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***  SIGNALING PROTEIN/ANTAGONIST 20-JUL-17 5WIU  ***

elNémo ID: 1912132234402220

Job options:

ID        	=	 1912132234402220
JOBID     	=	 SIGNALING PROTEIN/ANTAGONIST 20-JUL-17 5WIU
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    SIGNALING PROTEIN/ANTAGONIST            20-JUL-17   5WIU              
TITLE     STRUCTURE OF THE HUMAN D4 DOPAMINE RECEPTOR IN COMPLEX WITH           
TITLE    2 NEMONAPRIDE                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D(4) DOPAMINE RECEPTOR, SOLUBLE CYTOCHROME B562 CHIMERA;   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: D(2C) DOPAMINE RECEPTOR, DOPAMINE D4 RECEPTOR, CYTOCHROME B-
COMPND   5 562;                                                                 
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI;                 
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606, 562;                                           
SOURCE   5 GENE: DRD4, CYBC;                                                    
SOURCE   6 EXPRESSION_SYSTEM: INSECTA;                                          
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 50557;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1-HM                              
KEYWDS    GPCR, DOPAMINE RECEPTOR, ANTAGONIST, SODIUM, SIGNALING PROTEIN-       
KEYWDS   2 ANTAGONIST COMPLEX                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.WACKER,S.WANG,A.LEVIT,T.CHE,R.M.BETZ,J.D.MCCORVY,                   
AUTHOR   2 A.J.VENKATAKRISHNAN,X.-P.HUANG,R.O.DROR,B.K.SHOICHET,B.L.ROTH        
REVDAT   4   27-NOV-19 5WIU    1       REMARK                                   
REVDAT   3   17-JAN-18 5WIU    1       REMARK                                   
REVDAT   2   01-NOV-17 5WIU    1       JRNL                                     
REVDAT   1   18-OCT-17 5WIU    0                                                
JRNL        AUTH   S.WANG,D.WACKER,A.LEVIT,T.CHE,R.M.BETZ,J.D.MCCORVY,          
JRNL        AUTH 2 A.J.VENKATAKRISHNAN,X.P.HUANG,R.O.DROR,B.K.SHOICHET,B.L.ROTH 
JRNL        TITL   D4 DOPAMINE RECEPTOR HIGH-RESOLUTION STRUCTURES ENABLE THE   
JRNL        TITL 2 DISCOVERY OF SELECTIVE AGONISTS.                             
JRNL        REF    SCIENCE                       V. 358   381 2017              
JRNL        REFN                   ESSN 1095-9203                               
JRNL        PMID   29051383                                                     
JRNL        DOI    10.1126/SCIENCE.AAN5468                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.96 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.96                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.59                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 33027                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : FREE R-VALUE                    
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.207                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.840                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1599                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2736                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 275                                     
REMARK   3   SOLVENT ATOMS            : 98                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 41.61                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 50.47                          
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  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.230         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5WIU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUL-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000229114.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-NOV-15                          
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               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.033                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL CRYO-COOLED         
REMARK 200                                   SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33049                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.12800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.01                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.84700                            
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: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 3PBL & 1M6T                              
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL, PH 5.8-6.2, 160-200     
REMARK 280  MM AMMONIUM PHOSPHATE DIBASIC, 34% PEG400, LIPIDIC CUBIC PHASE,     
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.06450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       42.06450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       33.84400            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       82.02350            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       33.84400            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       82.02350            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       42.06450            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       33.84400            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       82.02350            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       42.06450            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       33.84400            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       82.02350            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7270 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19540 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 10.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 P    PO4 A1203  LIES ON A SPECIAL POSITION.                          
REMARK 375 P    PO4 A1204  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1393  LIES ON A SPECIAL POSITION.                          
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     GLY A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     THR A    -1                                                      
REMARK 465     THR A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     ASN A     3                                                      
REMARK 465     ARG A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     THR A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     ASP A    10                                                      
REMARK 465     GLY A    11                                                      
REMARK 465     LEU A    12                                                      
REMARK 465     LEU A    13                                                      
REMARK 465     ALA A    14                                                      
REMARK 465     GLY A    15                                                      
REMARK 465     ARG A    16                                                      
REMARK 465     GLY A    17                                                      
REMARK 465     PRO A    18                                                      
REMARK 465     ALA A    19                                                      
REMARK 465     ALA A    20                                                      
REMARK 465     GLY A    21                                                      
REMARK 465     ALA A    22                                                      
REMARK 465     SER A    23                                                      
REMARK 465     ALA A    24                                                      
REMARK 465     GLY A    25                                                      
REMARK 465     ALA A    26                                                      
REMARK 465     SER A    27                                                      
REMARK 465     ALA A    28                                                      
REMARK 465     GLY A    29                                                      
REMARK 465     LEU A    30                                                      
REMARK 465     ALA A    31                                                      
REMARK 465     GLY A    32                                                      
REMARK 465     GLN A    33                                                      
REMARK 465     VAL A   177                                                      
REMARK 465     ARG A   178                                                      
REMARK 465     GLY A   179                                                      
REMARK 465     ARG A   180                                                      
REMARK 465     ASP A   181                                                      
REMARK 465     ASP A  1054                                                      
REMARK 465     SER A  1055                                                      
REMARK 465     LEU A   463                                                      
REMARK 465     ARG A   464                                                      
REMARK 465     ALA A   465                                                      
REMARK 465     CYS A   466                                                      
REMARK 465     CYS A   467                                                      
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     GLU A  62    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  63    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A  97    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 102    CG   CD1  CD2                                       
REMARK 470     GLN A 146    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 150    NE   CZ   NH1  NH2                                  
REMARK 470     ASP A 176    CG   OD1  OD2                                       
REMARK 470     ARG A 217    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASP A1012    CG   OD1  OD2                                       
REMARK 470     LYS A1015    CG   CD   CE   NZ                                   
REMARK 470     LYS A1019    CE   NZ                                             
REMARK 470     ASP A1021    CG   OD1  OD2                                       
REMARK 470     LYS A1047    CD   CE   NZ                                        
REMARK 470     LYS A1051    CE   NZ                                             
REMARK 470     LYS A1059    CG   CD   CE   NZ                                   
REMARK 470     PHE A1061    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG A1062    NE   CZ   NH1  NH2                                  
REMARK 470     GLU A1092    CG   CD   OE1  OE2                                  
REMARK 470     GLN A1093    CG   CD   OE1  NE2                                  
REMARK 470     THR A1096    OG1  CG2                                            
REMARK 470     ARG A1098    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR A1101    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A1104    CG   CD   CE   NZ                                   
REMARK 470     TYR A1105    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A 391    CG   CD   CE   NZ                                   
REMARK 470     ARG A 394    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 454    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 456    NE   CZ   NH1  NH2                                  
REMARK 470     ASN A 457    CG   OD1  ND2                                       
REMARK 470     ARG A 460    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 461    NZ                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A 201      -61.30   -136.08                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     OLA A 1205                                                       
REMARK 610     OLA A 1206                                                       
REMARK 610     OLA A 1207                                                       
REMARK 610     OLA A 1208                                                       
REMARK 610     OLA A 1211                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AQD A 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 1203                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 1204                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1205                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1206                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1207                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1208                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1209                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1210                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1211                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1212                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1213                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1214                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1216                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1218                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1219                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1220                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1221                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1223                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5WIV   RELATED DB: PDB                                   
DBREF  5WIU A    1  1001  UNP    P21917   DRD4_HUMAN       1    228             
DBREF  5WIU A 1002  1106  UNP    P0ABE7   C562_ECOLX      24    128             
DBREF  5WIU A  383   467  UNP    P21917   DRD4_HUMAN     383    467             
SEQADV 5WIU GLY A   -3  UNP  P21917              EXPRESSION TAG                 
SEQADV 5WIU GLY A   -2  UNP  P21917              EXPRESSION TAG                 
SEQADV 5WIU THR A   -1  UNP  P21917              EXPRESSION TAG                 
SEQADV 5WIU THR A    0  UNP  P21917              EXPRESSION TAG                 
SEQADV 5WIU TRP A 1007  UNP  P0ABE7    MET    29 ENGINEERED MUTATION            
SEQADV 5WIU ILE A 1102  UNP  P0ABE7    HIS   124 ENGINEERED MUTATION            
SEQADV 5WIU LEU A 1106  UNP  P0ABE7    ARG   128 ENGINEERED MUTATION            
SEQRES   1 A  422  GLY GLY THR THR MET GLY ASN ARG SER THR ALA ASP ALA          
SEQRES   2 A  422  ASP GLY LEU LEU ALA GLY ARG GLY PRO ALA ALA GLY ALA          
SEQRES   3 A  422  SER ALA GLY ALA SER ALA GLY LEU ALA GLY GLN GLY ALA          
SEQRES   4 A  422  ALA ALA LEU VAL GLY GLY VAL LEU LEU ILE GLY ALA VAL          
SEQRES   5 A  422  LEU ALA GLY ASN SER LEU VAL CYS VAL SER VAL ALA THR          
SEQRES   6 A  422  GLU ARG ALA LEU GLN THR PRO THR ASN SER PHE ILE VAL          
SEQRES   7 A  422  SER LEU ALA ALA ALA ASP LEU LEU LEU ALA LEU LEU VAL          
SEQRES   8 A  422  LEU PRO LEU PHE VAL TYR SER GLU VAL GLN GLY GLY ALA          
SEQRES   9 A  422  TRP LEU LEU SER PRO ARG LEU CYS ASP ALA LEU MET ALA          
SEQRES  10 A  422  MET ASP VAL MET LEU CYS THR ALA SER ILE PHE ASN LEU          
SEQRES  11 A  422  CYS ALA ILE SER VAL ASP ARG PHE VAL ALA VAL ALA VAL          
SEQRES  12 A  422  PRO LEU ARG TYR ASN ARG GLN GLY GLY SER ARG ARG GLN          
SEQRES  13 A  422  LEU LEU LEU ILE GLY ALA THR TRP LEU LEU SER ALA ALA          
SEQRES  14 A  422  VAL ALA ALA PRO VAL LEU CYS GLY LEU ASN ASP VAL ARG          
SEQRES  15 A  422  GLY ARG ASP PRO ALA VAL CYS ARG LEU GLU ASP ARG ASP          
SEQRES  16 A  422  TYR VAL VAL TYR SER SER VAL CYS SER PHE PHE LEU PRO          
SEQRES  17 A  422  CYS PRO LEU MET LEU LEU LEU TYR TRP ALA THR PHE ARG          
SEQRES  18 A  422  GLY LEU GLN ARG TRP GLU VAL ALA ARG ARG ALA ASP LEU          
SEQRES  19 A  422  GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS VAL          
SEQRES  20 A  422  ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP ALA          
SEQRES  21 A  422  LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN LYS          
SEQRES  22 A  422  ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SER          
SEQRES  23 A  422  PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE LEU          
SEQRES  24 A  422  VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN GLU          
SEQRES  25 A  422  GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN LEU          
SEQRES  26 A  422  LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU ALA          
SEQRES  27 A  422  LYS ILE THR GLY ARG GLU ARG LYS ALA MET ARG VAL LEU          
SEQRES  28 A  422  PRO VAL VAL VAL GLY ALA PHE LEU LEU CYS TRP THR PRO          
SEQRES  29 A  422  PHE PHE VAL VAL HIS ILE THR GLN ALA LEU CYS PRO ALA          
SEQRES  30 A  422  CYS SER VAL PRO PRO ARG LEU VAL SER ALA VAL THR TRP          
SEQRES  31 A  422  LEU GLY TYR VAL ASN SER ALA LEU ASN PRO VAL ILE TYR          
SEQRES  32 A  422  THR VAL PHE ASN ALA GLU PHE ARG ASN VAL PHE ARG LYS          
SEQRES  33 A  422  ALA LEU ARG ALA CYS CYS                                      
HET    AQD  A1201      27                                                       
HET    PO4  A1202       5                                                       
HET    PO4  A1203       5                                                       
HET    PO4  A1204       5                                                       
HET    OLA  A1205      17                                                       
HET    OLA  A1206      17                                                       
HET    OLA  A1207      17                                                       
HET    OLA  A1208      17                                                       
HET    OLA  A1209      20                                                       
HET    OLA  A1210      20                                                       
HET    OLA  A1211      16                                                       
HET    OLA  A1212      20                                                       
HET    OLA  A1213      20                                                       
HET    PEG  A1214       7                                                       
HET    PEG  A1215       7                                                       
HET    PEG  A1216       7                                                       
HET    PEG  A1217       7                                                       
HET    PEG  A1218       7                                                       
HET    PEG  A1219       7                                                       
HET    PEG  A1220       7                                                       
HET    PEG  A1221       7                                                       
HET    PEG  A1222       7                                                       
HET    GOL  A1223       6                                                       
HETNAM     AQD NEMONAPRIDE                                                      
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     OLA OLEIC ACID                                                       
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     GOL GLYCEROL                                                         
HETSYN     AQD N-[(2R,3R)-1-BENZYL-2-METHYLPYRROLIDIN-3-YL]-5-CHLORO-           
HETSYN   2 AQD  2-METHOXY-4-(METHYLAMINO)BENZAMIDE                              
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  AQD    C21 H26 CL N3 O2                                             
FORMUL   3  PO4    3(O4 P 3-)                                                   
FORMUL   6  OLA    9(C18 H34 O2)                                                
FORMUL  15  PEG    9(C4 H10 O3)                                                 
FORMUL  24  GOL    C3 H8 O3                                                     
FORMUL  25  HOH   *98(H2 O)                                                     
HELIX    1 AA1 GLY A   34  GLU A   62  1                                  29    
HELIX    2 AA2 ARG A   63  GLN A   66  5                                   4    
HELIX    3 AA3 THR A   67  VAL A   87  1                                  21    
HELIX    4 AA4 VAL A   87  GLN A   97  1                                  11    
HELIX    5 AA5 SER A  104  VAL A  139  1                                  36    
HELIX    6 AA6 ARG A  150  CYS A  172  1                                  23    
HELIX    7 AA7 ASP A  189  PHE A  201  1                                  13    
HELIX    8 AA8 LEU A  203  ARG A  221  1                                  19    
HELIX    9 AA9 ARG A  226  LYS A 1019  1                                  21    
HELIX   10 AB1 ASN A 1022  GLN A 1041  1                                  20    
HELIX   11 AB2 PRO A 1045  ASP A 1050  1                                   6    
HELIX   12 AB3 GLU A 1057  GLU A 1081  1                                  25    
HELIX   13 AB4 LYS A 1083  ILE A 1102  1                                  20    
HELIX   14 AB5 ILE A 1102  THR A  386  1                                   9    
HELIX   15 AB6 GLY A  387  MET A  393  1                                   7    
HELIX   16 AB7 ARG A  394  CYS A  420  1                                  27    
HELIX   17 AB8 PRO A  426  ASN A  452  1                                  27    
HELIX   18 AB9 ASN A  452  LYS A  461  1                                  10    
SSBOND   1 CYS A  108    CYS A  185                          1555   1555  2.05  
SSBOND   2 CYS A  420    CYS A  423                          1555   1555  2.06  
SITE     1 AC1 12 LEU A 111  ASP A 115  THR A 120  LEU A 187                    
SITE     2 AC1 12 VAL A 193  SER A 196  SER A 200  PHE A 410                    
SITE     3 AC1 12 PHE A 411  THR A 434  TYR A 438  HOH A1326                    
SITE     1 AC2  7 TYR A 143  GLY A 148  SER A 149  ARG A 151                    
SITE     2 AC2  7 GLN A 152  GOL A1223  HOH A1352                               
SITE     1 AC3  1 ARG A 390                                                     
SITE     1 AC4  2 LEU A  85  HOH A1379                                          
SITE     1 AC5  8 VAL A  59  THR A  67  ASN A  70  SER A  71                    
SITE     2 AC5  8 SER A  75  LEU A 153  TRP A 160  PEG A1221                    
SITE     1 AC6  5 LEU A  44  ALA A  47  GLU A  95  TRP A 435                    
SITE     2 AC6  5 OLA A1207                                                     
SITE     1 AC7  5 ARG A 428  SER A 431  ALA A 432  OLA A1206                    
SITE     2 AC7  5 HOH A1316                                                     
SITE     1 AC8  7 PHE A 124  ASP A 132  ARG A 151  LEU A 155                    
SITE     2 AC8  7 LEU A 162  TYR A 195  HOH A1367                               
SITE     1 AC9  4 LEU A  54  SER A  58  PRO A 445  THR A 449                    
SITE     1 AD1  4 LEU A 209  PHE A 216  GLN A 220  ARG A 390                    
SITE     1 AD2  5 PHE A 134  ALA A 138  ASP A 191  CYS A 199                    
SITE     2 AD2  5 HOH A1365                                                     
SITE     1 AD3  3 GLY A 401  ALA A 402  PHE A 451                               
SITE     1 AD4  4 PHE A 202  THR A 416  ARG A 428  GLU A1081                    
SITE     1 AD5  2 LEU A 429  HOH A1301                                          
SITE     1 AD6  1 MET A 114                                                     
SITE     1 AD7  1 SER A  53                                                     
SITE     1 AD8  3 TYR A  93  LEU A 103  SER A 104                               
SITE     1 AD9  3 SER A 104  ARG A 106  HOH A1369                               
SITE     1 AE1  1 OLA A1205                                                     
SITE     1 AE2  5 ARG A 133  ALA A 136  ARG A 151  PO4 A1202                    
SITE     2 AE2  5 HOH A1367                                                     
CRYST1   67.688  164.047   84.129  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014774  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006096  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011887        0.00000                         
ATOM      1  N   GLY A  34     -20.681  20.730 -35.850  1.00 70.19           N  
ANISOU    1  N   GLY A  34    10398   9128   7143    923   -145   2253       N  
ATOM      2  CA  GLY A  34     -21.957  20.459 -35.211  1.00 64.51           C  
ANISOU    2  CA  GLY A  34     9559   8423   6528    975   -331   2153       C  
ATOM      3  C   GLY A  34     -22.617  19.194 -35.727  1.00 58.62           C  
ANISOU    3  C   GLY A  34     8770   7851   5651   1028   -513   2029       C  
ATOM      4  O   GLY A  34     -23.111  18.385 -34.948  1.00 58.07           O  
ANISOU    4  O   GLY A  34     8551   7817   5696    979   -609   1879       O  
ATOM      5  N   ALA A  35     -22.630  19.026 -37.046  1.00 59.19           N  
ANISOU    5  N   ALA A  35     8982   8026   5479   1128   -562   2094       N  
ATOM      6  CA  ALA A  35     -23.227  17.847 -37.662  1.00 58.66           C  
ANISOU    6  CA  ALA A  35     8901   8118   5269   1183   -752   1971       C  
ATOM      7  C   ALA A  35     -22.484  16.575 -37.266  1.00 59.08           C  
ANISOU    7  C   ALA A  35     8878   8230   5340   1062   -712   1798       C  
ATOM      8  O   ALA A  35     -23.094  15.521 -37.079  1.00 60.48           O  
ANISOU    8  O   ALA A  35     8961   8480   5538   1048   -872   1646       O  
ATOM      9  CB  ALA A  35     -23.259  17.999 -39.183  1.00 61.35           C  
ANISOU    9  CB  ALA A  35     9438   8554   5318   1326   -798   2078       C  
ATOM     10  N   ALA A  36     -21.167  16.679 -37.115  1.00 57.82           N  
ANISOU   10  N   ALA A  36     8753   8030   5185    973   -499   1823       N  
ATOM     11  CA  ALA A  36     -20.349  15.533 -36.742  1.00 54.09           C  
ANISOU   11  CA  ALA A  36     8215   7608   4730    871   -445   1671       C  
ATOM     12  C   ALA A  36     -20.617  15.112 -35.308  1.00 54.30           C  
ANISOU   12  C   ALA A  36     8055   7571   5004    761   -481   1542       C  
ATOM     13  O   ALA A  36     -20.604  13.924 -34.987  1.00 59.26           O  
ANISOU   13  O   ALA A  36     8608   8255   5653    711   -550   1387       O  
ATOM     14  CB  ALA A  36     -18.879  15.850 -36.935  1.00 55.56           C  
ANISOU   14  CB  ALA A  36     8464   7773   4874    811   -204   1746       C  
ATOM     15  N   ALA A  37     -20.859  16.084 -34.437  1.00 54.36           N  
ANISOU   15  N   ALA A  37     8001   7457   5196    730   -431   1608       N  
ATOM     16  CA  ALA A  37     -21.179  15.783 -33.044  1.00 54.38           C  
ANISOU   16  CA  ALA A  37     7840   7403   5420    644   -457   1499       C  
ATOM     17  C   ALA A  37     -22.522  15.075 -32.978  1.00 51.99           C  
ANISOU   17  C   ALA A  37     7447   7170   5137    693   -669   1412       C  
ATOM     18  O   ALA A  37     -22.714  14.122 -32.222  1.00 50.91           O  
ANISOU   18  O   ALA A  37     7191   7054   5099    621   -724   1280       O  
ATOM     19  CB  ALA A  37     -21.205  17.057 -32.212  1.00 54.24           C  
ANISOU   19  CB  ALA A  37     7798   7238   5570    624   -366   1587       C  
ATOM     20  N   LEU A  38     -23.450  15.556 -33.792  1.00 52.31           N  
ANISOU   20  N   LEU A  38     7544   7244   5085    816   -791   1496       N  
ATOM     21  CA  LEU A  38     -24.785  14.983 -33.853  1.00 52.81           C  
ANISOU   21  CA  LEU A  38     7512   7381   5172    869  -1007   1429       C  
ATOM     22  C   LEU A  38     -24.756  13.558 -34.393  1.00 51.54           C  
ANISOU   22  C   LEU A  38     7353   7332   4900    842  -1126   1291       C  
ATOM     23  O   LEU A  38     -25.307  12.650 -33.778  1.00 51.61           O  
ANISOU   23  O   LEU A  38     7226   7362   5022    779  -1227   1171       O  
ATOM     24  CB  LEU A  38     -25.692  15.859 -34.709  1.00 52.36           C  
ANISOU   24  CB  LEU A  38     7526   7344   5024   1020  -1117   1556       C  
ATOM     25  CG  LEU A  38     -27.107  15.326 -34.925  1.00 53.50           C  
ANISOU   25  CG  LEU A  38     7562   7579   5187   1086  -1361   1496       C  
ATOM     26  CD1 LEU A  38     -27.740  14.903 -33.602  1.00 53.67           C  
ANISOU   26  CD1 LEU A  38     7368   7574   5451   1002  -1386   1403       C  
ATOM     27  CD2 LEU A  38     -27.940  16.395 -35.595  1.00 54.69           C  
ANISOU   27  CD2 LEU A  38     7773   7731   5277   1246  -1450   1639       C  
ATOM     28  N   VAL A  39     -24.111  13.363 -35.539  1.00 53.35           N  
ANISOU   28  N   VAL A  39     7742   7625   4905    892  -1108   1310       N  
ATOM     29  CA  VAL A  39     -24.027  12.037 -36.147  1.00 51.74           C  
ANISOU   29  CA  VAL A  39     7571   7518   4571    886  -1222   1170       C  
ATOM     30  C   VAL A  39     -23.284  11.055 -35.250  1.00 52.50           C  
ANISOU   30  C   VAL A  39     7582   7584   4781    753  -1140   1037       C  
ATOM     31  O   VAL A  39     -23.807   9.991 -34.900  1.00 53.81           O  
ANISOU   31  O   VAL A  39     7653   7770   5022    699  -1274    903       O  
ATOM     32  CB  VAL A  39     -23.340  12.098 -37.523  1.00 55.63           C  
ANISOU   32  CB  VAL A  39     8271   8086   4781    982  -1182   1223       C  
ATOM     33  CG1 VAL A  39     -23.012  10.698 -38.015  1.00 57.00           C  
ANISOU   33  CG1 VAL A  39     8491   8340   4827    969  -1263   1058       C  
ATOM     34  CG2 VAL A  39     -24.232  12.811 -38.518  1.00 54.49           C  
ANISOU   34  CG2 VAL A  39     8222   7991   4491   1130  -1319   1333       C  
ATOM     35  N   GLY A  40     -22.069  11.417 -34.859  1.00 51.86           N  
ANISOU   35  N   GLY A  40     7529   7450   4725    696   -924   1077       N  
ATOM     36  CA  GLY A  40     -21.281  10.581 -33.966  1.00 49.15           C  
ANISOU   36  CA  GLY A  40     7106   7077   4492    582   -839    962       C  
ATOM     37  C   GLY A  40     -21.989  10.324 -32.649  1.00 47.20           C  
ANISOU   37  C   GLY A  40     6687   6771   4477    500   -896    900       C  
ATOM     38  O   GLY A  40     -21.926   9.220 -32.107  1.00 47.26           O  
ANISOU   38  O   GLY A  40     6624   6780   4553    428   -938    775       O  
ATOM     39  N   GLY A  41     -22.670  11.347 -32.142  1.00 44.35           N  
ANISOU   39  N   GLY A  41     6266   6354   4232    519   -891    993       N  
ATOM     40  CA  GLY A  41     -23.358  11.248 -30.871  1.00 45.41           C  
ANISOU   40  CA  GLY A  41     6239   6437   4576    459   -919    953       C  
ATOM     41  C   GLY A  41     -24.517  10.275 -30.917  1.00 44.68           C  
ANISOU   41  C   GLY A  41     6051   6404   4523    456  -1117    866       C  
ATOM     42  O   GLY A  41     -24.666   9.428 -30.041  1.00 45.52           O  
ANISOU   42  O   GLY A  41     6047   6493   4754    369  -1136    776       O  
ATOM     43  N   VAL A  42     -25.339  10.394 -31.952  1.00 46.61           N  
ANISOU   43  N   VAL A  42     6337   6715   4660    548  -1272    898       N  
ATOM     44  CA  VAL A  42     -26.482   9.507 -32.107  1.00 46.29           C  
ANISOU   44  CA  VAL A  42     6196   6731   4662    540  -1484    816       C  
ATOM     45  C   VAL A  42     -26.003   8.071 -32.266  1.00 46.17           C  
ANISOU   45  C   VAL A  42     6208   6736   4601    463  -1537    671       C  
ATOM     46  O   VAL A  42     -26.536   7.151 -31.638  1.00 47.79           O  
ANISOU   46  O   VAL A  42     6288   6928   4941    379  -1620    584       O  
ATOM     47  CB  VAL A  42     -27.361   9.933 -33.311  1.00 49.44           C  
ANISOU   47  CB  VAL A  42     6650   7205   4929    666  -1657    873       C  
ATOM     48  CG1 VAL A  42     -28.311   8.834 -33.704  1.00 51.10           C  
ANISOU   48  CG1 VAL A  42     6783   7481   5150    645  -1896    762       C  
ATOM     49  CG2 VAL A  42     -28.123  11.205 -32.984  1.00 49.70           C  
ANISOU   49  CG2 VAL A  42     6616   7210   5056    743  -1641   1003       C  
ATOM     50  N   LEU A  43     -24.971   7.876 -33.078  1.00 47.83           N  
ANISOU   50  N   LEU A  43     6580   6970   4623    495  -1476    650       N  
ATOM     51  CA  LEU A  43     -24.416   6.541 -33.268  1.00 44.26           C  
ANISOU   51  CA  LEU A  43     6174   6529   4114    444  -1514    508       C  
ATOM     52  C   LEU A  43     -23.861   6.000 -31.961  1.00 46.14           C  
ANISOU   52  C   LEU A  43     6314   6692   4524    327  -1396    453       C  
ATOM     53  O   LEU A  43     -24.075   4.829 -31.620  1.00 45.92           O  
ANISOU   53  O   LEU A  43     6233   6645   4570    255  -1485    340       O  
ATOM     54  CB  LEU A  43     -23.325   6.553 -34.334  1.00 45.41           C  
ANISOU   54  CB  LEU A  43     6511   6722   4022    519  -1433    508       C  
ATOM     55  CG  LEU A  43     -23.840   6.689 -35.762  1.00 47.94           C  
ANISOU   55  CG  LEU A  43     6961   7129   4123    642  -1584    523       C  
ATOM     56  CD1 LEU A  43     -22.671   6.753 -36.731  1.00 52.33           C  
ANISOU   56  CD1 LEU A  43     7708   7737   4437    723  -1459    540       C  
ATOM     57  CD2 LEU A  43     -24.773   5.542 -36.125  1.00 49.57           C  
ANISOU   57  CD2 LEU A  43     7139   7365   4330    628  -1842    381       C  
ATOM     58  N   LEU A  44     -23.166   6.856 -31.217  1.00 40.84           N  
ANISOU   58  N   LEU A  44     5625   5973   3921    308  -1205    534       N  
ATOM     59  CA  LEU A  44     -22.591   6.429 -29.955  1.00 40.84           C  
ANISOU   59  CA  LEU A  44     5541   5908   4068    211  -1095    487       C  
ATOM     60  C   LEU A  44     -23.676   5.980 -28.982  1.00 42.17           C  
ANISOU   60  C   LEU A  44     5552   6047   4425    144  -1185    458       C  
ATOM     61  O   LEU A  44     -23.582   4.898 -28.400  1.00 42.12           O  
ANISOU   61  O   LEU A  44     5498   6011   4495     68  -1209    369       O  
ATOM     62  CB  LEU A  44     -21.763   7.546 -29.336  1.00 41.25           C  
ANISOU   62  CB  LEU A  44     5596   5911   4164    205   -900    577       C  
ATOM     63  CG  LEU A  44     -21.182   7.208 -27.969  1.00 40.48           C  
ANISOU   63  CG  LEU A  44     5415   5752   4213    115   -797    530       C  
ATOM     64  CD1 LEU A  44     -20.236   6.042 -28.083  1.00 42.98           C  
ANISOU   64  CD1 LEU A  44     5777   6080   4472     83   -779    424       C  
ATOM     65  CD2 LEU A  44     -20.490   8.427 -27.369  1.00 40.48           C  
ANISOU   65  CD2 LEU A  44     5416   5697   4266    109   -633    614       C  
ATOM     66  N   ILE A  45     -24.705   6.808 -28.810  1.00 40.02           N  
ANISOU   66  N   ILE A  45     5197   5780   4228    179  -1228    541       N  
ATOM     67  CA  ILE A  45     -25.791   6.497 -27.882  1.00 39.43           C  
ANISOU   67  CA  ILE A  45     4954   5691   4337    126  -1291    533       C  
ATOM     68  C   ILE A  45     -26.496   5.195 -28.290  1.00 39.81           C  
ANISOU   68  C   ILE A  45     4956   5767   4403     75  -1479    437       C  
ATOM     69  O   ILE A  45     -26.757   4.324 -27.453  1.00 40.14           O  
ANISOU   69  O   ILE A  45     4899   5772   4580    -18  -1491    387       O  
ATOM     70  CB  ILE A  45     -26.800   7.677 -27.809  1.00 40.81           C  
ANISOU   70  CB  ILE A  45     5051   5882   4573    201  -1310    642       C  
ATOM     71  CG1 ILE A  45     -26.142   8.869 -27.085  1.00 39.89           C  
ANISOU   71  CG1 ILE A  45     4965   5704   4488    227  -1120    720       C  
ATOM     72  CG2 ILE A  45     -28.076   7.239 -27.091  1.00 43.38           C  
ANISOU   72  CG2 ILE A  45     5187   6221   5075    158  -1399    634       C  
ATOM     73  CD1 ILE A  45     -26.943  10.194 -27.125  1.00 41.32           C  
ANISOU   73  CD1 ILE A  45     5115   5881   4705    327  -1121    832       C  
ATOM     74  N   GLY A  46     -26.768   5.055 -29.583  1.00 42.49           N  
ANISOU   74  N   GLY A  46     5379   6163   4601    135  -1626    412       N  
ATOM     75  CA  GLY A  46     -27.353   3.831 -30.106  1.00 41.72           C  
ANISOU   75  CA  GLY A  46     5264   6082   4506     89  -1825    303       C  
ATOM     76  C   GLY A  46     -26.508   2.602 -29.804  1.00 43.08           C  
ANISOU   76  C   GLY A  46     5493   6196   4680      7  -1792    190       C  
ATOM     77  O   GLY A  46     -27.010   1.570 -29.344  1.00 43.72           O  
ANISOU   77  O   GLY A  46     5486   6234   4890    -89  -1882    122       O  
ATOM     78  N   ALA A  47     -25.208   2.706 -30.050  1.00 43.13           N  
ANISOU   78  N   ALA A  47     5642   6197   4550     47  -1658    176       N  
ATOM     79  CA  ALA A  47     -24.316   1.566 -29.847  1.00 42.28           C  
ANISOU   79  CA  ALA A  47     5599   6039   4427     -4  -1624     67       C  
ATOM     80  C   ALA A  47     -24.219   1.184 -28.375  1.00 41.79           C  
ANISOU   80  C   ALA A  47     5420   5902   4558   -104  -1527     72       C  
ATOM     81  O   ALA A  47     -24.179  -0.003 -28.035  1.00 43.23           O  
ANISOU   81  O   ALA A  47     5594   6026   4807   -175  -1581    -15       O  
ATOM     82  CB  ALA A  47     -22.928   1.867 -30.407  1.00 45.17           C  
ANISOU   82  CB  ALA A  47     6119   6431   4614     72  -1483     64       C  
ATOM     83  N   VAL A  48     -24.174   2.179 -27.496  1.00 39.57           N  
ANISOU   83  N   VAL A  48     5062   5614   4358   -103  -1386    173       N  
ATOM     84  CA  VAL A  48     -24.081   1.884 -26.076  1.00 40.39           C  
ANISOU   84  CA  VAL A  48     5068   5657   4620   -182  -1290    183       C  
ATOM     85  C   VAL A  48     -25.354   1.184 -25.604  1.00 42.36           C  
ANISOU   85  C   VAL A  48     5179   5885   5029   -261  -1409    176       C  
ATOM     86  O   VAL A  48     -25.285   0.184 -24.884  1.00 39.72           O  
ANISOU   86  O   VAL A  48     4812   5490   4790   -342  -1407    131       O  
ATOM     87  CB  VAL A  48     -23.852   3.142 -25.222  1.00 38.44           C  
ANISOU   87  CB  VAL A  48     4775   5407   4424   -156  -1128    282       C  
ATOM     88  CG1 VAL A  48     -23.920   2.780 -23.740  1.00 39.63           C  
ANISOU   88  CG1 VAL A  48     4828   5505   4726   -227  -1049    288       C  
ATOM     89  CG2 VAL A  48     -22.499   3.771 -25.543  1.00 37.57           C  
ANISOU   89  CG2 VAL A  48     4783   5302   4191   -106   -997    292       C  
ATOM     90  N   LEU A  49     -26.506   1.715 -26.013  1.00 41.57           N  
ANISOU   90  N   LEU A  49     4993   5836   4964   -237  -1512    227       N  
ATOM     91  CA  LEU A  49     -27.776   1.183 -25.548  1.00 39.98           C  
ANISOU   91  CA  LEU A  49     4627   5629   4937   -315  -1614    238       C  
ATOM     92  C   LEU A  49     -27.949  -0.240 -26.053  1.00 40.36           C  
ANISOU   92  C   LEU A  49     4701   5634   4998   -394  -1778    127       C  
ATOM     93  O   LEU A  49     -28.269  -1.140 -25.286  1.00 42.80           O  
ANISOU   93  O   LEU A  49     4928   5881   5454   -499  -1786    112       O  
ATOM     94  CB  LEU A  49     -28.957   2.071 -25.994  1.00 39.37           C  
ANISOU   94  CB  LEU A  49     4443   5626   4890   -256  -1704    312       C  
ATOM     95  CG  LEU A  49     -29.073   3.438 -25.309  1.00 43.37           C  
ANISOU   95  CG  LEU A  49     4893   6155   5432   -183  -1553    426       C  
ATOM     96  CD1 LEU A  49     -30.158   4.301 -25.952  1.00 45.00           C  
ANISOU   96  CD1 LEU A  49     5020   6434   5643    -98  -1660    493       C  
ATOM     97  CD2 LEU A  49     -29.304   3.305 -23.804  1.00 40.46           C  
ANISOU   97  CD2 LEU A  49     4396   5749   5226   -245  -1423    467       C  
ATOM     98  N   ALA A  50     -27.719  -0.455 -27.343  1.00 43.32           N  
ANISOU   98  N   ALA A  50     5206   6036   5218   -342  -1906     50       N  
ATOM     99  CA  ALA A  50     -27.942  -1.779 -27.917  1.00 45.08           C  
ANISOU   99  CA  ALA A  50     5471   6210   5447   -408  -2087    -73       C  
ATOM    100  C   ALA A  50     -26.987  -2.820 -27.365  1.00 45.15           C  
ANISOU  100  C   ALA A  50     5563   6121   5471   -464  -2010   -146       C  
ATOM    101  O   ALA A  50     -27.407  -3.920 -26.993  1.00 45.77           O  
ANISOU  101  O   ALA A  50     5591   6116   5684   -572  -2096   -196       O  
ATOM    102  CB  ALA A  50     -27.830  -1.730 -29.432  1.00 46.64           C  
ANISOU  102  CB  ALA A  50     5815   6465   5441   -315  -2234   -148       C  
ATOM    103  N   GLY A  51     -25.700  -2.484 -27.343  1.00 44.24           N  
ANISOU  103  N   GLY A  51     5574   6012   5223   -390  -1855   -150       N  
ATOM    104  CA  GLY A  51     -24.677  -3.420 -26.914  1.00 42.03           C  
ANISOU  104  CA  GLY A  51     5382   5650   4935   -414  -1784   -222       C  
ATOM    105  C   GLY A  51     -24.865  -3.827 -25.468  1.00 43.62           C  
ANISOU  105  C   GLY A  51     5468   5778   5328   -513  -1698   -170       C  
ATOM    106  O   GLY A  51     -24.885  -5.009 -25.145  1.00 44.82           O  
ANISOU  106  O   GLY A  51     5633   5834   5564   -588  -1754   -230       O  
ATOM    107  N   ASN A  52     -25.022  -2.848 -24.587  1.00 39.71           N  
ANISOU  107  N   ASN A  52     4870   5320   4896   -506  -1561    -56       N  
ATOM    108  CA  ASN A  52     -25.158  -3.163 -23.174  1.00 38.02           C  
ANISOU  108  CA  ASN A  52     4560   5049   4836   -581  -1462      1       C  
ATOM    109  C   ASN A  52     -26.488  -3.800 -22.785  1.00 39.72           C  
ANISOU  109  C   ASN A  52     4629   5228   5234   -692  -1561     32       C  
ATOM    110  O   ASN A  52     -26.551  -4.543 -21.806  1.00 41.22           O  
ANISOU  110  O   ASN A  52     4775   5343   5542   -770  -1512     55       O  
ATOM    111  CB  ASN A  52     -24.919  -1.918 -22.352  1.00 37.09           C  
ANISOU  111  CB  ASN A  52     4390   4982   4719   -530  -1290    100       C  
ATOM    112  CG  ASN A  52     -23.470  -1.519 -22.380  1.00 38.12           C  
ANISOU  112  CG  ASN A  52     4644   5121   4720   -457  -1170     73       C  
ATOM    113  OD1 ASN A  52     -22.654  -2.123 -21.688  1.00 40.15           O  
ANISOU  113  OD1 ASN A  52     4943   5324   4988   -473  -1100     44       O  
ATOM    114  ND2 ASN A  52     -23.125  -0.561 -23.227  1.00 38.07           N  
ANISOU  114  ND2 ASN A  52     4695   5178   4591   -377  -1153     84       N  
ATOM    115  N   SER A  53     -27.559  -3.509 -23.511  1.00 42.83           N  
ANISOU  115  N   SER A  53     4938   5676   5659   -699  -1698     42       N  
ATOM    116  CA ASER A  53     -28.824  -4.180 -23.240  0.49 44.42           C  
ANISOU  116  CA ASER A  53     4981   5845   6050   -817  -1807     66       C  
ATOM    117  CA BSER A  53     -28.816  -4.184 -23.211  0.51 44.60           C  
ANISOU  117  CA BSER A  53     5004   5867   6075   -818  -1803     68       C  
ATOM    118  C   SER A  53     -28.696  -5.650 -23.603  1.00 46.87           C  
ANISOU  118  C   SER A  53     5372   6042   6396   -907  -1944    -43       C  
ATOM    119  O   SER A  53     -29.193  -6.525 -22.895  1.00 47.44           O  
ANISOU  119  O   SER A  53     5360   6029   6637  -1027  -1956    -19       O  
ATOM    120  CB ASER A  53     -29.972  -3.532 -24.014  0.49 44.60           C  
ANISOU  120  CB ASER A  53     4889   5961   6098   -796  -1944     93       C  
ATOM    121  CB BSER A  53     -30.004  -3.526 -23.921  0.51 44.48           C  
ANISOU  121  CB BSER A  53     4863   5945   6094   -800  -1935    100       C  
ATOM    122  OG ASER A  53     -30.189  -2.205 -23.567  0.49 43.14           O  
ANISOU  122  OG ASER A  53     4622   5863   5906   -712  -1814    201       O  
ATOM    123  OG BSER A  53     -29.965  -3.720 -25.320  0.51 47.94           O  
ANISOU  123  OG BSER A  53     5408   6402   6406   -761  -2121     -3       O  
ATOM    124  N   LEU A  54     -28.019  -5.915 -24.718  1.00 49.85           N  
ANISOU  124  N   LEU A  54     5920   6413   6609   -843  -2043   -162       N  
ATOM    125  CA  LEU A  54     -27.860  -7.287 -25.203  1.00 50.60           C  
ANISOU  125  CA  LEU A  54     6120   6391   6716   -906  -2190   -290       C  
ATOM    126  C   LEU A  54     -27.040  -8.113 -24.219  1.00 48.85           C  
ANISOU  126  C   LEU A  54     5962   6054   6546   -945  -2067   -291       C  
ATOM    127  O   LEU A  54     -27.245  -9.317 -24.096  1.00 50.20           O  
ANISOU  127  O   LEU A  54     6154   6096   6826  -1043  -2162   -345       O  
ATOM    128  CB  LEU A  54     -27.209  -7.311 -26.595  1.00 50.17           C  
ANISOU  128  CB  LEU A  54     6255   6369   6441   -797  -2297   -420       C  
ATOM    129  CG  LEU A  54     -28.106  -7.063 -27.808  1.00 51.87           C  
ANISOU  129  CG  LEU A  54     6452   6654   6602   -777  -2510   -470       C  
ATOM    130  CD1 LEU A  54     -27.286  -6.537 -28.979  1.00 54.80           C  
ANISOU  130  CD1 LEU A  54     7009   7110   6705   -620  -2516   -536       C  
ATOM    131  CD2 LEU A  54     -28.853  -8.333 -28.212  1.00 54.77           C  
ANISOU  131  CD2 LEU A  54     6811   6913   7085   -892  -2731   -578       C  
ATOM    132  N   VAL A  55     -26.114  -7.462 -23.530  1.00 45.79           N  
ANISOU  132  N   VAL A  55     5608   5707   6083   -866  -1867   -232       N  
ATOM    133  CA  VAL A  55     -25.349  -8.098 -22.465  1.00 46.82           C  
ANISOU  133  CA  VAL A  55     5784   5748   6260   -887  -1742   -214       C  
ATOM    134  C   VAL A  55     -26.233  -8.410 -21.265  1.00 48.87           C  
ANISOU  134  C   VAL A  55     5890   5956   6723  -1007  -1692   -100       C  
ATOM    135  O   VAL A  55     -26.201  -9.524 -20.739  1.00 48.53           O  
ANISOU  135  O   VAL A  55     5874   5786   6781  -1087  -1707   -107       O  
ATOM    136  CB  VAL A  55     -24.159  -7.205 -22.018  1.00 46.99           C  
ANISOU  136  CB  VAL A  55     5862   5840   6152   -773  -1552   -179       C  
ATOM    137  CG1 VAL A  55     -23.599  -7.649 -20.665  1.00 46.78           C  
ANISOU  137  CG1 VAL A  55     5837   5744   6194   -795  -1417   -127       C  
ATOM    138  CG2 VAL A  55     -23.073  -7.205 -23.084  1.00 45.24           C  
ANISOU  138  CG2 VAL A  55     5804   5645   5741   -664  -1574   -290       C  
ATOM    139  N   CYS A  56     -27.037  -7.434 -20.847  1.00 48.34           N  
ANISOU  139  N   CYS A  56     5665   5986   6717  -1012  -1628      9       N  
ATOM    140  CA  CYS A  56     -27.894  -7.601 -19.671  1.00 50.44           C  
ANISOU  140  CA  CYS A  56     5772   6229   7163  -1107  -1549    132       C  
ATOM    141  C   CYS A  56     -28.908  -8.716 -19.875  1.00 47.88           C  
ANISOU  141  C   CYS A  56     5365   5808   7017  -1258  -1703    121       C  
ATOM    142  O   CYS A  56     -29.114  -9.553 -19.000  1.00 50.67           O  
ANISOU  142  O   CYS A  56     5684   6063   7505  -1356  -1655    180       O  
ATOM    143  CB  CYS A  56     -28.625  -6.299 -19.338  1.00 50.13           C  
ANISOU  143  CB  CYS A  56     5579   6321   7147  -1063  -1463    237       C  
ATOM    144  SG  CYS A  56     -27.578  -5.077 -18.517  1.00 51.04           S  
ANISOU  144  SG  CYS A  56     5759   6510   7124   -926  -1242    287       S  
ATOM    145  N   VAL A  57     -29.539  -8.719 -21.037  1.00 52.85           N  
ANISOU  145  N   VAL A  57     5967   6466   7650  -1278  -1893     47       N  
ATOM    146  CA  VAL A  57     -30.548  -9.716 -21.347  1.00 53.45           C  
ANISOU  146  CA  VAL A  57     5952   6451   7905  -1431  -2072     21       C  
ATOM    147  C   VAL A  57     -29.909 -11.094 -21.507  1.00 57.24           C  
ANISOU  147  C   VAL A  57     6602   6755   8393  -1488  -2154    -84       C  
ATOM    148  O   VAL A  57     -30.515 -12.106 -21.155  1.00 57.18           O  
ANISOU  148  O   VAL A  57     6533   6619   8574  -1638  -2219    -63       O  
ATOM    149  CB  VAL A  57     -31.332  -9.327 -22.616  1.00 54.69           C  
ANISOU  149  CB  VAL A  57     6049   6689   8041  -1421  -2280    -48       C  
ATOM    150  CG1 VAL A  57     -32.347 -10.393 -22.988  1.00 57.95           C  
ANISOU  150  CG1 VAL A  57     6389   7012   8617  -1552  -2433    -94       C  
ATOM    151  CG2 VAL A  57     -32.042  -7.994 -22.399  1.00 55.52           C  
ANISOU  151  CG2 VAL A  57     5977   6957   8160  -1359  -2199     67       C  
ATOM    152  N   SER A  58     -28.680 -11.138 -22.013  1.00 54.97           N  
ANISOU  152  N   SER A  58     6523   6453   7908  -1367  -2144   -191       N  
ATOM    153  CA ASER A  58     -28.018 -12.417 -22.217  0.80 53.84           C  
ANISOU  153  CA ASER A  58     6554   6143   7758  -1393  -2222   -303       C  
ATOM    154  CA BSER A  58     -27.976 -12.401 -22.215  0.20 53.10           C  
ANISOU  154  CA BSER A  58     6465   6052   7658  -1388  -2218   -303       C  
ATOM    155  C   SER A  58     -27.681 -13.073 -20.886  1.00 55.10           C  
ANISOU  155  C   SER A  58     6720   6191   8025  -1448  -2074   -208       C  
ATOM    156  O   SER A  58     -27.868 -14.285 -20.732  1.00 57.59           O  
ANISOU  156  O   SER A  58     7078   6334   8470  -1557  -2157   -233       O  
ATOM    157  CB ASER A  58     -26.766 -12.260 -23.075  0.80 50.37           C  
ANISOU  157  CB ASER A  58     6324   5737   7077  -1232  -2227   -434       C  
ATOM    158  CB BSER A  58     -26.672 -12.187 -22.988  0.20 49.88           C  
ANISOU  158  CB BSER A  58     6264   5683   7007  -1221  -2204   -425       C  
ATOM    159  OG ASER A  58     -27.114 -12.006 -24.427  0.80 50.28           O  
ANISOU  159  OG ASER A  58     6348   5790   6966  -1192  -2405   -542       O  
ATOM    160  OG BSER A  58     -25.733 -11.447 -22.223  0.20 49.07           O  
ANISOU  160  OG BSER A  58     6182   5657   6806  -1118  -1986   -350       O  
ATOM    161  N   VAL A  59     -27.218 -12.289 -19.919  1.00 53.22           N  
ANISOU  161  N   VAL A  59     6446   6042   7735  -1375  -1863    -97       N  
ATOM    162  CA  VAL A  59     -26.944 -12.855 -18.602  1.00 54.83           C  
ANISOU  162  CA  VAL A  59     6656   6154   8022  -1416  -1721      5       C  
ATOM    163  C   VAL A  59     -28.283 -13.291 -17.988  1.00 59.12           C  
ANISOU  163  C   VAL A  59     7018   6642   8801  -1588  -1733    127       C  
ATOM    164  O   VAL A  59     -28.347 -14.261 -17.231  1.00 59.41           O  
ANISOU  164  O   VAL A  59     7074   6537   8960  -1679  -1699    189       O  
ATOM    165  CB  VAL A  59     -26.201 -11.867 -17.678  1.00 52.16           C  
ANISOU  165  CB  VAL A  59     6318   5932   7571  -1297  -1507     89       C  
ATOM    166  CG1 VAL A  59     -26.010 -12.455 -16.284  1.00 50.01           C  
ANISOU  166  CG1 VAL A  59     6053   5573   7375  -1332  -1370    202       C  
ATOM    167  CG2 VAL A  59     -24.841 -11.492 -18.272  1.00 52.26           C  
ANISOU  167  CG2 VAL A  59     6490   5992   7375  -1143  -1490    -24       C  
ATOM    168  N   ALA A  60     -29.358 -12.604 -18.364  1.00 59.68           N  
ANISOU  168  N   ALA A  60     6910   6823   8942  -1632  -1787    163       N  
ATOM    169  CA  ALA A  60     -30.703 -12.958 -17.906  1.00 59.60           C  
ANISOU  169  CA  ALA A  60     6693   6782   9169  -1799  -1807    277       C  
ATOM    170  C   ALA A  60     -31.240 -14.256 -18.520  1.00 63.85           C  
ANISOU  170  C   ALA A  60     7254   7157   9849  -1937  -1995    197       C  
ATOM    171  O   ALA A  60     -31.827 -15.081 -17.823  1.00 65.82           O  
ANISOU  171  O   ALA A  60     7440   7307  10262  -2050  -1937    288       O  
ATOM    172  CB  ALA A  60     -31.666 -11.815 -18.201  1.00 60.49           C  
ANISOU  172  CB  ALA A  60     6603   7072   9307  -1780  -1816    327       C  
ATOM    173  N   THR A  61     -31.063 -14.424 -19.827  1.00 59.97           N  
ANISOU  173  N   THR A  61     6874   6659   9253  -1884  -2173     26       N  
ATOM    174  CA  THR A  61     -31.642 -15.551 -20.532  1.00 64.39           C  
ANISOU  174  CA  THR A  61     7469   7098   9897  -1962  -2323    -68       C  
ATOM    175  C   THR A  61     -30.835 -16.851 -20.352  1.00 66.88           C  
ANISOU  175  C   THR A  61     7987   7203  10220  -1984  -2341   -132       C  
ATOM    176  O   THR A  61     -31.415 -17.933 -20.326  1.00 69.61           O  
ANISOU  176  O   THR A  61     8326   7413  10710  -2094  -2397   -136       O  
ATOM    177  CB  THR A  61     -31.789 -15.253 -22.054  1.00 65.87           C  
ANISOU  177  CB  THR A  61     7710   7364   9953  -1884  -2509   -231       C  
ATOM    178  OG1 THR A  61     -30.524 -14.886 -22.606  1.00 66.69           O  
ANISOU  178  OG1 THR A  61     8012   7495   9831  -1737  -2524   -339       O  
ATOM    179  CG2 THR A  61     -32.763 -14.116 -22.308  1.00 64.54           C  
ANISOU  179  CG2 THR A  61     7337   7382   9802  -1869  -2517   -168       C  
ATOM    180  N   GLU A  62     -29.514 -16.750 -20.207  1.00 63.95           N  
ANISOU  180  N   GLU A  62     7795   6804   9700  -1877  -2294   -180       N  
ATOM    181  CA  GLU A  62     -28.647 -17.933 -20.296  1.00 61.06           C  
ANISOU  181  CA  GLU A  62     7648   6248   9304  -1854  -2339   -277       C  
ATOM    182  C   GLU A  62     -28.028 -18.390 -18.970  1.00 60.11           C  
ANISOU  182  C   GLU A  62     7583   6009   9246  -1880  -2191   -158       C  
ATOM    183  O   GLU A  62     -27.342 -17.629 -18.293  1.00 59.48           O  
ANISOU  183  O   GLU A  62     7508   6022   9070  -1793  -2045    -86       O  
ATOM    184  CB  GLU A  62     -27.529 -17.668 -21.306  1.00 57.93           C  
ANISOU  184  CB  GLU A  62     7445   5893   8673  -1688  -2414   -452       C  
ATOM    185  N   ARG A  63     -28.245 -19.655 -18.619  1.00 59.02           N  
ANISOU  185  N   ARG A  63     7499   5683   9242  -1968  -2205   -135       N  
ATOM    186  CA  ARG A  63     -27.758 -20.191 -17.348  1.00 58.04           C  
ANISOU  186  CA  ARG A  63     7435   5433   9183  -1992  -2066     -5       C  
ATOM    187  C   ARG A  63     -26.231 -20.255 -17.313  1.00 58.93           C  
ANISOU  187  C   ARG A  63     7771   5489   9131  -1842  -2054    -92       C  
ATOM    188  O   ARG A  63     -25.616 -20.083 -16.255  1.00 59.43           O  
ANISOU  188  O   ARG A  63     7860   5583   9138  -1765  -1873     22       O  
ATOM    189  CB  ARG A  63     -28.356 -21.581 -17.087  1.00 59.99           C  
ANISOU  189  CB  ARG A  63     7703   5483   9607  -2117  -2095     33       C  
ATOM    190  N   ALA A  64     -25.621 -20.471 -18.476  1.00 57.29           N  
ANISOU  190  N   ALA A  64     7712   5268   8788  -1735  -2188   -291       N  
ATOM    191  CA  ALA A  64     -24.165 -20.552 -18.569  1.00 58.40           C  
ANISOU  191  CA  ALA A  64     8049   5399   8741  -1547  -2146   -388       C  
ATOM    192  C   ALA A  64     -23.473 -19.204 -18.345  1.00 57.25           C  
ANISOU  192  C   ALA A  64     7847   5502   8403  -1391  -1979   -350       C  
ATOM    193  O   ALA A  64     -22.267 -19.161 -18.137  1.00 55.62           O  
ANISOU  193  O   ALA A  64     7756   5321   8055  -1235  -1893   -385       O  
ATOM    194  CB  ALA A  64     -23.758 -21.124 -19.918  1.00 58.35           C  
ANISOU  194  CB  ALA A  64     8209   5323   8638  -1470  -2324   -610       C  
ATOM    195  N   LEU A  65     -24.219 -18.104 -18.398  1.00 55.69           N  
ANISOU  195  N   LEU A  65     7470   5481   8207  -1431  -1940   -282       N  
ATOM    196  CA  LEU A  65     -23.612 -16.790 -18.147  1.00 52.20           C  
ANISOU  196  CA  LEU A  65     6977   5256   7602  -1296  -1784   -241       C  
ATOM    197  C   LEU A  65     -23.880 -16.307 -16.728  1.00 52.72           C  
ANISOU  197  C   LEU A  65     6920   5380   7730  -1328  -1599    -50       C  
ATOM    198  O   LEU A  65     -23.402 -15.245 -16.325  1.00 52.60           O  
ANISOU  198  O   LEU A  65     6863   5524   7597  -1226  -1465     -6       O  
ATOM    199  CB  LEU A  65     -24.112 -15.752 -19.144  1.00 50.26           C  
ANISOU  199  CB  LEU A  65     6639   5176   7282  -1279  -1849   -294       C  
ATOM    200  CG  LEU A  65     -23.712 -15.957 -20.603  1.00 51.66           C  
ANISOU  200  CG  LEU A  65     6949   5348   7330  -1203  -2008   -484       C  
ATOM    201  CD1 LEU A  65     -24.436 -14.965 -21.505  1.00 49.92           C  
ANISOU  201  CD1 LEU A  65     6625   5283   7058  -1205  -2082   -506       C  
ATOM    202  CD2 LEU A  65     -22.204 -15.868 -20.772  1.00 50.44           C  
ANISOU  202  CD2 LEU A  65     6951   5231   6984  -1021  -1924   -565       C  
ATOM    203  N   GLN A  66     -24.632 -17.092 -15.964  1.00 55.75           N  
ANISOU  203  N   GLN A  66     7254   5632   8296  -1467  -1589     64       N  
ATOM    204  CA  GLN A  66     -24.960 -16.711 -14.596  1.00 57.43           C  
ANISOU  204  CA  GLN A  66     7360   5900   8562  -1494  -1406    252       C  
ATOM    205  C   GLN A  66     -23.874 -17.178 -13.654  1.00 57.81           C  
ANISOU  205  C   GLN A  66     7550   5880   8535  -1395  -1299    292       C  
ATOM    206  O   GLN A  66     -23.958 -18.258 -13.062  1.00 62.26           O  
ANISOU  206  O   GLN A  66     8182   6270   9206  -1464  -1298    361       O  
ATOM    207  CB  GLN A  66     -26.324 -17.269 -14.189  1.00 59.47           C  
ANISOU  207  CB  GLN A  66     7476   6067   9051  -1691  -1423    379       C  
ATOM    208  CG  GLN A  66     -27.446 -16.497 -14.830  1.00 57.18           C  
ANISOU  208  CG  GLN A  66     6992   5903   8829  -1767  -1487    379       C  
ATOM    209  CD  GLN A  66     -28.776 -17.216 -14.823  1.00 59.90           C  
ANISOU  209  CD  GLN A  66     7194   6141   9425  -1978  -1569    455       C  
ATOM    210  OE1 GLN A  66     -28.952 -18.246 -14.164  1.00 60.83           O  
ANISOU  210  OE1 GLN A  66     7344   6088   9682  -2084  -1545    543       O  
ATOM    211  NE2 GLN A  66     -29.729 -16.672 -15.565  1.00 61.21           N  
ANISOU  211  NE2 GLN A  66     7194   6404   9657  -2041  -1672    426       N  
ATOM    212  N   THR A  67     -22.837 -16.351 -13.556  1.00 52.48           N  
ANISOU  212  N   THR A  67     6922   5341   7678  -1233  -1217    248       N  
ATOM    213  CA  THR A  67     -21.653 -16.623 -12.757  1.00 51.73           C  
ANISOU  213  CA  THR A  67     6954   5216   7484  -1109  -1131    262       C  
ATOM    214  C   THR A  67     -21.326 -15.406 -11.894  1.00 52.14           C  
ANISOU  214  C   THR A  67     6933   5451   7427  -1018   -972    340       C  
ATOM    215  O   THR A  67     -21.801 -14.302 -12.184  1.00 50.35           O  
ANISOU  215  O   THR A  67     6586   5371   7174  -1024   -944    343       O  
ATOM    216  CB  THR A  67     -20.447 -16.942 -13.651  1.00 53.89           C  
ANISOU  216  CB  THR A  67     7377   5461   7637   -981  -1218     88       C  
ATOM    217  OG1 THR A  67     -20.031 -15.741 -14.315  1.00 51.55           O  
ANISOU  217  OG1 THR A  67     7030   5350   7205   -892  -1198     10       O  
ATOM    218  CG2 THR A  67     -20.799 -18.012 -14.676  1.00 50.96           C  
ANISOU  218  CG2 THR A  67     7088   4921   7353  -1056  -1393    -22       C  
ATOM    219  N   PRO A  68     -20.510 -15.590 -10.838  1.00 48.13           N  
ANISOU  219  N   PRO A  68     6506   4929   6852   -927   -879    397       N  
ATOM    220  CA  PRO A  68     -20.120 -14.459  -9.982  1.00 47.69           C  
ANISOU  220  CA  PRO A  68     6399   5036   6684   -834   -745    452       C  
ATOM    221  C   PRO A  68     -19.454 -13.312 -10.729  1.00 48.45           C  
ANISOU  221  C   PRO A  68     6467   5284   6658   -741   -754    336       C  
ATOM    222  O   PRO A  68     -19.776 -12.143 -10.484  1.00 47.37           O  
ANISOU  222  O   PRO A  68     6230   5283   6485   -731   -677    374       O  
ATOM    223  CB  PRO A  68     -19.126 -15.091  -9.010  1.00 49.08           C  
ANISOU  223  CB  PRO A  68     6705   5147   6797   -735   -701    486       C  
ATOM    224  CG  PRO A  68     -19.573 -16.499  -8.907  1.00 51.64           C  
ANISOU  224  CG  PRO A  68     7104   5268   7250   -826   -755    542       C  
ATOM    225  CD  PRO A  68     -20.044 -16.873 -10.283  1.00 51.18           C  
ANISOU  225  CD  PRO A  68     7032   5138   7275   -914   -896    430       C  
ATOM    226  N   THR A  69     -18.516 -13.641 -11.611  1.00 44.27           N  
ANISOU  226  N   THR A  69     6028   4726   6064   -669   -837    200       N  
ATOM    227  CA  THR A  69     -17.872 -12.628 -12.426  1.00 44.98           C  
ANISOU  227  CA  THR A  69     6094   4952   6045   -590   -839     99       C  
ATOM    228  C   THR A  69     -18.915 -11.829 -13.204  1.00 43.20           C  
ANISOU  228  C   THR A  69     5757   4804   5854   -669   -866    100       C  
ATOM    229  O   THR A  69     -18.823 -10.607 -13.311  1.00 42.53           O  
ANISOU  229  O   THR A  69     5603   4853   5702   -630   -809    100       O  
ATOM    230  CB  THR A  69     -16.862 -13.243 -13.418  1.00 48.16           C  
ANISOU  230  CB  THR A  69     6607   5308   6385   -508   -924    -45       C  
ATOM    231  OG1 THR A  69     -15.795 -13.883 -12.697  1.00 49.51           O  
ANISOU  231  OG1 THR A  69     6869   5423   6517   -411   -899    -50       O  
ATOM    232  CG2 THR A  69     -16.291 -12.168 -14.334  1.00 41.94           C  
ANISOU  232  CG2 THR A  69     5783   4665   5487   -440   -912   -131       C  
ATOM    233  N   ASN A  70     -19.920 -12.513 -13.735  1.00 43.97           N  
ANISOU  233  N   ASN A  70     5834   4811   6060   -780   -960    104       N  
ATOM    234  CA  ASN A  70     -20.846 -11.830 -14.626  1.00 44.67           C  
ANISOU  234  CA  ASN A  70     5823   4975   6175   -840  -1015     87       C  
ATOM    235  C   ASN A  70     -21.852 -10.946 -13.897  1.00 42.38           C  
ANISOU  235  C   ASN A  70     5382   4775   5946   -893   -923    216       C  
ATOM    236  O   ASN A  70     -22.499 -10.123 -14.522  1.00 43.46           O  
ANISOU  236  O   ASN A  70     5427   5002   6084   -910   -948    211       O  
ATOM    237  CB  ASN A  70     -21.539 -12.847 -15.534  1.00 43.48           C  
ANISOU  237  CB  ASN A  70     5699   4702   6119   -937  -1174     25       C  
ATOM    238  CG  ASN A  70     -20.636 -13.288 -16.676  1.00 45.39           C  
ANISOU  238  CG  ASN A  70     6080   4910   6257   -854  -1274   -136       C  
ATOM    239  OD1 ASN A  70     -19.523 -12.773 -16.828  1.00 45.66           O  
ANISOU  239  OD1 ASN A  70     6168   5027   6155   -729  -1213   -189       O  
ATOM    240  ND2 ASN A  70     -21.087 -14.253 -17.461  1.00 43.32           N  
ANISOU  240  ND2 ASN A  70     5875   4523   6060   -921  -1425   -215       N  
ATOM    241  N   SER A  71     -21.971 -11.089 -12.582  1.00 42.46           N  
ANISOU  241  N   SER A  71     5373   4766   5994   -903   -813    331       N  
ATOM    242  CA ASER A  71     -22.758 -10.140 -11.804  0.47 42.20           C  
ANISOU  242  CA ASER A  71     5211   4837   5988   -916   -699    444       C  
ATOM    243  CA BSER A  71     -22.759 -10.133 -11.805  0.53 42.21           C  
ANISOU  243  CA BSER A  71     5212   4838   5988   -916   -699    444       C  
ATOM    244  C   SER A  71     -22.151  -8.749 -11.946  1.00 41.37           C  
ANISOU  244  C   SER A  71     5095   4870   5754   -807   -643    399       C  
ATOM    245  O   SER A  71     -22.863  -7.758 -12.110  1.00 40.01           O  
ANISOU  245  O   SER A  71     4816   4791   5593   -811   -615    432       O  
ATOM    246  CB ASER A  71     -22.814 -10.548 -10.331  0.47 42.40           C  
ANISOU  246  CB ASER A  71     5249   4824   6038   -918   -579    569       C  
ATOM    247  CB BSER A  71     -22.818 -10.512 -10.329  0.53 42.62           C  
ANISOU  247  CB BSER A  71     5275   4855   6064   -917   -577    570       C  
ATOM    248  OG ASER A  71     -21.528 -10.444  -9.729  0.47 42.69           O  
ANISOU  248  OG ASER A  71     5400   4872   5946   -800   -527    535       O  
ATOM    249  OG BSER A  71     -23.410 -11.774 -10.136  0.53 42.64           O  
ANISOU  249  OG BSER A  71     5285   4717   6198  -1028   -613    634       O  
ATOM    250  N   PHE A  72     -20.822  -8.677 -11.883  1.00 36.45           N  
ANISOU  250  N   PHE A  72     4579   4254   5017   -710   -628    327       N  
ATOM    251  CA  PHE A  72     -20.143  -7.386 -12.030  1.00 34.60           C  
ANISOU  251  CA  PHE A  72     4337   4135   4676   -621   -578    283       C  
ATOM    252  C   PHE A  72     -20.241  -6.858 -13.447  1.00 34.24           C  
ANISOU  252  C   PHE A  72     4272   4137   4601   -621   -656    207       C  
ATOM    253  O   PHE A  72     -20.278  -5.640 -13.671  1.00 34.44           O  
ANISOU  253  O   PHE A  72     4250   4255   4581   -584   -616    211       O  
ATOM    254  CB  PHE A  72     -18.670  -7.503 -11.651  1.00 35.24           C  
ANISOU  254  CB  PHE A  72     4517   4212   4660   -526   -553    224       C  
ATOM    255  CG  PHE A  72     -18.454  -7.923 -10.237  1.00 35.44           C  
ANISOU  255  CG  PHE A  72     4578   4204   4684   -502   -483    296       C  
ATOM    256  CD1 PHE A  72     -18.545  -7.004  -9.205  1.00 38.81           C  
