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***  TRANSPORT PROTEIN 10-AUG-07 2QX5  ***

elNémo ID: 21120602485632779

Job options:

ID        	=	 21120602485632779
JOBID     	=	 TRANSPORT PROTEIN 10-AUG-07 2QX5
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    TRANSPORT PROTEIN                       10-AUG-07   2QX5              
TITLE     STRUCTURE OF NUCLEOPORIN NIC96                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NUCLEOPORIN NIC96;                                         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 186-839;                                          
COMPND   5 SYNONYM: NUCLEAR PORE PROTEIN NIC96, 96 KDA NUCLEOPORIN-             
COMPND   6 INTERACTING COMPONENT;                                               
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 STRAIN: S288C;                                                       
SOURCE   6 GENE: NIC96;                                                         
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) RIL;                            
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    NUCLEOPORIN, MRNA TRANSPORT, NUCLEAR PORE COMPLEX, NUCLEUS,           
KEYWDS   2 PROTEIN TRANSPORT, TRANSLOCATION, TRANSPORT, TRANSPORT               
KEYWDS   3 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.JEUDY,T.U.SCHWARTZ                                                  
REVDAT   3   24-FEB-09 2QX5    1       VERSN                                    
REVDAT   2   04-DEC-07 2QX5    1       JRNL                                     
REVDAT   1   25-SEP-07 2QX5    0                                                
JRNL        AUTH   S.JEUDY,T.U.SCHWARTZ                                         
JRNL        TITL   CRYSTAL STRUCTURE OF NUCLEOPORIN NIC96 REVEALS A             
JRNL        TITL 2 NOVEL, INTRICATE HELICAL DOMAIN ARCHITECTURE                 
JRNL        REF    J.BIOL.CHEM.                  V. 282 34904 2007              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   17897938                                                     
JRNL        DOI    10.1074/JBC.M705479200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 54858                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.233                           
REMARK   3   FREE R VALUE                     : 0.285                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2756                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1  2.5400 -  2.5000    0.99        0   138  0.2860 0.3180        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 47.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2QX5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-AUG-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB044155.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-AUG-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0718                             
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55097                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08300                            
REMARK 200   FOR THE DATA SET  : 19.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.38100                            
REMARK 200   FOR SHELL         : 3.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.02                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG 3350, 0.1M BIS TRIS              
REMARK 280  PROPANE, 0.2M POTASSIUM THIOCYANATE, 1MM                            
REMARK 280  CETYLTRIMETHYLAMMONIUM BROMIDE, PH 8.2, VAPOR DIFFUSION,            
REMARK 280  HANGING DROP, TEMPERATURE 289K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       41.23900            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO A   179                                                      
REMARK 465     GLY A   180                                                      
REMARK 465     SER A   181                                                      
REMARK 465     GLU A   182                                                      
REMARK 465     PHE A   183                                                      
REMARK 465     GLU A   184                                                      
REMARK 465     LEU A   185                                                      
REMARK 465     GLY A   186                                                      
REMARK 465     ASN A   187                                                      
REMARK 465     LYS A   188                                                      
REMARK 465     GLY A   189                                                      
REMARK 465     ASN A   190                                                      
REMARK 465     ASN A   191                                                      
REMARK 465     ILE A   192                                                      
REMARK 465     LEU A   193                                                      
REMARK 465     ASN A   194                                                      
REMARK 465     SER A   195                                                      
REMARK 465     ASN A   196                                                      
REMARK 465     GLU A   197                                                      
REMARK 465     SER A   198                                                      
REMARK 465     ARG A   199                                                      
REMARK 465     LYS A   361                                                      
REMARK 465     LYS A   362                                                      
REMARK 465     VAL A   363                                                      
REMARK 465     GLU A   364                                                      
REMARK 465     GLN A   365                                                      
REMARK 465     ALA A   375                                                      
REMARK 465     SER A   376                                                      
REMARK 465     SER A   377                                                      
REMARK 465     LYS A   378                                                      
REMARK 465     ASP A   379                                                      
REMARK 465     HIS A   380                                                      
REMARK 465     GLY A   381                                                      
REMARK 465     LEU A   382                                                      
REMARK 465     PRO A   383                                                      
REMARK 465     VAL A   384                                                      
REMARK 465     GLU A   385                                                      
REMARK 465     TYR A   386                                                      
REMARK 465     SER A   387                                                      
REMARK 465     THR A   388                                                      
REMARK 465     LYS A   389                                                      
REMARK 465     LEU A   390                                                      
REMARK 465     HIS A   391                                                      
REMARK 465     THR A   392                                                      
REMARK 465     GLU A   393                                                      
REMARK 465     TYR A   394                                                      
REMARK 465     ASN A   395                                                      
REMARK 465     GLN A   396                                                      
REMARK 465     HIS A   397                                                      
REMARK 465     ILE A   398                                                      
REMARK 465     LYS A   399                                                      
REMARK 465     SER A   400                                                      
REMARK 465     SER A   401                                                      
REMARK 465     LEU A   402                                                      
REMARK 465     ASP A   403                                                      
REMARK 465     GLY A   404                                                      
REMARK 465     GLU A   445                                                      
REMARK 465     LYS A   446                                                      
REMARK 465     ASP A   447                                                      
REMARK 465     ALA A   448                                                      
REMARK 465     GLU A   449                                                      
REMARK 465     ASN A   450                                                      
REMARK 465     ASP A   451                                                      
REMARK 465     PRO A   452                                                      
REMARK 465     VAL A   453                                                      
REMARK 465     TYR A   454                                                      
REMARK 465     PHE A   516                                                      
REMARK 465     LYS A   517                                                      
REMARK 465     ILE A   518                                                      
REMARK 465     ASP A   519                                                      
REMARK 465     SER A   520                                                      
REMARK 465     SER A   521                                                      
REMARK 465     THR A   522                                                      
REMARK 465     ARG A   523                                                      
REMARK 465     LEU A   524                                                      
REMARK 465     THR A   525                                                      
REMARK 465     LYS A   526                                                      
REMARK 465     LYS A   527                                                      
REMARK 465     PRO A   528                                                      
REMARK 465     LYS A   529                                                      
REMARK 465     ARG A   530                                                      
REMARK 465     ASP A   531                                                      
REMARK 465     ILE A   532                                                      
REMARK 465     SER A   748                                                      
REMARK 465     ASP A   749                                                      
REMARK 465     GLU A   750                                                      
REMARK 465     LEU A   751                                                      
REMARK 465     SER A   752                                                      
REMARK 465     ASP A   836                                                      
REMARK 465     VAL A   837                                                      
REMARK 465     SER A   838                                                      
REMARK 465     LEU A   839                                                      
REMARK 465     PRO B   179                                                      
REMARK 465     GLY B   180                                                      
REMARK 465     SER B   181                                                      
REMARK 465     GLU B   182                                                      
REMARK 465     PHE B   183                                                      
REMARK 465     GLU B   184                                                      
REMARK 465     LEU B   185                                                      
REMARK 465     GLY B   186                                                      
REMARK 465     ASN B   187                                                      
REMARK 465     LYS B   188                                                      
REMARK 465     GLY B   189                                                      
REMARK 465     ASN B   190                                                      
REMARK 465     ASN B   191                                                      
REMARK 465     ILE B   192                                                      
REMARK 465     LEU B   193                                                      
REMARK 465     ASN B   194                                                      
REMARK 465     SER B   195                                                      
REMARK 465     ASN B   196                                                      
REMARK 465     GLU B   197                                                      
REMARK 465     SER B   198                                                      
REMARK 465     ARG B   199                                                      
REMARK 465     LYS B   357                                                      
REMARK 465     ALA B   358                                                      
REMARK 465     ASN B   359                                                      
REMARK 465     ILE B   360                                                      
REMARK 465     LYS B   361                                                      
REMARK 465     LYS B   362                                                      
REMARK 465     VAL B   363                                                      
REMARK 465     ALA B   375                                                      
REMARK 465     SER B   376                                                      
REMARK 465     SER B   377                                                      
REMARK 465     LYS B   378                                                      
REMARK 465     ASP B   379                                                      
REMARK 465     HIS B   380                                                      
REMARK 465     GLY B   381                                                      
REMARK 465     LEU B   382                                                      
REMARK 465     PRO B   383                                                      
REMARK 465     VAL B   384                                                      
REMARK 465     GLU B   385                                                      
REMARK 465     TYR B   386                                                      
REMARK 465     SER B   387                                                      
REMARK 465     THR B   388                                                      
REMARK 465     LYS B   389                                                      
REMARK 465     LEU B   390                                                      
REMARK 465     HIS B   391                                                      
REMARK 465     THR B   392                                                      
REMARK 465     GLU B   393                                                      
REMARK 465     TYR B   394                                                      
REMARK 465     ASN B   395                                                      
REMARK 465     GLN B   396                                                      
REMARK 465     HIS B   397                                                      
REMARK 465     ILE B   398                                                      
REMARK 465     LYS B   399                                                      
REMARK 465     SER B   400                                                      
REMARK 465     SER B   401                                                      
REMARK 465     LEU B   402                                                      
REMARK 465     ASP B   403                                                      
REMARK 465     GLY B   404                                                      
REMARK 465     LYS B   444                                                      
REMARK 465     GLU B   445                                                      
REMARK 465     LYS B   446                                                      
REMARK 465     ASP B   447                                                      
REMARK 465     ALA B   448                                                      
REMARK 465     GLU B   449                                                      
REMARK 465     ASN B   450                                                      
REMARK 465     ASP B   451                                                      
REMARK 465     PRO B   452                                                      
REMARK 465     VAL B   453                                                      
REMARK 465     TYR B   454                                                      
REMARK 465     PHE B   516                                                      
REMARK 465     LYS B   517                                                      
REMARK 465     ILE B   518                                                      
REMARK 465     ASP B   519                                                      
REMARK 465     SER B   520                                                      
REMARK 465     SER B   521                                                      
REMARK 465     THR B   522                                                      
REMARK 465     ARG B   523                                                      
REMARK 465     LEU B   524                                                      
REMARK 465     THR B   525                                                      
REMARK 465     LYS B   526                                                      
REMARK 465     LYS B   527                                                      
REMARK 465     PRO B   528                                                      
REMARK 465     LYS B   529                                                      
REMARK 465     ARG B   530                                                      
REMARK 465     ASP B   531                                                      
REMARK 465     ILE B   532                                                      
REMARK 465     ASP B   749                                                      
REMARK 465     GLU B   750                                                      
REMARK 465     LEU B   751                                                      
REMARK 465     SER B   752                                                      
REMARK 465     SER B   838                                                      
REMARK 465     LEU B   839                                                      
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     ASP A 267    CG   OD1  OD2                                       
REMARK 470     GLU A 272    CD   OE1  OE2                                       
REMARK 470     GLN A 281    CD   OE1  NE2                                       
REMARK 470     LYS A 291    CD   CE   NZ                                        
REMARK 470     LYS A 292    CG   CD   CE   NZ                                   
REMARK 470     ASN A 295    CG   OD1  ND2                                       
REMARK 470     LYS A 318    CG   CD   CE   NZ                                   
REMARK 470     LYS A 357    CD   CE   NZ                                        
REMARK 470     ARG A 422    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 455    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 456    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 570    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 616    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 618    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 625    CD   OE1  OE2                                       
REMARK 470     ARG A 629    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 630    NE   CZ   NH1  NH2                                  
REMARK 470     GLU A 633    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 671    CG   OD1  OD2                                       
REMARK 470     ASP A 678    CG   OD1  OD2                                       
REMARK 470     ARG A 704    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 755    CG   CD   CE   NZ                                   
REMARK 470     ARG A 811    NE   CZ   NH1  NH2                                  
REMARK 470     GLU B 210    CD   OE1  OE2                                       
REMARK 470     LYS B 264    CG   CD   CE   NZ                                   
REMARK 470     ASP B 267    CG   OD1  OD2                                       
REMARK 470     GLU B 272    CD   OE1  OE2                                       
REMARK 470     LYS B 291    CG   CD   CE   NZ                                   
REMARK 470     LYS B 292    CG   CD   CE   NZ                                   
REMARK 470     GLU B 296    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 315    CG   CD   CE   NZ                                   
REMARK 470     LYS B 318    CG   CD   CE   NZ                                   
REMARK 470     GLN B 365    CG   CD   OE1  NE2                                  
REMARK 470     LEU B 420    CG   CD1  CD2                                       
REMARK 470     GLU B 455    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 456    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 581    CG   CD1  CD2                                       
REMARK 470     GLN B 608    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 614    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 616    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 617    CG   CD   CE   NZ                                   
REMARK 470     GLU B 618    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 630    NE   CZ   NH1  NH2                                  
REMARK 470     GLU B 633    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 678    CG   OD1  OD2                                       
REMARK 470     LYS B 755    CG   CD   CE   NZ                                   
REMARK 470     ARG B 811    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU B 827    CD   OE1  OE2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 265       17.35     54.58                                   
REMARK 500    ASN A 269       92.31   -161.81                                   
REMARK 500    ASN A 295       58.30     38.51                                   
REMARK 500    GLU A 296      -99.53   -121.28                                   
REMARK 500    ALA A 316      -45.49     82.68                                   
REMARK 500    ASP A 317        2.51    -53.58                                   
REMARK 500    ASN A 324       18.57     83.52                                   
REMARK 500    ASN A 329       21.32     46.41                                   
REMARK 500    LYS A 357      -36.07    -39.45                                   
REMARK 500    ASN A 359        8.90    -62.36                                   
REMARK 500    ARG A 422       71.68   -107.55                                   
REMARK 500    SER A 475     -108.71     40.16                                   
REMARK 500    SER A 499       96.07   -179.49                                   
REMARK 500    LYS A 514       55.26     71.25                                   
REMARK 500    ASN B 229       -6.21     75.08                                   
REMARK 500    ILE B 268       82.86    -62.65                                   
REMARK 500    ASN B 293      -77.75   -116.54                                   
REMARK 500    LYS B 315       83.58    -69.72                                   
REMARK 500    ALA B 316      -47.13     71.95                                   
REMARK 500    ASN B 329       18.27     53.02                                   
REMARK 500    PRO B 406      -29.06    -39.30                                   
REMARK 500    ASP B 419       66.27   -101.54                                   
REMARK 500    ARG B 422       68.26   -115.85                                   
REMARK 500    SER B 475     -123.47     43.33                                   
REMARK 500    ASN B 476       30.57    -97.85                                   
REMARK 500    SER B 499      103.41   -167.72                                   
REMARK 500    LYS B 514       59.17     74.39                                   
REMARK 500    PRO B 566       -9.20    -58.64                                   
REMARK 500    ARG B 607       33.48    -97.48                                   
REMARK 500    ARG B 614      -70.82    -83.08                                   
REMARK 500    GLU B 616       32.98    -79.31                                   
REMARK 500    LYS B 617        5.10   -158.54                                   
REMARK 500    ILE B 835       88.33   -178.21                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LYS B  315     ALA B  316                  127.83                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 854                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 844                  
DBREF  2QX5 A  186   839  UNP    P34077   NIC96_YEAST    186    839             
DBREF  2QX5 B  186   839  UNP    P34077   NIC96_YEAST    186    839             
SEQADV 2QX5 PRO A  179  UNP  P34077              EXPRESSION TAG                 
SEQADV 2QX5 GLY A  180  UNP  P34077              EXPRESSION TAG                 
SEQADV 2QX5 SER A  181  UNP  P34077              EXPRESSION TAG                 
SEQADV 2QX5 GLU A  182  UNP  P34077              EXPRESSION TAG                 
SEQADV 2QX5 PHE A  183  UNP  P34077              EXPRESSION TAG                 
SEQADV 2QX5 GLU A  184  UNP  P34077              EXPRESSION TAG                 
SEQADV 2QX5 LEU A  185  UNP  P34077              EXPRESSION TAG                 
SEQADV 2QX5 PRO B  179  UNP  P34077              EXPRESSION TAG                 
SEQADV 2QX5 GLY B  180  UNP  P34077              EXPRESSION TAG                 
SEQADV 2QX5 SER B  181  UNP  P34077              EXPRESSION TAG                 
SEQADV 2QX5 GLU B  182  UNP  P34077              EXPRESSION TAG                 
SEQADV 2QX5 PHE B  183  UNP  P34077              EXPRESSION TAG                 
SEQADV 2QX5 GLU B  184  UNP  P34077              EXPRESSION TAG                 
SEQADV 2QX5 LEU B  185  UNP  P34077              EXPRESSION TAG                 
SEQRES   1 A  661  PRO GLY SER GLU PHE GLU LEU GLY ASN LYS GLY ASN ASN          
SEQRES   2 A  661  ILE LEU ASN SER ASN GLU SER ARG LEU ASN VAL ASN GLU          
SEQRES   3 A  661  ASN ASN ILE LEU ARG GLU LYS PHE GLU ASN TYR ALA ARG          
SEQRES   4 A  661  ILE VAL PHE GLN PHE ASN ASN SER ARG GLN ALA ASN GLY          
SEQRES   5 A  661  ASN PHE ASP ILE ALA ASN GLU PHE ILE SER ILE LEU SER          
SEQRES   6 A  661  SER ALA ASN GLY THR ARG ASN ALA GLN LEU LEU GLU SER          
SEQRES   7 A  661  TRP LYS ILE LEU GLU SER MET LYS SER LYS ASP ILE ASN          
SEQRES   8 A  661  ILE VAL GLU VAL GLY LYS GLN TYR LEU GLU GLN GLN PHE          
SEQRES   9 A  661  LEU GLN TYR THR ASP ASN LEU TYR LYS LYS ASN MET ASN          
SEQRES  10 A  661  GLU GLY LEU ALA THR ASN VAL ASN LYS ILE LYS SER PHE          
SEQRES  11 A  661  ILE ASP THR LYS LEU LYS LYS ALA ASP LYS SER TRP LYS          
SEQRES  12 A  661  ILE SER ASN LEU THR VAL ILE ASN GLY VAL PRO ILE TRP          
SEQRES  13 A  661  ALA LEU ILE PHE TYR LEU LEU ARG ALA GLY LEU ILE LYS          
SEQRES  14 A  661  GLU ALA LEU GLN VAL LEU VAL GLU ASN LYS ALA ASN ILE          
SEQRES  15 A  661  LYS LYS VAL GLU GLN SER PHE LEU THR TYR PHE LYS ALA          
SEQRES  16 A  661  TYR ALA SER SER LYS ASP HIS GLY LEU PRO VAL GLU TYR          
SEQRES  17 A  661  SER THR LYS LEU HIS THR GLU TYR ASN GLN HIS ILE LYS          
SEQRES  18 A  661  SER SER LEU ASP GLY ASP PRO TYR ARG LEU ALA VAL TYR          
SEQRES  19 A  661  LYS LEU ILE GLY ARG CYS ASP LEU SER ARG LYS ASN ILE          
SEQRES  20 A  661  PRO ALA VAL THR LEU SER ILE GLU ASP TRP LEU TRP MET          
SEQRES  21 A  661  HIS LEU MET LEU ILE LYS GLU LYS ASP ALA GLU ASN ASP          
SEQRES  22 A  661  PRO VAL TYR GLU ARG TYR SER LEU GLU ASP PHE GLN ASN          
SEQRES  23 A  661  ILE ILE ILE SER TYR GLY PRO SER ARG PHE SER ASN TYR          
SEQRES  24 A  661  TYR LEU GLN THR LEU LEU LEU SER GLY LEU TYR GLY LEU          
SEQRES  25 A  661  ALA ILE ASP TYR THR TYR THR PHE SER GLU MET ASP ALA          
SEQRES  26 A  661  VAL HIS LEU ALA ILE GLY LEU ALA SER LEU LYS LEU PHE          
SEQRES  27 A  661  LYS ILE ASP SER SER THR ARG LEU THR LYS LYS PRO LYS          
SEQRES  28 A  661  ARG ASP ILE ARG PHE ALA ASN ILE LEU ALA ASN TYR THR          
SEQRES  29 A  661  LYS SER PHE ARG TYR SER ASP PRO ARG VAL ALA VAL GLU          
SEQRES  30 A  661  TYR LEU VAL LEU ILE THR LEU ASN GLU GLY PRO THR ASP          
SEQRES  31 A  661  VAL GLU LEU CYS HIS GLU ALA LEU ARG GLU LEU VAL LEU          
SEQRES  32 A  661  GLU THR LYS GLU PHE THR VAL LEU LEU GLY LYS ILE GLY          
SEQRES  33 A  661  ARG ASP GLY ALA ARG ILE PRO GLY VAL ILE GLU GLU ARG          
SEQRES  34 A  661  GLN PRO LEU LEU HIS VAL ARG ASP GLU LYS GLU PHE LEU          
SEQRES  35 A  661  HIS THR ILE THR GLU GLN ALA ALA ARG ARG ALA ASP GLU          
SEQRES  36 A  661  ASP GLY ARG ILE TYR ASP SER ILE LEU LEU TYR GLN LEU          
SEQRES  37 A  661  ALA GLU GLU TYR ASP ILE VAL ILE THR LEU VAL ASN SER          
SEQRES  38 A  661  LEU LEU SER ASP THR LEU SER ALA SER ASP LEU ASP GLN          
SEQRES  39 A  661  PRO LEU VAL GLY PRO ASP ASP ASN SER GLU THR ASN PRO          
SEQRES  40 A  661  VAL LEU LEU ALA ARG ARG MET ALA SER ILE TYR PHE ASP          
SEQRES  41 A  661  ASN ALA GLY ILE SER ARG GLN ILE HIS VAL LYS ASN LYS          
SEQRES  42 A  661  GLU ILE CYS MET LEU LEU LEU ASN ILE SER SER ILE ARG          
SEQRES  43 A  661  GLU LEU TYR PHE ASN LYS GLN TRP GLN GLU THR LEU SER          
SEQRES  44 A  661  GLN MET GLU LEU LEU ASP LEU LEU PRO PHE SER ASP GLU          
SEQRES  45 A  661  LEU SER ALA ARG LYS LYS ALA GLN ASP PHE SER ASN LEU          
SEQRES  46 A  661  ASP ASP ASN ILE VAL LYS ASN ILE PRO ASN LEU LEU ILE          
SEQRES  47 A  661  ILE THR LEU SER CYS ILE SER ASN MET ILE HIS ILE LEU          
SEQRES  48 A  661  ASN GLU SER LYS TYR GLN SER SER THR LYS GLY GLN GLN          
SEQRES  49 A  661  ILE ASP SER LEU LYS ASN VAL ALA ARG GLN CYS MET ILE          
SEQRES  50 A  661  TYR ALA GLY MET ILE GLN TYR ARG MET PRO ARG GLU THR          
SEQRES  51 A  661  TYR SER THR LEU ILE ASN ILE ASP VAL SER LEU                  
SEQRES   1 B  661  PRO GLY SER GLU PHE GLU LEU GLY ASN LYS GLY ASN ASN          
SEQRES   2 B  661  ILE LEU ASN SER ASN GLU SER ARG LEU ASN VAL ASN GLU          
SEQRES   3 B  661  ASN ASN ILE LEU ARG GLU LYS PHE GLU ASN TYR ALA ARG          
SEQRES   4 B  661  ILE VAL PHE GLN PHE ASN ASN SER ARG GLN ALA ASN GLY          
SEQRES   5 B  661  ASN PHE ASP ILE ALA ASN GLU PHE ILE SER ILE LEU SER          
SEQRES   6 B  661  SER ALA ASN GLY THR ARG ASN ALA GLN LEU LEU GLU SER          
SEQRES   7 B  661  TRP LYS ILE LEU GLU SER MET LYS SER LYS ASP ILE ASN          
SEQRES   8 B  661  ILE VAL GLU VAL GLY LYS GLN TYR LEU GLU GLN GLN PHE          
SEQRES   9 B  661  LEU GLN TYR THR ASP ASN LEU TYR LYS LYS ASN MET ASN          
SEQRES  10 B  661  GLU GLY LEU ALA THR ASN VAL ASN LYS ILE LYS SER PHE          
SEQRES  11 B  661  ILE ASP THR LYS LEU LYS LYS ALA ASP LYS SER TRP LYS          
SEQRES  12 B  661  ILE SER ASN LEU THR VAL ILE ASN GLY VAL PRO ILE TRP          
SEQRES  13 B  661  ALA LEU ILE PHE TYR LEU LEU ARG ALA GLY LEU ILE LYS          
SEQRES  14 B  661  GLU ALA LEU GLN VAL LEU VAL GLU ASN LYS ALA ASN ILE          
SEQRES  15 B  661  LYS LYS VAL GLU GLN SER PHE LEU THR TYR PHE LYS ALA          
SEQRES  16 B  661  TYR ALA SER SER LYS ASP HIS GLY LEU PRO VAL GLU TYR          
SEQRES  17 B  661  SER THR LYS LEU HIS THR GLU TYR ASN GLN HIS ILE LYS          
SEQRES  18 B  661  SER SER LEU ASP GLY ASP PRO TYR ARG LEU ALA VAL TYR          
SEQRES  19 B  661  LYS LEU ILE GLY ARG CYS ASP LEU SER ARG LYS ASN ILE          
SEQRES  20 B  661  PRO ALA VAL THR LEU SER ILE GLU ASP TRP LEU TRP MET          
SEQRES  21 B  661  HIS LEU MET LEU ILE LYS GLU LYS ASP ALA GLU ASN ASP          
SEQRES  22 B  661  PRO VAL TYR GLU ARG TYR SER LEU GLU ASP PHE GLN ASN          
SEQRES  23 B  661  ILE ILE ILE SER TYR GLY PRO SER ARG PHE SER ASN TYR          
SEQRES  24 B  661  TYR LEU GLN THR LEU LEU LEU SER GLY LEU TYR GLY LEU          
SEQRES  25 B  661  ALA ILE ASP TYR THR TYR THR PHE SER GLU MET ASP ALA          
SEQRES  26 B  661  VAL HIS LEU ALA ILE GLY LEU ALA SER LEU LYS LEU PHE          
SEQRES  27 B  661  LYS ILE ASP SER SER THR ARG LEU THR LYS LYS PRO LYS          
SEQRES  28 B  661  ARG ASP ILE ARG PHE ALA ASN ILE LEU ALA ASN TYR THR          
SEQRES  29 B  661  LYS SER PHE ARG TYR SER ASP PRO ARG VAL ALA VAL GLU          
SEQRES  30 B  661  TYR LEU VAL LEU ILE THR LEU ASN GLU GLY PRO THR ASP          
SEQRES  31 B  661  VAL GLU LEU CYS HIS GLU ALA LEU ARG GLU LEU VAL LEU          
SEQRES  32 B  661  GLU THR LYS GLU PHE THR VAL LEU LEU GLY LYS ILE GLY          
SEQRES  33 B  661  ARG ASP GLY ALA ARG ILE PRO GLY VAL ILE GLU GLU ARG          
SEQRES  34 B  661  GLN PRO LEU LEU HIS VAL ARG ASP GLU LYS GLU PHE LEU          
SEQRES  35 B  661  HIS THR ILE THR GLU GLN ALA ALA ARG ARG ALA ASP GLU          
SEQRES  36 B  661  ASP GLY ARG ILE TYR ASP SER ILE LEU LEU TYR GLN LEU          
SEQRES  37 B  661  ALA GLU GLU TYR ASP ILE VAL ILE THR LEU VAL ASN SER          
SEQRES  38 B  661  LEU LEU SER ASP THR LEU SER ALA SER ASP LEU ASP GLN          
SEQRES  39 B  661  PRO LEU VAL GLY PRO ASP ASP ASN SER GLU THR ASN PRO          
SEQRES  40 B  661  VAL LEU LEU ALA ARG ARG MET ALA SER ILE TYR PHE ASP          
SEQRES  41 B  661  ASN ALA GLY ILE SER ARG GLN ILE HIS VAL LYS ASN LYS          
SEQRES  42 B  661  GLU ILE CYS MET LEU LEU LEU ASN ILE SER SER ILE ARG          
SEQRES  43 B  661  GLU LEU TYR PHE ASN LYS GLN TRP GLN GLU THR LEU SER          
SEQRES  44 B  661  GLN MET GLU LEU LEU ASP LEU LEU PRO PHE SER ASP GLU          
SEQRES  45 B  661  LEU SER ALA ARG LYS LYS ALA GLN ASP PHE SER ASN LEU          
SEQRES  46 B  661  ASP ASP ASN ILE VAL LYS ASN ILE PRO ASN LEU LEU ILE          
SEQRES  47 B  661  ILE THR LEU SER CYS ILE SER ASN MET ILE HIS ILE LEU          
SEQRES  48 B  661  ASN GLU SER LYS TYR GLN SER SER THR LYS GLY GLN GLN          
SEQRES  49 B  661  ILE ASP SER LEU LYS ASN VAL ALA ARG GLN CYS MET ILE          
SEQRES  50 B  661  TYR ALA GLY MET ILE GLN TYR ARG MET PRO ARG GLU THR          
SEQRES  51 B  661  TYR SER THR LEU ILE ASN ILE ASP VAL SER LEU                  
HET     CL  A 854       1                                                       
HET     CL  B 844       1                                                       
HETNAM      CL CHLORIDE ION                                                     
FORMUL   3   CL    2(CL 1-)                                                     
FORMUL   5  HOH   *123(H2 O)                                                    
HELIX    1   1 ASN A  205  ALA A  228  1                                  24    
HELIX    2   2 ASP A  233  SER A  244  1                                  12    
HELIX    3   3 GLY A  247  SER A  262  1                                  16    
HELIX    4   4 ASN A  269  MET A  294  1                                  26    
HELIX    5   5 THR A  300  LYS A  312  1                                  13    
HELIX    6   6 ILE A  333  ARG A  342  1                                  10    
HELIX    7   7 LEU A  345  ASN A  356  1                                  12    
HELIX    8   8 LYS A  357  ILE A  360  5                                   4    
HELIX    9   9 SER A  366  TYR A  374  1                                   9    
HELIX   10  10 ASP A  405  ARG A  417  1                                  13    
HELIX   11  11 ASP A  419  LYS A  423  5                                   5    
HELIX   12  12 ILE A  425  THR A  429  5                                   5    
HELIX   13  13 SER A  431  LEU A  442  1                                  12    
HELIX   14  14 SER A  458  GLY A  470  1                                  13    
HELIX   15  15 PRO A  471  SER A  475  5                                   5    
HELIX   16  16 TYR A  477  SER A  485  1                                   9    
HELIX   17  17 LEU A  487  THR A  497  1                                  11    
HELIX   18  18 SER A  499  LEU A  513  1                                  15    
HELIX   19  19 ARG A  533  LYS A  543  1                                  11    
HELIX   20  20 ASP A  549  LEU A  559  1                                  11    
HELIX   21  21 ILE A  560  ASN A  563  5                                   4    
HELIX   22  22 GLY A  565  LYS A  584  1                                  20    
HELIX   23  23 GLU A  585  GLY A  591  1                                   7    
HELIX   24  24 GLY A  602  ARG A  607  1                                   6    
HELIX   25  25 GLN A  608  HIS A  612  5                                   5    
HELIX   26  26 ASP A  615  ASP A  634  1                                  20    
HELIX   27  27 ARG A  636  ALA A  647  1                                  12    
HELIX   28  28 GLU A  649  SER A  668  1                                  20    
HELIX   29  29 ASN A  684  PHE A  697  1                                  14    
HELIX   30  30 ASN A  699  ARG A  704  1                                   6    
HELIX   31  31 HIS A  707  ASN A  729  1                                  23    
HELIX   32  32 GLN A  731  LEU A  742  1                                  12    
HELIX   33  33 ALA A  753  PHE A  760  1                                   8    
HELIX   34  34 SER A  761  LEU A  763  5                                   3    
HELIX   35  35 ASP A  764  LYS A  769  1                                   6    
HELIX   36  36 ASN A  770  GLU A  791  1                                  22    
HELIX   37  37 THR A  798  ILE A  820  1                                  23    
HELIX   38  38 GLN A  821  MET A  824  5                                   4    
HELIX   39  39 PRO A  825  ASN A  834  1                                  10    
HELIX   40  40 ASN B  205  ASN B  229  1                                  25    
HELIX   41  41 ASP B  233  SER B  244  1                                  12    
HELIX   42  42 GLY B  247  SER B  262  1                                  16    
HELIX   43  43 ASN B  269  LYS B  291  1                                  23    
HELIX   44  44 THR B  300  LYS B  312  1                                  13    
HELIX   45  45 PRO B  332  ARG B  342  1                                  11    
HELIX   46  46 LEU B  345  GLU B  355  1                                  11    
HELIX   47  47 SER B  366  TYR B  374  1                                   9    
HELIX   48  48 ASP B  405  ARG B  417  1                                  13    
HELIX   49  49 ASP B  419  LYS B  423  5                                   5    
HELIX   50  50 SER B  431  ILE B  443  1                                  13    
HELIX   51  51 SER B  458  GLY B  470  1                                  13    
HELIX   52  52 PRO B  471  PHE B  474  5                                   4    
HELIX   53  53 TYR B  477  SER B  485  1                                   9    
HELIX   54  54 LEU B  487  THR B  497  1                                  11    
HELIX   55  55 SER B  499  SER B  512  1                                  14    
HELIX   56  56 ARG B  533  THR B  542  1                                  10    
HELIX   57  57 LYS B  543  ARG B  546  5                                   4    
HELIX   58  58 ASP B  549  ILE B  560  1                                  12    
HELIX   59  59 THR B  561  ASN B  563  5                                   3    
HELIX   60  60 THR B  567  LYS B  584  1                                  18    
HELIX   61  61 GLU B  585  GLY B  591  1                                   7    
HELIX   62  62 GLY B  602  ARG B  607  1                                   6    
HELIX   63  63 GLN B  608  HIS B  612  5                                   5    
HELIX   64  64 GLU B  618  GLY B  635  1                                  18    
HELIX   65  65 ARG B  636  ALA B  647  1                                  12    
HELIX   66  66 GLU B  649  SER B  668  1                                  20    
HELIX   67  67 ASN B  684  PHE B  697  1                                  14    
HELIX   68  68 ASN B  699  ARG B  704  1                                   6    
HELIX   69  69 HIS B  707  ASN B  729  1                                  23    
HELIX   70  70 GLN B  731  LEU B  742  1                                  12    
HELIX   71  71 ALA B  753  PHE B  760  1                                   8    
HELIX   72  72 SER B  761  LEU B  763  5                                   3    
HELIX   73  73 ASP B  764  LYS B  769  1                                   6    
HELIX   74  74 ASN B  770  GLU B  791  1                                  22    
HELIX   75  75 THR B  798  ILE B  820  1                                  23    
HELIX   76  76 GLN B  821  MET B  824  5                                   4    
HELIX   77  77 PRO B  825  LEU B  832  1                                   8    
SHEET    1   A 2 VAL A 327  ILE A 328  0                                        
SHEET    2   A 2 VAL A 331  PRO A 332 -1  O  VAL A 331   N  ILE A 328           
SHEET    1   B 2 LYS A 592  ILE A 593  0                                        
SHEET    2   B 2 ARG A 599  ILE A 600 -1  O  ILE A 600   N  LYS A 592           
SHEET    1   C 2 LYS B 314  LYS B 315  0                                        
SHEET    2   C 2 SER B 319  TRP B 320 -1  O  SER B 319   N  LYS B 315           
SHEET    1   D 2 LYS B 592  ILE B 593  0                                        
SHEET    2   D 2 ARG B 599  ILE B 600 -1  O  ILE B 600   N  LYS B 592           
SITE     1 AC1  1 ASN A 773                                                     
SITE     1 AC2  2 ILE B 720  ASN B 773                                          
CRYST1   87.121   82.478  113.028  90.00  91.11  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011478  0.000000  0.000222        0.00000                         
SCALE2      0.000000  0.012124  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008849        0.00000                         
ATOM      1  N   LEU A 200     -21.871   9.322 -16.608  1.00 86.46           N  
ANISOU    1  N   LEU A 200    10750  11165  10935   -158    192  -1245       N  
ATOM      2  CA  LEU A 200     -20.878   9.041 -15.575  1.00 84.17           C  
ANISOU    2  CA  LEU A 200    10565  10691  10723   -106    195  -1194       C  
ATOM      3  C   LEU A 200     -21.472   9.198 -14.188  1.00 91.37           C  
ANISOU    3  C   LEU A 200    11518  11542  11657   -108    192  -1156       C  
ATOM      4  O   LEU A 200     -22.358  10.020 -13.959  1.00 95.42           O  
ANISOU    4  O   LEU A 200    11972  12148  12134   -105    162  -1128       O  
ATOM      5  CB  LEU A 200     -19.652   9.954 -15.711  1.00 76.93           C  
ANISOU    5  CB  LEU A 200     9641   9753   9836      4    143  -1109       C  
ATOM      6  CG  LEU A 200     -18.756  10.142 -14.470  1.00 71.96           C  
ANISOU    6  CG  LEU A 200     9089   8983   9269     73    127  -1031       C  
ATOM      7  CD1 LEU A 200     -17.915   8.911 -14.158  1.00 59.84           C  
ANISOU    7  CD1 LEU A 200     7649   7309   7780     71    175  -1055       C  
ATOM      8  CD2 LEU A 200     -17.853  11.357 -14.606  1.00 75.97           C  
ANISOU    8  CD2 LEU A 200     9566   9515   9786    164     71   -950       C  
ATOM      9  N   ASN A 201     -20.955   8.407 -13.261  1.00 86.88           N  
ANISOU    9  N   ASN A 201    11050  10817  11144   -105    225  -1149       N  
ATOM     10  CA  ASN A 201     -21.407   8.423 -11.891  1.00 86.34           C  
ANISOU   10  CA  ASN A 201    11028  10676  11100   -107    227  -1113       C  
ATOM     11  C   ASN A 201     -20.238   8.000 -11.021  1.00 83.50           C  
ANISOU   11  C   ASN A 201    10762  10159  10805    -44    239  -1061       C  
ATOM     12  O   ASN A 201     -19.796   6.856 -11.069  1.00 80.05           O  
ANISOU   12  O   ASN A 201    10398   9626  10392    -64    299  -1100       O  
ATOM     13  CB  ASN A 201     -22.619   7.500 -11.733  1.00 90.58           C  
ANISOU   13  CB  ASN A 201    11583  11224  11610   -221    285  -1199       C  
ATOM     14  CG  ASN A 201     -22.715   6.876 -10.352  1.00 96.94           C  
ANISOU   14  CG  ASN A 201    12482  11890  12460   -232    318  -1181       C  
ATOM     15  OD1 ASN A 201     -22.440   7.517  -9.334  1.00 92.75           O  
ANISOU   15  OD1 ASN A 201    11968  11314  11961   -165    279  -1099       O  
ATOM     16  ND2 ASN A 201     -23.123   5.614 -10.314  1.00103.55           N  
ANISOU   16  ND2 ASN A 201    13384  12663  13299   -321    399  -1261       N  
ATOM     17  N   VAL A 202     -19.730   8.950 -10.245  1.00 84.29           N  
ANISOU   17  N   VAL A 202    10857  10241  10928     34    187   -973       N  
ATOM     18  CA  VAL A 202     -18.514   8.767  -9.465  1.00 81.55           C  
ANISOU   18  CA  VAL A 202    10575   9783  10628    106    186   -913       C  
ATOM     19  C   VAL A 202     -18.642   7.699  -8.377  1.00 80.24           C  
ANISOU   19  C   VAL A 202    10499   9494  10494     86    242   -917       C  
ATOM     20  O   VAL A 202     -17.639   7.186  -7.870  1.00 70.07           O  
ANISOU   20  O   VAL A 202     9272   8113   9239    144    263   -878       O  
ATOM     21  CB  VAL A 202     -18.069  10.112  -8.854  1.00 75.71           C  
ANISOU   21  CB  VAL A 202     9802   9071   9895    176    122   -827       C  
ATOM     22  CG1 VAL A 202     -17.315   9.898  -7.564  1.00 72.78           C  
ANISOU   22  CG1 VAL A 202     9492   8600   9560    224    127   -769       C  
ATOM     23  CG2 VAL A 202     -17.241  10.898  -9.866  1.00 70.20           C  
ANISOU   23  CG2 VAL A 202     9050   8440   9182    224     85   -807       C  
ATOM     24  N   ASN A 203     -19.882   7.357  -8.039  1.00 85.64           N  
ANISOU   24  N   ASN A 203    11189  10186  11163      8    269   -962       N  
ATOM     25  CA  ASN A 203     -20.158   6.390  -6.980  1.00 86.16           C  
ANISOU   25  CA  ASN A 203    11341  10140  11257    -19    325   -967       C  
ATOM     26  C   ASN A 203     -20.550   5.012  -7.503  1.00 90.15           C  
ANISOU   26  C   ASN A 203    11906  10589  11758   -101    416  -1058       C  
ATOM     27  O   ASN A 203     -20.916   4.126  -6.729  1.00 92.41           O  
ANISOU   27  O   ASN A 203    12269  10778  12063   -137    479  -1074       O  
ATOM     28  CB  ASN A 203     -21.242   6.934  -6.052  1.00 80.17           C  
ANISOU   28  CB  ASN A 203    10559   9415  10487    -52    299   -951       C  
ATOM     29  CG  ASN A 203     -20.756   8.102  -5.226  1.00 72.85           C  
ANISOU   29  CG  ASN A 203     9604   8501   9574     27    232   -859       C  
ATOM     30  OD1 ASN A 203     -19.763   7.992  -4.510  1.00 71.07           O  
ANISOU   30  OD1 ASN A 203     9421   8200   9380     94    231   -800       O  
ATOM     31  ND2 ASN A 203     -21.452   9.230  -5.322  1.00 72.14           N  
ANISOU   31  ND2 ASN A 203     9441   8514   9455     21    181   -846       N  
ATOM     32  N   GLU A 204     -20.466   4.845  -8.819  1.00 89.69           N  
ANISOU   32  N   GLU A 204    11812  10591  11674   -133    428  -1120       N  
ATOM     33  CA  GLU A 204     -20.799   3.587  -9.480  1.00 90.75           C  
ANISOU   33  CA  GLU A 204    11999  10684  11799   -223    521  -1219       C  
ATOM     34  C   GLU A 204     -19.942   2.433  -8.954  1.00 90.71           C  
ANISOU   34  C   GLU A 204    12118  10505  11843   -182    603  -1202       C  
ATOM     35  O   GLU A 204     -20.463   1.373  -8.604  1.00 91.42           O  
ANISOU   35  O   GLU A 204    12291  10504  11941   -252    694  -1254       O  
ATOM     36  CB  GLU A 204     -20.639   3.743 -10.993  1.00 98.32           C  
ANISOU   36  CB  GLU A 204    12890  11747  12722   -247    510  -1276       C  
ATOM     37  CG  GLU A 204     -20.808   2.472 -11.797  1.00108.98           C  
ANISOU   37  CG  GLU A 204    14293  13055  14060   -339    610  -1385       C  
ATOM     38  CD  GLU A 204     -20.200   2.593 -13.184  1.00120.21           C  
ANISOU   38  CD  GLU A 204    15662  14551  15461   -328    597  -1418       C  
ATOM     39  OE1 GLU A 204     -20.607   3.502 -13.941  1.00123.81           O  
ANISOU   39  OE1 GLU A 204    16004  15167  15869   -339    532  -1426       O  
ATOM     40  OE2 GLU A 204     -19.310   1.781 -13.517  1.00124.12           O  
ANISOU   40  OE2 GLU A 204    16230  14945  15984   -301    656  -1432       O  
ATOM     41  N   ASN A 205     -18.629   2.643  -8.891  1.00 88.87           N  
ANISOU   41  N   ASN A 205    11898  10230  11637    -68    577  -1127       N  
ATOM     42  CA  ASN A 205     -17.724   1.623  -8.369  1.00 91.49           C  
ANISOU   42  CA  ASN A 205    12341  10412  12009     -3    654  -1092       C  
ATOM     43  C   ASN A 205     -16.557   2.220  -7.589  1.00 94.67           C  
ANISOU   43  C   ASN A 205    12737  10800  12434    131    597   -974       C  
ATOM     44  O   ASN A 205     -16.342   3.429  -7.609  1.00 95.08           O  
ANISOU   44  O   ASN A 205    12702  10952  12472    168    501   -929       O  
ATOM     45  CB  ASN A 205     -17.214   0.719  -9.494  1.00 92.11           C  
ANISOU   45  CB  ASN A 205    12463  10448  12087    -19    728  -1157       C  
ATOM     46  CG  ASN A 205     -16.253   1.430 -10.424  1.00 90.41           C  
ANISOU   46  CG  ASN A 205    12174  10317  11860     49    660  -1131       C  
ATOM     47  OD1 ASN A 205     -15.111   1.706 -10.061  1.00 88.84           O  
ANISOU   47  OD1 ASN A 205    11981  10095  11679    164    628  -1045       O  
ATOM     48  ND2 ASN A 205     -16.708   1.719 -11.639  1.00 86.87           N  
ANISOU   48  ND2 ASN A 205    11653   9977  11377    -23    639  -1207       N  
ATOM     49  N   ASN A 206     -15.808   1.364  -6.902  1.00 96.29           N  
ANISOU   49  N   ASN A 206    13034  10884  12667    204    663   -925       N  
ATOM     50  CA  ASN A 206     -14.721   1.820  -6.044  1.00 94.61           C  
ANISOU   50  CA  ASN A 206    12813  10669  12464    328    618   -814       C  
ATOM     51  C   ASN A 206     -13.451   2.172  -6.815  1.00 95.69           C  
ANISOU   51  C   ASN A 206    12910  10856  12591    411    581   -782       C  
ATOM     52  O   ASN A 206     -12.563   2.835  -6.288  1.00 98.40           O  
ANISOU   52  O   ASN A 206    13215  11243  12928    499    523   -700       O  
ATOM     53  CB  ASN A 206     -14.434   0.798  -4.935  1.00 96.39           C  
ANISOU   53  CB  ASN A 206    13145  10765  12715    386    704   -761       C  
ATOM     54  CG  ASN A 206     -15.487   0.825  -3.825  1.00106.23           C  
ANISOU   54  CG  ASN A 206    14409  11985  13969    331    707   -756       C  
ATOM     55  OD1 ASN A 206     -15.391   0.092  -2.836  1.00109.09           O  
ANISOU   55  OD1 ASN A 206    14850  12251  14349    373    772   -709       O  
ATOM     56  ND2 ASN A 206     -16.496   1.680  -3.986  1.00106.37           N  
ANISOU   56  ND2 ASN A 206    14351  12094  13970    244    640   -800       N  
ATOM     57  N   ILE A 207     -13.372   1.729  -8.066  1.00 98.05           N  
ANISOU   57  N   ILE A 207    13215  11157  12884    376    615   -852       N  
ATOM     58  CA  ILE A 207     -12.243   2.061  -8.931  1.00100.39           C  
ANISOU   58  CA  ILE A 207    13468  11509  13168    443    579   -833       C  
ATOM     59  C   ILE A 207     -12.336   3.513  -9.406  1.00 94.22           C  
ANISOU   59  C   ILE A 207    12568  10869  12362    426    466   -828       C  
ATOM     60  O   ILE A 207     -11.334   4.234  -9.453  1.00 90.32           O  
ANISOU   60  O   ILE A 207    12026  10434  11858    502    407   -769       O  
ATOM     61  CB  ILE A 207     -12.195   1.131 -10.169  1.00105.13           C  
ANISOU   61  CB  ILE A 207    14110  12068  13768    403    656   -918       C  
ATOM     62  CG1 ILE A 207     -11.987  -0.327  -9.742  1.00104.37           C  
ANISOU   62  CG1 ILE A 207    14146  11814  13696    430    785   -918       C  
ATOM     63  CG2 ILE A 207     -11.115   1.588 -11.144  1.00103.72           C  
ANISOU   63  CG2 ILE A 207    13873  11963  13572    464    607   -903       C  
ATOM     64  CD1 ILE A 207     -12.134  -1.333 -10.874  1.00102.36           C  
ANISOU   64  CD1 ILE A 207    13949  11501  13442    367    882  -1017       C  
ATOM     65  N   LEU A 208     -13.554   3.925  -9.754  1.00 88.42           N  
ANISOU   65  N   LEU A 208    11789  10192  11614    327    444   -890       N  
ATOM     66  CA  LEU A 208     -13.841   5.275 -10.232  1.00 79.44           C  
ANISOU   66  CA  LEU A 208    10547   9186  10452    309    353   -886       C  
ATOM     67  C   LEU A 208     -13.926   6.261  -9.067  1.00 78.96           C  
ANISOU   67  C   LEU A 208    10458   9150  10394    341    292   -812       C  
ATOM     68  O   LEU A 208     -13.552   7.427  -9.201  1.00 80.42           O  
ANISOU   68  O   LEU A 208    10575   9416  10565    372    221   -773       O  
ATOM     69  CB  LEU A 208     -15.164   5.271 -11.000  1.00 75.00           C  
ANISOU   69  CB  LEU A 208     9947   8687   9865    198    362   -975       C  
ATOM     70  CG  LEU A 208     -15.473   6.391 -11.990  1.00 74.79           C  
ANISOU   70  CG  LEU A 208     9813   8802   9801    179    293   -991       C  
ATOM     71  CD1 LEU A 208     -14.378   6.504 -13.038  1.00 69.43           C  
ANISOU   71  CD1 LEU A 208     9108   8157   9117    230    277   -988       C  
ATOM     72  CD2 LEU A 208     -16.814   6.123 -12.652  1.00 77.25           C  
ANISOU   72  CD2 LEU A 208    10091   9180  10078     69    320  -1081       C  
ATOM     73  N   ARG A 209     -14.423   5.781  -7.928  1.00 73.57           N  
ANISOU   73  N   ARG A 209     9830   8393   9729    328    326   -796       N  
ATOM     74  CA  ARG A 209     -14.592   6.604  -6.736  1.00 66.24           C  
ANISOU   74  CA  ARG A 209     8881   7482   8804    349    278   -733       C  
ATOM     75  C   ARG A 209     -13.263   7.131  -6.223  1.00 63.87           C  
ANISOU   75  C   ARG A 209     8566   7197   8503    445    240   -651       C  
ATOM     76  O   ARG A 209     -13.179   8.260  -5.740  1.00 60.73           O  
ANISOU   76  O   ARG A 209     8118   6861   8097    458    180   -609       O  
ATOM     77  CB  ARG A 209     -15.275   5.803  -5.622  1.00 70.32           C  
ANISOU   77  CB  ARG A 209     9468   7910   9340    323    332   -732       C  
ATOM     78  CG  ARG A 209     -15.293   6.512  -4.258  1.00 61.12           C  
ANISOU   78  CG  ARG A 209     8290   6754   8181    354    289   -660       C  
ATOM     79  CD  ARG A 209     -16.348   7.613  -4.221  1.00 51.81           C  
ANISOU   79  CD  ARG A 209     7045   5656   6985    295    233   -676       C  
ATOM     80  NE  ARG A 209     -16.160   8.534  -3.104  1.00 52.39           N  
ANISOU   80  NE  ARG A 209     7094   5753   7060    330    185   -609       N  
ATOM     81  CZ  ARG A 209     -16.975   9.550  -2.837  1.00 53.52           C  
ANISOU   81  CZ  ARG A 209     7189   5954   7191    295    141   -607       C  
ATOM     82  NH1 ARG A 209     -18.032   9.777  -3.607  1.00 55.49           N  
ANISOU   82  NH1 ARG A 209     7404   6257   7423    234    137   -661       N  
ATOM     83  NH2 ARG A 209     -16.733  10.343  -1.805  1.00 46.63           N  
ANISOU   83  NH2 ARG A 209     6301   5096   6320    324    107   -550       N  
ATOM     84  N   GLU A 210     -12.228   6.303  -6.320  1.00 70.53           N  
ANISOU   84  N   GLU A 210     9456   7991   9354    511    282   -629       N  
ATOM     85  CA  GLU A 210     -10.910   6.661  -5.810  1.00 69.96           C  
ANISOU   85  CA  GLU A 210     9366   7946   9269    604    254   -552       C  
ATOM     86  C   GLU A 210     -10.296   7.761  -6.654  1.00 71.51           C  
ANISOU   86  C   GLU A 210     9484   8243   9443    614    186   -550       C  
ATOM     87  O   GLU A 210      -9.679   8.690  -6.128  1.00 74.65           O  
ANISOU   87  O   GLU A 210     9838   8703   9824    645    137   -498       O  
ATOM     88  CB  GLU A 210      -9.986   5.440  -5.785  1.00 77.10           C  
ANISOU   88  CB  GLU A 210    10338   8778  10179    681    323   -527       C  
ATOM     89  CG  GLU A 210     -10.267   4.477  -4.638  1.00 88.81           C  
ANISOU   89  CG  GLU A 210    11901  10163  11681    704    392   -495       C  
ATOM     90  CD  GLU A 210     -10.031   5.110  -3.278  1.00 96.24           C  
ANISOU   90  CD  GLU A 210    12812  11143  12609    742    351   -420       C  
ATOM     91  OE1 GLU A 210      -8.876   5.503  -2.998  1.00 97.03           O  
ANISOU   91  OE1 GLU A 210    12875  11310  12683    820    320   -358       O  
ATOM     92  OE2 GLU A 210     -11.000   5.214  -2.489  1.00 97.46           O  
ANISOU   92  OE2 GLU A 210    12979  11272  12777    691    350   -425       O  
ATOM     93  N   LYS A 211     -10.474   7.649  -7.967  1.00 68.55           N  
ANISOU   93  N   LYS A 211     9093   7889   9065    581    191   -609       N  
ATOM     94  CA  LYS A 211      -9.954   8.638  -8.899  1.00 70.85           C  
ANISOU   94  CA  LYS A 211     9313   8273   9333    588    134   -610       C  
ATOM     95  C   LYS A 211     -10.592   9.992  -8.599  1.00 63.44           C  
ANISOU   95  C   LYS A 211     8318   7400   8386    550     77   -597       C  
ATOM     96  O   LYS A 211      -9.918  11.024  -8.560  1.00 63.89           O  
ANISOU   96  O   LYS A 211     8331   7519   8426    576     32   -560       O  
ATOM     97  CB  LYS A 211     -10.236   8.206 -10.343  1.00 79.83           C  
ANISOU   97  CB  LYS A 211    10441   9423  10467    550    154   -682       C  
ATOM     98  CG  LYS A 211      -9.520   9.044 -11.397  1.00 84.52           C  
ANISOU   98  CG  LYS A 211    10968  10106  11038    571    105   -680       C  
ATOM     99  CD  LYS A 211      -9.746   8.511 -12.803  1.00 84.32           C  
ANISOU   99  CD  LYS A 211    10933  10098  11006    536    129   -751       C  
ATOM    100  CE  LYS A 211      -9.077   7.167 -12.995  1.00 90.60           C  
ANISOU  100  CE  LYS A 211    11795  10813  11814    571    195   -767       C  
ATOM    101  NZ  LYS A 211      -9.100   6.751 -14.427  1.00 98.66           N  
ANISOU  101  NZ  LYS A 211    12800  11862  12825    540    215   -837       N  
ATOM    102  N   PHE A 212     -11.899   9.969  -8.375  1.00 52.74           N  
ANISOU  102  N   PHE A 212     6969   6030   7039    487     87   -629       N  
ATOM    103  CA  PHE A 212     -12.642  11.158  -7.981  1.00 59.68           C  
ANISOU  103  CA  PHE A 212     7806   6960   7909    457     46   -614       C  
ATOM    104  C   PHE A 212     -12.021  11.824  -6.753  1.00 55.43           C  
ANISOU  104  C   PHE A 212     7269   6420   7372    494     21   -547       C  
ATOM    105  O   PHE A 212     -11.774  13.035  -6.731  1.00 51.77           O  
ANISOU  105  O   PHE A 212     6764   6013   6894    499    -17   -521       O  
ATOM    106  CB  PHE A 212     -14.105  10.779  -7.722  1.00 59.02           C  
ANISOU  106  CB  PHE A 212     7738   6855   7832    391     70   -655       C  
ATOM    107  CG  PHE A 212     -14.891  11.822  -6.983  1.00 55.33           C  
ANISOU  107  CG  PHE A 212     7243   6420   7358    370     38   -628       C  
ATOM    108  CD1 PHE A 212     -15.406  12.920  -7.647  1.00 49.03           C  
ANISOU  108  CD1 PHE A 212     6386   5705   6538    357      7   -631       C  
ATOM    109  CD2 PHE A 212     -15.135  11.688  -5.625  1.00 54.59           C  
ANISOU  109  CD2 PHE A 212     7185   6276   7282    369     46   -598       C  
ATOM    110  CE1 PHE A 212     -16.141  13.873  -6.974  1.00 43.40           C  
ANISOU  110  CE1 PHE A 212     5654   5017   5819    345    -12   -604       C  
ATOM    111  CE2 PHE A 212     -15.866  12.634  -4.948  1.00 50.73           C  
ANISOU  111  CE2 PHE A 212     6672   5814   6787    350     21   -576       C  
ATOM    112  CZ  PHE A 212     -16.369  13.734  -5.626  1.00 52.64           C  
ANISOU  112  CZ  PHE A 212     6861   6133   7007    339     -6   -579       C  
ATOM    113  N   GLU A 213     -11.754  11.033  -5.727  1.00 54.71           N  
ANISOU  113  N   GLU A 213     7226   6268   7295    519     49   -521       N  
ATOM    114  CA  GLU A 213     -11.216  11.613  -4.509  1.00 63.81           C  
ANISOU  114  CA  GLU A 213     8372   7434   8440    548     28   -462       C  
ATOM    115  C   GLU A 213      -9.844  12.244  -4.761  1.00 63.55           C  
ANISOU  115  C   GLU A 213     8301   7464   8381    594      0   -429       C  
ATOM    116  O   GLU A 213      -9.573  13.359  -4.305  1.00 61.64           O  
ANISOU  116  O   GLU A 213     8025   7274   8123    586    -32   -404       O  
ATOM    117  CB  GLU A 213     -11.205  10.591  -3.364  1.00 66.33           C  
ANISOU  117  CB  GLU A 213     8746   7684   8773    573     68   -435       C  
ATOM    118  CG  GLU A 213     -12.620  10.228  -2.880  1.00 74.81           C  
ANISOU  118  CG  GLU A 213     9852   8704   9868    514     91   -464       C  
ATOM    119  CD  GLU A 213     -12.660   9.095  -1.854  1.00 82.86           C  
ANISOU  119  CD  GLU A 213    10935   9643  10903    538    142   -439       C  
ATOM    120  OE1 GLU A 213     -11.721   8.980  -1.032  1.00 90.53           O  
ANISOU  120  OE1 GLU A 213    11912  10622  11865    602    145   -379       O  
ATOM    121  OE2 GLU A 213     -13.647   8.325  -1.864  1.00 77.46           O  
ANISOU  121  OE2 GLU A 213    10296   8897  10238    492    184   -479       O  
ATOM    122  N   ASN A 214      -8.995  11.548  -5.513  1.00 69.36           N  
ANISOU  122  N   ASN A 214     9045   8199   9111    638     16   -435       N  
ATOM    123  CA  ASN A 214      -7.651  12.047  -5.826  1.00 73.56           C  
ANISOU  123  CA  ASN A 214     9538   8800   9612    682    -10   -407       C  
ATOM    124  C   ASN A 214      -7.652  13.358  -6.613  1.00 61.01           C  
ANISOU  124  C   ASN A 214     7895   7277   8008    647    -50   -423       C  
ATOM    125  O   ASN A 214      -6.844  14.263  -6.354  1.00 56.56           O  
ANISOU  125  O   ASN A 214     7298   6775   7417    654    -75   -395       O  
ATOM    126  CB  ASN A 214      -6.857  10.986  -6.586  1.00 86.50           C  
ANISOU  126  CB  ASN A 214    11197  10421  11246    737     20   -413       C  
ATOM    127  CG  ASN A 214      -6.370   9.868  -5.686  1.00 95.90           C  
ANISOU  127  CG  ASN A 214    12436  11564  12437    801     65   -371       C  
ATOM    128  OD1 ASN A 214      -5.639  10.105  -4.722  1.00 97.46           O  
ANISOU  128  OD1 ASN A 214    12616  11807  12608    841     54   -317       O  
ATOM    129  ND2 ASN A 214      -6.762   8.639  -6.005  1.00 99.44           N  
ANISOU  129  ND2 ASN A 214    12946  11925  12911    811    122   -397       N  
ATOM    130  N   TYR A 215      -8.562  13.446  -7.578  1.00 50.87           N  
ANISOU  130  N   TYR A 215     6605   5985   6737    609    -50   -467       N  
ATOM    131  CA  TYR A 215      -8.725  14.650  -8.378  1.00 47.20           C  
ANISOU  131  CA  TYR A 215     6095   5579   6259    584    -79   -477       C  
ATOM    132  C   TYR A 215      -9.319  15.783  -7.569  1.00 46.21           C  
ANISOU  132  C   TYR A 215     5961   5463   6132    552    -91   -455       C  
ATOM    133  O   TYR A 215      -8.905  16.932  -7.723  1.00 48.76           O  
ANISOU  133  O   TYR A 215     6257   5831   6437    546   -107   -439       O  
ATOM    134  CB  TYR A 215      -9.614  14.375  -9.591  1.00 59.27           C  
ANISOU  134  CB  TYR A 215     7612   7112   7794    557    -71   -526       C  
ATOM    135  CG  TYR A 215      -8.929  13.601 -10.690  1.00 60.43           C  
ANISOU  135  CG  TYR A 215     7756   7268   7936    582    -62   -554       C  
ATOM    136  CD1 TYR A 215      -7.729  12.946 -10.450  1.00 60.71           C  
ANISOU  136  CD1 TYR A 215     7812   7288   7967    634    -52   -532       C  
ATOM    137  CD2 TYR A 215      -9.494  13.503 -11.957  1.00 59.22           C  
ANISOU  137  CD2 TYR A 215     7577   7147   7778    558    -59   -600       C  
ATOM    138  CE1 TYR A 215      -7.098  12.230 -11.437  1.00 65.61           C  
ANISOU  138  CE1 TYR A 215     8433   7912   8583    661    -39   -555       C  
ATOM    139  CE2 TYR A 215      -8.873  12.783 -12.953  1.00 58.81           C  
ANISOU  139  CE2 TYR A 215     7523   7101   7721    576    -47   -630       C  
ATOM    140  CZ  TYR A 215      -7.673  12.148 -12.686  1.00 62.30           C  
