PHE A 106     -19.694  -7.379  34.326  1.00 38.77           C  
ANISOU  527  CD2 PHE A 106     4958   4451   5322   -525   1238   -236       C  
ATOM    528  CE1 PHE A 106     -20.834  -8.640  32.144  1.00 42.56           C  
ANISOU  528  CE1 PHE A 106     4868   4853   6451   -653   1125   -672       C  
ATOM    529  CE2 PHE A 106     -19.654  -8.780  34.229  1.00 43.16           C  
ANISOU  529  CE2 PHE A 106     5622   4751   6026   -564   1311   -223       C  
ATOM    530  CZ  PHE A 106     -20.229  -9.405  33.136  1.00 44.62           C  
ANISOU  530  CZ  PHE A 106     5506   4895   6553   -639   1274   -447       C  
ATOM    531  N   HIS A 107     -21.624  -2.700  35.458  1.00 41.04           N  
ANISOU  531  N   HIS A 107     4842   5228   5525   -607   1508   -410       N  
ATOM    532  CA  HIS A 107     -21.315  -1.283  35.652  1.00 39.78           C  
ANISOU  532  CA  HIS A 107     4676   5251   5186   -519   1398   -396       C  
ATOM    533  C   HIS A 107     -19.800  -1.019  35.544  1.00 38.66           C  
ANISOU  533  C   HIS A 107     4718   5256   4716   -365   1087   -264       C  
ATOM    534  O   HIS A 107     -19.000  -1.639  36.229  1.00 36.62           O  
ANISOU  534  O   HIS A 107     4762   4920   4231   -328   1071   -124       O  
ATOM    535  CB  HIS A 107     -21.857  -0.791  37.005  1.00 45.04           C  
ANISOU  535  CB  HIS A 107     5542   5817   5756   -613   1758   -366       C  
ATOM    536  CG  HIS A 107     -23.304  -0.412  36.967  1.00 52.22           C  
ANISOU  536  CG  HIS A 107     6133   6652   7055   -732   2030   -565       C  
ATOM    537  ND1 HIS A 107     -24.039  -0.144  38.101  1.00 57.48           N  
ANISOU  537  ND1 HIS A 107     6925   7179   7734   -858   2468   -595       N  
ATOM    538  CD2 HIS A 107     -24.157  -0.270  35.923  1.00 53.31           C  
ANISOU  538  CD2 HIS A 107     5824   6825   7608   -733   1914   -770       C  
ATOM    539  CE1 HIS A 107     -25.278   0.164  37.756  1.00 59.47           C  
ANISOU  539  CE1 HIS A 107     6762   7382   8452   -935   2631   -826       C  
ATOM    540  NE2 HIS A 107     -25.382   0.071  36.445  1.00 58.49           N  
ANISOU  540  NE2 HIS A 107     6283   7358   8582   -853   2266   -935       N  
ATOM    541  N   MET A 108     -19.427  -0.102  34.659  1.00 33.60           N  
ANISOU  541  N   MET A 108     3887   4802   4079   -272    841   -320       N  
ATOM    542  CA AMET A 108     -18.042   0.349  34.555  0.73 34.55           C  
ANISOU  542  CA AMET A 108     4112   5051   3964   -155    605   -240       C  
ATOM    543  CA BMET A 108     -18.045   0.370  34.532  0.27 34.11           C  
ANISOU  543  CA BMET A 108     4051   4998   3911   -154    602   -242       C  
ATOM    544  C   MET A 108     -18.015   1.814  34.977  1.00 34.88           C  
ANISOU  544  C   MET A 108     4154   5185   3912   -137    608   -251       C  
ATOM    545  O   MET A 108     -18.599   2.672  34.310  1.00 33.13           O  
ANISOU  545  O   MET A 108     3728   5027   3831   -130    580   -335       O  
ATOM    546  CB AMET A 108     -17.519   0.142  33.130  0.73 33.13           C  
ANISOU  546  CB AMET A 108     3759   4971   3856    -84    382   -296       C  
ATOM    547  CB BMET A 108     -17.529   0.269  33.093  0.27 32.64           C  
ANISOU  547  CB BMET A 108     3686   4922   3793    -82    376   -300       C  
ATOM    548  CG AMET A 108     -17.668  -1.320  32.722  0.73 35.17           C  
ANISOU  548  CG AMET A 108     4009   5115   4238   -109    396   -322       C  
ATOM    549  CG BMET A 108     -16.988  -1.085  32.705  0.27 33.74           C  
ANISOU  549  CG BMET A 108     3870   4991   3960    -57    312   -289       C  
ATOM    550  SD AMET A 108     -17.063  -1.780  31.097  0.73 41.12           S  
ANISOU  550  SD AMET A 108     4624   5959   5042    -33    182   -419       S  
ATOM    551  SD BMET A 108     -18.292  -2.298  32.503  0.27 36.80           S  
ANISOU  551  SD BMET A 108     4168   5202   4612   -172    475   -377       S  
ATOM    552  CE AMET A 108     -16.895  -3.545  31.344  0.73 39.78           C  
ANISOU  552  CE AMET A 108     4560   5588   4966    -54    243   -404       C  
ATOM    553  CE BMET A 108     -17.355  -3.671  31.842  0.27 39.03           C  
ANISOU  553  CE BMET A 108     4504   5420   4907   -106    344   -380       C  
ATOM    554  N   SER A 109     -17.376   2.088  36.105  1.00 31.74           N  
ANISOU  554  N   SER A 109     4006   4772   3280   -121    623   -177       N  
ATOM    555  CA  SER A 109     -17.480   3.418  36.689  1.00 32.08           C  
ANISOU  555  CA  SER A 109     4079   4865   3245   -126    672   -215       C  
ATOM    556  C   SER A 109     -16.148   4.084  36.863  1.00 33.21           C  
ANISOU  556  C   SER A 109     4297   5103   3219    -47    444   -198       C  
ATOM    557  O   SER A 109     -15.198   3.453  37.319  1.00 31.34           O  
ANISOU  557  O   SER A 109     4228   4847   2831      9    300   -140       O  
ATOM    558  CB  SER A 109     -18.167   3.348  38.071  1.00 34.28           C  
ANISOU  558  CB  SER A 109     4614   5017   3394   -206    959   -201       C  
ATOM    559  OG  SER A 109     -19.447   2.783  37.973  1.00 37.08           O  
ANISOU  559  OG  SER A 109     4855   5256   3979   -309   1234   -253       O  
ATOM    560  N   VAL A 110     -16.090   5.356  36.493  1.00 33.21           N  
ANISOU  560  N   VAL A 110     4159   5179   3281    -40    403   -262       N  
ATOM    561  CA  VAL A 110     -15.059   6.250  36.993  1.00 32.84           C  
ANISOU  561  CA  VAL A 110     4187   5180   3109     -9    267   -291       C  
ATOM    562  C   VAL A 110     -15.515   6.692  38.402  1.00 31.69           C  
ANISOU  562  C   VAL A 110     4285   4970   2785    -45    411   -322       C  
ATOM    563  O   VAL A 110     -16.566   7.332  38.524  1.00 31.04           O  
ANISOU  563  O   VAL A 110     4148   4849   2795    -95    621   -378       O  
ATOM    564  CB  VAL A 110     -14.891   7.481  36.132  1.00 31.92           C  
ANISOU  564  CB  VAL A 110     3878   5121   3131     -7    224   -343       C  
ATOM    565  CG1 VAL A 110     -13.708   8.297  36.685  1.00 30.11           C  
ANISOU  565  CG1 VAL A 110     3700   4916   2825      0     88   -404       C  
ATOM    566  CG2 VAL A 110     -14.666   7.099  34.658  1.00 32.57           C  
ANISOU  566  CG2 VAL A 110     3786   5250   3340     19    149   -314       C  
ATOM    567  N   VAL A 111     -14.781   6.326  39.444  1.00 32.38           N  
ANISOU  567  N   VAL A 111     4652   5031   2621     -9    298   -298       N  
ATOM    568  CA  VAL A 111     -15.310   6.506  40.807  1.00 33.76           C  
ANISOU  568  CA  VAL A 111     5162   5121   2544    -46    476   -315       C  
ATOM    569  C   VAL A 111     -15.453   7.977  41.167  1.00 35.58           C  
ANISOU  569  C   VAL A 111     5362   5376   2779    -76    532   -451       C  
ATOM    570  O   VAL A 111     -16.511   8.389  41.679  1.00 32.39           O  
ANISOU  570  O   VAL A 111     5032   4905   2370   -142    835   -507       O  
ATOM    571  CB  VAL A 111     -14.469   5.762  41.825  1.00 37.11           C  
ANISOU  571  CB  VAL A 111     5969   5494   2637     32    282   -249       C  
ATOM    572  CG1 VAL A 111     -14.921   6.093  43.267  1.00 40.92           C  
ANISOU  572  CG1 VAL A 111     6892   5888   2768     -1    461   -276       C  
ATOM    573  CG2 VAL A 111     -14.570   4.247  41.545  1.00 35.93           C  
ANISOU  573  CG2 VAL A 111     5890   5260   2502     55    302   -102       C  
ATOM    574  N   ARG A 112     -14.443   8.777  40.844  1.00 32.56           N  
ANISOU  574  N   ARG A 112     4839   5070   2464    -38    281   -525       N  
ATOM    575  CA  ARG A 112     -14.539  10.227  41.027  1.00 34.44           C  
ANISOU  575  CA  ARG A 112     5013   5304   2769    -73    331   -662       C  
ATOM    576  C   ARG A 112     -14.057  10.952  39.757  1.00 34.54           C  
ANISOU  576  C   ARG A 112     4686   5362   3075    -74    227   -678       C  
ATOM    577  O   ARG A 112     -12.860  11.079  39.525  1.00 35.15           O  
ANISOU  577  O   ARG A 112     4680   5480   3194    -56      2   -715       O  
ATOM    578  CB  ARG A 112     -13.717  10.687  42.248  1.00 37.82           C  
ANISOU  578  CB  ARG A 112     5716   5724   2930    -51    151   -779       C  
ATOM    579  CG  ARG A 112     -14.139  10.079  43.565  1.00 46.73           C  
ANISOU  579  CG  ARG A 112     7297   6785   3674    -43    262   -755       C  
ATOM    580  CD  ARG A 112     -13.240  10.515  44.766  1.00 45.63           C  
ANISOU  580  CD  ARG A 112     7488   6640   3209     10     -9   -890       C  
ATOM    581  NE  ARG A 112     -13.762   9.942  46.011  1.00 55.86           N  
ANISOU  581  NE  ARG A 112     9318   7846   4060     17    150   -844       N  
ATOM    582  CZ  ARG A 112     -14.514  10.599  46.896  1.00 60.76           C  
ANISOU  582  CZ  ARG A 112    10157   8401   4527    -45    436   -941       C  
ATOM    583  NH1 ARG A 112     -14.833  11.875  46.696  1.00 60.00           N  
ANISOU  583  NH1 ARG A 112     9880   8312   4606   -109    574  -1126       N  
ATOM    584  NH2 ARG A 112     -14.941   9.983  47.992  1.00 67.02           N  
ANISOU  584  NH2 ARG A 112    11291   9100   5072    -41    584   -843       N  
ATOM    585  N   ALA A 113     -14.986  11.437  38.942  1.00 30.42           N  
ANISOU  585  N   ALA A 113     3981   4812   2766    -90    393   -658       N  
ATOM    586  CA  ALA A 113     -14.627  11.937  37.609  1.00 26.49           C  
ANISOU  586  CA  ALA A 113     3251   4331   2482    -80    317   -622       C  
ATOM    587  C   ALA A 113     -13.811  13.207  37.688  1.00 29.11           C  
ANISOU  587  C   ALA A 113     3553   4625   2884   -112    252   -720       C  
ATOM    588  O   ALA A 113     -14.085  14.072  38.505  1.00 33.62           O  
ANISOU  588  O   ALA A 113     4215   5132   3428   -135    322   -829       O  
ATOM    589  CB  ALA A 113     -15.876  12.171  36.792  1.00 30.39           C  
ANISOU  589  CB  ALA A 113     3611   4780   3156    -54    448   -583       C  
ATOM    590  N   ARG A 114     -12.758  13.277  36.876  1.00 30.87           N  
ANISOU  590  N   ARG A 114     3651   4871   3209   -129    144   -703       N  
ATOM    591  CA  ARG A 114     -11.941  14.474  36.732  1.00 32.61           C  
ANISOU  591  CA  ARG A 114     3799   5021   3572   -192    129   -797       C  
ATOM    592  C   ARG A 114     -12.187  15.053  35.347  1.00 30.47           C  
ANISOU  592  C   ARG A 114     3444   4678   3455   -198    246   -688       C  
ATOM    593  O   ARG A 114     -12.519  14.310  34.425  1.00 32.29           O  
ANISOU  593  O   ARG A 114     3649   4958   3663   -152    256   -566       O  
ATOM    594  CB  ARG A 114     -10.439  14.159  36.875  1.00 34.69           C  
ANISOU  594  CB  ARG A 114     3969   5328   3885   -225    -45   -894       C  
ATOM    595  CG  ARG A 114     -10.057  13.492  38.183  1.00 39.36           C  
ANISOU  595  CG  ARG A 114     4690   5977   4288   -177   -254   -988       C  
ATOM    596  CD  ARG A 114      -8.699  12.801  38.038  1.00 45.78           C  
ANISOU  596  CD  ARG A 114     5351   6839   5205   -155   -473  -1057       C  
ATOM    597  NE  ARG A 114      -8.314  12.206  39.314  1.00 53.81           N  
ANISOU  597  NE  ARG A 114     6543   7886   6017    -71   -746  -1141       N  
ATOM    598  CZ  ARG A 114      -7.175  11.557  39.538  1.00 58.39           C  
ANISOU  598  CZ  ARG A 114     7026   8491   6667     -2  -1035  -1235       C  
ATOM    599  NH1 ARG A 114      -6.287  11.407  38.555  1.00 55.66           N  
ANISOU  599  NH1 ARG A 114     6362   8150   6635    -30  -1029  -1279       N  
ATOM    600  NH2 ARG A 114      -6.925  11.071  40.752  1.00 59.80           N  
ANISOU  600  NH2 ARG A 114     7445   8674   6602    105  -1327  -1294       N  
ATOM    601  N   ARG A 115     -12.018  16.363  35.192  1.00 32.26           N  
ANISOU  601  N   ARG A 115     3667   4770   3819   -249    325   -734       N  
ATOM    602  CA  ARG A 115     -12.139  16.972  33.872  1.00 33.33           C  
ANISOU  602  CA  ARG A 115     3809   4797   4056   -247    432   -605       C  
ATOM    603  C   ARG A 115     -11.336  16.174  32.824  1.00 36.23           C  
ANISOU  603  C   ARG A 115     4126   5234   4406   -273    442   -525       C  
ATOM    604  O   ARG A 115     -11.831  15.953  31.714  1.00 33.03           O  
ANISOU  604  O   ARG A 115     3793   4818   3939   -214    480   -380       O  
ATOM    605  CB  ARG A 115     -11.680  18.437  33.886  1.00 34.75           C  
ANISOU  605  CB  ARG A 115     4010   4786   4408   -333    536   -672       C  
ATOM    606  CG  ARG A 115     -12.572  19.384  34.677  1.00 37.98           C  
ANISOU  606  CG  ARG A 115     4485   5081   4866   -293    564   -749       C  
ATOM    607  CD  ARG A 115     -14.011  19.486  34.099  1.00 35.98           C  
ANISOU  607  CD  ARG A 115     4289   4770   4613   -147    581   -615       C  
ATOM    608  NE  ARG A 115     -14.013  19.699  32.657  1.00 33.91           N  
ANISOU  608  NE  ARG A 115     4106   4414   4363   -104    601   -427       N  
ATOM    609  CZ  ARG A 115     -13.806  20.873  32.063  1.00 34.28           C  
ANISOU  609  CZ  ARG A 115     4271   4234   4519   -123    695   -359       C  
ATOM    610  NH1 ARG A 115     -13.591  21.975  32.769  1.00 34.88           N  
ANISOU  610  NH1 ARG A 115     4351   4147   4755   -190    777   -483       N  
ATOM    611  NH2 ARG A 115     -13.829  20.949  30.751  1.00 38.97           N  
ANISOU  611  NH2 ARG A 115     5021   4741   5044    -72    713   -165       N  
ATOM    612  N   ASP A 116     -10.117  15.720  33.153  1.00 26.58           N  
ANISOU  612  N   ASP A 116     2781   4076   3242   -345    394   -638       N  
ATOM    613  CA  ASP A 116      -9.325  15.073  32.133  1.00 31.95           C  
ANISOU  613  CA  ASP A 116     3391   4792   3957   -376    461   -597       C  
ATOM    614  C   ASP A 116      -9.781  13.654  31.856  1.00 33.78           C  
ANISOU  614  C   ASP A 116     3635   5166   4035   -277    367   -518       C  
ATOM    615  O   ASP A 116      -9.182  12.990  31.032  1.00 35.83           O  
ANISOU  615  O   ASP A 116     3844   5461   4309   -288    423   -502       O  
ATOM    616  CB  ASP A 116      -7.823  15.076  32.491  1.00 40.25           C  
ANISOU  616  CB  ASP A 116     4236   5838   5220   -479    444   -785       C  
ATOM    617  CG  ASP A 116      -7.576  14.572  33.906  1.00 52.11           C  
ANISOU  617  CG  ASP A 116     5673   7435   6693   -429    176   -934       C  
ATOM    618  OD1 ASP A 116      -7.538  15.407  34.824  1.00 60.35           O  
ANISOU  618  OD1 ASP A 116     6735   8420   7777   -465    107  -1058       O  
ATOM    619  OD2 ASP A 116      -7.470  13.350  34.106  1.00 56.74           O  
ANISOU  619  OD2 ASP A 116     6236   8135   7189   -343     29   -923       O  
ATOM    620  N   ASP A 117     -10.848  13.181  32.497  1.00 31.31           N  
ANISOU  620  N   ASP A 117     3388   4911   3596   -192    265   -483       N  
ATOM    621  CA  ASP A 117     -11.400  11.886  32.101  1.00 29.12           C  
ANISOU  621  CA  ASP A 117     3125   4727   3212   -116    210   -408       C  
ATOM    622  C   ASP A 117     -12.318  11.994  30.876  1.00 33.46           C  
ANISOU  622  C   ASP A 117     3755   5245   3713    -63    260   -291       C  
ATOM    623  O   ASP A 117     -12.712  10.976  30.321  1.00 32.02           O  
ANISOU  623  O   ASP A 117     3575   5126   3465    -11    212   -254       O  
ATOM    624  CB  ASP A 117     -12.208  11.248  33.214  1.00 26.65           C  
ANISOU  624  CB  ASP A 117     2858   4458   2810    -69    133   -423       C  
ATOM    625  CG  ASP A 117     -11.366  10.735  34.351  1.00 31.91           C  
ANISOU  625  CG  ASP A 117     3529   5162   3433    -74     12   -511       C  
ATOM    626  OD1 ASP A 117     -10.331  10.057  34.115  1.00 30.96           O  
ANISOU  626  OD1 ASP A 117     3322   5080   3363    -66    -73   -545       O  
ATOM    627  OD2 ASP A 117     -11.774  11.000  35.513  1.00 32.13           O  
ANISOU  627  OD2 ASP A 117     3668   5171   3369    -72     -7   -557       O  
ATOM    628  N   SER A 118     -12.708  13.210  30.495  1.00 31.63           N  
ANISOU  628  N   SER A 118     3606   4899   3513    -59    321   -242       N  
ATOM    629  CA  SER A 118     -13.559  13.367  29.316  1.00 29.71           C  
ANISOU  629  CA  SER A 118     3482   4605   3200     30    294   -130       C  
ATOM    630  C   SER A 118     -12.893  12.718  28.096  1.00 30.75           C  
ANISOU  630  C   SER A 118     3693   4774   3216     17    343    -80       C  
ATOM    631  O   SER A 118     -11.706  12.912  27.844  1.00 34.08           O  
ANISOU  631  O   SER A 118     4114   5169   3665    -83    497   -102       O  
ATOM    632  CB  SER A 118     -13.838  14.831  29.007  1.00 27.79           C  
ANISOU  632  CB  SER A 118     3367   4188   3003     50    346    -65       C  
ATOM    633  OG  SER A 118     -14.514  15.469  30.040  1.00 34.25           O  
ANISOU  633  OG  SER A 118     4118   4955   3942     73    323   -133       O  
ATOM    634  N   GLY A 119     -13.659  11.936  27.362  1.00 29.87           N  
ANISOU  634  N   GLY A 119     3635   4716   3000    109    226    -46       N  
ATOM    635  CA  GLY A 119     -13.121  11.261  26.199  1.00 32.11           C  
ANISOU  635  CA  GLY A 119     4030   5034   3137    105    276    -24       C  
ATOM    636  C   GLY A 119     -13.982  10.127  25.708  1.00 33.96           C  
ANISOU  636  C   GLY A 119     4259   5350   3295    198    101    -52       C  
ATOM    637  O   GLY A 119     -15.163  10.001  26.056  1.00 32.98           O  
ANISOU  637  O   GLY A 119     4053   5230   3247    275    -65    -76       O  
ATOM    638  N   THR A 120     -13.345   9.252  24.949  1.00 34.08           N  
ANISOU  638  N   THR A 120     4327   5419   3203    177    162    -85       N  
ATOM    639  CA  THR A 120     -14.018   8.170  24.270  1.00 34.03           C  
ANISOU  639  CA  THR A 120     4350   5470   3109    252      7   -136       C  
ATOM    640  C   THR A 120     -13.763   6.833  24.941  1.00 33.41           C  
ANISOU  640  C   THR A 120     4063   5471   3160    214      5   -239       C  
ATOM    641  O   THR A 120     -12.618   6.521  25.251  1.00 31.96           O  
ANISOU  641  O   THR A 120     3802   5306   3034    147    148   -274       O  
ATOM    642  CB  THR A 120     -13.526   8.140  22.829  1.00 36.48           C  
ANISOU  642  CB  THR A 120     4941   5757   3162    266     93   -111       C  
ATOM    643  OG1 THR A 120     -13.789   9.425  22.269  1.00 40.75           O  
ANISOU  643  OG1 THR A 120     5743   6183   3558    312     91     20       O  
ATOM    644  CG2 THR A 120     -14.193   7.034  22.024  1.00 37.74           C  
ANISOU  644  CG2 THR A 120     5166   5972   3203    348    -95   -199       C  
ATOM    645  N   TYR A 121     -14.811   6.041  25.156  1.00 30.08           N  
ANISOU  645  N   TYR A 121     3544   5069   2816    260   -156   -297       N  
ATOM    646  CA  TYR A 121     -14.681   4.788  25.921  1.00 31.49           C  
ANISOU  646  CA  TYR A 121     3565   5273   3125    222   -143   -366       C  
ATOM    647  C   TYR A 121     -15.399   3.651  25.236  1.00 34.73           C  
ANISOU  647  C   TYR A 121     3963   5686   3546    257   -263   -463       C  
ATOM    648  O   TYR A 121     -16.335   3.882  24.477  1.00 35.79           O  
ANISOU  648  O   TYR A 121     4151   5811   3638    321   -422   -498       O  
ATOM    649  CB  TYR A 121     -15.259   4.917  27.338  1.00 27.88           C  
ANISOU  649  CB  TYR A 121     2984   4790   2820    193   -137   -350       C  
ATOM    650  CG  TYR A 121     -14.530   5.881  28.248  1.00 31.05           C  
ANISOU  650  CG  TYR A 121     3388   5185   3225    152    -45   -296       C  
ATOM    651  CD1 TYR A 121     -14.680   7.250  28.116  1.00 30.61           C  
ANISOU  651  CD1 TYR A 121     3388   5096   3146    160    -27   -248       C  
ATOM    652  CD2 TYR A 121     -13.652   5.403  29.227  1.00 30.66           C  
ANISOU  652  CD2 TYR A 121     3300   5142   3207    119     -7   -306       C  
ATOM    653  CE1 TYR A 121     -13.969   8.141  28.981  1.00 31.39           C  
ANISOU  653  CE1 TYR A 121     3478   5174   3275    108     55   -235       C  
ATOM    654  CE2 TYR A 121     -12.963   6.259  30.074  1.00 31.36           C  
ANISOU  654  CE2 TYR A 121     3385   5224   3306     87     25   -298       C  
ATOM    655  CZ  TYR A 121     -13.115   7.627  29.946  1.00 33.17           C  
ANISOU  655  CZ  TYR A 121     3645   5426   3532     69     69   -274       C  
ATOM    656  OH  TYR A 121     -12.391   8.481  30.783  1.00 30.38           O  
ANISOU  656  OH  TYR A 121     3278   5052   3214     24     95   -302       O  
ATOM    657  N   LEU A 122     -15.008   2.416  25.547  1.00 33.30           N  
ANISOU  657  N   LEU A 122     3708   5497   3447    227   -221   -522       N  
ATOM    658  CA  LEU A 122     -15.722   1.266  24.992  1.00 33.83           C  
ANISOU  658  CA  LEU A 122     3743   5537   3572    241   -324   -642       C  
ATOM    659  C   LEU A 122     -15.420   0.064  25.855  1.00 34.53           C  
ANISOU  659  C   LEU A 122     3743   5563   3814    197   -249   -660       C  
ATOM    660  O   LEU A 122     -14.543   0.116  26.716  1.00 34.68           O  
ANISOU  660  O   LEU A 122     3756   5574   3846    186   -160   -584       O  
ATOM    661  CB  LEU A 122     -15.329   0.991  23.507  1.00 31.64           C  
ANISOU  661  CB  LEU A 122     3627   5294   3100    286   -363   -725       C  
ATOM    662  CG  LEU A 122     -13.854   0.666  23.152  1.00 35.53           C  
ANISOU  662  CG  LEU A 122     4187   5803   3509    270   -175   -739       C  
ATOM    663  CD1 LEU A 122     -13.530  -0.773  23.469  1.00 39.44           C  
ANISOU  663  CD1 LEU A 122     4571   6245   4168    260   -149   -835       C  
ATOM    664  CD2 LEU A 122     -13.542   0.895  21.632  1.00 38.46           C  
ANISOU  664  CD2 LEU A 122     4809   6201   3602    303   -138   -795       C  
ATOM    665  N   CYS A 123     -16.177  -1.000  25.631  1.00 36.76           N  
ANISOU  665  N   CYS A 123     3967   5779   4221    180   -308   -769       N  
ATOM    666  CA ACYS A 123     -16.015  -2.293  26.278  0.37 37.02           C  
ANISOU  666  CA ACYS A 123     3963   5699   4404    142   -236   -787       C  
ATOM    667  CA BCYS A 123     -15.830  -2.261  26.262  0.63 37.27           C  
ANISOU  667  CA BCYS A 123     4006   5739   4416    149   -230   -779       C  
ATOM    668  C   CYS A 123     -15.651  -3.318  25.200  1.00 38.24           C  
ANISOU  668  C   CYS A 123     4149   5830   4549    170   -277   -932       C  
ATOM    669  O   CYS A 123     -16.195  -3.249  24.091  1.00 39.11           O  
ANISOU  669  O   CYS A 123     4285   5985   4590    190   -397  -1057       O  
ATOM    670  CB ACYS A 123     -17.318  -2.658  27.004  0.37 36.61           C  
ANISOU  670  CB ACYS A 123     3809   5537   4563     63   -203   -812       C  
ATOM    671  CB BCYS A 123     -16.860  -2.692  27.308  0.63 37.77           C  
ANISOU  671  CB BCYS A 123     3996   5681   4672     71   -165   -760       C  
ATOM    672  SG ACYS A 123     -17.513  -4.322  27.676  0.37 53.19           S  
ANISOU  672  SG ACYS A 123     5910   7424   6875    -13    -82   -838       S  
ATOM    673  SG BCYS A 123     -18.515  -3.004  26.705  0.63 35.46           S  
ANISOU  673  SG BCYS A 123     3540   5331   4604     16   -255   -945       S  
ATOM    674  N   GLY A 124     -14.776  -4.266  25.514  1.00 37.42           N  
ANISOU  674  N   GLY A 124     4060   5645   4513    187   -203   -930       N  
ATOM    675  CA  GLY A 124     -14.397  -5.246  24.534  1.00 36.38           C  