ANISOU  256  CD1 PHE A  72     4968   4706   5073   -461   -383    355       C  
ATOM    257  CD2 PHE A  72     -18.214  -9.242  -9.932  1.00 36.77           C  
ANISOU  257  CD2 PHE A  72     4827   4258   4884   -512   -519    307       C  
ATOM    258  CE1 PHE A  72     -18.366  -7.396  -7.888  1.00 37.78           C  
ANISOU  258  CE1 PHE A  72     4884   4552   4919   -426   -321    423       C  
ATOM    259  CE2 PHE A  72     -18.025  -9.632  -8.627  1.00 37.13           C  
ANISOU  259  CE2 PHE A  72     4919   4275   4916   -480   -454    386       C  
ATOM    260  CZ  PHE A  72     -18.100  -8.714  -7.605  1.00 38.77           C  
ANISOU  260  CZ  PHE A  72     5091   4571   5069   -435   -355    445       C  
ATOM    261  N   ILE A  73     -20.246  -7.773 -14.407  1.00 37.27           N  
ANISOU  261  N   ILE A  73     4709   4451   5003   -655   -769    137       N  
ATOM    262  CA  ILE A  73     -20.333  -7.384 -15.795  1.00 36.75           C  
ANISOU  262  CA  ILE A  73     4645   4430   4887   -644   -852     62       C  
ATOM    263  C   ILE A  73     -21.696  -6.767 -16.059  1.00 39.98           C  
ANISOU  263  C   ILE A  73     4933   4890   5369   -706   -880    124       C  
ATOM    264  O   ILE A  73     -21.809  -5.796 -16.808  1.00 38.22           O  
ANISOU  264  O   ILE A  73     4682   4752   5087   -669   -891    109       O  
ATOM    265  CB  ILE A  73     -20.091  -8.573 -16.709  1.00 39.82           C  
ANISOU  265  CB  ILE A  73     5132   4727   5272   -658   -976    -38       C  
ATOM    266  CG1 ILE A  73     -18.610  -8.971 -16.633  1.00 40.88           C  
ANISOU  266  CG1 ILE A  73     5379   4839   5312   -561   -942   -111       C  
ATOM    267  CG2 ILE A  73     -20.457  -8.239 -18.135  1.00 36.53           C  
ANISOU  267  CG2 ILE A  73     4718   4359   4803   -654  -1078   -106       C  
ATOM    268  CD1 ILE A  73     -18.234  -9.983 -17.690  1.00 47.65           C  
ANISOU  268  CD1 ILE A  73     6349   5622   6134   -538  -1055   -230       C  
ATOM    269  N   VAL A  74     -22.729  -7.323 -15.434  1.00 37.46           N  
ANISOU  269  N   VAL A  74     4534   4519   5179   -798   -886    203       N  
ATOM    270  CA  VAL A  74     -24.044  -6.707 -15.522  1.00 38.55           C  
ANISOU  270  CA  VAL A  74     4527   4717   5402   -849   -896    275       C  
ATOM    271  C   VAL A  74     -24.039  -5.297 -14.897  1.00 37.56           C  
ANISOU  271  C   VAL A  74     4342   4701   5228   -773   -765    338       C  
ATOM    272  O   VAL A  74     -24.578  -4.371 -15.474  1.00 37.79           O  
ANISOU  272  O   VAL A  74     4304   4808   5248   -750   -785    347       O  
ATOM    273  CB  VAL A  74     -25.118  -7.558 -14.847  1.00 38.44           C  
ANISOU  273  CB  VAL A  74     4419   4634   5551   -965   -900    364       C  
ATOM    274  CG1 VAL A  74     -26.413  -6.753 -14.710  1.00 42.15           C  
ANISOU  274  CG1 VAL A  74     4711   5195   6110   -995   -872    456       C  
ATOM    275  CG2 VAL A  74     -25.365  -8.835 -15.654  1.00 38.79           C  
ANISOU  275  CG2 VAL A  74     4507   4561   5670  -1058  -1062    295       C  
ATOM    276  N   SER A  75     -23.452  -5.163 -13.714  1.00 34.74           N  
ANISOU  276  N   SER A  75     4018   4342   4840   -731   -643    379       N  
ATOM    277  CA  SER A  75     -23.289  -3.868 -13.048  1.00 36.11           C  
ANISOU  277  CA  SER A  75     4164   4599   4957   -651   -526    417       C  
ATOM    278  C   SER A  75     -22.614  -2.812 -13.940  1.00 36.18           C  
ANISOU  278  C   SER A  75     4215   4666   4865   -580   -544    349       C  
ATOM    279  O   SER A  75     -23.059  -1.653 -14.020  1.00 35.10           O  
ANISOU  279  O   SER A  75     4020   4594   4720   -541   -507    382       O  
ATOM    280  CB  SER A  75     -22.485  -4.048 -11.753  1.00 37.91           C  
ANISOU  280  CB  SER A  75     4460   4805   5139   -607   -424    437       C  
ATOM    281  OG  SER A  75     -22.276  -2.804 -11.098  1.00 36.99           O  
ANISOU  281  OG  SER A  75     4332   4758   4963   -529   -326    455       O  
ATOM    282  N   LEU A  76     -21.539  -3.214 -14.609  1.00 35.40           N  
ANISOU  282  N   LEU A  76     4219   4542   4691   -559   -593    261       N  
ATOM    283  CA  LEU A  76     -20.850  -2.343 -15.569  1.00 33.15           C  
ANISOU  283  CA  LEU A  76     3977   4308   4310   -501   -603    206       C  
ATOM    284  C   LEU A  76     -21.723  -1.964 -16.739  1.00 34.36           C  
ANISOU  284  C   LEU A  76     4087   4499   4468   -514   -689    209       C  
ATOM    285  O   LEU A  76     -21.654  -0.849 -17.250  1.00 35.29           O  
ANISOU  285  O   LEU A  76     4203   4674   4533   -465   -668    219       O  
ATOM    286  CB  LEU A  76     -19.605  -3.037 -16.119  1.00 33.97           C  
ANISOU  286  CB  LEU A  76     4188   4383   4338   -473   -636    115       C  
ATOM    287  CG  LEU A  76     -18.422  -3.083 -15.160  1.00 37.81           C  
ANISOU  287  CG  LEU A  76     4720   4857   4789   -429   -556     98       C  
ATOM    288  CD1 LEU A  76     -17.392  -4.108 -15.650  1.00 40.99           C  
ANISOU  288  CD1 LEU A  76     5211   5219   5144   -403   -601     12       C  
ATOM    289  CD2 LEU A  76     -17.799  -1.701 -15.085  1.00 35.59           C  
ANISOU  289  CD2 LEU A  76     4427   4640   4454   -378   -478    102       C  
ATOM    290  N   ALA A  77     -22.510  -2.927 -17.200  1.00 34.49           N  
ANISOU  290  N   ALA A  77     4078   4477   4550   -580   -796    198       N  
ATOM    291  CA  ALA A  77     -23.408  -2.685 -18.306  1.00 35.55           C  
ANISOU  291  CA  ALA A  77     4168   4649   4693   -594   -906    193       C  
ATOM    292  C   ALA A  77     -24.454  -1.638 -17.897  1.00 36.94           C  
ANISOU  292  C   ALA A  77     4215   4887   4933   -583   -859    288       C  
ATOM    293  O   ALA A  77     -24.807  -0.764 -18.688  1.00 36.06           O  
ANISOU  293  O   ALA A  77     4085   4835   4782   -538   -897    298       O  
ATOM    294  CB  ALA A  77     -24.081  -4.011 -18.764  1.00 36.45           C  
ANISOU  294  CB  ALA A  77     4270   4694   4885   -683  -1047    154       C  
ATOM    295  N   ALA A  78     -24.914  -1.735 -16.650  1.00 34.75           N  
ANISOU  295  N   ALA A  78     3860   4597   4748   -612   -771    359       N  
ATOM    296  CA  ALA A  78     -25.887  -0.799 -16.092  1.00 36.85           C  
ANISOU  296  CA  ALA A  78     4001   4922   5077   -586   -704    449       C  
ATOM    297  C   ALA A  78     -25.335   0.622 -16.076  1.00 40.11           C  
ANISOU  297  C   ALA A  78     4460   5380   5399   -485   -623    452       C  
ATOM    298  O   ALA A  78     -26.016   1.569 -16.440  1.00 38.92           O  
ANISOU  298  O   ALA A  78     4248   5281   5260   -439   -631    492       O  
ATOM    299  CB  ALA A  78     -26.277  -1.225 -14.681  1.00 35.94           C  
ANISOU  299  CB  ALA A  78     3822   4787   5048   -620   -599    521       C  
ATOM    300  N   ALA A  79     -24.090   0.752 -15.638  1.00 34.93           N  
ANISOU  300  N   ALA A  79     3909   4698   4663   -453   -550    412       N  
ATOM    301  CA  ALA A  79     -23.400   2.035 -15.602  1.00 35.78           C  
ANISOU  301  CA  ALA A  79     4070   4828   4697   -376   -477    407       C  
ATOM    302  C   ALA A  79     -23.342   2.660 -16.984  1.00 37.47           C  
ANISOU  302  C   ALA A  79     4318   5071   4849   -345   -546    391       C  
ATOM    303  O   ALA A  79     -23.535   3.873 -17.135  1.00 37.75           O  
ANISOU  303  O   ALA A  79     4346   5130   4869   -287   -511    428       O  
ATOM    304  CB  ALA A  79     -21.993   1.859 -15.034  1.00 35.36           C  
ANISOU  304  CB  ALA A  79     4113   4741   4579   -365   -417    353       C  
ATOM    305  N   ASP A  80     -23.109   1.834 -18.002  1.00 35.83           N  
ANISOU  305  N   ASP A  80     4157   4857   4599   -377   -646    337       N  
ATOM    306  CA  ASP A  80     -23.044   2.357 -19.359  1.00 35.31           C  
ANISOU  306  CA  ASP A  80     4139   4826   4449   -337   -711    325       C  
ATOM    307  C   ASP A  80     -24.427   2.694 -19.929  1.00 36.74           C  
ANISOU  307  C   ASP A  80     4231   5050   4679   -328   -802    375       C  
ATOM    308  O   ASP A  80     -24.595   3.683 -20.650  1.00 36.34           O  
ANISOU  308  O   ASP A  80     4198   5035   4574   -265   -815    409       O  
ATOM    309  CB  ASP A  80     -22.285   1.371 -20.237  1.00 36.48           C  
ANISOU  309  CB  ASP A  80     4383   4961   4517   -354   -781    240       C  
ATOM    310  CG  ASP A  80     -20.765   1.379 -19.920  1.00 43.72           C  
ANISOU  310  CG  ASP A  80     5384   5858   5367   -333   -683    197       C  
ATOM    311  OD1 ASP A  80     -20.257   2.420 -19.430  1.00 41.74           O  
ANISOU  311  OD1 ASP A  80     5135   5615   5109   -302   -582    232       O  
ATOM    312  OD2 ASP A  80     -20.087   0.361 -20.154  1.00 45.82           O  
ANISOU  312  OD2 ASP A  80     5712   6100   5598   -345   -713    127       O  
ATOM    313  N   LEU A  81     -25.425   1.905 -19.569  1.00 36.24           N  
ANISOU  313  N   LEU A  81     4064   4981   4725   -389   -862    389       N  
ATOM    314  CA  LEU A  81     -26.787   2.217 -19.964  1.00 36.20           C  
ANISOU  314  CA  LEU A  81     3938   5024   4791   -382   -948    440       C  
ATOM    315  C   LEU A  81     -27.237   3.521 -19.344  1.00 36.63           C  
ANISOU  315  C   LEU A  81     3928   5111   4879   -307   -847    521       C  
ATOM    316  O   LEU A  81     -27.827   4.349 -20.020  1.00 38.24           O  
ANISOU  316  O   LEU A  81     4103   5359   5068   -243   -897    559       O  
ATOM    317  CB  LEU A  81     -27.746   1.096 -19.558  1.00 38.31           C  
ANISOU  317  CB  LEU A  81     4084   5275   5198   -480  -1015    448       C  
ATOM    318  CG  LEU A  81     -27.642  -0.183 -20.398  1.00 37.45           C  
ANISOU  318  CG  LEU A  81     4028   5125   5077   -555  -1165    362       C  
ATOM    319  CD1 LEU A  81     -28.584  -1.256 -19.835  1.00 41.12           C  
ANISOU  319  CD1 LEU A  81     4363   5550   5709   -670  -1216    384       C  
ATOM    320  CD2 LEU A  81     -27.972   0.093 -21.870  1.00 38.55           C  
ANISOU  320  CD2 LEU A  81     4200   5313   5135   -513  -1321    325       C  
ATOM    321  N   LEU A  82     -26.977   3.684 -18.050  1.00 34.15           N  
ANISOU  321  N   LEU A  82     3599   4773   4605   -305   -711    545       N  
ATOM    322  CA  LEU A  82     -27.342   4.907 -17.362  1.00 36.77           C  
ANISOU  322  CA  LEU A  82     3887   5123   4962   -222   -608    607       C  
ATOM    323  C   LEU A  82     -26.624   6.107 -17.973  1.00 37.34           C  
ANISOU  323  C   LEU A  82     4070   5183   4934   -144   -585    603       C  
ATOM    324  O   LEU A  82     -27.178   7.201 -18.039  1.00 38.12           O  
ANISOU  324  O   LEU A  82     4139   5298   5046    -63   -565    655       O  
ATOM    325  CB  LEU A  82     -27.027   4.784 -15.873  1.00 34.13           C  
ANISOU  325  CB  LEU A  82     3550   4762   4658   -229   -473    615       C  
ATOM    326  CG  LEU A  82     -28.038   3.911 -15.136  1.00 37.75           C  
ANISOU  326  CG  LEU A  82     3872   5240   5233   -286   -461    662       C  
ATOM    327  CD1 LEU A  82     -27.580   3.603 -13.702  1.00 37.05           C  
ANISOU  327  CD1 LEU A  82     3813   5123   5142   -291   -330    669       C  
ATOM    328  CD2 LEU A  82     -29.432   4.571 -15.169  1.00 38.12           C  
ANISOU  328  CD2 LEU A  82     3763   5353   5369   -233   -465    738       C  
ATOM    329  N   LEU A  83     -25.393   5.905 -18.428  1.00 33.82           N  
ANISOU  329  N   LEU A  83     3751   4707   4394   -166   -583    546       N  
ATOM    330  CA  LEU A  83     -24.651   6.975 -19.071  1.00 35.14           C  
ANISOU  330  CA  LEU A  83     4020   4859   4472   -109   -553    554       C  
ATOM    331  C   LEU A  83     -25.325   7.404 -20.371  1.00 35.66           C  
ANISOU  331  C   LEU A  83     4086   4967   4498    -61   -656    593       C  
ATOM    332  O   LEU A  83     -25.536   8.597 -20.609  1.00 35.89           O  
ANISOU  332  O   LEU A  83     4134   4989   4513     15   -630    651       O  
ATOM    333  CB  LEU A  83     -23.196   6.550 -19.338  1.00 34.04           C  
ANISOU  333  CB  LEU A  83     3993   4694   4248   -147   -524    490       C  
ATOM    334  CG  LEU A  83     -22.282   7.633 -19.929  1.00 35.01           C  
ANISOU  334  CG  LEU A  83     4214   4797   4292   -107   -469    508       C  
ATOM    335  CD1 LEU A  83     -21.901   8.708 -18.881  1.00 35.10           C  
ANISOU  335  CD1 LEU A  83     4235   4753   4349    -83   -357    526       C  
ATOM    336  CD2 LEU A  83     -21.019   7.010 -20.544  1.00 37.00           C  
ANISOU  336  CD2 LEU A  83     4551   5053   4456   -140   -462    450       C  
ATOM    337  N   ALA A  84     -25.675   6.431 -21.203  1.00 36.72           N  
ANISOU  337  N   ALA A  84     4206   5136   4609    -99   -781    560       N  
ATOM    338  CA  ALA A  84     -26.345   6.702 -22.475  1.00 37.22           C  
ANISOU  338  CA  ALA A  84     4274   5248   4619    -50   -906    586       C  
ATOM    339  C   ALA A  84     -27.712   7.369 -22.311  1.00 37.21           C  
ANISOU  339  C   ALA A  84     4143   5283   4710      8   -945    660       C  
ATOM    340  O   ALA A  84     -28.127   8.157 -23.164  1.00 38.70           O  
ANISOU  340  O   ALA A  84     4353   5501   4848     90  -1006    709       O  
ATOM    341  CB  ALA A  84     -26.496   5.414 -23.275  1.00 36.78           C  
ANISOU  341  CB  ALA A  84     4228   5218   4530   -107  -1049    515       C  
ATOM    342  N   LEU A  85     -28.410   7.056 -21.227  1.00 37.06           N  
ANISOU  342  N   LEU A  85     3991   5268   4824    -25   -906    674       N  
ATOM    343  CA  LEU A  85     -29.736   7.629 -20.987  1.00 40.36           C  
ANISOU  343  CA  LEU A  85     4260   5731   5344     36   -929    744       C  
ATOM    344  C   LEU A  85     -29.722   9.000 -20.304  1.00 42.34           C  
ANISOU  344  C   LEU A  85     4526   5953   5608    140   -799    802       C  
ATOM    345  O   LEU A  85     -30.546   9.865 -20.623  1.00 42.20           O  
ANISOU  345  O   LEU A  85     4454   5965   5616    238   -832    864       O  
ATOM    346  CB  LEU A  85     -30.565   6.665 -20.138  1.00 41.40           C  
ANISOU  346  CB  LEU A  85     4227   5886   5619    -43   -932    746       C  
ATOM    347  CG  LEU A  85     -30.889   5.291 -20.725  1.00 40.53           C  
ANISOU  347  CG  LEU A  85     4067   5790   5542   -153  -1081    694       C  
ATOM    348  CD1 LEU A  85     -31.629   4.462 -19.687  1.00 40.37           C  
ANISOU  348  CD1 LEU A  85     3885   5774   5679   -239  -1042    718       C  
ATOM    349  CD2 LEU A  85     -31.712   5.434 -21.987  1.00 40.60           C  
ANISOU  349  CD2 LEU A  85     4029   5860   5537   -116  -1264    701       C  
ATOM    350  N   LEU A  86     -28.805   9.185 -19.356  1.00 39.15           N  
ANISOU  350  N   LEU A  86     4198   5489   5190    123   -661    777       N  
ATOM    351  CA  LEU A  86     -28.845  10.350 -18.474  1.00 39.97           C  
ANISOU  351  CA  LEU A  86     4311   5553   5322    211   -538    812       C  
ATOM    352  C   LEU A  86     -27.801  11.415 -18.781  1.00 40.61           C  
ANISOU  352  C   LEU A  86     4554   5558   5317    254   -483    811       C  
ATOM    353  O   LEU A  86     -27.985  12.566 -18.419  1.00 42.18           O  
ANISOU  353  O   LEU A  86     4776   5712   5537    345   -421    847       O  
ATOM    354  CB  LEU A  86     -28.672   9.915 -17.016  1.00 37.29           C  
ANISOU  354  CB  LEU A  86     3936   5198   5036    174   -423    784       C  
ATOM    355  CG  LEU A  86     -29.725   8.965 -16.435  1.00 38.70           C  
ANISOU  355  CG  LEU A  86     3945   5441   5319    130   -432    807       C  
ATOM    356  CD1 LEU A  86     -29.463   8.717 -14.962  1.00 40.26           C  
ANISOU  356  CD1 LEU A  86     4140   5619   5539    118   -296    794       C  
ATOM    357  CD2 LEU A  86     -31.134   9.507 -16.648  1.00 42.22           C  
ANISOU  357  CD2 LEU A  86     4240   5951   5849    216   -470    878       C  
ATOM    358  N   VAL A  87     -26.705  11.045 -19.431  1.00 37.77           N  
ANISOU  358  N   VAL A  87     4305   5177   4868    190   -501    771       N  
ATOM    359  CA  VAL A  87     -25.603  11.980 -19.624  1.00 37.60           C  
ANISOU  359  CA  VAL A  87     4422   5080   4783    206   -430    775       C  
ATOM    360  C   VAL A  87     -25.332  12.302 -21.089  1.00 39.83           C  
ANISOU  360  C   VAL A  87     4793   5373   4967    228   -494    816       C  
ATOM    361  O   VAL A  87     -25.240  13.486 -21.470  1.00 39.55           O  
ANISOU  361  O   VAL A  87     4833   5286   4911    296   -464    879       O  
ATOM    362  CB  VAL A  87     -24.304  11.432 -18.977  1.00 37.65           C  
ANISOU  362  CB  VAL A  87     4486   5051   4768    118   -358    701       C  
ATOM    363  CG1 VAL A  87     -23.097  12.316 -19.317  1.00 38.54           C  
ANISOU  363  CG1 VAL A  87     4723   5093   4828    113   -294    706       C  
ATOM    364  CG2 VAL A  87     -24.473  11.324 -17.476  1.00 37.39           C  
ANISOU  364  CG2 VAL A  87     4398   5000   4809    117   -283    669       C  
ATOM    365  N   LEU A  88     -25.180  11.262 -21.908  1.00 36.93           N  
ANISOU  365  N   LEU A  88     4434   5065   4533    177   -579    781       N  
ATOM    366  CA  LEU A  88     -24.820  11.461 -23.316  1.00 39.25           C  
ANISOU  366  CA  LEU A  88     4831   5381   4703    204   -631    813       C  
ATOM    367  C   LEU A  88     -25.765  12.363 -24.141  1.00 38.97           C  
ANISOU  367  C   LEU A  88     4800   5363   4642    312   -705    904       C  
ATOM    368  O   LEU A  88     -25.298  13.112 -25.000  1.00 41.41           O  
ANISOU  368  O   LEU A  88     5227   5651   4858    358   -687    966       O  
ATOM    369  CB  LEU A  88     -24.683  10.109 -24.013  1.00 38.14           C  
ANISOU  369  CB  LEU A  88     4694   5304   4492    148   -728    744       C  
ATOM    370  CG  LEU A  88     -23.576   9.212 -23.450  1.00 37.34           C  
ANISOU  370  CG  LEU A  88     4617   5183   4389     59   -661    659       C  
ATOM    371  CD1 LEU A  88     -23.354   8.006 -24.342  1.00 37.31           C  
ANISOU  371  CD1 LEU A  88     4653   5229   4296     27   -756    591       C  
ATOM    372  CD2 LEU A  88     -22.282   9.993 -23.257  1.00 37.95           C  
ANISOU  372  CD2 LEU A  88     4782   5202   4434     51   -525    674       C  
ATOM    373  N   PRO A  89     -27.091  12.285 -23.920  1.00 42.09           N  
ANISOU  373  N   PRO A  89     5067   5803   5121    357   -789    922       N  
ATOM    374  CA  PRO A  89     -27.922  13.169 -24.755  1.00 40.89           C  
ANISOU  374  CA  PRO A  89     4926   5672   4939    475   -869   1011       C  
ATOM    375  C   PRO A  89     -27.609  14.667 -24.589  1.00 42.64           C  
ANISOU  375  C   PRO A  89     5240   5797   5164    556   -763   1093       C  
ATOM    376  O   PRO A  89     -27.402  15.377 -25.581  1.00 41.99           O  
ANISOU  376  O   PRO A  89     5274   5697   4984    620   -781   1168       O  
ATOM    377  CB  PRO A  89     -29.341  12.851 -24.280  1.00 40.83           C  
ANISOU  377  CB  PRO A  89     4731   5727   5055    504   -952   1012       C  
ATOM    378  CG  PRO A  89     -29.262  11.429 -23.863  1.00 39.57           C  
ANISOU  378  CG  PRO A  89     4493   5605   4937    381   -980    923       C  
ATOM    379  CD  PRO A  89     -27.907  11.297 -23.196  1.00 38.05           C  
ANISOU  379  CD  PRO A  89     4399   5341   4717    305   -838    873       C  
ATOM    380  N   LEU A  90     -27.561  15.136 -23.350  1.00 42.65           N  
ANISOU  380  N   LEU A  90     5203   5730   5272    556   -654   1078       N  
ATOM    381  CA  LEU A  90     -27.254  16.533 -23.093  1.00 42.93           C  
ANISOU  381  CA  LEU A  90     5332   5650   5327    625   -560   1138       C  
ATOM    382  C   LEU A  90     -25.788  16.825 -23.391  1.00 41.76           C  
ANISOU  382  C   LEU A  90     5334   5426   5108    551   -471   1139       C  
ATOM    383  O   LEU A  90     -25.431  17.949 -23.734  1.00 43.38           O  
ANISOU  383  O   LEU A  90     5649   5536   5295    597   -421   1214       O  
ATOM    384  CB  LEU A  90     -27.611  16.894 -21.654  1.00 44.79           C  
ANISOU  384  CB  LEU A  90     5494   5837   5686    651   -477   1104       C  
ATOM    385  CG  LEU A  90     -29.113  17.179 -21.525  1.00 45.46           C  
ANISOU  385  CG  LEU A  90     5450   5976   5846    775   -539   1149       C  
ATOM    386  CD1 LEU A  90     -29.517  17.408 -20.093  1.00 50.17           C  
ANISOU  386  CD1 LEU A  90     5967   6547   6550    811   -445   1111       C  
ATOM    387  CD2 LEU A  90     -29.481  18.389 -22.363  1.00 43.58           C  
ANISOU  387  CD2 LEU A  90     5295   5686   5578    907   -576   1251       C  
ATOM    388  N   PHE A  91     -24.936  15.810 -23.296  1.00 43.25           N  
ANISOU  388  N   PHE A  91     5521   5652   5261    438   -451   1061       N  
ATOM    389  CA  PHE A  91     -23.563  15.998 -23.741  1.00 41.21           C  
ANISOU  389  CA  PHE A  91     5380   5346   4931    372   -371   1068       C  
ATOM    390  C   PHE A  91     -23.500  16.249 -25.245  1.00 42.76           C  
ANISOU  390  C   PHE A  91     5676   5576   4995    420   -416   1155       C  
ATOM    391  O   PHE A  91     -22.838  17.189 -25.702  1.00 43.15           O  
ANISOU  391  O   PHE A  91     5838   5549   5010    430   -340   1236       O  
ATOM    392  CB  PHE A  91     -22.693  14.790 -23.392  1.00 42.83           C  
ANISOU  392  CB  PHE A  91     5556   5596   5120    260   -348    966       C  
ATOM    393  CG  PHE A  91     -21.383  14.788 -24.095  1.00 40.57           C  
ANISOU  393  CG  PHE A  91     5367   5301   4746    205   -282    977       C  
ATOM    394  CD1 PHE A  91     -20.420  15.731 -23.782  1.00 42.38           C  
ANISOU  394  CD1 PHE A  91     5658   5428   5016    169   -168   1006       C  
ATOM    395  CD2 PHE A  91     -21.115  13.852 -25.078  1.00 40.75           C  
ANISOU  395  CD2 PHE A  91     5417   5416   4650    191   -331    955       C  
ATOM    396  CE1 PHE A  91     -19.195  15.738 -24.437  1.00 43.49           C  
ANISOU  396  CE1 PHE A  91     5866   5569   5089    112    -93   1027       C  
ATOM    397  CE2 PHE A  91     -19.900  13.840 -25.732  1.00 40.76           C  
ANISOU  397  CE2 PHE A  91     5499   5422   4566    152   -252    969       C  
ATOM    398  CZ  PHE A  91     -18.933  14.788 -25.414  1.00 42.96           C  
ANISOU  398  CZ  PHE A  91     5819   5608   4895    110   -126   1012       C  
ATOM    399  N   VAL A  92     -24.191  15.413 -26.012  1.00 42.21           N  
ANISOU  399  N   VAL A  92     5570   5617   4850    449   -542   1142       N  
ATOM    400  CA  VAL A  92     -24.235  15.586 -27.463  1.00 43.12           C  
ANISOU  400  CA  VAL A  92     5789   5781   4814    514   -604   1218       C  
ATOM    401  C   VAL A  92     -24.856  16.935 -27.851  1.00 48.31           C  
ANISOU  401  C   VAL A  92     6505   6378   5472    633   -613   1347       C  
ATOM    402  O   VAL A  92     -24.342  17.642 -28.724  1.00 47.43           O  
ANISOU  402  O   VAL A  92     6529   6231   5259    669   -567   1446       O  
ATOM    403  CB  VAL A  92     -25.015  14.443 -28.138  1.00 45.23           C  
ANISOU  403  CB  VAL A  92     6001   6175   5011    530   -769   1161       C  
ATOM    404  CG1 VAL A  92     -25.256  14.743 -29.618  1.00 45.50           C  
ANISOU  404  CG1 VAL A  92     6148   6264   4874    628   -856   1243       C  
ATOM    405  CG2 VAL A  92     -24.249  13.152 -27.979  1.00 43.68           C  
ANISOU  405  CG2 VAL A  92     5789   6019   4787    424   -756   1045       C  
ATOM    406  N   TYR A  93     -25.955  17.286 -27.187  1.00 48.32           N  
ANISOU  406  N   TYR A  93     6405   6365   5589    699   -664   1351       N  
ATOM    407  CA  TYR A  93     -26.600  18.566 -27.410  1.00 50.03           C  
ANISOU  407  CA  TYR A  93     6669   6513   5828    828   -673   1466       C  
ATOM    408  C   TYR A  93     -25.623  19.712 -27.184  1.00 48.25           C  
ANISOU  408  C   TYR A  93     6573   6132   5627    808   -523   1531       C  
ATOM    409  O   TYR A  93     -25.566  20.665 -27.967  1.00 50.36           O  
ANISOU  409  O   TYR A  93     6965   6337   5832    883   -510   1654       O  
ATOM    410  CB  TYR A  93     -27.804  18.720 -26.491  1.00 51.62           C  
ANISOU  410  CB  TYR A  93     6721   6720   6172    897   -719   1442       C  
ATOM    411  CG  TYR A  93     -28.481  20.048 -26.653  1.00 53.11           C  
ANISOU  411  CG  TYR A  93     6956   6830   6393   1048   -727   1552       C  
ATOM    412  CD1 TYR A  93     -29.307  20.291 -27.734  1.00 52.66           C  
ANISOU  412  CD1 TYR A  93     6916   6837   6256   1172   -859   1640       C  
ATOM    413  CD2 TYR A  93     -28.285  21.065 -25.730  1.00 55.01           C  
ANISOU  413  CD2 TYR A  93     7233   6927   6741   1075   -613   1565       C  
ATOM    414  CE1 TYR A  93     -29.924  21.505 -27.891  1.00 57.07           C  
ANISOU  414  CE1 TYR A  93     7522   7318   6843   1324   -871   1747       C  
ATOM    415  CE2 TYR A  93     -28.900  22.280 -25.879  1.00 55.52           C  
ANISOU  415  CE2 TYR A  93     7353   6904   6839   1223   -622   1663       C  
ATOM    416  CZ  TYR A  93     -29.716  22.497 -26.960  1.00 59.13           C  
ANISOU  416  CZ  TYR A  93     7823   7426   7219   1350   -748   1759       C  
ATOM    417  OH  TYR A  93     -30.339  23.714 -27.107  1.00 66.85           O  
ANISOU  417  OH  TYR A  93     8858   8310   8231   1514   -761   1863       O  
ATOM    418  N   SER A  94     -24.871  19.613 -26.096  1.00 49.18           N  
ANISOU  418  N   SER A  94     6662   6185   5841    704   -417   1450       N  
ATOM    419  CA  SER A  94     -23.864  20.596 -25.757  1.00 52.06           C  
ANISOU  419  CA  SER A  94     7131   6397   6254    656   -285   1487       C  
ATOM    420  C   SER A  94     -22.849  20.734 -26.883  1.00 50.56           C  
ANISOU  420  C   SER A  94     7067   6202   5941    609   -228   1569       C  
ATOM    421  O   SER A  94     -22.549  21.844 -27.321  1.00 53.22           O  
ANISOU  421  O   SER A  94     7523   6425   6274    640   -167   1687       O  
ATOM    422  CB  SER A  94     -23.170  20.209 -24.452  1.00 53.95           C  
ANISOU  422  CB  SER A  94     7305   6599   6595    543   -208   1363       C  
ATOM    423  OG  SER A  94     -22.422  21.289 -23.932  1.00 59.31           O  
ANISOU  423  OG  SER A  94     8066   7115   7355    509   -106   1385       O  
ATOM    424  N   GLU A  95     -22.343  19.598 -27.357  1.00 53.79           N  
ANISOU  424  N   GLU A  95     7454   6733   6252    542   -243   1512       N  
ATOM    425  CA  GLU A  95     -21.345  19.551 -28.426  1.00 52.10           C  
ANISOU  425  CA  GLU A  95     7347   6544   5905    503   -175   1579       C  
ATOM    426  C   GLU A  95     -21.857  20.129 -29.751  1.00 53.69           C  
ANISOU  426  C   GLU A  95     7667   6767   5966    624   -225   1724       C  
ATOM    427  O   GLU A  95     -21.112  20.776 -30.489  1.00 53.62           O  
ANISOU  427  O   GLU A  95     7781   6708   5884    617   -128   1841       O  
ATOM    428  CB  GLU A  95     -20.876  18.109 -28.626  1.00 49.88           C  
ANISOU  428  CB  GLU A  95     7012   6399   5542    436   -200   1469       C  
ATOM    429  CG  GLU A  95     -20.062  17.588 -27.449  1.00 50.64           C  
ANISOU  429  CG  GLU A  95     7020   6468   5753    314   -127   1349       C  
ATOM    430  CD  GLU A  95     -18.712  18.276 -27.355  1.00 54.31           C  
ANISOU  430  CD  GLU A  95     7540   6839   6256    226     26   1394       C  
ATOM    431  OE1 GLU A  95     -17.836  17.984 -28.203  1.00 54.62           O  
ANISOU  431  OE1 GLU A  95     7631   6934   6187    195     93   1428       O  
ATOM    432  OE2 GLU A  95     -18.543  19.148 -26.474  1.00 56.03           O  
ANISOU  432  OE2 GLU A  95     7751   6926   6611    193     80   1399       O  
ATOM    433  N   VAL A  96     -23.129  19.893 -30.052  1.00 52.20           N  
ANISOU  433  N   VAL A  96     7437   6656   5742    735   -378   1722       N  
ATOM    434  CA  VAL A  96     -23.743  20.490 -31.232  1.00 53.35           C  
ANISOU  434  CA  VAL A  96     7691   6823   5756    871   -451   1858       C  
ATOM    435  C   VAL A  96     -23.808  22.013 -31.073  1.00 56.34           C  
ANISOU  435  C   VAL A  96     8160   7031   6216    931   -378   1993       C  
ATOM    436  O   VAL A  96     -23.647  22.748 -32.039  1.00 59.23           O  
ANISOU  436  O   VAL A  96     8671   7359   6474    998   -349   2142       O  
ATOM    437  CB  VAL A  96     -25.150  19.917 -31.486  1.00 52.81           C  
ANISOU  437  CB  VAL A  96     7532   6875   5660    976   -652   1815       C  
ATOM    438  CG1 VAL A  96     -25.846  20.658 -32.628  1.00 56.17           C  
ANISOU  438  CG1 VAL A  96     8068   7315   5958   1137   -743   1960       C  
ATOM    439  CG2 VAL A  96     -25.067  18.427 -31.778  1.00 50.71           C  
ANISOU  439  CG2 VAL A  96     7203   6757   5308    914   -736   1687       C  
ATOM    440  N   GLN A  97     -24.009  22.483 -29.845  1.00 57.45           N  
ANISOU  440  N   GLN A  97     8224   7061   6542    909   -342   1940       N  
ATOM    441  CA  GLN A  97     -24.033  23.918 -29.557  1.00 57.09           C  
ANISOU  441  CA  GLN A  97     8269   6828   6595    961   -274   2045       C  
ATOM    442  C   GLN A  97     -22.624  24.461 -29.311  1.00 54.51           C  
ANISOU  442  C   GLN A  97     8026   6363   6324    822   -104   2074       C  
ATOM    443  O   GLN A  97     -22.451  25.527 -28.708  1.00 54.97           O  
ANISOU  443  O   GLN A  97     8135   6238   6512    816    -37   2109       O  
ATOM    444  CB  GLN A  97     -24.928  24.212 -28.348  1.00 65.05           C  
ANISOU  444  CB  GLN A  97     9168   7779   7768   1019   -315   1966       C  
ATOM    445  N   GLY A  98     -21.623  23.716 -29.773  1.00 57.65           N  
ANISOU  445  N   GLY A  98     8429   6846   6629    713    -40   2052       N  
ATOM    446  CA  GLY A  98     -20.237  24.145 -29.699  1.00 60.96           C  
ANISOU  446  CA  GLY A  98     8905   7162   7094    576    120   2091       C  
ATOM    447  C   GLY A  98     -19.668  24.226 -28.292  1.00 62.20           C  
ANISOU  447  C   GLY A  98     8976   7218   7439    456    178   1965       C  
ATOM    448  O   GLY A  98     -18.771  25.029 -28.030  1.00 62.16           O  
ANISOU  448  O   GLY A  98     9023   7063   7532    362    288   2010       O  
ATOM    449  N   GLY A  99     -20.183  23.397 -27.389  1.00 61.56           N  
ANISOU  449  N   GLY A  99     8765   7218   7409    457    100   1811       N  
ATOM    450  CA  GLY A  99     -19.719  23.385 -26.012  1.00 58.89           C  
ANISOU  450  CA  GLY A  99     8350   6803   7224    363    140   1683       C  
ATOM    451  C   GLY A  99     -20.507  24.302 -25.092  1.00 58.62           C  
ANISOU  451  C   GLY A  99     8325   6631   7318    442    110   1664       C  
ATOM    452  O   GLY A  99     -20.343  24.260 -23.873  1.00 60.67           O  
ANISOU  452  O   GLY A  99     8525   6841   7688    395    123   1544       O  
ATOM    453  N   ALA A 100     -21.366  25.137 -25.668  1.00 58.68           N  
ANISOU  453  N   ALA A 100     8413   6579   7304    577     70   1782       N  
ATOM    454  CA  ALA A 100     -22.148  26.075 -24.869  1.00 60.57           C  
ANISOU  454  CA  ALA A 100     8671   6681   7660    679     46   1771       C  
ATOM    455  C   ALA A 100     -23.181  25.332 -24.033  1.00 58.49           C  
ANISOU  455  C   ALA A 100     8265   6537   7423    753    -35   1649       C  
ATOM    456  O   ALA A 100     -23.663  24.270 -24.426  1.00 57.71           O  
ANISOU  456  O   ALA A 100     8071   6618   7238    768   -106   1624       O  
ATOM    457  CB  ALA A 100     -22.824  27.105 -25.755  1.00 62.73           C  
ANISOU  457  CB  ALA A 100     9066   6868   7900    822     18   1935       C  
ATOM    458  N   TRP A 101     -23.495  25.895 -22.870  1.00 54.64           N  
ANISOU  458  N   TRP A 101     7765   5941   7054    796    -19   1574       N  
ATOM    459  CA  TRP A 101     -24.527  25.363 -21.987  1.00 53.05           C  
ANISOU  459  CA  TRP A 101     7431   5837   6888    881    -70   1477       C  
ATOM    460  C   TRP A 101     -25.572  26.447 -21.776  1.00 56.16           C  
ANISOU  460  C   TRP A 101     7865   6128   7345   1063    -94   1526       C  
ATOM    461  O   TRP A 101     -25.292  27.505 -21.194  1.00 56.71           O  
ANISOU  461  O   TRP A 101     8039   6007   7503   1085    -42   1515       O  
ATOM    462  CB  TRP A 101     -23.939  24.906 -20.655  1.00 49.63           C  
ANISOU  462  CB  TRP A 101     6940   5396   6520    782    -20   1324       C  
ATOM    463  CG  TRP A 101     -24.961  24.357 -19.715  1.00 49.85           C  
ANISOU  463  CG  TRP A 101     6837   5525   6577    866    -49   1238       C  
ATOM    464  CD1 TRP A 101     -25.519  24.985 -18.639  1.00 51.02           C  
ANISOU  464  CD1 TRP A 101     6986   5594   6804    969    -23   1180       C  
ATOM    465  CD2 TRP A 101     -25.559  23.061 -19.777  1.00 51.13           C  
ANISOU  465  CD2 TRP A 101     6850   5884   6692    857   -103   1206       C  
ATOM    466  NE1 TRP A 101     -26.414  24.150 -18.017  1.00 51.91           N  
ANISOU  466  NE1 TRP A 101     6950   5857   6918   1023    -42   1123       N  
ATOM    467  CE2 TRP A 101     -26.455  22.961 -18.696  1.00 52.21           C  
ANISOU  467  CE2 TRP A 101     6890   6058   6889    946    -95   1141       C  
ATOM    468  CE3 TRP A 101     -25.409  21.964 -20.631  1.00 52.61           C  
ANISOU  468  CE3 TRP A 101     6981   6215   6794    780   -156   1222       C  
ATOM    469  CZ2 TRP A 101     -27.203  21.814 -18.453  1.00 50.81           C  
ANISOU  469  CZ2 TRP A 101     6552   6050   6702    946   -132   1107       C  
ATOM    470  CZ3 TRP A 101     -26.155  20.829 -20.386  1.00 49.81           C  
ANISOU  470  CZ3 TRP A 101     6477   6016   6433    782   -209   1174       C  
ATOM    471  CH2 TRP A 101     -27.044  20.768 -19.310  1.00 50.30           C  
ANISOU  471  CH2 TRP A 101     6435   6106   6569    857   -195   1124       C  
ATOM    472  N   LEU A 102     -26.774  26.196 -22.272  1.00 55.83           N  
ANISOU  472  N   LEU A 102     7741   6208   7265   1197   -180   1579       N  
ATOM    473  CA  LEU A 102     -27.784  27.236 -22.302  1.00 57.51           C  
ANISOU  473  CA  LEU A 102     7990   6335   7527   1391   -210   1650       C  
ATOM    474  C   LEU A 102     -28.873  26.985 -21.265  1.00 59.39           C  
ANISOU  474  C   LEU A 102     8078   6653   7836   1504   -224   1562       C  
ATOM    475  O   LEU A 102     -29.809  27.773 -21.132  1.00 61.05           O  
ANISOU  475  O   LEU A 102     8288   6811   8097   1686   -244   1602       O  
ATOM    476  CB  LEU A 102     -28.385  27.335 -23.707  1.00 58.64           C  
ANISOU  476  CB  LEU A 102     8158   6547   7576   1489   -304   1795       C  
ATOM    477  N   LEU A 103     -28.736  25.890 -20.526  1.00 56.37           N  
ANISOU  477  N   LEU A 103     7568   6395   7455   1403   -205   1448       N  
ATOM    478  CA  LEU A 103     -29.730  25.500 -19.535  1.00 54.38           C  
ANISOU  478  CA  LEU A 103     7158   6241   7262   1492   -200   1375       C  
ATOM    479  C   LEU A 103     -29.279  25.928 -18.135  1.00 55.35           C  
ANISOU  479  C   LEU A 103     7335   6247   7449   1483    -98   1261       C  
ATOM    480  O   LEU A 103     -28.288  26.638 -17.994  1.00 54.37           O  
ANISOU  480  O   LEU A 103     7368   5951   7339   1419    -52   1242       O  
ATOM    481  CB  LEU A 103     -29.978  23.992 -19.616  1.00 53.30           C  
ANISOU  481  CB  LEU A 103     6848   6315   7087   1395   -247   1335       C  
ATOM    482  CG  LEU A 103     -30.281  23.506 -21.042  1.00 52.46           C  
ANISOU  482  CG  LEU A 103     6711   6319   6901   1387   -364   1425       C  
ATOM    483  CD1 LEU A 103     -30.503  22.013 -21.070  1.00 54.52           C  
ANISOU  483  CD1 LEU A 103     6813   6763   7139   1282   -419   1370       C  
ATOM    484  CD2 LEU A 103     -31.481  24.245 -21.648  1.00 53.94           C  
ANISOU  484  CD2 LEU A 103     6868   6519   7108   1583   -445   1527       C  
ATOM    485  N   SER A 104     -30.002  25.516 -17.102  1.00 52.95           N  
ANISOU  485  N   SER A 104     6903   6034   7182   1549    -64   1187       N  
ATOM    486  CA  SER A 104     -29.753  26.062 -15.772  1.00 51.68           C  
ANISOU  486  CA  SER A 104     6810   5762   7064   1590     25   1081       C  
ATOM    487  C   SER A 104     -28.478  25.506 -15.156  1.00 48.90           C  
ANISOU  487  C   SER A 104     6511   5385   6685   1404     67    979       C  
ATOM    488  O   SER A 104     -28.049  24.412 -15.500  1.00 48.83           O  
ANISOU  488  O   SER A 104     6429   5495   6630   1263     42    976       O  
ATOM    489  CB  SER A 104     -30.944  25.794 -14.851  1.00 53.11           C  
ANISOU  489  CB  SER A 104     6838   6062   7279   1734     66   1044       C  
ATOM    490  OG  SER A 104     -30.951  24.459 -14.406  1.00 51.52           O  
ANISOU  490  OG  SER A 104     6494   6031   7052   1623     81    998       O  
ATOM    491  N   PRO A 105     -27.846  26.285 -14.264  1.00 50.80           N  
ANISOU  491  N   PRO A 105     6884   5462   6954   1410    120    889       N  
ATOM    492  CA  PRO A 105     -26.653  25.804 -13.568  1.00 48.81           C  
ANISOU  492  CA  PRO A 105     6674   5189   6681   1248    147    781       C  
ATOM    493  C   PRO A 105     -26.955  24.647 -12.628  1.00 49.18           C  
ANISOU  493  C   PRO A 105     6589   5407   6691   1233    180    706       C  
ATOM    494  O   PRO A 105     -26.073  23.807 -12.425  1.00 48.28           O  
ANISOU  494  O   PRO A 105     6459   5343   6541   1081    178    654       O  
ATOM    495  CB  PRO A 105     -26.172  27.036 -12.798  1.00 51.85           C  
ANISOU  495  CB  PRO A 105     7230   5356   7117   1296    177    699       C  
ATOM    496  CG  PRO A 105     -27.352  27.905 -12.681  1.00 51.81           C  
ANISOU  496  CG  PRO A 105     7238   5299   7146   1517    190    733       C  
ATOM    497  CD  PRO A 105     -28.156  27.682 -13.921  1.00 52.50           C  
ANISOU  497  CD  PRO A 105     7230   5492   7227   1566    142    881       C  
ATOM    498  N   ARG A 106     -28.168  24.576 -12.082  1.00 46.24           N  
ANISOU  498  N   ARG A 106     6117   5125   6328   1387    214    711       N  
ATOM    499  CA  ARG A 106     -28.529  23.450 -11.213  1.00 45.70           C  
ANISOU  499  CA  ARG A 106     5916   5222   6227   1371    259    664       C  
ATOM    500  C   ARG A 106     -28.647  22.146 -12.016  1.00 45.00           C  
ANISOU  500  C   ARG A 106     5682   5296   6119   1247    207    730       C  
ATOM    501  O   ARG A 106     -28.300  21.061 -11.524  1.00 45.08           O  
ANISOU  501  O   ARG A 106     5633   5400   6096   1143    224    687       O  
ATOM    502  CB  ARG A 106     -29.841  23.723 -10.455  1.00 48.99           C  
ANISOU  502  CB  ARG A 106     6247   5703   6665   1572    327    666       C  
ATOM    503  CG  ARG A 106     -29.733  24.724  -9.286  1.00 57.03           C  
ANISOU  503  CG  ARG A 106     7406   6589   7675   1703    397    561       C  
ATOM    504  CD  ARG A 106     -28.470  24.486  -8.439  1.00 62.39           C  
ANISOU  504  CD  ARG A 106     8203   7205   8299   1578    407    437       C  
ATOM    505  NE  ARG A 106     -28.398  23.108  -7.957  1.00 66.07           N  
ANISOU  505  NE  ARG A 106     8551   7841   8713   1482    435    426       N  
ATOM    506  CZ  ARG A 106     -27.363  22.575  -7.307  1.00 63.02           C  
ANISOU  506  CZ  ARG A 106     8227   7449   8271   1363    432    338       C  
ATOM    507  NH1 ARG A 106     -26.273  23.285  -7.039  1.00 66.22           N  
ANISOU  507  NH1 ARG A 106     8796   7693   8671   1312    398    244       N  
ATOM    508  NH2 ARG A 106     -27.422  21.312  -6.922  1.00 50.23           N  
ANISOU  508  NH2 ARG A 106     6499   5980   6607   1293    459    347       N  
ATOM    509  N   LEU A 107     -29.146  22.237 -13.246  1.00 44.45           N  
ANISOU  509  N   LEU A 107     5565   5257   6068   1266    136    832       N  
ATOM    510  CA  LEU A 107     -29.180  21.046 -14.094  1.00 43.90           C  
ANISOU  510  CA  LEU A 107     5383   5323   5973   1146     68    880       C  
ATOM    511  C   LEU A 107     -27.749  20.630 -14.438  1.00 43.34           C  
ANISOU  511  C   LEU A 107     5412   5206   5852    971     49    841       C  
ATOM    512  O   LEU A 107     -27.427  19.450 -14.435  1.00 41.34           O  
ANISOU  512  O   LEU A 107     5092   5049   5568    855     34    816       O  
ATOM    513  CB  LEU A 107     -29.976  21.287 -15.365  1.00 43.03           C  
ANISOU  513  CB  LEU A 107     5221   5254   5876   1214    -21    989       C  
ATOM    514  CG  LEU A 107     -30.081  20.124 -16.354  1.00 41.95           C  
ANISOU  514  CG  LEU A 107     4983   5249   5706   1105   -114   1030       C  
ATOM    515  CD1 LEU A 107     -30.688  18.898 -15.705  1.00 41.60           C  
ANISOU  515  CD1 LEU A 107     4764   5350   5691   1060   -102   1000       C  
ATOM    516  CD2 LEU A 107     -30.880  20.534 -17.582  1.00 44.64           C  
ANISOU  516  CD2 LEU A 107     5293   5622   6048   1198   -215   1132       C  
ATOM    517  N   CYS A 108     -26.900  21.610 -14.740  1.00 42.54           N  
ANISOU  517  N   CYS A 108     5464   4950   5748    954     54    841       N  
ATOM    518  CA  CYS A 108     -25.482  21.318 -14.973  1.00 41.10           C  
ANISOU  518  CA  CYS A 108     5363   4721   5533    792     53    803       C  
ATOM    519  C   CYS A 108     -24.869  20.576 -13.797  1.00 41.40           C  
ANISOU  519  C   CYS A 108     5380   4793   5557    715     94    692       C  
ATOM    520  O   CYS A 108     -24.211  19.542 -13.987  1.00 41.70           O  
ANISOU  520  O   CYS A 108     5381   4907   5557    593     76    670       O  
ATOM    521  CB  CYS A 108     -24.690  22.602 -15.251  1.00 42.18           C  
ANISOU  521  CB  CYS A 108     5659   4671   5698    783     69    817       C  
ATOM    522  SG  CYS A 108     -22.918  22.257 -15.424  1.00 45.58           S  
ANISOU  522  SG  CYS A 108     6155   5055   6109    580     82    770       S  
ATOM    523  N   ASP A 109     -25.093  21.077 -12.582  1.00 41.66           N  
ANISOU  523  N   ASP A 109     5445   4773   5611    800    147    621       N  
ATOM    524  CA  ASP A 109     -24.598  20.386 -11.375  1.00 40.39           C  
ANISOU  524  CA  ASP A 109     5275   4653   5419    751    183    518       C  
ATOM    525  C   ASP A 109     -25.104  18.934 -11.278  1.00 42.07           C  
ANISOU  525  C   ASP A 109     5343   5038   5602    712    181    538       C  
ATOM    526  O   ASP A 109     -24.340  18.013 -10.941  1.00 39.45           O  
ANISOU  526  O   ASP A 109     5002   4751   5235    605    177    489       O  
ATOM    527  CB  ASP A 109     -25.000  21.133 -10.104  1.00 43.42           C  
ANISOU  527  CB  ASP A 109     5715   4974   5809    884    241    445       C  
ATOM    528  CG  ASP A 109     -24.294  22.483  -9.953  1.00 45.65           C  
ANISOU  528  CG  ASP A 109     6162   5058   6126    900    234    390       C  
ATOM    529  OD1 ASP A 109     -23.179  22.659 -10.478  1.00 45.09           O  
ANISOU  529  OD1 ASP A 109     6155   4904   6073    770    197    383       O  
ATOM    530  OD2 ASP A 109     -24.858  23.369  -9.284  1.00 46.15           O  
ANISOU  530  OD2 ASP A 109     6288   5043   6205   1044    268    352       O  
ATOM    531  N   ALA A 110     -26.394  18.742 -11.545  1.00 38.42           N  
ANISOU  531  N   ALA A 110     4765   4666   5164    798    181    611       N  
ATOM    532  CA  ALA A 110     -26.976  17.401 -11.586  1.00 37.94           C  
ANISOU  532  CA  ALA A 110     4558   4756   5101    749    169    643       C  
ATOM    533  C   ALA A 110     -26.263  16.498 -12.600  1.00 37.32           C  
ANISOU  533  C   ALA A 110     4471   4713   4994    602     93    657       C  
ATOM    534  O   ALA A 110     -25.889  15.358 -12.286  1.00 37.83           O  
ANISOU  534  O   ALA A 110     4497   4839   5035    510     91    626       O  
ATOM    535  CB  ALA A 110     -28.467  17.492 -11.907  1.00 37.52           C  
ANISOU  535  CB  ALA A 110     4370   4786   5102    858    162    726       C  
ATOM    536  N   LEU A 111     -26.058  17.015 -13.805  1.00 38.64           N  
ANISOU  536  N   LEU A 111     4687   4838   5157    591     36    706       N  
ATOM    537  CA  LEU A 111     -25.434  16.246 -14.873  1.00 37.89           C  
ANISOU  537  CA  LEU A 111     4595   4781   5019    477    -30    721       C  
ATOM    538  C   LEU A 111     -24.009  15.854 -14.540  1.00 37.73           C  
ANISOU  538  C   LEU A 111     4649   4722   4963    365     -7    647       C  
ATOM    539  O   LEU A 111     -23.599  14.721 -14.780  1.00 36.72           O  
ANISOU  539  O   LEU A 111     4487   4661   4804    276    -36    626       O  
ATOM    540  CB  LEU A 111     -25.432  17.040 -16.168  1.00 38.07           C  
ANISOU  540  CB  LEU A 111     4680   4759   5025    507    -79    795       C  
ATOM    541  CG  LEU A 111     -26.607  16.753 -17.091  1.00 46.20           C  
ANISOU  541  CG  LEU A 111     5614   5883   6058    563   -162    872       C  
ATOM    542  CD1 LEU A 111     -26.539  17.728 -18.239  1.00 44.90           C  
ANISOU  542  CD1 LEU A 111     5542   5657   5862    616   -200    950       C  
ATOM    543  CD2 LEU A 111     -26.546  15.321 -17.599  1.00 42.51           C  
ANISOU  543  CD2 LEU A 111     5074   5522   5555    461   -230    853       C  
ATOM    544  N   MET A 112     -23.263  16.811 -14.001  1.00 36.14           N  
ANISOU  544  N   MET A 112     4550   4409   4774    374     39    605       N  
ATOM    545  CA  MET A 112     -21.875  16.578 -13.654  1.00 36.96           C  
ANISOU  545  CA  MET A 112     4713   4473   4858    271     53    532       C  
ATOM    546  C   MET A 112     -21.753  15.557 -12.519  1.00 37.33           C  
ANISOU  546  C   MET A 112     4713   4584   4886    246     71    460       C  
ATOM    547  O   MET A 112     -20.844  14.721 -12.539  1.00 36.53           O  
ANISOU  547  O   MET A 112     4610   4514   4757    155     56    420       O  
ATOM    548  CB  MET A 112     -21.196  17.889 -13.282  1.00 35.97           C  
ANISOU  548  CB  MET A 112     4696   4201   4768    283     84    498       C  
ATOM    549  CG  MET A 112     -21.055  18.819 -14.473  1.00 37.05           C  
ANISOU  549  CG  MET A 112     4897   4260   4922    282     74    582       C  
ATOM    550  SD  MET A 112     -19.992  20.244 -14.191  1.00 40.27           S  
ANISOU  550  SD  MET A 112     5435   4473   5393    244    103    548       S  
ATOM    551  CE  MET A 112     -20.727  21.003 -12.734  1.00 41.71           C  
ANISOU  551  CE  MET A 112     5659   4578   5612    373    124    468       C  
ATOM    552  N   ALA A 113     -22.651  15.616 -11.534  1.00 32.05           N  
ANISOU  552  N   ALA A 113     4010   3940   4229    336    109    451       N  
ATOM    553  CA  ALA A 113     -22.602  14.641 -10.445  1.00 31.50           C  
ANISOU  553  CA  ALA A 113     3905   3934   4130    321    136    402       C  
ATOM    554  C   ALA A 113     -22.827  13.225 -10.992  1.00 32.41           C  
ANISOU  554  C   ALA A 113     3928   4150   4237    246     99    440       C  
ATOM    555  O   ALA A 113     -22.138  12.270 -10.599  1.00 31.96           O  
ANISOU  555  O   ALA A 113     3875   4120   4149    178     92    399       O  
ATOM    556  CB  ALA A 113     -23.617  14.969  -9.377  1.00 32.88           C  
ANISOU  556  CB  ALA A 113     4055   4127   4309    441    202    403       C  
ATOM    557  N   MET A 114     -23.786  13.094 -11.899  1.00 37.52           N  
ANISOU  557  N   MET A 114     4498   4846   4913    263     63    515       N  
ATOM    558  CA  MET A 114     -24.052  11.805 -12.547  1.00 36.01           C  
ANISOU  558  CA  MET A 114     4226   4734   4721    188      6    543       C  
ATOM    559  C   MET A 114     -22.854  11.343 -13.376  1.00 35.10           C  
ANISOU  559  C   MET A 114     4173   4603   4561     95    -43    509       C  
ATOM    560  O   MET A 114     -22.445  10.182 -13.310  1.00 36.72           O  
ANISOU  560  O   MET A 114     4363   4842   4748     26    -65    480       O  
ATOM    561  CB  MET A 114     -25.299  11.900 -13.428  1.00 35.71           C  
ANISOU  561  CB  MET A 114     4096   4747   4725    229    -44    620       C  
ATOM    562  CG  MET A 114     -25.745  10.564 -14.002  1.00 38.77           C  
ANISOU  562  CG  MET A 114     4393   5210   5128    153   -117    639       C  
ATOM    563  SD  MET A 114     -26.203   9.372 -12.711  1.00 48.67           S  
ANISOU  563  SD  MET A 114     5559   6513   6422    116    -61    637       S  
ATOM    564  CE  MET A 114     -27.605  10.202 -11.971  1.00 52.91           C  
ANISOU  564  CE  MET A 114     5991   7088   7024    240     16    701       C  
ATOM    565  N   ASP A 115     -22.310  12.261 -14.164  1.00 35.08           N  
ANISOU  565  N   ASP A 115     4240   4545   4542    100    -52    519       N  
ATOM    566  CA  ASP A 115     -21.098  12.030 -14.944  1.00 34.14           C  
ANISOU  566  CA  ASP A 115     4180   4413   4380     25    -72    495       C  
ATOM    567  C   ASP A 115     -19.996  11.443 -14.057  1.00 35.80           C  
ANISOU  567  C   ASP A 115     4413   4614   4577    -31    -46    415       C  
ATOM    568  O   ASP A 115     -19.447  10.378 -14.347  1.00 32.84           O  
ANISOU  568  O   ASP A 115     4027   4279   4171    -88    -74    387       O  
ATOM    569  CB  ASP A 115     -20.649  13.357 -15.567  1.00 33.12           C  
ANISOU  569  CB  ASP A 115     4127   4205   4250     44    -52    528       C  
ATOM    570  CG  ASP A 115     -19.841  13.196 -16.848  1.00 36.74           C  
ANISOU  570  CG  ASP A 115     4627   4677   4655    -11    -71    551       C  
ATOM    571  OD1 ASP A 115     -19.953  12.162 -17.536  1.00 36.29           O  
ANISOU  571  OD1 ASP A 115     4540   4696   4551    -37   -121    550       O  
ATOM    572  OD2 ASP A 115     -19.082  14.142 -17.175  1.00 37.90           O  
ANISOU  572  OD2 ASP A 115     4840   4753   4807    -27    -32    570       O  
ATOM    573  N   VAL A 116     -19.688  12.133 -12.963  1.00 31.28           N  
ANISOU  573  N   VAL A 116     3876   3984   4023     -4     -1    373       N  
ATOM    574  CA  VAL A 116     -18.626  11.683 -12.064  1.00 31.10           C  
ANISOU  574  CA  VAL A 116     3878   3953   3984    -44      9    294       C  
ATOM    575  C   VAL A 116     -18.982  10.322 -11.452  1.00 30.33           C  
ANISOU  575  C   VAL A 116     3732   3925   3866    -51      0    284       C  
ATOM    576  O   VAL A 116     -18.138   9.421 -11.368  1.00 28.95           O  
ANISOU  576  O   VAL A 116     3562   3771   3667   -100    -21    243       O  
ATOM    577  CB  VAL A 116     -18.364  12.707 -10.940  1.00 32.21           C  
ANISOU  577  CB  VAL A 116     4076   4020   4142     -1     43    240       C  
ATOM    578  CG1 VAL A 116     -17.444  12.100  -9.875  1.00 32.26           C  
ANISOU  578  CG1 VAL A 116     4101   4038   4120    -26     35    157       C  
ATOM    579  CG2 VAL A 116     -17.754  13.970 -11.523  1.00 30.65           C  
ANISOU  579  CG2 VAL A 116     3935   3729   3981    -21     47    244       C  
ATOM    580  N   MET A 117     -20.231  10.162 -11.036  1.00 34.01           N  
ANISOU  580  N   MET A 117     4149   4424   4349      0     19    328       N  
ATOM    581  CA  MET A 117     -20.619   8.923 -10.370  1.00 33.52           C  
ANISOU  581  CA  MET A 117     4042   4414   4279    -12     24    336       C  
ATOM    582  C   MET A 117     -20.507   7.712 -11.300  1.00 32.08           C  
ANISOU  582  C   MET A 117     3827   4267   4097    -86    -37    348       C  
ATOM    583  O   MET A 117     -20.047   6.641 -10.884  1.00 31.62           O  
ANISOU  583  O   MET A 117     3776   4218   4021   -121    -48    322       O  
ATOM    584  CB  MET A 117     -22.053   9.007  -9.820  1.00 32.53           C  
ANISOU  584  CB  MET A 117     3847   4325   4187     51     71    397       C  
ATOM    585  CG  MET A 117     -22.434   7.758  -8.985  1.00 34.58           C  
ANISOU  585  CG  MET A 117     4063   4629   4444     31     97    420       C  
ATOM    586  SD  MET A 117     -24.118   7.825  -8.387  1.00 39.63           S  
ANISOU  586  SD  MET A 117     4594   5327   5136     97    171    509       S  
ATOM    587  CE  MET A 117     -24.979   7.723  -9.956  1.00 43.35           C  
ANISOU  587  CE  MET A 117     4962   5825   5684     53     85    564       C  
ATOM    588  N   LEU A 118     -20.954   7.863 -12.543  1.00 32.60           N  
ANISOU  588  N   LEU A 118     3865   4346   4177    -98    -83    385       N  
ATOM    589  CA  LEU A 118     -21.043   6.712 -13.446  1.00 30.80           C  
ANISOU  589  CA  LEU A 118     3611   4148   3943   -156   -154    389       C  
ATOM    590  C   LEU A 118     -19.651   6.305 -13.917  1.00 32.71           C  
ANISOU  590  C   LEU A 118     3919   4377   4133   -196   -173    328       C  
ATOM    591  O   LEU A 118     -19.353   5.114 -14.077  1.00 33.43           O  
ANISOU  591  O   LEU A 118     4014   4478   4211   -235   -212    300       O  
ATOM    592  CB  LEU A 118     -21.949   7.015 -14.643  1.00 30.83           C  
ANISOU  592  CB  LEU A 118     3574   4178   3961   -145   -212    439       C  
ATOM    593  CG  LEU A 118     -23.450   7.168 -14.325  1.00 32.57           C  
ANISOU  593  CG  LEU A 118     3694   4432   4251   -109   -211    503       C  
ATOM    594  CD1 LEU A 118     -24.242   7.610 -15.551  1.00 34.16           C  
ANISOU  594  CD1 LEU A 118     3858   4662   4460    -83   -285    549       C  
ATOM    595  CD2 LEU A 118     -24.008   5.865 -13.762  1.00 33.96           C  
ANISOU  595  CD2 LEU A 118     3797   4630   4474   -162   -222    514       C  
ATOM    596  N   CYS A 119     -18.797   7.295 -14.127  1.00 34.02           N  
ANISOU  596  N   CYS A 119     4134   4515   4277   -185   -142    310       N  
ATOM    597  CA  CYS A 119     -17.404   7.022 -14.460  1.00 33.03           C  
ANISOU  597  CA  CYS A 119     4050   4385   4114   -218   -141    256       C  
ATOM    598  C   CYS A 119     -16.737   6.297 -13.295  1.00 32.15           C  
ANISOU  598  C   CYS A 119     3944   4269   4003   -226   -131    201       C  
ATOM    599  O   CYS A 119     -16.070   5.276 -13.473  1.00 32.21           O  
ANISOU  599  O   CYS A 119     3959   4291   3987   -247   -158    163       O  
ATOM    600  CB  CYS A 119     -16.667   8.327 -14.789  1.00 33.15           C  
ANISOU  600  CB  CYS A 119     4100   4365   4130   -217   -100    261       C  
ATOM    601  SG  CYS A 119     -14.939   8.074 -15.260  1.00 34.65           S  
ANISOU  601  SG  CYS A 119     4310   4565   4291   -261    -83    208       S  
ATOM    602  N   THR A 120     -16.932   6.821 -12.095  1.00 28.45           N  
ANISOU  602  N   THR A 120     3480   3779   3553   -195    -95    196       N  
ATOM    603  CA  THR A 120     -16.359   6.228 -10.901  1.00 30.11           C  
ANISOU  603  CA  THR A 120     3707   3987   3747   -187    -90    149       C  
ATOM    604  C   THR A 120     -16.911   4.814 -10.650  1.00 30.65           C  
ANISOU  604  C   THR A 120     3757   4077   3813   -196   -111    172       C  
ATOM    605  O   THR A 120     -16.152   3.893 -10.318  1.00 29.16           O  
ANISOU  605  O   THR A 120     3590   3888   3602   -204   -133    136       O  
ATOM    606  CB  THR A 120     -16.607   7.131  -9.688  1.00 31.30           C  
ANISOU  606  CB  THR A 120     3880   4112   3899   -137    -49    138       C  
ATOM    607  OG1 THR A 120     -16.029   8.432  -9.953  1.00 31.34           O  
ANISOU  607  OG1 THR A 120     3912   4074   3924   -140    -40    111       O  
ATOM    608  CG2 THR A 120     -15.968   6.542  -8.447  1.00 30.98           C  
ANISOU  608  CG2 THR A 120     3872   4077   3821   -116    -53     89       C  
ATOM    609  N   ALA A 121     -18.214   4.633 -10.844  1.00 31.24           N  
ANISOU  609  N   ALA A 121     3787   4164   3919   -198   -109    236       N  
ATOM    610  CA  ALA A 121     -18.814   3.322 -10.644  1.00 32.16           C  
ANISOU  610  CA  ALA A 121     3878   4287   4055   -226   -130    268       C  
ATOM    611  C   ALA A 121     -18.180   2.273 -11.570  1.00 31.93           C  
ANISOU  611  C   ALA A 121     3871   4247   4013   -269   -198    230       C  
ATOM    612  O   ALA A 121     -17.951   1.126 -11.162  1.00 30.65           O  
ANISOU  612  O   ALA A 121     3730   4065   3851   -284   -217    221       O  
ATOM    613  CB  ALA A 121     -20.354   3.390 -10.854  1.00 31.90           C  
ANISOU  613  CB  ALA A 121     3765   4274   4080   -232   -125    344       C  
ATOM    614  N   SER A 122     -17.895   2.660 -12.806  1.00 33.15           N  
ANISOU  614  N   SER A 122     4032   4413   4151   -278   -230    209       N  
ATOM    615  CA  SER A 122     -17.322   1.721 -13.754  1.00 33.89           C  
ANISOU  615  CA  SER A 122     4156   4504   4216   -301   -288    166       C  
ATOM    616  C   SER A 122     -15.972   1.245 -13.253  1.00 33.55           C  
ANISOU  616  C   SER A 122     4155   4451   4142   -284   -276    106       C  
ATOM    617  O   SER A 122     -15.707   0.035 -13.210  1.00 33.21           O  
ANISOU  617  O   SER A 122     4139   4384   4096   -289   -314     79       O  
ATOM    618  CB  SER A 122     -17.197   2.351 -15.139  1.00 33.86           C  
ANISOU  618  CB  SER A 122     4162   4527   4176   -297   -308    161       C  
ATOM    619  OG  SER A 122     -18.496   2.595 -15.675  1.00 36.83           O  
ANISOU  619  OG  SER A 122     4498   4916   4580   -306   -346    213       O  
ATOM    620  N   ILE A 123     -15.143   2.203 -12.853  1.00 32.06           N  
ANISOU  620  N   ILE A 123     3969   4273   3939   -262   -231     84       N  
ATOM    621  CA  ILE A 123     -13.809   1.903 -12.343  1.00 31.73           C  
ANISOU  621  CA  ILE A 123     3946   4233   3876   -242   -227     24       C  
ATOM    622  C   ILE A 123     -13.875   1.090 -11.067  1.00 33.05           C  
ANISOU  622  C   ILE A 123     4134   4378   4045   -221   -236     26       C  
ATOM    623  O   ILE A 123     -13.147   0.102 -10.922  1.00 32.91           O  
ANISOU  623  O   ILE A 123     4141   4352   4012   -203   -266    -10       O  
ATOM    624  CB  ILE A 123     -12.989   3.198 -12.083  1.00 32.09           C  
ANISOU  624  CB  ILE A 123     3979   4287   3927   -237   -188      1       C  
ATOM    625  CG1 ILE A 123     -13.149   4.127 -13.280  1.00 36.35           C  
ANISOU  625  CG1 ILE A 123     4508   4835   4467   -259   -166     30       C  
ATOM    626  CG2 ILE A 123     -11.531   2.839 -11.835  1.00 33.41           C  
ANISOU  626  CG2 ILE A 123     4140   4470   4084   -223   -199    -65       C  
ATOM    627  CD1 ILE A 123     -12.536   5.525 -13.203  1.00 37.41           C  
ANISOU  627  CD1 ILE A 123     4632   4955   4626   -272   -124     26       C  
ATOM    628  N   PHE A 124     -14.740   1.492 -10.141  1.00 29.09           N  
ANISOU  628  N   PHE A 124     3627   3870   3556   -213   -204     72       N  
ATOM    629  CA  PHE A 124     -14.852   0.792  -8.870  1.00 29.97           C  
ANISOU  629  CA  PHE A 124     3768   3966   3652   -185   -196     90       C  
ATOM    630  C   PHE A 124     -15.362  -0.642  -9.095  1.00 31.33           C  
ANISOU  630  C   PHE A 124     3951   4105   3847   -212   -228    125       C  
ATOM    631  O   PHE A 124     -14.974  -1.559  -8.361  1.00 32.19           O  
ANISOU  631  O   PHE A 124     4104   4189   3938   -189   -240    126       O  
ATOM    632  CB  PHE A 124     -15.763   1.534  -7.880  1.00 30.41           C  
ANISOU  632  CB  PHE A 124     3817   4031   3705   -159   -138    138       C  
ATOM    633  CG  PHE A 124     -15.117   2.751  -7.235  1.00 32.28           C  
ANISOU  633  CG  PHE A 124     4075   4277   3912   -118   -120     86       C  
ATOM    634  CD1 PHE A 124     -13.853   3.177  -7.618  1.00 29.80           C  
ANISOU  634  CD1 PHE A 124     3763   3965   3595   -126   -154     13       C  
ATOM    635  CD2 PHE A 124     -15.774   3.450  -6.235  1.00 33.16           C  
ANISOU  635  CD2 PHE A 124     4203   4394   4001    -71    -68    108       C  
ATOM    636  CE1 PHE A 124     -13.249   4.303  -7.026  1.00 30.43           C  
ANISOU  636  CE1 PHE A 124     3857   4038   3665   -105   -152    -41       C  
ATOM    637  CE2 PHE A 124     -15.187   4.591  -5.632  1.00 33.45           C  
ANISOU  637  CE2 PHE A 124     4275   4424   4012    -33    -67     44       C  
ATOM    638  CZ  PHE A 124     -13.918   5.009  -6.024  1.00 31.02           C  
ANISOU  638  CZ  PHE A 124     3966   4105   3716    -58   -117    -32       C  
ATOM    639  N   ASN A 125     -16.188  -0.853 -10.117  1.00 30.70           N  
ANISOU  639  N   ASN A 125     3839   4018   3807   -260   -252    151       N  
ATOM    640  CA  ASN A 125     -16.598  -2.218 -10.429  1.00 32.90           C  
ANISOU  640  CA  ASN A 125     4134   4248   4120   -298   -300    168       C  
ATOM    641  C   ASN A 125     -15.483  -3.063 -11.036  1.00 33.17           C  
ANISOU  641  C   ASN A 125     4222   4256   4125   -280   -356     93       C  
ATOM    642  O   ASN A 125     -15.404  -4.247 -10.744  1.00 33.77           O  
ANISOU  642  O   ASN A 125     4342   4274   4216   -281   -387     97       O  
ATOM    643  CB  ASN A 125     -17.799  -2.227 -11.353  1.00 34.03           C  
ANISOU  643  CB  ASN A 125     4223   4389   4317   -356   -333    204       C  
ATOM    644  CG  ASN A 125     -19.108  -2.135 -10.584  1.00 37.52           C  
ANISOU  644  CG  ASN A 125     4603   4835   4820   -383   -286    297       C  
ATOM    645  OD1 ASN A 125     -19.659  -3.146 -10.119  1.00 37.38           O  
ANISOU  645  OD1 ASN A 125     4581   4771   4852   -423   -290    349       O  
ATOM    646  ND2 ASN A 125     -19.596  -0.916 -10.415  1.00 38.97           N  
ANISOU  646  ND2 ASN A 125     4737   5069   5001   -356   -234    325       N  
ATOM    647  N   LEU A 126     -14.622  -2.476 -11.865  1.00 33.28           N  
ANISOU  647  N   LEU A 126     4234   4311   4101   -257   -360     31       N  
ATOM    648  CA  LEU A 126     -13.455  -3.226 -12.356  1.00 34.28           C  
ANISOU  648  CA  LEU A 126     4402   4429   4194   -218   -394    -42       C  
ATOM    649  C   LEU A 126     -12.579  -3.593 -11.187  1.00 34.17           C  
ANISOU  649  C   LEU A 126     4412   4405   4165   -166   -386    -56       C  
ATOM    650  O   LEU A 126     -12.034  -4.700 -11.136  1.00 37.87           O  
ANISOU  650  O   LEU A 126     4928   4832   4628   -131   -424    -86       O  
ATOM    651  CB  LEU A 126     -12.653  -2.431 -13.382  1.00 34.18           C  
ANISOU  651  CB  LEU A 126     4368   4476   4143   -201   -376    -90       C  
ATOM    652  CG  LEU A 126     -13.433  -2.253 -14.677  1.00 31.93           C  
ANISOU  652  CG  LEU A 126     4082   4201   3847   -233   -400    -81       C  
ATOM    653  CD1 LEU A 126     -12.676  -1.300 -15.600  1.00 33.91           C  
ANISOU  653  CD1 LEU A 126     4318   4516   4051   -214   -358   -103       C  
ATOM    654  CD2 LEU A 126     -13.617  -3.602 -15.344  1.00 32.51           C  
ANISOU  654  CD2 LEU A 126     4213   4225   3915   -232   -474   -121       C  
ATOM    655  N   CYS A 127     -12.449  -2.669 -10.240  1.00 32.87           N  
ANISOU  655  N   CYS A 127     4223   4275   3992   -153   -344    -38       N  
ATOM    656  CA ACYS A 127     -11.751  -2.936  -8.982  0.53 34.98           C  
ANISOU  656  CA ACYS A 127     4518   4539   4232    -97   -348    -48       C  
ATOM    657  CA BCYS A 127     -11.707  -2.963  -9.023  0.47 34.69           C  
ANISOU  657  CA BCYS A 127     4483   4503   4196    -97   -349    -51       C  
ATOM    658  C   CYS A 127     -12.374  -4.082  -8.209  1.00 37.18           C  
ANISOU  658  C   CYS A 127     4855   4756   4517    -92   -358     13       C  
ATOM    659  O   CYS A 127     -11.683  -4.974  -7.723  1.00 36.61           O  
ANISOU  659  O   CYS A 127     4831   4653   4424    -39   -392     -2       O  
ATOM    660  CB ACYS A 127     -11.749  -1.703  -8.091  0.53 35.38           C  
ANISOU  660  CB ACYS A 127     4548   4629   4266    -87   -310    -42       C  
ATOM    661  CB BCYS A 127     -11.554  -1.709  -8.169  0.47 36.03           C  
ANISOU  661  CB BCYS A 127     4627   4714   4347    -83   -315    -53       C  
ATOM    662  SG ACYS A 127     -10.527  -0.505  -8.543  0.53 32.18           S  
ANISOU  662  SG ACYS A 127     4087   4277   3863    -85   -309   -120       S  