ANISOU  140  CZ  TYR A 215     7993   7516   8164    629    -37   -607       C  
ATOM    141  OH  TYR A 215      -7.044  11.424 -13.667  1.00 68.58           O  
ANISOU  141  OH  TYR A 215     8789   8314   8954    652    -21   -635       O  
ATOM    142  N   ALA A 216     -10.297  15.466  -6.720  1.00 48.78           N  
ANISOU  142  N   ALA A 216     6313   5744   6476    528    -78   -457       N  
ATOM    143  CA  ALA A 216     -10.918  16.480  -5.859  1.00 49.29           C  
ANISOU  143  CA  ALA A 216     6375   5813   6542    499    -85   -437       C  
ATOM    144  C   ALA A 216      -9.906  17.123  -4.925  1.00 43.58           C  
ANISOU  144  C   ALA A 216     5646   5112   5801    508    -93   -400       C  
ATOM    145  O   ALA A 216      -9.958  18.327  -4.682  1.00 39.65           O  
ANISOU  145  O   ALA A 216     5136   4638   5293    484    -97   -388       O  
ATOM    146  CB  ALA A 216     -12.064  15.896  -5.057  1.00 46.96           C  
ANISOU  146  CB  ALA A 216     6109   5468   6267    473    -69   -446       C  
ATOM    147  N   ARG A 217      -8.981  16.327  -4.401  1.00 48.76           N  
ANISOU  147  N   ARG A 217     6311   5766   6449    541    -89   -382       N  
ATOM    148  CA  ARG A 217      -7.978  16.884  -3.503  1.00 56.87           C  
ANISOU  148  CA  ARG A 217     7321   6840   7447    546    -97   -349       C  
ATOM    149  C   ARG A 217      -7.082  17.877  -4.236  1.00 56.49           C  
ANISOU  149  C   ARG A 217     7239   6855   7369    539   -110   -352       C  
ATOM    150  O   ARG A 217      -6.673  18.895  -3.669  1.00 55.19           O  
ANISOU  150  O   ARG A 217     7059   6730   7181    508   -110   -342       O  
ATOM    151  CB  ARG A 217      -7.139  15.792  -2.845  1.00 60.95           C  
ANISOU  151  CB  ARG A 217     7846   7361   7949    598    -87   -322       C  
ATOM    152  CG  ARG A 217      -6.151  16.357  -1.835  1.00 74.08           C  
ANISOU  152  CG  ARG A 217     9479   9099   9570    598    -94   -289       C  
ATOM    153  CD  ARG A 217      -5.390  15.262  -1.119  1.00 82.85           C  
ANISOU  153  CD  ARG A 217    10592  10228  10659    662    -80   -250       C  
ATOM    154  NE  ARG A 217      -4.111  15.752  -0.614  1.00 92.94           N  
ANISOU  154  NE  ARG A 217    11820  11617  11877    673    -90   -225       N  
ATOM    155  CZ  ARG A 217      -3.035  15.940  -1.375  1.00102.81           C  
ANISOU  155  CZ  ARG A 217    13037  12938  13091    693   -101   -227       C  
ATOM    156  NH1 ARG A 217      -3.093  15.683  -2.677  1.00108.83           N  
ANISOU  156  NH1 ARG A 217    13811  13663  13875    709   -104   -252       N  
ATOM    157  NH2 ARG A 217      -1.903  16.384  -0.840  1.00102.49           N  
ANISOU  157  NH2 ARG A 217    12944  13012  12985    694   -108   -208       N  
ATOM    158  N   ILE A 218      -6.780  17.577  -5.498  1.00 52.90           N  
ANISOU  158  N   ILE A 218     6774   6411   6914    563   -115   -370       N  
ATOM    159  CA  ILE A 218      -6.021  18.501  -6.338  1.00 49.52           C  
ANISOU  159  CA  ILE A 218     6315   6039   6460    555   -126   -375       C  
ATOM    160  C   ILE A 218      -6.764  19.826  -6.517  1.00 46.45           C  
ANISOU  160  C   ILE A 218     5927   5645   6078    511   -118   -380       C  
ATOM    161  O   ILE A 218      -6.193  20.899  -6.316  1.00 48.87           O  
ANISOU  161  O   ILE A 218     6224   5986   6359    483   -111   -373       O  
ATOM    162  CB  ILE A 218      -5.714  17.882  -7.730  1.00 56.60           C  
ANISOU  162  CB  ILE A 218     7201   6945   7360    589   -133   -395       C  
ATOM    163  CG1 ILE A 218      -4.781  16.677  -7.590  1.00 51.89           C  
ANISOU  163  CG1 ILE A 218     6608   6356   6751    642   -130   -384       C  
ATOM    164  CG2 ILE A 218      -5.117  18.924  -8.681  1.00 42.87           C  
ANISOU  164  CG2 ILE A 218     5431   5260   5597    577   -142   -400       C  
ATOM    165  CD1 ILE A 218      -4.504  15.985  -8.914  1.00 50.22           C  
ANISOU  165  CD1 ILE A 218     6391   6146   6544    674   -131   -408       C  
ATOM    166  N   VAL A 219      -8.040  19.748  -6.892  1.00 43.66           N  
ANISOU  166  N   VAL A 219     5585   5251   5751    505   -113   -393       N  
ATOM    167  CA  VAL A 219      -8.860  20.948  -7.062  1.00 43.86           C  
ANISOU  167  CA  VAL A 219     5614   5273   5780    480    -98   -388       C  
ATOM    168  C   VAL A 219      -8.926  21.704  -5.741  1.00 50.41           C  
ANISOU  168  C   VAL A 219     6461   6086   6604    445    -82   -371       C  
ATOM    169  O   VAL A 219      -8.910  22.938  -5.703  1.00 47.43           O  
ANISOU  169  O   VAL A 219     6091   5713   6216    421    -59   -362       O  
ATOM    170  CB  VAL A 219     -10.274  20.594  -7.586  1.00 41.66           C  
ANISOU  170  CB  VAL A 219     5335   4973   5520    484    -95   -402       C  
ATOM    171  CG1 VAL A 219     -11.226  21.779  -7.493  1.00 39.31           C  
ANISOU  171  CG1 VAL A 219     5042   4672   5221    470    -74   -386       C  
ATOM    172  CG2 VAL A 219     -10.170  20.128  -9.008  1.00 47.51           C  
ANISOU  172  CG2 VAL A 219     6050   5746   6256    507   -104   -424       C  
ATOM    173  N   PHE A 220      -8.980  20.948  -4.652  1.00 56.65           N  
ANISOU  173  N   PHE A 220     7263   6857   7403    443    -88   -366       N  
ATOM    174  CA  PHE A 220      -8.991  21.537  -3.327  1.00 56.65           C  
ANISOU  174  CA  PHE A 220     7276   6852   7396    408    -75   -353       C  
ATOM    175  C   PHE A 220      -7.747  22.400  -3.092  1.00 48.14           C  
ANISOU  175  C   PHE A 220     6183   5827   6280    381    -66   -350       C  
ATOM    176  O   PHE A 220      -7.846  23.547  -2.645  1.00 43.87           O  
ANISOU  176  O   PHE A 220     5656   5284   5731    337    -38   -351       O  
ATOM    177  CB  PHE A 220      -9.116  20.457  -2.253  1.00 55.00           C  
ANISOU  177  CB  PHE A 220     7076   6625   7197    419    -84   -344       C  
ATOM    178  CG  PHE A 220      -9.381  21.007  -0.888  1.00 66.58           C  
ANISOU  178  CG  PHE A 220     8552   8085   8659    381    -72   -332       C  
ATOM    179  CD1 PHE A 220     -10.640  21.478  -0.551  1.00 74.10           C  
ANISOU  179  CD1 PHE A 220     9527   8994   9635    358    -59   -334       C  
ATOM    180  CD2 PHE A 220      -8.371  21.075   0.060  1.00 73.93           C  
ANISOU  180  CD2 PHE A 220     9466   9067   9557    368    -71   -320       C  
ATOM    181  CE1 PHE A 220     -10.889  21.993   0.709  1.00 75.02           C  
ANISOU  181  CE1 PHE A 220     9653   9104   9747    322    -46   -326       C  
ATOM    182  CE2 PHE A 220      -8.620  21.590   1.325  1.00 76.99           C  
ANISOU  182  CE2 PHE A 220     9858   9458   9937    327    -58   -315       C  
ATOM    183  CZ  PHE A 220      -9.880  22.048   1.648  1.00 73.41           C  
ANISOU  183  CZ  PHE A 220     9433   8948   9513    303    -45   -318       C  
ATOM    184  N   GLN A 221      -6.577  21.852  -3.392  1.00 54.78           N  
ANISOU  184  N   GLN A 221     6999   6719   7096    404    -82   -350       N  
ATOM    185  CA  GLN A 221      -5.328  22.596  -3.211  1.00 55.04           C  
ANISOU  185  CA  GLN A 221     7008   6822   7081    373    -74   -353       C  
ATOM    186  C   GLN A 221      -5.216  23.797  -4.151  1.00 55.35           C  
ANISOU  186  C   GLN A 221     7055   6863   7114    345    -51   -366       C  
ATOM    187  O   GLN A 221      -4.636  24.813  -3.778  1.00 55.22           O  
ANISOU  187  O   GLN A 221     7039   6877   7066    290    -23   -375       O  
ATOM    188  CB  GLN A 221      -4.128  21.676  -3.370  1.00 58.05           C  
ANISOU  188  CB  GLN A 221     7356   7270   7431    415    -97   -345       C  
ATOM    189  CG  GLN A 221      -4.111  20.524  -2.388  1.00 71.42           C  
ANISOU  189  CG  GLN A 221     9047   8966   9124    452   -107   -323       C  
ATOM    190  CD  GLN A 221      -2.897  19.637  -2.582  1.00 90.16           C  
ANISOU  190  CD  GLN A 221    11389  11409  11460    509   -120   -306       C  
ATOM    191  OE1 GLN A 221      -1.778  19.993  -2.196  1.00 89.74           O  
ANISOU  191  OE1 GLN A 221    11295  11454  11349    496   -121   -301       O  
ATOM    192  NE2 GLN A 221      -3.109  18.476  -3.192  1.00 99.81           N  
ANISOU  192  NE2 GLN A 221    12628  12586  12711    572   -126   -300       N  
ATOM    193  N   PHE A 222      -5.787  23.680  -5.355  1.00 52.52           N  
ANISOU  193  N   PHE A 222     6700   6473   6781    379    -58   -367       N  
ATOM    194  CA  PHE A 222      -5.819  24.772  -6.339  1.00 46.68           C  
ANISOU  194  CA  PHE A 222     5969   5730   6037    368    -32   -370       C  
ATOM    195  C   PHE A 222      -6.640  25.967  -5.834  1.00 53.67           C  
ANISOU  195  C   PHE A 222     6893   6568   6932    330     15   -363       C  
ATOM    196  O   PHE A 222      -6.237  27.121  -5.989  1.00 56.64           O  
ANISOU  196  O   PHE A 222     7287   6945   7289    294     58   -365       O  
ATOM    197  CB  PHE A 222      -6.367  24.268  -7.696  1.00 36.76           C  
ANISOU  197  CB  PHE A 222     4701   4466   4802    419    -50   -370       C  
ATOM    198  CG  PHE A 222      -6.432  25.332  -8.774  1.00 46.03           C  
ANISOU  198  CG  PHE A 222     5878   5643   5968    421    -22   -364       C  
ATOM    199  CD1 PHE A 222      -5.468  26.325  -8.858  1.00 51.94           C  
ANISOU  199  CD1 PHE A 222     6634   6416   6687    384      7   -367       C  
ATOM    200  CD2 PHE A 222      -7.446  25.321  -9.719  1.00 52.94           C  
ANISOU  200  CD2 PHE A 222     6748   6507   6860    458    -20   -356       C  
ATOM    201  CE1 PHE A 222      -5.527  27.295  -9.850  1.00 39.86           C  
ANISOU  201  CE1 PHE A 222     5113   4881   5150    391     41   -356       C  
ATOM    202  CE2 PHE A 222      -7.513  26.286 -10.708  1.00 43.99           C  
ANISOU  202  CE2 PHE A 222     5616   5383   5716    471     10   -341       C  
ATOM    203  CZ  PHE A 222      -6.546  27.272 -10.772  1.00 42.77           C  
ANISOU  203  CZ  PHE A 222     5476   5236   5537    440     42   -339       C  
ATOM    204  N   ASN A 223      -7.799  25.695  -5.241  1.00 50.98           N  
ANISOU  204  N   ASN A 223     6569   6182   6620    339     15   -354       N  
ATOM    205  CA  ASN A 223      -8.616  26.767  -4.693  1.00 45.17           C  
ANISOU  205  CA  ASN A 223     5871   5399   5892    312     62   -344       C  
ATOM    206  C   ASN A 223      -7.891  27.423  -3.520  1.00 48.18           C  
ANISOU  206  C   ASN A 223     6267   5790   6248    245     91   -356       C  
ATOM    207  O   ASN A 223      -7.931  28.644  -3.355  1.00 55.06           O  
ANISOU  207  O   ASN A 223     7175   6635   7112    205    149   -358       O  
ATOM    208  CB  ASN A 223     -10.000  26.251  -4.285  1.00 40.87           C  
ANISOU  208  CB  ASN A 223     5335   4816   5379    336     51   -333       C  
ATOM    209  CG  ASN A 223     -10.932  26.044  -5.478  1.00 41.24           C  
ANISOU  209  CG  ASN A 223     5369   4862   5437    388     43   -323       C  
ATOM    210  OD1 ASN A 223     -10.919  26.816  -6.437  1.00 44.61           O  
ANISOU  210  OD1 ASN A 223     5797   5297   5854    407     70   -311       O  
ATOM    211  ND2 ASN A 223     -11.748  24.996  -5.416  1.00 38.64           N  
ANISOU  211  ND2 ASN A 223     5026   4531   5127    408     12   -330       N  
ATOM    212  N   ASN A 224      -7.208  26.609  -2.719  1.00 46.70           N  
ANISOU  212  N   ASN A 224     6052   5647   6046    232     58   -366       N  
ATOM    213  CA  ASN A 224      -6.340  27.128  -1.656  1.00 53.59           C  
ANISOU  213  CA  ASN A 224     6920   6563   6880    164     81   -383       C  
ATOM    214  C   ASN A 224      -5.269  28.118  -2.142  1.00 60.87           C  
ANISOU  214  C   ASN A 224     7843   7525   7762    115    118   -403       C  
ATOM    215  O   ASN A 224      -5.005  29.128  -1.490  1.00 59.74           O  
ANISOU  215  O   ASN A 224     7722   7382   7593     40    171   -424       O  
ATOM    216  CB  ASN A 224      -5.655  25.982  -0.915  1.00 49.10           C  
ANISOU  216  CB  ASN A 224     6307   6059   6289    178     36   -380       C  
ATOM    217  CG  ASN A 224      -6.585  25.256   0.036  1.00 61.08           C  
ANISOU  217  CG  ASN A 224     7832   7539   7836    197     19   -365       C  
ATOM    218  OD1 ASN A 224      -7.702  25.709   0.320  1.00 62.55           O  
ANISOU  218  OD1 ASN A 224     8054   7661   8053    186     40   -361       O  
ATOM    219  ND2 ASN A 224      -6.124  24.117   0.542  1.00 57.49           N  
ANISOU  219  ND2 ASN A 224     7347   7128   7368    230    -15   -352       N  
ATOM    220  N   SER A 225      -4.650  27.817  -3.281  1.00 61.70           N  
ANISOU  220  N   SER A 225     7924   7662   7857    150     95   -402       N  
ATOM    221  CA  SER A 225      -3.638  28.690  -3.866  1.00 59.44           C  
ANISOU  221  CA  SER A 225     7638   7415   7532    105    128   -422       C  
ATOM    222  C   SER A 225      -4.272  29.951  -4.441  1.00 55.57           C  
ANISOU  222  C   SER A 225     7205   6847   7060     90    195   -417       C  
ATOM    223  O   SER A 225      -3.780  31.051  -4.213  1.00 54.82           O  
ANISOU  223  O   SER A 225     7141   6751   6938     17    259   -439       O  
ATOM    224  CB  SER A 225      -2.834  27.948  -4.942  1.00 64.81           C  
ANISOU  224  CB  SER A 225     8275   8152   8199    154     82   -419       C  
ATOM    225  OG  SER A 225      -2.132  28.849  -5.786  1.00 63.57           O  
ANISOU  225  OG  SER A 225     8125   8013   8014    122    117   -433       O  
ATOM    226  N   ARG A 226      -5.363  29.792  -5.183  1.00 55.24           N  
ANISOU  226  N   ARG A 226     7180   6748   7062    158    188   -388       N  
ATOM    227  CA  ARG A 226      -6.073  30.939  -5.741  1.00 56.71           C  
ANISOU  227  CA  ARG A 226     7419   6866   7263    166    255   -369       C  
ATOM    228  C   ARG A 226      -6.375  31.925  -4.634  1.00 62.68           C  
ANISOU  228  C   ARG A 226     8228   7572   8016    101    325   -379       C  
ATOM    229  O   ARG A 226      -6.260  33.137  -4.803  1.00 65.54           O  
ANISOU  229  O   ARG A 226     8643   7891   8367     64    407   -381       O  
ATOM    230  CB  ARG A 226      -7.405  30.510  -6.355  1.00 49.97           C  
ANISOU  230  CB  ARG A 226     6562   5976   6447    249    234   -335       C  
ATOM    231  CG  ARG A 226      -7.282  29.630  -7.567  1.00 58.15           C  
ANISOU  231  CG  ARG A 226     7550   7056   7487    309    177   -329       C  
ATOM    232  CD  ARG A 226      -8.648  29.128  -8.014  1.00 57.08           C  
ANISOU  232  CD  ARG A 226     7404   6904   7380    375    157   -305       C  
ATOM    233  NE  ARG A 226      -9.547  30.223  -8.345  1.00 50.91           N  
ANISOU  233  NE  ARG A 226     6659   6082   6601    402    221   -271       N  
ATOM    234  CZ  ARG A 226     -10.870  30.133  -8.299  1.00 50.36           C  
ANISOU  234  CZ  ARG A 226     6591   5997   6546    445    224   -247       C  
ATOM    235  NH1 ARG A 226     -11.445  28.997  -7.926  1.00 48.65           N  
ANISOU  235  NH1 ARG A 226     6343   5797   6345    454    168   -260       N  
ATOM    236  NH2 ARG A 226     -11.617  31.180  -8.617  1.00 44.95           N  
ANISOU  236  NH2 ARG A 226     5939   5283   5856    480    290   -208       N  
ATOM    237  N   GLN A 227      -6.777  31.380  -3.495  1.00 64.24           N  
ANISOU  237  N   GLN A 227     8415   7770   8223     87    298   -385       N  
ATOM    238  CA  GLN A 227      -7.310  32.183  -2.412  1.00 73.87           C  
ANISOU  238  CA  GLN A 227     9683   8937   9447     36    359   -392       C  
ATOM    239  C   GLN A 227      -6.190  32.781  -1.570  1.00 72.77           C  
ANISOU  239  C   GLN A 227     9549   8840   9262    -71    400   -437       C  
ATOM    240  O   GLN A 227      -6.308  33.900  -1.075  1.00 76.48           O  
ANISOU  240  O   GLN A 227    10076   9260   9723   -134    485   -454       O  
ATOM    241  CB  GLN A 227      -8.248  31.336  -1.554  1.00 66.36           C  
ANISOU  241  CB  GLN A 227     8716   7976   8524     65    312   -379       C  
ATOM    242  CG  GLN A 227      -8.989  32.117  -0.511  1.00 64.78           C  
ANISOU  242  CG  GLN A 227     8564   7716   8332     25    370   -381       C  
ATOM    243  CD  GLN A 227     -10.091  31.306   0.138  1.00 64.21           C  
ANISOU  243  CD  GLN A 227     8477   7628   8290     66    324   -362       C  
ATOM    244  OE1 GLN A 227     -10.403  31.496   1.318  1.00 58.30           O  
ANISOU  244  OE1 GLN A 227     7744   6864   7542     23    342   -372       O  
ATOM    245  NE2 GLN A 227     -10.690  30.393  -0.630  1.00 54.84           N  
ANISOU  245  NE2 GLN A 227     7261   6448   7127    142    268   -338       N  
ATOM    246  N   ALA A 228      -5.107  32.030  -1.411  1.00 64.58           N  
ANISOU  246  N   ALA A 228     8449   7900   8188    -92    345   -459       N  
ATOM    247  CA  ALA A 228      -3.930  32.540  -0.729  1.00 66.46           C  
ANISOU  247  CA  ALA A 228     8674   8211   8367   -195    379   -506       C  
ATOM    248  C   ALA A 228      -3.085  33.312  -1.728  1.00 74.94           C  
ANISOU  248  C   ALA A 228     9764   9296   9412   -229    424   -523       C  
ATOM    249  O   ALA A 228      -1.987  33.764  -1.415  1.00 76.43           O  
ANISOU  249  O   ALA A 228     9939   9559   9543   -320    455   -568       O  
ATOM    250  CB  ALA A 228      -3.133  31.408  -0.127  1.00 65.60           C  
ANISOU  250  CB  ALA A 228     8486   8219   8222   -192    304   -513       C  
ATOM    251  N   ASN A 229      -3.612  33.454  -2.939  1.00 85.60           N  
ANISOU  251  N   ASN A 229    11143  10583  10800   -156    429   -489       N  
ATOM    252  CA  ASN A 229      -2.918  34.165  -4.004  1.00 90.20           C  
ANISOU  252  CA  ASN A 229    11744  11166  11360   -173    472   -497       C  
ATOM    253  C   ASN A 229      -1.469  33.709  -4.117  1.00 82.48           C  
ANISOU  253  C   ASN A 229    10700  10313  10325   -215    430   -531       C  
ATOM    254  O   ASN A 229      -0.554  34.527  -4.168  1.00 81.17           O  
ANISOU  254  O   ASN A 229    10548  10181  10111   -304    488   -570       O  
ATOM    255  CB  ASN A 229      -2.979  35.674  -3.756  1.00 99.17           C  
ANISOU  255  CB  ASN A 229    12966  12227  12487   -255    596   -519       C  
ATOM    256  CG  ASN A 229      -2.706  36.480  -5.008  1.00105.28           C  
ANISOU  256  CG  ASN A 229    13783  12961  13258   -244    656   -507       C  
ATOM    257  OD1 ASN A 229      -3.140  36.115  -6.101  1.00111.86           O  
ANISOU  257  OD1 ASN A 229    14603  13778  14120   -145    619   -462       O  
ATOM    258  ND2 ASN A 229      -1.984  37.581  -4.857  1.00104.92           N  
ANISOU  258  ND2 ASN A 229    13788  12903  13174   -349    754   -550       N  
ATOM    259  N   GLY A 230      -1.270  32.396  -4.152  1.00 82.02           N  
ANISOU  259  N   GLY A 230    10572  10324  10268   -151    335   -515       N  
ATOM    260  CA  GLY A 230       0.064  31.829  -4.124  1.00 85.29           C  
ANISOU  260  CA  GLY A 230    10917  10869  10622   -175    290   -539       C  
ATOM    261  C   GLY A 230       0.426  30.967  -5.318  1.00 87.34           C  
ANISOU  261  C   GLY A 230    11133  11163  10888    -89    225   -515       C  
ATOM    262  O   GLY A 230      -0.213  31.031  -6.365  1.00 79.29           O  
ANISOU  262  O   GLY A 230    10140  10074   9913    -28    225   -489       O  
ATOM    263  N   ASN A 231       1.466  30.154  -5.140  1.00100.02           N  
ANISOU  263  N   ASN A 231    12670  12888  12445    -82    172   -524       N  
ATOM    264  CA  ASN A 231       2.042  29.334  -6.206  1.00102.06           C  
ANISOU  264  CA  ASN A 231    12883  13196  12697    -10    116   -508       C  
ATOM    265  C   ASN A 231       1.460  27.927  -6.265  1.00104.59           C  
ANISOU  265  C   ASN A 231    13182  13496  13061     95     49   -473       C  
ATOM    266  O   ASN A 231       1.551  27.160  -5.297  1.00111.70           O  
ANISOU  266  O   ASN A 231    14054  14440  13948    110     21   -464       O  
ATOM    267  CB  ASN A 231       3.560  29.233  -6.031  1.00 99.66           C  
ANISOU  267  CB  ASN A 231    12516  13042  12308    -54    103   -535       C  
ATOM    268  CG  ASN A 231       4.261  30.563  -6.231  1.00105.50           C  
ANISOU  268  CG  ASN A 231    13276  13810  12999   -164    172   -578       C  
ATOM    269  OD1 ASN A 231       4.376  31.059  -7.356  1.00107.17           O  
ANISOU  269  OD1 ASN A 231    13511  13986  13221   -159    192   -579       O  
ATOM    270  ND2 ASN A 231       4.750  31.142  -5.138  1.00107.65           N  
ANISOU  270  ND2 ASN A 231    13540  14150  13214   -267    214   -617       N  
ATOM    271  N   PHE A 232       0.875  27.584  -7.408  1.00 92.10           N  
ANISOU  271  N   PHE A 232    11613  11853  11527    164     28   -453       N  
ATOM    272  CA  PHE A 232       0.357  26.242  -7.610  1.00 76.37           C  
ANISOU  272  CA  PHE A 232     9604   9839   9572    253    -26   -429       C  
ATOM    273  C   PHE A 232       0.515  25.812  -9.058  1.00 71.69           C  
ANISOU  273  C   PHE A 232     8996   9249   8993    312    -53   -425       C  
ATOM    274  O   PHE A 232       0.235  26.574  -9.987  1.00 76.00           O  
ANISOU  274  O   PHE A 232     9563   9761   9553    305    -29   -426       O  
ATOM    275  CB  PHE A 232      -1.104  26.144  -7.180  1.00 70.28           C  
ANISOU  275  CB  PHE A 232     8874   8969   8860    271    -18   -414       C  
ATOM    276  CG  PHE A 232      -1.559  24.738  -6.936  1.00 67.09           C  
ANISOU  276  CG  PHE A 232     8457   8549   8485    337    -61   -398       C  
ATOM    277  CD1 PHE A 232      -1.087  24.027  -5.848  1.00 61.87           C  
ANISOU  277  CD1 PHE A 232     7773   7935   7798    342    -77   -391       C  
ATOM    278  CD2 PHE A 232      -2.452  24.124  -7.797  1.00 60.51           C  
ANISOU  278  CD2 PHE A 232     7634   7659   7697    392    -79   -391       C  
ATOM    279  CE1 PHE A 232      -1.495  22.730  -5.624  1.00 58.98           C  
ANISOU  279  CE1 PHE A 232     7407   7543   7460    405   -104   -373       C  
ATOM    280  CE2 PHE A 232      -2.868  22.825  -7.576  1.00 55.17           C  
ANISOU  280  CE2 PHE A 232     6956   6961   7047    442   -106   -383       C  
ATOM    281  CZ  PHE A 232      -2.387  22.127  -6.491  1.00 60.15           C  
ANISOU  281  CZ  PHE A 232     7575   7622   7658    451   -116   -372       C  
ATOM    282  N   ASP A 233       0.982  24.584  -9.239  1.00 63.97           N  
ANISOU  282  N   ASP A 233     7984   8314   8009    372    -97   -417       N  
ATOM    283  CA  ASP A 233       1.214  24.039 -10.561  1.00 57.00           C  
ANISOU  283  CA  ASP A 233     7082   7441   7135    427   -123   -417       C  
ATOM    284  C   ASP A 233       0.300  22.842 -10.757  1.00 47.71           C  
ANISOU  284  C   ASP A 233     5916   6203   6009    492   -147   -407       C  
ATOM    285  O   ASP A 233       0.666  21.707 -10.453  1.00 48.08           O  
ANISOU  285  O   ASP A 233     5949   6270   6050    539   -168   -399       O  
ATOM    286  CB  ASP A 233       2.684  23.634 -10.719  1.00 64.81           C  
ANISOU  286  CB  ASP A 233     8022   8539   8064    441   -146   -421       C  
ATOM    287  CG  ASP A 233       3.076  23.380 -12.169  1.00 71.48           C  
ANISOU  287  CG  ASP A 233     8847   9403   8911    482   -166   -427       C  
ATOM    288  OD1 ASP A 233       2.178  23.160 -13.018  1.00 74.35           O  
ANISOU  288  OD1 ASP A 233     9228   9699   9323    514   -170   -426       O  
ATOM    289  OD2 ASP A 233       4.294  23.392 -12.455  1.00 75.26           O  
ANISOU  289  OD2 ASP A 233     9286   9974   9334    480   -177   -433       O  
ATOM    290  N   ILE A 234      -0.895  23.099 -11.274  1.00 43.69           N  
ANISOU  290  N   ILE A 234     5433   5623   5544    496   -136   -408       N  
ATOM    291  CA  ILE A 234      -1.886  22.042 -11.406  1.00 47.72           C  
ANISOU  291  CA  ILE A 234     5955   6079   6098    538   -150   -408       C  
ATOM    292  C   ILE A 234      -1.421  20.955 -12.383  1.00 50.57           C  
ANISOU  292  C   ILE A 234     6293   6463   6458    591   -175   -419       C  
ATOM    293  O   ILE A 234      -1.608  19.766 -12.126  1.00 55.55           O  
ANISOU  293  O   ILE A 234     6933   7068   7107    627   -182   -420       O  
ATOM    294  CB  ILE A 234      -3.296  22.609 -11.766  1.00 71.31           C  
ANISOU  294  CB  ILE A 234     8964   9009   9120    528   -132   -407       C  
ATOM    295  CG1 ILE A 234      -4.391  21.561 -11.508  1.00 75.89           C  
ANISOU  295  CG1 ILE A 234     9558   9539   9737    551   -140   -413       C  
ATOM    296  CG2 ILE A 234      -3.326  23.128 -13.194  1.00 64.77           C  
ANISOU  296  CG2 ILE A 234     8119   8204   8288    542   -129   -410       C  
ATOM    297  CD1 ILE A 234      -5.814  22.085 -11.652  1.00 79.34           C  
ANISOU  297  CD1 ILE A 234    10009   9938  10197    541   -122   -409       C  
ATOM    298  N   ALA A 235      -0.784  21.352 -13.480  1.00 51.59           N  
ANISOU  298  N   ALA A 235     6396   6638   6567    596   -182   -427       N  
ATOM    299  CA  ALA A 235      -0.307  20.380 -14.465  1.00 52.70           C  
ANISOU  299  CA  ALA A 235     6515   6803   6705    644   -203   -440       C  
ATOM    300  C   ALA A 235       0.684  19.428 -13.822  1.00 52.77           C  
ANISOU  300  C   ALA A 235     6517   6845   6690    680   -213   -430       C  
ATOM    301  O   ALA A 235       0.645  18.213 -14.037  1.00 50.12           O  
ANISOU  301  O   ALA A 235     6189   6485   6369    728   -215   -436       O  
ATOM    302  CB  ALA A 235       0.326  21.084 -15.657  1.00 47.34           C  
ANISOU  302  CB  ALA A 235     5806   6178   6002    640   -209   -447       C  
ATOM    303  N   ASN A 236       1.571  19.996 -13.019  1.00 62.54           N  
ANISOU  303  N   ASN A 236     7739   8140   7884    657   -211   -416       N  
ATOM    304  CA  ASN A 236       2.539  19.205 -12.272  1.00 67.32           C  
ANISOU  304  CA  ASN A 236     8328   8800   8452    697   -217   -397       C  
ATOM    305  C   ASN A 236       1.850  18.163 -11.395  1.00 57.96           C  
ANISOU  305  C   ASN A 236     7175   7548   7298    732   -206   -381       C  
ATOM    306  O   ASN A 236       2.277  17.010 -11.332  1.00 60.47           O  
ANISOU  306  O   ASN A 236     7496   7870   7611    798   -203   -367       O  
ATOM    307  CB  ASN A 236       3.403  20.123 -11.412  1.00 76.37           C  
ANISOU  307  CB  ASN A 236     9446  10031   9539    647   -213   -389       C  
ATOM    308  CG  ASN A 236       4.559  19.398 -10.771  1.00 82.80           C  
ANISOU  308  CG  ASN A 236    10225  10940  10296    694   -220   -365       C  
ATOM    309  OD1 ASN A 236       5.506  18.997 -11.451  1.00 89.33           O  
ANISOU  309  OD1 ASN A 236    11019  11834  11087    738   -234   -362       O  
ATOM    310  ND2 ASN A 236       4.497  19.232  -9.449  1.00 72.71           N  
ANISOU  310  ND2 ASN A 236     8948   9677   9002    691   -210   -344       N  
ATOM    311  N   GLU A 237       0.779  18.585 -10.726  1.00 49.01           N  
ANISOU  311  N   GLU A 237     6071   6353   6198    690   -194   -383       N  
ATOM    312  CA  GLU A 237      -0.005  17.713  -9.858  1.00 50.52           C  
ANISOU  312  CA  GLU A 237     6297   6476   6422    711   -181   -371       C  
ATOM    313  C   GLU A 237      -0.578  16.485 -10.557  1.00 52.98           C  
ANISOU  313  C   GLU A 237     6638   6719   6775    756   -173   -385       C  
ATOM    314  O   GLU A 237      -0.386  15.367 -10.084  1.00 50.31           O  
ANISOU  314  O   GLU A 237     6320   6357   6438    808   -156   -368       O  
ATOM    315  CB  GLU A 237      -1.137  18.501  -9.195  1.00 53.53           C  
ANISOU  315  CB  GLU A 237     6702   6804   6832    653   -171   -375       C  
ATOM    316  CG  GLU A 237      -0.655  19.590  -8.261  1.00 61.45           C  
ANISOU  316  CG  GLU A 237     7689   7862   7798    601   -166   -365       C  
ATOM    317  CD  GLU A 237       0.237  19.043  -7.163  1.00 70.78           C  
ANISOU  317  CD  GLU A 237     8850   9108   8936    627   -167   -338       C  
ATOM    318  OE1 GLU A 237       1.263  19.690  -6.854  1.00 76.91           O  
ANISOU  318  OE1 GLU A 237     9588   9981   9654    599   -169   -336       O  
ATOM    319  OE2 GLU A 237      -0.082  17.957  -6.623  1.00 64.97           O  
ANISOU  319  OE2 GLU A 237     8134   8333   8218    676   -161   -319       O  
ATOM    320  N   PHE A 238      -1.292  16.692 -11.667  1.00 51.07           N  
ANISOU  320  N   PHE A 238     6398   6447   6561    735   -176   -417       N  
ATOM    321  CA  PHE A 238      -1.897  15.578 -12.403  1.00 44.48           C  
ANISOU  321  CA  PHE A 238     5587   5556   5759    760   -162   -444       C  
ATOM    322  C   PHE A 238      -0.829  14.700 -13.047  1.00 49.24           C  
ANISOU  322  C   PHE A 238     6182   6186   6342    819   -159   -444       C  
ATOM    323  O   PHE A 238      -0.986  13.477 -13.142  1.00 47.07           O  
ANISOU  323  O   PHE A 238     5941   5856   6086    855   -131   -454       O  
ATOM    324  CB  PHE A 238      -2.866  16.083 -13.479  1.00 44.21           C  
ANISOU  324  CB  PHE A 238     5540   5513   5745    722   -167   -478       C  
ATOM    325  CG  PHE A 238      -4.168  16.588 -12.937  1.00 48.30           C  
ANISOU  325  CG  PHE A 238     6073   5990   6287    678   -159   -480       C  
ATOM    326  CD1 PHE A 238      -4.288  17.899 -12.508  1.00 42.61           C  
ANISOU  326  CD1 PHE A 238     5343   5291   5556    645   -165   -459       C  
ATOM    327  CD2 PHE A 238      -5.274  15.757 -12.864  1.00 52.24           C  
ANISOU  327  CD2 PHE A 238     6600   6432   6816    666   -140   -505       C  
ATOM    328  CE1 PHE A 238      -5.469  18.377 -12.012  1.00 41.55           C  
ANISOU  328  CE1 PHE A 238     5225   5123   5441    613   -155   -457       C  
ATOM    329  CE2 PHE A 238      -6.472  16.228 -12.361  1.00 49.89           C  
ANISOU  329  CE2 PHE A 238     6312   6109   6534    628   -135   -505       C  
ATOM    330  CZ  PHE A 238      -6.566  17.547 -11.935  1.00 51.95           C  
ANISOU  330  CZ  PHE A 238     6561   6393   6785    607   -144   -478       C  
ATOM    331  N   ILE A 239       0.249  15.334 -13.508  1.00 45.22           N  
ANISOU  331  N   ILE A 239     5629   5759   5792    827   -182   -435       N  
ATOM    332  CA  ILE A 239       1.373  14.593 -14.060  1.00 45.03           C  
ANISOU  332  CA  ILE A 239     5592   5776   5740    889   -181   -430       C  
ATOM    333  C   ILE A 239       1.820  13.588 -13.014  1.00 55.40           C  
ANISOU  333  C   ILE A 239     6932   7075   7043    951   -155   -393       C  
ATOM    334  O   ILE A 239       2.072  12.421 -13.324  1.00 66.65           O  
ANISOU  334  O   ILE A 239     8384   8466   8474   1012   -127   -392       O  
ATOM    335  CB  ILE A 239       2.554  15.523 -14.459  1.00 49.92           C  
ANISOU  335  CB  ILE A 239     6157   6503   6307    883   -210   -420       C  
ATOM    336  CG1 ILE A 239       2.331  16.100 -15.865  1.00 45.47           C  
ANISOU  336  CG1 ILE A 239     5571   5952   5753    853   -226   -454       C  
ATOM    337  CG2 ILE A 239       3.880  14.772 -14.394  1.00 43.35           C  
ANISOU  337  CG2 ILE A 239     5307   5736   5429    957   -208   -394       C  
ATOM    338  CD1 ILE A 239       2.975  17.460 -16.090  1.00 42.88           C  
ANISOU  338  CD1 ILE A 239     5203   5702   5387    811   -246   -449       C  
ATOM    339  N   SER A 240       1.891  14.046 -11.767  1.00 53.19           N  
ANISOU  339  N   SER A 240     6646   6820   6743    936   -158   -361       N  
ATOM    340  CA  SER A 240       2.293  13.195 -10.661  1.00 59.26           C  
ANISOU  340  CA  SER A 240     7433   7590   7495    998   -133   -316       C  
ATOM    341  C   SER A 240       1.318  12.044 -10.444  1.00 56.11           C  
ANISOU  341  C   SER A 240     7102   7069   7149   1021    -91   -322       C  
ATOM    342  O   SER A 240       1.720  10.907 -10.222  1.00 68.46           O  
ANISOU  342  O   SER A 240     8698   8606   8708   1098    -53   -295       O  
ATOM    343  CB  SER A 240       2.440  14.022  -9.383  1.00 67.32           C  
ANISOU  343  CB  SER A 240     8428   8669   8483    963   -146   -289       C  
ATOM    344  OG  SER A 240       2.777  13.193  -8.279  1.00 80.67           O  
ANISOU  344  OG  SER A 240    10129  10370  10151   1028   -120   -240       O  
ATOM    345  N   ILE A 241       0.033  12.334 -10.529  1.00 55.90           N  
ANISOU  345  N   ILE A 241     7100   6970   7171    954    -91   -358       N  
ATOM    346  CA  ILE A 241      -0.978  11.317 -10.272  1.00 60.69           C  
ANISOU  346  CA  ILE A 241     7771   7466   7824    956    -48   -371       C  
ATOM    347  C   ILE A 241      -1.119  10.332 -11.434  1.00 69.81           C  
ANISOU  347  C   ILE A 241     8958   8565   9003    976    -16   -412       C  
ATOM    348  O   ILE A 241      -1.510   9.173 -11.238  1.00 67.07           O  
ANISOU  348  O   ILE A 241     8673   8130   8682   1001     39   -418       O  
ATOM    349  CB  ILE A 241      -2.336  11.959  -9.934  1.00 58.70           C  
ANISOU  349  CB  ILE A 241     7527   7170   7606    876    -59   -397       C  
ATOM    350  CG1 ILE A 241      -2.274  12.573  -8.536  1.00 70.79           C  
ANISOU  350  CG1 ILE A 241     9047   8730   9120    865    -71   -355       C  
ATOM    351  CG2 ILE A 241      -3.442  10.939 -10.025  1.00 59.23           C  
ANISOU  351  CG2 ILE A 241     7653   7133   7718    861    -16   -430       C  
ATOM    352  CD1 ILE A 241      -3.618  12.898  -7.951  1.00 81.56           C  
ANISOU  352  CD1 ILE A 241    10434  10036  10520    804    -69   -370       C  
ATOM    353  N   LEU A 242      -0.779  10.790 -12.639  1.00 72.12           N  
ANISOU  353  N   LEU A 242     9210   8908   9284    961    -43   -442       N  
ATOM    354  CA  LEU A 242      -0.949   9.982 -13.847  1.00 68.74           C  
ANISOU  354  CA  LEU A 242     8804   8440   8875    965    -16   -491       C  
ATOM    355  C   LEU A 242       0.298   9.181 -14.217  1.00 74.34           C  
ANISOU  355  C   LEU A 242     9520   9168   9557   1052      7   -469       C  
ATOM    356  O   LEU A 242       0.209   8.208 -14.966  1.00 77.66           O  
ANISOU  356  O   LEU A 242     9980   9533   9997   1068     52   -504       O  
ATOM    357  CB  LEU A 242      -1.367  10.858 -15.036  1.00 59.51           C  
ANISOU  357  CB  LEU A 242     7585   7318   7707    904    -54   -536       C  
ATOM    358  CG  LEU A 242      -2.716  11.577 -14.952  1.00 57.29           C  
ANISOU  358  CG  LEU A 242     7295   7023   7448    827    -68   -561       C  
ATOM    359  CD1 LEU A 242      -2.898  12.536 -16.111  1.00 52.94           C  
ANISOU  359  CD1 LEU A 242     6689   6541   6886    790   -104   -587       C  
ATOM    360  CD2 LEU A 242      -3.859  10.576 -14.902  1.00 66.48           C  
ANISOU  360  CD2 LEU A 242     8511   8101   8647    795    -21   -603       C  
ATOM    361  N   SER A 243       1.455   9.587 -13.700  1.00 73.58           N  
ANISOU  361  N   SER A 243     9385   9157   9414   1104    -18   -415       N  
ATOM    362  CA  SER A 243       2.706   8.911 -14.038  1.00 78.23           C  
ANISOU  362  CA  SER A 243     9971   9787   9967   1195      1   -387       C  
ATOM    363  C   SER A 243       2.732   7.497 -13.466  1.00 82.50           C  
ANISOU  363  C   SER A 243    10587  10238  10521   1274     77   -358       C  
ATOM    364  O   SER A 243       3.430   6.619 -13.986  1.00 78.75           O  
ANISOU  364  O   SER A 243    10137   9751  10034   1350    118   -350       O  
ATOM    365  CB  SER A 243       3.908   9.707 -13.535  1.00 79.87           C  
ANISOU  365  CB  SER A 243    10111  10127  10108   1227    -42   -336       C  
ATOM    366  OG  SER A 243       3.833   9.885 -12.134  1.00 86.96           O  
ANISOU  366  OG  SER A 243    11010  11039  10992   1233    -40   -290       O  
ATOM    367  N   SER A 244       1.963   7.291 -12.397  1.00 85.43           N  
ANISOU  367  N   SER A 244    10999  10545  10917   1258    101   -341       N  
ATOM    368  CA  SER A 244       1.826   5.979 -11.765  1.00 90.91           C  
ANISOU  368  CA  SER A 244    11776  11137  11629   1326    184   -312       C  
ATOM    369  C   SER A 244       0.644   5.191 -12.327  1.00 93.76           C  
ANISOU  369  C   SER A 244    12212  11362  12049   1268    240   -382       C  
ATOM    370  O   SER A 244       0.495   3.999 -12.044  1.00 97.86           O  
ANISOU  370  O   SER A 244    12816  11778  12590   1315    325   -372       O  
ATOM    371  CB  SER A 244       1.670   6.129 -10.251  1.00 94.04           C  
ANISOU  371  CB  SER A 244    12175  11541  12014   1343    185   -254       C  
ATOM    372  OG  SER A 244       2.790   6.795  -9.693  1.00 98.11           O  
ANISOU  372  OG  SER A 244    12617  12196  12463   1391    140   -195       O  
ATOM    373  N   ALA A 245      -0.198   5.863 -13.111  1.00 87.35           N  
ANISOU  373  N   ALA A 245    11370  10558  11261   1165    200   -451       N  
ATOM    374  CA  ALA A 245      -1.308   5.205 -13.794  1.00 81.66           C  
ANISOU  374  CA  ALA A 245    10702   9742  10585   1095    248   -528       C  
ATOM    375  C   ALA A 245      -0.767   4.276 -14.873  1.00 86.30           C  
ANISOU  375  C   ALA A 245    11322  10295  11172   1133    301   -562       C  
ATOM    376  O   ALA A 245       0.446   4.198 -15.080  1.00 90.86           O  
ANISOU  376  O   ALA A 245    11881  10927  11717   1219    295   -519       O  
ATOM    377  CB  ALA A 245      -2.233   6.234 -14.407  1.00 77.29           C  
ANISOU  377  CB  ALA A 245    10090   9237  10041    989    187   -584       C  
ATOM    378  N   ASN A 246      -1.663   3.577 -15.563  1.00 83.42           N  
ANISOU  378  N   ASN A 246    11006   9849  10839   1066    357   -641       N  
ATOM    379  CA  ASN A 246      -1.251   2.657 -16.622  1.00 85.98           C  
ANISOU  379  CA  ASN A 246    11369  10133  11165   1088    419   -685       C  
ATOM    380  C   ASN A 246      -2.326   2.383 -17.673  1.00 77.63           C  
ANISOU  380  C   ASN A 246    10320   9046  10129    973    446   -794       C  
ATOM    381  O   ASN A 246      -3.500   2.202 -17.353  1.00 76.91           O  
ANISOU  381  O   ASN A 246    10258   8902  10061    890    473   -837       O  
ATOM    382  CB  ASN A 246      -0.733   1.347 -16.023  1.00 96.21           C  
ANISOU  382  CB  ASN A 246    12769  11318  12469   1185    524   -643       C  
ATOM    383  CG  ASN A 246      -1.460   0.964 -14.749  1.00106.07           C  
ANISOU  383  CG  ASN A 246    14082  12478  13741   1177    570   -614       C  
ATOM    384  OD1 ASN A 246      -2.685   0.817 -14.734  1.00105.46           O  
ANISOU  384  OD1 ASN A 246    14034  12342  13694   1074    594   -678       O  
ATOM    385  ND2 ASN A 246      -0.706   0.802 -13.667  1.00113.34           N  
ANISOU  385  ND2 ASN A 246    15020  13401  14643   1287    583   -517       N  
ATOM    386  N   GLY A 247      -1.913   2.356 -18.932  1.00 73.87           N  
ANISOU  386  N   GLY A 247     9811   8617   9640    965    438   -840       N  
ATOM    387  CA  GLY A 247      -2.840   2.140 -20.023  1.00 79.67           C  
ANISOU  387  CA  GLY A 247    10535   9352  10382    856    461   -945       C  
ATOM    388  C   GLY A 247      -2.524   3.021 -21.216  1.00 87.68           C  
ANISOU  388  C   GLY A 247    11448  10497  11369    835    382   -970       C  
ATOM    389  O   GLY A 247      -1.576   3.809 -21.188  1.00 94.29           O  
ANISOU  389  O   GLY A 247    12228  11414  12184    902    312   -906       O  
ATOM    390  N   THR A 248      -3.317   2.877 -22.271  1.00 83.51           N  
ANISOU  390  N   THR A 248    10895   9996  10838    740    397  -1063       N  
ATOM    391  CA  THR A 248      -3.151   3.675 -23.475  1.00 75.97           C  
ANISOU  391  CA  THR A 248     9842   9169   9856    714    330  -1090       C  
ATOM    392  C   THR A 248      -3.613   5.105 -23.238  1.00 72.71           C  
ANISOU  392  C   THR A 248     9341   8857   9428    690    234  -1052       C  
ATOM    393  O   THR A 248      -2.877   6.058 -23.497  1.00 74.44           O  
ANISOU  393  O   THR A 248     9495   9162   9627    734    163  -1004       O  
ATOM    394  CB  THR A 248      -3.954   3.080 -24.642  1.00 76.97           C  
ANISOU  394  CB  THR A 248     9960   9309   9974    614    379  -1204       C  
ATOM    395  OG1 THR A 248      -3.338   1.858 -25.059  1.00 82.38           O  
ANISOU  395  OG1 THR A 248    10723   9907  10670    642    469  -1241       O  
ATOM    396  CG2 THR A 248      -4.006   4.055 -25.819  1.00 80.49           C  
ANISOU  396  CG2 THR A 248    10290   9907  10387    582    302  -1226       C  
ATOM    397  N   ARG A 249      -4.836   5.250 -22.741  1.00 67.77           N  
ANISOU  397  N   ARG A 249     8719   8220   8811    618    240  -1074       N  
ATOM    398  CA  ARG A 249      -5.408   6.568 -22.529  1.00 65.31           C  
ANISOU  398  CA  ARG A 249     8332   7997   8486    594    164  -1041       C  
ATOM    399  C   ARG A 249      -4.625   7.331 -21.467  1.00 64.14           C  
ANISOU  399  C   ARG A 249     8185   7843   8342    670    115   -943       C  
ATOM    400  O   ARG A 249      -4.390   8.534 -21.599  1.00 61.98           O  
ANISOU  400  O   ARG A 249     7845   7654   8049    683     48   -903       O  
ATOM    401  CB  ARG A 249      -6.880   6.459 -22.132  1.00 66.22           C  
ANISOU  401  CB  ARG A 249     8456   8099   8606    508    188  -1083       C  
ATOM    402  CG  ARG A 249      -7.777   5.894 -23.223  1.00 68.35           C  
ANISOU  402  CG  ARG A 249     8702   8413   8856    414    230  -1187       C  
ATOM    403  CD  ARG A 249      -7.597   6.641 -24.533  1.00 66.70           C  
ANISOU  403  CD  ARG A 249     8393   8340   8610    409    178  -1203       C  
ATOM    404  NE  ARG A 249      -8.705   6.420 -25.459  1.00 64.39           N  
ANISOU  404  NE  ARG A 249     8048   8134   8284    311    202  -1293       N  
ATOM    405  CZ  ARG A 249      -8.736   6.883 -26.706  1.00 57.30           C  
ANISOU  405  CZ  ARG A 249     7059   7366   7346    294    171  -1322       C  
ATOM    406  NH1 ARG A 249      -7.718   7.589 -27.178  1.00 50.67           N  
ANISOU  406  NH1 ARG A 249     6178   6571   6501    367    116  -1268       N  
ATOM    407  NH2 ARG A 249      -9.784   6.645 -27.481  1.00 57.90           N  
ANISOU  407  NH2 ARG A 249     7080   7536   7382    202    196  -1405       N  
ATOM    408  N   ASN A 250      -4.211   6.627 -20.421  1.00 58.77           N  
ANISOU  408  N   ASN A 250     7581   7066   7681    719    156   -906       N  
ATOM    409  CA  ASN A 250      -3.493   7.270 -19.332  1.00 65.41           C  
ANISOU  409  CA  ASN A 250     8419   7914   8519    784    116   -819       C  
ATOM    410  C   ASN A 250      -2.117   7.767 -19.760  1.00 59.77           C  
ANISOU  410  C   ASN A 250     7661   7272   7777    853     72   -776       C  
ATOM    411  O   ASN A 250      -1.645   8.802 -19.284  1.00 58.47           O  
ANISOU  411  O   ASN A 250     7454   7167   7594    874     16   -721       O  
ATOM    412  CB  ASN A 250      -3.408   6.345 -18.115  1.00 83.12           C  
ANISOU  412  CB  ASN A 250    10749  10049  10783    825    174   -786       C  
ATOM    413  CG  ASN A 250      -4.752   6.186 -17.411  1.00 92.66           C  
ANISOU  413  CG  ASN A 250    11991  11201  12016    755    200   -810       C  
ATOM    414  OD1 ASN A 250      -5.236   7.110 -16.752  1.00 87.70           O  
ANISOU  414  OD1 ASN A 250    11329  10608  11386    732    152   -780       O  
ATOM    415  ND2 ASN A 250      -5.363   5.011 -17.558  1.00 99.46           N  
ANISOU  415  ND2 ASN A 250    12920  11973  12896    717    281   -869       N  
ATOM    416  N   ALA A 251      -1.484   7.034 -20.671  1.00 56.36           N  
ANISOU  416  N   ALA A 251     7239   6836   7338    882    102   -807       N  
ATOM    417  CA  ALA A 251      -0.215   7.471 -21.246  1.00 57.97           C  
ANISOU  417  CA  ALA A 251     7396   7120   7511    941     61   -776       C  
ATOM    418  C   ALA A 251      -0.461   8.703 -22.107  1.00 55.42           C  
ANISOU  418  C   ALA A 251     6986   6901   7169    891     -6   -791       C  
ATOM    419  O   ALA A 251       0.369   9.611 -22.183  1.00 49.85           O  
ANISOU  419  O   ALA A 251     6231   6273   6437    920    -59   -749       O  
ATOM    420  CB  ALA A 251       0.399   6.362 -22.076  1.00 55.06           C  
ANISOU  420  CB  ALA A 251     7060   6719   7141    980    114   -810       C  
ATOM    421  N   GLN A 252      -1.624   8.728 -22.745  1.00 53.14           N  
ANISOU  421  N   GLN A 252     6680   6619   6891    815      2   -851       N  
ATOM    422  CA  GLN A 252      -2.003   9.833 -23.609  1.00 48.25           C  
ANISOU  422  CA  GLN A 252     5980   6100   6251    775    -50   -863       C  
ATOM    423  C   GLN A 252      -2.347  11.085 -22.787  1.00 51.41           C  
ANISOU  423  C   GLN A 252     6358   6528   6650    765    -93   -808       C  
ATOM    424  O   GLN A 252      -1.934  12.195 -23.129  1.00 56.05           O  
ANISOU  424  O   GLN A 252     6893   7190   7216    774   -139   -776       O  
ATOM    425  CB  GLN A 252      -3.162   9.405 -24.505  1.00 46.31           C  
ANISOU  425  CB  GLN A 252     5718   5872   6007    701    -21   -942       C  
ATOM    426  CG  GLN A 252      -3.634  10.467 -25.465  1.00 63.31           C  
ANISOU  426  CG  GLN A 252     7782   8140   8131    669    -67   -950       C  
ATOM    427  CD  GLN A 252      -4.435   9.887 -26.615  1.00 69.29           C  
ANISOU  427  CD  GLN A 252     8507   8946   8874    607    -37  -1035       C  
ATOM    428  OE1 GLN A 252      -4.294  10.315 -27.762  1.00 64.59           O  
ANISOU  428  OE1 GLN A 252     7843   8449   8251    603    -63  -1051       O  
ATOM    429  NE2 GLN A 252      -5.279   8.901 -26.313  1.00 69.83           N  
ANISOU  429  NE2 GLN A 252     8624   8952   8958    553     20  -1092       N  
ATOM    430  N   LEU A 253      -3.077  10.898 -21.690  1.00 44.21           N  
ANISOU  430  N   LEU A 253     5489   5550   5759    746    -73   -797       N  
ATOM    431  CA  LEU A 253      -3.394  11.995 -20.763  1.00 48.78           C  
ANISOU  431  CA  LEU A 253     6057   6140   6338    737   -104   -746       C  
ATOM    432  C   LEU A 253      -2.164  12.566 -20.071  1.00 46.26           C  
ANISOU  432  C   LEU A 253     5736   5837   6003    788   -132   -683       C  
ATOM    433  O   LEU A 253      -1.990  13.786 -19.996  1.00 49.01           O  
ANISOU  433  O   LEU A 253     6048   6238   6335    780   -167   -651       O  
ATOM    434  CB  LEU A 253      -4.409  11.541 -19.710  1.00 49.70           C  
ANISOU  434  CB  LEU A 253     6222   6180   6480    706    -73   -751       C  
ATOM    435  CG  LEU A 253      -5.771  11.224 -20.309  1.00 46.49           C  
ANISOU  435  CG  LEU A 253     5805   5783   6078    639    -50   -814       C  
ATOM    436  CD1 LEU A 253      -6.545  10.304 -19.398  1.00 44.74           C  
ANISOU  436  CD1 LEU A 253     5647   5470   5882    611     -3   -834       C  
ATOM    437  CD2 LEU A 253      -6.514  12.514 -20.563  1.00 46.94           C  
ANISOU  437  CD2 LEU A 253     5800   5917   6116    613    -88   -797       C  
ATOM    438  N   LEU A 254      -1.315  11.685 -19.554  1.00 47.05           N  
ANISOU  438  N   LEU A 254     5876   5897   6103    840   -109   -666       N  
ATOM    439  CA  LEU A 254      -0.052  12.123 -18.965  1.00 49.25           C  
ANISOU  439  CA  LEU A 254     6141   6218   6353    890   -133   -610       C  
ATOM    440  C   LEU A 254       0.748  13.021 -19.918  1.00 44.13           C  
ANISOU  440  C   LEU A 254     5432   5664   5672    892   -174   -607       C  
ATOM    441  O   LEU A 254       1.353  14.003 -19.492  1.00 48.36           O  
ANISOU  441  O   LEU A 254     5940   6253   6181    891   -203   -570       O  
ATOM    442  CB  LEU A 254       0.789  10.924 -18.518  1.00 47.06           C  
ANISOU  442  CB  LEU A 254     5908   5902   6071    962    -96   -591       C  
ATOM    443  CG  LEU A 254       2.230  11.250 -18.116  1.00 47.76           C  
ANISOU  443  CG  LEU A 254     5967   6065   6113   1021   -120   -537       C  
ATOM    444  CD1 LEU A 254       2.290  12.068 -16.840  1.00 44.34           C  
ANISOU  444  CD1 LEU A 254     5524   5658   5664   1007   -141   -492       C  
ATOM    445  CD2 LEU A 254       3.052   9.981 -17.975  1.00 47.16           C  
ANISOU  445  CD2 LEU A 254     5929   5963   6026   1108    -77   -518       C  
ATOM    446  N   GLU A 255       0.759  12.713 -21.209  1.00 46.39           N  
ANISOU  446  N   GLU A 255     5696   5974   5957    890   -173   -648       N  
ATOM    447  CA  GLU A 255       1.541  13.562 -22.104  1.00 47.72           C  
ANISOU  447  CA  GLU A 255     5807   6232   6093    895   -211   -641       C  
ATOM    448  C   GLU A 255       0.850  14.905 -22.378  1.00 46.79           C  
ANISOU  448  C   GLU A 255     5652   6152   5972    844   -235   -636       C  
ATOM    449  O   GLU A 255       1.504  15.951 -22.455  1.00 44.61           O  
ANISOU  449  O   GLU A 255     5347   5934   5670    841   -260   -607       O  
ATOM    450  CB  GLU A 255       1.916  12.842 -23.389  1.00 45.34           C  
ANISOU  450  CB  GLU A 255     5489   5953   5785    915   -204   -683       C  
ATOM    451  CG  GLU A 255       2.538  13.768 -24.409  1.00 56.05           C  
ANISOU  451  CG  GLU A 255     6783   7403   7111    911   -243   -679       C  
ATOM    452  CD  GLU A 255       3.211  13.038 -25.551  1.00 60.11           C  
ANISOU  452  CD  GLU A 255     7278   7949   7611    943   -239   -712       C  
ATOM    453  OE1 GLU A 255       4.113  13.643 -26.165  1.00 59.86           O  
ANISOU  453  OE1 GLU A 255     7202   7995   7548    958   -271   -699       O  
ATOM    454  OE2 GLU A 255       2.842  11.872 -25.835  1.00 63.18           O  
ANISOU  454  OE2 GLU A 255     7700   8283   8021    948   -200   -755       O  
ATOM    455  N   SER A 256      -0.475  14.875 -22.501  1.00 47.18           N  
ANISOU  455  N   SER A 256     5707   6172   6046    805   -221   -661       N  
ATOM    456  CA  SER A 256      -1.255  16.107 -22.652  1.00 46.46           C  
ANISOU  456  CA  SER A 256     5589   6114   5952    770   -233   -646       C  
ATOM    457  C   SER A 256      -0.991  17.087 -21.515  1.00 43.10           C  
ANISOU  457  C   SER A 256     5180   5675   5521    764   -240   -596       C  
ATOM    458  O   SER A 256      -0.786  18.273 -21.746  1.00 54.45           O  
ANISOU  458  O   SER A 256     6594   7153   6939    753   -250   -572       O  
ATOM    459  CB  SER A 256      -2.746  15.799 -22.739  1.00 48.83           C  
ANISOU  459  CB  SER A 256     5892   6391   6271    735   -213   -677       C  
ATOM    460  OG  SER A 256      -3.004  14.922 -23.819  1.00 51.29           O  
ANISOU  460  OG  SER A 256     6184   6725   6580    726   -201   -732       O  
ATOM    461  N   TRP A 257      -0.989  16.592 -20.284  1.00 47.91           N  
ANISOU  461  N   TRP A 257     5832   6228   6144    768   -228   -583       N  
ATOM    462  CA  TRP A 257      -0.602  17.424 -19.136  1.00 43.69           C  
ANISOU  462  CA  TRP A 257     5311   5692   5599    757   -232   -542       C  
ATOM    463  C   TRP A 257       0.839  17.985 -19.215  1.00 41.53           C  
ANISOU  463  C   TRP A 257     5012   5484   5284    771   -250   -521       C  
ATOM    464  O   TRP A 257       1.063  19.149 -18.873  1.00 44.40           O  
ANISOU  464  O   TRP A 257     5369   5872   5630    740   -251   -500       O  
ATOM    465  CB  TRP A 257      -0.857  16.682 -17.823  1.00 36.15           C  
ANISOU  465  CB  TRP A 257     4400   4674   4663    764   -216   -532       C  
ATOM    466  CG  TRP A 257      -2.313  16.697 -17.420  1.00 34.73           C  
ANISOU  466  CG  TRP A 257     4243   4439   4515    730   -200   -542       C  
ATOM    467  CD1 TRP A 257      -3.188  15.635 -17.414  1.00 28.48           C  
ANISOU  467  CD1 TRP A 257     3477   3593   3751    725   -178   -573       C  
ATOM    468  CD2 TRP A 257      -3.080  17.829 -16.970  1.00 37.31           C  
ANISOU  468  CD2 TRP A 257     4569   4761   4845    694   -198   -523       C  
ATOM    469  NE1 TRP A 257      -4.420  16.043 -16.988  1.00 33.91           N  
ANISOU  469  NE1 TRP A 257     4173   4256   4454    689   -170   -574       N  
ATOM    470  CE2 TRP A 257      -4.372  17.376 -16.709  1.00 39.01           C  
ANISOU  470  CE2 TRP A 257     4804   4930   5088    675   -183   -540       C  
ATOM    471  CE3 TRP A 257      -2.753  19.175 -16.765  1.00 39.07           C  
ANISOU  471  CE3 TRP A 257     4782   5013   5049    675   -202   -494       C  
ATOM    472  CZ2 TRP A 257      -5.380  18.241 -16.242  1.00 42.49           C  
ANISOU  472  CZ2 TRP A 257     5250   5359   5536    646   -175   -524       C  
ATOM    473  CZ3 TRP A 257      -3.754  20.022 -16.294  1.00 44.30           C  
ANISOU  473  CZ3 TRP A 257     5459   5651   5724    647   -186   -479       C  
ATOM    474  CH2 TRP A 257      -5.050  19.556 -16.047  1.00 39.91           C  
ANISOU  474  CH2 TRP A 257     4916   5054   5192    638   -176   -492       C  
ATOM    475  N   LYS A 258       1.801  17.177 -19.679  1.00 41.30           N  
ANISOU  475  N   LYS A 258     4970   5486   5237    813   -258   -529       N  
ATOM    476  CA  LYS A 258       3.143  17.683 -20.000  1.00 41.17           C  
ANISOU  476  CA  LYS A 258     4918   5550   5174    824   -277   -516       C  
ATOM    477  C   LYS A 258       3.104  18.798 -21.045  1.00 41.84           C  
ANISOU  477  C   LYS A 258     4971   5679   5247    793   -287   -522       C  
ATOM    478  O   LYS A 258       3.842  19.780 -20.946  1.00 42.07           O  
ANISOU  478  O   LYS A 258     4984   5758   5242    769   -291   -506       O  
ATOM    479  CB  LYS A 258       4.065  16.553 -20.465  1.00 46.95           C  
ANISOU  479  CB  LYS A 258     5640   6309   5889    884   -281   -524       C  
ATOM    480  CG  LYS A 258       4.782  15.842 -19.322  1.00 53.54           C  
ANISOU  480  CG  LYS A 258     6492   7147   6702    928   -271   -495       C  
ATOM    481  CD  LYS A 258       5.299  14.473 -19.726  1.00 47.91           C  
ANISOU  481  CD  LYS A 258     5792   6424   5989   1001   -255   -500       C  
ATOM    482  CE  LYS A 258       5.662  13.685 -18.481  1.00 54.08           C  
ANISOU  482  CE  LYS A 258     6603   7187   6757   1054   -231   -462       C  
ATOM    483  NZ  LYS A 258       6.424  12.438 -18.758  1.00 59.87           N  
ANISOU  483  NZ  LYS A 258     7351   7922   7476   1142   -206   -453       N  
ATOM    484  N   ILE A 259       2.237  18.648 -22.045  1.00 36.53           N  
ANISOU  484  N   ILE A 259     4289   4993   4600    792   -285   -546       N  
ATOM    485  CA  ILE A 259       2.034  19.711 -23.019  1.00 38.98           C  
ANISOU  485  CA  ILE A 259     4569   5344   4899    773   -287   -542       C  
ATOM    486  C   ILE A 259       1.503  20.984 -22.355  1.00 38.94           C  
ANISOU  486  C   ILE A 259     4584   5315   4896    734   -267   -513       C  
ATOM    487  O   ILE A 259       2.017  22.069 -22.592  1.00 40.04           O  
ANISOU  487  O   ILE A 259     4716   5488   5011    715   -260   -495       O  
ATOM    488  CB  ILE A 259       1.113  19.263 -24.189  1.00 39.94           C  
ANISOU  488  CB  ILE A 259     4666   5472   5037    781   -287   -572       C  
ATOM    489  CG1 ILE A 259       1.853  18.264 -25.081  1.00 39.00           C  
ANISOU  489  CG1 ILE A 259     4522   5387   4908    812   -301   -604       C  
ATOM    490  CG2 ILE A 259       0.676  20.458 -25.009  1.00 35.15           C  
ANISOU  490  CG2 ILE A 259     4030   4907   4419    769   -281   -555       C  
ATOM    491  CD1 ILE A 259       0.951  17.430 -25.952  1.00 44.10           C  
ANISOU  491  CD1 ILE A 259     5154   6031   5572    811   -292   -648       C  
ATOM    492  N   LEU A 260       0.475  20.856 -21.524  1.00 40.61           N  
ANISOU  492  N   LEU A 260     4827   5466   5137    722   -252   -508       N  
ATOM    493  CA  LEU A 260      -0.018  22.007 -20.763  1.00 44.46           C  
ANISOU  493  CA  LEU A 260     5342   5924   5627    689   -227   -480       C  
ATOM    494  C   LEU A 260       1.059  22.576 -19.831  1.00 46.80           C  
ANISOU  494  C   LEU A 260     5653   6232   5895    660   -221   -466       C  
ATOM    495  O   LEU A 260       1.289  23.784 -19.793  1.00 46.46           O  
ANISOU  495  O   LEU A 260     5620   6199   5835    627   -197   -451       O  
ATOM    496  CB  LEU A 260      -1.261  21.639 -19.961  1.00 37.22           C  
ANISOU  496  CB  LEU A 260     4454   4945   4744    682   -214   -480       C  
ATOM    497  CG  LEU A 260      -2.502  21.218 -20.744  1.00 37.90           C  
ANISOU  497  CG  LEU A 260     4521   5031   4847    695   -212   -497       C  
ATOM    498  CD1 LEU A 260      -3.747  21.418 -19.866  1.00 47.88           C  
ANISOU  498  CD1 LEU A 260     5814   6245   6134    677   -192   -486       C  
ATOM    499  CD2 LEU A 260      -2.614  22.018 -22.006  1.00 35.08           C  
ANISOU  499  CD2 LEU A 260     4127   4730   4470    707   -207   -487       C  
ATOM    500  N   GLU A 261       1.723  21.702 -19.087  1.00 39.93           N  
ANISOU  500  N   GLU A 261     4785   5369   5017    673   -237   -472       N  
ATOM    501  CA  GLU A 261       2.783  22.140 -18.184  1.00 54.43           C  
ANISOU  501  CA  GLU A 261     6621   7245   6814    645   -234   -462       C  
ATOM    502  C   GLU A 261       3.866  22.980 -18.878  1.00 55.14           C  
ANISOU  502  C   GLU A 261     6684   7408   6858    622   -234   -464       C  
ATOM    503  O   GLU A 261       4.265  24.031 -18.373  1.00 52.88           O  
ANISOU  503  O   GLU A 261     6409   7139   6545    567   -209   -460       O  
ATOM    504  CB  GLU A 261       3.401  20.937 -17.470  1.00 58.69           C  
ANISOU  504  CB  GLU A 261     7155   7802   7341    683   -251   -460       C  
ATOM    505  CG  GLU A 261       4.292  21.299 -16.304  1.00 73.41           C  
ANISOU  505  CG  GLU A 261     9013   9720   9160    655   -246   -447       C  
ATOM    506  CD  GLU A 261       5.741  21.376 -16.695  1.00 88.17           C  
ANISOU  506  CD  GLU A 261    10838  11695  10967    661   -261   -450       C  
ATOM    507  OE1 GLU A 261       6.273  20.348 -17.169  1.00 98.08           O  
ANISOU  507  OE1 GLU A 261    12073  12980  12214    724   -281   -449       O  
ATOM    508  OE2 GLU A 261       6.348  22.458 -16.526  1.00 88.90           O  
ANISOU  508  OE2 GLU A 261    10918  11841  11017    600   -248   -455       O  
ATOM    509  N   SER A 262       4.325  22.518 -20.041  1.00 58.49           N  
ANISOU  509  N   SER A 262     7076   7874   7274    659   -257   -475       N  
ATOM    510  CA  SER A 262       5.402  23.184 -20.766  1.00 53.32           C  
ANISOU  510  CA  SER A 262     6391   7294   6575    641   -260   -479       C  
ATOM    511  C   SER A 262       4.954  24.498 -21.387  1.00 50.62           C  
ANISOU  511  C   SER A 262     6064   6932   6238    605   -228   -471       C  
ATOM    512  O   SER A 262       5.677  25.105 -22.170  1.00 62.94           O  
ANISOU  512  O   SER A 262     7604   8543   7766    590   -224   -474       O  
ATOM    513  CB  SER A 262       5.962  22.268 -21.858  1.00 58.74           C  
ANISOU  513  CB  SER A 262     7038   8027   7252    696   -293   -493       C  
ATOM    514  OG  SER A 262       5.185  22.336 -23.039  1.00 67.40           O  
ANISOU  514  OG  SER A 262     8127   9103   8378    712   -293   -500       O  
ATOM    515  N   MET A 263       3.769  24.949 -21.009  1.00 61.59           N  
ANISOU  515  N   MET A 263     7489   8249   7663    593   -199   -457       N  
ATOM    516  CA  MET A 263       3.104  26.038 -21.702  1.00 61.20           C  
ANISOU  516  CA  MET A 263     7457   8173   7625    585   -161   -438       C  
ATOM    517  C   MET A 263       2.757  27.184 -20.756  1.00 66.07           C  
ANISOU  517  C   MET A 263     8126   8736   8242    532   -106   -422       C  
ATOM    518  O   MET A 263       2.389  28.271 -21.191  1.00 69.82           O  
ANISOU  518  O   MET A 263     8627   9185   8718    522    -58   -401       O  
ATOM    519  CB  MET A 263       1.834  25.479 -22.331  1.00 64.08           C  
ANISOU  519  CB  MET A 263     7810   8510   8027    634   -172   -434       C  
ATOM    520  CG  MET A 263       1.141  26.359 -23.334  1.00 66.65           C  
ANISOU  520  CG  MET A 263     8132   8837   8355    652   -141   -408       C  
ATOM    521  SD  MET A 263      -0.181  25.397 -24.084  1.00 67.33           S  
ANISOU  521  SD  MET A 263     8181   8933   8468    704   -165   -416       S  
ATOM    522  CE  MET A 263       0.740  24.016 -24.770  1.00106.48           C  
ANISOU  522  CE  MET A 263    13094  13948  13418    724   -220   -460       C  
ATOM    523  N   LYS A 264       2.877  26.934 -19.458  1.00 70.91           N  
ANISOU  523  N   LYS A 264     8756   9332   8853    502   -107   -431       N  
ATOM    524  CA  LYS A 264       2.517  27.927 -18.458  1.00 81.13           C  
ANISOU  524  CA  LYS A 264    10101  10574  10149    447    -53   -422       C  
ATOM    525  C   LYS A 264       3.474  29.110 -18.450  1.00 85.67           C  
ANISOU  525  C   LYS A 264    10695  11175  10680    377     -5   -432       C  
ATOM    526  O   LYS A 264       4.659  28.971 -18.759  1.00 84.99           O  
ANISOU  526  O   LYS A 264    10574  11167  10551    359    -26   -451       O  
ATOM    527  CB  LYS A 264       2.489  27.298 -17.062  1.00 90.99           C  
ANISOU  527  CB  LYS A 264    11356  11814  11401    430    -70   -432       C  
ATOM    528  CG  LYS A 264       1.379  26.278 -16.833  1.00 96.22           C  
ANISOU  528  CG  LYS A 264    12019  12429  12111    482    -99   -424       C  
ATOM    529  CD  LYS A 264       1.568  25.541 -15.509  1.00100.15           C  
ANISOU  529  CD  LYS A 264    12518  12929  12605    472   -117   -431       C  
ATOM    530  CE  LYS A 264       2.829  24.666 -15.520  1.00 99.85           C  
ANISOU  530  CE  LYS A 264    12436  12973  12528    492   -155   -442       C  
ATOM    531  NZ  LYS A 264       4.111  25.433 -15.465  1.00 90.70           N  
ANISOU  531  NZ  LYS A 264    11259  11895  11309    440   -142   -454       N  
ATOM    532  N   SER A 265       2.939  30.272 -18.084  1.00 95.37           N  
ANISOU  532  N   SER A 265    11982  12337  11918    337     66   -419       N  
ATOM    533  CA  SER A 265       3.729  31.483 -17.866  1.00 97.67           C  
ANISOU  533  CA  SER A 265    12309  12633  12168    252    133   -434       C  
ATOM    534  C   SER A 265       4.600  31.861 -19.062  1.00 94.87           C  
ANISOU  534  C   SER A 265    11935  12331  11781    249    138   -438       C  
ATOM    535  O   SER A 265       5.531  32.656 -18.941  1.00 95.34           O  
ANISOU  535  O   SER A 265    12010  12419  11795    170    184   -463       O  
ATOM    536  CB  SER A 265       4.569  31.367 -16.583  1.00101.62           C  
ANISOU  536  CB  SER A 265    12800  13184  12628    175    129   -471       C  
ATOM    537  OG  SER A 265       5.557  30.350 -16.680  1.00103.18           O  
ANISOU  537  OG  SER A 265    12929  13486  12790    194     58   -489       O  
ATOM    538  N   LYS A 266       4.277  31.297 -20.218  1.00 89.17           N  
ANISOU  538  N   LYS A 266    11176  11625  11081    329     96   -418       N  
ATOM    539  CA  LYS A 266       5.026  31.569 -21.430  1.00 85.99           C  
ANISOU  539  CA  LYS A 266    10748  11275  10650    336     94   -418       C  
ATOM    540  C   LYS A 266       4.221  32.517 -22.306  1.00 87.03           C  
ANISOU  540  C   LYS A 266    10920  11347  10803    370    157   -375       C  
ATOM    541  O   LYS A 266       2.995  32.562 -22.211  1.00 86.37           O  
ANISOU  541  O   LYS A 266    10858  11202  10758    418    174   -343       O  
ATOM    542  CB  LYS A 266       5.316  30.260 -22.171  1.00 81.72           C  