ANISOU  675  CA  GLY A 124     3954   5473   4396    217   -212  -1090       C  
ATOM    676  C   GLY A 124     -14.460  -6.623  25.131  1.00 37.42           C  
ANISOU  676  C   GLY A 124     4059   5412   4748    199   -176  -1114       C  
ATOM    677  O   GLY A 124     -14.205  -6.808  26.332  1.00 35.35           O  
ANISOU  677  O   GLY A 124     3817   5055   4561    202   -124   -966       O  
ATOM    678  N   ALA A 125     -14.842  -7.564  24.281  1.00 38.76           N  
ANISOU  678  N   ALA A 125     4222   5506   5000    183   -214  -1303       N  
ATOM    679  CA  ALA A 125     -14.786  -8.987  24.558  1.00 41.58           C  
ANISOU  679  CA  ALA A 125     4575   5643   5579    172   -167  -1364       C  
ATOM    680  C   ALA A 125     -13.855  -9.645  23.550  1.00 42.84           C  
ANISOU  680  C   ALA A 125     4770   5794   5714    251   -151  -1537       C  
ATOM    681  O   ALA A 125     -13.607  -9.107  22.475  1.00 44.03           O  
ANISOU  681  O   ALA A 125     4968   6099   5661    278   -169  -1650       O  
ATOM    682  CB  ALA A 125     -16.163  -9.611  24.469  1.00 38.43           C  
ANISOU  682  CB  ALA A 125     4104   5116   5381     56   -198  -1490       C  
ATOM    683  N   ILE A 126     -13.410 -10.846  23.867  1.00 42.53           N  
ANISOU  683  N   ILE A 126     4736   5545   5878    287   -102  -1569       N  
ATOM    684  CA  ILE A 126     -12.572 -11.585  22.954  1.00 43.11           C  
ANISOU  684  CA  ILE A 126     4820   5572   5986    365    -59  -1769       C  
ATOM    685  C   ILE A 126     -13.172 -12.966  22.678  1.00 49.76           C  
ANISOU  685  C   ILE A 126     5671   6179   7058    318    -67  -1946       C  
ATOM    686  O   ILE A 126     -13.793 -13.568  23.550  1.00 51.93           O  
ANISOU  686  O   ILE A 126     5947   6249   7534    254    -54  -1847       O  
ATOM    687  CB  ILE A 126     -11.154 -11.691  23.537  1.00 40.17           C  
ANISOU  687  CB  ILE A 126     4410   5150   5702    499     -3  -1677       C  
ATOM    688  CG1 ILE A 126     -10.201 -12.425  22.605  1.00 39.61           C  
ANISOU  688  CG1 ILE A 126     4307   5019   5723    589     88  -1914       C  
ATOM    689  CG2 ILE A 126     -11.171 -12.364  24.888  1.00 40.17           C  
ANISOU  689  CG2 ILE A 126     4449   4920   5893    536    -48  -1486       C  
ATOM    690  CD1 ILE A 126      -8.743 -12.233  23.089  1.00 40.14           C  
ANISOU  690  CD1 ILE A 126     4255   5080   5916    731    126  -1863       C  
ATOM    691  N   SER A 127     -13.017 -13.466  21.456  1.00 48.94           N  
ANISOU  691  N   SER A 127     5596   6082   6918    335    -63  -2221       N  
ATOM    692  CA  SER A 127     -13.480 -14.813  21.156  1.00 48.02           C  
ANISOU  692  CA  SER A 127     5480   5719   7048    292    -70  -2429       C  
ATOM    693  C   SER A 127     -12.411 -15.475  20.345  1.00 46.45           C  
ANISOU  693  C   SER A 127     5317   5464   6866    402     25  -2641       C  
ATOM    694  O   SER A 127     -11.610 -14.784  19.717  1.00 48.68           O  
ANISOU  694  O   SER A 127     5634   5942   6922    469    100  -2684       O  
ATOM    695  CB  SER A 127     -14.814 -14.817  20.392  1.00 52.12           C  
ANISOU  695  CB  SER A 127     5987   6280   7537    167   -213  -2643       C  
ATOM    696  OG  SER A 127     -15.130 -16.132  19.910  1.00 55.10           O  
ANISOU  696  OG  SER A 127     6359   6419   8158    122   -220  -2915       O  
ATOM    697  N   LEU A 128     -12.389 -16.807  20.365  1.00 45.63           N  
ANISOU  697  N   LEU A 128     5210   5071   7057    413     59  -2781       N  
ATOM    698  CA  LEU A 128     -11.432 -17.574  19.587  1.00 50.69           C  
ANISOU  698  CA  LEU A 128     5868   5615   7777    522    168  -3030       C  
ATOM    699  C   LEU A 128     -12.022 -18.091  18.290  1.00 54.19           C  
ANISOU  699  C   LEU A 128     6397   6055   8137    450    135  -3403       C  
ATOM    700  O   LEU A 128     -11.302 -18.686  17.482  1.00 56.69           O  
ANISOU  700  O   LEU A 128     6761   6307   8470    526    255  -3664       O  
ATOM    701  CB  LEU A 128     -10.913 -18.771  20.383  1.00 55.09           C  
ANISOU  701  CB  LEU A 128     6391   5812   8727    618    211  -2972       C  
ATOM    702  CG  LEU A 128     -10.604 -18.636  21.865  1.00 57.74           C  
ANISOU  702  CG  LEU A 128     6718   6035   9187    691    167  -2603       C  
ATOM    703  CD1 LEU A 128      -9.963 -19.929  22.338  1.00 59.13           C  
ANISOU  703  CD1 LEU A 128     6919   5825   9723    835    181  -2606       C  
ATOM    704  CD2 LEU A 128      -9.691 -17.450  22.101  1.00 59.48           C  
ANISOU  704  CD2 LEU A 128     6863   6526   9212    787    163  -2454       C  
ATOM    705  N   ALA A 129     -13.328 -17.916  18.091  1.00 52.57           N  
ANISOU  705  N   ALA A 129     6204   5899   7872    310    -34  -3465       N  
ATOM    706  CA  ALA A 129     -13.937 -18.518  16.910  1.00 55.45           C  
ANISOU  706  CA  ALA A 129     6650   6228   8191    251   -137  -3858       C  
ATOM    707  C   ALA A 129     -14.595 -17.469  16.007  1.00 55.57           C  
ANISOU  707  C   ALA A 129     6784   6547   7783    220   -332  -3951       C  
ATOM    708  O   ALA A 129     -15.233 -16.529  16.493  1.00 56.84           O  
ANISOU  708  O   ALA A 129     6879   6854   7862    176   -454  -3736       O  
ATOM    709  CB  ALA A 129     -14.932 -19.588  17.318  1.00 55.06           C  
ANISOU  709  CB  ALA A 129     6492   5871   8559    121   -210  -3968       C  
ATOM    710  N   PRO A 130     -14.426 -17.619  14.683  1.00 56.85           N  
ANISOU  710  N   PRO A 130     7155   6795   7652    256   -360  -4231       N  
ATOM    711  CA  PRO A 130     -13.710 -18.721  14.014  1.00 60.20           C  
ANISOU  711  CA  PRO A 130     7668   7059   8147    298   -191  -4422       C  
ATOM    712  C   PRO A 130     -12.193 -18.547  14.088  1.00 58.24           C  
ANISOU  712  C   PRO A 130     7443   6837   7850    421    133  -4347       C  
ATOM    713  O   PRO A 130     -11.448 -19.471  13.748  1.00 62.27           O  
ANISOU  713  O   PRO A 130     7964   7184   8513    475    311  -4479       O  
ATOM    714  CB  PRO A 130     -14.202 -18.630  12.563  1.00 62.12           C  
ANISOU  714  CB  PRO A 130     8186   7438   7979    280   -352  -4607       C  
ATOM    715  CG  PRO A 130     -14.444 -17.171  12.361  1.00 60.39           C  
ANISOU  715  CG  PRO A 130     8108   7501   7338    301   -469  -4433       C  
ATOM    716  CD  PRO A 130     -14.910 -16.613  13.719  1.00 59.38           C  
ANISOU  716  CD  PRO A 130     7693   7383   7484    264   -550  -4223       C  
ATOM    717  N   LYS A 131     -11.759 -17.368  14.537  1.00 57.89           N  
ANISOU  717  N   LYS A 131     7376   6989   7632    462    205  -4141       N  
ATOM    718  CA  LYS A 131     -10.335 -17.076  14.762  1.00 59.58           C  
ANISOU  718  CA  LYS A 131     7524   7230   7883    567    506  -4047       C  
ATOM    719  C   LYS A 131     -10.259 -16.071  15.913  1.00 57.86           C  
ANISOU  719  C   LYS A 131     7154   7128   7704    567    460  -3648       C  
ATOM    720  O   LYS A 131     -11.300 -15.554  16.330  1.00 59.86           O  
ANISOU  720  O   LYS A 131     7402   7459   7883    486    240  -3482       O  
ATOM    721  CB  LYS A 131      -9.665 -16.538  13.480  1.00 62.67           C  
ANISOU  721  CB  LYS A 131     8177   7795   7840    575    718  -4113       C  
ATOM    722  CG  LYS A 131     -10.155 -15.149  13.018  1.00 61.10           C  
ANISOU  722  CG  LYS A 131     8212   7865   7140    528    629  -3979       C  
ATOM    723  CD  LYS A 131      -9.798 -14.887  11.540  1.00 63.14           C  
ANISOU  723  CD  LYS A 131     8875   8197   6919    527    799  -4074       C  
ATOM    724  N   VAL A 132      -9.069 -15.798  16.456  1.00 51.31           N  
ANISOU  724  N   VAL A 132     6178   6296   7022    656    649  -3513       N  
ATOM    725  CA  VAL A 132      -8.993 -14.830  17.559  1.00 51.06           C  
ANISOU  725  CA  VAL A 132     6020   6371   7009    655    576  -3157       C  
ATOM    726  C   VAL A 132      -9.424 -13.453  17.057  1.00 50.05           C  
ANISOU  726  C   VAL A 132     6051   6520   6445    577    556  -3058       C  
ATOM    727  O   VAL A 132      -8.961 -12.998  16.012  1.00 52.94           O  
ANISOU  727  O   VAL A 132     6589   7007   6520    574    743  -3200       O  
ATOM    728  CB  VAL A 132      -7.577 -14.722  18.174  1.00 50.08           C  
ANISOU  728  CB  VAL A 132     5689   6201   7139    777    736  -3080       C  
ATOM    729  CG1 VAL A 132      -7.606 -13.755  19.261  1.00 44.23           C  
ANISOU  729  CG1 VAL A 132     4857   5567   6383    767    618  -2756       C  
ATOM    730  CG2 VAL A 132      -7.112 -16.054  18.714  1.00 52.93           C  
ANISOU  730  CG2 VAL A 132     5912   6257   7942    899    707  -3155       C  
ATOM    731  N   GLN A 133     -10.306 -12.793  17.797  1.00 50.49           N  
ANISOU  731  N   GLN A 133     6077   6651   6454    518    353  -2816       N  
ATOM    732  CA  GLN A 133     -10.848 -11.494  17.401  1.00 51.28           C  
ANISOU  732  CA  GLN A 133     6326   6977   6182    465    281  -2707       C  
ATOM    733  C   GLN A 133     -11.280 -10.702  18.625  1.00 45.41           C  
ANISOU  733  C   GLN A 133     5448   6283   5522    435    159  -2398       C  
ATOM    734  O   GLN A 133     -11.827 -11.260  19.557  1.00 42.56           O  
ANISOU  734  O   GLN A 133     4962   5790   5419    412     48  -2311       O  
ATOM    735  CB  GLN A 133     -12.049 -11.658  16.444  1.00 56.21           C  
ANISOU  735  CB  GLN A 133     7142   7636   6579    419     64  -2896       C  
ATOM    736  CG  GLN A 133     -13.107 -12.636  16.960  1.00 60.12           C  
ANISOU  736  CG  GLN A 133     7489   7958   7396    364   -146  -2967       C  
ATOM    737  CD  GLN A 133     -14.469 -12.447  16.306  1.00 64.69           C  
ANISOU  737  CD  GLN A 133     8155   8599   7825    314   -446  -3111       C  
ATOM    738  OE1 GLN A 133     -14.932 -11.313  16.133  1.00 66.19           O  
ANISOU  738  OE1 GLN A 133     8431   8960   7759    323   -582  -2992       O  
ATOM    739  NE2 GLN A 133     -15.126 -13.562  15.948  1.00 63.73           N  
ANISOU  739  NE2 GLN A 133     7997   8317   7901    269   -577  -3387       N  
ATOM    740  N   ILE A 134     -10.992  -9.410  18.645  1.00 45.08           N  
ANISOU  740  N   ILE A 134     5455   6410   5265    428    217  -2237       N  
ATOM    741  CA  ILE A 134     -11.589  -8.546  19.648  1.00 44.28           C  
ANISOU  741  CA  ILE A 134     5271   6370   5185    393     87  -1984       C  
ATOM    742  C   ILE A 134     -12.957  -8.130  19.126  1.00 46.76           C  
ANISOU  742  C   ILE A 134     5698   6757   5313    350   -133  -2017       C  
ATOM    743  O   ILE A 134     -13.112  -7.866  17.928  1.00 50.86           O  
ANISOU  743  O   ILE A 134     6434   7355   5534    367   -170  -2151       O  
ATOM    744  CB  ILE A 134     -10.754  -7.328  19.923  1.00 40.89           C  
ANISOU  744  CB  ILE A 134     4828   6059   4649    400    224  -1820       C  
ATOM    745  CG1 ILE A 134      -9.348  -7.767  20.348  1.00 43.21           C  
ANISOU  745  CG1 ILE A 134     4956   6274   5189    459    402  -1854       C  
ATOM    746  CG2 ILE A 134     -11.402  -6.433  21.016  1.00 36.69           C  
ANISOU  746  CG2 ILE A 134     4220   5578   4141    366     91  -1580       C  
ATOM    747  CD1 ILE A 134      -9.316  -8.758  21.521  1.00 40.56           C  
ANISOU  747  CD1 ILE A 134     4460   5766   5184    514    282  -1793       C  
ATOM    748  N   LYS A 135     -13.956  -8.112  19.997  1.00 44.24           N  
ANISOU  748  N   LYS A 135     5244   6392   5174    302   -283  -1916       N  
ATOM    749  CA  LYS A 135     -15.235  -7.512  19.616  1.00 43.24           C  
ANISOU  749  CA  LYS A 135     5150   6337   4943    280   -513  -1948       C  
ATOM    750  C   LYS A 135     -15.394  -6.245  20.420  1.00 39.05           C  
ANISOU  750  C   LYS A 135     4567   5897   4375    274   -510  -1704       C  
ATOM    751  O   LYS A 135     -15.603  -6.312  21.639  1.00 39.58           O  
ANISOU  751  O   LYS A 135     4476   5893   4668    228   -460  -1570       O  
ATOM    752  CB  LYS A 135     -16.413  -8.467  19.857  1.00 47.69           C  
ANISOU  752  CB  LYS A 135     5555   6755   5809    211   -663  -2097       C  
ATOM    753  CG  LYS A 135     -16.470  -9.670  18.898  1.00 52.49           C  
ANISOU  753  CG  LYS A 135     6226   7265   6453    210   -723  -2397       C  
ATOM    754  CD  LYS A 135     -17.638 -10.592  19.225  1.00 56.02           C  
ANISOU  754  CD  LYS A 135     6474   7533   7277    110   -842  -2557       C  
ATOM    755  N   GLU A 136     -15.268  -5.097  19.758  1.00 35.71           N  
ANISOU  755  N   GLU A 136     4315   5604   3648    321   -542  -1643       N  
ATOM    756  CA  GLU A 136     -15.370  -3.823  20.467  1.00 32.90           C  
ANISOU  756  CA  GLU A 136     3922   5315   3262    319   -530  -1425       C  
ATOM    757  C   GLU A 136     -16.836  -3.422  20.476  1.00 35.76           C  
ANISOU  757  C   GLU A 136     4211   5679   3699    328   -791  -1458       C  
ATOM    758  O   GLU A 136     -17.523  -3.626  19.487  1.00 36.05           O  
ANISOU  758  O   GLU A 136     4339   5722   3638    375  -1018  -1629       O  
ATOM    759  CB  GLU A 136     -14.548  -2.728  19.798  1.00 36.80           C  
ANISOU  759  CB  GLU A 136     4642   5903   3439    355   -411  -1331       C  
ATOM    760  CG  GLU A 136     -13.022  -2.978  19.626  1.00 47.50           C  
ANISOU  760  CG  GLU A 136     6035   7254   4759    340   -111  -1346       C  
ATOM    761  CD  GLU A 136     -12.323  -1.796  18.915  1.00 50.23           C  
ANISOU  761  CD  GLU A 136     6617   7659   4811    339     69  -1261       C  
ATOM    762  OE1 GLU A 136     -13.023  -1.028  18.212  1.00 51.42           O  
ANISOU  762  OE1 GLU A 136     7008   7840   4688    379    -73  -1216       O  
ATOM    763  OE2 GLU A 136     -11.084  -1.617  19.056  1.00 46.12           O  
ANISOU  763  OE2 GLU A 136     6042   7130   4352    302    350  -1244       O  
ATOM    764  N   SER A 137     -17.314  -2.834  21.561  1.00 34.32           N  
ANISOU  764  N   SER A 137     3863   5483   3694    294   -772  -1323       N  
ATOM    765  CA  SER A 137     -18.638  -2.222  21.521  1.00 38.59           C  
ANISOU  765  CA  SER A 137     4305   6025   4334    321   -999  -1366       C  
ATOM    766  C   SER A 137     -18.560  -0.969  20.651  1.00 40.09           C  
ANISOU  766  C   SER A 137     4731   6301   4199    432  -1135  -1291       C  
ATOM    767  O   SER A 137     -17.484  -0.502  20.322  1.00 38.35           O  
ANISOU  767  O   SER A 137     4726   6132   3715    445   -971  -1176       O  
ATOM    768  CB  SER A 137     -19.102  -1.851  22.919  1.00 36.52           C  
ANISOU  768  CB  SER A 137     3832   5714   4331    253   -877  -1250       C  
ATOM    769  OG  SER A 137     -18.306  -0.795  23.461  1.00 32.93           O  
ANISOU  769  OG  SER A 137     3470   5322   3720    268   -732  -1043       O  
ATOM    770  N   LEU A 138     -19.698  -0.397  20.310  1.00 37.05           N  
ANISOU  770  N   LEU A 138     4306   5910   3863    513  -1424  -1356       N  
ATOM    771  CA  LEU A 138     -19.717   0.977  19.829  1.00 40.15           C  
ANISOU  771  CA  LEU A 138     4919   6338   4000    628  -1541  -1220       C  
ATOM    772  C   LEU A 138     -19.149   1.894  20.899  1.00 40.98           C  
ANISOU  772  C   LEU A 138     4966   6448   4158    572  -1274   -999       C  
ATOM    773  O   LEU A 138     -19.180   1.586  22.119  1.00 41.48           O  
ANISOU  773  O   LEU A 138     4779   6486   4496    471  -1096   -975       O  
ATOM    774  CB  LEU A 138     -21.136   1.413  19.436  1.00 45.42           C  
ANISOU  774  CB  LEU A 138     5489   6966   4802    756  -1952  -1345       C  
ATOM    775  CG  LEU A 138     -21.800   0.509  18.404  1.00 46.57           C  
ANISOU  775  CG  LEU A 138     5667   7073   4955    804  -2246  -1583       C  
ATOM    776  CD1 LEU A 138     -23.325   0.761  18.372  1.00 51.66           C  
ANISOU  776  CD1 LEU A 138     6055   7602   5970    875  -2531  -1696       C  
ATOM    777  CD2 LEU A 138     -21.176   0.757  17.058  1.00 48.44           C  
ANISOU  777  CD2 LEU A 138     6391   7320   4693    888  -2292  -1506       C  
ATOM    778  N   ARG A 139     -18.577   3.002  20.447  1.00 39.20           N  
ANISOU  778  N   ARG A 139     5011   6236   3647    630  -1227   -841       N  
ATOM    779  CA  ARG A 139     -17.828   3.873  21.349  1.00 38.07           C  
ANISOU  779  CA  ARG A 139     4839   6091   3534    562   -962   -659       C  
ATOM    780  C   ARG A 139     -18.773   4.900  21.947  1.00 40.93           C  
ANISOU  780  C   ARG A 139     5073   6402   4075    621  -1088   -606       C  
ATOM    781  O   ARG A 139     -19.701   5.352  21.287  1.00 45.62           O  
ANISOU  781  O   ARG A 139     5732   6955   4645    756  -1383   -648       O  
ATOM    782  CB  ARG A 139     -16.666   4.523  20.601  1.00 40.39           C  
ANISOU  782  CB  ARG A 139     5463   6388   3495    558   -773   -537       C  
ATOM    783  CG  ARG A 139     -15.742   3.453  20.037  1.00 42.66           C  
ANISOU  783  CG  ARG A 139     5833   6715   3662    500   -607   -633       C  
ATOM    784  CD  ARG A 139     -14.610   3.975  19.153  1.00 49.30           C  
ANISOU  784  CD  ARG A 139     7004   7539   4190    475   -351   -558       C  
ATOM    785  NE  ARG A 139     -13.801   2.853  18.672  1.00 51.57           N  
ANISOU  785  NE  ARG A 139     7311   7854   4429    425   -175   -698       N  
ATOM    786  CZ  ARG A 139     -12.568   2.973  18.197  1.00 53.58           C  
ANISOU  786  CZ  ARG A 139     7712   8092   4555    355    170   -694       C  
ATOM    787  NH1 ARG A 139     -12.024   4.186  18.126  1.00 54.34           N  
ANISOU  787  NH1 ARG A 139     7963   8133   4549    310    379   -544       N  
ATOM    788  NH2 ARG A 139     -11.890   1.888  17.787  1.00 50.34           N  
ANISOU  788  NH2 ARG A 139     7280   7694   4154    324    329   -857       N  
ATOM    789  N   ALA A 140     -18.559   5.233  23.210  1.00 38.22           N  
ANISOU  789  N   ALA A 140     4551   6051   3921    535   -887   -538       N  
ATOM    790  CA  ALA A 140     -19.432   6.168  23.915  1.00 41.12           C  
ANISOU  790  CA  ALA A 140     4771   6358   4493    576   -944   -518       C  
ATOM    791  C   ALA A 140     -18.578   7.326  24.374  1.00 39.25           C  
ANISOU  791  C   ALA A 140     4659   6101   4155    542   -750   -358       C  
ATOM    792  O   ALA A 140     -17.363   7.181  24.502  1.00 38.22           O  
ANISOU  792  O   ALA A 140     4612   6008   3900    452   -545   -297       O  
ATOM    793  CB  ALA A 140     -20.095   5.506  25.096  1.00 41.31           C  
ANISOU  793  CB  ALA A 140     4490   6366   4841    488   -848   -618       C  
ATOM    794  N  AGLU A 141     -19.200   8.466  24.639  0.50 36.77           N  
ANISOU  794  N  AGLU A 141     4324   5707   3940    614   -817   -317       N  
ATOM    795  N  BGLU A 141     -19.168   8.494  24.587  0.50 36.84           N  
ANISOU  795  N  BGLU A 141     4347   5715   3935    617   -819   -312       N  
ATOM    796  CA AGLU A 141     -18.442   9.641  25.026  0.50 36.21           C  
ANISOU  796  CA AGLU A 141     4375   5584   3799    578   -642   -186       C  
ATOM    797  CA BGLU A 141     -18.335   9.591  25.040  0.50 35.54           C  
ANISOU  797  CA BGLU A 141     4295   5507   3703    566   -623   -183       C  
ATOM    798  C  AGLU A 141     -18.774  10.053  26.448  0.50 33.98           C  
ANISOU  798  C  AGLU A 141     3878   5275   3757    520   -514   -225       C  
ATOM    799  C  BGLU A 141     -18.746  10.015  26.432  0.50 33.89           C  
ANISOU  799  C  BGLU A 141     3869   5267   3740    518   -513   -225       C  
ATOM    800  O  AGLU A 141     -19.945  10.089  26.836  0.50 35.04           O  
ANISOU  800  O  AGLU A 141     3823   5368   4124    577   -605   -321       O  
ATOM    801  O  BGLU A 141     -19.930  10.007  26.787  0.50 34.96           O  
ANISOU  801  O  BGLU A 141     3814   5363   4105    575   -610   -323       O  
ATOM    802  CB AGLU A 141     -18.706  10.783  24.041  0.50 41.97           C  
ANISOU  802  CB AGLU A 141     5367   6198   4383    718   -797    -80       C  
ATOM    803  CB BGLU A 141     -18.364  10.772  24.056  0.50 41.41           C  
ANISOU  803  CB BGLU A 141     5328   6137   4269    683   -729    -60       C  
ATOM    804  CG AGLU A 141     -18.197  10.453  22.638  0.50 45.67           C  
ANISOU  804  CG AGLU A 141     6163   6679   4511    759   -858    -22       C  
ATOM    805  CG BGLU A 141     -19.676  11.456  23.838  0.50 47.62           C  
ANISOU  805  CG BGLU A 141     6062   6803   5229    836   -941    -67       C  
ATOM    806  CD AGLU A 141     -18.398  11.563  21.623  0.50 57.19           C  
ANISOU  806  CD AGLU A 141     7998   7990   5742    907  -1004    121       C  
ATOM    807  CD BGLU A 141     -19.602  12.534  22.748  0.50 56.78           C  
ANISOU  807  CD BGLU A 141     7561   7802   6211    926   -962    107       C  
ATOM    808  OE1AGLU A 141     -18.821  12.678  22.013  0.50 60.61           O  
ANISOU  808  OE1AGLU A 141     8423   8295   6312    977  -1047    189       O  
ATOM    809  OE1BGLU A 141     -18.473  12.963  22.425  0.50 58.96           O  
ANISOU  809  OE1BGLU A 141     8096   8063   6242    829   -744    226       O  
ATOM    810  OE2AGLU A 141     -18.127  11.316  20.424  0.50 61.12           O  
ANISOU  810  OE2AGLU A 141     8838   8479   5904    959  -1068    167       O  
ATOM    811  OE2BGLU A 141     -20.660  12.951  22.214  0.50 58.94           O  
ANISOU  811  OE2BGLU A 141     7841   7939   6615   1093  -1178    118       O  
ATOM    812  N   LEU A 142     -17.737  10.328  27.232  1.00 29.18           N  
ANISOU  812  N   LEU A 142     3293   4686   3107    405   -299   -179       N  
ATOM    813  CA  LEU A 142     -17.913  10.860  28.578  1.00 28.20           C  
ANISOU  813  CA  LEU A 142     3052   4529   3134    352   -174   -218       C  
ATOM    814  C   LEU A 142     -17.525  12.349  28.559  1.00 28.55           C  
ANISOU  814  C   LEU A 142     3219   4465   3162    365   -120   -147       C  
ATOM    815  O   LEU A 142     -16.449  12.707  28.054  1.00 29.52           O  
ANISOU  815  O   LEU A 142     3492   4573   3150    314    -43    -69       O  
ATOM    816  CB  LEU A 142     -17.031  10.075  29.583  1.00 30.01           C  
ANISOU  816  CB  LEU A 142     3243   4839   3321    230    -31   -245       C  
ATOM    817  CG  LEU A 142     -16.923  10.660  31.001  1.00 31.30           C  
ANISOU  817  CG  LEU A 142     3384   4972   3537    169     95   -286       C  
ATOM    818  CD1 LEU A 142     -18.279  10.680  31.645  1.00 31.83           C  
ANISOU  818  CD1 LEU A 142     3340   4987   3768    194    140   -366       C  
ATOM    819  CD2 LEU A 142     -15.922   9.878  31.925  1.00 26.32           C  
ANISOU  819  CD2 LEU A 142     2782   4408   2809     88    150   -302       C  
ATOM    820  N   ARG A 143     -18.380  13.214  29.091  1.00 27.94           N  
ANISOU  820  N   ARG A 143     3072   4290   3255    423   -129   -189       N  
ATOM    821  CA  ARG A 143     -18.016  14.621  29.220  1.00 29.12           C  
ANISOU  821  CA  ARG A 143     3334   4306   3426    425    -58   -137       C  
ATOM    822  C   ARG A 143     -18.148  14.943  30.693  1.00 31.81           C  
ANISOU  822  C   ARG A 143     3555   4636   3896    352     89   -254       C  
ATOM    823  O   ARG A 143     -19.211  14.743  31.289  1.00 30.81           O  
ANISOU  823  O   ARG A 143     3277   4500   3929    392    102   -359       O  