ATOM    663  SG BCYS A 127     -10.187  -1.808  -7.001  0.47 41.62           S  
ANISOU  663  SG BCYS A 127     5356   5446   5011     -5   -352   -111       S  
ATOM    664  N   ALA A 128     -13.698  -4.029  -8.067  1.00 31.91           N  
ANISOU  664  N   ALA A 128     4174   4067   3882   -144   -326     90       N  
ATOM    665  CA  ALA A 128     -14.439  -5.057  -7.332  1.00 34.76           C  
ANISOU  665  CA  ALA A 128     4576   4366   4265   -158   -317    172       C  
ATOM    666  C   ALA A 128     -14.257  -6.459  -7.922  1.00 34.93           C  
ANISOU  666  C   ALA A 128     4648   4302   4321   -172   -381    157       C  
ATOM    667  O   ALA A 128     -14.183  -7.435  -7.186  1.00 35.26           O  
ANISOU  667  O   ALA A 128     4755   4281   4363   -150   -388    200       O  
ATOM    668  CB  ALA A 128     -15.930  -4.715  -7.286  1.00 33.17           C  
ANISOU  668  CB  ALA A 128     4319   4168   4115   -223   -267    257       C  
ATOM    669  N   ILE A 129     -14.220  -6.554  -9.245  1.00 34.36           N  
ANISOU  669  N   ILE A 129     4559   4224   4273   -204   -427     98       N  
ATOM    670  CA  ILE A 129     -13.965  -7.829  -9.899  1.00 33.24           C  
ANISOU  670  CA  ILE A 129     4479   3997   4154   -203   -497     59       C  
ATOM    671  C   ILE A 129     -12.626  -8.376  -9.451  1.00 34.59           C  
ANISOU  671  C   ILE A 129     4708   4156   4277   -105   -517      9       C  
ATOM    672  O   ILE A 129     -12.511  -9.562  -9.127  1.00 37.36           O  
ANISOU  672  O   ILE A 129     5136   4413   4647    -83   -553     25       O  
ATOM    673  CB  ILE A 129     -13.968  -7.707 -11.428  1.00 35.39           C  
ANISOU  673  CB  ILE A 129     4735   4285   4427   -226   -543    -16       C  
ATOM    674  CG1 ILE A 129     -15.387  -7.407 -11.915  1.00 34.49           C  
ANISOU  674  CG1 ILE A 129     4567   4167   4370   -320   -552     35       C  
ATOM    675  CG2 ILE A 129     -13.456  -9.000 -12.071  1.00 35.34           C  
ANISOU  675  CG2 ILE A 129     4812   4191   4422   -194   -616    -84       C  
ATOM    676  CD1 ILE A 129     -15.478  -6.978 -13.362  1.00 33.54           C  
ANISOU  676  CD1 ILE A 129     4429   4088   4226   -333   -594    -28       C  
ATOM    677  N   SER A 130     -11.616  -7.512  -9.407  1.00 34.97           N  
ANISOU  677  N   SER A 130     4717   4295   4274    -47   -497    -47       N  
ATOM    678  CA  SER A 130     -10.280  -7.986  -9.057  1.00 36.43           C  
ANISOU  678  CA  SER A 130     4933   4487   4423     53   -525   -103       C  
ATOM    679  C   SER A 130     -10.257  -8.429  -7.596  1.00 37.55           C  
ANISOU  679  C   SER A 130     5128   4594   4543     97   -524    -37       C  
ATOM    680  O   SER A 130      -9.638  -9.427  -7.266  1.00 37.43           O  
ANISOU  680  O   SER A 130     5180   4524   4519    169   -567    -46       O  
ATOM    681  CB  SER A 130      -9.217  -6.913  -9.301  1.00 34.50           C  
ANISOU  681  CB  SER A 130     4611   4351   4146     90   -505   -171       C  
ATOM    682  OG  SER A 130      -9.331  -5.870  -8.352  1.00 35.68           O  
ANISOU  682  OG  SER A 130     4724   4553   4279     78   -471   -140       O  
ATOM    683  N   VAL A 131     -10.940  -7.689  -6.724  1.00 33.35           N  
ANISOU  683  N   VAL A 131     4579   4097   3997     65   -474     30       N  
ATOM    684  CA  VAL A 131     -11.031  -8.089  -5.313  1.00 33.43           C  
ANISOU  684  CA  VAL A 131     4654   4082   3966    113   -461    104       C  
ATOM    685  C   VAL A 131     -11.763  -9.445  -5.161  1.00 34.90           C  
ANISOU  685  C   VAL A 131     4919   4144   4196     84   -467    191       C  
ATOM    686  O   VAL A 131     -11.311 -10.340  -4.432  1.00 36.20           O  
ANISOU  686  O   VAL A 131     5170   4251   4333    154   -492    224       O  
ATOM    687  CB  VAL A 131     -11.744  -7.001  -4.483  1.00 34.22           C  
ANISOU  687  CB  VAL A 131     4724   4244   4032     91   -392    157       C  
ATOM    688  CG1 VAL A 131     -12.135  -7.534  -3.117  1.00 34.75           C  
ANISOU  688  CG1 VAL A 131     4872   4282   4049    133   -359    257       C  
ATOM    689  CG2 VAL A 131     -10.835  -5.773  -4.346  1.00 33.17           C  
ANISOU  689  CG2 VAL A 131     4539   4207   3855    133   -403     69       C  
ATOM    690  N   ASP A 132     -12.872  -9.591  -5.882  1.00 36.14           N  
ANISOU  690  N   ASP A 132     5047   4256   4429    -21   -451    227       N  
ATOM    691  CA  ASP A 132     -13.708 -10.800  -5.846  1.00 37.62           C  
ANISOU  691  CA  ASP A 132     5291   4315   4689    -83   -459    310       C  
ATOM    692  C   ASP A 132     -12.974 -12.038  -6.378  1.00 38.33           C  
ANISOU  692  C   ASP A 132     5466   4296   4800    -39   -543    253       C  
ATOM    693  O   ASP A 132     -13.030 -13.118  -5.777  1.00 37.69           O  
ANISOU  693  O   ASP A 132     5478   4103   4740    -23   -556    322       O  
ATOM    694  CB  ASP A 132     -14.992 -10.568  -6.663  1.00 39.43           C  
ANISOU  694  CB  ASP A 132     5443   4533   5006   -210   -447    337       C  
ATOM    695  CG  ASP A 132     -15.893 -11.792  -6.714  1.00 41.93           C  
ANISOU  695  CG  ASP A 132     5798   4708   5424   -298   -468    417       C  
ATOM    696  OD1 ASP A 132     -16.576 -12.046  -5.691  1.00 44.41           O  
ANISOU  696  OD1 ASP A 132     6122   4994   5759   -327   -398    546       O  
ATOM    697  OD2 ASP A 132     -15.952 -12.472  -7.775  1.00 42.59           O  
ANISOU  697  OD2 ASP A 132     5904   4710   5570   -342   -551    352       O  
ATOM    698  N   ARG A 133     -12.309 -11.880  -7.515  1.00 36.67           N  
ANISOU  698  N   ARG A 133     5232   4116   4585    -14   -593    132       N  
ATOM    699  CA  ARG A 133     -11.602 -12.991  -8.115  1.00 38.50           C  
ANISOU  699  CA  ARG A 133     5545   4253   4829     45   -668     61       C  
ATOM    700  C   ARG A 133     -10.373 -13.352  -7.272  1.00 37.70           C  
ANISOU  700  C   ARG A 133     5498   4160   4666    185   -684     49       C  
ATOM    701  O   ARG A 133     -10.041 -14.522  -7.161  1.00 38.79           O  
ANISOU  701  O   ARG A 133     5736   4180   4823    242   -733     52       O  
ATOM    702  CB  ARG A 133     -11.224 -12.682  -9.565  1.00 38.63           C  
ANISOU  702  CB  ARG A 133     5522   4317   4838     50   -701    -63       C  
ATOM    703  CG  ARG A 133     -12.425 -12.715 -10.550  1.00 38.34           C  
ANISOU  703  CG  ARG A 133     5466   4238   4865    -73   -727    -63       C  
ATOM    704  CD  ARG A 133     -13.198 -14.068 -10.529  1.00 39.54           C  
ANISOU  704  CD  ARG A 133     5708   4210   5108   -138   -786    -20       C  
ATOM    705  NE  ARG A 133     -14.251 -14.097  -9.506  1.00 41.59           N  
ANISOU  705  NE  ARG A 133     5943   4431   5429   -230   -735    124       N  
ATOM    706  CZ  ARG A 133     -14.835 -15.199  -9.041  1.00 43.87           C  
ANISOU  706  CZ  ARG A 133     6302   4566   5801   -287   -755    206       C  
ATOM    707  NH1 ARG A 133     -14.485 -16.402  -9.486  1.00 44.83           N  
ANISOU  707  NH1 ARG A 133     6535   4537   5960   -261   -839    152       N  
ATOM    708  NH2 ARG A 133     -15.766 -15.099  -8.105  1.00 43.60           N  
ANISOU  708  NH2 ARG A 133     6228   4524   5814   -365   -683    349       N  
ATOM    709  N   PHE A 134      -9.715 -12.367  -6.659  1.00 38.45           N  
ANISOU  709  N   PHE A 134     5531   4386   4693    242   -653     34       N  
ATOM    710  CA  PHE A 134      -8.578 -12.690  -5.798  1.00 39.11           C  
ANISOU  710  CA  PHE A 134     5655   4486   4718    376   -686     23       C  
ATOM    711  C   PHE A 134      -9.021 -13.525  -4.598  1.00 40.69           C  
ANISOU  711  C   PHE A 134     5966   4588   4907    396   -681    147       C  
ATOM    712  O   PHE A 134      -8.393 -14.537  -4.265  1.00 40.10           O  
ANISOU  712  O   PHE A 134     5983   4432   4823    494   -733    154       O  
ATOM    713  CB  PHE A 134      -7.838 -11.445  -5.291  1.00 38.26           C  
ANISOU  713  CB  PHE A 134     5458   4531   4547    420   -670    -20       C  
ATOM    714  CG  PHE A 134      -6.696 -11.785  -4.371  1.00 40.25           C  
ANISOU  714  CG  PHE A 134     5744   4808   4742    559   -724    -35       C  
ATOM    715  CD1 PHE A 134      -5.560 -12.408  -4.865  1.00 46.33           C  
ANISOU  715  CD1 PHE A 134     6510   5573   5521    664   -784   -118       C  
ATOM    716  CD2 PHE A 134      -6.780 -11.549  -3.010  1.00 39.05           C  
ANISOU  716  CD2 PHE A 134     5633   4683   4520    599   -720     35       C  
ATOM    717  CE1 PHE A 134      -4.507 -12.769  -4.017  1.00 46.35           C  
ANISOU  717  CE1 PHE A 134     6534   5600   5477    804   -847   -130       C  
ATOM    718  CE2 PHE A 134      -5.728 -11.906  -2.157  1.00 42.11           C  
ANISOU  718  CE2 PHE A 134     6058   5095   4846    738   -789     20       C  
ATOM    719  CZ  PHE A 134      -4.595 -12.512  -2.667  1.00 40.43           C  
ANISOU  719  CZ  PHE A 134     5827   4879   4656    838   -857    -61       C  
ATOM    720  N   VAL A 135     -10.101 -13.097  -3.953  1.00 39.98           N  
ANISOU  720  N   VAL A 135     5868   4508   4816    312   -612    251       N  
ATOM    721  CA  VAL A 135     -10.660 -13.835  -2.822  1.00 39.26           C  
ANISOU  721  CA  VAL A 135     5878   4330   4710    318   -580    393       C  
ATOM    722  C   VAL A 135     -11.134 -15.230  -3.232  1.00 39.41           C  
ANISOU  722  C   VAL A 135     5987   4164   4823    270   -609    445       C  
ATOM    723  O   VAL A 135     -10.969 -16.174  -2.476  1.00 40.97           O  
ANISOU  723  O   VAL A 135     6300   4260   5006    330   -622    528       O  
ATOM    724  CB  VAL A 135     -11.825 -13.045  -2.168  1.00 39.62           C  
ANISOU  724  CB  VAL A 135     5878   4434   4741    233   -478    495       C  
ATOM    725  CG1 VAL A 135     -12.656 -13.929  -1.205  1.00 39.00           C  
ANISOU  725  CG1 VAL A 135     5895   4251   4672    208   -419    667       C  
ATOM    726  CG2 VAL A 135     -11.280 -11.810  -1.447  1.00 37.49           C  
ANISOU  726  CG2 VAL A 135     5564   4318   4362    307   -459    452       C  
ATOM    727  N   ALA A 136     -11.720 -15.365  -4.420  1.00 40.97           N  
ANISOU  727  N   ALA A 136     6142   4309   5115    164   -629    395       N  
ATOM    728  CA  ALA A 136     -12.205 -16.671  -4.876  1.00 43.54           C  
ANISOU  728  CA  ALA A 136     6556   4444   5544    105   -674    426       C  
ATOM    729  C   ALA A 136     -11.040 -17.623  -5.042  1.00 41.29           C  
ANISOU  729  C   ALA A 136     6377   4072   5239    242   -758    353       C  
ATOM    730  O   ALA A 136     -11.112 -18.794  -4.673  1.00 42.91           O  
ANISOU  730  O   ALA A 136     6706   4110   5487    259   -787    423       O  
ATOM    731  CB  ALA A 136     -12.979 -16.545  -6.188  1.00 42.42           C  
ANISOU  731  CB  ALA A 136     6346   4279   5493    -23   -703    358       C  
ATOM    732  N   VAL A 137      -9.948 -17.099  -5.586  1.00 43.63           N  
ANISOU  732  N   VAL A 137     6620   4482   5475    343   -793    217       N  
ATOM    733  CA  VAL A 137      -8.760 -17.910  -5.840  1.00 44.11           C  
ANISOU  733  CA  VAL A 137     6756   4487   5516    493   -867    132       C  
ATOM    734  C   VAL A 137      -8.001 -18.181  -4.544  1.00 42.88           C  
ANISOU  734  C   VAL A 137     6663   4341   5287    629   -876    200       C  
ATOM    735  O   VAL A 137      -7.569 -19.306  -4.300  1.00 42.79           O  
ANISOU  735  O   VAL A 137     6774   4195   5289    725   -929    221       O  
ATOM    736  CB  VAL A 137      -7.825 -17.229  -6.870  1.00 44.88           C  
ANISOU  736  CB  VAL A 137     6755   4721   5578    557   -885    -27       C  
ATOM    737  CG1 VAL A 137      -6.528 -18.028  -7.029  1.00 47.65           C  
ANISOU  737  CG1 VAL A 137     7163   5036   5905    735   -949   -111       C  
ATOM    738  CG2 VAL A 137      -8.537 -17.106  -8.208  1.00 46.21           C  
ANISOU  738  CG2 VAL A 137     6892   4867   5800    445   -890    -96       C  
ATOM    739  N   ALA A 138      -7.854 -17.163  -3.699  1.00 42.85           N  
ANISOU  739  N   ALA A 138     6587   4489   5203    646   -832    234       N  
ATOM    740  CA  ALA A 138      -7.033 -17.301  -2.489  1.00 43.44           C  
ANISOU  740  CA  ALA A 138     6717   4602   5187    792   -859    279       C  
ATOM    741  C   ALA A 138      -7.747 -18.009  -1.332  1.00 42.91           C  
ANISOU  741  C   ALA A 138     6782   4420   5100    782   -825    455       C  
ATOM    742  O   ALA A 138      -7.097 -18.595  -0.476  1.00 43.49           O  
ANISOU  742  O   ALA A 138     6954   4460   5109    918   -867    505       O  
ATOM    743  CB  ALA A 138      -6.544 -15.937  -2.031  1.00 41.06           C  
ANISOU  743  CB  ALA A 138     6297   4500   4802    818   -842    230       C  
ATOM    744  N   VAL A 139      -9.076 -17.949  -1.307  1.00 44.32           N  
ANISOU  744  N   VAL A 139     6960   4545   5334    626   -745    556       N  
ATOM    745  CA  VAL A 139      -9.852 -18.521  -0.205  1.00 44.77           C  
ANISOU  745  CA  VAL A 139     7125   4509   5376    599   -682    744       C  
ATOM    746  C   VAL A 139     -10.896 -19.518  -0.707  1.00 47.72           C  
ANISOU  746  C   VAL A 139     7555   4684   5893    458   -663    826       C  
ATOM    747  O   VAL A 139     -12.073 -19.188  -0.831  1.00 46.41           O  
ANISOU  747  O   VAL A 139     7321   4519   5792    303   -586    894       O  
ATOM    748  CB  VAL A 139     -10.572 -17.418   0.626  1.00 46.89           C  
ANISOU  748  CB  VAL A 139     7327   4920   5567    546   -577    823       C  
ATOM    749  CG1 VAL A 139     -11.165 -18.002   1.916  1.00 43.31           C  
ANISOU  749  CG1 VAL A 139     6997   4397   5060    561   -500   1024       C  
ATOM    750  CG2 VAL A 139      -9.617 -16.266   0.932  1.00 42.25           C  
ANISOU  750  CG2 VAL A 139     6665   4526   4862    653   -610    710       C  
ATOM    751  N   PRO A 140     -10.457 -20.747  -1.003  1.00 53.37           N  
ANISOU  751  N   PRO A 140     8391   5220   6665    515   -741    816       N  
ATOM    752  CA  PRO A 140     -11.354 -21.857  -1.351  1.00 56.49           C  
ANISOU  752  CA  PRO A 140     8870   5389   7206    388   -743    899       C  
ATOM    753  C   PRO A 140     -12.391 -22.127  -0.264  1.00 52.09           C  
ANISOU  753  C   PRO A 140     8362   4766   6663    297   -634   1123       C  
ATOM    754  O   PRO A 140     -12.013 -22.507   0.848  1.00 52.12           O  
ANISOU  754  O   PRO A 140     8481   4747   6574    411   -610   1241       O  
ATOM    755  CB  PRO A 140     -10.396 -23.057  -1.477  1.00 60.23           C  
ANISOU  755  CB  PRO A 140     9496   5697   7691    532   -846    858       C  
ATOM    756  CG  PRO A 140      -9.056 -22.441  -1.765  1.00 59.51           C  
ANISOU  756  CG  PRO A 140     9341   5774   7496    702   -907    692       C  
ATOM    757  CD  PRO A 140      -9.041 -21.158  -0.992  1.00 55.52           C  
ANISOU  757  CD  PRO A 140     8727   5494   6873    712   -838    721       C  
ATOM    758  N   LEU A 141     -13.673 -21.961  -0.571  1.00 54.02           N  
ANISOU  758  N   LEU A 141     8521   4984   7019    103   -566   1188       N  
ATOM    759  CA  LEU A 141     -14.710 -22.287   0.406  1.00 54.37           C  
ANISOU  759  CA  LEU A 141     8599   4963   7098      6   -446   1414       C  
ATOM    760  C   LEU A 141     -15.670 -23.352  -0.110  1.00 55.96           C  
ANISOU  760  C   LEU A 141     8831   4928   7505   -175   -459   1490       C  
ATOM    761  O   LEU A 141     -15.917 -23.447  -1.307  1.00 57.10           O  
ANISOU  761  O   LEU A 141     8913   5016   7766   -272   -544   1360       O  
ATOM    762  CB  LEU A 141     -15.495 -21.035   0.784  1.00 51.53           C  
ANISOU  762  CB  LEU A 141     8087   4807   6687    -62   -324   1460       C  
ATOM    763  CG  LEU A 141     -14.739 -19.925   1.516  1.00 49.18           C  
ANISOU  763  CG  LEU A 141     7766   4732   6189     96   -295   1411       C  
ATOM    764  CD1 LEU A 141     -15.695 -18.797   1.823  1.00 48.66           C  
ANISOU  764  CD1 LEU A 141     7562   4828   6099     14   -170   1462       C  
ATOM    765  CD2 LEU A 141     -14.130 -20.467   2.780  1.00 51.00           C  
ANISOU  765  CD2 LEU A 141     8159   4931   6287    249   -277   1532       C  
ATOM    766  N   ARG A 142     -16.218 -24.135   0.808  1.00 59.45           N  
ANISOU  766  N   ARG A 142     9369   5232   7986   -221   -376   1705       N  
ATOM    767  CA  ARG A 142     -17.209 -25.145   0.481  1.00 62.64           C  
ANISOU  767  CA  ARG A 142     9796   5402   8603   -415   -376   1809       C  
ATOM    768  C   ARG A 142     -18.425 -24.971   1.380  1.00 63.70           C  
ANISOU  768  C   ARG A 142     9855   5569   8777   -548   -198   2043       C  
ATOM    769  O   ARG A 142     -18.314 -25.054   2.601  1.00 65.58           O  
ANISOU  769  O   ARG A 142    10184   5837   8896   -458    -88   2215       O  
ATOM    770  CB  ARG A 142     -16.622 -26.558   0.641  1.00 61.67           C  
ANISOU  770  CB  ARG A 142     9892   5013   8528   -346   -456   1857       C  
ATOM    771  CG  ARG A 142     -17.549 -27.685   0.201  1.00 64.36           C  
ANISOU  771  CG  ARG A 142    10274   5070   9111   -553   -485   1941       C  
ATOM    772  CD  ARG A 142     -16.897 -29.066   0.379  1.00 65.15           C  
ANISOU  772  CD  ARG A 142    10613   4890   9253   -466   -569   1984       C  
ATOM    773  NE  ARG A 142     -17.562 -29.897   1.390  1.00 70.64           N  
ANISOU  773  NE  ARG A 142    11393   5425  10021   -547   -446   2251       N  
ATOM    774  CZ  ARG A 142     -17.432 -31.222   1.484  1.00 78.98           C  
ANISOU  774  CZ  ARG A 142    12575   6256  11177   -531   -463   2290       C  
ATOM    775  NH1 ARG A 142     -18.072 -31.900   2.436  1.00 81.99           N  
ANISOU  775  NH1 ARG A 142    12989   6548  11615   -594   -307   2521       N  
ATOM    776  NH2 ARG A 142     -16.665 -31.885   0.624  1.00 81.74           N  
ANISOU  776  NH2 ARG A 142    13023   6467  11569   -446   -626   2099       N  
ATOM    777  N   TYR A 143     -19.584 -24.737   0.776  1.00 57.56           N  
ANISOU  777  N   TYR A 143     8913   4795   8164   -755   -171   2052       N  
ATOM    778  CA  TYR A 143     -20.800 -24.491   1.544  1.00 58.54           C  
ANISOU  778  CA  TYR A 143     8926   4975   8341   -885     10   2268       C  
ATOM    779  C   TYR A 143     -21.614 -25.743   1.767  1.00 59.80           C  
ANISOU  779  C   TYR A 143     9141   4874   8704  -1060     49   2464       C  
ATOM    780  O   TYR A 143     -21.648 -26.623   0.909  1.00 62.16           O  
ANISOU  780  O   TYR A 143     9489   4954   9176  -1161    -89   2388       O  
ATOM    781  CB  TYR A 143     -21.679 -23.455   0.846  1.00 56.92           C  
ANISOU  781  CB  TYR A 143     8482   4939   8207  -1008     31   2187       C  
ATOM    782  CG  TYR A 143     -20.997 -22.146   0.509  1.00 55.12           C  
ANISOU  782  CG  TYR A 143     8182   4954   7807   -866     -6   1995       C  
ATOM    783  CD1 TYR A 143     -19.908 -21.684   1.238  1.00 52.97           C  
ANISOU  783  CD1 TYR A 143     8014   4803   7309   -651     11   1962       C  
ATOM    784  CD2 TYR A 143     -21.467 -21.363  -0.530  1.00 51.27           C  
ANISOU  784  CD2 TYR A 143     7522   4571   7389   -952    -62   1854       C  
ATOM    785  CE1 TYR A 143     -19.297 -20.476   0.918  1.00 52.00           C  
ANISOU  785  CE1 TYR A 143     7817   4888   7051   -541    -25   1790       C  
ATOM    786  CE2 TYR A 143     -20.873 -20.167  -0.854  1.00 52.07           C  
ANISOU  786  CE2 TYR A 143     7561   4878   7347   -834    -88   1695       C  
ATOM    787  CZ  TYR A 143     -19.790 -19.723  -0.134  1.00 51.76           C  
ANISOU  787  CZ  TYR A 143     7621   4945   7100   -637    -68   1662       C  
ATOM    788  OH  TYR A 143     -19.221 -18.517  -0.485  1.00 51.18           O  
ANISOU  788  OH  TYR A 143     7477   5063   6908   -540    -97   1505       O  
ATOM    789  N   ASN A 144     -22.270 -25.819   2.923  1.00 61.12           N  
ANISOU  789  N   ASN A 144     9306   5064   8851  -1094    241   2717       N  
ATOM    790  CA  ASN A 144     -23.226 -26.889   3.200  1.00 64.53           C  
ANISOU  790  CA  ASN A 144     9747   5329   9440  -1258    332   2850       C  
ATOM    791  C   ASN A 144     -24.445 -26.756   2.293  1.00 66.96           C  
ANISOU  791  C   ASN A 144     9823   5651   9967  -1488    315   2780       C  
ATOM    792  O   ASN A 144     -24.920 -27.734   1.715  1.00 66.49           O  
ANISOU  792  O   ASN A 144     9767   5400  10095  -1635    246   2741       O  
ATOM    793  CB  ASN A 144     -23.679 -26.859   4.663  1.00 64.64           C  
ANISOU  793  CB  ASN A 144     9803   5446   9313  -1218    555   3072       C  
ATOM    794  CG  ASN A 144     -22.584 -27.246   5.632  1.00 65.93           C  
ANISOU  794  CG  ASN A 144    10219   5567   9263  -1003    559   3155       C  
ATOM    795  OD1 ASN A 144     -21.750 -28.107   5.344  1.00 69.19           O  
ANISOU  795  OD1 ASN A 144    10808   5779   9701   -929    432   3104       O  
ATOM    796  ND2 ASN A 144     -22.588 -26.615   6.805  1.00 66.29           N  
ANISOU  796  ND2 ASN A 144    10280   5814   9093   -887    697   3275       N  
ATOM    797  N   ARG A 145     -24.946 -25.527   2.192  1.00 64.77           N  
ANISOU  797  N   ARG A 145     9345   5607   9658  -1507    376   2762       N  
ATOM    798  CA  ARG A 145     -26.143 -25.217   1.420  1.00 64.62           C  
ANISOU  798  CA  ARG A 145     9083   5649   9822  -1699    368   2704       C  
ATOM    799  C   ARG A 145     -25.825 -24.879  -0.026  1.00 62.93           C  
ANISOU  799  C   ARG A 145     8806   5414   9691  -1734    147   2476       C  
ATOM    800  O   ARG A 145     -24.800 -24.263  -0.323  1.00 62.28           O  
ANISOU  800  O   ARG A 145     8794   5395   9473  -1590     53   2363       O  
ATOM    801  CB  ARG A 145     -26.905 -24.049   2.051  1.00 65.42           C  
ANISOU  801  CB  ARG A 145     8995   6017   9843  -1686    551   2797       C  
ATOM    802  CG  ARG A 145     -27.493 -24.340   3.420  1.00 71.53           C  
ANISOU  802  CG  ARG A 145     9799   6838  10542  -1677    776   3010       C  
ATOM    803  CD  ARG A 145     -28.220 -23.114   3.980  1.00 78.37           C  
ANISOU  803  CD  ARG A 145    10479   7980  11318  -1639    948   3071       C  
ATOM    804  NE  ARG A 145     -29.399 -22.735   3.194  1.00 84.38           N  
ANISOU  804  NE  ARG A 145    10974   8815  12273  -1803    934   3014       N  
ATOM    805  CZ  ARG A 145     -29.495 -21.618   2.476  1.00 82.44           C  
ANISOU  805  CZ  ARG A 145    10568   8723  12032  -1783    877   2893       C  
ATOM    806  NH1 ARG A 145     -28.485 -20.756   2.444  1.00 80.05           N  
ANISOU  806  NH1 ARG A 145    10343   8515  11558  -1618    837   2819       N  
ATOM    807  NH2 ARG A 145     -30.603 -21.354   1.792  1.00 80.67           N  
ANISOU  807  NH2 ARG A 145    10109   8560  11983  -1924    855   2848       N  
ATOM    808  N   GLN A 146     -26.723 -25.274  -0.920  1.00 71.04           N  
ANISOU  808  N   GLN A 146     9701   6371  10921  -1916     63   2394       N  
ATOM    809  CA  GLN A 146     -26.581 -24.978  -2.339  1.00 70.78           C  
ANISOU  809  CA  GLN A 146     9605   6329  10959  -1958   -148   2171       C  
ATOM    810  C   GLN A 146     -26.757 -23.488  -2.605  1.00 65.73           C  
ANISOU  810  C   GLN A 146     8788   5940  10248  -1922   -126   2126       C  
ATOM    811  O   GLN A 146     -27.413 -22.775  -1.841  1.00 66.50           O  
ANISOU  811  O   GLN A 146     8748   6214  10304  -1919     55   2259       O  
ATOM    812  CB  GLN A 146     -27.593 -25.792  -3.155  1.00 74.35           C  
ANISOU  812  CB  GLN A 146     9959   6657  11635  -2155   -242   2102       C  
ATOM    813  N   GLY A 147     -26.159 -23.013  -3.690  1.00 60.79           N  
ANISOU  813  N   GLY A 147     8173   5351   9572  -1867   -297   1910       N  
ATOM    814  CA  GLY A 147     -26.295 -21.629  -4.054  1.00 63.22           C  
ANISOU  814  CA  GLY A 147     8326   5919   9776  -1799   -276   1811       C  
ATOM    815  C   GLY A 147     -25.106 -20.826  -3.574  1.00 64.14           C  
ANISOU  815  C   GLY A 147     8550   6195   9624  -1560   -221   1741       C  
ATOM    816  O   GLY A 147     -24.272 -21.323  -2.813  1.00 66.48           O  
ANISOU  816  O   GLY A 147     9023   6421   9814  -1446   -181   1795       O  
ATOM    817  N   GLY A 148     -25.036 -19.585  -4.033  1.00 57.49           N  
ANISOU  817  N   GLY A 148     7601   5562   8681  -1487   -228   1623       N  
ATOM    818  CA  GLY A 148     -23.972 -18.675  -3.658  1.00 59.38           C  
ANISOU  818  CA  GLY A 148     7912   5963   8686  -1281   -186   1544       C  
ATOM    819  C   GLY A 148     -24.336 -17.886  -2.416  1.00 56.43           C  
ANISOU  819  C   GLY A 148     7476   5753   8214  -1217     14   1695       C  
ATOM    820  O   GLY A 148     -25.450 -17.986  -1.899  1.00 53.68           O  
ANISOU  820  O   GLY A 148     7011   5409   7975  -1329    134   1864       O  
ATOM    821  N   SER A 149     -23.391 -17.092  -1.932  1.00 50.15           N  
ANISOU  821  N   SER A 149     6752   5091   7209  -1035     50   1632       N  
ATOM    822  CA  SER A 149     -23.604 -16.331  -0.706  1.00 48.87           C  
ANISOU  822  CA  SER A 149     6567   5081   6920   -946    228   1753       C  
ATOM    823  C   SER A 149     -24.196 -14.965  -1.001  1.00 43.77           C  
ANISOU  823  C   SER A 149     5749   4627   6256   -940    275   1699       C  
ATOM    824  O   SER A 149     -24.590 -14.251  -0.083  1.00 48.40           O  
ANISOU  824  O   SER A 149     6289   5343   6756   -876    427   1793       O  
ATOM    825  CB  SER A 149     -22.290 -16.157   0.056  1.00 46.40           C  
ANISOU  825  CB  SER A 149     6426   4813   6392   -750    231   1709       C  
ATOM    826  OG  SER A 149     -21.393 -15.406  -0.723  1.00 45.06           O  
ANISOU  826  OG  SER A 149     6256   4725   6139   -664    116   1505       O  
ATOM    827  N   ARG A 150     -24.233 -14.612  -2.285  1.00 46.00           N  
ANISOU  827  N   ARG A 150     5949   4920   6607   -992    142   1547       N  
ATOM    828  CA  ARG A 150     -24.623 -13.280  -2.759  1.00 43.23           C  
ANISOU  828  CA  ARG A 150     5456   4737   6231   -968    154   1470       C  
ATOM    829  C   ARG A 150     -23.657 -12.196  -2.302  1.00 45.22           C  
ANISOU  829  C   ARG A 150     5779   5125   6277   -790    187   1382       C  
ATOM    830  O   ARG A 150     -23.977 -11.003  -2.340  1.00 42.49           O  
ANISOU  830  O   ARG A 150     5338   4919   5887   -746    235   1350       O  
ATOM    831  CB  ARG A 150     -26.041 -12.940  -2.321  1.00 45.72           C  
ANISOU  831  CB  ARG A 150     5594   5128   6648  -1050    291   1619       C  
ATOM    832  CG  ARG A 150     -27.070 -13.971  -2.794  1.00 48.86           C  
ANISOU  832  CG  ARG A 150     5891   5395   7280  -1249    251   1708       C  
ATOM    833  CD  ARG A 150     -28.469 -13.585  -2.371  1.00 54.35           C  
ANISOU  833  CD  ARG A 150     6378   6184   8086  -1327    394   1859       C  
ATOM    834  N   ARG A 151     -22.456 -12.598  -1.897  1.00 42.48           N  
ANISOU  834  N   ARG A 151     5597   4731   5813   -687    148   1338       N  
ATOM    835  CA  ARG A 151     -21.459 -11.596  -1.537  1.00 40.95           C  
ANISOU  835  CA  ARG A 151     5462   4656   5440   -532    152   1238       C  
ATOM    836  C   ARG A 151     -21.071 -10.692  -2.710  1.00 39.88           C  
ANISOU  836  C   ARG A 151     5262   4588   5300   -522     53   1068       C  
ATOM    837  O   ARG A 151     -20.608  -9.588  -2.491  1.00 39.75           O  
ANISOU  837  O   ARG A 151     5242   4686   5175   -428     76   1000       O  
ATOM    838  CB  ARG A 151     -20.223 -12.261  -0.941  1.00 40.92           C  
ANISOU  838  CB  ARG A 151     5631   4590   5326   -424    110   1219       C  
ATOM    839  CG  ARG A 151     -19.456 -13.163  -1.871  1.00 41.93           C  
ANISOU  839  CG  ARG A 151     5831   4592   5511   -444    -37   1119       C  
ATOM    840  CD  ARG A 151     -18.309 -13.830  -1.081  1.00 44.66           C  
ANISOU  840  CD  ARG A 151     6341   4883   5745   -318    -63   1126       C  
ATOM    841  NE  ARG A 151     -17.663 -14.914  -1.813  1.00 43.52           N  
ANISOU  841  NE  ARG A 151     6281   4592   5663   -325   -186   1058       N  
ATOM    842  CZ  ARG A 151     -16.571 -15.547  -1.396  1.00 46.83           C  
ANISOU  842  CZ  ARG A 151     6834   4954   6005   -207   -239   1037       C  
ATOM    843  NH1 ARG A 151     -15.979 -15.194  -0.255  1.00 43.07           N  
ANISOU  843  NH1 ARG A 151     6423   4562   5381    -77   -192   1076       N  
ATOM    844  NH2 ARG A 151     -16.054 -16.518  -2.138  1.00 47.15           N  
ANISOU  844  NH2 ARG A 151     6947   4856   6110   -208   -347    967       N  
ATOM    845  N   GLN A 152     -21.248 -11.151  -3.946  1.00 37.63           N  
ANISOU  845  N   GLN A 152     4938   4229   5129   -617    -58   1000       N  
ATOM    846  CA  GLN A 152     -20.989 -10.280  -5.088  1.00 38.57           C  
ANISOU  846  CA  GLN A 152     4999   4419   5237   -608   -138    859       C  
ATOM    847  C   GLN A 152     -22.016  -9.147  -5.134  1.00 38.00           C  
ANISOU  847  C   GLN A 152     4782   4463   5192   -633    -67    896       C  
ATOM    848  O   GLN A 152     -21.670  -7.999  -5.386  1.00 38.16           O  
ANISOU  848  O   GLN A 152     4779   4583   5139   -565    -65    817       O  
ATOM    849  CB  GLN A 152     -20.999 -11.050  -6.414  1.00 40.18           C  
ANISOU  849  CB  GLN A 152     5207   4523   5538   -692   -276    776       C  
ATOM    850  CG  GLN A 152     -19.773 -11.953  -6.634  1.00 41.28           C  
ANISOU  850  CG  GLN A 152     5492   4563   5631   -632   -363    693       C  
ATOM    851  CD  GLN A 152     -19.840 -13.215  -5.795  1.00 43.57           C  
ANISOU  851  CD  GLN A 152     5874   4716   5966   -655   -341    801       C  
ATOM    852  OE1 GLN A 152     -20.921 -13.726  -5.537  1.00 42.62           O  
ANISOU  852  OE1 GLN A 152     5701   4530   5961   -767   -302    920       O  
ATOM    853  NE2 GLN A 152     -18.693 -13.712  -5.358  1.00 41.83           N  
ANISOU  853  NE2 GLN A 152     5783   4450   5659   -548   -363    770       N  
ATOM    854  N   LEU A 153     -23.278  -9.472  -4.894  1.00 37.58           N  
ANISOU  854  N   LEU A 153     4629   4393   5255   -728     -6   1020       N  
ATOM    855  CA ALEU A 153     -24.316  -8.447  -4.889  0.46 37.16           C  
ANISOU  855  CA ALEU A 153     4427   4455   5239   -739     68   1064       C  
ATOM    856  CA BLEU A 153     -24.326  -8.458  -4.874  0.54 37.19           C  
ANISOU  856  CA BLEU A 153     4430   4458   5243   -740     70   1066       C  
ATOM    857  C   LEU A 153     -24.045  -7.398  -3.822  1.00 37.17           C  
ANISOU  857  C   LEU A 153     4456   4567   5099   -607    192   1082       C  
ATOM    858  O   LEU A 153     -24.222  -6.212  -4.061  1.00 37.10           O  
ANISOU  858  O   LEU A 153     4385   4655   5058   -555    210   1033       O  
ATOM    859  CB ALEU A 153     -25.686  -9.064  -4.668  0.46 38.39           C  
ANISOU  859  CB ALEU A 153     4456   4579   5552   -862    128   1209       C  
ATOM    860  CB BLEU A 153     -25.680  -9.091  -4.609  0.54 38.64           C  
ANISOU  860  CB BLEU A 153     4491   4609   5582   -861    133   1215       C  
ATOM    861  CG ALEU A 153     -26.261  -9.773  -5.892  0.46 40.85           C  
ANISOU  861  CG ALEU A 153     4691   4803   6027  -1006    -13   1174       C  
ATOM    862  CG BLEU A 153     -26.820  -8.150  -4.237  0.54 37.71           C  
ANISOU  862  CG BLEU A 153     4211   4617   5500   -850    254   1299       C  
ATOM    863  CD1ALEU A 153     -27.554 -10.491  -5.542  0.46 41.25           C  
ANISOU  863  CD1ALEU A 153     4611   4809   6255  -1144     46   1329       C  
ATOM    864  CD1BLEU A 153     -27.148  -7.274  -5.417  0.54 40.16           C  
ANISOU  864  CD1BLEU A 153     4417   4991   5849   -858    158   1200       C  
ATOM    865  CD2ALEU A 153     -26.487  -8.760  -7.012  0.46 39.16           C  
ANISOU  865  CD2ALEU A 153     4387   4679   5814   -991    -98   1068       C  
ATOM    866  CD2BLEU A 153     -28.044  -8.950  -3.804  0.54 37.30           C  
ANISOU  866  CD2BLEU A 153     4036   4529   5608   -973    336   1467       C  
ATOM    867  N   LEU A 154     -23.629  -7.851  -2.646  1.00 35.67           N  
ANISOU  867  N   LEU A 154     4370   4357   4824   -547    271   1152       N  
ATOM    868  CA  LEU A 154     -23.331  -6.948  -1.550  1.00 34.30           C  
ANISOU  868  CA  LEU A 154     4248   4283   4501   -413    376   1160       C  
ATOM    869  C   LEU A 154     -22.142  -6.064  -1.925  1.00 34.49           C  
ANISOU  869  C   LEU A 154     4341   4347   4419   -323    290    997       C  
ATOM    870  O   LEU A 154     -22.173  -4.848  -1.723  1.00 33.88           O  
ANISOU  870  O   LEU A 154     4238   4358   4275   -249    332    952       O  
ATOM    871  CB  LEU A 154     -23.069  -7.745  -0.277  1.00 34.35           C  
ANISOU  871  CB  LEU A 154     4372   4253   4427   -364    458   1267       C  
ATOM    872  CG  LEU A 154     -24.296  -8.507   0.214  1.00 34.74           C  
ANISOU  872  CG  LEU A 154     4346   4272   4582   -454    577   1453       C  
ATOM    873  CD1 LEU A 154     -23.922  -9.480   1.319  1.00 35.89           C  
ANISOU  873  CD1 LEU A 154     4633   4354   4651   -415    641   1567       C  
ATOM    874  CD2 LEU A 154     -25.357  -7.519   0.699  1.00 35.13           C  
ANISOU  874  CD2 LEU A 154     4271   4451   4626   -418    724   1522       C  
ATOM    875  N   LEU A 155     -21.119  -6.666  -2.522  1.00 34.66           N  
ANISOU  875  N   LEU A 155     4439   4297   4434   -332    171    909       N  
ATOM    876  CA  LEU A 155     -19.961  -5.894  -2.967  1.00 35.22           C  
ANISOU  876  CA  LEU A 155     4553   4404   4424   -263     93    763       C  
ATOM    877  C   LEU A 155     -20.359  -4.875  -4.043  1.00 34.47           C  
ANISOU  877  C   LEU A 155     4356   4361   4381   -297     64    698       C  
ATOM    878  O   LEU A 155     -19.962  -3.723  -3.973  1.00 35.29           O  
ANISOU  878  O   LEU A 155     4460   4529   4418   -231     75    631       O  
ATOM    879  CB  LEU A 155     -18.859  -6.824  -3.486  1.00 35.73           C  
ANISOU  879  CB  LEU A 155     4702   4388   4487   -264    -18    690       C  
ATOM    880  CG  LEU A 155     -17.572  -6.148  -3.964  1.00 37.58           C  
ANISOU  880  CG  LEU A 155     4965   4662   4650   -198    -92    548       C  
ATOM    881  CD1 LEU A 155     -16.959  -5.308  -2.847  1.00 35.21           C  
ANISOU  881  CD1 LEU A 155     4713   4435   4231    -92    -50    525       C  
ATOM    882  CD2 LEU A 155     -16.591  -7.214  -4.454  1.00 37.40           C  
ANISOU  882  CD2 LEU A 155     5014   4562   4635   -190   -186    489       C  
ATOM    883  N   ILE A 156     -21.165  -5.296  -5.016  1.00 37.33           N  
ANISOU  883  N   ILE A 156     4634   4688   4862   -398     21    720       N  
ATOM    884  CA  ILE A 156     -21.651  -4.383  -6.054  1.00 36.84           C  
ANISOU  884  CA  ILE A 156     4478   4676   4844   -424    -13    673       C  
ATOM    885  C   ILE A 156     -22.418  -3.202  -5.442  1.00 34.92           C  
ANISOU  885  C   ILE A 156     4164   4521   4583   -371     91    722       C  
ATOM    886  O   ILE A 156     -22.189  -2.055  -5.810  1.00 35.20           O  
ANISOU  886  O   ILE A 156     4188   4605   4581   -322     83    656       O  
ATOM    887  CB  ILE A 156     -22.538  -5.125  -7.072  1.00 36.02           C  
ANISOU  887  CB  ILE A 156     4293   4522   4872   -540    -87    699       C  
ATOM    888  CG1 ILE A 156     -21.660  -6.014  -7.968  1.00 36.58           C  
ANISOU  888  CG1 ILE A 156     4447   4511   4940   -568   -208    607       C  
ATOM    889  CG2 ILE A 156     -23.312  -4.128  -7.940  1.00 34.00           C  
ANISOU  889  CG2 ILE A 156     3925   4334   4659   -553   -108    683       C  
ATOM    890  CD1 ILE A 156     -22.461  -7.095  -8.757  1.00 35.45           C  
ANISOU  890  CD1 ILE A 156     4261   4283   4925   -687   -296    628       C  
ATOM    891  N   GLY A 157     -23.305  -3.483  -4.496  1.00 33.46           N  
ANISOU  891  N   GLY A 157     3937   4352   4424   -374    197    839       N  
ATOM    892  CA  GLY A 157     -24.001  -2.419  -3.792  1.00 35.30           C  
ANISOU  892  CA  GLY A 157     4115   4673   4626   -299    312    883       C  
ATOM    893  C   GLY A 157     -23.023  -1.450  -3.121  1.00 34.48           C  
ANISOU  893  C   GLY A 157     4120   4604   4378   -177    334    798       C  
ATOM    894  O   GLY A 157     -23.185  -0.239  -3.191  1.00 33.12           O  
ANISOU  894  O   GLY A 157     3923   4481   4181   -117    357    757       O  
ATOM    895  N   ALA A 158     -22.005  -1.987  -2.462  1.00 33.24           N  
ANISOU  895  N   ALA A 158     4085   4415   4131   -140    316    771       N  
ATOM    896  CA  ALA A 158     -21.020  -1.128  -1.813  1.00 32.94           C  
ANISOU  896  CA  ALA A 158     4145   4406   3964    -34    312    680       C  
ATOM    897  C   ALA A 158     -20.314  -0.258  -2.837  1.00 32.29           C  
ANISOU  897  C   ALA A 158     4053   4320   3896    -43    221    560       C  
ATOM    898  O   ALA A 158     -20.061   0.914  -2.588  1.00 33.44           O  
ANISOU  898  O   ALA A 158     4220   4496   3990     23    234    498       O  
ATOM    899  CB  ALA A 158     -20.023  -1.952  -1.043  1.00 31.97           C  
ANISOU  899  CB  ALA A 158     4143   4251   3753      5    284    671       C  
ATOM    900  N   THR A 159     -20.032  -0.836  -3.997  1.00 33.16           N  
ANISOU  900  N   THR A 159     4135   4388   4077   -124    131    531       N  
ATOM    901  CA  THR A 159     -19.344  -0.143  -5.080  1.00 33.92           C  
ANISOU  901  CA  THR A 159     4222   4482   4183   -138     55    434       C  
ATOM    902  C   THR A 159     -20.121   1.087  -5.552  1.00 36.09           C  
ANISOU  902  C   THR A 159     4426   4792   4493   -128     85    438       C  
ATOM    903  O   THR A 159     -19.536   2.148  -5.815  1.00 33.71           O  
ANISOU  903  O   THR A 159     4147   4498   4164    -96     68    367       O  
ATOM    904  CB  THR A 159     -19.126  -1.103  -6.275  1.00 36.53           C  
ANISOU  904  CB  THR A 159     4538   4768   4576   -218    -33    415       C  
ATOM    905  OG1 THR A 159     -18.030  -1.989  -5.982  1.00 38.38           O  
ANISOU  905  OG1 THR A 159     4853   4964   4766   -201    -78    375       O  
ATOM    906  CG2 THR A 159     -18.800  -0.353  -7.501  1.00 39.49           C  
ANISOU  906  CG2 THR A 159     4886   5155   4964   -234    -86    348       C  
ATOM    907  N   TRP A 160     -21.438   0.938  -5.674  1.00 34.12           N  
ANISOU  907  N   TRP A 160     4087   4562   4315   -157    128    525       N  
ATOM    908  CA  TRP A 160     -22.273   2.030  -6.143  1.00 33.46           C  
ANISOU  908  CA  TRP A 160     3927   4514   4272   -136    151    539       C  
ATOM    909  C   TRP A 160     -22.430   3.094  -5.071  1.00 34.20           C  
ANISOU  909  C   TRP A 160     4051   4640   4303    -31    243    536       C  
ATOM    910  O   TRP A 160     -22.455   4.274  -5.371  1.00 34.55           O  
ANISOU  910  O   TRP A 160     4094   4688   4343     14    243    497       O  
ATOM    911  CB  TRP A 160     -23.646   1.510  -6.596  1.00 34.51           C  
ANISOU  911  CB  TRP A 160     3934   4666   4512   -196    158    632       C  
ATOM    912  CG  TRP A 160     -23.579   0.930  -7.968  1.00 34.28           C  
ANISOU  912  CG  TRP A 160     3877   4606   4542   -283     41    604       C  
ATOM    913  CD1 TRP A 160     -23.312  -0.370  -8.306  1.00 35.76           C  
ANISOU  913  CD1 TRP A 160     4087   4743   4759   -362    -25    600       C  
ATOM    914  CD2 TRP A 160     -23.749   1.637  -9.199  1.00 34.90           C  
ANISOU  914  CD2 TRP A 160     3919   4699   4642   -288    -28    571       C  
ATOM    915  NE1 TRP A 160     -23.324  -0.515  -9.676  1.00 34.16           N  
ANISOU  915  NE1 TRP A 160     3863   4526   4589   -413   -133    557       N  
ATOM    916  CE2 TRP A 160     -23.596   0.703 -10.245  1.00 34.80           C  
ANISOU  916  CE2 TRP A 160     3909   4653   4662   -368   -135    544       C  
ATOM    917  CE3 TRP A 160     -24.023   2.978  -9.518  1.00 38.49           C  
ANISOU  917  CE3 TRP A 160     4351   5185   5087   -225    -12    564       C  
ATOM    918  CZ2 TRP A 160     -23.703   1.064 -11.587  1.00 35.87           C  
ANISOU  918  CZ2 TRP A 160     4027   4800   4803   -382   -224    511       C  
ATOM    919  CZ3 TRP A 160     -24.131   3.336 -10.854  1.00 37.51           C  
ANISOU  919  CZ3 TRP A 160     4206   5065   4979   -243    -97    544       C  
ATOM    920  CH2 TRP A 160     -23.969   2.386 -11.871  1.00 37.20           C  
ANISOU  920  CH2 TRP A 160     4172   5006   4955   -319   -201    518       C  
ATOM    921  N   LEU A 161     -22.526   2.679  -3.820  1.00 30.64           N  
ANISOU  921  N   LEU A 161     3640   4206   3795     14    321    576       N  
ATOM    922  CA  LEU A 161     -22.657   3.650  -2.756  1.00 31.22           C  
ANISOU  922  CA  LEU A 161     3762   4312   3787    129    406    561       C  
ATOM    923  C   LEU A 161     -21.359   4.466  -2.631  1.00 33.86           C  
ANISOU  923  C   LEU A 161     4207   4613   4046    171    343    434       C  
ATOM    924  O   LEU A 161     -21.403   5.669  -2.416  1.00 33.12           O  
ANISOU  924  O   LEU A 161     4141   4517   3926    242    364    385       O  
ATOM    925  CB  LEU A 161     -22.988   2.959  -1.450  1.00 31.40           C  
ANISOU  925  CB  LEU A 161     3819   4366   3744    176    505    636       C  
ATOM    926  CG  LEU A 161     -24.441   2.459  -1.314  1.00 34.10           C  
ANISOU  926  CG  LEU A 161     4035   4754   4167    152    608    775       C  
ATOM    927  CD1 LEU A 161     -24.621   1.933   0.069  1.00 33.58           C  
ANISOU  927  CD1 LEU A 161     4028   4722   4009    215    725    851       C  
ATOM    928  CD2 LEU A 161     -25.438   3.572  -1.588  1.00 34.89           C  
ANISOU  928  CD2 LEU A 161     4038   4901   4317    209    663    788       C  
ATOM    929  N   LEU A 162     -20.219   3.809  -2.790  1.00 31.61           N  
ANISOU  929  N   LEU A 162     3977   4297   3737    126    262    383       N  
ATOM    930  CA ALEU A 162     -18.918   4.488  -2.749  0.51 32.38           C  
ANISOU  930  CA ALEU A 162     4152   4366   3786    146    192    266       C  
ATOM    931  CA BLEU A 162     -18.938   4.517  -2.704  0.49 32.07           C  
ANISOU  931  CA BLEU A 162     4113   4327   3744    150    195    266       C  
ATOM    932  C   LEU A 162     -18.781   5.508  -3.860  0.92 31.86           C  
ANISOU  932  C   LEU A 162     4049   4272   3784    113    152    221       C  
ATOM    933  O   LEU A 162     -18.269   6.608  -3.662  0.95 33.47           O  
ANISOU  933  O   LEU A 162     4300   4450   3967    149    138    147       O  
ATOM    934  CB ALEU A 162     -17.788   3.471  -2.864  0.51 31.72           C  
ANISOU  934  CB ALEU A 162     4104   4264   3685    103    114    231       C  
ATOM    935  CB BLEU A 162     -17.766   3.523  -2.683  0.49 32.11           C  
ANISOU  935  CB BLEU A 162     4163   4315   3721    115    119    228       C  
ATOM    936  CG ALEU A 162     -17.577   2.650  -1.606  0.51 33.04           C  
ANISOU  936  CG ALEU A 162     4344   4446   3762    159    136    257       C  
ATOM    937  CG BLEU A 162     -16.371   4.102  -2.411  0.49 33.16           C  
ANISOU  937  CG BLEU A 162     4360   4433   3807    140     46    111       C  
ATOM    938  CD1ALEU A 162     -16.504   1.614  -1.863  0.51 34.06           C  
ANISOU  938  CD1ALEU A 162     4500   4551   3889    124     52    228       C  
ATOM    939  CD1BLEU A 162     -16.384   4.966  -1.163  0.49 35.38           C  
ANISOU  939  CD1BLEU A 162     4718   4725   3999    237     75     65       C  
ATOM    940  CD2ALEU A 162     -17.204   3.580  -0.463  0.51 32.93           C  
ANISOU  940  CD2ALEU A 162     4417   4451   3646    259    149    189       C  
ATOM    941  CD2BLEU A 162     -15.300   2.994  -2.302  0.49 32.07           C  
ANISOU  941  CD2BLEU A 162     4251   4291   3642    125    -24     86       C  
ATOM    942  N   SER A 163     -19.221   5.119  -5.054  1.00 32.43           N  
ANISOU  942  N   SER A 163     4044   4343   3933     41    128    267       N  
ATOM    943  CA  SER A 163     -19.184   6.019  -6.206  1.00 32.45           C  
ANISOU  943  CA  SER A 163     4018   4325   3987     14     95    246       C  
ATOM    944  C   SER A 163     -20.050   7.252  -5.972  1.00 34.80           C  
ANISOU  944  C   SER A 163     4304   4620   4297     84    151    264       C  
ATOM    945  O   SER A 163     -19.661   8.382  -6.306  1.00 35.70           O  
ANISOU  945  O   SER A 163     4451   4692   4421     99    136    217       O  
ATOM    946  CB  SER A 163     -19.649   5.296  -7.462  1.00 31.36           C  
ANISOU  946  CB  SER A 163     3809   4196   3909    -59     53    295       C  
ATOM    947  OG  SER A 163     -18.936   4.082  -7.594  1.00 34.44           O  
ANISOU  947  OG  SER A 163     4220   4580   4287   -108      6    277       O  
ATOM    948  N   ALA A 164     -21.221   7.031  -5.384  1.00 33.30           N  
ANISOU  948  N   ALA A 164     4068   4472   4114    129    223    335       N  
ATOM    949  CA  ALA A 164     -22.113   8.131  -5.050  1.00 33.41           C  
ANISOU  949  CA  ALA A 164     4066   4492   4136    220    289    353       C  
ATOM    950  C   ALA A 164     -21.450   9.031  -4.017  1.00 33.99           C  
ANISOU  950  C   ALA A 164     4253   4530   4131    302    309    265       C  
ATOM    951  O   ALA A 164     -21.591  10.248  -4.076  1.00 34.44           O  
ANISOU  951  O   ALA A 164     4341   4546   4199    361    319    230       O  
ATOM    952  CB  ALA A 164     -23.447   7.606  -4.528  1.00 34.06           C  
ANISOU  952  CB  ALA A 164     4060   4641   4241    255    377    451       C  
ATOM    953  N   ALA A 165     -20.718   8.430  -3.076  1.00 32.75           N  
ANISOU  953  N   ALA A 165     4166   4382   3895    310    304    225       N  
ATOM    954  CA  ALA A 165     -20.044   9.213  -2.039  1.00 34.16           C  
ANISOU  954  CA  ALA A 165     4460   4530   3990    388    301    127       C  
ATOM    955  C   ALA A 165     -18.976  10.165  -2.633  1.00 34.57           C  
ANISOU  955  C   ALA A 165     4556   4502   4078    344    214     31       C  
ATOM    956  O   ALA A 165     -18.845  11.312  -2.205  1.00 35.55           O  
ANISOU  956  O   ALA A 165     4750   4571   4185    406    212    -41       O  
ATOM    957  CB  ALA A 165     -19.415   8.283  -0.992  1.00 31.45           C  
ANISOU  957  CB  ALA A 165     4181   4219   3549    405    293    108       C  
ATOM    958  N   VAL A 166     -18.227   9.677  -3.611  1.00 32.65           N  
ANISOU  958  N   VAL A 166     4273   4248   3886    240    147     31       N  
ATOM    959  CA  VAL A 166     -17.258  10.492  -4.316  1.00 33.73           C  
ANISOU  959  CA  VAL A 166     4427   4317   4072    182     83    -34       C  
ATOM    960  C   VAL A 166     -17.961  11.637  -5.056  1.00 34.38           C  
ANISOU  960  C   VAL A 166     4495   4348   4217    199    110     -2       C  
ATOM    961  O   VAL A 166     -17.519  12.792  -4.995  1.00 34.09           O  
ANISOU  961  O   VAL A 166     4517   4231   4203    210     90    -63       O  
ATOM    962  CB  VAL A 166     -16.425   9.651  -5.313  1.00 32.58           C  
ANISOU  962  CB  VAL A 166     4229   4188   3961     79     29    -23       C  
ATOM    963  CG1 VAL A 166     -15.484  10.554  -6.135  1.00 32.59           C  
ANISOU  963  CG1 VAL A 166     4234   4126   4021     16    -12    -67       C  
ATOM    964  CG2 VAL A 166     -15.627   8.563  -4.568  1.00 31.05           C  
ANISOU  964  CG2 VAL A 166     4057   4033   3710     76     -7    -60       C  
ATOM    965  N   ALA A 167     -19.064  11.329  -5.724  1.00 31.17           N  
ANISOU  965  N   ALA A 167     4014   3984   3844    205    147     93       N  
ATOM    966  CA  ALA A 167     -19.738  12.310  -6.575  1.00 32.15           C  
ANISOU  966  CA  ALA A 167     4118   4068   4028    227    159    136       C  
ATOM    967  C   ALA A 167     -20.602  13.319  -5.824  1.00 31.90           C  
ANISOU  967  C   ALA A 167     4124   4008   3989    349    218    129       C  
ATOM    968  O   ALA A 167     -20.919  14.375  -6.363  1.00 33.25           O  
ANISOU  968  O   ALA A 167     4311   4116   4207    383    219    142       O  
ATOM    969  CB  ALA A 167     -20.605  11.581  -7.619  1.00 32.63           C  
ANISOU  969  CB  ALA A 167     4078   4192   4128    192    156    234       C  
ATOM    970  N   ALA A 168     -21.008  12.987  -4.603  1.00 35.27           N  
ANISOU  970  N   ALA A 168     4568   4481   4351    426    273    114       N  
ATOM    971  CA  ALA A 168     -22.039  13.742  -3.891  1.00 34.79           C  
ANISOU  971  CA  ALA A 168     4524   4422   4272    564    352    122       C  
ATOM    972  C   ALA A 168     -21.784  15.271  -3.746  1.00 34.79           C  
ANISOU  972  C   ALA A 168     4630   4304   4285    632    337     42       C  
ATOM    973  O   ALA A 168     -22.736  16.051  -3.852  1.00 36.06           O  
ANISOU  973  O   ALA A 168     4779   4446   4476    732    385     74       O  
ATOM    974  CB  ALA A 168     -22.268  13.122  -2.512  1.00 33.90           C  
ANISOU  974  CB  ALA A 168     4439   4379   4062    637    419    110       C  
ATOM    975  N   PRO A 169     -20.523  15.699  -3.504  1.00 35.95           N  
ANISOU  975  N   PRO A 169     4875   4367   4419    581    267    -63       N  
ATOM    976  CA  PRO A 169     -20.337  17.152  -3.355  1.00 36.58           C  
ANISOU  976  CA  PRO A 169     5059   4313   4526    637    248   -139       C  
ATOM    977  C   PRO A 169     -20.678  17.942  -4.618  1.00 37.70           C  
ANISOU  977  C   PRO A 169     5173   4382   4769    615    239    -70       C  
ATOM    978  O   PRO A 169     -21.006  19.115  -4.504  1.00 38.89           O  
ANISOU  978  O   PRO A 169     5399   4430   4948    700    250    -99       O  
ATOM    979  CB  PRO A 169     -18.838  17.286  -3.022  1.00 35.38           C  
ANISOU  979  CB  PRO A 169     4983   4092   4367    546    157   -252       C  
ATOM    980  CG  PRO A 169     -18.472  15.962  -2.399  1.00 37.01           C  
ANISOU  980  CG  PRO A 169     5158   4414   4492    519    152   -257       C  
ATOM    981  CD  PRO A 169     -19.279  14.964  -3.190  1.00 36.11           C  
ANISOU  981  CD  PRO A 169     4918   4401   4401    488    202   -124       C  
ATOM    982  N   VAL A 170     -20.612  17.315  -5.789  1.00 34.71           N  
ANISOU  982  N   VAL A 170     4703   4052   4435    514    218     18       N  
ATOM    983  CA  VAL A 170     -20.899  18.022  -7.027  1.00 34.90           C  
ANISOU  983  CA  VAL A 170     4711   4015   4534    499    205     92       C  
ATOM    984  C   VAL A 170     -22.339  18.547  -7.045  1.00 36.59           C  
ANISOU  984  C   VAL A 170     4896   4243   4764    641    259    155       C  
ATOM    985  O   VAL A 170     -22.583  19.661  -7.510  1.00 36.09           O  
ANISOU  985  O   VAL A 170     4884   4076   4751    694    254    174       O  
ATOM    986  CB  VAL A 170     -20.653  17.135  -8.249  1.00 36.20           C  
ANISOU  986  CB  VAL A 170     4788   4250   4715    385    172    172       C  
ATOM    987  CG1 VAL A 170     -21.078  17.847  -9.521  1.00 37.56           C  
ANISOU  987  CG1 VAL A 170     4953   4375   4941    392    161    260       C  
ATOM    988  CG2 VAL A 170     -19.164  16.757  -8.332  1.00 35.52           C  
ANISOU  988  CG2 VAL A 170     4727   4144   4625    256    125    112       C  
ATOM    989  N   LEU A 171     -23.270  17.764  -6.502  1.00 40.91           N  
ANISOU  989  N   LEU A 171     5357   4913   5275    706    314    190       N  
ATOM    990  CA  LEU A 171     -24.671  18.181  -6.391  1.00 40.78           C  
ANISOU  990  CA  LEU A 171     5282   4933   5278    851    377    249       C  
ATOM    991  C   LEU A 171     -24.887  19.439  -5.551  1.00 42.40           C  
ANISOU  991  C   LEU A 171     5603   5037   5471    999    418    175       C  
ATOM    992  O   LEU A 171     -25.878  20.148  -5.737  1.00 45.40           O  
ANISOU  992  O   LEU A 171     5959   5402   5888   1127    454    220       O  
ATOM    993  CB  LEU A 171     -25.518  17.048  -5.796  1.00 41.33           C  
ANISOU  993  CB  LEU A 171     5231   5155   5316    879    443    299       C  
ATOM    994  CG  LEU A 171     -26.028  15.972  -6.749  1.00 44.08           C  
ANISOU  994  CG  LEU A 171     5430   5609   5711    788    412    402       C  
ATOM    995  CD1 LEU A 171     -26.859  14.944  -5.984  1.00 45.67           C  
ANISOU  995  CD1 LEU A 171     5519   5938   5897    812    489    451       C  
ATOM    996  CD2 LEU A 171     -26.860  16.610  -7.842  1.00 44.64           C  
ANISOU  996  CD2 LEU A 171     5436   5670   5855    837    382    479       C  
ATOM    997  N   CYS A 172     -23.987  19.720  -4.615  1.00 48.27           N  
ANISOU  997  N   CYS A 172     6472   5709   6159    994    405     55       N  
ATOM    998  CA  CYS A 172     -24.178  20.865  -3.717  1.00 47.97           C  
ANISOU  998  CA  CYS A 172     6562   5569   6095   1143    436    -38       C  
ATOM    999  C   CYS A 172     -23.756  22.186  -4.372  1.00 52.44           C  
ANISOU  999  C   CYS A 172     7235   5946   6744   1134    376    -64       C  
ATOM   1000  O   CYS A 172     -23.944  23.263  -3.790  1.00 51.73           O  
ANISOU 1000  O   CYS A 172     7264   5738   6652   1260    389   -142       O  
ATOM   1001  CB  CYS A 172     -23.397  20.675  -2.417  1.00 50.74           C  
ANISOU 1001  CB  CYS A 172     7019   5913   6346   1149    428   -168       C  
ATOM   1002  SG  CYS A 172     -23.870  19.211  -1.456  1.00 48.22           S  
ANISOU 1002  SG  CYS A 172     6612   5796   5913   1179    514   -131       S  
ATOM   1003  N   GLY A 173     -23.177  22.104  -5.568  1.00 49.59           N  
ANISOU 1003  N   GLY A 173     6841   5550   6451    991    315      0       N  
ATOM   1004  CA  GLY A 173     -22.755  23.297  -6.287  1.00 50.26           C  
ANISOU 1004  CA  GLY A 173     7022   5455   6620    966    269      4       C  
ATOM   1005  C   GLY A 173     -21.329  23.703  -5.968  1.00 50.25           C  
ANISOU 1005  C   GLY A 173     7130   5322   6639    844    203   -106       C  
ATOM   1006  O   GLY A 173     -21.058  24.325  -4.938  1.00 50.88           O  
ANISOU 1006  O   GLY A 173     7328   5307   6699    905    188   -234       O  
ATOM   1007  N   LEU A 174     -20.412  23.360  -6.864  1.00 48.96           N  
ANISOU 1007  N   LEU A 174     6927   5155   6519    675    159    -60       N  
ATOM   1008  CA  LEU A 174     -18.998  23.636  -6.639  1.00 49.68           C  
ANISOU 1008  CA  LEU A 174     7084   5142   6649    538     96   -153       C  
ATOM   1009  C   LEU A 174     -18.453  24.781  -7.503  1.00 52.09           C  
ANISOU 1009  C   LEU A 174     7462   5260   7069    461     69   -114       C  
ATOM   1010  O   LEU A 174     -17.358  25.286  -7.247  1.00 53.03           O  
ANISOU 1010  O   LEU A 174     7645   5256   7249    355     16   -196       O  
ATOM   1011  CB  LEU A 174     -18.179  22.371  -6.886  1.00 48.33           C  
ANISOU 1011  CB  LEU A 174     6808   5107   6446    399     75   -140       C  
ATOM   1012  CG  LEU A 174     -18.546  21.159  -6.030  1.00 47.42           C  
ANISOU 1012  CG  LEU A 174     6630   5163   6226    450     97   -170       C  
ATOM   1013  CD1 LEU A 174     -17.638  19.969  -6.354  1.00 44.47           C  
ANISOU 1013  CD1 LEU A 174     6168   4895   5833    314     67   -159       C  
ATOM   1014  CD2 LEU A 174     -18.492  21.506  -4.546  1.00 47.21           C  
ANISOU 1014  CD2 LEU A 174     6703   5096   6137    545     86   -309       C  
ATOM   1015  N   ASN A 175     -19.205  25.188  -8.522  1.00 54.28           N  
ANISOU 1015  N   ASN A 175     7730   5515   7380    511    102     16       N  
ATOM   1016  CA  ASN A 175     -18.742  26.255  -9.408  1.00 55.84           C  
ANISOU 1016  CA  ASN A 175     8005   5532   7679    443     89     80       C  
ATOM   1017  C   ASN A 175     -19.025  27.634  -8.827  1.00 61.26           C  
ANISOU 1017  C   ASN A 175     8845   6005   8426    547     76     12       C  
ATOM   1018  O   ASN A 175     -19.893  27.784  -7.961  1.00 59.05           O  
ANISOU 1018  O   ASN A 175     8599   5740   8095    714     93    -55       O  
ATOM   1019  CB  ASN A 175     -19.384  26.129 -10.793  1.00 56.48           C  
ANISOU 1019  CB  ASN A 175     8030   5675   7757    462    119    254       C  
ATOM   1020  CG  ASN A 175     -18.916  24.890 -11.551  1.00 57.44           C  
ANISOU 1020  CG  ASN A 175     8026   5969   7827    341    122    317       C  
ATOM   1021  OD1 ASN A 175     -17.894  24.277 -11.211  1.00 58.24           O  
ANISOU 1021  OD1 ASN A 175     8090   6115   7923    219    105    247       O  
ATOM   1022  ND2 ASN A 175     -19.663  24.516 -12.586  1.00 53.02           N  
ANISOU 1022  ND2 ASN A 175     7406   5509   7230    384    136    444       N  
ATOM   1023  N   ASP A 176     -18.289  28.632  -9.318  1.00 63.24           N  
ANISOU 1023  N   ASP A 176     9188   6054   8789    450     51     34       N  
ATOM   1024  CA  ASP A 176     -18.362  30.004  -8.818  1.00 63.98           C  
ANISOU 1024  CA  ASP A 176     9446   5900   8962    520     24    -40       C  
ATOM   1025  C   ASP A 176     -19.793  30.536  -8.747  1.00 69.76           C  
ANISOU 1025  C   ASP A 176    10231   6610   9663    753     62     -3       C  
ATOM   1026  O   ASP A 176     -20.341  30.728  -7.659  1.00 73.59           O  
ANISOU 1026  O   ASP A 176    10774   7087  10101    903     63   -124       O  
ATOM   1027  CB  ASP A 176     -17.509  30.924  -9.699  1.00 59.29           C  
ANISOU 1027  CB  ASP A 176     8923   5099   8506    371      9     39       C  
ATOM   1028  N   PRO A 182     -20.168  30.132 -16.463  1.00 71.90           N  
ANISOU 1028  N   PRO A 182    10329   7089   9901    530    179    983       N  
ATOM   1029  CA  PRO A 182     -21.547  29.704 -16.182  1.00 72.27           C  
ANISOU 1029  CA  PRO A 182    10302   7277   9879    719    155    967       C  
ATOM   1030  C   PRO A 182     -22.365  29.501 -17.469  1.00 69.92           C  
ANISOU 1030  C   PRO A 182     9969   7088   9507    806    139   1131       C  
ATOM   1031  O   PRO A 182     -23.503  29.030 -17.419  1.00 69.90           O  
ANISOU 1031  O   PRO A 182     9875   7229   9454    945    110   1136       O  
ATOM   1032  CB  PRO A 182     -22.103  30.856 -15.349  1.00 73.33           C  
ANISOU 1032  CB  PRO A 182    10553   7219  10091    864    149    902       C  
ATOM   1033  CG  PRO A 182     -21.354  32.072 -15.846  1.00 73.32           C  
ANISOU 1033  CG  PRO A 182    10712   6957  10189    788    159    974       C  
ATOM   1034  CD  PRO A 182     -19.983  31.596 -16.317  1.00 71.37           C  
ANISOU 1034  CD  PRO A 182    10429   6738   9952    550    183    997       C  
ATOM   1035  N   ALA A 183     -21.774  29.877 -18.601  1.00 69.02           N  
ANISOU 1035  N   ALA A 183     9928   6907   9390    726    157   1267       N  
ATOM   1036  CA  ALA A 183     -22.361  29.626 -19.909  1.00 62.45           C  
ANISOU 1036  CA  ALA A 183     9078   6188   8463    793    135   1423       C  
ATOM   1037  C   ALA A 183     -21.838  28.302 -20.471  1.00 59.14           C  
ANISOU 1037  C   ALA A 183     8546   5981   7942    669    136   1423       C  
ATOM   1038  O   ALA A 183     -22.056  27.964 -21.637  1.00 57.25           O  
ANISOU 1038  O   ALA A 183     8301   5845   7606    690    117   1539       O  
ATOM   1039  CB  ALA A 183     -22.049  30.778 -20.860  1.00 64.14           C  
ANISOU 1039  CB  ALA A 183     9452   6212   8708    793    162   1584       C  
ATOM   1040  N   VAL A 184     -21.121  27.566 -19.633  1.00 53.33           N  
ANISOU 1040  N   VAL A 184     7734   5305   7224    549    154   1287       N  
ATOM   1041  CA  VAL A 184     -20.535  26.290 -20.023  1.00 53.44           C  
ANISOU 1041  CA  VAL A 184     7647   5504   7155    434    157   1267       C  
ATOM   1042  C   VAL A 184     -20.726  25.327 -18.862  1.00 54.79           C  
ANISOU 1042  C   VAL A 184     7701   5791   7326    427    134   1112       C  
ATOM   1043  O   VAL A 184     -20.917  25.752 -17.722  1.00 56.80           O  
ANISOU 1043  O   VAL A 184     7972   5962   7649    471    137   1015       O  
ATOM   1044  CB  VAL A 184     -19.038  26.410 -20.354  1.00 55.46           C  
ANISOU 1044  CB  VAL A 184     7942   5692   7439    255    223   1286       C  
ATOM   1045  CG1 VAL A 184     -18.806  27.377 -21.521  1.00 55.52           C  
ANISOU 1045  CG1 VAL A 184     8072   5580   7444    253    266   1462       C  
ATOM   1046  CG2 VAL A 184     -18.269  26.860 -19.120  1.00 59.15           C  
ANISOU 1046  CG2 VAL A 184     8426   6021   8028    168    241   1158       C  
ATOM   1047  N   CYS A 185     -20.689  24.034 -19.138  1.00 48.17           N  
ANISOU 1047  N   CYS A 185     6757   5140   6406    381    114   1089       N  
ATOM   1048  CA  CYS A 185     -20.890  23.058 -18.077  1.00 47.50           C  
ANISOU 1048  CA  CYS A 185     6567   5164   6318    374     96    961       C  
ATOM   1049  C   CYS A 185     -19.600  22.311 -17.793  1.00 46.34           C  
ANISOU 1049  C   CYS A 185     6387   5057   6164    220    122    883       C  
ATOM   1050  O   CYS A 185     -19.279  21.345 -18.469  1.00 47.39           O  
ANISOU 1050  O   CYS A 185     6466   5314   6226    161    114    900       O  
ATOM   1051  CB  CYS A 185     -22.007  22.079 -18.434  1.00 48.09           C  
ANISOU 1051  CB  CYS A 185     6533   5415   6323    450     40    983       C  
ATOM   1052  SG  CYS A 185     -22.494  21.040 -17.019  1.00 50.16           S  
ANISOU 1052  SG  CYS A 185     6672   5786   6598    463     35    853       S  
ATOM   1053  N   ARG A 186     -18.856  22.787 -16.799  1.00 47.98           N  
ANISOU 1053  N   ARG A 186     6630   5153   6447    163    146    791       N  
ATOM   1054  CA  ARG A 186     -17.571  22.199 -16.430  1.00 45.86           C  
ANISOU 1054  CA  ARG A 186     6324   4911   6189     24    161    711       C  
ATOM   1055  C   ARG A 186     -17.411  22.164 -14.917  1.00 45.23           C  
ANISOU 1055  C   ARG A 186     6237   4797   6150     29    145    568       C  
ATOM   1056  O   ARG A 186     -18.018  22.964 -14.203  1.00 45.79           O  
ANISOU 1056  O   ARG A 186     6369   4770   6261    120    139    532       O  
ATOM   1057  CB  ARG A 186     -16.415  23.001 -17.033  1.00 48.16           C  
ANISOU 1057  CB  ARG A 186     6677   5079   6541    -90    205    767       C  
ATOM   1058  CG  ARG A 186     -16.403  23.099 -18.534  1.00 52.31           C  
ANISOU 1058  CG  ARG A 186     7230   5634   7012    -97    238    918       C  
ATOM   1059  CD  ARG A 186     -15.049  23.613 -19.036  1.00 56.91           C  
ANISOU 1059  CD  ARG A 186     7840   6130   7653   -238    304    968       C  
ATOM   1060  NE  ARG A 186     -15.167  24.295 -20.318  1.00 56.01           N  
ANISOU 1060  NE  ARG A 186     7807   5965   7509   -220    350   1137       N  
ATOM   1061  CZ  ARG A 186     -15.054  25.606 -20.498  1.00 56.22           C  
ANISOU 1061  CZ  ARG A 186     7939   5799   7624   -232    383   1219       C  
ATOM   1062  NH1 ARG A 186     -14.775  26.420 -19.482  1.00 50.97           N  
ANISOU 1062  NH1 ARG A 186     7312   4962   7092   -270    369   1136       N  
ATOM   1063  NH2 ARG A 186     -15.191  26.105 -21.716  1.00 58.73           N  
ANISOU 1063  NH2 ARG A 186     8334   6088   7891   -205    428   1387       N  
ATOM   1064  N   LEU A 187     -16.586  21.239 -14.432  1.00 40.57           N  
ANISOU 1064  N   LEU A 187     5583   4291   5542    -57    136    484       N  
ATOM   1065  CA  LEU A 187     -16.215  21.221 -13.028  1.00 41.78           C  
ANISOU 1065  CA  LEU A 187     5743   4411   5721    -63    114    347       C  
ATOM   1066  C   LEU A 187     -15.096  22.221 -12.826  1.00 43.58           C  
ANISOU 1066  C   LEU A 187     6032   4478   6048   -161    111    306       C  
ATOM   1067  O   LEU A 187     -13.955  21.957 -13.203  1.00 44.51           O  
ANISOU 1067  O   LEU A 187     6105   4612   6194   -287    119    307       O  
ATOM   1068  CB  LEU A 187     -15.761  19.828 -12.575  1.00 42.26           C  
ANISOU 1068  CB  LEU A 187     5714   4620   5723   -108     96    279       C  
ATOM   1069  CG  LEU A 187     -16.818  18.756 -12.374  1.00 45.44           C  