ANISOU  542  CB  LYS A 266    10133  10805  10110    402      6   -426       C  
ATOM    543  CG  LYS A 266       6.371  30.368 -23.257  1.00 75.76           C  
ANISOU  543  CG  LYS A 266     9341  10128   9317    400     -9   -437       C  
ATOM    544  CD  LYS A 266       6.681  29.006 -23.854  1.00 77.33           C  
ANISOU  544  CD  LYS A 266     9472  10392   9516    463    -91   -450       C  
ATOM    545  CE  LYS A 266       7.275  28.066 -22.824  1.00 77.61           C  
ANISOU  545  CE  LYS A 266     9485  10468   9534    455   -133   -473       C  
ATOM    546  NZ  LYS A 266       7.757  26.801 -23.445  1.00 78.24           N  
ANISOU  546  NZ  LYS A 266     9509  10611   9609    517   -198   -485       N  
ATOM    547  N   ASP A 267       4.909  33.288 -23.141  1.00 90.83           N  
ANISOU  547  N   ASP A 267    11409  11850  11254    349    196   -372       N  
ATOM    548  CA  ASP A 267       4.230  34.163 -24.089  1.00 92.68           C  
ANISOU  548  CA  ASP A 267    11676  12037  11502    396    259   -322       C  
ATOM    549  C   ASP A 267       3.264  33.324 -24.924  1.00 92.06           C  
ANISOU  549  C   ASP A 267    11542  11984  11454    500    201   -293       C  
ATOM    550  O   ASP A 267       3.652  32.288 -25.472  1.00 99.65           O  
ANISOU  550  O   ASP A 267    12434  13020  12410    528    121   -315       O  
ATOM    551  CB  ASP A 267       5.248  34.870 -24.991  1.00 91.11           C  
ANISOU  551  CB  ASP A 267    11479  11875  11262    363    294   -326       C  
ATOM    552  N   ILE A 268       2.009  33.757 -25.009  1.00 84.50           N  
ANISOU  552  N   ILE A 268    10613  10970  10522    555    246   -245       N  
ATOM    553  CA  ILE A 268       1.000  32.999 -25.745  1.00 82.10           C  
ANISOU  553  CA  ILE A 268    10251  10706  10237    643    198   -221       C  
ATOM    554  C   ILE A 268       1.262  33.010 -27.247  1.00 76.24           C  
ANISOU  554  C   ILE A 268     9457  10036   9474    693    184   -203       C  
ATOM    555  O   ILE A 268       1.128  34.038 -27.912  1.00 75.56           O  
ANISOU  555  O   ILE A 268     9400   9937   9374    721    254   -155       O  
ATOM    556  CB  ILE A 268      -0.423  33.519 -25.488  1.00 90.76           C  
ANISOU  556  CB  ILE A 268    11384  11746  11356    694    253   -170       C  
ATOM    557  CG1 ILE A 268      -0.800  33.317 -24.021  1.00 90.08           C  
ANISOU  557  CG1 ILE A 268    11338  11596  11293    651    254   -191       C  
ATOM    558  CG2 ILE A 268      -1.418  32.804 -26.402  1.00 92.83           C  
ANISOU  558  CG2 ILE A 268    11573  12077  11621    780    208   -148       C  
ATOM    559  CD1 ILE A 268      -2.178  33.831 -23.668  1.00 86.21           C  
ANISOU  559  CD1 ILE A 268    10884  11051  10822    699    309   -141       C  
ATOM    560  N   ASN A 269       1.638  31.853 -27.773  1.00 68.70           N  
ANISOU  560  N   ASN A 269     8429   9158   8516    708     98   -240       N  
ATOM    561  CA  ASN A 269       1.977  31.733 -29.177  1.00 61.88           C  
ANISOU  561  CA  ASN A 269     7506   8374   7630    748     74   -232       C  
ATOM    562  C   ASN A 269       1.928  30.275 -29.591  1.00 57.19           C  
ANISOU  562  C   ASN A 269     6837   7850   7044    773    -15   -274       C  
ATOM    563  O   ASN A 269       2.911  29.544 -29.463  1.00 64.41           O  
ANISOU  563  O   ASN A 269     7730   8793   7951    743    -66   -320       O  
ATOM    564  CB  ASN A 269       3.357  32.322 -29.436  1.00 67.62           C  
ANISOU  564  CB  ASN A 269     8251   9117   8326    696     93   -247       C  
ATOM    565  CG  ASN A 269       3.667  32.423 -30.899  1.00 67.32           C  
ANISOU  565  CG  ASN A 269     8162   9154   8265    739     83   -230       C  
ATOM    566  OD1 ASN A 269       3.039  31.756 -31.722  1.00 73.09           O  
ANISOU  566  OD1 ASN A 269     8827   9944   8999    801     41   -223       O  
ATOM    567  ND2 ASN A 269       4.641  33.255 -31.242  1.00 68.71           N  
ANISOU  567  ND2 ASN A 269     8363   9332   8411    700    124   -226       N  
ATOM    568  N   ILE A 270       0.767  29.860 -30.081  1.00 49.93           N  
ANISOU  568  N   ILE A 270     5877   6960   6133    829    -27   -259       N  
ATOM    569  CA  ILE A 270       0.477  28.451 -30.287  1.00 50.59           C  
ANISOU  569  CA  ILE A 270     5903   7091   6229    842    -95   -305       C  
ATOM    570  C   ILE A 270       1.543  27.738 -31.130  1.00 52.15           C  
ANISOU  570  C   ILE A 270     6049   7357   6409    838   -148   -345       C  
ATOM    571  O   ILE A 270       1.977  26.641 -30.791  1.00 53.30           O  
ANISOU  571  O   ILE A 270     6182   7504   6565    821   -196   -393       O  
ATOM    572  CB  ILE A 270      -0.928  28.269 -30.885  1.00 46.27           C  
ANISOU  572  CB  ILE A 270     5311   6591   5680    895    -90   -285       C  
ATOM    573  CG1 ILE A 270      -1.977  28.742 -29.872  1.00 41.38           C  
ANISOU  573  CG1 ILE A 270     4741   5903   5078    898    -47   -253       C  
ATOM    574  CG2 ILE A 270      -1.166  26.807 -31.306  1.00 37.87           C  
ANISOU  574  CG2 ILE A 270     4184   5584   4620    896   -151   -344       C  
ATOM    575  CD1 ILE A 270      -3.363  28.915 -30.456  1.00 46.19           C  
ANISOU  575  CD1 ILE A 270     5308   6572   5671    958    -24   -215       C  
ATOM    576  N   VAL A 271       1.979  28.375 -32.206  1.00 47.13           N  
ANISOU  576  N   VAL A 271     5386   6774   5745    858   -134   -322       N  
ATOM    577  CA  VAL A 271       2.966  27.774 -33.082  1.00 45.58           C  
ANISOU  577  CA  VAL A 271     5139   6649   5529    858   -181   -357       C  
ATOM    578  C   VAL A 271       4.356  27.683 -32.432  1.00 48.85           C  
ANISOU  578  C   VAL A 271     5582   7044   5934    808   -199   -386       C  
ATOM    579  O   VAL A 271       4.991  26.639 -32.483  1.00 51.59           O  
ANISOU  579  O   VAL A 271     5899   7423   6280    806   -251   -429       O  
ATOM    580  CB  VAL A 271       3.017  28.512 -34.414  1.00 49.91           C  
ANISOU  580  CB  VAL A 271     5649   7267   6048    895   -159   -320       C  
ATOM    581  CG1 VAL A 271       4.053  27.883 -35.353  1.00 41.26           C  
ANISOU  581  CG1 VAL A 271     4497   6250   4931    894   -211   -359       C  
ATOM    582  CG2 VAL A 271       1.626  28.504 -35.037  1.00 46.23           C  
ANISOU  582  CG2 VAL A 271     5139   6847   5578    950   -144   -291       C  
ATOM    583  N   GLU A 272       4.815  28.756 -31.797  1.00 48.99           N  
ANISOU  583  N   GLU A 272     5657   7014   5942    767   -151   -362       N  
ATOM    584  CA  GLU A 272       6.130  28.741 -31.152  1.00 46.86           C  
ANISOU  584  CA  GLU A 272     5406   6749   5651    712   -164   -392       C  
ATOM    585  C   GLU A 272       6.213  27.736 -30.005  1.00 55.11           C  
ANISOU  585  C   GLU A 272     6458   7768   6711    697   -201   -425       C  
ATOM    586  O   GLU A 272       7.258  27.119 -29.773  1.00 61.22           O  
ANISOU  586  O   GLU A 272     7213   8585   7464    682   -238   -456       O  
ATOM    587  CB  GLU A 272       6.495  30.131 -30.648  1.00 46.69           C  
ANISOU  587  CB  GLU A 272     5448   6681   5611    657    -92   -368       C  
ATOM    588  CG  GLU A 272       6.793  31.096 -31.777  1.00 59.48           C  
ANISOU  588  CG  GLU A 272     7064   8329   7205    665    -51   -337       C  
ATOM    589  N   VAL A 273       5.099  27.578 -29.305  1.00 52.38           N  
ANISOU  589  N   VAL A 273     6141   7360   6401    707   -187   -415       N  
ATOM    590  CA  VAL A 273       4.993  26.691 -28.160  1.00 45.56           C  
ANISOU  590  CA  VAL A 273     5293   6461   5557    697   -212   -438       C  
ATOM    591  C   VAL A 273       4.896  25.220 -28.568  1.00 50.40           C  
ANISOU  591  C   VAL A 273     5862   7103   6183    738   -266   -471       C  
ATOM    592  O   VAL A 273       5.381  24.342 -27.860  1.00 55.67           O  
ANISOU  592  O   VAL A 273     6534   7767   6853    737   -291   -494       O  
ATOM    593  CB  VAL A 273       3.759  27.089 -27.314  1.00 51.08           C  
ANISOU  593  CB  VAL A 273     6038   7081   6289    692   -174   -415       C  
ATOM    594  CG1 VAL A 273       3.249  25.911 -26.497  1.00 51.44           C  
ANISOU  594  CG1 VAL A 273     6086   7095   6363    702   -206   -438       C  
ATOM    595  CG2 VAL A 273       4.087  28.298 -26.439  1.00 46.41           C  
ANISOU  595  CG2 VAL A 273     5505   6444   5683    635   -118   -397       C  
ATOM    596  N   GLY A 274       4.277  24.957 -29.715  1.00 47.43           N  
ANISOU  596  N   GLY A 274     5445   6761   5814    775   -275   -474       N  
ATOM    597  CA  GLY A 274       4.177  23.603 -30.235  1.00 43.35           C  
ANISOU  597  CA  GLY A 274     4891   6273   5308    805   -314   -513       C  
ATOM    598  C   GLY A 274       5.527  23.094 -30.712  1.00 43.62           C  
ANISOU  598  C   GLY A 274     4896   6364   5314    813   -347   -537       C  
ATOM    599  O   GLY A 274       5.922  21.956 -30.435  1.00 41.67           O  
ANISOU  599  O   GLY A 274     4648   6113   5073    829   -371   -566       O  
ATOM    600  N   LYS A 275       6.232  23.950 -31.443  1.00 45.23           N  
ANISOU  600  N   LYS A 275     5078   6620   5486    806   -343   -521       N  
ATOM    601  CA  LYS A 275       7.605  23.682 -31.858  1.00 45.04           C  
ANISOU  601  CA  LYS A 275     5026   6662   5427    808   -372   -539       C  
ATOM    602  C   LYS A 275       8.530  23.421 -30.659  1.00 48.71           C  
ANISOU  602  C   LYS A 275     5516   7118   5873    789   -380   -544       C  
ATOM    603  O   LYS A 275       9.168  22.367 -30.582  1.00 46.48           O  
ANISOU  603  O   LYS A 275     5217   6861   5581    818   -409   -566       O  
ATOM    604  CB  LYS A 275       8.127  24.832 -32.715  1.00 41.23           C  
ANISOU  604  CB  LYS A 275     4525   6229   4910    793   -357   -517       C  
ATOM    605  CG  LYS A 275       7.750  24.681 -34.170  1.00 47.96           C  
ANISOU  605  CG  LYS A 275     5324   7137   5762    829   -370   -521       C  
ATOM    606  CD  LYS A 275       7.512  26.011 -34.832  1.00 50.45           C  
ANISOU  606  CD  LYS A 275     5639   7468   6062    824   -331   -478       C  
ATOM    607  CE  LYS A 275       8.681  26.936 -34.663  1.00 54.80           C  
ANISOU  607  CE  LYS A 275     6211   8032   6576    782   -312   -466       C  
ATOM    608  NZ  LYS A 275       8.382  28.263 -35.254  1.00 54.61           N  
ANISOU  608  NZ  LYS A 275     6204   8004   6541    779   -257   -420       N  
ATOM    609  N   GLN A 276       8.585  24.371 -29.726  1.00 50.29           N  
ANISOU  609  N   GLN A 276     5756   7288   6065    742   -348   -523       N  
ATOM    610  CA  GLN A 276       9.351  24.200 -28.493  1.00 44.51           C  
ANISOU  610  CA  GLN A 276     5042   6562   5308    717   -351   -527       C  
ATOM    611  C   GLN A 276       9.058  22.855 -27.839  1.00 45.19           C  
ANISOU  611  C   GLN A 276     5134   6616   5420    760   -372   -539       C  
ATOM    612  O   GLN A 276       9.975  22.133 -27.463  1.00 46.48           O  
ANISOU  612  O   GLN A 276     5282   6824   5554    782   -393   -546       O  
ATOM    613  CB  GLN A 276       9.064  25.339 -27.515  1.00 41.81           C  
ANISOU  613  CB  GLN A 276     4748   6172   4965    656   -305   -509       C  
ATOM    614  CG  GLN A 276       9.566  26.683 -27.982  1.00 49.41           C  
ANISOU  614  CG  GLN A 276     5718   7160   5894    604   -268   -499       C  
ATOM    615  CD  GLN A 276       9.174  27.820 -27.064  1.00 64.03           C  
ANISOU  615  CD  GLN A 276     7629   8948   7749    542   -207   -485       C  
ATOM    616  OE1 GLN A 276       8.007  27.976 -26.702  1.00 74.75           O  
ANISOU  616  OE1 GLN A 276     9024  10226   9151    553   -182   -466       O  
ATOM    617  NE2 GLN A 276      10.154  28.626 -26.680  1.00 72.73           N  
ANISOU  617  NE2 GLN A 276     8742  10090   8800    470   -177   -497       N  
ATOM    618  N   TYR A 277       7.781  22.512 -27.711  1.00 51.78           N  
ANISOU  618  N   TYR A 277     5992   7376   6305    773   -361   -538       N  
ATOM    619  CA  TYR A 277       7.428  21.244 -27.091  1.00 42.14           C  
ANISOU  619  CA  TYR A 277     4787   6112   5111    808   -370   -551       C  
ATOM    620  C   TYR A 277       7.957  20.040 -27.860  1.00 38.82           C  
ANISOU  620  C   TYR A 277     4338   5726   4685    860   -395   -576       C  
ATOM    621  O   TYR A 277       8.516  19.124 -27.276  1.00 44.37           O  
ANISOU  621  O   TYR A 277     5050   6430   5379    894   -400   -578       O  
ATOM    622  CB  TYR A 277       5.914  21.076 -26.876  1.00 39.53           C  
ANISOU  622  CB  TYR A 277     4486   5702   4833    805   -352   -552       C  
ATOM    623  CG  TYR A 277       5.627  19.700 -26.322  1.00 38.79           C  
ANISOU  623  CG  TYR A 277     4413   5562   4765    837   -354   -570       C  
ATOM    624  CD1 TYR A 277       5.841  19.410 -24.974  1.00 35.52           C  
ANISOU  624  CD1 TYR A 277     4032   5114   4350    837   -347   -555       C  
ATOM    625  CD2 TYR A 277       5.214  18.677 -27.149  1.00 34.39           C  
ANISOU  625  CD2 TYR A 277     3843   4997   4227    865   -358   -603       C  
ATOM    626  CE1 TYR A 277       5.627  18.137 -24.476  1.00 31.72           C  
ANISOU  626  CE1 TYR A 277     3576   4585   3891    872   -340   -566       C  
ATOM    627  CE2 TYR A 277       4.993  17.415 -26.662  1.00 33.93           C  
ANISOU  627  CE2 TYR A 277     3815   4885   4192    891   -346   -622       C  
ATOM    628  CZ  TYR A 277       5.207  17.144 -25.336  1.00 39.44           C  
ANISOU  628  CZ  TYR A 277     4551   5543   4892    899   -336   -600       C  
ATOM    629  OH  TYR A 277       4.977  15.866 -24.880  1.00 46.34           O  
ANISOU  629  OH  TYR A 277     5462   6357   5790    930   -316   -613       O  
ATOM    630  N   LEU A 278       7.756  20.028 -29.169  1.00 43.96           N  
ANISOU  630  N   LEU A 278     4956   6408   5340    871   -404   -594       N  
ATOM    631  CA  LEU A 278       8.073  18.845 -29.963  1.00 43.61           C  
ANISOU  631  CA  LEU A 278     4889   6384   5296    915   -418   -626       C  
ATOM    632  C   LEU A 278       9.579  18.661 -30.078  1.00 40.46           C  
ANISOU  632  C   LEU A 278     4464   6060   4847    942   -439   -622       C  
ATOM    633  O   LEU A 278      10.089  17.537 -30.130  1.00 33.53           O  
ANISOU  633  O   LEU A 278     3587   5187   3965    992   -442   -636       O  
ATOM    634  CB  LEU A 278       7.430  18.946 -31.350  1.00 38.90           C  
ANISOU  634  CB  LEU A 278     4254   5815   4709    912   -422   -648       C  
ATOM    635  CG  LEU A 278       5.925  18.708 -31.368  1.00 33.94           C  
ANISOU  635  CG  LEU A 278     3639   5135   4122    897   -401   -664       C  
ATOM    636  CD1 LEU A 278       5.364  19.053 -32.739  1.00 36.89           C  
ANISOU  636  CD1 LEU A 278     3960   5568   4488    893   -405   -677       C  
ATOM    637  CD2 LEU A 278       5.603  17.265 -31.015  1.00 25.46           C  
ANISOU  637  CD2 LEU A 278     2596   4003   3076    915   -388   -700       C  
ATOM    638  N   GLU A 279      10.279  19.785 -30.124  1.00 41.85           N  
ANISOU  638  N   GLU A 279     4620   6297   4985    909   -447   -602       N  
ATOM    639  CA  GLU A 279      11.731  19.801 -30.139  1.00 41.64           C  
ANISOU  639  CA  GLU A 279     4563   6360   4899    922   -466   -597       C  
ATOM    640  C   GLU A 279      12.284  19.285 -28.818  1.00 43.57           C  
ANISOU  640  C   GLU A 279     4826   6608   5120    942   -462   -581       C  
ATOM    641  O   GLU A 279      13.125  18.386 -28.804  1.00 41.56           O  
ANISOU  641  O   GLU A 279     4555   6400   4836    999   -473   -580       O  
ATOM    642  CB  GLU A 279      12.219  21.217 -30.427  1.00 44.18           C  
ANISOU  642  CB  GLU A 279     4866   6738   5183    864   -464   -585       C  
ATOM    643  CG  GLU A 279      11.998  21.610 -31.881  1.00 44.64           C  
ANISOU  643  CG  GLU A 279     4892   6821   5247    864   -471   -595       C  
ATOM    644  CD  GLU A 279      12.048  23.101 -32.108  1.00 46.00           C  
ANISOU  644  CD  GLU A 279     5067   7009   5400    806   -449   -576       C  
ATOM    645  OE1 GLU A 279      12.510  23.837 -31.221  1.00 45.57           O  
ANISOU  645  OE1 GLU A 279     5036   6962   5318    757   -429   -564       O  
ATOM    646  OE2 GLU A 279      11.620  23.541 -33.188  1.00 52.92           O  
ANISOU  646  OE2 GLU A 279     5925   7894   6287    809   -445   -573       O  
ATOM    647  N   GLN A 280      11.810  19.855 -27.715  1.00 44.70           N  
ANISOU  647  N   GLN A 280     5002   6708   5274    900   -443   -564       N  
ATOM    648  CA  GLN A 280      12.186  19.384 -26.387  1.00 47.82           C  
ANISOU  648  CA  GLN A 280     5413   7108   5647    918   -435   -545       C  
ATOM    649  C   GLN A 280      11.957  17.882 -26.250  1.00 48.57           C  
ANISOU  649  C   GLN A 280     5530   7154   5772    997   -430   -546       C  
ATOM    650  O   GLN A 280      12.800  17.162 -25.714  1.00 49.54           O  
ANISOU  650  O   GLN A 280     5643   7324   5855   1052   -430   -528       O  
ATOM    651  CB  GLN A 280      11.403  20.136 -25.310  1.00 38.87           C  
ANISOU  651  CB  GLN A 280     4318   5914   4537    860   -412   -533       C  
ATOM    652  CG  GLN A 280      11.085  19.304 -24.078  1.00 60.80           C  
ANISOU  652  CG  GLN A 280     7127   8644   7330    893   -400   -517       C  
ATOM    653  CD  GLN A 280       9.838  19.779 -23.359  1.00 77.65           C  
ANISOU  653  CD  GLN A 280     9307  10682   9515    848   -377   -513       C  
ATOM    654  OE1 GLN A 280       8.734  19.307 -23.631  1.00 66.28           O  
ANISOU  654  OE1 GLN A 280     7895   9155   8133    862   -369   -523       O  
ATOM    655  NE2 GLN A 280      10.008  20.718 -22.436  1.00 85.01           N  
ANISOU  655  NE2 GLN A 280    10245  11634  10420    788   -363   -502       N  
ATOM    656  N   GLN A 281      10.811  17.417 -26.736  1.00 46.55           N  
ANISOU  656  N   GLN A 281     5302   6806   5579   1002   -418   -567       N  
ATOM    657  CA  GLN A 281      10.417  16.023 -26.568  1.00 52.40           C  
ANISOU  657  CA  GLN A 281     6079   7477   6355   1060   -398   -576       C  
ATOM    658  C   GLN A 281      11.342  15.091 -27.343  1.00 52.53           C  
ANISOU  658  C   GLN A 281     6075   7541   6345   1129   -401   -586       C  
ATOM    659  O   GLN A 281      11.672  14.000 -26.877  1.00 54.19           O  
ANISOU  659  O   GLN A 281     6311   7727   6551   1196   -378   -573       O  
ATOM    660  CB  GLN A 281       8.969  15.818 -27.016  1.00 47.26           C  
ANISOU  660  CB  GLN A 281     5455   6734   5767   1032   -381   -606       C  
ATOM    661  CG  GLN A 281       8.562  14.360 -27.154  1.00 53.96           C  
ANISOU  661  CG  GLN A 281     6342   7511   6651   1078   -350   -632       C  
ATOM    662  N   PHE A 282      11.758  15.528 -28.527  1.00 52.43           N  
ANISOU  662  N   PHE A 282     6016   7592   6312   1116   -426   -605       N  
ATOM    663  CA  PHE A 282      12.693  14.762 -29.342  1.00 54.66           C  
ANISOU  663  CA  PHE A 282     6274   7930   6566   1177   -432   -616       C  
ATOM    664  C   PHE A 282      14.063  14.678 -28.676  1.00 52.72           C  
ANISOU  664  C   PHE A 282     6003   7780   6249   1226   -441   -577       C  
ATOM    665  O   PHE A 282      14.689  13.618 -28.655  1.00 61.40           O  
ANISOU  665  O   PHE A 282     7110   8891   7329   1309   -425   -567       O  
ATOM    666  CB  PHE A 282      12.823  15.381 -30.735  1.00 54.95           C  
ANISOU  666  CB  PHE A 282     6261   8025   6593   1146   -459   -643       C  
ATOM    667  CG  PHE A 282      13.886  14.746 -31.584  1.00 45.05           C  
ANISOU  667  CG  PHE A 282     4974   6842   5302   1204   -471   -653       C  
ATOM    668  CD1 PHE A 282      13.729  13.458 -32.066  1.00 50.91           C  
ANISOU  668  CD1 PHE A 282     5741   7533   6070   1258   -443   -680       C  
ATOM    669  CD2 PHE A 282      15.044  15.438 -31.901  1.00 33.24           C  
ANISOU  669  CD2 PHE A 282     3424   5465   3742   1200   -503   -638       C  
ATOM    670  CE1 PHE A 282      14.706  12.870 -32.848  1.00 44.22           C  
ANISOU  670  CE1 PHE A 282     4866   6748   5187   1316   -449   -689       C  
ATOM    671  CE2 PHE A 282      16.024  14.856 -32.682  1.00 41.27           C  
ANISOU  671  CE2 PHE A 282     4407   6554   4721   1257   -515   -647       C  
ATOM    672  CZ  PHE A 282      15.854  13.571 -33.156  1.00 41.87           C  
ANISOU  672  CZ  PHE A 282     4510   6575   4826   1319   -488   -670       C  
ATOM    673  N   LEU A 283      14.522  15.801 -28.134  1.00 49.79           N  
ANISOU  673  N   LEU A 283     5602   7481   5833   1174   -461   -557       N  
ATOM    674  CA  LEU A 283      15.750  15.827 -27.352  1.00 51.80           C  
ANISOU  674  CA  LEU A 283     5825   7848   6010   1205   -469   -523       C  
ATOM    675  C   LEU A 283      15.711  14.796 -26.221  1.00 50.24           C  
ANISOU  675  C   LEU A 283     5663   7612   5813   1278   -438   -490       C  
ATOM    676  O   LEU A 283      16.537  13.885 -26.166  1.00 54.03           O  
ANISOU  676  O   LEU A 283     6134   8143   6253   1370   -428   -466       O  
ATOM    677  CB  LEU A 283      15.943  17.222 -26.770  1.00 53.92           C  
ANISOU  677  CB  LEU A 283     6070   8177   6240   1113   -480   -518       C  
ATOM    678  CG  LEU A 283      17.362  17.642 -26.406  1.00 62.05           C  
ANISOU  678  CG  LEU A 283     7040   9368   7168   1108   -496   -502       C  
ATOM    679  CD1 LEU A 283      18.350  17.335 -27.541  1.00 57.63           C  
ANISOU  679  CD1 LEU A 283     6430   8902   6564   1154   -520   -511       C  
ATOM    680  CD2 LEU A 283      17.369  19.120 -26.073  1.00 63.41           C  
ANISOU  680  CD2 LEU A 283     7201   9576   7316    993   -495   -514       C  
ATOM    681  N   GLN A 284      14.741  14.939 -25.326  1.00 50.10           N  
ANISOU  681  N   GLN A 284     5690   7505   5841   1243   -419   -484       N  
ATOM    682  CA  GLN A 284      14.518  13.953 -24.266  1.00 56.66           C  
ANISOU  682  CA  GLN A 284     6564   8279   6684   1309   -385   -452       C  
ATOM    683  C   GLN A 284      14.489  12.525 -24.823  1.00 53.86           C  
ANISOU  683  C   GLN A 284     6248   7858   6358   1403   -351   -456       C  
ATOM    684  O   GLN A 284      15.031  11.600 -24.223  1.00 62.62           O  
ANISOU  684  O   GLN A 284     7373   8981   7440   1497   -321   -416       O  
ATOM    685  CB  GLN A 284      13.232  14.270 -23.479  1.00 67.38           C  
ANISOU  685  CB  GLN A 284     7972   9527   8104   1249   -369   -457       C  
ATOM    686  CG  GLN A 284      13.184  15.707 -22.932  1.00 80.38           C  
ANISOU  686  CG  GLN A 284     9593  11222   9727   1152   -390   -457       C  
ATOM    687  CD  GLN A 284      11.986  15.991 -22.012  1.00 80.69           C  
ANISOU  687  CD  GLN A 284     9680  11160   9820   1103   -371   -455       C  
ATOM    688  OE1 GLN A 284      10.852  15.570 -22.278  1.00 73.29           O  
ANISOU  688  OE1 GLN A 284     8788  10106   8953   1100   -355   -474       O  
ATOM    689  NE2 GLN A 284      12.240  16.729 -20.932  1.00 79.51           N  
ANISOU  689  NE2 GLN A 284     9516  11063   9631   1058   -372   -436       N  
ATOM    690  N   TYR A 285      13.877  12.346 -25.984  1.00 45.31           N  
ANISOU  690  N   TYR A 285     5180   6709   5328   1380   -350   -503       N  
ATOM    691  CA  TYR A 285      13.785  11.019 -26.576  1.00 51.82           C  
ANISOU  691  CA  TYR A 285     6047   7461   6182   1452   -309   -520       C  
ATOM    692  C   TYR A 285      15.156  10.484 -26.961  1.00 57.33           C  
ANISOU  692  C   TYR A 285     6711   8258   6814   1544   -309   -496       C  
ATOM    693  O   TYR A 285      15.429   9.297 -26.802  1.00 64.37           O  
ANISOU  693  O   TYR A 285     7645   9107   7705   1640   -258   -476       O  
ATOM    694  CB  TYR A 285      12.891  11.036 -27.813  1.00 50.52           C  
ANISOU  694  CB  TYR A 285     5889   7232   6073   1394   -311   -584       C  
ATOM    695  CG  TYR A 285      13.043   9.802 -28.661  1.00 52.95           C  
ANISOU  695  CG  TYR A 285     6227   7495   6397   1455   -270   -613       C  
ATOM    696  CD1 TYR A 285      12.647   8.559 -28.185  1.00 65.98           C  
ANISOU  696  CD1 TYR A 285     7954   9033   8081   1509   -201   -612       C  
ATOM    697  CD2 TYR A 285      13.571   9.877 -29.933  1.00 55.60           C  
ANISOU  697  CD2 TYR A 285     6517   7895   6712   1457   -293   -644       C  
ATOM    698  CE1 TYR A 285      12.775   7.422 -28.957  1.00 69.20           C  
ANISOU  698  CE1 TYR A 285     8400   9388   8504   1560   -149   -644       C  
ATOM    699  CE2 TYR A 285      13.707   8.744 -30.718  1.00 68.86           C  
ANISOU  699  CE2 TYR A 285     8227   9531   8406   1509   -249   -676       C  
ATOM    700  CZ  TYR A 285      13.306   7.521 -30.224  1.00 73.65           C  
ANISOU  700  CZ  TYR A 285     8916  10019   9047   1558   -174   -678       C  
ATOM    701  OH  TYR A 285      13.446   6.396 -31.002  1.00 79.09           O  
ANISOU  701  OH  TYR A 285     9645  10656   9751   1605   -118   -715       O  
ATOM    702  N   THR A 286      16.010  11.359 -27.488  1.00 56.60           N  
ANISOU  702  N   THR A 286     6546   8295   6665   1518   -359   -497       N  
ATOM    703  CA  THR A 286      17.354  10.948 -27.868  1.00 52.81           C  
ANISOU  703  CA  THR A 286     6023   7930   6113   1602   -365   -473       C  
ATOM    704  C   THR A 286      18.189  10.681 -26.616  1.00 53.66           C  
ANISOU  704  C   THR A 286     6117   8123   6150   1678   -350   -406       C  
ATOM    705  O   THR A 286      19.124   9.885 -26.644  1.00 59.46           O  
ANISOU  705  O   THR A 286     6840   8921   6831   1788   -329   -371       O  
ATOM    706  CB  THR A 286      18.048  11.975 -28.781  1.00 43.50           C  
ANISOU  706  CB  THR A 286     4767   6874   4887   1546   -421   -495       C  
ATOM    707  OG1 THR A 286      18.018  13.267 -28.169  1.00 48.33           O  
ANISOU  707  OG1 THR A 286     5346   7544   5474   1454   -453   -488       O  
ATOM    708  CG2 THR A 286      17.351  12.049 -30.118  1.00 44.84           C  
ANISOU  708  CG2 THR A 286     4943   6978   5116   1497   -430   -553       C  
ATOM    709  N   ASP A 287      17.846  11.343 -25.514  1.00 60.89           N  
ANISOU  709  N   ASP A 287     7030   9044   7059   1624   -359   -387       N  
ATOM    710  CA  ASP A 287      18.531  11.088 -24.250  1.00 68.24           C  
ANISOU  710  CA  ASP A 287     7944  10064   7922   1692   -343   -324       C  
ATOM    711  C   ASP A 287      18.284   9.657 -23.821  1.00 65.72           C  
ANISOU  711  C   ASP A 287     7696   9642   7632   1811   -276   -287       C  
ATOM    712  O   ASP A 287      19.224   8.887 -23.631  1.00 71.67           O  
ANISOU  712  O   ASP A 287     8436  10472   8324   1932   -249   -236       O  
ATOM    713  CB  ASP A 287      18.049  12.035 -23.150  1.00 82.40           C  
ANISOU  713  CB  ASP A 287     9729  11866   9713   1601   -358   -319       C  
ATOM    714  CG  ASP A 287      18.695  13.401 -23.231  1.00 94.89           C  
ANISOU  714  CG  ASP A 287    11235  13590  11230   1504   -407   -336       C  
ATOM    715  OD1 ASP A 287      19.557  13.593 -24.116  1.00100.82           O  
ANISOU  715  OD1 ASP A 287    11934  14440  11931   1511   -432   -349       O  
ATOM    716  OD2 ASP A 287      18.340  14.282 -22.415  1.00 97.17           O  
ANISOU  716  OD2 ASP A 287    11518  13887  11515   1417   -415   -340       O  
ATOM    717  N   ASN A 288      17.010   9.306 -23.683  1.00 62.96           N  
ANISOU  717  N   ASN A 288     7425   9121   7377   1776   -244   -313       N  
ATOM    718  CA  ASN A 288      16.616   7.964 -23.272  1.00 68.86           C  
ANISOU  718  CA  ASN A 288     8257   9744   8163   1872   -169   -287       C  
ATOM    719  C   ASN A 288      17.274   6.889 -24.118  1.00 70.60           C  
ANISOU  719  C   ASN A 288     8499   9956   8370   1981   -125   -282       C  
ATOM    720  O   ASN A 288      17.635   5.824 -23.614  1.00 82.75           O  
ANISOU  720  O   ASN A 288    10082  11467   9890   2105    -59   -227       O  
ATOM    721  CB  ASN A 288      15.096   7.817 -23.315  1.00 64.42           C  
ANISOU  721  CB  ASN A 288     7770   9003   7705   1793   -144   -336       C  
ATOM    722  CG  ASN A 288      14.395   8.862 -22.479  1.00 64.52           C  
ANISOU  722  CG  ASN A 288     7766   9016   7732   1692   -181   -340       C  
ATOM    723  OD1 ASN A 288      14.930   9.323 -21.467  1.00 62.73           O  
ANISOU  723  OD1 ASN A 288     7500   8888   7447   1703   -198   -292       O  
ATOM    724  ND2 ASN A 288      13.199   9.257 -22.901  1.00 70.19           N  
ANISOU  724  ND2 ASN A 288     8511   9633   8523   1592   -191   -396       N  
ATOM    725  N   LEU A 289      17.424   7.171 -25.406  1.00 61.23           N  
ANISOU  725  N   LEU A 289     7283   8790   7193   1938   -157   -335       N  
ATOM    726  CA  LEU A 289      18.075   6.240 -26.311  1.00 62.20           C  
ANISOU  726  CA  LEU A 289     7422   8911   7302   2032   -120   -339       C  
ATOM    727  C   LEU A 289      19.559   6.086 -25.997  1.00 65.04           C  
ANISOU  727  C   LEU A 289     7720   9439   7552   2150   -125   -267       C  
ATOM    728  O   LEU A 289      20.095   4.980 -26.034  1.00 75.75           O  
ANISOU  728  O   LEU A 289     9116  10778   8888   2283    -60   -228       O  
ATOM    729  CB  LEU A 289      17.912   6.690 -27.760  1.00 68.10           C  
ANISOU  729  CB  LEU A 289     8137   9662   8076   1951   -161   -413       C  
ATOM    730  CG  LEU A 289      16.965   5.880 -28.639  1.00 72.77           C  
ANISOU  730  CG  LEU A 289     8804  10095   8752   1927   -109   -481       C  
ATOM    731  CD1 LEU A 289      17.390   6.048 -30.076  1.00 75.77           C  
ANISOU  731  CD1 LEU A 289     9136  10533   9121   1906   -141   -530       C  
ATOM    732  CD2 LEU A 289      16.990   4.415 -28.249  1.00 72.62           C  
ANISOU  732  CD2 LEU A 289     8879   9964   8750   2042     -6   -452       C  
ATOM    733  N   TYR A 290      20.230   7.196 -25.713  1.00 55.90           N  
ANISOU  733  N   TYR A 290     6468   8451   6322   2101   -196   -252       N  
ATOM    734  CA  TYR A 290      21.651   7.140 -25.397  1.00 61.64           C  
ANISOU  734  CA  TYR A 290     7120   9369   6930   2201   -207   -188       C  
ATOM    735  C   TYR A 290      21.856   6.402 -24.077  1.00 63.76           C  
ANISOU  735  C   TYR A 290     7415   9649   7160   2318   -149   -104       C  
ATOM    736  O   TYR A 290      22.669   5.490 -23.988  1.00 61.31           O  
ANISOU  736  O   TYR A 290     7109   9392   6793   2468   -100    -43       O  
ATOM    737  CB  TYR A 290      22.235   8.546 -25.313  1.00 60.94           C  
ANISOU  737  CB  TYR A 290     6927   9458   6770   2099   -288   -201       C  
ATOM    738  CG  TYR A 290      23.740   8.594 -25.423  1.00 62.06           C  
ANISOU  738  CG  TYR A 290     6977   9818   6785   2176   -310   -160       C  
ATOM    739  CD1 TYR A 290      24.369   8.512 -26.659  1.00 60.84           C  
ANISOU  739  CD1 TYR A 290     6791   9714   6611   2196   -330   -188       C  
ATOM    740  CD2 TYR A 290      24.533   8.733 -24.290  1.00 54.80           C  
ANISOU  740  CD2 TYR A 290     5994   9068   5759   2226   -311    -96       C  
ATOM    741  CE1 TYR A 290      25.763   8.560 -26.760  1.00 61.95           C  
ANISOU  741  CE1 TYR A 290     6842  10068   6629   2266   -351   -150       C  
ATOM    742  CE2 TYR A 290      25.912   8.784 -24.380  1.00 54.49           C  
ANISOU  742  CE2 TYR A 290     5860   9250   5592   2294   -331    -59       C  
ATOM    743  CZ  TYR A 290      26.525   8.698 -25.613  1.00 62.29           C  
ANISOU  743  CZ  TYR A 290     6821  10285   6563   2315   -351    -86       C  
ATOM    744  OH  TYR A 290      27.904   8.750 -25.693  1.00 64.33           O  
ANISOU  744  OH  TYR A 290     6981  10775   6687   2383   -371    -49       O  
ATOM    745  N   LYS A 291      21.091   6.792 -23.061  1.00 70.53           N  
ANISOU  745  N   LYS A 291     8293  10457   8049   2254   -151    -98       N  
ATOM    746  CA  LYS A 291      21.168   6.172 -21.743  1.00 77.58           C  
ANISOU  746  CA  LYS A 291     9210  11359   8910   2354    -99    -19       C  
ATOM    747  C   LYS A 291      20.844   4.679 -21.798  1.00 88.50           C  
ANISOU  747  C   LYS A 291    10703  12577  10345   2484      1     12       C  
ATOM    748  O   LYS A 291      20.981   3.974 -20.803  1.00102.46           O  
ANISOU  748  O   LYS A 291    12502  14344  12085   2596     61     89       O  
ATOM    749  CB  LYS A 291      20.222   6.886 -20.770  1.00 73.24           C  
ANISOU  749  CB  LYS A 291     8671  10756   8401   2242   -120    -33       C  
ATOM    750  CG  LYS A 291      20.382   6.484 -19.310  1.00 72.47           C  
ANISOU  750  CG  LYS A 291     8574  10708   8254   2328    -81     50       C  
ATOM    751  N   LYS A 292      20.410   4.201 -22.958  1.00 85.86           N  
ANISOU  751  N   LYS A 292    10431  12108  10086   2467     26    -48       N  
ATOM    752  CA  LYS A 292      20.105   2.785 -23.134  1.00 82.22           C  
ANISOU  752  CA  LYS A 292    10084  11480   9677   2575    134    -33       C  
ATOM    753  C   LYS A 292      21.176   2.100 -23.973  1.00 79.40           C  
ANISOU  753  C   LYS A 292     9716  11185   9265   2700    166    -11       C  
ATOM    754  O   LYS A 292      21.722   1.074 -23.574  1.00 88.93           O  
ANISOU  754  O   LYS A 292    10968  12386  10435   2863    251     66       O  
ATOM    755  CB  LYS A 292      18.729   2.603 -23.780  1.00 83.53           C  
ANISOU  755  CB  LYS A 292    10337  11435   9966   2461    157   -126       C  
ATOM    756  N   ASN A 293      21.478   2.674 -25.132  1.00 78.55           N  
ANISOU  756  N   ASN A 293     9551  11141   9153   2629    103    -73       N  
ATOM    757  CA  ASN A 293      22.503   2.124 -26.019  1.00 91.97           C  
ANISOU  757  CA  ASN A 293    11233  12912  10801   2736    124    -59       C  
ATOM    758  C   ASN A 293      23.908   2.219 -25.427  1.00 96.56           C  
ANISOU  758  C   ASN A 293    11721  13722  11245   2862    107     36       C  
ATOM    759  O   ASN A 293      24.612   1.218 -25.324  1.00103.12           O  
ANISOU  759  O   ASN A 293    12582  14570  12028   3033    183    106       O  
ATOM    760  CB  ASN A 293      22.472   2.824 -27.378  1.00 95.33           C  
ANISOU  760  CB  ASN A 293    11608  13364  11250   2618     52   -150       C  
ATOM    761  CG  ASN A 293      21.145   2.650 -28.093  1.00103.93           C  
ANISOU  761  CG  ASN A 293    12778  14253  12460   2505     74   -244       C  
ATOM    762  OD1 ASN A 293      20.545   1.575 -28.061  1.00104.35           O  
ANISOU  762  OD1 ASN A 293    12939  14133  12574   2550    171   -252       O  
ATOM    763  ND2 ASN A 293      20.680   3.711 -28.746  1.00108.31           N  
ANISOU  763  ND2 ASN A 293    13277  14833  13043   2355     -9   -315       N  
ATOM    764  N   MET A 294      24.304   3.427 -25.036  1.00 91.10           N  
ANISOU  764  N   MET A 294    10918  13210  10488   2776     12     37       N  
ATOM    765  CA  MET A 294      25.653   3.678 -24.537  1.00 83.62           C  
ANISOU  765  CA  MET A 294     9860  12516   9396   2867    -16    112       C  
ATOM    766  C   MET A 294      25.719   3.735 -23.013  1.00 82.47           C  
ANISOU  766  C   MET A 294     9691  12451   9192   2912     -1    190       C  
ATOM    767  O   MET A 294      26.791   3.918 -22.442  1.00 82.74           O  
ANISOU  767  O   MET A 294     9629  12714   9097   2988    -19    257       O  
ATOM    768  CB  MET A 294      26.191   4.982 -25.123  1.00 81.54           C  
ANISOU  768  CB  MET A 294     9480  12422   9077   2738   -123     58       C  
ATOM    769  CG  MET A 294      26.251   5.006 -26.644  1.00 82.54           C  
ANISOU  769  CG  MET A 294     9613  12504   9246   2697   -146    -13       C  
ATOM    770  SD  MET A 294      27.502   3.905 -27.332  1.00143.49           S  
ANISOU  770  SD  MET A 294    17322  20311  16887   2893    -94     41       S  
ATOM    771  CE  MET A 294      28.984   4.495 -26.511  1.00 73.32           C  
ANISOU  771  CE  MET A 294     8284  11758   7815   2956   -143    121       C  
ATOM    772  N   ASN A 295      24.567   3.573 -22.369  1.00 83.71           N  
ANISOU  772  N   ASN A 295     9932  12432   9441   2864     32    179       N  
ATOM    773  CA  ASN A 295      24.440   3.672 -20.911  1.00 84.27           C  
ANISOU  773  CA  ASN A 295     9988  12557   9473   2887     45    244       C  
ATOM    774  C   ASN A 295      25.289   4.768 -20.266  1.00 86.41           C  
ANISOU  774  C   ASN A 295    10117  13096   9619   2835    -33    264       C  
ATOM    775  O   ASN A 295      26.113   4.488 -19.398  1.00 93.69           O  
ANISOU  775  O   ASN A 295    10979  14191  10428   2954    -11    353       O  
ATOM    776  CB  ASN A 295      24.733   2.322 -20.249  1.00 87.14           C  
ANISOU  776  CB  ASN A 295    10417  12886   9808   3095    155    349       C  
ATOM    777  N   GLU A 296      25.083   6.015 -20.683  1.00 89.54           N  
ANISOU  777  N   GLU A 296    10459  13531  10030   2656   -118    181       N  
ATOM    778  CA  GLU A 296      25.840   7.134 -20.123  1.00 90.66           C  
ANISOU  778  CA  GLU A 296    10473  13917  10057   2577   -185    183       C  
ATOM    779  C   GLU A 296      24.962   8.205 -19.480  1.00 88.62           C  
ANISOU  779  C   GLU A 296    10214  13610   9846   2403   -225    131       C  
ATOM    780  O   GLU A 296      24.533   8.065 -18.335  1.00 86.63           O  
ANISOU  780  O   GLU A 296     9981  13336   9597   2418   -198    170       O  
ATOM    781  CB  GLU A 296      26.754   7.768 -21.174  1.00 86.99           C  
ANISOU  781  CB  GLU A 296     9924  13602   9527   2529   -244    140       C  
ATOM    782  CG  GLU A 296      27.761   6.801 -21.748  1.00 87.62           C  
ANISOU  782  CG  GLU A 296     9986  13766   9539   2704   -209    195       C  
ATOM    783  CD  GLU A 296      29.124   7.431 -21.971  1.00 85.96           C  
ANISOU  783  CD  GLU A 296     9639  13844   9180   2698   -263    202       C  
ATOM    784  OE1 GLU A 296      29.243   8.359 -22.802  1.00 79.29           O  
ANISOU  784  OE1 GLU A 296     8752  13034   8340   2563   -326    125       O  
ATOM    785  OE2 GLU A 296      30.085   6.985 -21.315  1.00 91.00           O  
ANISOU  785  OE2 GLU A 296    10207  14679   9690   2834   -238    287       O  
ATOM    786  N   GLY A 297      24.712   9.286 -20.210  1.00 88.53           N  
ANISOU  786  N   GLY A 297    10183  13585   9871   2242   -285     46       N  
ATOM    787  CA  GLY A 297      23.933  10.381 -19.663  1.00 86.52           C  
ANISOU  787  CA  GLY A 297     9930  13289   9657   2078   -317     -3       C  
ATOM    788  C   GLY A 297      24.639  11.727 -19.666  1.00 85.30           C  
ANISOU  788  C   GLY A 297     9673  13327   9411   1946   -375    -44       C  
ATOM    789  O   GLY A 297      24.005  12.760 -19.465  1.00 91.24           O  
ANISOU  789  O   GLY A 297    10433  14029  10203   1796   -398    -98       O  
ATOM    790  N   LEU A 298      25.948  11.726 -19.899  1.00 81.96           N  
ANISOU  790  N   LEU A 298     9156  13123   8864   2000   -391    -21       N  
ATOM    791  CA  LEU A 298      26.708  12.973 -19.909  1.00 73.09           C  
ANISOU  791  CA  LEU A 298     7933  12196   7641   1869   -438    -65       C  
ATOM    792  C   LEU A 298      27.322  13.378 -21.267  1.00 74.60           C  
ANISOU  792  C   LEU A 298     8090  12440   7814   1828   -475   -112       C  
ATOM    793  O   LEU A 298      28.201  14.241 -21.314  1.00 86.57           O  
ANISOU  793  O   LEU A 298     9515  14153   9225   1744   -505   -140       O  
ATOM    794  CB  LEU A 298      27.789  12.954 -18.825  1.00 59.64           C  
ANISOU  794  CB  LEU A 298     6121  10764   5775   1920   -433     -9       C  
ATOM    795  CG  LEU A 298      27.306  13.049 -17.374  1.00 64.50           C  
ANISOU  795  CG  LEU A 298     6738  11387   6381   1899   -409     19       C  
ATOM    796  CD1 LEU A 298      28.449  13.484 -16.487  1.00 55.23           C  
ANISOU  796  CD1 LEU A 298     5430  10527   5029   1884   -418     42       C  
ATOM    797  CD2 LEU A 298      26.150  14.023 -17.239  1.00 66.01           C  
ANISOU  797  CD2 LEU A 298     6994  11406   6680   1725   -421    -53       C  
ATOM    798  N   ALA A 299      26.879  12.778 -22.366  1.00 63.44           N  
ANISOU  798  N   ALA A 299     6745  10860   6497   1881   -469   -126       N  
ATOM    799  CA  ALA A 299      27.417  13.182 -23.672  1.00 64.68           C  
ANISOU  799  CA  ALA A 299     6868  11065   6640   1840   -506   -172       C  
ATOM    800  C   ALA A 299      26.791  14.495 -24.130  1.00 60.63           C  
ANISOU  800  C   ALA A 299     6372  10476   6188   1654   -537   -251       C  
ATOM    801  O   ALA A 299      25.762  14.919 -23.602  1.00 50.39           O  
ANISOU  801  O   ALA A 299     5132   9045   4969   1574   -526   -270       O  
ATOM    802  CB  ALA A 299      27.226  12.091 -24.721  1.00 52.18           C  
ANISOU  802  CB  ALA A 299     5347   9350   5131   1957   -486   -164       C  
ATOM    803  N   THR A 300      27.437  15.149 -25.087  1.00 54.35           N  
ANISOU  803  N   THR A 300     5526   9773   5351   1590   -570   -291       N  
ATOM    804  CA  THR A 300      26.926  16.387 -25.652  1.00 57.90           C  
ANISOU  804  CA  THR A 300     5994  10153   5852   1428   -591   -359       C  
ATOM    805  C   THR A 300      25.643  16.101 -26.418  1.00 65.14           C  
ANISOU  805  C   THR A 300     7007  10823   6920   1430   -583   -381       C  
ATOM    806  O   THR A 300      25.456  14.997 -26.922  1.00 66.66           O  
ANISOU  806  O   THR A 300     7235  10933   7160   1545   -570   -362       O  
ATOM    807  CB  THR A 300      27.884  16.908 -26.698  1.00 59.98           C  
ANISOU  807  CB  THR A 300     6192  10549   6047   1388   -623   -390       C  
ATOM    808  OG1 THR A 300      27.889  15.981 -27.784  1.00 55.53           O  
ANISOU  808  OG1 THR A 300     5651   9916   5532   1497   -629   -381       O  
ATOM    809  CG2 THR A 300      29.304  17.012 -26.134  1.00 66.17           C  
ANISOU  809  CG2 THR A 300     6867  11609   6666   1404   -633   -368       C  
ATOM    810  N   ASN A 301      24.765  17.099 -26.511  1.00 66.90           N  
ANISOU  810  N   ASN A 301     7270  10937   7211   1301   -584   -424       N  
ATOM    811  CA  ASN A 301      23.637  17.047 -27.439  1.00 65.27           C  
ANISOU  811  CA  ASN A 301     7134  10537   7129   1285   -582   -453       C  
ATOM    812  C   ASN A 301      24.028  16.442 -28.790  1.00 65.27           C  
ANISOU  812  C   ASN A 301     7119  10544   7138   1354   -600   -463       C  
ATOM    813  O   ASN A 301      23.502  15.405 -29.180  1.00 65.58           O  
ANISOU  813  O   ASN A 301     7205  10469   7244   1441   -584   -456       O  
ATOM    814  CB  ASN A 301      23.069  18.446 -27.668  1.00 60.92           C  
ANISOU  814  CB  ASN A 301     6599   9935   6612   1138   -585   -495       C  
ATOM    815  CG  ASN A 301      22.216  18.929 -26.518  1.00 63.85           C  
ANISOU  815  CG  ASN A 301     7016  10224   7020   1073   -560   -492       C  
ATOM    816  OD1 ASN A 301      21.563  18.141 -25.825  1.00 54.56           O  
ANISOU  816  OD1 ASN A 301     5882   8957   5891   1135   -542   -466       O  
ATOM    817  ND2 ASN A 301      22.205  20.242 -26.314  1.00 74.12           N  
ANISOU  817  ND2 ASN A 301     8312  11549   8299    944   -551   -520       N  
ATOM    818  N   VAL A 302      24.956  17.090 -29.492  1.00 64.93           N  
ANISOU  818  N   VAL A 302     7012  10636   7024   1310   -628   -483       N  
ATOM    819  CA  VAL A 302      25.405  16.632 -30.810  1.00 57.98           C  
ANISOU  819  CA  VAL A 302     6109   9778   6143   1366   -648   -496       C  
ATOM    820  C   VAL A 302      25.741  15.141 -30.859  1.00 58.99           C  
ANISOU  820  C   VAL A 302     6244   9904   6264   1523   -632   -460       C  
ATOM    821  O   VAL A 302      25.482  14.464 -31.854  1.00 59.78           O  
ANISOU  821  O   VAL A 302     6370   9924   6419   1578   -629   -476       O  
ATOM    822  CB  VAL A 302      26.643  17.433 -31.297  1.00 81.88           C  
ANISOU  822  CB  VAL A 302     9052  12996   9063   1311   -679   -512       C  
ATOM    823  CG1 VAL A 302      27.257  16.789 -32.539  1.00 76.36           C  
ANISOU  823  CG1 VAL A 302     8321  12343   8349   1391   -701   -518       C  
ATOM    824  CG2 VAL A 302      26.265  18.874 -31.570  1.00 81.26           C  
ANISOU  824  CG2 VAL A 302     8981  12889   9004   1159   -683   -553       C  
ATOM    825  N   ASN A 303      26.338  14.627 -29.795  1.00 60.96           N  
ANISOU  825  N   ASN A 303     6472  10248   6442   1599   -615   -412       N  
ATOM    826  CA  ASN A 303      26.685  13.213 -29.771  1.00 64.27           C  
ANISOU  826  CA  ASN A 303     6906  10662   6850   1761   -585   -368       C  
ATOM    827  C   ASN A 303      25.502  12.287 -29.505  1.00 58.13           C  
ANISOU  827  C   ASN A 303     6230   9673   6186   1815   -538   -359       C  
ATOM    828  O   ASN A 303      25.448  11.175 -30.021  1.00 61.94           O  
ANISOU  828  O   ASN A 303     6753  10079   6702   1920   -506   -351       O  
ATOM    829  CB  ASN A 303      27.834  12.950 -28.795  1.00 67.10           C  
ANISOU  829  CB  ASN A 303     7197  11219   7078   1841   -579   -308       C  
ATOM    830  CG  ASN A 303      29.189  13.155 -29.438  1.00 65.79           C  
ANISOU  830  CG  ASN A 303     6936  11263   6797   1861   -612   -308       C  
ATOM    831  OD1 ASN A 303      29.425  12.717 -30.566  1.00 68.63           O  
ANISOU  831  OD1 ASN A 303     7298  11602   7175   1911   -620   -323       O  
ATOM    832  ND2 ASN A 303      30.087  13.832 -28.727  1.00 61.19           N  
ANISOU  832  ND2 ASN A 303     6268  10891   6091   1817   -631   -295       N  
ATOM    833  N   LYS A 304      24.549  12.748 -28.710  1.00 59.14           N  
ANISOU  833  N   LYS A 304     6400   9703   6369   1739   -529   -366       N  
ATOM    834  CA  LYS A 304      23.361  11.953 -28.450  1.00 60.81           C  
ANISOU  834  CA  LYS A 304     6704   9715   6684   1772   -485   -365       C  
ATOM    835  C   LYS A 304      22.607  11.793 -29.764  1.00 55.94           C  
ANISOU  835  C   LYS A 304     6128   8969   6159   1740   -487   -421       C  
ATOM    836  O   LYS A 304      21.943  10.784 -29.997  1.00 63.12           O  
ANISOU  836  O   LYS A 304     7106   9738   7138   1797   -444   -429       O  
ATOM    837  CB  LYS A 304      22.458  12.638 -27.426  1.00 54.52           C  
ANISOU  837  CB  LYS A 304     5938   8850   5928   1681   -482   -367       C  
ATOM    838  CG  LYS A 304      23.061  12.831 -26.057  1.00 67.65           C  
ANISOU  838  CG  LYS A 304     7561  10638   7504   1697   -477   -318       C  
ATOM    839  CD  LYS A 304      22.147  13.741 -25.234  1.00 78.12           C  
ANISOU  839  CD  LYS A 304     8913  11896   8874   1579   -480   -336       C  
ATOM    840  CE  LYS A 304      22.560  13.832 -23.768  1.00 77.27           C  
ANISOU  840  CE  LYS A 304     8774  11896   8690   1593   -468   -290       C  
ATOM    841  NZ  LYS A 304      22.157  12.623 -22.991  1.00 79.33           N  
ANISOU  841  NZ  LYS A 304     9091  12070   8982   1711   -421   -239       N  
ATOM    842  N   ILE A 305      22.726  12.801 -30.619  1.00 50.93           N  
ANISOU  842  N   ILE A 305     5448   8386   5517   1646   -532   -462       N  
ATOM    843  CA  ILE A 305      21.970  12.861 -31.865  1.00 51.15           C  
ANISOU  843  CA  ILE A 305     5499   8314   5622   1600   -539   -515       C  
ATOM    844  C   ILE A 305      22.613  12.083 -33.010  1.00 60.48           C  
ANISOU  844  C   ILE A 305     6662   9530   6788   1677   -539   -529       C  
ATOM    845  O   ILE A 305      21.909  11.485 -33.818  1.00 61.64           O  
ANISOU  845  O   ILE A 305     6850   9566   7006   1685   -518   -566       O  
ATOM    846  CB  ILE A 305      21.721  14.314 -32.291  1.00 46.38           C  
ANISOU  846  CB  ILE A 305     4861   7740   5022   1470   -579   -546       C  
ATOM    847  CG1 ILE A 305      20.576  14.910 -31.461  1.00 49.61           C  
ANISOU  847  CG1 ILE A 305     5317   8043   5489   1392   -565   -547       C  
ATOM    848  CG2 ILE A 305      21.401  14.361 -33.755  1.00 48.49           C  
ANISOU  848  CG2 ILE A 305     5120   7973   5331   1447   -594   -590       C  
ATOM    849  CD1 ILE A 305      20.479  16.401 -31.554  1.00 50.95           C  
ANISOU  849  CD1 ILE A 305     5461   8251   5647   1274   -588   -563       C  
ATOM    850  N   LYS A 306      23.944  12.087 -33.077  1.00 68.76           N  
ANISOU  850  N   LYS A 306     7645  10740   7738   1731   -559   -502       N  
ATOM    851  CA  LYS A 306      24.667  11.255 -34.035  1.00 62.00           C  
ANISOU  851  CA  LYS A 306     6773   9927   6858   1822   -553   -506       C  
ATOM    852  C   LYS A 306      24.463   9.798 -33.673  1.00 57.04           C  
ANISOU  852  C   LYS A 306     6216   9195   6260   1947   -485   -480       C  
ATOM    853  O   LYS A 306      24.260   8.955 -34.531  1.00 60.57           O  
ANISOU  853  O   LYS A 306     6700   9561   6751   1994   -454   -509       O  
ATOM    854  CB  LYS A 306      26.164  11.556 -34.005  1.00 67.40           C  
ANISOU  854  CB  LYS A 306     7369  10823   7418   1861   -585   -475       C  
ATOM    855  CG  LYS A 306      26.545  12.947 -34.451  1.00 71.39           C  
ANISOU  855  CG  LYS A 306     7804  11441   7880   1740   -643   -504       C  
ATOM    856  CD  LYS A 306      28.045  13.051 -34.625  1.00 71.91           C  
ANISOU  856  CD  LYS A 306     7783  11719   7821   1783   -670   -482       C  
ATOM    857  CE  LYS A 306      28.482  14.491 -34.813  1.00 75.91           C  
ANISOU  857  CE  LYS A 306     8224  12345   8272   1651   -716   -508       C  
ATOM    858  NZ  LYS A 306      29.886  14.568 -35.297  1.00 77.94           N  
ANISOU  858  NZ  LYS A 306     8394  12806   8414   1683   -746   -501       N  
ATOM    859  N   SER A 307      24.535   9.509 -32.383  1.00 52.27           N  
ANISOU  859  N   SER A 307     5633   8595   5631   1999   -456   -426       N  
ATOM    860  CA  SER A 307      24.225   8.183 -31.881  1.00 61.97           C  
ANISOU  860  CA  SER A 307     6943   9707   6895   2114   -380   -394       C  
ATOM    861  C   SER A 307      22.809   7.778 -32.295  1.00 62.13           C  
ANISOU  861  C   SER A 307     7052   9519   7038   2059   -343   -451       C  
ATOM    862  O   SER A 307      22.566   6.621 -32.631  1.00 62.23           O  
ANISOU  862  O   SER A 307     7133   9419   7091   2133   -278   -460       O  
ATOM    863  CB  SER A 307      24.377   8.149 -30.353  1.00 66.64           C  
ANISOU  863  CB  SER A 307     7539  10340   7443   2158   -360   -327       C  
ATOM    864  OG  SER A 307      23.925   6.919 -29.814  1.00 68.53           O  
ANISOU  864  OG  SER A 307     7869  10443   7726   2261   -278   -295       O  
ATOM    865  N   PHE A 308      21.880   8.731 -32.269  1.00 59.08           N  
ANISOU  865  N   PHE A 308     6662   9083   6702   1927   -380   -489       N  
ATOM    866  CA  PHE A 308      20.524   8.476 -32.742  1.00 53.47           C  
ANISOU  866  CA  PHE A 308     6016   8205   6094   1863   -353   -547       C  
ATOM    867  C   PHE A 308      20.515   8.245 -34.238  1.00 55.56           C  
ANISOU  867  C   PHE A 308     6267   8462   6382   1848   -359   -606       C  
ATOM    868  O   PHE A 308      19.976   7.251 -34.712  1.00 62.66           O  
ANISOU  868  O   PHE A 308     7228   9245   7334   1874   -302   -642       O  
ATOM    869  CB  PHE A 308      19.587   9.638 -32.431  1.00 50.84           C  
ANISOU  869  CB  PHE A 308     5673   7844   5800   1734   -392   -568       C  
ATOM    870  CG  PHE A 308      18.292   9.568 -33.184  1.00 54.40           C  
ANISOU  870  CG  PHE A 308     6162   8170   6338   1659   -379   -632       C  
ATOM    871  CD1 PHE A 308      17.262   8.766 -32.731  1.00 54.28           C  
ANISOU  871  CD1 PHE A 308     6227   8007   6389   1663   -321   -646       C  
ATOM    872  CD2 PHE A 308      18.118  10.274 -34.367  1.00 47.66           C  
ANISOU  872  CD2 PHE A 308     5258   7357   5493   1586   -421   -677       C  
ATOM    873  CE1 PHE A 308      16.074   8.683 -33.429  1.00 59.78           C  
ANISOU  873  CE1 PHE A 308     6948   8610   7154   1589   -307   -710       C  
ATOM    874  CE2 PHE A 308      16.937  10.198 -35.069  1.00 44.46           C  
ANISOU  874  CE2 PHE A 308     4875   6862   5155   1522   -408   -734       C  
ATOM    875  CZ  PHE A 308      15.911   9.404 -34.603  1.00 51.74           C  
ANISOU  875  CZ  PHE A 308     5872   7650   6138   1520   -352   -753       C  
ATOM    876  N   ILE A 309      21.108   9.181 -34.973  1.00 61.34           N  
ANISOU  876  N   ILE A 309     6918   9318   7069   1799   -424   -619       N  
ATOM    877  CA  ILE A 309      21.164   9.129 -36.433  1.00 54.89           C  
ANISOU  877  CA  ILE A 309     6072   8519   6265   1778   -440   -673       C  
ATOM    878  C   ILE A 309      21.825   7.853 -36.887  1.00 62.78           C  
ANISOU  878  C   ILE A 309     7097   9508   7247   1892   -390   -672       C  
ATOM    879  O   ILE A 309      21.516   7.327 -37.944  1.00 76.78           O  
ANISOU  879  O   ILE A 309     8885  11230   9057   1885   -369   -727       O  
ATOM    880  CB  ILE A 309      22.000  10.288 -36.993  1.00 50.35           C  
ANISOU  880  CB  ILE A 309     5403   8101   5625   1730   -512   -669       C  
ATOM    881  CG1 ILE A 309      21.159  11.554 -37.133  1.00 39.97           C  
ANISOU  881  CG1 ILE A 309     4069   6774   4345   1604   -551   -692       C  
ATOM    882  CG2 ILE A 309      22.662   9.895 -38.326  1.00 42.57           C  
ANISOU  882  CG2 ILE A 309     4380   7178   4617   1767   -523   -700       C  
ATOM    883  CD1 ILE A 309      21.980  12.763 -37.557  1.00 40.06           C  
ANISOU  883  CD1 ILE A 309     4000   6929   4291   1551   -610   -685       C  
ATOM    884  N   ASP A 310      22.752   7.365 -36.081  1.00 72.47           N  
ANISOU  884  N   ASP A 310     8330  10793   8414   2001   -367   -608       N  
ATOM    885  CA  ASP A 310      23.545   6.208 -36.451  1.00 86.45           C  
ANISOU  885  CA  ASP A 310    10122  12570  10153   2130   -315   -592       C  
ATOM    886  C   ASP A 310      22.752   4.918 -36.283  1.00 86.32           C  
ANISOU  886  C   ASP A 310    10220  12368  10210   2179   -216   -610       C  
ATOM    887  O   ASP A 310      22.968   3.955 -37.014  1.00 93.33           O  
ANISOU  887  O   ASP A 310    11146  13206  11109   2244   -160   -635       O  
ATOM    888  CB  ASP A 310      24.843   6.170 -35.634  1.00 97.65           C  
ANISOU  888  CB  ASP A 310    11498  14137  11468   2240   -322   -509       C  
ATOM    889  CG  ASP A 310      25.711   4.970 -35.963  1.00110.99           C  
ANISOU  889  CG  ASP A 310    13211  15841  13117   2393   -261   -479       C  
ATOM    890  OD1 ASP A 310      25.450   3.878 -35.417  1.00118.58           O  
ANISOU  890  OD1 ASP A 310    14263  16684  14108   2487   -172   -451       O  
ATOM    891  OD2 ASP A 310      26.664   5.118 -36.757  1.00114.61           O  
ANISOU  891  OD2 ASP A 310    13603  16430  13515   2423   -297   -482       O  
ATOM    892  N   THR A 311      21.823   4.902 -35.336  1.00 84.89           N  
ANISOU  892  N   THR A 311    10096  12080  10079   2143   -189   -601       N  
ATOM    893  CA  THR A 311      21.034   3.700 -35.088  1.00 87.20           C  
ANISOU  893  CA  THR A 311    10501  12190  10438   2180    -88   -619       C  
ATOM    894  C   THR A 311      19.657   3.752 -35.757  1.00 87.36           C  
ANISOU  894  C   THR A 311    10556  12090  10548   2050    -78   -710       C  
ATOM    895  O   THR A 311      18.854   2.834 -35.607  1.00 93.69           O  
ANISOU  895  O   THR A 311    11451  12739  11408   2050      6   -741       O  
ATOM    896  CB  THR A 311      20.884   3.397 -33.568  1.00 83.11           C  
ANISOU  896  CB  THR A 311    10038  11622   9917   2240    -45   -547       C  
ATOM    897  OG1 THR A 311      20.176   4.464 -32.922  1.00 87.23           O  
ANISOU  897  OG1 THR A 311    10529  12156  10459   2130   -105   -549       O  
ATOM    898  CG2 THR A 311      22.258   3.212 -32.907  1.00 80.00           C  
ANISOU  898  CG2 THR A 311     9607  11365   9425   2382    -43   -452       C  
ATOM    899  N   LYS A 312      19.389   4.817 -36.504  1.00 81.83           N  
ANISOU  899  N   LYS A 312     9777  11465   9850   1942   -159   -753       N  
ATOM    900  CA  LYS A 312      18.111   4.944 -37.196  1.00 85.78           C  
ANISOU  900  CA  LYS A 312    10291  11884  10419   1824   -156   -835       C  
ATOM    901  C   LYS A 312      18.286   5.168 -38.692  1.00 83.30           C  
ANISOU  901  C   LYS A 312     9913  11641  10097   1780   -191   -895       C  
ATOM    902  O   LYS A 312      17.333   5.488 -39.394  1.00 86.39           O  
ANISOU  902  O   LYS A 312    10285  12011  10526   1679   -204   -959       O  
ATOM    903  CB  LYS A 312      17.284   6.086 -36.602  1.00 93.15           C  
ANISOU  903  CB  LYS A 312    11195  12826  11373   1724   -212   -826       C  
ATOM    904  CG  LYS A 312      16.793   5.851 -35.180  1.00101.17           C  
ANISOU  904  CG  LYS A 312    12276  13752  12412   1743   -174   -782       C  
ATOM    905  CD  LYS A 312      15.563   4.960 -35.145  1.00101.75           C  
ANISOU  905  CD  LYS A 312    12438  13665  12558   1704    -96   -838       C  
ATOM    906  CE  LYS A 312      14.988   4.877 -33.739  1.00 97.41           C  
ANISOU  906  CE  LYS A 312    11946  13032  12032   1709    -67   -795       C  
ATOM    907  NZ  LYS A 312      13.824   3.955 -33.693  1.00 99.03           N  
ANISOU  907  NZ  LYS A 312    12241  13082  12303   1669     16   -851       N  
ATOM    908  N   LEU A 313      19.507   5.010 -39.181  1.00 82.59           N  
ANISOU  908  N   LEU A 313     9785  11646   9949   1859   -205   -873       N  
ATOM    909  CA  LEU A 313      19.769   5.204 -40.598  1.00 86.32           C  
ANISOU  909  CA  LEU A 313    10194  12194  10408   1825   -239   -927       C  
ATOM    910  C   LEU A 313      20.696   4.113 -41.105  1.00 97.67           C  
ANISOU  910  C   LEU A 313    11659  13633  11818   1933   -184   -930       C  
ATOM    911  O   LEU A 313      21.351   4.257 -42.134  1.00104.09           O  
ANISOU  911  O   LEU A 313    12411  14541  12597   1940   -218   -952       O  
ATOM    912  CB  LEU A 313      20.381   6.585 -40.853  1.00 88.37           C  
ANISOU  912  CB  LEU A 313    10349  12612  10616   1785   -341   -898       C  
ATOM    913  CG  LEU A 313      19.549   7.816 -40.463  1.00 91.08           C  
ANISOU  913  CG  LEU A 313    10662  12964  10981   1680   -394   -892       C  
ATOM    914  CD1 LEU A 313      20.304   9.099 -40.780  1.00 93.00           C  
ANISOU  914  CD1 LEU A 313    10812  13357  11165   1648   -477   -864       C  
ATOM    915  CD2 LEU A 313      18.208   7.808 -41.164  1.00 88.74           C  
ANISOU  915  CD2 LEU A 313    10374  12595  10747   1585   -379   -963       C  
ATOM    916  N   LYS A 314      20.754   3.015 -40.366  1.00 97.60           N  
ANISOU  916  N   LYS A 314    11746  13516  11823   2023    -93   -904       N  
ATOM    917  CA  LYS A 314      21.544   1.873 -40.789  1.00 98.41           C  
ANISOU  917  CA  LYS A 314    11894  13594  11904   2137    -18   -903       C  
ATOM    918  C   LYS A 314      20.726   0.594 -40.636  1.00104.28           C  
ANISOU  918  C   LYS A 314    12765  14144  12712   2146    110   -948       C  
ATOM    919  O   LYS A 314      19.883   0.477 -39.744  1.00 99.02           O  
ANISOU  919  O   LYS A 314    12160  13375  12090   2114    144   -940       O  
ATOM    920  CB  LYS A 314      22.882   1.820 -40.037  1.00 91.63           C  
ANISOU  920  CB  LYS A 314    11015  12836  10964   2280    -27   -800       C  
ATOM    921  CG  LYS A 314      23.735   3.071 -40.273  1.00 86.81           C  
ANISOU  921  CG  LYS A 314    10277  12425  10282   2256   -146   -769       C  
ATOM    922  CD  LYS A 314      25.201   2.890 -39.903  1.00 86.29           C  
ANISOU  922  CD  LYS A 314    10174  12492  10119   2397   -151   -686       C  
ATOM    923  CE  LYS A 314      26.051   4.034 -40.470  1.00 85.56           C  
ANISOU  923  CE  LYS A 314     9956  12598   9955   2355   -261   -680       C  
ATOM    924  NZ  LYS A 314      27.525   3.872 -40.258  1.00 85.03           N  
ANISOU  924  NZ  LYS A 314     9837  12689   9781   2484   -270   -609       N  
ATOM    925  N   LYS A 315      20.966  -0.348 -41.542  1.00110.66           N  
ANISOU  925  N   LYS A 315    13615  14904  13528   2181    183  -1001       N  
ATOM    926  CA  LYS A 315      20.152  -1.557 -41.650  1.00116.77           C  
ANISOU  926  CA  LYS A 315    14510  15492  14363   2163    314  -1068       C  
ATOM    927  C   LYS A 315      20.734  -2.715 -40.840  1.00122.13           C  
ANISOU  927  C   LYS A 315    15305  16067  15033   2321    434  -1000       C  
ATOM    928  O   LYS A 315      20.362  -3.866 -41.047  1.00128.48           O  
ANISOU  928  O   LYS A 315    16223  16717  15878   2334    564  -1051       O  
ATOM    929  CB  LYS A 315      20.044  -1.960 -43.123  1.00117.22           C  
ANISOU  929  CB  LYS A 315    14555  15550  14433   2102    341  -1173       C  
ATOM    930  CG  LYS A 315      18.879  -2.877 -43.472  1.00118.23           C  
ANISOU  930  CG  LYS A 315    14780  15516  14628   2008    455  -1281       C  
ATOM    931  CD  LYS A 315      17.560  -2.197 -43.178  1.00116.23           C  
ANISOU  931  CD  LYS A 315    14500  15247  14416   1863    409  -1321       C  
ATOM    932  CE  LYS A 315      16.437  -2.753 -44.034  1.00114.36           C  
ANISOU  932  CE  LYS A 315    14295  14934  14224   1726    480  -1455       C  
ATOM    933  NZ  LYS A 315      15.173  -1.990 -43.831  1.00111.43           N  
ANISOU  933  NZ  LYS A 315    13877  14581  13879   1588    424  -1490       N  
ATOM    934  N   ALA A 316      21.627  -2.390 -39.909  1.00116.59           N  
ANISOU  934  N   ALA A 316    14572  15453  14272   2438    395   -886       N  
ATOM    935  CA  ALA A 316      22.521  -3.369 -39.292  1.00112.21           C  
ANISOU  935  CA  ALA A 316    14095  14861  13681   2622    492   -800       C  
ATOM    936  C   ALA A 316      23.735  -3.602 -40.195  1.00112.66           C  
ANISOU  936  C   ALA A 316    14106  15025  13675   2720    487   -789       C  
ATOM    937  O   ALA A 316      24.861  -3.554 -39.727  1.00109.91           O  
ANISOU  937  O   ALA A 316    13719  14793  13248   2859    468   -690       O  
ATOM    938  CB  ALA A 316      21.792  -4.680 -39.005  1.00109.44           C  
ANISOU  938  CB  ALA A 316    13905  14282  13394   2644    656   -832       C  
ATOM    939  N   ASP A 317      23.466  -3.770 -41.494  1.00119.63           N  
ANISOU  939  N   ASP A 317    14980  15886  14587   2635    495   -893       N  
ATOM    940  CA  ASP A 317      24.457  -4.016 -42.549  1.00128.76           C  
ANISOU  940  CA  ASP A 317    16096  17131  15696   2702    492   -906       C  
ATOM    941  C   ASP A 317      25.572  -2.978 -42.580  1.00133.32           C  
ANISOU  941  C   ASP A 317    16532  17939  16185   2746    357   -836       C  
ATOM    942  O   ASP A 317      26.467  -3.059 -43.409  1.00133.43           O  
ANISOU  942  O   ASP A 317    16495  18051  16149   2803    340   -839       O  
ATOM    943  CB  ASP A 317      23.790  -4.056 -43.931  1.00131.65           C  
ANISOU  943  CB  ASP A 317    16447  17465  16110   2560    492  -1041       C  