ATOM    824  CB  ARG A 143     -18.900  15.598  28.399  1.00 32.19           C  
ANISOU  824  CB  ARG A 143     3811   4527   3894    599   -225    -78       C  
ATOM    825  CG  ARG A 143     -18.742  15.605  26.851  1.00 72.08           C  
ANISOU  825  CG  ARG A 143     9122   9534   8730    699   -389     67       C  
ATOM    826  CD  ARG A 143     -17.356  16.075  26.328  1.00 68.54           C  
ANISOU  826  CD  ARG A 143     8941   9034   8068    584   -195    203       C  
ATOM    827  NE  ARG A 143     -16.472  14.925  26.184  1.00 65.66           N  
ANISOU  827  NE  ARG A 143     8544   8841   7564    460    -92    175       N  
ATOM    828  CZ  ARG A 143     -16.127  14.364  25.035  1.00 65.27           C  
ANISOU  828  CZ  ARG A 143     8688   8827   7286    478   -117    241       C  
ATOM    829  NH1 ARG A 143     -16.527  14.865  23.871  1.00 68.09           N  
ANISOU  829  NH1 ARG A 143     9353   9060   7458    612   -251    364       N  
ATOM    830  NH2 ARG A 143     -15.356  13.300  25.059  1.00 64.84           N  
ANISOU  830  NH2 ARG A 143     8549   8916   7173    372    -12    179       N  
ATOM    831  N   VAL A 144     -17.054  15.426  31.274  1.00 31.58           N  
ANISOU  831  N   VAL A 144     3595   4599   3804    239    213   -261       N  
ATOM    832  CA  VAL A 144     -17.060  15.813  32.671  1.00 33.73           C  
ANISOU  832  CA  VAL A 144     3825   4856   4136    173    329   -387       C  
ATOM    833  C   VAL A 144     -17.126  17.330  32.681  1.00 35.73           C  
ANISOU  833  C   VAL A 144     4139   4924   4514    200    374   -398       C  
ATOM    834  O   VAL A 144     -16.283  17.992  32.061  1.00 34.95           O  
ANISOU  834  O   VAL A 144     4149   4740   4391    160    390   -319       O  
ATOM    835  CB  VAL A 144     -15.810  15.300  33.407  1.00 30.37           C  
ANISOU  835  CB  VAL A 144     3428   4536   3576     49    366   -432       C  
ATOM    836  CG1 VAL A 144     -15.869  15.688  34.866  1.00 25.47           C  
ANISOU  836  CG1 VAL A 144     2836   3895   2948     -1    447   -573       C  
ATOM    837  CG2 VAL A 144     -15.731  13.767  33.277  1.00 28.73           C  
ANISOU  837  CG2 VAL A 144     3184   4472   3260     46    309   -400       C  
ATOM    838  N   THR A 145     -18.123  17.885  33.363  1.00 34.70           N  
ANISOU  838  N   THR A 145     3940   4703   4543    260    428   -504       N  
ATOM    839  CA  THR A 145     -18.271  19.329  33.386  1.00 38.68           C  
ANISOU  839  CA  THR A 145     4497   4997   5201    305    467   -528       C  
ATOM    840  C   THR A 145     -17.688  19.973  34.650  1.00 39.11           C  
ANISOU  840  C   THR A 145     4590   5015   5255    185    613   -685       C  
ATOM    841  O   THR A 145     -17.593  19.345  35.698  1.00 40.05           O  
ANISOU  841  O   THR A 145     4697   5258   5261    110    680   -801       O  
ATOM    842  CB  THR A 145     -19.746  19.728  33.225  1.00 43.79           C  
ANISOU  842  CB  THR A 145     5026   5519   6092    479    414   -577       C  
ATOM    843  OG1 THR A 145     -20.542  19.124  34.250  1.00 47.54           O  
ANISOU  843  OG1 THR A 145     5341   6073   6648    456    543   -746       O  
ATOM    844  CG2 THR A 145     -20.265  19.255  31.844  1.00 47.11           C  
ANISOU  844  CG2 THR A 145     5442   5947   6510    624    181   -436       C  
ATOM    845  N   GLU A 146     -17.281  21.223  34.522  1.00 34.62           N  
ANISOU  845  N   GLU A 146     4105   4254   4794    168    651   -689       N  
ATOM    846  CA  GLU A 146     -16.800  22.005  35.653  1.00 37.67           C  
ANISOU  846  CA  GLU A 146     4528   4567   5218     64    762   -877       C  
ATOM    847  C   GLU A 146     -17.894  22.193  36.709  1.00 44.41           C  
ANISOU  847  C   GLU A 146     5330   5388   6154    123    875  -1060       C  
ATOM    848  O   GLU A 146     -19.018  22.626  36.400  1.00 48.08           O  
ANISOU  848  O   GLU A 146     5715   5721   6833    266    891  -1062       O  
ATOM    849  CB  GLU A 146     -16.275  23.353  35.133  1.00 39.38           C  
ANISOU  849  CB  GLU A 146     4838   4529   5596     37    801   -838       C  
ATOM    850  CG  GLU A 146     -15.174  24.083  35.976  1.00 46.34           C  
ANISOU  850  CG  GLU A 146     5752   5338   6518   -137    877  -1024       C  
ATOM    851  CD  GLU A 146     -14.011  23.192  36.426  1.00 44.09           C  
ANISOU  851  CD  GLU A 146     5419   5271   6062   -276    806  -1099       C  
ATOM    852  OE1 GLU A 146     -13.718  22.203  35.738  1.00 38.29           O  
ANISOU  852  OE1 GLU A 146     4648   4689   5212   -270    741   -954       O  
ATOM    853  OE2 GLU A 146     -13.404  23.480  37.506  1.00 35.48           O  
ANISOU  853  OE2 GLU A 146     4331   4190   4959   -377    788  -1326       O  
ATOM    854  N   ARG A 147     -17.589  21.856  37.962  1.00 43.22           N  
ANISOU  854  N   ARG A 147     5237   5346   5838     23    953  -1230       N  
ATOM    855  CA  ARG A 147     -18.543  22.093  39.030  1.00 40.73           C  
ANISOU  855  CA  ARG A 147     4929   4980   5565     51   1138  -1426       C  
ATOM    856  C   ARG A 147     -18.561  23.575  39.319  1.00 45.72           C  
ANISOU  856  C   ARG A 147     5598   5376   6399     61   1215  -1572       C  
ATOM    857  O   ARG A 147     -17.523  24.215  39.276  1.00 46.46           O  
ANISOU  857  O   ARG A 147     5768   5400   6486    -29   1145  -1593       O  
ATOM    858  CB  ARG A 147     -18.188  21.304  40.289  1.00 39.75           C  
ANISOU  858  CB  ARG A 147     4961   5017   5124    -51   1203  -1547       C  
ATOM    859  CG  ARG A 147     -19.242  21.450  41.419  1.00 53.91           C  
ANISOU  859  CG  ARG A 147     6821   6751   6912    -41   1484  -1753       C  
ATOM    860  CD  ARG A 147     -18.911  20.580  42.645  1.00 55.20           C  
ANISOU  860  CD  ARG A 147     7249   7055   6670   -133   1556  -1833       C  
ATOM    861  NE  ARG A 147     -18.748  19.158  42.308  1.00 55.18           N  
ANISOU  861  NE  ARG A 147     7248   7220   6499   -143   1464  -1643       N  
ATOM    862  CZ  ARG A 147     -19.726  18.247  42.335  1.00 53.32           C  
ANISOU  862  CZ  ARG A 147     6961   7013   6285   -132   1657  -1595       C  
ATOM    863  NH1 ARG A 147     -20.956  18.606  42.660  1.00 58.92           N  
ANISOU  863  NH1 ARG A 147     7576   7604   7208   -110   1962  -1734       N  
ATOM    864  NH2 ARG A 147     -19.483  16.976  42.010  1.00 45.09           N  
ANISOU  864  NH2 ARG A 147     5932   6097   5102   -148   1559  -1428       N  
ATOM    865  N   ARG A 148     -19.729  24.139  39.611  1.00 49.33           N  
ANISOU  865  N   ARG A 148     5976   5683   7083    164   1374  -1698       N  
ATOM    866  CA  ARG A 148     -19.797  25.572  39.908  1.00 59.43           C  
ANISOU  866  CA  ARG A 148     7292   6703   8586    188   1458  -1856       C  
ATOM    867  C   ARG A 148     -19.120  25.893  41.249  1.00 66.19           C  
ANISOU  867  C   ARG A 148     8334   7582   9233     40   1562  -2110       C  
ATOM    868  O   ARG A 148     -18.922  25.010  42.085  1.00 64.66           O  
ANISOU  868  O   ARG A 148     8258   7587   8722    -40   1601  -2179       O  
ATOM    869  CB  ARG A 148     -21.254  26.062  39.925  1.00 61.22           C  
ANISOU  869  CB  ARG A 148     7352   6751   9156    359   1602  -1966       C  
ATOM    870  N   ALA A 149     -18.741  27.151  41.441  1.00 73.75           N  
ANISOU  870  N   ALA A 149     9350   8315  10355     10   1584  -2250       N  
ATOM    871  CA  ALA A 149     -18.303  27.606  42.757  1.00 81.09           C  
ANISOU  871  CA  ALA A 149    10459   9228  11124   -104   1675  -2557       C  
ATOM    872  C   ALA A 149     -19.497  27.637  43.712  1.00 86.57           C  
ANISOU  872  C   ALA A 149    11190   9887  11817    -40   1966  -2779       C  
ATOM    873  O   ALA A 149     -19.341  27.591  44.936  1.00 90.73           O  
ANISOU  873  O   ALA A 149    11937  10471  12064   -125   2082  -3022       O  
ATOM    874  CB  ALA A 149     -17.646  28.978  42.661  1.00 84.53           C  
ANISOU  874  CB  ALA A 149    10924   9396  11799   -162   1641  -2676       C  
TER     875      ALA A 149                                                      
ATOM    876  N   LEU B  20      -3.012  -5.202  36.329  1.00 62.50           N  
ANISOU  876  N   LEU B  20     9807   9782   4160   2346   1138    760       N  
ATOM    877  CA  LEU B  20      -3.676  -5.607  35.106  1.00 58.16           C  
ANISOU  877  CA  LEU B  20     8804   8611   4682   2971   1236    992       C  
ATOM    878  C   LEU B  20      -2.682  -6.066  34.062  1.00 56.80           C  
ANISOU  878  C   LEU B  20     7765   9094   4723   2746    714   1049       C  
ATOM    879  O   LEU B  20      -1.649  -5.434  33.856  1.00 58.08           O  
ANISOU  879  O   LEU B  20     7988   9726   4354   1942    402    750       O  
ATOM    880  CB  LEU B  20      -4.487  -4.469  34.521  1.00 62.55           C  
ANISOU  880  CB  LEU B  20    10141   8069   5557   2835   1708    751       C  
ATOM    881  CG  LEU B  20      -5.846  -4.191  35.138  1.00 71.78           C  
ANISOU  881  CG  LEU B  20    12027   8200   7048   3362   2409    907       C  
ATOM    882  CD1 LEU B  20      -6.577  -3.220  34.232  1.00 73.47           C  
ANISOU  882  CD1 LEU B  20    12506   7590   7818   3013   2649    929       C  
ATOM    883  CD2 LEU B  20      -6.627  -5.482  35.330  1.00 70.22           C  
ANISOU  883  CD2 LEU B  20    10977   8255   7449   3520   2121   1346       C  
ATOM    884  N   PHE B  21      -3.008  -7.160  33.393  1.00 52.83           N  
ANISOU  884  N   PHE B  21     6487   8553   5033   3417    684   1415       N  
ATOM    885  CA  PHE B  21      -2.252  -7.576  32.236  1.00 49.20           C  
ANISOU  885  CA  PHE B  21     5469   8298   4926   2899    406   1312       C  
ATOM    886  C   PHE B  21      -2.431  -6.524  31.140  1.00 45.14           C  
ANISOU  886  C   PHE B  21     5281   7328   4542   2877    401   1134       C  
ATOM    887  O   PHE B  21      -3.572  -6.224  30.766  1.00 41.12           O  
ANISOU  887  O   PHE B  21     5200   5942   4480   2791    684   1034       O  
ATOM    888  CB  PHE B  21      -2.720  -8.955  31.778  1.00 45.59           C  
ANISOU  888  CB  PHE B  21     4890   7268   5164   2397    452   1215       C  
ATOM    889  CG  PHE B  21      -2.020  -9.444  30.541  1.00 44.10           C  
ANISOU  889  CG  PHE B  21     4442   7169   5145   2128    355   1205       C  
ATOM    890  CD1 PHE B  21      -0.744  -9.943  30.619  1.00 47.89           C  
ANISOU  890  CD1 PHE B  21     4549   8169   5478   1984    244   1336       C  
ATOM    891  CD2 PHE B  21      -2.637  -9.366  29.306  1.00 47.32           C  
ANISOU  891  CD2 PHE B  21     4991   7151   5836   2001    390   1102       C  
ATOM    892  CE1 PHE B  21      -0.084 -10.378  29.501  1.00 50.70           C  
ANISOU  892  CE1 PHE B  21     4757   8513   5995   1768    221   1360       C  
ATOM    893  CE2 PHE B  21      -1.982  -9.802  28.164  1.00 45.36           C  
ANISOU  893  CE2 PHE B  21     4563   6948   5722   1794    315   1081       C  
ATOM    894  CZ  PHE B  21      -0.700 -10.310  28.263  1.00 46.66           C  
ANISOU  894  CZ  PHE B  21     4431   7530   5766   1695    253   1205       C  
ATOM    895  N   THR B  22      -1.327  -5.933  30.650  1.00 45.73           N  
ANISOU  895  N   THR B  22     5337   7801   4237   2149    103    874       N  
ATOM    896  CA  THR B  22      -1.426  -4.916  29.583  1.00 42.62           C  
ANISOU  896  CA  THR B  22     5349   6854   3992   1799    187    587       C  
ATOM    897  C   THR B  22      -0.482  -5.153  28.398  1.00 41.92           C  
ANISOU  897  C   THR B  22     4707   7116   4103   1531   -132    581       C  
ATOM    898  O   THR B  22       0.589  -5.754  28.538  1.00 39.02           O  
ANISOU  898  O   THR B  22     3771   7487   3567   1326   -435    709       O  
ATOM    899  CB  THR B  22      -1.122  -3.507  30.104  1.00 47.30           C  
ANISOU  899  CB  THR B  22     6763   7288   3921   1074    338    142       C  
ATOM    900  OG1 THR B  22       0.190  -3.506  30.667  1.00 50.41           O  
ANISOU  900  OG1 THR B  22     6942   8564   3648    444    -62      0       O  
ATOM    901  CG2 THR B  22      -2.154  -3.066  31.181  1.00 49.21           C  
ANISOU  901  CG2 THR B  22     7764   6949   3984   1273    836    100       C  
ATOM    902  N   VAL B  23      -0.850  -4.624  27.242  1.00 35.34           N  
ANISOU  902  N   VAL B  23     4057   5738   3634   1526    -19    490       N  
ATOM    903  CA  VAL B  23      -0.070  -4.727  26.033  1.00 33.17           C  
ANISOU  903  CA  VAL B  23     3403   5644   3557   1286   -233    458       C  
ATOM    904  C   VAL B  23       0.269  -3.333  25.564  1.00 35.05           C  
ANISOU  904  C   VAL B  23     4186   5587   3543    737   -146    120       C  
ATOM    905  O   VAL B  23      -0.560  -2.478  25.628  1.00 35.02           O  
ANISOU  905  O   VAL B  23     4758   4964   3583    793    202     41       O  
ATOM    906  CB  VAL B  23      -0.862  -5.479  24.963  1.00 42.34           C  
ANISOU  906  CB  VAL B  23     4319   6393   5376   1655   -158    633       C  
ATOM    907  CG1 VAL B  23      -0.345  -5.254  23.563  1.00 38.71           C  
ANISOU  907  CG1 VAL B  23     3720   5942   5047   1427   -273    557       C  
ATOM    908  CG2 VAL B  23      -0.929  -6.944  25.284  1.00 38.47           C  
ANISOU  908  CG2 VAL B  23     3718   5765   5135   1412   -155    591       C  
ATOM    909  N   THR B  24       1.496  -3.100  25.120  1.00 35.92           N  
ANISOU  909  N   THR B  24     4108   6094   3445    219   -382    -36       N  
ATOM    910  CA  THR B  24       1.915  -1.805  24.632  1.00 38.14           C  
ANISOU  910  CA  THR B  24     4840   6085   3568   -291   -254   -370       C  
ATOM    911  C   THR B  24       2.588  -1.903  23.276  1.00 40.73           C  
ANISOU  911  C   THR B  24     4833   6443   4201   -378   -389   -329       C  
ATOM    912  O   THR B  24       3.078  -2.932  22.922  1.00 43.51           O  
ANISOU  912  O   THR B  24     4608   7161   4762   -229   -607    -95       O  
ATOM    913  CB  THR B  24       2.878  -1.114  25.598  1.00 46.28           C  
ANISOU  913  CB  THR B  24     6103   7498   3985   -979   -360   -693       C  
ATOM    914  OG1 THR B  24       4.027  -1.913  25.765  1.00 46.90           O  
ANISOU  914  OG1 THR B  24     5526   8343   3949  -1168   -801   -505       O  
ATOM    915  CG2 THR B  24       2.246  -0.930  26.930  1.00 47.29           C  
ANISOU  915  CG2 THR B  24     6720   7552   3697   -995   -155   -807       C  
ATOM    916  N   VAL B  25       2.579  -0.831  22.519  1.00 38.94           N  
ANISOU  916  N   VAL B  25     4973   5795   4028   -599   -173   -525       N  
ATOM    917  CA  VAL B  25       3.218  -0.824  21.225  1.00 40.66           C  
ANISOU  917  CA  VAL B  25     4953   5998   4498   -675   -254   -492       C  
ATOM    918  C   VAL B  25       4.124   0.358  21.145  1.00 49.10           C  
ANISOU  918  C   VAL B  25     6279   7003   5372  -1232   -160   -817       C  
ATOM    919  O   VAL B  25       3.670   1.459  20.999  1.00 53.14           O  
ANISOU  919  O   VAL B  25     7264   7039   5889  -1327    220   -994       O  
ATOM    920  CB  VAL B  25       2.234  -0.699  20.078  1.00 54.36           C  
ANISOU  920  CB  VAL B  25     6786   7270   6597   -287    -66   -305       C  
ATOM    921  CG1 VAL B  25       1.591  -2.018  19.766  1.00 59.16           C  
ANISOU  921  CG1 VAL B  25     7254   7870   7356   -425   -110   -312       C  
ATOM    922  CG2 VAL B  25       1.210   0.360  20.374  1.00 51.02           C  
ANISOU  922  CG2 VAL B  25     6067   6894   6423    228   -170     -4       C  
ATOM    923  N   PRO B  26       5.421   0.113  21.192  1.00 53.75           N  
ANISOU  923  N   PRO B  26     6517   8048   5857  -1601   -448   -851       N  
ATOM    924  CA  PRO B  26       6.367   1.232  21.186  1.00 57.08           C  
ANISOU  924  CA  PRO B  26     7149   8423   6116  -2184   -379  -1185       C  
ATOM    925  C   PRO B  26       6.514   1.805  19.778  1.00 52.07           C  
ANISOU  925  C   PRO B  26     6595   7343   5848  -2093   -141  -1199       C  
ATOM    926  O   PRO B  26       6.907   2.947  19.616  1.00 54.90           O  
ANISOU  926  O   PRO B  26     7244   7429   6186  -2431    115  -1491       O  
ATOM    927  CB  PRO B  26       7.667   0.604  21.707  1.00 62.67           C  
ANISOU  927  CB  PRO B  26     7328   9804   6678  -2553   -816  -1057       C  
ATOM    928  CG  PRO B  26       7.572  -0.819  21.361  1.00 61.18           C  
ANISOU  928  CG  PRO B  26     6596   9851   6797  -2078   -975   -596       C  
ATOM    929  CD  PRO B  26       6.089  -1.191  21.326  1.00 56.87           C  
ANISOU  929  CD  PRO B  26     6271   8989   6349  -1508   -781   -528       C  
ATOM    930  N   LYS B  27       6.116   1.044  18.770  1.00 48.04           N  
ANISOU  930  N   LYS B  27     5864   6737   5653  -1640   -169   -897       N  
ATOM    931  CA  LYS B  27       6.121   1.574  17.418  1.00 47.65           C  
ANISOU  931  CA  LYS B  27     5936   6300   5870  -1525     61   -871       C  
ATOM    932  C   LYS B  27       4.809   1.202  16.758  1.00 43.29           C  
ANISOU  932  C   LYS B  27     5455   5533   5462  -1033    155   -615       C  
ATOM    933  O   LYS B  27       4.538   0.025  16.564  1.00 43.91           O  
ANISOU  933  O   LYS B  27     5241   5816   5625   -784    -54   -405       O  
ATOM    934  CB  LYS B  27       7.325   1.029  16.652  1.00 50.64           C  
ANISOU  934  CB  LYS B  27     5951   6835   6454  -1637    -97   -757       C  
ATOM    935  CG  LYS B  27       7.419   1.471  15.203  1.00 53.14           C  
ANISOU  935  CG  LYS B  27     6406   6777   7009  -1504    141   -711       C  
ATOM    936  CD  LYS B  27       8.634   0.840  14.533  1.00 55.35           C  
ANISOU  936  CD  LYS B  27     6369   7136   7526  -1609     60   -568       C  
ATOM    937  CE  LYS B  27       8.934   1.499  13.201  1.00 58.42           C  
ANISOU  937  CE  LYS B  27     6965   7121   8110  -1542    342   -576       C  
ATOM    938  NZ  LYS B  27       9.728   0.608  12.336  1.00 59.37           N  
ANISOU  938  NZ  LYS B  27     6870   7211   8476  -1508    360   -358       N  
ATOM    939  N   GLU B  28       3.974   2.184  16.430  1.00 40.82           N  
ANISOU  939  N   GLU B  28     5487   4813   5209   -909    504   -590       N  
ATOM    940  CA  GLU B  28       2.655   1.841  15.917  1.00 44.01           C  
ANISOU  940  CA  GLU B  28     5894   5079   5749   -480    535   -249       C  
ATOM    941  C   GLU B  28       2.562   1.849  14.390  1.00 44.43           C  
ANISOU  941  C   GLU B  28     5880   5066   5936   -338    548    -30       C  
ATOM    942  O   GLU B  28       1.615   1.293  13.833  1.00 45.11           O  
ANISOU  942  O   GLU B  28     5867   5193   6081    -68    428    267       O  
ATOM    943  CB  GLU B  28       1.585   2.760  16.502  1.00 51.11           C  
ANISOU  943  CB  GLU B  28     7137   5585   6696   -364    941   -155       C  
ATOM    944  CG  GLU B  28       1.802   4.241  16.332  1.00 60.68           C  
ANISOU  944  CG  GLU B  28     8673   6401   7982   -569   1478   -281       C  
ATOM    945  CD  GLU B  28       0.794   5.079  17.152  1.00 65.46           C  
ANISOU  945  CD  GLU B  28     9655   6542   8676   -503   2034   -191       C  
ATOM    946  OE1 GLU B  28      -0.050   4.488  17.874  1.00 56.50           O  
ANISOU  946  OE1 GLU B  28     8540   5398   7530   -281   1942    -26       O  
ATOM    947  OE2 GLU B  28       0.852   6.332  17.068  1.00 74.70           O  
ANISOU  947  OE2 GLU B  28    11104   7297   9982   -661   2649   -268       O  
ATOM    948  N   LEU B  29       3.545   2.447  13.721  1.00 40.79           N  
ANISOU  948  N   LEU B  29     5469   4524   5507   -541    680   -170       N  
ATOM    949  CA  LEU B  29       3.527   2.546  12.267  1.00 39.31           C  
ANISOU  949  CA  LEU B  29     5277   4273   5386   -420    738     34       C  
ATOM    950  C   LEU B  29       4.800   1.981  11.631  1.00 38.09           C  
ANISOU  950  C   LEU B  29     4989   4230   5254   -597    609   -105       C  
ATOM    951  O   LEU B  29       5.900   2.392  11.950  1.00 37.80           O  
ANISOU  951  O   LEU B  29     4942   4128   5293   -841    690   -327       O  
ATOM    952  CB  LEU B  29       3.346   3.999  11.835  1.00 44.93           C  
ANISOU  952  CB  LEU B  29     6213   4638   6222   -380   1213    125       C  
ATOM    953  CG  LEU B  29       3.402   4.281  10.336  1.00 47.96           C  
ANISOU  953  CG  LEU B  29     6598   4986   6640   -245   1322    377       C  
ATOM    954  CD1 LEU B  29       2.344   3.481   9.572  1.00 46.92           C  
ANISOU  954  CD1 LEU B  29     6352   5112   6365    -38   1026    764       C  
ATOM    955  CD2 LEU B  29       3.175   5.756  10.142  1.00 53.44           C  
ANISOU  955  CD2 LEU B  29     7440   5327   7536   -155   1903    524       C  
ATOM    956  N   TYR B  30       4.617   1.027  10.726  1.00 33.10           N  
ANISOU  956  N   TYR B  30     4264   3738   4576   -502    446     46       N  
ATOM    957  CA  TYR B  30       5.703   0.406  10.010  1.00 35.59           C  
ANISOU  957  CA  TYR B  30     4508   4057   4957   -645    452    -17       C  
ATOM    958  C   TYR B  30       5.574   0.797   8.541  1.00 39.60           C  
ANISOU  958  C   TYR B  30     5235   4430   5381   -573    612    125       C  
ATOM    959  O   TYR B  30       4.509   0.663   7.931  1.00 38.67           O  
ANISOU  959  O   TYR B  30     5181   4438   5073   -445    519    331       O  
ATOM    960  CB  TYR B  30       5.648  -1.106  10.169  1.00 32.27           C  
ANISOU  960  CB  TYR B  30     3850   3864   4547   -653    272     10       C  
ATOM    961  CG  TYR B  30       5.931  -1.620  11.574  1.00 34.35           C  
ANISOU  961  CG  TYR B  30     3821   4331   4899   -698    133    -47       C  
ATOM    962  CD1 TYR B  30       7.171  -2.148  11.892  1.00 35.46           C  
ANISOU  962  CD1 TYR B  30     3693   4550   5229   -883    164    -35       C  
ATOM    963  CD2 TYR B  30       4.953  -1.572  12.573  1.00 37.16           C  
ANISOU  963  CD2 TYR B  30     4152   4806   5163   -546     -4    -35       C  
ATOM    964  CE1 TYR B  30       7.450  -2.613  13.160  1.00 40.39           C  
ANISOU  964  CE1 TYR B  30     3990   5466   5892   -936     13      6       C  
ATOM    965  CE2 TYR B  30       5.208  -2.046  13.861  1.00 35.61           C  
ANISOU  965  CE2 TYR B  30     3706   4844   4981   -580   -129    -64       C  
ATOM    966  CZ  TYR B  30       6.450  -2.574  14.151  1.00 38.84           C  
ANISOU  966  CZ  TYR B  30     3807   5431   5519   -781   -147    -33       C  
ATOM    967  OH  TYR B  30       6.709  -3.064  15.417  1.00 37.39           O  
ANISOU  967  OH  TYR B  30     3310   5586   5310   -820   -296     32       O  
ATOM    968  N   ILE B  31       6.653   1.290   7.973  1.00 38.79           N  
ANISOU  968  N   ILE B  31     5228   4095   5417   -660    843     54       N  
ATOM    969  CA  ILE B  31       6.641   1.686   6.582  1.00 38.51           C  
ANISOU  969  CA  ILE B  31     5420   3930   5283   -572   1037    201       C  
ATOM    970  C   ILE B  31       7.670   0.824   5.868  1.00 43.88           C  
ANISOU  970  C   ILE B  31     6155   4480   6037   -718   1141    139       C  
ATOM    971  O   ILE B  31       8.849   0.939   6.117  1.00 46.53           O  
ANISOU  971  O   ILE B  31     6412   4584   6683   -819   1298     50       O  
ATOM    972  CB  ILE B  31       6.948   3.171   6.442  1.00 43.79           C  
ANISOU  972  CB  ILE B  31     6191   4319   6127   -471   1377    219       C  