ANISOU 1069  CG  LEU A 187     6054   5165   6047    -24     90    288       C  
ATOM   1070  CD1 LEU A 187     -16.178  17.449 -11.967  1.00 41.71           C  
ANISOU 1070  CD1 LEU A 187     5514   4805   5528    -82     72    227       C  
ATOM   1071  CD2 LEU A 187     -17.815  19.212 -11.319  1.00 48.77           C  
ANISOU 1071  CD2 LEU A 187     6511   5552   6466     99     96    246       C  
ATOM   1072  N   GLU A 188     -15.418  23.370 -12.250  1.00 44.43           N  
ANISOU 1072  N   GLU A 188     6238   4427   6216   -105     99    269       N  
ATOM   1073  CA  GLU A 188     -14.440  24.438 -12.126  1.00 47.44           C  
ANISOU 1073  CA  GLU A 188     6688   4625   6714   -206     87    236       C  
ATOM   1074  C   GLU A 188     -13.669  24.337 -10.815  1.00 50.77           C  
ANISOU 1074  C   GLU A 188     7109   5021   7161   -252     26     68       C  
ATOM   1075  O   GLU A 188     -12.655  25.004 -10.647  1.00 53.95           O  
ANISOU 1075  O   GLU A 188     7536   5294   7669   -367     -3     19       O  
ATOM   1076  CB  GLU A 188     -15.127  25.805 -12.245  1.00 51.10           C  
ANISOU 1076  CB  GLU A 188     7278   4899   7239   -123     94    280       C  
ATOM   1077  CG  GLU A 188     -15.949  25.985 -13.522  1.00 54.37           C  
ANISOU 1077  CG  GLU A 188     7704   5334   7621    -56    140    451       C  
ATOM   1078  CD  GLU A 188     -16.906  27.182 -13.475  1.00 61.04           C  
ANISOU 1078  CD  GLU A 188     8669   6017   8506     80    139    486       C  
ATOM   1079  OE1 GLU A 188     -17.005  27.863 -12.422  1.00 61.99           O  
ANISOU 1079  OE1 GLU A 188     8870   6009   8674    135    109    370       O  
ATOM   1080  OE2 GLU A 188     -17.572  27.445 -14.503  1.00 62.30           O  
ANISOU 1080  OE2 GLU A 188     8849   6179   8643    146    164    628       O  
ATOM   1081  N   ASP A 189     -14.139  23.508  -9.885  1.00 44.24           N  
ANISOU 1081  N   ASP A 189     6253   4316   6239   -164      4    -18       N  
ATOM   1082  CA  ASP A 189     -13.460  23.389  -8.594  1.00 42.71           C  
ANISOU 1082  CA  ASP A 189     6075   4109   6044   -184    -63   -178       C  
ATOM   1083  C   ASP A 189     -12.197  22.552  -8.736  1.00 41.30           C  
ANISOU 1083  C   ASP A 189     5789   4023   5879   -324    -88   -202       C  
ATOM   1084  O   ASP A 189     -12.258  21.335  -8.897  1.00 40.35           O  
ANISOU 1084  O   ASP A 189     5581   4072   5676   -314    -71   -175       O  
ATOM   1085  CB  ASP A 189     -14.384  22.782  -7.539  1.00 45.94           C  
ANISOU 1085  CB  ASP A 189     6499   4621   6334    -35    -64   -246       C  
ATOM   1086  CG  ASP A 189     -13.798  22.856  -6.141  1.00 49.30           C  
ANISOU 1086  CG  ASP A 189     6979   5015   6738    -24   -138   -415       C  
ATOM   1087  OD1 ASP A 189     -12.628  22.475  -5.930  1.00 45.24           O  
ANISOU 1087  OD1 ASP A 189     6414   4524   6250   -139   -196   -478       O  
ATOM   1088  OD2 ASP A 189     -14.496  23.361  -5.243  1.00 58.65           O  
ANISOU 1088  OD2 ASP A 189     8262   6146   7877    107   -143   -489       O  
ATOM   1089  N   ARG A 190     -11.047  23.209  -8.660  1.00 40.76           N  
ANISOU 1089  N   ARG A 190     5722   3838   5925   -452   -132   -255       N  
ATOM   1090  CA  ARG A 190      -9.799  22.513  -8.910  1.00 42.02           C  
ANISOU 1090  CA  ARG A 190     5761   4085   6119   -584   -148   -265       C  
ATOM   1091  C   ARG A 190      -9.478  21.481  -7.827  1.00 40.43           C  
ANISOU 1091  C   ARG A 190     5516   4014   5833   -548   -216   -386       C  
ATOM   1092  O   ARG A 190      -8.981  20.405  -8.137  1.00 40.38           O  
ANISOU 1092  O   ARG A 190     5404   4151   5789   -583   -204   -362       O  
ATOM   1093  CB  ARG A 190      -8.659  23.516  -9.054  1.00 42.16           C  
ANISOU 1093  CB  ARG A 190     5773   3943   6301   -739   -180   -289       C  
ATOM   1094  CG  ARG A 190      -8.788  24.403 -10.298  1.00 44.04           C  
ANISOU 1094  CG  ARG A 190     6043   4065   6626   -798    -96   -136       C  
ATOM   1095  CD  ARG A 190      -7.779  25.555 -10.272  1.00 46.31           C  
ANISOU 1095  CD  ARG A 190     6344   4154   7097   -953   -129   -162       C  
ATOM   1096  NE  ARG A 190      -6.431  25.076  -9.978  1.00 44.97           N  
ANISOU 1096  NE  ARG A 190     6038   4051   6997  -1087   -179   -238       N  
ATOM   1097  CZ  ARG A 190      -5.479  25.804  -9.402  1.00 50.65           C  
ANISOU 1097  CZ  ARG A 190     6744   4633   7868  -1213   -265   -338       C  
ATOM   1098  NH1 ARG A 190      -5.723  27.049  -9.026  1.00 48.76           N  
ANISOU 1098  NH1 ARG A 190     6638   4166   7723  -1224   -312   -384       N  
ATOM   1099  NH2 ARG A 190      -4.275  25.276  -9.185  1.00 53.51           N  
ANISOU 1099  NH2 ARG A 190     6956   5083   8292  -1326   -312   -399       N  
ATOM   1100  N   ASP A 191      -9.757  21.804  -6.569  1.00 38.80           N  
ANISOU 1100  N   ASP A 191     5399   3754   5588   -466   -284   -514       N  
ATOM   1101  CA  ASP A 191      -9.495  20.861  -5.481  1.00 36.13           C  
ANISOU 1101  CA  ASP A 191     5040   3537   5151   -414   -349   -622       C  
ATOM   1102  C   ASP A 191     -10.346  19.598  -5.669  1.00 36.52           C  
ANISOU 1102  C   ASP A 191     5047   3760   5070   -320   -282   -540       C  
ATOM   1103  O   ASP A 191      -9.884  18.470  -5.452  1.00 37.07           O  
ANISOU 1103  O   ASP A 191     5043   3959   5082   -328   -303   -556       O  
ATOM   1104  CB  ASP A 191      -9.797  21.486  -4.118  1.00 41.21           C  
ANISOU 1104  CB  ASP A 191     5815   4095   5748   -316   -423   -766       C  
ATOM   1105  CG  ASP A 191      -8.895  22.678  -3.797  1.00 49.58           C  
ANISOU 1105  CG  ASP A 191     6924   4971   6943   -417   -520   -876       C  
ATOM   1106  OD1 ASP A 191      -7.689  22.469  -3.589  1.00 51.64           O  
ANISOU 1106  OD1 ASP A 191     7105   5249   7267   -529   -605   -946       O  
ATOM   1107  OD2 ASP A 191      -9.394  23.817  -3.715  1.00 53.24           O  
ANISOU 1107  OD2 ASP A 191     7505   5269   7455   -381   -519   -898       O  
ATOM   1108  N   TYR A 192     -11.596  19.781  -6.070  1.00 32.86           N  
ANISOU 1108  N   TYR A 192     4626   3292   4569   -230   -206   -453       N  
ATOM   1109  CA  TYR A 192     -12.449  18.607  -6.233  1.00 32.39           C  
ANISOU 1109  CA  TYR A 192     4517   3386   4404   -154   -151   -378       C  
ATOM   1110  C   TYR A 192     -11.953  17.711  -7.377  1.00 33.20           C  
ANISOU 1110  C   TYR A 192     4509   3586   4522   -244   -124   -288       C  
ATOM   1111  O   TYR A 192     -11.926  16.480  -7.255  1.00 32.47           O  
ANISOU 1111  O   TYR A 192     4360   3619   4359   -229   -126   -282       O  
ATOM   1112  CB  TYR A 192     -13.913  19.006  -6.482  1.00 33.26           C  
ANISOU 1112  CB  TYR A 192     4671   3479   4486    -41    -84   -299       C  
ATOM   1113  CG  TYR A 192     -14.754  17.763  -6.653  1.00 34.29           C  
ANISOU 1113  CG  TYR A 192     4732   3764   4532     15    -38   -224       C  
ATOM   1114  CD1 TYR A 192     -15.209  17.055  -5.550  1.00 33.20           C  
ANISOU 1114  CD1 TYR A 192     4605   3708   4299    102    -33   -268       C  
ATOM   1115  CD2 TYR A 192     -15.019  17.257  -7.915  1.00 33.27           C  
ANISOU 1115  CD2 TYR A 192     4530   3697   4417    -28     -4   -110       C  
ATOM   1116  CE1 TYR A 192     -15.946  15.878  -5.711  1.00 33.69           C  
ANISOU 1116  CE1 TYR A 192     4598   3899   4304    133      9   -191       C  
ATOM   1117  CE2 TYR A 192     -15.720  16.111  -8.081  1.00 34.26           C  
ANISOU 1117  CE2 TYR A 192     4591   3947   4481      5     20    -52       C  
ATOM   1118  CZ  TYR A 192     -16.189  15.421  -6.990  1.00 34.88           C  
ANISOU 1118  CZ  TYR A 192     4671   4094   4487     78     28    -89       C  
ATOM   1119  OH  TYR A 192     -16.901  14.268  -7.211  1.00 35.42           O  
ANISOU 1119  OH  TYR A 192     4671   4273   4515     93     53    -21       O  
ATOM   1120  N   VAL A 193     -11.578  18.332  -8.490  1.00 34.89           N  
ANISOU 1120  N   VAL A 193     4702   3734   4820   -329    -96   -216       N  
ATOM   1121  CA  VAL A 193     -11.135  17.587  -9.657  1.00 33.88           C  
ANISOU 1121  CA  VAL A 193     4485   3697   4692   -399    -58   -131       C  
ATOM   1122  C   VAL A 193      -9.892  16.739  -9.331  1.00 33.17           C  
ANISOU 1122  C   VAL A 193     4313   3686   4606   -466   -101   -200       C  
ATOM   1123  O   VAL A 193      -9.818  15.566  -9.733  1.00 33.82           O  
ANISOU 1123  O   VAL A 193     4333   3889   4629   -459    -86   -169       O  
ATOM   1124  CB  VAL A 193     -10.857  18.540 -10.847  1.00 33.16           C  
ANISOU 1124  CB  VAL A 193     4400   3513   4685   -476    -10    -37       C  
ATOM   1125  CG1 VAL A 193     -10.118  17.818 -11.984  1.00 34.11           C  
ANISOU 1125  CG1 VAL A 193     4430   3730   4799   -552     33     35       C  
ATOM   1126  CG2 VAL A 193     -12.166  19.109 -11.359  1.00 34.80           C  
ANISOU 1126  CG2 VAL A 193     4677   3677   4870   -388     30     54       C  
ATOM   1127  N   VAL A 194      -8.947  17.296  -8.575  1.00 34.92           N  
ANISOU 1127  N   VAL A 194     4535   3838   4896   -522   -165   -301       N  
ATOM   1128  CA  VAL A 194      -7.769  16.523  -8.171  1.00 34.20           C  
ANISOU 1128  CA  VAL A 194     4357   3826   4813   -571   -221   -374       C  
ATOM   1129  C   VAL A 194      -8.187  15.349  -7.286  1.00 34.62           C  
ANISOU 1129  C   VAL A 194     4424   3988   4742   -469   -255   -419       C  
ATOM   1130  O   VAL A 194      -7.773  14.201  -7.515  1.00 33.58           O  
ANISOU 1130  O   VAL A 194     4220   3966   4571   -469   -255   -406       O  
ATOM   1131  CB  VAL A 194      -6.726  17.374  -7.412  1.00 35.55           C  
ANISOU 1131  CB  VAL A 194     4522   3900   5086   -649   -308   -487       C  
ATOM   1132  CG1 VAL A 194      -5.542  16.500  -7.013  1.00 35.54           C  
ANISOU 1132  CG1 VAL A 194     4413   4000   5090   -684   -375   -558       C  
ATOM   1133  CG2 VAL A 194      -6.241  18.543  -8.278  1.00 36.26           C  
ANISOU 1133  CG2 VAL A 194     4594   3865   5319   -770   -269   -431       C  
ATOM   1134  N   TYR A 195      -9.009  15.647  -6.288  1.00 34.90           N  
ANISOU 1134  N   TYR A 195     4556   3986   4717   -376   -278   -468       N  
ATOM   1135  CA  TYR A 195      -9.569  14.637  -5.386  1.00 35.35           C  
ANISOU 1135  CA  TYR A 195     4643   4136   4651   -271   -291   -491       C  
ATOM   1136  C   TYR A 195     -10.199  13.463  -6.125  1.00 37.04           C  
ANISOU 1136  C   TYR A 195     4810   4454   4811   -248   -227   -388       C  
ATOM   1137  O   TYR A 195      -9.838  12.288  -5.899  1.00 33.42           O  
ANISOU 1137  O   TYR A 195     4312   4085   4300   -234   -250   -396       O  
ATOM   1138  CB  TYR A 195     -10.607  15.300  -4.465  1.00 35.89           C  
ANISOU 1138  CB  TYR A 195     4826   4148   4663   -165   -282   -525       C  
ATOM   1139  CG  TYR A 195     -11.592  14.343  -3.837  1.00 35.21           C  
ANISOU 1139  CG  TYR A 195     4766   4157   4454    -54   -243   -491       C  
ATOM   1140  CD1 TYR A 195     -11.163  13.326  -2.978  1.00 38.62           C  
ANISOU 1140  CD1 TYR A 195     5198   4673   4802    -18   -287   -535       C  
ATOM   1141  CD2 TYR A 195     -12.952  14.458  -4.095  1.00 36.62           C  
ANISOU 1141  CD2 TYR A 195     4964   4341   4607     15   -160   -408       C  
ATOM   1142  CE1 TYR A 195     -12.080  12.433  -2.400  1.00 37.02           C  
ANISOU 1142  CE1 TYR A 195     5021   4550   4493     76   -238   -486       C  
ATOM   1143  CE2 TYR A 195     -13.875  13.591  -3.517  1.00 40.39           C  
ANISOU 1143  CE2 TYR A 195     5449   4905   4991    104   -113   -365       C  
ATOM   1144  CZ  TYR A 195     -13.433  12.583  -2.673  1.00 42.13           C  
ANISOU 1144  CZ  TYR A 195     5677   5201   5131    129   -146   -400       C  
ATOM   1145  OH  TYR A 195     -14.355  11.734  -2.113  1.00 44.09           O  
ANISOU 1145  OH  TYR A 195     5934   5526   5294    208    -87   -340       O  
ATOM   1146  N   SER A 196     -11.125  13.764  -7.026  1.00 33.74           N  
ANISOU 1146  N   SER A 196     4396   4018   4406   -241   -159   -293       N  
ATOM   1147  CA  SER A 196     -11.805  12.690  -7.734  1.00 34.44           C  
ANISOU 1147  CA  SER A 196     4444   4196   4448   -221   -117   -205       C  
ATOM   1148  C   SER A 196     -10.903  11.993  -8.744  1.00 34.22           C  
ANISOU 1148  C   SER A 196     4339   4221   4441   -295   -117   -180       C  
ATOM   1149  O   SER A 196     -11.026  10.788  -8.929  1.00 34.93           O  
ANISOU 1149  O   SER A 196     4399   4390   4481   -278   -117   -158       O  
ATOM   1150  CB  SER A 196     -13.067  13.197  -8.443  1.00 36.72           C  
ANISOU 1150  CB  SER A 196     4751   4459   4743   -187    -61   -115       C  
ATOM   1151  OG  SER A 196     -13.646  12.137  -9.222  1.00 36.04           O  
ANISOU 1151  OG  SER A 196     4616   4456   4621   -183    -41    -40       O  
ATOM   1152  N   SER A 197     -10.010  12.726  -9.400  1.00 33.57           N  
ANISOU 1152  N   SER A 197     4226   4094   4434   -375   -110   -181       N  
ATOM   1153  CA  SER A 197      -9.057  12.114 -10.328  1.00 31.60           C  
ANISOU 1153  CA  SER A 197     3898   3906   4201   -434    -94   -160       C  
ATOM   1154  C   SER A 197      -8.216  11.057  -9.592  1.00 32.05           C  
ANISOU 1154  C   SER A 197     3911   4034   4231   -419   -150   -236       C  
ATOM   1155  O   SER A 197      -7.969   9.976 -10.116  1.00 33.21           O  
ANISOU 1155  O   SER A 197     4018   4259   4343   -409   -141   -218       O  
ATOM   1156  CB  SER A 197      -8.134  13.164 -10.959  1.00 34.02           C  
ANISOU 1156  CB  SER A 197     4169   4150   4605   -528    -68   -146       C  
ATOM   1157  OG  SER A 197      -8.852  13.984 -11.878  1.00 35.78           O  
ANISOU 1157  OG  SER A 197     4437   4316   4842   -535     -9    -52       O  
ATOM   1158  N   VAL A 198      -7.796  11.383  -8.380  1.00 35.05           N  
ANISOU 1158  N   VAL A 198     4309   4384   4625   -409   -215   -324       N  
ATOM   1159  CA  VAL A 198      -7.049  10.451  -7.550  1.00 33.86           C  
ANISOU 1159  CA  VAL A 198     4130   4297   4439   -377   -282   -396       C  
ATOM   1160  C   VAL A 198      -7.918   9.308  -7.043  1.00 34.69           C  
ANISOU 1160  C   VAL A 198     4286   4454   4440   -287   -283   -373       C  
ATOM   1161  O   VAL A 198      -7.571   8.136  -7.185  1.00 34.27           O  
ANISOU 1161  O   VAL A 198     4201   4467   4354   -265   -295   -367       O  
ATOM   1162  CB  VAL A 198      -6.427  11.174  -6.353  1.00 35.35           C  
ANISOU 1162  CB  VAL A 198     4338   4437   4656   -381   -368   -503       C  
ATOM   1163  CG1 VAL A 198      -5.800  10.162  -5.407  1.00 34.96           C  
ANISOU 1163  CG1 VAL A 198     4275   4461   4547   -323   -449   -570       C  
ATOM   1164  CG2 VAL A 198      -5.382  12.206  -6.843  1.00 36.76           C  
ANISOU 1164  CG2 VAL A 198     4442   4559   4967   -494   -378   -528       C  
ATOM   1165  N   CYS A 199      -9.063   9.651  -6.463  1.00 33.37           N  
ANISOU 1165  N   CYS A 199     4197   4253   4227   -234   -263   -354       N  
ATOM   1166  CA  CYS A 199      -9.897   8.646  -5.820  1.00 34.32           C  
ANISOU 1166  CA  CYS A 199     4362   4418   4259   -157   -255   -324       C  
ATOM   1167  C   CYS A 199     -10.597   7.753  -6.818  1.00 34.83           C  
ANISOU 1167  C   CYS A 199     4398   4519   4315   -165   -207   -236       C  
ATOM   1168  O   CYS A 199     -10.756   6.548  -6.579  1.00 33.88           O  
ANISOU 1168  O   CYS A 199     4283   4440   4149   -133   -216   -216       O  
ATOM   1169  CB  CYS A 199     -10.926   9.316  -4.913  1.00 38.61           C  
ANISOU 1169  CB  CYS A 199     4985   4925   4760    -91   -231   -326       C  
ATOM   1170  SG  CYS A 199     -10.169   9.777  -3.355  1.00 72.65           S  
ANISOU 1170  SG  CYS A 199     9362   9218   9022    -40   -314   -449       S  
ATOM   1171  N   SER A 200     -10.985   8.324  -7.954  1.00 34.79           N  
ANISOU 1171  N   SER A 200     4371   4493   4355   -208   -164   -183       N  
ATOM   1172  CA  SER A 200     -11.747   7.564  -8.934  1.00 34.51           C  
ANISOU 1172  CA  SER A 200     4317   4490   4306   -213   -135   -109       C  
ATOM   1173  C   SER A 200     -10.864   6.846  -9.919  1.00 35.92           C  
ANISOU 1173  C   SER A 200     4451   4707   4491   -249   -145   -114       C  
ATOM   1174  O   SER A 200     -11.314   5.882 -10.513  1.00 35.56           O  
ANISOU 1174  O   SER A 200     4403   4690   4418   -242   -146    -80       O  
ATOM   1175  CB  SER A 200     -12.710   8.466  -9.711  1.00 33.60           C  
ANISOU 1175  CB  SER A 200     4208   4343   4217   -221    -94    -44       C  
ATOM   1176  OG  SER A 200     -13.634   9.078  -8.833  1.00 38.37           O  
ANISOU 1176  OG  SER A 200     4849   4917   4814   -169    -76    -37       O  
ATOM   1177  N   PHE A 201      -9.622   7.281 -10.104  1.00 31.69           N  
ANISOU 1177  N   PHE A 201     3877   4172   3993   -286   -152   -159       N  
ATOM   1178  CA  PHE A 201      -8.814   6.699 -11.172  1.00 31.23           C  
ANISOU 1178  CA  PHE A 201     3769   4160   3936   -310   -138   -156       C  
ATOM   1179  C   PHE A 201      -7.367   6.362 -10.808  1.00 31.93           C  
ANISOU 1179  C   PHE A 201     3798   4284   4051   -313   -169   -226       C  
ATOM   1180  O   PHE A 201      -6.979   5.194 -10.874  1.00 32.76           O  
ANISOU 1180  O   PHE A 201     3890   4433   4123   -275   -190   -246       O  
ATOM   1181  CB  PHE A 201      -8.829   7.635 -12.390  1.00 33.87           C  
ANISOU 1181  CB  PHE A 201     4090   4479   4299   -358    -80   -101       C  
ATOM   1182  CG  PHE A 201      -8.137   7.075 -13.604  1.00 32.74           C  
ANISOU 1182  CG  PHE A 201     3909   4394   4135   -368    -46    -87       C  
ATOM   1183  CD1 PHE A 201      -8.779   6.153 -14.415  1.00 34.92           C  
ANISOU 1183  CD1 PHE A 201     4218   4704   4346   -333    -48    -59       C  
ATOM   1184  CD2 PHE A 201      -6.858   7.492 -13.942  1.00 34.68           C  
ANISOU 1184  CD2 PHE A 201     4086   4661   4430   -410    -11   -103       C  
ATOM   1185  CE1 PHE A 201      -8.154   5.651 -15.534  1.00 36.37           C  
ANISOU 1185  CE1 PHE A 201     4384   4943   4492   -325    -15    -55       C  
ATOM   1186  CE2 PHE A 201      -6.224   6.995 -15.064  1.00 34.46           C  
ANISOU 1186  CE2 PHE A 201     4023   4698   4373   -404     39    -86       C  
ATOM   1187  CZ  PHE A 201      -6.875   6.062 -15.855  1.00 34.68           C  
ANISOU 1187  CZ  PHE A 201     4102   4759   4314   -353     37    -67       C  
ATOM   1188  N   PHE A 202      -6.564   7.349 -10.427  1.00 35.36           N  
ANISOU 1188  N   PHE A 202     4192   4694   4550   -358   -179   -265       N  
ATOM   1189  CA  PHE A 202      -5.124   7.100 -10.295  1.00 35.12           C  
ANISOU 1189  CA  PHE A 202     4071   4708   4564   -372   -207   -325       C  
ATOM   1190  C   PHE A 202      -4.776   6.210  -9.095  1.00 37.62           C  
ANISOU 1190  C   PHE A 202     4398   5054   4844   -304   -292   -391       C  
ATOM   1191  O   PHE A 202      -3.713   5.620  -9.058  1.00 37.22           O  
ANISOU 1191  O   PHE A 202     4274   5056   4811   -285   -323   -434       O  
ATOM   1192  CB  PHE A 202      -4.353   8.420 -10.211  1.00 34.59           C  
ANISOU 1192  CB  PHE A 202     3946   4599   4598   -455   -206   -349       C  
ATOM   1193  CG  PHE A 202      -4.326   9.181 -11.509  1.00 35.38           C  
ANISOU 1193  CG  PHE A 202     4019   4681   4741   -523   -112   -272       C  
ATOM   1194  CD1 PHE A 202      -3.736   8.632 -12.638  1.00 35.75           C  
ANISOU 1194  CD1 PHE A 202     4004   4802   4780   -526    -46   -235       C  
ATOM   1195  CD2 PHE A 202      -4.914  10.436 -11.611  1.00 37.71           C  
ANISOU 1195  CD2 PHE A 202     4366   4885   5076   -572    -86   -233       C  
ATOM   1196  CE1 PHE A 202      -3.720   9.333 -13.846  1.00 38.11           C  
ANISOU 1196  CE1 PHE A 202     4292   5091   5099   -580     50   -151       C  
ATOM   1197  CE2 PHE A 202      -4.899  11.154 -12.819  1.00 37.70           C  
ANISOU 1197  CE2 PHE A 202     4354   4861   5108   -629      3   -146       C  
ATOM   1198  CZ  PHE A 202      -4.315  10.605 -13.934  1.00 36.95           C  
ANISOU 1198  CZ  PHE A 202     4199   4847   4993   -634     73   -100       C  
ATOM   1199  N   LEU A 203      -5.669   6.125  -8.118  1.00 41.41           N  
ANISOU 1199  N   LEU A 203     4967   5501   5268   -258   -324   -394       N  
ATOM   1200  CA  LEU A 203      -5.446   5.253  -6.967  1.00 41.70           C  
ANISOU 1200  CA  LEU A 203     5035   5562   5248   -182   -397   -438       C  
ATOM   1201  C   LEU A 203      -6.024   3.830  -7.166  1.00 43.74           C  
ANISOU 1201  C   LEU A 203     5338   5841   5440   -124   -384   -390       C  
ATOM   1202  O   LEU A 203      -5.333   2.835  -6.913  1.00 42.44           O  
ANISOU 1202  O   LEU A 203     5159   5710   5256    -71   -429   -417       O  
ATOM   1203  CB  LEU A 203      -6.014   5.923  -5.711  1.00 43.01           C  
ANISOU 1203  CB  LEU A 203     5280   5685   5375   -155   -433   -466       C  
ATOM   1204  CG  LEU A 203      -5.621   5.438  -4.329  1.00 45.10           C  
ANISOU 1204  CG  LEU A 203     5589   5973   5575    -77   -520   -525       C  
ATOM   1205  CD1 LEU A 203      -4.109   5.208  -4.259  1.00 49.64           C  
ANISOU 1205  CD1 LEU A 203     6068   6595   6198    -81   -600   -599       C  
ATOM   1206  CD2 LEU A 203      -6.061   6.473  -3.305  1.00 48.42           C  
ANISOU 1206  CD2 LEU A 203     6085   6349   5964    -60   -545   -569       C  
ATOM   1207  N   PRO A 204      -7.274   3.709  -7.648  1.00 42.05           N  
ANISOU 1207  N   PRO A 204     5175   5600   5203   -134   -330   -319       N  
ATOM   1208  CA  PRO A 204      -7.745   2.343  -7.913  1.00 41.41           C  
ANISOU 1208  CA  PRO A 204     5129   5524   5081    -97   -329   -280       C  
ATOM   1209  C   PRO A 204      -7.022   1.590  -9.049  1.00 42.00           C  
ANISOU 1209  C   PRO A 204     5159   5629   5170    -96   -324   -293       C  
ATOM   1210  O   PRO A 204      -6.909   0.348  -8.974  1.00 39.81           O  
ANISOU 1210  O   PRO A 204     4910   5350   4864    -45   -353   -296       O  
ATOM   1211  CB  PRO A 204      -9.224   2.545  -8.276  1.00 42.33           C  
ANISOU 1211  CB  PRO A 204     5284   5609   5190   -123   -280   -206       C  
ATOM   1212  CG  PRO A 204      -9.371   3.964  -8.589  1.00 43.89           C  
ANISOU 1212  CG  PRO A 204     5459   5792   5424   -168   -246   -204       C  
ATOM   1213  CD  PRO A 204      -8.368   4.689  -7.768  1.00 42.65           C  
ANISOU 1213  CD  PRO A 204     5283   5635   5286   -165   -283   -274       C  
ATOM   1214  N   CYS A 205      -6.544   2.292 -10.077  1.00 39.52           N  
ANISOU 1214  N   CYS A 205     4784   5338   4894   -142   -282   -297       N  
ATOM   1215  CA  CYS A 205      -5.935   1.587 -11.198  1.00 41.08           C  
ANISOU 1215  CA  CYS A 205     4948   5574   5085   -126   -260   -308       C  
ATOM   1216  C   CYS A 205      -4.697   0.753 -10.798  1.00 40.75           C  
ANISOU 1216  C   CYS A 205     4863   5572   5049    -61   -304   -369       C  
ATOM   1217  O   CYS A 205      -4.640  -0.429 -11.124  1.00 41.69           O  
ANISOU 1217  O   CYS A 205     5014   5692   5135     -3   -319   -378       O  
ATOM   1218  CB  CYS A 205      -5.607   2.566 -12.329  1.00 40.96           C  
ANISOU 1218  CB  CYS A 205     4878   5584   5100   -182   -191   -287       C  
ATOM   1219  SG  CYS A 205      -7.099   3.077 -13.208  1.00 54.92           S  
ANISOU 1219  SG  CYS A 205     6714   7316   6838   -222   -151   -209       S  
ATOM   1220  N   PRO A 206      -3.724   1.331 -10.069  1.00 41.44           N  
ANISOU 1220  N   PRO A 206     4878   5688   5181    -65   -335   -415       N  
ATOM   1221  CA  PRO A 206      -2.617   0.454  -9.655  1.00 42.30           C  
ANISOU 1221  CA  PRO A 206     4939   5839   5294     12   -390   -470       C  
ATOM   1222  C   PRO A 206      -3.045  -0.688  -8.728  1.00 42.02           C  
ANISOU 1222  C   PRO A 206     5001   5768   5199     93   -456   -467       C  
ATOM   1223  O   PRO A 206      -2.510  -1.788  -8.816  1.00 43.35           O  
ANISOU 1223  O   PRO A 206     5172   5948   5351    173   -484   -489       O  
ATOM   1224  CB  PRO A 206      -1.662   1.412  -8.921  1.00 43.71           C  
ANISOU 1224  CB  PRO A 206     5022   6048   5537    -20   -433   -521       C  
ATOM   1225  CG  PRO A 206      -2.495   2.597  -8.571  1.00 41.47           C  
ANISOU 1225  CG  PRO A 206     4784   5709   5262    -96   -419   -497       C  
ATOM   1226  CD  PRO A 206      -3.461   2.731  -9.702  1.00 41.76           C  
ANISOU 1226  CD  PRO A 206     4867   5720   5280   -136   -332   -428       C  
ATOM   1227  N   LEU A 207      -3.989  -0.425  -7.841  1.00 41.81           N  
ANISOU 1227  N   LEU A 207     5055   5693   5138     79   -474   -435       N  
ATOM   1228  CA  LEU A 207      -4.442  -1.455  -6.931  1.00 41.50           C  
ANISOU 1228  CA  LEU A 207     5112   5617   5040    149   -519   -411       C  
ATOM   1229  C   LEU A 207      -5.108  -2.595  -7.691  1.00 42.97           C  
ANISOU 1229  C   LEU A 207     5359   5757   5209    162   -494   -368       C  
ATOM   1230  O   LEU A 207      -4.818  -3.761  -7.446  1.00 44.98           O  
ANISOU 1230  O   LEU A 207     5659   5989   5443    235   -535   -371       O  
ATOM   1231  CB  LEU A 207      -5.400  -0.871  -5.895  1.00 42.96           C  
ANISOU 1231  CB  LEU A 207     5367   5769   5185    132   -518   -375       C  
ATOM   1232  CG  LEU A 207      -4.751   0.214  -5.026  1.00 49.50           C  
ANISOU 1232  CG  LEU A 207     6159   6628   6021    129   -564   -436       C  
ATOM   1233  CD1 LEU A 207      -5.721   0.706  -3.945  1.00 53.26           C  
ANISOU 1233  CD1 LEU A 207     6725   7074   6435    139   -558   -407       C  
ATOM   1234  CD2 LEU A 207      -3.418  -0.242  -4.425  1.00 50.08           C  
ANISOU 1234  CD2 LEU A 207     6187   6748   6092    202   -657   -503       C  
ATOM   1235  N   MET A 208      -5.998  -2.262  -8.614  1.00 38.09           N  
ANISOU 1235  N   MET A 208     4750   5120   4603     93   -438   -331       N  
ATOM   1236  CA  MET A 208      -6.626  -3.283  -9.437  1.00 38.06           C  
ANISOU 1236  CA  MET A 208     4801   5070   4590     95   -431   -306       C  
ATOM   1237  C   MET A 208      -5.630  -4.073 -10.309  1.00 39.38           C  
ANISOU 1237  C   MET A 208     4947   5260   4758    155   -441   -363       C  
ATOM   1238  O   MET A 208      -5.766  -5.295 -10.456  1.00 39.89           O  
ANISOU 1238  O   MET A 208     5080   5269   4808    203   -474   -365       O  
ATOM   1239  CB  MET A 208      -7.733  -2.635 -10.278  1.00 40.81           C  
ANISOU 1239  CB  MET A 208     5151   5407   4948     14   -384   -262       C  
ATOM   1240  CG  MET A 208      -7.659  -2.808 -11.773  1.00 44.41           C  
ANISOU 1240  CG  MET A 208     5596   5878   5398      3   -363   -282       C  
ATOM   1241  SD  MET A 208      -9.067  -1.953 -12.543  1.00 44.37           S  
ANISOU 1241  SD  MET A 208     5598   5863   5398    -81   -329   -220       S  
ATOM   1242  CE  MET A 208      -9.064  -0.362 -11.728  1.00 46.99           C  
ANISOU 1242  CE  MET A 208     5880   6219   5756   -118   -290   -197       C  
ATOM   1243  N   LEU A 209      -4.619  -3.405 -10.854  1.00 34.79           N  
ANISOU 1243  N   LEU A 209     4271   4753   4196    157   -411   -406       N  
ATOM   1244  CA  LEU A 209      -3.609  -4.099 -11.656  1.00 37.20           C  
ANISOU 1244  CA  LEU A 209     4541   5097   4497    230   -403   -460       C  
ATOM   1245  C   LEU A 209      -2.802  -5.087 -10.804  1.00 37.92           C  
ANISOU 1245  C   LEU A 209     4641   5179   4587    335   -471   -496       C  
ATOM   1246  O   LEU A 209      -2.481  -6.182 -11.264  1.00 39.79           O  
ANISOU 1246  O   LEU A 209     4918   5394   4808    418   -486   -527       O  
ATOM   1247  CB  LEU A 209      -2.676  -3.097 -12.344  1.00 38.69           C  
ANISOU 1247  CB  LEU A 209     4606   5378   4717    203   -339   -483       C  
ATOM   1248  CG  LEU A 209      -3.392  -2.253 -13.401  1.00 42.28           C  
ANISOU 1248  CG  LEU A 209     5069   5838   5159    120   -267   -441       C  
ATOM   1249  CD1 LEU A 209      -2.473  -1.172 -13.921  1.00 42.85           C  
ANISOU 1249  CD1 LEU A 209     5022   5988   5273     81   -195   -442       C  
ATOM   1250  CD2 LEU A 209      -3.911  -3.105 -14.547  1.00 43.44           C  
ANISOU 1250  CD2 LEU A 209     5297   5962   5245    153   -255   -445       C  
ATOM   1251  N   LEU A 210      -2.496  -4.717  -9.561  1.00 38.89           N  
ANISOU 1251  N   LEU A 210     4740   5316   4722    344   -518   -495       N  
ATOM   1252  CA ALEU A 210      -1.787  -5.617  -8.652  0.48 39.76           C  
ANISOU 1252  CA ALEU A 210     4869   5419   4820    454   -596   -519       C  
ATOM   1253  CA BLEU A 210      -1.773  -5.625  -8.672  0.52 39.73           C  
ANISOU 1253  CA BLEU A 210     4864   5416   4817    455   -595   -520       C  
ATOM   1254  C   LEU A 210      -2.628  -6.844  -8.293  1.00 40.47           C  
ANISOU 1254  C   LEU A 210     5105   5401   4871    494   -629   -472       C  
ATOM   1255  O   LEU A 210      -2.119  -7.983  -8.203  1.00 40.59           O  
ANISOU 1255  O   LEU A 210     5165   5382   4877    599   -674   -491       O  
ATOM   1256  CB ALEU A 210      -1.387  -4.878  -7.378  0.48 39.35           C  
ANISOU 1256  CB ALEU A 210     4775   5405   4771    452   -651   -529       C  
ATOM   1257  CB BLEU A 210      -1.309  -4.883  -7.416  0.52 39.56           C  
ANISOU 1257  CB BLEU A 210     4794   5437   4800    455   -651   -533       C  
ATOM   1258  CG ALEU A 210      -0.899  -5.766  -6.235  0.48 40.37           C  
ANISOU 1258  CG ALEU A 210     4955   5520   4863    570   -745   -535       C  
ATOM   1259  CG BLEU A 210      -0.166  -3.876  -7.615  0.52 39.58           C  
ANISOU 1259  CG BLEU A 210     4634   5538   4867    429   -647   -592       C  
ATOM   1260  CD1ALEU A 210       0.424  -6.439  -6.592  0.48 41.25           C  
ANISOU 1260  CD1ALEU A 210     4981   5685   5006    679   -780   -597       C  
ATOM   1261  CD1BLEU A 210       0.078  -3.079  -6.348  0.52 41.14           C  
ANISOU 1261  CD1BLEU A 210     4808   5756   5066    413   -722   -614       C  
ATOM   1262  CD2ALEU A 210      -0.767  -4.959  -4.953  0.48 40.70           C  
ANISOU 1262  CD2ALEU A 210     4987   5594   4882    562   -806   -544       C  
ATOM   1263  CD2BLEU A 210       1.112  -4.580  -8.047  0.52 40.61           C  
ANISOU 1263  CD2BLEU A 210     4669   5731   5029    529   -664   -646       C  
ATOM   1264  N   LEU A 211      -3.917  -6.622  -8.072  1.00 36.97           N  
ANISOU 1264  N   LEU A 211     4735   4899   4413    411   -605   -406       N  
ATOM   1265  CA  LEU A 211      -4.803  -7.720  -7.696  1.00 39.90           C  
ANISOU 1265  CA  LEU A 211     5232   5161   4766    424   -627   -345       C  
ATOM   1266  C   LEU A 211      -5.051  -8.674  -8.855  1.00 40.87           C  
ANISOU 1266  C   LEU A 211     5406   5219   4906    430   -624   -364       C  
ATOM   1267  O   LEU A 211      -5.075  -9.889  -8.648  1.00 41.62           O  
ANISOU 1267  O   LEU A 211     5592   5222   4998    491   -667   -353       O  
ATOM   1268  CB  LEU A 211      -6.132  -7.182  -7.160  1.00 38.76           C  
ANISOU 1268  CB  LEU A 211     5128   4987   4614    332   -591   -265       C  
ATOM   1269  CG  LEU A 211      -6.045  -6.691  -5.718  1.00 40.48           C  
ANISOU 1269  CG  LEU A 211     5358   5233   4788    361   -608   -237       C  
ATOM   1270  CD1 LEU A 211      -7.363  -6.090  -5.262  1.00 42.62           C  
ANISOU 1270  CD1 LEU A 211     5659   5487   5049    283   -553   -161       C  
ATOM   1271  CD2 LEU A 211      -5.652  -7.870  -4.819  1.00 42.33           C  
ANISOU 1271  CD2 LEU A 211     5681   5417   4985    465   -667   -211       C  
ATOM   1272  N   TYR A 212      -5.254  -8.148 -10.063  1.00 38.81           N  
ANISOU 1272  N   TYR A 212     5099   4993   4654    372   -579   -393       N  
ATOM   1273  CA  TYR A 212      -5.428  -9.022 -11.222  1.00 39.41           C  
ANISOU 1273  CA  TYR A 212     5233   5014   4727    390   -587   -430       C  
ATOM   1274  C   TYR A 212      -4.172  -9.872 -11.389  1.00 43.18           C  
ANISOU 1274  C   TYR A 212     5711   5499   5195    526   -615   -502       C  
ATOM   1275  O   TYR A 212      -4.263 -11.079 -11.639  1.00 41.19           O  
ANISOU 1275  O   TYR A 212     5559   5148   4942    584   -658   -523       O  
ATOM   1276  CB  TYR A 212      -5.724  -8.224 -12.493  1.00 39.47           C  
ANISOU 1276  CB  TYR A 212     5194   5080   4724    325   -535   -451       C  
ATOM   1277  CG  TYR A 212      -7.180  -7.793 -12.609  1.00 39.74           C  
ANISOU 1277  CG  TYR A 212     5255   5075   4772    209   -528   -386       C  
ATOM   1278  CD1 TYR A 212      -8.200  -8.739 -12.693  1.00 42.47           C  
ANISOU 1278  CD1 TYR A 212     5691   5308   5137    174   -575   -360       C  
ATOM   1279  CD2 TYR A 212      -7.533  -6.446 -12.624  1.00 37.54           C  
ANISOU 1279  CD2 TYR A 212     4904   4863   4496    136   -478   -351       C  
ATOM   1280  CE1 TYR A 212      -9.524  -8.358 -12.794  1.00 40.12           C  
ANISOU 1280  CE1 TYR A 212     5393   4985   4866     70   -573   -299       C  
ATOM   1281  CE2 TYR A 212      -8.859  -6.054 -12.717  1.00 40.38           C  
ANISOU 1281  CE2 TYR A 212     5277   5193   4871     47   -473   -291       C  
ATOM   1282  CZ  TYR A 212      -9.849  -7.021 -12.798  1.00 41.68           C  
ANISOU 1282  CZ  TYR A 212     5513   5263   5059     15   -520   -265       C  
ATOM   1283  OH  TYR A 212     -11.167  -6.640 -12.891  1.00 39.10           O  
ANISOU 1283  OH  TYR A 212     5176   4919   4763    -73   -518   -204       O  
ATOM   1284  N   TRP A 213      -3.003  -9.254 -11.202  1.00 40.29           N  
ANISOU 1284  N   TRP A 213     5231   5244   4831    578   -596   -540       N  
ATOM   1285  CA  TRP A 213      -1.732  -9.981 -11.339  1.00 41.90           C  
ANISOU 1285  CA  TRP A 213     5406   5479   5035    720   -617   -607       C  
ATOM   1286  C   TRP A 213      -1.563 -11.118 -10.318  1.00 44.36           C  
ANISOU 1286  C   TRP A 213     5809   5699   5346    819   -699   -590       C  
ATOM   1287  O   TRP A 213      -1.179 -12.246 -10.678  1.00 46.08           O  
ANISOU 1287  O   TRP A 213     6096   5853   5560    929   -729   -632       O  
ATOM   1288  CB  TRP A 213      -0.555  -9.015 -11.231  1.00 41.84           C  
ANISOU 1288  CB  TRP A 213     5231   5615   5052    739   -585   -640       C  
ATOM   1289  CG  TRP A 213       0.767  -9.720 -11.125  1.00 51.26           C  
ANISOU 1289  CG  TRP A 213     6367   6852   6257    893   -616   -701       C  
ATOM   1290  CD1 TRP A 213       1.513 -10.231 -12.149  1.00 49.59           C  
ANISOU 1290  CD1 TRP A 213     6121   6681   6038    992   -573   -765       C  
ATOM   1291  CD2 TRP A 213       1.498  -9.991  -9.920  1.00 56.56           C  
ANISOU 1291  CD2 TRP A 213     7006   7539   6944    979   -697   -703       C  
ATOM   1292  NE1 TRP A 213       2.666 -10.800 -11.657  1.00 49.44           N  
ANISOU 1292  NE1 TRP A 213     6039   6704   6043   1136   -620   -806       N  
ATOM   1293  CE2 TRP A 213       2.678 -10.670 -10.293  1.00 54.55           C  
ANISOU 1293  CE2 TRP A 213     6687   7335   6706   1130   -704   -769       C  
ATOM   1294  CE3 TRP A 213       1.265  -9.731  -8.563  1.00 56.80           C  
ANISOU 1294  CE3 TRP A 213     7063   7551   6967    957   -766   -658       C  
ATOM   1295  CZ2 TRP A 213       3.625 -11.089  -9.352  1.00 54.43           C  
ANISOU 1295  CZ2 TRP A 213     6622   7351   6708   1255   -789   -787       C  
ATOM   1296  CZ3 TRP A 213       2.211 -10.149  -7.629  1.00 53.92           C  
ANISOU 1296  CZ3 TRP A 213     6663   7217   6605   1081   -854   -678       C  
ATOM   1297  CH2 TRP A 213       3.374 -10.815  -8.031  1.00 52.20           C  
ANISOU 1297  CH2 TRP A 213     6371   7049   6413   1226   -870   -741       C  
ATOM   1298  N   ALA A 214      -1.844 -10.827  -9.053  1.00 40.73           N  
ANISOU 1298  N   ALA A 214     5364   5229   4884    790   -733   -528       N  
ATOM   1299  CA  ALA A 214      -1.805 -11.839  -8.001  1.00 41.17           C  
ANISOU 1299  CA  ALA A 214     5523   5194   4924    878   -805   -487       C  
ATOM   1300  C   ALA A 214      -2.780 -12.988  -8.276  1.00 42.62           C  
ANISOU 1300  C   ALA A 214     5864   5213   5116    859   -818   -446       C  
ATOM   1301  O   ALA A 214      -2.453 -14.144  -8.048  1.00 45.51           O  
ANISOU 1301  O   ALA A 214     6322   5485   5483    966   -871   -447       O  
ATOM   1302  CB  ALA A 214      -2.114 -11.212  -6.659  1.00 39.55           C  
ANISOU 1302  CB  ALA A 214     5321   5014   4692    841   -824   -421       C  
ATOM   1303  N   THR A 215      -3.975 -12.651  -8.754  1.00 40.72           N  
ANISOU 1303  N   THR A 215     5649   4934   4890    722   -778   -408       N  
ATOM   1304  CA  THR A 215      -5.009 -13.632  -9.054  1.00 43.83           C  
ANISOU 1304  CA  THR A 215     6170   5171   5311    672   -797   -369       C  
ATOM   1305  C   THR A 215      -4.576 -14.600 -10.147  1.00 43.17           C  
ANISOU 1305  C   THR A 215     6146   5020   5237    752   -829   -460       C  
ATOM   1306  O   THR A 215      -4.698 -15.817  -9.994  1.00 42.16           O  
ANISOU 1306  O   THR A 215     6142   4744   5131    803   -882   -449       O  
ATOM   1307  CB  THR A 215      -6.315 -12.957  -9.490  1.00 42.49           C  
ANISOU 1307  CB  THR A 215     5981   5000   5163    511   -755   -326       C  
ATOM   1308  OG1 THR A 215      -6.835 -12.196  -8.399  1.00 42.29           O  
ANISOU 1308  OG1 THR A 215     5923   5017   5128    451   -722   -238       O  
ATOM   1309  CG2 THR A 215      -7.348 -14.013  -9.901  1.00 43.75           C  
ANISOU 1309  CG2 THR A 215     6254   4998   5372    449   -791   -298       C  
ATOM   1310  N   PHE A 216      -4.072 -14.065 -11.251  1.00 44.56           N  
ANISOU 1310  N   PHE A 216     6241   5297   5391    768   -792   -547       N  
ATOM   1311  CA  PHE A 216      -3.601 -14.919 -12.336  1.00 46.36           C  
ANISOU 1311  CA  PHE A 216     6529   5480   5607    865   -811   -645       C  
ATOM   1312  C   PHE A 216      -2.434 -15.782 -11.886  1.00 47.07           C  
ANISOU 1312  C   PHE A 216     6643   5547   5695   1043   -850   -684       C  
ATOM   1313  O   PHE A 216      -2.342 -16.961 -12.241  1.00 48.22           O  
ANISOU 1313  O   PHE A 216     6910   5563   5847   1132   -899   -730       O  
ATOM   1314  CB  PHE A 216      -3.217 -14.076 -13.546  1.00 46.27           C  
ANISOU 1314  CB  PHE A 216     6421   5607   5554    859   -743   -716       C  
ATOM   1315  CG  PHE A 216      -4.391 -13.676 -14.384  1.00 44.90           C  
ANISOU 1315  CG  PHE A 216     6276   5411   5371    725   -731   -706       C  
ATOM   1316  CD1 PHE A 216      -4.941 -14.572 -15.294  1.00 48.27           C  
ANISOU 1316  CD1 PHE A 216     6828   5725   5788    730   -782   -764       C  
ATOM   1317  CD2 PHE A 216      -4.952 -12.414 -14.269  1.00 48.01           C  
ANISOU 1317  CD2 PHE A 216     6579   5894   5767    602   -682   -645       C  
ATOM   1318  CE1 PHE A 216      -6.027 -14.217 -16.074  1.00 49.73           C  
ANISOU 1318  CE1 PHE A 216     7035   5897   5964    612   -792   -759       C  
ATOM   1319  CE2 PHE A 216      -6.043 -12.046 -15.047  1.00 47.45           C  
ANISOU 1319  CE2 PHE A 216     6532   5809   5689    492   -681   -632       C  
ATOM   1320  CZ  PHE A 216      -6.581 -12.953 -15.951  1.00 50.15           C  
ANISOU 1320  CZ  PHE A 216     6987   6049   6019    496   -740   -689       C  
ATOM   1321  N   ARG A 217      -1.545 -15.205 -11.090  1.00 45.38           N  
ANISOU 1321  N   ARG A 217     6317   5451   5475   1100   -839   -668       N  
ATOM   1322  CA  ARG A 217      -0.402 -15.966 -10.595  1.00 47.60           C  
ANISOU 1322  CA  ARG A 217     6601   5727   5757   1281   -887   -701       C  
ATOM   1323  C   ARG A 217      -0.887 -17.049  -9.625  1.00 47.94           C  
ANISOU 1323  C   ARG A 217     6806   5594   5816   1311   -963   -625       C  
ATOM   1324  O   ARG A 217      -0.401 -18.190  -9.650  1.00 46.50           O  
ANISOU 1324  O   ARG A 217     6720   5308   5642   1453  -1015   -657       O  
ATOM   1325  CB  ARG A 217       0.614 -15.037  -9.927  1.00 46.26           C  
ANISOU 1325  CB  ARG A 217     6260   5730   5586   1320   -877   -703       C  
ATOM   1326  CG  ARG A 217       2.000 -15.642  -9.768  1.00 51.59           C  
ANISOU 1326  CG  ARG A 217     6881   6452   6268   1520   -916   -764       C  
ATOM   1327  N   GLY A 218      -1.869 -16.692  -8.800  1.00 50.20           N  
ANISOU 1327  N   GLY A 218     7127   5842   6106   1181   -960   -519       N  
ATOM   1328  CA  GLY A 218      -2.485 -17.620  -7.868  1.00 47.98           C  
ANISOU 1328  CA  GLY A 218     6997   5395   5838   1182  -1008   -418       C  
ATOM   1329  C   GLY A 218      -3.088 -18.844  -8.542  1.00 49.83           C  
ANISOU 1329  C   GLY A 218     7386   5428   6118   1174  -1042   -432       C  
ATOM   1330  O   GLY A 218      -2.913 -19.972  -8.079  1.00 50.06           O  
ANISOU 1330  O   GLY A 218     7546   5309   6165   1269  -1099   -400       O  
ATOM   1331  N   LEU A 219      -3.799 -18.627  -9.640  1.00 50.80           N  
ANISOU 1331  N   LEU A 219     7504   5538   6262   1062  -1016   -480       N  
ATOM   1332  CA  LEU A 219      -4.394 -19.736 -10.368  1.00 51.81           C  
ANISOU 1332  CA  LEU A 219     7776   5472   6436   1042  -1066   -515       C  
ATOM   1333  C   LEU A 219      -3.358 -20.638 -11.023  1.00 51.36           C  
ANISOU 1333  C   LEU A 219     7785   5364   6365   1231  -1108   -634       C  
ATOM   1334  O   LEU A 219      -3.484 -21.869 -10.981  1.00 51.85           O  
ANISOU 1334  O   LEU A 219     8007   5225   6469   1286  -1174   -636       O  
ATOM   1335  CB  LEU A 219      -5.365 -19.229 -11.432  1.00 51.54           C  
ANISOU 1335  CB  LEU A 219     7714   5455   6416    888  -1045   -552       C  
ATOM   1336  CG  LEU A 219      -6.690 -18.697 -10.897  1.00 49.53           C  
ANISOU 1336  CG  LEU A 219     7431   5185   6202    697  -1019   -431       C  
ATOM   1337  CD1 LEU A 219      -7.460 -17.961 -11.975  1.00 48.63           C  
ANISOU 1337  CD1 LEU A 219     7253   5137   6088    571  -1000   -476       C  
ATOM   1338  CD2 LEU A 219      -7.499 -19.848 -10.319  1.00 50.01           C  
ANISOU 1338  CD2 LEU A 219     7635   5024   6345    639  -1070   -340       C  
ATOM   1339  N   GLN A 220      -2.343 -20.029 -11.631  1.00 50.58           N  
ANISOU 1339  N   GLN A 220     7563   5441   6213   1331  -1065   -731       N  
ATOM   1340  CA  GLN A 220      -1.268 -20.783 -12.258  1.00 51.75           C  
ANISOU 1340  CA  GLN A 220     7747   5575   6340   1532  -1085   -847       C  
ATOM   1341  C   GLN A 220      -0.696 -21.841 -11.324  1.00 52.62           C  
ANISOU 1341  C   GLN A 220     7957   5560   6475   1685  -1153   -810       C  
ATOM   1342  O   GLN A 220      -0.393 -22.962 -11.743  1.00 50.92           O  
ANISOU 1342  O   GLN A 220     7875   5200   6274   1817  -1204   -880       O  
ATOM   1343  CB  GLN A 220      -0.156 -19.854 -12.700  1.00 52.92           C  
ANISOU 1343  CB  GLN A 220     7708   5961   6439   1617  -1010   -917       C  
ATOM   1344  CG  GLN A 220      -0.393 -19.228 -14.040  1.00 57.74           C  
ANISOU 1344  CG  GLN A 220     8269   6663   7005   1552   -944   -995       C  
ATOM   1345  CD  GLN A 220       0.858 -19.244 -14.893  1.00 62.27           C  
ANISOU 1345  CD  GLN A 220     8762   7365   7530   1731   -887  -1108       C  
ATOM   1346  OE1 GLN A 220       1.887 -19.779 -14.486  1.00 60.59           O  
ANISOU 1346  OE1 GLN A 220     8525   7165   7329   1906   -905  -1135       O  
ATOM   1347  NE2 GLN A 220       0.773 -18.667 -16.087  1.00 66.93           N  
ANISOU 1347  NE2 GLN A 220     9310   8056   8063   1696   -814  -1170       N  
ATOM   1348  N   ARG A 221      -0.570 -21.480 -10.052  1.00 54.35           N  
ANISOU 1348  N   ARG A 221     8126   5831   6695   1675  -1160   -700       N  
ATOM   1349  CA  ARG A 221      -0.030 -22.383  -9.041  1.00 54.61           C  
ANISOU 1349  CA  ARG A 221     8252   5761   6737   1825  -1228   -644       C  
ATOM   1350  C   ARG A 221      -0.892 -23.633  -8.850  1.00 53.42           C  
ANISOU 1350  C   ARG A 221     8326   5331   6641   1790  -1287   -580       C  
ATOM   1351  O   ARG A 221      -0.409 -24.661  -8.373  1.00 56.22           O  
ANISOU 1351  O   ARG A 221     8803   5550   7010   1944  -1350   -560       O  
ATOM   1352  CB  ARG A 221       0.127 -21.636  -7.710  1.00 59.21           C  
ANISOU 1352  CB  ARG A 221     8746   6463   7288   1802  -1226   -535       C  
ATOM   1353  CG  ARG A 221       1.559 -21.545  -7.199  1.00 64.30           C  
ANISOU 1353  CG  ARG A 221     9285   7244   7902   2002  -1263   -573       C  
ATOM   1354  CD  ARG A 221       1.972 -20.107  -6.935  1.00 64.58           C  
ANISOU 1354  CD  ARG A 221     9108   7521   7909   1939  -1222   -584       C  
ATOM   1355  NE  ARG A 221       1.029 -19.419  -6.057  1.00 68.03           N  
ANISOU 1355  NE  ARG A 221     9559   7966   8323   1775  -1205   -472       N  
ATOM   1356  CZ  ARG A 221       1.068 -18.115  -5.796  1.00 70.01           C  
ANISOU 1356  CZ  ARG A 221     9660   8387   8552   1681  -1168   -472       C  
ATOM   1357  NH1 ARG A 221       2.010 -17.354  -6.341  1.00 69.14           N  
ANISOU 1357  NH1 ARG A 221     9366   8450   8452   1717  -1145   -568       N  
ATOM   1358  NH2 ARG A 221       0.165 -17.566  -4.992  1.00 71.83           N  
ANISOU 1358  NH2 ARG A 221     9924   8612   8755   1551  -1149   -373       N  
ATOM   1359  N   TRP A 222      -2.163 -23.554  -9.232  1.00 55.52           N  
ANISOU 1359  N   TRP A 222     8643   5504   6946   1589  -1270   -546       N  
ATOM   1360  CA  TRP A 222      -3.063 -24.707  -9.107  1.00 55.05           C  
ANISOU 1360  CA  TRP A 222     8781   5170   6964   1522  -1325   -483       C  
ATOM   1361  C   TRP A 222      -3.064 -25.631 -10.316  1.00 55.82           C  
ANISOU 1361  C   TRP A 222     9003   5107   7098   1575  -1381   -621       C  
ATOM   1362  O   TRP A 222      -3.642 -26.712 -10.267  1.00 55.41           O  
ANISOU 1362  O   TRP A 222     9128   4802   7123   1542  -1444   -589       O  
ATOM   1363  CB  TRP A 222      -4.493 -24.237  -8.850  1.00 57.85           C  
ANISOU 1363  CB  TRP A 222     9122   5495   7364   1272  -1289   -370       C  
ATOM   1364  CG  TRP A 222      -4.680 -23.736  -7.469  1.00 64.79           C  
ANISOU 1364  CG  TRP A 222     9958   6445   8215   1233  -1247   -211       C  
ATOM   1365  CD1 TRP A 222      -4.530 -22.455  -7.039  1.00 64.45           C  
ANISOU 1365  CD1 TRP A 222     9753   6629   8106   1198  -1185   -188       C  
ATOM   1366  CD2 TRP A 222      -5.026 -24.512  -6.316  1.00 67.50           C  
ANISOU 1366  CD2 TRP A 222    10434   6628   8585   1236  -1263    -53       C  
ATOM   1367  NE1 TRP A 222      -4.772 -22.378  -5.690  1.00 66.77           N  
ANISOU 1367  NE1 TRP A 222    10075   6921   8372   1186  -1166    -37       N  
ATOM   1368  CE2 TRP A 222      -5.080 -23.628  -5.222  1.00 68.26           C  
ANISOU 1368  CE2 TRP A 222    10443   6881   8612   1210  -1206     56       C  
ATOM   1369  CE3 TRP A 222      -5.302 -25.866  -6.104  1.00 68.10           C  
ANISOU 1369  CE3 TRP A 222    10704   6436   8735   1258  -1318     10       C  
ATOM   1370  CZ2 TRP A 222      -5.398 -24.051  -3.933  1.00 68.43           C  
ANISOU 1370  CZ2 TRP A 222    10567   6817   8618   1216  -1195    229       C  
ATOM   1371  CZ3 TRP A 222      -5.614 -26.287  -4.819  1.00 69.86           C  
ANISOU 1371  CZ3 TRP A 222    11023   6564   8956   1253  -1303    196       C  
ATOM   1372  CH2 TRP A 222      -5.664 -25.378  -3.753  1.00 67.96           C  
ANISOU 1372  CH2 TRP A 222    10692   6501   8629   1236  -1238    305       C  
ATOM   1373  N   GLU A 223      -2.423 -25.213 -11.399  1.00 53.35           N  
ANISOU 1373  N   GLU A 223     8606   4937   6730   1657  -1355   -773       N  
ATOM   1374  CA  GLU A 223      -2.490 -25.962 -12.648  1.00 51.98           C  
ANISOU 1374  CA  GLU A 223     8552   4634   6564   1706  -1402   -921       C  
ATOM   1375  C   GLU A 223      -1.482 -27.110 -12.710  1.00 54.41           C  
ANISOU 1375  C   GLU A 223     8986   4815   6871   1957  -1458  -1002       C  
ATOM   1376  O   GLU A 223      -0.276 -26.901 -12.569  1.00 52.63           O  
ANISOU 1376  O   GLU A 223     8663   4744   6592   2148  -1424  -1042       O  
ATOM   1377  CB  GLU A 223      -2.313 -24.994 -13.826  1.00 50.06           C  
ANISOU 1377  CB  GLU A 223     8174   4602   6242   1687  -1337  -1040       C  
ATOM   1378  CG  GLU A 223      -3.461 -24.000 -13.906  1.00 50.18           C  
ANISOU 1378  CG  GLU A 223     8100   4698   6269   1442  -1302   -969       C  
ATOM   1379  CD  GLU A 223      -3.305 -22.916 -14.979  1.00 51.68           C  
ANISOU 1379  CD  GLU A 223     8155   5107   6376   1418  -1230  -1058       C  
ATOM   1380  OE1 GLU A 223      -2.354 -22.960 -15.787  1.00 51.83           O  
ANISOU 1380  OE1 GLU A 223     8154   5216   6322   1583  -1199  -1181       O  
ATOM   1381  OE2 GLU A 223      -4.169 -22.026 -15.024  1.00 51.38           O  
ANISOU 1381  OE2 GLU A 223     8033   5146   6342   1237  -1199   -998       O  
ATOM   1382  N   VAL A 224      -1.978 -28.338 -12.903  1.00 50.99           N  
ANISOU 1382  N   VAL A 224     8769   4094   6509   1957  -1547  -1025       N  
ATOM   1383  CA  VAL A 224      -1.084 -29.481 -12.944  1.00 52.37           C  
ANISOU 1383  CA  VAL A 224     9088   4120   6691   2203  -1606  -1099       C  
ATOM   1384  C   VAL A 224      -0.264 -29.429 -14.218  1.00 52.66           C  
ANISOU 1384  C   VAL A 224     9093   4270   6643   2377  -1580  -1301       C  
ATOM   1385  O   VAL A 224      -0.709 -28.897 -15.233  1.00 52.13           O  
ANISOU 1385  O   VAL A 224     8985   4289   6533   2278  -1552  -1391       O  
ATOM   1386  CB  VAL A 224      -1.841 -30.874 -12.869  1.00 56.02           C  
ANISOU 1386  CB  VAL A 224     9789   4238   7258   2136  -1704  -1069       C  
ATOM   1387  CG1 VAL A 224      -2.768 -30.928 -11.661  1.00 57.43           C  
ANISOU 1387  CG1 VAL A 224    10019   4274   7528   1961  -1720   -861       C  
ATOM   1388  CG2 VAL A 224      -2.636 -31.118 -14.138  1.00 54.30           C  
ANISOU 1388  CG2 VAL A 224     9640   3937   7056   2005  -1743  -1195       C  
ATOM   1389  N   ALA A 225       0.934 -29.992 -14.154  1.00 50.22           N  
ANISOU 1389  N   ALA A 225     8772   4008   6300   2610  -1570  -1345       N  
ATOM   1390  CA  ALA A 225       1.790 -30.145 -15.324  1.00 51.32           C  
ANISOU 1390  CA  ALA A 225     8871   4275   6356   2772  -1522  -1508       C  
ATOM   1391  C   ALA A 225       1.170 -31.045 -16.391  1.00 52.95           C  
ANISOU 1391  C   ALA A 225     9250   4306   6562   2713  -1577  -1613       C  
ATOM   1392  O   ALA A 225       1.183 -30.717 -17.579  1.00 52.95           O  
ANISOU 1392  O   ALA A 225     9224   4413   6481   2722  -1538  -1739       O  
ATOM   1393  CB  ALA A 225       3.151 -30.698 -14.906  1.00 52.92           C  
ANISOU 1393  CB  ALA A 225     9021   4547   6539   3015  -1507  -1509       C  
ATOM   1394  N   ARG A 226       0.633 -32.183 -15.975  1.00 54.12           N  
ANISOU 1394  N   ARG A 226     9574   4190   6799   2653  -1666  -1556       N  
ATOM   1395  CA  ARG A 226       0.060 -33.122 -16.935  1.00 56.00           C  
ANISOU 1395  CA  ARG A 226     9976   4249   7053   2599  -1735  -1658       C  
ATOM   1396  C   ARG A 226      -1.409 -32.792 -17.244  1.00 54.97           C  
ANISOU 1396  C   ARG A 226     9889   4021   6978   2324  -1786  -1640       C  
ATOM   1397  O   ARG A 226      -2.314 -33.567 -16.943  1.00 56.01           O  
ANISOU 1397  O   ARG A 226    10148   3914   7221   2172  -1868  -1577       O  
ATOM   1398  CB  ARG A 226       0.226 -34.545 -16.425  1.00 58.54           C  
ANISOU 1398  CB  ARG A 226    10459   4331   7451   2669  -1805  -1617       C  
ATOM   1399  CG  ARG A 226       1.708 -34.939 -16.352  1.00 59.95           C  
ANISOU 1399  CG  ARG A 226    10596   4616   7567   2956  -1761  -1664       C  
ATOM   1400  CD  ARG A 226       1.935 -36.354 -15.912  1.00 62.67           C  
ANISOU 1400  CD  ARG A 226    11107   4726   7979   3046  -1829  -1634       C  
ATOM   1401  NE  ARG A 226       3.363 -36.663 -15.866  1.00 64.05           N  
ANISOU 1401  NE  ARG A 226    11223   5021   8093   3323  -1788  -1681       N  
ATOM   1402  CZ  ARG A 226       4.095 -36.993 -16.925  1.00 65.65           C  
ANISOU 1402  CZ  ARG A 226    11431   5298   8216   3494  -1759  -1837       C  
ATOM   1403  NH1 ARG A 226       3.538 -37.078 -18.125  1.00 66.11           N  
ANISOU 1403  NH1 ARG A 226    11565   5320   8235   3424  -1774  -1965       N  
ATOM   1404  NH2 ARG A 226       5.388 -37.264 -16.784  1.00 67.00           N  
ANISOU 1404  NH2 ARG A 226    11530   5581   8346   3741  -1718  -1862       N  
ATOM   1405  N   ARG A 227      -1.599 -31.640 -17.883  1.00 54.89           N  
ANISOU 1405  N   ARG A 227     9759   4205   6890   2266  -1733  -1696       N  
ATOM   1406  CA AARG A 227      -2.925 -31.111 -18.198  0.51 53.70           C  
ANISOU 1406  CA AARG A 227     9610   4014   6779   2014  -1775  -1680       C  
ATOM   1407  CA BARG A 227      -2.922 -31.111 -18.205  0.49 53.70           C  
ANISOU 1407  CA BARG A 227     9611   4015   6779   2015  -1775  -1681       C  
ATOM   1408  C   ARG A 227      -3.752 -32.046 -19.081  1.00 55.69           C  
ANISOU 1408  C   ARG A 227    10010   4080   7070   1908  -1879  -1765       C  
ATOM   1409  O   ARG A 227      -4.926 -32.283 -18.805  1.00 55.78           O  
ANISOU 1409  O   ARG A 227    10069   3925   7198   1686  -1954  -1691       O  
ATOM   1410  CB AARG A 227      -2.799 -29.749 -18.887  0.51 51.73           C  
ANISOU 1410  CB AARG A 227     9213   4029   6414   2012  -1693  -1746       C  
ATOM   1411  CB BARG A 227      -2.779 -29.757 -18.904  0.49 51.76           C  
ANISOU 1411  CB BARG A 227     9217   4035   6416   2016  -1692  -1749       C  
ATOM   1412  CG AARG A 227      -4.131 -29.058 -19.157  0.51 50.37           C  
ANISOU 1412  CG AARG A 227     9019   3845   6275   1758  -1734  -1722       C  
ATOM   1413  CG BARG A 227      -4.086 -29.122 -19.345  0.49 50.60           C  
ANISOU 1413  CG BARG A 227     9056   3880   6290   1772  -1736  -1744       C  
ATOM   1414  CD AARG A 227      -4.030 -28.000 -20.256  0.51 49.31           C  
ANISOU 1414  CD AARG A 227     8786   3950   6000   1772  -1669  -1826       C  
ATOM   1415  CD BARG A 227      -3.873 -27.681 -19.804  0.49 48.55           C  
ANISOU 1415  CD BARG A 227     8639   3893   5915   1777  -1639  -1779       C  
ATOM   1416  NE AARG A 227      -3.528 -28.558 -21.510  0.51 51.21           N  
ANISOU 1416  NE AARG A 227     9094   4231   6131   1914  -1668  -1973       N  
ATOM   1417  NE BARG A 227      -3.089 -26.946 -18.820  0.49 47.03           N  
ANISOU 1417  NE BARG A 227     8260   3893   5718   1828  -1522  -1650       N  
ATOM   1418  CZ AARG A 227      -4.291 -29.135 -22.435  0.51 52.68           C  
ANISOU 1418  CZ AARG A 227     9392   4312   6312   1828  -1762  -2053       C  
ATOM   1419  CZ BARG A 227      -3.040 -25.623 -18.706  0.49 44.98           C  
ANISOU 1419  CZ BARG A 227     7792   3888   5408   1744  -1417  -1574       C  
ATOM   1420  NH1AARG A 227      -5.602 -29.231 -22.256  0.51 52.47           N  
ANISOU 1420  NH1AARG A 227     9401   4140   6396   1591  -1865  -1998       N  
ATOM   1421  NH1BARG A 227      -3.741 -24.837 -19.514  0.49 44.91           N  
ANISOU 1421  NH1BARG A 227     7731   3985   5346   1609  -1401  -1599       N  
ATOM   1422  NH2AARG A 227      -3.745 -29.617 -23.541  0.51 54.52           N  
ANISOU 1422  NH2AARG A 227     9694   4591   6432   1981  -1754  -2186       N  
ATOM   1423  NH2BARG A 227      -2.291 -25.085 -17.762  0.49 43.97           N  
ANISOU 1423  NH2BARG A 227     7516   3903   5287   1797  -1336  -1472       N  
ATOM   1424  N   ALA A1001      -3.143 -32.546 -20.151  1.00 56.87           N  
ANISOU 1424  N   ALA A1001     7009   7044   7554  -3453     51   -315       N  
ATOM   1425  CA  ALA A1001      -3.850 -33.366 -21.116  1.00 57.14           C  
ANISOU 1425  CA  ALA A1001     7170   7212   7330  -3664    184   -265       C  
ATOM   1426  C   ALA A1001      -4.368 -34.638 -20.458  1.00 54.26           C  
ANISOU 1426  C   ALA A1001     6682   6826   7107  -3170    290   -428       C  
ATOM   1427  O   ALA A1001      -5.499 -35.035 -20.698  1.00 53.10           O  
ANISOU 1427  O   ALA A1001     6687   6626   6862  -3108    201   -259       O  
ATOM   1428  CB  ALA A1001      -2.947 -33.694 -22.298  1.00 60.59           C  
ANISOU 1428  CB  ALA A1001     7573   7958   7489  -4251    561   -489       C  
ATOM   1429  N   ASP A1002      -3.555 -35.259 -19.609  1.00 53.47           N  
ANISOU 1429  N   ASP A1002     6306   6747   7265  -2839    430   -720       N  
ATOM   1430  CA  ASP A1002      -3.989 -36.473 -18.898  1.00 51.20           C  
ANISOU 1430  CA  ASP A1002     5913   6408   7132  -2394    472   -833       C  
ATOM   1431  C   ASP A1002      -5.222 -36.178 -18.046  1.00 48.58           C  
ANISOU 1431  C   ASP A1002     5771   5866   6822  -2063    182   -595       C  
ATOM   1432  O   ASP A1002      -6.155 -36.970 -18.015  1.00 47.03           O  
ANISOU 1432  O   ASP A1002     5644   5643   6581  -1890    199   -554       O  
ATOM   1433  CB  ASP A1002      -2.885 -37.034 -17.996  1.00 51.57           C  
ANISOU 1433  CB  ASP A1002     5631   6441   7522  -2119    522  -1089       C  
ATOM   1434  CG  ASP A1002      -1.730 -37.644 -18.777  1.00 54.62           C  
ANISOU 1434  CG  ASP A1002     5706   6984   8064  -2367    886  -1430       C  
ATOM   1435  OD1 ASP A1002      -1.903 -37.974 -19.966  1.00 56.13           O  
ANISOU 1435  OD1 ASP A1002     5964   7328   8033  -2729   1184  -1536       O  
ATOM   1436  OD2 ASP A1002      -0.631 -37.781 -18.197  1.00 56.09           O  
ANISOU 1436  OD2 ASP A1002     5563   7130   8617  -2237    882  -1613       O  
ATOM   1437  N   LEU A1003      -5.237 -35.034 -17.355  1.00 49.79           N  
ANISOU 1437  N   LEU A1003     5993   5857   7070  -1998    -46   -479       N  
ATOM   1438  CA  LEU A1003      -6.377 -34.754 -16.483  1.00 48.72           C  
ANISOU 1438  CA  LEU A1003     5988   5499   7025  -1710   -230   -361       C  
ATOM   1439  C   LEU A1003      -7.608 -34.382 -17.300  1.00 47.98           C  
ANISOU 1439  C   LEU A1003     6055   5287   6890  -1849   -346   -102       C  
ATOM   1440  O   LEU A1003      -8.726 -34.777 -16.952  1.00 47.07           O  
ANISOU 1440  O   LEU A1003     5986   5054   6844  -1624   -383    -53       O  
ATOM   1441  CB  LEU A1003      -6.047 -33.670 -15.459  1.00 49.18           C  
ANISOU 1441  CB  LEU A1003     6058   5391   7237  -1629   -386   -392       C  
ATOM   1442  CG  LEU A1003      -7.106 -33.430 -14.378  1.00 48.54           C  
ANISOU 1442  CG  LEU A1003     6079   5086   7278  -1368   -468   -408       C  
ATOM   1443  CD1 LEU A1003      -7.370 -34.684 -13.540  1.00 48.09           C  
ANISOU 1443  CD1 LEU A1003     6016   5114   7141  -1112   -383   -535       C  
ATOM   1444  CD2 LEU A1003      -6.647 -32.290 -13.485  1.00 49.43           C  
ANISOU 1444  CD2 LEU A1003     6216   5049   7517  -1392   -565   -500       C  
ATOM   1445  N   GLU A1004      -7.404 -33.692 -18.413  1.00 52.14           N  
ANISOU 1445  N   GLU A1004     6661   5846   7304  -2262   -422     81       N  
ATOM   1446  CA  GLU A1004      -8.491 -33.430 -19.348  1.00 51.93           C  
ANISOU 1446  CA  GLU A1004     6788   5715   7228  -2491   -618    403       C  
ATOM   1447  C   GLU A1004      -9.082 -34.734 -19.884  1.00 51.15           C  
ANISOU 1447  C   GLU A1004     6722   5790   6923  -2493   -461    374       C  
ATOM   1448  O   GLU A1004     -10.300 -34.848 -20.038  1.00 50.52           O  
ANISOU 1448  O   GLU A1004     6708   5566   6923  -2424   -628    576       O  
ATOM   1449  CB  GLU A1004      -8.005 -32.561 -20.505  1.00 53.57           C  
ANISOU 1449  CB  GLU A1004     7125   5977   7254  -3062   -753    634       C  
ATOM   1450  CG  GLU A1004      -7.873 -31.083 -20.151  1.00 55.18           C  
ANISOU 1450  CG  GLU A1004     7340   5886   7739  -3098  -1039    801       C  
ATOM   1451  CD  GLU A1004      -9.215 -30.367 -20.091  1.00 56.12           C  
ANISOU 1451  CD  GLU A1004     7491   5590   8243  -2988  -1420   1122       C  
ATOM   1452  OE1 GLU A1004     -10.247 -31.004 -20.349  1.00 55.49           O  
ANISOU 1452  OE1 GLU A1004     7426   5475   8183  -2902  -1479   1239       O  
ATOM   1453  OE2 GLU A1004      -9.240 -29.156 -19.789  1.00 57.91           O  
ANISOU 1453  OE2 GLU A1004     7694   5490   8818  -2990  -1663   1245       O  
ATOM   1454  N   ASP A1005      -8.223 -35.711 -20.161  1.00 50.49           N  
ANISOU 1454  N   ASP A1005     6558   5984   6642  -2573   -136    101       N  
ATOM   1455  CA  ASP A1005      -8.694 -37.035 -20.593  1.00 49.91           C  
ANISOU 1455  CA  ASP A1005     6496   6057   6410  -2559     64      2       C  
ATOM   1456  C   ASP A1005      -9.576 -37.707 -19.546  1.00 48.65           C  
ANISOU 1456  C   ASP A1005     6287   5751   6447  -2044     23    -33       C  
ATOM   1457  O   ASP A1005     -10.615 -38.260 -19.879  1.00 47.87           O  
ANISOU 1457  O   ASP A1005     6272   5634   6282  -2032    -12     83       O  
ATOM   1458  CB  ASP A1005      -7.520 -37.955 -20.920  1.00 50.91           C  
ANISOU 1458  CB  ASP A1005     6459   6426   6457  -2680    459   -372       C  
ATOM   1459  CG  ASP A1005      -6.913 -37.664 -22.275  1.00 54.10           C  
ANISOU 1459  CG  ASP A1005     6961   7053   6541  -3340    635   -403       C  
ATOM   1460  OD1 ASP A1005      -7.617 -37.112 -23.151  1.00 57.97           O  
ANISOU 1460  OD1 ASP A1005     7715   7554   6756  -3758    427    -78       O  
ATOM   1461  OD2 ASP A1005      -5.715 -37.960 -22.458  1.00 56.37           O  
ANISOU 1461  OD2 ASP A1005     7052   7492   6873  -3485    965   -749       O  
ATOM   1462  N   ASN A1006      -9.137 -37.668 -18.290  1.00 49.16           N  
ANISOU 1462  N   ASN A1006     6232   5728   6720  -1683     24   -191       N  
ATOM   1463  CA  ASN A1006      -9.902 -38.218 -17.177  1.00 47.21           C  
ANISOU 1463  CA  ASN A1006     5981   5359   6599  -1282     -6   -236       C  
ATOM   1464  C   ASN A1006     -11.257 -37.547 -17.036  1.00 46.51           C  
ANISOU 1464  C   ASN A1006     5986   5046   6642  -1214   -193    -36       C  
ATOM   1465  O   ASN A1006     -12.275 -38.213 -16.829  1.00 45.74           O  
ANISOU 1465  O   ASN A1006     5913   4900   6568  -1051   -169    -18       O  
ATOM   1466  CB  ASN A1006      -9.129 -38.082 -15.865  1.00 48.20           C  
ANISOU 1466  CB  ASN A1006     6022   5439   6853  -1053    -32   -397       C  
ATOM   1467  CG  ASN A1006      -7.819 -38.848 -15.875  1.00 53.78           C  
ANISOU 1467  CG  ASN A1006     6547   6295   7591  -1061     94   -586       C  
ATOM   1468  OD1 ASN A1006      -7.662 -39.834 -16.599  1.00 52.58           O  
ANISOU 1468  OD1 ASN A1006     6313   6256   7410  -1126    276   -681       O  
ATOM   1469  ND2 ASN A1006      -6.884 -38.417 -15.050  1.00 51.37           N  
ANISOU 1469  ND2 ASN A1006     6152   5964   7404  -1004     -3   -663       N  
ATOM   1470  N   TRP A1007     -11.258 -36.224 -17.158  1.00 52.20           N  
ANISOU 1470  N   TRP A1007     6723   5598   7514  -1347   -379    104       N  
ATOM   1471  CA  TRP A1007     -12.468 -35.427 -17.036  1.00 50.58           C  
ANISOU 1471  CA  TRP A1007     6518   5085   7616  -1281   -581    274       C  
ATOM   1472  C   TRP A1007     -13.436 -35.786 -18.156  1.00 51.18           C  
ANISOU 1472  C   TRP A1007     6643   5155   7646  -1468   -718    547       C  
ATOM   1473  O   TRP A1007     -14.629 -35.997 -17.924  1.00 51.57           O  
ANISOU 1473  O   TRP A1007     6642   5035   7919  -1295   -775    599       O  
ATOM   1474  CB  TRP A1007     -12.118 -33.926 -17.068  1.00 51.41           C  
ANISOU 1474  CB  TRP A1007     6607   4966   7959  -1426   -785    384       C  
ATOM   1475  CG  TRP A1007     -13.183 -33.034 -16.524  1.00 56.50           C  
ANISOU 1475  CG  TRP A1007     7159   5200   9108  -1260   -934    420       C  