ATOM    944  CG  ASP A 317      22.695  -5.113 -44.027  1.00134.59           C  
ANISOU  944  CG  ASP A 317    16955  17620  16562   2496    633  -1129       C  
ATOM    945  OD1 ASP A 317      22.363  -5.742 -42.988  1.00136.91           O  
ANISOU  945  OD1 ASP A 317    17359  17778  16883   2552    727  -1086       O  
ATOM    946  OD2 ASP A 317      22.147  -5.316 -45.141  1.00132.50           O  
ANISOU  946  OD2 ASP A 317    16687  17326  16330   2382    655  -1246       O  
ATOM    947  N   LYS A 318      25.549  -2.033 -41.648  1.00136.14           N  
ANISOU  947  N   LYS A 318    16826  18383  16516   2722    270   -774       N  
ATOM    948  CA  LYS A 318      26.377  -0.837 -41.766  1.00134.71           C  
ANISOU  948  CA  LYS A 318    16504  18419  16259   2707    133   -735       C  
ATOM    949  C   LYS A 318      26.067  -0.158 -43.082  1.00134.52           C  
ANISOU  949  C   LYS A 318    16403  18451  16257   2570     56   -828       C  
ATOM    950  O   LYS A 318      26.875   0.591 -43.606  1.00136.90           O  
ANISOU  950  O   LYS A 318    16599  18922  16497   2566    -34   -816       O  
ATOM    951  CB  LYS A 318      27.875  -1.168 -41.669  1.00134.88           C  
ANISOU  951  CB  LYS A 318    16490  18578  16180   2880    141   -649       C  
ATOM    952  N   SER A 319      24.903  -0.478 -43.615  1.00129.94           N  
ANISOU  952  N   SER A 319    15878  17733  15760   2462    101   -922       N  
ATOM    953  CA  SER A 319      24.383   0.069 -44.863  1.00124.14           C  
ANISOU  953  CA  SER A 319    15077  17038  15053   2325     43  -1017       C  
ATOM    954  C   SER A 319      23.310   1.121 -44.599  1.00112.17           C  
ANISOU  954  C   SER A 319    13519  15523  13576   2180    -30  -1040       C  
ATOM    955  O   SER A 319      22.336   0.814 -43.915  1.00108.36           O  
ANISOU  955  O   SER A 319    13112  14911  13150   2141     23  -1053       O  
ATOM    956  CB  SER A 319      23.820  -1.047 -45.746  1.00127.97           C  
ANISOU  956  CB  SER A 319    15642  17388  15591   2299    149  -1115       C  
ATOM    957  OG  SER A 319      22.689  -1.650 -45.143  1.00128.81           O  
ANISOU  957  OG  SER A 319    15854  17320  15767   2251    238  -1148       O  
ATOM    958  N   TRP A 320      23.532   2.307 -45.097  1.00104.86           N  
ANISOU  958  N   TRP A 320    12481  14742  12619   2112   -141  -1040       N  
ATOM    959  CA  TRP A 320      22.547   3.359 -44.976  1.00 98.85           C  
ANISOU  959  CA  TRP A 320    11678  13990  11892   1982   -206  -1059       C  
ATOM    960  C   TRP A 320      21.208   2.888 -45.517  1.00 98.54           C  
ANISOU  960  C   TRP A 320    11684  13832  11925   1882   -151  -1154       C  
ATOM    961  O   TRP A 320      21.149   2.242 -46.556  1.00102.10           O  
ANISOU  961  O   TRP A 320    12140  14266  12386   1867   -110  -1226       O  
ATOM    962  CB  TRP A 320      23.018   4.629 -45.693  1.00 96.04           C  
ANISOU  962  CB  TRP A 320    11200  13801  11490   1926   -318  -1054       C  
ATOM    963  CG  TRP A 320      24.248   5.251 -45.083  1.00 98.95           C  
ANISOU  963  CG  TRP A 320    11516  14300  11780   1997   -376   -968       C  
ATOM    964  CD1 TRP A 320      25.519   5.224 -45.587  1.00 99.38           C  
ANISOU  964  CD1 TRP A 320    11515  14483  11764   2071   -404   -944       C  
ATOM    965  CD2 TRP A 320      24.326   5.968 -43.842  1.00 99.08           C  
ANISOU  965  CD2 TRP A 320    11527  14344  11775   1995   -408   -899       C  
ATOM    966  NE1 TRP A 320      26.378   5.892 -44.745  1.00101.20           N  
ANISOU  966  NE1 TRP A 320    11702  14826  11924   2110   -452   -867       N  
ATOM    967  CE2 TRP A 320      25.672   6.357 -43.667  1.00100.28           C  
ANISOU  967  CE2 TRP A 320    11615  14650  11837   2062   -455   -840       C  
ATOM    968  CE3 TRP A 320      23.388   6.327 -42.867  1.00 93.89           C  
ANISOU  968  CE3 TRP A 320    10910  13603  11162   1939   -402   -885       C  
ATOM    969  CZ2 TRP A 320      26.101   7.086 -42.559  1.00103.63           C  
ANISOU  969  CZ2 TRP A 320    12013  15150  12211   2067   -491   -773       C  
ATOM    970  CZ3 TRP A 320      23.816   7.050 -41.768  1.00 96.91           C  
ANISOU  970  CZ3 TRP A 320    11270  14051  11501   1949   -439   -816       C  
ATOM    971  CH2 TRP A 320      25.160   7.420 -41.621  1.00104.44           C  
ANISOU  971  CH2 TRP A 320    12159  15162  12362   2009   -482   -763       C  
ATOM    972  N   LYS A 321      20.136   3.206 -44.799  1.00 99.64           N  
ANISOU  972  N   LYS A 321    11853  13897  12109   1810   -148  -1156       N  
ATOM    973  CA  LYS A 321      18.803   2.745 -45.166  1.00 97.94           C  
ANISOU  973  CA  LYS A 321    11680  13578  11956   1710    -91  -1244       C  
ATOM    974  C   LYS A 321      18.224   3.616 -46.265  1.00104.21           C  
ANISOU  974  C   LYS A 321    12375  14473  12749   1597   -161  -1300       C  
ATOM    975  O   LYS A 321      17.317   3.206 -46.988  1.00110.69           O  
ANISOU  975  O   LYS A 321    13200  15257  13599   1514   -120  -1389       O  
ATOM    976  CB  LYS A 321      17.876   2.779 -43.952  1.00 95.91           C  
ANISOU  976  CB  LYS A 321    11487  13215  11740   1680    -64  -1221       C  
ATOM    977  CG  LYS A 321      18.408   2.026 -42.748  1.00 97.34           C  
ANISOU  977  CG  LYS A 321    11761  13306  11918   1796      1  -1151       C  
ATOM    978  CD  LYS A 321      17.531   2.227 -41.518  1.00 95.66           C  
ANISOU  978  CD  LYS A 321    11598  13008  11742   1762     13  -1121       C  
ATOM    979  CE  LYS A 321      16.136   1.670 -41.732  1.00 98.09           C  
ANISOU  979  CE  LYS A 321    11963  13195  12112   1659     82  -1210       C  
ATOM    980  NZ  LYS A 321      15.395   1.510 -40.447  1.00 98.32           N  
ANISOU  980  NZ  LYS A 321    12067  13113  12178   1652    121  -1179       N  
ATOM    981  N   ILE A 322      18.752   4.827 -46.382  1.00102.48           N  
ANISOU  981  N   ILE A 322    12063  14384  12489   1593   -261  -1248       N  
ATOM    982  CA  ILE A 322      18.236   5.782 -47.346  1.00103.61           C  
ANISOU  982  CA  ILE A 322    12112  14628  12627   1498   -326  -1282       C  
ATOM    983  C   ILE A 322      19.329   6.207 -48.324  1.00105.24           C  
ANISOU  983  C   ILE A 322    12234  14973  12780   1529   -386  -1273       C  
ATOM    984  O   ILE A 322      20.337   6.806 -47.942  1.00109.44           O  
ANISOU  984  O   ILE A 322    12735  15580  13267   1584   -438  -1203       O  
ATOM    985  CB  ILE A 322      17.577   6.987 -46.640  1.00105.21           C  
ANISOU  985  CB  ILE A 322    12288  14849  12840   1441   -382  -1234       C  
ATOM    986  CG1 ILE A 322      16.952   7.947 -47.652  1.00105.79           C  
ANISOU  986  CG1 ILE A 322    12268  15021  12907   1354   -436  -1263       C  
ATOM    987  CG2 ILE A 322      18.568   7.703 -45.746  1.00108.67           C  
ANISOU  987  CG2 ILE A 322    12716  15336  13239   1501   -432  -1142       C  
ATOM    988  CD1 ILE A 322      15.952   8.896 -47.018  1.00104.76           C  
ANISOU  988  CD1 ILE A 322    12131  14876  12799   1293   -460  -1232       C  
ATOM    989  N   SER A 323      19.121   5.864 -49.590  1.00101.74           N  
ANISOU  989  N   SER A 323    11750  14569  12336   1489   -374  -1349       N  
ATOM    990  CA  SER A 323      20.110   6.099 -50.629  1.00103.08           C  
ANISOU  990  CA  SER A 323    11844  14864  12458   1517   -421  -1353       C  
ATOM    991  C   SER A 323      20.231   7.577 -50.969  1.00103.43           C  
ANISOU  991  C   SER A 323    11790  15040  12471   1474   -517  -1310       C  
ATOM    992  O   SER A 323      19.275   8.341 -50.814  1.00101.95           O  
ANISOU  992  O   SER A 323    11582  14851  12305   1402   -538  -1304       O  
ATOM    993  CB  SER A 323      19.749   5.305 -51.885  1.00104.62           C  
ANISOU  993  CB  SER A 323    12024  15065  12663   1476   -376  -1453       C  
ATOM    994  OG  SER A 323      19.605   3.925 -51.593  1.00105.00           O  
ANISOU  994  OG  SER A 323    12175  14977  12742   1508   -271  -1499       O  
ATOM    995  N   ASN A 324      21.416   7.967 -51.429  1.00103.07           N  
ANISOU  995  N   ASN A 324    11687  15104  12371   1520   -568  -1278       N  
ATOM    996  CA  ASN A 324      21.687   9.335 -51.865  1.00100.05           C  
ANISOU  996  CA  ASN A 324    11214  14847  11952   1481   -650  -1240       C  
ATOM    997  C   ASN A 324      22.044  10.292 -50.734  1.00 88.92           C  
ANISOU  997  C   ASN A 324     9815  13447  10524   1489   -687  -1158       C  
ATOM    998  O   ASN A 324      21.968  11.504 -50.900  1.00 92.35           O  
ANISOU  998  O   ASN A 324    10197  13951  10942   1439   -737  -1127       O  
ATOM    999  CB  ASN A 324      20.516   9.896 -52.677  1.00103.73           C  
ANISOU  999  CB  ASN A 324    11627  15343  12443   1389   -662  -1280       C  
ATOM   1000  CG  ASN A 324      20.285   9.136 -53.965  1.00110.82           C  
ANISOU 1000  CG  ASN A 324    12489  16276  13341   1367   -637  -1366       C  
ATOM   1001  OD1 ASN A 324      21.108   9.176 -54.882  1.00113.32           O  
ANISOU 1001  OD1 ASN A 324    12747  16691  13619   1389   -667  -1376       O  
ATOM   1002  ND2 ASN A 324      19.159   8.438 -54.043  1.00112.12           N  
ANISOU 1002  ND2 ASN A 324    12686  16366  13547   1317   -578  -1432       N  
ATOM   1003  N   LEU A 325      22.439   9.751 -49.590  1.00 72.37           N  
ANISOU 1003  N   LEU A 325     7787  11283   8427   1551   -656  -1122       N  
ATOM   1004  CA  LEU A 325      22.895  10.584 -48.488  1.00 70.60           C  
ANISOU 1004  CA  LEU A 325     7567  11083   8173   1558   -687  -1049       C  
ATOM   1005  C   LEU A 325      24.283  11.174 -48.759  1.00 78.42           C  
ANISOU 1005  C   LEU A 325     8492  12217   9085   1589   -741  -1013       C  
ATOM   1006  O   LEU A 325      25.233  10.443 -49.034  1.00 87.83           O  
ANISOU 1006  O   LEU A 325     9677  13456  10239   1666   -734  -1015       O  
ATOM   1007  CB  LEU A 325      22.930   9.771 -47.197  1.00 73.27           C  
ANISOU 1007  CB  LEU A 325     7990  11323   8526   1622   -636  -1021       C  
ATOM   1008  CG  LEU A 325      21.590   9.298 -46.645  1.00 79.96           C  
ANISOU 1008  CG  LEU A 325     8910  12025   9446   1586   -581  -1047       C  
ATOM   1009  CD1 LEU A 325      21.828   8.400 -45.455  1.00 81.43           C  
ANISOU 1009  CD1 LEU A 325     9179  12122   9637   1667   -526  -1013       C  
ATOM   1010  CD2 LEU A 325      20.711  10.484 -46.262  1.00 78.40           C  
ANISOU 1010  CD2 LEU A 325     8696  11820   9271   1499   -614  -1027       C  
ATOM   1011  N   THR A 326      24.400  12.495 -48.682  1.00 73.84           N  
ANISOU 1011  N   THR A 326     7868  11709   8480   1528   -790   -980       N  
ATOM   1012  CA  THR A 326      25.712  13.133 -48.693  1.00 72.14           C  
ANISOU 1012  CA  THR A 326     7598  11629   8184   1543   -835   -943       C  
ATOM   1013  C   THR A 326      26.456  12.768 -47.404  1.00 74.39           C  
ANISOU 1013  C   THR A 326     7917  11920   8427   1608   -820   -897       C  
ATOM   1014  O   THR A 326      25.961  13.014 -46.306  1.00 78.08           O  
ANISOU 1014  O   THR A 326     8430  12321   8917   1587   -803   -870       O  
ATOM   1015  CB  THR A 326      25.593  14.663 -48.791  1.00 61.43           C  
ANISOU 1015  CB  THR A 326     6201  10328   6811   1452   -873   -920       C  
ATOM   1016  OG1 THR A 326      24.737  15.012 -49.886  1.00 63.52           O  
ANISOU 1016  OG1 THR A 326     6438  10582   7116   1401   -879   -953       O  
ATOM   1017  CG2 THR A 326      26.960  15.291 -49.002  1.00 53.99           C  
ANISOU 1017  CG2 THR A 326     5199   9535   5781   1454   -915   -897       C  
ATOM   1018  N   VAL A 327      27.640  12.177 -47.526  1.00 73.20           N  
ANISOU 1018  N   VAL A 327     7741  11859   8212   1691   -825   -884       N  
ATOM   1019  CA  VAL A 327      28.364  11.731 -46.337  1.00 79.51           C  
ANISOU 1019  CA  VAL A 327     8564  12684   8963   1769   -805   -834       C  
ATOM   1020  C   VAL A 327      29.782  12.294 -46.212  1.00 76.53           C  
ANISOU 1020  C   VAL A 327     8113  12489   8474   1786   -849   -799       C  
ATOM   1021  O   VAL A 327      30.443  12.590 -47.207  1.00 81.01           O  
ANISOU 1021  O   VAL A 327     8617  13163   8999   1775   -886   -816       O  
ATOM   1022  CB  VAL A 327      28.419  10.191 -46.249  1.00 84.15           C  
ANISOU 1022  CB  VAL A 327     9210  13193   9570   1885   -744   -839       C  
ATOM   1023  CG1 VAL A 327      27.014   9.615 -46.195  1.00 71.80           C  
ANISOU 1023  CG1 VAL A 327     7724  11449   8108   1857   -691   -878       C  
ATOM   1024  CG2 VAL A 327      29.204   9.619 -47.431  1.00 94.90           C  
ANISOU 1024  CG2 VAL A 327    10530  14631  10897   1944   -750   -866       C  
ATOM   1025  N   ILE A 328      30.230  12.437 -44.971  1.00 70.07           N  
ANISOU 1025  N   ILE A 328     7302  11716   7606   1808   -843   -751       N  
ATOM   1026  CA  ILE A 328      31.562  12.921 -44.663  1.00 76.27           C  
ANISOU 1026  CA  ILE A 328     8015  12691   8274   1820   -877   -718       C  
ATOM   1027  C   ILE A 328      32.003  12.231 -43.387  1.00 91.97           C  
ANISOU 1027  C   ILE A 328    10026  14704  10215   1917   -843   -664       C  
ATOM   1028  O   ILE A 328      31.191  12.039 -42.483  1.00104.13           O  
ANISOU 1028  O   ILE A 328    11630  16125  11810   1914   -808   -649       O  
ATOM   1029  CB  ILE A 328      31.578  14.441 -44.435  1.00 71.83           C  
ANISOU 1029  CB  ILE A 328     7417  12194   7683   1685   -914   -720       C  
ATOM   1030  CG1 ILE A 328      31.646  15.189 -45.768  1.00 71.64           C  
ANISOU 1030  CG1 ILE A 328     7345  12214   7663   1611   -952   -757       C  
ATOM   1031  CG2 ILE A 328      32.759  14.836 -43.566  1.00 77.74           C  
ANISOU 1031  CG2 ILE A 328     8110  13118   8310   1690   -929   -683       C  
ATOM   1032  CD1 ILE A 328      30.298  15.398 -46.443  1.00 68.87           C  
ANISOU 1032  CD1 ILE A 328     7035  11711   7421   1552   -942   -791       C  
ATOM   1033  N   ASN A 329      33.279  11.854 -43.313  1.00 90.18           N  
ANISOU 1033  N   ASN A 329     9742  14639   9881   2007   -852   -631       N  
ATOM   1034  CA  ASN A 329      33.814  11.142 -42.148  1.00 96.99           C  
ANISOU 1034  CA  ASN A 329    10615  15555  10683   2121   -816   -569       C  
ATOM   1035  C   ASN A 329      32.917   9.988 -41.689  1.00 94.91           C  
ANISOU 1035  C   ASN A 329    10455  15098  10510   2208   -745   -556       C  
ATOM   1036  O   ASN A 329      32.993   9.550 -40.535  1.00 87.47           O  
ANISOU 1036  O   ASN A 329     9539  14154   9541   2279   -708   -503       O  
ATOM   1037  CB  ASN A 329      34.067  12.106 -40.978  1.00102.93           C  
ANISOU 1037  CB  ASN A 329    11330  16410  11367   2045   -835   -542       C  
ATOM   1038  CG  ASN A 329      35.361  12.899 -41.135  1.00103.57           C  
ANISOU 1038  CG  ASN A 329    11303  16734  11314   2004   -885   -539       C  
ATOM   1039  OD1 ASN A 329      35.785  13.602 -40.211  1.00102.16           O  
ANISOU 1039  OD1 ASN A 329    11083  16678  11057   1947   -896   -521       O  
ATOM   1040  ND2 ASN A 329      35.995  12.786 -42.304  1.00 96.46           N  
ANISOU 1040  ND2 ASN A 329    10356  15912  10384   2028   -912   -561       N  
ATOM   1041  N   GLY A 330      32.069   9.507 -42.599  1.00 96.88           N  
ANISOU 1041  N   GLY A 330    10759  15190  10861   2196   -723   -606       N  
ATOM   1042  CA  GLY A 330      31.145   8.425 -42.309  1.00 96.46           C  
ANISOU 1042  CA  GLY A 330    10810  14943  10899   2256   -649   -609       C  
ATOM   1043  C   GLY A 330      29.829   8.867 -41.695  1.00 95.06           C  
ANISOU 1043  C   GLY A 330    10690  14617  10810   2156   -640   -627       C  
ATOM   1044  O   GLY A 330      29.079   8.037 -41.183  1.00102.25           O  
ANISOU 1044  O   GLY A 330    11687  15378  11786   2200   -576   -622       O  
ATOM   1045  N   VAL A 331      29.543  10.168 -41.743  1.00 88.18           N  
ANISOU 1045  N   VAL A 331     9776  13786   9942   2024   -696   -646       N  
ATOM   1046  CA  VAL A 331      28.309  10.702 -41.158  1.00 90.41           C  
ANISOU 1046  CA  VAL A 331    10107  13941  10302   1928   -689   -660       C  
ATOM   1047  C   VAL A 331      27.582  11.678 -42.082  1.00 78.23           C  
ANISOU 1047  C   VAL A 331     8544  12368   8812   1801   -727   -711       C  
ATOM   1048  O   VAL A 331      28.205  12.540 -42.705  1.00 74.29           O  
ANISOU 1048  O   VAL A 331     7975  11990   8262   1748   -776   -720       O  
ATOM   1049  CB  VAL A 331      28.559  11.375 -39.787  1.00 99.57           C  
ANISOU 1049  CB  VAL A 331    11254  15167  11411   1902   -699   -611       C  
ATOM   1050  CG1 VAL A 331      29.078  10.351 -38.768  1.00 99.35           C  
ANISOU 1050  CG1 VAL A 331    11253  15157  11338   2036   -652   -552       C  
ATOM   1051  CG2 VAL A 331      29.515  12.553 -39.927  1.00104.13           C  
ANISOU 1051  CG2 VAL A 331    11741  15929  11895   1831   -758   -608       C  
ATOM   1052  N   PRO A 332      26.249  11.542 -42.155  1.00 67.87           N  
ANISOU 1052  N   PRO A 332     7291  10900   7597   1753   -701   -743       N  
ATOM   1053  CA  PRO A 332      25.319  12.227 -43.056  1.00 61.72           C  
ANISOU 1053  CA  PRO A 332     6501  10072   6877   1653   -721   -789       C  
ATOM   1054  C   PRO A 332      25.014  13.658 -42.645  1.00 63.62           C  
ANISOU 1054  C   PRO A 332     6722  10338   7113   1548   -753   -774       C  
ATOM   1055  O   PRO A 332      24.086  13.890 -41.877  1.00 76.01           O  
ANISOU 1055  O   PRO A 332     8338  11810   8731   1508   -732   -767       O  
ATOM   1056  CB  PRO A 332      24.061  11.380 -42.906  1.00 66.61           C  
ANISOU 1056  CB  PRO A 332     7198  10524   7587   1659   -667   -818       C  
ATOM   1057  CG  PRO A 332      24.079  11.071 -41.450  1.00 64.33           C  
ANISOU 1057  CG  PRO A 332     6961  10191   7293   1702   -636   -771       C  
ATOM   1058  CD  PRO A 332      25.519  10.636 -41.251  1.00 66.29           C  
ANISOU 1058  CD  PRO A 332     7176  10561   7452   1802   -640   -731       C  
ATOM   1059  N   ILE A 333      25.757  14.607 -43.196  1.00 70.72           N  
ANISOU 1059  N   ILE A 333     7555  11361   7954   1502   -796   -772       N  
ATOM   1060  CA  ILE A 333      25.688  16.000 -42.760  1.00 72.41           C  
ANISOU 1060  CA  ILE A 333     7755  11608   8148   1405   -814   -755       C  
ATOM   1061  C   ILE A 333      24.283  16.639 -42.764  1.00 68.62           C  
ANISOU 1061  C   ILE A 333     7315  11007   7749   1328   -798   -766       C  
ATOM   1062  O   ILE A 333      23.922  17.340 -41.807  1.00 65.82           O  
ANISOU 1062  O   ILE A 333     6991  10618   7402   1276   -786   -744       O  
ATOM   1063  CB  ILE A 333      26.705  16.883 -43.529  1.00 68.05           C  
ANISOU 1063  CB  ILE A 333     7130  11204   7522   1362   -854   -758       C  
ATOM   1064  CG1 ILE A 333      26.234  17.165 -44.954  1.00 70.83           C  
ANISOU 1064  CG1 ILE A 333     7456  11542   7912   1331   -869   -791       C  
ATOM   1065  CG2 ILE A 333      28.053  16.201 -43.579  1.00 74.21           C  
ANISOU 1065  CG2 ILE A 333     7865  12114   8218   1444   -870   -748       C  
ATOM   1066  CD1 ILE A 333      27.060  18.229 -45.656  1.00 68.09           C  
ANISOU 1066  CD1 ILE A 333     7049  11322   7502   1273   -901   -790       C  
ATOM   1067  N   TRP A 334      23.501  16.402 -43.818  1.00 55.55           N  
ANISOU 1067  N   TRP A 334     5657   9300   6149   1323   -796   -799       N  
ATOM   1068  CA  TRP A 334      22.154  16.974 -43.913  1.00 59.88           C  
ANISOU 1068  CA  TRP A 334     6232   9755   6764   1261   -780   -806       C  
ATOM   1069  C   TRP A 334      21.186  16.280 -42.957  1.00 64.73           C  
ANISOU 1069  C   TRP A 334     6915  10241   7438   1279   -743   -806       C  
ATOM   1070  O   TRP A 334      20.281  16.903 -42.397  1.00 63.41           O  
ANISOU 1070  O   TRP A 334     6781  10005   7308   1228   -727   -793       O  
ATOM   1071  CB  TRP A 334      21.620  16.905 -45.347  1.00 62.28           C  
ANISOU 1071  CB  TRP A 334     6499  10068   7096   1252   -789   -842       C  
ATOM   1072  CG  TRP A 334      22.391  17.763 -46.302  1.00 70.96           C  
ANISOU 1072  CG  TRP A 334     7534  11283   8145   1225   -823   -837       C  
ATOM   1073  CD1 TRP A 334      23.258  17.341 -47.271  1.00 70.00           C  
ANISOU 1073  CD1 TRP A 334     7360  11255   7984   1261   -849   -859       C  
ATOM   1074  CD2 TRP A 334      22.388  19.197 -46.366  1.00 71.66           C  
ANISOU 1074  CD2 TRP A 334     7610  11404   8214   1155   -828   -809       C  
ATOM   1075  NE1 TRP A 334      23.784  18.422 -47.938  1.00 71.06           N  
ANISOU 1075  NE1 TRP A 334     7444  11480   8074   1216   -874   -845       N  
ATOM   1076  CE2 TRP A 334      23.265  19.572 -47.404  1.00 73.05           C  
ANISOU 1076  CE2 TRP A 334     7723  11693   8338   1150   -857   -815       C  
ATOM   1077  CE3 TRP A 334      21.727  20.196 -45.649  1.00 69.59           C  
ANISOU 1077  CE3 TRP A 334     7387  11081   7972   1098   -803   -779       C  
ATOM   1078  CZ2 TRP A 334      23.497  20.906 -47.744  1.00 69.92           C  
ANISOU 1078  CZ2 TRP A 334     7308  11347   7912   1088   -859   -791       C  
ATOM   1079  CZ3 TRP A 334      21.955  21.524 -45.990  1.00 73.76           C  
ANISOU 1079  CZ3 TRP A 334     7900  11655   8472   1038   -800   -755       C  
ATOM   1080  CH2 TRP A 334      22.834  21.865 -47.024  1.00 76.56           C  
ANISOU 1080  CH2 TRP A 334     8197  12118   8776   1033   -826   -761       C  
ATOM   1081  N   ALA A 335      21.378  14.983 -42.765  1.00 58.70           N  
ANISOU 1081  N   ALA A 335     6177   9443   6682   1352   -722   -820       N  
ATOM   1082  CA  ALA A 335      20.591  14.280 -41.773  1.00 50.19           C  
ANISOU 1082  CA  ALA A 335     5170   8247   5655   1372   -681   -816       C  
ATOM   1083  C   ALA A 335      20.909  14.869 -40.400  1.00 60.71           C  
ANISOU 1083  C   ALA A 335     6523   9588   6958   1359   -682   -768       C  
ATOM   1084  O   ALA A 335      20.005  15.198 -39.629  1.00 59.28           O  
ANISOU 1084  O   ALA A 335     6383   9323   6818   1319   -664   -758       O  
ATOM   1085  CB  ALA A 335      20.895  12.809 -41.809  1.00 42.08           C  
ANISOU 1085  CB  ALA A 335     4174   7182   4633   1460   -647   -833       C  
ATOM   1086  N   LEU A 336      22.202  15.006 -40.106  1.00 61.48           N  
ANISOU 1086  N   LEU A 336     6584   9797   6978   1390   -702   -741       N  
ATOM   1087  CA  LEU A 336      22.650  15.618 -38.857  1.00 58.55           C  
ANISOU 1087  CA  LEU A 336     6217   9469   6562   1368   -704   -702       C  
ATOM   1088  C   LEU A 336      22.132  17.041 -38.732  1.00 57.00           C  
ANISOU 1088  C   LEU A 336     6018   9262   6376   1261   -712   -699       C  
ATOM   1089  O   LEU A 336      21.714  17.471 -37.664  1.00 60.10           O  
ANISOU 1089  O   LEU A 336     6446   9609   6780   1224   -695   -680       O  
ATOM   1090  CB  LEU A 336      24.180  15.627 -38.763  1.00 54.72           C  
ANISOU 1090  CB  LEU A 336     5674   9141   5975   1408   -727   -680       C  
ATOM   1091  CG  LEU A 336      24.751  16.318 -37.519  1.00 48.76           C  
ANISOU 1091  CG  LEU A 336     4908   8465   5156   1372   -729   -647       C  
ATOM   1092  CD1 LEU A 336      24.317  15.567 -36.272  1.00 51.37           C  
ANISOU 1092  CD1 LEU A 336     5292   8717   5510   1426   -694   -619       C  
ATOM   1093  CD2 LEU A 336      26.277  16.424 -37.573  1.00 44.99           C  
ANISOU 1093  CD2 LEU A 336     4358   8174   4564   1399   -755   -632       C  
ATOM   1094  N   ILE A 337      22.159  17.777 -39.830  1.00 51.79           N  
ANISOU 1094  N   ILE A 337     5321   8644   5713   1214   -733   -716       N  
ATOM   1095  CA  ILE A 337      21.737  19.160 -39.773  1.00 50.27           C  
ANISOU 1095  CA  ILE A 337     5133   8440   5526   1121   -729   -708       C  
ATOM   1096  C   ILE A 337      20.238  19.226 -39.473  1.00 50.79           C  
ANISOU 1096  C   ILE A 337     5253   8369   5675   1099   -700   -708       C  
ATOM   1097  O   ILE A 337      19.797  20.028 -38.645  1.00 43.62           O  
ANISOU 1097  O   ILE A 337     4380   7418   4778   1044   -680   -689       O  
ATOM   1098  CB  ILE A 337      22.158  19.915 -41.051  1.00 52.36           C  
ANISOU 1098  CB  ILE A 337     5347   8785   5764   1087   -750   -719       C  
ATOM   1099  CG1 ILE A 337      23.693  20.077 -41.036  1.00 57.13           C  
ANISOU 1099  CG1 ILE A 337     5900   9535   6273   1089   -775   -715       C  
ATOM   1100  CG2 ILE A 337      21.397  21.244 -41.197  1.00 42.11           C  
ANISOU 1100  CG2 ILE A 337     4069   7440   4492   1005   -729   -707       C  
ATOM   1101  CD1 ILE A 337      24.255  21.060 -42.007  1.00 53.43           C  
ANISOU 1101  CD1 ILE A 337     5386   9152   5762   1034   -791   -722       C  
ATOM   1102  N   PHE A 338      19.484  18.328 -40.100  1.00 47.03           N  
ANISOU 1102  N   PHE A 338     4786   7832   5253   1140   -695   -733       N  
ATOM   1103  CA  PHE A 338      18.042  18.255 -39.941  1.00 43.42           C  
ANISOU 1103  CA  PHE A 338     4370   7262   4867   1121   -669   -740       C  
ATOM   1104  C   PHE A 338      17.638  17.908 -38.515  1.00 53.10           C  
ANISOU 1104  C   PHE A 338     5653   8405   6115   1128   -644   -723       C  
ATOM   1105  O   PHE A 338      16.719  18.517 -37.966  1.00 56.05           O  
ANISOU 1105  O   PHE A 338     6061   8711   6524   1083   -625   -710       O  
ATOM   1106  CB  PHE A 338      17.460  17.241 -40.926  1.00 48.91           C  
ANISOU 1106  CB  PHE A 338     5054   7930   5600   1157   -665   -782       C  
ATOM   1107  CG  PHE A 338      15.999  16.917 -40.693  1.00 47.65           C  
ANISOU 1107  CG  PHE A 338     4934   7666   5506   1140   -635   -798       C  
ATOM   1108  CD1 PHE A 338      15.000  17.692 -41.261  1.00 50.95           C  
ANISOU 1108  CD1 PHE A 338     5334   8078   5947   1095   -631   -798       C  
ATOM   1109  CD2 PHE A 338      15.628  15.811 -39.934  1.00 47.97           C  
ANISOU 1109  CD2 PHE A 338     5027   7621   5579   1173   -606   -811       C  
ATOM   1110  CE1 PHE A 338      13.659  17.382 -41.059  1.00 57.17           C  
ANISOU 1110  CE1 PHE A 338     6150   8789   6785   1079   -604   -813       C  
ATOM   1111  CE2 PHE A 338      14.295  15.495 -39.731  1.00 51.62           C  
ANISOU 1111  CE2 PHE A 338     5523   7994   6095   1149   -577   -831       C  
ATOM   1112  CZ  PHE A 338      13.307  16.281 -40.289  1.00 55.23           C  
ANISOU 1112  CZ  PHE A 338     5956   8458   6571   1100   -578   -834       C  
ATOM   1113  N   TYR A 339      18.313  16.935 -37.906  1.00 53.05           N  
ANISOU 1113  N   TYR A 339     5661   8408   6088   1189   -640   -719       N  
ATOM   1114  CA  TYR A 339      17.944  16.519 -36.548  1.00 44.37           C  
ANISOU 1114  CA  TYR A 339     4615   7234   5009   1204   -614   -698       C  
ATOM   1115  C   TYR A 339      18.420  17.473 -35.456  1.00 45.20           C  
ANISOU 1115  C   TYR A 339     4721   7382   5071   1160   -617   -664       C  
ATOM   1116  O   TYR A 339      17.925  17.434 -34.328  1.00 49.87           O  
ANISOU 1116  O   TYR A 339     5355   7911   5683   1151   -596   -647       O  
ATOM   1117  CB  TYR A 339      18.374  15.082 -36.262  1.00 35.58           C  
ANISOU 1117  CB  TYR A 339     3524   6103   3891   1295   -595   -699       C  
ATOM   1118  CG  TYR A 339      17.575  14.082 -37.053  1.00 51.00           C  
ANISOU 1118  CG  TYR A 339     5502   7973   5902   1320   -570   -742       C  
ATOM   1119  CD1 TYR A 339      18.154  13.378 -38.101  1.00 49.48           C  
ANISOU 1119  CD1 TYR A 339     5282   7824   5693   1368   -573   -769       C  
ATOM   1120  CD2 TYR A 339      16.225  13.865 -36.783  1.00 57.51           C  
ANISOU 1120  CD2 TYR A 339     6374   8684   6794   1288   -541   -760       C  
ATOM   1121  CE1 TYR A 339      17.427  12.470 -38.842  1.00 47.13           C  
ANISOU 1121  CE1 TYR A 339     5007   7455   5444   1377   -543   -818       C  
ATOM   1122  CE2 TYR A 339      15.491  12.958 -37.532  1.00 60.59           C  
ANISOU 1122  CE2 TYR A 339     6783   9011   7229   1296   -513   -810       C  
ATOM   1123  CZ  TYR A 339      16.103  12.268 -38.564  1.00 53.05           C  
ANISOU 1123  CZ  TYR A 339     5802   8098   6255   1337   -512   -841       C  
ATOM   1124  OH  TYR A 339      15.391  11.360 -39.312  1.00 54.34           O  
ANISOU 1124  OH  TYR A 339     5984   8203   6459   1333   -477   -899       O  
ATOM   1125  N   LEU A 340      19.366  18.333 -35.800  1.00 44.01           N  
ANISOU 1125  N   LEU A 340     4523   7341   4857   1125   -640   -659       N  
ATOM   1126  CA  LEU A 340      19.766  19.414 -34.917  1.00 45.58           C  
ANISOU 1126  CA  LEU A 340     4721   7587   5012   1057   -635   -639       C  
ATOM   1127  C   LEU A 340      18.669  20.454 -34.902  1.00 42.61           C  
ANISOU 1127  C   LEU A 340     4380   7124   4686    981   -613   -639       C  
ATOM   1128  O   LEU A 340      18.248  20.904 -33.834  1.00 57.23           O  
ANISOU 1128  O   LEU A 340     6269   8927   6549    941   -590   -625       O  
ATOM   1129  CB  LEU A 340      21.089  20.038 -35.365  1.00 48.16           C  
ANISOU 1129  CB  LEU A 340     4987   8058   5251   1030   -658   -642       C  
ATOM   1130  CG  LEU A 340      22.340  19.545 -34.639  1.00 58.92           C  
ANISOU 1130  CG  LEU A 340     6314   9543   6529   1072   -669   -627       C  
ATOM   1131  CD1 LEU A 340      22.297  18.053 -34.398  1.00 68.15           C  
ANISOU 1131  CD1 LEU A 340     7499  10677   7717   1186   -664   -614       C  
ATOM   1132  CD2 LEU A 340      23.580  19.921 -35.403  1.00 61.09           C  
ANISOU 1132  CD2 LEU A 340     6522   9967   6722   1060   -696   -637       C  
ATOM   1133  N   LEU A 341      18.201  20.834 -36.086  1.00 42.78           N  
ANISOU 1133  N   LEU A 341     4388   7131   4737    967   -617   -651       N  
ATOM   1134  CA  LEU A 341      17.013  21.680 -36.204  1.00 47.13           C  
ANISOU 1134  CA  LEU A 341     4971   7597   5339    919   -591   -643       C  
ATOM   1135  C   LEU A 341      15.835  21.067 -35.458  1.00 41.33           C  
ANISOU 1135  C   LEU A 341     4285   6751   4668    938   -572   -642       C  
ATOM   1136  O   LEU A 341      15.209  21.719 -34.625  1.00 48.52           O  
ANISOU 1136  O   LEU A 341     5237   7601   5599    896   -545   -624       O  
ATOM   1137  CB  LEU A 341      16.626  21.857 -37.662  1.00 56.33           C  
ANISOU 1137  CB  LEU A 341     6104   8776   6523    927   -600   -654       C  
ATOM   1138  CG  LEU A 341      17.173  23.084 -38.375  1.00 66.07           C  
ANISOU 1138  CG  LEU A 341     7312  10075   7716    879   -596   -643       C  
ATOM   1139  CD1 LEU A 341      16.399  23.305 -39.684  1.00 58.62           C  
ANISOU 1139  CD1 LEU A 341     6344   9127   6803    893   -595   -643       C  
ATOM   1140  CD2 LEU A 341      17.072  24.299 -37.470  1.00 66.13           C  
ANISOU 1140  CD2 LEU A 341     7365  10046   7713    807   -555   -619       C  
ATOM   1141  N   ARG A 342      15.561  19.803 -35.769  1.00 35.18           N  
ANISOU 1141  N   ARG A 342     3504   5945   3917    999   -581   -662       N  
ATOM   1142  CA  ARG A 342      14.488  19.022 -35.154  1.00 40.90           C  
ANISOU 1142  CA  ARG A 342     4274   6567   4699   1019   -560   -669       C  
ATOM   1143  C   ARG A 342      14.598  18.933 -33.632  1.00 53.12           C  
ANISOU 1143  C   ARG A 342     5863   8078   6242   1016   -545   -646       C  
ATOM   1144  O   ARG A 342      13.647  18.526 -32.947  1.00 44.33           O  
ANISOU 1144  O   ARG A 342     4794   6874   5175   1019   -524   -645       O  
ATOM   1145  CB  ARG A 342      14.487  17.609 -35.746  1.00 38.10           C  
ANISOU 1145  CB  ARG A 342     3914   6199   4362   1081   -562   -701       C  
ATOM   1146  CG  ARG A 342      13.344  16.704 -35.279  1.00 34.67           C  
ANISOU 1146  CG  ARG A 342     3529   5656   3986   1094   -532   -718       C  
ATOM   1147  CD  ARG A 342      11.943  17.171 -35.727  1.00 31.97           C  
ANISOU 1147  CD  ARG A 342     3188   5269   3689   1049   -520   -732       C  
ATOM   1148  NE  ARG A 342      11.093  17.202 -34.537  1.00 55.52           N  
ANISOU 1148  NE  ARG A 342     6224   8165   6705   1030   -496   -716       N  
ATOM   1149  CZ  ARG A 342      10.585  16.120 -33.967  1.00 42.78           C  
ANISOU 1149  CZ  ARG A 342     4654   6474   5126   1052   -471   -734       C  
ATOM   1150  NH1 ARG A 342      10.791  14.929 -34.502  1.00 52.53           N  
ANISOU 1150  NH1 ARG A 342     5892   7700   6366   1091   -459   -770       N  
ATOM   1151  NH2 ARG A 342       9.861  16.232 -32.886  1.00 44.10           N  
ANISOU 1151  NH2 ARG A 342     4865   6570   5320   1033   -452   -717       N  
ATOM   1152  N   ALA A 343      15.765  19.286 -33.096  1.00 48.57           N  
ANISOU 1152  N   ALA A 343     5267   7584   5602   1009   -555   -629       N  
ATOM   1153  CA  ALA A 343      15.937  19.252 -31.656  1.00 40.09           C  
ANISOU 1153  CA  ALA A 343     4221   6500   4512   1004   -541   -606       C  
ATOM   1154  C   ALA A 343      15.881  20.661 -31.064  1.00 43.10           C  
ANISOU 1154  C   ALA A 343     4612   6889   4874    916   -526   -594       C  
ATOM   1155  O   ALA A 343      15.940  20.833 -29.849  1.00 49.03           O  
ANISOU 1155  O   ALA A 343     5385   7635   5611    894   -511   -580       O  
ATOM   1156  CB  ALA A 343      17.234  18.564 -31.307  1.00 41.12           C  
ANISOU 1156  CB  ALA A 343     4320   6729   4576   1061   -555   -595       C  
ATOM   1157  N   GLY A 344      15.740  21.660 -31.932  1.00 41.46           N  
ANISOU 1157  N   GLY A 344     4394   6691   4668    868   -523   -600       N  
ATOM   1158  CA  GLY A 344      15.753  23.052 -31.518  1.00 38.41           C  
ANISOU 1158  CA  GLY A 344     4026   6306   4262    782   -494   -591       C  
ATOM   1159  C   GLY A 344      17.166  23.613 -31.400  1.00 54.68           C  
ANISOU 1159  C   GLY A 344     6049   8490   6236    739   -500   -597       C  
ATOM   1160  O   GLY A 344      17.367  24.716 -30.882  1.00 57.45           O  
ANISOU 1160  O   GLY A 344     6419   8853   6557    656   -468   -597       O  
ATOM   1161  N   LEU A 345      18.150  22.857 -31.889  1.00 53.25           N  
ANISOU 1161  N   LEU A 345     5817   8406   6010    791   -536   -605       N  
ATOM   1162  CA  LEU A 345      19.550  23.217 -31.706  1.00 51.00           C  
ANISOU 1162  CA  LEU A 345     5486   8263   5630    757   -545   -612       C  
ATOM   1163  C   LEU A 345      20.116  23.932 -32.926  1.00 46.68           C  
ANISOU 1163  C   LEU A 345     4905   7779   5052    722   -552   -625       C  
ATOM   1164  O   LEU A 345      20.944  23.388 -33.639  1.00 53.92           O  
ANISOU 1164  O   LEU A 345     5772   8788   5930    768   -586   -633       O  
ATOM   1165  CB  LEU A 345      20.382  21.971 -31.383  1.00 52.81           C  
ANISOU 1165  CB  LEU A 345     5674   8577   5814    844   -575   -604       C  
ATOM   1166  CG  LEU A 345      19.989  21.133 -30.156  1.00 50.56           C  
ANISOU 1166  CG  LEU A 345     5417   8244   5548    893   -565   -584       C  
ATOM   1167  CD1 LEU A 345      20.855  19.895 -30.088  1.00 38.30           C  
ANISOU 1167  CD1 LEU A 345     3826   6777   3949    997   -586   -568       C  
ATOM   1168  CD2 LEU A 345      20.050  21.917 -28.818  1.00 33.11           C  
ANISOU 1168  CD2 LEU A 345     3221   6057   3302    814   -539   -579       C  
ATOM   1169  N   ILE A 346      19.665  25.161 -33.152  1.00 55.23           N  
ANISOU 1169  N   ILE A 346     6022   8811   6152    644   -515   -626       N  
ATOM   1170  CA  ILE A 346      20.034  25.922 -34.338  1.00 54.47           C  
ANISOU 1170  CA  ILE A 346     5906   8754   6037    612   -510   -633       C  
ATOM   1171  C   ILE A 346      21.505  26.350 -34.295  1.00 59.62           C  
ANISOU 1171  C   ILE A 346     6512   9554   6587    555   -516   -652       C  
ATOM   1172  O   ILE A 346      22.183  26.379 -35.315  1.00 59.05           O  
ANISOU 1172  O   ILE A 346     6396   9560   6480    564   -539   -661       O  
ATOM   1173  CB  ILE A 346      19.121  27.151 -34.499  1.00 59.04           C  
ANISOU 1173  CB  ILE A 346     6544   9230   6659    551   -453   -619       C  
ATOM   1174  CG1 ILE A 346      17.685  26.783 -34.127  1.00 76.85           C  
ANISOU 1174  CG1 ILE A 346     8844  11355   8999    594   -442   -599       C  
ATOM   1175  CG2 ILE A 346      19.152  27.662 -35.918  1.00 59.80           C  
ANISOU 1175  CG2 ILE A 346     6622   9342   6758    555   -451   -613       C  
ATOM   1176  CD1 ILE A 346      16.684  27.891 -34.373  1.00 80.35           C  
ANISOU 1176  CD1 ILE A 346     9342  11701   9487    560   -385   -576       C  
ATOM   1177  N   LYS A 347      21.993  26.666 -33.103  1.00 60.23           N  
ANISOU 1177  N   LYS A 347     6594   9681   6610    493   -495   -662       N  
ATOM   1178  CA  LYS A 347      23.387  27.050 -32.910  1.00 68.61           C  
ANISOU 1178  CA  LYS A 347     7604  10903   7561    429   -496   -687       C  
ATOM   1179  C   LYS A 347      24.314  25.956 -33.439  1.00 71.42           C  
ANISOU 1179  C   LYS A 347     7883  11386   7868    519   -558   -685       C  
ATOM   1180  O   LYS A 347      25.253  26.221 -34.193  1.00 67.92           O  
ANISOU 1180  O   LYS A 347     7392  11054   7361    497   -573   -701       O  
ATOM   1181  CB  LYS A 347      23.651  27.297 -31.419  1.00 67.89           C  
ANISOU 1181  CB  LYS A 347     7520  10856   7419    363   -468   -697       C  
ATOM   1182  CG  LYS A 347      25.049  27.777 -31.083  1.00 77.57           C  
ANISOU 1182  CG  LYS A 347     8689  12267   8518    278   -462   -729       C  
ATOM   1183  CD  LYS A 347      25.248  27.901 -29.567  1.00 77.58           C  
ANISOU 1183  CD  LYS A 347     8687  12325   8465    219   -436   -741       C  
ATOM   1184  CE  LYS A 347      26.656  28.399 -29.238  1.00 89.63           C  
ANISOU 1184  CE  LYS A 347    10144  14061   9850    122   -426   -780       C  
ATOM   1185  NZ  LYS A 347      27.028  28.278 -27.788  1.00 96.19           N  
ANISOU 1185  NZ  LYS A 347    10943  15000  10606     83   -414   -789       N  
ATOM   1186  N   GLU A 348      24.022  24.723 -33.045  1.00 69.24           N  
ANISOU 1186  N   GLU A 348     7600  11085   7621    624   -588   -665       N  
ATOM   1187  CA  GLU A 348      24.818  23.569 -33.425  1.00 63.52           C  
ANISOU 1187  CA  GLU A 348     6816  10463   6856    726   -634   -658       C  
ATOM   1188  C   GLU A 348      24.677  23.243 -34.916  1.00 71.53           C  
ANISOU 1188  C   GLU A 348     7817  11449   7912    780   -661   -662       C  
ATOM   1189  O   GLU A 348      25.681  23.025 -35.613  1.00 73.48           O  
ANISOU 1189  O   GLU A 348     8004  11818   8096    805   -691   -671       O  
ATOM   1190  CB  GLU A 348      24.436  22.368 -32.559  1.00 56.31           C  
ANISOU 1190  CB  GLU A 348     5917   9505   5971    823   -641   -632       C  
ATOM   1191  CG  GLU A 348      24.910  22.462 -31.094  1.00 61.77           C  
ANISOU 1191  CG  GLU A 348     6595  10283   6593    793   -625   -622       C  
ATOM   1192  CD  GLU A 348      24.028  23.344 -30.206  1.00 71.87           C  
ANISOU 1192  CD  GLU A 348     7935  11458   7915    699   -582   -629       C  
ATOM   1193  OE1 GLU A 348      23.092  24.001 -30.722  1.00 72.58           O  
ANISOU 1193  OE1 GLU A 348     8079  11416   8082    653   -562   -637       O  
ATOM   1194  OE2 GLU A 348      24.276  23.373 -28.978  1.00 69.68           O  
ANISOU 1194  OE2 GLU A 348     7648  11239   7588    674   -567   -623       O  
ATOM   1195  N   ALA A 349      23.439  23.219 -35.407  1.00 63.80           N  
ANISOU 1195  N   ALA A 349     6887  10320   7033    796   -651   -658       N  
ATOM   1196  CA  ALA A 349      23.172  22.959 -36.829  1.00 61.51           C  
ANISOU 1196  CA  ALA A 349     6582  10006   6784    838   -672   -666       C  
ATOM   1197  C   ALA A 349      23.966  23.899 -37.724  1.00 55.38           C  
ANISOU 1197  C   ALA A 349     5767   9324   5952    776   -676   -679       C  
ATOM   1198  O   ALA A 349      24.475  23.501 -38.764  1.00 63.60           O  
ANISOU 1198  O   ALA A 349     6762  10430   6975    820   -708   -688       O  
ATOM   1199  CB  ALA A 349      21.673  23.096 -37.123  1.00 51.80           C  
ANISOU 1199  CB  ALA A 349     5406   8623   5655    839   -650   -659       C  
ATOM   1200  N   LEU A 350      24.053  25.154 -37.304  1.00 56.99           N  
ANISOU 1200  N   LEU A 350     5996   9529   6129    671   -637   -682       N  
ATOM   1201  CA  LEU A 350      24.793  26.175 -38.022  1.00 63.64           C  
ANISOU 1201  CA  LEU A 350     6815  10450   6915    595   -625   -696       C  
ATOM   1202  C   LEU A 350      26.288  25.855 -38.013  1.00 57.41           C  
ANISOU 1202  C   LEU A 350     5953   9843   6019    597   -659   -713       C  
ATOM   1203  O   LEU A 350      26.962  26.016 -39.015  1.00 55.50           O  
ANISOU 1203  O   LEU A 350     5667   9684   5738    593   -679   -724       O  
ATOM   1204  CB  LEU A 350      24.534  27.541 -37.380  1.00 68.33           C  
ANISOU 1204  CB  LEU A 350     7468  10992   7504    477   -558   -698       C  
ATOM   1205  CG  LEU A 350      25.085  28.782 -38.079  1.00 73.97           C  
ANISOU 1205  CG  LEU A 350     8185  11749   8173    383   -520   -711       C  
ATOM   1206  CD1 LEU A 350      24.487  28.917 -39.472  1.00 75.51           C  
ANISOU 1206  CD1 LEU A 350     8381  11883   8425    430   -525   -692       C  
ATOM   1207  CD2 LEU A 350      24.798  30.016 -37.235  1.00 73.08           C  
ANISOU 1207  CD2 LEU A 350     8143  11568   8055    267   -440   -717       C  
ATOM   1208  N   GLN A 351      26.799  25.394 -36.879  1.00 55.28           N  
ANISOU 1208  N   GLN A 351     5665   9645   5695    605   -665   -713       N  
ATOM   1209  CA  GLN A 351      28.215  25.072 -36.769  1.00 61.51           C  
ANISOU 1209  CA  GLN A 351     6376  10627   6369    614   -695   -725       C  
ATOM   1210  C   GLN A 351      28.588  23.963 -37.742  1.00 72.69           C  
ANISOU 1210  C   GLN A 351     7742  12090   7787    734   -746   -716       C  
ATOM   1211  O   GLN A 351      29.625  24.026 -38.401  1.00 76.43           O  
ANISOU 1211  O   GLN A 351     8153  12702   8184    730   -772   -729       O  
ATOM   1212  CB  GLN A 351      28.575  24.660 -35.342  1.00 51.10           C  
ANISOU 1212  CB  GLN A 351     5041   9380   4993    623   -690   -716       C  
ATOM   1213  CG  GLN A 351      28.288  25.737 -34.323  1.00 59.44           C  
ANISOU 1213  CG  GLN A 351     6142  10405   6039    497   -636   -732       C  
ATOM   1214  CD  GLN A 351      28.559  25.292 -32.912  1.00 61.93           C  
ANISOU 1214  CD  GLN A 351     6437  10793   6300    509   -632   -722       C  
ATOM   1215  OE1 GLN A 351      28.775  24.108 -32.652  1.00 67.97           O  
ANISOU 1215  OE1 GLN A 351     7169  11603   7053    629   -665   -693       O  
ATOM   1216  NE2 GLN A 351      28.547  26.241 -31.987  1.00 65.81           N  
ANISOU 1216  NE2 GLN A 351     6951  11296   6756    387   -585   -745       N  
ATOM   1217  N   VAL A 352      27.734  22.950 -37.831  1.00 68.16           N  
ANISOU 1217  N   VAL A 352     7199  11400   7299    835   -757   -698       N  
ATOM   1218  CA  VAL A 352      27.997  21.825 -38.711  1.00 60.81           C  
ANISOU 1218  CA  VAL A 352     6233  10495   6376    948   -794   -695       C  
ATOM   1219  C   VAL A 352      28.052  22.290 -40.157  1.00 65.57           C  
ANISOU 1219  C   VAL A 352     6814  11106   6993    924   -810   -713       C  
ATOM   1220  O   VAL A 352      28.923  21.877 -40.909  1.00 72.79           O  
ANISOU 1220  O   VAL A 352     7671  12130   7856    969   -843   -721       O  
ATOM   1221  CB  VAL A 352      26.940  20.726 -38.557  1.00 54.27           C  
ANISOU 1221  CB  VAL A 352     5455   9521   5644   1041   -788   -681       C  
ATOM   1222  CG1 VAL A 352      27.088  19.705 -39.662  1.00 55.71           C  
ANISOU 1222  CG1 VAL A 352     5612   9709   5846   1137   -813   -689       C  
ATOM   1223  CG2 VAL A 352      27.047  20.060 -37.185  1.00 53.92           C  
ANISOU 1223  CG2 VAL A 352     5425   9484   5577   1089   -774   -657       C  
ATOM   1224  N   LEU A 353      27.126  23.160 -40.544  1.00 63.63           N  
ANISOU 1224  N   LEU A 353     6613  10751   6813    859   -785   -716       N  
ATOM   1225  CA  LEU A 353      27.152  23.730 -41.883  1.00 59.84           C  
ANISOU 1225  CA  LEU A 353     6111  10285   6341    832   -793   -727       C  
ATOM   1226  C   LEU A 353      28.436  24.537 -42.122  1.00 75.41           C  
ANISOU 1226  C   LEU A 353     8033  12409   8209    759   -798   -741       C  
ATOM   1227  O   LEU A 353      29.073  24.406 -43.171  1.00 70.60           O  
ANISOU 1227  O   LEU A 353     7371  11885   7566    782   -829   -751       O  
ATOM   1228  CB  LEU A 353      25.923  24.602 -42.136  1.00 53.37           C  
ANISOU 1228  CB  LEU A 353     5349   9329   5600    781   -754   -716       C  
ATOM   1229  CG  LEU A 353      25.580  24.839 -43.613  1.00 62.10           C  
ANISOU 1229  CG  LEU A 353     6434  10424   6739    795   -763   -717       C  
ATOM   1230  CD1 LEU A 353      25.307  23.523 -44.331  1.00 66.00           C  
ANISOU 1230  CD1 LEU A 353     6897  10911   7271    897   -802   -728       C  
ATOM   1231  CD2 LEU A 353      24.398  25.781 -43.788  1.00 60.86           C  
ANISOU 1231  CD2 LEU A 353     6330  10148   6646    753   -716   -696       C  
ATOM   1232  N   VAL A 354      28.820  25.365 -41.152  1.00 76.86           N  
ANISOU 1232  N   VAL A 354     8233  12631   8338    665   -765   -746       N  
ATOM   1233  CA  VAL A 354      30.028  26.179 -41.286  1.00 68.32           C  
ANISOU 1233  CA  VAL A 354     7108  11701   7150    576   -760   -769       C  
ATOM   1234  C   VAL A 354      31.258  25.306 -41.494  1.00 78.82           C  
ANISOU 1234  C   VAL A 354     8351  13206   8390    644   -813   -775       C  
ATOM   1235  O   VAL A 354      32.068  25.552 -42.392  1.00 86.23           O  
ANISOU 1235  O   VAL A 354     9239  14254   9272    626   -834   -790       O  
ATOM   1236  CB  VAL A 354      30.265  27.064 -40.055  1.00 65.26           C  
ANISOU 1236  CB  VAL A 354     6748  11338   6709    460   -710   -782       C  
ATOM   1237  CG1 VAL A 354      31.644  27.702 -40.122  1.00 69.80           C  
ANISOU 1237  CG1 VAL A 354     7265  12100   7155    367   -707   -815       C  
ATOM   1238  CG2 VAL A 354      29.205  28.127 -39.955  1.00 68.26           C  
ANISOU 1238  CG2 VAL A 354     7216  11556   7164    381   -646   -777       C  
ATOM   1239  N   GLU A 355      31.389  24.280 -40.660  1.00 74.65           N  
ANISOU 1239  N   GLU A 355     7809  12708   7848    728   -831   -760       N  
ATOM   1240  CA  GLU A 355      32.538  23.383 -40.714  1.00 69.47           C  
ANISOU 1240  CA  GLU A 355     7074  12221   7101    811   -872   -756       C  
ATOM   1241  C   GLU A 355      32.771  22.745 -42.089  1.00 82.64           C  
ANISOU 1241  C   GLU A 355     8705  13909   8785    895   -912   -758       C  
ATOM   1242  O   GLU A 355      33.900  22.711 -42.574  1.00 89.90           O  
ANISOU 1242  O   GLU A 355     9553  14993   9612    901   -940   -768       O  
ATOM   1243  CB  GLU A 355      32.422  22.296 -39.645  1.00 66.72           C  
ANISOU 1243  CB  GLU A 355     6732  11866   6753    911   -873   -727       C  
ATOM   1244  CG  GLU A 355      33.511  21.236 -39.748  1.00 79.37           C  
ANISOU 1244  CG  GLU A 355     8260  13628   8269   1028   -907   -710       C  
ATOM   1245  CD  GLU A 355      34.893  21.763 -39.374  1.00 80.42           C  
ANISOU 1245  CD  GLU A 355     8309  13999   8248    967   -916   -721       C  
ATOM   1246  OE1 GLU A 355      35.058  22.251 -38.238  1.00 83.72           O  
ANISOU 1246  OE1 GLU A 355     8723  14478   8610    896   -892   -723       O  
ATOM   1247  OE2 GLU A 355      35.814  21.673 -40.210  1.00 78.09           O  
ANISOU 1247  OE2 GLU A 355     7948  13839   7883    988   -947   -731       O  
ATOM   1248  N   ASN A 356      31.704  22.244 -42.709  1.00 83.86           N  
ANISOU 1248  N   ASN A 356     8905  13906   9053    954   -913   -752       N  
ATOM   1249  CA  ASN A 356      31.812  21.526 -43.977  1.00 79.48           C  
ANISOU 1249  CA  ASN A 356     8318  13360   8522   1036   -946   -759       C  
ATOM   1250  C   ASN A 356      31.668  22.422 -45.197  1.00 90.08           C  
ANISOU 1250  C   ASN A 356     9649  14693   9883    967   -951   -777       C  
ATOM   1251  O   ASN A 356      31.539  21.928 -46.317  1.00 99.10           O  
ANISOU 1251  O   ASN A 356    10769  15825  11058   1023   -974   -785       O  
ATOM   1252  CB  ASN A 356      30.779  20.408 -44.056  1.00 75.56           C  
ANISOU 1252  CB  ASN A 356     7867  12714   8126   1134   -940   -752       C  
ATOM   1253  CG  ASN A 356      30.922  19.399 -42.927  1.00 91.97           C  
ANISOU 1253  CG  ASN A 356     9962  14793  10190   1220   -929   -728       C  
ATOM   1254  OD1 ASN A 356      31.934  18.704 -42.822  1.00 97.47           O  
ANISOU 1254  OD1 ASN A 356    10612  15615  10809   1297   -945   -716       O  
ATOM   1255  ND2 ASN A 356      29.897  19.298 -42.090  1.00102.70           N  
ANISOU 1255  ND2 ASN A 356    11387  16013  11619   1214   -898   -717       N  
ATOM   1256  N   LYS A 357      31.690  23.733 -44.977  1.00 96.78           N  
ANISOU 1256  N   LYS A 357    10516  15547  10708    846   -921   -782       N  
ATOM   1257  CA  LYS A 357      31.357  24.691 -46.025  1.00108.26           C  
ANISOU 1257  CA  LYS A 357    11974  16979  12180    776   -909   -789       C  
ATOM   1258  C   LYS A 357      31.923  24.253 -47.372  1.00113.92           C  
ANISOU 1258  C   LYS A 357    12626  17786  12874    821   -952   -801       C  
ATOM   1259  O   LYS A 357      31.299  24.457 -48.414  1.00115.91           O  
ANISOU 1259  O   LYS A 357    12884  17974  13180    816   -948   -798       O  
ATOM   1260  CB  LYS A 357      31.878  26.083 -45.663  1.00109.52           C  
ANISOU 1260  CB  LYS A 357    12148  17190  12274    638   -867   -799       C  
ATOM   1261  CG  LYS A 357      31.951  27.043 -46.839  1.00110.77           C  
ANISOU 1261  CG  LYS A 357    12307  17346  12434    571   -848   -803       C  
ATOM   1262  N   ALA A 358      33.107  23.651 -47.343  1.00111.05           N  
ANISOU 1262  N   ALA A 358    12195  17574  12424    869   -990   -810       N  
ATOM   1263  CA  ALA A 358      33.959  23.579 -48.525  1.00108.83           C  
ANISOU 1263  CA  ALA A 358    11847  17398  12103    899  -1030   -824       C  
ATOM   1264  C   ALA A 358      33.746  22.271 -49.280  1.00110.42           C  
ANISOU 1264  C   ALA A 358    12035  17570  12351   1026  -1050   -827       C  
ATOM   1265  O   ALA A 358      33.897  22.216 -50.500  1.00109.44           O  
ANISOU 1265  O   ALA A 358    11886  17461  12234   1044  -1048   -841       O  
ATOM   1266  CB  ALA A 358      35.421  23.737 -48.134  1.00105.65           C  
ANISOU 1266  CB  ALA A 358    11380  17197  11566    863  -1042   -836       C  
ATOM   1267  N   ASN A 359      33.393  21.221 -48.546  1.00112.80           N  
ANISOU 1267  N   ASN A 359    12356  17821  12681   1111  -1058   -816       N  
ATOM   1268  CA  ASN A 359      33.100  19.927 -49.151  1.00115.36           C  
ANISOU 1268  CA  ASN A 359    12683  18090  13059   1226  -1066   -823       C  
ATOM   1269  C   ASN A 359      31.905  19.991 -50.096  1.00119.05           C  
ANISOU 1269  C   ASN A 359    13177  18428  13628   1214  -1058   -838       C  
ATOM   1270  O   ASN A 359      31.417  18.963 -50.566  1.00121.99           O  
ANISOU 1270  O   ASN A 359    13556  18740  14055   1289  -1061   -853       O  
ATOM   1271  CB  ASN A 359      32.859  18.872 -48.070  1.00112.49           C  
ANISOU 1271  CB  ASN A 359    12360  17665  12716   1308  -1048   -805       C  
ATOM   1272  CG  ASN A 359      34.024  18.749 -47.107  1.00114.49           C  
ANISOU 1272  CG  ASN A 359    12578  18063  12859   1331  -1054   -784       C  
ATOM   1273  OD1 ASN A 359      35.185  18.782 -47.512  1.00117.43           O  
ANISOU 1273  OD1 ASN A 359    12881  18600  13137   1344  -1083   -787       O  
ATOM   1274  ND2 ASN A 359      33.717  18.604 -45.823  1.00113.19           N  
ANISOU 1274  ND2 ASN A 359    12455  17850  12701   1338  -1026   -761       N  
ATOM   1275  N   ILE A 360      31.437  21.205 -50.370  1.00116.72           N  
ANISOU 1275  N   ILE A 360    12894  18101  13351   1119  -1045   -832       N  
ATOM   1276  CA  ILE A 360      30.041  21.426 -50.727  1.00112.72           C  
ANISOU 1276  CA  ILE A 360    12427  17458  12942   1102  -1024   -830       C  
ATOM   1277  C   ILE A 360      29.883  21.637 -52.229  1.00110.26           C  
ANISOU 1277  C   ILE A 360    12081  17170  12644   1099  -1026   -845       C  
ATOM   1278  O   ILE A 360      30.272  20.787 -53.029  1.00108.95           O  
ANISOU 1278  O   ILE A 360    11886  17044  12466   1158  -1033   -871       O  
ATOM   1279  CB  ILE A 360      29.453  22.639 -49.983  1.00109.94           C  
ANISOU 1279  CB  ILE A 360    12130  17034  12609   1011   -983   -806       C  
ATOM   1280  CG1 ILE A 360      30.179  23.921 -50.397  1.00110.91           C  
ANISOU 1280  CG1 ILE A 360    12228  17244  12668    924   -978   -801       C  
ATOM   1281  CG2 ILE A 360      29.540  22.434 -48.478  1.00108.55           C  
ANISOU 1281  CG2 ILE A 360    11996  16827  12419   1008   -964   -796       C  
ATOM   1282  CD1 ILE A 360      29.282  25.138 -50.455  1.00109.84           C  
ANISOU 1282  CD1 ILE A 360    12143  17013  12577    850   -929   -777       C  
ATOM   1283  N   SER A 366      25.149  29.211 -51.467  1.00100.75           N  
ANISOU 1283  N   SER A 366    11180  15480  11619    730   -701   -627       N  
ATOM   1284  CA  SER A 366      25.077  29.833 -50.150  1.00104.67           C  
ANISOU 1284  CA  SER A 366    11756  15896  12116    665   -648   -620       C  
ATOM   1285  C   SER A 366      23.650  29.819 -49.611  1.00103.62           C  
ANISOU 1285  C   SER A 366    11677  15635  12059    696   -614   -592       C  
ATOM   1286  O   SER A 366      23.088  30.865 -49.287  1.00100.06           O  
ANISOU 1286  O   SER A 366    11292  15099  11626    659   -541   -555       O  
ATOM   1287  CB  SER A 366      25.604  31.268 -50.205  1.00108.98           C  
ANISOU 1287  CB  SER A 366    12346  16442  12618    574   -578   -601       C  
ATOM   1288  OG  SER A 366      27.017  31.297 -50.111  1.00111.67           O  
ANISOU 1288  OG  SER A 366    12656  16897  12877    515   -602   -640       O  
ATOM   1289  N   PHE A 367      23.069  28.627 -49.519  1.00101.61           N  
ANISOU 1289  N   PHE A 367    11395  15366  11847    764   -661   -610       N  
ATOM   1290  CA  PHE A 367      22.043  28.350 -48.521  1.00 88.57           C  
ANISOU 1290  CA  PHE A 367     9797  13605  10252    778   -640   -602       C  
ATOM   1291  C   PHE A 367      22.558  28.617 -47.111  1.00 84.07           C  
ANISOU 1291  C   PHE A 367     9284  12999   9660    714   -616   -612       C  
ATOM   1292  O   PHE A 367      21.778  28.859 -46.190  1.00 85.44           O  
ANISOU 1292  O   PHE A 367     9517  13073   9873    703   -579   -597       O  
ATOM   1293  CB  PHE A 367      21.558  26.904 -48.638  1.00 88.34           C  
ANISOU 1293  CB  PHE A 367     9729  13576  10260    850   -693   -633       C  
ATOM   1294  CG  PHE A 367      20.686  26.463 -47.498  1.00 93.48           C  
ANISOU 1294  CG  PHE A 367    10433  14124  10962    860   -677   -633       C  
ATOM   1295  CD1 PHE A 367      19.328  26.733 -47.502  1.00 94.89           C  
ANISOU 1295  CD1 PHE A 367    10639  14222  11194    876   -642   -604       C  
ATOM   1296  CD2 PHE A 367      21.224  25.777 -46.422  1.00 90.22           C  
ANISOU 1296  CD2 PHE A 367    10040  13702  10538    856   -696   -657       C  
ATOM   1297  CE1 PHE A 367      18.523  26.329 -46.454  1.00 93.06           C  
ANISOU 1297  CE1 PHE A 367    10455  13898  11007    882   -628   -605       C  
ATOM   1298  CE2 PHE A 367      20.424  25.370 -45.371  1.00 84.72           C  
ANISOU 1298  CE2 PHE A 367     9393  12910   9888    865   -681   -655       C  
ATOM   1299  CZ  PHE A 367      19.072  25.646 -45.387  1.00 85.87           C  
ANISOU 1299  CZ  PHE A 367     9568  12971  10090    874   -648   -632       C  
ATOM   1300  N   LEU A 368      23.877  28.572 -46.950  1.00 80.72           N  
ANISOU 1300  N   LEU A 368     8836  12669   9166    671   -636   -639       N  
ATOM   1301  CA  LEU A 368      24.503  28.874 -45.668  1.00 79.37           C  
ANISOU 1301  CA  LEU A 368     8703  12499   8957    605   -616   -655       C  
ATOM   1302  C   LEU A 368      24.351  30.349 -45.314  1.00 81.55           C  
ANISOU 1302  C   LEU A 368     9050  12712   9225    513   -531   -634       C  
ATOM   1303  O   LEU A 368      24.273  30.712 -44.141  1.00 81.11           O  
ANISOU 1303  O   LEU A 368     9048  12603   9166    458   -492   -638       O  
ATOM   1304  CB  LEU A 368      25.983  28.488 -45.690  1.00 76.60           C  
ANISOU 1304  CB  LEU A 368     8291  12294   8520    589   -662   -689       C  
ATOM   1305  CG  LEU A 368      26.819  28.936 -44.490  1.00 85.97           C  
ANISOU 1305  CG  LEU A 368     9495  13534   9636    504   -640   -710       C  
ATOM   1306  CD1 LEU A 368      26.105  28.611 -43.187  1.00 81.93           C  
ANISOU 1306  CD1 LEU A 368     9033  12937   9161    507   -623   -706       C  
ATOM   1307  CD2 LEU A 368      28.197  28.294 -44.525  1.00 94.19           C  
ANISOU 1307  CD2 LEU A 368    10458  14740  10591    522   -698   -740       C  
ATOM   1308  N   THR A 369      24.311  31.197 -46.338  1.00 86.22           N  
ANISOU 1308  N   THR A 369     9643  13305   9812    499   -497   -610       N  
ATOM   1309  CA  THR A 369      24.107  32.627 -46.141  1.00 92.02           C  
ANISOU 1309  CA  THR A 369    10457  13964  10542    420   -399   -584       C  
ATOM   1310  C   THR A 369      22.733  32.910 -45.541  1.00 92.56           C  
ANISOU 1310  C   THR A 369    10594  13889  10685    447   -349   -546       C  
ATOM   1311  O   THR A 369      22.601  33.720 -44.623  1.00 89.02           O  
ANISOU 1311  O   THR A 369    10224  13363  10237    377   -279   -543       O  
ATOM   1312  CB  THR A 369      24.250  33.405 -47.462  1.00 96.19           C  
ANISOU 1312  CB  THR A 369    10975  14521  11053    417   -367   -555       C  
ATOM   1313  OG1 THR A 369      25.602  33.316 -47.928  1.00 97.20           O  
ANISOU 1313  OG1 THR A 369    11044  14785  11104    376   -407   -594       O  
ATOM   1314  CG2 THR A 369      23.882  34.867 -47.262  1.00 94.65           C  
ANISOU 1314  CG2 THR A 369    10877  14224  10860    347   -248   -521       C  
ATOM   1315  N   TYR A 370      21.714  32.238 -46.066  1.00 91.16           N  
ANISOU 1315  N   TYR A 370    10387  13684  10566    544   -383   -521       N  
ATOM   1316  CA  TYR A 370      20.353  32.400 -45.570  1.00 96.59           C  
ANISOU 1316  CA  TYR A 370    11129  14253  11319    578   -342   -485       C  
ATOM   1317  C   TYR A 370      20.185  31.753 -44.199  1.00 98.51           C  
ANISOU 1317  C   TYR A 370    11397  14451  11581    565   -363   -514       C  
ATOM   1318  O   TYR A 370      19.541  32.314 -43.312  1.00105.25           O  
ANISOU 1318  O   TYR A 370    12322  15205  12465    538   -305   -495       O  
ATOM   1319  CB  TYR A 370      19.348  31.804 -46.558  1.00102.09           C  
ANISOU 1319  CB  TYR A 370    11774  14956  12060    678   -374   -458       C  
ATOM   1320  CG  TYR A 370      17.907  31.925 -46.114  1.00111.54           C  
ANISOU 1320  CG  TYR A 370    13017  16047  13316    715   -333   -421       C  
ATOM   1321  CD1 TYR A 370      17.276  33.161 -46.067  1.00111.97           C  
ANISOU 1321  CD1 TYR A 370    13142  16020  13382    704   -239   -363       C  
ATOM   1322  CD2 TYR A 370      17.178  30.803 -45.742  1.00114.24           C  
ANISOU 1322  CD2 TYR A 370    13336  16372  13700    763   -383   -441       C  
ATOM   1323  CE1 TYR A 370      15.960  33.277 -45.662  1.00108.97           C  
ANISOU 1323  CE1 TYR A 370    12801  15554  13050    745   -201   -326       C  
ATOM   1324  CE2 TYR A 370      15.862  30.909 -45.336  1.00113.49           C  
ANISOU 1324  CE2 TYR A 370    13278  16192  13653    794   -347   -409       C  
ATOM   1325  CZ  TYR A 370      15.258  32.147 -45.298  1.00109.51           C  
ANISOU 1325  CZ  TYR A 370    12836  15617  13156    787   -259   -350       C  
ATOM   1326  OH  TYR A 370      13.947  32.258 -44.894  1.00105.42           O  
ANISOU 1326  OH  TYR A 370    12351  15025  12680    825   -224   -315       O  
ATOM   1327  N   PHE A 371      20.769  30.571 -44.032  1.00 95.05           N  
ANISOU 1327  N   PHE A 371    10902  14089  11125    588   -440   -556       N  
ATOM   1328  CA  PHE A 371      20.680  29.842 -42.769  1.00 88.68           C  
ANISOU 1328  CA  PHE A 371    10113  13251  10331    587   -462   -579       C  
ATOM   1329  C   PHE A 371      21.126  30.696 -41.585  1.00 86.84           C  
ANISOU 1329  C   PHE A 371     9941  12991  10064    489   -406   -587       C  
ATOM   1330  O   PHE A 371      20.470  30.714 -40.546  1.00 86.95           O  
ANISOU 1330  O   PHE A 371    10005  12921  10111    478   -379   -581       O  
ATOM   1331  CB  PHE A 371      21.498  28.552 -42.829  1.00 89.06           C  
ANISOU 1331  CB  PHE A 371    10093  13396  10350    631   -541   -616       C  
ATOM   1332  CG  PHE A 371      21.172  27.577 -41.736  1.00 84.01           C  
ANISOU 1332  CG  PHE A 371     9466  12716   9737    663   -564   -628       C  
ATOM   1333  CD1 PHE A 371      20.098  27.794 -40.888  1.00 88.47           C  
ANISOU 1333  CD1 PHE A 371    10093  13166  10356    655   -525   -610       C  
ATOM   1334  CD2 PHE A 371      21.916  26.423 -41.581  1.00 80.20           C  
ANISOU 1334  CD2 PHE A 371     8937  12310   9225    709   -620   -655       C  
ATOM   1335  CE1 PHE A 371      19.792  26.894 -39.888  1.00 88.19           C  
ANISOU 1335  CE1 PHE A 371    10072  13093  10344    685   -544   -620       C  
ATOM   1336  CE2 PHE A 371      21.611  25.515 -40.591  1.00 84.21           C  
ANISOU 1336  CE2 PHE A 371     9463  12776   9757    746   -632   -660       C  
ATOM   1337  CZ  PHE A 371      20.545  25.752 -39.740  1.00 89.02           C  
ANISOU 1337  CZ  PHE A 371    10133  13270  10420    731   -596   -643       C  
ATOM   1338  N   LYS A 372      22.242  31.399 -41.751  1.00 89.18           N  
ANISOU 1338  N   LYS A 372    10230  13365  10290    413   -385   -606       N  
ATOM   1339  CA  LYS A 372      22.727  32.318 -40.730  1.00 93.47           C  
ANISOU 1339  CA  LYS A 372    10829  13897  10790    300   -320   -624       C  
ATOM   1340  C   LYS A 372      21.681  33.378 -40.399  1.00 99.62           C  
ANISOU 1340  C   LYS A 372    11704  14530  11620    269   -226   -589       C  
ATOM   1341  O   LYS A 372      21.479  33.721 -39.234  1.00 93.09           O  
ANISOU 1341  O   LYS A 372    10932  13644  10795    211   -181   -599       O  
ATOM   1342  CB  LYS A 372      24.027  32.986 -41.184  1.00 93.50           C  
ANISOU 1342  CB  LYS A 372    10810  14010  10707    216   -303   -651       C  
ATOM   1343  CG  LYS A 372      25.178  32.019 -41.405  1.00 96.86           C  
ANISOU 1343  CG  LYS A 372    11141  14595  11067    242   -390   -686       C  
ATOM   1344  CD  LYS A 372      26.518  32.736 -41.365  1.00102.69           C  
ANISOU 1344  CD  LYS A 372    11862  15454  11704    129   -364   -724       C  
ATOM   1345  CE  LYS A 372      27.660  31.789 -41.694  1.00110.79           C  