ATOM    973  CG1 ILE B  31       5.761   3.992   6.965  1.00 47.95           C  
ANISOU  973  CG1 ILE B  31     6704   4902   6612   -311   1439    382       C  
ATOM    974  CG2 ILE B  31       7.230   3.528   5.005  1.00 44.84           C  
ANISOU  974  CG2 ILE B  31     6529   4303   6205   -354   1627    386       C  
ATOM    975  CD1 ILE B  31       6.084   5.446   7.279  1.00 51.11           C  
ANISOU  975  CD1 ILE B  31     7166   4964   7288   -275   1906    310       C  
ATOM    976  N   ILE B  32       7.220  -0.089   5.020  1.00 42.96           N  
ANISOU  976  N   ILE B  32     6170   4495   5659   -773   1086    201       N  
ATOM    977  CA  ILE B  32       8.123  -1.097   4.462  1.00 43.12           C  
ANISOU  977  CA  ILE B  32     6274   4325   5785   -954   1307    135       C  
ATOM    978  C   ILE B  32       8.120  -1.054   2.932  1.00 45.07           C  
ANISOU  978  C   ILE B  32     6939   4453   5734  -1000   1523    193       C  
ATOM    979  O   ILE B  32       7.065  -0.878   2.312  1.00 46.79           O  
ANISOU  979  O   ILE B  32     7302   4963   5514   -980   1335    297       O  
ATOM    980  CB  ILE B  32       7.717  -2.501   4.951  1.00 41.14           C  
ANISOU  980  CB  ILE B  32     5827   4288   5515  -1080   1183     72       C  
ATOM    981  CG1 ILE B  32       7.667  -2.509   6.493  1.00 43.57           C  
ANISOU  981  CG1 ILE B  32     5728   4772   6053  -1001    956     58       C  
ATOM    982  CG2 ILE B  32       8.670  -3.556   4.425  1.00 42.52           C  
ANISOU  982  CG2 ILE B  32     6073   4181   5900  -1278   1587     50       C  
ATOM    983  CD1 ILE B  32       8.978  -2.111   7.138  1.00 47.81           C  
ANISOU  983  CD1 ILE B  32     6066   5123   6975  -1063   1081     74       C  
ATOM    984  N   GLU B  33       9.292  -1.206   2.329  1.00 47.25           N  
ANISOU  984  N   GLU B  33     7398   4311   6243  -1071   1922    181       N  
ATOM    985  CA  GLU B  33       9.390  -1.266   0.878  1.00 51.43           C  
ANISOU  985  CA  GLU B  33     8403   4680   6459  -1144   2198    214       C  
ATOM    986  C   GLU B  33       8.730  -2.523   0.355  1.00 48.95           C  
ANISOU  986  C   GLU B  33     8293   4581   5724  -1451   2169     92       C  
ATOM    987  O   GLU B  33       8.893  -3.626   0.909  1.00 51.23           O  
ANISOU  987  O   GLU B  33     8407   4825   6234  -1618   2264    -19       O  
ATOM    988  CB  GLU B  33      10.842  -1.217   0.416  1.00 59.64           C  
ANISOU  988  CB  GLU B  33     9507   5260   7894  -1047   2594    200       C  
ATOM    989  CG  GLU B  33      11.622  -0.080   0.998  1.00 64.78           C  
ANISOU  989  CG  GLU B  33     9851   5788   8976   -786   2570    246       C  
ATOM    990  CD  GLU B  33      12.555   0.549   0.001  1.00 77.49           C  
ANISOU  990  CD  GLU B  33    11587   7179  10676   -562   2848    268       C  
ATOM    991  OE1 GLU B  33      12.894  -0.122  -1.006  1.00 81.94           O  
ANISOU  991  OE1 GLU B  33    12412   7654  11067   -592   3069    227       O  
ATOM    992  OE2 GLU B  33      12.942   1.724   0.223  1.00 82.24           O  
ANISOU  992  OE2 GLU B  33    12025   7703  11520   -371   2889    301       O  
ATOM    993  N   HIS B  34       7.929  -2.334  -0.676  1.00 44.67           N  
ANISOU  993  N   HIS B  34     4623   8075   4274    780    -88    192       N  
ATOM    994  CA  HIS B  34       7.298  -3.433  -1.384  1.00 48.78           C  
ANISOU  994  CA  HIS B  34     4864   9335   4335    137     25   -163       C  
ATOM    995  C   HIS B  34       8.246  -4.623  -1.634  1.00 46.34           C  
ANISOU  995  C   HIS B  34     4848   8489   4270   -488    387   -595       C  
ATOM    996  O   HIS B  34       9.374  -4.436  -2.071  1.00 42.45           O  
ANISOU  996  O   HIS B  34     4652   7423   4053   -463    507   -501       O  
ATOM    997  CB  HIS B  34       6.763  -2.935  -2.722  1.00 56.08           C  
ANISOU  997  CB  HIS B  34     5459  11213   4636    123   -114     92       C  
ATOM    998  CG  HIS B  34       5.878  -3.927  -3.392  1.00 62.90           C  
ANISOU  998  CG  HIS B  34     5962  13061   4875   -595    -58   -263       C  
ATOM    999  ND1 HIS B  34       6.324  -4.763  -4.393  1.00 71.37           N  
ANISOU  999  ND1 HIS B  34     7164  14274   5678  -1324    195   -654       N  
ATOM   1000  CD2 HIS B  34       4.589  -4.264  -3.159  1.00 65.09           C  
ANISOU 1000  CD2 HIS B  34     5777  14207   4749   -770   -177   -330       C  
ATOM   1001  CE1 HIS B  34       5.331  -5.549  -4.777  1.00 78.01           C  
ANISOU 1001  CE1 HIS B  34     7651  16034   5954  -1968    221   -976       C  
ATOM   1002  NE2 HIS B  34       4.271  -5.272  -4.038  1.00 75.05           N  
ANISOU 1002  NE2 HIS B  34     6884  16089   5542  -1636    -19   -762       N  
ATOM   1003  N   GLY B  35       7.778  -5.843  -1.370  1.00 46.16           N  
ANISOU 1003  N   GLY B  35     4738   8627   4175  -1038    626  -1040       N  
ATOM   1004  CA  GLY B  35       8.616  -7.019  -1.521  1.00 47.20           C  
ANISOU 1004  CA  GLY B  35     5155   8160   4617  -1588   1113  -1416       C  
ATOM   1005  C   GLY B  35       9.688  -7.266  -0.438  1.00 41.02           C  
ANISOU 1005  C   GLY B  35     4676   6302   4608  -1363   1285  -1304       C  
ATOM   1006  O   GLY B  35      10.420  -8.245  -0.528  1.00 44.43           O  
ANISOU 1006  O   GLY B  35     5308   6190   5382  -1739   1764  -1503       O  
ATOM   1007  N  ASER B  36       9.775  -6.418   0.582  0.24 37.94           N  
ANISOU 1007  N  ASER B  36     4308   5630   4477   -791    948   -970       N  
ATOM   1008  N  BSER B  36       9.786  -6.394   0.564  0.76 37.11           N  
ANISOU 1008  N  BSER B  36     4205   5526   4370   -784    943   -963       N  
ATOM   1009  CA ASER B  36      10.718  -6.697   1.668  0.24 36.08           C  
ANISOU 1009  CA ASER B  36     4282   4558   4867   -669   1060   -836       C  
ATOM   1010  CA BSER B  36      10.704  -6.653   1.676  0.76 36.59           C  
ANISOU 1010  CA BSER B  36     4346   4632   4925   -652   1044   -827       C  
ATOM   1011  C  ASER B  36      10.004  -7.122   2.951  0.24 35.38           C  
ANISOU 1011  C  ASER B  36     4068   4524   4852   -627   1018   -928       C  
ATOM   1012  C  BSER B  36       9.953  -7.316   2.830  0.76 36.23           C  
ANISOU 1012  C  BSER B  36     4160   4670   4935   -717   1084   -989       C  
ATOM   1013  O  ASER B  36       8.863  -6.733   3.201  0.24 34.94           O  
ANISOU 1013  O  ASER B  36     3804   5040   4432   -465    778   -975       O  
ATOM   1014  O  BSER B  36       8.724  -7.301   2.850  0.76 35.46           O  
ANISOU 1014  O  BSER B  36     3817   5235   4422   -745    954  -1152       O  
ATOM   1015  CB ASER B  36      11.613  -5.488   1.941  0.24 36.35           C  
ANISOU 1015  CB ASER B  36     4513   4132   5166   -189    767   -419       C  
ATOM   1016  CB BSER B  36      11.383  -5.364   2.150  0.76 36.69           C  
ANISOU 1016  CB BSER B  36     4526   4252   5163   -119    695   -414       C  
ATOM   1017  OG ASER B  36      10.858  -4.361   2.329  0.24 37.10           O  
ANISOU 1017  OG ASER B  36     4540   4548   5009    255    394   -261       O  
ATOM   1018  OG BSER B  36      12.329  -4.899   1.186  0.76 39.17           O  
ANISOU 1018  OG BSER B  36     5002   4309   5570    -86    739   -235       O  
ATOM   1019  N   ASP B  37      10.698  -7.923   3.754  1.00 36.58           N  
ANISOU 1019  N   ASP B  37     4318   4092   5487   -747   1282   -890       N  
ATOM   1020  CA  ASP B  37      10.130  -8.523   4.984  1.00 37.16           C  
ANISOU 1020  CA  ASP B  37     4280   4172   5669   -761   1328   -962       C  
ATOM   1021  C   ASP B  37       9.856  -7.496   6.085  1.00 35.60           C  
ANISOU 1021  C   ASP B  37     4103   4009   5414   -299    877   -735       C  
ATOM   1022  O   ASP B  37      10.470  -6.457   6.119  1.00 36.66           O  
ANISOU 1022  O   ASP B  37     4403   3919   5608     -4    611   -480       O  
ATOM   1023  CB  ASP B  37      11.083  -9.583   5.575  1.00 38.44           C  
ANISOU 1023  CB  ASP B  37     4514   3691   6402   -937   1751   -826       C  
ATOM   1024  CG  ASP B  37      11.277 -10.783   4.673  1.00 43.73           C  
ANISOU 1024  CG  ASP B  37     5311   4367   6939  -1103   2102  -1054       C  
ATOM   1025  OD1 ASP B  37      10.839 -10.752   3.517  1.00 44.18           O  
ANISOU 1025  OD1 ASP B  37     5386   4702   6697  -1423   2215  -1364       O  
ATOM   1026  OD2 ASP B  37      11.841 -11.788   5.126  1.00 44.73           O  
ANISOU 1026  OD2 ASP B  37     5497   4257   7241   -937   2273   -951       O  
ATOM   1027  N   VAL B  38       8.970  -7.814   7.024  1.00 35.97           N  
ANISOU 1027  N   VAL B  38     4016   4286   5364   -273    854   -848       N  
ATOM   1028  CA  VAL B  38       8.783  -6.937   8.176  1.00 33.63           C  
ANISOU 1028  CA  VAL B  38     3808   3936   5033    106    532   -670       C  
ATOM   1029  C   VAL B  38       8.447  -7.770   9.404  1.00 34.40           C  
ANISOU 1029  C   VAL B  38     3822   3988   5259      4    666   -717       C  
ATOM   1030  O   VAL B  38       7.878  -8.855   9.295  1.00 34.50           O  
ANISOU 1030  O   VAL B  38     3648   4186   5275   -284    971   -943       O  
ATOM   1031  CB  VAL B  38       7.692  -5.892   7.944  1.00 33.85           C  
ANISOU 1031  CB  VAL B  38     3754   4465   4644    444    285   -697       C  
ATOM   1032  CG1 VAL B  38       6.288  -6.541   7.830  1.00 36.65           C  
ANISOU 1032  CG1 VAL B  38     3763   5477   4684    297    391   -950       C  
ATOM   1033  CG2 VAL B  38       7.674  -4.885   9.085  1.00 37.72           C  
ANISOU 1033  CG2 VAL B  38     4457   4732   5143    817     73   -536       C  
ATOM   1034  N   THR B  39       8.856  -7.279  10.564  1.00 37.67           N  
ANISOU 1034  N   THR B  39     4392   4152   5770    189    471   -504       N  
ATOM   1035  CA  THR B  39       8.531  -7.921  11.831  1.00 36.24           C  
ANISOU 1035  CA  THR B  39     4139   3981   5649    135    553   -488       C  
ATOM   1036  C   THR B  39       7.718  -6.941  12.674  1.00 34.97           C  
ANISOU 1036  C   THR B  39     4090   4029   5168    437    300   -542       C  
ATOM   1037  O   THR B  39       8.221  -5.906  13.110  1.00 38.33           O  
ANISOU 1037  O   THR B  39     4781   4243   5538    597     71   -409       O  
ATOM   1038  CB  THR B  39       9.795  -8.354  12.590  1.00 43.87           C  
ANISOU 1038  CB  THR B  39     5159   4530   6978      9    595   -129       C  
ATOM   1039  OG1 THR B  39      10.460  -9.401  11.863  1.00 42.54           O  
ANISOU 1039  OG1 THR B  39     4869   4111   7184   -230    984    -42       O  
ATOM   1040  CG2 THR B  39       9.413  -8.872  13.954  1.00 47.38           C  
ANISOU 1040  CG2 THR B  39     5524   5071   7406    -11    636    -55       C  
ATOM   1041  N   LEU B  40       6.435  -7.223  12.841  1.00 30.76           N  
ANISOU 1041  N   LEU B  40     3364   3903   4419    494    392   -753       N  
ATOM   1042  CA  LEU B  40       5.551  -6.330  13.601  1.00 32.50           C  
ANISOU 1042  CA  LEU B  40     3676   4308   4365    823    262   -790       C  
ATOM   1043  C   LEU B  40       5.532  -6.811  15.075  1.00 37.02           C  
ANISOU 1043  C   LEU B  40     4311   4781   4973    743    313   -755       C  
ATOM   1044  O   LEU B  40       5.585  -8.017  15.341  1.00 37.32           O  
ANISOU 1044  O   LEU B  40     4157   4829   5192    491    514   -751       O  
ATOM   1045  CB  LEU B  40       4.139  -6.329  13.019  1.00 36.32           C  
ANISOU 1045  CB  LEU B  40     3850   5363   4588    960    332   -947       C  
ATOM   1046  CG  LEU B  40       4.041  -6.109  11.490  1.00 45.78           C  
ANISOU 1046  CG  LEU B  40     4870   6857   5668    941    294   -955       C  
ATOM   1047  CD1 LEU B  40       2.646  -6.421  10.967  1.00 48.96           C  
ANISOU 1047  CD1 LEU B  40     4836   7996   5770    915    358  -1076       C  
ATOM   1048  CD2 LEU B  40       4.397  -4.681  11.142  1.00 47.82           C  
ANISOU 1048  CD2 LEU B  40     5366   6934   5870   1330    119   -745       C  
ATOM   1049  N   GLU B  41       5.446  -5.880  16.017  1.00 34.50           N  
ANISOU 1049  N   GLU B  41     4277   4359   4474    938    190   -728       N  
ATOM   1050  CA  GLU B  41       5.673  -6.243  17.410  1.00 36.14           C  
ANISOU 1050  CA  GLU B  41     4590   4488   4653    793    193   -654       C  
ATOM   1051  C   GLU B  41       4.801  -5.494  18.382  1.00 35.37           C  
ANISOU 1051  C   GLU B  41     4708   4481   4250   1017    225   -788       C  
ATOM   1052  O   GLU B  41       4.434  -4.331  18.165  1.00 35.79           O  
ANISOU 1052  O   GLU B  41     4988   4460   4152   1301    225   -869       O  
ATOM   1053  CB  GLU B  41       7.139  -6.005  17.773  1.00 41.04           C  
ANISOU 1053  CB  GLU B  41     5426   4789   5379    563      0   -408       C  
ATOM   1054  CG  GLU B  41       8.104  -6.958  17.074  1.00 49.77           C  
ANISOU 1054  CG  GLU B  41     6292   5756   6863    340     67   -177       C  
ATOM   1055  CD  GLU B  41       9.578  -6.630  17.356  1.00 57.67           C  
ANISOU 1055  CD  GLU B  41     7427   6508   7977    137   -147    157       C  
ATOM   1056  OE1 GLU B  41       9.882  -5.449  17.648  1.00 58.68           O  
ANISOU 1056  OE1 GLU B  41     7885   6534   7876    145   -375    107       O  
ATOM   1057  OE2 GLU B  41      10.424  -7.551  17.289  1.00 61.84           O  
ANISOU 1057  OE2 GLU B  41     7721   6940   8834    -43    -41    490       O  
ATOM   1058  N   CYS B  42       4.458  -6.166  19.469  1.00 31.21           N  
ANISOU 1058  N   CYS B  42     4119   4085   3653    909    321   -784       N  
ATOM   1059  CA  CYS B  42       3.902  -5.459  20.588  1.00 33.63           C  
ANISOU 1059  CA  CYS B  42     4725   4400   3653   1037    373   -897       C  
ATOM   1060  C   CYS B  42       4.404  -6.176  21.834  1.00 34.18           C  
ANISOU 1060  C   CYS B  42     4815   4520   3653    725    339   -747       C  
ATOM   1061  O   CYS B  42       4.823  -7.349  21.766  1.00 35.93           O  
ANISOU 1061  O   CYS B  42     4713   4812   4127    531    371   -536       O  
ATOM   1062  CB  CYS B  42       2.349  -5.381  20.534  1.00 47.34           C  
ANISOU 1062  CB  CYS B  42     6285   6418   5283   1388    612  -1061       C  
ATOM   1063  SG  CYS B  42       1.472  -6.981  20.617  1.00 54.10           S  
ANISOU 1063  SG  CYS B  42     6605   7676   6276   1269    806  -1080       S  
ATOM   1064  N   ASN B  43       4.430  -5.438  22.940  1.00 36.79           N  
ANISOU 1064  N   ASN B  43     5539   4802   3638    656    315   -828       N  
ATOM   1065  CA  ASN B  43       5.008  -5.917  24.168  1.00 38.29           C  
ANISOU 1065  CA  ASN B  43     5777   5131   3642    310    222   -640       C  
ATOM   1066  C   ASN B  43       3.931  -6.211  25.187  1.00 44.89           C  
ANISOU 1066  C   ASN B  43     6626   6187   4245    411    453   -764       C  
ATOM   1067  O   ASN B  43       2.837  -5.661  25.112  1.00 41.32           O  
ANISOU 1067  O   ASN B  43     6294   5706   3700    736    677  -1032       O  
ATOM   1068  CB  ASN B  43       5.969  -4.877  24.742  1.00 48.07           C  
ANISOU 1068  CB  ASN B  43     7481   6232   4553    -12      3   -660       C  
ATOM   1069  CG  ASN B  43       7.024  -4.462  23.739  1.00 50.32           C  
ANISOU 1069  CG  ASN B  43     7775   6275   5068   -102   -212   -541       C  
ATOM   1070  OD1 ASN B  43       7.325  -3.290  23.587  1.00 57.91           O  
ANISOU 1070  OD1 ASN B  43     9149   6978   5877   -149   -254   -733       O  
ATOM   1071  ND2 ASN B  43       7.574  -5.423  23.044  1.00 44.09           N  
ANISOU 1071  ND2 ASN B  43     6554   5525   4673   -124   -277   -232       N  
ATOM   1072  N   PHE B  44       4.234  -7.060  26.162  1.00 43.33           N  
ANISOU 1072  N   PHE B  44     6281   6226   3957    159    428   -510       N  
ATOM   1073  CA  PHE B  44       3.262  -7.240  27.227  1.00 45.35           C  
ANISOU 1073  CA  PHE B  44     6609   6685   3936    233    653   -629       C  
ATOM   1074  C   PHE B  44       3.932  -7.209  28.581  1.00 53.45           C  
ANISOU 1074  C   PHE B  44     7849   7939   4521   -174    505   -446       C  
ATOM   1075  O   PHE B  44       5.112  -7.564  28.721  1.00 52.80           O  
ANISOU 1075  O   PHE B  44     7615   7986   4459   -503    239    -56       O  
ATOM   1076  CB  PHE B  44       2.460  -8.525  27.017  1.00 44.67           C  
ANISOU 1076  CB  PHE B  44     6024   6763   4187    413    903   -530       C  
ATOM   1077  CG  PHE B  44       3.297  -9.747  26.877  1.00 48.06           C  
ANISOU 1077  CG  PHE B  44     6052   7242   4965    211    877   -101       C  
ATOM   1078  CD1 PHE B  44       3.613 -10.508  27.985  1.00 53.57           C  
ANISOU 1078  CD1 PHE B  44     6616   8174   5564     25    918    270       C  
ATOM   1079  CD2 PHE B  44       3.765 -10.146  25.622  1.00 52.78           C  
ANISOU 1079  CD2 PHE B  44     6404   7647   6004    224    877    -29       C  
ATOM   1080  CE1 PHE B  44       4.386 -11.648  27.858  1.00 56.93           C  
ANISOU 1080  CE1 PHE B  44     6641   8603   6387    -90   1000    768       C  
ATOM   1081  CE2 PHE B  44       4.537 -11.288  25.478  1.00 52.65           C  
ANISOU 1081  CE2 PHE B  44     6042   7584   6377     72    989    391       C  
ATOM   1082  CZ  PHE B  44       4.850 -12.041  26.609  1.00 55.11           C  
ANISOU 1082  CZ  PHE B  44     6196   8093   6649    -57   1072    822       C  
ATOM   1083  N   ASP B  45       3.155  -6.759  29.566  1.00 60.34           N  
ANISOU 1083  N   ASP B  45     9058   8898   4972   -159    700   -704       N  
ATOM   1084  CA  ASP B  45       3.655  -6.433  30.889  1.00 69.25           C  
ANISOU 1084  CA  ASP B  45    10529  10277   5505   -614    586   -666       C  
ATOM   1085  C   ASP B  45       2.883  -7.200  31.942  1.00 78.36           C  
ANISOU 1085  C   ASP B  45    11552  11755   6468   -573    812   -569       C  
ATOM   1086  O   ASP B  45       1.640  -7.122  32.030  1.00 76.11           O  
ANISOU 1086  O   ASP B  45    11338  11369   6213   -211   1171   -855       O  
ATOM   1087  CB  ASP B  45       3.554  -4.929  31.156  1.00 71.36           C  
ANISOU 1087  CB  ASP B  45    11510  10264   5339   -742    692  -1162       C  
ATOM   1088  N   THR B  46       3.654  -7.942  32.725  1.00117.53           N  
ANISOU 1088  N   THR B  46    18518  13246  12891   -716    857  -1346       N  
ATOM   1089  CA  THR B  46       3.159  -8.792  33.785  1.00122.03           C  
ANISOU 1089  CA  THR B  46    18844  14174  13349   -633   1011  -1350       C  
ATOM   1090  C   THR B  46       4.152  -8.726  34.941  1.00125.08           C  
ANISOU 1090  C   THR B  46    19190  14916  13418  -1019    900  -1209       C  
ATOM   1091  O   THR B  46       5.354  -8.573  34.718  1.00128.01           O  
ANISOU 1091  O   THR B  46    19514  15362  13762  -1288    753   -976       O  
ATOM   1092  CB  THR B  46       2.995 -10.241  33.306  1.00124.30           C  
ANISOU 1092  CB  THR B  46    18746  14629  13853   -407   1185  -1043       C  
ATOM   1093  OG1 THR B  46       2.312 -10.997  34.309  1.00124.51           O  
ANISOU 1093  OG1 THR B  46    18550  14813  13946   -597   1092   -637       O  
ATOM   1094  CG2 THR B  46       4.362 -10.878  33.051  1.00123.96           C  
ANISOU 1094  CG2 THR B  46    18739  14229  14130    -13   1291  -1192       C  
ATOM   1095  N   GLY B  47       3.658  -8.837  36.170  1.00125.71           N  
ANISOU 1095  N   GLY B  47    19292  15218  13255  -1067    970  -1377       N  
ATOM   1096  CA  GLY B  47       4.515  -8.742  37.342  1.00122.63           C  
ANISOU 1096  CA  GLY B  47    18916  15139  12537  -1426    842  -1269       C  
ATOM   1097  C   GLY B  47       4.897 -10.072  37.975  1.00116.92           C  
ANISOU 1097  C   GLY B  47    17915  14796  11712  -1485    867   -929       C  
ATOM   1098  O   GLY B  47       5.089 -10.155  39.186  1.00120.04           O  
ANISOU 1098  O   GLY B  47    18382  15439  11790  -1710    814   -934       O  
ATOM   1099  N   SER B  48       4.995 -11.095  37.155  1.00112.19           N  
ANISOU 1099  N   SER B  48    17038  14218  11371  -1287    925   -643       N  
ATOM   1100  CA  SER B  48       5.372 -12.390  37.667  1.00107.95           C  
ANISOU 1100  CA  SER B  48    16268  13993  10755  -1315    894   -313       C  
ATOM   1101  C   SER B  48       6.014 -13.170  36.570  1.00104.79           C  
ANISOU 1101  C   SER B  48    15547  13588  10680  -1173    842     14       C  
ATOM   1102  O   SER B  48       5.763 -12.937  35.410  1.00 98.98           O  
ANISOU 1102  O   SER B  48    14774  12605  10229   -991    934    -28       O  
ATOM   1103  CB  SER B  48       4.136 -13.109  38.185  1.00103.44           C  
ANISOU 1103  CB  SER B  48    15726  13493  10082  -1158   1140   -433       C  
ATOM   1104  N   HIS B  49       6.807 -14.142  36.949  1.00106.08           N  
ANISOU 1104  N   HIS B  49    15492  14016  10799  -1247    678    326       N  
ATOM   1105  CA  HIS B  49       7.725 -14.723  36.032  1.00109.44           C  
ANISOU 1105  CA  HIS B  49    15581  14485  11516  -1189    558    591       C  
ATOM   1106  C   HIS B  49       6.799 -15.237  34.976  1.00109.74           C  
ANISOU 1106  C   HIS B  49    15515  14332  11849   -845    808    610       C  
ATOM   1107  O   HIS B  49       5.643 -15.491  35.257  1.00110.33           O  
ANISOU 1107  O   HIS B  49    15713  14352  11854   -677   1012    489       O  
ATOM   1108  CB  HIS B  49       8.432 -15.892  36.690  1.00111.32           C  
ANISOU 1108  CB  HIS B  49    15610  15015  11670  -1226    328    883       C  
ATOM   1109  N   VAL B  50       7.253 -15.286  33.737  1.00108.29           N  
ANISOU 1109  N   VAL B  50    15126  14033  11987   -761    815    711       N  
ATOM   1110  CA  VAL B  50       6.320 -15.373  32.640  1.00103.91           C  
ANISOU 1110  CA  VAL B  50    14573  13208  11701   -462   1049    650       C  
ATOM   1111  C   VAL B  50       6.006 -16.830  32.475  1.00100.58           C  
ANISOU 1111  C   VAL B  50    13867  12923  11427   -203   1127    904       C  
ATOM   1112  O   VAL B  50       6.870 -17.628  32.146  1.00100.44           O  
ANISOU 1112  O   VAL B  50    13531  13068  11562   -202    992   1166       O  
ATOM   1113  CB  VAL B  50       6.881 -14.791  31.330  1.00102.46           C  
ANISOU 1113  CB  VAL B  50    14355  12807  11769   -517   1040    645       C  
ATOM   1114  N   ASN B  51       4.916 -17.223  33.099  1.00 99.47           N  
ANISOU 1114  N   ASN B  51    13835  12720  11240     11   1339    792       N  
ATOM   1115  CA  ASN B  51       4.611 -18.631  33.226  1.00 96.35           C  
ANISOU 1115  CA  ASN B  51    13313  12537  10760    111   1373    993       C  
ATOM   1116  C   ASN B  51       4.181 -19.295  32.000  1.00 91.66           C  
ANISOU 1116  C   ASN B  51    12464  11860  10504    439   1523   1164       C  
ATOM   1117  O   ASN B  51       3.990 -20.509  31.981  1.00 88.58           O  
ANISOU 1117  O   ASN B  51    12002  11577  10076    573   1613   1295       O  
ATOM   1118  CB  ASN B  51       3.725 -18.823  34.446  1.00 96.71           C  
ANISOU 1118  CB  ASN B  51    13633  12621  10492     66   1543    740       C  
ATOM   1119  N   LEU B  52       4.102 -18.525  30.936  1.00 90.63           N  
ANISOU 1119  N   LEU B  52    12236  11516  10683    545   1559   1148       N  
ATOM   1120  CA  LEU B  52       3.542 -19.122  29.782  1.00 88.19           C  
ANISOU 1120  CA  LEU B  52    11845  10996  10666    882   1789   1126       C  