ATOM   1476  CD1 TRP A1007     -14.442 -33.391 -16.133  1.00 56.99           C  
ANISOU 1476  CD1 TRP A1007     7134   5087   9431  -1038   -899    375       C  
ATOM   1477  CD2 TRP A1007     -13.082 -31.622 -16.306  1.00 58.62           C  
ANISOU 1477  CD2 TRP A1007     7367   5141   9766  -1312  -1111    462       C  
ATOM   1478  NE1 TRP A1007     -15.134 -32.283 -15.689  1.00 55.43           N  
ANISOU 1478  NE1 TRP A1007     6786   4455   9818   -944  -1015    350       N  
ATOM   1479  CE2 TRP A1007     -14.322 -31.186 -15.787  1.00 58.84           C  
ANISOU 1479  CE2 TRP A1007     7236   4770  10350  -1102  -1156    407       C  
ATOM   1480  CE3 TRP A1007     -12.065 -30.685 -16.503  1.00 58.71           C  
ANISOU 1480  CE3 TRP A1007     7422   5135   9752  -1528  -1220    520       C  
ATOM   1481  CZ2 TRP A1007     -14.568 -29.854 -15.457  1.00 62.06           C  
ANISOU 1481  CZ2 TRP A1007     7508   4729  11343  -1084  -1298    384       C  
ATOM   1482  CZ3 TRP A1007     -12.312 -29.358 -16.178  1.00 58.29           C  
ANISOU 1482  CZ3 TRP A1007     7278   4657  10212  -1519  -1395    542       C  
ATOM   1483  CH2 TRP A1007     -13.555 -28.958 -15.661  1.00 62.92           C  
ANISOU 1483  CH2 TRP A1007     7688   4816  11403  -1289  -1430    464       C  
ATOM   1484  N   GLU A1008     -12.904 -35.885 -19.369  1.00 51.71           N  
ANISOU 1484  N   GLU A1008     6815   5425   7405  -1874   -753    698       N  
ATOM   1485  CA  GLU A1008     -13.682 -36.298 -20.530  1.00 51.00           C  
ANISOU 1485  CA  GLU A1008     6835   5397   7145  -2183   -894    966       C  
ATOM   1486  C   GLU A1008     -14.269 -37.706 -20.377  1.00 52.02           C  
ANISOU 1486  C   GLU A1008     6955   5665   7145  -1981   -676    811       C  
ATOM   1487  O   GLU A1008     -15.420 -37.951 -20.739  1.00 50.19           O  
ANISOU 1487  O   GLU A1008     6741   5336   6994  -2009   -843   1013       O  
ATOM   1488  CB  GLU A1008     -12.816 -36.237 -21.786  1.00 57.57           C  
ANISOU 1488  CB  GLU A1008     7831   6496   7549  -2760   -867   1057       C  
ATOM   1489  CG  GLU A1008     -13.464 -36.839 -23.023  1.00 62.26           C  
ANISOU 1489  CG  GLU A1008     8603   7242   7811  -3203   -953   1280       C  
ATOM   1490  CD  GLU A1008     -12.623 -36.642 -24.273  1.00 68.03           C  
ANISOU 1490  CD  GLU A1008     9545   8246   8056  -3912   -900   1347       C  
ATOM   1491  OE1 GLU A1008     -11.707 -35.804 -24.236  1.00 69.64           O  
ANISOU 1491  OE1 GLU A1008     9744   8452   8265  -4059   -901   1324       O  
ATOM   1492  OE2 GLU A1008     -12.878 -37.317 -25.294  1.00 70.30           O  
ANISOU 1492  OE2 GLU A1008    10019   8758   7933  -4376   -836   1404       O  
ATOM   1493  N   THR A1009     -13.466 -38.627 -19.852  1.00 48.95           N  
ANISOU 1493  N   THR A1009     6521   5475   6604  -1792   -340    473       N  
ATOM   1494  CA  THR A1009     -13.911 -40.002 -19.657  1.00 47.85           C  
ANISOU 1494  CA  THR A1009     6372   5438   6371  -1603   -139    320       C  
ATOM   1495  C   THR A1009     -15.100 -40.044 -18.715  1.00 50.55           C  
ANISOU 1495  C   THR A1009     6658   5561   6987  -1244   -226    351       C  
ATOM   1496  O   THR A1009     -16.041 -40.821 -18.916  1.00 50.91           O  
ANISOU 1496  O   THR A1009     6726   5614   7004  -1207   -212    403       O  
ATOM   1497  CB  THR A1009     -12.790 -40.890 -19.097  1.00 49.79           C  
ANISOU 1497  CB  THR A1009     6524   5835   6560  -1427    154    -17       C  
ATOM   1498  OG1 THR A1009     -11.730 -40.974 -20.049  1.00 50.32           O  
ANISOU 1498  OG1 THR A1009     6583   6101   6434  -1786    324   -132       O  
ATOM   1499  CG2 THR A1009     -13.306 -42.292 -18.811  1.00 54.14           C  
ANISOU 1499  CG2 THR A1009     7064   6424   7083  -1218    309   -141       C  
ATOM   1500  N   LEU A1010     -15.044 -39.208 -17.681  1.00 51.52           N  
ANISOU 1500  N   LEU A1010     6706   5495   7373  -1020   -278    280       N  
ATOM   1501  CA  LEU A1010     -16.136 -39.073 -16.721  1.00 51.85           C  
ANISOU 1501  CA  LEU A1010     6677   5313   7711   -746   -285    224       C  
ATOM   1502  C   LEU A1010     -17.407 -38.517 -17.358  1.00 50.27           C  
ANISOU 1502  C   LEU A1010     6399   4872   7829   -832   -532    488       C  
ATOM   1503  O   LEU A1010     -18.484 -39.108 -17.238  1.00 51.13           O  
ANISOU 1503  O   LEU A1010     6454   4920   8054   -719   -503    494       O  
ATOM   1504  CB  LEU A1010     -15.716 -38.171 -15.554  1.00 51.38           C  
ANISOU 1504  CB  LEU A1010     6572   5103   7846   -595   -248     37       C  
ATOM   1505  CG  LEU A1010     -14.645 -38.732 -14.621  1.00 52.16           C  
ANISOU 1505  CG  LEU A1010     6731   5385   7703   -491    -80   -198       C  
ATOM   1506  CD1 LEU A1010     -14.211 -37.689 -13.596  1.00 55.70           C  
ANISOU 1506  CD1 LEU A1010     7172   5697   8293   -452    -84   -354       C  
ATOM   1507  CD2 LEU A1010     -15.146 -39.986 -13.924  1.00 54.19           C  
ANISOU 1507  CD2 LEU A1010     7041   5727   7823   -328     72   -318       C  
ATOM   1508  N   ASN A1011     -17.286 -37.384 -18.035  1.00 54.29           N  
ANISOU 1508  N   ASN A1011     6885   5220   8522  -1052   -814    733       N  
ATOM   1509  CA  ASN A1011     -18.457 -36.722 -18.585  1.00 53.73           C  
ANISOU 1509  CA  ASN A1011     6689   4829   8898  -1139  -1160   1043       C  
ATOM   1510  C   ASN A1011     -19.058 -37.494 -19.756  1.00 54.51           C  
ANISOU 1510  C   ASN A1011     6884   5074   8752  -1416  -1330   1332       C  
ATOM   1511  O   ASN A1011     -20.270 -37.599 -19.856  1.00 56.15           O  
ANISOU 1511  O   ASN A1011     6954   5079   9300  -1352  -1501   1478       O  
ATOM   1512  CB  ASN A1011     -18.107 -35.297 -18.995  1.00 55.41           C  
ANISOU 1512  CB  ASN A1011     6866   4789   9397  -1341  -1489   1283       C  
ATOM   1513  CG  ASN A1011     -17.834 -34.414 -17.792  1.00 59.75           C  
ANISOU 1513  CG  ASN A1011     7280   5094  10330  -1065  -1346    986       C  
ATOM   1514  OD1 ASN A1011     -17.519 -34.910 -16.709  1.00 61.21           O  
ANISOU 1514  OD1 ASN A1011     7482   5418  10357   -819   -982    602       O  
ATOM   1515  ND2 ASN A1011     -17.961 -33.120 -17.967  1.00 62.35           N  
ANISOU 1515  ND2 ASN A1011     7488   5045  11159  -1148  -1650   1170       N  
ATOM   1516  N   ASP A1012     -18.213 -38.048 -20.623  1.00 53.30           N  
ANISOU 1516  N   ASP A1012     6951   5270   8030  -1750  -1254   1374       N  
ATOM   1517  CA  ASP A1012     -18.683 -38.863 -21.741  1.00 56.69           C  
ANISOU 1517  CA  ASP A1012     7527   5891   8121  -2100  -1346   1580       C  
ATOM   1518  C   ASP A1012     -19.440 -40.110 -21.280  1.00 56.14           C  
ANISOU 1518  C   ASP A1012     7407   5895   8027  -1820  -1110   1387       C  
ATOM   1519  O   ASP A1012     -20.523 -40.415 -21.784  1.00 53.40           O  
ANISOU 1519  O   ASP A1012     7040   5475   7773  -1932  -1321   1614       O  
ATOM   1520  CB  ASP A1012     -17.512 -39.283 -22.624  1.00 56.81           C  
ANISOU 1520  CB  ASP A1012     7773   6282   7531  -2531  -1153   1502       C  
ATOM   1521  N   ASN A1013     -18.871 -40.840 -20.328  1.00 51.57           N  
ANISOU 1521  N   ASN A1013     6811   5449   7333  -1490   -716   1000       N  
ATOM   1522  CA  ASN A1013     -19.486 -42.089 -19.891  1.00 52.35           C  
ANISOU 1522  CA  ASN A1013     6900   5626   7363  -1272   -496    828       C  
ATOM   1523  C   ASN A1013     -20.749 -41.874 -19.075  1.00 51.79           C  
ANISOU 1523  C   ASN A1013     6646   5282   7751   -979   -562    833       C  
ATOM   1524  O   ASN A1013     -21.589 -42.771 -18.976  1.00 52.85           O  
ANISOU 1524  O   ASN A1013     6763   5442   7874   -897   -478    798       O  
ATOM   1525  CB  ASN A1013     -18.491 -42.925 -19.095  1.00 52.06           C  
ANISOU 1525  CB  ASN A1013     6897   5762   7120  -1050   -141    476       C  
ATOM   1526  CG  ASN A1013     -17.558 -43.699 -19.990  1.00 53.11           C  
ANISOU 1526  CG  ASN A1013     7142   6159   6878  -1321     35    376       C  
ATOM   1527  OD1 ASN A1013     -17.969 -44.660 -20.638  1.00 55.23           O  
ANISOU 1527  OD1 ASN A1013     7488   6546   6952  -1475    122    371       O  
ATOM   1528  ND2 ASN A1013     -16.299 -43.279 -20.049  1.00 52.73           N  
ANISOU 1528  ND2 ASN A1013     7084   6196   6756  -1410    121    258       N  
ATOM   1529  N   LEU A1014     -20.885 -40.694 -18.487  1.00 52.24           N  
ANISOU 1529  N   LEU A1014     6546   5061   8240   -841   -676    832       N  
ATOM   1530  CA  LEU A1014     -22.131 -40.328 -17.844  1.00 53.38           C  
ANISOU 1530  CA  LEU A1014     6449   4890   8944   -626   -713    791       C  
ATOM   1531  C   LEU A1014     -23.236 -40.271 -18.895  1.00 55.12           C  
ANISOU 1531  C   LEU A1014     6559   4956   9427   -827  -1090   1171       C  
ATOM   1532  O   LEU A1014     -24.383 -40.639 -18.633  1.00 56.95           O  
ANISOU 1532  O   LEU A1014     6611   5048   9980   -695  -1070   1140       O  
ATOM   1533  CB  LEU A1014     -21.984 -38.992 -17.122  1.00 52.49           C  
ANISOU 1533  CB  LEU A1014     6167   4468   9309   -491   -741    674       C  
ATOM   1534  CG  LEU A1014     -21.404 -39.101 -15.716  1.00 56.71           C  
ANISOU 1534  CG  LEU A1014     6758   5082   9705   -272   -347    242       C  
ATOM   1535  CD1 LEU A1014     -20.904 -37.751 -15.210  1.00 58.25           C  
ANISOU 1535  CD1 LEU A1014     6865   5041  10225   -243   -380    131       C  
ATOM   1536  CD2 LEU A1014     -22.483 -39.649 -14.798  1.00 59.88           C  
ANISOU 1536  CD2 LEU A1014     7045   5402  10306    -94    -76    -24       C  
ATOM   1537  N   LYS A1015     -22.877 -39.826 -20.095  1.00 55.78           N  
ANISOU 1537  N   LYS A1015     6763   5080   9352  -1202  -1450   1542       N  
ATOM   1538  CA  LYS A1015     -23.825 -39.739 -21.193  1.00 57.96           C  
ANISOU 1538  CA  LYS A1015     6991   5226   9805  -1512  -1920   1994       C  
ATOM   1539  C   LYS A1015     -24.092 -41.122 -21.772  1.00 56.47           C  
ANISOU 1539  C   LYS A1015     6998   5371   9087  -1693  -1792   1999       C  
ATOM   1540  O   LYS A1015     -25.191 -41.403 -22.215  1.00 57.45           O  
ANISOU 1540  O   LYS A1015     7019   5386   9422  -1795  -2049   2233       O  
ATOM   1541  CB  LYS A1015     -23.311 -38.779 -22.279  1.00 60.92           C  
ANISOU 1541  CB  LYS A1015     7501   5549  10096  -1973  -2383   2425       C  
ATOM   1542  N   VAL A1016     -23.082 -41.984 -21.766  1.00 54.03           N  
ANISOU 1542  N   VAL A1016     6939   5435   8155  -1737  -1404   1727       N  
ATOM   1543  CA  VAL A1016     -23.264 -43.363 -22.201  1.00 54.64           C  
ANISOU 1543  CA  VAL A1016     7182   5794   7784  -1871  -1203   1639       C  
ATOM   1544  C   VAL A1016     -24.260 -44.055 -21.282  1.00 56.54           C  
ANISOU 1544  C   VAL A1016     7246   5924   8312  -1484  -1023   1455       C  
ATOM   1545  O   VAL A1016     -25.141 -44.775 -21.740  1.00 53.93           O  
ANISOU 1545  O   VAL A1016     6923   5631   7936  -1609  -1107   1573       O  
ATOM   1546  CB  VAL A1016     -21.938 -44.150 -22.218  1.00 53.19           C  
ANISOU 1546  CB  VAL A1016     7206   5939   7063  -1920   -780   1306       C  
ATOM   1547  CG1 VAL A1016     -22.206 -45.629 -22.452  1.00 51.04           C  
ANISOU 1547  CG1 VAL A1016     7045   5870   6479  -1967   -525   1138       C  
ATOM   1548  CG2 VAL A1016     -21.016 -43.606 -23.294  1.00 56.78           C  
ANISOU 1548  CG2 VAL A1016     7851   6557   7168  -2421   -890   1446       C  
ATOM   1549  N   ILE A1017     -24.131 -43.800 -19.985  1.00 52.91           N  
ANISOU 1549  N   ILE A1017     6643   5335   8125  -1072   -778   1164       N  
ATOM   1550  CA  ILE A1017     -25.027 -44.372 -18.989  1.00 55.63           C  
ANISOU 1550  CA  ILE A1017     6842   5587   8710   -767   -552    943       C  
ATOM   1551  C   ILE A1017     -26.471 -43.885 -19.149  1.00 56.02           C  
ANISOU 1551  C   ILE A1017     6588   5322   9373   -758   -828   1141       C  
ATOM   1552  O   ILE A1017     -27.417 -44.661 -19.005  1.00 54.28           O  
ANISOU 1552  O   ILE A1017     6288   5103   9235   -704   -743   1095       O  
ATOM   1553  CB  ILE A1017     -24.529 -44.064 -17.563  1.00 54.49           C  
ANISOU 1553  CB  ILE A1017     6656   5383   8667   -456   -241    587       C  
ATOM   1554  CG1 ILE A1017     -23.222 -44.812 -17.309  1.00 52.69           C  
ANISOU 1554  CG1 ILE A1017     6676   5436   7907   -439     -6    408       C  
ATOM   1555  CG2 ILE A1017     -25.578 -44.464 -16.514  1.00 54.53           C  
ANISOU 1555  CG2 ILE A1017     6512   5271   8935   -246      3    347       C  
ATOM   1556  CD1 ILE A1017     -22.559 -44.481 -15.987  1.00 53.00           C  
ANISOU 1556  CD1 ILE A1017     6731   5447   7960   -232    204    131       C  
ATOM   1557  N   GLU A1018     -26.651 -42.609 -19.463  1.00 59.68           N  
ANISOU 1557  N   GLU A1018     6853   5484  10336   -818  -1183   1372       N  
ATOM   1558  CA  GLU A1018     -28.002 -42.083 -19.605  1.00 61.04           C  
ANISOU 1558  CA  GLU A1018     6647   5270  11276   -787  -1497   1567       C  
ATOM   1559  C   GLU A1018     -28.789 -42.730 -20.747  1.00 62.96           C  
ANISOU 1559  C   GLU A1018     6929   5587  11407  -1103  -1864   1958       C  
ATOM   1560  O   GLU A1018     -30.003 -42.913 -20.647  1.00 67.33           O  
ANISOU 1560  O   GLU A1018     7183   5929  12468  -1022  -1963   2001       O  
ATOM   1561  CB  GLU A1018     -27.953 -40.576 -19.799  1.00 61.20           C  
ANISOU 1561  CB  GLU A1018     6436   4892  11926   -814  -1884   1787       C  
ATOM   1562  CG  GLU A1018     -28.000 -39.810 -18.496  1.00 69.76           C  
ANISOU 1562  CG  GLU A1018     7243   5682  13579   -451  -1550   1352       C  
ATOM   1563  CD  GLU A1018     -29.409 -39.666 -17.933  1.00 71.29           C  
ANISOU 1563  CD  GLU A1018     6951   5484  14653   -239  -1480   1172       C  
ATOM   1564  OE1 GLU A1018     -29.874 -38.512 -17.832  1.00 72.70           O  
ANISOU 1564  OE1 GLU A1018     6723   5173  15726   -148  -1698   1200       O  
ATOM   1565  OE2 GLU A1018     -30.039 -40.691 -17.572  1.00 69.40           O  
ANISOU 1565  OE2 GLU A1018     6707   5413  14248   -170  -1184    972       O  
ATOM   1566  N   LYS A1019     -28.098 -43.097 -21.819  1.00 63.71           N  
ANISOU 1566  N   LYS A1019     7387   5990  10829  -1504  -2032   2207       N  
ATOM   1567  CA  LYS A1019     -28.774 -43.633 -22.996  1.00 65.48           C  
ANISOU 1567  CA  LYS A1019     7714   6309  10855  -1929  -2413   2599       C  
ATOM   1568  C   LYS A1019     -28.474 -45.108 -23.238  1.00 62.57           C  
ANISOU 1568  C   LYS A1019     7679   6373   9724  -2062  -2037   2385       C  
ATOM   1569  O   LYS A1019     -28.731 -45.626 -24.328  1.00 62.93           O  
ANISOU 1569  O   LYS A1019     7928   6593   9388  -2525  -2277   2652       O  
ATOM   1570  CB  LYS A1019     -28.383 -42.821 -24.233  1.00 68.88           C  
ANISOU 1570  CB  LYS A1019     8323   6732  11118  -2460  -2973   3100       C  
ATOM   1571  CG  LYS A1019     -26.892 -42.823 -24.519  1.00 66.47           C  
ANISOU 1571  CG  LYS A1019     8401   6761  10096  -2682  -2711   2954       C  
ATOM   1572  CD  LYS A1019     -26.544 -41.871 -25.659  1.00 70.10           C  
ANISOU 1572  CD  LYS A1019     8996   7328  10309  -3078  -3192   3295       C  
ATOM   1573  N   ALA A1020     -27.948 -45.790 -22.227  1.00 54.79           N  
ANISOU 1573  N   ALA A1020     6749   5534   8535  -1697  -1475   1914       N  
ATOM   1574  CA  ALA A1020     -27.579 -47.194 -22.383  1.00 54.78           C  
ANISOU 1574  CA  ALA A1020     7023   5868   7923  -1781  -1119   1687       C  
ATOM   1575  C   ALA A1020     -28.791 -48.038 -22.717  1.00 56.50           C  
ANISOU 1575  C   ALA A1020     7191   6089   8189  -1894  -1219   1803       C  
ATOM   1576  O   ALA A1020     -29.904 -47.709 -22.325  1.00 56.87           O  
ANISOU 1576  O   ALA A1020     6920   5873   8813  -1721  -1390   1899       O  
ATOM   1577  CB  ALA A1020     -26.915 -47.718 -21.133  1.00 54.00           C  
ANISOU 1577  CB  ALA A1020     6948   5837   7734  -1365   -618   1243       C  
ATOM   1578  N   ASP A1021     -28.549 -49.127 -23.442  1.00 55.66           N  
ANISOU 1578  N   ASP A1021     7371   6265   7511  -2199  -1081   1751       N  
ATOM   1579  CA  ASP A1021     -29.583 -50.092 -23.796  1.00 57.51           C  
ANISOU 1579  CA  ASP A1021     7617   6550   7685  -2348  -1129   1823       C  
ATOM   1580  C   ASP A1021     -29.707 -51.188 -22.764  1.00 56.11           C  
ANISOU 1580  C   ASP A1021     7422   6409   7487  -1967   -663   1441       C  
ATOM   1581  O   ASP A1021     -30.763 -51.812 -22.634  1.00 56.78           O  
ANISOU 1581  O   ASP A1021     7405   6447   7722  -1940   -677   1466       O  
ATOM   1582  CB  ASP A1021     -29.284 -50.725 -25.156  1.00 58.65           C  
ANISOU 1582  CB  ASP A1021     8112   6976   7197  -2958  -1198   1931       C  
ATOM   1583  N   ASN A1022     -28.621 -51.464 -22.051  1.00 50.31           N  
ANISOU 1583  N   ASN A1022     6795   5753   6566  -1715   -284   1115       N  
ATOM   1584  CA  ASN A1022     -28.647 -52.575 -21.111  1.00 48.88           C  
ANISOU 1584  CA  ASN A1022     6653   5599   6321  -1432     88    814       C  
ATOM   1585  C   ASN A1022     -27.643 -52.393 -19.982  1.00 48.13           C  
ANISOU 1585  C   ASN A1022     6564   5471   6252  -1092    339    562       C  
ATOM   1586  O   ASN A1022     -26.874 -51.432 -19.963  1.00 49.37           O  
ANISOU 1586  O   ASN A1022     6693   5604   6462  -1062    267    582       O  
ATOM   1587  CB  ASN A1022     -28.387 -53.904 -21.840  1.00 46.34           C  
ANISOU 1587  CB  ASN A1022     6576   5463   5569  -1684    265    697       C  
ATOM   1588  CG  ASN A1022     -27.209 -53.827 -22.774  1.00 48.17           C  
ANISOU 1588  CG  ASN A1022     6995   5855   5453  -1987    328    627       C  
ATOM   1589  OD1 ASN A1022     -26.075 -53.666 -22.333  1.00 47.18           O  
ANISOU 1589  OD1 ASN A1022     6877   5732   5316  -1805    517    428       O  
ATOM   1590  ND2 ASN A1022     -27.466 -53.938 -24.076  1.00 46.69           N  
ANISOU 1590  ND2 ASN A1022     6962   5809   4969  -2505    174    779       N  
ATOM   1591  N   ALA A1023     -27.659 -53.335 -19.048  1.00 39.84           N  
ANISOU 1591  N   ALA A1023     5569   4417   5151   -883    595    356       N  
ATOM   1592  CA  ALA A1023     -26.842 -53.261 -17.846  1.00 41.68           C  
ANISOU 1592  CA  ALA A1023     5831   4609   5398   -616    767    167       C  
ATOM   1593  C   ALA A1023     -25.361 -53.420 -18.151  1.00 42.78           C  
ANISOU 1593  C   ALA A1023     6083   4826   5347   -632    832     65       C  
ATOM   1594  O   ALA A1023     -24.528 -52.832 -17.459  1.00 46.85           O  
ANISOU 1594  O   ALA A1023     6576   5305   5920   -477    846     -6       O  
ATOM   1595  CB  ALA A1023     -27.289 -54.309 -16.835  1.00 38.55           C  
ANISOU 1595  CB  ALA A1023     5508   4184   4954   -493    952     41       C  
ATOM   1596  N   ALA A1024     -25.029 -54.198 -19.181  1.00 41.45           N  
ANISOU 1596  N   ALA A1024     6013   4755   4979   -849    895     23       N  
ATOM   1597  CA  ALA A1024     -23.625 -54.419 -19.529  1.00 42.71           C  
ANISOU 1597  CA  ALA A1024     6214   4964   5051   -889   1029   -155       C  
ATOM   1598  C   ALA A1024     -22.966 -53.117 -19.948  1.00 42.86           C  
ANISOU 1598  C   ALA A1024     6184   5034   5066   -994    915    -83       C  
ATOM   1599  O   ALA A1024     -21.864 -52.805 -19.509  1.00 43.39           O  
ANISOU 1599  O   ALA A1024     6203   5079   5204   -857    973   -201       O  
ATOM   1600  CB  ALA A1024     -23.485 -55.457 -20.639  1.00 44.60           C  
ANISOU 1600  CB  ALA A1024     6550   5289   5106  -1178   1199   -298       C  
ATOM   1601  N   GLN A1025     -23.650 -52.362 -20.799  1.00 42.68           N  
ANISOU 1601  N   GLN A1025     6169   5062   4984  -1262    708    144       N  
ATOM   1602  CA  GLN A1025     -23.165 -51.055 -21.214  1.00 43.35           C  
ANISOU 1602  CA  GLN A1025     6224   5164   5084  -1405    530    282       C  
ATOM   1603  C   GLN A1025     -23.019 -50.109 -20.025  1.00 49.95           C  
ANISOU 1603  C   GLN A1025     6919   5845   6216  -1051    459    291       C  
ATOM   1604  O   GLN A1025     -22.024 -49.385 -19.938  1.00 48.09           O  
ANISOU 1604  O   GLN A1025     6665   5619   5988  -1037    459    244       O  
ATOM   1605  CB  GLN A1025     -24.097 -50.435 -22.260  1.00 47.37           C  
ANISOU 1605  CB  GLN A1025     6761   5689   5547  -1778    201    618       C  
ATOM   1606  CG  GLN A1025     -24.146 -51.215 -23.575  1.00 46.24           C  
ANISOU 1606  CG  GLN A1025     6825   5746   4998  -2285    255    617       C  
ATOM   1607  CD  GLN A1025     -25.264 -50.749 -24.495  1.00 51.26           C  
ANISOU 1607  CD  GLN A1025     7504   6379   5594  -2686   -171   1026       C  
ATOM   1608  OE1 GLN A1025     -25.723 -49.605 -24.408  1.00 51.66           O  
ANISOU 1608  OE1 GLN A1025     7416   6263   5950  -2651   -547   1340       O  
ATOM   1609  NE2 GLN A1025     -25.694 -51.625 -25.396  1.00 53.02           N  
ANISOU 1609  NE2 GLN A1025     7907   6756   5481  -3096   -141   1034       N  
ATOM   1610  N   VAL A1026     -23.999 -50.114 -19.117  1.00 42.78           N  
ANISOU 1610  N   VAL A1026     5913   4801   5538   -814    435    313       N  
ATOM   1611  CA  VAL A1026     -23.928 -49.262 -17.931  1.00 46.48           C  
ANISOU 1611  CA  VAL A1026     6270   5130   6260   -548    442    243       C  
ATOM   1612  C   VAL A1026     -22.723 -49.692 -17.090  1.00 46.22           C  
ANISOU 1612  C   VAL A1026     6324   5149   6089   -382    620     32       C  
ATOM   1613  O   VAL A1026     -21.929 -48.853 -16.660  1.00 44.39           O  
ANISOU 1613  O   VAL A1026     6062   4887   5919   -311    590    -12       O  
ATOM   1614  CB  VAL A1026     -25.224 -49.305 -17.073  1.00 44.15           C  
ANISOU 1614  CB  VAL A1026     5853   4695   6226   -397    489    209       C  
ATOM   1615  CG1 VAL A1026     -25.021 -48.567 -15.748  1.00 41.59           C  
ANISOU 1615  CG1 VAL A1026     5467   4259   6076   -201    607     27       C  
ATOM   1616  CG2 VAL A1026     -26.388 -48.673 -17.826  1.00 45.79           C  
ANISOU 1616  CG2 VAL A1026     5873   4769   6755   -528    238    440       C  
ATOM   1617  N   LYS A1027     -22.570 -51.001 -16.892  1.00 41.53           N  
ANISOU 1617  N   LYS A1027     5825   4606   5348   -339    761    -73       N  
ATOM   1618  CA  LYS A1027     -21.451 -51.531 -16.109  1.00 42.93           C  
ANISOU 1618  CA  LYS A1027     6050   4773   5489   -197    836   -212       C  
ATOM   1619  C   LYS A1027     -20.090 -51.182 -16.732  1.00 43.52           C  
ANISOU 1619  C   LYS A1027     6071   4902   5564   -265    840   -281       C  
ATOM   1620  O   LYS A1027     -19.136 -50.835 -16.020  1.00 42.74           O  
ANISOU 1620  O   LYS A1027     5936   4765   5538   -148    802   -340       O  
ATOM   1621  CB  LYS A1027     -21.573 -53.057 -15.948  1.00 40.91           C  
ANISOU 1621  CB  LYS A1027     5874   4495   5176   -164    931   -274       C  
ATOM   1622  CG  LYS A1027     -20.311 -53.710 -15.385  1.00 45.32           C  
ANISOU 1622  CG  LYS A1027     6425   4977   5819    -47    921   -369       C  
ATOM   1623  CD  LYS A1027     -20.593 -55.064 -14.726  1.00 46.54           C  
ANISOU 1623  CD  LYS A1027     6671   5022   5989     18    915   -358       C  
ATOM   1624  CE  LYS A1027     -19.310 -55.751 -14.248  1.00 50.38           C  
ANISOU 1624  CE  LYS A1027     7092   5352   6696    126    810   -398       C  
ATOM   1625  NZ  LYS A1027     -19.549 -57.185 -13.809  1.00 52.15           N  
ANISOU 1625  NZ  LYS A1027     7392   5408   7013    157    753   -351       N  
ATOM   1626  N   ASP A1028     -19.994 -51.279 -18.053  1.00 40.46           N  
ANISOU 1626  N   ASP A1028     5686   4613   5075   -510    894   -286       N  
ATOM   1627  CA  ASP A1028     -18.737 -50.985 -18.726  1.00 40.54           C  
ANISOU 1627  CA  ASP A1028     5641   4696   5066   -655    974   -409       C  
ATOM   1628  C   ASP A1028     -18.395 -49.507 -18.542  1.00 44.70           C  
ANISOU 1628  C   ASP A1028     6128   5219   5636   -661    817   -297       C  
ATOM   1629  O   ASP A1028     -17.256 -49.160 -18.236  1.00 44.37           O  
ANISOU 1629  O   ASP A1028     6008   5173   5678   -599    842   -404       O  
ATOM   1630  CB  ASP A1028     -18.796 -51.313 -20.220  1.00 46.84           C  
ANISOU 1630  CB  ASP A1028     6507   5639   5652  -1052   1103   -462       C  
ATOM   1631  CG  ASP A1028     -18.945 -52.810 -20.498  1.00 54.20           C  
ANISOU 1631  CG  ASP A1028     7463   6557   6574  -1081   1319   -654       C  
ATOM   1632  OD1 ASP A1028     -18.640 -53.638 -19.606  1.00 55.04           O  
ANISOU 1632  OD1 ASP A1028     7494   6516   6902   -784   1366   -764       O  
ATOM   1633  OD2 ASP A1028     -19.379 -53.159 -21.620  1.00 56.42           O  
ANISOU 1633  OD2 ASP A1028     7853   6960   6623  -1444   1415   -680       O  
ATOM   1634  N   ALA A1029     -19.396 -48.649 -18.730  1.00 43.40           N  
ANISOU 1634  N   ALA A1029     5986   5021   5482   -737    637    -81       N  
ATOM   1635  CA  ALA A1029     -19.192 -47.205 -18.622  1.00 44.54           C  
ANISOU 1635  CA  ALA A1029     6079   5101   5744   -757    464     39       C  
ATOM   1636  C   ALA A1029     -18.791 -46.825 -17.204  1.00 47.28           C  
ANISOU 1636  C   ALA A1029     6373   5343   6250   -457    479    -73       C  
ATOM   1637  O   ALA A1029     -17.851 -46.040 -17.001  1.00 48.56           O  
ANISOU 1637  O   ALA A1029     6497   5501   6453   -455    442   -112       O  
ATOM   1638  CB  ALA A1029     -20.442 -46.453 -19.043  1.00 42.50           C  
ANISOU 1638  CB  ALA A1029     5792   4734   5624   -868    225    300       C  
ATOM   1639  N   LEU A1030     -19.505 -47.380 -16.226  1.00 41.12           N  
ANISOU 1639  N   LEU A1030     5612   4493   5519   -265    535   -127       N  
ATOM   1640  CA  LEU A1030     -19.185 -47.139 -14.821  1.00 43.00           C  
ANISOU 1640  CA  LEU A1030     5870   4665   5805    -92    559   -242       C  
ATOM   1641  C   LEU A1030     -17.763 -47.585 -14.492  1.00 43.12           C  
ANISOU 1641  C   LEU A1030     5895   4735   5753    -47    559   -331       C  
ATOM   1642  O   LEU A1030     -17.063 -46.925 -13.727  1.00 44.01           O  
ANISOU 1642  O   LEU A1030     6006   4819   5897     -6    495   -376       O  
ATOM   1643  CB  LEU A1030     -20.186 -47.848 -13.901  1.00 42.11           C  
ANISOU 1643  CB  LEU A1030     5827   4509   5666     -8    651   -295       C  
ATOM   1644  CG  LEU A1030     -21.547 -47.170 -13.731  1.00 40.54           C  
ANISOU 1644  CG  LEU A1030     5538   4190   5676    -10    686   -296       C  
ATOM   1645  CD1 LEU A1030     -22.510 -48.119 -13.042  1.00 40.35           C  
ANISOU 1645  CD1 LEU A1030     5583   4169   5580      8    832   -371       C  
ATOM   1646  CD2 LEU A1030     -21.412 -45.910 -12.892  1.00 40.25           C  
ANISOU 1646  CD2 LEU A1030     5447   4036   5809     17    707   -421       C  
ATOM   1647  N   THR A1031     -17.340 -48.701 -15.080  1.00 41.50           N  
ANISOU 1647  N   THR A1031     5673   4581   5515    -69    628   -372       N  
ATOM   1648  CA  THR A1031     -15.997 -49.224 -14.862  1.00 42.21           C  
ANISOU 1648  CA  THR A1031     5678   4655   5706    -11    617   -472       C  
ATOM   1649  C   THR A1031     -14.937 -48.228 -15.356  1.00 46.23           C  
ANISOU 1649  C   THR A1031     6073   5216   6276   -107    607   -522       C  
ATOM   1650  O   THR A1031     -13.917 -48.007 -14.697  1.00 46.43           O  
ANISOU 1650  O   THR A1031     6019   5200   6421    -34    512   -564       O  
ATOM   1651  CB  THR A1031     -15.800 -50.569 -15.575  1.00 42.67           C  
ANISOU 1651  CB  THR A1031     5672   4702   5838    -35    752   -576       C  
ATOM   1652  OG1 THR A1031     -16.786 -51.500 -15.112  1.00 44.17           O  
ANISOU 1652  OG1 THR A1031     5980   4835   5967     37    746   -513       O  
ATOM   1653  CG2 THR A1031     -14.414 -51.133 -15.303  1.00 42.80           C  
ANISOU 1653  CG2 THR A1031     5505   4616   6143     57    723   -702       C  
ATOM   1654  N   LYS A1032     -15.196 -47.623 -16.512  1.00 45.48           N  
ANISOU 1654  N   LYS A1032     5984   5211   6087   -317    669   -487       N  
ATOM   1655  CA  LYS A1032     -14.277 -46.641 -17.080  1.00 47.41           C  
ANISOU 1655  CA  LYS A1032     6156   5518   6338   -486    666   -514       C  
ATOM   1656  C   LYS A1032     -14.252 -45.363 -16.227  1.00 47.89           C  
ANISOU 1656  C   LYS A1032     6238   5500   6458   -397    490   -421       C  
ATOM   1657  O   LYS A1032     -13.206 -44.742 -16.057  1.00 49.27           O  
ANISOU 1657  O   LYS A1032     6335   5686   6701   -423    454   -478       O  
ATOM   1658  CB  LYS A1032     -14.665 -46.314 -18.521  1.00 48.98           C  
ANISOU 1658  CB  LYS A1032     6425   5833   6351   -836    719   -437       C  
ATOM   1659  CG  LYS A1032     -14.751 -47.518 -19.444  1.00 48.83           C  
ANISOU 1659  CG  LYS A1032     6423   5912   6218  -1017    942   -579       C  
ATOM   1660  CD  LYS A1032     -14.961 -47.059 -20.889  1.00 52.79           C  
ANISOU 1660  CD  LYS A1032     7051   6572   6436  -1509    970   -493       C  
ATOM   1661  CE  LYS A1032     -15.590 -48.147 -21.777  1.00 53.84           C  
ANISOU 1661  CE  LYS A1032     7289   6802   6367  -1753   1136   -566       C  
ATOM   1662  NZ  LYS A1032     -17.086 -48.166 -21.682  1.00 53.85           N  
ANISOU 1662  NZ  LYS A1032     7403   6739   6320  -1694    898   -278       N  
ATOM   1663  N   MET A1033     -15.406 -44.983 -15.689  1.00 47.59           N  
ANISOU 1663  N   MET A1033     6280   5368   6433   -310    411   -319       N  
ATOM   1664  CA  MET A1033     -15.506 -43.820 -14.813  1.00 46.84           C  
ANISOU 1664  CA  MET A1033     6194   5160   6445   -242    313   -312       C  
ATOM   1665  C   MET A1033     -14.692 -44.010 -13.543  1.00 46.41           C  
ANISOU 1665  C   MET A1033     6164   5101   6369   -126    291   -429       C  
ATOM   1666  O   MET A1033     -14.034 -43.081 -13.060  1.00 47.79           O  
ANISOU 1666  O   MET A1033     6325   5243   6589   -151    218   -468       O  
ATOM   1667  CB  MET A1033     -16.963 -43.549 -14.453  1.00 43.76           C  
ANISOU 1667  CB  MET A1033     5825   4636   6166   -181    313   -271       C  
ATOM   1668  CG  MET A1033     -17.796 -43.071 -15.611  1.00 44.16           C  
ANISOU 1668  CG  MET A1033     5820   4623   6335   -321    206    -80       C  
ATOM   1669  SD  MET A1033     -19.462 -42.678 -15.082  1.00 49.10           S  
ANISOU 1669  SD  MET A1033     6349   5014   7294   -211    200    -76       S  
ATOM   1670  CE  MET A1033     -19.145 -41.394 -13.879  1.00 54.01           C  
ANISOU 1670  CE  MET A1033     6917   5453   8150   -125    247   -277       C  
ATOM   1671  N   ARG A1034     -14.769 -45.219 -12.994  1.00 42.18           N  
ANISOU 1671  N   ARG A1034     5680   4584   5763    -36    313   -456       N  
ATOM   1672  CA  ARG A1034     -14.042 -45.557 -11.786  1.00 45.13           C  
ANISOU 1672  CA  ARG A1034     6108   4940   6101      6    195   -486       C  
ATOM   1673  C   ARG A1034     -12.554 -45.380 -12.011  1.00 46.39           C  
ANISOU 1673  C   ARG A1034     6108   5119   6397     -9     94   -510       C  
ATOM   1674  O   ARG A1034     -11.856 -44.809 -11.177  1.00 47.49           O  
ANISOU 1674  O   ARG A1034     6268   5241   6535    -43    -51   -515       O  
ATOM   1675  CB  ARG A1034     -14.327 -46.998 -11.349  1.00 45.40           C  
ANISOU 1675  CB  ARG A1034     6214   4954   6083     65    168   -444       C  
ATOM   1676  CG  ARG A1034     -13.879 -47.279  -9.927  1.00 49.20           C  
ANISOU 1676  CG  ARG A1034     6833   5398   6462     16    -38   -392       C  
ATOM   1677  CD  ARG A1034     -14.159 -48.709  -9.467  1.00 52.24           C  
ANISOU 1677  CD  ARG A1034     7314   5727   6810     29   -136   -287       C  
ATOM   1678  NE  ARG A1034     -13.888 -48.831  -8.039  1.00 53.05           N  
ANISOU 1678  NE  ARG A1034     7629   5808   6718   -137   -384   -182       N  
ATOM   1679  CZ  ARG A1034     -12.695 -49.104  -7.519  1.00 58.08           C  
ANISOU 1679  CZ  ARG A1034     8208   6367   7492   -172   -727    -46       C  
ATOM   1680  NH1 ARG A1034     -11.655 -49.331  -8.309  1.00 58.72           N  
ANISOU 1680  NH1 ARG A1034     7967   6362   7982     -7   -802    -56       N  
ATOM   1681  NH2 ARG A1034     -12.547 -49.174  -6.203  1.00 57.85           N  
ANISOU 1681  NH2 ARG A1034     8437   6339   7205   -421  -1001     96       N  
ATOM   1682  N   ALA A1035     -12.083 -45.878 -13.148  1.00 43.99           N  
ANISOU 1682  N   ALA A1035     5640   4855   6218    -25    198   -556       N  
ATOM   1683  CA  ALA A1035     -10.673 -45.799 -13.490  1.00 47.98           C  
ANISOU 1683  CA  ALA A1035     5927   5372   6933    -60    180   -648       C  
ATOM   1684  C   ALA A1035     -10.231 -44.345 -13.661  1.00 46.34           C  
ANISOU 1684  C   ALA A1035     5711   5213   6682   -185    156   -649       C  
ATOM   1685  O   ALA A1035      -9.142 -43.978 -13.231  1.00 48.01           O  
ANISOU 1685  O   ALA A1035     5804   5410   7028   -195     39   -686       O  
ATOM   1686  CB  ALA A1035     -10.396 -46.587 -14.748  1.00 45.99           C  
ANISOU 1686  CB  ALA A1035     5508   5160   6804   -131    410   -789       C  
ATOM   1687  N   ALA A1036     -11.084 -43.533 -14.281  1.00 45.81           N  
ANISOU 1687  N   ALA A1036     5757   5175   6475   -292    225   -584       N  
ATOM   1688  CA  ALA A1036     -10.778 -42.122 -14.532  1.00 46.64           C  
ANISOU 1688  CA  ALA A1036     5865   5277   6578   -433    172   -548       C  
ATOM   1689  C   ALA A1036     -10.783 -41.316 -13.239  1.00 47.25           C  
ANISOU 1689  C   ALA A1036     6027   5257   6669   -356     32   -553       C  
ATOM   1690  O   ALA A1036      -9.956 -40.430 -13.049  1.00 49.19           O  
ANISOU 1690  O   ALA A1036     6227   5495   6968   -435    -45   -580       O  
ATOM   1691  CB  ALA A1036     -11.766 -41.531 -15.526  1.00 44.47           C  
ANISOU 1691  CB  ALA A1036     5675   4991   6232   -588    190   -414       C  
ATOM   1692  N   ALA A1037     -11.714 -41.638 -12.348  1.00 48.19           N  
ANISOU 1692  N   ALA A1037     6280   5312   6719   -252     30   -557       N  
ATOM   1693  CA  ALA A1037     -11.789 -40.983 -11.049  1.00 47.21           C  
ANISOU 1693  CA  ALA A1037     6278   5117   6544   -267    -30   -632       C  
ATOM   1694  C   ALA A1037     -10.524 -41.242 -10.224  1.00 52.62           C  
ANISOU 1694  C   ALA A1037     6951   5854   7188   -302   -208   -643       C  
ATOM   1695  O   ALA A1037      -9.992 -40.329  -9.584  1.00 50.90           O  
ANISOU 1695  O   ALA A1037     6777   5614   6950   -405   -293   -698       O  
ATOM   1696  CB  ALA A1037     -13.026 -41.449 -10.289  1.00 47.25           C  
ANISOU 1696  CB  ALA A1037     6434   5075   6445   -229     69   -683       C  
ATOM   1697  N   LEU A1038     -10.042 -42.485 -10.239  1.00 49.27           N  
ANISOU 1697  N   LEU A1038     6447   5466   6806   -231   -293   -583       N  
ATOM   1698  CA  LEU A1038      -8.830 -42.826  -9.487  1.00 51.81           C  
ANISOU 1698  CA  LEU A1038     6696   5780   7210   -263   -555   -535       C  
ATOM   1699  C   LEU A1038      -7.573 -42.210 -10.090  1.00 54.10           C  
ANISOU 1699  C   LEU A1038     6737   6091   7727   -299   -591   -584       C  
ATOM   1700  O   LEU A1038      -6.641 -41.857  -9.368  1.00 55.09           O  
ANISOU 1700  O   LEU A1038     6822   6203   7908   -380   -820   -557       O  
ATOM   1701  CB  LEU A1038      -8.660 -44.337  -9.405  1.00 50.84           C  
ANISOU 1701  CB  LEU A1038     6487   5604   7225   -159   -675   -445       C  
ATOM   1702  CG  LEU A1038      -9.484 -44.957  -8.279  1.00 56.00           C  
ANISOU 1702  CG  LEU A1038     7431   6236   7610   -225   -792   -341       C  
ATOM   1703  CD1 LEU A1038      -9.947 -46.370  -8.641  1.00 58.89           C  
ANISOU 1703  CD1 LEU A1038     7752   6538   8084    -97   -765   -275       C  
ATOM   1704  CD2 LEU A1038      -8.688 -44.943  -6.984  1.00 60.60           C  
ANISOU 1704  CD2 LEU A1038     8124   6790   8109   -406  -1178   -206       C  
ATOM   1705  N   ASP A1039      -7.543 -42.101 -11.414  1.00 54.19           N  
ANISOU 1705  N   ASP A1039     6594   6148   7846   -296   -369   -653       N  
ATOM   1706  CA  ASP A1039      -6.418 -41.474 -12.084  1.00 53.48           C  
ANISOU 1706  CA  ASP A1039     6284   6103   7931   -403   -332   -734       C  
ATOM   1707  C   ASP A1039      -6.391 -39.982 -11.744  1.00 52.61           C  
ANISOU 1707  C   ASP A1039     6308   5989   7692   -530   -394   -718       C  
ATOM   1708  O   ASP A1039      -5.345 -39.451 -11.381  1.00 53.03           O  
ANISOU 1708  O   ASP A1039     6253   6047   7850   -608   -529   -745       O  
ATOM   1709  CB  ASP A1039      -6.498 -41.689 -13.593  1.00 58.63           C  
ANISOU 1709  CB  ASP A1039     6821   6839   8618   -495    -47   -823       C  
ATOM   1710  CG  ASP A1039      -5.174 -41.422 -14.291  1.00 63.49           C  
ANISOU 1710  CG  ASP A1039     7155   7516   9451   -652     58   -975       C  
ATOM   1711  OD1 ASP A1039      -4.264 -40.844 -13.654  1.00 66.55           O  
ANISOU 1711  OD1 ASP A1039     7438   7877   9973   -667   -117   -978       O  
ATOM   1712  OD2 ASP A1039      -5.041 -41.780 -15.481  1.00 63.64           O  
ANISOU 1712  OD2 ASP A1039     7063   7623   9493   -808    338  -1116       O  
ATOM   1713  N   ALA A1040      -7.550 -39.328 -11.837  1.00 51.83           N  
ANISOU 1713  N   ALA A1040     6413   5845   7435   -547   -308   -683       N  
ATOM   1714  CA  ALA A1040      -7.689 -37.898 -11.539  1.00 52.58           C  
ANISOU 1714  CA  ALA A1040     6613   5857   7507   -653   -346   -697       C  
ATOM   1715  C   ALA A1040      -7.347 -37.554 -10.091  1.00 55.23           C  
ANISOU 1715  C   ALA A1040     7067   6156   7762   -691   -495   -764       C  
ATOM   1716  O   ALA A1040      -6.824 -36.469  -9.804  1.00 54.84           O  
ANISOU 1716  O   ALA A1040     7032   6064   7739   -817   -557   -815       O  
ATOM   1717  CB  ALA A1040      -9.107 -37.427 -11.860  1.00 49.79           C  
ANISOU 1717  CB  ALA A1040     6381   5382   7154   -631   -246   -658       C  
ATOM   1718  N   GLN A1041      -7.651 -38.479  -9.184  1.00 57.05           N  
ANISOU 1718  N   GLN A1041     7411   6406   7858   -641   -562   -755       N  
ATOM   1719  CA  GLN A1041      -7.335 -38.325  -7.766  1.00 56.98           C  
ANISOU 1719  CA  GLN A1041     7581   6401   7669   -789   -738   -790       C  
ATOM   1720  C   GLN A1041      -5.834 -38.214  -7.513  1.00 57.11           C  
ANISOU 1720  C   GLN A1041     7445   6461   7793   -881  -1011   -727       C  
ATOM   1721  O   GLN A1041      -5.412 -37.707  -6.480  1.00 58.45           O  
ANISOU 1721  O   GLN A1041     7763   6638   7809  -1083  -1186   -749       O  
ATOM   1722  CB  GLN A1041      -7.915 -39.501  -6.967  1.00 58.70           C  
ANISOU 1722  CB  GLN A1041     7970   6646   7687   -790   -804   -727       C  
ATOM   1723  CG  GLN A1041      -7.654 -39.451  -5.469  1.00 60.49           C  
ANISOU 1723  CG  GLN A1041     8461   6907   7615  -1069  -1018   -725       C  
ATOM   1724  CD  GLN A1041      -8.298 -40.605  -4.717  1.00 63.96           C  
ANISOU 1724  CD  GLN A1041     9121   7378   7804  -1152  -1094   -628       C  
ATOM   1725  OE1 GLN A1041      -8.215 -41.756  -5.139  1.00 63.68           O  
ANISOU 1725  OE1 GLN A1041     8951   7323   7922   -980  -1210   -458       O  
ATOM   1726  NE2 GLN A1041      -8.935 -40.298  -3.589  1.00 62.58           N  
ANISOU 1726  NE2 GLN A1041     9291   7244   7244  -1462  -1006   -764       N  
ATOM   1727  N   LYS A1042      -5.026 -38.680  -8.460  1.00 57.16           N  
ANISOU 1727  N   LYS A1042     7143   6495   8081   -772  -1029   -677       N  
ATOM   1728  CA  LYS A1042      -3.572 -38.688  -8.289  1.00 58.85           C  
ANISOU 1728  CA  LYS A1042     7112   6720   8529   -836  -1279   -639       C  
ATOM   1729  C   LYS A1042      -2.912 -37.453  -8.908  1.00 58.92           C  
ANISOU 1729  C   LYS A1042     7001   6755   8631   -949  -1180   -734       C  
ATOM   1730  O   LYS A1042      -1.695 -37.262  -8.802  1.00 59.42           O  
ANISOU 1730  O   LYS A1042     6840   6832   8906  -1031  -1356   -734       O  
ATOM   1731  CB  LYS A1042      -2.974 -39.963  -8.891  1.00 61.84           C  
ANISOU 1731  CB  LYS A1042     7148   7068   9279   -677  -1316   -606       C  
ATOM   1732  CG  LYS A1042      -3.206 -41.209  -8.027  1.00 64.91           C  
ANISOU 1732  CG  LYS A1042     7608   7376   9678   -610  -1589   -442       C  
ATOM   1733  CD  LYS A1042      -2.575 -42.461  -8.613  1.00 66.23           C  
ANISOU 1733  CD  LYS A1042     7375   7430  10359   -434  -1633   -439       C  
ATOM   1734  CE  LYS A1042      -3.340 -42.958  -9.824  1.00 67.72           C  
ANISOU 1734  CE  LYS A1042     7519   7654  10556   -301  -1205   -588       C  
ATOM   1735  NZ  LYS A1042      -2.909 -44.332 -10.233  1.00 69.39           N  
ANISOU 1735  NZ  LYS A1042     7382   7713  11268   -142  -1215   -632       N  
ATOM   1736  N   ALA A1043      -3.718 -36.621  -9.557  1.00 59.71           N  
ANISOU 1736  N   ALA A1043     7233   6838   8615   -972   -934   -792       N  
ATOM   1737  CA  ALA A1043      -3.201 -35.425 -10.207  1.00 61.08           C  
ANISOU 1737  CA  ALA A1043     7334   7010   8863  -1120   -865   -837       C  
ATOM   1738  C   ALA A1043      -3.103 -34.307  -9.188  1.00 59.84           C  
ANISOU 1738  C   ALA A1043     7365   6778   8593  -1266   -993   -889       C  
ATOM   1739  O   ALA A1043      -4.073 -33.597  -8.941  1.00 64.60           O  
ANISOU 1739  O   ALA A1043     8181   7262   9102  -1285   -887   -950       O  
ATOM   1740  CB  ALA A1043      -4.085 -35.019 -11.372  1.00 59.72           C  
ANISOU 1740  CB  ALA A1043     7222   6805   8664  -1133   -643   -807       C  
ATOM   1741  N   THR A1044      -1.933 -34.166  -8.580  1.00 62.77           N  
ANISOU 1741  N   THR A1044     7632   7195   9022  -1385  -1219   -890       N  
ATOM   1742  CA  THR A1044      -1.745 -33.165  -7.539  1.00 64.82           C  
ANISOU 1742  CA  THR A1044     8094   7404   9131  -1587  -1350   -962       C  
ATOM   1743  C   THR A1044      -1.230 -31.853  -8.123  1.00 67.69           C  
ANISOU 1743  C   THR A1044     8387   7715   9615  -1728  -1285  -1019       C  
ATOM   1744  O   THR A1044      -0.190 -31.823  -8.787  1.00 64.96           O  
ANISOU 1744  O   THR A1044     7774   7448   9458  -1779  -1325   -985       O  
ATOM   1745  CB  THR A1044      -0.774 -33.668  -6.448  1.00 66.73           C  
ANISOU 1745  CB  THR A1044     8304   7715   9334  -1717  -1719   -882       C  
ATOM   1746  OG1 THR A1044      -1.299 -34.865  -5.862  1.00 69.30           O  
ANISOU 1746  OG1 THR A1044     8741   8060   9531  -1639  -1831   -780       O  
ATOM   1747  CG2 THR A1044      -0.601 -32.629  -5.362  1.00 65.57           C  
ANISOU 1747  CG2 THR A1044     8420   7544   8950  -2013  -1838   -980       C  
ATOM   1748  N   PRO A1045      -1.975 -30.758  -7.891  1.00 69.00           N  
ANISOU 1748  N   PRO A1045     8772   7721   9723  -1809  -1167  -1127       N  
ATOM   1749  CA  PRO A1045      -1.505 -29.422  -8.281  1.00 68.98           C  
ANISOU 1749  CA  PRO A1045     8742   7614   9854  -1977  -1160  -1164       C  
ATOM   1750  C   PRO A1045      -0.238 -29.043  -7.544  1.00 68.76           C  
ANISOU 1750  C   PRO A1045     8669   7668   9788  -2188  -1380  -1205       C  
ATOM   1751  O   PRO A1045      -0.039 -29.512  -6.425  1.00 70.19           O  
ANISOU 1751  O   PRO A1045     8959   7923   9788  -2261  -1550  -1233       O  
ATOM   1752  CB  PRO A1045      -2.665 -28.504  -7.882  1.00 69.05           C  
ANISOU 1752  CB  PRO A1045     8973   7362   9902  -1993  -1010  -1315       C  
ATOM   1753  CG  PRO A1045      -3.456 -29.288  -6.880  1.00 71.21           C  
ANISOU 1753  CG  PRO A1045     9425   7669   9964  -1930   -941  -1431       C  
ATOM   1754  CD  PRO A1045      -3.310 -30.720  -7.271  1.00 68.34           C  
ANISOU 1754  CD  PRO A1045     8936   7508   9522  -1757  -1012  -1248       C  
ATOM   1755  N   PRO A1046       0.609 -28.202  -8.161  1.00 68.27           N  
ANISOU 1755  N   PRO A1046     8464   7599   9878  -2336  -1407  -1185       N  
ATOM   1756  CA  PRO A1046       1.854 -27.738  -7.549  1.00 70.55           C  
ANISOU 1756  CA  PRO A1046     8674   7955  10175  -2559  -1625  -1220       C  
ATOM   1757  C   PRO A1046       1.626 -27.087  -6.182  1.00 73.61           C  
ANISOU 1757  C   PRO A1046     9368   8250  10351  -2749  -1714  -1377       C  
ATOM   1758  O   PRO A1046       2.512 -27.130  -5.329  1.00 77.03           O  
ANISOU 1758  O   PRO A1046     9801   8786  10682  -2948  -1978  -1373       O  
ATOM   1759  CB  PRO A1046       2.379 -26.721  -8.569  1.00 70.71           C  
ANISOU 1759  CB  PRO A1046     8572   7925  10370  -2708  -1543  -1198       C  
ATOM   1760  CG  PRO A1046       1.816 -27.193  -9.865  1.00 65.66           C  
ANISOU 1760  CG  PRO A1046     7844   7309   9795  -2579  -1342  -1090       C  
ATOM   1761  CD  PRO A1046       0.450 -27.688  -9.532  1.00 66.78           C  
ANISOU 1761  CD  PRO A1046     8186   7349   9840  -2357  -1256  -1097       C  
ATOM   1762  N   LYS A1047       0.443 -26.506  -5.982  1.00 74.61           N  
ANISOU 1762  N   LYS A1047     9736   8172  10442  -2725  -1493  -1531       N  
ATOM   1763  CA  LYS A1047       0.091 -25.862  -4.717  1.00 77.15           C  
ANISOU 1763  CA  LYS A1047    10358   8386  10570  -2959  -1451  -1791       C  
ATOM   1764  C   LYS A1047       0.160 -26.842  -3.539  1.00 79.05           C  
ANISOU 1764  C   LYS A1047    10777   8825  10433  -3092  -1617  -1790       C  
ATOM   1765  O   LYS A1047       0.561 -26.472  -2.434  1.00 79.97           O  
ANISOU 1765  O   LYS A1047    11114   8989  10282  -3444  -1746  -1921       O  
ATOM   1766  CB  LYS A1047      -1.311 -25.244  -4.805  1.00 75.08           C  
ANISOU 1766  CB  LYS A1047    10227   7823  10478  -2861  -1121  -2005       C  
ATOM   1767  CG  LYS A1047      -1.564 -24.136  -3.791  1.00 74.03           C  
ANISOU 1767  CG  LYS A1047    10325   7477  10324  -3148   -966  -2380       C  
ATOM   1768  N   LEU A1048      -0.225 -28.091  -3.790  1.00 83.09           N  
ANISOU 1768  N   LEU A1048    11214   9448  10907  -2860  -1641  -1623       N  
ATOM   1769  CA  LEU A1048      -0.243 -29.124  -2.757  1.00 83.50           C  
ANISOU 1769  CA  LEU A1048    11444   9661  10622  -2996  -1850  -1548       C  
ATOM   1770  C   LEU A1048       0.850 -30.172  -2.962  1.00 84.59           C  
ANISOU 1770  C   LEU A1048    11293   9952  10894  -2908  -2252  -1227       C  
ATOM   1771  O   LEU A1048       0.913 -31.161  -2.230  1.00 86.90           O  
ANISOU 1771  O   LEU A1048    11680  10338  10999  -2998  -2528  -1067       O  
ATOM   1772  CB  LEU A1048      -1.607 -29.822  -2.721  1.00 81.10           C  
ANISOU 1772  CB  LEU A1048    11288   9321  10204  -2829  -1584  -1617       C  
ATOM   1773  CG  LEU A1048      -2.855 -28.946  -2.641  1.00 79.03           C  
ANISOU 1773  CG  LEU A1048    11197   8842   9991  -2839  -1143  -1961       C  
ATOM   1774  CD1 LEU A1048      -4.108 -29.806  -2.699  1.00 76.58           C  
ANISOU 1774  CD1 LEU A1048    10949   8518   9629  -2651   -916  -1990       C  
ATOM   1775  CD2 LEU A1048      -2.826 -28.115  -1.377  1.00 82.30           C  
ANISOU 1775  CD2 LEU A1048    11933   9224  10112  -3294  -1065  -2286       C  
ATOM   1776  N   GLU A1049       1.700 -29.972  -3.963  1.00 83.69           N  
ANISOU 1776  N   GLU A1049    10809   9839  11149  -2761  -2283  -1142       N  
ATOM   1777  CA  GLU A1049       2.737 -30.956  -4.252  1.00 84.40           C  
ANISOU 1777  CA  GLU A1049    10521  10018  11531  -2652  -2589   -919       C  
ATOM   1778  C   GLU A1049       3.805 -30.920  -3.165  1.00 87.62           C  
ANISOU 1778  C   GLU A1049    10933  10481  11877  -2973  -3086   -794       C  
ATOM   1779  O   GLU A1049       4.457 -31.926  -2.880  1.00 89.16           O  
ANISOU 1779  O   GLU A1049    10904  10696  12276  -2948  -3483   -563       O  
ATOM   1780  CB  GLU A1049       3.361 -30.706  -5.622  1.00 84.13           C  
ANISOU 1780  CB  GLU A1049    10086   9983  11898  -2494  -2403   -943       C  
ATOM   1781  CG  GLU A1049       2.869 -31.652  -6.706  1.00 84.64           C  
ANISOU 1781  CG  GLU A1049     9950  10058  12150  -2187  -2153   -915       C  
ATOM   1782  CD  GLU A1049       3.795 -31.675  -7.904  1.00 86.93           C  
ANISOU 1782  CD  GLU A1049     9806  10399  12826  -2155  -2016   -957       C  
ATOM   1783  OE1 GLU A1049       4.660 -30.774  -7.998  1.00 82.84           O  
ANISOU 1783  OE1 GLU A1049     9174   9898  12405  -2355  -2063  -1008       O  
ATOM   1784  OE2 GLU A1049       3.661 -32.589  -8.748  1.00 89.93           O  
ANISOU 1784  OE2 GLU A1049     9965  10806  13399  -1972  -1829   -971       O  
ATOM   1785  N   ASP A1050       3.974 -29.750  -2.558  1.00 90.92           N  
ANISOU 1785  N   ASP A1050    11598  10892  12055  -3295  -3094   -939       N  
ATOM   1786  CA  ASP A1050       4.904 -29.597  -1.451  1.00 93.44           C  
ANISOU 1786  CA  ASP A1050    12005  11279  12221  -3695  -3583   -822       C  
ATOM   1787  C   ASP A1050       4.218 -29.905  -0.119  1.00 95.21           C  
ANISOU 1787  C   ASP A1050    12744  11561  11870  -4045  -3732   -814       C  
ATOM   1788  O   ASP A1050       4.768 -29.628   0.950  1.00 97.72           O  
ANISOU 1788  O   ASP A1050    13296  11952  11881  -4518  -4108   -749       O  
ATOM   1789  CB  ASP A1050       5.492 -28.185  -1.419  1.00 92.50           C  
ANISOU 1789  CB  ASP A1050    11920  11135  12092  -3946  -3521  -1002       C  
ATOM   1790  CG  ASP A1050       6.438 -27.914  -2.579  1.00 91.53           C  
ANISOU 1790  CG  ASP A1050    11291  10995  12492  -3747  -3472   -970       C  
ATOM   1791  OD1 ASP A1050       6.815 -28.877  -3.284  1.00 91.54           O  
ANISOU 1791  OD1 ASP A1050    10879  11015  12885  -3467  -3528   -827       O  
ATOM   1792  OD2 ASP A1050       6.837 -26.742  -2.761  1.00 88.48           O  
ANISOU 1792  OD2 ASP A1050    10917  10571  12131  -3916  -3364  -1113       O  
ATOM   1793  N   LYS A1051       3.016 -30.469  -0.193  1.00 95.08           N  
ANISOU 1793  N   LYS A1051    12922  11527  11678  -3870  -3430   -886       N  
ATOM   1794  CA  LYS A1051       2.253 -30.855   0.992  1.00 93.09           C  
ANISOU 1794  CA  LYS A1051    13167  11349  10853  -4233  -3483   -914       C  
ATOM   1795  C   LYS A1051       2.414 -32.346   1.295  1.00 93.43           C  
ANISOU 1795  C   LYS A1051    13146  11441  10913  -4198  -3948   -516       C  
ATOM   1796  O   LYS A1051       2.702 -33.149   0.403  1.00 92.83           O  
ANISOU 1796  O   LYS A1051    12628  11296  11345  -3755  -4024   -327       O  
ATOM   1797  CB  LYS A1051       0.765 -30.523   0.812  1.00 89.32           C  
ANISOU 1797  CB  LYS A1051    12935  10797  10204  -4110  -2845  -1274       C  
ATOM   1798  CG  LYS A1051       0.264 -29.343   1.634  1.00 87.48           C  
ANISOU 1798  CG  LYS A1051    13110  10530   9598  -4544  -2515  -1702       C  
ATOM   1799  CD  LYS A1051       1.032 -28.069   1.321  1.00 85.94           C  
ANISOU 1799  CD  LYS A1051    12767  10241   9645  -4594  -2490  -1842       C  
ATOM   1800  N   SER A1052       2.215 -32.707   2.558  1.00 92.21           N  
ANISOU 1800  N   SER A1052    13446  11390  10199  -4716  -4248   -405       N  
ATOM   1801  CA  SER A1052       2.328 -34.094   2.997  1.00 93.56           C  
ANISOU 1801  CA  SER A1052    13621  11573  10356  -4751  -4745     32       C  
ATOM   1802  C   SER A1052       0.961 -34.697   3.337  1.00 92.13           C  
ANISOU 1802  C   SER A1052    13843  11442   9722  -4839  -4434    -79       C  
ATOM   1803  O   SER A1052       0.014 -33.966   3.638  1.00 87.84           O  
ANISOU 1803  O   SER A1052    13654  10955   8766  -5022  -3867   -498       O  
ATOM   1804  CB  SER A1052       3.267 -34.175   4.204  1.00 98.25           C  
ANISOU 1804  CB  SER A1052    14375  12232  10722  -5145  -5239    401       C  
ATOM   1805  OG  SER A1052       2.568 -33.927   5.409  1.00101.90           O  
ANISOU 1805  OG  SER A1052    15456  12841  10420  -5652  -5013    300       O  
ATOM   1806  N   PRO A1053       0.848 -36.037   3.263  1.00 93.96           N  
ANISOU 1806  N   PRO A1053    13969  11621  10111  -4678  -4764    274       N  
ATOM   1807  CA  PRO A1053      -0.375 -36.736   3.676  1.00 92.71           C  
ANISOU 1807  CA  PRO A1053    14200  11521   9502  -4810  -4531    232       C  
ATOM   1808  C   PRO A1053      -0.526 -36.803   5.193  1.00 96.78           C  
ANISOU 1808  C   PRO A1053    15257  12181   9335  -5403  -4590    385       C  
ATOM   1809  O   PRO A1053      -0.808 -35.779   5.816  1.00 98.88           O  
ANISOU 1809  O   PRO A1053    15838  12563   9170  -5743  -4178     46       O  
ATOM   1810  CB  PRO A1053      -0.193 -38.138   3.089  1.00 92.48           C  
ANISOU 1810  CB  PRO A1053    13795  11345   9999  -4377  -4878    629       C  
ATOM   1811  CG  PRO A1053       1.279 -38.312   2.995  1.00 95.47           C  
ANISOU 1811  CG  PRO A1053    13735  11602  10936  -4316  -5542    985       C  
ATOM   1812  CD  PRO A1053       1.818 -36.957   2.640  1.00 94.93           C  
ANISOU 1812  CD  PRO A1053    13519  11583  10967  -4286  -5269    673       C  
ATOM   1813  N   PRO A1056      -4.058 -33.140   5.913  1.00 91.23           N  
ANISOU 1813  N   PRO A1056    15350  11604   7708  -5873  -1864  -1728       N  
ATOM   1814  CA  PRO A1056      -4.768 -31.861   6.036  1.00 92.82           C  
ANISOU 1814  CA  PRO A1056    15573  11717   7977  -5911  -1151  -2330       C  
ATOM   1815  C   PRO A1056      -5.247 -31.355   4.676  1.00 89.93           C  
ANISOU 1815  C   PRO A1056    14825  11082   8261  -5338   -843  -2626       C  
ATOM   1816  O   PRO A1056      -6.330 -31.748   4.229  1.00 91.33           O  
ANISOU 1816  O   PRO A1056    14930  11168   8604  -5092   -491  -2796       O  
ATOM   1817  CB  PRO A1056      -3.714 -30.930   6.641  1.00 95.24           C  
ANISOU 1817  CB  PRO A1056    15962  12079   8145  -6231  -1345  -2311       C  
ATOM   1818  CG  PRO A1056      -2.403 -31.560   6.291  1.00 94.16           C  
ANISOU 1818  CG  PRO A1056    15653  11979   8144  -6125  -2148  -1745       C  
ATOM   1819  CD  PRO A1056      -2.643 -33.030   6.308  1.00 93.36           C  
ANISOU 1819  CD  PRO A1056    15605  11942   7926  -6082  -2486  -1338       C  
ATOM   1820  N   GLU A1057      -4.449 -30.510   4.031  1.00 92.72           N  
ANISOU 1820  N   GLU A1057    14941  11300   8987  -5159   -990  -2650       N  
ATOM   1821  CA  GLU A1057      -4.742 -30.017   2.687  1.00 88.25           C  
ANISOU 1821  CA  GLU A1057    14020  10457   9052  -4673   -784  -2818       C  
ATOM   1822  C   GLU A1057      -4.951 -31.166   1.711  1.00 91.70           C  
ANISOU 1822  C   GLU A1057    14158  10910   9773  -4122   -947  -2418       C  
ATOM   1823  O   GLU A1057      -5.862 -31.140   0.874  1.00 91.33           O  
ANISOU 1823  O   GLU A1057    13889  10697  10116  -3704   -598  -2530       O  
ATOM   1824  CB  GLU A1057      -3.603 -29.126   2.191  1.00 86.74           C  
ANISOU 1824  CB  GLU A1057    13592  10189   9177  -4566  -1030  -2711       C  
ATOM   1825  CG  GLU A1057      -3.443 -27.823   2.961  1.00 89.76           C  
ANISOU 1825  CG  GLU A1057    14134  10513   9457  -4903   -783  -3072       C  
ATOM   1826  CD  GLU A1057      -4.535 -26.821   2.649  1.00 92.83           C  
ANISOU 1826  CD  GLU A1057    14395  10590  10288  -4691   -156  -3546       C  
ATOM   1827  OE1 GLU A1057      -5.249 -27.002   1.639  1.00 90.47           O  
ANISOU 1827  OE1 GLU A1057    13862  10078  10435  -4299      9  -3577       O  
ATOM   1828  OE2 GLU A1057      -4.679 -25.848   3.415  1.00100.73           O  
ANISOU 1828  OE2 GLU A1057    15501  11536  11234  -4920    153  -3869       O  
ATOM   1829  N   MET A1058      -4.093 -32.175   1.819  1.00 91.65           N  
ANISOU 1829  N   MET A1058    14130  11074   9618  -4145  -1505  -1949       N  
ATOM   1830  CA  MET A1058      -4.160 -33.327   0.934  1.00 88.52           C  
ANISOU 1830  CA  MET A1058    13440  10679   9517  -3663  -1671  -1595       C  
ATOM   1831  C   MET A1058      -5.405 -34.153   1.212  1.00 86.01           C  
ANISOU 1831  C   MET A1058    13326  10392   8963  -3681  -1407  -1676       C  
ATOM   1832  O   MET A1058      -5.951 -34.783   0.310  1.00 84.73           O  
ANISOU 1832  O   MET A1058    12922  10165   9107  -3231  -1282  -1571       O  
ATOM   1833  CB  MET A1058      -2.898 -34.183   1.075  1.00 87.72           C  
ANISOU 1833  CB  MET A1058    13212  10678   9442  -3706  -2343  -1115       C  
ATOM   1834  CG  MET A1058      -1.672 -33.572   0.409  1.00 86.87           C  
ANISOU 1834  CG  MET A1058    12730  10519   9759  -3527  -2564  -1009       C  
ATOM   1835  SD  MET A1058      -1.862 -33.481  -1.387  1.00 89.14           S  
ANISOU 1835  SD  MET A1058    12516  10672  10681  -2863  -2222  -1039       S  
ATOM   1836  CE  MET A1058      -2.460 -35.126  -1.756  1.00 80.44           C  
ANISOU 1836  CE  MET A1058    11320   9587   9658  -2563  -2274   -803       C  
ATOM   1837  N   LYS A1059      -5.853 -34.136   2.464  1.00 86.74           N  
ANISOU 1837  N   LYS A1059    13880  10597   8480  -4259  -1302  -1883       N  
ATOM   1838  CA  LYS A1059      -7.061 -34.855   2.858  1.00 88.16           C  
ANISOU 1838  CA  LYS A1059    14294  10827   8374  -4385   -997  -2018       C  
ATOM   1839  C   LYS A1059      -8.299 -34.267   2.178  1.00 85.97           C  
ANISOU 1839  C   LYS A1059    13811  10352   8503  -4033   -333  -2447       C  
ATOM   1840  O   LYS A1059      -9.166 -35.005   1.716  1.00 85.12           O  
ANISOU 1840  O   LYS A1059    13598  10213   8530  -3750   -161  -2401       O  
ATOM   1841  CB  LYS A1059      -7.225 -34.833   4.381  1.00 89.95           C  
ANISOU 1841  CB  LYS A1059    15020  11248   7908  -5104   -935  -2138       C  
ATOM   1842  N   ASP A1060      -8.371 -32.940   2.110  1.00 84.82           N  
ANISOU 1842  N   ASP A1060    13584  10038   8607  -4055     -3  -2841       N  
ATOM   1843  CA  ASP A1060      -9.481 -32.261   1.444  1.00 83.75           C  
ANISOU 1843  CA  ASP A1060    13183   9623   9014  -3717    536  -3212       C  
ATOM   1844  C   ASP A1060      -9.581 -32.646  -0.031  1.00 82.93           C  
ANISOU 1844  C   ASP A1060    12653   9404   9453  -3054    394  -2860       C  
ATOM   1845  O   ASP A1060     -10.657 -32.983  -0.520  1.00 80.89           O  
ANISOU 1845  O   ASP A1060    12248   9036   9451  -2793    661  -2931       O  
ATOM   1846  CB  ASP A1060      -9.341 -30.735   1.561  1.00 95.68           C  
ANISOU 1846  CB  ASP A1060    14633  10905  10815  -3838    800  -3627       C  
ATOM   1847  CG  ASP A1060      -9.368 -30.248   2.998  1.00101.62           C  
ANISOU 1847  CG  ASP A1060    15656  11829  11127  -4326   1034  -3860       C  
ATOM   1848  OD1 ASP A1060     -10.260 -30.681   3.758  1.00104.34           O  
ANISOU 1848  OD1 ASP A1060    16143  12298  11202  -4538   1374  -4012       O  
ATOM   1849  OD2 ASP A1060      -8.516 -29.406   3.362  1.00103.96           O  
ANISOU 1849  OD2 ASP A1060    16013  12136  11352  -4528    911  -3898       O  
ATOM   1850  N   PHE A1061      -8.450 -32.590  -0.731  1.00 81.95           N  
ANISOU 1850  N   PHE A1061    12333   9313   9490  -2838    -11  -2503       N  
ATOM   1851  CA  PHE A1061      -8.402 -32.818  -2.175  1.00 80.20           C  
ANISOU 1851  CA  PHE A1061    11739   9006   9729  -2325   -116  -2213       C  
ATOM   1852  C   PHE A1061      -8.932 -34.188  -2.589  1.00 81.22           C  
ANISOU 1852  C   PHE A1061    11818   9236   9805  -2093   -165  -1973       C  
ATOM   1853  O   PHE A1061      -9.805 -34.305  -3.453  1.00 78.83           O  
ANISOU 1853  O   PHE A1061    11326   8810   9816  -1791     29  -1971       O  
ATOM   1854  CB  PHE A1061      -6.964 -32.662  -2.682  1.00 79.99           C  
ANISOU 1854  CB  PHE A1061    11544   9055   9793  -2256   -510  -1922       C  
ATOM   1855  N   ARG A1062      -8.390 -35.222  -1.958  1.00 77.87           N  
ANISOU 1855  N   ARG A1062    11564   9013   9010  -2264   -472  -1747       N  
ATOM   1856  CA  ARG A1062      -8.681 -36.595  -2.328  1.00 74.56           C  
ANISOU 1856  CA  ARG A1062    11089   8670   8572  -2058   -592  -1483       C  
ATOM   1857  C   ARG A1062     -10.070 -37.035  -1.873  1.00 72.84           C  
ANISOU 1857  C   ARG A1062    11064   8447   8163  -2150   -250  -1682       C  
ATOM   1858  O   ARG A1062     -10.702 -37.873  -2.517  1.00 72.47           O  
ANISOU 1858  O   ARG A1062    10896   8389   8251  -1881   -188  -1558       O  
ATOM   1859  CB  ARG A1062      -7.611 -37.519  -1.742  1.00 76.37           C  
ANISOU 1859  CB  ARG A1062    11404   9039   8574  -2231  -1102  -1149       C  
ATOM   1860  CG  ARG A1062      -6.184 -37.059  -2.026  1.00 75.19           C  
ANISOU 1860  CG  ARG A1062    11035   8888   8646  -2199  -1438   -994       C  
ATOM   1861  CD  ARG A1062      -5.187 -38.173  -1.772  1.00 78.01           C  
ANISOU 1861  CD  ARG A1062    11302   9293   9044  -2228  -1979   -614       C  
ATOM   1862  N   HIS A1063     -10.541 -36.464  -0.768  1.00 76.30           N  
ANISOU 1862  N   HIS A1063    11798   8900   8293  -2571      7  -2031       N  
ATOM   1863  CA  HIS A1063     -11.808 -36.872  -0.162  1.00 76.65           C  
ANISOU 1863  CA  HIS A1063    12046   8965   8113  -2773    384  -2291       C  
ATOM   1864  C   HIS A1063     -12.988 -36.817  -1.128  1.00 73.59           C  
ANISOU 1864  C   HIS A1063    11351   8389   8222  -2356    739  -2422       C  
ATOM   1865  O   HIS A1063     -13.866 -37.675  -1.085  1.00 70.21           O  
ANISOU 1865  O   HIS A1063    10971   8003   7703  -2336    885  -2418       O  
ATOM   1866  CB  HIS A1063     -12.118 -36.008   1.060  1.00 76.76           C  
ANISOU 1866  CB  HIS A1063    12371   8991   7802  -3330    736  -2783       C  
ATOM   1867  CG  HIS A1063     -13.529 -36.143   1.546  1.00 77.08           C  
ANISOU 1867  CG  HIS A1063    12521   8999   7769  -3528   1292  -3207       C  
ATOM   1868  ND1 HIS A1063     -14.083 -37.359   1.884  1.00 77.52           N  
ANISOU 1868  ND1 HIS A1063    12777   9217   7461  -3675   1277  -3062       N  
ATOM   1869  CD2 HIS A1063     -14.496 -35.219   1.735  1.00 79.30           C  
ANISOU 1869  CD2 HIS A1063    12627   9101   8403  -3535   1866  -3693       C  
ATOM   1870  CE1 HIS A1063     -15.334 -37.175   2.269  1.00 77.51           C  
ANISOU 1870  CE1 HIS A1063    12716   9172   7563  -3775   1845  -3443       C  
ATOM   1871  NE2 HIS A1063     -15.612 -35.889   2.188  1.00 81.18           N  
ANISOU 1871  NE2 HIS A1063    12900   9434   8510  -3655   2197  -3793       N  
ATOM   1872  N   GLY A1064     -13.015 -35.803  -1.988  1.00 72.31           N  
ANISOU 1872  N   GLY A1064    10880   8005   8591  -2064    835  -2508       N  
ATOM   1873  CA  GLY A1064     -14.056 -35.706  -2.993  1.00 70.64           C  
ANISOU 1873  CA  GLY A1064    10354   7583   8902  -1695   1041  -2536       C  
ATOM   1874  C   GLY A1064     -14.049 -36.926  -3.894  1.00 67.09           C  
ANISOU 1874  C   GLY A1064     9801   7251   8438  -1399    799  -2124       C  
ATOM   1875  O   GLY A1064     -15.092 -37.524  -4.150  1.00 66.58           O  
ANISOU 1875  O   GLY A1064     9673   7154   8472  -1282    973  -2145       O  
ATOM   1876  N   PHE A1065     -12.861 -37.304  -4.357  1.00 61.86           N  
ANISOU 1876  N   PHE A1065     9104   6716   7685  -1301    421  -1787       N  
ATOM   1877  CA  PHE A1065     -12.705 -38.443  -5.256  1.00 63.05           C  
ANISOU 1877  CA  PHE A1065     9128   6957   7872  -1045    225  -1457       C  
ATOM   1878  C   PHE A1065     -13.051 -39.752  -4.555  1.00 61.75           C  
ANISOU 1878  C   PHE A1065     9177   6928   7357  -1164    186  -1377       C  
ATOM   1879  O   PHE A1065     -13.463 -40.711  -5.193  1.00 61.21           O  
ANISOU 1879  O   PHE A1065     9021   6879   7358   -968    170  -1216       O  
ATOM   1880  CB  PHE A1065     -11.275 -38.517  -5.808  1.00 64.60           C  
ANISOU 1880  CB  PHE A1065     9192   7229   8124   -963   -106  -1210       C  
ATOM   1881  CG  PHE A1065     -10.923 -37.399  -6.752  1.00 67.06           C  
ANISOU 1881  CG  PHE A1065     9291   7428   8759   -857    -91  -1216       C  
ATOM   1882  CD1 PHE A1065     -11.506 -37.323  -8.009  1.00 64.76           C  