ANISOU 1345  CE  LYS A 372    12787  16651  12658    168   -450   -751       C  
ATOM   1346  NZ  LYS A 372      28.956  32.510 -41.835  1.00113.92           N  
ANISOU 1346  NZ  LYS A 372    13156  17181  12948     58   -427   -789       N  
ATOM   1347  N   ALA A 373      21.020  33.892 -41.430  1.00104.74           N  
ANISOU 1347  N   ALA A 373    12367  15125  12304    313   -192   -544       N  
ATOM   1348  CA  ALA A 373      19.894  34.799 -41.243  1.00106.08           C  
ANISOU 1348  CA  ALA A 373    12623  15158  12525    314   -103   -497       C  
ATOM   1349  C   ALA A 373      18.785  34.141 -40.428  1.00105.96           C  
ANISOU 1349  C   ALA A 373    12624  15064  12573    370   -124   -485       C  
ATOM   1350  O   ALA A 373      18.129  34.792 -39.615  1.00115.44           O  
ANISOU 1350  O   ALA A 373    13902  16160  13799    338    -53   -468       O  
ATOM   1351  CB  ALA A 373      19.360  35.266 -42.589  1.00106.37           C  
ANISOU 1351  CB  ALA A 373    12654  15179  12584    380    -75   -443       C  
ATOM   1352  N   TYR A 374      18.582  32.847 -40.652  1.00101.39           N  
ANISOU 1352  N   TYR A 374    11974  14533  12016    450   -216   -497       N  
ATOM   1353  CA  TYR A 374      17.562  32.096 -39.929  1.00105.95           C  
ANISOU 1353  CA  TYR A 374    12562  15044  12650    501   -239   -491       C  
ATOM   1354  C   TYR A 374      18.169  30.901 -39.201  1.00111.45           C  
ANISOU 1354  C   TYR A 374    13216  15801  13330    507   -313   -536       C  
ATOM   1355  O   TYR A 374      18.470  30.975 -38.010  1.00111.90           O  
ANISOU 1355  O   TYR A 374    13303  15844  13368    451   -298   -556       O  
ATOM   1356  CB  TYR A 374      16.464  31.626 -40.886  1.00103.21           C  
ANISOU 1356  CB  TYR A 374    12180  14681  12353    599   -264   -458       C  
ATOM   1357  CG  TYR A 374      15.565  30.557 -40.309  1.00103.22           C  
ANISOU 1357  CG  TYR A 374    12171  14642  12404    652   -305   -467       C  
ATOM   1358  CD1 TYR A 374      14.205  30.539 -40.590  1.00103.60           C  
ANISOU 1358  CD1 TYR A 374    12226  14635  12501    710   -288   -432       C  
ATOM   1359  CD2 TYR A 374      16.076  29.564 -39.483  1.00 95.75           C  
ANISOU 1359  CD2 TYR A 374    11209  13721  11452    646   -358   -509       C  
ATOM   1360  CE1 TYR A 374      13.379  29.564 -40.065  1.00 97.60           C  
ANISOU 1360  CE1 TYR A 374    11459  13840  11783    748   -321   -446       C  
ATOM   1361  CE2 TYR A 374      15.258  28.584 -38.953  1.00 86.40           C  
ANISOU 1361  CE2 TYR A 374    10024  12491  10313    692   -387   -517       C  
ATOM   1362  CZ  TYR A 374      13.911  28.589 -39.247  1.00 88.30           C  
ANISOU 1362  CZ  TYR A 374    10274  12672  10603    737   -369   -489       C  
ATOM   1363  OH  TYR A 374      13.092  27.615 -38.722  1.00 88.32           O  
ANISOU 1363  OH  TYR A 374    10278  12632  10649    772   -393   -503       O  
ATOM   1364  N   ASP A 405      20.201  15.397 -51.233  1.00 93.77           N  
ANISOU 1364  N   ASP A 405    10275  14226  11127   1251   -815  -1032       N  
ATOM   1365  CA  ASP A 405      19.647  14.215 -50.582  1.00 86.75           C  
ANISOU 1365  CA  ASP A 405     9450  13229  10281   1272   -770  -1067       C  
ATOM   1366  C   ASP A 405      18.397  14.561 -49.781  1.00 72.73           C  
ANISOU 1366  C   ASP A 405     7719  11364   8552   1231   -744  -1052       C  
ATOM   1367  O   ASP A 405      18.208  15.707 -49.372  1.00 71.16           O  
ANISOU 1367  O   ASP A 405     7518  11172   8348   1202   -758  -1001       O  
ATOM   1368  CB  ASP A 405      20.692  13.565 -49.673  1.00 87.59           C  
ANISOU 1368  CB  ASP A 405     9606  13305  10368   1335   -763  -1048       C  
ATOM   1369  CG  ASP A 405      20.818  14.268 -48.336  1.00 90.61           C  
ANISOU 1369  CG  ASP A 405    10031  13651  10746   1327   -767   -988       C  
ATOM   1370  OD1 ASP A 405      19.782  14.471 -47.669  1.00 95.13           O  
ANISOU 1370  OD1 ASP A 405    10644  14139  11362   1293   -743   -980       O  
ATOM   1371  OD2 ASP A 405      21.954  14.617 -47.951  1.00 84.48           O  
ANISOU 1371  OD2 ASP A 405     9242  12939   9917   1352   -791   -951       O  
ATOM   1372  N   PRO A 406      17.547  13.564 -49.559  1.00 56.55           N  
ANISOU 1372  N   PRO A 406     5712   9229   6545   1228   -700  -1098       N  
ATOM   1373  CA  PRO A 406      16.200  13.803 -49.032  1.00 53.87           C  
ANISOU 1373  CA  PRO A 406     5401   8821   6247   1183   -675  -1096       C  
ATOM   1374  C   PRO A 406      16.218  14.761 -47.845  1.00 57.78           C  
ANISOU 1374  C   PRO A 406     5934   9274   6744   1176   -685  -1026       C  
ATOM   1375  O   PRO A 406      15.345  15.622 -47.735  1.00 56.77           O  
ANISOU 1375  O   PRO A 406     5799   9143   6630   1137   -683  -1000       O  
ATOM   1376  CB  PRO A 406      15.756  12.412 -48.578  1.00 58.83           C  
ANISOU 1376  CB  PRO A 406     6095   9344   6912   1194   -620  -1150       C  
ATOM   1377  CG  PRO A 406      17.023  11.709 -48.245  1.00 63.86           C  
ANISOU 1377  CG  PRO A 406     6767   9966   7530   1263   -616  -1141       C  
ATOM   1378  CD  PRO A 406      18.045  12.219 -49.221  1.00 49.92           C  
ANISOU 1378  CD  PRO A 406     4927   8326   5714   1280   -665  -1131       C  
ATOM   1379  N   TYR A 407      17.206  14.607 -46.969  1.00 52.81           N  
ANISOU 1379  N   TYR A 407     5345   8622   6098   1216   -690   -995       N  
ATOM   1380  CA  TYR A 407      17.321  15.453 -45.788  1.00 53.52           C  
ANISOU 1380  CA  TYR A 407     5471   8680   6185   1203   -695   -936       C  
ATOM   1381  C   TYR A 407      17.758  16.866 -46.162  1.00 56.69           C  
ANISOU 1381  C   TYR A 407     5826   9165   6548   1171   -728   -895       C  
ATOM   1382  O   TYR A 407      17.343  17.841 -45.536  1.00 55.18           O  
ANISOU 1382  O   TYR A 407     5656   8946   6364   1135   -721   -855       O  
ATOM   1383  CB  TYR A 407      18.306  14.845 -44.787  1.00 47.70           C  
ANISOU 1383  CB  TYR A 407     4776   7919   5427   1256   -690   -916       C  
ATOM   1384  CG  TYR A 407      17.725  13.718 -43.964  1.00 54.37           C  
ANISOU 1384  CG  TYR A 407     5693   8650   6316   1284   -643   -934       C  
ATOM   1385  CD1 TYR A 407      18.006  12.393 -44.269  1.00 60.02           C  
ANISOU 1385  CD1 TYR A 407     6431   9337   7038   1338   -613   -973       C  
ATOM   1386  CD2 TYR A 407      16.896  13.979 -42.881  1.00 53.39           C  
ANISOU 1386  CD2 TYR A 407     5619   8440   6226   1257   -623   -912       C  
ATOM   1387  CE1 TYR A 407      17.478  11.359 -43.519  1.00 61.38           C  
ANISOU 1387  CE1 TYR A 407     6677   9394   7249   1363   -558   -989       C  
ATOM   1388  CE2 TYR A 407      16.363  12.952 -42.126  1.00 57.21           C  
ANISOU 1388  CE2 TYR A 407     6171   8818   6749   1280   -577   -927       C  
ATOM   1389  CZ  TYR A 407      16.657  11.644 -42.449  1.00 64.39           C  
ANISOU 1389  CZ  TYR A 407     7105   9695   7664   1333   -543   -965       C  
ATOM   1390  OH  TYR A 407      16.128  10.618 -41.700  1.00 65.64           O  
ANISOU 1390  OH  TYR A 407     7340   9738   7861   1356   -485   -979       O  
ATOM   1391  N   ARG A 408      18.599  16.968 -47.186  1.00 56.31           N  
ANISOU 1391  N   ARG A 408     5719   9217   6460   1184   -757   -905       N  
ATOM   1392  CA  ARG A 408      18.966  18.261 -47.751  1.00 59.79           C  
ANISOU 1392  CA  ARG A 408     6114   9738   6864   1150   -780   -872       C  
ATOM   1393  C   ARG A 408      17.760  18.948 -48.383  1.00 61.81           C  
ANISOU 1393  C   ARG A 408     6348   9992   7147   1116   -767   -864       C  
ATOM   1394  O   ARG A 408      17.651  20.174 -48.364  1.00 68.93           O  
ANISOU 1394  O   ARG A 408     7247  10907   8036   1086   -762   -819       O  
ATOM   1395  CB  ARG A 408      20.081  18.097 -48.786  1.00 76.53           C  
ANISOU 1395  CB  ARG A 408     8174  11969   8936   1174   -813   -889       C  
ATOM   1396  CG  ARG A 408      20.635  19.411 -49.314  1.00 90.61           C  
ANISOU 1396  CG  ARG A 408     9916  13837  10675   1139   -833   -854       C  
ATOM   1397  CD  ARG A 408      21.025  19.296 -50.779  1.00102.93           C  
ANISOU 1397  CD  ARG A 408    11401  15498  12208   1152   -860   -879       C  
ATOM   1398  NE  ARG A 408      20.871  20.564 -51.486  1.00111.46           N  
ANISOU 1398  NE  ARG A 408    12447  16633  13272   1115   -861   -844       N  
ATOM   1399  CZ  ARG A 408      21.068  20.719 -52.792  1.00115.99           C  
ANISOU 1399  CZ  ARG A 408    12950  17299  13820   1121   -881   -855       C  
ATOM   1400  NH1 ARG A 408      21.426  19.684 -53.538  1.00116.61           N  
ANISOU 1400  NH1 ARG A 408    12987  17429  13892   1155   -903   -905       N  
ATOM   1401  NH2 ARG A 408      20.905  21.910 -53.351  1.00116.42           N  
ANISOU 1401  NH2 ARG A 408    12981  17394  13858   1094   -873   -814       N  
ATOM   1402  N   LEU A 409      16.857  18.150 -48.943  1.00 58.75           N  
ANISOU 1402  N   LEU A 409     5943   9590   6789   1122   -754   -908       N  
ATOM   1403  CA  LEU A 409      15.612  18.664 -49.472  1.00 52.95           C  
ANISOU 1403  CA  LEU A 409     5180   8868   6073   1097   -738   -902       C  
ATOM   1404  C   LEU A 409      14.746  19.223 -48.337  1.00 62.86           C  
ANISOU 1404  C   LEU A 409     6494  10030   7358   1076   -709   -863       C  
ATOM   1405  O   LEU A 409      14.097  20.265 -48.492  1.00 63.92           O  
ANISOU 1405  O   LEU A 409     6617  10178   7491   1060   -695   -820       O  
ATOM   1406  CB  LEU A 409      14.872  17.543 -50.209  1.00 59.18           C  
ANISOU 1406  CB  LEU A 409     5937   9671   6879   1097   -726   -971       C  
ATOM   1407  CG  LEU A 409      13.569  17.918 -50.929  1.00 74.02           C  
ANISOU 1407  CG  LEU A 409     7764  11599   8761   1073   -710   -974       C  
ATOM   1408  CD1 LEU A 409      13.865  18.824 -52.111  1.00 74.24           C  
ANISOU 1408  CD1 LEU A 409     7713  11749   8747   1079   -732   -944       C  
ATOM   1409  CD2 LEU A 409      12.803  16.674 -51.377  1.00 73.74           C  
ANISOU 1409  CD2 LEU A 409     7710  11567   8741   1056   -688  -1056       C  
ATOM   1410  N   ALA A 410      14.748  18.530 -47.197  1.00 57.77           N  
ANISOU 1410  N   ALA A 410     5916   9294   6742   1082   -696   -875       N  
ATOM   1411  CA  ALA A 410      13.913  18.914 -46.055  1.00 58.35           C  
ANISOU 1411  CA  ALA A 410     6048   9276   6847   1062   -668   -844       C  
ATOM   1412  C   ALA A 410      14.363  20.230 -45.428  1.00 56.73           C  
ANISOU 1412  C   ALA A 410     5868   9063   6623   1042   -667   -782       C  
ATOM   1413  O   ALA A 410      13.539  21.090 -45.092  1.00 54.86           O  
ANISOU 1413  O   ALA A 410     5652   8792   6402   1021   -642   -744       O  
ATOM   1414  CB  ALA A 410      13.897  17.807 -45.008  1.00 55.02           C  
ANISOU 1414  CB  ALA A 410     5688   8761   6454   1076   -653   -871       C  
ATOM   1415  N   VAL A 411      15.677  20.374 -45.271  1.00 49.76           N  
ANISOU 1415  N   VAL A 411     4984   8218   5703   1047   -688   -774       N  
ATOM   1416  CA  VAL A 411      16.251  21.542 -44.616  1.00 42.80           C  
ANISOU 1416  CA  VAL A 411     4130   7335   4795   1014   -680   -728       C  
ATOM   1417  C   VAL A 411      16.032  22.819 -45.422  1.00 54.78           C  
ANISOU 1417  C   VAL A 411     5622   8896   6297    991   -666   -691       C  
ATOM   1418  O   VAL A 411      15.640  23.845 -44.875  1.00 55.11           O  
ANISOU 1418  O   VAL A 411     5705   8891   6345    960   -631   -651       O  
ATOM   1419  CB  VAL A 411      17.738  21.353 -44.364  1.00 43.88           C  
ANISOU 1419  CB  VAL A 411     4259   7531   4883   1021   -705   -734       C  
ATOM   1420  CG1 VAL A 411      18.354  22.659 -43.920  1.00 57.89           C  
ANISOU 1420  CG1 VAL A 411     6051   9327   6619    969   -692   -697       C  
ATOM   1421  CG2 VAL A 411      17.963  20.278 -43.316  1.00 44.90           C  
ANISOU 1421  CG2 VAL A 411     4426   7612   5023   1052   -706   -750       C  
ATOM   1422  N   TYR A 412      16.292  22.759 -46.723  1.00 57.53           N  
ANISOU 1422  N   TYR A 412     5906   9332   6623   1008   -687   -704       N  
ATOM   1423  CA  TYR A 412      16.024  23.892 -47.596  1.00 51.92           C  
ANISOU 1423  CA  TYR A 412     5165   8666   5895    998   -669   -665       C  
ATOM   1424  C   TYR A 412      14.542  24.222 -47.531  1.00 54.56           C  
ANISOU 1424  C   TYR A 412     5513   8952   6265   1005   -632   -638       C  
ATOM   1425  O   TYR A 412      14.147  25.383 -47.385  1.00 57.63           O  
ANISOU 1425  O   TYR A 412     5930   9314   6653    993   -591   -584       O  
ATOM   1426  CB  TYR A 412      16.387  23.552 -49.045  1.00 55.71           C  
ANISOU 1426  CB  TYR A 412     5564   9255   6349   1023   -700   -689       C  
ATOM   1427  CG  TYR A 412      17.767  23.954 -49.496  1.00 66.32           C  
ANISOU 1427  CG  TYR A 412     6883  10674   7641   1012   -723   -686       C  
ATOM   1428  CD1 TYR A 412      18.882  23.217 -49.129  1.00 76.15           C  
ANISOU 1428  CD1 TYR A 412     8129  11942   8863   1017   -756   -720       C  
ATOM   1429  CD2 TYR A 412      17.951  25.048 -50.326  1.00 73.74           C  
ANISOU 1429  CD2 TYR A 412     7796  11670   8551   1000   -708   -647       C  
ATOM   1430  CE1 TYR A 412      20.142  23.567 -49.559  1.00 78.18           C  
ANISOU 1430  CE1 TYR A 412     8355  12284   9065   1005   -778   -720       C  
ATOM   1431  CE2 TYR A 412      19.209  25.406 -50.765  1.00 75.45           C  
ANISOU 1431  CE2 TYR A 412     7989  11961   8718    983   -728   -649       C  
ATOM   1432  CZ  TYR A 412      20.302  24.662 -50.379  1.00 76.54           C  
ANISOU 1432  CZ  TYR A 412     8123  12130   8831    983   -765   -687       C  
ATOM   1433  OH  TYR A 412      21.561  25.020 -50.820  1.00 71.95           O  
ANISOU 1433  OH  TYR A 412     7511  11637   8192    964   -786   -690       O  
ATOM   1434  N   LYS A 413      13.715  23.193 -47.660  1.00 53.48           N  
ANISOU 1434  N   LYS A 413     5355   8807   6157   1024   -641   -678       N  
ATOM   1435  CA  LYS A 413      12.270  23.391 -47.605  1.00 58.46           C  
ANISOU 1435  CA  LYS A 413     5987   9411   6813   1031   -610   -659       C  
ATOM   1436  C   LYS A 413      11.830  24.071 -46.302  1.00 64.78           C  
ANISOU 1436  C   LYS A 413     6868  10106   7639   1011   -572   -617       C  
ATOM   1437  O   LYS A 413      11.066  25.032 -46.341  1.00 65.62           O  
ANISOU 1437  O   LYS A 413     6984  10202   7746   1017   -533   -564       O  
ATOM   1438  CB  LYS A 413      11.526  22.071 -47.807  1.00 47.65           C  
ANISOU 1438  CB  LYS A 413     4590   8048   5467   1038   -621   -722       C  
ATOM   1439  CG  LYS A 413      10.041  22.210 -47.703  1.00 56.59           C  
ANISOU 1439  CG  LYS A 413     5717   9168   6616   1038   -590   -708       C  
ATOM   1440  CD  LYS A 413       9.367  20.875 -47.871  1.00 75.01           C  
ANISOU 1440  CD  LYS A 413     8027  11509   8967   1029   -595   -782       C  
ATOM   1441  CE  LYS A 413       9.359  20.480 -49.318  1.00 84.10           C  
ANISOU 1441  CE  LYS A 413     9085  12785  10085   1035   -612   -821       C  
ATOM   1442  NZ  LYS A 413       8.800  21.598 -50.120  1.00 91.42           N  
ANISOU 1442  NZ  LYS A 413     9952  13806  10978   1056   -598   -761       N  
ATOM   1443  N   LEU A 414      12.325  23.585 -45.160  1.00 59.11           N  
ANISOU 1443  N   LEU A 414     6206   9316   6937    993   -581   -637       N  
ATOM   1444  CA  LEU A 414      11.954  24.150 -43.857  1.00 59.92           C  
ANISOU 1444  CA  LEU A 414     6384   9322   7063    970   -547   -605       C  
ATOM   1445  C   LEU A 414      12.494  25.563 -43.645  1.00 63.68           C  
ANISOU 1445  C   LEU A 414     6894   9788   7514    941   -514   -553       C  
ATOM   1446  O   LEU A 414      11.755  26.463 -43.234  1.00 72.17           O  
ANISOU 1446  O   LEU A 414     8011  10808   8602    933   -466   -509       O  
ATOM   1447  CB  LEU A 414      12.401  23.234 -42.712  1.00 57.48           C  
ANISOU 1447  CB  LEU A 414     6118   8952   6769    961   -564   -638       C  
ATOM   1448  CG  LEU A 414      11.857  21.807 -42.800  1.00 60.62           C  
ANISOU 1448  CG  LEU A 414     6501   9336   7195    985   -579   -691       C  
ATOM   1449  CD1 LEU A 414      12.442  20.903 -41.737  1.00 50.96           C  
ANISOU 1449  CD1 LEU A 414     5324   8058   5983    990   -589   -714       C  
ATOM   1450  CD2 LEU A 414      10.330  21.799 -42.752  1.00 62.84           C  
ANISOU 1450  CD2 LEU A 414     6786   9582   7509    983   -553   -687       C  
ATOM   1451  N   ILE A 415      13.783  25.751 -43.910  1.00 62.51           N  
ANISOU 1451  N   ILE A 415     6732   9691   7326    924   -533   -562       N  
ATOM   1452  CA  ILE A 415      14.409  27.063 -43.758  1.00 69.53           C  
ANISOU 1452  CA  ILE A 415     7656  10576   8185    882   -495   -525       C  
ATOM   1453  C   ILE A 415      13.883  28.042 -44.806  1.00 71.21           C  
ANISOU 1453  C   ILE A 415     7850  10818   8390    901   -457   -476       C  
ATOM   1454  O   ILE A 415      13.479  29.161 -44.481  1.00 76.08           O  
ANISOU 1454  O   ILE A 415     8521  11377   9010    885   -394   -427       O  
ATOM   1455  CB  ILE A 415      15.955  26.984 -43.848  1.00 80.15           C  
ANISOU 1455  CB  ILE A 415     8981  11991   9480    854   -526   -551       C  
ATOM   1456  CG1 ILE A 415      16.494  25.914 -42.896  1.00 78.63           C  
ANISOU 1456  CG1 ILE A 415     8797  11790   9287    855   -563   -591       C  
ATOM   1457  CG2 ILE A 415      16.573  28.324 -43.511  1.00 78.54           C  
ANISOU 1457  CG2 ILE A 415     8823  11775   9242    791   -476   -523       C  
ATOM   1458  CD1 ILE A 415      16.157  26.166 -41.456  1.00 80.85           C  
ANISOU 1458  CD1 ILE A 415     9146  11984   9588    821   -531   -580       C  
ATOM   1459  N   GLY A 416      13.878  27.613 -46.062  1.00 69.75           N  
ANISOU 1459  N   GLY A 416     7588  10721   8191    940   -490   -488       N  
ATOM   1460  CA  GLY A 416      13.369  28.446 -47.132  1.00 78.97           C  
ANISOU 1460  CA  GLY A 416     8725  11935   9344    971   -456   -438       C  
ATOM   1461  C   GLY A 416      11.872  28.667 -47.017  1.00 92.07           C  
ANISOU 1461  C   GLY A 416    10394  13558  11032   1007   -417   -399       C  
ATOM   1462  O   GLY A 416      11.354  29.717 -47.406  1.00 97.14           O  
ANISOU 1462  O   GLY A 416    11046  14198  11663   1032   -359   -333       O  
ATOM   1463  N   ARG A 417      11.174  27.679 -46.467  1.00 93.32           N  
ANISOU 1463  N   ARG A 417    10548  13687  11222   1013   -442   -437       N  
ATOM   1464  CA  ARG A 417       9.719  27.714 -46.425  1.00 96.93           C  
ANISOU 1464  CA  ARG A 417    10997  14132  11698   1047   -414   -410       C  
ATOM   1465  C   ARG A 417       9.228  27.766 -47.862  1.00102.94           C  
ANISOU 1465  C   ARG A 417    11668  15015  12430   1095   -417   -392       C  
ATOM   1466  O   ARG A 417       8.311  28.515 -48.190  1.00110.02           O  
ANISOU 1466  O   ARG A 417    12553  15934  13315   1136   -370   -330       O  
ATOM   1467  CB  ARG A 417       9.229  28.934 -45.639  1.00 92.61           C  
ANISOU 1467  CB  ARG A 417    10531  13495  11163   1044   -342   -342       C  
ATOM   1468  CG  ARG A 417       7.879  28.758 -44.964  1.00 90.18           C  
ANISOU 1468  CG  ARG A 417    10242  13138  10885   1062   -319   -329       C  
ATOM   1469  CD  ARG A 417       7.773  29.644 -43.725  1.00 92.84           C  
ANISOU 1469  CD  ARG A 417    10680  13352  11242   1035   -261   -291       C  
ATOM   1470  NE  ARG A 417       9.003  29.599 -42.935  1.00 95.04           N  
ANISOU 1470  NE  ARG A 417    11011  13577  11523    973   -277   -326       N  
ATOM   1471  CZ  ARG A 417       9.107  29.983 -41.665  1.00 94.97           C  
ANISOU 1471  CZ  ARG A 417    11083  13470  11533    929   -246   -323       C  
ATOM   1472  NH1 ARG A 417       8.044  30.443 -41.009  1.00 84.66           N  
ANISOU 1472  NH1 ARG A 417     9824  12093  10251    942   -196   -285       N  
ATOM   1473  NH2 ARG A 417      10.281  29.896 -41.048  1.00 96.04           N  
ANISOU 1473  NH2 ARG A 417    11247  13587  11655    872   -264   -359       N  
ATOM   1474  N   CYS A 418       9.860  26.975 -48.723  1.00100.34           N  
ANISOU 1474  N   CYS A 418    11271  14772  12082   1094   -469   -444       N  
ATOM   1475  CA  CYS A 418       9.506  26.959 -50.137  1.00104.67           C  
ANISOU 1475  CA  CYS A 418    11722  15453  12596   1133   -477   -436       C  
ATOM   1476  C   CYS A 418       8.729  25.700 -50.531  1.00105.10           C  
ANISOU 1476  C   CYS A 418    11707  15573  12653   1135   -510   -503       C  
ATOM   1477  O   CYS A 418       8.693  24.717 -49.783  1.00104.55           O  
ANISOU 1477  O   CYS A 418    11669  15440  12616   1105   -532   -564       O  
ATOM   1478  CB  CYS A 418      10.745  27.163 -51.030  1.00105.82           C  
ANISOU 1478  CB  CYS A 418    11832  15666  12708   1130   -503   -441       C  
ATOM   1479  SG  CYS A 418      12.344  26.547 -50.385  1.00 82.66           S  
ANISOU 1479  SG  CYS A 418     8943  12680   9782   1078   -550   -503       S  
ATOM   1480  N   ASP A 419       8.097  25.755 -51.702  1.00101.57           N  
ANISOU 1480  N   ASP A 419    11166  15257  12169   1169   -507   -491       N  
ATOM   1481  CA  ASP A 419       7.305  24.643 -52.223  1.00100.45           C  
ANISOU 1481  CA  ASP A 419    10946  15202  12017   1160   -529   -560       C  
ATOM   1482  C   ASP A 419       6.174  24.243 -51.265  1.00 95.48           C  
ANISOU 1482  C   ASP A 419    10352  14509  11416   1144   -508   -575       C  
ATOM   1483  O   ASP A 419       5.981  23.062 -50.972  1.00 94.57           O  
ANISOU 1483  O   ASP A 419    10239  14370  11322   1105   -528   -657       O  
ATOM   1484  CB  ASP A 419       8.217  23.447 -52.529  1.00 99.87           C  
ANISOU 1484  CB  ASP A 419    10855  15138  11952   1125   -579   -653       C  
ATOM   1485  CG  ASP A 419       7.519  22.360 -53.334  1.00102.07           C  
ANISOU 1485  CG  ASP A 419    11046  15525  12211   1107   -591   -731       C  
ATOM   1486  OD1 ASP A 419       7.915  21.182 -53.199  1.00102.39           O  
ANISOU 1486  OD1 ASP A 419    11101  15530  12273   1072   -613   -817       O  
ATOM   1487  OD2 ASP A 419       6.578  22.676 -54.096  1.00103.71           O  
ANISOU 1487  OD2 ASP A 419    11171  15856  12378   1128   -574   -708       O  
ATOM   1488  N   LEU A 420       5.418  25.228 -50.788  1.00 94.13           N  
ANISOU 1488  N   LEU A 420    10214  14308  11245   1176   -462   -496       N  
ATOM   1489  CA  LEU A 420       4.386  24.959 -49.787  1.00 96.31           C  
ANISOU 1489  CA  LEU A 420    10530  14516  11547   1163   -442   -503       C  
ATOM   1490  C   LEU A 420       3.254  24.102 -50.335  1.00 88.07           C  
ANISOU 1490  C   LEU A 420     9397  13589  10476   1152   -447   -557       C  
ATOM   1491  O   LEU A 420       2.496  23.498 -49.575  1.00 88.74           O  
ANISOU 1491  O   LEU A 420     9508  13625  10583   1122   -440   -595       O  
ATOM   1492  CB  LEU A 420       3.835  26.255 -49.182  1.00101.57           C  
ANISOU 1492  CB  LEU A 420    11252  15126  12216   1204   -385   -402       C  
ATOM   1493  CG  LEU A 420       4.866  27.110 -48.445  1.00106.49           C  
ANISOU 1493  CG  LEU A 420    11977  15618  12866   1195   -367   -358       C  
ATOM   1494  CD1 LEU A 420       5.666  27.942 -49.455  1.00112.71           C  
ANISOU 1494  CD1 LEU A 420    12736  16470  13619   1225   -357   -310       C  
ATOM   1495  CD2 LEU A 420       4.208  27.995 -47.401  1.00102.64           C  
ANISOU 1495  CD2 LEU A 420    11571  15029  12399   1211   -309   -292       C  
ATOM   1496  N   SER A 421       3.140  24.052 -51.654  1.00 86.51           N  
ANISOU 1496  N   SER A 421     9091  13553  10226   1171   -456   -565       N  
ATOM   1497  CA  SER A 421       2.159  23.179 -52.283  1.00 92.14           C  
ANISOU 1497  CA  SER A 421     9708  14402  10901   1146   -460   -632       C  
ATOM   1498  C   SER A 421       2.443  21.737 -51.880  1.00 92.52           C  
ANISOU 1498  C   SER A 421     9788  14377  10987   1071   -485   -750       C  
ATOM   1499  O   SER A 421       1.523  20.929 -51.739  1.00 90.08           O  
ANISOU 1499  O   SER A 421     9454  14101  10672   1028   -474   -814       O  
ATOM   1500  CB  SER A 421       2.207  23.326 -53.806  1.00 96.32           C  
ANISOU 1500  CB  SER A 421    10112  15122  11364   1174   -469   -627       C  
ATOM   1501  OG  SER A 421       1.961  24.667 -54.189  1.00 99.35           O  
ANISOU 1501  OG  SER A 421    10471  15568  11711   1254   -436   -508       O  
ATOM   1502  N   ARG A 422       3.727  21.433 -51.688  1.00 93.92           N  
ANISOU 1502  N   ARG A 422    10024  14460  11201   1057   -513   -776       N  
ATOM   1503  CA  ARG A 422       4.172  20.101 -51.288  1.00 88.69           C  
ANISOU 1503  CA  ARG A 422     9406  13715  10576   1003   -529   -875       C  
ATOM   1504  C   ARG A 422       4.636  20.087 -49.835  1.00 84.55           C  
ANISOU 1504  C   ARG A 422     9006  13008  10112    997   -527   -857       C  
ATOM   1505  O   ARG A 422       5.833  19.979 -49.562  1.00 90.34           O  
ANISOU 1505  O   ARG A 422     9790  13668  10867   1002   -548   -860       O  
ATOM   1506  CB  ARG A 422       5.309  19.629 -52.196  1.00 86.66           C  
ANISOU 1506  CB  ARG A 422     9115  13504  10308    999   -560   -920       C  
ATOM   1507  N   LYS A 423       3.682  20.196 -48.912  1.00 83.13           N  
ANISOU 1507  N   LYS A 423     8867  12767   9951    988   -501   -839       N  
ATOM   1508  CA  LYS A 423       3.976  20.245 -47.477  1.00 87.54           C  
ANISOU 1508  CA  LYS A 423     9538  13162  10563    983   -495   -818       C  
ATOM   1509  C   LYS A 423       4.658  18.973 -46.962  1.00 92.65           C  
ANISOU 1509  C   LYS A 423    10242  13714  11246    951   -506   -895       C  
ATOM   1510  O   LYS A 423       5.395  19.012 -45.973  1.00 91.37           O  
ANISOU 1510  O   LYS A 423    10162  13438  11118    957   -512   -875       O  
ATOM   1511  CB  LYS A 423       2.697  20.525 -46.667  1.00 80.49           C  
ANISOU 1511  CB  LYS A 423     8668  12235   9679    978   -463   -791       C  
ATOM   1512  CG  LYS A 423       2.273  21.993 -46.628  1.00 71.50           C  
ANISOU 1512  CG  LYS A 423     7524  11122   8520   1027   -440   -687       C  
ATOM   1513  CD  LYS A 423       0.757  22.137 -46.599  1.00 77.04           C  
ANISOU 1513  CD  LYS A 423     8183  11892   9197   1033   -410   -671       C  
ATOM   1514  CE  LYS A 423       0.115  21.907 -47.982  1.00 72.73           C  
ANISOU 1514  CE  LYS A 423     7508  11539   8586   1038   -410   -698       C  
ATOM   1515  NZ  LYS A 423      -1.383  21.803 -47.909  1.00 60.73           N  
ANISOU 1515  NZ  LYS A 423     5937  10105   7033   1032   -383   -702       N  
ATOM   1516  N   ASN A 424       4.415  17.854 -47.638  1.00 94.41           N  
ANISOU 1516  N   ASN A 424    10422  13991  11459    918   -503   -982       N  
ATOM   1517  CA  ASN A 424       4.924  16.564 -47.177  1.00102.28           C  
ANISOU 1517  CA  ASN A 424    11480  14892  12490    893   -497  -1055       C  
ATOM   1518  C   ASN A 424       6.150  16.034 -47.921  1.00106.17           C  
ANISOU 1518  C   ASN A 424    11957  15410  12973    906   -518  -1091       C  
ATOM   1519  O   ASN A 424       6.182  15.987 -49.152  1.00105.55           O  
ANISOU 1519  O   ASN A 424    11794  15452  12857    901   -528  -1121       O  
ATOM   1520  CB  ASN A 424       3.811  15.516 -47.172  1.00106.19           C  
ANISOU 1520  CB  ASN A 424    11968  15390  12988    836   -460  -1138       C  
ATOM   1521  CG  ASN A 424       2.800  15.748 -46.059  1.00109.28           C  
ANISOU 1521  CG  ASN A 424    12407  15711  13402    822   -437  -1110       C  
ATOM   1522  OD1 ASN A 424       3.000  16.603 -45.189  1.00104.97           O  
ANISOU 1522  OD1 ASN A 424    11912  15096  12877    856   -447  -1032       O  
ATOM   1523  ND2 ASN A 424       1.709  14.985 -46.080  1.00111.29           N  
ANISOU 1523  ND2 ASN A 424    12646  15987  13651    766   -403  -1178       N  
ATOM   1524  N   ILE A 425       7.158  15.646 -47.146  1.00106.83           N  
ANISOU 1524  N   ILE A 425    12118  15386  13086    927   -524  -1086       N  
ATOM   1525  CA  ILE A 425       8.355  14.997 -47.665  1.00105.63           C  
ANISOU 1525  CA  ILE A 425    11965  15243  12926    947   -539  -1121       C  
ATOM   1526  C   ILE A 425       8.638  13.787 -46.782  1.00101.60           C  
ANISOU 1526  C   ILE A 425    11543  14606  12453    950   -508  -1163       C  
ATOM   1527  O   ILE A 425       9.502  13.837 -45.909  1.00104.36           O  
ANISOU 1527  O   ILE A 425    11953  14883  12816    987   -518  -1122       O  
ATOM   1528  CB  ILE A 425       9.555  15.956 -47.663  1.00104.72           C  
ANISOU 1528  CB  ILE A 425    11845  15150  12793    989   -579  -1051       C  
ATOM   1529  CG1 ILE A 425       9.627  16.702 -46.330  1.00 94.75           C  
ANISOU 1529  CG1 ILE A 425    10652  13798  11552   1000   -578   -982       C  
ATOM   1530  CG2 ILE A 425       9.440  16.950 -48.816  1.00111.82           C  
ANISOU 1530  CG2 ILE A 425    12655  16181  13652    993   -601  -1020       C  
ATOM   1531  CD1 ILE A 425      10.665  17.786 -46.296  1.00 92.21           C  
ANISOU 1531  CD1 ILE A 425    10326  13505  11205   1022   -607   -918       C  
ATOM   1532  N   PRO A 426       7.895  12.693 -47.018  1.00100.59           N  
ANISOU 1532  N   PRO A 426    11423  14461  12337    908   -465  -1245       N  
ATOM   1533  CA  PRO A 426       7.724  11.507 -46.162  1.00 97.41           C  
ANISOU 1533  CA  PRO A 426    11112  13927  11973    898   -414  -1291       C  
ATOM   1534  C   PRO A 426       8.986  10.706 -45.801  1.00 96.03           C  
ANISOU 1534  C   PRO A 426    11004  13673  11811    953   -402  -1292       C  
ATOM   1535  O   PRO A 426       9.058  10.210 -44.674  1.00 93.29           O  
ANISOU 1535  O   PRO A 426    10744  13209  11495    974   -373  -1277       O  
ATOM   1536  CB  PRO A 426       6.749  10.633 -46.966  1.00 96.68           C  
ANISOU 1536  CB  PRO A 426    10986  13876  11871    829   -367  -1391       C  
ATOM   1537  CG  PRO A 426       6.047  11.588 -47.882  1.00 96.96           C  
ANISOU 1537  CG  PRO A 426    10912  14064  11866    802   -399  -1378       C  
ATOM   1538  CD  PRO A 426       7.090  12.591 -48.248  1.00100.39           C  
ANISOU 1538  CD  PRO A 426    11307  14557  12279    861   -457  -1303       C  
ATOM   1539  N   ALA A 427       9.945  10.565 -46.714  1.00 91.78           N  
ANISOU 1539  N   ALA A 427    10426  13202  11246    982   -422  -1307       N  
ATOM   1540  CA  ALA A 427      11.133   9.751 -46.429  1.00 90.79           C  
ANISOU 1540  CA  ALA A 427    10358  13013  11125   1044   -406  -1307       C  
ATOM   1541  C   ALA A 427      11.810  10.106 -45.098  1.00 89.48           C  
ANISOU 1541  C   ALA A 427    10253  12778  10968   1101   -422  -1225       C  
ATOM   1542  O   ALA A 427      12.244   9.224 -44.355  1.00 94.17           O  
ANISOU 1542  O   ALA A 427    10924  13277  11578   1146   -382  -1224       O  
ATOM   1543  CB  ALA A 427      12.128   9.838 -47.565  1.00 85.44           C  
ANISOU 1543  CB  ALA A 427     9616  12438  10409   1072   -439  -1317       C  
ATOM   1544  N   VAL A 428      11.891  11.400 -44.805  1.00 77.82           N  
ANISOU 1544  N   VAL A 428     8741  11351   9476   1099   -474  -1157       N  
ATOM   1545  CA  VAL A 428      12.497  11.873 -43.565  1.00 77.63           C  
ANISOU 1545  CA  VAL A 428     8763  11281   9452   1137   -490  -1085       C  
ATOM   1546  C   VAL A 428      11.496  12.076 -42.411  1.00 85.13           C  
ANISOU 1546  C   VAL A 428     9765  12143  10437   1108   -468  -1063       C  
ATOM   1547  O   VAL A 428      11.864  12.575 -41.346  1.00 93.55           O  
ANISOU 1547  O   VAL A 428    10864  13177  11502   1128   -481  -1004       O  
ATOM   1548  CB  VAL A 428      13.288  13.168 -43.801  1.00 67.86           C  
ANISOU 1548  CB  VAL A 428     7470  10140   8175   1144   -548  -1026       C  
ATOM   1549  CG1 VAL A 428      14.251  12.969 -44.950  1.00 68.40           C  
ANISOU 1549  CG1 VAL A 428     7483  10300   8206   1171   -571  -1049       C  
ATOM   1550  CG2 VAL A 428      12.347  14.333 -44.085  1.00 56.70           C  
ANISOU 1550  CG2 VAL A 428     6013   8767   6763   1093   -564  -1005       C  
ATOM   1551  N   THR A 429      10.237  11.696 -42.619  1.00 81.32           N  
ANISOU 1551  N   THR A 429     9286  11631   9981   1057   -435  -1112       N  
ATOM   1552  CA  THR A 429       9.241  11.742 -41.548  1.00 69.57           C  
ANISOU 1552  CA  THR A 429     7849  10057   8526   1029   -410  -1099       C  
ATOM   1553  C   THR A 429       8.979  10.343 -41.011  1.00 73.68           C  
ANISOU 1553  C   THR A 429     8451  10466   9080   1034   -346  -1146       C  
ATOM   1554  O   THR A 429       8.327   9.532 -41.666  1.00 75.44           O  
ANISOU 1554  O   THR A 429     8672  10680   9311    993   -304  -1222       O  
ATOM   1555  CB  THR A 429       7.891  12.305 -42.021  1.00 63.34           C  
ANISOU 1555  CB  THR A 429     7012   9317   7739    966   -410  -1118       C  
ATOM   1556  OG1 THR A 429       8.088  13.501 -42.783  1.00 68.39           O  
ANISOU 1556  OG1 THR A 429     7574  10067   8346    967   -457  -1079       O  
ATOM   1557  CG2 THR A 429       7.029  12.617 -40.824  1.00 61.05           C  
ANISOU 1557  CG2 THR A 429     6770   8950   7477    946   -396  -1086       C  
ATOM   1558  N   LEU A 430       9.472  10.064 -39.812  1.00 80.16           N  
ANISOU 1558  N   LEU A 430     9341  11202   9913   1080   -332  -1103       N  
ATOM   1559  CA  LEU A 430       9.398   8.711 -39.270  1.00 82.41           C  
ANISOU 1559  CA  LEU A 430     9712  11372  10227   1103   -262  -1135       C  
ATOM   1560  C   LEU A 430       8.357   8.546 -38.155  1.00 74.83           C  
ANISOU 1560  C   LEU A 430     8814  10314   9304   1070   -227  -1130       C  
ATOM   1561  O   LEU A 430       8.142   7.437 -37.666  1.00 73.55           O  
ANISOU 1561  O   LEU A 430     8730  10046   9168   1081   -159  -1158       O  
ATOM   1562  CB  LEU A 430      10.784   8.259 -38.798  1.00 87.63           C  
ANISOU 1562  CB  LEU A 430    10410  12016  10870   1197   -257  -1090       C  
ATOM   1563  CG  LEU A 430      11.902   8.436 -39.839  1.00 89.17           C  
ANISOU 1563  CG  LEU A 430    10543  12315  11023   1234   -294  -1091       C  
ATOM   1564  CD1 LEU A 430      13.283   8.331 -39.203  1.00 87.55           C  
ANISOU 1564  CD1 LEU A 430    10356  12125  10785   1328   -305  -1027       C  
ATOM   1565  CD2 LEU A 430      11.753   7.442 -40.989  1.00 90.72           C  
ANISOU 1565  CD2 LEU A 430    10739  12505  11225   1218   -248  -1175       C  
ATOM   1566  N   SER A 431       7.705   9.644 -37.774  1.00 61.73           N  
ANISOU 1566  N   SER A 431     7122   8686   7647   1032   -267  -1094       N  
ATOM   1567  CA  SER A 431       6.731   9.618 -36.684  1.00 62.40           C  
ANISOU 1567  CA  SER A 431     7258   8687   7763   1003   -242  -1083       C  
ATOM   1568  C   SER A 431       5.730  10.764 -36.778  1.00 55.41           C  
ANISOU 1568  C   SER A 431     6320   7860   6875    946   -277  -1069       C  
ATOM   1569  O   SER A 431       5.932  11.718 -37.522  1.00 54.25           O  
ANISOU 1569  O   SER A 431     6102   7812   6700    942   -322  -1049       O  
ATOM   1570  CB  SER A 431       7.440   9.688 -35.332  1.00 66.25           C  
ANISOU 1570  CB  SER A 431     7801   9115   8255   1062   -245  -1012       C  
ATOM   1571  OG  SER A 431       7.859  11.017 -35.063  1.00 67.96           O  
ANISOU 1571  OG  SER A 431     7972   9402   8448   1066   -306   -950       O  
ATOM   1572  N   ILE A 432       4.654  10.676 -36.003  1.00 55.54           N  
ANISOU 1572  N   ILE A 432     6372   7813   6917    908   -251  -1074       N  
ATOM   1573  CA  ILE A 432       3.647  11.728 -36.010  1.00 48.19           C  
ANISOU 1573  CA  ILE A 432     5396   6934   5981    864   -276  -1054       C  
ATOM   1574  C   ILE A 432       4.217  13.032 -35.457  1.00 45.67           C  
ANISOU 1574  C   ILE A 432     5064   6640   5650    895   -323   -970       C  
ATOM   1575  O   ILE A 432       3.927  14.116 -35.969  1.00 51.54           O  
ANISOU 1575  O   ILE A 432     5749   7460   6373    882   -351   -944       O  
ATOM   1576  CB  ILE A 432       2.375  11.313 -35.247  1.00 42.96           C  
ANISOU 1576  CB  ILE A 432     4776   6201   5346    817   -236  -1079       C  
ATOM   1577  CG1 ILE A 432       1.669  10.177 -35.987  1.00 45.89           C  
ANISOU 1577  CG1 ILE A 432     5147   6571   5718    763   -184  -1174       C  
ATOM   1578  CG2 ILE A 432       1.424  12.496 -35.101  1.00 38.25           C  
ANISOU 1578  CG2 ILE A 432     4135   5657   4739    790   -262  -1041       C  
ATOM   1579  CD1 ILE A 432       0.569   9.498 -35.167  1.00 58.30           C  
ANISOU 1579  CD1 ILE A 432     6778   8057   7316    713   -132  -1210       C  
ATOM   1580  N   GLU A 433       5.030  12.920 -34.413  1.00 44.73           N  
ANISOU 1580  N   GLU A 433     4997   6458   5539    936   -324   -929       N  
ATOM   1581  CA  GLU A 433       5.684  14.081 -33.834  1.00 43.05           C  
ANISOU 1581  CA  GLU A 433     4776   6271   5309    954   -360   -860       C  
ATOM   1582  C   GLU A 433       6.437  14.851 -34.903  1.00 46.57           C  
ANISOU 1582  C   GLU A 433     5156   6819   5718    963   -397   -848       C  
ATOM   1583  O   GLU A 433       6.394  16.080 -34.934  1.00 47.91           O  
ANISOU 1583  O   GLU A 433     5300   7031   5873    949   -417   -807       O  
ATOM   1584  CB  GLU A 433       6.643  13.670 -32.706  1.00 50.77           C  
ANISOU 1584  CB  GLU A 433     5807   7198   6287   1000   -355   -826       C  
ATOM   1585  CG  GLU A 433       5.968  13.304 -31.380  1.00 48.18           C  
ANISOU 1585  CG  GLU A 433     5543   6772   5990    992   -325   -813       C  
ATOM   1586  CD  GLU A 433       5.581  11.828 -31.292  1.00 57.44           C  
ANISOU 1586  CD  GLU A 433     6770   7864   7192   1003   -273   -860       C  
ATOM   1587  OE1 GLU A 433       5.460  11.168 -32.350  1.00 58.72           O  
ANISOU 1587  OE1 GLU A 433     6916   8042   7354    994   -255   -916       O  
ATOM   1588  OE2 GLU A 433       5.400  11.323 -30.161  1.00 57.40           O  
ANISOU 1588  OE2 GLU A 433     6825   7777   7208   1017   -244   -842       O  
ATOM   1589  N   ASP A 434       7.123  14.123 -35.784  1.00 44.33           N  
ANISOU 1589  N   ASP A 434     4852   6572   5420    987   -398   -884       N  
ATOM   1590  CA  ASP A 434       7.911  14.758 -36.837  1.00 45.86           C  
ANISOU 1590  CA  ASP A 434     4982   6866   5577    998   -433   -876       C  
ATOM   1591  C   ASP A 434       7.007  15.520 -37.806  1.00 50.94           C  
ANISOU 1591  C   ASP A 434     5565   7578   6213    961   -442   -883       C  
ATOM   1592  O   ASP A 434       7.347  16.622 -38.245  1.00 46.10           O  
ANISOU 1592  O   ASP A 434     4911   7030   5573    962   -467   -845       O  
ATOM   1593  CB  ASP A 434       8.785  13.742 -37.595  1.00 56.14           C  
ANISOU 1593  CB  ASP A 434     6274   8192   6865   1034   -430   -916       C  
ATOM   1594  CG  ASP A 434       9.737  12.967 -36.675  1.00 67.58           C  
ANISOU 1594  CG  ASP A 434     7779   9585   8312   1089   -415   -898       C  
ATOM   1595  OD1 ASP A 434       9.663  13.121 -35.440  1.00 77.17           O  
ANISOU 1595  OD1 ASP A 434     9039  10745   9539   1095   -407   -859       O  
ATOM   1596  OD2 ASP A 434      10.560  12.183 -37.192  1.00 74.43           O  
ANISOU 1596  OD2 ASP A 434     8644  10471   9164   1132   -408   -919       O  
ATOM   1597  N   TRP A 435       5.853  14.934 -38.127  1.00 52.59           N  
ANISOU 1597  N   TRP A 435     5767   7777   6439    930   -415   -931       N  
ATOM   1598  CA  TRP A 435       4.881  15.548 -39.035  1.00 41.57           C  
ANISOU 1598  CA  TRP A 435     4304   6464   5025    900   -418   -939       C  
ATOM   1599  C   TRP A 435       4.318  16.862 -38.471  1.00 46.04           C  
ANISOU 1599  C   TRP A 435     4871   7030   5590    897   -423   -871       C  
ATOM   1600  O   TRP A 435       4.319  17.892 -39.156  1.00 49.88           O  
ANISOU 1600  O   TRP A 435     5308   7594   6050    905   -437   -834       O  
ATOM   1601  CB  TRP A 435       3.753  14.564 -39.328  1.00 45.43           C  
ANISOU 1601  CB  TRP A 435     4787   6949   5524    858   -383  -1010       C  
ATOM   1602  CG  TRP A 435       2.821  14.995 -40.413  1.00 53.92           C  
ANISOU 1602  CG  TRP A 435     5777   8142   6568    831   -384  -1028       C  
ATOM   1603  CD1 TRP A 435       3.037  14.905 -41.756  1.00 54.02           C  
ANISOU 1603  CD1 TRP A 435     5714   8264   6547    828   -395  -1062       C  
ATOM   1604  CD2 TRP A 435       1.512  15.569 -40.253  1.00 57.73           C  
ANISOU 1604  CD2 TRP A 435     6233   8660   7042    807   -372  -1010       C  
ATOM   1605  NE1 TRP A 435       1.948  15.389 -42.447  1.00 59.35           N  
ANISOU 1605  NE1 TRP A 435     6314   9048   7189    805   -391  -1064       N  
ATOM   1606  CE2 TRP A 435       0.999  15.803 -41.551  1.00 57.81           C  
ANISOU 1606  CE2 TRP A 435     6145   8811   7007    795   -376  -1031       C  
ATOM   1607  CE3 TRP A 435       0.727  15.910 -39.144  1.00 61.16           C  
ANISOU 1607  CE3 TRP A 435     6713   9028   7498    798   -358   -976       C  
ATOM   1608  CZ2 TRP A 435      -0.266  16.365 -41.769  1.00 46.44           C  
ANISOU 1608  CZ2 TRP A 435     4650   7457   5538    781   -364  -1015       C  
ATOM   1609  CZ3 TRP A 435      -0.534  16.463 -39.361  1.00 59.07           C  
ANISOU 1609  CZ3 TRP A 435     6397   8838   7209    782   -346   -963       C  
ATOM   1610  CH2 TRP A 435      -1.014  16.684 -40.665  1.00 55.50           C  
ANISOU 1610  CH2 TRP A 435     5846   8535   6707    777   -349   -980       C  
ATOM   1611  N   LEU A 436       3.859  16.838 -37.221  1.00 43.27           N  
ANISOU 1611  N   LEU A 436     4582   6590   5269    887   -406   -852       N  
ATOM   1612  CA  LEU A 436       3.309  18.049 -36.609  1.00 46.53           C  
ANISOU 1612  CA  LEU A 436     5006   6991   5683    883   -402   -791       C  
ATOM   1613  C   LEU A 436       4.359  19.145 -36.570  1.00 53.46           C  
ANISOU 1613  C   LEU A 436     5885   7887   6542    902   -420   -735       C  
ATOM   1614  O   LEU A 436       4.079  20.294 -36.916  1.00 56.15           O  
ANISOU 1614  O   LEU A 436     6201   8267   6864    906   -415   -690       O  
ATOM   1615  CB  LEU A 436       2.802  17.776 -35.197  1.00 42.52           C  
ANISOU 1615  CB  LEU A 436     4567   6379   5209    869   -383   -783       C  
ATOM   1616  CG  LEU A 436       1.735  16.700 -35.047  1.00 44.79           C  
ANISOU 1616  CG  LEU A 436     4867   6633   5517    841   -357   -839       C  
ATOM   1617  CD1 LEU A 436       1.684  16.286 -33.609  1.00 48.90           C  
ANISOU 1617  CD1 LEU A 436     5465   7043   6071    837   -341   -829       C  
ATOM   1618  CD2 LEU A 436       0.384  17.218 -35.513  1.00 50.78           C  
ANISOU 1618  CD2 LEU A 436     5577   7457   6260    819   -345   -837       C  
ATOM   1619  N   TRP A 437       5.572  18.782 -36.152  1.00 48.80           N  
ANISOU 1619  N   TRP A 437     5322   7270   5948    916   -435   -737       N  
ATOM   1620  CA  TRP A 437       6.690  19.728 -36.125  1.00 42.78           C  
ANISOU 1620  CA  TRP A 437     4558   6538   5159    922   -451   -696       C  
ATOM   1621  C   TRP A 437       7.001  20.291 -37.523  1.00 41.93           C  
ANISOU 1621  C   TRP A 437     4385   6528   5019    931   -465   -692       C  
ATOM   1622  O   TRP A 437       7.212  21.493 -37.670  1.00 50.14           O  
ANISOU 1622  O   TRP A 437     5419   7592   6039    925   -458   -647       O  
ATOM   1623  CB  TRP A 437       7.938  19.095 -35.482  1.00 37.72           C  
ANISOU 1623  CB  TRP A 437     3944   5878   4508    939   -465   -704       C  
ATOM   1624  CG  TRP A 437       9.142  20.010 -35.451  1.00 45.14           C  
ANISOU 1624  CG  TRP A 437     4874   6867   5408    934   -480   -671       C  
ATOM   1625  CD1 TRP A 437       9.448  20.933 -34.488  1.00 48.32           C  
ANISOU 1625  CD1 TRP A 437     5310   7247   5800    907   -469   -634       C  
ATOM   1626  CD2 TRP A 437      10.195  20.077 -36.421  1.00 44.20           C  
ANISOU 1626  CD2 TRP A 437     4709   6833   5252    949   -505   -679       C  
ATOM   1627  NE1 TRP A 437      10.619  21.573 -34.800  1.00 45.51           N  
ANISOU 1627  NE1 TRP A 437     4932   6959   5399    897   -482   -621       N  
ATOM   1628  CE2 TRP A 437      11.099  21.073 -35.981  1.00 49.74           C  
ANISOU 1628  CE2 TRP A 437     5419   7563   5919    926   -507   -646       C  
ATOM   1629  CE3 TRP A 437      10.461  19.412 -37.617  1.00 51.51           C  
ANISOU 1629  CE3 TRP A 437     5587   7818   6167    974   -523   -714       C  
ATOM   1630  CZ2 TRP A 437      12.248  21.410 -36.698  1.00 57.88           C  
ANISOU 1630  CZ2 TRP A 437     6409   8679   6903    927   -528   -646       C  
ATOM   1631  CZ3 TRP A 437      11.607  19.747 -38.335  1.00 57.15           C  
ANISOU 1631  CZ3 TRP A 437     6260   8614   6838    983   -548   -710       C  
ATOM   1632  CH2 TRP A 437      12.485  20.736 -37.872  1.00 59.43           C  
ANISOU 1632  CH2 TRP A 437     6558   8932   7093    959   -551   -675       C  
ATOM   1633  N   MET A 438       7.026  19.433 -38.542  1.00 46.90           N  
ANISOU 1633  N   MET A 438     4969   7210   5641    943   -478   -739       N  
ATOM   1634  CA  MET A 438       7.250  19.888 -39.922  1.00 46.64           C  
ANISOU 1634  CA  MET A 438     4867   7280   5576    953   -492   -738       C  
ATOM   1635  C   MET A 438       6.271  20.995 -40.317  1.00 50.50           C  
ANISOU 1635  C   MET A 438     5328   7805   6055    950   -471   -694       C  
ATOM   1636  O   MET A 438       6.677  22.068 -40.752  1.00 53.28           O  
ANISOU 1636  O   MET A 438     5663   8197   6382    959   -469   -648       O  
ATOM   1637  CB  MET A 438       7.125  18.728 -40.901  1.00 54.27           C  
ANISOU 1637  CB  MET A 438     5786   8294   6538    957   -500   -804       C  
ATOM   1638  CG  MET A 438       8.092  17.586 -40.644  1.00 64.45           C  
ANISOU 1638  CG  MET A 438     7106   9547   7834    973   -509   -844       C  
ATOM   1639  SD  MET A 438       9.666  17.758 -41.498  1.00 99.64           S  
ANISOU 1639  SD  MET A 438    11522  14088  12250   1000   -544   -840       S  
ATOM   1640  CE  MET A 438       9.149  17.479 -43.185  1.00102.67           C  
ANISOU 1640  CE  MET A 438    11819  14576  12616    994   -549   -887       C  
ATOM   1641  N   HIS A 439       4.978  20.736 -40.151  1.00 47.83           N  
ANISOU 1641  N   HIS A 439     4986   7454   5732    942   -451   -705       N  
ATOM   1642  CA  HIS A 439       3.957  21.728 -40.470  1.00 43.16           C  
ANISOU 1642  CA  HIS A 439     4366   6906   5126    952   -426   -656       C  
ATOM   1643  C   HIS A 439       4.122  23.020 -39.685  1.00 50.76           C  
ANISOU 1643  C   HIS A 439     5384   7808   6093    957   -402   -584       C  
ATOM   1644  O   HIS A 439       4.130  24.103 -40.270  1.00 54.10           O  
ANISOU 1644  O   HIS A 439     5787   8276   6491    979   -382   -531       O  
ATOM   1645  CB  HIS A 439       2.569  21.154 -40.223  1.00 52.51           C  
ANISOU 1645  CB  HIS A 439     5542   8088   6323    938   -408   -684       C  
ATOM   1646  CG  HIS A 439       2.072  20.297 -41.347  1.00 60.24           C  
ANISOU 1646  CG  HIS A 439     6444   9168   7279    927   -415   -745       C  
ATOM   1647  ND1 HIS A 439       2.553  19.039 -41.585  1.00 61.19           N  
ANISOU 1647  ND1 HIS A 439     6563   9278   7408    905   -429   -821       N  
ATOM   1648  CD2 HIS A 439       1.134  20.542 -42.294  1.00 55.81           C  
ANISOU 1648  CD2 HIS A 439     5800   8726   6678    935   -404   -742       C  
ATOM   1649  CE1 HIS A 439       1.933  18.527 -42.642  1.00 60.78           C  
ANISOU 1649  CE1 HIS A 439     6434   9331   7327    888   -425   -872       C  
ATOM   1650  NE2 HIS A 439       1.069  19.414 -43.079  1.00 59.94           N  
ANISOU 1650  NE2 HIS A 439     6272   9313   7188    905   -414   -825       N  
ATOM   1651  N   LEU A 440       4.239  22.909 -38.361  1.00 39.34           N  
ANISOU 1651  N   LEU A 440     4010   6261   4677    937   -395   -583       N  
ATOM   1652  CA  LEU A 440       4.404  24.090 -37.525  1.00 40.18           C  
ANISOU 1652  CA  LEU A 440     4175   6305   4787    929   -365   -525       C  
ATOM   1653  C   LEU A 440       5.552  24.959 -38.043  1.00 43.53           C  
ANISOU 1653  C   LEU A 440     4594   6763   5181    928   -363   -497       C  
ATOM   1654  O   LEU A 440       5.460  26.186 -38.058  1.00 48.04           O  
ANISOU 1654  O   LEU A 440     5189   7324   5741    931   -322   -443       O  
ATOM   1655  CB  LEU A 440       4.628  23.697 -36.053  1.00 45.04           C  
ANISOU 1655  CB  LEU A 440     4859   6823   5432    901   -366   -538       C  
ATOM   1656  CG  LEU A 440       3.391  23.200 -35.292  1.00 42.31           C  
ANISOU 1656  CG  LEU A 440     4536   6422   5117    895   -352   -548       C  
ATOM   1657  CD1 LEU A 440       3.755  22.349 -34.078  1.00 41.73           C  
ANISOU 1657  CD1 LEU A 440     4515   6271   5071    876   -364   -577       C  
ATOM   1658  CD2 LEU A 440       2.500  24.368 -34.903  1.00 38.77           C  
ANISOU 1658  CD2 LEU A 440     4114   5945   4670    900   -308   -490       C  
ATOM   1659  N   MET A 441       6.632  24.310 -38.466  1.00 39.63           N  
ANISOU 1659  N   MET A 441     4075   6309   4673    925   -402   -536       N  
ATOM   1660  CA  MET A 441       7.776  25.014 -39.034  1.00 55.74           C  
ANISOU 1660  CA  MET A 441     6102   8396   6679    920   -406   -519       C  
ATOM   1661  C   MET A 441       7.350  25.922 -40.183  1.00 62.86           C  
ANISOU 1661  C   MET A 441     6963   9361   7558    946   -381   -476       C  
ATOM   1662  O   MET A 441       7.918  26.996 -40.382  1.00 67.53           O  
ANISOU 1662  O   MET A 441     7574   9958   8128    938   -353   -437       O  
ATOM   1663  CB  MET A 441       8.833  24.018 -39.514  1.00 50.19           C  
ANISOU 1663  CB  MET A 441     5363   7747   5961    925   -454   -568       C  
ATOM   1664  CG  MET A 441       9.793  23.560 -38.428  1.00 51.50           C  
ANISOU 1664  CG  MET A 441     5570   7871   6126    906   -470   -587       C  
ATOM   1665  SD  MET A 441      10.786  24.910 -37.762  1.00 57.54           S  
ANISOU 1665  SD  MET A 441     6377   8627   6858    859   -444   -550       S  
ATOM   1666  CE  MET A 441      10.706  24.555 -36.008  1.00116.50           C  
ANISOU 1666  CE  MET A 441    13908  16010  14347    835   -435   -555       C  
ATOM   1667  N   LEU A 442       6.347  25.483 -40.937  1.00 63.70           N  
ANISOU 1667  N   LEU A 442     7015   9523   7665    977   -385   -484       N  
ATOM   1668  CA  LEU A 442       6.130  25.982 -42.289  1.00 65.17           C  
ANISOU 1668  CA  LEU A 442     7134   9810   7819   1012   -377   -457       C  
ATOM   1669  C   LEU A 442       5.225  27.210 -42.285  1.00 74.14           C  
ANISOU 1669  C   LEU A 442     8288  10936   8947   1042   -316   -379       C  
ATOM   1670  O   LEU A 442       4.975  27.812 -43.329  1.00 83.50           O  
ANISOU 1670  O   LEU A 442     9424  12202  10100   1083   -296   -337       O  
ATOM   1671  CB  LEU A 442       5.528  24.888 -43.174  1.00 58.26           C  
ANISOU 1671  CB  LEU A 442     6178   9023   6936   1026   -409   -509       C  
ATOM   1672  CG  LEU A 442       6.477  23.770 -43.609  1.00 56.09           C  
ANISOU 1672  CG  LEU A 442     5874   8781   6659   1011   -458   -579       C  
ATOM   1673  CD1 LEU A 442       5.725  22.696 -44.380  1.00 47.96           C  
ANISOU 1673  CD1 LEU A 442     4774   7825   5622   1012   -473   -638       C  
ATOM   1674  CD2 LEU A 442       7.623  24.329 -44.439  1.00 58.58           C  
ANISOU 1674  CD2 LEU A 442     6162   9155   6941   1020   -472   -561       C  
ATOM   1675  N   ILE A 443       4.737  27.575 -41.104  1.00 63.04           N  
ANISOU 1675  N   ILE A 443     6953   9431   7567   1028   -283   -357       N  
ATOM   1676  CA  ILE A 443       3.464  28.277 -40.985  1.00 64.90           C  
ANISOU 1676  CA  ILE A 443     7198   9660   7802   1066   -231   -298       C  
ATOM   1677  C   ILE A 443       3.663  29.788 -41.021  1.00 79.10           C  
ANISOU 1677  C   ILE A 443     9048  11421   9585   1086   -160   -218       C  
ATOM   1678  O   ILE A 443       4.735  30.291 -40.687  1.00 73.13           O  
ANISOU 1678  O   ILE A 443     8345  10610   8830   1046   -147   -219       O  
ATOM   1679  CB  ILE A 443       2.729  27.896 -39.687  1.00 51.66           C  
ANISOU 1679  CB  ILE A 443     5573   7895   6162   1043   -225   -313       C  
ATOM   1680  CG1 ILE A 443       1.891  26.633 -39.899  1.00 46.40           C  
ANISOU 1680  CG1 ILE A 443     4846   7283   5499   1044   -264   -370       C  
ATOM   1681  CG2 ILE A 443       1.856  29.047 -39.211  1.00 34.17           C  
ANISOU 1681  CG2 ILE A 443     3406   5629   3946   1074   -154   -237       C  
ATOM   1682  CD1 ILE A 443       1.116  26.202 -38.673  1.00 48.88           C  
ANISOU 1682  CD1 ILE A 443     5208   7516   5848   1021   -258   -386       C  
ATOM   1683  N   LYS A 444       2.622  30.507 -41.429  1.00 95.43           N  
ANISOU 1683  N   LYS A 444    11101  13524  11635   1147   -107   -150       N  
ATOM   1684  CA  LYS A 444       2.791  31.811 -42.059  1.00 96.28           C  
ANISOU 1684  CA  LYS A 444    11228  13640  11715   1191    -37    -69       C  
ATOM   1685  C   LYS A 444       4.117  31.894 -42.808  1.00 96.82           C  
ANISOU 1685  C   LYS A 444    11279  13744  11764   1165    -61    -90       C  
ATOM   1686  O   LYS A 444       5.111  32.389 -42.277  1.00100.67           O  
ANISOU 1686  O   LYS A 444    11837  14152  12260   1111    -41    -97       O  
ATOM   1687  CB  LYS A 444       2.707  32.926 -41.014  1.00 93.84           C  
ANISOU 1687  CB  LYS A 444    11033  13196  11425   1178     46    -18       C  
ATOM   1688  CG  LYS A 444       2.577  32.427 -39.584  1.00 96.14           C  
ANISOU 1688  CG  LYS A 444    11383  13389  11758   1120     26    -65       C  
ATOM   1689  CD  LYS A 444       1.673  33.332 -38.763  1.00 92.63           C  
ANISOU 1689  CD  LYS A 444    11015  12855  11327   1145    109     -3       C  
ATOM   1690  CE  LYS A 444       2.003  33.247 -37.282  1.00 88.39           C  
ANISOU 1690  CE  LYS A 444    10560  12197  10827   1068    110    -43       C  
ATOM   1691  NZ  LYS A 444       2.420  31.874 -36.884  1.00 80.55           N  
ANISOU 1691  NZ  LYS A 444     9529  11223   9853   1018     15   -129       N  
ATOM   1692  N   GLU A 455       2.395  30.997 -51.091  1.00137.27           N  
ANISOU 1692  N   GLU A 455    15942  19586  16628   1540      3    165       N  
ATOM   1693  CA  GLU A 455       3.503  31.272 -50.184  1.00128.16           C  
ANISOU 1693  CA  GLU A 455    14736  18470  15490   1464    -97     49       C  
ATOM   1694  C   GLU A 455       3.057  31.189 -48.728  1.00122.81           C  
ANISOU 1694  C   GLU A 455    14101  17701  14861   1398   -137    -28       C  
ATOM   1695  O   GLU A 455       3.864  31.346 -47.811  1.00125.02           O  
ANISOU 1695  O   GLU A 455    14438  17885  15180   1326   -175    -92       O  
ATOM   1696  CB  GLU A 455       4.102  32.650 -50.472  1.00121.35           C  
ANISOU 1696  CB  GLU A 455    13912  17557  14638   1414   -116     23       C  
ATOM   1697  N   ARG A 456       1.768  30.941 -48.522  1.00113.08           N  
ANISOU 1697  N   ARG A 456    12837  16506  13620   1427   -125    -18       N  
ATOM   1698  CA  ARG A 456       1.096  31.348 -47.294  1.00104.94           C  
ANISOU 1698  CA  ARG A 456    11900  15350  12624   1426    -79     13       C  
ATOM   1699  C   ARG A 456       0.376  30.171 -46.643  1.00 92.54           C  
ANISOU 1699  C   ARG A 456    10307  13780  11075   1381   -127    -64       C  
ATOM   1700  O   ARG A 456      -0.559  29.611 -47.214  1.00 97.36           O  
ANISOU 1700  O   ARG A 456    10821  14525  11648   1404   -143    -80       O  
ATOM   1701  CB  ARG A 456       0.105  32.480 -47.574  1.00101.21           C  
ANISOU 1701  CB  ARG A 456    11429  14911  12113   1525     10    133       C  
ATOM   1702  N   TYR A 457       0.819  29.802 -45.446  1.00 72.29           N  
ANISOU 1702  N   TYR A 457     7831  11071   8565   1315   -145   -112       N  
ATOM   1703  CA  TYR A 457       0.291  28.629 -44.761  1.00 61.73           C  
ANISOU 1703  CA  TYR A 457     6486   9715   7254   1265   -189   -192       C  
ATOM   1704  C   TYR A 457       0.003  28.929 -43.294  1.00 58.48           C  
ANISOU 1704  C   TYR A 457     6179   9154   6888   1242   -160   -177       C  
ATOM   1705  O   TYR A 457       0.920  29.032 -42.479  1.00 64.85           O  
ANISOU 1705  O   TYR A 457     7069   9839   7731   1197   -163   -192       O  
ATOM   1706  CB  TYR A 457       1.268  27.457 -44.875  1.00 60.89           C  
ANISOU 1706  CB  TYR A 457     6364   9602   7168   1200   -259   -291       C  
ATOM   1707  CG  TYR A 457       0.777  26.184 -44.222  1.00 56.80           C  
ANISOU 1707  CG  TYR A 457     5847   9056   6678   1150   -294   -374       C  
ATOM   1708  CD1 TYR A 457      -0.525  25.741 -44.411  1.00 62.13           C  
ANISOU 1708  CD1 TYR A 457     6460   9817   7330   1158   -287   -390       C  
ATOM   1709  CD2 TYR A 457       1.617  25.426 -43.416  1.00 48.93           C  
ANISOU 1709  CD2 TYR A 457     4912   7954   5726   1095   -327   -435       C  
ATOM   1710  CE1 TYR A 457      -0.978  24.579 -43.816  1.00 62.71           C  
ANISOU 1710  CE1 TYR A 457     6542   9858   7429   1104   -310   -469       C  
ATOM   1711  CE2 TYR A 457       1.173  24.263 -42.817  1.00 47.07           C  
ANISOU 1711  CE2 TYR A 457     4686   7682   5517   1053   -348   -506       C  
ATOM   1712  CZ  TYR A 457      -0.125  23.844 -43.020  1.00 57.16           C  
ANISOU 1712  CZ  TYR A 457     5910   9033   6776   1054   -338   -525       C  
ATOM   1713  OH  TYR A 457      -0.572  22.686 -42.426  1.00 53.77           O  
ANISOU 1713  OH  TYR A 457     5497   8562   6372   1005   -350   -599       O  
ATOM   1714  N   SER A 458      -1.277  29.069 -42.964  1.00 58.35           N  
ANISOU 1714  N   SER A 458     6151   9158   6862   1273   -131   -148       N  
ATOM   1715  CA  SER A 458      -1.680  29.584 -41.661  1.00 57.12           C  
ANISOU 1715  CA  SER A 458     6091   8873   6739   1270    -87   -111       C  
ATOM   1716  C   SER A 458      -1.953  28.448 -40.680  1.00 56.33           C  
ANISOU 1716  C   SER A 458     6012   8712   6678   1207   -129   -189       C  
ATOM   1717  O   SER A 458      -2.124  27.297 -41.080  1.00 52.04           O  
ANISOU 1717  O   SER A 458     5404   8240   6129   1176   -179   -263       O  
ATOM   1718  CB  SER A 458      -2.920  30.471 -41.795  1.00 59.26           C  
ANISOU 1718  CB  SER A 458     6341   9205   6972   1355    -20    -19       C  
ATOM   1719  OG  SER A 458      -4.069  29.699 -42.098  1.00 64.16           O  
ANISOU 1719  OG  SER A 458     6872   9943   7562   1362    -46    -51       O  
ATOM   1720  N   LEU A 459      -1.991  28.780 -39.394  1.00 51.06           N  
ANISOU 1720  N   LEU A 459     5440   7911   6050   1185   -103   -173       N  
ATOM   1721  CA  LEU A 459      -2.393  27.826 -38.368  1.00 49.01           C  
ANISOU 1721  CA  LEU A 459     5208   7588   5827   1132   -134   -235       C  
ATOM   1722  C   LEU A 459      -3.770  27.243 -38.666  1.00 51.48           C  
ANISOU 1722  C   LEU A 459     5444   8004   6112   1148   -141   -253       C  
ATOM   1723  O   LEU A 459      -3.944  26.025 -38.706  1.00 55.04           O  
ANISOU 1723  O   LEU A 459     5858   8484   6569   1102   -185   -334       O  
ATOM   1724  CB  LEU A 459      -2.390  28.489 -36.989  1.00 44.58           C  
ANISOU 1724  CB  LEU A 459     4751   6885   5303   1116    -95   -202       C  
ATOM   1725  CG  LEU A 459      -2.770  27.595 -35.806  1.00 55.58           C  
ANISOU 1725  CG  LEU A 459     6174   8211   6734   1064   -126   -262       C  
ATOM   1726  CD1 LEU A 459      -1.818  26.414 -35.698  1.00 46.72           C  
ANISOU 1726  CD1 LEU A 459     5049   7070   5634   1010   -187   -344       C  
ATOM   1727  CD2 LEU A 459      -2.789  28.395 -34.512  1.00 50.67           C  
ANISOU 1727  CD2 LEU A 459     5649   7461   6143   1050    -86   -227       C  
ATOM   1728  N   GLU A 460      -4.746  28.121 -38.876  1.00 55.10           N  
ANISOU 1728  N   GLU A 460     5879   8523   6535   1214    -90   -177       N  
ATOM   1729  CA  GLU A 460      -6.091  27.697 -39.266  1.00 57.52           C  
ANISOU 1729  CA  GLU A 460     6098   8962   6796   1237    -89   -183       C  
ATOM   1730  C   GLU A 460      -6.075  26.668 -40.409  1.00 57.38           C  
ANISOU 1730  C   GLU A 460     5972   9090   6742   1211   -136   -256       C  
ATOM   1731  O   GLU A 460      -6.869  25.723 -40.418  1.00 61.49           O  
ANISOU 1731  O   GLU A 460     6439   9681   7246   1172   -156   -321       O  
ATOM   1732  CB  GLU A 460      -6.923  28.916 -39.679  1.00 70.26           C  
ANISOU 1732  CB  GLU A 460     7686  10653   8358   1336    -23    -72       C  
ATOM   1733  CG  GLU A 460      -7.215  29.899 -38.546  1.00 89.16           C  
ANISOU 1733  CG  GLU A 460    10183  12912  10781   1365     38     -1       C  
ATOM   1734  CD  GLU A 460      -5.981  30.657 -38.065  1.00101.81           C  
ANISOU 1734  CD  GLU A 460    11895  14358  12431   1346     63     22       C  
ATOM   1735  OE1 GLU A 460      -5.040  30.854 -38.871  1.00 96.51           O  
ANISOU 1735  OE1 GLU A 460    11209  13710  11750   1349     55     24       O  
ATOM   1736  OE2 GLU A 460      -5.961  31.060 -36.876  1.00109.95           O  
ANISOU 1736  OE2 GLU A 460    13023  15250  13502   1323     92     35       O  
ATOM   1737  N   ASP A 461      -5.168  26.852 -41.367  1.00 42.27           N  
ANISOU 1737  N   ASP A 461     4027   7221   4814   1226   -149   -252       N  
ATOM   1738  CA  ASP A 461      -4.968  25.880 -42.436  1.00 55.63           C  
ANISOU 1738  CA  ASP A 461     5626   9036   6476   1194   -193   -328       C  
ATOM   1739  C   ASP A 461      -4.448  24.555 -41.887  1.00 61.26           C  
ANISOU 1739  C   ASP A 461     6376   9663   7238   1105   -239   -436       C  
ATOM   1740  O   ASP A 461      -4.911  23.489 -42.300  1.00 68.54           O  
ANISOU 1740  O   ASP A 461     7235  10667   8141   1060   -259   -517       O  
ATOM   1741  CB  ASP A 461      -3.992  26.419 -43.491  1.00 64.56           C  
ANISOU 1741  CB  ASP A 461     6727  10217   7587   1229   -197   -295       C  
ATOM   1742  CG  ASP A 461      -4.532  27.628 -44.230  1.00 69.93           C  
ANISOU 1742  CG  ASP A 461     7358  11002   8208   1326   -145   -187       C  
ATOM   1743  OD1 ASP A 461      -5.765  27.709 -44.431  1.00 73.88           O  
ANISOU 1743  OD1 ASP A 461     7791  11621   8659   1365   -121   -159       O  
ATOM   1744  OD2 ASP A 461      -3.717  28.490 -44.621  1.00 73.41           O  
ANISOU 1744  OD2 ASP A 461     7828  11414   8650   1364   -124   -128       O  
ATOM   1745  N   PHE A 462      -3.481  24.624 -40.967  1.00 53.66           N  
ANISOU 1745  N   PHE A 462     5515   8539   6334   1081   -248   -438       N  
ATOM   1746  CA  PHE A 462      -2.956  23.425 -40.315  1.00 40.66           C  
ANISOU 1746  CA  PHE A 462     3915   6799   4734   1014   -282   -525       C  
ATOM   1747  C   PHE A 462      -4.054  22.699 -39.553  1.00 33.90           C  