ATOM   1121  C   LEU B  52       4.042 -20.065  28.732  1.00 86.56           C  
ANISOU 1121  C   LEU B  52    11328  10766  10794    968   1736   1386       C  
ATOM   1122  O   LEU B  52       4.939 -19.772  27.983  1.00 85.97           O  
ANISOU 1122  O   LEU B  52    11233  10645  10785    772   1611   1388       O  
ATOM   1123  CB  LEU B  52       2.987 -17.897  29.127  1.00 87.40           C  
ANISOU 1123  CB  LEU B  52    12047  10564  10597    956   1908    749       C  
ATOM   1124  N   GLY B  53       3.385 -21.212  28.727  1.00 84.58           N  
ANISOU 1124  N   GLY B  53    10839  10549  10747   1240   1849   1579       N  
ATOM   1125  CA  GLY B  53       2.553 -21.755  27.687  1.00 84.37           C  
ANISOU 1125  CA  GLY B  53    10850  10259  10948   1555   2095   1462       C  
ATOM   1126  C   GLY B  53       1.089 -21.401  27.848  1.00 85.94           C  
ANISOU 1126  C   GLY B  53    11213  10451  10989   1700   2294   1243       C  
ATOM   1127  O   GLY B  53       0.232 -22.016  27.250  1.00 86.95           O  
ANISOU 1127  O   GLY B  53    11206  10585  11247   1953   2471   1307       O  
ATOM   1128  N   ALA B  54       0.817 -20.472  28.752  1.00 83.82           N  
ANISOU 1128  N   ALA B  54    11232  10166  10448   1525   2279    944       N  
ATOM   1129  CA  ALA B  54      -0.485 -19.895  29.019  1.00 77.01           C  
ANISOU 1129  CA  ALA B  54    10581   9123   9555   1680   2477    521       C  
ATOM   1130  C   ALA B  54      -0.697 -18.644  28.130  1.00 71.62           C  
ANISOU 1130  C   ALA B  54    10094   8043   9075   1795   2434    260       C  
ATOM   1131  O   ALA B  54      -1.736 -18.011  28.141  1.00 71.58           O  
ANISOU 1131  O   ALA B  54    10269   7822   9106   1969   2529   -144       O  
ATOM   1132  CB  ALA B  54      -0.589 -19.520  30.484  1.00 76.88           C  
ANISOU 1132  CB  ALA B  54    10777   9291   9144   1426   2475    290       C  
ATOM   1133  N   ILE B  55       0.303 -18.295  27.355  1.00 67.24           N  
ANISOU 1133  N   ILE B  55     9520   7385   8645   1680   2273    468       N  
ATOM   1134  CA  ILE B  55       0.181 -17.161  26.501  1.00 66.95           C  
ANISOU 1134  CA  ILE B  55     9762   6940   8736   1717   2194    252       C  
ATOM   1135  C   ILE B  55      -0.157 -17.502  25.074  1.00 67.05           C  
ANISOU 1135  C   ILE B  55     9688   6686   9103   2023   2285    333       C  
ATOM   1136  O   ILE B  55       0.469 -18.340  24.478  1.00 66.51           O  
ANISOU 1136  O   ILE B  55     9325   6746   9200   2041   2320    679       O  
ATOM   1137  CB  ILE B  55       1.494 -16.386  26.484  1.00 67.80           C  
ANISOU 1137  CB  ILE B  55     9989   7041   8732   1340   1982    365       C  
ATOM   1138  CG1 ILE B  55       1.484 -15.310  27.538  1.00 72.90           C  
ANISOU 1138  CG1 ILE B  55    10914   7730   9053   1096   1865    103       C  
ATOM   1139  CG2 ILE B  55       1.736 -15.695  25.159  1.00 65.66           C  
ANISOU 1139  CG2 ILE B  55     9961   6339   8646   1360   1918    298       C  
ATOM   1140  CD1 ILE B  55       2.739 -14.496  27.542  1.00 76.42           C  
ANISOU 1140  CD1 ILE B  55    11438   8252   9345    687   1670    213       C  
ATOM   1141  N   THR B  56      -1.217 -16.911  24.585  1.00 47.66           N  
ANISOU 1141  N   THR B  56     8634   4154   5321    642   2450    802       N  
ATOM   1142  CA  THR B  56      -1.536 -16.897  23.172  1.00 51.32           C  
ANISOU 1142  CA  THR B  56     8646   4778   6076    310   2315    562       C  
ATOM   1143  C   THR B  56      -1.153 -15.501  22.668  1.00 49.38           C  
ANISOU 1143  C   THR B  56     7913   5043   5808    283   1829    539       C  
ATOM   1144  O   THR B  56      -1.229 -14.530  23.418  1.00 51.69           O  
ANISOU 1144  O   THR B  56     8163   5456   6019    328   1732    629       O  
ATOM   1145  CB  THR B  56      -3.043 -17.190  22.918  1.00 71.03           C  
ANISOU 1145  CB  THR B  56    11004   7017   8969   -160   2661    363       C  
ATOM   1146  OG1 THR B  56      -3.392 -18.445  23.501  1.00 74.68           O  
ANISOU 1146  OG1 THR B  56    11963   6931   9481   -162   3206    391       O  
ATOM   1147  CG2 THR B  56      -3.354 -17.244  21.424  1.00 70.90           C  
ANISOU 1147  CG2 THR B  56    10553   7209   9177   -477   2444     84       C  
ATOM   1148  N   ALA B  57      -0.700 -15.387  21.427  1.00 41.88           N  
ANISOU 1148  N   ALA B  57     6653   4356   4905    224   1567    422       N  
ATOM   1149  CA  ALA B  57      -0.611 -14.082  20.809  1.00 33.93           C  
ANISOU 1149  CA  ALA B  57     5202   3751   3940    128   1222    392       C  
ATOM   1150  C   ALA B  57      -1.081 -14.236  19.399  1.00 35.38           C  
ANISOU 1150  C   ALA B  57     5115   4048   4278   -121   1144    196       C  
ATOM   1151  O   ALA B  57      -0.800 -15.244  18.771  1.00 38.27           O  
ANISOU 1151  O   ALA B  57     5632   4294   4616   -113   1231     91       O  
ATOM   1152  CB  ALA B  57       0.857 -13.530  20.835  1.00 36.33           C  
ANISOU 1152  CB  ALA B  57     5430   4344   4029    426    919    505       C  
ATOM   1153  N   SER B  58      -1.749 -13.224  18.873  1.00 35.97           N  
ANISOU 1153  N   SER B  58     4823   4361   4482   -305    969    149       N  
ATOM   1154  CA  SER B  58      -2.133 -13.252  17.472  1.00 38.71           C  
ANISOU 1154  CA  SER B  58     4923   4898   4886   -483    804    -26       C  
ATOM   1155  C   SER B  58      -2.071 -11.861  16.920  1.00 37.40           C  
ANISOU 1155  C   SER B  58     4439   5079   4693   -447    534     63       C  
ATOM   1156  O   SER B  58      -2.246 -10.867  17.651  1.00 35.31           O  
ANISOU 1156  O   SER B  58     4080   4849   4486   -405    533    201       O  
ATOM   1157  CB  SER B  58      -3.550 -13.819  17.295  1.00 53.42           C  
ANISOU 1157  CB  SER B  58     6670   6615   7014   -815    939   -237       C  
ATOM   1158  OG  SER B  58      -3.592 -15.182  17.691  1.00 64.20           O  
ANISOU 1158  OG  SER B  58     8381   7587   8426   -884   1266   -339       O  
ATOM   1159  N   LEU B  59      -1.827 -11.788  15.617  1.00 32.74           N  
ANISOU 1159  N   LEU B  59     3739   4711   3990   -452    346    -16       N  
ATOM   1160  CA  LEU B  59      -1.876 -10.533  14.926  1.00 33.05           C  
ANISOU 1160  CA  LEU B  59     3528   5044   3984   -404    137     82       C  
ATOM   1161  C   LEU B  59      -3.023 -10.604  13.914  1.00 43.26           C  
ANISOU 1161  C   LEU B  59     4615   6503   5320   -573    -36    -80       C  
ATOM   1162  O   LEU B  59      -2.955 -11.349  12.937  1.00 47.27           O  
ANISOU 1162  O   LEU B  59     5211   7069   5679   -635   -123   -265       O  
ATOM   1163  CB  LEU B  59      -0.544 -10.237  14.247  1.00 35.74           C  
ANISOU 1163  CB  LEU B  59     3937   5528   4113   -214     79    168       C  
ATOM   1164  CG  LEU B  59      -0.479  -8.825  13.679  1.00 36.52           C  
ANISOU 1164  CG  LEU B  59     3849   5853   4173   -142    -37    322       C  
ATOM   1165  CD1 LEU B  59      -0.232  -7.796  14.759  1.00 35.91           C  
ANISOU 1165  CD1 LEU B  59     3705   5716   4223   -100     31    481       C  
ATOM   1166  CD2 LEU B  59       0.580  -8.796  12.670  1.00 39.62           C  
ANISOU 1166  CD2 LEU B  59     4320   6366   4367    -13    -33    350       C  
ATOM   1167  N   GLN B  60      -4.081  -9.846  14.153  1.00 39.57           N  
ANISOU 1167  N   GLN B  60     3869   6119   5047   -635    -96    -28       N  
ATOM   1168  CA  GLN B  60      -5.260  -9.955  13.305  1.00 44.90           C  
ANISOU 1168  CA  GLN B  60     4262   6996   5803   -782   -315   -200       C  
ATOM   1169  C   GLN B  60      -5.456  -8.737  12.424  1.00 42.61           C  
ANISOU 1169  C   GLN B  60     3772   7041   5378   -591   -578    -38       C  
ATOM   1170  O   GLN B  60      -5.641  -7.623  12.914  1.00 38.62           O  
ANISOU 1170  O   GLN B  60     3138   6547   4989   -453   -519    192       O  
ATOM   1171  CB  GLN B  60      -6.487 -10.178  14.165  1.00 46.57           C  
ANISOU 1171  CB  GLN B  60     4236   7057   6401   -985   -165   -284       C  
ATOM   1172  CG  GLN B  60      -6.467 -11.510  14.903  1.00 54.37           C  
ANISOU 1172  CG  GLN B  60     5469   7672   7519  -1191    144   -457       C  
ATOM   1173  CD  GLN B  60      -6.650 -12.710  13.974  1.00 64.33           C  
ANISOU 1173  CD  GLN B  60     6785   8929   8728  -1425     48   -798       C  
ATOM   1174  OE1 GLN B  60      -7.229 -12.588  12.885  1.00 71.72           O  
ANISOU 1174  OE1 GLN B  60     7460  10177   9613  -1514   -290   -971       O  
ATOM   1175  NE2 GLN B  60      -6.177 -13.874  14.408  1.00 63.51           N  
ANISOU 1175  NE2 GLN B  60     7052   8463   8617  -1509    346   -901       N  
ATOM   1176  N   LYS B  61      -5.452  -8.952  11.110  1.00 42.99           N  
ANISOU 1176  N   LYS B  61     3842   7340   5154   -565   -847   -157       N  
ATOM   1177  CA  LYS B  61      -5.655  -7.833  10.207  1.00 38.43           C  
ANISOU 1177  CA  LYS B  61     3146   7075   4380   -323  -1088     32       C  
ATOM   1178  C   LYS B  61      -7.097  -7.330  10.336  1.00 41.13           C  
ANISOU 1178  C   LYS B  61     3039   7593   4995   -332  -1270     42       C  
ATOM   1179  O   LYS B  61      -8.078  -8.102  10.326  1.00 44.45           O  
ANISOU 1179  O   LYS B  61     3189   8076   5623   -575  -1409   -238       O  
ATOM   1180  CB  LYS B  61      -5.309  -8.216   8.759  1.00 49.92           C  
ANISOU 1180  CB  LYS B  61     4809   8762   5395   -256  -1328    -97       C  
ATOM   1181  CG  LYS B  61      -5.010  -7.020   7.886  1.00 50.07           C  
ANISOU 1181  CG  LYS B  61     4916   9005   5104     83  -1430    198       C  
ATOM   1182  CD  LYS B  61      -4.664  -7.435   6.472  1.00 54.24           C  
ANISOU 1182  CD  LYS B  61     5734   9743   5130    171  -1626     72       C  
ATOM   1183  CE  LYS B  61      -4.271  -6.245   5.603  1.00 51.20           C  
ANISOU 1183  CE  LYS B  61     5538   9521   4396    545  -1630    414       C  
ATOM   1184  NZ  LYS B  61      -5.303  -5.218   5.441  1.00 50.86           N  
ANISOU 1184  NZ  LYS B  61     5226   9714   4385    773  -1875    630       N  
ATOM   1185  N   VAL B  62      -7.247  -6.037  10.451  1.00 43.87           N  
ANISOU 1185  N   VAL B  62     3278   8008   5381    -66  -1244    358       N  
ATOM   1186  CA  VAL B  62      -8.551  -5.463  10.589  1.00 44.83           C  
ANISOU 1186  CA  VAL B  62     2946   8300   5787      7  -1387    416       C  
ATOM   1187  C   VAL B  62      -9.388  -5.612   9.320  1.00 52.62           C  
ANISOU 1187  C   VAL B  62     3716   9701   6577    102  -1875    291       C  
ATOM   1188  O   VAL B  62     -10.440  -6.176   9.361  1.00 56.68           O  
ANISOU 1188  O   VAL B  62     3886  10258   7390    -61  -2037     64       O  
ATOM   1189  CB  VAL B  62      -8.481  -3.998  11.006  1.00 43.44           C  
ANISOU 1189  CB  VAL B  62     2763   8040   5703    315  -1187    803       C  
ATOM   1190  CG1 VAL B  62      -9.854  -3.381  10.973  1.00 50.36           C  
ANISOU 1190  CG1 VAL B  62     3205   9057   6874    462  -1319    858       C  
ATOM   1191  CG2 VAL B  62      -7.947  -3.878  12.401  1.00 41.17           C  
ANISOU 1191  CG2 VAL B  62     2669   7343   5631    192   -748    861       C  
ATOM   1192  N   GLU B  63      -8.904  -5.157   8.185  1.00 55.98           N  
ANISOU 1192  N   GLU B  63     4451  10290   6529    363  -2045    425       N  
ATOM   1193  CA  GLU B  63      -9.733  -5.260   6.997  1.00 70.47           C  
ANISOU 1193  CA  GLU B  63     6241  12377   8157    552  -2458    383       C  
ATOM   1194  C   GLU B  63     -10.090  -6.674   6.563  1.00 84.42           C  
ANISOU 1194  C   GLU B  63     7778  14280  10017    235  -2803    -52       C  
ATOM   1195  O   GLU B  63     -11.237  -6.922   6.272  1.00 92.29           O  
ANISOU 1195  O   GLU B  63     8497  15454  11114    309  -3144    -98       O  
ATOM   1196  CB  GLU B  63      -9.158  -4.458   5.834  1.00 70.62           C  
ANISOU 1196  CB  GLU B  63     6742  12504   7587    822  -2525    542       C  
ATOM   1197  N   ASP B  64      -9.128  -7.585   6.585  1.00 85.46           N  
ANISOU 1197  N   ASP B  64     8028  14318  10126   -125  -2707   -370       N  
ATOM   1198  CA  ASP B  64      -9.289  -8.983   6.190  1.00 97.58           C  
ANISOU 1198  CA  ASP B  64     9451  15923  11702   -478  -2979   -827       C  
ATOM   1199  C   ASP B  64     -10.580  -9.642   6.609  1.00104.54           C  
ANISOU 1199  C   ASP B  64     9782  16839  13100   -645  -3152   -952       C  
ATOM   1200  O   ASP B  64     -11.424  -9.913   5.767  1.00112.02           O  
ANISOU 1200  O   ASP B  64    10559  18045  13960   -535  -3581   -975       O  
ATOM   1201  CB  ASP B  64      -8.129  -9.848   6.690  1.00 97.62           C  
ANISOU 1201  CB  ASP B  64     9637  15696  11759   -859  -2687  -1128       C  
ATOM   1202  N   PRO B  68     -10.494 -14.729   5.787  1.00116.51           N  
ANISOU 1202  N   PRO B  68    12523  17506  14238  -2372  -2688  -2893       N  
ATOM   1203  CA  PRO B  68      -9.523 -14.470   4.739  1.00115.35           C  
ANISOU 1203  CA  PRO B  68    12851  17560  13416  -2073  -2862  -2825       C  
ATOM   1204  C   PRO B  68      -8.097 -14.880   5.116  1.00108.70           C  
ANISOU 1204  C   PRO B  68    12519  16424  12358  -2030  -2399  -2785       C  
ATOM   1205  O   PRO B  68      -7.396 -14.242   5.894  1.00100.74           O  
ANISOU 1205  O   PRO B  68    11578  15240  11460  -1752  -2074  -2335       O  
ATOM   1206  CB  PRO B  68      -9.677 -12.976   4.532  1.00114.27           C  
ANISOU 1206  CB  PRO B  68    12501  17767  13148  -1604  -3110  -2344       C  
ATOM   1207  CG  PRO B  68     -11.141 -12.739   4.750  1.00118.30           C  
ANISOU 1207  CG  PRO B  68    12431  18385  14134  -1717  -3353  -2358       C  
ATOM   1208  CD  PRO B  68     -11.641 -13.810   5.677  1.00119.42           C  
ANISOU 1208  CD  PRO B  68    12368  18178  14830  -2207  -3038  -2678       C  
ATOM   1209  N   HIS B  69      -7.928 -16.148   4.834  1.00111.88           N  
ANISOU 1209  N   HIS B  69    13358  16609  12542  -2250  -2284  -3167       N  
ATOM   1210  CA  HIS B  69      -6.828 -16.718   5.474  1.00110.83           C  
ANISOU 1210  CA  HIS B  69    13567  15888  12656  -2396  -1698  -3209       C  
ATOM   1211  C   HIS B  69      -5.914 -17.651   4.978  1.00115.95           C  
ANISOU 1211  C   HIS B  69    14844  16336  12877  -2402  -1536  -3468       C  
ATOM   1212  O   HIS B  69      -6.338 -18.818   4.744  1.00120.78           O  
ANISOU 1212  O   HIS B  69    15599  16807  13485  -2796  -1566  -3991       O  
ATOM   1213  CB  HIS B  69      -7.373 -17.326   6.792  1.00112.06           C  
ANISOU 1213  CB  HIS B  69    13413  15751  13414  -2880  -1520  -3510       C  
ATOM   1214  CG  HIS B  69      -6.387 -18.171   7.539  1.00118.11           C  
ANISOU 1214  CG  HIS B  69    14038  16580  14259  -3248  -1819  -3981       C  
ATOM   1215  ND1 HIS B  69      -5.708 -17.713   8.648  1.00121.55           N  
ANISOU 1215  ND1 HIS B  69    14012  17446  14725  -3209  -2368  -3968       N  
ATOM   1216  CD2 HIS B  69      -5.977 -19.447   7.347  1.00122.49           C  
ANISOU 1216  CD2 HIS B  69    14879  16737  14925  -3601  -1596  -4383       C  
ATOM   1217  CE1 HIS B  69      -4.914 -18.668   9.100  1.00128.90           C  
ANISOU 1217  CE1 HIS B  69    14932  18293  15752  -3555  -2524  -4379       C  
ATOM   1218  NE2 HIS B  69      -5.058 -19.730   8.329  1.00129.64           N  
ANISOU 1218  NE2 HIS B  69    15468  17881  15909  -3808  -2049  -4641       N  
ATOM   1219  N   ARG B  70      -4.721 -17.138   4.649  1.00114.04           N  
ANISOU 1219  N   ARG B  70    14970  16073  12286  -1979  -1341  -3127       N  
ATOM   1220  CA  ARG B  70      -3.823 -18.258   4.776  1.00112.98           C  
ANISOU 1220  CA  ARG B  70    15269  15450  12207  -1852   -776  -3017       C  
ATOM   1221  C   ARG B  70      -3.127 -17.515   5.909  1.00105.58           C  
ANISOU 1221  C   ARG B  70    14169  14414  11531  -1529   -516  -2474       C  
ATOM   1222  O   ARG B  70      -2.018 -17.873   6.287  1.00105.30           O  
ANISOU 1222  O   ARG B  70    14427  14088  11496  -1298   -121  -2287       O  
ATOM   1223  CB  ARG B  70      -2.849 -18.564   3.641  1.00116.54           C  
ANISOU 1223  CB  ARG B  70    16265  15900  12115  -1636   -671  -3100       C  
ATOM   1224  N   GLU B  71      -3.768 -16.540   6.535  1.00100.31           N  
ANISOU 1224  N   GLU B  71    13034  13965  11113  -1512   -718  -2239       N  
ATOM   1225  CA  GLU B  71      -3.183 -15.221   6.679  1.00 89.47           C  
ANISOU 1225  CA  GLU B  71    11517  12824   9652  -1140   -770  -1774       C  
ATOM   1226  C   GLU B  71      -1.882 -15.275   7.487  1.00 76.87           C  
ANISOU 1226  C   GLU B  71    10116  10939   8152   -881   -351  -1470       C  
ATOM   1227  O   GLU B  71      -1.608 -16.244   8.152  1.00 77.81           O  
ANISOU 1227  O   GLU B  71    10423  10689   8452   -950    -46  -1552       O  
ATOM   1228  CB  GLU B  71      -4.171 -14.252   7.336  1.00 87.85           C  
ANISOU 1228  CB  GLU B  71    10806  12820   9753  -1183   -988  -1602       C  
ATOM   1229  CG  GLU B  71      -4.728 -13.148   6.430  1.00 86.37           C  
ANISOU 1229  CG  GLU B  71    10390  13114   9313  -1029  -1427  -1504       C  
ATOM   1230  CD  GLU B  71      -6.011 -12.568   6.958  1.00 82.99           C  
ANISOU 1230  CD  GLU B  71     9429  12859   9243  -1144  -1655  -1477       C  
ATOM   1231  OE1 GLU B  71      -6.432 -11.492   6.577  1.00 80.10           O  
ANISOU 1231  OE1 GLU B  71     8830  12828   8777   -928  -1933  -1270       O  
ATOM   1232  OE2 GLU B  71      -6.615 -13.201   7.802  1.00 85.14           O  
ANISOU 1232  OE2 GLU B  71     9521  12900   9928  -1433  -1502  -1647       O  
ATOM   1233  N   ARG B  72      -1.038 -14.558   6.769  1.00 65.86           N  
ANISOU 1233  N   ARG B  72     8690   9726   6609   -570   -346  -1135       N  
ATOM   1234  CA  ARG B  72       0.384 -14.299   6.736  1.00 54.71           C  
ANISOU 1234  CA  ARG B  72     7564   8277   4947   -301   -115  -1017       C  
ATOM   1235  C   ARG B  72       1.400 -13.965   7.767  1.00 46.15           C  
ANISOU 1235  C   ARG B  72     6391   7051   4092    -79    151   -704       C  
ATOM   1236  O   ARG B  72       2.530 -14.258   7.569  1.00 46.68           O  
ANISOU 1236  O   ARG B  72     6633   7026   4076    123    399   -640       O  
ATOM   1237  CB  ARG B  72       0.558 -13.219   5.687  1.00 51.55           C  
ANISOU 1237  CB  ARG B  72     7171   8213   4203   -125   -288   -871       C  
ATOM   1238  CG  ARG B  72      -0.002 -13.564   4.330  1.00 53.12           C  
ANISOU 1238  CG  ARG B  72     7705   8556   3923   -145   -427  -1139       C  
ATOM   1239  CD  ARG B  72       0.524 -12.585   3.306  1.00 51.88           C  
ANISOU 1239  CD  ARG B  72     7649   8661   3403    142   -455   -874       C  
ATOM   1240  NE  ARG B  72       1.757 -13.084   2.788  1.00 55.84           N  
ANISOU 1240  NE  ARG B  72     8491   9016   3709    352    -47   -805       N  
ATOM   1241  CZ  ARG B  72       2.786 -12.389   2.386  1.00 55.88           C  
ANISOU 1241  CZ  ARG B  72     8540   9076   3614    611    193   -489       C  
ATOM   1242  NH1 ARG B  72       3.806 -13.045   1.966  1.00 61.32           N  
ANISOU 1242  NH1 ARG B  72     9502   9614   4184    774    601   -473       N  
ATOM   1243  NH2 ARG B  72       2.815 -11.103   2.380  1.00 58.36           N  
ANISOU 1243  NH2 ARG B  72     8641   9563   3969    707     81   -196       N  
ATOM   1244  N   ALA B  73       1.033 -13.313   8.822  1.00 41.84           N  
ANISOU 1244  N   ALA B  73     5561   6508   3830   -110     88   -527       N  
ATOM   1245  CA  ALA B  73       2.039 -12.903   9.774  1.00 39.81           C  
ANISOU 1245  CA  ALA B  73     5200   6174   3751     82    255   -270       C  
ATOM   1246  C   ALA B  73       2.232 -13.993  10.778  1.00 45.23           C  
ANISOU 1246  C   ALA B  73     6027   6555   4605     91    438   -325       C  
ATOM   1247  O   ALA B  73       1.299 -14.386  11.438  1.00 45.12           O  
ANISOU 1247  O   ALA B  73     6010   6393   4740    -96    421   -421       O  
ATOM   1248  CB  ALA B  73       1.632 -11.633  10.453  1.00 39.35           C  
ANISOU 1248  CB  ALA B  73     4845   6248   3858     58    115    -70       C  
ATOM   1249  N   THR B  74       3.442 -14.487  10.903  1.00 34.99           N  
ANISOU 1249  N   THR B  74     4850   5150   3293    337    646   -247       N  
ATOM   1250  CA  THR B  74       3.656 -15.619  11.770  1.00 37.58           C  
ANISOU 1250  CA  THR B  74     5387   5165   3725    427    843   -269       C  
ATOM   1251  C   THR B  74       4.344 -15.226  13.081  1.00 37.02           C  
ANISOU 1251  C   THR B  74     5163   5105   3797    644    826    -23       C  
ATOM   1252  O   THR B  74       5.317 -14.477  13.082  1.00 37.96           O  
ANISOU 1252  O   THR B  74     5052   5433   3937    818    769    128       O  
ATOM   1253  CB  THR B  74       4.468 -16.687  11.072  1.00 43.56           C  
ANISOU 1253  CB  THR B  74     6441   5748   4361    612   1106   -364       C  
ATOM   1254  OG1 THR B  74       3.836 -16.981   9.830  1.00 49.20           O  
ANISOU 1254  OG1 THR B  74     7337   6480   4878    394   1083   -634       O  
ATOM   1255  CG2 THR B  74       4.494 -17.946  11.920  1.00 45.70           C  
ANISOU 1255  CG2 THR B  74     7009   5626   4728    713   1352   -385       C  
ATOM   1256  N   LEU B  75       3.835 -15.758  14.182  1.00 34.30           N  
ANISOU 1256  N   LEU B  75     4964   4527   3541    620    889     -5       N  
ATOM   1257  CA  LEU B  75       4.362 -15.463  15.521  1.00 33.45           C  
ANISOU 1257  CA  LEU B  75     4797   4426   3485    835    836    204       C  
ATOM   1258  C   LEU B  75       5.764 -16.055  15.671  1.00 35.36           C  
ANISOU 1258  C   LEU B  75     5091   4659   3685   1245    925    324       C  
ATOM   1259  O   LEU B  75       5.977 -17.199  15.310  1.00 38.87           O  
ANISOU 1259  O   LEU B  75     5820   4860   4089   1381   1166    268       O  
ATOM   1260  CB  LEU B  75       3.444 -16.027  16.606  1.00 34.03           C  
ANISOU 1260  CB  LEU B  75     5124   4199   3608    748    964    207       C  
ATOM   1261  CG  LEU B  75       3.881 -15.838  18.067  1.00 36.37           C  
ANISOU 1261  CG  LEU B  75     5490   4473   3855    998    914    414       C  
ATOM   1262  CD1 LEU B  75       3.922 -14.351  18.444  1.00 31.54           C  
ANISOU 1262  CD1 LEU B  75     4543   4172   3269    910    638    477       C  
ATOM   1263  CD2 LEU B  75       2.986 -16.634  19.025  1.00 38.85           C  
ANISOU 1263  CD2 LEU B  75     6187   4396   4179    949   1176    431       C  
ATOM   1264  N   LEU B  76       6.695 -15.274  16.214  1.00 34.81           N  
ANISOU 1264  N   LEU B  76     4730   4847   3649   1435    735    470       N  
ATOM   1265  CA  LEU B  76       8.029 -15.802  16.587  1.00 37.41           C  
ANISOU 1265  CA  LEU B  76     5010   5224   3980   1872    753    601       C  
ATOM   1266  C   LEU B  76       8.068 -16.133  18.089  1.00 41.31           C  
ANISOU 1266  C   LEU B  76     5685   5625   4385   2111    654    743       C  
ATOM   1267  O   LEU B  76       8.232 -15.251  18.927  1.00 40.95           O  
ANISOU 1267  O   LEU B  76     5441   5795   4324   2097    383    794       O  
ATOM   1268  CB  LEU B  76       9.110 -14.785  16.219  1.00 37.28           C  
ANISOU 1268  CB  LEU B  76     4503   5576   4087   1923    594    635       C  
ATOM   1269  CG  LEU B  76       9.029 -14.252  14.777  1.00 42.18           C  