ANISOU 1882  CD1 PHE A1065     8812   7051   8743   -663     -9  -1123       C  
ATOM   1883  CD2 PHE A1065      -9.996 -36.432  -6.388  1.00 71.74           C  
ANISOU 1883  CD2 PHE A1065     9898   8005   9355  -1008   -198  -1281       C  
ATOM   1884  CE1 PHE A1065     -11.185 -36.304  -8.881  1.00 63.82           C  
ANISOU 1884  CE1 PHE A1065     8544   6827   8879   -649    -52  -1070       C  
ATOM   1885  CE2 PHE A1065      -9.665 -35.405  -7.258  1.00 71.29           C  
ANISOU 1885  CE2 PHE A1065     9667   7835   9583   -952   -204  -1260       C  
ATOM   1886  CZ  PHE A1065     -10.262 -35.342  -8.507  1.00 69.76           C  
ANISOU 1886  CZ  PHE A1065     9308   7552   9646   -786   -142  -1141       C  
ATOM   1887  N   ASP A1066     -12.864 -39.794  -3.240  1.00 62.92           N  
ANISOU 1887  N   ASP A1066     9634   7172   7102  -1542    149  -1477       N  
ATOM   1888  CA  ASP A1066     -13.213 -40.979  -2.472  1.00 65.39           C  
ANISOU 1888  CA  ASP A1066    10210   7606   7028  -1759     73  -1371       C  
ATOM   1889  C   ASP A1066     -14.728 -41.154  -2.416  1.00 63.10           C  
ANISOU 1889  C   ASP A1066     9952   7275   6747  -1771    510  -1623       C  
ATOM   1890  O   ASP A1066     -15.234 -42.268  -2.551  1.00 61.50           O  
ANISOU 1890  O   ASP A1066     9788   7118   6459  -1708    481  -1467       O  
ATOM   1891  CB  ASP A1066     -12.622 -40.898  -1.066  1.00 69.41           C  
ANISOU 1891  CB  ASP A1066    11097   8243   7032  -2286   -116  -1386       C  
ATOM   1892  CG  ASP A1066     -11.107 -40.944  -1.072  1.00 76.03           C  
ANISOU 1892  CG  ASP A1066    11869   9107   7910  -2281   -641  -1069       C  
ATOM   1893  OD1 ASP A1066     -10.547 -41.793  -1.801  1.00 75.90           O  
ANISOU 1893  OD1 ASP A1066    11618   9053   8168  -1970   -940   -752       O  
ATOM   1894  OD2 ASP A1066     -10.478 -40.127  -0.357  1.00 78.65           O  
ANISOU 1894  OD2 ASP A1066    12356   9483   8043  -2601   -734  -1169       O  
ATOM   1895  N   ILE A1067     -15.445 -40.049  -2.226  1.00 65.90           N  
ANISOU 1895  N   ILE A1067    10252   7510   7277  -1850    916  -2030       N  
ATOM   1896  CA  ILE A1067     -16.906 -40.071  -2.253  1.00 63.86           C  
ANISOU 1896  CA  ILE A1067     9908   7153   7205  -1828   1361  -2323       C  
ATOM   1897  C   ILE A1067     -17.411 -40.521  -3.623  1.00 63.54           C  
ANISOU 1897  C   ILE A1067     9538   7009   7594  -1360   1295  -2088       C  
ATOM   1898  O   ILE A1067     -18.337 -41.329  -3.721  1.00 61.92           O  
ANISOU 1898  O   ILE A1067     9326   6824   7376  -1324   1437  -2083       O  
ATOM   1899  CB  ILE A1067     -17.511 -38.685  -1.915  1.00 66.44           C  
ANISOU 1899  CB  ILE A1067    10112   7269   7862  -1945   1801  -2837       C  
ATOM   1900  CG1 ILE A1067     -17.154 -38.274  -0.482  1.00 69.78           C  
ANISOU 1900  CG1 ILE A1067    10916   7819   7778  -2523   1964  -3162       C  
ATOM   1901  CG2 ILE A1067     -19.020 -38.702  -2.105  1.00 62.49           C  
ANISOU 1901  CG2 ILE A1067     9389   6598   7758  -1850   2235  -3132       C  
ATOM   1902  CD1 ILE A1067     -17.896 -37.046   0.018  1.00 70.77           C  
ANISOU 1902  CD1 ILE A1067    10904   7740   8244  -2693   2505  -3748       C  
ATOM   1903  N   LEU A1068     -16.786 -40.005  -4.674  1.00 60.61           N  
ANISOU 1903  N   LEU A1068     8922   6546   7560  -1066   1078  -1891       N  
ATOM   1904  CA  LEU A1068     -17.163 -40.340  -6.040  1.00 59.65           C  
ANISOU 1904  CA  LEU A1068     8535   6352   7777   -726    987  -1656       C  
ATOM   1905  C   LEU A1068     -16.985 -41.826  -6.337  1.00 58.65           C  
ANISOU 1905  C   LEU A1068     8492   6393   7399   -648    802  -1371       C  
ATOM   1906  O   LEU A1068     -17.897 -42.477  -6.845  1.00 57.48           O  
ANISOU 1906  O   LEU A1068     8264   6225   7350   -532    898  -1321       O  
ATOM   1907  CB  LEU A1068     -16.345 -39.522  -7.034  1.00 60.96           C  
ANISOU 1907  CB  LEU A1068     8505   6435   8220   -562    773  -1490       C  
ATOM   1908  CG  LEU A1068     -16.900 -39.462  -8.456  1.00 59.41           C  
ANISOU 1908  CG  LEU A1068     8056   6124   8393   -339    710  -1297       C  
ATOM   1909  CD1 LEU A1068     -18.173 -38.651  -8.479  1.00 60.45           C  
ANISOU 1909  CD1 LEU A1068     7998   5978   8991   -307    915  -1495       C  
ATOM   1910  CD2 LEU A1068     -15.872 -38.886  -9.419  1.00 62.63           C  
ANISOU 1910  CD2 LEU A1068     8359   6534   8903   -293    471  -1088       C  
ATOM   1911  N   VAL A1069     -15.805 -42.358  -6.034  1.00 55.30           N  
ANISOU 1911  N   VAL A1069     8196   6097   6718   -713    518  -1184       N  
ATOM   1912  CA  VAL A1069     -15.525 -43.769  -6.290  1.00 54.87           C  
ANISOU 1912  CA  VAL A1069     8173   6128   6546   -629    317   -929       C  
ATOM   1913  C   VAL A1069     -16.497 -44.647  -5.512  1.00 54.72           C  
ANISOU 1913  C   VAL A1069     8375   6157   6259   -799    450   -976       C  
ATOM   1914  O   VAL A1069     -16.972 -45.659  -6.021  1.00 55.68           O  
ANISOU 1914  O   VAL A1069     8455   6282   6417   -671    446   -847       O  
ATOM   1915  CB  VAL A1069     -14.076 -44.136  -5.921  1.00 58.55           C  
ANISOU 1915  CB  VAL A1069     8686   6650   6910   -693    -52   -734       C  
ATOM   1916  CG1 VAL A1069     -13.869 -45.634  -5.968  1.00 60.45           C  
ANISOU 1916  CG1 VAL A1069     8947   6898   7125   -635   -269   -499       C  
ATOM   1917  CG2 VAL A1069     -13.102 -43.447  -6.860  1.00 58.00           C  
ANISOU 1917  CG2 VAL A1069     8356   6549   7131   -524   -146   -694       C  
ATOM   1918  N   GLY A1070     -16.804 -44.240  -4.285  1.00 58.48           N  
ANISOU 1918  N   GLY A1070     9100   6676   6444  -1140    599  -1189       N  
ATOM   1919  CA  GLY A1070     -17.738 -44.977  -3.454  1.00 59.78           C  
ANISOU 1919  CA  GLY A1070     9513   6912   6288  -1412    778  -1279       C  
ATOM   1920  C   GLY A1070     -19.113 -45.043  -4.087  1.00 57.87           C  
ANISOU 1920  C   GLY A1070     9071   6588   6328  -1233   1129  -1443       C  
ATOM   1921  O   GLY A1070     -19.779 -46.077  -4.067  1.00 57.02           O  
ANISOU 1921  O   GLY A1070     9043   6526   6097  -1263   1171  -1362       O  
ATOM   1922  N   GLN A1071     -19.544 -43.930  -4.663  1.00 60.18           N  
ANISOU 1922  N   GLN A1071     9086   6732   7046  -1058   1338  -1650       N  
ATOM   1923  CA  GLN A1071     -20.830 -43.904  -5.335  1.00 58.55           C  
ANISOU 1923  CA  GLN A1071     8624   6398   7225   -883   1586  -1760       C  
ATOM   1924  C   GLN A1071     -20.802 -44.697  -6.634  1.00 59.57           C  
ANISOU 1924  C   GLN A1071     8595   6533   7505   -581   1347  -1416       C  
ATOM   1925  O   GLN A1071     -21.781 -45.369  -6.975  1.00 61.45           O  
ANISOU 1925  O   GLN A1071     8763   6759   7825   -527   1458  -1397       O  
ATOM   1926  CB  GLN A1071     -21.258 -42.474  -5.615  1.00 58.46           C  
ANISOU 1926  CB  GLN A1071     8321   6151   7739   -789   1780  -2020       C  
ATOM   1927  CG  GLN A1071     -21.561 -41.644  -4.387  1.00 61.64           C  
ANISOU 1927  CG  GLN A1071     8818   6495   8107  -1109   2157  -2496       C  
ATOM   1928  CD  GLN A1071     -21.958 -40.240  -4.759  1.00 63.56           C  
ANISOU 1928  CD  GLN A1071     8703   6417   9029   -966   2315  -2746       C  
ATOM   1929  OE1 GLN A1071     -21.224 -39.544  -5.457  1.00 64.14           O  
ANISOU 1929  OE1 GLN A1071     8653   6393   9323   -781   2039  -2547       O  
ATOM   1930  NE2 GLN A1071     -23.139 -39.819  -4.314  1.00 65.09           N  
ANISOU 1930  NE2 GLN A1071     8697   6413   9619  -1066   2760  -3190       N  
ATOM   1931  N   ILE A1072     -19.690 -44.613  -7.364  1.00 52.26           N  
ANISOU 1931  N   ILE A1072     7610   5631   6614   -426   1054  -1181       N  
ATOM   1932  CA  ILE A1072     -19.528 -45.413  -8.575  1.00 50.59           C  
ANISOU 1932  CA  ILE A1072     7286   5452   6485   -230    881   -918       C  
ATOM   1933  C   ILE A1072     -19.588 -46.899  -8.227  1.00 53.93           C  
ANISOU 1933  C   ILE A1072     7887   5971   6632   -279    825   -802       C  
ATOM   1934  O   ILE A1072     -20.168 -47.702  -8.974  1.00 49.57           O  
ANISOU 1934  O   ILE A1072     7266   5421   6146   -182    846   -704       O  
ATOM   1935  CB  ILE A1072     -18.201 -45.105  -9.290  1.00 54.23           C  
ANISOU 1935  CB  ILE A1072     7661   5939   7004   -138    649   -767       C  
ATOM   1936  CG1 ILE A1072     -18.260 -43.729  -9.956  1.00 54.38           C  
ANISOU 1936  CG1 ILE A1072     7495   5842   7327    -96    658   -803       C  
ATOM   1937  CG2 ILE A1072     -17.890 -46.171 -10.343  1.00 53.39           C  
ANISOU 1937  CG2 ILE A1072     7487   5893   6907    -30    544   -584       C  
ATOM   1938  CD1 ILE A1072     -17.029 -43.387 -10.762  1.00 56.32           C  
ANISOU 1938  CD1 ILE A1072     7659   6132   7606    -68    473   -670       C  
ATOM   1939  N   ASP A1073     -18.998 -47.267  -7.089  1.00 51.69           N  
ANISOU 1939  N   ASP A1073     7846   5753   6043   -470    718   -788       N  
ATOM   1940  CA  ASP A1073     -18.977 -48.675  -6.686  1.00 54.94           C  
ANISOU 1940  CA  ASP A1073     8440   6204   6231   -552    577   -616       C  
ATOM   1941  C   ASP A1073     -20.388 -49.165  -6.354  1.00 52.91           C  
ANISOU 1941  C   ASP A1073     8281   5969   5853   -679    846   -731       C  
ATOM   1942  O   ASP A1073     -20.755 -50.285  -6.700  1.00 51.10           O  
ANISOU 1942  O   ASP A1073     8073   5734   5610   -624    802   -594       O  
ATOM   1943  CB  ASP A1073     -18.051 -48.900  -5.489  1.00 58.23           C  
ANISOU 1943  CB  ASP A1073     9116   6660   6350   -808    304   -504       C  
ATOM   1944  CG  ASP A1073     -16.584 -48.984  -5.889  1.00 63.83           C  
ANISOU 1944  CG  ASP A1073     9676   7313   7263   -650    -49   -311       C  
ATOM   1945  OD1 ASP A1073     -16.300 -49.122  -7.099  1.00 64.03           O  
ANISOU 1945  OD1 ASP A1073     9431   7289   7610   -371    -34   -284       O  
ATOM   1946  OD2 ASP A1073     -15.714 -48.932  -4.992  1.00 64.17           O  
ANISOU 1946  OD2 ASP A1073     9870   7363   7150   -851   -339   -196       O  
ATOM   1947  N   ASP A1074     -21.175 -48.322  -5.688  1.00 53.83           N  
ANISOU 1947  N   ASP A1074     8433   6091   5927   -864   1154  -1021       N  
ATOM   1948  CA  ASP A1074     -22.565 -48.657  -5.405  1.00 52.32           C  
ANISOU 1948  CA  ASP A1074     8260   5906   5711   -996   1482  -1204       C  
ATOM   1949  C   ASP A1074     -23.351 -48.835  -6.715  1.00 51.93           C  
ANISOU 1949  C   ASP A1074     7899   5770   6062   -693   1531  -1140       C  
ATOM   1950  O   ASP A1074     -24.145 -49.773  -6.853  1.00 49.80           O  
ANISOU 1950  O   ASP A1074     7654   5522   5743   -718   1605  -1091       O  
ATOM   1951  CB  ASP A1074     -23.202 -47.584  -4.516  1.00 56.93           C  
ANISOU 1951  CB  ASP A1074     8852   6470   6311  -1252   1874  -1626       C  
ATOM   1952  CG  ASP A1074     -22.607 -47.562  -3.113  1.00 65.09           C  
ANISOU 1952  CG  ASP A1074    10288   7638   6805  -1707   1861  -1709       C  
ATOM   1953  OD1 ASP A1074     -21.979 -48.572  -2.730  1.00 66.85           O  
ANISOU 1953  OD1 ASP A1074    10797   7959   6644  -1856   1528  -1396       O  
ATOM   1954  OD2 ASP A1074     -22.762 -46.545  -2.397  1.00 69.17           O  
ANISOU 1954  OD2 ASP A1074    10837   8144   7303  -1951   2160  -2080       O  
ATOM   1955  N   ALA A1075     -23.102 -47.950  -7.680  1.00 48.94           N  
ANISOU 1955  N   ALA A1075     7252   5295   6047   -460   1451  -1108       N  
ATOM   1956  CA  ALA A1075     -23.744 -48.031  -8.991  1.00 47.86           C  
ANISOU 1956  CA  ALA A1075     6858   5084   6244   -259   1408   -984       C  
ATOM   1957  C   ALA A1075     -23.324 -49.280  -9.775  1.00 46.13           C  
ANISOU 1957  C   ALA A1075     6712   4948   5865   -174   1209   -724       C  
ATOM   1958  O   ALA A1075     -24.122 -49.855 -10.519  1.00 44.26           O  
ANISOU 1958  O   ALA A1075     6384   4703   5728   -133   1232   -649       O  
ATOM   1959  CB  ALA A1075     -23.441 -46.791  -9.799  1.00 45.04           C  
ANISOU 1959  CB  ALA A1075     6265   4607   6243   -128   1296   -951       C  
ATOM   1960  N   LEU A1076     -22.067 -49.685  -9.622  1.00 43.91           N  
ANISOU 1960  N   LEU A1076     6565   4723   5396   -161   1016   -610       N  
ATOM   1961  CA  LEU A1076     -21.564 -50.865 -10.318  1.00 44.08           C  
ANISOU 1961  CA  LEU A1076     6605   4765   5378    -81    871   -441       C  
ATOM   1962  C   LEU A1076     -22.296 -52.103  -9.833  1.00 45.54           C  
ANISOU 1962  C   LEU A1076     6949   4956   5397   -172    924   -405       C  
ATOM   1963  O   LEU A1076     -22.692 -52.940 -10.623  1.00 42.27           O  
ANISOU 1963  O   LEU A1076     6488   4533   5039   -120    937   -338       O  
ATOM   1964  CB  LEU A1076     -20.050 -51.018 -10.113  1.00 47.97           C  
ANISOU 1964  CB  LEU A1076     7131   5249   5845    -45    650   -362       C  
ATOM   1965  CG  LEU A1076     -19.150 -50.391 -11.189  1.00 47.68           C  
ANISOU 1965  CG  LEU A1076     6897   5218   6002     59    593   -357       C  
ATOM   1966  CD1 LEU A1076     -17.735 -50.187 -10.653  1.00 52.88           C  
ANISOU 1966  CD1 LEU A1076     7551   5855   6687     68    401   -334       C  
ATOM   1967  CD2 LEU A1076     -19.113 -51.259 -12.451  1.00 45.48           C  
ANISOU 1967  CD2 LEU A1076     6515   4944   5821    104    633   -327       C  
ATOM   1968  N   LYS A1077     -22.489 -52.195  -8.526  1.00 46.79           N  
ANISOU 1968  N   LYS A1077     7323   5140   5315   -368    964   -457       N  
ATOM   1969  CA  LYS A1077     -23.214 -53.317  -7.953  1.00 49.81           C  
ANISOU 1969  CA  LYS A1077     7900   5536   5489   -533   1013   -411       C  
ATOM   1970  C   LYS A1077     -24.624 -53.416  -8.533  1.00 46.75           C  
ANISOU 1970  C   LYS A1077     7371   5156   5238   -509   1268   -515       C  
ATOM   1971  O   LYS A1077     -25.090 -54.505  -8.862  1.00 43.97           O  
ANISOU 1971  O   LYS A1077     7062   4792   4852   -514   1258   -419       O  
ATOM   1972  CB  LYS A1077     -23.272 -53.187  -6.433  1.00 51.86           C  
ANISOU 1972  CB  LYS A1077     8455   5860   5391   -875   1056   -482       C  
ATOM   1973  CG  LYS A1077     -24.048 -54.287  -5.758  1.00 55.80           C  
ANISOU 1973  CG  LYS A1077     9203   6390   5607  -1142   1114   -428       C  
ATOM   1974  CD  LYS A1077     -23.928 -54.171  -4.253  1.00 60.62           C  
ANISOU 1974  CD  LYS A1077    10179   7094   5758  -1604   1112   -468       C  
ATOM   1975  CE  LYS A1077     -24.904 -55.103  -3.567  1.00 65.02           C  
ANISOU 1975  CE  LYS A1077    11001   7715   5987  -1966   1258   -467       C  
ATOM   1976  NZ  LYS A1077     -25.106 -56.342  -4.375  1.00 66.08           N  
ANISOU 1976  NZ  LYS A1077    11061   7742   6306  -1745   1093   -230       N  
ATOM   1977  N   LEU A1078     -25.292 -52.275  -8.674  1.00 45.61           N  
ANISOU 1977  N   LEU A1078     7024   4993   5311   -484   1469   -705       N  
ATOM   1978  CA  LEU A1078     -26.633 -52.231  -9.264  1.00 43.29           C  
ANISOU 1978  CA  LEU A1078     6510   4658   5279   -453   1649   -783       C  
ATOM   1979  C   LEU A1078     -26.625 -52.691 -10.728  1.00 44.04           C  
ANISOU 1979  C   LEU A1078     6468   4739   5528   -290   1467   -575       C  
ATOM   1980  O   LEU A1078     -27.456 -53.507 -11.140  1.00 44.90           O  
ANISOU 1980  O   LEU A1078     6556   4856   5649   -325   1510   -524       O  
ATOM   1981  CB  LEU A1078     -27.217 -50.814  -9.163  1.00 43.63           C  
ANISOU 1981  CB  LEU A1078     6287   4596   5694   -434   1830  -1012       C  
ATOM   1982  CG  LEU A1078     -27.465 -50.280  -7.752  1.00 45.13           C  
ANISOU 1982  CG  LEU A1078     6581   4795   5771   -673   2139  -1343       C  
ATOM   1983  CD1 LEU A1078     -27.768 -48.787  -7.795  1.00 46.01           C  
ANISOU 1983  CD1 LEU A1078     6376   4731   6376   -599   2287  -1588       C  
ATOM   1984  CD2 LEU A1078     -28.601 -51.032  -7.076  1.00 46.23           C  
ANISOU 1984  CD2 LEU A1078     6795   4986   5783   -914   2442  -1517       C  
ATOM   1985  N   ALA A1079     -25.685 -52.159 -11.505  1.00 40.36           N  
ANISOU 1985  N   ALA A1079     5925   4264   5145   -171   1286   -476       N  
ATOM   1986  CA  ALA A1079     -25.565 -52.510 -12.916  1.00 39.27           C  
ANISOU 1986  CA  ALA A1079     5703   4146   5073   -128   1151   -322       C  
ATOM   1987  C   ALA A1079     -25.273 -53.996 -13.083  1.00 39.62           C  
ANISOU 1987  C   ALA A1079     5908   4225   4921   -148   1134   -263       C  
ATOM   1988  O   ALA A1079     -25.815 -54.655 -13.970  1.00 38.69           O  
ANISOU 1988  O   ALA A1079     5763   4126   4812   -200   1139   -205       O  
ATOM   1989  CB  ALA A1079     -24.473 -51.682 -13.578  1.00 39.98           C  
ANISOU 1989  CB  ALA A1079     5726   4244   5221    -80   1010   -269       C  
ATOM   1990  N   ASN A1080     -24.418 -54.511 -12.210  1.00 41.22           N  
ANISOU 1990  N   ASN A1080     6271   4406   4983   -133   1083   -267       N  
ATOM   1991  CA  ASN A1080     -24.016 -55.913 -12.254  1.00 43.58           C  
ANISOU 1991  CA  ASN A1080     6685   4650   5222   -132   1017   -202       C  
ATOM   1992  C   ASN A1080     -25.190 -56.860 -12.000  1.00 41.64           C  
ANISOU 1992  C   ASN A1080     6546   4400   4877   -239   1115   -181       C  
ATOM   1993  O   ASN A1080     -25.251 -57.967 -12.551  1.00 41.00           O  
ANISOU 1993  O   ASN A1080     6495   4265   4819   -245   1104   -143       O  
ATOM   1994  CB  ASN A1080     -22.906 -56.167 -11.236  1.00 46.47           C  
ANISOU 1994  CB  ASN A1080     7177   4940   5541   -120    839   -144       C  
ATOM   1995  CG  ASN A1080     -22.223 -57.486 -11.462  1.00 50.64           C  
ANISOU 1995  CG  ASN A1080     7718   5316   6206    -68    703    -70       C  
ATOM   1996  OD1 ASN A1080     -21.841 -57.808 -12.586  1.00 46.25           O  
ANISOU 1996  OD1 ASN A1080     7007   4724   5840      9    765   -150       O  
ATOM   1997  ND2 ASN A1080     -22.066 -58.265 -10.398  1.00 55.16           N  
ANISOU 1997  ND2 ASN A1080     8476   5778   6706   -156    515     73       N  
ATOM   1998  N   GLU A1081     -26.117 -56.411 -11.162  1.00 46.60           N  
ANISOU 1998  N   GLU A1081     7214   5074   5417   -349   1248   -246       N  
ATOM   1999  CA  GLU A1081     -27.311 -57.180 -10.846  1.00 45.84           C  
ANISOU 1999  CA  GLU A1081     7195   4991   5229   -492   1387   -261       C  
ATOM   2000  C   GLU A1081     -28.406 -56.952 -11.880  1.00 44.77           C  
ANISOU 2000  C   GLU A1081     6832   4879   5298   -472   1483   -289       C  
ATOM   2001  O   GLU A1081     -29.484 -57.510 -11.778  1.00 45.48           O  
ANISOU 2001  O   GLU A1081     6921   4980   5379   -584   1605   -313       O  
ATOM   2002  CB  GLU A1081     -27.795 -56.824  -9.436  1.00 46.94           C  
ANISOU 2002  CB  GLU A1081     7476   5178   5183   -700   1549   -383       C  
ATOM   2003  CG  GLU A1081     -26.869 -57.377  -8.359  1.00 51.09           C  
ANISOU 2003  CG  GLU A1081     8313   5682   5415   -846   1365   -263       C  
ATOM   2004  CD  GLU A1081     -26.938 -56.628  -7.042  1.00 58.34           C  
ANISOU 2004  CD  GLU A1081     9398   6685   6083  -1115   1500   -409       C  
ATOM   2005  OE1 GLU A1081     -27.522 -55.516  -6.986  1.00 59.06           O  
ANISOU 2005  OE1 GLU A1081     9306   6818   6316  -1119   1770   -664       O  
ATOM   2006  OE2 GLU A1081     -26.402 -57.166  -6.049  1.00 61.89           O  
ANISOU 2006  OE2 GLU A1081    10166   7138   6211  -1363   1320   -269       O  
ATOM   2007  N   GLY A1082     -28.111 -56.140 -12.885  1.00 37.86           N  
ANISOU 2007  N   GLY A1082     5771   4007   4606   -372   1390   -257       N  
ATOM   2008  CA  GLY A1082     -29.044 -55.863 -13.961  1.00 39.87           C  
ANISOU 2008  CA  GLY A1082     5822   4266   5061   -411   1359   -198       C  
ATOM   2009  C   GLY A1082     -30.073 -54.787 -13.655  1.00 42.79           C  
ANISOU 2009  C   GLY A1082     5936   4568   5755   -413   1433   -276       C  
ATOM   2010  O   GLY A1082     -31.045 -54.633 -14.388  1.00 46.61           O  
ANISOU 2010  O   GLY A1082     6209   5008   6491   -465   1360   -196       O  
ATOM   2011  N   LYS A1083     -29.869 -54.042 -12.572  1.00 43.30           N  
ANISOU 2011  N   LYS A1083     5994   4596   5862   -383   1571   -447       N  
ATOM   2012  CA  LYS A1083     -30.837 -53.023 -12.173  1.00 45.18           C  
ANISOU 2012  CA  LYS A1083     5939   4712   6514   -390   1723   -622       C  
ATOM   2013  C   LYS A1083     -30.520 -51.710 -12.881  1.00 48.82           C  
ANISOU 2013  C   LYS A1083     6163   5051   7335   -277   1516   -536       C  
ATOM   2014  O   LYS A1083     -29.961 -50.801 -12.280  1.00 47.45           O  
ANISOU 2014  O   LYS A1083     5975   4823   7231   -228   1580   -673       O  
ATOM   2015  CB  LYS A1083     -30.828 -52.841 -10.655  1.00 44.77           C  
ANISOU 2015  CB  LYS A1083     6013   4681   6317   -502   2037   -915       C  
ATOM   2016  CG  LYS A1083     -31.336 -54.057  -9.889  1.00 44.76           C  
ANISOU 2016  CG  LYS A1083     6249   4784   5973   -707   2234   -982       C  
ATOM   2017  CD  LYS A1083     -31.230 -53.860  -8.385  1.00 45.25           C  
ANISOU 2017  CD  LYS A1083     6522   4907   5765   -950   2523  -1253       C  
ATOM   2018  CE  LYS A1083     -31.502 -55.177  -7.654  1.00 49.44           C  
ANISOU 2018  CE  LYS A1083     7393   5557   5836  -1226   2618  -1219       C  
ATOM   2019  NZ  LYS A1083     -32.959 -55.416  -7.478  1.00 54.34           N  
ANISOU 2019  NZ  LYS A1083     7827   6169   6651  -1392   2951  -1437       N  
ATOM   2020  N   VAL A1084     -30.869 -51.628 -14.161  1.00 46.34           N  
ANISOU 2020  N   VAL A1084     5696   4696   7217   -289   1241   -287       N  
ATOM   2021  CA  VAL A1084     -30.435 -50.521 -15.019  1.00 47.68           C  
ANISOU 2021  CA  VAL A1084     5721   4766   7627   -263    946   -101       C  
ATOM   2022  C   VAL A1084     -30.960 -49.168 -14.546  1.00 48.96           C  
ANISOU 2022  C   VAL A1084     5535   4663   8404   -175    975   -237       C  
ATOM   2023  O   VAL A1084     -30.194 -48.223 -14.439  1.00 47.41           O  
ANISOU 2023  O   VAL A1084     5332   4398   8284   -114    910   -255       O  
ATOM   2024  CB  VAL A1084     -30.876 -50.750 -16.484  1.00 47.96           C  
ANISOU 2024  CB  VAL A1084     5697   4815   7709   -420    606    230       C  
ATOM   2025  CG1 VAL A1084     -30.452 -49.603 -17.364  1.00 48.13           C  
ANISOU 2025  CG1 VAL A1084     5618   4737   7931   -488    256    472       C  
ATOM   2026  CG2 VAL A1084     -30.292 -52.056 -17.009  1.00 47.16           C  
ANISOU 2026  CG2 VAL A1084     5927   4951   7042   -536    640    284       C  
ATOM   2027  N   LYS A1085     -32.258 -49.103 -14.250  1.00 51.17           N  
ANISOU 2027  N   LYS A1085     5500   4773   9169   -176   1097   -367       N  
ATOM   2028  CA  LYS A1085     -32.918 -47.877 -13.779  1.00 54.15           C  
ANISOU 2028  CA  LYS A1085     5446   4820  10309    -90   1186   -579       C  
ATOM   2029  C   LYS A1085     -32.235 -47.337 -12.528  1.00 52.28           C  
ANISOU 2029  C   LYS A1085     5334   4596   9933    -54   1555   -965       C  
ATOM   2030  O   LYS A1085     -31.906 -46.138 -12.447  1.00 51.08           O  
ANISOU 2030  O   LYS A1085     5007   4231  10170     24   1494  -1034       O  
ATOM   2031  CB  LYS A1085     -34.395 -48.140 -13.476  1.00 55.70           C  
ANISOU 2031  CB  LYS A1085     5276   4856  11033   -118   1386   -770       C  
ATOM   2032  CG  LYS A1085     -35.373 -47.766 -14.590  1.00 62.27           C  
ANISOU 2032  CG  LYS A1085     5669   5414  12577   -120    936   -440       C  
ATOM   2033  CD  LYS A1085     -34.891 -46.570 -15.383  1.00 66.16           C  
ANISOU 2033  CD  LYS A1085     6016   5674  13446    -75    460   -127       C  
ATOM   2034  CE  LYS A1085     -35.786 -46.314 -16.596  1.00 68.36           C  
ANISOU 2034  CE  LYS A1085     5941   5701  14330   -170   -133    335       C  
ATOM   2035  NZ  LYS A1085     -35.117 -45.381 -17.552  1.00 67.23           N  
ANISOU 2035  NZ  LYS A1085     5840   5433  14274   -250   -692    771       N  
ATOM   2036  N   GLU A1086     -32.047 -48.228 -11.554  1.00 53.55           N  
ANISOU 2036  N   GLU A1086     5814   4993   9538   -158   1908  -1196       N  
ATOM   2037  CA  GLU A1086     -31.403 -47.881 -10.294  1.00 53.85           C  
ANISOU 2037  CA  GLU A1086     6061   5099   9301   -237   2237  -1537       C  
ATOM   2038  C   GLU A1086     -29.979 -47.402 -10.528  1.00 51.67           C  
ANISOU 2038  C   GLU A1086     6008   4896   8726   -160   1984  -1355       C  
ATOM   2039  O   GLU A1086     -29.559 -46.407  -9.944  1.00 53.10           O  
ANISOU 2039  O   GLU A1086     6145   4971   9057   -161   2100  -1572       O  
ATOM   2040  CB  GLU A1086     -31.394 -49.072  -9.326  1.00 51.14           C  
ANISOU 2040  CB  GLU A1086     6097   5015   8318   -449   2525  -1683       C  
ATOM   2041  CG  GLU A1086     -32.729 -49.380  -8.676  1.00 52.90           C  
ANISOU 2041  CG  GLU A1086     6135   5188   8775   -622   2940  -2019       C  
ATOM   2042  CD  GLU A1086     -33.436 -50.539  -9.346  1.00 62.11           C  
ANISOU 2042  CD  GLU A1086     7296   6435   9867   -624   2812  -1778       C  
ATOM   2043  OE1 GLU A1086     -33.222 -50.741 -10.569  1.00 64.86           O  
ANISOU 2043  OE1 GLU A1086     7602   6774  10267   -462   2394  -1386       O  
ATOM   2044  OE2 GLU A1086     -34.182 -51.267  -8.652  1.00 64.66           O  
ANISOU 2044  OE2 GLU A1086     7690   6847  10031   -841   3140  -1990       O  
ATOM   2045  N   ALA A1087     -29.236 -48.119 -11.373  1.00 49.81           N  
ANISOU 2045  N   ALA A1087     5998   4835   8091   -119   1676  -1001       N  
ATOM   2046  CA  ALA A1087     -27.855 -47.753 -11.662  1.00 48.48           C  
ANISOU 2046  CA  ALA A1087     6009   4746   7664    -66   1461   -849       C  
ATOM   2047  C   ALA A1087     -27.793 -46.396 -12.349  1.00 51.02           C  
ANISOU 2047  C   ALA A1087     6056   4847   8481     12   1244   -752       C  
ATOM   2048  O   ALA A1087     -26.870 -45.619 -12.118  1.00 49.67           O  
ANISOU 2048  O   ALA A1087     5946   4658   8268     36   1201   -793       O  
ATOM   2049  CB  ALA A1087     -27.173 -48.813 -12.522  1.00 47.56           C  
ANISOU 2049  CB  ALA A1087     6112   4823   7137    -69   1247   -569       C  
ATOM   2050  N   GLN A1088     -28.771 -46.119 -13.200  1.00 52.49           N  
ANISOU 2050  N   GLN A1088     5941   4848   9155     26   1057   -587       N  
ATOM   2051  CA  GLN A1088     -28.805 -44.841 -13.888  1.00 55.66           C  
ANISOU 2051  CA  GLN A1088     6070   4980  10100     61    758   -419       C  
ATOM   2052  C   GLN A1088     -29.107 -43.717 -12.905  1.00 55.51           C  
ANISOU 2052  C   GLN A1088     5788   4672  10633    139   1005   -787       C  
ATOM   2053  O   GLN A1088     -28.467 -42.666 -12.963  1.00 55.13           O  
ANISOU 2053  O   GLN A1088     5690   4477  10778    172    876   -768       O  
ATOM   2054  CB  GLN A1088     -29.821 -44.868 -15.025  1.00 56.92           C  
ANISOU 2054  CB  GLN A1088     5967   4980  10678      2    405    -89       C  
ATOM   2055  CG  GLN A1088     -29.343 -45.714 -16.196  1.00 56.78           C  
ANISOU 2055  CG  GLN A1088     6236   5237  10099   -165    130    275       C  
ATOM   2056  CD  GLN A1088     -30.378 -45.829 -17.284  1.00 57.23           C  
ANISOU 2056  CD  GLN A1088     6096   5175  10473   -316   -245    621       C  
ATOM   2057  OE1 GLN A1088     -31.555 -46.070 -17.012  1.00 56.38           O  
ANISOU 2057  OE1 GLN A1088     5718   4918  10786   -265   -172    537       O  
ATOM   2058  NE2 GLN A1088     -29.950 -45.650 -18.527  1.00 56.66           N  
ANISOU 2058  NE2 GLN A1088     6161   5175  10192   -557   -655   1013       N  
ATOM   2059  N   ALA A1089     -30.043 -43.938 -11.982  1.00 56.85           N  
ANISOU 2059  N   ALA A1089     5798   4761  11041    130   1404  -1167       N  
ATOM   2060  CA  ALA A1089     -30.341 -42.908 -10.974  1.00 59.38           C  
ANISOU 2060  CA  ALA A1089     5869   4808  11886    141   1759  -1640       C  
ATOM   2061  C   ALA A1089     -29.130 -42.643 -10.075  1.00 56.59           C  
ANISOU 2061  C   ALA A1089     5880   4643  10977     60   1958  -1854       C  
ATOM   2062  O   ALA A1089     -28.889 -41.513  -9.661  1.00 57.90           O  
ANISOU 2062  O   ALA A1089     5903   4583  11514     73   2059  -2092       O  
ATOM   2063  CB  ALA A1089     -31.546 -43.306 -10.136  1.00 59.74           C  
ANISOU 2063  CB  ALA A1089     5705   4784  12210     57   2240  -2076       C  
ATOM   2064  N   ALA A1090     -28.369 -43.689  -9.780  1.00 57.84           N  
ANISOU 2064  N   ALA A1090     6493   5186  10297    -34   1982  -1757       N  
ATOM   2065  CA  ALA A1090     -27.165 -43.543  -8.978  1.00 57.88           C  
ANISOU 2065  CA  ALA A1090     6848   5376   9768   -137   2064  -1873       C  
ATOM   2066  C   ALA A1090     -26.120 -42.747  -9.741  1.00 62.33           C  
ANISOU 2066  C   ALA A1090     7406   5884  10392    -21   1697  -1601       C  
ATOM   2067  O   ALA A1090     -25.372 -41.966  -9.147  1.00 61.94           O  
ANISOU 2067  O   ALA A1090     7441   5806  10288    -74   1765  -1772       O  
ATOM   2068  CB  ALA A1090     -26.608 -44.901  -8.580  1.00 55.78           C  
ANISOU 2068  CB  ALA A1090     7008   5461   8724   -256   2063  -1753       C  
ATOM   2069  N   ALA A1091     -26.070 -42.942 -11.057  1.00 61.29           N  
ANISOU 2069  N   ALA A1091     7197   5751  10338     76   1321  -1188       N  
ATOM   2070  CA  ALA A1091     -25.126 -42.203 -11.889  1.00 60.97           C  
ANISOU 2070  CA  ALA A1091     7163   5676  10325    108    981   -917       C  
ATOM   2071  C   ALA A1091     -25.471 -40.711 -11.933  1.00 63.48           C  
ANISOU 2071  C   ALA A1091     7153   5601  11365    155    913  -1002       C  
ATOM   2072  O   ALA A1091     -24.593 -39.875 -12.130  1.00 61.65           O  
ANISOU 2072  O   ALA A1091     6961   5315  11147    144    746   -917       O  
ATOM   2073  CB  ALA A1091     -25.082 -42.784 -13.297  1.00 59.51           C  
ANISOU 2073  CB  ALA A1091     7010   5603  10000     81    639   -492       C  
ATOM   2074  N   GLU A1092     -26.746 -40.383 -11.743  1.00 63.84           N  
ANISOU 2074  N   GLU A1092     6843   5340  12074    204   1043  -1183       N  
ATOM   2075  CA  GLU A1092     -27.180 -38.988 -11.744  1.00 70.95           C  
ANISOU 2075  CA  GLU A1092     7346   5767  13846    271    982  -1301       C  
ATOM   2076  C   GLU A1092     -26.767 -38.293 -10.448  1.00 69.03           C  
ANISOU 2076  C   GLU A1092     7155   5458  13618    223   1412  -1828       C  
ATOM   2077  O   GLU A1092     -26.492 -37.092 -10.433  1.00 66.93           O  
ANISOU 2077  O   GLU A1092     6715   4928  13787    243   1322  -1883       O  
ATOM   2078  CB  GLU A1092     -28.697 -38.891 -11.937  1.00 75.40           C  
ANISOU 2078  CB  GLU A1092     7426   5966  15257    345    994  -1367       C  
ATOM   2079  N   GLN A1093     -26.728 -39.061  -9.363  1.00 74.41           N  
ANISOU 2079  N   GLN A1093     8102   6426  13746     94   1848  -2179       N  
ATOM   2080  CA  GLN A1093     -26.303 -38.556  -8.060  1.00 70.36           C  
ANISOU 2080  CA  GLN A1093     7742   5966  13027    -84   2255  -2659       C  
ATOM   2081  C   GLN A1093     -24.792 -38.355  -8.045  1.00 68.81           C  
ANISOU 2081  C   GLN A1093     7903   5970  12271   -126   2039  -2483       C  
ATOM   2082  O   GLN A1093     -24.253 -37.649  -7.195  1.00 71.61           O  
ANISOU 2082  O   GLN A1093     8367   6294  12549   -269   2247  -2806       O  
ATOM   2083  CB  GLN A1093     -26.730 -39.517  -6.942  1.00 69.00           C  
ANISOU 2083  CB  GLN A1093     7806   6098  12314   -326   2696  -2978       C  
ATOM   2084  N   LEU A1094     -24.115 -38.985  -8.997  1.00 67.11           N  
ANISOU 2084  N   LEU A1094     7853   5982  11664    -38   1630  -1983       N  
ATOM   2085  CA  LEU A1094     -22.679 -38.812  -9.162  1.00 67.35           C  
ANISOU 2085  CA  LEU A1094     8137   6204  11248    -67   1390  -1776       C  
ATOM   2086  C   LEU A1094     -22.417 -37.450  -9.760  1.00 71.33           C  
ANISOU 2086  C   LEU A1094     8415   6395  12291     -3   1165  -1680       C  
ATOM   2087  O   LEU A1094     -21.409 -36.804  -9.461  1.00 74.75           O  
ANISOU 2087  O   LEU A1094     8977   6859  12565    -70   1122  -1731       O  
ATOM   2088  CB  LEU A1094     -22.092 -39.905 -10.059  1.00 66.13           C  
ANISOU 2088  CB  LEU A1094     8163   6348  10614    -20   1098  -1353       C  
ATOM   2089  CG  LEU A1094     -21.848 -41.265  -9.414  1.00 68.36           C  
ANISOU 2089  CG  LEU A1094     8742   6949  10284    -97   1222  -1384       C  
ATOM   2090  CD1 LEU A1094     -21.797 -42.356 -10.459  1.00 68.40           C  
ANISOU 2090  CD1 LEU A1094     8785   7116  10088    -20   1013  -1045       C  
ATOM   2091  CD2 LEU A1094     -20.548 -41.217  -8.669  1.00 69.71           C  
ANISOU 2091  CD2 LEU A1094     9171   7294  10022   -208   1183  -1433       C  
ATOM   2092  N   LYS A1095     -23.338 -37.016 -10.610  1.00 73.75           N  
ANISOU 2092  N   LYS A1095     8379   6380  13263    102    975  -1509       N  
ATOM   2093  CA  LYS A1095     -23.231 -35.706 -11.233  1.00 78.48           C  
ANISOU 2093  CA  LYS A1095     8738   6603  14480    136    681  -1351       C  
ATOM   2094  C   LYS A1095     -23.195 -34.611 -10.168  1.00 82.39           C  
ANISOU 2094  C   LYS A1095     9111   6810  15385    109   1001  -1847       C  
ATOM   2095  O   LYS A1095     -22.416 -33.666 -10.274  1.00 84.06           O  
ANISOU 2095  O   LYS A1095     9344   6893  15703     74    840  -1794       O  
ATOM   2096  CB  LYS A1095     -24.392 -35.481 -12.202  1.00 77.76           C  
ANISOU 2096  CB  LYS A1095     8266   6153  15126    217    373  -1066       C  
ATOM   2097  CG  LYS A1095     -24.487 -34.081 -12.766  1.00 80.20           C  
ANISOU 2097  CG  LYS A1095     8270   6067  16136    222     12   -862       C  
ATOM   2098  CD  LYS A1095     -25.417 -34.062 -13.970  1.00 80.77           C  
ANISOU 2098  CD  LYS A1095     8060   5983  16646    208   -481   -373       C  
ATOM   2099  CE  LYS A1095     -25.006 -35.127 -14.985  1.00 78.38           C  
ANISOU 2099  CE  LYS A1095     8103   5929  15750     73   -767     80       C  
ATOM   2100  NZ  LYS A1095     -25.849 -35.085 -16.216  1.00 77.63           N  
ANISOU 2100  NZ  LYS A1095     7802   5702  15990    -41  -1309    601       N  
ATOM   2101  N   THR A1096     -24.021 -34.751  -9.130  1.00 81.24           N  
ANISOU 2101  N   THR A1096     8853   6707  15308     60   1456  -2293       N  
ATOM   2102  CA  THR A1096     -24.102 -33.740  -8.066  1.00 83.76           C  
ANISOU 2102  CA  THR A1096     9042   6961  15824    -61   1796  -2731       C  
ATOM   2103  C   THR A1096     -22.842 -33.718  -7.191  1.00 79.45           C  
ANISOU 2103  C   THR A1096     8941   6650  14598   -249   1969  -2954       C  
ATOM   2104  O   THR A1096     -22.390 -32.655  -6.769  1.00 77.45           O  
ANISOU 2104  O   THR A1096     8646   6289  14493   -328   2026  -3127       O  
ATOM   2105  CB  THR A1096     -25.338 -33.960  -7.160  1.00 77.98           C  
ANISOU 2105  CB  THR A1096     8079   6268  15280   -177   2273  -3146       C  
ATOM   2106  N   THR A1097     -22.286 -34.897  -6.923  1.00 79.53           N  
ANISOU 2106  N   THR A1097     9364   6972  13883   -341   2024  -2939       N  
ATOM   2107  CA  THR A1097     -21.049 -35.024  -6.157  1.00 79.35           C  
ANISOU 2107  CA  THR A1097     9764   7237  13149   -558   2063  -3036       C  
ATOM   2108  C   THR A1097     -19.900 -34.334  -6.876  1.00 80.55           C  
ANISOU 2108  C   THR A1097     9936   7367  13304   -476   1653  -2695       C  
ATOM   2109  O   THR A1097     -19.142 -33.575  -6.267  1.00 79.33           O  
ANISOU 2109  O   THR A1097     9903   7193  13047   -632   1714  -2897       O  
ATOM   2110  CB  THR A1097     -20.680 -36.497  -5.926  1.00 76.65           C  
ANISOU 2110  CB  THR A1097     9777   7358  11989   -644   1993  -2818       C  
ATOM   2111  OG1 THR A1097     -21.756 -37.161  -5.249  1.00 78.43           O  
ANISOU 2111  OG1 THR A1097    10018   7622  12159   -773   2376  -3120       O  
ATOM   2112  CG2 THR A1097     -19.402 -36.615  -5.101  1.00 75.32           C  
ANISOU 2112  CG2 THR A1097     9997   7482  11137   -890   1921  -2828       C  
ATOM   2113  N   ARG A1098     -19.785 -34.607  -8.175  1.00 81.01           N  
ANISOU 2113  N   ARG A1098     9890   7442  13448   -288   1254  -2195       N  
ATOM   2114  CA  ARG A1098     -18.784 -33.964  -9.019  1.00 79.98           C  
ANISOU 2114  CA  ARG A1098     9762   7292  13336   -264    879  -1856       C  
ATOM   2115  C   ARG A1098     -18.913 -32.439  -8.966  1.00 78.03           C  
ANISOU 2115  C   ARG A1098     9282   6590  13777   -272    875  -2030       C  
ATOM   2116  O   ARG A1098     -17.908 -31.730  -8.932  1.00 81.94           O  
ANISOU 2116  O   ARG A1098     9876   7092  14166   -361    750  -1996       O  
ATOM   2117  CB  ARG A1098     -18.899 -34.465 -10.464  1.00 76.80           C  
ANISOU 2117  CB  ARG A1098     9281   6950  12949   -164    516  -1349       C  
ATOM   2118  N   ASN A1099     -20.143 -31.933  -8.933  1.00 77.40           N  
ANISOU 2118  N   ASN A1099     8861   6080  14466   -181   1015  -2235       N  
ATOM   2119  CA  ASN A1099     -20.355 -30.490  -8.849  1.00 82.55           C  
ANISOU 2119  CA  ASN A1099     9221   6431  15713   -166    983  -2324       C  
ATOM   2120  C   ASN A1099     -19.907 -29.934  -7.505  1.00 81.67           C  
ANISOU 2120  C   ASN A1099     9250   6411  15370   -346   1387  -2829       C  
ATOM   2121  O   ASN A1099     -19.370 -28.832  -7.425  1.00 82.23           O  
ANISOU 2121  O   ASN A1099     9273   6317  15654   -393   1312  -2873       O  
ATOM   2122  CB  ASN A1099     -21.826 -30.132  -9.081  1.00 84.26           C  
ANISOU 2122  CB  ASN A1099     8950   6403  16661    -34   1000  -2328       C  
ATOM   2123  CG  ASN A1099     -22.359 -30.688 -10.379  1.00 83.34           C  
ANISOU 2123  CG  ASN A1099     8707   6220  16739     82    566  -1809       C  
ATOM   2124  OD1 ASN A1099     -21.592 -31.027 -11.280  1.00 82.78           O  
ANISOU 2124  OD1 ASN A1099     8874   6223  16355     45    198  -1388       O  
ATOM   2125  ND2 ASN A1099     -23.678 -30.788 -10.486  1.00 84.46           N  
ANISOU 2125  ND2 ASN A1099     8466   6231  17395    166    607  -1837       N  
ATOM   2126  N   ALA A1100     -20.117 -30.719  -6.455  1.00 80.91           N  
ANISOU 2126  N   ALA A1100     9359   6597  14787   -497   1794  -3183       N  
ATOM   2127  CA  ALA A1100     -19.907 -30.252  -5.091  1.00 84.67           C  
ANISOU 2127  CA  ALA A1100     9978   7200  14995   -767   2206  -3662       C  
ATOM   2128  C   ALA A1100     -18.427 -30.186  -4.711  1.00 84.06           C  
ANISOU 2128  C   ALA A1100    10320   7312  14306   -969   2087  -3665       C  
ATOM   2129  O   ALA A1100     -17.907 -29.115  -4.387  1.00 83.70           O  
ANISOU 2129  O   ALA A1100    10259   7147  14396  -1067   2105  -3808       O  
ATOM   2130  CB  ALA A1100     -20.666 -31.149  -4.110  1.00 87.14           C  
ANISOU 2130  CB  ALA A1100    10400   7782  14929   -962   2639  -3972       C  
ATOM   2131  N   TYR A1101     -17.749 -31.329  -4.755  1.00 79.92           N  
ANISOU 2131  N   TYR A1101    10146   7073  13148  -1046   1951  -3510       N  
ATOM   2132  CA  TYR A1101     -16.382 -31.409  -4.244  1.00 82.39           C  
ANISOU 2132  CA  TYR A1101    10823   7675  12805  -1281   1801  -3464       C  
ATOM   2133  C   TYR A1101     -15.312 -31.441  -5.337  1.00 82.61           C  
ANISOU 2133  C   TYR A1101    10827   7824  12737  -1097   1292  -2906       C  
ATOM   2134  O   TYR A1101     -14.126 -31.307  -5.043  1.00 82.00           O  
ANISOU 2134  O   TYR A1101    10943   7948  12267  -1249   1117  -2823       O  
ATOM   2135  CB  TYR A1101     -16.234 -32.645  -3.350  1.00 85.16           C  
ANISOU 2135  CB  TYR A1101    11541   8456  12359  -1528   1889  -3490       C  
ATOM   2136  N   ILE A1102     -15.731 -31.600  -6.591  1.00 80.61           N  
ANISOU 2136  N   ILE A1102    10335   7451  12843   -824   1065  -2543       N  
ATOM   2137  CA  ILE A1102     -14.794 -31.879  -7.678  1.00 80.99           C  
ANISOU 2137  CA  ILE A1102    10394   7688  12691   -729    661  -2049       C  
ATOM   2138  C   ILE A1102     -14.737 -30.809  -8.785  1.00 77.10           C  
ANISOU 2138  C   ILE A1102     9678   6882  12734   -658    399  -1803       C  
ATOM   2139  O   ILE A1102     -13.685 -30.211  -9.000  1.00 77.30           O  
ANISOU 2139  O   ILE A1102     9760   6949  12661   -757    218  -1687       O  
ATOM   2140  CB  ILE A1102     -15.119 -33.249  -8.321  1.00 75.97           C  
ANISOU 2140  CB  ILE A1102     9775   7300  11791   -593    568  -1758       C  
ATOM   2141  CG1 ILE A1102     -14.857 -34.378  -7.320  1.00 75.24           C  
ANISOU 2141  CG1 ILE A1102     9941   7537  11109   -700    694  -1876       C  
ATOM   2142  CG2 ILE A1102     -14.296 -33.476  -9.584  1.00 75.39           C  
ANISOU 2142  CG2 ILE A1102     9669   7378  11597   -546    240  -1330       C  
ATOM   2143  CD1 ILE A1102     -15.364 -35.723  -7.766  1.00 73.16           C  
ANISOU 2143  CD1 ILE A1102     9689   7449  10660   -573    668  -1674       C  
ATOM   2144  N   GLN A1103     -15.860 -30.566  -9.465  1.00 74.03           N  
ANISOU 2144  N   GLN A1103     9038   6168  12922   -523    343  -1699       N  
ATOM   2145  CA  GLN A1103     -15.877 -29.816 -10.731  1.00 75.52           C  
ANISOU 2145  CA  GLN A1103     9053   6093  13547   -509    -42  -1296       C  
ATOM   2146  C   GLN A1103     -15.182 -28.449 -10.669  1.00 76.11           C  
ANISOU 2146  C   GLN A1103     9096   5902  13920   -626   -161  -1338       C  
ATOM   2147  O   GLN A1103     -14.413 -28.098 -11.567  1.00 72.14           O  
ANISOU 2147  O   GLN A1103     8645   5458  13307   -743   -484   -971       O  
ATOM   2148  CB  GLN A1103     -17.323 -29.639 -11.214  1.00 77.86           C  
ANISOU 2148  CB  GLN A1103     9040   5978  14564   -374   -116  -1218       C  
ATOM   2149  CG  GLN A1103     -17.486 -29.400 -12.719  1.00 78.39           C  
ANISOU 2149  CG  GLN A1103     9006   5902  14877   -428   -624   -632       C  
ATOM   2150  CD  GLN A1103     -17.516 -30.683 -13.530  1.00 79.20           C  
ANISOU 2150  CD  GLN A1103     9257   6418  14418   -460   -733   -310       C  
ATOM   2151  OE1 GLN A1103     -17.068 -31.736 -13.072  1.00 81.97           O  
ANISOU 2151  OE1 GLN A1103     9807   7195  14144   -431   -483   -466       O  
ATOM   2152  NE2 GLN A1103     -18.061 -30.605 -14.741  1.00 78.65           N  
ANISOU 2152  NE2 GLN A1103     9091   6198  14593   -556  -1133    151       N  
ATOM   2153  N   LYS A1104     -15.441 -27.682  -9.612  1.00 70.86           N  
ANISOU 2153  N   LYS A1104     8359   4951  13613   -643    129  -1814       N  
ATOM   2154  CA  LYS A1104     -14.828 -26.374  -9.470  1.00 73.52           C  
ANISOU 2154  CA  LYS A1104     8663   4998  14273   -760     47  -1907       C  
ATOM   2155  C   LYS A1104     -13.308 -26.492  -9.419  1.00 78.09           C  
ANISOU 2155  C   LYS A1104     9525   6005  14140   -932    -63  -1781       C  
ATOM   2156  O   LYS A1104     -12.594 -25.661  -9.978  1.00 82.98           O  
ANISOU 2156  O   LYS A1104    10138   6509  14880  -1043   -325  -1561       O  
ATOM   2157  CB  LYS A1104     -15.344 -25.658  -8.216  1.00 76.79           C  
ANISOU 2157  CB  LYS A1104     8981   5305  14890   -757    471  -2441       C  
ATOM   2158  N   TYR A1105     -12.812 -27.535  -8.763  1.00 74.45           N  
ANISOU 2158  N   TYR A1105     9291   6015  12981   -973    105  -1899       N  
ATOM   2159  CA  TYR A1105     -11.370 -27.692  -8.610  1.00 74.00           C  
ANISOU 2159  CA  TYR A1105     9434   6326  12357  -1127    -13  -1806       C  
ATOM   2160  C   TYR A1105     -10.739 -28.278  -9.876  1.00 66.51           C  
ANISOU 2160  C   TYR A1105     8474   5640  11157  -1109   -304  -1333       C  
ATOM   2161  O   TYR A1105      -9.589 -27.977 -10.179  1.00 66.74           O  
ANISOU 2161  O   TYR A1105     8548   5818  10992  -1249   -459  -1201       O  
ATOM   2162  CB  TYR A1105     -11.041 -28.561  -7.392  1.00 76.69           C  
ANISOU 2162  CB  TYR A1105    10002   7013  12122  -1223    192  -2068       C  
ATOM   2163  N   LEU A1106     -11.485 -29.099 -10.611  1.00 63.79           N  
ANISOU 2163  N   LEU A1106     8065   5352  10818   -980   -344  -1118       N  
ATOM   2164  CA  LEU A1106     -10.994 -29.618 -11.888  1.00 62.69           C  
ANISOU 2164  CA  LEU A1106     7925   5443  10449  -1041   -558   -729       C  
ATOM   2165  C   LEU A1106     -10.746 -28.451 -12.849  1.00 65.11           C  
ANISOU 2165  C   LEU A1106     8171   5510  11059  -1223   -830   -458       C  
ATOM   2166  O   LEU A1106      -9.715 -28.384 -13.507  1.00 64.23           O  
ANISOU 2166  O   LEU A1106     8115   5611  10679  -1421   -946   -281       O  
ATOM   2167  CB  LEU A1106     -11.975 -30.617 -12.510  1.00 61.55           C  
ANISOU 2167  CB  LEU A1106     7740   5362  10282   -922   -552   -565       C  
ATOM   2168  CG  LEU A1106     -11.881 -32.107 -12.129  1.00 63.07           C  
ANISOU 2168  CG  LEU A1106     8022   5913  10029   -815   -382   -653       C  
ATOM   2169  CD1 LEU A1106     -12.801 -32.983 -12.980  1.00 60.71           C  
ANISOU 2169  CD1 LEU A1106     7683   5660   9725   -747   -409   -451       C  
ATOM   2170  CD2 LEU A1106     -10.452 -32.611 -12.218  1.00 64.61           C  
ANISOU 2170  CD2 LEU A1106     8275   6445   9828   -911   -410   -623       C  
ATOM   2171  N   ALA A 383     -11.695 -27.527 -12.911  1.00 63.07           N  
ANISOU 2171  N   ALA A 383     9729   3408  10824   -685   -617   1490       N  
ATOM   2172  CA  ALA A 383     -11.594 -26.389 -13.822  1.00 59.04           C  
ANISOU 2172  CA  ALA A 383     9104   3096  10234   -646   -672   1260       C  
ATOM   2173  C   ALA A 383     -10.427 -25.483 -13.451  1.00 59.01           C  
ANISOU 2173  C   ALA A 383     9094   3328  10000   -416   -657   1291       C  
ATOM   2174  O   ALA A 383      -9.853 -24.806 -14.301  1.00 58.10           O  
ANISOU 2174  O   ALA A 383     8922   3400   9752   -280   -690   1043       O  
ATOM   2175  CB  ALA A 383     -12.881 -25.606 -13.826  1.00 62.21           C  
ANISOU 2175  CB  ALA A 383     9334   3666  10637   -891   -596   1290       C  
ATOM   2176  N   LYS A 384     -10.080 -25.471 -12.173  1.00 61.22           N  
ANISOU 2176  N   LYS A 384     9422   3665  10175   -367   -584   1579       N  
ATOM   2177  CA  LYS A 384      -8.961 -24.665 -11.728  1.00 63.16           C  
ANISOU 2177  CA  LYS A 384     9645   4189  10162   -144   -566   1592       C  
ATOM   2178  C   LYS A 384      -7.661 -25.346 -12.148  1.00 61.27           C  
ANISOU 2178  C   LYS A 384     9511   3782   9989    115   -688   1471       C  
ATOM   2179  O   LYS A 384      -6.815 -24.756 -12.820  1.00 58.15           O  
ANISOU 2179  O   LYS A 384     9051   3561   9484    288   -717   1253       O  
ATOM   2180  CB  LYS A 384      -9.008 -24.482 -10.216  1.00 62.72           C  
ANISOU 2180  CB  LYS A 384     9626   4241   9961   -164   -471   1929       C  
ATOM   2181  CG  LYS A 384      -8.304 -23.250  -9.717  1.00 61.45           C  
ANISOU 2181  CG  LYS A 384     9386   4460   9502    -25   -431   1927       C  
ATOM   2182  CD  LYS A 384      -8.219 -23.291  -8.210  1.00 67.47           C  
ANISOU 2182  CD  LYS A 384    10237   5281  10117     -9   -372   2254       C  
ATOM   2183  CE  LYS A 384      -9.595 -23.357  -7.583  1.00 72.25           C  
ANISOU 2183  CE  LYS A 384    10834   5869  10750   -264   -223   2466       C  
ATOM   2184  NZ  LYS A 384      -9.500 -23.951  -6.218  1.00 76.35           N  
ANISOU 2184  NZ  LYS A 384    11512   6308  11189   -242   -178   2809       N  
ATOM   2185  N   ILE A 385      -7.540 -26.613 -11.778  1.00 57.56           N  
ANISOU 2185  N   ILE A 385     9191   2987   9694    140   -738   1603       N  
ATOM   2186  CA  ILE A 385      -6.279 -27.340 -11.923  1.00 59.00           C  
ANISOU 2186  CA  ILE A 385     9464   3042   9913    407   -823   1528       C  
ATOM   2187  C   ILE A 385      -5.981 -27.782 -13.360  1.00 59.39           C  
ANISOU 2187  C   ILE A 385     9520   2952  10094    495   -898   1181       C  
ATOM   2188  O   ILE A 385      -4.848 -28.126 -13.670  1.00 60.06           O  
ANISOU 2188  O   ILE A 385     9635   2997  10187    742   -951   1065       O  
ATOM   2189  CB  ILE A 385      -6.237 -28.555 -10.973  1.00 62.48           C  
ANISOU 2189  CB  ILE A 385    10049   3273  10419    418   -802   1769       C  
ATOM   2190  CG1 ILE A 385      -7.262 -29.614 -11.372  1.00 65.11           C  
ANISOU 2190  CG1 ILE A 385    10448   3330  10960    215   -780   1735       C  
ATOM   2191  CG2 ILE A 385      -6.459 -28.091  -9.536  1.00 62.32           C  
ANISOU 2191  CG2 ILE A 385    10043   3423  10213    360   -717   2101       C  
ATOM   2192  CD1 ILE A 385      -7.442 -30.699 -10.337  1.00 69.89           C  
ANISOU 2192  CD1 ILE A 385    11200   3736  11620    177   -732   2011       C  
ATOM   2193  N   THR A 386      -6.979 -27.733 -14.240  1.00 59.10           N  
ANISOU 2193  N   THR A 386     9445   2868  10141    304   -898   1010       N  
ATOM   2194  CA  THR A 386      -6.764 -27.981 -15.668  1.00 59.32           C  
ANISOU 2194  CA  THR A 386     9485   2818  10235    383   -966    658       C  
ATOM   2195  C   THR A 386      -6.396 -26.698 -16.416  1.00 56.09           C  
ANISOU 2195  C   THR A 386     8969   2673   9668    471   -970    454       C  
ATOM   2196  O   THR A 386      -6.001 -26.742 -17.580  1.00 56.08           O  
ANISOU 2196  O   THR A 386     8984   2663   9663    590  -1010    161       O  
ATOM   2197  CB  THR A 386      -8.010 -28.579 -16.357  1.00 60.93           C  
ANISOU 2197  CB  THR A 386     9706   2856  10590    144   -990    539       C  
ATOM   2198  OG1 THR A 386      -9.114 -27.671 -16.215  1.00 59.03           O  
ANISOU 2198  OG1 THR A 386     9344   2780  10306    -92   -947    608       O  
ATOM   2199  CG2 THR A 386      -8.362 -29.941 -15.764  1.00 64.59           C  
ANISOU 2199  CG2 THR A 386    10282   3033  11225     59   -983    706       C  
ATOM   2200  N   GLY A 387      -6.555 -25.552 -15.761  1.00 54.36           N  
ANISOU 2200  N   GLY A 387     8619   2795   9242    406   -871    594       N  
ATOM   2201  CA  GLY A 387      -6.231 -24.282 -16.376  1.00 52.20           C  
ANISOU 2201  CA  GLY A 387     8208   2881   8745    468   -812    420       C  
ATOM   2202  C   GLY A 387      -7.419 -23.619 -17.046  1.00 51.14           C  
ANISOU 2202  C   GLY A 387     7989   2873   8569    252   -788    306       C  
ATOM   2203  O   GLY A 387      -7.274 -22.592 -17.680  1.00 49.61           O  
ANISOU 2203  O   GLY A 387     7697   2949   8202    287   -747    156       O  
ATOM   2204  N   ARG A 388      -8.602 -24.212 -16.906  1.00 52.90           N  
ANISOU 2204  N   ARG A 388     8243   2893   8965     27   -818    386       N  
ATOM   2205  CA  ARG A 388      -9.807 -23.664 -17.534  1.00 51.35           C  
ANISOU 2205  CA  ARG A 388     7949   2794   8765   -183   -819    280       C  
ATOM   2206  C   ARG A 388     -10.264 -22.364 -16.890  1.00 50.51           C  
ANISOU 2206  C   ARG A 388     7686   3035   8470   -277   -700    419       C  
ATOM   2207  O   ARG A 388     -10.671 -21.436 -17.585  1.00 50.23           O  
ANISOU 2207  O   ARG A 388     7549   3216   8321   -322   -689    273       O  
ATOM   2208  CB  ARG A 388     -10.946 -24.695 -17.490  1.00 53.04           C  
ANISOU 2208  CB  ARG A 388     8213   2683   9256   -411   -887    339       C  
ATOM   2209  CG  ARG A 388     -10.679 -25.904 -18.351  1.00 55.29           C  
ANISOU 2209  CG  ARG A 388     8654   2613   9741   -342  -1029    136       C  
ATOM   2210  CD  ARG A 388     -11.947 -26.400 -19.050  1.00 60.02           C  
ANISOU 2210  CD  ARG A 388     9219   3109  10475   -569  -1094      7       C  
ATOM   2211  NE  ARG A 388     -11.750 -27.650 -19.779  1.00 63.19           N  
ANISOU 2211  NE  ARG A 388     9753   3266  10991   -507  -1179   -178       N  
ATOM   2212  CZ  ARG A 388     -12.677 -28.204 -20.558  1.00 68.36           C  
ANISOU 2212  CZ  ARG A 388    10403   3811  11759   -662  -1269   -340       C  
ATOM   2213  NH1 ARG A 388     -13.846 -27.598 -20.723  1.00 67.93           N  
ANISOU 2213  NH1 ARG A 388    10204   3883  11722   -878  -1286   -343       N  
ATOM   2214  NH2 ARG A 388     -12.438 -29.351 -21.179  1.00 70.26           N  
ANISOU 2214  NH2 ARG A 388    10775   3821  12099   -596  -1346   -504       N  
ATOM   2215  N   GLU A 389     -10.194 -22.286 -15.567  1.00 50.40           N  
ANISOU 2215  N   GLU A 389     7665   3072   8413   -296   -614    699       N  
ATOM   2216  CA  GLU A 389     -10.643 -21.077 -14.874  1.00 47.88           C  
ANISOU 2216  CA  GLU A 389     7212   3070   7912   -376   -496    826       C  
ATOM   2217  C   GLU A 389      -9.782 -19.871 -15.229  1.00 48.95           C  
ANISOU 2217  C   GLU A 389     7272   3516   7811   -212   -469    691       C  
ATOM   2218  O   GLU A 389     -10.284 -18.741 -15.390  1.00 45.15           O  
ANISOU 2218  O   GLU A 389     6668   3285   7203   -282   -412    646       O  
ATOM   2219  CB  GLU A 389     -10.639 -21.299 -13.364  1.00 52.68           C  
ANISOU 2219  CB  GLU A 389     7860   3666   8490   -402   -411   1146       C  
ATOM   2220  CG  GLU A 389     -11.103 -20.078 -12.580  1.00 57.40           C  
ANISOU 2220  CG  GLU A 389     8337   4585   8888   -472   -281   1268       C  
ATOM   2221  CD  GLU A 389     -11.273 -20.380 -11.107  1.00 64.24           C  
ANISOU 2221  CD  GLU A 389     9265   5430   9713   -516   -188   1587       C  
ATOM   2222  OE1 GLU A 389     -11.461 -21.573 -10.770  1.00 66.82           O  
ANISOU 2222  OE1 GLU A 389     9704   5466  10219   -574   -209   1736       O  
ATOM   2223  OE2 GLU A 389     -11.216 -19.427 -10.295  1.00 64.27           O  
ANISOU 2223  OE2 GLU A 389     9218   5701   9500   -489    -95   1686       O  
ATOM   2224  N   ARG A 390      -8.483 -20.103 -15.355  1.00 48.44           N  
ANISOU 2224  N   ARG A 390     7271   3428   7704      6   -509    628       N  
ATOM   2225  CA  ARG A 390      -7.581 -19.024 -15.740  1.00 49.02           C  
ANISOU 2225  CA  ARG A 390     7264   3775   7587    158   -480    500       C  
ATOM   2226  C   ARG A 390      -7.871 -18.561 -17.172  1.00 47.42           C  
ANISOU 2226  C   ARG A 390     7018   3644   7354    139   -500    239       C  
ATOM   2227  O   ARG A 390      -7.873 -17.365 -17.456  1.00 47.94           O  
ANISOU 2227  O   ARG A 390     6982   3971   7262    138   -447    177       O  
ATOM   2228  CB  ARG A 390      -6.116 -19.457 -15.599  1.00 50.04           C  
ANISOU 2228  CB  ARG A 390     7447   3852   7715    397   -518    488       C  
ATOM   2229  CG  ARG A 390      -5.200 -18.305 -15.173  1.00 51.50           C  
ANISOU 2229  CG  ARG A 390     7524   4335   7707    516   -469    509       C  
ATOM   2230  CD  ARG A 390      -3.901 -18.272 -15.948  1.00 48.04           C  
ANISOU 2230  CD  ARG A 390     7058   3935   7259    733   -487    332       C  
ATOM   2231  NE  ARG A 390      -3.208 -19.561 -16.031  1.00 49.94           N  
ANISOU 2231  NE  ARG A 390     7404   3909   7660    885   -560    315       N  
ATOM   2232  CZ  ARG A 390      -2.182 -19.755 -16.853  1.00 54.02           C  
ANISOU 2232  CZ  ARG A 390     7906   4413   8207   1079   -566    135       C  
ATOM   2233  NH1 ARG A 390      -1.778 -18.751 -17.618  1.00 55.98           N  
ANISOU 2233  NH1 ARG A 390     8043   4899   8329   1122   -494    -17       N  
ATOM   2234  NH2 ARG A 390      -1.555 -20.922 -16.916  1.00 53.63           N  
ANISOU 2234  NH2 ARG A 390     7950   4114   8313   1235   -631    111       N  
ATOM   2235  N   LYS A 391      -8.136 -19.518 -18.060  1.00 48.03           N  
ANISOU 2235  N   LYS A 391     7188   3481   7582    125   -585     89       N  
ATOM   2236  CA  LYS A 391      -8.497 -19.240 -19.451  1.00 45.79           C  
ANISOU 2236  CA  LYS A 391     6899   3235   7262    107   -629   -164       C  
ATOM   2237  C   LYS A 391      -9.795 -18.426 -19.554  1.00 46.38           C  
ANISOU 2237  C   LYS A 391     6867   3457   7300    -98   -616   -146       C  
ATOM   2238  O   LYS A 391      -9.924 -17.535 -20.397  1.00 49.67           O  
ANISOU 2238  O   LYS A 391     7229   4063   7582    -87   -612   -289       O  
ATOM   2239  CB  LYS A 391      -8.636 -20.568 -20.234  1.00 46.65           C  
ANISOU 2239  CB  LYS A 391     7151   3017   7558    117   -745   -323       C  
ATOM   2240  N   ALA A 392     -10.747 -18.711 -18.674  1.00 48.76           N  
ANISOU 2240  N   ALA A 392     7131   3674   7720   -277   -601     42       N  
ATOM   2241  CA  ALA A 392     -12.048 -18.040 -18.706  1.00 46.63           C  
ANISOU 2241  CA  ALA A 392     6737   3524   7457   -472   -586     67       C  
ATOM   2242  C   ALA A 392     -11.958 -16.606 -18.226  1.00 49.93           C  
ANISOU 2242  C   ALA A 392     7034   4268   7669   -447   -476    144       C  
ATOM   2243  O   ALA A 392     -12.902 -15.819 -18.393  1.00 49.57           O  
ANISOU 2243  O   ALA A 392     6874   4366   7596   -564   -460    133       O  
ATOM   2244  CB  ALA A 392     -13.064 -18.816 -17.862  1.00 47.58           C  
ANISOU 2244  CB  ALA A 392     6839   3454   7784   -671   -575    260       C  
ATOM   2245  N   MET A 393     -10.829 -16.260 -17.619  1.00 49.75           N  
ANISOU 2245  N   MET A 393     7030   4355   7516   -293   -412    217       N  
ATOM   2246  CA  MET A 393     -10.641 -14.913 -17.096  1.00 49.08           C  
ANISOU 2246  CA  MET A 393     6843   4558   7245   -264   -319    282       C  
ATOM   2247  C   MET A 393      -9.944 -14.022 -18.111  1.00 46.03           C  
ANISOU 2247  C   MET A 393     6432   4344   6715   -142   -323     98       C  
ATOM   2248  O   MET A 393      -9.713 -12.846 -17.846  1.00 46.01           O  
ANISOU 2248  O   MET A 393     6346   4565   6569   -113   -258    124       O  
ATOM   2249  CB  MET A 393      -9.834 -14.947 -15.803  1.00 49.34           C  
ANISOU 2249  CB  MET A 393     6904   4630   7214   -177   -261    468       C  
ATOM   2250  CG  MET A 393     -10.682 -15.114 -14.558  1.00 50.06           C  
ANISOU 2250  CG  MET A 393     6981   4703   7338   -312   -192    696       C  
ATOM   2251  SD  MET A 393      -9.659 -15.218 -13.065  1.00 61.42           S  
ANISOU 2251  SD  MET A 393     8491   6184   8662   -184   -155    908       S  
ATOM   2252  CE  MET A 393      -8.539 -13.860 -13.310  1.00 56.03           C  
ANISOU 2252  CE  MET A 393     7730   5776   7781    -26   -153    778       C  
ATOM   2253  N   ARG A 394      -9.630 -14.596 -19.270  1.00 45.45           N  
ANISOU 2253  N   ARG A 394     6436   4154   6681    -73   -396    -87       N  
ATOM   2254  CA  ARG A 394      -8.890 -13.911 -20.328  1.00 46.25           C  
ANISOU 2254  CA  ARG A 394     6536   4396   6641     56   -384   -258       C  
ATOM   2255  C   ARG A 394      -9.539 -12.606 -20.751  1.00 44.49           C  
ANISOU 2255  C   ARG A 394     6219   4391   6295    -16   -357   -291       C  
ATOM   2256  O   ARG A 394      -8.843 -11.646 -21.073  1.00 45.00           O  
ANISOU 2256  O   ARG A 394     6244   4636   6217     76   -298   -332       O  
ATOM   2257  CB  ARG A 394      -8.736 -14.824 -21.556  1.00 50.23           C  
ANISOU 2257  CB  ARG A 394     7160   4728   7199    121   -468   -463       C  
ATOM   2258  N   VAL A 395     -10.866 -12.554 -20.732  1.00 40.27           N  
ANISOU 2258  N   VAL A 395     5637   3833   5830   -179   -400   -266       N  
ATOM   2259  CA  VAL A 395     -11.555 -11.349 -21.171  1.00 40.25           C  
ANISOU 2259  CA  VAL A 395     5544   4020   5729   -235   -393   -299       C  
ATOM   2260  C   VAL A 395     -11.315 -10.150 -20.221  1.00 40.85           C  
ANISOU 2260  C   VAL A 395     5519   4301   5699   -222   -282   -165       C  
ATOM   2261  O   VAL A 395     -11.344  -8.994 -20.656  1.00 40.84           O  
ANISOU 2261  O   VAL A 395     5466   4472   5581   -201   -257   -206       O  
ATOM   2262  CB  VAL A 395     -13.068 -11.595 -21.322  1.00 42.20           C  
ANISOU 2262  CB  VAL A 395     5734   4194   6105   -410   -474   -302       C  
ATOM   2263  CG1 VAL A 395     -13.731 -11.744 -19.969  1.00 42.66           C  
ANISOU 2263  CG1 VAL A 395     5707   4229   6274   -531   -405   -102       C  
ATOM   2264  CG2 VAL A 395     -13.709 -10.471 -22.119  1.00 41.62           C  
ANISOU 2264  CG2 VAL A 395     5590   4290   5932   -432   -507   -382       C  
ATOM   2265  N   LEU A 396     -11.037 -10.420 -18.947  1.00 39.44           N  
ANISOU 2265  N   LEU A 396     5331   4100   5554   -226   -223     -9       N  
ATOM   2266  CA  LEU A 396     -10.949  -9.348 -17.959  1.00 39.37           C  
ANISOU 2266  CA  LEU A 396     5240   4272   5447   -225   -134    107       C  
ATOM   2267  C   LEU A 396      -9.794  -8.361 -18.234  1.00 39.04           C  
ANISOU 2267  C   LEU A 396     5182   4386   5265    -96    -98     48       C  
ATOM   2268  O   LEU A 396     -10.017  -7.158 -18.154  1.00 39.58           O  
ANISOU 2268  O   LEU A 396     5178   4613   5249   -113    -57     54       O  
ATOM   2269  CB  LEU A 396     -10.842  -9.925 -16.547  1.00 37.39           C  
ANISOU 2269  CB  LEU A 396     5011   3962   5232   -242    -90    284       C  
ATOM   2270  CG  LEU A 396     -12.074 -10.718 -16.106  1.00 42.60           C  
ANISOU 2270  CG  LEU A 396     5661   4491   6034   -396    -87    384       C  
ATOM   2271  CD1 LEU A 396     -11.884 -11.382 -14.738  1.00 40.91           C  
ANISOU 2271  CD1 LEU A 396     5501   4206   5836   -401    -33    581       C  
ATOM   2272  CD2 LEU A 396     -13.325  -9.836 -16.134  1.00 43.08           C  
ANISOU 2272  CD2 LEU A 396     5597   4676   6094   -511    -47    388       C  
ATOM   2273  N   PRO A 397      -8.577  -8.853 -18.571  1.00 41.04           N  
ANISOU 2273  N   PRO A 397     5493   4588   5511     31   -109     -9       N  
ATOM   2274  CA  PRO A 397      -7.494  -7.917 -18.912  1.00 40.26           C  
ANISOU 2274  CA  PRO A 397     5354   4636   5307    137    -63    -62       C  
ATOM   2275  C   PRO A 397      -7.804  -7.064 -20.128  1.00 40.02           C  
ANISOU 2275  C   PRO A 397     5308   4701   5198    126    -54   -174       C  
ATOM   2276  O   PRO A 397      -7.358  -5.915 -20.209  1.00 38.38           O  
ANISOU 2276  O   PRO A 397     5040   4638   4904    154     -1   -173       O  
ATOM   2277  CB  PRO A 397      -6.307  -8.836 -19.224  1.00 39.57           C  
ANISOU 2277  CB  PRO A 397     5323   4448   5263    272    -76   -118       C  
ATOM   2278  CG  PRO A 397      -6.590 -10.083 -18.508  1.00 40.51           C  
ANISOU 2278  CG  PRO A 397     5510   4386   5497    248   -126    -37       C  
ATOM   2279  CD  PRO A 397      -8.070 -10.235 -18.451  1.00 41.96           C  
ANISOU 2279  CD  PRO A 397     5700   4513   5730     88   -152     -2       C  
ATOM   2280  N   VAL A 398      -8.547  -7.619 -21.074  1.00 38.65           N  
ANISOU 2280  N   VAL A 398     5196   4437   5054     86   -115   -267       N  
ATOM   2281  CA  VAL A 398      -8.918  -6.834 -22.240  1.00 38.87           C  
ANISOU 2281  CA  VAL A 398     5228   4556   4986     82   -125   -362       C  
ATOM   2282  C   VAL A 398      -9.880  -5.703 -21.848  1.00 39.87           C  
ANISOU 2282  C   VAL A 398     5262   4798   5087    -14   -118   -291       C  
ATOM   2283  O   VAL A 398      -9.690  -4.565 -22.272  1.00 38.40           O  
ANISOU 2283  O   VAL A 398     5047   4740   4803     13    -80   -302       O  
ATOM   2284  CB  VAL A 398      -9.540  -7.707 -23.336  1.00 39.71           C  
ANISOU 2284  CB  VAL A 398     5431   4540   5118     64   -223   -494       C  
ATOM   2285  CG1 VAL A 398      -9.786  -6.879 -24.587  1.00 38.36           C  
ANISOU 2285  CG1 VAL A 398     5288   4477   4809     86   -241   -588       C  
ATOM   2286  CG2 VAL A 398      -8.610  -8.889 -23.656  1.00 39.26           C  
ANISOU 2286  CG2 VAL A 398     5473   4345   5099    172   -227   -577       C  
ATOM   2287  N   VAL A 399     -10.901  -6.013 -21.050  1.00 36.50           N  
ANISOU 2287  N   VAL A 399     4790   4321   4758   -121   -145   -213       N  
ATOM   2288  CA  VAL A 399     -11.799  -4.979 -20.533  1.00 36.23           C  
ANISOU 2288  CA  VAL A 399     4655   4396   4714   -195   -120   -144       C  