ANISOU 1747  C   PHE A 462     3069   5922   3889    976   -274   -567       C  
ATOM   1748  O   PHE A 462      -4.193  21.478 -39.638  1.00 42.77           O  
ANISOU 1748  O   PHE A 462     4175   7057   5018    923   -291   -654       O  
ATOM   1749  CB  PHE A 462      -1.796  23.766 -39.373  1.00 49.89           C  
ANISOU 1749  CB  PHE A 462     5184   7819   5951   1004   -288   -506       C  
ATOM   1750  CG  PHE A 462      -1.134  22.553 -38.757  1.00 57.63           C  
ANISOU 1750  CG  PHE A 462     6209   8716   6972    952   -319   -582       C  
ATOM   1751  CD1 PHE A 462      -0.894  21.424 -39.520  1.00 55.19           C  
ANISOU 1751  CD1 PHE A 462     5852   8464   6654    927   -344   -659       C  
ATOM   1752  CD2 PHE A 462      -0.748  22.545 -37.422  1.00 59.94           C  
ANISOU 1752  CD2 PHE A 462     6592   8876   7308    933   -317   -576       C  
ATOM   1753  CE1 PHE A 462      -0.298  20.311 -38.970  1.00 54.35           C  
ANISOU 1753  CE1 PHE A 462     5794   8276   6583    892   -360   -721       C  
ATOM   1754  CE2 PHE A 462      -0.135  21.434 -36.867  1.00 54.95           C  
ANISOU 1754  CE2 PHE A 462     5998   8174   6706    900   -339   -635       C  
ATOM   1755  CZ  PHE A 462       0.089  20.318 -37.637  1.00 56.34           C  
ANISOU 1755  CZ  PHE A 462     6132   8398   6874    884   -358   -705       C  
ATOM   1756  N   GLN A 463      -4.848  23.462 -38.820  1.00 37.12           N  
ANISOU 1756  N   GLN A 463     3508   6298   4299   1003   -243   -505       N  
ATOM   1757  CA  GLN A 463      -5.959  22.901 -38.054  1.00 41.30           C  
ANISOU 1757  CA  GLN A 463     4045   6812   4834    971   -233   -536       C  
ATOM   1758  C   GLN A 463      -6.995  22.222 -38.962  1.00 55.20           C  
ANISOU 1758  C   GLN A 463     5699   8739   6537    951   -232   -589       C  
ATOM   1759  O   GLN A 463      -7.480  21.130 -38.657  1.00 60.25           O  
ANISOU 1759  O   GLN A 463     6337   9372   7184    886   -237   -670       O  
ATOM   1760  CB  GLN A 463      -6.613  23.997 -37.222  1.00 42.20           C  
ANISOU 1760  CB  GLN A 463     4205   6876   4951   1014   -195   -451       C  
ATOM   1761  CG  GLN A 463      -5.660  24.653 -36.238  1.00 51.98           C  
ANISOU 1761  CG  GLN A 463     5551   7956   6243   1017   -187   -411       C  
ATOM   1762  CD  GLN A 463      -6.261  25.872 -35.535  1.00 48.50           C  
ANISOU 1762  CD  GLN A 463     5159   7467   5803   1063   -137   -323       C  
ATOM   1763  OE1 GLN A 463      -6.995  26.656 -36.133  1.00 52.97           O  
ANISOU 1763  OE1 GLN A 463     5678   8126   6324   1125   -101   -259       O  
ATOM   1764  NE2 GLN A 463      -5.921  26.043 -34.268  1.00 44.05           N  
ANISOU 1764  NE2 GLN A 463     4688   6761   5287   1035   -130   -318       N  
ATOM   1765  N   ASN A 464      -7.335  22.875 -40.072  1.00 53.23           N  
ANISOU 1765  N   ASN A 464     5357   8642   6224   1004   -220   -543       N  
ATOM   1766  CA  ASN A 464      -8.228  22.283 -41.059  1.00 49.40           C  
ANISOU 1766  CA  ASN A 464     4754   8347   5670    983   -220   -594       C  
ATOM   1767  C   ASN A 464      -7.774  20.893 -41.471  1.00 46.16           C  
ANISOU 1767  C   ASN A 464     4327   7940   5271    898   -246   -715       C  
ATOM   1768  O   ASN A 464      -8.566  19.947 -41.446  1.00 43.50           O  
ANISOU 1768  O   ASN A 464     3956   7656   4914    831   -239   -797       O  
ATOM   1769  CB  ASN A 464      -8.317  23.160 -42.306  1.00 52.92           C  
ANISOU 1769  CB  ASN A 464     5103   8958   6047   1059   -208   -526       C  
ATOM   1770  CG  ASN A 464      -9.205  24.365 -42.109  1.00 52.24           C  
ANISOU 1770  CG  ASN A 464     5003   8923   5922   1147   -165   -413       C  
ATOM   1771  OD1 ASN A 464     -10.055  24.394 -41.219  1.00 49.20           O  
ANISOU 1771  OD1 ASN A 464     4648   8502   5542   1141   -146   -402       O  
ATOM   1772  ND2 ASN A 464      -9.011  25.372 -42.945  1.00 56.24           N  
ANISOU 1772  ND2 ASN A 464     5467   9513   6387   1233   -143   -325       N  
ATOM   1773  N   ILE A 465      -6.504  20.779 -41.860  1.00 39.93           N  
ANISOU 1773  N   ILE A 465     3564   7096   4511    901   -270   -727       N  
ATOM   1774  CA  ILE A 465      -5.937  19.495 -42.249  1.00 41.11           C  
ANISOU 1774  CA  ILE A 465     3711   7234   4677    832   -288   -835       C  
ATOM   1775  C   ILE A 465      -6.108  18.471 -41.141  1.00 50.54           C  
ANISOU 1775  C   ILE A 465     4990   8291   5923    766   -280   -903       C  
ATOM   1776  O   ILE A 465      -6.513  17.332 -41.383  1.00 48.67           O  
ANISOU 1776  O   ILE A 465     4731   8088   5675    694   -267  -1001       O  
ATOM   1777  CB  ILE A 465      -4.432  19.605 -42.574  1.00 43.21           C  
ANISOU 1777  CB  ILE A 465     4013   7432   4974    855   -315   -825       C  
ATOM   1778  CG1 ILE A 465      -4.202  20.520 -43.783  1.00 45.60           C  
ANISOU 1778  CG1 ILE A 465     4230   7873   5224    915   -321   -766       C  
ATOM   1779  CG2 ILE A 465      -3.856  18.231 -42.858  1.00 42.66           C  
ANISOU 1779  CG2 ILE A 465     3954   7332   4924    792   -325   -933       C  
ATOM   1780  CD1 ILE A 465      -2.742  20.712 -44.138  1.00 42.54           C  
ANISOU 1780  CD1 ILE A 465     3871   7432   4860    936   -347   -753       C  
ATOM   1781  N   ILE A 466      -5.797  18.881 -39.916  1.00 51.39           N  
ANISOU 1781  N   ILE A 466     5196   8245   6085    788   -280   -851       N  
ATOM   1782  CA  ILE A 466      -5.877  17.974 -38.786  1.00 46.30           C  
ANISOU 1782  CA  ILE A 466     4637   7462   5491    736   -271   -902       C  
ATOM   1783  C   ILE A 466      -7.290  17.466 -38.625  1.00 45.41           C  
ANISOU 1783  C   ILE A 466     4489   7415   5349    684   -244   -949       C  
ATOM   1784  O   ILE A 466      -7.530  16.263 -38.601  1.00 52.12           O  
ANISOU 1784  O   ILE A 466     5350   8247   6205    612   -227  -1044       O  
ATOM   1785  CB  ILE A 466      -5.408  18.645 -37.490  1.00 47.14           C  
ANISOU 1785  CB  ILE A 466     4842   7418   5651    771   -275   -831       C  
ATOM   1786  CG1 ILE A 466      -3.881  18.688 -37.455  1.00 45.99           C  
ANISOU 1786  CG1 ILE A 466     4746   7190   5538    793   -298   -818       C  
ATOM   1787  CG2 ILE A 466      -5.937  17.904 -36.274  1.00 41.61           C  
ANISOU 1787  CG2 ILE A 466     4213   6609   4989    725   -258   -866       C  
ATOM   1788  CD1 ILE A 466      -3.343  19.709 -36.493  1.00 46.42           C  
ANISOU 1788  CD1 ILE A 466     4869   7146   5621    830   -301   -737       C  
ATOM   1789  N   ILE A 467      -8.229  18.393 -38.513  1.00 49.22           N  
ANISOU 1789  N   ILE A 467     4931   7974   5796    721   -234   -883       N  
ATOM   1790  CA  ILE A 467      -9.622  18.039 -38.318  1.00 46.09           C  
ANISOU 1790  CA  ILE A 467     4492   7658   5361    677   -210   -919       C  
ATOM   1791  C   ILE A 467     -10.111  17.206 -39.502  1.00 52.33           C  
ANISOU 1791  C   ILE A 467     5180   8616   6087    615   -199  -1013       C  
ATOM   1792  O   ILE A 467     -10.812  16.208 -39.329  1.00 57.46           O  
ANISOU 1792  O   ILE A 467     5825   9281   6725    530   -176  -1103       O  
ATOM   1793  CB  ILE A 467     -10.472  19.304 -38.194  1.00 53.81           C  
ANISOU 1793  CB  ILE A 467     5430   8718   6298    748   -198   -818       C  
ATOM   1794  CG1 ILE A 467     -10.121  20.050 -36.905  1.00 42.74           C  
ANISOU 1794  CG1 ILE A 467     4137   7143   4958    791   -197   -741       C  
ATOM   1795  CG2 ILE A 467     -11.969  18.969 -38.286  1.00 51.14           C  
ANISOU 1795  CG2 ILE A 467     5014   8523   5894    707   -175   -856       C  
ATOM   1796  CD1 ILE A 467     -10.561  21.492 -36.931  1.00 43.79           C  
ANISOU 1796  CD1 ILE A 467     4248   7329   5060    881   -178   -626       C  
ATOM   1797  N   SER A 468      -9.725  17.621 -40.705  1.00 43.38           N  
ANISOU 1797  N   SER A 468     3964   7609   4909    653   -213   -994       N  
ATOM   1798  CA  SER A 468     -10.113  16.922 -41.914  1.00 47.55           C  
ANISOU 1798  CA  SER A 468     4383   8314   5370    595   -204  -1081       C  
ATOM   1799  C   SER A 468      -9.832  15.423 -41.825  1.00 53.66           C  
ANISOU 1799  C   SER A 468     5207   9005   6177    491   -187  -1211       C  
ATOM   1800  O   SER A 468     -10.707  14.613 -42.117  1.00 61.58           O  
ANISOU 1800  O   SER A 468     6159  10106   7134    403   -156  -1305       O  
ATOM   1801  CB  SER A 468      -9.416  17.527 -43.122  1.00 55.13           C  
ANISOU 1801  CB  SER A 468     5270   9382   6296    654   -226  -1041       C  
ATOM   1802  OG  SER A 468      -9.650  16.743 -44.275  1.00 66.06           O  
ANISOU 1802  OG  SER A 468     6554  10926   7619    589   -217  -1137       O  
ATOM   1803  N   TYR A 469      -8.619  15.058 -41.415  1.00 50.64           N  
ANISOU 1803  N   TYR A 469     4926   8446   5870    500   -199  -1217       N  
ATOM   1804  CA  TYR A 469      -8.235  13.649 -41.285  1.00 53.21           C  
ANISOU 1804  CA  TYR A 469     5315   8670   6232    420   -172  -1327       C  
ATOM   1805  C   TYR A 469      -8.855  12.955 -40.063  1.00 62.39           C  
ANISOU 1805  C   TYR A 469     6566   9705   7433    363   -138  -1365       C  
ATOM   1806  O   TYR A 469      -9.103  11.749 -40.084  1.00 70.15           O  
ANISOU 1806  O   TYR A 469     7577  10658   8420    274    -94  -1472       O  
ATOM   1807  CB  TYR A 469      -6.705  13.502 -41.266  1.00 56.18           C  
ANISOU 1807  CB  TYR A 469     5765   8914   6667    464   -194  -1311       C  
ATOM   1808  CG  TYR A 469      -6.056  13.607 -42.631  1.00 60.31           C  
ANISOU 1808  CG  TYR A 469     6207   9556   7153    480   -213  -1326       C  
ATOM   1809  CD1 TYR A 469      -5.480  14.793 -43.060  1.00 59.39           C  
ANISOU 1809  CD1 TYR A 469     6050   9492   7023    566   -254  -1229       C  
ATOM   1810  CD2 TYR A 469      -6.028  12.519 -43.494  1.00 63.41           C  
ANISOU 1810  CD2 TYR A 469     6567  10006   7521    406   -185  -1439       C  
ATOM   1811  CE1 TYR A 469      -4.895  14.892 -44.307  1.00 65.18           C  
ANISOU 1811  CE1 TYR A 469     6708  10337   7721    581   -272  -1241       C  
ATOM   1812  CE2 TYR A 469      -5.439  12.606 -44.749  1.00 55.66           C  
ANISOU 1812  CE2 TYR A 469     5507   9138   6503    420   -203  -1455       C  
ATOM   1813  CZ  TYR A 469      -4.876  13.796 -45.153  1.00 63.75           C  
ANISOU 1813  CZ  TYR A 469     6488  10218   7516    510   -250  -1354       C  
ATOM   1814  OH  TYR A 469      -4.284  13.901 -46.402  1.00 64.68           O  
ANISOU 1814  OH  TYR A 469     6527  10452   7597    525   -269  -1367       O  
ATOM   1815  N   GLY A 470      -9.100  13.710 -38.995  1.00 55.15           N  
ANISOU 1815  N   GLY A 470     5698   8711   6545    413   -152  -1279       N  
ATOM   1816  CA  GLY A 470      -9.749  13.156 -37.818  1.00 52.93           C  
ANISOU 1816  CA  GLY A 470     5493   8321   6297    365   -123  -1306       C  
ATOM   1817  C   GLY A 470      -8.889  12.209 -36.995  1.00 51.04           C  
ANISOU 1817  C   GLY A 470     5381   7877   6134    349   -104  -1340       C  
ATOM   1818  O   GLY A 470      -7.745  11.933 -37.346  1.00 57.86           O  
ANISOU 1818  O   GLY A 470     6275   8684   7025    376   -113  -1345       O  
ATOM   1819  N   PRO A 471      -9.445  11.704 -35.883  1.00 62.34           N  
ANISOU 1819  N   PRO A 471     6888   9202   7598    310    -74  -1358       N  
ATOM   1820  CA  PRO A 471      -8.750  10.794 -34.964  1.00 68.74           C  
ANISOU 1820  CA  PRO A 471     7823   9817   8477    303    -47  -1379       C  
ATOM   1821  C   PRO A 471      -8.271   9.527 -35.658  1.00 73.59           C  
ANISOU 1821  C   PRO A 471     8463  10404   9096    249     -1  -1481       C  
ATOM   1822  O   PRO A 471      -7.278   8.923 -35.253  1.00 80.79           O  
ANISOU 1822  O   PRO A 471     9465  11175  10059    280     14  -1479       O  
ATOM   1823  CB  PRO A 471      -9.838  10.455 -33.927  1.00 66.54           C  
ANISOU 1823  CB  PRO A 471     7589   9486   8208    249    -14  -1399       C  
ATOM   1824  CG  PRO A 471     -11.135  10.829 -34.598  1.00 61.26           C  
ANISOU 1824  CG  PRO A 471     6806   9008   7463    200    -12  -1427       C  
ATOM   1825  CD  PRO A 471     -10.781  12.049 -35.370  1.00 64.26           C  
ANISOU 1825  CD  PRO A 471     7100   9507   7810    281    -65  -1347       C  
ATOM   1826  N   SER A 472      -8.979   9.134 -36.704  1.00 76.78           N  
ANISOU 1826  N   SER A 472     8784  10948   9440    172     25  -1568       N  
ATOM   1827  CA  SER A 472      -8.637   7.938 -37.455  1.00 76.88           C  
ANISOU 1827  CA  SER A 472     8815  10947   9449    107     80  -1677       C  
ATOM   1828  C   SER A 472      -7.156   7.865 -37.832  1.00 74.21           C  
ANISOU 1828  C   SER A 472     8512  10540   9146    180     59  -1648       C  
ATOM   1829  O   SER A 472      -6.541   6.805 -37.742  1.00 78.70           O  
ANISOU 1829  O   SER A 472     9166  10987   9750    165    111  -1701       O  
ATOM   1830  CB  SER A 472      -9.495   7.864 -38.715  1.00 76.63           C  
ANISOU 1830  CB  SER A 472     8657  11125   9333     24     94  -1759       C  
ATOM   1831  OG  SER A 472      -8.880   7.037 -39.687  1.00 83.64           O  
ANISOU 1831  OG  SER A 472     9543  12025  10214    -15    129  -1845       O  
ATOM   1832  N   ARG A 473      -6.587   8.996 -38.238  1.00 71.40           N  
ANISOU 1832  N   ARG A 473     8091  10260   8776    263    -11  -1562       N  
ATOM   1833  CA  ARG A 473      -5.246   9.013 -38.826  1.00 69.22           C  
ANISOU 1833  CA  ARG A 473     7821   9964   8515    324    -35  -1542       C  
ATOM   1834  C   ARG A 473      -4.137   9.436 -37.867  1.00 62.07           C  
ANISOU 1834  C   ARG A 473     6996   8923   7664    419    -70  -1445       C  
ATOM   1835  O   ARG A 473      -3.008   9.685 -38.291  1.00 60.40           O  
ANISOU 1835  O   ARG A 473     6778   8713   7457    479   -101  -1411       O  
ATOM   1836  CB  ARG A 473      -5.225   9.918 -40.064  1.00 77.64           C  
ANISOU 1836  CB  ARG A 473     8760  11217   9524    346    -84  -1519       C  
ATOM   1837  CG  ARG A 473      -6.285   9.568 -41.097  1.00 85.08           C  
ANISOU 1837  CG  ARG A 473     9601  12329  10396    255    -54  -1611       C  
ATOM   1838  CD  ARG A 473      -6.029   8.198 -41.712  1.00 90.30           C  
ANISOU 1838  CD  ARG A 473    10290  12961  11057    178      9  -1735       C  
ATOM   1839  NE  ARG A 473      -5.223   8.286 -42.925  1.00 92.24           N  
ANISOU 1839  NE  ARG A 473    10472  13298  11278    202    -15  -1749       N  
ATOM   1840  CZ  ARG A 473      -5.718   8.627 -44.111  1.00 98.75           C  
ANISOU 1840  CZ  ARG A 473    11165  14327  12030    169    -28  -1781       C  
ATOM   1841  NH1 ARG A 473      -7.011   8.915 -44.227  1.00100.82           N  
ANISOU 1841  NH1 ARG A 473    11345  14730  12233    115    -20  -1799       N  
ATOM   1842  NH2 ARG A 473      -4.927   8.686 -45.177  1.00 98.83           N  
ANISOU 1842  NH2 ARG A 473    11121  14411  12019    194    -50  -1791       N  
ATOM   1843  N   PHE A 474      -4.444   9.526 -36.580  1.00 57.60           N  
ANISOU 1843  N   PHE A 474     6501   8251   7134    430    -64  -1402       N  
ATOM   1844  CA  PHE A 474      -3.424   9.924 -35.614  1.00 62.07           C  
ANISOU 1844  CA  PHE A 474     7136   8705   7743    512    -93  -1315       C  
ATOM   1845  C   PHE A 474      -3.207   8.856 -34.545  1.00 62.46           C  
ANISOU 1845  C   PHE A 474     7302   8589   7840    511    -41  -1333       C  
ATOM   1846  O   PHE A 474      -2.655   9.124 -33.489  1.00 62.86           O  
ANISOU 1846  O   PHE A 474     7412   8551   7923    568    -57  -1263       O  
ATOM   1847  CB  PHE A 474      -3.747  11.299 -35.008  1.00 58.71           C  
ANISOU 1847  CB  PHE A 474     6683   8311   7314    550   -142  -1221       C  
ATOM   1848  CG  PHE A 474      -3.697  12.423 -36.015  1.00 56.74           C  
ANISOU 1848  CG  PHE A 474     6334   8205   7021    577   -187  -1182       C  
ATOM   1849  CD1 PHE A 474      -4.854  12.859 -36.657  1.00 53.16           C  
ANISOU 1849  CD1 PHE A 474     5794   7886   6520    542   -186  -1197       C  
ATOM   1850  CD2 PHE A 474      -2.489  13.020 -36.345  1.00 54.29           C  
ANISOU 1850  CD2 PHE A 474     6013   7903   6710    639   -226  -1130       C  
ATOM   1851  CE1 PHE A 474      -4.805  13.884 -37.593  1.00 47.76           C  
ANISOU 1851  CE1 PHE A 474     5019   7334   5792    578   -220  -1152       C  
ATOM   1852  CE2 PHE A 474      -2.430  14.043 -37.287  1.00 51.58           C  
ANISOU 1852  CE2 PHE A 474     5585   7686   6327    664   -259  -1092       C  
ATOM   1853  CZ  PHE A 474      -3.585  14.477 -37.907  1.00 50.26           C  
ANISOU 1853  CZ  PHE A 474     5337   7644   6117    639   -254  -1099       C  
ATOM   1854  N   SER A 475      -3.638   7.637 -34.848  1.00 70.58           N  
ANISOU 1854  N   SER A 475     8365   9583   8871    444     29  -1429       N  
ATOM   1855  CA  SER A 475      -3.510   6.509 -33.935  1.00 72.90           C  
ANISOU 1855  CA  SER A 475     8777   9715   9207    441     97  -1453       C  
ATOM   1856  C   SER A 475      -3.794   6.890 -32.483  1.00 69.25           C  
ANISOU 1856  C   SER A 475     8368   9167   8776    468     84  -1381       C  
ATOM   1857  O   SER A 475      -4.939   7.148 -32.101  1.00 60.40           O  
ANISOU 1857  O   SER A 475     7231   8072   7648    413     87  -1392       O  
ATOM   1858  CB  SER A 475      -2.119   5.894 -34.044  1.00 78.30           C  
ANISOU 1858  CB  SER A 475     9518  10321   9911    513    115  -1440       C  
ATOM   1859  OG  SER A 475      -2.176   4.509 -33.756  1.00 88.88           O  
ANISOU 1859  OG  SER A 475    10959  11534  11278    486    211  -1503       O  
ATOM   1860  N   ASN A 476      -2.742   6.918 -31.676  1.00 68.09           N  
ANISOU 1860  N   ASN A 476     8282   8931   8659    554     71  -1309       N  
ATOM   1861  CA  ASN A 476      -2.881   7.315 -30.280  1.00 67.18           C  
ANISOU 1861  CA  ASN A 476     8213   8742   8569    584     57  -1238       C  
ATOM   1862  C   ASN A 476      -2.149   8.613 -29.945  1.00 56.88           C  
ANISOU 1862  C   ASN A 476     6867   7487   7257    653    -22  -1141       C  
ATOM   1863  O   ASN A 476      -1.533   8.731 -28.888  1.00 55.53           O  
ANISOU 1863  O   ASN A 476     6746   7248   7105    708    -31  -1078       O  
ATOM   1864  CB  ASN A 476      -2.460   6.182 -29.333  1.00 74.30           C  
ANISOU 1864  CB  ASN A 476     9230   9493   9508    617    123  -1235       C  
ATOM   1865  CG  ASN A 476      -1.071   5.660 -29.625  1.00 91.85           C  
ANISOU 1865  CG  ASN A 476    11484  11682  11732    697    136  -1216       C  
ATOM   1866  OD1 ASN A 476      -0.365   6.169 -30.502  1.00 99.70           O  
ANISOU 1866  OD1 ASN A 476    12413  12766  12701    725     90  -1207       O  
ATOM   1867  ND2 ASN A 476      -0.670   4.630 -28.893  1.00 98.40           N  
ANISOU 1867  ND2 ASN A 476    12413  12386  12588    739    205  -1208       N  
ATOM   1868  N   TYR A 477      -2.239   9.583 -30.852  1.00 50.06           N  
ANISOU 1868  N   TYR A 477     5913   6746   6361    645    -72  -1133       N  
ATOM   1869  CA  TYR A 477      -1.635  10.900 -30.658  1.00 46.27           C  
ANISOU 1869  CA  TYR A 477     5395   6316   5870    695   -135  -1050       C  
ATOM   1870  C   TYR A 477      -2.592  12.037 -31.067  1.00 46.28           C  
ANISOU 1870  C   TYR A 477     5321   6418   5845    665   -166  -1033       C  
ATOM   1871  O   TYR A 477      -2.151  13.132 -31.417  1.00 51.66           O  
ANISOU 1871  O   TYR A 477     5956   7166   6507    697   -208   -981       O  
ATOM   1872  CB  TYR A 477      -0.304  11.007 -31.433  1.00 37.94           C  
ANISOU 1872  CB  TYR A 477     4313   5305   4797    747   -162  -1036       C  
ATOM   1873  CG  TYR A 477       0.695  11.957 -30.804  1.00 40.85           C  
ANISOU 1873  CG  TYR A 477     4683   5678   5162    803   -207   -953       C  
ATOM   1874  CD1 TYR A 477       1.319  11.635 -29.601  1.00 46.75           C  
ANISOU 1874  CD1 TYR A 477     5496   6341   5927    843   -197   -914       C  
ATOM   1875  CD2 TYR A 477       1.010  13.171 -31.403  1.00 37.39           C  
ANISOU 1875  CD2 TYR A 477     4180   5331   4695    813   -253   -916       C  
ATOM   1876  CE1 TYR A 477       2.223  12.498 -29.005  1.00 42.66           C  
ANISOU 1876  CE1 TYR A 477     4972   5842   5395    882   -234   -846       C  
ATOM   1877  CE2 TYR A 477       1.926  14.041 -30.825  1.00 42.48           C  
ANISOU 1877  CE2 TYR A 477     4829   5979   5331    850   -285   -850       C  
ATOM   1878  CZ  TYR A 477       2.527  13.697 -29.618  1.00 49.34           C  
ANISOU 1878  CZ  TYR A 477     5758   6776   6214    879   -276   -819       C  
ATOM   1879  OH  TYR A 477       3.426  14.555 -29.016  1.00 42.18           O  
ANISOU 1879  OH  TYR A 477     4848   5889   5288    903   -304   -762       O  
ATOM   1880  N   TYR A 478      -3.896  11.781 -31.035  1.00 41.64           N  
ANISOU 1880  N   TYR A 478     4723   5846   5253    606   -139  -1075       N  
ATOM   1881  CA  TYR A 478      -4.860  12.789 -31.477  1.00 51.18           C  
ANISOU 1881  CA  TYR A 478     5855   7166   6427    588   -161  -1057       C  
ATOM   1882  C   TYR A 478      -5.114  13.893 -30.429  1.00 55.07           C  
ANISOU 1882  C   TYR A 478     6365   7628   6931    616   -183   -975       C  
ATOM   1883  O   TYR A 478      -5.236  15.072 -30.773  1.00 55.10           O  
ANISOU 1883  O   TYR A 478     6318   7707   6911    642   -209   -922       O  
ATOM   1884  CB  TYR A 478      -6.172  12.139 -31.935  1.00 52.86           C  
ANISOU 1884  CB  TYR A 478     6032   7437   6615    512   -124  -1135       C  
ATOM   1885  CG  TYR A 478      -7.055  13.072 -32.735  1.00 45.68           C  
ANISOU 1885  CG  TYR A 478     5021   6684   5653    504   -144  -1121       C  
ATOM   1886  CD1 TYR A 478      -6.648  13.551 -33.966  1.00 42.54           C  
ANISOU 1886  CD1 TYR A 478     4545   6401   5218    528   -168  -1115       C  
ATOM   1887  CD2 TYR A 478      -8.289  13.484 -32.246  1.00 52.74           C  
ANISOU 1887  CD2 TYR A 478     5896   7615   6530    481   -136  -1106       C  
ATOM   1888  CE1 TYR A 478      -7.442  14.411 -34.699  1.00 51.05           C  
ANISOU 1888  CE1 TYR A 478     5528   7629   6242    534   -180  -1091       C  
ATOM   1889  CE2 TYR A 478      -9.096  14.342 -32.966  1.00 49.40           C  
ANISOU 1889  CE2 TYR A 478     5376   7342   6050    489   -148  -1082       C  
ATOM   1890  CZ  TYR A 478      -8.668  14.801 -34.197  1.00 56.94           C  
ANISOU 1890  CZ  TYR A 478     6254   8413   6968    518   -169  -1072       C  
ATOM   1891  OH  TYR A 478      -9.452  15.652 -34.936  1.00 54.59           O  
ANISOU 1891  OH  TYR A 478     5858   8274   6608    538   -175  -1039       O  
ATOM   1892  N   LEU A 479      -5.177  13.520 -29.156  1.00 47.64           N  
ANISOU 1892  N   LEU A 479     5499   6575   6026    614   -167   -962       N  
ATOM   1893  CA  LEU A 479      -5.316  14.524 -28.108  1.00 46.14           C  
ANISOU 1893  CA  LEU A 479     5332   6350   5848    637   -185   -889       C  
ATOM   1894  C   LEU A 479      -4.129  15.495 -28.131  1.00 44.06           C  
ANISOU 1894  C   LEU A 479     5063   6096   5581    690   -219   -825       C  
ATOM   1895  O   LEU A 479      -4.316  16.725 -28.106  1.00 40.46           O  
ANISOU 1895  O   LEU A 479     4582   5678   5111    705   -233   -771       O  
ATOM   1896  CB  LEU A 479      -5.470  13.870 -26.728  1.00 39.90           C  
ANISOU 1896  CB  LEU A 479     4623   5442   5096    626   -162   -888       C  
ATOM   1897  CG  LEU A 479      -5.799  14.844 -25.592  1.00 41.26           C  
ANISOU 1897  CG  LEU A 479     4816   5580   5279    638   -175   -823       C  
ATOM   1898  CD1 LEU A 479      -6.972  15.722 -25.971  1.00 37.58           C  
ANISOU 1898  CD1 LEU A 479     4294   5197   4786    622   -178   -810       C  
ATOM   1899  CD2 LEU A 479      -6.057  14.120 -24.284  1.00 38.03           C  
ANISOU 1899  CD2 LEU A 479     4481   5065   4905    623   -151   -827       C  
ATOM   1900  N   GLN A 480      -2.917  14.941 -28.211  1.00 36.93           N  
ANISOU 1900  N   GLN A 480     4184   5161   4686    716   -225   -833       N  
ATOM   1901  CA  GLN A 480      -1.701  15.752 -28.232  1.00 42.93           C  
ANISOU 1901  CA  GLN A 480     4938   5940   5435    756   -255   -782       C  
ATOM   1902  C   GLN A 480      -1.733  16.661 -29.446  1.00 38.65           C  
ANISOU 1902  C   GLN A 480     4324   5501   4860    763   -273   -770       C  
ATOM   1903  O   GLN A 480      -1.438  17.856 -29.368  1.00 39.44           O  
ANISOU 1903  O   GLN A 480     4414   5624   4948    779   -286   -716       O  
ATOM   1904  CB  GLN A 480      -0.435  14.882 -28.283  1.00 47.85           C  
ANISOU 1904  CB  GLN A 480     5585   6535   6061    788   -256   -797       C  
ATOM   1905  CG  GLN A 480      -0.141  14.056 -27.030  1.00 45.35           C  
ANISOU 1905  CG  GLN A 480     5340   6120   5770    803   -234   -790       C  
ATOM   1906  CD  GLN A 480      -0.734  12.649 -27.100  1.00 50.81           C  
ANISOU 1906  CD  GLN A 480     6069   6753   6482    784   -189   -851       C  
ATOM   1907  OE1 GLN A 480      -1.818  12.444 -27.650  1.00 58.70           O  
ANISOU 1907  OE1 GLN A 480     7047   7774   7482    736   -172   -898       O  
ATOM   1908  NE2 GLN A 480      -0.021  11.676 -26.543  1.00 46.73           N  
ANISOU 1908  NE2 GLN A 480     5609   6167   5979    821   -163   -850       N  
ATOM   1909  N   THR A 481      -2.101  16.077 -30.575  1.00 42.06           N  
ANISOU 1909  N   THR A 481     4709   5997   5275    747   -267   -823       N  
ATOM   1910  CA  THR A 481      -2.213  16.816 -31.818  1.00 40.69           C  
ANISOU 1910  CA  THR A 481     4459   5936   5065    756   -282   -814       C  
ATOM   1911  C   THR A 481      -3.176  17.990 -31.671  1.00 46.31           C  
ANISOU 1911  C   THR A 481     5146   6686   5762    760   -276   -763       C  
ATOM   1912  O   THR A 481      -2.851  19.123 -32.033  1.00 51.63           O  
ANISOU 1912  O   THR A 481     5798   7403   6417    790   -285   -708       O  
ATOM   1913  CB  THR A 481      -2.653  15.880 -32.935  1.00 39.25           C  
ANISOU 1913  CB  THR A 481     4228   5822   4864    726   -269   -890       C  
ATOM   1914  OG1 THR A 481      -1.624  14.898 -33.138  1.00 44.68           O  
ANISOU 1914  OG1 THR A 481     4944   6470   5565    734   -268   -929       O  
ATOM   1915  CG2 THR A 481      -2.905  16.651 -34.213  1.00 34.11           C  
ANISOU 1915  CG2 THR A 481     3487   5305   4168    738   -283   -877       C  
ATOM   1916  N   LEU A 482      -4.353  17.714 -31.117  1.00 40.41           N  
ANISOU 1916  N   LEU A 482     4411   5922   5023    731   -256   -778       N  
ATOM   1917  CA  LEU A 482      -5.354  18.747 -30.862  1.00 36.02           C  
ANISOU 1917  CA  LEU A 482     3836   5398   4450    742   -245   -727       C  
ATOM   1918  C   LEU A 482      -4.845  19.875 -29.966  1.00 43.89           C  
ANISOU 1918  C   LEU A 482     4885   6328   5465    770   -245   -653       C  
ATOM   1919  O   LEU A 482      -5.053  21.059 -30.268  1.00 43.91           O  
ANISOU 1919  O   LEU A 482     4865   6373   5446    801   -235   -595       O  
ATOM   1920  CB  LEU A 482      -6.628  18.126 -30.273  1.00 39.16           C  
ANISOU 1920  CB  LEU A 482     4244   5783   4854    701   -223   -761       C  
ATOM   1921  CG  LEU A 482      -7.407  17.265 -31.285  1.00 43.39           C  
ANISOU 1921  CG  LEU A 482     4712   6420   5354    661   -212   -836       C  
ATOM   1922  CD1 LEU A 482      -8.712  16.765 -30.706  1.00 36.39           C  
ANISOU 1922  CD1 LEU A 482     3829   5533   4463    613   -187   -870       C  
ATOM   1923  CD2 LEU A 482      -7.642  18.015 -32.611  1.00 37.11           C  
ANISOU 1923  CD2 LEU A 482     3821   5776   4504    690   -218   -814       C  
ATOM   1924  N   LEU A 483      -4.185  19.514 -28.865  1.00 35.78           N  
ANISOU 1924  N   LEU A 483     3926   5197   4473    760   -249   -654       N  
ATOM   1925  CA  LEU A 483      -3.618  20.520 -27.967  1.00 36.47           C  
ANISOU 1925  CA  LEU A 483     4060   5226   4571    773   -246   -595       C  
ATOM   1926  C   LEU A 483      -2.448  21.290 -28.597  1.00 45.97           C  
ANISOU 1926  C   LEU A 483     5248   6463   5754    795   -257   -567       C  
ATOM   1927  O   LEU A 483      -2.321  22.507 -28.405  1.00 49.19           O  
ANISOU 1927  O   LEU A 483     5672   6865   6154    804   -240   -515       O  
ATOM   1928  CB  LEU A 483      -3.177  19.886 -26.650  1.00 31.18           C  
ANISOU 1928  CB  LEU A 483     3455   4460   3934    756   -249   -605       C  
ATOM   1929  CG  LEU A 483      -4.297  19.260 -25.842  1.00 42.54           C  
ANISOU 1929  CG  LEU A 483     4920   5850   5394    732   -233   -625       C  
ATOM   1930  CD1 LEU A 483      -3.743  18.353 -24.743  1.00 49.24           C  
ANISOU 1930  CD1 LEU A 483     5827   6612   6272    724   -234   -640       C  
ATOM   1931  CD2 LEU A 483      -5.161  20.360 -25.264  1.00 37.46           C  
ANISOU 1931  CD2 LEU A 483     4287   5198   4750    732   -215   -577       C  
ATOM   1932  N   LEU A 484      -1.591  20.575 -29.328  1.00 36.30           N  
ANISOU 1932  N   LEU A 484     4000   5271   4522    800   -280   -603       N  
ATOM   1933  CA  LEU A 484      -0.444  21.188 -30.001  1.00 44.68           C  
ANISOU 1933  CA  LEU A 484     5041   6375   5560    817   -293   -584       C  
ATOM   1934  C   LEU A 484      -0.857  22.165 -31.103  1.00 47.50           C  
ANISOU 1934  C   LEU A 484     5347   6812   5887    838   -281   -551       C  
ATOM   1935  O   LEU A 484      -0.210  23.197 -31.303  1.00 46.18           O  
ANISOU 1935  O   LEU A 484     5186   6657   5705    849   -272   -510       O  
ATOM   1936  CB  LEU A 484       0.490  20.115 -30.578  1.00 47.14           C  
ANISOU 1936  CB  LEU A 484     5334   6709   5867    823   -318   -631       C  
ATOM   1937  CG  LEU A 484       1.359  19.401 -29.540  1.00 43.60           C  
ANISOU 1937  CG  LEU A 484     4937   6194   5436    823   -326   -641       C  
ATOM   1938  CD1 LEU A 484       2.215  18.350 -30.197  1.00 38.26           C  
ANISOU 1938  CD1 LEU A 484     4244   5542   4752    842   -342   -681       C  
ATOM   1939  CD2 LEU A 484       2.203  20.416 -28.795  1.00 33.27           C  
ANISOU 1939  CD2 LEU A 484     3655   4870   4115    818   -326   -595       C  
ATOM   1940  N   SER A 485      -1.925  21.838 -31.826  1.00 39.57           N  
ANISOU 1940  N   SER A 485     4293   5872   4871    844   -276   -570       N  
ATOM   1941  CA  SER A 485      -2.410  22.741 -32.866  1.00 45.07           C  
ANISOU 1941  CA  SER A 485     4933   6661   5532    876   -261   -531       C  
ATOM   1942  C   SER A 485      -3.282  23.854 -32.284  1.00 47.28           C  
ANISOU 1942  C   SER A 485     5238   6916   5809    895   -221   -467       C  
ATOM   1943  O   SER A 485      -3.687  24.770 -33.001  1.00 50.99           O  
ANISOU 1943  O   SER A 485     5674   7451   6247    935   -195   -416       O  
ATOM   1944  CB  SER A 485      -3.142  21.980 -33.987  1.00 44.87           C  
ANISOU 1944  CB  SER A 485     4827   6744   5478    874   -269   -578       C  
ATOM   1945  OG  SER A 485      -4.229  21.195 -33.506  1.00 43.71           O  
ANISOU 1945  OG  SER A 485     4680   6588   5340    844   -261   -617       O  
ATOM   1946  N   GLY A 486      -3.560  23.774 -30.982  1.00 46.26           N  
ANISOU 1946  N   GLY A 486     5172   6693   5711    872   -212   -465       N  
ATOM   1947  CA  GLY A 486      -4.401  24.752 -30.308  1.00 32.62           C  
ANISOU 1947  CA  GLY A 486     3478   4932   3986    888   -171   -408       C  
ATOM   1948  C   GLY A 486      -5.899  24.576 -30.525  1.00 40.19           C  
ANISOU 1948  C   GLY A 486     4390   5955   4924    904   -157   -405       C  
ATOM   1949  O   GLY A 486      -6.655  25.554 -30.498  1.00 44.53           O  
ANISOU 1949  O   GLY A 486     4940   6524   5456    943   -118   -344       O  
ATOM   1950  N   LEU A 487      -6.334  23.339 -30.754  1.00 36.53           N  
ANISOU 1950  N   LEU A 487     3888   5531   4459    874   -183   -472       N  
ATOM   1951  CA  LEU A 487      -7.763  23.053 -30.878  1.00 33.31           C  
ANISOU 1951  CA  LEU A 487     3434   5197   4026    873   -171   -483       C  
ATOM   1952  C   LEU A 487      -8.303  22.649 -29.514  1.00 35.18           C  
ANISOU 1952  C   LEU A 487     3730   5338   4298    838   -166   -498       C  
ATOM   1953  O   LEU A 487      -8.694  21.498 -29.282  1.00 41.65           O  
ANISOU 1953  O   LEU A 487     4547   6152   5128    792   -177   -564       O  
ATOM   1954  CB  LEU A 487      -8.026  21.963 -31.920  1.00 34.22           C  
ANISOU 1954  CB  LEU A 487     3472   5418   4113    846   -191   -556       C  
ATOM   1955  CG  LEU A 487      -7.634  22.386 -33.348  1.00 50.14           C  
ANISOU 1955  CG  LEU A 487     5415   7551   6087    883   -195   -539       C  
ATOM   1956  CD1 LEU A 487      -7.494  21.186 -34.268  1.00 40.26           C  
ANISOU 1956  CD1 LEU A 487     4105   6374   4818    842   -218   -626       C  
ATOM   1957  CD2 LEU A 487      -8.625  23.397 -33.919  1.00 49.19           C  
ANISOU 1957  CD2 LEU A 487     5233   7546   5911    943   -164   -470       C  
ATOM   1958  N   TYR A 488      -8.316  23.606 -28.602  1.00 36.49           N  
ANISOU 1958  N   TYR A 488     3955   5428   4483    857   -142   -439       N  
ATOM   1959  CA  TYR A 488      -8.586  23.286 -27.197  1.00 40.20           C  
ANISOU 1959  CA  TYR A 488     4490   5794   4991    823   -140   -450       C  
ATOM   1960  C   TYR A 488      -9.981  22.728 -26.948  1.00 42.62           C  
ANISOU 1960  C   TYR A 488     4769   6141   5284    805   -133   -475       C  
ATOM   1961  O   TYR A 488     -10.136  21.719 -26.258  1.00 52.48           O  
ANISOU 1961  O   TYR A 488     6046   7336   6559    758   -145   -527       O  
ATOM   1962  CB  TYR A 488      -8.296  24.493 -26.306  1.00 34.66           C  
ANISOU 1962  CB  TYR A 488     3856   5008   4307    841   -110   -386       C  
ATOM   1963  CG  TYR A 488      -6.909  25.066 -26.534  1.00 46.64           C  
ANISOU 1963  CG  TYR A 488     5399   6493   5830    845   -111   -368       C  
ATOM   1964  CD1 TYR A 488      -6.736  26.406 -26.839  1.00 44.36           C  
ANISOU 1964  CD1 TYR A 488     5125   6207   5524    882    -69   -305       C  
ATOM   1965  CD2 TYR A 488      -5.776  24.258 -26.465  1.00 42.20           C  
ANISOU 1965  CD2 TYR A 488     4848   5903   5285    814   -147   -415       C  
ATOM   1966  CE1 TYR A 488      -5.490  26.933 -27.036  1.00 44.83           C  
ANISOU 1966  CE1 TYR A 488     5209   6240   5583    874    -65   -295       C  
ATOM   1967  CE2 TYR A 488      -4.514  24.781 -26.673  1.00 45.35           C  
ANISOU 1967  CE2 TYR A 488     5263   6288   5679    814   -149   -401       C  
ATOM   1968  CZ  TYR A 488      -4.378  26.122 -26.956  1.00 50.53           C  
ANISOU 1968  CZ  TYR A 488     5933   6948   6318    838   -109   -345       C  
ATOM   1969  OH  TYR A 488      -3.129  26.661 -27.165  1.00 55.59           O  
ANISOU 1969  OH  TYR A 488     6592   7580   6951    827   -105   -337       O  
ATOM   1970  N   GLY A 489     -10.990  23.381 -27.516  1.00 45.25           N  
ANISOU 1970  N   GLY A 489     5046   6575   5570    845   -109   -436       N  
ATOM   1971  CA  GLY A 489     -12.351  22.903 -27.410  1.00 42.11           C  
ANISOU 1971  CA  GLY A 489     4607   6248   5145    828   -102   -460       C  
ATOM   1972  C   GLY A 489     -12.503  21.480 -27.911  1.00 46.09           C  
ANISOU 1972  C   GLY A 489     5068   6804   5640    765   -125   -555       C  
ATOM   1973  O   GLY A 489     -13.131  20.645 -27.251  1.00 50.42           O  
ANISOU 1973  O   GLY A 489     5633   7323   6200    712   -124   -604       O  
ATOM   1974  N   LEU A 490     -11.926  21.199 -29.077  1.00 44.22           N  
ANISOU 1974  N   LEU A 490     4781   6640   5382    767   -138   -583       N  
ATOM   1975  CA  LEU A 490     -11.959  19.848 -29.637  1.00 46.72           C  
ANISOU 1975  CA  LEU A 490     5063   6998   5689    703   -150   -679       C  
ATOM   1976  C   LEU A 490     -11.176  18.826 -28.774  1.00 45.34           C  
ANISOU 1976  C   LEU A 490     4976   6675   5579    655   -160   -731       C  
ATOM   1977  O   LEU A 490     -11.612  17.687 -28.611  1.00 46.83           O  
ANISOU 1977  O   LEU A 490     5171   6851   5772    593   -150   -805       O  
ATOM   1978  CB  LEU A 490     -11.446  19.854 -31.081  1.00 48.81           C  
ANISOU 1978  CB  LEU A 490     5255   7374   5918    720   -161   -693       C  
ATOM   1979  CG  LEU A 490     -12.202  20.661 -32.136  1.00 50.14           C  
ANISOU 1979  CG  LEU A 490     5322   7718   6012    770   -148   -649       C  
ATOM   1980  CD1 LEU A 490     -11.590  20.394 -33.509  1.00 37.86           C  
ANISOU 1980  CD1 LEU A 490     3699   6262   4426    772   -163   -681       C  
ATOM   1981  CD2 LEU A 490     -13.679  20.294 -32.141  1.00 44.89           C  
ANISOU 1981  CD2 LEU A 490     4594   7171   5293    738   -131   -680       C  
ATOM   1982  N   ALA A 491     -10.024  19.223 -28.234  1.00 33.12           N  
ANISOU 1982  N   ALA A 491     3492   5019   4073    683   -173   -692       N  
ATOM   1983  CA  ALA A 491      -9.322  18.376 -27.255  1.00 41.01           C  
ANISOU 1983  CA  ALA A 491     4572   5884   5125    653   -178   -722       C  
ATOM   1984  C   ALA A 491     -10.243  17.912 -26.135  1.00 41.75           C  
ANISOU 1984  C   ALA A 491     4706   5918   5238    616   -161   -739       C  
ATOM   1985  O   ALA A 491     -10.260  16.731 -25.771  1.00 48.13           O  
ANISOU 1985  O   ALA A 491     5550   6668   6068    572   -151   -798       O  
ATOM   1986  CB  ALA A 491      -8.115  19.108 -26.649  1.00 41.76           C  
ANISOU 1986  CB  ALA A 491     4721   5896   5250    690   -191   -666       C  
ATOM   1987  N   ILE A 492     -10.992  18.847 -25.568  1.00 32.36           N  
ANISOU 1987  N   ILE A 492     3518   4736   4040    637   -153   -684       N  
ATOM   1988  CA  ILE A 492     -11.900  18.493 -24.475  1.00 48.38           C  
ANISOU 1988  CA  ILE A 492     5582   6714   6085    603   -139   -695       C  
ATOM   1989  C   ILE A 492     -12.978  17.506 -24.926  1.00 52.36           C  
ANISOU 1989  C   ILE A 492     6042   7294   6558    546   -123   -769       C  
ATOM   1990  O   ILE A 492     -13.166  16.465 -24.292  1.00 50.06           O  
ANISOU 1990  O   ILE A 492     5796   6931   6292    494   -110   -821       O  
ATOM   1991  CB  ILE A 492     -12.519  19.735 -23.809  1.00 43.07           C  
ANISOU 1991  CB  ILE A 492     4918   6039   5406    640   -128   -620       C  
ATOM   1992  CG1 ILE A 492     -11.428  20.521 -23.068  1.00 40.02           C  
ANISOU 1992  CG1 ILE A 492     4597   5552   5057    670   -134   -565       C  
ATOM   1993  CG2 ILE A 492     -13.641  19.330 -22.862  1.00 36.52           C  
ANISOU 1993  CG2 ILE A 492     4109   5186   4582    603   -115   -638       C  
ATOM   1994  CD1 ILE A 492     -11.637  22.037 -23.146  1.00 54.05           C  
ANISOU 1994  CD1 ILE A 492     6367   7356   6814    723   -113   -487       C  
ATOM   1995  N   ASP A 493     -13.669  17.850 -26.018  1.00 41.71           N  
ANISOU 1995  N   ASP A 493     4604   6095   5150    554   -119   -772       N  
ATOM   1996  CA  ASP A 493     -14.611  16.956 -26.700  1.00 47.45           C  
ANISOU 1996  CA  ASP A 493     5268   6931   5830    491   -103   -853       C  
ATOM   1997  C   ASP A 493     -14.044  15.548 -26.823  1.00 47.36           C  
ANISOU 1997  C   ASP A 493     5297   6851   5848    427    -91   -942       C  
ATOM   1998  O   ASP A 493     -14.685  14.565 -26.434  1.00 52.95           O  
ANISOU 1998  O   ASP A 493     6028   7533   6558    356    -64  -1010       O  
ATOM   1999  CB  ASP A 493     -14.896  17.453 -28.125  1.00 61.94           C  
ANISOU 1999  CB  ASP A 493     6994   8945   7595    518   -106   -846       C  
ATOM   2000  CG  ASP A 493     -15.969  18.523 -28.170  1.00 75.60           C  
ANISOU 2000  CG  ASP A 493     8663  10792   9271    568    -97   -778       C  
ATOM   2001  OD1 ASP A 493     -16.877  18.511 -27.293  1.00 76.84           O  
ANISOU 2001  OD1 ASP A 493     8838  10934   9426    549    -84   -774       O  
ATOM   2002  OD2 ASP A 493     -15.927  19.378 -29.087  1.00 79.69           O  
ANISOU 2002  OD2 ASP A 493     9113  11420   9744    631    -99   -726       O  
ATOM   2003  N   TYR A 494     -12.853  15.453 -27.409  1.00 43.44           N  
ANISOU 2003  N   TYR A 494     4810   6326   5370    453   -106   -943       N  
ATOM   2004  CA  TYR A 494     -12.237  14.164 -27.681  1.00 43.17           C  
ANISOU 2004  CA  TYR A 494     4813   6232   5359    407    -88  -1022       C  
ATOM   2005  C   TYR A 494     -11.998  13.394 -26.401  1.00 51.39           C  
ANISOU 2005  C   TYR A 494     5957   7111   6457    387    -69  -1033       C  
ATOM   2006  O   TYR A 494     -12.279  12.197 -26.325  1.00 64.56           O  
ANISOU 2006  O   TYR A 494     7660   8736   8133    323    -29  -1110       O  
ATOM   2007  CB  TYR A 494     -10.925  14.341 -28.431  1.00 39.01           C  
ANISOU 2007  CB  TYR A 494     4279   5701   4841    454   -110  -1005       C  
ATOM   2008  CG  TYR A 494     -10.256  13.032 -28.775  1.00 45.31           C  
ANISOU 2008  CG  TYR A 494     5115   6440   5659    417    -86  -1082       C  
ATOM   2009  CD1 TYR A 494     -10.842  12.151 -29.668  1.00 48.49           C  
ANISOU 2009  CD1 TYR A 494     5476   6922   6027    346    -53  -1176       C  
ATOM   2010  CD2 TYR A 494      -9.024  12.685 -28.226  1.00 47.77           C  
ANISOU 2010  CD2 TYR A 494     5505   6625   6020    454    -90  -1061       C  
ATOM   2011  CE1 TYR A 494     -10.233  10.960 -30.000  1.00 51.00           C  
ANISOU 2011  CE1 TYR A 494     5838   7175   6364    312    -19  -1248       C  
ATOM   2012  CE2 TYR A 494      -8.406  11.500 -28.552  1.00 42.98           C  
ANISOU 2012  CE2 TYR A 494     4938   5962   5430    434    -59  -1124       C  
ATOM   2013  CZ  TYR A 494      -9.015  10.637 -29.441  1.00 49.98           C  
ANISOU 2013  CZ  TYR A 494     5792   6911   6287    362    -21  -1218       C  
ATOM   2014  OH  TYR A 494      -8.415   9.442 -29.773  1.00 58.67           O  
ANISOU 2014  OH  TYR A 494     6942   7944   7405    341     23  -1284       O  
ATOM   2015  N   THR A 495     -11.478  14.079 -25.390  1.00 46.44           N  
ANISOU 2015  N   THR A 495     5383   6395   5867    439    -90   -957       N  
ATOM   2016  CA  THR A 495     -11.252  13.443 -24.098  1.00 47.13           C  
ANISOU 2016  CA  THR A 495     5562   6341   6004    430    -73   -955       C  
ATOM   2017  C   THR A 495     -12.558  12.958 -23.461  1.00 45.39           C  
ANISOU 2017  C   THR A 495     5355   6113   5779    368    -44   -992       C  
ATOM   2018  O   THR A 495     -12.563  11.958 -22.754  1.00 44.75           O  
ANISOU 2018  O   THR A 495     5344   5930   5729    336    -11  -1027       O  
ATOM   2019  CB  THR A 495     -10.491  14.376 -23.145  1.00 48.10           C  
ANISOU 2019  CB  THR A 495     5724   6395   6157    491   -102   -868       C  
ATOM   2020  OG1 THR A 495      -9.372  14.931 -23.850  1.00 50.23           O  
ANISOU 2020  OG1 THR A 495     5970   6696   6420    539   -128   -838       O  
ATOM   2021  CG2 THR A 495      -9.995  13.612 -21.919  1.00 38.90           C  
ANISOU 2021  CG2 THR A 495     4648   5097   5038    492    -86   -865       C  
ATOM   2022  N   TYR A 496     -13.663  13.651 -23.729  1.00 42.06           N  
ANISOU 2022  N   TYR A 496     4865   5803   5313    356    -51   -983       N  
ATOM   2023  CA  TYR A 496     -14.969  13.190 -23.260  1.00 58.91           C  
ANISOU 2023  CA  TYR A 496     6996   7957   7428    291    -23  -1025       C  
ATOM   2024  C   TYR A 496     -15.349  11.822 -23.827  1.00 66.28           C  
ANISOU 2024  C   TYR A 496     7932   8907   8346    202     24  -1134       C  
ATOM   2025  O   TYR A 496     -16.133  11.093 -23.218  1.00 72.73           O  
ANISOU 2025  O   TYR A 496     8783   9686   9165    136     60  -1182       O  
ATOM   2026  CB  TYR A 496     -16.075  14.191 -23.612  1.00 61.29           C  
ANISOU 2026  CB  TYR A 496     7210   8407   7671    302    -36   -993       C  
ATOM   2027  CG  TYR A 496     -16.388  15.222 -22.548  1.00 48.84           C  
ANISOU 2027  CG  TYR A 496     5656   6790   6110    352    -53   -909       C  
ATOM   2028  CD1 TYR A 496     -15.941  16.531 -22.677  1.00 42.06           C  
ANISOU 2028  CD1 TYR A 496     4780   5953   5250    431    -77   -823       C  
ATOM   2029  CD2 TYR A 496     -17.162  14.899 -21.439  1.00 54.42           C  
ANISOU 2029  CD2 TYR A 496     6405   7440   6831    314    -37   -918       C  
ATOM   2030  CE1 TYR A 496     -16.223  17.483 -21.723  1.00 44.06           C  
ANISOU 2030  CE1 TYR A 496     5061   6164   5516    471    -81   -751       C  
ATOM   2031  CE2 TYR A 496     -17.468  15.859 -20.469  1.00 53.39           C  
ANISOU 2031  CE2 TYR A 496     6296   7277   6715    357    -50   -843       C  
ATOM   2032  CZ  TYR A 496     -16.988  17.150 -20.623  1.00 47.62           C  
ANISOU 2032  CZ  TYR A 496     5550   6562   5982    435    -70   -761       C  
ATOM   2033  OH  TYR A 496     -17.254  18.129 -19.695  1.00 50.07           O  
ANISOU 2033  OH  TYR A 496     5887   6832   6304    475    -72   -691       O  
ATOM   2034  N   THR A 497     -14.818  11.477 -24.997  1.00 65.11           N  
ANISOU 2034  N   THR A 497     7747   8813   8178    194     29  -1178       N  
ATOM   2035  CA  THR A 497     -15.193  10.214 -25.634  1.00 66.65           C  
ANISOU 2035  CA  THR A 497     7942   9030   8352    100     82  -1291       C  
ATOM   2036  C   THR A 497     -14.631   8.970 -24.939  1.00 67.03           C  
ANISOU 2036  C   THR A 497     8108   8901   8458     73    133  -1331       C  
ATOM   2037  O   THR A 497     -15.101   7.862 -25.185  1.00 77.20           O  
ANISOU 2037  O   THR A 497     9421  10177   9735    -17    196  -1428       O  
ATOM   2038  CB  THR A 497     -14.825  10.172 -27.146  1.00 65.64           C  
ANISOU 2038  CB  THR A 497     7737   9022   8182     94     78  -1333       C  
ATOM   2039  OG1 THR A 497     -13.396  10.183 -27.316  1.00 63.99           O  
ANISOU 2039  OG1 THR A 497     7570   8726   8016    162     60  -1298       O  
ATOM   2040  CG2 THR A 497     -15.462  11.346 -27.895  1.00 59.58           C  
ANISOU 2040  CG2 THR A 497     6848   8444   7348    125     38  -1291       C  
ATOM   2041  N   PHE A 498     -13.635   9.143 -24.077  1.00 61.59           N  
ANISOU 2041  N   PHE A 498     7493   8081   7826    150    114  -1259       N  
ATOM   2042  CA  PHE A 498     -13.082   8.003 -23.344  1.00 62.91           C  
ANISOU 2042  CA  PHE A 498     7773   8084   8045    144    167  -1280       C  
ATOM   2043  C   PHE A 498     -12.940   8.214 -21.825  1.00 65.96           C  
ANISOU 2043  C   PHE A 498     8230   8355   8476    190    156  -1206       C  
ATOM   2044  O   PHE A 498     -12.493   7.315 -21.105  1.00 64.76           O  
ANISOU 2044  O   PHE A 498     8173   8070   8365    199    201  -1209       O  
ATOM   2045  CB  PHE A 498     -11.749   7.522 -23.964  1.00 64.34           C  
ANISOU 2045  CB  PHE A 498     7985   8217   8247    191    177  -1285       C  
ATOM   2046  CG  PHE A 498     -10.641   8.548 -23.948  1.00 59.99           C  
ANISOU 2046  CG  PHE A 498     7409   7680   7707    292    109  -1192       C  
ATOM   2047  CD1 PHE A 498     -10.285   9.227 -25.104  1.00 64.41           C  
ANISOU 2047  CD1 PHE A 498     7885   8354   8232    314     69  -1187       C  
ATOM   2048  CD2 PHE A 498      -9.938   8.813 -22.785  1.00 61.98           C  
ANISOU 2048  CD2 PHE A 498     7718   7834   7996    359     91  -1114       C  
ATOM   2049  CE1 PHE A 498      -9.251  10.165 -25.094  1.00 59.76           C  
ANISOU 2049  CE1 PHE A 498     7278   7776   7651    397     14  -1107       C  
ATOM   2050  CE2 PHE A 498      -8.909   9.748 -22.769  1.00 60.38           C  
ANISOU 2050  CE2 PHE A 498     7492   7654   7796    437     35  -1038       C  
ATOM   2051  CZ  PHE A 498      -8.566  10.423 -23.930  1.00 53.18           C  
ANISOU 2051  CZ  PHE A 498     6503   6848   6853    453     -1  -1037       C  
ATOM   2052  N   SER A 499     -13.322   9.390 -21.337  1.00 63.17           N  
ANISOU 2052  N   SER A 499     7834   8054   8114    221    103  -1139       N  
ATOM   2053  CA  SER A 499     -13.189   9.676 -19.910  1.00 66.04           C  
ANISOU 2053  CA  SER A 499     8256   8321   8515    260     91  -1071       C  
ATOM   2054  C   SER A 499     -13.681  11.057 -19.511  1.00 69.76           C  
ANISOU 2054  C   SER A 499     8675   8860   8971    288     39  -1004       C  
ATOM   2055  O   SER A 499     -12.934  12.035 -19.598  1.00 68.76           O  
ANISOU 2055  O   SER A 499     8525   8756   8846    352     -4   -940       O  
ATOM   2056  CB  SER A 499     -11.740   9.533 -19.473  1.00 55.15           C  
ANISOU 2056  CB  SER A 499     6933   6847   7174    337     83  -1019       C  
ATOM   2057  OG  SER A 499     -11.556  10.153 -18.220  1.00 62.96           O  
ANISOU 2057  OG  SER A 499     7950   7785   8185    379     57   -944       O  
ATOM   2058  N   GLU A 500     -14.926  11.132 -19.046  1.00 69.10           N  
ANISOU 2058  N   GLU A 500     8579   8805   8870    240     49  -1019       N  
ATOM   2059  CA  GLU A 500     -15.507  12.420 -18.696  1.00 68.54           C  
ANISOU 2059  CA  GLU A 500     8462   8800   8782    269     11   -957       C  
ATOM   2060  C   GLU A 500     -14.725  13.098 -17.587  1.00 61.84           C  
ANISOU 2060  C   GLU A 500     7661   7862   7973    332    -15   -875       C  
ATOM   2061  O   GLU A 500     -14.607  14.320 -17.567  1.00 66.88           O  
ANISOU 2061  O   GLU A 500     8267   8542   8601    377    -47   -814       O  
ATOM   2062  CB  GLU A 500     -16.978  12.297 -18.294  1.00 78.69           C  
ANISOU 2062  CB  GLU A 500     9728  10131  10040    208     30   -987       C  
ATOM   2063  CG  GLU A 500     -17.489  13.563 -17.598  1.00 84.58           C  
ANISOU 2063  CG  GLU A 500    10451  10906  10777    251     -2   -910       C  
ATOM   2064  CD  GLU A 500     -19.003  13.628 -17.463  1.00 84.28           C  
ANISOU 2064  CD  GLU A 500    10369  10958  10695    201     11   -935       C  
ATOM   2065  OE1 GLU A 500     -19.497  14.645 -16.919  1.00 66.42           O  
ANISOU 2065  OE1 GLU A 500     8090   8723   8424    240     -8   -873       O  
ATOM   2066  OE2 GLU A 500     -19.693  12.675 -17.900  1.00 91.43           O  
ANISOU 2066  OE2 GLU A 500    11258  11910  11571    123     44  -1018       O  
ATOM   2067  N   MET A 501     -14.182  12.309 -16.669  1.00 56.06           N  
ANISOU 2067  N   MET A 501     7008   7011   7283    334      4   -873       N  
ATOM   2068  CA  MET A 501     -13.510  12.883 -15.510  1.00 52.07           C  
ANISOU 2068  CA  MET A 501     6542   6436   6807    384    -17   -802       C  
ATOM   2069  C   MET A 501     -12.243  13.612 -15.924  1.00 49.72           C  
ANISOU 2069  C   MET A 501     6226   6157   6508    444    -49   -757       C  
ATOM   2070  O   MET A 501     -11.969  14.725 -15.475  1.00 42.91           O  
ANISOU 2070  O   MET A 501     5353   5305   5645    475    -75   -700       O  
ATOM   2071  CB  MET A 501     -13.186  11.806 -14.477  1.00 52.26           C  
ANISOU 2071  CB  MET A 501     6647   6342   6867    381     16   -806       C  
ATOM   2072  CG  MET A 501     -12.678  12.358 -13.154  1.00 64.44           C  
ANISOU 2072  CG  MET A 501     8221   7831   8432    423     -4   -736       C  
ATOM   2073  SD  MET A 501     -12.478  11.073 -11.907  1.00 70.90           S  
ANISOU 2073  SD  MET A 501     9128   8525   9284    426     41   -734       S  
ATOM   2074  CE  MET A 501     -14.030  10.193 -12.114  1.00 44.20           C  
ANISOU 2074  CE  MET A 501     5761   5135   5899    337     87   -812       C  
ATOM   2075  N   ASP A 502     -11.467  12.981 -16.792  1.00 54.48           N  
ANISOU 2075  N   ASP A 502     6827   6764   7110    455    -41   -787       N  
ATOM   2076  CA  ASP A 502     -10.234  13.593 -17.258  1.00 52.03           C  
ANISOU 2076  CA  ASP A 502     6496   6480   6793    508    -70   -750       C  
ATOM   2077  C   ASP A 502     -10.512  14.805 -18.139  1.00 49.44           C  
ANISOU 2077  C   ASP A 502     6099   6253   6434    516    -97   -732       C  
ATOM   2078  O   ASP A 502      -9.765  15.783 -18.104  1.00 47.87           O  
ANISOU 2078  O   ASP A 502     5889   6069   6231    553   -121   -683       O  
ATOM   2079  CB  ASP A 502      -9.369  12.561 -17.966  1.00 55.06           C  
ANISOU 2079  CB  ASP A 502     6897   6843   7181    521    -52   -787       C  
ATOM   2080  CG  ASP A 502      -8.800  11.538 -17.002  1.00 61.50           C  
ANISOU 2080  CG  ASP A 502     7787   7554   8025    543    -20   -780       C  
ATOM   2081  OD1 ASP A 502      -7.954  11.922 -16.148  1.00 55.14           O  
ANISOU 2081  OD1 ASP A 502     7000   6724   7226    589    -39   -721       O  
ATOM   2082  OD2 ASP A 502      -9.197  10.355 -17.098  1.00 62.81           O  
ANISOU 2082  OD2 ASP A 502     7994   7668   8202    512     28   -832       O  
ATOM   2083  N   ALA A 503     -11.600  14.754 -18.906  1.00 41.02           N  
ANISOU 2083  N   ALA A 503     4986   5260   5341    480    -88   -771       N  
ATOM   2084  CA  ALA A 503     -12.018  15.907 -19.696  1.00 41.32           C  
ANISOU 2084  CA  ALA A 503     4956   5402   5343    498   -105   -744       C  
ATOM   2085  C   ALA A 503     -12.283  17.138 -18.824  1.00 44.26           C  
ANISOU 2085  C   ALA A 503     5339   5760   5719    524   -114   -675       C  
ATOM   2086  O   ALA A 503     -11.790  18.246 -19.123  1.00 39.91           O  
ANISOU 2086  O   ALA A 503     4770   5237   5157    564   -125   -626       O  
ATOM   2087  CB  ALA A 503     -13.248  15.567 -20.528  1.00 44.79           C  
ANISOU 2087  CB  ALA A 503     5337   5940   5742    455    -89   -796       C  
ATOM   2088  N   VAL A 504     -13.064  16.941 -17.753  1.00 37.23           N  
ANISOU 2088  N   VAL A 504     4482   4822   4843    499   -102   -674       N  
ATOM   2089  CA  VAL A 504     -13.373  18.015 -16.812  1.00 31.82           C  
ANISOU 2089  CA  VAL A 504     3814   4113   4164    517   -104   -615       C  
ATOM   2090  C   VAL A 504     -12.079  18.666 -16.344  1.00 32.69           C  
ANISOU 2090  C   VAL A 504     3958   4170   4294    549   -116   -571       C  
ATOM   2091  O   VAL A 504     -11.925  19.884 -16.394  1.00 43.20           O  
ANISOU 2091  O   VAL A 504     5281   5520   5614    576   -114   -524       O  
ATOM   2092  CB  VAL A 504     -14.182  17.504 -15.576  1.00 38.87           C  
ANISOU 2092  CB  VAL A 504     4747   4945   5077    482    -92   -626       C  
ATOM   2093  CG1 VAL A 504     -14.199  18.552 -14.453  1.00 28.24           C  
ANISOU 2093  CG1 VAL A 504     3431   3555   3744    502    -93   -566       C  
ATOM   2094  CG2 VAL A 504     -15.598  17.144 -15.976  1.00 36.63           C  
ANISOU 2094  CG2 VAL A 504     4422   4734   4762    446    -78   -665       C  
ATOM   2095  N   HIS A 505     -11.132  17.838 -15.933  1.00 28.46           N  
ANISOU 2095  N   HIS A 505     3458   3573   3781    547   -121   -586       N  
ATOM   2096  CA  HIS A 505      -9.897  18.337 -15.350  1.00 34.84           C  
ANISOU 2096  CA  HIS A 505     4292   4346   4598    570   -132   -549       C  
ATOM   2097  C   HIS A 505      -8.906  18.922 -16.352  1.00 43.97           C  
ANISOU 2097  C   HIS A 505     5419   5553   5735    596   -144   -537       C  
ATOM   2098  O   HIS A 505      -8.164  19.848 -16.034  1.00 49.26           O  
ANISOU 2098  O   HIS A 505     6097   6220   6399    606   -147   -501       O  
ATOM   2099  CB  HIS A 505      -9.287  17.252 -14.475  1.00 34.71           C  
ANISOU 2099  CB  HIS A 505     4320   4262   4604    568   -130   -559       C  
ATOM   2100  CG  HIS A 505     -10.110  16.972 -13.254  1.00 51.72           C  
ANISOU 2100  CG  HIS A 505     6510   6362   6778    545   -117   -555       C  
ATOM   2101  ND1 HIS A 505     -11.082  16.004 -13.220  1.00 53.73           N  
ANISOU 2101  ND1 HIS A 505     6778   6595   7043    516    -98   -595       N  
ATOM   2102  CD2 HIS A 505     -10.129  17.585 -12.044  1.00 55.03           C  
ANISOU 2102  CD2 HIS A 505     6953   6750   7205    541   -117   -519       C  
ATOM   2103  CE1 HIS A 505     -11.660  16.012 -12.024  1.00 56.53           C  
ANISOU 2103  CE1 HIS A 505     7164   6904   7413    500    -91   -579       C  
ATOM   2104  NE2 HIS A 505     -11.096  16.954 -11.300  1.00 60.01           N  
ANISOU 2104  NE2 HIS A 505     7610   7338   7853    516   -103   -532       N  
ATOM   2105  N   LEU A 506      -8.913  18.402 -17.571  1.00 43.56           N  
ANISOU 2105  N   LEU A 506     5330   5550   5670    601   -149   -572       N  
ATOM   2106  CA  LEU A 506      -8.146  19.022 -18.633  1.00 39.45           C  
ANISOU 2106  CA  LEU A 506     4774   5088   5128    626   -160   -560       C  
ATOM   2107  C   LEU A 506      -8.708  20.410 -18.892  1.00 36.90           C  
ANISOU 2107  C   LEU A 506     4429   4805   4785    638   -149   -518       C  
ATOM   2108  O   LEU A 506      -7.969  21.360 -19.143  1.00 40.68           O  
ANISOU 2108  O   LEU A 506     4906   5297   5253    655   -147   -485       O  
ATOM   2109  CB  LEU A 506      -8.237  18.199 -19.911  1.00 49.28           C  
ANISOU 2109  CB  LEU A 506     5979   6386   6359    624   -163   -609       C  
ATOM   2110  CG  LEU A 506      -6.910  17.880 -20.593  1.00 64.19           C  
ANISOU 2110  CG  LEU A 506     7858   8289   8241    646   -178   -619       C  
ATOM   2111  CD1 LEU A 506      -6.203  16.704 -19.893  1.00 64.35           C  
ANISOU 2111  CD1 LEU A 506     7926   8239   8284    650   -174   -638       C  
ATOM   2112  CD2 LEU A 506      -7.169  17.561 -22.053  1.00 71.15           C  
ANISOU 2112  CD2 LEU A 506     8685   9249   9101    645   -180   -658       C  
ATOM   2113  N   ALA A 507     -10.030  20.524 -18.839  1.00 35.33           N  
ANISOU 2113  N   ALA A 507     4216   4628   4580    630   -135   -518       N  
ATOM   2114  CA  ALA A 507     -10.679  21.809 -19.066  1.00 40.79           C  
ANISOU 2114  CA  ALA A 507     4889   5359   5249    656   -114   -470       C  
ATOM   2115  C   ALA A 507     -10.333  22.782 -17.940  1.00 38.95           C  
ANISOU 2115  C   ALA A 507     4711   5055   5032    655    -97   -425       C  
ATOM   2116  O   ALA A 507     -10.139  23.974 -18.180  1.00 37.78           O  
ANISOU 2116  O   ALA A 507     4568   4916   4871    679    -72   -381       O  
ATOM   2117  CB  ALA A 507     -12.168  21.630 -19.170  1.00 47.55           C  
ANISOU 2117  CB  ALA A 507     5714   6266   6086    651   -102   -479       C  
ATOM   2118  N   ILE A 508     -10.234  22.271 -16.712  1.00 38.29           N  
ANISOU 2118  N   ILE A 508     4670   4903   4976    626   -103   -436       N  
ATOM   2119  CA  ILE A 508      -9.798  23.109 -15.609  1.00 35.86           C  
ANISOU 2119  CA  ILE A 508     4409   4535   4679    615    -87   -404       C  
ATOM   2120  C   ILE A 508      -8.399  23.635 -15.907  1.00 40.21           C  
ANISOU 2120  C   ILE A 508     4966   5092   5221    617    -88   -394       C  
ATOM   2121  O   ILE A 508      -8.124  24.816 -15.716  1.00 48.25           O  
ANISOU 2121  O   ILE A 508     6006   6096   6229    614    -57   -362       O  
ATOM   2122  CB  ILE A 508      -9.810  22.382 -14.256  1.00 41.90           C  
ANISOU 2122  CB  ILE A 508     5212   5239   5471    586    -96   -418       C  
ATOM   2123  CG1 ILE A 508     -11.240  22.063 -13.808  1.00 49.53           C  
ANISOU 2123  CG1 ILE A 508     6179   6196   6444    576    -88   -424       C  
ATOM   2124  CG2 ILE A 508      -9.188  23.260 -13.207  1.00 40.95           C  
ANISOU 2124  CG2 ILE A 508     5130   5077   5353    567    -79   -391       C  
ATOM   2125  CD1 ILE A 508     -11.324  21.130 -12.595  1.00 42.81           C  
ANISOU 2125  CD1 ILE A 508     5361   5285   5618    549    -97   -442       C  
ATOM   2126  N   GLY A 509      -7.519  22.757 -16.391  1.00 42.99           N  
ANISOU 2126  N   GLY A 509     5299   5464   5571    620   -117   -423       N  
ATOM   2127  CA  GLY A 509      -6.172  23.144 -16.775  1.00 35.25           C  
ANISOU 2127  CA  GLY A 509     4314   4506   4574    621   -123   -419       C  
ATOM   2128  C   GLY A 509      -6.078  24.226 -17.846  1.00 41.73           C  
ANISOU 2128  C   GLY A 509     5116   5368   5372    640   -102   -395       C  
ATOM   2129  O   GLY A 509      -5.333  25.196 -17.687  1.00 47.76           O  
ANISOU 2129  O   GLY A 509     5900   6124   6122    626    -80   -375       O  
ATOM   2130  N   LEU A 510      -6.811  24.068 -18.944  1.00 44.55           N  
ANISOU 2130  N   LEU A 510     5433   5775   5720    669   -105   -398       N  
ATOM   2131  CA  LEU A 510      -6.753  25.057 -20.026  1.00 48.14           C  
ANISOU 2131  CA  LEU A 510     5865   6278   6150    698    -82   -368       C  
ATOM   2132  C   LEU A 510      -7.296  26.401 -19.539  1.00 49.14           C  
ANISOU 2132  C   LEU A 510     6029   6368   6273    704    -29   -318       C  
ATOM   2133  O   LEU A 510      -6.791  27.471 -19.910  1.00 48.11           O  
ANISOU 2133  O   LEU A 510     5916   6236   6127    712      8   -287       O  
ATOM   2134  CB  LEU A 510      -7.528  24.571 -21.257  1.00 39.08           C  
ANISOU 2134  CB  LEU A 510     4656   5209   4985    729    -95   -381       C  
ATOM   2135  CG  LEU A 510      -7.038  23.231 -21.809  1.00 42.91           C  
ANISOU 2135  CG  LEU A 510     5108   5723   5473    718   -136   -436       C  
ATOM   2136  CD1 LEU A 510      -8.112  22.556 -22.633  1.00 34.37           C  
ANISOU 2136  CD1 LEU A 510     3972   4710   4376    726   -141   -464       C  
ATOM   2137  CD2 LEU A 510      -5.745  23.411 -22.619  1.00 47.94           C  
ANISOU 2137  CD2 LEU A 510     5729   6391   6095    728   -150   -438       C  
ATOM   2138  N   ALA A 511      -8.326  26.329 -18.701  1.00 37.91           N  
ANISOU 2138  N   ALA A 511     4627   4913   4865    700    -18   -311       N  
ATOM   2139  CA  ALA A 511      -8.967  27.518 -18.145  1.00 46.80           C  
ANISOU 2139  CA  ALA A 511     5794   5999   5990    710     39   -264       C  
ATOM   2140  C   ALA A 511      -8.004  28.269 -17.257  1.00 49.67           C  
ANISOU 2140  C   ALA A 511     6217   6294   6360    667     68   -260       C  
ATOM   2141  O   ALA A 511      -7.940  29.494 -17.293  1.00 57.48           O  
ANISOU 2141  O   ALA A 511     7244   7255   7340    673    128   -224       O  
ATOM   2142  CB  ALA A 511     -10.219  27.138 -17.345  1.00 36.81           C  
ANISOU 2142  CB  ALA A 511     4533   4716   4737    709     37   -265       C  
ATOM   2143  N   SER A 512      -7.260  27.532 -16.445  1.00 43.20           N  
ANISOU 2143  N   SER A 512     5405   5453   5554    622     31   -297       N  
ATOM   2144  CA  SER A 512      -6.324  28.169 -15.537  1.00 52.21           C  
ANISOU 2144  CA  SER A 512     6592   6554   6692    570     56   -300       C  
ATOM   2145  C   SER A 512      -5.181  28.780 -16.337  1.00 54.84           C  
ANISOU 2145  C   SER A 512     6921   6916   7000    561     72   -300       C  
ATOM   2146  O   SER A 512      -4.403  29.568 -15.814  1.00 57.86           O  
ANISOU 2146  O   SER A 512     7339   7275   7368    513    108   -303       O  
ATOM   2147  CB  SER A 512      -5.795  27.178 -14.503  1.00 55.07           C  
ANISOU 2147  CB  SER A 512     6952   6908   7065    535     14   -334       C  
ATOM   2148  OG  SER A 512      -4.562  26.639 -14.922  1.00 63.42           O  
ANISOU 2148  OG  SER A 512     7981   8011   8105    529    -21   -357       O  