ANISOU 1269  CG  LEU B  76     4998   6287   4741   1694    718    536       C  
ATOM   1270  CD1 LEU B  76      10.035 -13.122  14.567  1.00 39.49           C  
ANISOU 1270  CD1 LEU B  76     4180   6255   4570   1694    631    584       C  
ATOM   1271  CD2 LEU B  76       9.197 -15.374  13.688  1.00 38.52           C  
ANISOU 1271  CD2 LEU B  76     4814   5625   4195   1822   1036    458       C  
ATOM   1272  N   GLU B  77       7.837 -17.393  18.425  1.00 39.69           N  
ANISOU 1272  N   GLU B  77     4778   5378   4924   1296    363    625       N  
ATOM   1273  CA  GLU B  77       7.582 -17.774  19.811  1.00 44.60           C  
ANISOU 1273  CA  GLU B  77     5477   6106   5362   1498    410    791       C  
ATOM   1274  C   GLU B  77       8.796 -17.544  20.715  1.00 45.19           C  
ANISOU 1274  C   GLU B  77     5476   6439   5256   1685    181    920       C  
ATOM   1275  O   GLU B  77       8.660 -17.279  21.907  1.00 50.57           O  
ANISOU 1275  O   GLU B  77     6241   7303   5670   1821     74    971       O  
ATOM   1276  CB  GLU B  77       7.165 -19.248  19.893  1.00 53.70           C  
ANISOU 1276  CB  GLU B  77     6705   7051   6646   1605    766    988       C  
ATOM   1277  CG  GLU B  77       5.752 -19.535  19.448  1.00 60.50           C  
ANISOU 1277  CG  GLU B  77     7642   7685   7661   1442    969    884       C  
ATOM   1278  CD  GLU B  77       5.413 -21.020  19.487  1.00 69.41           C  
ANISOU 1278  CD  GLU B  77     8826   8562   8985   1522   1338   1059       C  
ATOM   1279  OE1 GLU B  77       6.328 -21.864  19.283  1.00 71.22           O  
ANISOU 1279  OE1 GLU B  77     9036   8718   9305   1636   1471   1204       O  
ATOM   1280  OE2 GLU B  77       4.226 -21.339  19.734  1.00 71.86           O  
ANISOU 1280  OE2 GLU B  77     9184   8725   9396   1475   1521   1065       O  
ATOM   1281  N   GLU B  78       9.979 -17.635  20.132  1.00 43.81           N  
ANISOU 1281  N   GLU B  78     5142   6279   5226   1691    102    975       N  
ATOM   1282  CA  GLU B  78      11.199 -17.584  20.904  1.00 49.48           C  
ANISOU 1282  CA  GLU B  78     5724   7232   5845   1865   -125   1140       C  
ATOM   1283  C   GLU B  78      11.365 -16.221  21.569  1.00 52.51           C  
ANISOU 1283  C   GLU B  78     6084   7858   6011   1793   -512    944       C  
ATOM   1284  O   GLU B  78      12.129 -16.083  22.505  1.00 56.31           O  
ANISOU 1284  O   GLU B  78     6500   8583   6313   1928   -767   1039       O  
ATOM   1285  CB  GLU B  78      12.406 -17.900  20.023  1.00 49.92           C  
ANISOU 1285  CB  GLU B  78     5573   7213   6183   1872    -96   1247       C  
ATOM   1286  CG  GLU B  78      12.947 -16.717  19.222  1.00 50.53           C  
ANISOU 1286  CG  GLU B  78     5498   7306   6396   1674   -312   1035       C  
ATOM   1287  CD  GLU B  78      12.175 -16.483  17.911  1.00 50.44           C  
ANISOU 1287  CD  GLU B  78     5589   7055   6520   1461   -123    828       C  
ATOM   1288  OE1 GLU B  78      11.111 -17.143  17.702  1.00 49.57           O  
ANISOU 1288  OE1 GLU B  78     5663   6787   6385   1430    115    802       O  
ATOM   1289  OE2 GLU B  78      12.624 -15.622  17.113  1.00 46.37           O  
ANISOU 1289  OE2 GLU B  78     4963   6517   6139   1328   -223    699       O  
ATOM   1290  N   GLN B  79      10.655 -15.206  21.103  1.00 49.31           N  
ANISOU 1290  N   GLN B  79     5732   7386   5619   1580   -564    668       N  
ATOM   1291  CA  GLN B  79      10.848 -13.899  21.717  1.00 54.81           C  
ANISOU 1291  CA  GLN B  79     6416   8265   6144   1502   -894    461       C  
ATOM   1292  C   GLN B  79       9.832 -13.573  22.824  1.00 51.85           C  
ANISOU 1292  C   GLN B  79     6290   7972   5437   1563   -887    380       C  
ATOM   1293  O   GLN B  79       9.952 -12.548  23.510  1.00 50.98           O  
ANISOU 1293  O   GLN B  79     6233   8009   5127   1520  -1140    193       O  
ATOM   1294  CB  GLN B  79      10.857 -12.834  20.623  1.00 64.12           C  
ANISOU 1294  CB  GLN B  79     7485   9325   7551   1261   -952    231       C  
ATOM   1295  CG  GLN B  79      12.236 -12.808  19.927  1.00 71.51           C  
ANISOU 1295  CG  GLN B  79     8155  10262   8754   1237  -1060    304       C  
ATOM   1296  CD  GLN B  79      12.219 -12.131  18.588  1.00 75.16           C  
ANISOU 1296  CD  GLN B  79     8532  10547   9479   1051   -979    170       C  
ATOM   1297  OE1 GLN B  79      11.348 -11.304  18.305  1.00 75.81           O  
ANISOU 1297  OE1 GLN B  79     8707  10563   9535    913   -961    -20       O  
ATOM   1298  NE2 GLN B  79      13.186 -12.481  17.740  1.00 77.35           N  
ANISOU 1298  NE2 GLN B  79     8634  10739  10016   1067   -901    296       N  
ATOM   1299  N   LEU B  80       8.870 -14.465  23.035  1.00 49.02           N  
ANISOU 1299  N   LEU B  80     6090   7501   5034   1671   -577    525       N  
ATOM   1300  CA  LEU B  80       7.907 -14.277  24.108  1.00 51.73           C  
ANISOU 1300  CA  LEU B  80     6675   7895   5085   1773   -492    506       C  
ATOM   1301  C   LEU B  80       8.547 -14.120  25.503  1.00 55.40           C  
ANISOU 1301  C   LEU B  80     7257   8653   5139   1971   -739    557       C  
ATOM   1302  O   LEU B  80       8.093 -13.287  26.285  1.00 56.56           O  
ANISOU 1302  O   LEU B  80     7598   8886   5005   1972   -825    386       O  
ATOM   1303  CB  LEU B  80       6.910 -15.428  24.115  1.00 50.36           C  
ANISOU 1303  CB  LEU B  80     6604   7532   5000   1878    -91    711       C  
ATOM   1304  CG  LEU B  80       5.920 -15.352  22.953  1.00 48.15           C  
ANISOU 1304  CG  LEU B  80     6266   6987   5041   1656    104    593       C  
ATOM   1305  CD1 LEU B  80       5.095 -16.625  22.877  1.00 51.51           C  
ANISOU 1305  CD1 LEU B  80     6739   7201   5631   1727    475    791       C  
ATOM   1306  CD2 LEU B  80       5.013 -14.117  23.041  1.00 44.05           C  
ANISOU 1306  CD2 LEU B  80     5818   6449   4469   1525     62    373       C  
ATOM   1307  N   PRO B  81       9.599 -14.902  25.824  1.00 58.66           N  
ANISOU 1307  N   PRO B  81     7562   9223   5503   2144   -855    794       N  
ATOM   1308  CA  PRO B  81      10.204 -14.675  27.148  1.00 62.15           C  
ANISOU 1308  CA  PRO B  81     8116   9988   5509   2323  -1161    831       C  
ATOM   1309  C   PRO B  81      10.839 -13.287  27.307  1.00 63.28           C  
ANISOU 1309  C   PRO B  81     8200  10292   5553   2132  -1607    496       C  
ATOM   1310  O   PRO B  81      11.115 -12.879  28.430  1.00 65.63           O  
ANISOU 1310  O   PRO B  81     8658  10843   5434   2227  -1883    422       O  
ATOM   1311  CB  PRO B  81      11.286 -15.758  27.241  1.00 65.57           C  
ANISOU 1311  CB  PRO B  81     8359  10546   6008   2527  -1216   1180       C  
ATOM   1312  CG  PRO B  81      10.900 -16.781  26.236  1.00 63.57           C  
ANISOU 1312  CG  PRO B  81     8019   9984   6149   2519   -790   1356       C  
ATOM   1313  CD  PRO B  81      10.182 -16.078  25.148  1.00 60.09           C  
ANISOU 1313  CD  PRO B  81     7558   9299   5974   2223   -686   1063       C  
ATOM   1314  N   LEU B  82      11.072 -12.585  26.201  1.00 62.19           N  
ANISOU 1314  N   LEU B  82     7846   9999   5783   1870  -1667    298       N  
ATOM   1315  CA  LEU B  82      11.525 -11.189  26.246  1.00 65.18           C  
ANISOU 1315  CA  LEU B  82     8163  10447   6155   1656  -2014    -43       C  
ATOM   1316  C   LEU B  82      10.360 -10.223  26.447  1.00 61.76           C  
ANISOU 1316  C   LEU B  82     7990   9888   5589   1545  -1879   -321       C  
ATOM   1317  O   LEU B  82      10.544  -9.011  26.413  1.00 62.06           O  
ANISOU 1317  O   LEU B  82     8007   9912   5662   1354  -2080   -625       O  
ATOM   1318  CB  LEU B  82      12.276 -10.803  24.961  1.00 66.50           C  
ANISOU 1318  CB  LEU B  82     7986  10475   6805   1446  -2081   -103       C  
ATOM   1319  CG  LEU B  82      13.649 -11.418  24.722  1.00 71.74           C  
ANISOU 1319  CG  LEU B  82     8331  11249   7678   1515  -2261    126       C  
ATOM   1320  CD1 LEU B  82      14.531 -10.423  23.985  1.00 74.29           C  
ANISOU 1320  CD1 LEU B  82     8354  11514   8360   1282  -2484    -56       C  
ATOM   1321  CD2 LEU B  82      14.270 -11.826  26.055  1.00 76.78           C  
ANISOU 1321  CD2 LEU B  82     9014  12217   7941   1724  -2566    269       C  
ATOM   1322  N   GLY B  83       9.162 -10.765  26.628  1.00 57.80           N  
ANISOU 1322  N   GLY B  83     7708   9265   4987   1666  -1507   -202       N  
ATOM   1323  CA  GLY B  83       7.969  -9.942  26.760  1.00 52.94           C  
ANISOU 1323  CA  GLY B  83     7308   8497   4309   1588  -1308   -403       C  
ATOM   1324  C   GLY B  83       7.471  -9.300  25.469  1.00 49.05           C  
ANISOU 1324  C   GLY B  83     6645   7753   4239   1351  -1170   -532       C  
ATOM   1325  O   GLY B  83       6.804  -8.269  25.501  1.00 43.27           O  
ANISOU 1325  O   GLY B  83     6015   6912   3512   1244  -1106   -744       O  
ATOM   1326  N   LYS B  84       7.776  -9.906  24.331  1.00 41.10           N  
ANISOU 1326  N   LYS B  84     5397   6648   3573   1284  -1104   -393       N  
ATOM   1327  CA  LYS B  84       7.350  -9.358  23.055  1.00 45.89           C  
ANISOU 1327  CA  LYS B  84     5858   7048   4532   1083   -992   -487       C  
ATOM   1328  C   LYS B  84       6.620 -10.405  22.248  1.00 40.66           C  
ANISOU 1328  C   LYS B  84     5158   6226   4065   1101   -700   -291       C  
ATOM   1329  O   LYS B  84       6.992 -11.577  22.219  1.00 39.22           O  
ANISOU 1329  O   LYS B  84     4943   6063   3896   1215   -630    -87       O  
ATOM   1330  CB  LYS B  84       8.524  -8.860  22.197  1.00 53.74           C  
ANISOU 1330  CB  LYS B  84     6590   8049   5780    937  -1214   -567       C  
ATOM   1331  CG  LYS B  84       9.560  -8.016  22.877  1.00 65.52           C  
ANISOU 1331  CG  LYS B  84     8027   9698   7171    889  -1563   -745       C  
ATOM   1332  CD  LYS B  84      10.240  -7.076  21.866  1.00 69.89           C  
ANISOU 1332  CD  LYS B  84     8328  10143   8083    687  -1668   -879       C  
ATOM   1333  CE  LYS B  84      11.012  -7.826  20.787  1.00 69.93           C  
ANISOU 1333  CE  LYS B  84     8093  10097   8379    694  -1612   -673       C  
ATOM   1334  NZ  LYS B  84      12.040  -8.704  21.395  1.00 73.12           N  
ANISOU 1334  NZ  LYS B  84     8402  10686   8695    838  -1789   -497       N  
ATOM   1335  N   ALA B  85       5.593  -9.945  21.572  1.00 33.88           N  
ANISOU 1335  N   ALA B  85     4293   5201   3377    979   -539   -357       N  
ATOM   1336  CA  ALA B  85       4.914 -10.732  20.581  1.00 33.81           C  
ANISOU 1336  CA  ALA B  85     4215   5034   3596    924   -334   -238       C  
ATOM   1337  C   ALA B  85       5.343 -10.155  19.238  1.00 33.43           C  
ANISOU 1337  C   ALA B  85     3995   4924   3782    750   -429   -331       C  
ATOM   1338  O   ALA B  85       5.006  -8.999  18.917  1.00 34.59           O  
ANISOU 1338  O   ALA B  85     4106   5032   4005    640   -471   -465       O  
ATOM   1339  CB  ALA B  85       3.397 -10.645  20.783  1.00 31.76           C  
ANISOU 1339  CB  ALA B  85     4043   4651   3372    919   -106   -215       C  
ATOM   1340  N   SER B  86       6.131 -10.940  18.503  1.00 34.84           N  
ANISOU 1340  N   SER B  86     4084   5085   4070    749   -433   -242       N  
ATOM   1341  CA  SER B  86       6.682 -10.528  17.217  1.00 33.15           C  
ANISOU 1341  CA  SER B  86     3738   4810   4049    625   -483   -294       C  
ATOM   1342  C   SER B  86       6.126 -11.391  16.148  1.00 31.01           C  
ANISOU 1342  C   SER B  86     3489   4402   3892    567   -315   -230       C  
ATOM   1343  O   SER B  86       6.130 -12.622  16.269  1.00 32.28           O  
ANISOU 1343  O   SER B  86     3707   4513   4046    641   -186   -116       O  
ATOM   1344  CB  SER B  86       8.216 -10.643  17.180  1.00 35.86           C  
ANISOU 1344  CB  SER B  86     3957   5228   4442    677   -612   -249       C  
ATOM   1345  OG  SER B  86       8.796  -9.895  18.223  1.00 40.58           O  
ANISOU 1345  OG  SER B  86     4523   5970   4927    710   -828   -332       O  
ATOM   1346  N   PHE B  87       5.726 -10.742  15.070  1.00 31.21           N  
ANISOU 1346  N   PHE B  87     3473   4363   4024    436   -321   -303       N  
ATOM   1347  CA  PHE B  87       5.101 -11.404  13.940  1.00 27.27           C  
ANISOU 1347  CA  PHE B  87     3015   3752   3596    346   -217   -288       C  
ATOM   1348  C   PHE B  87       5.822 -11.039  12.654  1.00 32.24           C  
ANISOU 1348  C   PHE B  87     3606   4351   4291    290   -238   -315       C  
ATOM   1349  O   PHE B  87       5.979  -9.865  12.330  1.00 34.68           O  
ANISOU 1349  O   PHE B  87     3837   4693   4645    252   -317   -360       O  
ATOM   1350  CB  PHE B  87       3.625 -10.991  13.834  1.00 25.29           C  
ANISOU 1350  CB  PHE B  87     2761   3469   3378    253   -206   -318       C  
ATOM   1351  CG  PHE B  87       2.820 -11.332  15.064  1.00 28.39           C  
ANISOU 1351  CG  PHE B  87     3197   3857   3733    325   -120   -267       C  
ATOM   1352  CD1 PHE B  87       2.136 -12.538  15.156  1.00 29.94           C  
ANISOU 1352  CD1 PHE B  87     3439   3952   3984    321     20   -195       C  
ATOM   1353  CD2 PHE B  87       2.747 -10.437  16.121  1.00 30.93           C  
ANISOU 1353  CD2 PHE B  87     3529   4251   3971    398   -152   -295       C  
ATOM   1354  CE1 PHE B  87       1.368 -12.851  16.304  1.00 31.78           C  
ANISOU 1354  CE1 PHE B  87     3711   4159   4206    412    154   -110       C  
ATOM   1355  CE2 PHE B  87       2.011 -10.745  17.276  1.00 32.26           C  
ANISOU 1355  CE2 PHE B  87     3779   4408   4070    496    -28   -231       C  
ATOM   1356  CZ  PHE B  87       1.315 -11.956  17.348  1.00 32.61           C  
ANISOU 1356  CZ  PHE B  87     3850   4352   4188    513    138   -119       C  
ATOM   1357  N   HIS B  88       6.279 -12.026  11.918  1.00 28.66           N  
ANISOU 1357  N   HIS B  88     3223   3813   3852    298   -129   -279       N  
ATOM   1358  CA  HIS B  88       7.042 -11.797  10.715  1.00 30.79           C  
ANISOU 1358  CA  HIS B  88     3501   4038   4160    282    -90   -282       C  
ATOM   1359  C   HIS B  88       6.187 -11.988   9.487  1.00 34.45           C  
ANISOU 1359  C   HIS B  88     4088   4439   4562    165    -63   -345       C  
ATOM   1360  O   HIS B  88       5.472 -12.936   9.382  1.00 31.09           O  
ANISOU 1360  O   HIS B  88     3765   3945   4104    105    -14   -381       O  
ATOM   1361  CB  HIS B  88       8.250 -12.701  10.701  1.00 31.36           C  
ANISOU 1361  CB  HIS B  88     3585   4046   4286    393     42   -191       C  
ATOM   1362  CG  HIS B  88       9.123 -12.589   9.498  1.00 37.07           C  
ANISOU 1362  CG  HIS B  88     4334   4688   5064    411    156   -164       C  
ATOM   1363  ND1 HIS B  88       8.888 -13.313   8.359  1.00 39.73           N  
ANISOU 1363  ND1 HIS B  88     4870   4900   5324    368    309   -206       N  
ATOM   1364  CD2 HIS B  88      10.272 -11.918   9.282  1.00 35.70           C  
ANISOU 1364  CD2 HIS B  88     4022   4519   5023    477    168    -94       C  
ATOM   1365  CE1 HIS B  88       9.832 -13.072   7.483  1.00 41.99           C  
ANISOU 1365  CE1 HIS B  88     5172   5124   5660    430    436   -152       C  
ATOM   1366  NE2 HIS B  88      10.691 -12.234   8.020  1.00 39.53           N  
ANISOU 1366  NE2 HIS B  88     4634   4879   5506    498    365    -67       N  
ATOM   1367  N   ILE B  89       6.258 -11.028   8.585  1.00 31.70           N  
ANISOU 1367  N   ILE B  89     3721   4121   4204    133   -106   -356       N  
ATOM   1368  CA  ILE B  89       5.730 -11.176   7.254  1.00 30.60           C  
ANISOU 1368  CA  ILE B  89     3723   3952   3950     52    -99   -400       C  
ATOM   1369  C   ILE B  89       6.807 -11.086   6.194  1.00 31.44           C  
ANISOU 1369  C   ILE B  89     3921   4002   4024    124     37   -361       C  
ATOM   1370  O   ILE B  89       7.513 -10.135   6.075  1.00 31.62           O  
ANISOU 1370  O   ILE B  89     3834   4044   4135    192     60   -290       O  
ATOM   1371  CB  ILE B  89       4.631 -10.161   6.916  1.00 34.20           C  
ANISOU 1371  CB  ILE B  89     4109   4503   4382    -27   -250   -401       C  
ATOM   1372  CG1 ILE B  89       3.588 -10.098   8.013  1.00 35.29           C  
ANISOU 1372  CG1 ILE B  89     4134   4676   4598    -72   -334   -408       C  
ATOM   1373  CG2 ILE B  89       3.975 -10.522   5.603  1.00 35.86           C  
ANISOU 1373  CG2 ILE B  89     4479   4720   4427   -119   -301   -449       C  
ATOM   1374  CD1 ILE B  89       2.793  -8.834   8.010  1.00 36.18           C  
ANISOU 1374  CD1 ILE B  89     4112   4865   4768    -94   -430   -361       C  
ATOM   1375  N   PRO B  90       6.858 -12.201   5.391  1.00 33.41           N  
ANISOU 1375  N   PRO B  90     4399   4147   4150    100    159   -420       N  
ATOM   1376  CA  PRO B  90       7.860 -12.159   4.332  1.00 36.58           C  
ANISOU 1376  CA  PRO B  90     4932   4469   4496    192    346   -374       C  
ATOM   1377  C   PRO B  90       7.382 -11.436   3.079  1.00 38.45           C  
ANISOU 1377  C   PRO B  90     5296   4775   4540    161    289   -386       C  
ATOM   1378  O   PRO B  90       6.262 -11.581   2.730  1.00 37.74           O  
ANISOU 1378  O   PRO B  90     5291   4752   4295     38    122   -478       O  
ATOM   1379  CB  PRO B  90       8.115 -13.622   4.069  1.00 38.28           C  
ANISOU 1379  CB  PRO B  90     5368   4524   4653    194    534   -441       C  
ATOM   1380  CG  PRO B  90       6.803 -14.214   4.176  1.00 39.61           C  
ANISOU 1380  CG  PRO B  90     5614   4707   4728     28    380   -584       C  
ATOM   1381  CD  PRO B  90       6.176 -13.565   5.324  1.00 32.57           C  
ANISOU 1381  CD  PRO B  90     4465   3944   3968      1    190   -535       C  
ATOM   1382  N   GLN B  91       8.237 -10.663   2.439  1.00 37.21           N  
ANISOU 1382  N   GLN B  91     5130   4599   4409    280    427   -270       N  
ATOM   1383  CA  GLN B  91       7.973 -10.168   1.108  1.00 37.62           C  
ANISOU 1383  CA  GLN B  91     5371   4697   4225    302    445   -245       C  
ATOM   1384  C   GLN B  91       6.651  -9.449   0.958  1.00 37.27           C  
ANISOU 1384  C   GLN B  91     5263   4826   4071    194    163   -266       C  
ATOM   1385  O   GLN B  91       5.825  -9.867   0.220  1.00 37.38           O  
ANISOU 1385  O   GLN B  91     5459   4900   3845     91     24   -371       O  
ATOM   1386  CB  GLN B  91       8.170 -11.243   0.051  1.00 41.56           C  
ANISOU 1386  CB  GLN B  91     6247   5092   4452    312    611   -342       C  
ATOM   1387  CG  GLN B  91       9.581 -11.768   0.003  1.00 50.35           C  
ANISOU 1387  CG  GLN B  91     7413   6010   5706    463    961   -262       C  
ATOM   1388  CD  GLN B  91       9.836 -12.792  -1.076  1.00 63.63           C  
ANISOU 1388  CD  GLN B  91     9513   7546   7117    496   1198   -361       C  
ATOM   1389  OE1 GLN B  91       8.967 -13.177  -1.807  1.00 69.50           O  
ANISOU 1389  OE1 GLN B  91    10533   8340   7533    383   1069   -528       O  
ATOM   1390  NE2 GLN B  91      11.053 -13.224  -1.167  1.00 68.09           N  
ANISOU 1390  NE2 GLN B  91    10119   7920   7832    650   1549   -258       N  
ATOM   1391  N   VAL B  92       6.433  -8.428   1.759  1.00 35.54           N  
ANISOU 1391  N   VAL B  92     4766   4674   4064    206     74   -174       N  
ATOM   1392  CA  VAL B  92       5.139  -7.812   1.852  1.00 34.02           C  
ANISOU 1392  CA  VAL B  92     4458   4618   3849    117   -161   -166       C  
ATOM   1393  C   VAL B  92       4.561  -7.375   0.522  1.00 35.12           C  
ANISOU 1393  C   VAL B  92     4743   4873   3729    136   -239    -93       C  
ATOM   1394  O   VAL B  92       5.243  -6.929  -0.328  1.00 33.80           O  
ANISOU 1394  O   VAL B  92     4686   4686   3471    263    -78     12       O  
ATOM   1395  CB  VAL B  92       5.149  -6.613   2.800  1.00 34.52           C  
ANISOU 1395  CB  VAL B  92     4230   4693   4194    150   -177    -79       C  
ATOM   1396  CG1 VAL B  92       5.715  -6.978   4.144  1.00 35.55           C  
ANISOU 1396  CG1 VAL B  92     4236   4749   4523    140   -145   -152       C  
ATOM   1397  CG2 VAL B  92       5.943  -5.496   2.215  1.00 38.30           C  
ANISOU 1397  CG2 VAL B  92     4653   5132   4767    279    -14     70       C  
ATOM   1398  N   GLN B  93       3.267  -7.530   0.392  1.00 36.04           N  
ANISOU 1398  N   GLN B  93     4844   5115   3736     13   -492   -135       N  
ATOM   1399  CA  GLN B  93       2.515  -7.217  -0.816  1.00 36.76           C  
ANISOU 1399  CA  GLN B  93     5055   5367   3545     10   -659    -67       C  
ATOM   1400  C   GLN B  93       1.576  -6.059  -0.492  1.00 38.51           C  
ANISOU 1400  C   GLN B  93     4982   5707   3942     21   -803    109       C  
ATOM   1401  O   GLN B  93       1.367  -5.724   0.689  1.00 37.05           O  
ANISOU 1401  O   GLN B  93     4551   5463   4063     -6   -784    117       O  
ATOM   1402  CB  GLN B  93       1.721  -8.447  -1.287  1.00 39.54           C  
ANISOU 1402  CB  GLN B  93     5606   5766   3650   -171   -880   -268       C  
ATOM   1403  CG  GLN B  93       2.574  -9.701  -1.673  1.00 48.33           C  
ANISOU 1403  CG  GLN B  93     7058   6723   4584   -188   -700   -464       C  
ATOM   1404  CD  GLN B  93       1.739 -10.982  -1.845  1.00 47.61           C  
ANISOU 1404  CD  GLN B  93     7120   6614   4357   -412   -902   -712       C  
ATOM   1405  OE1 GLN B  93       0.552 -10.924  -2.161  1.00 44.52           O  
ANISOU 1405  OE1 GLN B  93     6657   6375   3883   -552  -1225   -739       O  
ATOM   1406  NE2 GLN B  93       2.356 -12.143  -1.601  1.00 46.87           N  
ANISOU 1406  NE2 GLN B  93     7204   6315   4288   -450   -706   -883       N  
ATOM   1407  N   VAL B  94       1.024  -5.438  -1.530  1.00 37.85           N  
ANISOU 1407  N   VAL B  94     4938   5788   3656     79   -927    263       N  
ATOM   1408  CA  VAL B  94      -0.031  -4.450  -1.384  1.00 42.05           C  
ANISOU 1408  CA  VAL B  94     5193   6444   4339     94  -1078    461       C  
ATOM   1409  C   VAL B  94      -1.129  -4.946  -0.416  1.00 42.32           C  
ANISOU 1409  C   VAL B  94     5012   6482   4585    -84  -1275    368       C  
ATOM   1410  O   VAL B  94      -1.591  -4.191   0.425  1.00 39.68           O  
ANISOU 1410  O   VAL B  94     4407   6114   4555    -58  -1231    482       O  
ATOM   1411  CB  VAL B  94      -0.653  -4.094  -2.768  1.00 45.84           C  
ANISOU 1411  CB  VAL B  94     5783   7152   4481    157  -1276    629       C  
ATOM   1412  CG1 VAL B  94      -1.864  -3.240  -2.599  1.00 44.43           C  
ANISOU 1412  CG1 VAL B  94     5285   7109   4489    164  -1458    853       C  
ATOM   1413  CG2 VAL B  94       0.372  -3.384  -3.650  1.00 43.42           C  
ANISOU 1413  CG2 VAL B  94     5660   6826   4013    384  -1010    796       C  
ATOM   1414  N   ARG B  95      -1.523  -6.215  -0.516  1.00 38.35           N  
ANISOU 1414  N   ARG B  95     4638   5989   3946   -259  -1450    160       N  
ATOM   1415  CA  ARG B  95      -2.574  -6.735   0.361  1.00 42.01           C  
ANISOU 1415  CA  ARG B  95     4885   6428   4647   -422  -1601     95       C  
ATOM   1416  C   ARG B  95      -2.225  -6.737   1.860  1.00 40.15           C  
ANISOU 1416  C   ARG B  95     4510   6014   4732   -399  -1374     53       C  
ATOM   1417  O   ARG B  95      -3.117  -6.889   2.702  1.00 43.99           O  
ANISOU 1417  O   ARG B  95     4790   6469   5456   -479  -1427     67       O  