ATOM   2289  C   VAL A 399     -11.036  -3.892 -19.750  1.00 37.17           C  
ANISOU 2289  C   VAL A 399     4727   4648   4750   -142    -32    -78       C  
ATOM   2290  O   VAL A 399     -11.266  -2.701 -19.959  1.00 34.14           O  
ANISOU 2290  O   VAL A 399     4295   4372   4305   -141    -12    -84       O  
ATOM   2291  CB  VAL A 399     -12.890  -5.582 -19.631  1.00 37.35           C  
ANISOU 2291  CB  VAL A 399     4743   4468   4982   -312   -125    -54       C  
ATOM   2292  CG1 VAL A 399     -13.746  -4.480 -18.996  1.00 34.45           C  
ANISOU 2292  CG1 VAL A 399     4261   4227   4602   -364    -72     14       C  
ATOM   2293  CG2 VAL A 399     -13.773  -6.522 -20.451  1.00 38.92           C  
ANISOU 2293  CG2 VAL A 399     4963   4532   5294   -390   -233   -130       C  
ATOM   2294  N   VAL A 400     -10.145  -4.303 -18.851  1.00 36.78           N  
ANISOU 2294  N   VAL A 400     4695   4577   4704    -96      6    -17       N  
ATOM   2295  CA  VAL A 400      -9.342  -3.355 -18.082  1.00 35.42           C  
ANISOU 2295  CA  VAL A 400     4479   4517   4460    -47     61     29       C  
ATOM   2296  C   VAL A 400      -8.443  -2.548 -19.018  1.00 33.96           C  
ANISOU 2296  C   VAL A 400     4289   4404   4211     24     81    -46       C  
ATOM   2297  O   VAL A 400      -8.372  -1.335 -18.898  1.00 31.99           O  
ANISOU 2297  O   VAL A 400     3988   4253   3912     21    112    -38       O  
ATOM   2298  CB  VAL A 400      -8.492  -4.069 -17.002  1.00 36.82           C  
ANISOU 2298  CB  VAL A 400     4683   4652   4653      2     66    104       C  
ATOM   2299  CG1 VAL A 400      -7.519  -3.105 -16.334  1.00 35.15           C  
ANISOU 2299  CG1 VAL A 400     4427   4556   4374     60     90    122       C  
ATOM   2300  CG2 VAL A 400      -9.405  -4.735 -15.973  1.00 37.16           C  
ANISOU 2300  CG2 VAL A 400     4742   4638   4741    -75     72    212       C  
ATOM   2301  N   GLY A 401      -7.785  -3.214 -19.963  1.00 37.75           N  
ANISOU 2301  N   GLY A 401     4824   4828   4693     88     71   -120       N  
ATOM   2302  CA  GLY A 401      -6.924  -2.533 -20.916  1.00 35.73           C  
ANISOU 2302  CA  GLY A 401     4564   4642   4370    154    119   -179       C  
ATOM   2303  C   GLY A 401      -7.631  -1.457 -21.734  1.00 36.12           C  
ANISOU 2303  C   GLY A 401     4610   4765   4350    115    122   -201       C  
ATOM   2304  O   GLY A 401      -7.117  -0.338 -21.879  1.00 35.97           O  
ANISOU 2304  O   GLY A 401     4550   4831   4285    131    176   -184       O  
ATOM   2305  N   ALA A 402      -8.808  -1.789 -22.265  1.00 34.34           N  
ANISOU 2305  N   ALA A 402     4425   4496   4128     64     53   -235       N  
ATOM   2306  CA  ALA A 402      -9.605  -0.837 -23.030  1.00 35.53           C  
ANISOU 2306  CA  ALA A 402     4575   4707   4218     36     26   -249       C  
ATOM   2307  C   ALA A 402     -10.000   0.359 -22.163  1.00 36.76           C  
ANISOU 2307  C   ALA A 402     4641   4937   4391     -6     54   -173       C  
ATOM   2308  O   ALA A 402     -10.011   1.501 -22.632  1.00 33.88           O  
ANISOU 2308  O   ALA A 402     4267   4636   3971      6     72   -163       O  
ATOM   2309  CB  ALA A 402     -10.858  -1.508 -23.598  1.00 35.16           C  
ANISOU 2309  CB  ALA A 402     4562   4594   4202    -18    -83   -302       C  
ATOM   2310  N   PHE A 403     -10.348   0.091 -20.909  1.00 37.53           N  
ANISOU 2310  N   PHE A 403     4684   5017   4557    -49     59   -118       N  
ATOM   2311  CA  PHE A 403     -10.712   1.154 -19.991  1.00 34.48           C  
ANISOU 2311  CA  PHE A 403     4226   4699   4177    -75     92    -63       C  
ATOM   2312  C   PHE A 403      -9.538   2.119 -19.756  1.00 34.87           C  
ANISOU 2312  C   PHE A 403     4259   4806   4183    -28    146    -53       C  
ATOM   2313  O   PHE A 403      -9.707   3.344 -19.794  1.00 32.88           O  
ANISOU 2313  O   PHE A 403     3977   4601   3914    -31    161    -46       O  
ATOM   2314  CB  PHE A 403     -11.185   0.589 -18.655  1.00 34.95           C  
ANISOU 2314  CB  PHE A 403     4251   4739   4288   -118    107     -3       C  
ATOM   2315  CG  PHE A 403     -11.908   1.592 -17.832  1.00 35.73           C  
ANISOU 2315  CG  PHE A 403     4284   4907   4386   -141    142     31       C  
ATOM   2316  CD1 PHE A 403     -11.214   2.414 -16.961  1.00 35.59           C  
ANISOU 2316  CD1 PHE A 403     4255   4947   4321   -107    183     47       C  
ATOM   2317  CD2 PHE A 403     -13.276   1.765 -17.988  1.00 37.84           C  
ANISOU 2317  CD2 PHE A 403     4492   5180   4704   -188    126     34       C  
ATOM   2318  CE1 PHE A 403     -11.878   3.374 -16.228  1.00 39.60           C  
ANISOU 2318  CE1 PHE A 403     4715   5511   4819   -113    217     56       C  
ATOM   2319  CE2 PHE A 403     -13.962   2.713 -17.258  1.00 39.25           C  
ANISOU 2319  CE2 PHE A 403     4602   5423   4887   -191    170     54       C  
ATOM   2320  CZ  PHE A 403     -13.260   3.533 -16.384  1.00 40.13           C  
ANISOU 2320  CZ  PHE A 403     4724   5586   4936   -148    220     61       C  
ATOM   2321  N   LEU A 404      -8.355   1.571 -19.512  1.00 34.18           N  
ANISOU 2321  N   LEU A 404     4184   4704   4099     14    169    -55       N  
ATOM   2322  CA  LEU A 404      -7.168   2.410 -19.326  1.00 33.53           C  
ANISOU 2322  CA  LEU A 404     4061   4671   4007     47    210    -50       C  
ATOM   2323  C   LEU A 404      -6.850   3.205 -20.577  1.00 33.27           C  
ANISOU 2323  C   LEU A 404     4040   4664   3937     62    248    -71       C  
ATOM   2324  O   LEU A 404      -6.479   4.382 -20.493  1.00 34.49           O  
ANISOU 2324  O   LEU A 404     4154   4854   4097     51    278    -53       O  
ATOM   2325  CB  LEU A 404      -5.958   1.558 -18.927  1.00 33.72           C  
ANISOU 2325  CB  LEU A 404     4076   4674   4061    101    214    -51       C  
ATOM   2326  CG  LEU A 404      -6.144   0.845 -17.587  1.00 35.49           C  
ANISOU 2326  CG  LEU A 404     4306   4875   4305     95    174     -5       C  
ATOM   2327  CD1 LEU A 404      -4.919  -0.020 -17.255  1.00 36.88           C  
ANISOU 2327  CD1 LEU A 404     4475   5021   4518    167    158      1       C  
ATOM   2328  CD2 LEU A 404      -6.444   1.815 -16.472  1.00 37.69           C  
ANISOU 2328  CD2 LEU A 404     4550   5213   4557     64    169     24       C  
ATOM   2329  N   LEU A 405      -6.983   2.576 -21.740  1.00 32.55           N  
ANISOU 2329  N   LEU A 405     4014   4548   3804     88    248   -108       N  
ATOM   2330  CA  LEU A 405      -6.708   3.261 -22.999  1.00 35.70           C  
ANISOU 2330  CA  LEU A 405     4451   4979   4132    112    294   -115       C  
ATOM   2331  C   LEU A 405      -7.651   4.428 -23.213  1.00 33.86           C  
ANISOU 2331  C   LEU A 405     4222   4768   3877     74    266    -82       C  
ATOM   2332  O   LEU A 405      -7.228   5.517 -23.630  1.00 34.07           O  
ANISOU 2332  O   LEU A 405     4243   4821   3883     75    317    -44       O  
ATOM   2333  CB  LEU A 405      -6.812   2.301 -24.186  1.00 38.54           C  
ANISOU 2333  CB  LEU A 405     4909   5314   4421    157    284   -178       C  
ATOM   2334  CG  LEU A 405      -5.595   1.405 -24.437  1.00 44.26           C  
ANISOU 2334  CG  LEU A 405     5643   6025   5150    230    350   -220       C  
ATOM   2335  CD1 LEU A 405      -5.881   0.428 -25.576  1.00 43.52           C  
ANISOU 2335  CD1 LEU A 405     5670   5892   4974    281    324   -308       C  
ATOM   2336  CD2 LEU A 405      -4.363   2.258 -24.742  1.00 42.45           C  
ANISOU 2336  CD2 LEU A 405     5356   5861   4912    259    471   -184       C  
ATOM   2337  N   CYS A 406      -8.919   4.192 -22.910  1.00 31.97           N  
ANISOU 2337  N   CYS A 406     3981   4508   3658     41    187    -90       N  
ATOM   2338  CA  CYS A 406      -9.983   5.171 -23.140  1.00 33.40           C  
ANISOU 2338  CA  CYS A 406     4153   4703   3833     22    142    -67       C  
ATOM   2339  C   CYS A 406     -10.041   6.318 -22.145  1.00 31.69           C  
ANISOU 2339  C   CYS A 406     3866   4501   3673      2    166    -30       C  
ATOM   2340  O   CYS A 406     -10.451   7.422 -22.504  1.00 32.78           O  
ANISOU 2340  O   CYS A 406     4007   4641   3806      9    155     -3       O  
ATOM   2341  CB  CYS A 406     -11.330   4.466 -23.147  1.00 33.51           C  
ANISOU 2341  CB  CYS A 406     4160   4694   3879     -8     50    -95       C  
ATOM   2342  SG  CYS A 406     -11.583   3.559 -24.662  1.00 37.55           S  
ANISOU 2342  SG  CYS A 406     4779   5181   4307     18    -26   -160       S  
ATOM   2343  N   TRP A 407      -9.658   6.062 -20.898  1.00 30.02           N  
ANISOU 2343  N   TRP A 407     3605   4293   3510    -13    189    -31       N  
ATOM   2344  CA  TRP A 407      -9.797   7.055 -19.842  1.00 29.98           C  
ANISOU 2344  CA  TRP A 407     3548   4300   3543    -24    201    -20       C  
ATOM   2345  C   TRP A 407      -8.498   7.704 -19.345  1.00 30.34           C  
ANISOU 2345  C   TRP A 407     3570   4350   3608    -22    238    -20       C  
ATOM   2346  O   TRP A 407      -8.547   8.735 -18.689  1.00 31.19           O  
ANISOU 2346  O   TRP A 407     3651   4454   3745    -29    235    -27       O  
ATOM   2347  CB  TRP A 407     -10.524   6.425 -18.655  1.00 28.66           C  
ANISOU 2347  CB  TRP A 407     3348   4144   3397    -41    192    -23       C  
ATOM   2348  CG  TRP A 407     -11.988   6.320 -18.923  1.00 31.54           C  
ANISOU 2348  CG  TRP A 407     3688   4507   3787    -57    159    -21       C  
ATOM   2349  CD1 TRP A 407     -12.695   5.195 -19.262  1.00 33.99           C  
ANISOU 2349  CD1 TRP A 407     3999   4797   4120    -85    124    -22       C  
ATOM   2350  CD2 TRP A 407     -12.923   7.399 -18.912  1.00 32.19           C  
ANISOU 2350  CD2 TRP A 407     3729   4601   3899    -43    149    -23       C  
ATOM   2351  NE1 TRP A 407     -14.037   5.514 -19.441  1.00 34.04           N  
ANISOU 2351  NE1 TRP A 407     3947   4813   4175    -98     89    -23       N  
ATOM   2352  CE2 TRP A 407     -14.193   6.864 -19.232  1.00 32.30           C  
ANISOU 2352  CE2 TRP A 407     3700   4616   3956    -63    107    -22       C  
ATOM   2353  CE3 TRP A 407     -12.815   8.774 -18.644  1.00 29.48           C  
ANISOU 2353  CE3 TRP A 407     3376   4256   3567    -14    165    -30       C  
ATOM   2354  CZ2 TRP A 407     -15.335   7.649 -19.296  1.00 33.28           C  
ANISOU 2354  CZ2 TRP A 407     3757   4753   4133    -43     83    -24       C  
ATOM   2355  CZ3 TRP A 407     -13.951   9.550 -18.707  1.00 30.51           C  
ANISOU 2355  CZ3 TRP A 407     3463   4387   3744     12    145    -34       C  
ATOM   2356  CH2 TRP A 407     -15.200   8.985 -19.035  1.00 33.09           C  
ANISOU 2356  CH2 TRP A 407     3732   4728   4112      3    105    -29       C  
ATOM   2357  N   THR A 408      -7.349   7.110 -19.632  1.00 29.53           N  
ANISOU 2357  N   THR A 408     3467   4250   3503    -10    265    -20       N  
ATOM   2358  CA  THR A 408      -6.104   7.711 -19.151  1.00 29.46           C  
ANISOU 2358  CA  THR A 408     3404   4247   3542    -17    287    -22       C  
ATOM   2359  C   THR A 408      -5.900   9.120 -19.760  1.00 30.64           C  
ANISOU 2359  C   THR A 408     3546   4372   3722    -41    318      2       C  
ATOM   2360  O   THR A 408      -5.633  10.044 -19.021  1.00 31.13           O  
ANISOU 2360  O   THR A 408     3571   4416   3842    -66    299    -13       O  
ATOM   2361  CB  THR A 408      -4.893   6.797 -19.404  1.00 29.84           C  
ANISOU 2361  CB  THR A 408     3426   4306   3605     11    317    -26       C  
ATOM   2362  OG1 THR A 408      -5.057   5.602 -18.641  1.00 30.87           O  
ANISOU 2362  OG1 THR A 408     3571   4436   3724     35    274    -38       O  
ATOM   2363  CG2 THR A 408      -3.591   7.465 -18.951  1.00 31.74           C  
ANISOU 2363  CG2 THR A 408     3579   4556   3926     -3    328    -29       C  
ATOM   2364  N   PRO A 409      -6.080   9.298 -21.086  1.00 28.33           N  
ANISOU 2364  N   PRO A 409     3304   4073   3388    -33    358     39       N  
ATOM   2365  CA  PRO A 409      -5.944  10.683 -21.577  1.00 29.98           C  
ANISOU 2365  CA  PRO A 409     3519   4243   3631    -59    388     86       C  
ATOM   2366  C   PRO A 409      -6.876  11.668 -20.866  1.00 32.13           C  
ANISOU 2366  C   PRO A 409     3791   4474   3944    -67    328     71       C  
ATOM   2367  O   PRO A 409      -6.441  12.762 -20.542  1.00 31.82           O  
ANISOU 2367  O   PRO A 409     3725   4382   3982    -98    333     77       O  
ATOM   2368  CB  PRO A 409      -6.319  10.582 -23.061  1.00 29.47           C  
ANISOU 2368  CB  PRO A 409     3541   4186   3470    -31    421    135       C  
ATOM   2369  CG  PRO A 409      -6.012   9.068 -23.418  1.00 29.20           C  
ANISOU 2369  CG  PRO A 409     3527   4198   3370      6    438     95       C  
ATOM   2370  CD  PRO A 409      -6.420   8.349 -22.170  1.00 28.46           C  
ANISOU 2370  CD  PRO A 409     3389   4106   3318      2    369     40       C  
ATOM   2371  N   PHE A 410      -8.126  11.277 -20.634  1.00 29.34           N  
ANISOU 2371  N   PHE A 410     3459   4137   3552    -39    277     48       N  
ATOM   2372  CA  PHE A 410      -9.093  12.126 -19.962  1.00 29.36           C  
ANISOU 2372  CA  PHE A 410     3450   4110   3593    -27    236     24       C  
ATOM   2373  C   PHE A 410      -8.585  12.562 -18.598  1.00 29.96           C  
ANISOU 2373  C   PHE A 410     3485   4177   3720    -42    229    -33       C  
ATOM   2374  O   PHE A 410      -8.643  13.748 -18.243  1.00 30.17           O  
ANISOU 2374  O   PHE A 410     3511   4145   3807    -44    215    -54       O  
ATOM   2375  CB  PHE A 410     -10.435  11.397 -19.803  1.00 28.97           C  
ANISOU 2375  CB  PHE A 410     3395   4099   3514     -1    199      6       C  
ATOM   2376  CG  PHE A 410     -11.499  12.229 -19.144  1.00 30.32           C  
ANISOU 2376  CG  PHE A 410     3537   4254   3731     29    176    -21       C  
ATOM   2377  CD1 PHE A 410     -11.639  12.248 -17.755  1.00 28.05           C  
ANISOU 2377  CD1 PHE A 410     3215   3990   3455     34    192    -77       C  
ATOM   2378  CD2 PHE A 410     -12.349  13.000 -19.907  1.00 30.57           C  
ANISOU 2378  CD2 PHE A 410     3579   4248   3786     65    140      7       C  
ATOM   2379  CE1 PHE A 410     -12.633  13.047 -17.139  1.00 29.70           C  
ANISOU 2379  CE1 PHE A 410     3396   4189   3701     79    192   -115       C  
ATOM   2380  CE2 PHE A 410     -13.357  13.771 -19.302  1.00 31.62           C  
ANISOU 2380  CE2 PHE A 410     3671   4363   3979    111    124    -25       C  
ATOM   2381  CZ  PHE A 410     -13.496  13.793 -17.923  1.00 30.27           C  
ANISOU 2381  CZ  PHE A 410     3461   4219   3822    119    160    -92       C  
ATOM   2382  N   PHE A 411      -8.113  11.607 -17.805  1.00 30.10           N  
ANISOU 2382  N   PHE A 411     3480   4247   3712    -47    226    -63       N  
ATOM   2383  CA  PHE A 411      -7.735  11.983 -16.451  1.00 31.72           C  
ANISOU 2383  CA  PHE A 411     3664   4456   3933    -50    197   -125       C  
ATOM   2384  C   PHE A 411      -6.399  12.715 -16.404  1.00 33.41           C  
ANISOU 2384  C   PHE A 411     3843   4627   4225    -90    184   -139       C  
ATOM   2385  O   PHE A 411      -6.202  13.559 -15.541  1.00 33.26           O  
ANISOU 2385  O   PHE A 411     3817   4575   4244    -98    140   -203       O  
ATOM   2386  CB  PHE A 411      -7.717  10.774 -15.526  1.00 27.78           C  
ANISOU 2386  CB  PHE A 411     3164   4023   3368    -34    186   -138       C  
ATOM   2387  CG  PHE A 411      -9.098  10.353 -15.113  1.00 28.85           C  
ANISOU 2387  CG  PHE A 411     3316   4191   3454    -10    204   -135       C  
ATOM   2388  CD1 PHE A 411      -9.839  11.149 -14.235  1.00 29.49           C  
ANISOU 2388  CD1 PHE A 411     3401   4279   3524     18    209   -185       C  
ATOM   2389  CD2 PHE A 411      -9.681   9.234 -15.660  1.00 28.39           C  
ANISOU 2389  CD2 PHE A 411     3260   4150   3376    -15    219    -90       C  
ATOM   2390  CE1 PHE A 411     -11.120  10.809 -13.881  1.00 29.71           C  
ANISOU 2390  CE1 PHE A 411     3418   4345   3525     40    248   -176       C  
ATOM   2391  CE2 PHE A 411     -10.982   8.868 -15.317  1.00 29.02           C  
ANISOU 2391  CE2 PHE A 411     3328   4255   3443     -9    241    -81       C  
ATOM   2392  CZ  PHE A 411     -11.713   9.658 -14.419  1.00 29.92           C  
ANISOU 2392  CZ  PHE A 411     3428   4391   3551     19    265   -117       C  
ATOM   2393  N   VAL A 412      -5.493  12.407 -17.323  1.00 30.95           N  
ANISOU 2393  N   VAL A 412     3503   4314   3942   -115    223    -88       N  
ATOM   2394  CA  VAL A 412      -4.250  13.179 -17.371  1.00 31.51           C  
ANISOU 2394  CA  VAL A 412     3511   4339   4120   -168    226    -89       C  
ATOM   2395  C   VAL A 412      -4.581  14.631 -17.746  1.00 33.96           C  
ANISOU 2395  C   VAL A 412     3849   4552   4504   -198    231    -72       C  
ATOM   2396  O   VAL A 412      -4.124  15.563 -17.080  1.00 35.36           O  
ANISOU 2396  O   VAL A 412     3998   4664   4775   -237    183   -125       O  
ATOM   2397  CB  VAL A 412      -3.241  12.569 -18.338  1.00 30.41           C  
ANISOU 2397  CB  VAL A 412     3323   4227   4002   -181    299    -30       C  
ATOM   2398  CG1 VAL A 412      -2.037  13.527 -18.558  1.00 31.94           C  
ANISOU 2398  CG1 VAL A 412     3430   4366   4339   -254    327     -9       C  
ATOM   2399  CG2 VAL A 412      -2.780  11.197 -17.775  1.00 29.53           C  
ANISOU 2399  CG2 VAL A 412     3180   4190   3851   -141    272    -59       C  
ATOM   2400  N   VAL A 413      -5.407  14.827 -18.773  1.00 29.88           N  
ANISOU 2400  N   VAL A 413     3393   4014   3945   -176    273     -5       N  
ATOM   2401  CA  VAL A 413      -5.797  16.191 -19.151  1.00 32.31           C  
ANISOU 2401  CA  VAL A 413     3740   4213   4322   -190    271     27       C  
ATOM   2402  C   VAL A 413      -6.487  16.911 -17.996  1.00 33.93           C  
ANISOU 2402  C   VAL A 413     3959   4371   4561   -162    197    -71       C  
ATOM   2403  O   VAL A 413      -6.142  18.067 -17.667  1.00 34.62           O  
ANISOU 2403  O   VAL A 413     4044   4350   4759   -197    167   -103       O  
ATOM   2404  CB  VAL A 413      -6.715  16.211 -20.398  1.00 32.95           C  
ANISOU 2404  CB  VAL A 413     3896   4291   4331   -147    300    116       C  
ATOM   2405  CG1 VAL A 413      -7.382  17.564 -20.560  1.00 35.55           C  
ANISOU 2405  CG1 VAL A 413     4275   4503   4729   -132    270    141       C  
ATOM   2406  CG2 VAL A 413      -5.908  15.847 -21.653  1.00 32.15           C  
ANISOU 2406  CG2 VAL A 413     3808   4217   4191   -173    388    214       C  
ATOM   2407  N   HIS A 414      -7.419  16.235 -17.331  1.00 32.71           N  
ANISOU 2407  N   HIS A 414     3817   4293   4318   -102    175   -125       N  
ATOM   2408  CA  HIS A 414      -8.207  16.956 -16.347  1.00 34.47           C  
ANISOU 2408  CA  HIS A 414     4060   4480   4555    -55    134   -215       C  
ATOM   2409  C   HIS A 414      -7.437  17.237 -15.070  1.00 33.80           C  
ANISOU 2409  C   HIS A 414     3962   4388   4493    -77     81   -324       C  
ATOM   2410  O   HIS A 414      -7.594  18.301 -14.483  1.00 33.29           O  
ANISOU 2410  O   HIS A 414     3924   4238   4487    -63     40   -405       O  
ATOM   2411  CB  HIS A 414      -9.507  16.219 -16.056  1.00 30.54           C  
ANISOU 2411  CB  HIS A 414     3567   4069   3967     13    149   -228       C  
ATOM   2412  CG  HIS A 414     -10.564  16.504 -17.074  1.00 33.28           C  
ANISOU 2412  CG  HIS A 414     3928   4388   4329     54    155   -163       C  
ATOM   2413  ND1 HIS A 414     -10.615  15.870 -18.292  1.00 32.29           N  
ANISOU 2413  ND1 HIS A 414     3812   4290   4165     40    168    -71       N  
ATOM   2414  CD2 HIS A 414     -11.556  17.430 -17.086  1.00 33.13           C  
ANISOU 2414  CD2 HIS A 414     3918   4307   4362    117    138   -181       C  
ATOM   2415  CE1 HIS A 414     -11.619  16.363 -19.002  1.00 34.23           C  
ANISOU 2415  CE1 HIS A 414     4075   4501   4429     90    143    -32       C  
ATOM   2416  NE2 HIS A 414     -12.214  17.298 -18.284  1.00 33.35           N  
ANISOU 2416  NE2 HIS A 414     3955   4335   4383    140    126    -92       N  
ATOM   2417  N   ILE A 415      -6.594  16.311 -14.635  1.00 32.08           N  
ANISOU 2417  N   ILE A 415     3708   4251   4231   -103     67   -333       N  
ATOM   2418  CA  ILE A 415      -5.862  16.594 -13.413  1.00 33.66           C  
ANISOU 2418  CA  ILE A 415     3900   4449   4441   -116    -13   -441       C  
ATOM   2419  C   ILE A 415      -4.779  17.655 -13.695  1.00 34.24           C  
ANISOU 2419  C   ILE A 415     3930   4403   4678   -199    -55   -455       C  
ATOM   2420  O   ILE A 415      -4.493  18.504 -12.844  1.00 34.23           O  
ANISOU 2420  O   ILE A 415     3942   4333   4730   -212   -139   -567       O  
ATOM   2421  CB  ILE A 415      -5.251  15.302 -12.783  1.00 32.01           C  
ANISOU 2421  CB  ILE A 415     3666   4356   4141   -108    -39   -441       C  
ATOM   2422  CG1 ILE A 415      -5.070  15.508 -11.271  1.00 34.57           C  
ANISOU 2422  CG1 ILE A 415     4028   4709   4397    -78   -131   -564       C  
ATOM   2423  CG2 ILE A 415      -3.944  14.900 -13.457  1.00 30.57           C  
ANISOU 2423  CG2 ILE A 415     3396   4173   4044   -169    -38   -382       C  
ATOM   2424  CD1 ILE A 415      -4.439  14.322 -10.553  1.00 36.91           C  
ANISOU 2424  CD1 ILE A 415     4315   5111   4599    -58   -180   -556       C  
ATOM   2425  N   THR A 416      -4.219  17.645 -14.901  1.00 35.10           N  
ANISOU 2425  N   THR A 416     3990   4479   4866   -256      8   -343       N  
ATOM   2426  CA  THR A 416      -3.218  18.647 -15.267  1.00 35.56           C  
ANISOU 2426  CA  THR A 416     3993   4417   5100   -351     -5   -328       C  
ATOM   2427  C   THR A 416      -3.824  20.059 -15.195  1.00 36.95           C  
ANISOU 2427  C   THR A 416     4237   4439   5364   -352    -35   -368       C  
ATOM   2428  O   THR A 416      -3.272  20.954 -14.543  1.00 37.83           O  
ANISOU 2428  O   THR A 416     4333   4444   5596   -404   -119   -461       O  
ATOM   2429  CB  THR A 416      -2.659  18.397 -16.665  1.00 33.45           C  
ANISOU 2429  CB  THR A 416     3679   4153   4878   -400    107   -180       C  
ATOM   2430  OG1 THR A 416      -1.878  17.187 -16.656  1.00 35.37           O  
ANISOU 2430  OG1 THR A 416     3844   4517   5078   -398    127   -167       O  
ATOM   2431  CG2 THR A 416      -1.761  19.542 -17.073  1.00 37.64           C  
ANISOU 2431  CG2 THR A 416     4153   4545   5604   -509    120   -140       C  
ATOM   2432  N   GLN A 417      -4.962  20.241 -15.854  1.00 36.30           N  
ANISOU 2432  N   GLN A 417     4227   4336   5230   -290     20   -304       N  
ATOM   2433  CA  GLN A 417      -5.698  21.505 -15.802  1.00 38.26           C  
ANISOU 2433  CA  GLN A 417     4545   4436   5556   -258     -9   -338       C  
ATOM   2434  C   GLN A 417      -5.966  21.966 -14.380  1.00 38.67           C  
ANISOU 2434  C   GLN A 417     4631   4462   5601   -212   -100   -521       C  
ATOM   2435  O   GLN A 417      -5.795  23.147 -14.035  1.00 38.15           O  
ANISOU 2435  O   GLN A 417     4594   4235   5665   -235   -163   -600       O  
ATOM   2436  CB  GLN A 417      -7.026  21.364 -16.522  1.00 39.67           C  
ANISOU 2436  CB  GLN A 417     4781   4641   5651   -166     40   -262       C  
ATOM   2437  CG  GLN A 417      -6.945  21.342 -18.028  1.00 43.08           C  
ANISOU 2437  CG  GLN A 417     5227   5051   6090   -194    111    -87       C  
ATOM   2438  CD  GLN A 417      -8.343  21.294 -18.643  1.00 47.11           C  
ANISOU 2438  CD  GLN A 417     5794   5581   6524    -92    116    -34       C  
ATOM   2439  OE1 GLN A 417      -9.229  20.571 -18.168  1.00 50.34           O  
ANISOU 2439  OE1 GLN A 417     6191   6100   6837    -18    105    -94       O  
ATOM   2440  NE2 GLN A 417      -8.568  22.141 -19.645  1.00 42.37           N  
ANISOU 2440  NE2 GLN A 417     5252   4863   5982    -86    126     81       N  
ATOM   2441  N   ALA A 418      -6.390  21.025 -13.549  1.00 36.63           N  
ANISOU 2441  N   ALA A 418     4378   4356   5184   -144   -105   -589       N  
ATOM   2442  CA  ALA A 418      -6.769  21.345 -12.177  1.00 37.04           C  
ANISOU 2442  CA  ALA A 418     4483   4416   5174    -77   -169   -760       C  
ATOM   2443  C   ALA A 418      -5.540  21.691 -11.345  1.00 36.29           C  
ANISOU 2443  C   ALA A 418     4370   4278   5142   -148   -285   -875       C  
ATOM   2444  O   ALA A 418      -5.588  22.597 -10.508  1.00 38.28           O  
ANISOU 2444  O   ALA A 418     4680   4437   5427   -125   -367  -1028       O  
ATOM   2445  CB  ALA A 418      -7.543  20.167 -11.531  1.00 34.83           C  
ANISOU 2445  CB  ALA A 418     4217   4320   4695      9   -123   -773       C  
ATOM   2446  N   LEU A 419      -4.439  20.994 -11.576  1.00 36.44           N  
ANISOU 2446  N   LEU A 419     4303   4359   5185   -230   -302   -814       N  
ATOM   2447  CA  LEU A 419      -3.206  21.256 -10.825  1.00 36.95           C  
ANISOU 2447  CA  LEU A 419     4318   4392   5329   -303   -433   -919       C  
ATOM   2448  C   LEU A 419      -2.507  22.516 -11.326  1.00 38.61           C  
ANISOU 2448  C   LEU A 419     4485   4400   5786   -416   -473   -921       C  
ATOM   2449  O   LEU A 419      -1.856  23.224 -10.549  1.00 40.71           O  
ANISOU 2449  O   LEU A 419     4744   4574   6149   -466   -610  -1062       O  
ATOM   2450  CB  LEU A 419      -2.243  20.076 -10.930  1.00 38.99           C  
ANISOU 2450  CB  LEU A 419     4475   4781   5558   -341   -438   -847       C  
ATOM   2451  CG  LEU A 419      -2.601  18.765 -10.200  1.00 38.23           C  
ANISOU 2451  CG  LEU A 419     4418   4868   5241   -249   -437   -854       C  
ATOM   2452  CD1 LEU A 419      -1.711  17.650 -10.722  1.00 37.01           C  
ANISOU 2452  CD1 LEU A 419     4156   4803   5103   -283   -412   -745       C  
ATOM   2453  CD2 LEU A 419      -2.438  18.921  -8.693  1.00 38.09           C  
ANISOU 2453  CD2 LEU A 419     4466   4886   5120   -203   -580  -1022       C  
ATOM   2454  N   CYS A 420      -2.642  22.786 -12.623  1.00 42.53           N  
ANISOU 2454  N   CYS A 420     4959   4822   6378   -459   -360   -761       N  
ATOM   2455  CA  CYS A 420      -1.842  23.823 -13.297  1.00 43.51           C  
ANISOU 2455  CA  CYS A 420     5025   4760   6746   -589   -362   -703       C  
ATOM   2456  C   CYS A 420      -2.667  24.572 -14.332  1.00 40.77           C  
ANISOU 2456  C   CYS A 420     4756   4285   6451   -569   -267   -581       C  
ATOM   2457  O   CYS A 420      -2.699  24.188 -15.505  1.00 43.51           O  
ANISOU 2457  O   CYS A 420     5083   4672   6776   -583   -145   -403       O  
ATOM   2458  CB  CYS A 420      -0.606  23.194 -13.976  1.00 43.34           C  
ANISOU 2458  CB  CYS A 420     4853   4805   6808   -694   -306   -583       C  
ATOM   2459  SG  CYS A 420       0.545  24.362 -14.799  1.00 45.84           S  
ANISOU 2459  SG  CYS A 420     5061   4911   7445   -882   -276   -484       S  
ATOM   2460  N   PRO A 421      -3.350  25.638 -13.901  1.00 43.77           N  
ANISOU 2460  N   PRO A 421     5233   4508   6889   -522   -328   -682       N  
ATOM   2461  CA  PRO A 421      -4.154  26.468 -14.804  1.00 44.12           C  
ANISOU 2461  CA  PRO A 421     5358   4404   7001   -487   -264   -571       C  
ATOM   2462  C   PRO A 421      -3.343  27.010 -15.979  1.00 47.24           C  
ANISOU 2462  C   PRO A 421     5707   4665   7577   -623   -194   -384       C  
ATOM   2463  O   PRO A 421      -3.887  27.125 -17.075  1.00 47.89           O  
ANISOU 2463  O   PRO A 421     5843   4721   7634   -591   -101   -214       O  
ATOM   2464  CB  PRO A 421      -4.624  27.614 -13.902  1.00 45.29           C  
ANISOU 2464  CB  PRO A 421     5597   4375   7238   -434   -373   -754       C  
ATOM   2465  CG  PRO A 421      -4.595  27.023 -12.522  1.00 49.12           C  
ANISOU 2465  CG  PRO A 421     6083   5005   7577   -376   -458   -957       C  
ATOM   2466  CD  PRO A 421      -3.385  26.133 -12.516  1.00 45.36           C  
ANISOU 2466  CD  PRO A 421     5485   4660   7091   -486   -469   -914       C  
ATOM   2467  N   ALA A 422      -2.070  27.325 -15.755  1.00 44.25           N  
ANISOU 2467  N   ALA A 422     5229   4209   7375   -772   -239   -410       N  
ATOM   2468  CA  ALA A 422      -1.207  27.838 -16.819  1.00 46.29           C  
ANISOU 2468  CA  ALA A 422     5422   4344   7821   -918   -148   -223       C  
ATOM   2469  C   ALA A 422      -0.866  26.768 -17.857  1.00 43.72           C  
ANISOU 2469  C   ALA A 422     5029   4208   7374   -928      9    -39       C  
ATOM   2470  O   ALA A 422      -0.435  27.099 -18.961  1.00 44.70           O  
ANISOU 2470  O   ALA A 422     5136   4262   7584  -1011    133    155       O  
ATOM   2471  CB  ALA A 422       0.075  28.423 -16.231  1.00 46.00           C  
ANISOU 2471  CB  ALA A 422     5264   4180   8034  -1084   -243   -314       C  
ATOM   2472  N   CYS A 423      -1.034  25.491 -17.498  1.00 41.03           N  
ANISOU 2472  N   CYS A 423     4659   4099   6832   -843      9    -99       N  
ATOM   2473  CA  CYS A 423      -0.787  24.395 -18.430  1.00 43.57           C  
ANISOU 2473  CA  CYS A 423     4934   4598   7024   -830    147     45       C  
ATOM   2474  C   CYS A 423      -1.990  24.277 -19.362  1.00 45.48           C  
ANISOU 2474  C   CYS A 423     5312   4867   7103   -720    224    163       C  
ATOM   2475  O   CYS A 423      -2.856  23.416 -19.186  1.00 44.76           O  
ANISOU 2475  O   CYS A 423     5268   4917   6821   -603    209    117       O  
ATOM   2476  CB  CYS A 423      -0.529  23.064 -17.685  1.00 40.60           C  
ANISOU 2476  CB  CYS A 423     4483   4432   6510   -776    104    -63       C  
ATOM   2477  SG  CYS A 423       0.809  23.145 -16.438  1.00 43.69           S  
ANISOU 2477  SG  CYS A 423     4717   4811   7071   -877    -40   -225       S  
ATOM   2478  N   SER A 424      -2.028  25.156 -20.353  1.00 45.62           N  
ANISOU 2478  N   SER A 424     5390   4740   7204   -764    298    323       N  
ATOM   2479  CA  SER A 424      -3.184  25.322 -21.221  1.00 43.48           C  
ANISOU 2479  CA  SER A 424     5260   4453   6807   -659    332    436       C  
ATOM   2480  C   SER A 424      -3.386  24.154 -22.153  1.00 43.55           C  
ANISOU 2480  C   SER A 424     5287   4659   6601   -598    431    537       C  
ATOM   2481  O   SER A 424      -2.562  23.920 -23.025  1.00 47.13           O  
ANISOU 2481  O   SER A 424     5705   5152   7048   -665    558    670       O  
ATOM   2482  CB  SER A 424      -3.032  26.613 -22.041  1.00 48.26           C  
ANISOU 2482  CB  SER A 424     5934   4836   7565   -729    381    602       C  
ATOM   2483  OG  SER A 424      -4.054  26.698 -23.020  1.00 50.10           O  
ANISOU 2483  OG  SER A 424     6305   5071   7659   -621    410    737       O  
ATOM   2484  N   VAL A 425      -4.479  23.413 -21.972  1.00 41.94           N  
ANISOU 2484  N   VAL A 425     5135   4576   6225   -471    377    468       N  
ATOM   2485  CA  VAL A 425      -4.817  22.321 -22.873  1.00 39.76           C  
ANISOU 2485  CA  VAL A 425     4894   4466   5747   -406    443    545       C  
ATOM   2486  C   VAL A 425      -5.736  22.827 -23.971  1.00 43.39           C  
ANISOU 2486  C   VAL A 425     5489   4870   6128   -335    449    684       C  
ATOM   2487  O   VAL A 425      -6.716  23.498 -23.677  1.00 44.72           O  
ANISOU 2487  O   VAL A 425     5712   4945   6334   -265    356    650       O  
ATOM   2488  CB  VAL A 425      -5.513  21.167 -22.121  1.00 41.68           C  
ANISOU 2488  CB  VAL A 425     5111   4865   5861   -321    376    404       C  
ATOM   2489  CG1 VAL A 425      -5.823  20.002 -23.071  1.00 41.56           C  
ANISOU 2489  CG1 VAL A 425     5133   5000   5657   -265    429    468       C  
ATOM   2490  CG2 VAL A 425      -4.640  20.703 -20.962  1.00 44.57           C  
ANISOU 2490  CG2 VAL A 425     5362   5281   6291   -376    348    274       C  
ATOM   2491  N   PRO A 426      -5.430  22.509 -25.239  1.00 41.95           N  
ANISOU 2491  N   PRO A 426     5364   4748   5829   -340    554    837       N  
ATOM   2492  CA  PRO A 426      -6.297  22.971 -26.323  1.00 41.07           C  
ANISOU 2492  CA  PRO A 426     5398   4591   5614   -262    539    978       C  
ATOM   2493  C   PRO A 426      -7.731  22.466 -26.138  1.00 41.39           C  
ANISOU 2493  C   PRO A 426     5473   4708   5545   -131    408    888       C  
ATOM   2494  O   PRO A 426      -7.941  21.262 -25.965  1.00 40.01           O  
ANISOU 2494  O   PRO A 426     5256   4691   5254    -98    395    796       O  
ATOM   2495  CB  PRO A 426      -5.655  22.368 -27.569  1.00 42.93           C  
ANISOU 2495  CB  PRO A 426     5685   4937   5689   -279    679   1116       C  
ATOM   2496  CG  PRO A 426      -4.238  22.106 -27.174  1.00 42.24           C  
ANISOU 2496  CG  PRO A 426     5461   4876   5711   -397    796   1089       C  
ATOM   2497  CD  PRO A 426      -4.315  21.691 -25.746  1.00 40.28           C  
ANISOU 2497  CD  PRO A 426     5093   4655   5557   -400    688    884       C  
ATOM   2498  N   PRO A 427      -8.704  23.386 -26.116  1.00 39.03           N  
ANISOU 2498  N   PRO A 427     5236   4286   5306    -58    311    909       N  
ATOM   2499  CA  PRO A 427     -10.098  22.976 -25.921  1.00 39.68           C  
ANISOU 2499  CA  PRO A 427     5319   4439   5320     66    190    825       C  
ATOM   2500  C   PRO A 427     -10.494  21.805 -26.816  1.00 39.19           C  
ANISOU 2500  C   PRO A 427     5296   4550   5046    116    182    855       C  
ATOM   2501  O   PRO A 427     -11.225  20.929 -26.386  1.00 37.66           O  
ANISOU 2501  O   PRO A 427     5039   4465   4803    164    117    739       O  
ATOM   2502  CB  PRO A 427     -10.883  24.255 -26.282  1.00 38.70           C  
ANISOU 2502  CB  PRO A 427     5282   4142   5278    145    110    916       C  
ATOM   2503  CG  PRO A 427      -9.963  25.350 -25.878  1.00 40.20           C  
ANISOU 2503  CG  PRO A 427     5474   4145   5656     48    166    946       C  
ATOM   2504  CD  PRO A 427      -8.579  24.855 -26.263  1.00 37.75           C  
ANISOU 2504  CD  PRO A 427     5138   3902   5302    -83    307   1013       C  
ATOM   2505  N   ARG A 428      -9.970  21.781 -28.034  1.00 43.28           N  
ANISOU 2505  N   ARG A 428     5918   5087   5440     99    254   1005       N  
ATOM   2506  CA  ARG A 428     -10.217  20.708 -28.988  1.00 44.45           C  
ANISOU 2506  CA  ARG A 428     6130   5390   5368    147    248   1025       C  
ATOM   2507  C   ARG A 428      -9.788  19.333 -28.435  1.00 42.07           C  
ANISOU 2507  C   ARG A 428     5728   5231   5024    109    290    883       C  
ATOM   2508  O   ARG A 428     -10.424  18.320 -28.712  1.00 42.38           O  
ANISOU 2508  O   ARG A 428     5778   5382   4942    161    222    818       O  
ATOM   2509  CB  ARG A 428      -9.483  21.034 -30.284  1.00 44.71           C  
ANISOU 2509  CB  ARG A 428     6301   5414   5273    128    360   1212       C  
ATOM   2510  CG  ARG A 428      -9.573  20.041 -31.405  1.00 52.07           C  
ANISOU 2510  CG  ARG A 428     7338   6498   5949    183    370   1238       C  
ATOM   2511  CD  ARG A 428      -8.623  20.502 -32.518  1.00 56.51           C  
ANISOU 2511  CD  ARG A 428     8028   7046   6396    151    534   1431       C  
ATOM   2512  NE  ARG A 428      -7.639  19.483 -32.886  1.00 60.18           N  
ANISOU 2512  NE  ARG A 428     8480   7648   6737    117    688   1399       N  
ATOM   2513  CZ  ARG A 428      -6.635  19.690 -33.740  1.00 63.51           C  
ANISOU 2513  CZ  ARG A 428     8976   8090   7065     80    881   1545       C  
ATOM   2514  NH1 ARG A 428      -6.470  20.880 -34.309  1.00 65.54           N  
ANISOU 2514  NH1 ARG A 428     9334   8231   7338     58    944   1749       N  
ATOM   2515  NH2 ARG A 428      -5.790  18.707 -34.020  1.00 62.46           N  
ANISOU 2515  NH2 ARG A 428     8814   8087   6830     69   1022   1492       N  
ATOM   2516  N   LEU A 429      -8.734  19.330 -27.628  1.00 38.61           N  
ANISOU 2516  N   LEU A 429     5192   4773   4703     18    384    834       N  
ATOM   2517  CA  LEU A 429      -8.196  18.099 -27.053  1.00 37.73           C  
ANISOU 2517  CA  LEU A 429     4989   4779   4569    -14    423    715       C  
ATOM   2518  C   LEU A 429      -9.044  17.700 -25.857  1.00 39.90           C  
ANISOU 2518  C   LEU A 429     5176   5075   4909     14    317    570       C  
ATOM   2519  O   LEU A 429      -9.308  16.521 -25.642  1.00 37.23           O  
ANISOU 2519  O   LEU A 429     4804   4839   4502     32    293    487       O  
ATOM   2520  CB  LEU A 429      -6.733  18.274 -26.626  1.00 39.94           C  
ANISOU 2520  CB  LEU A 429     5183   5034   4960   -115    545    722       C  
ATOM   2521  CG  LEU A 429      -6.107  17.046 -25.943  1.00 45.25           C  
ANISOU 2521  CG  LEU A 429     5751   5813   5628   -135    572    604       C  
ATOM   2522  CD1 LEU A 429      -6.197  15.845 -26.875  1.00 45.08           C  
ANISOU 2522  CD1 LEU A 429     5795   5913   5422    -79    604    606       C  
ATOM   2523  CD2 LEU A 429      -4.655  17.260 -25.504  1.00 46.70           C  
ANISOU 2523  CD2 LEU A 429     5825   5974   5946   -228    670    607       C  
ATOM   2524  N   VAL A 430      -9.455  18.698 -25.070  1.00 37.86           N  
ANISOU 2524  N   VAL A 430     4886   4711   4787     18    265    541       N  
ATOM   2525  CA  VAL A 430     -10.350  18.451 -23.946  1.00 36.56           C  
ANISOU 2525  CA  VAL A 430     4648   4571   4674     58    186    412       C  
ATOM   2526  C   VAL A 430     -11.592  17.732 -24.466  1.00 34.17           C  
ANISOU 2526  C   VAL A 430     4362   4350   4272    135    106    405       C  
ATOM   2527  O   VAL A 430     -12.004  16.708 -23.908  1.00 35.11           O  
ANISOU 2527  O   VAL A 430     4417   4559   4365    139     85    316       O  
ATOM   2528  CB  VAL A 430     -10.745  19.749 -23.220  1.00 40.20           C  
ANISOU 2528  CB  VAL A 430     5098   4897   5279     81    143    382       C  
ATOM   2529  CG1 VAL A 430     -11.710  19.436 -22.072  1.00 38.05           C  
ANISOU 2529  CG1 VAL A 430     4750   4674   5035    137     90    248       C  
ATOM   2530  CG2 VAL A 430      -9.489  20.476 -22.714  1.00 40.45           C  
ANISOU 2530  CG2 VAL A 430     5111   4832   5429    -11    200    377       C  
ATOM   2531  N   SER A 431     -12.134  18.239 -25.569  1.00 41.72           N  
ANISOU 2531  N   SER A 431     5406   5270   5175    190     55    505       N  
ATOM   2532  CA ASER A 431     -13.288  17.624 -26.210  0.48 43.41           C  
ANISOU 2532  CA ASER A 431     5636   5557   5302    261    -50    500       C  
ATOM   2533  CA BSER A 431     -13.296  17.622 -26.198  0.52 44.20           C  
ANISOU 2533  CA BSER A 431     5734   5657   5402    261    -51    499       C  
ATOM   2534  C   SER A 431     -12.974  16.216 -26.706  1.00 42.06           C  
ANISOU 2534  C   SER A 431     5483   5504   4993    233    -32    468       C  
ATOM   2535  O   SER A 431     -13.755  15.302 -26.510  1.00 41.01           O  
ANISOU 2535  O   SER A 431     5295   5441   4848    249   -102    390       O  
ATOM   2536  CB ASER A 431     -13.774  18.482 -27.372  0.48 42.57           C  
ANISOU 2536  CB ASER A 431     5642   5389   5145    331   -122    627       C  
ATOM   2537  CB BSER A 431     -13.819  18.489 -27.345  0.52 42.64           C  
ANISOU 2537  CB BSER A 431     5647   5397   5157    334   -126    624       C  
ATOM   2538  OG ASER A 431     -14.853  17.858 -28.039  0.48 39.76           O  
ANISOU 2538  OG ASER A 431     5297   5110   4701    400   -252    613       O  
ATOM   2539  OG BSER A 431     -14.358  19.712 -26.860  0.52 44.13           O  
ANISOU 2539  OG BSER A 431     5811   5463   5493    383   -170    638       O  
ATOM   2540  N   ALA A 432     -11.821  16.049 -27.355  1.00 38.43           N  
ANISOU 2540  N   ALA A 432     5097   5059   4444    193     69    528       N  
ATOM   2541  CA  ALA A 432     -11.430  14.736 -27.878  1.00 36.64           C  
ANISOU 2541  CA  ALA A 432     4903   4934   4086    183     98    487       C  
ATOM   2542  C   ALA A 432     -11.335  13.663 -26.790  1.00 38.09           C  
ANISOU 2542  C   ALA A 432     4975   5165   4333    144    108    365       C  
ATOM   2543  O   ALA A 432     -11.844  12.551 -26.974  1.00 37.01           O  
ANISOU 2543  O   ALA A 432     4837   5086   4138    157     48    299       O  
ATOM   2544  CB  ALA A 432     -10.109  14.825 -28.614  1.00 37.24           C  
ANISOU 2544  CB  ALA A 432     5053   5019   4079    153    239    568       C  
ATOM   2545  N   VAL A 433     -10.674  13.975 -25.673  1.00 33.05           N  
ANISOU 2545  N   VAL A 433     4251   4494   3812     95    174    336       N  
ATOM   2546  CA  VAL A 433     -10.499  12.965 -24.620  1.00 33.54           C  
ANISOU 2546  CA  VAL A 433     4227   4602   3914     65    185    240       C  
ATOM   2547  C   VAL A 433     -11.821  12.656 -23.907  1.00 34.92           C  
ANISOU 2547  C   VAL A 433     4339   4792   4137     87     97    177       C  
ATOM   2548  O   VAL A 433     -11.972  11.579 -23.314  1.00 34.68           O  
ANISOU 2548  O   VAL A 433     4261   4806   4109     68     92    117       O  
ATOM   2549  CB  VAL A 433      -9.436  13.369 -23.553  1.00 32.33           C  
ANISOU 2549  CB  VAL A 433     4004   4420   3860     14    255    218       C  
ATOM   2550  CG1 VAL A 433      -8.081  13.593 -24.210  1.00 32.59           C  
ANISOU 2550  CG1 VAL A 433     4059   4444   3879    -20    355    280       C  
ATOM   2551  CG2 VAL A 433      -9.881  14.590 -22.737  1.00 34.16           C  
ANISOU 2551  CG2 VAL A 433     4203   4577   4199     17    222    205       C  
ATOM   2552  N   THR A 434     -12.783  13.572 -23.973  1.00 34.78           N  
ANISOU 2552  N   THR A 434     4314   4735   4167    129     35    198       N  
ATOM   2553  CA  THR A 434     -14.098  13.291 -23.398  1.00 33.81           C  
ANISOU 2553  CA  THR A 434     4107   4636   4101    155    -34    145       C  
ATOM   2554  C   THR A 434     -14.824  12.241 -24.259  1.00 33.94           C  
ANISOU 2554  C   THR A 434     4137   4705   4054    162   -119    134       C  
ATOM   2555  O   THR A 434     -15.294  11.208 -23.746  1.00 34.49           O  
ANISOU 2555  O   THR A 434     4139   4814   4152    132   -133     79       O  
ATOM   2556  CB  THR A 434     -14.930  14.574 -23.268  1.00 36.23           C  
ANISOU 2556  CB  THR A 434     4389   4883   4494    216    -79    163       C  
ATOM   2557  OG1 THR A 434     -14.248  15.464 -22.383  1.00 36.06           O  
ANISOU 2557  OG1 THR A 434     4361   4801   4540    203    -11    147       O  
ATOM   2558  CG2 THR A 434     -16.316  14.268 -22.691  1.00 33.86           C  
ANISOU 2558  CG2 THR A 434     3973   4622   4269    250   -132    109       C  
ATOM   2559  N   TRP A 435     -14.851  12.481 -25.566  1.00 37.21           N  
ANISOU 2559  N   TRP A 435     4650   5112   4375    198   -177    188       N  
ATOM   2560  CA  TRP A 435     -15.436  11.535 -26.513  1.00 39.22           C  
ANISOU 2560  CA  TRP A 435     4945   5411   4547    210   -281    163       C  
ATOM   2561  C   TRP A 435     -14.800  10.158 -26.358  1.00 38.21           C  
ANISOU 2561  C   TRP A 435     4826   5314   4376    157   -232    100       C  
ATOM   2562  O   TRP A 435     -15.492   9.146 -26.355  1.00 36.91           O  
ANISOU 2562  O   TRP A 435     4622   5168   4234    135   -308     39       O  
ATOM   2563  CB  TRP A 435     -15.289  12.029 -27.966  1.00 36.53           C  
ANISOU 2563  CB  TRP A 435     4751   5067   4061    265   -333    236       C  
ATOM   2564  CG  TRP A 435     -16.307  13.083 -28.385  1.00 39.10           C  
ANISOU 2564  CG  TRP A 435     5076   5360   4420    337   -452    295       C  
ATOM   2565  CD1 TRP A 435     -16.107  14.419 -28.452  1.00 40.93           C  
ANISOU 2565  CD1 TRP A 435     5348   5524   4679    376   -421    388       C  
ATOM   2566  CD2 TRP A 435     -17.672  12.864 -28.788  1.00 40.05           C  
ANISOU 2566  CD2 TRP A 435     5145   5505   4569    383   -630    264       C  
ATOM   2567  NE1 TRP A 435     -17.248  15.054 -28.870  1.00 42.11           N  
ANISOU 2567  NE1 TRP A 435     5485   5651   4865    456   -566    422       N  
ATOM   2568  CE2 TRP A 435     -18.226  14.125 -29.083  1.00 39.92           C  
ANISOU 2568  CE2 TRP A 435     5140   5438   4590    464   -701    345       C  
ATOM   2569  CE3 TRP A 435     -18.472  11.729 -28.924  1.00 38.98           C  
ANISOU 2569  CE3 TRP A 435     4944   5417   4450    359   -746    175       C  
ATOM   2570  CZ2 TRP A 435     -19.550  14.289 -29.507  1.00 40.14           C  
ANISOU 2570  CZ2 TRP A 435     5108   5477   4668    535   -887    340       C  
ATOM   2571  CZ3 TRP A 435     -19.800  11.892 -29.353  1.00 38.09           C  
ANISOU 2571  CZ3 TRP A 435     4763   5316   4396    413   -934    165       C  
ATOM   2572  CH2 TRP A 435     -20.317  13.157 -29.640  1.00 38.40           C  
ANISOU 2572  CH2 TRP A 435     4805   5318   4466    505  -1004    246       C  
ATOM   2573  N   LEU A 436     -13.481  10.121 -26.229  1.00 33.86           N  
ANISOU 2573  N   LEU A 436     4321   4762   3784    136   -111    117       N  
ATOM   2574  CA  LEU A 436     -12.781   8.845 -26.115  1.00 34.19           C  
ANISOU 2574  CA  LEU A 436     4376   4824   3793    106    -64     60       C  
ATOM   2575  C   LEU A 436     -13.212   8.094 -24.852  1.00 34.92           C  
ANISOU 2575  C   LEU A 436     4358   4912   3998     61    -68      9       C  
ATOM   2576  O   LEU A 436     -13.461   6.900 -24.906  1.00 33.95           O  
ANISOU 2576  O   LEU A 436     4236   4787   3876     39   -107    -42       O  
ATOM   2577  CB  LEU A 436     -11.278   9.058 -26.124  1.00 31.86           C  
ANISOU 2577  CB  LEU A 436     4114   4530   3463    101     70     92       C  
ATOM   2578  CG  LEU A 436     -10.408   7.818 -25.925  1.00 32.44           C  
ANISOU 2578  CG  LEU A 436     4187   4617   3522     90    128     37       C  
ATOM   2579  CD1 LEU A 436     -10.645   6.772 -27.022  1.00 33.36           C  
ANISOU 2579  CD1 LEU A 436     4402   4747   3525    124     73    -19       C  
ATOM   2580  CD2 LEU A 436      -8.944   8.272 -25.885  1.00 31.55           C  
ANISOU 2580  CD2 LEU A 436     4066   4511   3410     88    260     78       C  
ATOM   2581  N   GLY A 437     -13.312   8.805 -23.731  1.00 33.02           N  
ANISOU 2581  N   GLY A 437     4034   4664   3847     48    -25     25       N  
ATOM   2582  CA  GLY A 437     -13.858   8.244 -22.506  1.00 32.66           C  
ANISOU 2582  CA  GLY A 437     3896   4627   3888     14    -16     -5       C  
ATOM   2583  C   GLY A 437     -15.241   7.607 -22.677  1.00 32.53           C  
ANISOU 2583  C   GLY A 437     3819   4616   3924     -2   -105    -29       C  
ATOM   2584  O   GLY A 437     -15.476   6.477 -22.226  1.00 32.21           O  
ANISOU 2584  O   GLY A 437     3745   4571   3923    -49   -105    -51       O  
ATOM   2585  N   TYR A 438     -16.144   8.317 -23.342  1.00 33.15           N  
ANISOU 2585  N   TYR A 438     3880   4697   4018     34   -189    -18       N  
ATOM   2586  CA  TYR A 438     -17.523   7.851 -23.516  1.00 34.97           C  
ANISOU 2586  CA  TYR A 438     4020   4936   4330     19   -291    -43       C  
ATOM   2587  C   TYR A 438     -17.623   6.680 -24.483  1.00 34.99           C  
ANISOU 2587  C   TYR A 438     4082   4925   4287    -11   -391    -87       C  
ATOM   2588  O   TYR A 438     -18.469   5.822 -24.311  1.00 35.31           O  
ANISOU 2588  O   TYR A 438     4039   4956   4421    -65   -450   -120       O  
ATOM   2589  CB  TYR A 438     -18.419   8.996 -23.997  1.00 35.69           C  
ANISOU 2589  CB  TYR A 438     4071   5033   4459     85   -375    -20       C  
ATOM   2590  CG  TYR A 438     -18.670  10.050 -22.943  1.00 35.97           C  
ANISOU 2590  CG  TYR A 438     4020   5067   4578    120   -292     -3       C  
ATOM   2591  CD1 TYR A 438     -18.543   9.752 -21.591  1.00 34.21           C  
ANISOU 2591  CD1 TYR A 438     3731   4863   4405     83   -175    -20       C  
ATOM   2592  CD2 TYR A 438     -19.053  11.345 -23.301  1.00 35.31           C  
ANISOU 2592  CD2 TYR A 438     3938   4960   4518    200   -337     27       C  
ATOM   2593  CE1 TYR A 438     -18.779  10.715 -20.616  1.00 34.41           C  
ANISOU 2593  CE1 TYR A 438     3696   4893   4486    127    -99    -26       C  
ATOM   2594  CE2 TYR A 438     -19.301  12.313 -22.334  1.00 36.05           C  
ANISOU 2594  CE2 TYR A 438     3963   5040   4695    245   -265     21       C  
ATOM   2595  CZ  TYR A 438     -19.159  11.995 -20.994  1.00 34.57           C  
ANISOU 2595  CZ  TYR A 438     3713   4879   4541    209   -144    -15       C  
ATOM   2596  OH  TYR A 438     -19.414  12.964 -20.026  1.00 38.25           O  
ANISOU 2596  OH  TYR A 438     4128   5335   5070    266    -72    -41       O  
ATOM   2597  N   VAL A 439     -16.755   6.657 -25.492  1.00 34.03           N  
ANISOU 2597  N   VAL A 439     4106   4800   4025     23   -402    -91       N  
ATOM   2598  CA  VAL A 439     -16.685   5.555 -26.456  1.00 35.72           C  
ANISOU 2598  CA  VAL A 439     4411   4997   4163     13   -488   -155       C  
ATOM   2599  C   VAL A 439     -16.409   4.209 -25.765  1.00 35.91           C  
ANISOU 2599  C   VAL A 439     4410   4980   4254    -54   -444   -199       C  
ATOM   2600  O   VAL A 439     -16.905   3.169 -26.203  1.00 35.93           O  
ANISOU 2600  O   VAL A 439     4424   4942   4284    -90   -546   -266       O  
ATOM   2601  CB  VAL A 439     -15.607   5.826 -27.530  1.00 36.97           C  
ANISOU 2601  CB  VAL A 439     4738   5172   4137     75   -453   -146       C  
ATOM   2602  CG1 VAL A 439     -15.128   4.536 -28.177  1.00 39.90           C  
ANISOU 2602  CG1 VAL A 439     5212   5521   4426     73   -476   -230       C  
ATOM   2603  CG2 VAL A 439     -16.141   6.794 -28.591  1.00 37.47           C  
ANISOU 2603  CG2 VAL A 439     4867   5262   4108    141   -554   -107       C  
ATOM   2604  N   ASN A 440     -15.662   4.227 -24.665  1.00 35.35           N  
ANISOU 2604  N   ASN A 440     4306   4908   4219    -70   -309   -161       N  
ATOM   2605  CA  ASN A 440     -15.462   3.002 -23.887  1.00 35.42           C  
ANISOU 2605  CA  ASN A 440     4291   4869   4297   -126   -271   -178       C  
ATOM   2606  C   ASN A 440     -16.769   2.270 -23.549  1.00 35.35           C  
ANISOU 2606  C   ASN A 440     4177   4826   4428   -204   -346   -191       C  
ATOM   2607  O   ASN A 440     -16.815   1.042 -23.546  1.00 36.87           O  
ANISOU 2607  O   ASN A 440     4388   4947   4672   -255   -379   -225       O  
ATOM   2608  CB  ASN A 440     -14.717   3.282 -22.585  1.00 34.24           C  
ANISOU 2608  CB  ASN A 440     4103   4737   4168   -128   -139   -123       C  
ATOM   2609  CG  ASN A 440     -14.399   2.005 -21.825  1.00 37.24           C  
ANISOU 2609  CG  ASN A 440     4485   5063   4600   -170   -105   -120       C  
ATOM   2610  OD1 ASN A 440     -15.004   1.722 -20.794  1.00 40.24           O  
ANISOU 2610  OD1 ASN A 440     4787   5439   5064   -221    -72    -78       O  
ATOM   2611  ND2 ASN A 440     -13.484   1.207 -22.355  1.00 36.95           N  
ANISOU 2611  ND2 ASN A 440     4543   4983   4514   -143   -107   -159       N  
ATOM   2612  N   SER A 441     -17.827   3.033 -23.290  1.00 36.71           N  
ANISOU 2612  N   SER A 441     4231   5039   4678   -212   -372   -164       N  
ATOM   2613  CA  SER A 441     -19.106   2.450 -22.888  1.00 37.18           C  
ANISOU 2613  CA  SER A 441     4149   5078   4899   -292   -421   -164       C  
ATOM   2614  C   SER A 441     -19.734   1.601 -23.990  1.00 38.18           C  
ANISOU 2614  C   SER A 441     4293   5150   5064   -333   -595   -242       C  
ATOM   2615  O   SER A 441     -20.618   0.787 -23.727  1.00 40.34           O  
ANISOU 2615  O   SER A 441     4458   5375   5493   -425   -644   -252       O  
ATOM   2616  CB  SER A 441     -20.070   3.554 -22.455  1.00 38.91           C  
ANISOU 2616  CB  SER A 441     4225   5364   5196   -267   -405   -128       C  
ATOM   2617  OG  SER A 441     -19.687   4.063 -21.182  1.00 40.01           O  
ANISOU 2617  OG  SER A 441     4333   5539   5328   -251   -243    -73       O  
ATOM   2618  N   ALA A 442     -19.277   1.796 -25.221  1.00 37.44           N  
ANISOU 2618  N   ALA A 442     4337   5061   4827   -266   -689   -298       N  
ATOM   2619  CA  ALA A 442     -19.744   0.998 -26.351  1.00 39.28           C  
ANISOU 2619  CA  ALA A 442     4627   5244   5053   -287   -872   -397       C  
ATOM   2620  C   ALA A 442     -18.876  -0.230 -26.625  1.00 41.79           C  
ANISOU 2620  C   ALA A 442     5085   5476   5317   -301   -862   -466       C  
ATOM   2621  O   ALA A 442     -19.302  -1.148 -27.334  1.00 40.90           O  
ANISOU 2621  O   ALA A 442     5014   5291   5236   -340  -1011   -565       O  
ATOM   2622  CB  ALA A 442     -19.818   1.865 -27.601  1.00 37.42           C  
ANISOU 2622  CB  ALA A 442     4485   5067   4664   -193   -989   -423       C  
ATOM   2623  N   LEU A 443     -17.664  -0.253 -26.065  1.00 40.32           N  
ANISOU 2623  N   LEU A 443     4968   5291   5061   -265   -701   -423       N  
ATOM   2624  CA  LEU A 443     -16.674  -1.277 -26.411  1.00 39.23           C  
ANISOU 2624  CA  LEU A 443     4971   5080   4857   -240   -680   -489       C  
ATOM   2625  C   LEU A 443     -16.862  -2.591 -25.696  1.00 40.27           C  
ANISOU 2625  C   LEU A 443     5066   5089   5147   -329   -681   -497       C  
ATOM   2626  O   LEU A 443     -16.614  -3.647 -26.285  1.00 40.02           O  
ANISOU 2626  O   LEU A 443     5138   4956   5112   -329   -752   -594       O  
ATOM   2627  CB  LEU A 443     -15.251  -0.788 -26.114  1.00 40.17           C  
ANISOU 2627  CB  LEU A 443     5157   5248   4859   -159   -515   -438       C  
ATOM   2628  CG  LEU A 443     -14.776   0.479 -26.815  1.00 40.68           C  
ANISOU 2628  CG  LEU A 443     5278   5413   4766    -74   -477   -412       C  
ATOM   2629  CD1 LEU A 443     -13.339   0.825 -26.387  1.00 40.40           C  
ANISOU 2629  CD1 LEU A 443     5272   5409   4668    -20   -311   -362       C  
ATOM   2630  CD2 LEU A 443     -14.881   0.319 -28.321  1.00 39.15           C  
ANISOU 2630  CD2 LEU A 443     5224   5226   4426    -19   -591   -504       C  
ATOM   2631  N   ASN A 444     -17.254  -2.548 -24.423  1.00 41.44           N  
ANISOU 2631  N   ASN A 444     5081   5237   5427   -399   -593   -394       N  
ATOM   2632  CA  ASN A 444     -17.316  -3.799 -23.641  1.00 43.91           C  
ANISOU 2632  CA  ASN A 444     5376   5426   5883   -483   -566   -366       C  
ATOM   2633  C   ASN A 444     -18.182  -4.912 -24.240  1.00 43.76           C  
ANISOU 2633  C   ASN A 444     5352   5274   6001   -577   -725   -454       C  
ATOM   2634  O   ASN A 444     -17.769  -6.068 -24.227  1.00 46.05           O  
ANISOU 2634  O   ASN A 444     5727   5425   6344   -598   -741   -490       O  
ATOM   2635  CB  ASN A 444     -17.774  -3.517 -22.209  1.00 44.05           C  
ANISOU 2635  CB  ASN A 444     5254   5482   6001   -546   -443   -231       C  
ATOM   2636  CG  ASN A 444     -16.635  -3.035 -21.329  1.00 46.51           C  
ANISOU 2636  CG  ASN A 444     5610   5856   6204   -470   -293   -155       C  
ATOM   2637  OD1 ASN A 444     -15.535  -2.776 -21.813  1.00 44.09           O  
ANISOU 2637  OD1 ASN A 444     5407   5575   5770   -377   -278   -196       O  
ATOM   2638  ND2 ASN A 444     -16.900  -2.887 -20.037  1.00 47.66           N  
ANISOU 2638  ND2 ASN A 444     5673   6036   6401   -509   -183    -45       N  
ATOM   2639  N   PRO A 445     -19.381  -4.589 -24.759  1.00 42.61           N  
ANISOU 2639  N   PRO A 445     5102   5157   5931   -633   -855   -493       N  
ATOM   2640  CA  PRO A 445     -20.140  -5.691 -25.369  1.00 44.27           C  
ANISOU 2640  CA  PRO A 445     5309   5227   6284   -730  -1031   -595       C  
ATOM   2641  C   PRO A 445     -19.373  -6.370 -26.506  1.00 44.47           C  
ANISOU 2641  C   PRO A 445     5547   5172   6179   -654  -1136   -750       C  
ATOM   2642  O   PRO A 445     -19.448  -7.590 -26.669  1.00 46.80           O  
ANISOU 2642  O   PRO A 445     5897   5298   6585   -718  -1219   -827       O  
ATOM   2643  CB  PRO A 445     -21.404  -4.999 -25.896  1.00 43.68           C  
ANISOU 2643  CB  PRO A 445     5091   5231   6274   -766  -1175   -625       C  
ATOM   2644  CG  PRO A 445     -21.595  -3.850 -24.948  1.00 41.13           C  
ANISOU 2644  CG  PRO A 445     4629   5046   5952   -742  -1015   -486       C  
ATOM   2645  CD  PRO A 445     -20.188  -3.357 -24.665  1.00 41.81           C  
ANISOU 2645  CD  PRO A 445     4860   5189   5836   -624   -857   -443       C  
ATOM   2646  N   VAL A 446     -18.633  -5.582 -27.274  1.00 44.44           N  
ANISOU 2646  N   VAL A 446     5665   5280   5942   -517  -1120   -793       N  
ATOM   2647  CA  VAL A 446     -17.831  -6.128 -28.357  1.00 45.04           C  
ANISOU 2647  CA  VAL A 446     5950   5307   5858   -422  -1181   -937       C  
ATOM   2648  C   VAL A 446     -16.707  -6.982 -27.799  1.00 44.73           C  
ANISOU 2648  C   VAL A 446     5995   5166   5834   -386  -1049   -924       C  
ATOM   2649  O   VAL A 446     -16.430  -8.064 -28.316  1.00 45.28           O  
ANISOU 2649  O   VAL A 446     6189   5097   5919   -371  -1124  -1050       O  
ATOM   2650  CB  VAL A 446     -17.232  -5.029 -29.236  1.00 46.83           C  
ANISOU 2650  CB  VAL A 446     6281   5689   5824   -283  -1150   -952       C  
ATOM   2651  CG1 VAL A 446     -16.463  -5.644 -30.385  1.00 45.02           C  
ANISOU 2651  CG1 VAL A 446     6271   5420   5416   -179  -1196  -1107       C  
ATOM   2652  CG2 VAL A 446     -18.330  -4.105 -29.748  1.00 43.99           C  
ANISOU 2652  CG2 VAL A 446     5841   5427   5447   -300  -1288   -944       C  
ATOM   2653  N   ILE A 447     -16.063  -6.493 -26.744  1.00 42.19           N  
ANISOU 2653  N   ILE A 447     5609   4909   5512   -364   -866   -780       N  
ATOM   2654  CA  ILE A 447     -14.958  -7.221 -26.120  1.00 43.77           C  
ANISOU 2654  CA  ILE A 447     5872   5026   5731   -317   -748   -749       C  
ATOM   2655  C   ILE A 447     -15.406  -8.595 -25.617  1.00 46.12           C  
ANISOU 2655  C   ILE A 447     6163   5120   6239   -421   -809   -753       C  
ATOM   2656  O   ILE A 447     -14.723  -9.594 -25.860  1.00 49.46           O  
ANISOU 2656  O   ILE A 447     6709   5406   6677   -369   -823   -832       O  
ATOM   2657  CB  ILE A 447     -14.347  -6.418 -24.960  1.00 43.03           C  
ANISOU 2657  CB  ILE A 447     5693   5041   5615   -292   -575   -590       C  
ATOM   2658  CG1 ILE A 447     -13.683  -5.153 -25.500  1.00 42.22           C  
ANISOU 2658  CG1 ILE A 447     5616   5104   5322   -187   -507   -591       C  
ATOM   2659  CG2 ILE A 447     -13.320  -7.260 -24.206  1.00 42.90           C  
ANISOU 2659  CG2 ILE A 447     5726   4930   5645   -249   -486   -547       C  
ATOM   2660  CD1 ILE A 447     -13.002  -4.304 -24.418  1.00 41.48           C  
ANISOU 2660  CD1 ILE A 447     5444   5109   5208   -161   -357   -460       C  
ATOM   2661  N   TYR A 448     -16.561  -8.657 -24.950  1.00 46.85           N  
ANISOU 2661  N   TYR A 448     6111   5182   6506   -567   -841   -669       N  
ATOM   2662  CA  TYR A 448     -17.085  -9.947 -24.476  1.00 47.05           C  
ANISOU 2662  CA  TYR A 448     6119   5001   6758   -691   -893   -652       C  
ATOM   2663  C   TYR A 448     -17.306 -10.911 -25.627  1.00 48.50           C  
ANISOU 2663  C   TYR A 448     6420   5022   6986   -704  -1081   -847       C  
ATOM   2664  O   TYR A 448     -16.942 -12.082 -25.541  1.00 50.21           O  
ANISOU 2664  O   TYR A 448     6732   5040   7306   -713  -1105   -886       O  
ATOM   2665  CB  TYR A 448     -18.410  -9.785 -23.732  1.00 48.90           C  
ANISOU 2665  CB  TYR A 448     6156   5246   7178   -855   -891   -536       C  
ATOM   2666  CG  TYR A 448     -18.366  -8.806 -22.606  1.00 46.55           C  
ANISOU 2666  CG  TYR A 448     5745   5110   6830   -843   -714   -365       C  
ATOM   2667  CD1 TYR A 448     -17.242  -8.696 -21.802  1.00 47.04           C  
ANISOU 2667  CD1 TYR A 448     5877   5209   6789   -752   -567   -272       C  
ATOM   2668  CD2 TYR A 448     -19.444  -7.975 -22.352  1.00 47.26           C  
ANISOU 2668  CD2 TYR A 448     5658   5319   6978   -912   -705   -309       C  
ATOM   2669  CE1 TYR A 448     -17.190  -7.777 -20.771  1.00 47.83           C  
ANISOU 2669  CE1 TYR A 448     5889   5456   6828   -735   -422   -137       C  
ATOM   2670  CE2 TYR A 448     -19.404  -7.058 -21.331  1.00 48.16           C  
ANISOU 2670  CE2 TYR A 448     5684   5579   7037   -887   -542   -174       C  
ATOM   2671  CZ  TYR A 448     -18.272  -6.961 -20.542  1.00 47.30           C  
ANISOU 2671  CZ  TYR A 448     5664   5500   6808   -801   -405    -94       C  
ATOM   2672  OH  TYR A 448     -18.239  -6.053 -19.518  1.00 49.13           O  
ANISOU 2672  OH  TYR A 448     5823   5872   6974   -774   -261     20       O  
ATOM   2673  N   THR A 449     -17.923 -10.405 -26.694  1.00 53.87           N  
ANISOU 2673  N   THR A 449     7099   5781   7589   -699  -1226   -971       N  
ATOM   2674  CA  THR A 449     -18.314 -11.222 -27.838  1.00 53.76           C  
ANISOU 2674  CA  THR A 449     7193   5630   7603   -719  -1441  -1177       C  
ATOM   2675  C   THR A 449     -17.093 -11.805 -28.529  1.00 54.17           C  
ANISOU 2675  C   THR A 449     7473   5612   7497   -562  -1425  -1317       C  
ATOM   2676  O   THR A 449     -17.124 -12.934 -29.009  1.00 57.13           O  
ANISOU 2676  O   THR A 449     7961   5787   7958   -579  -1550  -1465       O  
ATOM   2677  CB  THR A 449     -19.138 -10.412 -28.863  1.00 51.13           C  
ANISOU 2677  CB  THR A 449     6829   5431   7168   -715  -1608  -1275       C  
ATOM   2678  OG1 THR A 449     -20.262  -9.818 -28.207  1.00 55.63           O  
ANISOU 2678  OG1 THR A 449     7164   6074   7898   -842  -1611  -1147       O  
ATOM   2679  CG2 THR A 449     -19.646 -11.315 -29.984  1.00 53.24           C  
ANISOU 2679  CG2 THR A 449     7206   5548   7474   -749  -1864  -1501       C  
ATOM   2680  N   VAL A 450     -16.019 -11.025 -28.578  1.00 53.41           N  
ANISOU 2680  N   VAL A 450     7434   5676   7182   -409  -1268  -1274       N  
ATOM   2681  CA  VAL A 450     -14.785 -11.465 -29.212  1.00 52.80           C  
ANISOU 2681  CA  VAL A 450     7545   5565   6951   -243  -1213  -1395       C  
ATOM   2682  C   VAL A 450     -13.973 -12.362 -28.285  1.00 54.41           C  
ANISOU 2682  C   VAL A 450     7766   5618   7290   -220  -1101  -1323       C  
ATOM   2683  O   VAL A 450     -13.508 -13.421 -28.697  1.00 55.60           O  
ANISOU 2683  O   VAL A 450     8057   5596   7474   -157  -1148  -1458       O  
ATOM   2684  CB  VAL A 450     -13.910 -10.263 -29.651  1.00 53.53           C  
ANISOU 2684  CB  VAL A 450     7673   5889   6776    -94  -1075  -1366       C  
ATOM   2685  CG1 VAL A 450     -12.575 -10.748 -30.206  1.00 53.11           C  
ANISOU 2685  CG1 VAL A 450     7783   5809   6587     80   -980  -1474       C  
ATOM   2686  CG2 VAL A 450     -14.635  -9.422 -30.688  1.00 52.23           C  
ANISOU 2686  CG2 VAL A 450     7533   5861   6452    -91  -1196  -1435       C  
ATOM   2687  N   PHE A 451     -13.820 -11.955 -27.028  1.00 52.66           N  
ANISOU 2687  N   PHE A 451     7411   5453   7142   -263   -963  -1116       N  
ATOM   2688  CA  PHE A 451     -12.817 -12.590 -26.174  1.00 53.03           C  
ANISOU 2688  CA  PHE A 451     7487   5405   7256   -197   -846  -1032       C  
ATOM   2689  C   PHE A 451     -13.317 -13.546 -25.100  1.00 55.35           C  
ANISOU 2689  C   PHE A 451     7732   5501   7797   -328   -864   -911       C  
ATOM   2690  O   PHE A 451     -12.508 -14.195 -24.451  1.00 58.44           O  
ANISOU 2690  O   PHE A 451     8171   5787   8248   -264   -795   -844       O  
ATOM   2691  CB  PHE A 451     -11.957 -11.520 -25.500  1.00 50.25           C  
ANISOU 2691  CB  PHE A 451     7058   5256   6780   -115   -672   -890       C  
ATOM   2692  CG  PHE A 451     -11.152 -10.705 -26.462  1.00 53.71           C  
ANISOU 2692  CG  PHE A 451     7553   5861   6993     29   -613   -982       C  
ATOM   2693  CD1 PHE A 451      -9.963 -11.195 -26.974  1.00 57.05           C  
ANISOU 2693  CD1 PHE A 451     8087   6248   7343    188   -554  -1082       C  
ATOM   2694  CD2 PHE A 451     -11.571  -9.445 -26.848  1.00 53.37           C  
ANISOU 2694  CD2 PHE A 451     7452   6008   6818      9   -603   -958       C  
ATOM   2695  CE1 PHE A 451      -9.215 -10.441 -27.866  1.00 55.82           C  
ANISOU 2695  CE1 PHE A 451     7975   6253   6980    315   -470  -1151       C  