ATOM   2149  N   LEU A 513      -5.099  28.398 -17.611  1.00 60.75           N  
ANISOU 2149  N   LEU A 513     7624   7721   7740    603     45   -300       N  
ATOM   2150  CA  LEU A 513      -4.134  28.953 -18.561  1.00 57.20           C  
ANISOU 2150  CA  LEU A 513     7164   7306   7265    603     58   -296       C  
ATOM   2151  C   LEU A 513      -4.736  30.024 -19.447  1.00 57.35           C  
ANISOU 2151  C   LEU A 513     7193   7326   7272    646    115   -249       C  
ATOM   2152  O   LEU A 513      -4.041  30.617 -20.262  1.00 60.92           O  
ANISOU 2152  O   LEU A 513     7644   7801   7704    650    137   -238       O  
ATOM   2153  CB  LEU A 513      -3.544  27.849 -19.435  1.00 51.81           C  
ANISOU 2153  CB  LEU A 513     6422   6689   6575    623     -5   -326       C  
ATOM   2154  CG  LEU A 513      -2.540  26.934 -18.740  1.00 49.85           C  
ANISOU 2154  CG  LEU A 513     6166   6451   6326    591    -50   -364       C  
ATOM   2155  CD1 LEU A 513      -2.268  25.702 -19.553  1.00 43.46           C  
ANISOU 2155  CD1 LEU A 513     5306   5690   5516    623   -103   -390       C  
ATOM   2156  CD2 LEU A 513      -1.277  27.693 -18.478  1.00 51.09           C  
ANISOU 2156  CD2 LEU A 513     6340   6618   6452    544    -28   -368       C  
ATOM   2157  N   LYS A 514      -6.032  30.268 -19.283  1.00 53.17           N  
ANISOU 2157  N   LYS A 514     6673   6777   6753    684    143   -217       N  
ATOM   2158  CA  LYS A 514      -6.704  31.349 -19.994  1.00 59.45           C  
ANISOU 2158  CA  LYS A 514     7483   7574   7533    739    209   -159       C  
ATOM   2159  C   LYS A 514      -6.851  31.026 -21.477  1.00 66.77           C  
ANISOU 2159  C   LYS A 514     8340   8592   8437    798    183   -147       C  
ATOM   2160  O   LYS A 514      -6.418  31.794 -22.336  1.00 67.74           O  
ANISOU 2160  O   LYS A 514     8467   8732   8540    823    222   -117       O  
ATOM   2161  CB  LYS A 514      -5.941  32.663 -19.815  1.00 66.75           C  
ANISOU 2161  CB  LYS A 514     8477   8437   8447    708    289   -139       C  
ATOM   2162  CG  LYS A 514      -5.784  33.099 -18.368  1.00 77.09           C  
ANISOU 2162  CG  LYS A 514     9855   9664   9772    640    325   -155       C  
ATOM   2163  CD  LYS A 514      -6.963  33.944 -17.914  1.00 87.35           C  
ANISOU 2163  CD  LYS A 514    11206  10903  11079    676    400   -106       C  
ATOM   2164  CE  LYS A 514      -6.713  34.551 -16.544  1.00 93.54           C  
ANISOU 2164  CE  LYS A 514    12065  11601  11874    601    452   -125       C  
ATOM   2165  NZ  LYS A 514      -7.981  34.953 -15.874  1.00 95.79           N  
ANISOU 2165  NZ  LYS A 514    12387  11834  12173    636    498    -88       N  
ATOM   2166  N   LEU A 515      -7.464  29.883 -21.770  1.00 71.65           N  
ANISOU 2166  N   LEU A 515     8896   9271   9058    815    123   -174       N  
ATOM   2167  CA  LEU A 515      -7.606  29.421 -23.145  1.00 74.17           C  
ANISOU 2167  CA  LEU A 515     9139   9689   9351    859     93   -176       C  
ATOM   2168  C   LEU A 515      -8.385  28.112 -23.209  1.00 85.61           C  
ANISOU 2168  C   LEU A 515    10531  11192  10804    856     37   -219       C  
ATOM   2169  O   LEU A 515      -8.010  27.190 -23.934  1.00 99.72           O  
ANISOU 2169  O   LEU A 515    12268  13037  12586    848    -10   -262       O  
ATOM   2170  CB  LEU A 515      -6.232  29.248 -23.797  1.00 69.71           C  
ANISOU 2170  CB  LEU A 515     8561   9145   8781    836     66   -203       C  
ATOM   2171  CG  LEU A 515      -5.220  28.395 -23.030  1.00 64.09           C  
ANISOU 2171  CG  LEU A 515     7863   8397   8090    774     17   -260       C  
ATOM   2172  CD1 LEU A 515      -5.453  26.916 -23.296  1.00 68.34           C  
ANISOU 2172  CD1 LEU A 515     8350   8981   8637    774    -47   -310       C  
ATOM   2173  CD2 LEU A 515      -3.797  28.792 -23.393  1.00 60.79           C  
ANISOU 2173  CD2 LEU A 515     7455   7984   7658    749     18   -268       C  
ATOM   2174  N   ARG A 533     -18.889  27.478 -21.777  1.00 72.83           N  
ANISOU 2174  N   ARG A 533     8658  10033   8980   1037    126   -109       N  
ATOM   2175  CA  ARG A 533     -19.305  26.109 -21.497  1.00 70.67           C  
ANISOU 2175  CA  ARG A 533     8352   9788   8710    952     77   -198       C  
ATOM   2176  C   ARG A 533     -18.492  25.508 -20.355  1.00 65.76           C  
ANISOU 2176  C   ARG A 533     7817   9002   8166    876     49   -247       C  
ATOM   2177  O   ARG A 533     -18.715  24.365 -19.956  1.00 64.97           O  
ANISOU 2177  O   ARG A 533     7713   8893   8081    805     17   -318       O  
ATOM   2178  CB  ARG A 533     -19.171  25.241 -22.750  1.00 66.40           C  
ANISOU 2178  CB  ARG A 533     7725   9370   8132    925     45   -256       C  
ATOM   2179  CG  ARG A 533     -17.842  24.513 -22.862  1.00 56.85           C  
ANISOU 2179  CG  ARG A 533     6555   8068   6979    867      9   -316       C  
ATOM   2180  CD  ARG A 533     -17.807  23.611 -24.085  1.00 70.11           C  
ANISOU 2180  CD  ARG A 533     8150   9869   8619    836    -16   -380       C  
ATOM   2181  NE  ARG A 533     -18.270  22.260 -23.782  1.00 78.53           N  
ANISOU 2181  NE  ARG A 533     9205  10943   9690    747    -37   -472       N  
ATOM   2182  CZ  ARG A 533     -19.469  21.976 -23.284  1.00 78.73           C  
ANISOU 2182  CZ  ARG A 533     9207  11021   9686    721    -28   -488       C  
ATOM   2183  NH1 ARG A 533     -20.333  22.950 -23.031  1.00 90.13           N  
ANISOU 2183  NH1 ARG A 533    10633  12521  11093    785     -1   -415       N  
ATOM   2184  NH2 ARG A 533     -19.806  20.717 -23.039  1.00 66.59           N  
ANISOU 2184  NH2 ARG A 533     7668   9480   8154    631    -39   -578       N  
ATOM   2185  N   PHE A 534     -17.550  26.287 -19.832  1.00 55.89           N  
ANISOU 2185  N   PHE A 534     6645   7630   6961    889     68   -210       N  
ATOM   2186  CA  PHE A 534     -16.807  25.895 -18.641  1.00 56.08           C  
ANISOU 2186  CA  PHE A 534     6747   7513   7048    828     48   -243       C  
ATOM   2187  C   PHE A 534     -17.738  25.703 -17.448  1.00 59.03           C  
ANISOU 2187  C   PHE A 534     7146   7850   7432    803     52   -248       C  
ATOM   2188  O   PHE A 534     -17.739  24.649 -16.813  1.00 54.20           O  
ANISOU 2188  O   PHE A 534     6547   7198   6847    740     20   -305       O  
ATOM   2189  CB  PHE A 534     -15.738  26.938 -18.310  1.00 48.26           C  
ANISOU 2189  CB  PHE A 534     5826   6422   6086    844     78   -200       C  
ATOM   2190  CG  PHE A 534     -14.784  26.507 -17.232  1.00 52.51           C  
ANISOU 2190  CG  PHE A 534     6428   6844   6677    780     54   -237       C  
ATOM   2191  CD1 PHE A 534     -14.312  25.206 -17.186  1.00 49.49           C  
ANISOU 2191  CD1 PHE A 534     6034   6455   6315    730      5   -302       C  
ATOM   2192  CD2 PHE A 534     -14.360  27.403 -16.265  1.00 52.50           C  
ANISOU 2192  CD2 PHE A 534     6499   6748   6701    773     89   -206       C  
ATOM   2193  CE1 PHE A 534     -13.434  24.807 -16.196  1.00 53.03           C  
ANISOU 2193  CE1 PHE A 534     6535   6812   6804    684    -13   -326       C  
ATOM   2194  CE2 PHE A 534     -13.482  27.010 -15.272  1.00 51.15           C  
ANISOU 2194  CE2 PHE A 534     6375   6494   6567    715     68   -239       C  
ATOM   2195  CZ  PHE A 534     -13.019  25.710 -15.238  1.00 50.64           C  
ANISOU 2195  CZ  PHE A 534     6290   6432   6517    677     15   -294       C  
ATOM   2196  N   ALA A 535     -18.530  26.728 -17.151  1.00 58.53           N  
ANISOU 2196  N   ALA A 535     7093   7798   7347    857     97   -184       N  
ATOM   2197  CA  ALA A 535     -19.472  26.672 -16.035  1.00 65.53           C  
ANISOU 2197  CA  ALA A 535     8001   8657   8239    842    105   -181       C  
ATOM   2198  C   ALA A 535     -20.350  25.437 -16.170  1.00 54.94           C  
ANISOU 2198  C   ALA A 535     6598   7403   6873    796     68   -242       C  
ATOM   2199  O   ALA A 535     -20.687  24.774 -15.194  1.00 53.34           O  
ANISOU 2199  O   ALA A 535     6421   7150   6695    741     50   -279       O  
ATOM   2200  CB  ALA A 535     -20.331  27.916 -16.014  1.00 72.41           C  
ANISOU 2200  CB  ALA A 535     8875   9564   9075    924    164    -99       C  
ATOM   2201  N   ASN A 536     -20.698  25.128 -17.407  1.00 45.88           N  
ANISOU 2201  N   ASN A 536     5368   6391   5673    813     60   -257       N  
ATOM   2202  CA  ASN A 536     -21.560  24.005 -17.706  1.00 44.72           C  
ANISOU 2202  CA  ASN A 536     5154   6348   5488    760     36   -323       C  
ATOM   2203  C   ASN A 536     -20.819  22.673 -17.593  1.00 54.12           C  
ANISOU 2203  C   ASN A 536     6370   7471   6724    673      0   -409       C  
ATOM   2204  O   ASN A 536     -21.391  21.675 -17.165  1.00 62.25           O  
ANISOU 2204  O   ASN A 536     7395   8504   7753    607    -12   -470       O  
ATOM   2205  CB  ASN A 536     -22.160  24.193 -19.099  1.00 51.04           C  
ANISOU 2205  CB  ASN A 536     5851   7334   6208    807     47   -309       C  
ATOM   2206  CG  ASN A 536     -23.479  23.495 -19.256  1.00 76.37           C  
ANISOU 2206  CG  ASN A 536     8979  10686   9352    770     43   -353       C  
ATOM   2207  OD1 ASN A 536     -24.078  23.053 -18.274  1.00 89.63           O  
ANISOU 2207  OD1 ASN A 536    10686  12325  11046    722     38   -380       O  
ATOM   2208  ND2 ASN A 536     -23.952  23.388 -20.493  1.00 86.48           N  
ANISOU 2208  ND2 ASN A 536    10156  12147  10555    788     46   -363       N  
ATOM   2209  N   ILE A 537     -19.544  22.666 -17.983  1.00 52.22           N  
ANISOU 2209  N   ILE A 537     6156   7167   6517    677    -12   -414       N  
ATOM   2210  CA  ILE A 537     -18.676  21.505 -17.795  1.00 50.50           C  
ANISOU 2210  CA  ILE A 537     5974   6868   6345    612    -39   -481       C  
ATOM   2211  C   ILE A 537     -18.614  21.123 -16.308  1.00 55.33           C  
ANISOU 2211  C   ILE A 537     6661   7353   7008    572    -44   -491       C  
ATOM   2212  O   ILE A 537     -18.746  19.950 -15.951  1.00 62.12           O  
ANISOU 2212  O   ILE A 537     7537   8180   7885    512    -52   -551       O  
ATOM   2213  CB  ILE A 537     -17.248  21.775 -18.363  1.00 45.85           C  
ANISOU 2213  CB  ILE A 537     5404   6235   5780    636    -50   -468       C  
ATOM   2214  CG1 ILE A 537     -17.264  21.734 -19.891  1.00 54.34           C  
ANISOU 2214  CG1 ILE A 537     6401   7438   6807    657    -52   -481       C  
ATOM   2215  CG2 ILE A 537     -16.229  20.770 -17.844  1.00 33.87           C  
ANISOU 2215  CG2 ILE A 537     3942   4612   4315    589    -71   -516       C  
ATOM   2216  CD1 ILE A 537     -16.004  22.279 -20.539  1.00 46.54           C  
ANISOU 2216  CD1 ILE A 537     5423   6427   5832    694    -57   -454       C  
ATOM   2217  N   LEU A 538     -18.433  22.119 -15.443  1.00 50.82           N  
ANISOU 2217  N   LEU A 538     6140   6711   6460    605    -30   -431       N  
ATOM   2218  CA  LEU A 538     -18.326  21.883 -13.996  1.00 58.25           C  
ANISOU 2218  CA  LEU A 538     7146   7539   7445    571    -34   -434       C  
ATOM   2219  C   LEU A 538     -19.661  21.538 -13.318  1.00 55.55           C  
ANISOU 2219  C   LEU A 538     6796   7222   7089    544    -28   -448       C  
ATOM   2220  O   LEU A 538     -19.728  20.635 -12.478  1.00 41.66           O  
ANISOU 2220  O   LEU A 538     5071   5399   5359    493    -37   -486       O  
ATOM   2221  CB  LEU A 538     -17.696  23.094 -13.305  1.00 55.50           C  
ANISOU 2221  CB  LEU A 538     6851   7116   7121    604    -16   -374       C  
ATOM   2222  CG  LEU A 538     -16.295  23.442 -13.808  1.00 49.31           C  
ANISOU 2222  CG  LEU A 538     6083   6303   6351    619    -20   -365       C  
ATOM   2223  CD1 LEU A 538     -15.903  24.845 -13.384  1.00 51.02           C  
ANISOU 2223  CD1 LEU A 538     6341   6472   6573    648     15   -307       C  
ATOM   2224  CD2 LEU A 538     -15.295  22.418 -13.323  1.00 40.48           C  
ANISOU 2224  CD2 LEU A 538     4994   5117   5268    577    -48   -407       C  
ATOM   2225  N   ALA A 539     -20.715  22.264 -13.682  1.00 55.67           N  
ANISOU 2225  N   ALA A 539     6763   7332   7055    583     -8   -413       N  
ATOM   2226  CA  ALA A 539     -22.053  21.991 -13.163  1.00 51.58           C  
ANISOU 2226  CA  ALA A 539     6224   6865   6511    560     -2   -426       C  
ATOM   2227  C   ALA A 539     -22.464  20.553 -13.468  1.00 52.75           C  
ANISOU 2227  C   ALA A 539     6341   7056   6644    485    -16   -510       C  
ATOM   2228  O   ALA A 539     -23.006  19.864 -12.609  1.00 62.57           O  
ANISOU 2228  O   ALA A 539     7610   8264   7902    431    -18   -544       O  
ATOM   2229  CB  ALA A 539     -23.063  22.974 -13.739  1.00 53.55           C  
ANISOU 2229  CB  ALA A 539     6412   7239   6694    627     25   -371       C  
ATOM   2230  N   ASN A 540     -22.182  20.098 -14.687  1.00 51.97           N  
ANISOU 2230  N   ASN A 540     6193   7033   6519    476    -22   -547       N  
ATOM   2231  CA  ASN A 540     -22.501  18.732 -15.096  1.00 51.21           C  
ANISOU 2231  CA  ASN A 540     6074   6977   6408    396    -23   -637       C  
ATOM   2232  C   ASN A 540     -21.708  17.648 -14.381  1.00 53.77           C  
ANISOU 2232  C   ASN A 540     6477   7157   6797    341    -27   -683       C  
ATOM   2233  O   ASN A 540     -22.260  16.614 -13.997  1.00 62.53           O  
ANISOU 2233  O   ASN A 540     7602   8250   7907    271    -15   -743       O  
ATOM   2234  CB  ASN A 540     -22.342  18.569 -16.606  1.00 46.94           C  
ANISOU 2234  CB  ASN A 540     5460   6555   5821    400    -24   -666       C  
ATOM   2235  CG  ASN A 540     -23.397  19.325 -17.383  1.00 54.08           C  
ANISOU 2235  CG  ASN A 540     6268   7640   6642    444    -13   -634       C  
ATOM   2236  OD1 ASN A 540     -24.399  19.781 -16.819  1.00 57.86           O  
ANISOU 2236  OD1 ASN A 540     6730   8164   7090    460     -2   -603       O  
ATOM   2237  ND2 ASN A 540     -23.177  19.471 -18.684  1.00 54.54           N  
ANISOU 2237  ND2 ASN A 540     6258   7808   6657    469    -13   -638       N  
ATOM   2238  N   TYR A 541     -20.409  17.873 -14.222  1.00 48.95           N  
ANISOU 2238  N   TYR A 541     5916   6448   6235    376    -39   -654       N  
ATOM   2239  CA  TYR A 541     -19.548  16.914 -13.541  1.00 48.00           C  
ANISOU 2239  CA  TYR A 541     5868   6201   6171    344    -40   -683       C  
ATOM   2240  C   TYR A 541     -19.991  16.767 -12.079  1.00 52.14           C  
ANISOU 2240  C   TYR A 541     6446   6643   6724    322    -35   -670       C  
ATOM   2241  O   TYR A 541     -19.762  15.737 -11.430  1.00 54.40           O  
ANISOU 2241  O   TYR A 541     6784   6842   7042    284    -25   -703       O  
ATOM   2242  CB  TYR A 541     -18.089  17.372 -13.621  1.00 40.15           C  
ANISOU 2242  CB  TYR A 541     4903   5143   5208    393    -56   -644       C  
ATOM   2243  CG  TYR A 541     -17.148  16.537 -12.790  1.00 45.44           C  
ANISOU 2243  CG  TYR A 541     5643   5693   5928    380    -55   -654       C  
ATOM   2244  CD1 TYR A 541     -16.906  15.210 -13.114  1.00 45.27           C  
ANISOU 2244  CD1 TYR A 541     5642   5642   5917    344    -39   -714       C  
ATOM   2245  CD2 TYR A 541     -16.505  17.069 -11.682  1.00 48.63           C  
ANISOU 2245  CD2 TYR A 541     6092   6020   6363    406    -64   -604       C  
ATOM   2246  CE1 TYR A 541     -16.038  14.438 -12.374  1.00 41.79           C  
ANISOU 2246  CE1 TYR A 541     5266   5096   5516    348    -31   -713       C  
ATOM   2247  CE2 TYR A 541     -15.626  16.299 -10.926  1.00 41.65           C  
ANISOU 2247  CE2 TYR A 541     5264   5048   5515    404    -62   -607       C  
ATOM   2248  CZ  TYR A 541     -15.407  14.983 -11.281  1.00 40.23           C  
ANISOU 2248  CZ  TYR A 541     5103   4838   5343    382    -45   -657       C  
ATOM   2249  OH  TYR A 541     -14.566  14.193 -10.548  1.00 49.26           O  
ANISOU 2249  OH  TYR A 541     6303   5897   6517    394    -34   -650       O  
ATOM   2250  N   THR A 542     -20.631  17.814 -11.577  1.00 49.05           N  
ANISOU 2250  N   THR A 542     6041   6278   6318    352    -38   -618       N  
ATOM   2251  CA  THR A 542     -21.106  17.851 -10.200  1.00 56.73           C  
ANISOU 2251  CA  THR A 542     7056   7184   7313    336    -35   -601       C  
ATOM   2252  C   THR A 542     -22.307  16.929  -9.968  1.00 63.17           C  
ANISOU 2252  C   THR A 542     7861   8034   8107    270    -21   -656       C  
ATOM   2253  O   THR A 542     -22.464  16.373  -8.886  1.00 64.31           O  
ANISOU 2253  O   THR A 542     8055   8099   8282    237    -15   -665       O  
ATOM   2254  CB  THR A 542     -21.447  19.298  -9.791  1.00 51.76           C  
ANISOU 2254  CB  THR A 542     6419   6574   6673    388    -33   -531       C  
ATOM   2255  OG1 THR A 542     -20.323  19.872  -9.108  1.00 53.62           O  
ANISOU 2255  OG1 THR A 542     6707   6715   6950    415    -38   -489       O  
ATOM   2256  CG2 THR A 542     -22.644  19.333  -8.889  1.00 55.06           C  
ANISOU 2256  CG2 THR A 542     6839   7002   7078    367    -25   -527       C  
ATOM   2257  N   LYS A 543     -23.126  16.743 -11.002  1.00 61.80           N  
ANISOU 2257  N   LYS A 543     7618   7985   7876    247    -12   -694       N  
ATOM   2258  CA  LYS A 543     -24.408  16.045 -10.872  1.00 60.63           C  
ANISOU 2258  CA  LYS A 543     7444   7903   7689    178      5   -749       C  
ATOM   2259  C   LYS A 543     -24.384  14.749 -10.056  1.00 60.19           C  
ANISOU 2259  C   LYS A 543     7457   7739   7673    105     25   -804       C  
ATOM   2260  O   LYS A 543     -25.290  14.507  -9.260  1.00 66.92           O  
ANISOU 2260  O   LYS A 543     8319   8590   8516     64     35   -816       O  
ATOM   2261  CB  LYS A 543     -25.026  15.787 -12.245  1.00 63.91           C  
ANISOU 2261  CB  LYS A 543     7773   8475   8034    150     16   -801       C  
ATOM   2262  CG  LYS A 543     -25.624  17.023 -12.905  1.00 72.05           C  
ANISOU 2262  CG  LYS A 543     8720   9652   9003    219      7   -744       C  
ATOM   2263  CD  LYS A 543     -26.459  16.641 -14.128  1.00 78.93           C  
ANISOU 2263  CD  LYS A 543     9492  10708   9788    178     20   -802       C  
ATOM   2264  CE  LYS A 543     -26.632  17.816 -15.080  1.00 85.99           C  
ANISOU 2264  CE  LYS A 543    10304  11743  10624    268     14   -737       C  
ATOM   2265  NZ  LYS A 543     -26.652  17.372 -16.510  1.00 91.38           N  
ANISOU 2265  NZ  LYS A 543    10907  12566  11249    241     20   -792       N  
ATOM   2266  N   SER A 544     -23.355  13.928 -10.239  1.00 48.88           N  
ANISOU 2266  N   SER A 544     6074   6216   6281     94     35   -831       N  
ATOM   2267  CA  SER A 544     -23.299  12.608  -9.595  1.00 55.24           C  
ANISOU 2267  CA  SER A 544     6952   6915   7120     32     69   -882       C  
ATOM   2268  C   SER A 544     -22.815  12.561  -8.137  1.00 62.73           C  
ANISOU 2268  C   SER A 544     7977   7731   8126     57     65   -833       C  
ATOM   2269  O   SER A 544     -23.105  11.594  -7.437  1.00 69.11           O  
ANISOU 2269  O   SER A 544     8840   8465   8953      7     98   -865       O  
ATOM   2270  CB  SER A 544     -22.446  11.634 -10.415  1.00 55.81           C  
ANISOU 2270  CB  SER A 544     7051   6946   7207     13     96   -933       C  
ATOM   2271  OG  SER A 544     -21.078  12.027 -10.414  1.00 58.68           O  
ANISOU 2271  OG  SER A 544     7441   7245   7611     89     72   -878       O  
ATOM   2272  N   PHE A 545     -22.049  13.558  -7.691  1.00 55.16           N  
ANISOU 2272  N   PHE A 545     7025   6743   7192    130     33   -759       N  
ATOM   2273  CA  PHE A 545     -21.522  13.565  -6.313  1.00 50.04           C  
ANISOU 2273  CA  PHE A 545     6437   5986   6589    153     28   -713       C  
ATOM   2274  C   PHE A 545     -22.025  14.774  -5.520  1.00 42.52           C  
ANISOU 2274  C   PHE A 545     5467   5058   5631    179      4   -658       C  
ATOM   2275  O   PHE A 545     -21.528  15.099  -4.453  1.00 54.79           O  
ANISOU 2275  O   PHE A 545     7057   6546   7215    204     -6   -613       O  
ATOM   2276  CB  PHE A 545     -19.996  13.556  -6.322  1.00 55.17           C  
ANISOU 2276  CB  PHE A 545     7119   6572   7272    207     19   -680       C  
ATOM   2277  CG  PHE A 545     -19.386  14.795  -6.923  1.00 60.60           C  
ANISOU 2277  CG  PHE A 545     7764   7314   7947    260    -12   -638       C  
ATOM   2278  CD1 PHE A 545     -19.236  15.949  -6.166  1.00 54.11           C  
ANISOU 2278  CD1 PHE A 545     6941   6487   7131    293    -31   -580       C  
ATOM   2279  CD2 PHE A 545     -18.949  14.803  -8.242  1.00 57.67           C  
ANISOU 2279  CD2 PHE A 545     7358   6997   7558    273    -15   -660       C  
ATOM   2280  CE1 PHE A 545     -18.669  17.092  -6.711  1.00 51.69           C  
ANISOU 2280  CE1 PHE A 545     6606   6221   6813    336    -46   -545       C  
ATOM   2281  CE2 PHE A 545     -18.380  15.939  -8.791  1.00 53.65           C  
ANISOU 2281  CE2 PHE A 545     6814   6532   7036    321    -37   -619       C  
ATOM   2282  CZ  PHE A 545     -18.242  17.085  -8.022  1.00 55.11           C  
ANISOU 2282  CZ  PHE A 545     7007   6705   7229    352    -49   -562       C  
ATOM   2283  N   ARG A 546     -23.019  15.432  -6.082  1.00 38.92           N  
ANISOU 2283  N   ARG A 546     4951   4707   5130    175     -1   -661       N  
ATOM   2284  CA  ARG A 546     -23.627  16.626  -5.546  1.00 42.08           C  
ANISOU 2284  CA  ARG A 546     5330   5143   5515    207    -14   -610       C  
ATOM   2285  C   ARG A 546     -24.327  16.380  -4.191  1.00 59.42           C  
ANISOU 2285  C   ARG A 546     7559   7291   7725    174     -9   -606       C  
ATOM   2286  O   ARG A 546     -24.278  17.238  -3.288  1.00 53.26           O  
ANISOU 2286  O   ARG A 546     6796   6480   6961    204    -18   -555       O  
ATOM   2287  CB  ARG A 546     -24.665  17.036  -6.567  1.00 57.20           C  
ANISOU 2287  CB  ARG A 546     7169   7197   7367    208    -10   -624       C  
ATOM   2288  CG  ARG A 546     -25.107  18.445  -6.526  1.00 69.25           C  
ANISOU 2288  CG  ARG A 546     8664   8782   8868    268    -14   -561       C  
ATOM   2289  CD  ARG A 546     -25.837  18.718  -7.819  1.00 66.06           C  
ANISOU 2289  CD  ARG A 546     8178   8527   8395    284     -7   -571       C  
ATOM   2290  NE  ARG A 546     -26.421  20.046  -7.841  1.00 65.37           N  
ANISOU 2290  NE  ARG A 546     8058   8507   8273    353      1   -504       N  
ATOM   2291  CZ  ARG A 546     -27.718  20.281  -7.737  1.00 66.04           C  
ANISOU 2291  CZ  ARG A 546     8096   8694   8304    356     11   -498       C  
ATOM   2292  NH1 ARG A 546     -28.569  19.267  -7.615  1.00 72.07           N  
ANISOU 2292  NH1 ARG A 546     8835   9508   9039    280     11   -561       N  
ATOM   2293  NH2 ARG A 546     -28.162  21.528  -7.776  1.00 75.55           N  
ANISOU 2293  NH2 ARG A 546     9277   9950   9477    434     28   -427       N  
ATOM   2294  N   TYR A 547     -24.990  15.225  -4.055  1.00 55.14           N  
ANISOU 2294  N   TYR A 547     7029   6743   7177    108     10   -663       N  
ATOM   2295  CA  TYR A 547     -25.732  14.911  -2.835  1.00 58.34           C  
ANISOU 2295  CA  TYR A 547     7465   7110   7593     71     17   -664       C  
ATOM   2296  C   TYR A 547     -24.891  14.180  -1.808  1.00 59.80           C  
ANISOU 2296  C   TYR A 547     7724   7165   7832     68     26   -653       C  
ATOM   2297  O   TYR A 547     -25.072  14.364  -0.599  1.00 60.79           O  
ANISOU 2297  O   TYR A 547     7876   7244   7976     70     20   -622       O  
ATOM   2298  CB  TYR A 547     -26.992  14.105  -3.152  1.00 56.12           C  
ANISOU 2298  CB  TYR A 547     7157   6898   7268     -6     40   -731       C  
ATOM   2299  CG  TYR A 547     -28.006  14.906  -3.914  1.00 52.16           C  
ANISOU 2299  CG  TYR A 547     6571   6548   6698      4     31   -730       C  
ATOM   2300  CD1 TYR A 547     -28.024  14.896  -5.302  1.00 58.34           C  
ANISOU 2300  CD1 TYR A 547     7296   7432   7438      4     35   -761       C  
ATOM   2301  CD2 TYR A 547     -28.923  15.703  -3.251  1.00 50.52           C  
ANISOU 2301  CD2 TYR A 547     6339   6391   6467     22     21   -693       C  
ATOM   2302  CE1 TYR A 547     -28.947  15.643  -6.008  1.00 61.94           C  
ANISOU 2302  CE1 TYR A 547     7666   8044   7823     25     30   -751       C  
ATOM   2303  CE2 TYR A 547     -29.851  16.452  -3.947  1.00 55.64           C  
ANISOU 2303  CE2 TYR A 547     6907   7188   7046     46     18   -682       C  
ATOM   2304  CZ  TYR A 547     -29.858  16.422  -5.326  1.00 62.99           C  
ANISOU 2304  CZ  TYR A 547     7777   8227   7931     50     23   -709       C  
ATOM   2305  OH  TYR A 547     -30.777  17.167  -6.032  1.00 72.72           O  
ANISOU 2305  OH  TYR A 547     8922   9624   9085     85     24   -689       O  
ATOM   2306  N   SER A 548     -23.965  13.361  -2.293  1.00 60.82           N  
ANISOU 2306  N   SER A 548     7884   7241   7983     70     41   -674       N  
ATOM   2307  CA  SER A 548     -23.131  12.552  -1.414  1.00 60.23           C  
ANISOU 2307  CA  SER A 548     7879   7054   7953     80     59   -659       C  
ATOM   2308  C   SER A 548     -21.884  13.320  -0.974  1.00 66.33           C  
ANISOU 2308  C   SER A 548     8658   7797   8749    148     32   -595       C  
ATOM   2309  O   SER A 548     -21.239  12.966   0.018  1.00 68.82           O  
ANISOU 2309  O   SER A 548     9015   8042   9091    169     37   -563       O  
ATOM   2310  CB  SER A 548     -22.748  11.242  -2.101  1.00 55.50           C  
ANISOU 2310  CB  SER A 548     7317   6410   7362     53    101   -711       C  
ATOM   2311  OG  SER A 548     -21.908  11.481  -3.211  1.00 60.29           O  
ANISOU 2311  OG  SER A 548     7897   7047   7962     89     90   -713       O  
ATOM   2312  N   ASP A 549     -21.549  14.378  -1.707  1.00 57.61           N  
ANISOU 2312  N   ASP A 549     7509   6753   7628    183      6   -575       N  
ATOM   2313  CA  ASP A 549     -20.393  15.191  -1.354  1.00 51.97           C  
ANISOU 2313  CA  ASP A 549     6798   6022   6928    235    -14   -523       C  
ATOM   2314  C   ASP A 549     -20.597  16.664  -1.662  1.00 52.84           C  
ANISOU 2314  C   ASP A 549     6866   6193   7017    257    -32   -495       C  
ATOM   2315  O   ASP A 549     -19.933  17.210  -2.532  1.00 62.98           O  
ANISOU 2315  O   ASP A 549     8130   7508   8293    287    -39   -486       O  
ATOM   2316  CB  ASP A 549     -19.142  14.687  -2.072  1.00 53.53           C  
ANISOU 2316  CB  ASP A 549     7004   6200   7133    265    -11   -528       C  
ATOM   2317  CG  ASP A 549     -18.757  13.279  -1.656  1.00 61.41           C  
ANISOU 2317  CG  ASP A 549     8056   7124   8154    260     19   -542       C  
ATOM   2318  OD1 ASP A 549     -17.932  13.138  -0.719  1.00 67.64           O  
ANISOU 2318  OD1 ASP A 549     8872   7871   8959    292     19   -501       O  
ATOM   2319  OD2 ASP A 549     -19.292  12.315  -2.253  1.00 56.87           O  
ANISOU 2319  OD2 ASP A 549     7495   6536   7576    224     49   -593       O  
ATOM   2320  N   PRO A 550     -21.506  17.322  -0.931  1.00 62.46           N  
ANISOU 2320  N   PRO A 550     8079   7425   8228    247    -33   -477       N  
ATOM   2321  CA  PRO A 550     -21.789  18.745  -1.162  1.00 57.59           C  
ANISOU 2321  CA  PRO A 550     7435   6856   7592    275    -36   -444       C  
ATOM   2322  C   PRO A 550     -20.554  19.645  -1.025  1.00 54.67           C  
ANISOU 2322  C   PRO A 550     7077   6462   7233    307    -38   -408       C  
ATOM   2323  O   PRO A 550     -20.523  20.687  -1.660  1.00 48.12           O  
ANISOU 2323  O   PRO A 550     6229   5668   6386    335    -30   -388       O  
ATOM   2324  CB  PRO A 550     -22.814  19.088  -0.062  1.00 55.40           C  
ANISOU 2324  CB  PRO A 550     7166   6573   7312    257    -32   -430       C  
ATOM   2325  CG  PRO A 550     -23.408  17.785   0.324  1.00 56.43           C  
ANISOU 2325  CG  PRO A 550     7310   6682   7449    212    -29   -468       C  
ATOM   2326  CD  PRO A 550     -22.314  16.769   0.172  1.00 59.67           C  
ANISOU 2326  CD  PRO A 550     7750   7038   7884    211    -27   -484       C  
ATOM   2327  N   ARG A 551     -19.574  19.269  -0.204  1.00 56.48           N  
ANISOU 2327  N   ARG A 551     7336   6640   7485    302    -44   -400       N  
ATOM   2328  CA  ARG A 551     -18.340  20.049  -0.092  1.00 58.01           C  
ANISOU 2328  CA  ARG A 551     7533   6828   7679    320    -44   -375       C  
ATOM   2329  C   ARG A 551     -17.478  19.967  -1.357  1.00 51.77           C  
ANISOU 2329  C   ARG A 551     6726   6064   6880    345    -49   -384       C  
ATOM   2330  O   ARG A 551     -16.806  20.930  -1.727  1.00 48.71           O  
ANISOU 2330  O   ARG A 551     6332   5694   6483    359    -43   -368       O  
ATOM   2331  CB  ARG A 551     -17.508  19.607   1.110  1.00 61.38           C  
ANISOU 2331  CB  ARG A 551     7983   7220   8120    311    -49   -362       C  
ATOM   2332  CG  ARG A 551     -18.213  19.768   2.424  1.00 77.47           C  
ANISOU 2332  CG  ARG A 551    10036   9235  10165    286    -44   -350       C  
ATOM   2333  CD  ARG A 551     -17.250  19.708   3.607  1.00 89.84           C  
ANISOU 2333  CD  ARG A 551    11612  10790  11732    280    -47   -330       C  
ATOM   2334  NE  ARG A 551     -17.978  19.625   4.874  1.00 92.88           N  
ANISOU 2334  NE  ARG A 551    12011  11155  12126    256    -44   -322       N  
ATOM   2335  CZ  ARG A 551     -17.494  20.027   6.045  1.00 95.35           C  
ANISOU 2335  CZ  ARG A 551    12324  11473  12433    240    -41   -304       C  
ATOM   2336  NH1 ARG A 551     -16.277  20.553   6.117  1.00 93.91           N  
ANISOU 2336  NH1 ARG A 551    12129  11323  12231    241    -39   -296       N  
ATOM   2337  NH2 ARG A 551     -18.231  19.910   7.143  1.00101.14           N  
ANISOU 2337  NH2 ARG A 551    13067  12189  13174    219    -40   -297       N  
ATOM   2338  N   VAL A 552     -17.470  18.815  -2.012  1.00 46.82           N  
ANISOU 2338  N   VAL A 552     6095   5437   6257    345    -55   -414       N  
ATOM   2339  CA  VAL A 552     -16.697  18.702  -3.243  1.00 53.41           C  
ANISOU 2339  CA  VAL A 552     6911   6299   7083    368    -60   -426       C  
ATOM   2340  C   VAL A 552     -17.419  19.466  -4.355  1.00 53.25           C  
ANISOU 2340  C   VAL A 552     6855   6338   7039    378    -55   -429       C  
ATOM   2341  O   VAL A 552     -16.785  20.120  -5.182  1.00 52.21           O  
ANISOU 2341  O   VAL A 552     6706   6236   6896    403    -56   -418       O  
ATOM   2342  CB  VAL A 552     -16.419  17.230  -3.635  1.00 50.86           C  
ANISOU 2342  CB  VAL A 552     6601   5954   6771    366    -57   -459       C  
ATOM   2343  CG1 VAL A 552     -15.579  17.172  -4.878  1.00 47.43           C  
ANISOU 2343  CG1 VAL A 552     6145   5550   6326    390    -63   -471       C  
ATOM   2344  CG2 VAL A 552     -15.708  16.493  -2.486  1.00 40.93           C  
ANISOU 2344  CG2 VAL A 552     5380   4642   5531    372    -53   -442       C  
ATOM   2345  N   ALA A 553     -18.749  19.423  -4.346  1.00 43.49           N  
ANISOU 2345  N   ALA A 553     5605   5127   5791    363    -48   -440       N  
ATOM   2346  CA  ALA A 553     -19.506  20.185  -5.317  1.00 42.03           C  
ANISOU 2346  CA  ALA A 553     5379   5016   5574    383    -40   -433       C  
ATOM   2347  C   ALA A 553     -19.159  21.675  -5.262  1.00 44.92           C  
ANISOU 2347  C   ALA A 553     5751   5382   5934    418    -25   -384       C  
ATOM   2348  O   ALA A 553     -18.992  22.326  -6.297  1.00 49.68           O  
ANISOU 2348  O   ALA A 553     6329   6031   6516    452    -16   -370       O  
ATOM   2349  CB  ALA A 553     -20.979  19.967  -5.119  1.00 44.97           C  
ANISOU 2349  CB  ALA A 553     5732   5428   5926    363    -34   -447       C  
ATOM   2350  N   VAL A 554     -19.022  22.202  -4.051  1.00 44.49           N  
ANISOU 2350  N   VAL A 554     5732   5275   5897    408    -16   -361       N  
ATOM   2351  CA  VAL A 554     -18.745  23.626  -3.850  1.00 41.13           C  
ANISOU 2351  CA  VAL A 554     5326   4837   5467    428     13   -322       C  
ATOM   2352  C   VAL A 554     -17.370  23.980  -4.384  1.00 46.16           C  
ANISOU 2352  C   VAL A 554     5968   5467   6105    435     15   -318       C  
ATOM   2353  O   VAL A 554     -17.155  25.063  -4.942  1.00 45.20           O  
ANISOU 2353  O   VAL A 554     5850   5356   5969    461     44   -293       O  
ATOM   2354  CB  VAL A 554     -18.895  24.031  -2.346  1.00 42.59           C  
ANISOU 2354  CB  VAL A 554     5547   4967   5666    401     26   -308       C  
ATOM   2355  CG1 VAL A 554     -18.106  25.278  -2.024  1.00 33.22           C  
ANISOU 2355  CG1 VAL A 554     4391   3750   4480    399     60   -284       C  
ATOM   2356  CG2 VAL A 554     -20.369  24.235  -2.003  1.00 36.67           C  
ANISOU 2356  CG2 VAL A 554     4791   4236   4906    408     38   -296       C  
ATOM   2357  N   GLU A 555     -16.450  23.035  -4.236  1.00 47.76           N  
ANISOU 2357  N   GLU A 555     6172   5654   6321    417    -13   -342       N  
ATOM   2358  CA  GLU A 555     -15.085  23.195  -4.715  1.00 47.41           C  
ANISOU 2358  CA  GLU A 555     6126   5615   6272    423    -17   -343       C  
ATOM   2359  C   GLU A 555     -15.018  23.357  -6.247  1.00 52.91           C  
ANISOU 2359  C   GLU A 555     6792   6361   6952    455    -17   -346       C  
ATOM   2360  O   GLU A 555     -14.312  24.230  -6.765  1.00 56.23           O  
ANISOU 2360  O   GLU A 555     7214   6791   7361    467      0   -330       O  
ATOM   2361  CB  GLU A 555     -14.260  21.997  -4.271  1.00 50.03           C  
ANISOU 2361  CB  GLU A 555     6461   5931   6617    411    -44   -363       C  
ATOM   2362  CG  GLU A 555     -12.933  22.371  -3.660  1.00 68.39           C  
ANISOU 2362  CG  GLU A 555     8797   8254   8935    398    -43   -353       C  
ATOM   2363  CD  GLU A 555     -13.072  23.242  -2.425  1.00 69.99           C  
ANISOU 2363  CD  GLU A 555     9022   8434   9137    365    -21   -338       C  
ATOM   2364  OE1 GLU A 555     -13.751  22.824  -1.464  1.00 76.03           O  
ANISOU 2364  OE1 GLU A 555     9798   9174   9914    352    -25   -336       O  
ATOM   2365  OE2 GLU A 555     -12.483  24.343  -2.411  1.00 68.87           O  
ANISOU 2365  OE2 GLU A 555     8890   8300   8980    349      5   -330       O  
ATOM   2366  N   TYR A 556     -15.754  22.522  -6.969  1.00 45.38           N  
ANISOU 2366  N   TYR A 556     5808   5441   5993    464    -32   -368       N  
ATOM   2367  CA  TYR A 556     -15.750  22.595  -8.423  1.00 43.90           C  
ANISOU 2367  CA  TYR A 556     5582   5314   5784    492    -33   -374       C  
ATOM   2368  C   TYR A 556     -16.529  23.793  -8.960  1.00 42.11           C  
ANISOU 2368  C   TYR A 556     5340   5129   5531    528     -2   -337       C  
ATOM   2369  O   TYR A 556     -16.183  24.347  -9.995  1.00 48.46           O  
ANISOU 2369  O   TYR A 556     6123   5972   6316    560      9   -322       O  
ATOM   2370  CB  TYR A 556     -16.252  21.285  -9.036  1.00 42.05           C  
ANISOU 2370  CB  TYR A 556     5319   5112   5546    479    -52   -419       C  
ATOM   2371  CG  TYR A 556     -15.203  20.209  -9.022  1.00 41.08           C  
ANISOU 2371  CG  TYR A 556     5211   4955   5442    467    -70   -448       C  
ATOM   2372  CD1 TYR A 556     -14.969  19.455  -7.877  1.00 32.99           C  
ANISOU 2372  CD1 TYR A 556     4224   3869   4443    445    -74   -455       C  
ATOM   2373  CD2 TYR A 556     -14.423  19.962 -10.153  1.00 36.97           C  
ANISOU 2373  CD2 TYR A 556     4668   4468   4913    484    -79   -464       C  
ATOM   2374  CE1 TYR A 556     -13.982  18.477  -7.856  1.00 41.62           C  
ANISOU 2374  CE1 TYR A 556     5333   4933   5548    449    -82   -471       C  
ATOM   2375  CE2 TYR A 556     -13.440  18.992 -10.153  1.00 34.45           C  
ANISOU 2375  CE2 TYR A 556     4364   4118   4607    482    -90   -485       C  
ATOM   2376  CZ  TYR A 556     -13.213  18.257  -9.004  1.00 45.34           C  
ANISOU 2376  CZ  TYR A 556     5782   5436   6009    469    -89   -486       C  
ATOM   2377  OH  TYR A 556     -12.227  17.296  -9.003  1.00 52.41           O  
ANISOU 2377  OH  TYR A 556     6695   6305   6914    482    -92   -498       O  
ATOM   2378  N   LEU A 557     -17.574  24.207  -8.260  1.00 45.11           N  
ANISOU 2378  N   LEU A 557     5729   5502   5907    530     17   -317       N  
ATOM   2379  CA  LEU A 557     -18.381  25.315  -8.757  1.00 43.27           C  
ANISOU 2379  CA  LEU A 557     5483   5314   5644    578     55   -274       C  
ATOM   2380  C   LEU A 557     -17.616  26.610  -8.528  1.00 44.25           C  
ANISOU 2380  C   LEU A 557     5654   5385   5776    593     97   -235       C  
ATOM   2381  O   LEU A 557     -17.804  27.600  -9.228  1.00 46.62           O  
ANISOU 2381  O   LEU A 557     5951   5710   6052    642    138   -194       O  
ATOM   2382  CB  LEU A 557     -19.747  25.368  -8.063  1.00 34.28           C  
ANISOU 2382  CB  LEU A 557     4341   4190   4495    580     66   -262       C  
ATOM   2383  CG  LEU A 557     -20.745  24.219  -8.285  1.00 51.04           C  
ANISOU 2383  CG  LEU A 557     6416   6378   6599    558     37   -302       C  
ATOM   2384  CD1 LEU A 557     -22.010  24.286  -7.367  1.00 38.17           C  
ANISOU 2384  CD1 LEU A 557     4788   4755   4959    550     47   -293       C  
ATOM   2385  CD2 LEU A 557     -21.147  24.171  -9.738  1.00 48.53           C  
ANISOU 2385  CD2 LEU A 557     6033   6172   6236    592     38   -304       C  
ATOM   2386  N   VAL A 558     -16.746  26.600  -7.531  1.00 41.80           N  
ANISOU 2386  N   VAL A 558     5385   5004   5492    548     93   -248       N  
ATOM   2387  CA  VAL A 558     -15.971  27.784  -7.207  1.00 43.43           C  
ANISOU 2387  CA  VAL A 558     5639   5161   5702    541    139   -225       C  
ATOM   2388  C   VAL A 558     -14.929  28.053  -8.303  1.00 45.66           C  
ANISOU 2388  C   VAL A 558     5910   5467   5973    554    142   -225       C  
ATOM   2389  O   VAL A 558     -14.484  29.182  -8.507  1.00 48.02           O  
ANISOU 2389  O   VAL A 558     6242   5741   6263    562    194   -200       O  
ATOM   2390  CB  VAL A 558     -15.341  27.631  -5.815  1.00 46.24           C  
ANISOU 2390  CB  VAL A 558     6030   5460   6079    480    131   -246       C  
ATOM   2391  CG1 VAL A 558     -14.171  28.568  -5.632  1.00 52.75           C  
ANISOU 2391  CG1 VAL A 558     6890   6253   6898    450    169   -244       C  
ATOM   2392  CG2 VAL A 558     -16.402  27.865  -4.753  1.00 48.81           C  
ANISOU 2392  CG2 VAL A 558     6378   5756   6413    473    150   -234       C  
ATOM   2393  N   LEU A 559     -14.563  26.999  -9.018  1.00 38.14           N  
ANISOU 2393  N   LEU A 559     4914   4557   5019    555     92   -255       N  
ATOM   2394  CA  LEU A 559     -13.723  27.115 -10.202  1.00 41.01           C  
ANISOU 2394  CA  LEU A 559     5256   4957   5369    574     88   -256       C  
ATOM   2395  C   LEU A 559     -14.366  27.952 -11.309  1.00 47.40           C  
ANISOU 2395  C   LEU A 559     6046   5812   6150    635    126   -215       C  
ATOM   2396  O   LEU A 559     -13.669  28.476 -12.176  1.00 42.30           O  
ANISOU 2396  O   LEU A 559     5398   5183   5492    654    143   -202       O  
ATOM   2397  CB  LEU A 559     -13.388  25.730 -10.749  1.00 33.46           C  
ANISOU 2397  CB  LEU A 559     4257   4039   4416    567     31   -297       C  
ATOM   2398  CG  LEU A 559     -12.390  24.935  -9.927  1.00 38.69           C  
ANISOU 2398  CG  LEU A 559     4936   4666   5098    527      0   -327       C  
ATOM   2399  CD1 LEU A 559     -12.361  23.489 -10.360  1.00 41.65           C  
ANISOU 2399  CD1 LEU A 559     5282   5065   5480    527    -41   -364       C  
ATOM   2400  CD2 LEU A 559     -11.014  25.562 -10.035  1.00 49.77           C  
ANISOU 2400  CD2 LEU A 559     6353   6066   6492    513     11   -323       C  
ATOM   2401  N   ILE A 560     -15.690  28.075 -11.293  1.00 44.48           N  
ANISOU 2401  N   ILE A 560     5661   5472   5766    669    141   -192       N  
ATOM   2402  CA  ILE A 560     -16.370  28.830 -12.339  1.00 51.41           C  
ANISOU 2402  CA  ILE A 560     6512   6412   6608    740    181   -145       C  
ATOM   2403  C   ILE A 560     -15.858  30.272 -12.446  1.00 62.52           C  
ANISOU 2403  C   ILE A 560     7975   7769   8012    767    254    -96       C  
ATOM   2404  O   ILE A 560     -15.807  30.831 -13.537  1.00 64.76           O  
ANISOU 2404  O   ILE A 560     8241   8097   8269    821    283    -61       O  
ATOM   2405  CB  ILE A 560     -17.906  28.825 -12.157  1.00 51.55           C  
ANISOU 2405  CB  ILE A 560     6503   6480   6602    776    192   -121       C  
ATOM   2406  CG1 ILE A 560     -18.459  27.407 -12.331  1.00 46.65           C  
ANISOU 2406  CG1 ILE A 560     5822   5927   5975    746    130   -175       C  
ATOM   2407  CG2 ILE A 560     -18.562  29.782 -13.149  1.00 47.39           C  
ANISOU 2407  CG2 ILE A 560     5951   6024   6030    865    246    -57       C  
ATOM   2408  CD1 ILE A 560     -19.967  27.325 -12.326  1.00 44.03           C  
ANISOU 2408  CD1 ILE A 560     5448   5676   5607    775    138   -159       C  
ATOM   2409  N   THR A 561     -15.482  30.870 -11.317  1.00 67.46           N  
ANISOU 2409  N   THR A 561     8668   8302   8660    725    288    -96       N  
ATOM   2410  CA  THR A 561     -14.987  32.247 -11.312  1.00 64.02           C  
ANISOU 2410  CA  THR A 561     8299   7804   8222    734    372    -60       C  
ATOM   2411  C   THR A 561     -13.521  32.311 -11.721  1.00 62.47           C  
ANISOU 2411  C   THR A 561     8113   7595   8030    691    365    -87       C  
ATOM   2412  O   THR A 561     -12.880  33.358 -11.605  1.00 62.85           O  
ANISOU 2412  O   THR A 561     8221   7584   8076    671    434    -74       O  
ATOM   2413  CB  THR A 561     -15.123  32.894  -9.931  1.00 56.45           C  
ANISOU 2413  CB  THR A 561     7412   6756   7282    693    421    -59       C  
ATOM   2414  OG1 THR A 561     -14.179  32.294  -9.033  1.00 49.99           O  
ANISOU 2414  OG1 THR A 561     6601   5907   6486    605    376   -116       O  
ATOM   2415  CG2 THR A 561     -16.530  32.708  -9.396  1.00 67.17           C  
ANISOU 2415  CG2 THR A 561     8756   8129   8637    728    419    -38       C  
ATOM   2416  N   LEU A 562     -12.992  31.180 -12.173  1.00 58.80           N  
ANISOU 2416  N   LEU A 562     7591   7184   7568    672    287   -128       N  
ATOM   2417  CA  LEU A 562     -11.651  31.137 -12.743  1.00 67.95           C  
ANISOU 2417  CA  LEU A 562     8745   8352   8722    644    272   -152       C  
ATOM   2418  C   LEU A 562     -11.562  32.227 -13.799  1.00 81.28           C  
ANISOU 2418  C   LEU A 562    10448  10048  10387    695    337   -105       C  
ATOM   2419  O   LEU A 562     -10.535  32.878 -13.969  1.00 82.63           O  
ANISOU 2419  O   LEU A 562    10654  10190  10553    664    373   -109       O  
ATOM   2420  CB  LEU A 562     -11.398  29.783 -13.393  1.00 58.04           C  
ANISOU 2420  CB  LEU A 562     7420   7165   7466    646    189   -189       C  
ATOM   2421  CG  LEU A 562      -9.957  29.307 -13.318  1.00 60.13           C  
ANISOU 2421  CG  LEU A 562     7681   7430   7735    596    153   -230       C  
ATOM   2422  CD1 LEU A 562      -9.429  29.562 -11.928  1.00 52.86           C  
ANISOU 2422  CD1 LEU A 562     6808   6452   6826    532    168   -247       C  
ATOM   2423  CD2 LEU A 562      -9.873  27.831 -13.673  1.00 66.40           C  
ANISOU 2423  CD2 LEU A 562     8422   8273   8536    599     79   -268       C  
ATOM   2424  N   ASN A 563     -12.668  32.409 -14.506  1.00 88.44           N  
ANISOU 2424  N   ASN A 563    11326  11001  11275    774    356    -60       N  
ATOM   2425  CA  ASN A 563     -12.837  33.518 -15.421  1.00 97.26           C  
ANISOU 2425  CA  ASN A 563    12461  12126  12366    842    432      2       C  
ATOM   2426  C   ASN A 563     -13.607  34.625 -14.707  1.00105.12           C  
ANISOU 2426  C   ASN A 563    13528  13051  13362    872    524     53       C  
ATOM   2427  O   ASN A 563     -14.647  34.373 -14.098  1.00107.60           O  
ANISOU 2427  O   ASN A 563    13833  13373  13679    890    515     62       O  
ATOM   2428  CB  ASN A 563     -13.575  33.034 -16.669  1.00103.73           C  
ANISOU 2428  CB  ASN A 563    13195  13063  13154    919    399     26       C  
ATOM   2429  CG  ASN A 563     -12.858  31.874 -17.356  1.00106.19           C  
ANISOU 2429  CG  ASN A 563    13440  13440  13467    887    312    -30       C  
ATOM   2430  OD1 ASN A 563     -11.627  31.847 -17.432  1.00110.96           O  
ANISOU 2430  OD1 ASN A 563    14062  14015  14083    839    299    -60       O  
ATOM   2431  ND2 ASN A 563     -13.625  30.909 -17.852  1.00101.15           N  
ANISOU 2431  ND2 ASN A 563    12725  12895  12812    909    258    -48       N  
ATOM   2432  N   GLU A 564     -13.091  35.848 -14.760  1.00109.51           N  
ANISOU 2432  N   GLU A 564    14160  13533  13915    872    619     84       N  
ATOM   2433  CA  GLU A 564     -13.628  36.922 -13.922  1.00109.80           C  
ANISOU 2433  CA  GLU A 564    14284  13477  13958    883    720    121       C  
ATOM   2434  C   GLU A 564     -14.762  37.725 -14.568  1.00107.29           C  
ANISOU 2434  C   GLU A 564    13974  13180  13609   1008    800    212       C  
ATOM   2435  O   GLU A 564     -15.204  38.736 -14.020  1.00103.16           O  
ANISOU 2435  O   GLU A 564    13533  12575  13088   1034    903    255       O  
ATOM   2436  CB  GLU A 564     -12.504  37.849 -13.449  1.00111.38           C  
ANISOU 2436  CB  GLU A 564    14577  13573  14170    802    798     98       C  
ATOM   2437  CG  GLU A 564     -11.601  37.226 -12.392  1.00113.48           C  
ANISOU 2437  CG  GLU A 564    14843  13817  14457    680    738     14       C  
ATOM   2438  CD  GLU A 564     -10.617  38.220 -11.801  1.00118.54           C  
ANISOU 2438  CD  GLU A 564    15573  14368  15098    589    826    -14       C  
ATOM   2439  OE1 GLU A 564      -9.790  37.811 -10.957  1.00119.29           O  
ANISOU 2439  OE1 GLU A 564    15664  14462  15199    487    786    -80       O  
ATOM   2440  OE2 GLU A 564     -10.673  39.411 -12.180  1.00120.90           O  
ANISOU 2440  OE2 GLU A 564    15947  14602  15387    619    943     30       O  
ATOM   2441  N   GLY A 565     -15.235  37.267 -15.724  1.00107.41           N  
ANISOU 2441  N   GLY A 565    13904  13313  13593   1087    758    243       N  
ATOM   2442  CA  GLY A 565     -16.343  37.918 -16.402  1.00106.38           C  
ANISOU 2442  CA  GLY A 565    13760  13239  13422   1218    826    336       C  
ATOM   2443  C   GLY A 565     -17.566  38.054 -15.513  1.00102.93           C  
ANISOU 2443  C   GLY A 565    13337  12790  12980   1254    852    364       C  
ATOM   2444  O   GLY A 565     -17.855  37.164 -14.712  1.00105.16           O  
ANISOU 2444  O   GLY A 565    13588  13086  13282   1193    773    308       O  
ATOM   2445  N   PRO A 566     -18.298  39.171 -15.648  1.00 95.46           N  
ANISOU 2445  N   PRO A 566    12442  11821  12006   1359    967    455       N  
ATOM   2446  CA  PRO A 566     -19.486  39.387 -14.814  1.00 85.38           C  
ANISOU 2446  CA  PRO A 566    11183  10538  10722   1404   1000    489       C  
ATOM   2447  C   PRO A 566     -20.572  38.367 -15.127  1.00 81.70           C  
ANISOU 2447  C   PRO A 566    10592  10235  10217   1447    907    488       C  
ATOM   2448  O   PRO A 566     -21.434  38.111 -14.284  1.00 82.87           O  
ANISOU 2448  O   PRO A 566    10731  10391  10363   1444    891    482       O  
ATOM   2449  CB  PRO A 566     -19.951  40.788 -15.212  1.00 85.90           C  
ANISOU 2449  CB  PRO A 566    11321  10562  10756   1531   1150    599       C  
ATOM   2450  CG  PRO A 566     -19.381  41.022 -16.564  1.00 91.29           C  
ANISOU 2450  CG  PRO A 566    11976  11297  11412   1583   1169    635       C  
ATOM   2451  CD  PRO A 566     -18.116  40.224 -16.663  1.00 93.50           C  
ANISOU 2451  CD  PRO A 566    12231  11565  11729   1454   1071    537       C  
ATOM   2452  N   THR A 567     -20.524  37.786 -16.321  1.00 72.35           N  
ANISOU 2452  N   THR A 567     9310   9183   8996   1480    850    488       N  
ATOM   2453  CA  THR A 567     -21.515  36.797 -16.724  1.00 70.84           C  
ANISOU 2453  CA  THR A 567     8995   9162   8759   1507    768    477       C  
ATOM   2454  C   THR A 567     -21.380  35.462 -15.986  1.00 70.63           C  
ANISOU 2454  C   THR A 567     8932   9134   8770   1383    653    371       C  
ATOM   2455  O   THR A 567     -22.374  34.891 -15.542  1.00 69.95           O  
ANISOU 2455  O   THR A 567     8796   9116   8663   1381    616    358       O  
ATOM   2456  CB  THR A 567     -21.485  36.539 -18.243  1.00 77.79           C  
ANISOU 2456  CB  THR A 567     9777  10193   9586   1568    743    500       C  
ATOM   2457  OG1 THR A 567     -22.371  35.453 -18.562  1.00 69.53           O  
ANISOU 2457  OG1 THR A 567     8609   9316   8495   1564    660    465       O  
ATOM   2458  CG2 THR A 567     -20.055  36.202 -18.708  1.00 80.88           C  
ANISOU 2458  CG2 THR A 567    10181  10531  10018   1487    700    440       C  
ATOM   2459  N   ASP A 568     -20.157  34.961 -15.850  1.00 72.88           N  
ANISOU 2459  N   ASP A 568     9241   9346   9105   1282    603    299       N  
ATOM   2460  CA  ASP A 568     -19.963  33.644 -15.241  1.00 78.00           C  
ANISOU 2460  CA  ASP A 568     9856   9995   9786   1177    501    206       C  
ATOM   2461  C   ASP A 568     -19.786  33.696 -13.714  1.00 69.63           C  
ANISOU 2461  C   ASP A 568     8876   8805   8777   1102    505    174       C  
ATOM   2462  O   ASP A 568     -19.716  32.664 -13.047  1.00 63.26           O  
ANISOU 2462  O   ASP A 568     8050   7989   7996   1023    432    107       O  
ATOM   2463  CB  ASP A 568     -18.830  32.868 -15.932  1.00 83.66           C  
ANISOU 2463  CB  ASP A 568    10539  10727  10519   1117    435    146       C  
ATOM   2464  CG  ASP A 568     -17.499  33.571 -15.835  1.00 93.43           C  
ANISOU 2464  CG  ASP A 568    11857  11851  11792   1083    474    144       C  
ATOM   2465  OD1 ASP A 568     -16.700  33.474 -16.794  1.00 98.15           O  
ANISOU 2465  OD1 ASP A 568    12429  12481  12383   1084    458    136       O  
ATOM   2466  OD2 ASP A 568     -17.249  34.224 -14.799  1.00 96.72           O  
ANISOU 2466  OD2 ASP A 568    12359  12151  12239   1049    523    148       O  
ATOM   2467  N   VAL A 569     -19.721  34.899 -13.160  1.00 66.06           N  
ANISOU 2467  N   VAL A 569     8513   8250   8335   1126    598    221       N  
ATOM   2468  CA  VAL A 569     -19.805  35.046 -11.715  1.00 61.96           C  
ANISOU 2468  CA  VAL A 569     8060   7628   7853   1067    612    198       C  
ATOM   2469  C   VAL A 569     -21.260  34.849 -11.292  1.00 62.24           C  
ANISOU 2469  C   VAL A 569     8059   7726   7861   1115    607    224       C  
ATOM   2470  O   VAL A 569     -21.534  34.302 -10.227  1.00 60.12           O  
ANISOU 2470  O   VAL A 569     7798   7427   7618   1053    567    182       O  
ATOM   2471  CB  VAL A 569     -19.320  36.418 -11.249  1.00 66.99           C  
ANISOU 2471  CB  VAL A 569     8809   8135   8507   1069    725    233       C  
ATOM   2472  CG1 VAL A 569     -19.623  36.601  -9.778  1.00 67.80           C  
ANISOU 2472  CG1 VAL A 569     8972   8150   8638   1016    745    213       C  
ATOM   2473  CG2 VAL A 569     -17.823  36.578 -11.531  1.00 72.16           C  
ANISOU 2473  CG2 VAL A 569     9500   8731   9185   1001    728    195       C  
ATOM   2474  N   GLU A 570     -22.187  35.287 -12.142  1.00 54.26           N  
ANISOU 2474  N   GLU A 570     7005   6815   6794   1227    649    295       N  
ATOM   2475  CA  GLU A 570     -23.606  35.027 -11.933  1.00 47.98           C  
ANISOU 2475  CA  GLU A 570     6154   6119   5957   1279    638    321       C  
ATOM   2476  C   GLU A 570     -23.909  33.545 -12.115  1.00 49.88           C  
ANISOU 2476  C   GLU A 570     6296   6469   6186   1218    527    249       C  
ATOM   2477  O   GLU A 570     -24.714  32.974 -11.387  1.00 65.00           O  
ANISOU 2477  O   GLU A 570     8186   8412   8097   1188    492    223       O  
ATOM   2478  CB  GLU A 570     -24.475  35.874 -12.875  1.00 48.91           C  
ANISOU 2478  CB  GLU A 570     6239   6340   6004   1425    714    422       C  
ATOM   2479  N   LEU A 571     -23.262  32.910 -13.078  1.00 50.26           N  
ANISOU 2479  N   LEU A 571     6292   6574   6231   1194    476    213       N  
ATOM   2480  CA  LEU A 571     -23.421  31.470 -13.229  1.00 57.76           C  
ANISOU 2480  CA  LEU A 571     7164   7605   7176   1122    382    135       C  
ATOM   2481  C   LEU A 571     -22.998  30.736 -11.956  1.00 61.38           C  
ANISOU 2481  C   LEU A 571     7671   7954   7698   1015    334     65       C  
ATOM   2482  O   LEU A 571     -23.642  29.759 -11.561  1.00 59.93           O  
ANISOU 2482  O   LEU A 571     7446   7816   7508    968    284     18       O  
ATOM   2483  CB  LEU A 571     -22.623  30.947 -14.424  1.00 51.12           C  
ANISOU 2483  CB  LEU A 571     6273   6821   6328   1108    344    103       C  
ATOM   2484  CG  LEU A 571     -23.111  31.408 -15.800  1.00 55.82           C  
ANISOU 2484  CG  LEU A 571     6795   7562   6852   1209    376    163       C  
ATOM   2485  CD1 LEU A 571     -22.083  31.086 -16.888  1.00 41.61           C  
ANISOU 2485  CD1 LEU A 571     4966   5786   5057   1192    347    135       C  
ATOM   2486  CD2 LEU A 571     -24.465  30.786 -16.112  1.00 50.60           C  
ANISOU 2486  CD2 LEU A 571     6031   7074   6122   1229    350    156       C  
ATOM   2487  N   CYS A 572     -21.922  31.207 -11.319  1.00 58.13           N  
ANISOU 2487  N   CYS A 572     7344   7404   7339    975    355     58       N  
ATOM   2488  CA  CYS A 572     -21.405  30.565 -10.106  1.00 56.74           C  
ANISOU 2488  CA  CYS A 572     7209   7132   7216    879    314     -1       C  
ATOM   2489  C   CYS A 572     -22.376  30.688  -8.938  1.00 52.66           C  
ANISOU 2489  C   CYS A 572     6716   6590   6703    874    328      9       C  
ATOM   2490  O   CYS A 572     -22.683  29.703  -8.280  1.00 55.18           O  
ANISOU 2490  O   CYS A 572     7016   6913   7036    816    274    -39       O  
ATOM   2491  CB  CYS A 572     -20.038  31.130  -9.696  1.00 54.25           C  
ANISOU 2491  CB  CYS A 572     6969   6700   6943    837    339    -10       C  
ATOM   2492  SG  CYS A 572     -19.362  30.372  -8.174  1.00 52.26           S  
ANISOU 2492  SG  CYS A 572     6757   6354   6744    728    291    -75       S  
ATOM   2493  N   HIS A 573     -22.848  31.898  -8.676  1.00 53.44           N  
ANISOU 2493  N   HIS A 573     6860   6656   6788    936    406     73       N  
ATOM   2494  CA  HIS A 573     -23.820  32.100  -7.612  1.00 64.18           C  
ANISOU 2494  CA  HIS A 573     8241   7997   8146    940    425     88       C  
ATOM   2495  C   HIS A 573     -25.088  31.295  -7.849  1.00 63.27           C  
ANISOU 2495  C   HIS A 573     8041   8013   7986    960    381     80       C  
ATOM   2496  O   HIS A 573     -25.608  30.679  -6.917  1.00 67.04           O  
ANISOU 2496  O   HIS A 573     8514   8481   8475    909    347     47       O  
ATOM   2497  CB  HIS A 573     -24.162  33.579  -7.449  1.00 65.32           C  
ANISOU 2497  CB  HIS A 573     8451   8090   8277   1018    531    164       C  
ATOM   2498  CG  HIS A 573     -22.975  34.432  -7.168  1.00 68.51           C  
ANISOU 2498  CG  HIS A 573     8945   8365   8721    985    588    164       C  
ATOM   2499  ND1 HIS A 573     -22.976  35.802  -7.366  1.00 70.81           N  
ANISOU 2499  ND1 HIS A 573     9306   8599   9001   1054    700    230       N  
ATOM   2500  CD2 HIS A 573     -21.734  34.121  -6.730  1.00 66.87           C  
ANISOU 2500  CD2 HIS A 573     8771   8081   8557    890    558    105       C  
ATOM   2501  CE1 HIS A 573     -21.796  36.288  -7.048  1.00 76.84           C  
ANISOU 2501  CE1 HIS A 573    10142   9253   9801    989    735    203       C  
ATOM   2502  NE2 HIS A 573     -21.018  35.287  -6.656  1.00 73.91           N  
ANISOU 2502  NE2 HIS A 573     9744   8877   9460    890    646    128       N  
ATOM   2503  N   GLU A 574     -25.579  31.307  -9.087  1.00 54.72           N  
ANISOU 2503  N   GLU A 574     6886   7059   6846   1029    386    110       N  
ATOM   2504  CA  GLU A 574     -26.788  30.565  -9.436  1.00 57.88           C  
ANISOU 2504  CA  GLU A 574     7193   7612   7188   1042    349     98       C  
ATOM   2505  C   GLU A 574     -26.610  29.080  -9.178  1.00 59.50           C  
ANISOU 2505  C   GLU A 574     7366   7824   7417    933    267      5       C  
ATOM   2506  O   GLU A 574     -27.520  28.402  -8.709  1.00 63.58           O  
ANISOU 2506  O   GLU A 574     7847   8397   7914    898    238    -25       O  
ATOM   2507  CB  GLU A 574     -27.180  30.803 -10.896  1.00 58.78           C  
ANISOU 2507  CB  GLU A 574     7226   7878   7229   1128    368    141       C  
ATOM   2508  CG  GLU A 574     -27.949  32.093 -11.105  1.00 80.89           C  
ANISOU 2508  CG  GLU A 574    10032  10725   9978   1257    454    245       C  
ATOM   2509  CD  GLU A 574     -29.122  32.230 -10.135  1.00100.25           C  
ANISOU 2509  CD  GLU A 574    12485  13198  12406   1275    470    265       C  
ATOM   2510  OE1 GLU A 574     -30.125  31.494 -10.289  1.00105.56           O  
ANISOU 2510  OE1 GLU A 574    13067  14018  13022   1265    430    241       O  
ATOM   2511  OE2 GLU A 574     -29.039  33.077  -9.217  1.00102.95           O  
ANISOU 2511  OE2 GLU A 574    12918  13413  12785   1294    526    301       O  
ATOM   2512  N   ALA A 575     -25.419  28.580  -9.465  1.00 52.13           N  
ANISOU 2512  N   ALA A 575     6451   6829   6526    879    234    -39       N  
ATOM   2513  CA  ALA A 575     -25.159  27.163  -9.315  1.00 48.72           C  
ANISOU 2513  CA  ALA A 575     5998   6395   6118    787    168   -122       C  
ATOM   2514  C   ALA A 575     -25.079  26.808  -7.840  1.00 55.10           C  
ANISOU 2514  C   ALA A 575     6866   7093   6978    722    152   -150       C  
ATOM   2515  O   ALA A 575     -25.461  25.710  -7.437  1.00 59.03           O  
ANISOU 2515  O   ALA A 575     7345   7604   7480    659    113   -204       O  
ATOM   2516  CB  ALA A 575     -23.876  26.790 -10.023  1.00 41.18           C  
ANISOU 2516  CB  ALA A 575     5049   5406   5192    761    145   -153       C  
ATOM   2517  N   LEU A 576     -24.571  27.748  -7.046  1.00 54.34           N  
ANISOU 2517  N   LEU A 576     6842   6889   6917    735    188   -114       N  
ATOM   2518  CA  LEU A 576     -24.406  27.547  -5.619  1.00 55.39           C  
ANISOU 2518  CA  LEU A 576     7029   6921   7094    676    177   -135       C  
ATOM   2519  C   LEU A 576     -25.757  27.647  -4.942  1.00 61.62           C  
ANISOU 2519  C   LEU A 576     7806   7750   7858    690    188   -118       C  
ATOM   2520  O   LEU A 576     -26.054  26.883  -4.027  1.00 63.01           O  
ANISOU 2520  O   LEU A 576     7987   7900   8053    631    156   -155       O  
ATOM   2521  CB  LEU A 576     -23.418  28.558  -5.026  1.00 49.36           C  
ANISOU 2521  CB  LEU A 576     6342   6045   6368    675    219   -110       C  
ATOM   2522  CG  LEU A 576     -21.945  28.186  -5.208  1.00 47.68           C  
ANISOU 2522  CG  LEU A 576     6148   5780   6188    630    193   -144       C  
ATOM   2523  CD1 LEU A 576     -21.017  29.340  -4.829  1.00 50.22           C  
ANISOU 2523  CD1 LEU A 576     6537   6016   6530    627    246   -121       C  
ATOM   2524  CD2 LEU A 576     -21.599  26.929  -4.417  1.00 41.94           C  
ANISOU 2524  CD2 LEU A 576     5421   5021   5493    557    136   -199       C  
ATOM   2525  N   ARG A 577     -26.584  28.580  -5.401  1.00 57.85           N  
ANISOU 2525  N   ARG A 577     7308   7339   7332    773    237    -59       N  
ATOM   2526  CA  ARG A 577     -27.944  28.656  -4.894  1.00 57.86           C  
ANISOU 2526  CA  ARG A 577     7284   7404   7296    796    247    -39       C  
ATOM   2527  C   ARG A 577     -28.652  27.326  -5.119  1.00 60.85           C  
ANISOU 2527  C   ARG A 577     7590   7885   7645    742    190    -98       C  
ATOM   2528  O   ARG A 577     -29.248  26.777  -4.191  1.00 53.38           O  
ANISOU 2528  O   ARG A 577     6647   6928   6707    692    168   -127       O  
ATOM   2529  CB  ARG A 577     -28.721  29.800  -5.545  1.00 60.66           C  
ANISOU 2529  CB  ARG A 577     7617   7840   7591    911    312     42       C  
ATOM   2530  CG  ARG A 577     -28.328  31.167  -5.015  1.00 59.29           C  
ANISOU 2530  CG  ARG A 577     7532   7550   7445    959    389    101       C  
ATOM   2531  CD  ARG A 577     -29.158  32.289  -5.625  1.00 59.60           C  
ANISOU 2531  CD  ARG A 577     7559   7664   7423   1087    467    190       C  
ATOM   2532  NE  ARG A 577     -28.592  33.590  -5.273  1.00 73.50           N  
ANISOU 2532  NE  ARG A 577     9419   9294   9214   1128    555    241       N  
ATOM   2533  CZ  ARG A 577     -27.775  34.298  -6.050  1.00 78.60           C  
ANISOU 2533  CZ  ARG A 577    10099   9899   9866   1167    605    273       C  
ATOM   2534  NH1 ARG A 577     -27.433  33.844  -7.249  1.00 81.65           N  
ANISOU 2534  NH1 ARG A 577    10423  10371  10229   1180    570    264       N  
ATOM   2535  NH2 ARG A 577     -27.305  35.468  -5.632  1.00 76.79           N  
ANISOU 2535  NH2 ARG A 577     9969   9543   9664   1190    695    311       N  
ATOM   2536  N   GLU A 578     -28.564  26.800  -6.341  1.00 60.20           N  
ANISOU 2536  N   GLU A 578     7445   7899   7530    745    170   -121       N  
ATOM   2537  CA  GLU A 578     -29.216  25.536  -6.684  1.00 55.13           C  
ANISOU 2537  CA  GLU A 578     6735   7359   6853    682    128   -187       C  
ATOM   2538  C   GLU A 578     -28.604  24.341  -5.961  1.00 59.07           C  
ANISOU 2538  C   GLU A 578     7275   7757   7413    580     86   -260       C  
ATOM   2539  O   GLU A 578     -29.242  23.300  -5.810  1.00 61.36           O  
ANISOU 2539  O   GLU A 578     7535   8094   7685    514     62   -316       O  
ATOM   2540  CB  GLU A 578     -29.198  25.298  -8.191  1.00 54.80           C  
ANISOU 2540  CB  GLU A 578     6617   7447   6759    705    123   -198       C  
ATOM   2541  CG  GLU A 578     -30.123  26.208  -8.973  1.00 68.63           C  
ANISOU 2541  CG  GLU A 578     8301   9349   8427    807    163   -130       C  
ATOM   2542  CD  GLU A 578     -30.202  25.825 -10.434  1.00 87.44           C  
ANISOU 2542  CD  GLU A 578    10593  11884  10748    818    153   -150       C  
ATOM   2543  OE1 GLU A 578     -29.134  25.539 -11.030  1.00 99.34           O  
ANISOU 2543  OE1 GLU A 578    12116  13338  12291    795    137   -177       O  
ATOM   2544  OE2 GLU A 578     -31.329  25.810 -10.986  1.00 89.54           O  
ANISOU 2544  OE2 GLU A 578    10766  12333  10923    849    162   -140       O  
ATOM   2545  N   LEU A 579     -27.365  24.477  -5.513  1.00 52.26           N  
ANISOU 2545  N   LEU A 579     6481   6760   6616    565     82   -258       N  
ATOM   2546  CA  LEU A 579     -26.787  23.422  -4.702  1.00 54.95           C  
ANISOU 2546  CA  LEU A 579     6863   7004   7010    485     49   -312       C  
ATOM   2547  C   LEU A 579     -27.483  23.357  -3.329  1.00 59.63           C  
ANISOU 2547  C   LEU A 579     7486   7555   7617    456     49   -310       C  
ATOM   2548  O   LEU A 579     -27.957  22.296  -2.903  1.00 57.76           O  
ANISOU 2548  O   LEU A 579     7242   7322   7381    393     28   -358       O  
ATOM   2549  CB  LEU A 579     -25.290  23.637  -4.528  1.00 47.27           C  
ANISOU 2549  CB  LEU A 579     5947   5922   6093    483     47   -305       C  
ATOM   2550  CG  LEU A 579     -24.616  22.550  -3.699  1.00 46.50           C  
ANISOU 2550  CG  LEU A 579     5889   5735   6044    417     18   -349       C  