ATOM   1418  CB  ARG B  95      -2.953  -8.163  -0.031  1.00 40.54           C  
ANISOU 1418  CB  ARG B  95     4875   6235   4294   -628  -1791   -145       C  
ATOM   1419  CG  ARG B  95      -1.852  -9.233   0.131  1.00 38.83           C  
ANISOU 1419  CG  ARG B  95     4942   5834   3979   -644  -1575   -372       C  
ATOM   1420  CD  ARG B  95      -2.483 -10.588  -0.172  1.00 46.45           C  
ANISOU 1420  CD  ARG B  95     6034   6757   4858   -875  -1763   -609       C  
ATOM   1421  NE  ARG B  95      -1.572 -11.724  -0.327  1.00 50.99           N  
ANISOU 1421  NE  ARG B  95     6929   7151   5292   -904  -1570   -832       N  
ATOM   1422  CZ  ARG B  95      -1.718 -12.889   0.308  1.00 53.61           C  
ANISOU 1422  CZ  ARG B  95     7276   7302   5793  -1040  -1504  -1002       C  
ATOM   1423  NH1 ARG B  95      -0.882 -13.893   0.075  1.00 50.51           N  
ANISOU 1423  NH1 ARG B  95     7183   6731   5277  -1046  -1299  -1182       N  
ATOM   1424  NH2 ARG B  95      -2.719 -13.054   1.167  1.00 57.43           N  
ANISOU 1424  NH2 ARG B  95     7470   7760   6591  -1155  -1608   -970       N  
ATOM   1425  N   ASP B  96      -0.944  -6.609   2.195  1.00 35.98           N  
ANISOU 1425  N   ASP B  96     4093   5370   4207   -289  -1129      8       N  
ATOM   1426  CA  ASP B  96      -0.544  -6.602   3.624  1.00 36.54           C  
ANISOU 1426  CA  ASP B  96     4055   5305   4525   -261   -957    -40       C  
ATOM   1427  C   ASP B  96      -0.744  -5.239   4.281  1.00 40.24           C  
ANISOU 1427  C   ASP B  96     4303   5763   5223   -164   -869    108       C  
ATOM   1428  O   ASP B  96      -0.668  -5.109   5.517  1.00 36.55           O  
ANISOU 1428  O   ASP B  96     3748   5205   4935   -149   -763     66       O  
ATOM   1429  CB  ASP B  96       0.928  -7.027   3.778  1.00 32.01           C  
ANISOU 1429  CB  ASP B  96     3647   4620   3894   -191   -765   -139       C  
ATOM   1430  CG  ASP B  96       1.187  -8.461   3.290  1.00 37.69           C  
ANISOU 1430  CG  ASP B  96     4602   5290   4427   -274   -775   -296       C  
ATOM   1431  OD1 ASP B  96       0.476  -9.407   3.724  1.00 35.26           O  
ANISOU 1431  OD1 ASP B  96     4287   4946   4165   -398   -853   -394       O  
ATOM   1432  OD2 ASP B  96       2.091  -8.643   2.443  1.00 38.06           O  
ANISOU 1432  OD2 ASP B  96     4850   5309   4301   -209   -670   -316       O  
ATOM   1433  N   GLU B  97      -0.944  -4.219   3.455  1.00 43.03           N  
ANISOU 1433  N   GLU B  97     4596   6198   5554    -86   -890    281       N  
ATOM   1434  CA  GLU B  97      -1.061  -2.847   3.944  1.00 41.46           C  
ANISOU 1434  CA  GLU B  97     4207   5950   5595     17   -755    426       C  
ATOM   1435  C   GLU B  97      -2.360  -2.700   4.709  1.00 36.02           C  
ANISOU 1435  C   GLU B  97     3315   5263   5109    -30   -810    494       C  
ATOM   1436  O   GLU B  97      -3.407  -3.174   4.270  1.00 38.79           O  
ANISOU 1436  O   GLU B  97     3593   5720   5424   -111  -1006    558       O  
ATOM   1437  CB  GLU B  97      -1.015  -1.802   2.794  1.00 43.33           C  
ANISOU 1437  CB  GLU B  97     4422   6263   5779    139   -728    646       C  
ATOM   1438  CG  GLU B  97      -0.911  -0.348   3.330  1.00 57.97           C  
ANISOU 1438  CG  GLU B  97     6096   7996   7933    251   -511    777       C  
ATOM   1439  CD  GLU B  97      -0.720   0.742   2.260  1.00 59.34           C  
ANISOU 1439  CD  GLU B  97     6241   8199   8106    403   -405   1026       C  
ATOM   1440  OE1 GLU B  97       0.391   0.848   1.670  1.00 55.03           O  
ANISOU 1440  OE1 GLU B  97     5828   7606   7474    475   -275   1022       O  
ATOM   1441  OE2 GLU B  97      -1.679   1.523   2.039  1.00 62.85           O  
ANISOU 1441  OE2 GLU B  97     6514   8698   8669    471   -418   1257       O  
ATOM   1442  N   GLY B  98      -2.291  -2.059   5.869  1.00 42.74           N  
ANISOU 1442  N   GLY B  98     5399   7196   3643     28   -802    992       N  
ATOM   1443  CA  GLY B  98      -3.497  -1.734   6.603  1.00 40.83           C  
ANISOU 1443  CA  GLY B  98     4890   7044   3580    220  -1011   1094       C  
ATOM   1444  C   GLY B  98      -3.244  -1.824   8.103  1.00 39.89           C  
ANISOU 1444  C   GLY B  98     4757   6465   3934    312   -878    888       C  
ATOM   1445  O   GLY B  98      -2.102  -1.907   8.561  1.00 38.24           O  
ANISOU 1445  O   GLY B  98     4711   5897   3920    280   -674    756       O  
ATOM   1446  N   GLN B  99      -4.341  -1.837   8.848  1.00 39.23           N  
ANISOU 1446  N   GLN B  99     4445   6464   3996    412  -1000    865       N  
ATOM   1447  CA  GLN B  99      -4.321  -1.868  10.293  1.00 40.04           C  
ANISOU 1447  CA  GLN B  99     4522   6229   4462    500   -889    696       C  
ATOM   1448  C   GLN B  99      -4.461  -3.303  10.792  1.00 34.54           C  
ANISOU 1448  C   GLN B  99     3822   5575   3727    257   -826    343       C  
ATOM   1449  O   GLN B  99      -5.124  -4.128  10.161  1.00 37.11           O  
ANISOU 1449  O   GLN B  99     4057   6225   3818     38   -902    212       O  
ATOM   1450  CB  GLN B  99      -5.458  -0.990  10.841  1.00 46.09           C  
ANISOU 1450  CB  GLN B  99     5052   7017   5444    770   -973    888       C  
ATOM   1451  CG  GLN B  99      -5.293  -0.610  12.270  1.00 53.11           C  
ANISOU 1451  CG  GLN B  99     5973   7526   6680    884   -807    749       C  
ATOM   1452  CD  GLN B  99      -6.473   0.184  12.768  1.00 62.24           C  
ANISOU 1452  CD  GLN B  99     6894   8682   8072   1143   -812    895       C  
ATOM   1453  OE1 GLN B  99      -7.618  -0.141  12.465  1.00 63.39           O  
ANISOU 1453  OE1 GLN B  99     6767   9183   8136   1165   -964    966       O  
ATOM   1454  NE2 GLN B  99      -6.202   1.235  13.536  1.00 66.04           N  
ANISOU 1454  NE2 GLN B  99     7455   8769   8868   1322   -615    912       N  
ATOM   1455  N   TYR B 100      -3.827  -3.578  11.926  1.00 31.25           N  
ANISOU 1455  N   TYR B 100     3498   4841   3535    283   -671    201       N  
ATOM   1456  CA  TYR B 100      -3.766  -4.904  12.533  1.00 31.65           C  
ANISOU 1456  CA  TYR B 100     3590   4824   3611    121   -534    -41       C  
ATOM   1457  C   TYR B 100      -4.054  -4.734  14.015  1.00 34.48           C  
ANISOU 1457  C   TYR B 100     3892   5032   4177    259   -489    -62       C  
ATOM   1458  O   TYR B 100      -3.684  -3.709  14.576  1.00 32.70           O  
ANISOU 1458  O   TYR B 100     3680   4666   4077    426   -502     23       O  
ATOM   1459  CB  TYR B 100      -2.371  -5.534  12.374  1.00 29.13           C  
ANISOU 1459  CB  TYR B 100     3465   4298   3306     47   -352   -115       C  
ATOM   1460  CG  TYR B 100      -1.989  -5.952  10.938  1.00 29.04           C  
ANISOU 1460  CG  TYR B 100     3561   4408   3065   -148   -291   -178       C  
ATOM   1461  CD1 TYR B 100      -2.038  -7.280  10.549  1.00 26.45           C  
ANISOU 1461  CD1 TYR B 100     3309   4079   2662   -391   -100   -424       C  
ATOM   1462  CD2 TYR B 100      -1.535  -5.013  10.023  1.00 29.07           C  
ANISOU 1462  CD2 TYR B 100     3618   4490   2939   -101   -361     -4       C  
ATOM   1463  CE1 TYR B 100      -1.684  -7.671   9.238  1.00 31.66           C  
ANISOU 1463  CE1 TYR B 100     4093   4863   3074   -618      8   -558       C  
ATOM   1464  CE2 TYR B 100      -1.164  -5.390   8.733  1.00 31.74           C  
ANISOU 1464  CE2 TYR B 100     4079   4978   3002   -298   -275    -71       C  
ATOM   1465  CZ  TYR B 100      -1.245  -6.719   8.357  1.00 33.45           C  
ANISOU 1465  CZ  TYR B 100     4369   5234   3108   -567    -96   -376       C  
ATOM   1466  OH  TYR B 100      -0.902  -7.081   7.081  1.00 36.51           O  
ANISOU 1466  OH  TYR B 100     4900   5788   3186   -805     31   -509       O  
ATOM   1467  N   GLN B 101      -4.684  -5.715  14.649  1.00 36.18           N  
ANISOU 1467  N   GLN B 101     4063   5265   4420    159   -392   -196       N  
ATOM   1468  CA  GLN B 101      -4.710  -5.780  16.126  1.00 32.90           C  
ANISOU 1468  CA  GLN B 101     3661   4713   4126    263   -290   -212       C  
ATOM   1469  C   GLN B 101      -3.656  -6.753  16.637  1.00 31.33           C  
ANISOU 1469  C   GLN B 101     3622   4343   3938    242   -128   -216       C  
ATOM   1470  O   GLN B 101      -3.618  -7.931  16.239  1.00 33.85           O  
ANISOU 1470  O   GLN B 101     4007   4596   4258    100     33   -283       O  
ATOM   1471  CB  GLN B 101      -6.098  -6.212  16.648  1.00 29.75           C  
ANISOU 1471  CB  GLN B 101     3103   4429   3771    198   -231   -294       C  
ATOM   1472  CG  GLN B 101      -7.218  -5.282  16.242  1.00 35.28           C  
ANISOU 1472  CG  GLN B 101     3556   5336   4511    280   -385   -238       C  
ATOM   1473  CD  GLN B 101      -8.606  -5.895  16.366  1.00 43.66           C  
ANISOU 1473  CD  GLN B 101     4374   6601   5613    142   -342   -345       C  
ATOM   1474  OE1 GLN B 101      -8.820  -7.073  16.071  1.00 47.85           O  
ANISOU 1474  OE1 GLN B 101     4912   7182   6085   -126   -243   -502       O  
ATOM   1475  NE2 GLN B 101      -9.554  -5.085  16.807  1.00 41.56           N  
ANISOU 1475  NE2 GLN B 101     3875   6427   5489    311   -366   -282       N  
ATOM   1476  N   CYS B 102      -2.806  -6.273  17.537  1.00 28.72           N  
ANISOU 1476  N   CYS B 102     3336   3950   3627    381   -147   -145       N  
ATOM   1477  CA  CYS B 102      -1.849  -7.136  18.208  1.00 30.40           C  
ANISOU 1477  CA  CYS B 102     3625   4084   3840    434    -31    -59       C  
ATOM   1478  C   CYS B 102      -2.483  -7.620  19.485  1.00 35.08           C  
ANISOU 1478  C   CYS B 102     4225   4714   4390    473     69    -20       C  
ATOM   1479  O   CYS B 102      -2.691  -6.804  20.371  1.00 35.21           O  
ANISOU 1479  O   CYS B 102     4207   4840   4330    530    -10    -52       O  
ATOM   1480  CB  CYS B 102      -0.567  -6.361  18.511  1.00 31.66           C  
ANISOU 1480  CB  CYS B 102     3762   4278   3989    526   -147     -4       C  
ATOM   1481  SG  CYS B 102       0.908  -7.387  18.669  1.00 52.31           S  
ANISOU 1481  SG  CYS B 102     6371   6851   6655    627    -45    174       S  
ATOM   1482  N   ILE B 103      -2.786  -8.919  19.595  1.00 33.75           N  
ANISOU 1482  N   ILE B 103     4122   4429   4274    426    297     33       N  
ATOM   1483  CA  ILE B 103      -3.660  -9.415  20.674  1.00 34.24           C  
ANISOU 1483  CA  ILE B 103     4202   4506   4302    423    456     77       C  
ATOM   1484  C   ILE B 103      -2.896 -10.420  21.490  1.00 38.10           C  
ANISOU 1484  C   ILE B 103     4799   4905   4774    566    638    347       C  
ATOM   1485  O   ILE B 103      -2.285 -11.339  20.955  1.00 38.67           O  
ANISOU 1485  O   ILE B 103     4936   4761   4994    590    814    446       O  
ATOM   1486  CB  ILE B 103      -4.962 -10.076  20.135  1.00 37.37           C  
ANISOU 1486  CB  ILE B 103     4555   4831   4813    202    631    -87       C  
ATOM   1487  CG1 ILE B 103      -5.729  -9.100  19.243  1.00 38.13           C  
ANISOU 1487  CG1 ILE B 103     4476   5105   4906    109    407   -271       C  
ATOM   1488  CG2 ILE B 103      -5.864 -10.591  21.266  1.00 39.82           C  
ANISOU 1488  CG2 ILE B 103     4878   5132   5121    177    859    -39       C  
ATOM   1489  CD1 ILE B 103      -6.847  -9.744  18.430  1.00 40.86           C  
ANISOU 1489  CD1 ILE B 103     4699   5507   5320   -160    495   -461       C  
ATOM   1490  N   ILE B 104      -2.876 -10.223  22.795  1.00 34.98           N  
ANISOU 1490  N   ILE B 104     4418   4687   4185    682    613    491       N  
ATOM   1491  CA  ILE B 104      -2.132 -11.140  23.620  1.00 36.61           C  
ANISOU 1491  CA  ILE B 104     4699   4890   4323    874    750    852       C  
ATOM   1492  C   ILE B 104      -3.049 -11.596  24.749  1.00 38.22           C  
ANISOU 1492  C   ILE B 104     4995   5137   4390    867    969    972       C  
ATOM   1493  O   ILE B 104      -3.690 -10.777  25.418  1.00 38.53           O  
ANISOU 1493  O   ILE B 104     5008   5401   4229    799    877    813       O  
ATOM   1494  CB  ILE B 104      -0.826 -10.487  24.135  1.00 38.06           C  
ANISOU 1494  CB  ILE B 104     4778   5385   4297   1038    456    990       C  
ATOM   1495  CG1 ILE B 104      -0.063  -9.851  22.953  1.00 38.30           C  
ANISOU 1495  CG1 ILE B 104     4708   5354   4489    988    278    811       C  
ATOM   1496  CG2 ILE B 104       0.029 -11.508  24.881  1.00 37.06           C  
ANISOU 1496  CG2 ILE B 104     4657   5319   4106   1303    563   1465       C  
ATOM   1497  CD1 ILE B 104       1.276  -9.246  23.299  1.00 44.53           C  
ANISOU 1497  CD1 ILE B 104     5339   6433   5148   1090     18    898       C  
ATOM   1498  N   ILE B 105      -3.131 -12.915  24.894  1.00 39.09           N  
ANISOU 1498  N   ILE B 105     5228   4974   4652    927   1328   1240       N  
ATOM   1499  CA  ILE B 105      -3.963 -13.578  25.867  1.00 43.63           C  
ANISOU 1499  CA  ILE B 105     5924   5501   5153    915   1645   1419       C  
ATOM   1500  C   ILE B 105      -3.053 -14.276  26.871  1.00 47.53           C  
ANISOU 1500  C   ILE B 105     6506   6090   5464   1236   1733   1983       C  
ATOM   1501  O   ILE B 105      -2.060 -14.924  26.481  1.00 46.72           O  
ANISOU 1501  O   ILE B 105     6395   5808   5549   1444   1794   2260       O  
ATOM   1502  CB  ILE B 105      -4.883 -14.630  25.228  1.00 48.67           C  
ANISOU 1502  CB  ILE B 105     6643   5691   6160    693   2084   1298       C  
ATOM   1503  CG1 ILE B 105      -5.767 -14.013  24.149  1.00 51.06           C  
ANISOU 1503  CG1 ILE B 105     6790   6007   6603    382   1946    786       C  
ATOM   1504  CG2 ILE B 105      -5.727 -15.315  26.301  1.00 51.55           C  
ANISOU 1504  CG2 ILE B 105     7139   5978   6471    667   2474   1511       C  
ATOM   1505  CD1 ILE B 105      -6.645 -15.048  23.441  1.00 56.20           C  
ANISOU 1505  CD1 ILE B 105     7466   6306   7580     70   2343    578       C  
ATOM   1506  N   TYR B 106      -3.396 -14.143  28.146  1.00 48.76           N  
ANISOU 1506  N   TYR B 106     6730   6551   5247   1290   1755   2172       N  
ATOM   1507  CA  TYR B 106      -2.626 -14.729  29.242  1.00 56.60           C  
ANISOU 1507  CA  TYR B 106     7788   7781   5938   1608   1792   2776       C  
ATOM   1508  C   TYR B 106      -3.608 -15.297  30.250  1.00 59.64           C  
ANISOU 1508  C   TYR B 106     8370   8137   6152   1570   2181   2993       C  
ATOM   1509  O   TYR B 106      -4.196 -14.555  31.052  1.00 60.34           O  
ANISOU 1509  O   TYR B 106     8479   8599   5850   1435   2087   2804       O  
ATOM   1510  CB  TYR B 106      -1.716 -13.671  29.879  1.00 59.28           C  
ANISOU 1510  CB  TYR B 106     7966   8773   5783   1693   1275   2768       C  
ATOM   1511  CG  TYR B 106      -0.729 -14.164  30.926  1.00 65.71           C  
ANISOU 1511  CG  TYR B 106     8700   9952   6313   1961   1129   3252       C  
ATOM   1512  CD1 TYR B 106       0.158 -15.195  30.643  1.00 68.62           C  
ANISOU 1512  CD1 TYR B 106     8969  10069   7035   2227   1233   3613       C  
ATOM   1513  CD2 TYR B 106      -0.635 -13.547  32.169  1.00 69.13           C  
ANISOU 1513  CD2 TYR B 106     9104  10975   6186   1889    870   3215       C  
ATOM   1514  CE1 TYR B 106       1.080 -15.631  31.579  1.00 75.75           C  
ANISOU 1514  CE1 TYR B 106     9719  11324   7737   2455   1084   3997       C  
ATOM   1515  CE2 TYR B 106       0.299 -13.986  33.124  1.00 76.21           C  
ANISOU 1515  CE2 TYR B 106     9873  12235   6849   2075    691   3585       C  
ATOM   1516  CZ  TYR B 106       1.151 -15.030  32.810  1.00 79.07           C  
ANISOU 1516  CZ  TYR B 106    10106  12363   7573   2379    793   4004       C  
ATOM   1517  OH  TYR B 106       2.091 -15.488  33.707  1.00 86.71           O  
ANISOU 1517  OH  TYR B 106    10904  13718   8325   2600    639   4414       O  
ATOM   1518  N   GLY B 107      -3.818 -16.608  30.194  1.00 62.02           N  
ANISOU 1518  N   GLY B 107     8782   7944   6838   1627   2591   3225       N  
ATOM   1519  CA  GLY B 107      -4.861 -17.221  31.004  1.00 64.59           C  
ANISOU 1519  CA  GLY B 107     9263   8129   7149   1511   2959   3290       C  
ATOM   1520  C   GLY B 107      -6.211 -16.799  30.443  1.00 65.16           C  
ANISOU 1520  C   GLY B 107     9335   8024   7397   1117   3180   2789       C  
ATOM   1521  O   GLY B 107      -6.517 -17.060  29.267  1.00 65.57           O  
ANISOU 1521  O   GLY B 107     9341   7677   7894    922   3346   2502       O  
ATOM   1522  N   VAL B 108      -7.020 -16.134  31.262  1.00 63.74           N  
ANISOU 1522  N   VAL B 108     9165   8177   6877    976   3181   2633       N  
ATOM   1523  CA  VAL B 108      -8.264 -15.567  30.764  1.00 60.51           C  
ANISOU 1523  CA  VAL B 108     8638   7701   6652    641   3327   2116       C  
ATOM   1524  C   VAL B 108      -8.163 -14.048  30.627  1.00 57.38           C  
ANISOU 1524  C   VAL B 108     8051   7719   6031    605   2819   1686       C  
ATOM   1525  O   VAL B 108      -9.096 -13.411  30.140  1.00 59.94           O  
ANISOU 1525  O   VAL B 108     8195   8022   6559    389   2796   1233       O  
ATOM   1526  CB  VAL B 108      -9.485 -15.931  31.653  1.00 66.32           C  
ANISOU 1526  CB  VAL B 108     9432   8396   7370    456   3685   2073       C  
ATOM   1527  CG1 VAL B 108      -9.923 -17.362  31.384  1.00 70.30           C  
ANISOU 1527  CG1 VAL B 108    10020   8342   8347    347   4087   2182       C  
ATOM   1528  CG2 VAL B 108      -9.194 -15.701  33.143  1.00 68.15           C  
ANISOU 1528  CG2 VAL B 108     9811   9069   7015    619   3596   2371       C  
ATOM   1529  N   ALA B 109      -7.027 -13.488  31.028  1.00 51.92           N  
ANISOU 1529  N   ALA B 109     7375   7394   4959    815   2435   1841       N  
ATOM   1530  CA  ALA B 109      -6.759 -12.069  30.868  1.00 47.80           C  
ANISOU 1530  CA  ALA B 109     6703   7187   4273    764   2005   1433       C  
ATOM   1531  C   ALA B 109      -6.228 -11.758  29.465  1.00 47.65           C  
ANISOU 1531  C   ALA B 109     6523   6958   4623    754   1718   1220       C  
ATOM   1532  O   ALA B 109      -5.648 -12.625  28.797  1.00 50.59           O  
ANISOU 1532  O   ALA B 109     6918   7061   5241    844   1771   1447       O  
ATOM   1533  CB  ALA B 109      -5.781 -11.604  31.904  1.00 50.21           C  
ANISOU 1533  CB  ALA B 109     7068   8014   3997    904   1738   1621       C  
ATOM   1534  N   TRP B 110      -6.409 -10.520  29.014  1.00 40.75           N  
ANISOU 1534  N   TRP B 110     5503   6183   3796    653   1463    801       N  
ATOM   1535  CA  TRP B 110      -5.962 -10.158  27.670  1.00 35.45           C  
ANISOU 1535  CA  TRP B 110     4699   5341   3430    637   1214    627       C  
ATOM   1536  C   TRP B 110      -5.938  -8.649  27.468  1.00 33.56           C  
ANISOU 1536  C   TRP B 110     4343   5251   3159    591    948    271       C  
ATOM   1537  O   TRP B 110      -6.520  -7.889  28.251  1.00 34.91           O  
ANISOU 1537  O   TRP B 110     4517   5579   3168    539   1019     74       O  
ATOM   1538  CB  TRP B 110      -6.876 -10.806  26.630  1.00 37.60           C  
ANISOU 1538  CB  TRP B 110     4896   5279   4111    484   1415    507       C  
ATOM   1539  CG  TRP B 110      -8.307 -10.389  26.811  1.00 36.45           C  
ANISOU 1539  CG  TRP B 110     4623   5165   4061    331   1575    248       C  
ATOM   1540  CD1 TRP B 110      -9.220 -10.921  27.674  1.00 41.65           C  
ANISOU 1540  CD1 TRP B 110     5329   5816   4681    252   1936    305       C  
ATOM   1541  CD2 TRP B 110      -8.972  -9.323  26.131  1.00 35.59           C  
ANISOU 1541  CD2 TRP B 110     4289   5110   4125    273   1406    -65       C  
ATOM   1542  NE1 TRP B 110     -10.427 -10.269  27.556  1.00 41.88           N  
ANISOU 1542  NE1 TRP B 110     5138   5901   4875    134   2002      8       N  
ATOM   1543  CE2 TRP B 110     -10.306  -9.291  26.605  1.00 39.69           C  
ANISOU 1543  CE2 TRP B 110     4679   5663   4737    171   1671   -196       C  
ATOM   1544  CE3 TRP B 110      -8.583  -8.427  25.122  1.00 33.96           C  
ANISOU 1544  CE3 TRP B 110     3964   4914   4027    316   1088   -202       C  
ATOM   1545  CZ2 TRP B 110     -11.249  -8.363  26.138  1.00 38.05           C  
ANISOU 1545  CZ2 TRP B 110     4188   5524   4747    156   1604   -437       C  
ATOM   1546  CZ3 TRP B 110      -9.513  -7.513  24.665  1.00 35.12           C  
ANISOU 1546  CZ3 TRP B 110     3875   5109   4359    305   1028   -403       C  
ATOM   1547  CH2 TRP B 110     -10.833  -7.486  25.168  1.00 34.32           C  
ANISOU 1547  CH2 TRP B 110     3608   5061   4371    245   1273   -509       C  
ATOM   1548  N   ASP B 111      -5.268  -8.223  26.403  1.00 34.63           N  
ANISOU 1548  N   ASP B 111     4391   5293   3473    606    704    190       N  
ATOM   1549  CA  ASP B 111      -5.205  -6.818  26.016  1.00 33.87           C  
ANISOU 1549  CA  ASP B 111     4200   5229   3440    573    509    -99       C  
ATOM   1550  C   ASP B 111      -4.785  -6.784  24.538  1.00 33.04           C  
ANISOU 1550  C   ASP B 111     4014   4936   3602    574    351   -101       C  
ATOM   1551  O   ASP B 111      -4.424  -7.808  23.980  1.00 34.78           O  
ANISOU 1551  O   ASP B 111     4267   5039   3908    584    395     69       O  
ATOM   1552  CB  ASP B 111      -4.225  -6.034  26.905  1.00 34.02           C  
ANISOU 1552  CB  ASP B 111     4265   5522   3138    575    348   -173       C  
ATOM   1553  CG  ASP B 111      -4.444  -4.517  26.845  1.00 36.61           C  
ANISOU 1553  CG  ASP B 111     4546   5809   3555    498    313   -538       C  
ATOM   1554  OD1 ASP B 111      -3.551  -3.755  27.285  1.00 36.03           O  
ANISOU 1554  OD1 ASP B 111     4489   5904   3297    422    181   -695       O  
ATOM   1555  OD2 ASP B 111      -5.501  -4.071  26.361  1.00 35.08           O  
ANISOU 1555  OD2 ASP B 111     4278   5412   3639    509    440   -666       O  
ATOM   1556  N   TYR B 112      -4.871  -5.625  23.909  1.00 35.61           N  
ANISOU 1556  N   TYR B 112     4255   5211   4064    564    224   -286       N  
ATOM   1557  CA  TYR B 112      -4.484  -5.480  22.509  1.00 32.86           C  
ANISOU 1557  CA  TYR B 112     3851   4734   3900    560     84   -266       C  
ATOM   1558  C   TYR B 112      -4.129  -4.035  22.174  1.00 32.50           C  
ANISOU 1558  C   TYR B 112     3770   4640   3938    585    -36   -395       C  
ATOM   1559  O   TYR B 112      -4.454  -3.114  22.942  1.00 30.73           O  
ANISOU 1559  O   TYR B 112     3549   4426   3702    592     35   -557       O  
ATOM   1560  CB  TYR B 112      -5.615  -5.973  21.578  1.00 33.54           C  
ANISOU 1560  CB  TYR B 112     3829   4756   4157    494    146   -277       C  
ATOM   1561  CG  TYR B 112      -6.837  -5.066  21.496  1.00 34.88           C  
ANISOU 1561  CG  TYR B 112     3828   4961   4465    529    160   -386       C  
ATOM   1562  CD1 TYR B 112      -7.158  -4.385  20.311  1.00 32.29           C  
ANISOU 1562  CD1 TYR B 112     3357   4636   4275    570     15   -363       C  
ATOM   1563  CD2 TYR B 112      -7.649  -4.849  22.616  1.00 35.84           C  
ANISOU 1563  CD2 TYR B 112     3915   5126   4576    552    341   -473       C  
ATOM   1564  CE1 TYR B 112      -8.287  -3.538  20.242  1.00 34.35           C  
ANISOU 1564  CE1 TYR B 112     3405   4938   4710    680     38   -377       C  
ATOM   1565  CE2 TYR B 112      -8.743  -4.013  22.562  1.00 36.31           C  
ANISOU 1565  CE2 TYR B 112     3778   5191   4828    632    404   -553       C  
ATOM   1566  CZ  TYR B 112      -9.078  -3.365  21.361  1.00 36.45           C  