ATOM   2696  CE2 PHE A 451     -10.821  -8.686 -27.732  1.00 52.94           C  
ANISOU 2696  CE2 PHE A 451     7459   6099   6558    133   -533  -1017       C  
ATOM   2697  CZ  PHE A 451      -9.644  -9.187 -28.239  1.00 52.53           C  
ANISOU 2697  CZ  PHE A 451     7511   6020   6429    280   -457  -1110       C  
ATOM   2698  N   ASN A 452     -14.624 -13.641 -24.893  1.00 55.52           N  
ANISOU 2698  N   ASN A 452     7654   5471   7969   -508   -950   -870       N  
ATOM   2699  CA  ASN A 452     -15.130 -14.627 -23.940  1.00 54.63           C  
ANISOU 2699  CA  ASN A 452     7503   5153   8102   -645   -955   -745       C  
ATOM   2700  C   ASN A 452     -15.970 -15.705 -24.605  1.00 56.70           C  
ANISOU 2700  C   ASN A 452     7812   5174   8558   -765  -1141   -885       C  
ATOM   2701  O   ASN A 452     -16.943 -15.415 -25.292  1.00 57.51           O  
ANISOU 2701  O   ASN A 452     7851   5316   8686   -857  -1271   -983       O  
ATOM   2702  CB  ASN A 452     -15.955 -13.975 -22.834  1.00 56.54           C  
ANISOU 2702  CB  ASN A 452     7561   5509   8413   -780   -860   -535       C  
ATOM   2703  CG  ASN A 452     -16.523 -15.001 -21.869  1.00 58.84           C  
ANISOU 2703  CG  ASN A 452     7816   5592   8951   -933   -842   -385       C  
ATOM   2704  OD1 ASN A 452     -17.652 -15.472 -22.037  1.00 55.49           O  
ANISOU 2704  OD1 ASN A 452     7314   5048   8724  -1103   -939   -403       O  
ATOM   2705  ND2 ASN A 452     -15.727 -15.382 -20.870  1.00 57.26           N  
ANISOU 2705  ND2 ASN A 452     7672   5338   8747   -873   -725   -232       N  
ATOM   2706  N   ALA A 453     -15.599 -16.956 -24.367  1.00 61.60           N  
ANISOU 2706  N   ALA A 453     8541   5532   9331   -765  -1167   -892       N  
ATOM   2707  CA  ALA A 453     -16.199 -18.072 -25.071  1.00 59.83           C  
ANISOU 2707  CA  ALA A 453     8396   5040   9296   -858  -1357  -1058       C  
ATOM   2708  C   ALA A 453     -17.709 -18.161 -24.874  1.00 62.04           C  
ANISOU 2708  C   ALA A 453     8509   5261   9802  -1107  -1452  -1002       C  
ATOM   2709  O   ALA A 453     -18.461 -18.366 -25.834  1.00 62.22           O  
ANISOU 2709  O   ALA A 453     8535   5219   9889  -1182  -1648  -1190       O  
ATOM   2710  CB  ALA A 453     -15.536 -19.372 -24.634  1.00 64.38           C  
ANISOU 2710  CB  ALA A 453     9107   5325  10028   -820  -1347  -1031       C  
ATOM   2711  N   GLU A 454     -18.157 -18.023 -23.631  1.00 61.99           N  
ANISOU 2711  N   GLU A 454     8355   5280   9918  -1231  -1316   -747       N  
ATOM   2712  CA  GLU A 454     -19.571 -18.232 -23.343  1.00 63.70           C  
ANISOU 2712  CA  GLU A 454     8391   5421  10391  -1474  -1375   -672       C  
ATOM   2713  C   GLU A 454     -20.403 -17.133 -24.002  1.00 59.43           C  
ANISOU 2713  C   GLU A 454     7700   5116   9763  -1506  -1455   -761       C  
ATOM   2714  O   GLU A 454     -21.405 -17.430 -24.648  1.00 59.56           O  
ANISOU 2714  O   GLU A 454     7639   5042   9949  -1644  -1641   -882       O  
ATOM   2715  CB  GLU A 454     -19.824 -18.288 -21.835  1.00 66.01           C  
ANISOU 2715  CB  GLU A 454     8567   5713  10803  -1583  -1174   -365       C  
ATOM   2716  N   PHE A 455     -19.975 -15.874 -23.873  1.00 57.04           N  
ANISOU 2716  N   PHE A 455     7362   5102   9208  -1374  -1332   -708       N  
ATOM   2717  CA  PHE A 455     -20.681 -14.782 -24.541  1.00 58.02           C  
ANISOU 2717  CA  PHE A 455     7365   5443   9236  -1375  -1413   -788       C  
ATOM   2718  C   PHE A 455     -20.670 -14.981 -26.056  1.00 60.04           C  
ANISOU 2718  C   PHE A 455     7756   5653   9403  -1310  -1647  -1065       C  
ATOM   2719  O   PHE A 455     -21.697 -14.839 -26.721  1.00 57.07           O  
ANISOU 2719  O   PHE A 455     7281   5290   9112  -1405  -1830  -1169       O  
ATOM   2720  CB  PHE A 455     -20.064 -13.430 -24.182  1.00 56.12           C  
ANISOU 2720  CB  PHE A 455     7101   5487   8736  -1228  -1243   -692       C  
ATOM   2721  CG  PHE A 455     -20.590 -12.834 -22.905  1.00 56.94           C  
ANISOU 2721  CG  PHE A 455     7014   5710   8909  -1311  -1063   -463       C  
ATOM   2722  CD1 PHE A 455     -21.878 -12.311 -22.843  1.00 57.99           C  
ANISOU 2722  CD1 PHE A 455     6930   5931   9173  -1436  -1098   -428       C  
ATOM   2723  CD2 PHE A 455     -19.794 -12.783 -21.772  1.00 55.74           C  
ANISOU 2723  CD2 PHE A 455     6902   5591   8685  -1251   -863   -289       C  
ATOM   2724  CE1 PHE A 455     -22.363 -11.754 -21.675  1.00 53.49           C  
ANISOU 2724  CE1 PHE A 455     6190   5480   8655  -1496   -913   -229       C  
ATOM   2725  CE2 PHE A 455     -20.274 -12.217 -20.599  1.00 56.41           C  
ANISOU 2725  CE2 PHE A 455     6836   5797   8801  -1314   -694    -92       C  
ATOM   2726  CZ  PHE A 455     -21.555 -11.702 -20.551  1.00 54.43           C  
ANISOU 2726  CZ  PHE A 455     6374   5634   8673  -1433   -707    -64       C  
ATOM   2727  N   ARG A 456     -19.498 -15.315 -26.587  1.00 63.94           N  
ANISOU 2727  N   ARG A 456     8473   6100   9722  -1139  -1640  -1184       N  
ATOM   2728  CA  ARG A 456     -19.324 -15.564 -28.014  1.00 64.77           C  
ANISOU 2728  CA  ARG A 456     8749   6164   9695  -1046  -1834  -1455       C  
ATOM   2729  C   ARG A 456     -20.246 -16.666 -28.539  1.00 64.84           C  
ANISOU 2729  C   ARG A 456     8766   5916   9954  -1204  -2080  -1613       C  
ATOM   2730  O   ARG A 456     -20.832 -16.541 -29.618  1.00 68.50           O  
ANISOU 2730  O   ARG A 456     9247   6457  10325  -1190  -2245  -1769       O  
ATOM   2731  CB  ARG A 456     -17.861 -15.922 -28.300  1.00 66.06           C  
ANISOU 2731  CB  ARG A 456     9138   6290   9674   -839  -1742  -1536       C  
ATOM   2732  CG  ARG A 456     -17.533 -16.087 -29.766  1.00 66.87           C  
ANISOU 2732  CG  ARG A 456     9442   6387   9580   -705  -1894  -1814       C  
ATOM   2733  CD  ARG A 456     -16.041 -16.242 -29.953  1.00 66.54           C  
ANISOU 2733  CD  ARG A 456     9577   6359   9345   -484  -1746  -1864       C  
ATOM   2734  N   ASN A 457     -20.381 -17.748 -27.779  1.00 65.55           N  
ANISOU 2734  N   ASN A 457     8832   5773  10299  -1322  -2034  -1513       N  
ATOM   2735  CA  ASN A 457     -21.242 -18.848 -28.201  1.00 67.46           C  
ANISOU 2735  CA  ASN A 457     9057   5852  10723  -1443  -2164  -1591       C  
ATOM   2736  C   ASN A 457     -22.713 -18.462 -28.089  1.00 69.49           C  
ANISOU 2736  C   ASN A 457     9057   6210  11135  -1624  -2227  -1514       C  
ATOM   2737  O   ASN A 457     -23.521 -18.834 -28.935  1.00 71.13           O  
ANISOU 2737  O   ASN A 457     9242   6397  11386  -1677  -2401  -1651       O  
ATOM   2738  CB  ASN A 457     -20.958 -20.106 -27.384  1.00 70.35           C  
ANISOU 2738  CB  ASN A 457     9476   5946  11310  -1512  -2078  -1483       C  
ATOM   2739  N   VAL A 458     -23.059 -17.704 -27.053  1.00 66.33           N  
ANISOU 2739  N   VAL A 458     8459   5927  10816  -1709  -2083  -1297       N  
ATOM   2740  CA  VAL A 458     -24.427 -17.214 -26.901  1.00 71.77           C  
ANISOU 2740  CA  VAL A 458     8883   6743  11642  -1853  -2112  -1218       C  
ATOM   2741  C   VAL A 458     -24.767 -16.249 -28.042  1.00 71.55           C  
ANISOU 2741  C   VAL A 458     8844   6927  11415  -1756  -2278  -1379       C  
ATOM   2742  O   VAL A 458     -25.875 -16.255 -28.570  1.00 71.90           O  
ANISOU 2742  O   VAL A 458     8759   7014  11548  -1834  -2417  -1436       O  
ATOM   2743  CB  VAL A 458     -24.629 -16.518 -25.540  1.00 71.62           C  
ANISOU 2743  CB  VAL A 458     8666   6833  11714  -1931  -1888   -952       C  
ATOM   2744  CG1 VAL A 458     -25.938 -15.731 -25.523  1.00 72.57           C  
ANISOU 2744  CG1 VAL A 458     8514   7142  11917  -2020  -1909   -900       C  
ATOM   2745  CG2 VAL A 458     -24.598 -17.542 -24.417  1.00 72.67           C  
ANISOU 2745  CG2 VAL A 458     8788   6767  12056  -2052  -1729   -763       C  
ATOM   2746  N   PHE A 459     -23.789 -15.432 -28.428  1.00 72.89           N  
ANISOU 2746  N   PHE A 459     9161   7224  11310  -1579  -2262  -1445       N  
ATOM   2747  CA  PHE A 459     -23.917 -14.566 -29.595  1.00 71.02           C  
ANISOU 2747  CA  PHE A 459     8976   7179  10829  -1455  -2409  -1594       C  
ATOM   2748  C   PHE A 459     -24.079 -15.385 -30.872  1.00 75.57           C  
ANISOU 2748  C   PHE A 459     9714   7664  11335  -1413  -2609  -1816       C  
ATOM   2749  O   PHE A 459     -25.098 -15.281 -31.554  1.00 75.69           O  
ANISOU 2749  O   PHE A 459     9636   7739  11382  -1460  -2776  -1885       O  
ATOM   2750  CB  PHE A 459     -22.696 -13.652 -29.708  1.00 72.45           C  
ANISOU 2750  CB  PHE A 459     9312   7494  10720  -1270  -2323  -1612       C  
ATOM   2751  CG  PHE A 459     -22.717 -12.734 -30.903  1.00 72.81           C  
ANISOU 2751  CG  PHE A 459     9444   7742  10477  -1126  -2445  -1737       C  
ATOM   2752  CD1 PHE A 459     -23.359 -11.503 -30.838  1.00 70.86           C  
ANISOU 2752  CD1 PHE A 459     9028   7701  10194  -1128  -2460  -1649       C  
ATOM   2753  CD2 PHE A 459     -22.067 -13.089 -32.081  1.00 73.02           C  
ANISOU 2753  CD2 PHE A 459     9729   7758  10259   -976  -2526  -1928       C  
ATOM   2754  CE1 PHE A 459     -23.366 -10.647 -31.927  1.00 67.69           C  
ANISOU 2754  CE1 PHE A 459     8721   7477   9519   -988  -2567  -1736       C  
ATOM   2755  CE2 PHE A 459     -22.074 -12.242 -33.176  1.00 71.60           C  
ANISOU 2755  CE2 PHE A 459     9643   7769   9791   -840  -2615  -2012       C  
ATOM   2756  CZ  PHE A 459     -22.724 -11.019 -33.100  1.00 70.45           C  
ANISOU 2756  CZ  PHE A 459     9337   7815   9614   -848  -2641  -1909       C  
ATOM   2757  N   ARG A 460     -23.071 -16.211 -31.166  1.00 76.62           N  
ANISOU 2757  N   ARG A 460    10085   7650  11380  -1318  -2589  -1927       N  
ATOM   2758  CA  ARG A 460     -22.989 -16.992 -32.405  1.00 76.54           C  
ANISOU 2758  CA  ARG A 460    10268   7556  11258  -1243  -2752  -2155       C  
ATOM   2759  C   ARG A 460     -24.276 -17.723 -32.767  1.00 84.23           C  
ANISOU 2759  C   ARG A 460    11123   8427  12453  -1403  -2936  -2214       C  
ATOM   2760  O   ARG A 460     -24.513 -18.013 -33.940  1.00 87.91           O  
ANISOU 2760  O   ARG A 460    11705   8895  12801  -1347  -3116  -2403       O  
ATOM   2761  CB  ARG A 460     -21.843 -18.011 -32.321  1.00 75.05           C  
ANISOU 2761  CB  ARG A 460    10295   7169  11050  -1156  -2666  -2225       C  
ATOM   2762  N   LYS A 461     -25.099 -18.039 -31.770  1.00 83.23           N  
ANISOU 2762  N   LYS A 461    10769   8211  12644  -1600  -2884  -2052       N  
ATOM   2763  CA  LYS A 461     -26.452 -18.493 -32.063  1.00 87.21           C  
ANISOU 2763  CA  LYS A 461    11108   8662  13367  -1760  -3050  -2087       C  
ATOM   2764  C   LYS A 461     -27.347 -17.256 -32.207  1.00 87.23           C  
ANISOU 2764  C   LYS A 461    10903   8910  13330  -1769  -3106  -2026       C  
ATOM   2765  O   LYS A 461     -28.175 -16.935 -31.351  1.00 88.70           O  
ANISOU 2765  O   LYS A 461    10828   9143  13730  -1904  -3024  -1855       O  
ATOM   2766  CB  LYS A 461     -26.965 -19.486 -31.002  1.00 86.86           C  
ANISOU 2766  CB  LYS A 461    10919   8405  13680  -1967  -2960  -1942       C  
ATOM   2767  CG  LYS A 461     -26.919 -19.020 -29.561  1.00 83.14           C  
ANISOU 2767  CG  LYS A 461    10278   7981  13332  -2044  -2713  -1674       C  
ATOM   2768  CD  LYS A 461     -27.899 -19.813 -28.711  1.00 84.54           C  
ANISOU 2768  CD  LYS A 461    10252   8012  13857  -2270  -2654  -1526       C  
ATOM   2769  CE  LYS A 461     -27.557 -21.288 -28.703  1.00 86.30           C  
ANISOU 2769  CE  LYS A 461    10635   7938  14219  -2327  -2680  -1581       C  
ATOM   2770  N   ALA A 462     -27.129 -16.547 -33.309  1.00 88.72           N  
ANISOU 2770  N   ALA A 462    11224   9261  13227  -1608  -3230  -2161       N  
ATOM   2771  CA  ALA A 462     -27.956 -15.419 -33.688  1.00 86.97           C  
ANISOU 2771  CA  ALA A 462    10848   9259  12938  -1585  -3324  -2133       C  
ATOM   2772  C   ALA A 462     -29.367 -15.895 -34.005  1.00 92.01           C  
ANISOU 2772  C   ALA A 462    11299   9842  13818  -1735  -3515  -2178       C  
ATOM   2773  O   ALA A 462     -30.305 -15.604 -33.267  1.00 95.93           O  
ANISOU 2773  O   ALA A 462    11516  10381  14552  -1865  -3466  -2034       O  
ATOM   2774  CB  ALA A 462     -27.355 -14.701 -34.881  1.00 86.10           C  
ANISOU 2774  CB  ALA A 462    10961   9307  12445  -1375  -3417  -2265       C  
TER    2775      ALA A 462                                                      
HETATM 2776  CAB AQD A1201     -16.765  11.793 -16.344  1.00 26.89           C  
HETATM 2777  OAR AQD A1201     -16.479  13.184 -16.085  1.00 31.19           O  
HETATM 2778  CAW AQD A1201     -15.615  13.449 -14.994  1.00 27.18           C  
HETATM 2779  CAK AQD A1201     -15.231  12.434 -14.098  1.00 32.67           C  
HETATM 2780  CAV AQD A1201     -14.376  12.763 -13.031  1.00 27.75           C  
HETATM 2781  NAP AQD A1201     -13.960  11.763 -12.096  1.00 31.76           N  
HETATM 2782  CAA AQD A1201     -14.651  10.489 -12.085  1.00 29.80           C  
HETATM 2783  CAU AQD A1201     -13.891  14.071 -12.887  1.00 35.13           C  
HETATM 2784 CLA  AQD A1201     -12.777  14.490 -11.593  1.00 41.84          CL  
HETATM 2785  CAL AQD A1201     -14.265  15.058 -13.780  1.00 32.20           C  
HETATM 2786  CAX AQD A1201     -15.118  14.748 -14.834  1.00 28.31           C  
HETATM 2787  CAS AQD A1201     -15.526  15.904 -15.744  1.00 33.92           C  
HETATM 2788  OAD AQD A1201     -14.929  16.950 -15.642  1.00 36.55           O  
HETATM 2789  NAQ AQD A1201     -16.638  15.809 -16.648  1.00 34.47           N  
HETATM 2790  CAZ AQD A1201     -16.997  16.959 -17.469  1.00 40.86           C  
HETATM 2791  CAY AQD A1201     -17.416  16.578 -18.817  1.00 51.93           C  
HETATM 2792  CAC AQD A1201     -16.699  15.290 -19.320  1.00 33.08           C  
HETATM 2793  CAM AQD A1201     -18.166  17.653 -16.797  1.00 41.57           C  
HETATM 2794  CAN AQD A1201     -19.349  17.390 -17.881  1.00 61.28           C  
HETATM 2795  NBA AQD A1201     -18.795  16.355 -18.773  1.00 60.99           N  
HETATM 2796  CAO AQD A1201     -19.331  16.401 -20.098  1.00 68.84           C  
HETATM 2797  CAT AQD A1201     -20.852  16.758 -20.138  1.00 54.50           C  
HETATM 2798  CAI AQD A1201     -21.259  18.001 -20.632  1.00 53.54           C  
HETATM 2799  CAG AQD A1201     -22.616  18.335 -20.665  1.00 59.38           C  
HETATM 2800  CAF AQD A1201     -23.565  17.421 -20.210  1.00 61.98           C  
HETATM 2801  CAH AQD A1201     -23.166  16.184 -19.721  1.00 69.04           C  
HETATM 2802  CAJ AQD A1201     -21.806  15.847 -19.682  1.00 58.81           C  
HETATM 2803  P   PO4 A1202     -20.076 -17.196  -3.851  1.00 55.90           P  
HETATM 2804  O1  PO4 A1202     -21.181 -16.493  -4.618  1.00 56.26           O  
HETATM 2805  O2  PO4 A1202     -19.786 -18.542  -4.468  1.00 53.71           O  
HETATM 2806  O3  PO4 A1202     -18.816 -16.372  -3.924  1.00 44.88           O  
HETATM 2807  O4  PO4 A1202     -20.489 -17.369  -2.407  1.00 54.31           O  
HETATM 2808  P   PO4 A1203      -0.005 -20.445 -21.044  0.50 65.76           P  
HETATM 2809  O1  PO4 A1203      -0.310 -19.573 -22.240  0.50 64.53           O  
HETATM 2810  O2  PO4 A1203       1.192 -21.317 -21.340  0.50 66.68           O  
HETATM 2811  O3  PO4 A1203      -1.197 -21.324 -20.746  0.50 66.67           O  
HETATM 2812  O4  PO4 A1203       0.293 -19.569 -19.849  0.50 64.51           O  
HETATM 2813  P   PO4 A1204     -33.844  11.443 -21.031  0.50 54.23           P  
HETATM 2814  O1  PO4 A1204     -33.585  10.565 -22.235  0.50 54.23           O  
HETATM 2815  O2  PO4 A1204     -35.052  12.320 -21.288  0.50 54.23           O  
HETATM 2816  O3  PO4 A1204     -32.635  12.318 -20.775  0.50 54.23           O  
HETATM 2817  O4  PO4 A1204     -34.105  10.566 -19.828  0.50 54.23           O  
HETATM 2818  C1  OLA A1205     -25.664 -12.774 -12.593  1.00 72.89           C  
HETATM 2819  O1  OLA A1205     -24.593 -12.950 -13.221  1.00 73.33           O  
HETATM 2820  O2  OLA A1205     -26.009 -13.630 -11.743  1.00 76.06           O  
HETATM 2821  C2  OLA A1205     -26.523 -11.555 -12.868  1.00 62.37           C  
HETATM 2822  C3  OLA A1205     -26.764 -10.728 -11.608  1.00 52.15           C  
HETATM 2823  C4  OLA A1205     -26.643  -9.238 -11.902  1.00 55.48           C  
HETATM 2824  C5  OLA A1205     -26.421  -8.462 -10.608  1.00 57.14           C  
HETATM 2825  C6  OLA A1205     -27.123  -7.111 -10.627  1.00 60.63           C  
HETATM 2826  C7  OLA A1205     -26.186  -5.995 -10.177  1.00 54.09           C  
HETATM 2827  C8  OLA A1205     -26.235  -4.791 -11.114  1.00 47.70           C  
HETATM 2828  C9  OLA A1205     -27.208  -3.755 -10.606  1.00 44.50           C  
HETATM 2829  C10 OLA A1205     -26.773  -2.546 -10.266  1.00 40.03           C  
HETATM 2830  C11 OLA A1205     -27.319  -1.312 -10.938  1.00 35.88           C  
HETATM 2831  C12 OLA A1205     -27.373  -0.200  -9.897  1.00 41.42           C  
HETATM 2832  C13 OLA A1205     -27.987   1.076 -10.452  1.00 43.84           C  
HETATM 2833  C14 OLA A1205     -27.630   2.237  -9.531  1.00 45.82           C  
HETATM 2834  C15 OLA A1205     -28.530   3.442  -9.772  1.00 55.54           C  
HETATM 2835  C1  OLA A1206     -17.334  19.034 -31.555  1.00 99.28           C  
HETATM 2836  O1  OLA A1206     -17.330  19.410 -32.747  1.00105.51           O  
HETATM 2837  O2  OLA A1206     -17.618  19.856 -30.656  1.00105.04           O  
HETATM 2838  C2  OLA A1206     -16.998  17.606 -31.210  1.00 79.86           C  
HETATM 2839  C3  OLA A1206     -16.754  16.813 -32.487  1.00 66.97           C  
HETATM 2840  C4  OLA A1206     -17.387  15.434 -32.369  1.00 52.94           C  
HETATM 2841  C5  OLA A1206     -16.516  14.348 -32.983  1.00 57.15           C  
HETATM 2842  C6  OLA A1206     -17.333  13.075 -33.197  1.00 51.34           C  
HETATM 2843  C7  OLA A1206     -16.780  11.899 -32.399  1.00 43.21           C  
HETATM 2844  C8  OLA A1206     -17.698  10.694 -32.554  1.00 44.16           C  
HETATM 2845  C9  OLA A1206     -17.170   9.496 -31.798  1.00 48.27           C  
HETATM 2846  C10 OLA A1206     -17.994   8.459 -31.599  1.00 49.02           C  
HETATM 2847  C11 OLA A1206     -18.157   7.440 -32.702  1.00 46.78           C  
HETATM 2848  C12 OLA A1206     -18.298   6.032 -32.135  1.00 51.42           C  
HETATM 2849  C13 OLA A1206     -19.777   5.665 -32.030  1.00 47.86           C  
HETATM 2850  C14 OLA A1206     -20.197   4.721 -33.147  1.00 52.84           C  
HETATM 2851  C15 OLA A1206     -20.488   3.331 -32.593  1.00 43.07           C  
HETATM 2852  C1  OLA A1207     -13.735  19.273 -31.056  1.00103.20           C  
HETATM 2853  O1  OLA A1207     -14.378  19.425 -32.117  1.00112.35           O  
HETATM 2854  O2  OLA A1207     -13.879  20.128 -30.152  1.00 98.09           O  
HETATM 2855  C2  OLA A1207     -12.801  18.089 -30.885  1.00 92.94           C  
HETATM 2856  C3  OLA A1207     -13.596  16.810 -30.629  1.00 80.87           C  
HETATM 2857  C4  OLA A1207     -13.425  15.775 -31.735  1.00 66.30           C  
HETATM 2858  C5  OLA A1207     -12.217  14.889 -31.480  1.00 50.07           C  
HETATM 2859  C6  OLA A1207     -12.375  13.552 -32.176  1.00 46.47           C  
HETATM 2860  C7  OLA A1207     -12.954  12.518 -31.218  1.00 40.27           C  
HETATM 2861  C8  OLA A1207     -12.356  11.153 -31.517  1.00 36.49           C  
HETATM 2862  C9  OLA A1207     -12.614  10.189 -30.380  1.00 34.97           C  
HETATM 2863  C10 OLA A1207     -13.121   8.975 -30.621  1.00 36.20           C  
HETATM 2864  C11 OLA A1207     -12.284   7.933 -31.331  1.00 46.24           C  
HETATM 2865  C12 OLA A1207     -12.448   6.594 -30.628  1.00 53.31           C  
HETATM 2866  C13 OLA A1207     -11.611   5.500 -31.283  1.00 50.02           C  
HETATM 2867  C14 OLA A1207     -12.325   4.155 -31.199  1.00 46.12           C  
HETATM 2868  C15 OLA A1207     -11.304   3.030 -31.041  1.00 55.66           C  
HETATM 2869  C1  OLA A1208     -16.063  10.947   1.992  1.00 60.84           C  
HETATM 2870  O1  OLA A1208     -15.657  12.078   2.362  1.00 50.74           O  
HETATM 2871  O2  OLA A1208     -16.690  10.237   2.812  1.00 65.11           O  
HETATM 2872  C2  OLA A1208     -15.820  10.480   0.571  1.00 51.60           C  
HETATM 2873  C3  OLA A1208     -15.293   9.046   0.524  1.00 45.64           C  
HETATM 2874  C4  OLA A1208     -14.274   8.892  -0.607  1.00 48.05           C  
HETATM 2875  C5  OLA A1208     -13.409   7.657  -0.405  1.00 51.34           C  
HETATM 2876  C6  OLA A1208     -13.325   6.776  -1.652  1.00 47.47           C  
HETATM 2877  C7  OLA A1208     -11.981   6.048  -1.736  1.00 50.30           C  
HETATM 2878  C8  OLA A1208     -11.726   5.496  -3.142  1.00 48.14           C  
HETATM 2879  C9  OLA A1208     -10.465   4.663  -3.205  1.00 48.02           C  
HETATM 2880  C10 OLA A1208     -10.353   3.729  -4.154  1.00 45.94           C  
HETATM 2881  C11 OLA A1208     -10.145   2.268  -3.828  1.00 55.85           C  
HETATM 2882  C12 OLA A1208     -11.053   1.404  -4.707  1.00 45.63           C  
HETATM 2883  C13 OLA A1208     -12.466   1.251  -4.131  1.00 43.28           C  
HETATM 2884  C14 OLA A1208     -13.194   0.123  -4.865  1.00 34.91           C  
HETATM 2885  C15 OLA A1208     -14.443  -0.361  -4.131  1.00 35.18           C  
HETATM 2886  C1  OLA A1209     -17.264 -12.964 -33.470  1.00 93.42           C  
HETATM 2887  O1  OLA A1209     -18.255 -13.494 -32.921  1.00 97.06           O  
HETATM 2888  O2  OLA A1209     -16.152 -13.530 -33.387  1.00 90.76           O  
HETATM 2889  C2  OLA A1209     -17.411 -11.659 -34.221  1.00 90.38           C  
HETATM 2890  C3  OLA A1209     -18.038 -10.604 -33.318  1.00 80.15           C  
HETATM 2891  C4  OLA A1209     -17.242  -9.303 -33.364  1.00 72.06           C  
HETATM 2892  C5  OLA A1209     -17.782  -8.345 -34.422  1.00 68.55           C  
HETATM 2893  C6  OLA A1209     -18.485  -7.154 -33.774  1.00 63.43           C  
HETATM 2894  C7  OLA A1209     -19.885  -7.567 -33.336  1.00 63.48           C  
HETATM 2895  C8  OLA A1209     -20.615  -6.445 -32.607  1.00 59.59           C  
HETATM 2896  C9  OLA A1209     -21.647  -7.079 -31.707  1.00 57.29           C  
HETATM 2897  C10 OLA A1209     -21.621  -6.844 -30.398  1.00 57.16           C  
HETATM 2898  C11 OLA A1209     -22.663  -5.941 -29.782  1.00 54.95           C  
HETATM 2899  C12 OLA A1209     -23.218  -6.622 -28.540  1.00 53.45           C  
HETATM 2900  C13 OLA A1209     -23.366  -8.110 -28.798  1.00 56.12           C  
HETATM 2901  C14 OLA A1209     -24.201  -8.767 -27.713  1.00 52.33           C  
HETATM 2902  C15 OLA A1209     -23.382  -8.939 -26.443  1.00 47.51           C  
HETATM 2903  C16 OLA A1209     -23.889 -10.144 -25.666  1.00 55.13           C  
HETATM 2904  C17 OLA A1209     -23.642 -11.417 -26.464  1.00 59.13           C  
HETATM 2905  C18 OLA A1209     -24.964 -12.103 -26.794  1.00 57.72           C  
HETATM 2906  C1  OLA A1210      -1.628 -15.037 -16.997  1.00 73.35           C  
HETATM 2907  O1  OLA A1210      -2.350 -15.789 -17.694  1.00 64.99           O  
HETATM 2908  O2  OLA A1210      -0.994 -15.507 -16.018  1.00 72.02           O  
HETATM 2909  C2  OLA A1210      -1.529 -13.569 -17.343  1.00 70.92           C  
HETATM 2910  C3  OLA A1210      -2.808 -13.134 -18.053  1.00 67.91           C  
HETATM 2911  C4  OLA A1210      -2.516 -12.053 -19.085  1.00 64.64           C  
HETATM 2912  C5  OLA A1210      -1.923 -10.822 -18.414  1.00 63.86           C  
HETATM 2913  C6  OLA A1210      -2.861 -10.259 -17.347  1.00 70.74           C  
HETATM 2914  C7  OLA A1210      -2.107  -9.777 -16.107  1.00 68.94           C  
HETATM 2915  C8  OLA A1210      -3.033  -9.025 -15.149  1.00 55.95           C  
HETATM 2916  C9  OLA A1210      -3.288  -7.613 -15.632  1.00 58.74           C  
HETATM 2917  C10 OLA A1210      -4.446  -7.310 -16.224  1.00 55.58           C  
HETATM 2918  C11 OLA A1210      -4.725  -5.908 -16.701  1.00 29.01           C  
HETATM 2919  C12 OLA A1210      -4.017  -5.664 -18.034  1.00 41.83           C  
HETATM 2920  C13 OLA A1210      -3.643  -4.193 -18.168  1.00 38.94           C  
HETATM 2921  C14 OLA A1210      -3.625  -3.752 -19.630  1.00 48.59           C  
HETATM 2922  C15 OLA A1210      -2.683  -2.575 -19.840  1.00 53.94           C  
HETATM 2923  C16 OLA A1210      -2.607  -2.192 -21.317  1.00 55.89           C  
HETATM 2924  C17 OLA A1210      -3.280  -0.848 -21.566  1.00 52.72           C  
HETATM 2925  C18 OLA A1210      -2.733   0.219 -20.623  1.00 59.37           C  
HETATM 2926  C1  OLA A1211      -5.599 -19.769   4.106  1.00 71.40           C  
HETATM 2927  O1  OLA A1211      -4.640 -19.061   4.481  1.00 71.00           O  
HETATM 2928  O2  OLA A1211      -5.681 -20.933   4.561  1.00 76.30           O  
HETATM 2929  C2  OLA A1211      -6.625 -19.232   3.125  1.00 64.03           C  
HETATM 2930  C3  OLA A1211      -7.005 -17.799   3.496  1.00 46.11           C  
HETATM 2931  C4  OLA A1211      -6.242 -16.802   2.625  1.00 49.50           C  
HETATM 2932  C5  OLA A1211      -6.181 -15.392   3.218  1.00 41.17           C  
HETATM 2933  C6  OLA A1211      -6.172 -14.379   2.081  1.00 47.05           C  
HETATM 2934  C7  OLA A1211      -6.592 -12.972   2.489  1.00 45.88           C  
HETATM 2935  C8  OLA A1211      -7.275 -12.304   1.298  1.00 52.96           C  
HETATM 2936  C9  OLA A1211      -7.503 -10.828   1.511  1.00 56.39           C  
HETATM 2937  C10 OLA A1211      -7.513 -10.026   0.446  1.00 51.71           C  
HETATM 2938  C11 OLA A1211      -8.467  -8.865   0.330  1.00 51.29           C  
HETATM 2939  C12 OLA A1211      -7.697  -7.694  -0.277  1.00 51.27           C  
HETATM 2940  C13 OLA A1211      -8.563  -6.443  -0.340  1.00 59.79           C  
HETATM 2941  C14 OLA A1211      -8.018  -5.456  -1.364  1.00 55.97           C  
HETATM 2942  C1  OLA A1212      -8.142 -12.470 -31.173  1.00 73.95           C  
HETATM 2943  O1  OLA A1212      -7.043 -12.678 -31.735  1.00 78.24           O  
HETATM 2944  O2  OLA A1212      -8.672 -13.394 -30.510  1.00 68.02           O  
HETATM 2945  C2  OLA A1212      -8.809 -11.118 -31.286  1.00 74.20           C  
HETATM 2946  C3  OLA A1212      -8.003 -10.221 -32.222  1.00 69.78           C  
HETATM 2947  C4  OLA A1212      -8.807  -9.012 -32.705  1.00 69.93           C  
HETATM 2948  C5  OLA A1212      -8.779  -7.843 -31.721  1.00 73.84           C  
HETATM 2949  C6  OLA A1212      -9.544  -6.634 -32.256  1.00 75.04           C  
HETATM 2950  C7  OLA A1212     -10.414  -6.011 -31.169  1.00 82.64           C  
HETATM 2951  C8  OLA A1212      -9.776  -4.763 -30.563  1.00 78.49           C  
HETATM 2952  C9  OLA A1212     -10.624  -4.268 -29.410  1.00 75.19           C  
HETATM 2953  C10 OLA A1212     -10.168  -3.345 -28.557  1.00 67.33           C  
HETATM 2954  C11 OLA A1212      -9.836  -3.709 -27.127  1.00 54.78           C  
HETATM 2955  C12 OLA A1212      -8.674  -2.854 -26.633  1.00 53.68           C  
HETATM 2956  C13 OLA A1212      -7.614  -3.723 -25.969  1.00 55.64           C  
HETATM 2957  C14 OLA A1212      -6.979  -3.019 -24.779  1.00 52.26           C  
HETATM 2958  C15 OLA A1212      -5.594  -3.577 -24.468  1.00 49.20           C  
HETATM 2959  C16 OLA A1212      -5.639  -5.071 -24.160  1.00 51.39           C  
HETATM 2960  C17 OLA A1212      -4.493  -5.504 -23.246  1.00 45.62           C  
HETATM 2961  C18 OLA A1212      -4.379  -7.032 -23.163  1.00 40.45           C  
HETATM 2962  C1  OLA A1213       3.571  20.957 -10.907  1.00 78.74           C  
HETATM 2963  O1  OLA A1213       4.492  20.287 -11.428  1.00 77.39           O  
HETATM 2964  O2  OLA A1213       3.862  21.728  -9.967  1.00 83.85           O  
HETATM 2965  C2  OLA A1213       2.141  20.847 -11.400  1.00 68.60           C  
HETATM 2966  C3  OLA A1213       1.941  19.497 -12.083  1.00 60.43           C  
HETATM 2967  C4  OLA A1213       1.297  19.648 -13.459  1.00 51.66           C  
HETATM 2968  C5  OLA A1213       1.264  18.343 -14.263  1.00 48.95           C  
HETATM 2969  C6  OLA A1213       0.920  17.113 -13.425  1.00 47.34           C  
HETATM 2970  C7  OLA A1213       0.005  16.160 -14.197  1.00 48.50           C  
HETATM 2971  C8  OLA A1213       0.552  14.749 -14.337  1.00 52.53           C  
HETATM 2972  C9  OLA A1213      -0.275  13.801 -13.494  1.00 49.60           C  
HETATM 2973  C10 OLA A1213      -0.675  12.625 -13.990  1.00 39.86           C  
HETATM 2974  C11 OLA A1213       0.343  11.545 -14.277  1.00 50.63           C  
HETATM 2975  C12 OLA A1213      -0.324  10.175 -14.253  1.00 57.34           C  
HETATM 2976  C13 OLA A1213       0.571   9.108 -14.876  1.00 66.27           C  
HETATM 2977  C14 OLA A1213      -0.212   8.140 -15.761  1.00 54.32           C  
HETATM 2978  C15 OLA A1213      -1.065   7.171 -14.944  1.00 60.74           C  
HETATM 2979  C16 OLA A1213      -1.138   5.801 -15.621  1.00 57.57           C  
HETATM 2980  C17 OLA A1213      -2.488   5.105 -15.437  1.00 52.98           C  
HETATM 2981  C18 OLA A1213      -2.727   4.667 -13.992  1.00 43.02           C  
HETATM 2982  C1  PEG A1214      -2.839  13.876 -24.342  1.00 69.35           C  
HETATM 2983  O1  PEG A1214      -2.966  12.463 -24.079  1.00 67.16           O  
HETATM 2984  C2  PEG A1214      -1.881  14.701 -23.429  1.00 49.71           C  
HETATM 2985  O2  PEG A1214      -1.898  15.993 -23.575  1.00 66.75           O  
HETATM 2986  C3  PEG A1214      -1.162  16.862 -22.656  1.00 53.97           C  
HETATM 2987  C4  PEG A1214      -1.710  18.285 -22.420  1.00 58.22           C  
HETATM 2988  O4  PEG A1214      -0.940  19.206 -21.773  1.00 47.00           O  
HETATM 2989  C1  PEG A1215      -1.946  14.864  -6.755  1.00 49.91           C  
HETATM 2990  O1  PEG A1215      -1.353  13.674  -7.319  1.00 60.64           O  
HETATM 2991  C2  PEG A1215      -1.208  15.564  -5.570  1.00 90.06           C  
HETATM 2992  O2  PEG A1215      -1.114  16.854  -5.598  1.00 90.65           O  
HETATM 2993  C3  PEG A1215       0.004  17.504  -4.926  1.00 90.86           C  
HETATM 2994  C4  PEG A1215       0.691  18.703  -5.610  1.00 83.59           C  
HETATM 2995  O4  PEG A1215       1.773  18.460  -6.397  1.00 74.58           O  
HETATM 2996  C1  PEG A1216     -25.102  10.936  -5.613  1.00 56.65           C  
HETATM 2997  O1  PEG A1216     -25.469  11.640  -4.407  1.00 49.20           O  
HETATM 2998  C2  PEG A1216     -24.794  11.791  -6.881  1.00 45.88           C  
HETATM 2999  O2  PEG A1216     -25.223  11.363  -8.026  1.00 54.82           O  
HETATM 3000  C3  PEG A1216     -26.648  11.362  -8.325  1.00 53.24           C  
HETATM 3001  C4  PEG A1216     -27.234  12.573  -9.069  1.00 56.09           C  
HETATM 3002  O4  PEG A1216     -28.539  12.513  -9.449  1.00 58.91           O  
HETATM 3003  C1  PEG A1217     -29.048  13.657 -28.802  1.00 57.52           C  
HETATM 3004  O1  PEG A1217     -29.251  15.049 -29.116  1.00 54.10           O  
HETATM 3005  C2  PEG A1217     -30.212  12.679 -29.145  1.00 65.39           C  
HETATM 3006  O2  PEG A1217     -30.144  11.460 -28.725  1.00 65.94           O  
HETATM 3007  C3  PEG A1217     -30.046  10.351 -29.672  1.00 58.10           C  
HETATM 3008  C4  PEG A1217     -30.774   9.037 -29.317  1.00 61.57           C  
HETATM 3009  O4  PEG A1217     -30.582   7.934 -30.094  1.00 59.13           O  
HETATM 3010  C1  PEG A1218     -35.661  -5.405 -14.133  1.00 59.15           C  
HETATM 3011  O1  PEG A1218     -35.258  -4.077 -14.523  1.00 61.23           O  
HETATM 3012  C2  PEG A1218     -35.656  -6.532 -15.219  1.00 85.22           C  
HETATM 3013  O2  PEG A1218     -34.528  -7.097 -15.519  1.00 80.53           O  
HETATM 3014  C3  PEG A1218     -34.442  -8.548 -15.630  1.00 73.26           C  
HETATM 3015  C4  PEG A1218     -34.725  -9.380 -14.366  1.00 65.45           C  
HETATM 3016  O4  PEG A1218     -34.447 -10.706 -14.415  1.00 70.12           O  
HETATM 3017  C1  PEG A1219     -33.159  24.326 -17.642  1.00 58.92           C  
HETATM 3018  O1  PEG A1219     -34.049  25.339 -18.162  1.00 69.72           O  
HETATM 3019  C2  PEG A1219     -33.780  23.240 -16.709  1.00 65.39           C  
HETATM 3020  O2  PEG A1219     -34.520  22.315 -17.241  1.00 68.31           O  
HETATM 3021  C3  PEG A1219     -34.959  21.206 -16.405  1.00 51.94           C  
HETATM 3022  C4  PEG A1219     -35.211  19.850 -17.078  1.00 57.66           C  
HETATM 3023  O4  PEG A1219     -35.470  18.796 -16.265  1.00 62.29           O  
HETATM 3024  C1  PEG A1220     -33.781  24.528 -12.801  1.00 68.07           C  
HETATM 3025  O1  PEG A1220     -32.817  25.246 -12.000  1.00 66.58           O  
HETATM 3026  C2  PEG A1220     -34.245  23.122 -12.303  1.00 67.82           C  
HETATM 3027  O2  PEG A1220     -33.739  22.079 -12.880  1.00 77.05           O  
HETATM 3028  C3  PEG A1220     -33.031  21.079 -12.088  1.00 70.25           C  
HETATM 3029  C4  PEG A1220     -33.048  19.622 -12.585  1.00 62.07           C  
HETATM 3030  O4  PEG A1220     -32.445  18.656 -11.839  1.00 49.50           O  
HETATM 3031  C1  PEG A1221     -26.247   4.629  -5.240  1.00 39.74           C  
HETATM 3032  O1  PEG A1221     -26.929   5.818  -4.789  1.00 44.86           O  
HETATM 3033  C2  PEG A1221     -27.128   3.536  -5.928  1.00 73.93           C  
HETATM 3034  O2  PEG A1221     -27.267   2.398  -5.323  1.00 71.73           O  
HETATM 3035  C3  PEG A1221     -27.657   1.229  -6.094  1.00 62.34           C  
HETATM 3036  C4  PEG A1221     -27.197  -0.153  -5.602  1.00 62.40           C  
HETATM 3037  O4  PEG A1221     -27.415  -1.215  -6.424  1.00 68.34           O  
HETATM 3038  C1  PEG A1222      -1.862  14.298   0.897  1.00 64.98           C  
HETATM 3039  O1  PEG A1222      -2.298  15.659   0.718  1.00 60.91           O  
HETATM 3040  C2  PEG A1222      -1.693  13.449  -0.397  1.00 69.48           C  
HETATM 3041  O2  PEG A1222      -2.571  13.643  -1.322  1.00 73.17           O  
HETATM 3042  C3  PEG A1222      -2.853  12.580  -2.278  1.00 71.88           C  
HETATM 3043  C4  PEG A1222      -1.792  12.238  -3.339  1.00 67.51           C  
HETATM 3044  O4  PEG A1222      -1.879  11.017  -3.931  1.00 69.24           O  
HETATM 3045  C1  GOL A1223     -16.192 -18.106  -5.680  1.00 66.48           C  
HETATM 3046  O1  GOL A1223     -16.297 -16.733  -5.359  1.00 71.83           O  
HETATM 3047  C2  GOL A1223     -16.781 -18.333  -7.055  1.00 53.80           C  
HETATM 3048  O2  GOL A1223     -15.730 -18.409  -7.989  1.00 45.74           O  
HETATM 3049  C3  GOL A1223     -17.549 -19.630  -7.137  1.00 58.49           C  
HETATM 3050  O3  GOL A1223     -18.798 -19.408  -6.524  1.00 55.92           O  
HETATM 3051  O   HOH A1301      -0.720  21.147 -21.302  0.90 49.71           O  
HETATM 3052  O   HOH A1302      -7.457 -27.814 -20.093  1.00 55.76           O  
HETATM 3053  O   HOH A1303       1.127 -36.613 -19.447  1.00 48.86           O  
HETATM 3054  O   HOH A1304       1.261 -24.559 -12.641  1.00 54.10           O  
HETATM 3055  O   HOH A1305     -33.908 -51.360 -12.871  1.00 52.37           O  
HETATM 3056  O   HOH A1306     -21.474 -44.599  -1.531  1.00 64.87           O  
HETATM 3057  O   HOH A1307     -20.392  -4.845 -19.083  1.00 43.78           O  
HETATM 3058  O   HOH A1308      -4.601 -37.447 -14.681  1.00 50.68           O  
HETATM 3059  O   HOH A1309     -13.560 -17.194  -1.349  1.00 48.13           O  
HETATM 3060  O   HOH A1310     -19.881  19.775 -24.400  1.00 56.31           O  
HETATM 3061  O   HOH A1311     -17.372 -13.900 -17.597  1.00 50.18           O  
HETATM 3062  O   HOH A1312     -15.609  19.495 -24.650  1.00 53.00           O  
HETATM 3063  O   HOH A1313     -17.872  20.168 -20.250  1.00 54.75           O  
HETATM 3064  O   HOH A1314     -23.516 -13.513  -8.264  1.00 52.49           O  
HETATM 3065  O   HOH A1315     -12.908  20.579 -15.092  1.00 50.29           O  
HETATM 3066  O   HOH A1316     -13.560  22.113 -28.562  1.00 54.57           O  
HETATM 3067  O   HOH A1317     -14.449 -14.284 -17.042  1.00 52.86           O  
HETATM 3068  O   HOH A1318      -9.627   9.854 -22.844  1.00 29.91           O  
HETATM 3069  O   HOH A1319     -17.861 -15.925 -15.725  1.00 51.03           O  
HETATM 3070  O   HOH A1320      -4.949  24.369 -17.955  1.00 44.18           O  
HETATM 3071  O   HOH A1321     -20.717  22.725 -21.784  1.00 56.68           O  
HETATM 3072  O   HOH A1322     -33.425 -44.015 -16.091  1.00 58.80           O  
HETATM 3073  O   HOH A1323     -19.966  25.335 -15.316  1.00 57.25           O  
HETATM 3074  O   HOH A1324     -16.653  12.939  -1.642  1.00 41.29           O  
HETATM 3075  O   HOH A1325     -27.144 -21.143 -20.551  1.00 62.52           O  
HETATM 3076  O   HOH A1326     -14.979  19.541 -16.261  1.00 37.53           O  
HETATM 3077  O   HOH A1327     -25.597 -50.402  -4.700  1.00 57.39           O  
HETATM 3078  O   HOH A1328     -13.487  -1.331 -20.882  1.00 39.71           O  
HETATM 3079  O   HOH A1329      -5.372 -20.588  -3.464  1.00 55.52           O  
HETATM 3080  O   HOH A1330     -21.212  21.485  -8.918  1.00 40.14           O  
HETATM 3081  O   HOH A1331     -23.469  24.465 -12.580  1.00 52.28           O  
HETATM 3082  O   HOH A1332     -12.438 -49.593 -13.087  1.00 48.04           O  
HETATM 3083  O   HOH A1333      -6.902  24.254 -19.905  1.00 50.48           O  
HETATM 3084  O   HOH A1334     -11.569  24.847  -4.971  1.00 59.04           O  
HETATM 3085  O   HOH A1335     -10.916 -48.959 -10.905  1.00 54.76           O  
HETATM 3086  O   HOH A1336     -22.157  24.878  -9.267  1.00 54.13           O  
HETATM 3087  O   HOH A1337      -6.013 -42.753  -6.870  1.00 59.94           O  
HETATM 3088  O   HOH A1338     -17.682   5.782 -20.452  1.00 41.50           O  
HETATM 3089  O   HOH A1339     -22.109  -1.626 -27.265  1.00 46.18           O  
HETATM 3090  O   HOH A1340     -20.350  -2.452 -20.233  1.00 44.70           O  
HETATM 3091  O   HOH A1341     -30.040 -45.715  -7.330  1.00 57.99           O  
HETATM 3092  O   HOH A1342       0.012 -27.388 -17.429  1.00 51.25           O  
HETATM 3093  O   HOH A1343     -16.208 -17.409 -19.044  1.00 57.09           O  
HETATM 3094  O   HOH A1344     -20.565 -48.842 -22.231  1.00 47.83           O  
HETATM 3095  O   HOH A1345     -28.530  13.867 -20.806  1.00 42.65           O  
HETATM 3096  O   HOH A1346      -6.707 -22.152 -13.912  1.00 46.62           O  
HETATM 3097  O   HOH A1347       1.536 -31.146 -11.699  1.00 57.37           O  
HETATM 3098  O   HOH A1348      -3.193  25.655 -25.454  1.00 43.89           O  
HETATM 3099  O   HOH A1349     -25.159  15.614  -2.543  1.00 41.02           O  
HETATM 3100  O   HOH A1350      -4.627 -21.709 -17.869  1.00 50.37           O  
HETATM 3101  O   HOH A1351     -21.875  25.851 -13.672  1.00 58.76           O  
HETATM 3102  O   HOH A1352     -23.854 -15.543  -4.907  1.00 51.43           O  
HETATM 3103  O   HOH A1353      -3.244 -27.676 -15.933  1.00 47.31           O  
HETATM 3104  O   HOH A1354      -2.706 -35.266 -14.721  1.00 46.56           O  
HETATM 3105  O   HOH A1355      -9.273 -41.381 -18.361  1.00 49.20           O  
HETATM 3106  O   HOH A1356     -19.083   9.500 -17.034  1.00 36.83           O  
HETATM 3107  O   HOH A1357     -24.900  26.197  -8.974  1.00 63.86           O  
HETATM 3108  O   HOH A1358     -17.230 -16.272 -12.113  1.00 51.19           O  
HETATM 3109  O   HOH A1359     -15.615  -0.939 -18.403  1.00 48.52           O  
HETATM 3110  O   HOH A1360     -13.328  21.874 -24.706  1.00 44.67           O  
HETATM 3111  O   HOH A1361     -13.835 -14.951 -14.486  1.00 49.16           O  
HETATM 3112  O   HOH A1362     -18.773 -15.447 -19.399  1.00 50.28           O  
HETATM 3113  O   HOH A1363     -19.097 -42.710  -1.319  1.00 61.93           O  
HETATM 3114  O   HOH A1364     -20.303   4.417 -17.364  1.00 42.41           O  
HETATM 3115  O   HOH A1365      -5.469 -22.206   7.133  1.00 56.07           O  
HETATM 3116  O   HOH A1366      -9.913  19.902 -15.070  1.00 36.18           O  
HETATM 3117  O   HOH A1367     -15.007 -14.325  -4.067  1.00 50.20           O  
HETATM 3118  O   HOH A1368     -33.229 -43.814 -13.530  1.00 53.98           O  
HETATM 3119  O   HOH A1369     -30.387  26.756 -11.612  1.00 59.89           O  
HETATM 3120  O   HOH A1370     -24.666 -42.442  -6.388  1.00 62.81           O  
HETATM 3121  O   HOH A1371     -26.126 -20.392   0.781  1.00 61.55           O  
HETATM 3122  O   HOH A1372     -10.821  26.016  -7.900  1.00 42.17           O  
HETATM 3123  O   HOH A1373     -13.881 -19.656  -3.090  1.00 57.88           O  
HETATM 3124  O   HOH A1374      -6.976  25.772 -21.837  1.00 44.12           O  
HETATM 3125  O   HOH A1375      -0.663 -28.884 -22.087  1.00 53.02           O  
HETATM 3126  O   HOH A1376     -16.500   3.901 -19.319  1.00 41.65           O  
HETATM 3127  O   HOH A1377      -0.648 -34.686 -19.634  1.00 43.97           O  
HETATM 3128  O   HOH A1378       0.992 -33.345 -13.266  1.00 52.25           O  
HETATM 3129  O   HOH A1379     -35.142   9.302 -17.348  1.00 56.82           O  
HETATM 3130  O   HOH A1380     -23.546 -27.947   9.292  1.00 68.56           O  
HETATM 3131  O   HOH A1381     -27.876 -41.805 -15.761  1.00 57.09           O  
HETATM 3132  O   HOH A1382      -3.467 -19.811  -4.767  1.00 60.90           O  
HETATM 3133  O   HOH A1383     -13.247 -17.596 -22.557  1.00 56.27           O  
HETATM 3134  O   HOH A1384      -0.904 -37.921 -15.133  1.00 58.06           O  
HETATM 3135  O   HOH A1385     -23.867 -12.714  -5.645  1.00 46.81           O  
HETATM 3136  O   HOH A1386     -14.382  19.326 -19.244  1.00 44.46           O  
HETATM 3137  O   HOH A1387     -16.691  21.605 -27.795  1.00 62.46           O  
HETATM 3138  O   HOH A1388     -11.509  23.106 -20.463  1.00 48.90           O  
HETATM 3139  O   HOH A1389     -32.139 -45.280 -20.943  1.00 67.00           O  
HETATM 3140  O   HOH A1390     -12.328  21.241 -18.798  1.00 45.29           O  
HETATM 3141  O   HOH A1391     -10.175 -52.147  -7.660  1.00 70.74           O  
HETATM 3142  O   HOH A1392      -0.487  27.423 -12.873  1.00 47.68           O  
HETATM 3143  O   HOH A1393      -0.001 -31.898 -21.032  0.50 36.22           O  
HETATM 3144  O   HOH A1394     -10.008 -27.870 -23.056  1.00 68.73           O  
HETATM 3145  O   HOH A1395      -9.849  21.928 -13.438  1.00 48.90           O  
HETATM 3146  O   HOH A1396      -8.657 -43.640 -16.955  1.00 53.85           O  
HETATM 3147  O   HOH A1397     -18.627   6.690 -17.902  1.00 40.13           O  
HETATM 3148  O   HOH A1398     -12.063  23.493 -22.878  1.00 44.98           O  
CONECT  522 1052                                                                
CONECT 1052  522                                                                
CONECT 2459 2477                                                                
CONECT 2477 2459                                                                
CONECT 2776 2777                                                                
CONECT 2777 2776 2778                                                           
CONECT 2778 2777 2779 2786                                                      
CONECT 2779 2778 2780                                                           
CONECT 2780 2779 2781 2783                                                      
CONECT 2781 2780 2782                                                           
CONECT 2782 2781                                                                
CONECT 2783 2780 2784 2785                                                      
CONECT 2784 2783                                                                
CONECT 2785 2783 2786                                                           
CONECT 2786 2778 2785 2787                                                      
CONECT 2787 2786 2788 2789                                                      
CONECT 2788 2787                                                                
CONECT 2789 2787 2790                                                           
CONECT 2790 2789 2791 2793                                                      
CONECT 2791 2790 2792 2795                                                      
CONECT 2792 2791                                                                
CONECT 2793 2790 2794                                                           
CONECT 2794 2793 2795                                                           
CONECT 2795 2791 2794 2796                                                      
CONECT 2796 2795 2797                                                           
CONECT 2797 2796 2798 2802                                                      
CONECT 2798 2797 2799                                                           
CONECT 2799 2798 2800                                                           
CONECT 2800 2799 2801                                                           
CONECT 2801 2800 2802                                                           
CONECT 2802 2797 2801                                                           
CONECT 2803 2804 2805 2806 2807                                                 
CONECT 2804 2803                                                                
CONECT 2805 2803                                                                
CONECT 2806 2803                                                                
CONECT 2807 2803                                                                
CONECT 2808 2809 2810 2811 2812                                                 
CONECT 2809 2808                                                                
CONECT 2810 2808                                                                
CONECT 2811 2808                                                                
CONECT 2812 2808                                                                
CONECT 2813 2814 2815 2816 2817                                                 
CONECT 2814 2813                                                                
CONECT 2815 2813                                                                
CONECT 2816 2813                                                                
CONECT 2817 2813                                                                
CONECT 2818 2819 2820 2821                                                      
CONECT 2819 2818                                                                
CONECT 2820 2818                                                                
CONECT 2821 2818 2822                                                           
CONECT 2822 2821 2823                                                           
CONECT 2823 2822 2824                                                           
CONECT 2824 2823 2825                                                           
CONECT 2825 2824 2826                                                           
CONECT 2826 2825 2827                                                           
CONECT 2827 2826 2828                                                           
CONECT 2828 2827 2829                                                           
CONECT 2829 2828 2830                                                           
CONECT 2830 2829 2831                                                           
CONECT 2831 2830 2832                                                           
CONECT 2832 2831 2833                                                           
CONECT 2833 2832 2834                                                           
CONECT 2834 2833                                                                
CONECT 2835 2836 2837 2838                                                      
CONECT 2836 2835                                                                
CONECT 2837 2835                                                                
CONECT 2838 2835 2839                                                           
CONECT 2839 2838 2840                                                           
CONECT 2840 2839 2841                                                           
CONECT 2841 2840 2842                                                           
CONECT 2842 2841 2843                                                           
CONECT 2843 2842 2844                                                           
CONECT 2844 2843 2845                                                           
CONECT 2845 2844 2846                                                           
CONECT 2846 2845 2847                                                           
CONECT 2847 2846 2848                                                           
CONECT 2848 2847 2849                                                           
CONECT 2849 2848 2850                                                           
CONECT 2850 2849 2851                                                           
CONECT 2851 2850                                                                
CONECT 2852 2853 2854 2855                                                      
CONECT 2853 2852                                                                
CONECT 2854 2852                                                                
CONECT 2855 2852 2856                                                           
CONECT 2856 2855 2857                                                           
CONECT 2857 2856 2858                                                           
CONECT 2858 2857 2859                                                           
CONECT 2859 2858 2860                                                           
CONECT 2860 2859 2861                                                           
CONECT 2861 2860 2862                                                           
CONECT 2862 2861 2863                                                           
CONECT 2863 2862 2864                                                           
CONECT 2864 2863 2865                                                           
CONECT 2865 2864 2866                                                           
CONECT 2866 2865 2867                                                           
CONECT 2867 2866 2868                                                           
CONECT 2868 2867                                                                
CONECT 2869 2870 2871 2872                                                      
CONECT 2870 2869                                                                
CONECT 2871 2869                                                                
CONECT 2872 2869 2873                                                           
CONECT 2873 2872 2874                                                           
CONECT 2874 2873 2875                                                           
CONECT 2875 2874 2876                                                           
CONECT 2876 2875 2877                                                           
CONECT 2877 2876 2878                                                           
CONECT 2878 2877 2879                                                           
CONECT 2879 2878 2880                                                           
CONECT 2880 2879 2881                                                           
CONECT 2881 2880 2882                                                           
CONECT 2882 2881 2883                                                           
CONECT 2883 2882 2884                                                           
CONECT 2884 2883 2885                                                           
CONECT 2885 2884                                                                
CONECT 2886 2887 2888 2889                                                      
CONECT 2887 2886                                                                
CONECT 2888 2886                                                                
CONECT 2889 2886 2890                                                           
CONECT 2890 2889 2891                                                           
CONECT 2891 2890 2892                                                           
CONECT 2892 2891 2893                                                           
CONECT 2893 2892 2894                                                           
CONECT 2894 2893 2895                                                           
CONECT 2895 2894 2896                                                           
CONECT 2896 2895 2897                                                           
CONECT 2897 2896 2898                                                           
CONECT 2898 2897 2899                                                           
CONECT 2899 2898 2900                                                           
CONECT 2900 2899 2901                                                           
CONECT 2901 2900 2902                                                           
CONECT 2902 2901 2903                                                           
CONECT 2903 2902 2904                                                           
CONECT 2904 2903 2905                                                           
CONECT 2905 2904                                                                
CONECT 2906 2907 2908 2909                                                      
CONECT 2907 2906                                                                
CONECT 2908 2906                                                                
CONECT 2909 2906 2910                                                           
CONECT 2910 2909 2911                                                           
CONECT 2911 2910 2912                                                           
CONECT 2912 2911 2913                                                           
CONECT 2913 2912 2914                                                           
CONECT 2914 2913 2915                                                           
CONECT 2915 2914 2916                                                           
CONECT 2916 2915 2917                                                           
CONECT 2917 2916 2918                                                           
CONECT 2918 2917 2919                                                           
CONECT 2919 2918 2920                                                           
CONECT 2920 2919 2921                                                           
CONECT 2921 2920 2922                                                           
CONECT 2922 2921 2923                                                           
CONECT 2923 2922 2924                                                           
CONECT 2924 2923 2925                                                           
CONECT 2925 2924                                                                
CONECT 2926 2927 2928 2929                                                      
CONECT 2927 2926                                                                
CONECT 2928 2926                                                                
CONECT 2929 2926 2930                                                           
CONECT 2930 2929 2931                                                           
CONECT 2931 2930 2932                                                           
CONECT 2932 2931 2933                                                           
CONECT 2933 2932 2934                                                           
CONECT 2934 2933 2935                                                           
CONECT 2935 2934 2936                                                           
CONECT 2936 2935 2937                                                           
CONECT 2937 2936 2938                                                           
CONECT 2938 2937 2939                                                           
CONECT 2939 2938 2940                                                           
CONECT 2940 2939 2941                                                           
CONECT 2941 2940                                                                
CONECT 2942 2943 2944 2945                                                      
CONECT 2943 2942                                                                
CONECT 2944 2942                                                                
CONECT 2945 2942 2946                                                           
CONECT 2946 2945 2947                                                           
CONECT 2947 2946 2948                                                           
CONECT 2948 2947 2949                                                           
CONECT 2949 2948 2950                                                           
CONECT 2950 2949 2951                                                           
CONECT 2951 2950 2952                                                           
CONECT 2952 2951 2953                                                           
CONECT 2953 2952 2954                                                           
CONECT 2954 2953 2955                                                           
CONECT 2955 2954 2956                                                           
CONECT 2956 2955 2957                                                           
CONECT 2957 2956 2958                                                           
CONECT 2958 2957 2959                                                           
CONECT 2959 2958 2960                                                           
CONECT 2960 2959 2961                                                           
CONECT 2961 2960                                                                
CONECT 2962 2963 2964 2965                                                      
CONECT 2963 2962                                                                
CONECT 2964 2962                                                                
CONECT 2965 2962 2966                                                           
CONECT 2966 2965 2967                                                           
CONECT 2967 2966 2968                                                           
CONECT 2968 2967 2969                                                           
CONECT 2969 2968 2970                                                           
CONECT 2970 2969 2971                                                           
CONECT 2971 2970 2972                                                           
CONECT 2972 2971 2973                                                           
CONECT 2973 2972 2974                                                           
CONECT 2974 2973 2975                                                           
CONECT 2975 2974 2976                                                           
CONECT 2976 2975 2977                                                           
CONECT 2977 2976 2978                                                           
CONECT 2978 2977 2979                                                           
CONECT 2979 2978 2980                                                           
CONECT 2980 2979 2981                                                           
CONECT 2981 2980                                                                
CONECT 2982 2983 2984                                                           
CONECT 2983 2982                                                                
CONECT 2984 2982 2985                                                           
CONECT 2985 2984 2986                                                           
CONECT 2986 2985 2987                                                           
CONECT 2987 2986 2988                                                           
CONECT 2988 2987                                                                
CONECT 2989 2990 2991                                                           
CONECT 2990 2989                                                                
CONECT 2991 2989 2992                                                           
CONECT 2992 2991 2993                                                           
CONECT 2993 2992 2994                                                           
CONECT 2994 2993 2995                                                           
CONECT 2995 2994                                                                
CONECT 2996 2997 2998                                                           
CONECT 2997 2996                                                                
CONECT 2998 2996 2999                                                           
CONECT 2999 2998 3000                                                           
CONECT 3000 2999 3001                                                           
CONECT 3001 3000 3002                                                           
CONECT 3002 3001                                                                
CONECT 3003 3004 3005                                                           
CONECT 3004 3003                                                                
CONECT 3005 3003 3006                                                           
CONECT 3006 3005 3007                                                           
CONECT 3007 3006 3008                                                           
CONECT 3008 3007 3009                                                           
CONECT 3009 3008                                                                
CONECT 3010 3011 3012                                                           
CONECT 3011 3010                                                                
CONECT 3012 3010 3013                                                           
CONECT 3013 3012 3014                                                           
CONECT 3014 3013 3015                                                           
CONECT 3015 3014 3016                                                           
CONECT 3016 3015                                                                
CONECT 3017 3018 3019                                                           
CONECT 3018 3017                                                                
CONECT 3019 3017 3020                                                           
CONECT 3020 3019 3021                                                           
CONECT 3021 3020 3022                                                           
CONECT 3022 3021 3023                                                           
CONECT 3023 3022                                                                
CONECT 3024 3025 3026                                                           
CONECT 3025 3024                                                                
CONECT 3026 3024 3027                                                           
CONECT 3027 3026 3028                                                           
CONECT 3028 3027 3029                                                           
CONECT 3029 3028 3030                                                           
CONECT 3030 3029                                                                
CONECT 3031 3032 3033                                                           
CONECT 3032 3031                                                                
CONECT 3033 3031 3034                                                           
CONECT 3034 3033 3035                                                           
CONECT 3035 3034 3036                                                           
CONECT 3036 3035 3037                                                           
CONECT 3037 3036                                                                
CONECT 3038 3039 3040                                                           
CONECT 3039 3038                                                                
CONECT 3040 3038 3041                                                           
CONECT 3041 3040 3042                                                           
CONECT 3042 3041 3043                                                           
CONECT 3043 3042 3044                                                           
CONECT 3044 3043                                                                
CONECT 3045 3046 3047                                                           
CONECT 3046 3045                                                                
CONECT 3047 3045 3048 3049                                                      
CONECT 3048 3047                                                                
CONECT 3049 3047 3050                                                           
CONECT 3050 3049                                                                
MASTER      427    0   23   18    0    0   29    6 3109    1  279   33          
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.