ANISOU 1566  CZ  TYR B 112     3611   5206   5034    719    245   -481       C  
ATOM   1567  OH  TYR B 112     -10.201  -2.530  21.315  1.00 35.18           O  
ANISOU 1567  OH  TYR B 112     3195   5059   5112    872    322   -480       O  
ATOM   1568  N   LYS B 113      -3.441  -3.849  21.039  1.00 28.94           N  
ANISOU 1568  N   LYS B 113     3311   4103   3583    583   -155   -334       N  
ATOM   1569  CA  LYS B 113      -3.166  -2.526  20.496  1.00 26.59           C  
ANISOU 1569  CA  LYS B 113     2995   3686   3421    607   -209   -396       C  
ATOM   1570  C   LYS B 113      -3.337  -2.586  18.969  1.00 31.07           C  
ANISOU 1570  C   LYS B 113     3521   4198   4086    624   -283   -259       C  
ATOM   1571  O   LYS B 113      -3.412  -3.676  18.397  1.00 29.01           O  
ANISOU 1571  O   LYS B 113     3261   4003   3757    562   -296   -195       O  
ATOM   1572  CB  LYS B 113      -1.756  -2.070  20.860  1.00 28.04           C  
ANISOU 1572  CB  LYS B 113     3227   3886   3541    539   -268   -467       C  
ATOM   1573  CG  LYS B 113      -1.579  -1.710  22.400  1.00 32.02           C  
ANISOU 1573  CG  LYS B 113     3757   4547   3862    467   -227   -666       C  
ATOM   1574  CD  LYS B 113      -2.429  -0.535  22.774  1.00 34.30           C  
ANISOU 1574  CD  LYS B 113     4066   4678   4288    467    -62   -880       C  
ATOM   1575  CE  LYS B 113      -2.374  -0.238  24.298  1.00 36.00           C  
ANISOU 1575  CE  LYS B 113     4339   5083   4255    340     29  -1150       C  
ATOM   1576  NZ  LYS B 113      -3.056  -1.333  25.025  1.00 36.79           N  
ANISOU 1576  NZ  LYS B 113     4455   5395   4128    392     66  -1031       N  
ATOM   1577  N   TYR B 114      -3.385  -1.431  18.321  1.00 31.27           N  
ANISOU 1577  N   TYR B 114     3528   4101   4254    693   -296   -215       N  
ATOM   1578  CA  TYR B 114      -3.408  -1.389  16.859  1.00 30.06           C  
ANISOU 1578  CA  TYR B 114     3354   3967   4102    708   -382    -39       C  
ATOM   1579  C   TYR B 114      -1.996  -1.114  16.351  1.00 33.63           C  
ANISOU 1579  C   TYR B 114     3918   4310   4549    641   -380    -14       C  
ATOM   1580  O   TYR B 114      -1.247  -0.378  17.002  1.00 29.21           O  
ANISOU 1580  O   TYR B 114     3399   3616   4082    614   -316   -120       O  
ATOM   1581  CB  TYR B 114      -4.371  -0.313  16.372  1.00 33.28           C  
ANISOU 1581  CB  TYR B 114     3652   4326   4668    881   -378    112       C  
ATOM   1582  CG  TYR B 114      -5.850  -0.705  16.509  1.00 37.98           C  
ANISOU 1582  CG  TYR B 114     4036   5118   5276    946   -410    133       C  
ATOM   1583  CD1 TYR B 114      -6.430  -1.596  15.617  1.00 40.03           C  
ANISOU 1583  CD1 TYR B 114     4174   5667   5369    848   -553    197       C  
ATOM   1584  CD2 TYR B 114      -6.656  -0.159  17.501  1.00 37.65           C  
ANISOU 1584  CD2 TYR B 114     3898   4988   5418   1069   -266     51       C  
ATOM   1585  CE1 TYR B 114      -7.775  -1.958  15.710  1.00 42.70           C  
ANISOU 1585  CE1 TYR B 114     4255   6236   5734    855   -587    188       C  
ATOM   1586  CE2 TYR B 114      -8.007  -0.528  17.628  1.00 40.31           C  
ANISOU 1586  CE2 TYR B 114     3988   5524   5805   1121   -268     69       C  
ATOM   1587  CZ  TYR B 114      -8.558  -1.443  16.734  1.00 43.63           C  
ANISOU 1587  CZ  TYR B 114     4245   6263   6069   1005   -445    141       C  
ATOM   1588  OH  TYR B 114      -9.903  -1.819  16.804  1.00 47.57           O  
ANISOU 1588  OH  TYR B 114     4431   7015   6630   1003   -457    132       O  
ATOM   1589  N   LEU B 115      -1.647  -1.747  15.224  1.00 31.20           N  
ANISOU 1589  N   LEU B 115     3646   4083   4124    572   -422     80       N  
ATOM   1590  CA  LEU B 115      -0.421  -1.507  14.463  1.00 33.70           C  
ANISOU 1590  CA  LEU B 115     4049   4313   4441    510   -378    135       C  
ATOM   1591  C   LEU B 115      -0.811  -1.213  13.026  1.00 35.12           C  
ANISOU 1591  C   LEU B 115     4259   4574   4510    523   -413    329       C  
ATOM   1592  O   LEU B 115      -1.764  -1.810  12.523  1.00 32.02           O  
ANISOU 1592  O   LEU B 115     3807   4405   3955    499   -506    356       O  
ATOM   1593  CB  LEU B 115       0.497  -2.735  14.480  1.00 36.04           C  
ANISOU 1593  CB  LEU B 115     4372   4655   4667    413   -327     60       C  
ATOM   1594  CG  LEU B 115       1.133  -3.203  15.772  1.00 40.20           C  
ANISOU 1594  CG  LEU B 115     4845   5193   5238    428   -315    -28       C  
ATOM   1595  CD1 LEU B 115       1.877  -4.523  15.615  1.00 35.56           C  
ANISOU 1595  CD1 LEU B 115     4259   4618   4634    416   -218      2       C  
ATOM   1596  CD2 LEU B 115       2.050  -2.102  16.264  1.00 44.19           C  
ANISOU 1596  CD2 LEU B 115     5303   5637   5850    399   -325    -90       C  
ATOM   1597  N   THR B 116      -0.082  -0.333  12.349  1.00 36.33           N  
ANISOU 1597  N   THR B 116     4495   4590   4719    533   -335    464       N  
ATOM   1598  CA  THR B 116      -0.366  -0.074  10.942  1.00 37.35           C  
ANISOU 1598  CA  THR B 116     4677   4856   4658    551   -365    711       C  
ATOM   1599  C   THR B 116       0.857  -0.407  10.095  1.00 38.10           C  
ANISOU 1599  C   THR B 116     4902   4932   4641    396   -232    696       C  
ATOM   1600  O   THR B 116       1.973  -0.056  10.449  1.00 34.51           O  
ANISOU 1600  O   THR B 116     4474   4255   4383    349    -89    623       O  
ATOM   1601  CB  THR B 116      -0.786   1.391  10.692  1.00 44.84           C  
ANISOU 1601  CB  THR B 116     5628   5641   5768    756   -321   1009       C  
ATOM   1602  OG1 THR B 116      -2.013   1.658  11.383  1.00 50.90           O  
ANISOU 1602  OG1 THR B 116     6240   6436   6662    931   -404   1033       O  
ATOM   1603  CG2 THR B 116      -1.028   1.639   9.181  1.00 40.62           C  
ANISOU 1603  CG2 THR B 116     5148   5331   4953    803   -373   1364       C  
ATOM   1604  N   LEU B 117       0.625  -1.103   8.978  1.00 36.95           N  
ANISOU 1604  N   LEU B 117     4814   5057   4168    286   -264    728       N  
ATOM   1605  CA  LEU B 117       1.677  -1.385   8.033  1.00 35.28           C  
ANISOU 1605  CA  LEU B 117     4743   4843   3817    137    -81    713       C  
ATOM   1606  C   LEU B 117       1.396  -0.640   6.758  1.00 33.83           C  
ANISOU 1606  C   LEU B 117     4661   4842   3350    162    -98   1032       C  
ATOM   1607  O   LEU B 117       0.330  -0.776   6.187  1.00 38.43           O  
ANISOU 1607  O   LEU B 117     5195   5783   3625    171   -295   1147       O  
ATOM   1608  CB  LEU B 117       1.787  -2.875   7.759  1.00 35.26           C  
ANISOU 1608  CB  LEU B 117     4775   4980   3642    -55     -6    435       C  
ATOM   1609  CG  LEU B 117       2.755  -3.382   6.693  1.00 37.15           C  
ANISOU 1609  CG  LEU B 117     5167   5236   3711   -233    250    349       C  
ATOM   1610  CD1 LEU B 117       4.210  -2.932   6.918  1.00 37.68           C  
ANISOU 1610  CD1 LEU B 117     5230   5007   4081   -192    476    382       C  
ATOM   1611  CD2 LEU B 117       2.638  -4.874   6.787  1.00 39.90           C  
ANISOU 1611  CD2 LEU B 117     5528   5608   4023   -386    368     29       C  
ATOM   1612  N  ALYS B 118       2.356   0.171   6.333  0.51 35.23           N  
ANISOU 1612  N  ALYS B 118     4956   4803   3627    168    111   1199       N  
ATOM   1613  N  BLYS B 118       2.377   0.154   6.339  0.49 35.20           N  
ANISOU 1613  N  BLYS B 118     4953   4797   3626    165    114   1192       N  
ATOM   1614  CA ALYS B 118       2.270   0.879   5.061  0.51 41.08           C  
ANISOU 1614  CA ALYS B 118     5839   5699   4071    198    162   1573       C  
ATOM   1615  CA BLYS B 118       2.341   0.913   5.091  0.49 41.27           C  
ANISOU 1615  CA BLYS B 118     5865   5695   4119    198    178   1570       C  
ATOM   1616  C  ALYS B 118       3.351   0.347   4.119  0.51 44.17           C  
ANISOU 1616  C  ALYS B 118     6399   6147   4238    -35    422   1462       C  
ATOM   1617  C  BLYS B 118       3.371   0.329   4.119  0.49 44.12           C  
ANISOU 1617  C  BLYS B 118     6393   6139   4232    -39    427   1455       C  
ATOM   1618  O  ALYS B 118       4.494   0.128   4.517  0.51 43.43           O  
ANISOU 1618  O  ALYS B 118     6294   5774   4434   -128    653   1243       O  
ATOM   1619  O  BLYS B 118       4.509   0.060   4.501  0.49 43.29           O  
ANISOU 1619  O  BLYS B 118     6277   5765   4405   -138    656   1227       O  
ATOM   1620  CB ALYS B 118       2.416   2.392   5.262  0.51 43.62           C  
ANISOU 1620  CB ALYS B 118     6195   5654   4725    403    292   1920       C  
ATOM   1621  CB BLYS B 118       2.632   2.398   5.356  0.49 43.61           C  
ANISOU 1621  CB BLYS B 118     6199   5589   4781    380    335   1876       C  
ATOM   1622  CG ALYS B 118       1.184   3.054   5.870  0.51 44.10           C  
ANISOU 1622  CG ALYS B 118     6114   5684   4959    680    101   2122       C  
ATOM   1623  CG BLYS B 118       2.546   3.294   4.131  0.49 47.87           C  
ANISOU 1623  CG BLYS B 118     6903   6203   5081    483    444   2389       C  
ATOM   1624  N   VAL B 119       2.968   0.118   2.873  1.00 45.61           N  
ANISOU 1624  N   VAL B 119     6707   6742   3879   -135    386   1603       N  
ATOM   1625  CA  VAL B 119       3.862  -0.469   1.880  1.00 51.10           C  
ANISOU 1625  CA  VAL B 119     7590   7546   4278   -387    673   1452       C  
ATOM   1626  C   VAL B 119       4.182   0.580   0.832  1.00 54.40           C  
ANISOU 1626  C   VAL B 119     8200   8020   4451   -343    836   1914       C  
ATOM   1627  O   VAL B 119       3.282   0.984   0.111  1.00 59.47           O  
ANISOU 1627  O   VAL B 119     8880   9065   4651   -255    621   2278       O  
ATOM   1628  CB  VAL B 119       3.201  -1.712   1.242  1.00 52.68           C  
ANISOU 1628  CB  VAL B 119     7824   8227   3964   -636    564   1144       C  
ATOM   1629  CG1 VAL B 119       4.074  -2.326   0.208  1.00 57.21           C  
ANISOU 1629  CG1 VAL B 119     8619   8899   4221   -916    925    931       C  
ATOM   1630  CG2 VAL B 119       2.873  -2.739   2.334  1.00 48.97           C  
ANISOU 1630  CG2 VAL B 119     7186   7613   3806   -666    474    734       C  
ATOM   1631  N   LYS B 120       5.404   1.102   0.809  1.00 57.03           N  
ANISOU 1631  N   LYS B 120     8615   7960   5094   -377   1205   1956       N  
ATOM   1632  CA  LYS B 120       5.932   1.965  -0.264  1.00 64.53           C  
ANISOU 1632  CA  LYS B 120     9793   8905   5822   -396   1494   2364       C  
ATOM   1633  C   LYS B 120       6.414   1.226  -1.478  1.00 66.76           C  
ANISOU 1633  C   LYS B 120    10283   9533   5550   -672   1734   2224       C  
ATOM   1634  O   LYS B 120       6.823   0.105  -1.364  1.00 66.57           O  
ANISOU 1634  O   LYS B 120    10220   9531   5543   -866   1845   1734       O  
ATOM   1635  CB  LYS B 120       7.161   2.723   0.183  1.00 69.57           C  
ANISOU 1635  CB  LYS B 120    10412   8975   7048   -413   1872   2372       C  
ATOM   1636  CG  LYS B 120       7.195   3.214   1.594  1.00 67.42           C  
ANISOU 1636  CG  LYS B 120     9915   8276   7426   -286   1772   2241       C  
ATOM   1637  CD  LYS B 120       8.585   3.689   1.930  1.00 69.90           C  
ANISOU 1637  CD  LYS B 120    10160   8159   8240   -439   2159   2098       C  
ATOM   1638  CE  LYS B 120       9.624   2.639   1.621  1.00 71.33           C  
ANISOU 1638  CE  LYS B 120    10279   8451   8374   -655   2382   1744       C  
ATOM   1639  NZ  LYS B 120      10.830   2.828   2.455  1.00 72.38           N  
ANISOU 1639  NZ  LYS B 120    10146   8260   9096   -770   2583   1482       N  
ATOM   1640  N   ALA B 121       6.461   1.886  -2.630  1.00 69.76           N  
ANISOU 1640  N   ALA B 121    10901  10137   5469   -684   1889   2666       N  
ATOM   1641  CA  ALA B 121       7.093   1.309  -3.806  1.00 75.65           C  
ANISOU 1641  CA  ALA B 121    11823  11181   5741   -951   2189   2499       C  
ATOM   1642  C   ALA B 121       8.553   1.752  -3.897  1.00 76.62           C  
ANISOU 1642  C   ALA B 121    11952  10834   6325  -1041   2680   2465       C  
ATOM   1643  O   ALA B 121       8.913   2.828  -3.416  1.00 77.21           O  
ANISOU 1643  O   ALA B 121    11983  10459   6895   -908   2779   2744       O  
ATOM   1644  CB  ALA B 121       6.347   1.704  -5.038  1.00 84.92           C  
ANISOU 1644  CB  ALA B 121    13224  12772   6271   -818   2038   2848       C  
TER    1645      ALA B 121                                                      
HETATM 1646 MG    MG A 201     -12.423  21.789  37.851  1.00 10.21          MG  
HETATM 1647  O   HOH A 301     -23.200  -0.301  40.120  1.00 39.37           O  
HETATM 1648  O   HOH A 302      -6.321   6.088  29.395  1.00 43.19           O  
HETATM 1649  O   HOH A 303     -22.083  -2.141  20.937  1.00 41.28           O  
HETATM 1650  O   HOH A 304     -25.261  12.245  34.406  1.00 52.54           O  
HETATM 1651  O   HOH A 305     -24.885   3.029  32.595  1.00 47.29           O  
HETATM 1652  O   HOH A 306     -10.403   9.535  25.067  1.00 36.60           O  
HETATM 1653  O   HOH A 307      -4.587 -10.265  34.955  1.00 61.56           O  
HETATM 1654  O   HOH A 308      -8.230  -8.835  30.592  1.00 36.54           O  
HETATM 1655  O   HOH A 309     -21.281  20.925  35.993  1.00 50.08           O  
HETATM 1656  O   HOH A 310     -25.252  -1.782  28.133  1.00 54.09           O  
HETATM 1657  O   HOH A 311      -8.911 -19.801  17.605  1.00 54.02           O  
HETATM 1658  O   HOH A 312     -23.034  14.524  38.000  1.00 40.79           O  
HETATM 1659  O   HOH A 313     -16.657  12.218  48.606  1.00 69.31           O  
HETATM 1660  O   HOH A 314     -10.109   8.110  32.307  1.00 33.09           O  
HETATM 1661  O   HOH A 315     -11.900   7.714  39.918  1.00 36.82           O  
HETATM 1662  O   HOH A 316     -16.739  11.026  49.721  1.00 69.52           O  
HETATM 1663  O   HOH A 317     -14.905  23.868  39.927  1.00 45.13           O  
HETATM 1664  O   HOH A 318     -15.672   0.253  18.397  1.00 44.41           O  
HETATM 1665  O   HOH A 319     -25.031   6.323  34.427  1.00 49.13           O  
HETATM 1666  O   HOH A 320      -7.828  10.805  33.107  1.00 47.89           O  
HETATM 1667  O   HOH A 321     -21.450   9.546  21.544  1.00 44.60           O  
HETATM 1668  O   HOH A 322      -6.222   1.301  35.492  1.00 47.37           O  
HETATM 1669  O   HOH A 323     -16.498  18.765  29.401  1.00 57.18           O  
HETATM 1670  O   HOH A 324     -24.129 -11.311  39.009  1.00 73.80           O  
HETATM 1671  O   HOH A 325     -15.980  19.531  42.414  1.00 54.58           O  
HETATM 1672  O   HOH A 326     -18.847   0.126  38.624  1.00 43.58           O  
HETATM 1673  O   HOH A 327     -14.776  -4.993  16.979  1.00 49.61           O  
HETATM 1674  O   HOH A 328     -23.492  -0.094  22.392  1.00 47.19           O  
HETATM 1675  O   HOH A 329     -23.090   8.084  36.258  1.00 44.88           O  
HETATM 1676  O   HOH A 330     -22.806   9.951  40.206  1.00 54.76           O  
HETATM 1677  O   HOH A 331     -17.418  22.428  31.944  1.00 40.14           O  
HETATM 1678  O   HOH A 332     -10.349  11.123  41.000  1.00 42.33           O  
HETATM 1679  O   HOH A 333     -14.338 -11.481  26.493  1.00 44.42           O  
HETATM 1680  O   HOH A 334      -9.238   3.184  16.875  1.00 56.84           O  
HETATM 1681  O   HOH A 335     -14.904  13.729  44.439  1.00 43.93           O  
HETATM 1682  O   HOH A 336     -26.738   3.100  30.515  1.00 57.55           O  
HETATM 1683  O   HOH A 337     -11.226  17.652  37.643  1.00 41.73           O  
HETATM 1684  O   HOH A 338      -6.248   8.367  35.809  1.00 44.88           O  
HETATM 1685  O   HOH A 339     -25.610  11.969  30.497  1.00 45.95           O  
HETATM 1686  O   HOH A 340     -12.611  15.391  40.612  1.00 39.82           O  
HETATM 1687  O   HOH A 341     -22.882  16.125  43.554  1.00 63.16           O  
HETATM 1688  O   HOH A 342     -23.972  -5.676  19.453  1.00 56.39           O  
HETATM 1689  O   HOH A 343     -19.242  -7.960  40.741  1.00 55.27           O  
HETATM 1690  O   HOH A 344     -24.809  15.560  34.889  1.00 69.17           O  
HETATM 1691  O   HOH A 345      -6.648 -17.237  15.642  1.00 53.29           O  
HETATM 1692  O   HOH A 346     -26.583   9.077  25.046  1.00 67.01           O  
HETATM 1693  O   HOH A 347     -27.329   5.575  24.313  1.00 59.43           O  
HETATM 1694  O   HOH A 348     -12.627  -6.523  39.220  1.00 65.30           O  
HETATM 1695  O   HOH A 349     -18.344   3.513  17.529  1.00 40.36           O  
HETATM 1696  O   HOH A 350     -21.135 -14.442  22.657  1.00 54.40           O  
HETATM 1697  O   HOH A 351      -5.701  13.730  36.592  1.00 58.09           O  
HETATM 1698  O   HOH A 352      -5.104   1.400  43.064  1.00 68.56           O  
HETATM 1699  O   HOH A 353      -9.955  -4.337  37.118  1.00 56.18           O  
HETATM 1700  O   HOH A 354     -21.258  -0.014  40.488  1.00 59.28           O  
HETATM 1701  O   HOH A 355      -7.618   7.364  31.834  1.00 35.02           O  
HETATM 1702  O   HOH A 356     -11.877 -22.060  17.397  1.00 57.27           O  
HETATM 1703  O   HOH A 357      -6.402   3.744  38.398  1.00 58.98           O  
HETATM 1704  O   HOH A 358     -14.658  21.820  42.169  1.00 67.54           O  
HETATM 1705  O   HOH A 359      -6.500   6.864  26.851  1.00 50.83           O  
HETATM 1706  O   HOH A 360     -13.418  17.631  41.547  1.00 50.58           O  
HETATM 1707  O   HOH A 361     -18.336 -14.096  21.741  1.00 59.29           O  
HETATM 1708  O   HOH A 362     -10.486   8.212  42.653  1.00 58.03           O  
HETATM 1709  O   HOH A 363     -12.866 -16.068  33.587  1.00 63.38           O  
HETATM 1710  O   HOH A 364     -26.605  10.470  22.549  1.00 52.94           O  
HETATM 1711  O   HOH A 365     -24.686  10.560  35.917  1.00 46.11           O  
HETATM 1712  O   HOH A 366     -12.820  14.810  43.469  1.00 60.93           O  
HETATM 1713  O   HOH A 367     -11.481 -15.730  36.023  1.00 71.36           O  
HETATM 1714  O   HOH A 368     -15.832 -26.075  25.786  1.00 67.53           O  
HETATM 1715  O   HOH A 369     -24.323   5.290  19.367  1.00 61.98           O  
HETATM 1716  O   HOH A 370     -26.836   7.978  32.921  1.00 49.25           O  
HETATM 1717  O   HOH A 371     -17.404   6.366  16.634  1.00 62.38           O  
HETATM 1718  O   HOH A 372     -13.775 -25.449  26.888  1.00 79.87           O  
HETATM 1719  O   HOH A 373       1.844   8.012  23.188  1.00 76.81           O  
HETATM 1720  O   HOH B 201       1.990  -6.171  -4.313  1.00 46.07           O  
HETATM 1721  O   HOH B 202       5.380  -1.733  18.078  1.00 42.03           O  
HETATM 1722  O   HOH B 203       9.131  -3.175  16.236  1.00 42.13           O  
HETATM 1723  O   HOH B 204      -8.426 -10.736  11.463  1.00 55.62           O  
HETATM 1724  O   HOH B 205      -3.752  -1.172  27.706  1.00 30.61           O  
HETATM 1725  O   HOH B 206     -10.654  -8.957  15.970  1.00 47.50           O  
HETATM 1726  O   HOH B 207     -11.161  -2.151  14.499  1.00 68.03           O  
HETATM 1727  O   HOH B 208       6.936 -13.148  20.077  1.00 42.17           O  
HETATM 1728  O   HOH B 209      13.293 -15.900  14.555  1.00 39.68           O  
HETATM 1729  O   HOH B 210      11.909  -5.197  -1.529  1.00 51.43           O  
HETATM 1730  O   HOH B 211       5.055 -12.031  -1.300  1.00 69.82           O  
HETATM 1731  O   HOH B 212       6.716 -24.401  18.382  1.00 56.79           O  
HETATM 1732  O   HOH B 213      -0.676  -9.652   6.203  1.00 43.69           O  
HETATM 1733  O   HOH B 214      10.080 -18.999  15.961  1.00 37.23           O  
HETATM 1734  O   HOH B 215      12.672 -11.935   1.844  1.00 53.58           O  
HETATM 1735  O   HOH B 216      -6.450  -3.897   7.581  1.00 43.31           O  
HETATM 1736  O   HOH B 217       5.516 -14.125   0.045  1.00 59.28           O  
HETATM 1737  O   HOH B 218      -8.793   2.192  14.011  1.00 73.70           O  
HETATM 1738  O   HOH B 219      13.594  -2.415  -2.493  1.00 62.89           O  
HETATM 1739  O   HOH B 220      -4.486  -3.749   1.719  1.00 45.17           O  
HETATM 1740  O   HOH B 221       1.348 -17.126  14.225  1.00 42.61           O  
HETATM 1741  O   HOH B 222      -1.105   2.064  14.167  1.00 60.92           O  
HETATM 1742  O   HOH B 223      13.398 -18.359  23.686  1.00 51.45           O  
HETATM 1743  O   HOH B 224      13.040  -9.195  13.096  1.00 55.34           O  
HETATM 1744  O   HOH B 225       0.200 -17.959  20.530  1.00 49.36           O  
HETATM 1745  O   HOH B 226      -5.277 -11.712   9.904  1.00 41.48           O  
HETATM 1746  O   HOH B 227      11.006  -5.310  10.589  1.00 41.18           O  
HETATM 1747  O   HOH B 228      11.708 -14.287   3.627  1.00 52.01           O  
HETATM 1748  O   HOH B 229       5.103   4.636  14.892  1.00 66.66           O  
HETATM 1749  O   HOH B 230      13.643  -7.930   3.769  1.00 42.90           O  
HETATM 1750  O   HOH B 231      -3.550   2.482  14.129  1.00 55.95           O  
HETATM 1751  O   HOH B 232       7.650 -19.522  16.191  1.00 43.67           O  
HETATM 1752  O   HOH B 233      -6.853  -1.015   7.397  1.00 54.42           O  
HETATM 1753  O   HOH B 234      -5.766 -19.056  27.135  1.00 51.70           O  
HETATM 1754  O   HOH B 235       4.323 -19.716  14.727  1.00 60.95           O  
HETATM 1755  O   HOH B 236       0.653  -0.503  30.031  1.00 51.73           O  
HETATM 1756  O   HOH B 237      10.560  -2.550  -4.237  1.00 57.19           O  
HETATM 1757  O   HOH B 238       9.220   2.118   9.552  1.00 49.01           O  
HETATM 1758  O   HOH B 239       0.813   1.581  23.702  1.00 57.37           O  
HETATM 1759  O   HOH B 240       9.526 -22.018  19.625  1.00 51.94           O  
HETATM 1760  O   HOH B 241       7.671  -5.745  27.881  1.00 60.74           O  
HETATM 1761  O   HOH B 242       3.767 -23.040  34.067  1.00 59.96           O  
HETATM 1762  O   HOH B 243      11.291  -2.217  13.161  1.00 63.39           O  
HETATM 1763  O   HOH B 244       5.609 -12.232  -2.646  1.00 69.92           O  
HETATM 1764  O   HOH B 245       4.113  -1.839  -3.839  1.00 71.29           O  
HETATM 1765  O   HOH B 246      14.673  -7.560   1.360  1.00 55.30           O  
HETATM 1766  O   HOH B 247      12.775  -6.171  14.964  1.00 65.93           O  
HETATM 1767  O   HOH B 248     -11.511  -6.158  13.611  1.00 61.64           O  
HETATM 1768  O   HOH B 249      -0.042   2.480  25.710  1.00 60.35           O  
HETATM 1769  O   HOH B 250      -3.229   5.299   8.016  1.00 78.22           O  
HETATM 1770  O   HOH B 251      -0.692 -21.465  15.484  1.00 65.91           O  
HETATM 1771  O   HOH B 252       3.479 -25.209  38.916  1.00 63.56           O  
CONECT  110 1646                                                                
CONECT  111 1646                                                                
CONECT  167  672                                                                
CONECT  168  673                                                                
CONECT  672  167                                                                
CONECT  673  168                                                                
CONECT  852 1646                                                                
CONECT  853 1646                                                                
CONECT 1063 1481                                                                
CONECT 1481 1063                                                                
CONECT 1646  110  111  852  853                                                 
MASTER      411    0    1    3   21    0    1    6 1724    2   11   21          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.