ATOM   2551  CD1 LEU A 579     -24.810  21.220  -4.418  1.00 38.65           C  
ANISOU 2551  CD1 LEU A 579     4861   4789   5036    373     -1   -410       C  
ATOM   2552  CD2 LEU A 579     -23.138  22.868  -3.466  1.00 36.11           C  
ANISOU 2552  CD2 LEU A 579     4618   4332   4769    420     17   -337       C  
ATOM   2553  N   VAL A 580     -27.549  24.495  -2.641  1.00 57.97           N  
ANISOU 2553  N   VAL A 580     7310   7299   7416    498     78   -256       N  
ATOM   2554  CA  VAL A 580     -28.117  24.523  -1.297  1.00 61.81           C  
ANISOU 2554  CA  VAL A 580     7827   7740   7918    472     79   -252       C  
ATOM   2555  C   VAL A 580     -29.613  24.206  -1.318  1.00 59.10           C  
ANISOU 2555  C   VAL A 580     7430   7507   7520    470     76   -261       C  
ATOM   2556  O   VAL A 580     -30.073  23.383  -0.547  1.00 51.89           O  
ANISOU 2556  O   VAL A 580     6521   6581   6616    409     55   -298       O  
ATOM   2557  CB  VAL A 580     -27.819  25.857  -0.537  1.00 61.25           C  
ANISOU 2557  CB  VAL A 580     7812   7591   7868    512    120   -198       C  
ATOM   2558  CG1 VAL A 580     -26.503  26.462  -1.007  1.00 54.44           C  
ANISOU 2558  CG1 VAL A 580     6984   6669   7033    530    138   -183       C  
ATOM   2559  CG2 VAL A 580     -28.948  26.848  -0.693  1.00 61.91           C  
ANISOU 2559  CG2 VAL A 580     7876   7745   7903    584    162   -145       C  
ATOM   2560  N   LEU A 581     -30.353  24.825  -2.233  1.00 63.52           N  
ANISOU 2560  N   LEU A 581     7934   8184   8017    536    100   -227       N  
ATOM   2561  CA  LEU A 581     -31.784  24.581  -2.351  1.00 63.59           C  
ANISOU 2561  CA  LEU A 581     7877   8329   7957    538     99   -233       C  
ATOM   2562  C   LEU A 581     -32.129  23.114  -2.603  1.00 67.53           C  
ANISOU 2562  C   LEU A 581     8335   8885   8439    446     63   -314       C  
ATOM   2563  O   LEU A 581     -33.021  22.561  -1.957  1.00 71.71           O  
ANISOU 2563  O   LEU A 581     8850   9449   8949    397     54   -344       O  
ATOM   2564  CB  LEU A 581     -32.402  25.480  -3.424  1.00 73.76           C  
ANISOU 2564  CB  LEU A 581     9103   9752   9170    636    134   -176       C  
ATOM   2565  CG  LEU A 581     -33.023  26.766  -2.852  1.00 86.94           C  
ANISOU 2565  CG  LEU A 581    10795  11419  10821    723    182    -96       C  
ATOM   2566  CD1 LEU A 581     -32.053  27.496  -1.901  1.00 83.57           C  
ANISOU 2566  CD1 LEU A 581    10470  10811  10473    725    206    -71       C  
ATOM   2567  CD2 LEU A 581     -33.539  27.693  -3.960  1.00 85.94           C  
ANISOU 2567  CD2 LEU A 581    10612  11423  10618    839    228    -26       C  
ATOM   2568  N   GLU A 582     -31.412  22.480  -3.523  1.00 67.07           N  
ANISOU 2568  N   GLU A 582     8263   8832   8388    420     50   -354       N  
ATOM   2569  CA  GLU A 582     -31.696  21.091  -3.877  1.00 67.48           C  
ANISOU 2569  CA  GLU A 582     8284   8932   8422    329     31   -437       C  
ATOM   2570  C   GLU A 582     -31.054  20.017  -2.982  1.00 66.62           C  
ANISOU 2570  C   GLU A 582     8247   8683   8385    247     15   -487       C  
ATOM   2571  O   GLU A 582     -31.555  18.893  -2.923  1.00 61.43           O  
ANISOU 2571  O   GLU A 582     7579   8050   7713    166     12   -553       O  
ATOM   2572  CB  GLU A 582     -31.358  20.834  -5.341  1.00 75.90           C  
ANISOU 2572  CB  GLU A 582     9297  10085   9455    335     31   -462       C  
ATOM   2573  CG  GLU A 582     -32.271  21.566  -6.297  1.00 84.44           C  
ANISOU 2573  CG  GLU A 582    10288  11352  10445    403     49   -426       C  
ATOM   2574  CD  GLU A 582     -31.766  21.519  -7.724  1.00 96.71           C  
ANISOU 2574  CD  GLU A 582    11792  12982  11971    424     50   -436       C  
ATOM   2575  OE1 GLU A 582     -31.557  20.406  -8.249  1.00102.20           O  
ANISOU 2575  OE1 GLU A 582    12472  13696  12665    343     38   -515       O  
ATOM   2576  OE2 GLU A 582     -31.574  22.598  -8.321  1.00100.32           O  
ANISOU 2576  OE2 GLU A 582    12231  13479  12408    521     69   -366       O  
ATOM   2577  N   THR A 583     -29.964  20.336  -2.288  1.00 61.64           N  
ANISOU 2577  N   THR A 583     7686   7912   7824    266     10   -457       N  
ATOM   2578  CA  THR A 583     -29.366  19.339  -1.398  1.00 56.40           C  
ANISOU 2578  CA  THR A 583     7083   7126   7218    203     -2   -492       C  
ATOM   2579  C   THR A 583     -29.743  19.568   0.071  1.00 59.98           C  
ANISOU 2579  C   THR A 583     7576   7517   7696    193     -3   -468       C  
ATOM   2580  O   THR A 583     -29.796  18.622   0.869  1.00 51.37           O  
ANISOU 2580  O   THR A 583     6520   6366   6633    134     -8   -501       O  
ATOM   2581  CB  THR A 583     -27.843  19.293  -1.530  1.00 54.93           C  
ANISOU 2581  CB  THR A 583     6944   6841   7087    220     -8   -483       C  
ATOM   2582  OG1 THR A 583     -27.281  20.446  -0.899  1.00 54.58           O  
ANISOU 2582  OG1 THR A 583     6931   6739   7069    271     -4   -424       O  
ATOM   2583  CG2 THR A 583     -27.437  19.259  -2.998  1.00 62.34           C  
ANISOU 2583  CG2 THR A 583     7842   7845   8001    241     -7   -499       C  
ATOM   2584  N   LYS A 584     -29.988  20.830   0.414  1.00 59.84           N  
ANISOU 2584  N   LYS A 584     7556   7510   7669    253      7   -410       N  
ATOM   2585  CA  LYS A 584     -30.427  21.214   1.749  1.00 57.58           C  
ANISOU 2585  CA  LYS A 584     7300   7177   7399    248      9   -385       C  
ATOM   2586  C   LYS A 584     -29.428  20.784   2.805  1.00 64.28           C  
ANISOU 2586  C   LYS A 584     8213   7898   8314    215     -2   -390       C  
ATOM   2587  O   LYS A 584     -29.792  20.533   3.956  1.00 72.79           O  
ANISOU 2587  O   LYS A 584     9314   8935   9407    183     -7   -391       O  
ATOM   2588  CB  LYS A 584     -31.807  20.637   2.034  1.00 62.83           C  
ANISOU 2588  CB  LYS A 584     7930   7922   8021    206      6   -415       C  
ATOM   2589  CG  LYS A 584     -32.741  20.817   0.857  1.00 71.07           C  
ANISOU 2589  CG  LYS A 584     8895   9122   8987    230     15   -421       C  
ATOM   2590  CD  LYS A 584     -34.150  20.396   1.161  1.00 75.22           C  
ANISOU 2590  CD  LYS A 584     9376   9748   9456    188     15   -448       C  
ATOM   2591  CE  LYS A 584     -35.058  20.756   0.007  1.00 82.45           C  
ANISOU 2591  CE  LYS A 584    10201  10845  10280    226     27   -442       C  
ATOM   2592  NZ  LYS A 584     -36.427  20.227   0.233  1.00 99.46           N  
ANISOU 2592  NZ  LYS A 584    12302  13122  12368    172     26   -480       N  
ATOM   2593  N   GLU A 585     -28.164  20.702   2.397  1.00 58.74           N  
ANISOU 2593  N   GLU A 585     7533   7142   7642    225     -6   -390       N  
ATOM   2594  CA  GLU A 585     -27.066  20.426   3.311  1.00 50.15           C  
ANISOU 2594  CA  GLU A 585     6496   5953   6606    208    -14   -385       C  
ATOM   2595  C   GLU A 585     -26.652  21.718   3.974  1.00 50.15           C  
ANISOU 2595  C   GLU A 585     6518   5917   6618    240      0   -339       C  
ATOM   2596  O   GLU A 585     -25.515  22.178   3.840  1.00 57.95           O  
ANISOU 2596  O   GLU A 585     7525   6869   7625    257      6   -325       O  
ATOM   2597  CB  GLU A 585     -25.898  19.818   2.557  1.00 54.54           C  
ANISOU 2597  CB  GLU A 585     7060   6483   7181    210    -21   -403       C  
ATOM   2598  CG  GLU A 585     -26.274  18.562   1.814  1.00 61.70           C  
ANISOU 2598  CG  GLU A 585     7951   7418   8074    173    -22   -455       C  
ATOM   2599  CD  GLU A 585     -26.313  17.365   2.720  1.00 61.33           C  
ANISOU 2599  CD  GLU A 585     7942   7307   8053    125    -21   -480       C  
ATOM   2600  OE1 GLU A 585     -25.555  17.359   3.707  1.00 68.98           O  
ANISOU 2600  OE1 GLU A 585     8948   8206   9056    132    -25   -454       O  
ATOM   2601  OE2 GLU A 585     -27.093  16.434   2.445  1.00 63.85           O  
ANISOU 2601  OE2 GLU A 585     8254   7651   8355     78    -10   -525       O  
ATOM   2602  N   PHE A 586     -27.597  22.291   4.704  1.00 55.98           N  
ANISOU 2602  N   PHE A 586     7257   6670   7344    243     11   -321       N  
ATOM   2603  CA  PHE A 586     -27.457  23.625   5.257  1.00 53.35           C  
ANISOU 2603  CA  PHE A 586     6946   6309   7014    272     39   -281       C  
ATOM   2604  C   PHE A 586     -26.268  23.792   6.194  1.00 48.40           C  
ANISOU 2604  C   PHE A 586     6360   5606   6426    247     40   -277       C  
ATOM   2605  O   PHE A 586     -25.479  24.731   6.060  1.00 42.39           O  
ANISOU 2605  O   PHE A 586     5618   4820   5669    264     66   -259       O  
ATOM   2606  CB  PHE A 586     -28.748  24.004   5.959  1.00 44.77           C  
ANISOU 2606  CB  PHE A 586     5853   5251   5907    276     51   -266       C  
ATOM   2607  CG  PHE A 586     -29.950  23.967   5.063  1.00 45.50           C  
ANISOU 2607  CG  PHE A 586     5896   5445   5948    306     54   -265       C  
ATOM   2608  CD1 PHE A 586     -31.116  23.335   5.472  1.00 37.99           C  
ANISOU 2608  CD1 PHE A 586     4918   4545   4972    276     39   -285       C  
ATOM   2609  CD2 PHE A 586     -29.915  24.565   3.807  1.00 36.35           C  
ANISOU 2609  CD2 PHE A 586     4711   4343   4759    363     74   -244       C  
ATOM   2610  CE1 PHE A 586     -32.237  23.317   4.665  1.00 39.31           C  
ANISOU 2610  CE1 PHE A 586     5028   4829   5078    299     44   -286       C  
ATOM   2611  CE2 PHE A 586     -31.040  24.545   2.988  1.00 45.60           C  
ANISOU 2611  CE2 PHE A 586     5824   5632   5870    394     79   -240       C  
ATOM   2612  CZ  PHE A 586     -32.202  23.918   3.419  1.00 44.97           C  
ANISOU 2612  CZ  PHE A 586     5713   5614   5760    360     63   -263       C  
ATOM   2613  N   THR A 587     -26.132  22.876   7.138  1.00 42.70           N  
ANISOU 2613  N   THR A 587     5647   4852   5723    205     16   -294       N  
ATOM   2614  CA  THR A 587     -25.031  22.963   8.089  1.00 48.69           C  
ANISOU 2614  CA  THR A 587     6431   5561   6506    182     15   -289       C  
ATOM   2615  C   THR A 587     -23.683  23.063   7.364  1.00 49.36           C  
ANISOU 2615  C   THR A 587     6518   5640   6597    194     16   -291       C  
ATOM   2616  O   THR A 587     -22.929  24.010   7.578  1.00 53.40           O  
ANISOU 2616  O   THR A 587     7044   6138   7108    193     39   -279       O  
ATOM   2617  CB  THR A 587     -25.055  21.771   9.069  1.00 48.52           C  
ANISOU 2617  CB  THR A 587     6416   5518   6502    146     -9   -302       C  
ATOM   2618  OG1 THR A 587     -26.378  21.632   9.611  1.00 54.25           O  
ANISOU 2618  OG1 THR A 587     7137   6257   7220    131    -11   -304       O  
ATOM   2619  CG2 THR A 587     -24.052  21.962  10.207  1.00 43.85           C  
ANISOU 2619  CG2 THR A 587     5839   4900   5924    127     -8   -290       C  
ATOM   2620  N   VAL A 588     -23.401  22.085   6.505  1.00 44.48           N  
ANISOU 2620  N   VAL A 588     5886   5033   5980    202     -3   -309       N  
ATOM   2621  CA  VAL A 588     -22.169  22.044   5.712  1.00 46.43           C  
ANISOU 2621  CA  VAL A 588     6131   5281   6229    218     -6   -311       C  
ATOM   2622  C   VAL A 588     -21.946  23.280   4.820  1.00 46.15           C  
ANISOU 2622  C   VAL A 588     6093   5264   6179    247     19   -297       C  
ATOM   2623  O   VAL A 588     -20.870  23.881   4.839  1.00 42.98           O  
ANISOU 2623  O   VAL A 588     5702   4852   5778    244     32   -291       O  
ATOM   2624  CB  VAL A 588     -22.134  20.786   4.801  1.00 56.71           C  
ANISOU 2624  CB  VAL A 588     7421   6593   7534    224    -24   -336       C  
ATOM   2625  CG1 VAL A 588     -21.050  20.931   3.776  1.00 52.85           C  
ANISOU 2625  CG1 VAL A 588     6923   6115   7041    248    -25   -338       C  
ATOM   2626  CG2 VAL A 588     -21.919  19.515   5.626  1.00 55.48           C  
ANISOU 2626  CG2 VAL A 588     7282   6402   7396    203    -36   -345       C  
ATOM   2627  N   LEU A 589     -22.973  23.642   4.050  1.00 48.96           N  
ANISOU 2627  N   LEU A 589     6433   5655   6516    274     31   -292       N  
ATOM   2628  CA  LEU A 589     -22.943  24.776   3.115  1.00 45.59           C  
ANISOU 2628  CA  LEU A 589     6003   5248   6070    315     63   -269       C  
ATOM   2629  C   LEU A 589     -23.012  26.173   3.748  1.00 42.47           C  
ANISOU 2629  C   LEU A 589     5642   4822   5673    321    111   -241       C  
ATOM   2630  O   LEU A 589     -22.255  27.069   3.377  1.00 54.55           O  
ANISOU 2630  O   LEU A 589     7193   6334   7201    332    145   -229       O  
ATOM   2631  CB  LEU A 589     -24.110  24.643   2.130  1.00 50.87           C  
ANISOU 2631  CB  LEU A 589     6635   5984   6710    350     63   -267       C  
ATOM   2632  CG  LEU A 589     -23.974  23.787   0.863  1.00 54.87           C  
ANISOU 2632  CG  LEU A 589     7105   6540   7204    358     40   -292       C  
ATOM   2633  CD1 LEU A 589     -23.049  22.591   1.046  1.00 62.27           C  
ANISOU 2633  CD1 LEU A 589     8051   7439   8168    321      9   -326       C  
ATOM   2634  CD2 LEU A 589     -25.343  23.348   0.400  1.00 42.28           C  
ANISOU 2634  CD2 LEU A 589     5468   5023   5575    363     34   -304       C  
ATOM   2635  N   LEU A 590     -23.937  26.354   4.688  1.00 39.83           N  
ANISOU 2635  N   LEU A 590     5317   4478   5338    312    120   -233       N  
ATOM   2636  CA  LEU A 590     -24.278  27.671   5.222  1.00 37.17           C  
ANISOU 2636  CA  LEU A 590     5015   4112   4995    324    176   -206       C  
ATOM   2637  C   LEU A 590     -23.738  27.889   6.628  1.00 37.28           C  
ANISOU 2637  C   LEU A 590     5060   4076   5028    267    185   -218       C  
ATOM   2638  O   LEU A 590     -23.799  28.992   7.161  1.00 44.07           O  
ANISOU 2638  O   LEU A 590     5958   4901   5887    262    239   -206       O  
ATOM   2639  CB  LEU A 590     -25.798  27.844   5.243  1.00 52.31           C  
ANISOU 2639  CB  LEU A 590     6918   6068   6890    362    187   -184       C  
ATOM   2640  CG  LEU A 590     -26.466  28.485   4.026  1.00 58.95           C  
ANISOU 2640  CG  LEU A 590     7741   6963   7696    438    221   -149       C  
ATOM   2641  CD1 LEU A 590     -25.794  28.096   2.719  1.00 60.81           C  
ANISOU 2641  CD1 LEU A 590     7948   7232   7924    455    201   -158       C  
ATOM   2642  CD2 LEU A 590     -27.938  28.136   3.999  1.00 59.94           C  
ANISOU 2642  CD2 LEU A 590     7825   7162   7787    465    207   -139       C  
ATOM   2643  N   GLY A 591     -23.224  26.829   7.236  1.00 35.77           N  
ANISOU 2643  N   GLY A 591     4854   3886   4853    226    137   -243       N  
ATOM   2644  CA  GLY A 591     -22.604  26.943   8.537  1.00 35.87           C  
ANISOU 2644  CA  GLY A 591     4882   3872   4875    173    141   -254       C  
ATOM   2645  C   GLY A 591     -23.545  26.575   9.657  1.00 51.04           C  
ANISOU 2645  C   GLY A 591     6801   5789   6802    154    126   -254       C  
ATOM   2646  O   GLY A 591     -24.623  26.013   9.438  1.00 53.85           O  
ANISOU 2646  O   GLY A 591     7141   6166   7155    176    105   -250       O  
ATOM   2647  N   LYS A 592     -23.132  26.910  10.869  1.00 48.40           N  
ANISOU 2647  N   LYS A 592     6481   5439   6471    108    139   -261       N  
ATOM   2648  CA  LYS A 592     -23.876  26.557  12.061  1.00 51.01           C  
ANISOU 2648  CA  LYS A 592     6807   5767   6807     84    124   -261       C  
ATOM   2649  C   LYS A 592     -23.437  27.503  13.182  1.00 54.77           C  
ANISOU 2649  C   LYS A 592     7305   6226   7278     35    165   -270       C  
ATOM   2650  O   LYS A 592     -22.405  28.161  13.069  1.00 48.29           O  
ANISOU 2650  O   LYS A 592     6497   5403   6448     10    196   -282       O  
ATOM   2651  CB  LYS A 592     -23.618  25.086  12.410  1.00 58.88           C  
ANISOU 2651  CB  LYS A 592     7778   6781   7814     73     70   -268       C  
ATOM   2652  CG  LYS A 592     -23.964  24.685  13.831  1.00 72.56           C  
ANISOU 2652  CG  LYS A 592     9506   8512   9550     38     56   -268       C  
ATOM   2653  CD  LYS A 592     -23.279  23.381  14.234  1.00 76.91           C  
ANISOU 2653  CD  LYS A 592    10038   9075  10107     32     19   -267       C  
ATOM   2654  CE  LYS A 592     -21.768  23.551  14.365  1.00 74.92           C  
ANISOU 2654  CE  LYS A 592     9775   8849   9843     19     25   -269       C  
ATOM   2655  NZ  LYS A 592     -21.092  23.631  13.046  1.00 76.22           N  
ANISOU 2655  NZ  LYS A 592     9940   9016  10004     47     27   -274       N  
ATOM   2656  N   ILE A 593     -24.232  27.592  14.248  1.00 49.04           N  
ANISOU 2656  N   ILE A 593     6584   5495   6555     15    168   -268       N  
ATOM   2657  CA  ILE A 593     -23.949  28.513  15.343  1.00 46.06           C  
ANISOU 2657  CA  ILE A 593     6227   5104   6170    -38    212   -282       C  
ATOM   2658  C   ILE A 593     -23.281  27.763  16.488  1.00 48.70           C  
ANISOU 2658  C   ILE A 593     6530   5474   6501    -87    176   -295       C  
ATOM   2659  O   ILE A 593     -23.785  26.728  16.921  1.00 52.87           O  
ANISOU 2659  O   ILE A 593     7034   6015   7037    -77    129   -285       O  
ATOM   2660  CB  ILE A 593     -25.254  29.167  15.863  1.00 48.43           C  
ANISOU 2660  CB  ILE A 593     6552   5378   6471    -26    244   -270       C  
ATOM   2661  CG1 ILE A 593     -25.988  29.886  14.726  1.00 36.50           C  
ANISOU 2661  CG1 ILE A 593     5066   3846   4955     40    284   -246       C  
ATOM   2662  CG2 ILE A 593     -24.977  30.097  17.057  1.00 40.83           C  
ANISOU 2662  CG2 ILE A 593     5614   4399   5502    -89    295   -291       C  
ATOM   2663  CD1 ILE A 593     -25.220  31.042  14.120  1.00 39.52           C  
ANISOU 2663  CD1 ILE A 593     5491   4194   5332     39    354   -248       C  
ATOM   2664  N   GLY A 594     -22.148  28.272  16.967  1.00 38.18           N  
ANISOU 2664  N   GLY A 594     5194   4164   5150   -140    202   -317       N  
ATOM   2665  CA  GLY A 594     -21.490  27.687  18.130  1.00 44.85           C  
ANISOU 2665  CA  GLY A 594     6000   5064   5979   -184    175   -325       C  
ATOM   2666  C   GLY A 594     -21.986  28.190  19.488  1.00 47.18           C  
ANISOU 2666  C   GLY A 594     6297   5362   6266   -235    199   -338       C  
ATOM   2667  O   GLY A 594     -22.709  29.187  19.582  1.00 46.93           O  
ANISOU 2667  O   GLY A 594     6306   5285   6240   -245    248   -346       O  
ATOM   2668  N   ARG A 595     -21.576  27.513  20.555  1.00 53.72           N  
ANISOU 2668  N   ARG A 595     7083   6251   7079   -263    168   -337       N  
ATOM   2669  CA  ARG A 595     -22.034  27.859  21.907  1.00 45.78           C  
ANISOU 2669  CA  ARG A 595     6070   5260   6063   -313    183   -349       C  
ATOM   2670  C   ARG A 595     -21.707  29.283  22.372  1.00 48.55           C  
ANISOU 2670  C   ARG A 595     6445   5609   6392   -388    257   -391       C  
ATOM   2671  O   ARG A 595     -22.236  29.745  23.380  1.00 55.61           O  
ANISOU 2671  O   ARG A 595     7346   6502   7282   -429    281   -405       O  
ATOM   2672  CB  ARG A 595     -21.481  26.877  22.926  1.00 42.19           C  
ANISOU 2672  CB  ARG A 595     5557   4885   5587   -325    141   -336       C  
ATOM   2673  CG  ARG A 595     -22.215  25.569  23.011  1.00 44.81           C  
ANISOU 2673  CG  ARG A 595     5879   5202   5943   -269     86   -297       C  
ATOM   2674  CD  ARG A 595     -22.141  25.066  24.446  1.00 56.19           C  
ANISOU 2674  CD  ARG A 595     7279   6706   7364   -295     69   -286       C  
ATOM   2675  NE  ARG A 595     -23.359  24.358  24.822  1.00 61.27           N  
ANISOU 2675  NE  ARG A 595     7934   7309   8036   -268     41   -263       N  
ATOM   2676  CZ  ARG A 595     -23.621  23.120  24.434  1.00 65.87           C  
ANISOU 2676  CZ  ARG A 595     8519   7869   8638   -214      6   -232       C  
ATOM   2677  NH1 ARG A 595     -22.748  22.482  23.671  1.00 74.46           N  
ANISOU 2677  NH1 ARG A 595     9600   8968   9722   -176     -5   -218       N  
ATOM   2678  NH2 ARG A 595     -24.746  22.527  24.796  1.00 71.54           N  
ANISOU 2678  NH2 ARG A 595     9251   8555   9378   -202    -13   -219       N  
ATOM   2679  N   ASP A 596     -20.831  29.976  21.655  1.00 52.54           N  
ANISOU 2679  N   ASP A 596     6967   6112   6882   -410    299   -414       N  
ATOM   2680  CA  ASP A 596     -20.509  31.362  21.992  1.00 56.39           C  
ANISOU 2680  CA  ASP A 596     7492   6585   7348   -489    385   -460       C  
ATOM   2681  C   ASP A 596     -21.391  32.337  21.218  1.00 55.41           C  
ANISOU 2681  C   ASP A 596     7446   6353   7253   -454    447   -454       C  
ATOM   2682  O   ASP A 596     -21.281  33.556  21.370  1.00 53.12           O  
ANISOU 2682  O   ASP A 596     7208   6023   6953   -508    536   -487       O  
ATOM   2683  CB  ASP A 596     -19.023  31.670  21.762  1.00 65.13           C  
ANISOU 2683  CB  ASP A 596     8576   7756   8413   -549    410   -496       C  
ATOM   2684  CG  ASP A 596     -18.553  31.338  20.344  1.00 71.00           C  
ANISOU 2684  CG  ASP A 596     9325   8482   9168   -488    387   -474       C  
ATOM   2685  OD1 ASP A 596     -19.362  30.836  19.531  1.00 70.42           O  
ANISOU 2685  OD1 ASP A 596     9271   8351   9134   -402    352   -434       O  
ATOM   2686  OD2 ASP A 596     -17.357  31.580  20.047  1.00 74.74           O  
ANISOU 2686  OD2 ASP A 596     9781   9010   9607   -531    406   -501       O  
ATOM   2687  N   GLY A 597     -22.273  31.794  20.387  1.00 46.56           N  
ANISOU 2687  N   GLY A 597     6335   5192   6164   -363    407   -410       N  
ATOM   2688  CA  GLY A 597     -23.187  32.622  19.630  1.00 48.62           C  
ANISOU 2688  CA  GLY A 597     6658   5371   6444   -311    462   -391       C  
ATOM   2689  C   GLY A 597     -22.669  32.987  18.257  1.00 52.38           C  
ANISOU 2689  C   GLY A 597     7161   5819   6921   -275    489   -383       C  
ATOM   2690  O   GLY A 597     -23.402  33.554  17.445  1.00 55.54           O  
ANISOU 2690  O   GLY A 597     7606   6164   7334   -213    529   -355       O  
ATOM   2691  N   ALA A 598     -21.409  32.654  17.991  1.00 50.05           N  
ANISOU 2691  N   ALA A 598     6834   5573   6609   -310    467   -403       N  
ATOM   2692  CA  ALA A 598     -20.768  33.033  16.735  1.00 49.28           C  
ANISOU 2692  CA  ALA A 598     6760   5456   6509   -287    495   -401       C  
ATOM   2693  C   ALA A 598     -20.980  31.972  15.671  1.00 44.35           C  
ANISOU 2693  C   ALA A 598     6101   4846   5901   -203    419   -364       C  
ATOM   2694  O   ALA A 598     -20.939  30.771  15.946  1.00 48.81           O  
ANISOU 2694  O   ALA A 598     6615   5459   6470   -190    342   -355       O  
ATOM   2695  CB  ALA A 598     -19.271  33.283  16.947  1.00 50.42           C  
ANISOU 2695  CB  ALA A 598     6886   5653   6620   -372    516   -446       C  
ATOM   2696  N   ARG A 599     -21.217  32.418  14.450  1.00 43.19           N  
ANISOU 2696  N   ARG A 599     5988   4660   5764   -146    448   -343       N  
ATOM   2697  CA  ARG A 599     -21.378  31.479  13.353  1.00 42.81           C  
ANISOU 2697  CA  ARG A 599     5907   4632   5726    -74    384   -315       C  
ATOM   2698  C   ARG A 599     -20.054  30.792  13.024  1.00 48.04           C  
ANISOU 2698  C   ARG A 599     6530   5346   6377    -97    341   -332       C  
ATOM   2699  O   ARG A 599     -19.005  31.428  12.911  1.00 49.84           O  
ANISOU 2699  O   ARG A 599     6770   5582   6586   -144    382   -357       O  
ATOM   2700  CB  ARG A 599     -21.949  32.165  12.105  1.00 39.94           C  
ANISOU 2700  CB  ARG A 599     5581   4229   5367     -4    429   -285       C  
ATOM   2701  CG  ARG A 599     -22.144  31.211  10.940  1.00 39.94           C  
ANISOU 2701  CG  ARG A 599     5541   4263   5373     63    366   -263       C  
ATOM   2702  CD  ARG A 599     -22.751  31.887   9.724  1.00 41.47           C  
ANISOU 2702  CD  ARG A 599     5760   4436   5561    137    409   -228       C  
ATOM   2703  NE  ARG A 599     -21.865  32.900   9.164  1.00 49.17           N  
ANISOU 2703  NE  ARG A 599     6777   5377   6528    125    479   -234       N  
ATOM   2704  CZ  ARG A 599     -22.067  34.211   9.267  1.00 59.56           C  
ANISOU 2704  CZ  ARG A 599     8157   6633   7838    126    577   -223       C  
ATOM   2705  NH1 ARG A 599     -23.134  34.678   9.901  1.00 62.26           N  
ANISOU 2705  NH1 ARG A 599     8528   6947   8182    148    615   -204       N  
ATOM   2706  NH2 ARG A 599     -21.203  35.060   8.728  1.00 65.43           N  
ANISOU 2706  NH2 ARG A 599     8944   7343   8575    107    644   -232       N  
ATOM   2707  N   ILE A 600     -20.127  29.474  12.904  1.00 40.02           N  
ANISOU 2707  N   ILE A 600     5469   4367   5371    -65    264   -319       N  
ATOM   2708  CA  ILE A 600     -19.041  28.663  12.408  1.00 34.55           C  
ANISOU 2708  CA  ILE A 600     4740   3719   4670    -60    221   -324       C  
ATOM   2709  C   ILE A 600     -19.242  28.480  10.912  1.00 49.86           C  
ANISOU 2709  C   ILE A 600     6682   5642   6619      4    210   -307       C  
ATOM   2710  O   ILE A 600     -20.094  27.698  10.496  1.00 56.18           O  
ANISOU 2710  O   ILE A 600     7470   6440   7435     51    173   -290       O  
ATOM   2711  CB  ILE A 600     -19.051  27.304  13.094  1.00 43.14           C  
ANISOU 2711  CB  ILE A 600     5787   4844   5762    -53    157   -315       C  
ATOM   2712  CG1 ILE A 600     -18.808  27.496  14.596  1.00 42.50           C  
ANISOU 2712  CG1 ILE A 600     5691   4793   5662   -114    168   -329       C  
ATOM   2713  CG2 ILE A 600     -18.011  26.372  12.485  1.00 40.30           C  
ANISOU 2713  CG2 ILE A 600     5394   4525   5394    -30    118   -312       C  
ATOM   2714  CD1 ILE A 600     -18.896  26.227  15.390  1.00 43.93           C  
ANISOU 2714  CD1 ILE A 600     5838   5008   5847   -102    115   -313       C  
ATOM   2715  N   PRO A 601     -18.444  29.193  10.096  1.00 49.31           N  
ANISOU 2715  N   PRO A 601     6628   5570   6538     -1    246   -315       N  
ATOM   2716  CA  PRO A 601     -18.589  29.227   8.637  1.00 51.10           C  
ANISOU 2716  CA  PRO A 601     6859   5786   6769     58    246   -299       C  
ATOM   2717  C   PRO A 601     -18.839  27.860   8.003  1.00 49.96           C  
ANISOU 2717  C   PRO A 601     6676   5669   6637    105    177   -289       C  
ATOM   2718  O   PRO A 601     -18.293  26.850   8.442  1.00 43.13           O  
ANISOU 2718  O   PRO A 601     5782   4832   5772     93    132   -297       O  
ATOM   2719  CB  PRO A 601     -17.239  29.775   8.165  1.00 57.58           C  
ANISOU 2719  CB  PRO A 601     7685   6623   7571     26    274   -317       C  
ATOM   2720  CG  PRO A 601     -16.741  30.577   9.314  1.00 57.96           C  
ANISOU 2720  CG  PRO A 601     7753   6670   7601    -53    322   -345       C  
ATOM   2721  CD  PRO A 601     -17.203  29.849  10.539  1.00 51.47           C  
ANISOU 2721  CD  PRO A 601     6905   5868   6784    -70    282   -345       C  
ATOM   2722  N   GLY A 602     -19.687  27.842   6.980  1.00 52.58           N  
ANISOU 2722  N   GLY A 602     7009   5995   6975    160    176   -271       N  
ATOM   2723  CA  GLY A 602     -19.860  26.664   6.154  1.00 51.49           C  
ANISOU 2723  CA  GLY A 602     6837   5884   6843    196    124   -272       C  
ATOM   2724  C   GLY A 602     -18.846  26.726   5.022  1.00 51.73           C  
ANISOU 2724  C   GLY A 602     6858   5931   6865    212    124   -276       C  
ATOM   2725  O   GLY A 602     -17.990  27.612   4.993  1.00 49.14           O  
ANISOU 2725  O   GLY A 602     6549   5596   6526    190    160   -280       O  
ATOM   2726  N   VAL A 603     -18.944  25.798   4.082  1.00 44.53           N  
ANISOU 2726  N   VAL A 603     5920   5043   5956    245     87   -280       N  
ATOM   2727  CA  VAL A 603     -17.956  25.696   3.023  1.00 50.22           C  
ANISOU 2727  CA  VAL A 603     6628   5785   6670    261     80   -286       C  
ATOM   2728  C   VAL A 603     -18.011  26.882   2.070  1.00 49.42           C  
ANISOU 2728  C   VAL A 603     6541   5682   6556    288    125   -270       C  
ATOM   2729  O   VAL A 603     -16.980  27.390   1.651  1.00 53.72           O  
ANISOU 2729  O   VAL A 603     7091   6228   7090    278    142   -274       O  
ATOM   2730  CB  VAL A 603     -18.115  24.379   2.248  1.00 64.91           C  
ANISOU 2730  CB  VAL A 603     8459   7667   8536    286     37   -299       C  
ATOM   2731  CG1 VAL A 603     -17.346  24.437   0.957  1.00 74.70           C  
ANISOU 2731  CG1 VAL A 603     9684   8931   9766    311     34   -302       C  
ATOM   2732  CG2 VAL A 603     -17.625  23.213   3.106  1.00 69.97           C  
ANISOU 2732  CG2 VAL A 603     9097   8301   9188    266      6   -310       C  
ATOM   2733  N   ILE A 604     -19.214  27.338   1.743  1.00 42.34           N  
ANISOU 2733  N   ILE A 604     5648   4787   5654    323    147   -249       N  
ATOM   2734  CA  ILE A 604     -19.362  28.485   0.859  1.00 39.07           C  
ANISOU 2734  CA  ILE A 604     5250   4372   5224    364    200   -222       C  
ATOM   2735  C   ILE A 604     -18.784  29.774   1.440  1.00 47.96           C  
ANISOU 2735  C   ILE A 604     6429   5446   6348    334    266   -216       C  
ATOM   2736  O   ILE A 604     -18.303  30.632   0.706  1.00 54.71           O  
ANISOU 2736  O   ILE A 604     7306   6290   7193    350    313   -203       O  
ATOM   2737  CB  ILE A 604     -20.821  28.730   0.504  1.00 34.93           C  
ANISOU 2737  CB  ILE A 604     4715   3873   4685    418    217   -193       C  
ATOM   2738  CG1 ILE A 604     -21.403  27.508  -0.205  1.00 43.42           C  
ANISOU 2738  CG1 ILE A 604     5735   5011   5752    436    161   -208       C  
ATOM   2739  CG2 ILE A 604     -20.937  29.950  -0.361  1.00 39.98           C  
ANISOU 2739  CG2 ILE A 604     5376   4511   5305    473    282   -153       C  
ATOM   2740  CD1 ILE A 604     -22.896  27.637  -0.527  1.00 46.15           C  
ANISOU 2740  CD1 ILE A 604     6054   5411   6070    482    172   -184       C  
ATOM   2741  N   GLU A 605     -18.845  29.931   2.755  1.00 54.55           N  
ANISOU 2741  N   GLU A 605     7285   6250   7191    286    277   -227       N  
ATOM   2742  CA  GLU A 605     -18.315  31.145   3.356  1.00 53.87           C  
ANISOU 2742  CA  GLU A 605     7252   6117   7100    242    349   -232       C  
ATOM   2743  C   GLU A 605     -16.792  31.108   3.369  1.00 51.87           C  
ANISOU 2743  C   GLU A 605     6993   5878   6837    186    343   -264       C  
ATOM   2744  O   GLU A 605     -16.144  32.148   3.284  1.00 61.18           O  
ANISOU 2744  O   GLU A 605     8212   7031   8004    153    408   -272       O  
ATOM   2745  CB  GLU A 605     -18.876  31.354   4.758  1.00 55.11           C  
ANISOU 2745  CB  GLU A 605     7430   6245   7263    204    365   -239       C  
ATOM   2746  CG  GLU A 605     -18.595  32.731   5.335  1.00 62.30           C  
ANISOU 2746  CG  GLU A 605     8404   7100   8167    160    458   -245       C  
ATOM   2747  CD  GLU A 605     -19.078  32.888   6.780  1.00 65.98           C  
ANISOU 2747  CD  GLU A 605     8887   7543   8638    113    472   -259       C  
ATOM   2748  OE1 GLU A 605     -20.006  32.151   7.196  1.00 63.47           O  
ANISOU 2748  OE1 GLU A 605     8541   7243   8331    138    423   -247       O  
ATOM   2749  OE2 GLU A 605     -18.525  33.759   7.492  1.00 66.06           O  
ANISOU 2749  OE2 GLU A 605     8939   7521   8639     45    537   -285       O  
ATOM   2750  N   GLU A 606     -16.229  29.908   3.464  1.00 39.64           N  
ANISOU 2750  N   GLU A 606     5397   4375   5290    175    270   -282       N  
ATOM   2751  CA  GLU A 606     -14.782  29.735   3.385  1.00 56.24           C  
ANISOU 2751  CA  GLU A 606     7481   6513   7375    135    256   -308       C  
ATOM   2752  C   GLU A 606     -14.206  30.161   2.018  1.00 59.51           C  
ANISOU 2752  C   GLU A 606     7899   6935   7780    162    275   -302       C  
ATOM   2753  O   GLU A 606     -13.141  30.754   1.952  1.00 59.26           O  
ANISOU 2753  O   GLU A 606     7877   6912   7726    117    307   -321       O  
ATOM   2754  CB  GLU A 606     -14.405  28.281   3.663  1.00 60.99           C  
ANISOU 2754  CB  GLU A 606     8034   7160   7980    141    181   -316       C  
ATOM   2755  CG  GLU A 606     -14.721  27.787   5.062  1.00 63.25           C  
ANISOU 2755  CG  GLU A 606     8312   7448   8270    111    161   -320       C  
ATOM   2756  CD  GLU A 606     -14.613  26.273   5.157  1.00 73.97           C  
ANISOU 2756  CD  GLU A 606     9633   8835   9637    139     97   -317       C  
ATOM   2757  OE1 GLU A 606     -14.262  25.647   4.130  1.00 77.10           O  
ANISOU 2757  OE1 GLU A 606    10011   9247  10035    177     71   -316       O  
ATOM   2758  OE2 GLU A 606     -14.878  25.706   6.244  1.00 75.65           O  
ANISOU 2758  OE2 GLU A 606     9838   9051   9854    124     79   -315       O  
ATOM   2759  N   ARG A 607     -14.915  29.852   0.937  1.00 56.06           N  
ANISOU 2759  N   ARG A 607     7447   6500   7351    230    257   -278       N  
ATOM   2760  CA  ARG A 607     -14.469  30.195  -0.410  1.00 47.20           C  
ANISOU 2760  CA  ARG A 607     6323   5392   6220    264    271   -268       C  
ATOM   2761  C   ARG A 607     -15.042  31.526  -0.883  1.00 54.32           C  
ANISOU 2761  C   ARG A 607     7273   6251   7117    294    353   -237       C  
ATOM   2762  O   ARG A 607     -15.144  31.760  -2.083  1.00 58.06           O  
ANISOU 2762  O   ARG A 607     7740   6739   7583    347    366   -214       O  
ATOM   2763  CB  ARG A 607     -14.895  29.107  -1.404  1.00 38.13           C  
ANISOU 2763  CB  ARG A 607     5125   4284   5077    322    211   -261       C  
ATOM   2764  CG  ARG A 607     -14.228  27.763  -1.199  1.00 39.94           C  
ANISOU 2764  CG  ARG A 607     5316   4547   5311    307    143   -287       C  
ATOM   2765  CD  ARG A 607     -12.725  27.920  -1.172  1.00 42.34           C  
ANISOU 2765  CD  ARG A 607     5616   4874   5597    269    144   -306       C  
ATOM   2766  NE  ARG A 607     -12.048  26.637  -1.100  1.00 44.89           N  
ANISOU 2766  NE  ARG A 607     5903   5235   5920    273     86   -321       N  
ATOM   2767  CZ  ARG A 607     -10.744  26.496  -0.889  1.00 47.27           C  
ANISOU 2767  CZ  ARG A 607     6187   5576   6198    246     76   -335       C  
ATOM   2768  NH1 ARG A 607      -9.980  27.567  -0.730  1.00 50.16           N  
ANISOU 2768  NH1 ARG A 607     6568   5951   6538    198    119   -345       N  
ATOM   2769  NH2 ARG A 607     -10.202  25.285  -0.831  1.00 45.30           N  
ANISOU 2769  NH2 ARG A 607     5907   5359   5947    266     30   -339       N  
ATOM   2770  N   GLN A 608     -15.429  32.402   0.038  1.00 66.90           N  
ANISOU 2770  N   GLN A 608     8916   7792   8711    264    415   -234       N  
ATOM   2771  CA  GLN A 608     -16.135  33.624  -0.377  1.00 68.68           C  
ANISOU 2771  CA  GLN A 608     9195   7968   8932    310    504   -194       C  
ATOM   2772  C   GLN A 608     -15.251  34.602  -1.154  1.00 55.48           C  
ANISOU 2772  C   GLN A 608     7563   6270   7245    300    574   -192       C  
ATOM   2773  O   GLN A 608     -15.714  35.236  -2.099  1.00 51.98           O  
ANISOU 2773  O   GLN A 608     7141   5813   6795    371    624   -148       O  
ATOM   2774  CB  GLN A 608     -16.849  34.323   0.798  1.00 69.47           C  
ANISOU 2774  CB  GLN A 608     9346   8011   9039    286    563   -190       C  
ATOM   2775  CG  GLN A 608     -17.999  35.248   0.348  1.00 71.81           C  
ANISOU 2775  CG  GLN A 608     9685   8270   9331    369    640   -133       C  
ATOM   2776  CD  GLN A 608     -19.153  35.322   1.354  1.00 79.27           C  
ANISOU 2776  CD  GLN A 608    10644   9193  10282    380    652   -119       C  
ATOM   2777  OE1 GLN A 608     -18.943  35.536   2.548  1.00 78.88           O  
ANISOU 2777  OE1 GLN A 608    10623   9106  10241    307    671   -151       O  
ATOM   2778  NE2 GLN A 608     -20.378  35.155   0.865  1.00 82.35           N  
ANISOU 2778  NE2 GLN A 608    11008   9617  10663    470    641    -73       N  
ATOM   2779  N   PRO A 609     -13.983  34.741  -0.747  1.00 50.59           N  
ANISOU 2779  N   PRO A 609     6953   5653   6616    213    581   -237       N  
ATOM   2780  CA  PRO A 609     -13.061  35.551  -1.558  1.00 56.38           C  
ANISOU 2780  CA  PRO A 609     7718   6372   7332    196    641   -241       C  
ATOM   2781  C   PRO A 609     -13.129  35.202  -3.052  1.00 60.37           C  
ANISOU 2781  C   PRO A 609     8187   6917   7835    280    607   -207       C  
ATOM   2782  O   PRO A 609     -13.192  36.105  -3.890  1.00 61.40           O  
ANISOU 2782  O   PRO A 609     8357   7014   7956    320    681   -174       O  
ATOM   2783  CB  PRO A 609     -11.690  35.189  -0.989  1.00 45.39           C  
ANISOU 2783  CB  PRO A 609     6299   5025   5920     98    608   -300       C  
ATOM   2784  CG  PRO A 609     -11.981  34.873   0.470  1.00 53.40           C  
ANISOU 2784  CG  PRO A 609     7309   6041   6941     46    589   -324       C  
ATOM   2785  CD  PRO A 609     -13.365  34.266   0.508  1.00 44.68           C  
ANISOU 2785  CD  PRO A 609     6186   4928   5864    126    546   -285       C  
ATOM   2786  N   LEU A 610     -13.129  33.910  -3.372  1.00 58.54           N  
ANISOU 2786  N   LEU A 610     7880   6754   7609    305    504   -215       N  
ATOM   2787  CA  LEU A 610     -13.149  33.449  -4.764  1.00 59.37           C  
ANISOU 2787  CA  LEU A 610     7941   6909   7709    374    465   -194       C  
ATOM   2788  C   LEU A 610     -14.487  33.673  -5.459  1.00 63.75           C  
ANISOU 2788  C   LEU A 610     8491   7468   8262    469    487   -140       C  
ATOM   2789  O   LEU A 610     -14.607  33.462  -6.664  1.00 72.21           O  
ANISOU 2789  O   LEU A 610     9525   8588   9322    529    468   -117       O  
ATOM   2790  CB  LEU A 610     -12.791  31.960  -4.842  1.00 54.23           C  
ANISOU 2790  CB  LEU A 610     7218   6323   7063    369    359   -223       C  
ATOM   2791  CG  LEU A 610     -11.469  31.600  -4.163  1.00 53.78           C  
ANISOU 2791  CG  LEU A 610     7151   6285   6997    291    332   -269       C  
ATOM   2792  CD1 LEU A 610     -11.165  30.103  -4.239  1.00 43.24           C  
ANISOU 2792  CD1 LEU A 610     5755   5006   5668    302    239   -288       C  
ATOM   2793  CD2 LEU A 610     -10.351  32.429  -4.766  1.00 56.94           C  
ANISOU 2793  CD2 LEU A 610     7573   6686   7374    259    379   -279       C  
ATOM   2794  N   LEU A 611     -15.486  34.104  -4.698  1.00 65.11           N  
ANISOU 2794  N   LEU A 611     8696   7602   8441    484    526   -118       N  
ATOM   2795  CA  LEU A 611     -16.859  34.199  -5.193  1.00 67.64           C  
ANISOU 2795  CA  LEU A 611     9000   7948   8751    576    539    -66       C  
ATOM   2796  C   LEU A 611     -17.169  35.524  -5.879  1.00 61.21           C  
ANISOU 2796  C   LEU A 611     8239   7100   7919    645    646     -6       C  
ATOM   2797  O   LEU A 611     -18.189  35.656  -6.550  1.00 63.38           O  
ANISOU 2797  O   LEU A 611     8489   7419   8172    738    661     47       O  
ATOM   2798  CB  LEU A 611     -17.845  33.973  -4.043  1.00 66.98           C  
ANISOU 2798  CB  LEU A 611     8923   7850   8679    567    530    -67       C  
ATOM   2799  CG  LEU A 611     -18.121  32.533  -3.625  1.00 66.42           C  
ANISOU 2799  CG  LEU A 611     8788   7830   8619    541    427   -103       C  
ATOM   2800  CD1 LEU A 611     -19.150  32.518  -2.510  1.00 66.41           C  
ANISOU 2800  CD1 LEU A 611     8800   7808   8625    536    433    -97       C  
ATOM   2801  CD2 LEU A 611     -18.624  31.747  -4.822  1.00 70.92           C  
ANISOU 2801  CD2 LEU A 611     9288   8487   9172    601    375    -92       C  
ATOM   2802  N   HIS A 612     -16.295  36.506  -5.690  1.00 56.91           N  
ANISOU 2802  N   HIS A 612     7766   6479   7376    598    726    -14       N  
ATOM   2803  CA  HIS A 612     -16.477  37.829  -6.275  1.00 60.11           C  
ANISOU 2803  CA  HIS A 612     8242   6831   7767    658    846     42       C  
ATOM   2804  C   HIS A 612     -17.874  38.405  -6.025  1.00 61.60           C  
ANISOU 2804  C   HIS A 612     8458   7000   7946    745    910    105       C  
ATOM   2805  O   HIS A 612     -18.538  38.893  -6.948  1.00 59.73           O  
ANISOU 2805  O   HIS A 612     8219   6790   7684    855    959    176       O  
ATOM   2806  CB  HIS A 612     -16.147  37.789  -7.769  1.00 63.90           C  
ANISOU 2806  CB  HIS A 612     8683   7368   8227    720    836     72       C  
ATOM   2807  CG  HIS A 612     -14.764  37.285  -8.050  1.00 68.73           C  
ANISOU 2807  CG  HIS A 612     9270   8002   8844    641    780     14       C  
ATOM   2808  ND1 HIS A 612     -13.656  38.114  -8.009  1.00 68.48           N  
ANISOU 2808  ND1 HIS A 612     9303   7906   8810    575    852     -9       N  
ATOM   2809  CD2 HIS A 612     -14.301  36.058  -8.326  1.00 68.50           C  
ANISOU 2809  CD2 HIS A 612     9161   8048   8818    616    668    -27       C  
ATOM   2810  CE1 HIS A 612     -12.577  37.411  -8.268  1.00 74.25           C  
ANISOU 2810  CE1 HIS A 612     9987   8687   9540    516    778    -58       C  
ATOM   2811  NE2 HIS A 612     -12.941  36.139  -8.473  1.00 76.99           N  
ANISOU 2811  NE2 HIS A 612    10246   9115   9891    545    666    -68       N  
ATOM   2812  N   VAL A 613     -18.305  38.357  -4.765  1.00 62.33           N  
ANISOU 2812  N   VAL A 613     8575   7053   8055    700    910     82       N  
ATOM   2813  CA  VAL A 613     -19.629  38.847  -4.386  1.00 63.15           C  
ANISOU 2813  CA  VAL A 613     8703   7141   8149    777    966    137       C  
ATOM   2814  C   VAL A 613     -19.676  40.374  -4.335  1.00 63.81           C  
ANISOU 2814  C   VAL A 613     8901   7117   8227    811   1124    184       C  
ATOM   2815  O   VAL A 613     -18.649  41.035  -4.179  1.00 63.26           O  
ANISOU 2815  O   VAL A 613     8902   6966   8169    735   1191    151       O  
ATOM   2816  CB  VAL A 613     -20.082  38.279  -3.013  1.00 59.35           C  
ANISOU 2816  CB  VAL A 613     8211   6652   7687    715    914     96       C  
ATOM   2817  CG1 VAL A 613     -20.309  36.780  -3.100  1.00 54.99           C  
ANISOU 2817  CG1 VAL A 613     7555   6202   7138    703    775     65       C  
ATOM   2818  CG2 VAL A 613     -19.062  38.612  -1.933  1.00 60.73           C  
ANISOU 2818  CG2 VAL A 613     8446   6743   7885    588    944     32       C  
ATOM   2819  N   ARG A 614     -20.877  40.926  -4.474  1.00 66.84           N  
ANISOU 2819  N   ARG A 614     9302   7503   8589    925   1189    260       N  
ATOM   2820  CA  ARG A 614     -21.076  42.369  -4.388  1.00 73.78           C  
ANISOU 2820  CA  ARG A 614    10299   8271   9462    975   1354    314       C  
ATOM   2821  C   ARG A 614     -20.989  42.880  -2.941  1.00 71.77           C  
ANISOU 2821  C   ARG A 614    10129   7905   9234    881   1417    268       C  
ATOM   2822  O   ARG A 614     -20.451  43.963  -2.695  1.00 73.03           O  
ANISOU 2822  O   ARG A 614    10401   7946   9402    841   1548    262       O  
ATOM   2823  CB  ARG A 614     -22.406  42.765  -5.039  1.00 84.47           C  
ANISOU 2823  CB  ARG A 614    11637   9680  10776   1144   1407    420       C  
ATOM   2824  CG  ARG A 614     -22.368  42.694  -6.563  1.00101.85           C  
ANISOU 2824  CG  ARG A 614    13782  11972  12943   1243   1396    477       C  
ATOM   2825  CD  ARG A 614     -23.751  42.847  -7.203  1.00114.15           C  
ANISOU 2825  CD  ARG A 614    15291  13635  14448   1412   1422    579       C  
ATOM   2826  NE  ARG A 614     -23.663  42.849  -8.663  1.00120.20           N  
ANISOU 2826  NE  ARG A 614    16001  14494  15175   1505   1420    635       N  
ATOM   2827  CZ  ARG A 614     -24.678  42.568  -9.478  1.00127.39           C  
ANISOU 2827  CZ  ARG A 614    16817  15557  16027   1632   1393    704       C  
ATOM   2828  NH1 ARG A 614     -25.870  42.252  -8.980  1.00133.02           N  
ANISOU 2828  NH1 ARG A 614    17480  16349  16712   1680   1363    725       N  
ATOM   2829  NH2 ARG A 614     -24.501  42.593 -10.794  1.00127.22           N  
ANISOU 2829  NH2 ARG A 614    16744  15623  15970   1708   1394    750       N  
ATOM   2830  N   ASP A 615     -21.509  42.094  -1.996  1.00 70.57           N  
ANISOU 2830  N   ASP A 615     9925   7794   9093    841   1328    233       N  
ATOM   2831  CA  ASP A 615     -21.496  42.459  -0.572  1.00 74.96           C  
ANISOU 2831  CA  ASP A 615    10546   8263   9671    751   1373    186       C  
ATOM   2832  C   ASP A 615     -21.210  41.249   0.316  1.00 68.45           C  
ANISOU 2832  C   ASP A 615     9644   7498   8866    645   1234    109       C  
ATOM   2833  O   ASP A 615     -22.020  40.322   0.403  1.00 67.51           O  
ANISOU 2833  O   ASP A 615     9443   7464   8742    685   1135    119       O  
ATOM   2834  CB  ASP A 615     -22.821  43.107  -0.160  1.00 74.25           C  
ANISOU 2834  CB  ASP A 615    10500   8141   9568    849   1455    253       C  
ATOM   2835  CG  ASP A 615     -22.733  43.820   1.177  1.00 80.23           C  
ANISOU 2835  CG  ASP A 615    11353   8784  10347    762   1544    211       C  
ATOM   2836  OD1 ASP A 615     -23.424  44.849   1.337  1.00 85.51           O  
ANISOU 2836  OD1 ASP A 615    12110   9374  11006    836   1677    268       O  
ATOM   2837  OD2 ASP A 615     -21.979  43.362   2.067  1.00 85.13           O  
ANISOU 2837  OD2 ASP A 615    11959   9397  10988    623   1486    124       O  
ATOM   2838  N   GLU A 616     -20.056  41.274   0.977  1.00 65.01           N  
ANISOU 2838  N   GLU A 616     9234   7020   8446    511   1234     32       N  
ATOM   2839  CA  GLU A 616     -19.589  40.145   1.772  1.00 72.33           C  
ANISOU 2839  CA  GLU A 616    10088   8006   9386    414   1111    -37       C  
ATOM   2840  C   GLU A 616     -20.694  39.567   2.648  1.00 79.84           C  
ANISOU 2840  C   GLU A 616    11003   8989  10345    435   1054    -30       C  
ATOM   2841  O   GLU A 616     -20.890  38.354   2.699  1.00 85.82           O  
ANISOU 2841  O   GLU A 616    11673   9828  11106    434    933    -45       O  
ATOM   2842  CB  GLU A 616     -18.401  40.563   2.640  1.00 77.97           C  
ANISOU 2842  CB  GLU A 616    10851   8670  10105    270   1154   -114       C  
ATOM   2843  N   LYS A 617     -21.425  40.440   3.330  1.00 79.51           N  
ANISOU 2843  N   LYS A 617    11032   8876  10304    454   1150     -7       N  
ATOM   2844  CA  LYS A 617     -22.424  39.985   4.289  1.00 79.40           C  
ANISOU 2844  CA  LYS A 617    10989   8886  10295    461   1104     -6       C  
ATOM   2845  C   LYS A 617     -23.808  39.691   3.697  1.00 74.96           C  
ANISOU 2845  C   LYS A 617    10380   8389   9713    595   1076     67       C  
ATOM   2846  O   LYS A 617     -24.504  38.790   4.172  1.00 76.40           O  
ANISOU 2846  O   LYS A 617    10496   8636   9895    597    986     59       O  
ATOM   2847  CB  LYS A 617     -22.508  40.941   5.488  1.00 74.79           C  
ANISOU 2847  CB  LYS A 617    10494   8205   9719    400   1209    -29       C  
ATOM   2848  CG  LYS A 617     -21.259  40.895   6.378  1.00 69.68           C  
ANISOU 2848  CG  LYS A 617     9858   7536   9081    244   1203   -117       C  
ATOM   2849  CD  LYS A 617     -21.372  41.810   7.591  1.00 66.91           C  
ANISOU 2849  CD  LYS A 617     9590   7100   8734    172   1309   -150       C  
ATOM   2850  CE  LYS A 617     -21.292  43.285   7.211  1.00 68.18           C  
ANISOU 2850  CE  LYS A 617     9875   7143   8889    192   1483   -127       C  
ATOM   2851  NZ  LYS A 617     -19.902  43.746   6.918  1.00 72.06           N  
ANISOU 2851  NZ  LYS A 617    10404   7603   9372     90   1538   -182       N  
ATOM   2852  N   GLU A 618     -24.201  40.422   2.659  1.00 67.96           N  
ANISOU 2852  N   GLU A 618     9522   7495   8804    706   1154    137       N  
ATOM   2853  CA  GLU A 618     -25.541  40.245   2.092  1.00 69.35           C  
ANISOU 2853  CA  GLU A 618     9649   7754   8948    838   1139    210       C  
ATOM   2854  C   GLU A 618     -25.723  38.996   1.205  1.00 72.32           C  
ANISOU 2854  C   GLU A 618     9907   8265   9307    867   1009    208       C  
ATOM   2855  O   GLU A 618     -26.848  38.515   1.051  1.00 71.45           O  
ANISOU 2855  O   GLU A 618     9732   8248   9168    936    965    241       O  
ATOM   2856  CB  GLU A 618     -26.009  41.511   1.357  1.00 66.74           C  
ANISOU 2856  CB  GLU A 618     9389   7379   8589    963   1279    298       C  
ATOM   2857  N   PHE A 619     -24.643  38.461   0.633  1.00 65.57           N  
ANISOU 2857  N   PHE A 619     9022   7425   8465    810    953    167       N  
ATOM   2858  CA  PHE A 619     -24.784  37.268  -0.217  1.00 68.77           C  
ANISOU 2858  CA  PHE A 619     9323   7950   8855    831    839    159       C  
ATOM   2859  C   PHE A 619     -25.291  36.016   0.513  1.00 59.10           C  
ANISOU 2859  C   PHE A 619     8030   6787   7640    780    729    115       C  
ATOM   2860  O   PHE A 619     -26.244  35.376   0.074  1.00 55.33           O  
ANISOU 2860  O   PHE A 619     7480   6410   7131    834    679    134       O  
ATOM   2861  CB  PHE A 619     -23.492  36.923  -0.971  1.00 72.04           C  
ANISOU 2861  CB  PHE A 619     9723   8367   9284    783    803    123       C  
ATOM   2862  CG  PHE A 619     -23.610  35.673  -1.799  1.00 71.29           C  
ANISOU 2862  CG  PHE A 619     9527   8386   9175    796    694    107       C  
ATOM   2863  CD1 PHE A 619     -24.390  35.661  -2.942  1.00 77.70           C  
ANISOU 2863  CD1 PHE A 619    10285   9292   9944    899    696    160       C  
ATOM   2864  CD2 PHE A 619     -22.977  34.500  -1.419  1.00 70.26           C  
ANISOU 2864  CD2 PHE A 619     9354   8272   9069    708    596     40       C  
ATOM   2865  CE1 PHE A 619     -24.523  34.509  -3.706  1.00 80.69           C  
ANISOU 2865  CE1 PHE A 619    10572   9780  10306    899    603    136       C  
ATOM   2866  CE2 PHE A 619     -23.109  33.341  -2.181  1.00 72.40           C  
ANISOU 2866  CE2 PHE A 619     9543   8637   9329    716    509     22       C  
ATOM   2867  CZ  PHE A 619     -23.882  33.349  -3.323  1.00 75.31           C  
ANISOU 2867  CZ  PHE A 619     9860   9098   9656    805    512     65       C  
ATOM   2868  N   LEU A 620     -24.630  35.647   1.603  1.00 62.72           N  
ANISOU 2868  N   LEU A 620     8507   7190   8132    674    696     55       N  
ATOM   2869  CA  LEU A 620     -25.047  34.478   2.361  1.00 62.89           C  
ANISOU 2869  CA  LEU A 620     8473   7256   8164    625    602     16       C  
ATOM   2870  C   LEU A 620     -26.345  34.740   3.111  1.00 49.62           C  
ANISOU 2870  C   LEU A 620     6800   5585   6470    662    625     44       C  
ATOM   2871  O   LEU A 620     -27.183  33.861   3.230  1.00 49.95           O  
ANISOU 2871  O   LEU A 620     6781   5700   6499    669    559     38       O  
ATOM   2872  CB  LEU A 620     -23.960  34.041   3.339  1.00 68.30           C  
ANISOU 2872  CB  LEU A 620     9174   7893   8885    512    565    -47       C  
ATOM   2873  CG  LEU A 620     -23.026  32.944   2.833  1.00 74.42           C  
ANISOU 2873  CG  LEU A 620     9898   8708   9670    471    481    -87       C  
ATOM   2874  CD1 LEU A 620     -22.513  32.139   4.019  1.00 81.75           C  
ANISOU 2874  CD1 LEU A 620    10815   9624  10621    383    424   -137       C  
ATOM   2875  CD2 LEU A 620     -23.727  32.034   1.831  1.00 71.56           C  
ANISOU 2875  CD2 LEU A 620     9464   8436   9288    527    420    -75       C  
ATOM   2876  N   HIS A 621     -26.502  35.960   3.606  1.00 40.43           N  
ANISOU 2876  N   HIS A 621     5712   4342   5307    682    727     73       N  
ATOM   2877  CA  HIS A 621     -27.703  36.327   4.330  1.00 55.68           C  
ANISOU 2877  CA  HIS A 621     7657   6276   7223    724    761    105       C  
ATOM   2878  C   HIS A 621     -28.947  36.192   3.465  1.00 62.54           C  
ANISOU 2878  C   HIS A 621     8466   7254   8041    838    753    164       C  
ATOM   2879  O   HIS A 621     -29.997  35.758   3.944  1.00 72.34           O  
ANISOU 2879  O   HIS A 621     9667   8557   9264    854    717    170       O  
ATOM   2880  CB  HIS A 621     -27.604  37.751   4.871  1.00 62.21           C  
ANISOU 2880  CB  HIS A 621     8588   6991   8057    734    890    128       C  
ATOM   2881  CG  HIS A 621     -28.849  38.209   5.574  1.00 71.98           C  
ANISOU 2881  CG  HIS A 621     9845   8228   9277    789    936    167       C  
ATOM   2882  ND1 HIS A 621     -29.116  37.894   6.883  1.00 70.28           N  
ANISOU 2882  ND1 HIS A 621     9631   7992   9080    718    904    127       N  
ATOM   2883  CD2 HIS A 621     -29.892  38.947   5.131  1.00 73.15           C  
ANISOU 2883  CD2 HIS A 621    10008   8400   9386    914   1012    245       C  
ATOM   2884  CE1 HIS A 621     -30.281  38.426   7.230  1.00 72.43           C  
ANISOU 2884  CE1 HIS A 621     9920   8272   9327    793    957    176       C  
ATOM   2885  NE2 HIS A 621     -30.770  39.069   6.187  1.00 74.09           N  
ANISOU 2885  NE2 HIS A 621    10139   8511   9501    915   1024    249       N  
ATOM   2886  N   THR A 622     -28.829  36.561   2.196  1.00 52.33           N  
ANISOU 2886  N   THR A 622     7163   5998   6722    916    787    208       N  
ATOM   2887  CA  THR A 622     -29.969  36.522   1.297  1.00 53.52           C  
ANISOU 2887  CA  THR A 622     7250   6274   6813   1031    788    269       C  
ATOM   2888  C   THR A 622     -30.367  35.087   0.975  1.00 53.16           C  
ANISOU 2888  C   THR A 622     7096   6353   6748    997    668    227       C  
ATOM   2889  O   THR A 622     -31.549  34.732   1.005  1.00 53.15           O  
ANISOU 2889  O   THR A 622     7035   6458   6703   1038    643    245       O  
ATOM   2890  CB  THR A 622     -29.695  37.330   0.014  1.00 56.75           C  
ANISOU 2890  CB  THR A 622     7674   6693   7194   1128    862    331       C  
ATOM   2891  OG1 THR A 622     -29.813  38.727   0.311  1.00 54.63           O  
ANISOU 2891  OG1 THR A 622     7506   6326   6925   1191    996    389       O  
ATOM   2892  CG2 THR A 622     -30.699  36.973  -1.081  1.00 54.86           C  
ANISOU 2892  CG2 THR A 622     7336   6623   6884   1231    835    381       C  
ATOM   2893  N   ILE A 623     -29.376  34.258   0.689  1.00 47.04           N  
ANISOU 2893  N   ILE A 623     6299   5568   6005    917    599    169       N  
ATOM   2894  CA  ILE A 623     -29.632  32.848   0.448  1.00 49.80           C  
ANISOU 2894  CA  ILE A 623     6564   6013   6345    870    496    119       C  
ATOM   2895  C   ILE A 623     -30.249  32.177   1.676  1.00 56.46           C  
ANISOU 2895  C   ILE A 623     7398   6854   7202    807    450     83       C  
ATOM   2896  O   ILE A 623     -31.185  31.383   1.553  1.00 57.50           O  
ANISOU 2896  O   ILE A 623     7460   7089   7297    807    401     70       O  
ATOM   2897  CB  ILE A 623     -28.346  32.114   0.061  1.00 52.93           C  
ANISOU 2897  CB  ILE A 623     6955   6377   6779    796    442     64       C  
ATOM   2898  CG1 ILE A 623     -27.979  32.456  -1.385  1.00 71.84           C  
ANISOU 2898  CG1 ILE A 623     9327   8820   9147    861    466     95       C  
ATOM   2899  CG2 ILE A 623     -28.526  30.626   0.227  1.00 49.97           C  
ANISOU 2899  CG2 ILE A 623     6521   6057   6410    726    349      3       C  
ATOM   2900  CD1 ILE A 623     -26.726  31.776  -1.891  1.00 77.53           C  
ANISOU 2900  CD1 ILE A 623    10040   9518   9899    799    416     46       C  
ATOM   2901  N   THR A 624     -29.721  32.511   2.854  1.00 49.35           N  
ANISOU 2901  N   THR A 624     6564   5838   6347    748    469     63       N  
ATOM   2902  CA  THR A 624     -30.154  31.927   4.117  1.00 41.34           C  
ANISOU 2902  CA  THR A 624     5548   4807   5350    683    428     29       C  
ATOM   2903  C   THR A 624     -31.598  32.325   4.451  1.00 43.73           C  
ANISOU 2903  C   THR A 624     5835   5169   5610    747    457     71       C  
ATOM   2904  O   THR A 624     -32.448  31.474   4.686  1.00 44.24           O  
ANISOU 2904  O   THR A 624     5843   5312   5652    727    402     51       O  
ATOM   2905  CB  THR A 624     -29.209  32.354   5.267  1.00 48.49           C  
ANISOU 2905  CB  THR A 624     6527   5589   6308    611    452      2       C  
ATOM   2906  OG1 THR A 624     -27.871  31.951   4.961  1.00 55.77           O  
ANISOU 2906  OG1 THR A 624     7455   6476   7260    555    423    -35       O  
ATOM   2907  CG2 THR A 624     -29.616  31.709   6.576  1.00 41.10           C  
ANISOU 2907  CG2 THR A 624     5584   4643   5389    545    408    -31       C  
ATOM   2908  N   GLU A 625     -31.870  33.623   4.459  1.00 46.84           N  
ANISOU 2908  N   GLU A 625     6280   5526   5989    823    550    130       N  
ATOM   2909  CA  GLU A 625     -33.221  34.108   4.673  1.00 46.75           C  
ANISOU 2909  CA  GLU A 625     6254   5578   5929    904    589    182       C  
ATOM   2910  C   GLU A 625     -34.213  33.405   3.741  1.00 57.16           C  
ANISOU 2910  C   GLU A 625     7470   7067   7180    955    542    196       C  
ATOM   2911  O   GLU A 625     -35.272  32.974   4.180  1.00 70.33           O  
ANISOU 2911  O   GLU A 625     9091   8817   8814    955    511    193       O  
ATOM   2912  CB  GLU A 625     -33.278  35.624   4.488  1.00 53.08           C  
ANISOU 2912  CB  GLU A 625     7131   6319   6719   1001    712    254       C  
ATOM   2913  CG  GLU A 625     -34.688  36.180   4.324  1.00 62.08           C  
ANISOU 2913  CG  GLU A 625     8245   7553   7791   1123    763    328       C  
ATOM   2914  N   GLN A 626     -33.860  33.278   2.464  1.00 63.22           N  
ANISOU 2914  N   GLN A 626     8200   7896   7926    991    535    206       N  
ATOM   2915  CA  GLN A 626     -34.728  32.629   1.470  1.00 61.97           C  
ANISOU 2915  CA  GLN A 626     7937   7915   7695   1033    495    214       C  
ATOM   2916  C   GLN A 626     -34.996  31.155   1.763  1.00 52.76           C  
ANISOU 2916  C   GLN A 626     6708   6809   6531    927    398    135       C  
ATOM   2917  O   GLN A 626     -36.143  30.719   1.807  1.00 56.87           O  
ANISOU 2917  O   GLN A 626     7161   7454   6993    936    375    132       O  
ATOM   2918  CB  GLN A 626     -34.147  32.768   0.064  1.00 61.70           C  
ANISOU 2918  CB  GLN A 626     7877   7925   7642   1081    508    234       C  
ATOM   2919  CG  GLN A 626     -34.402  34.115  -0.585  1.00 73.61           C  
ANISOU 2919  CG  GLN A 626     9411   9450   9109   1220    609    330       C  
ATOM   2920  CD  GLN A 626     -33.866  34.178  -2.011  1.00 89.34           C  
ANISOU 2920  CD  GLN A 626    11369  11500  11078   1268    616    351       C  
ATOM   2921  OE1 GLN A 626     -32.681  33.926  -2.264  1.00 80.89           O  
ANISOU 2921  OE1 GLN A 626    10329  10345  10061   1204    593    308       O  
ATOM   2922  NE2 GLN A 626     -34.743  34.514  -2.950  1.00 98.51           N  
ANISOU 2922  NE2 GLN A 626    12460  12819  12153   1384    649    418       N  
ATOM   2923  N   ALA A 627     -33.932  30.390   1.953  1.00 43.73           N  
ANISOU 2923  N   ALA A 627     5589   5578   5450    830    348     71       N  
ATOM   2924  CA  ALA A 627     -34.052  28.994   2.349  1.00 42.14           C  
ANISOU 2924  CA  ALA A 627     5350   5400   5261    728    270     -3       C  
ATOM   2925  C   ALA A 627     -34.884  28.833   3.643  1.00 55.11           C  
ANISOU 2925  C   ALA A 627     7003   7032   6905    693    260    -12       C  
ATOM   2926  O   ALA A 627     -35.497  27.784   3.872  1.00 54.65           O  
ANISOU 2926  O   ALA A 627     6897   7037   6828    632    210    -59       O  
ATOM   2927  CB  ALA A 627     -32.667  28.381   2.524  1.00 37.15           C  
ANISOU 2927  CB  ALA A 627     4761   4654   4700    646    235    -54       C  
ATOM   2928  N   ALA A 628     -34.890  29.869   4.482  1.00 48.70           N  
ANISOU 2928  N   ALA A 628     6253   6137   6115    728    312     29       N  
ATOM   2929  CA  ALA A 628     -35.663  29.870   5.721  1.00 50.73           C  
ANISOU 2929  CA  ALA A 628     6523   6381   6373    704    309     26       C  
ATOM   2930  C   ALA A 628     -37.172  29.937   5.475  1.00 55.62           C  
ANISOU 2930  C   ALA A 628     7072   7152   6908    767    317     58       C  
ATOM   2931  O   ALA A 628     -37.938  29.159   6.053  1.00 53.01           O  
ANISOU 2931  O   ALA A 628     6703   6878   6559    713    273     23       O  
ATOM   2932  CB  ALA A 628     -35.227  31.017   6.612  1.00 49.17           C  
ANISOU 2932  CB  ALA A 628     6412   6055   6216    723    372     58       C  
ATOM   2933  N   ARG A 629     -37.599  30.871   4.631  1.00 60.75           N  
ANISOU 2933  N   ARG A 629     7705   7875   7503    882    376    127       N  
ATOM   2934  CA  ARG A 629     -39.014  30.978   4.272  1.00 66.86           C  
ANISOU 2934  CA  ARG A 629     8399   8822   8181    957    387    166       C  
ATOM   2935  C   ARG A 629     -39.493  29.700   3.575  1.00 66.40           C  
ANISOU 2935  C   ARG A 629     8241   8916   8072    896    318    108       C  
ATOM   2936  O   ARG A 629     -40.639  29.293   3.729  1.00 65.80           O  
ANISOU 2936  O   ARG A 629     8097   8974   7930    889    298     99       O  
ATOM   2937  CB  ARG A 629     -39.257  32.200   3.380  1.00 64.33           C  
ANISOU 2937  CB  ARG A 629     8078   8557   7808   1105    471    259       C  
ATOM   2938  N   ARG A 630     -38.596  29.070   2.819  1.00 61.51           N  
ANISOU 2938  N   ARG A 630     7615   8274   7481    845    285     64       N  
ATOM   2939  CA  ARG A 630     -38.896  27.825   2.129  1.00 55.97           C  
ANISOU 2939  CA  ARG A 630     6832   7695   6740    773    229     -2       C  
ATOM   2940  C   ARG A 630     -39.091  26.677   3.109  1.00 56.99           C  
ANISOU 2940  C   ARG A 630     6968   7785   6900    648    175    -78       C  
ATOM   2941  O   ARG A 630     -39.997  25.866   2.947  1.00 58.49           O  
ANISOU 2941  O   ARG A 630     7086   8107   7029    599    148   -120       O  
ATOM   2942  CB  ARG A 630     -37.769  27.490   1.157  1.00 63.80           C  
ANISOU 2942  CB  ARG A 630     7830   8647   7765    751    215    -28       C  
ATOM   2943  CG  ARG A 630     -38.148  26.535   0.037  1.00 70.35           C  
ANISOU 2943  CG  ARG A 630     8565   9635   8530    713    182    -78       C  
ATOM   2944  CD  ARG A 630     -37.064  26.478  -1.033  1.00 56.93           C  
ANISOU 2944  CD  ARG A 630     6870   7904   6856    720    181    -86       C  
ATOM   2945  N   ALA A 631     -38.240  26.615   4.129  1.00 47.51           N  
ANISOU 2945  N   ALA A 631     5853   6409   5790    596    165    -95       N  
ATOM   2946  CA  ALA A 631     -38.321  25.570   5.158  1.00 46.61           C  
ANISOU 2946  CA  ALA A 631     5757   6240   5714    486    121   -157       C  
ATOM   2947  C   ALA A 631     -39.610  25.595   6.004  1.00 53.27           C  
ANISOU 2947  C   ALA A 631     6573   7157   6512    482    120   -151       C  
ATOM   2948  O   ALA A 631     -40.197  24.543   6.294  1.00 40.20           O  
ANISOU 2948  O   ALA A 631     4885   5554   4837    397     86   -208       O  
ATOM   2949  CB  ALA A 631     -37.099  25.632   6.071  1.00 45.60           C  
ANISOU 2949  CB  ALA A 631     5718   5925   5682    447    117   -164       C  
ATOM   2950  N   ASP A 632     -40.046  26.779   6.420  1.00 49.98           N  
ANISOU 2950  N   ASP A 632     6173   6739   6078    570    164    -83       N  
ATOM   2951  CA  ASP A 632     -41.231  26.827   7.262  1.00 72.07           C  
ANISOU 2951  CA  ASP A 632     8946   9604   8833    570    163    -75       C  
ATOM   2952  C   ASP A 632     -42.507  26.661   6.432  1.00 76.47           C  
ANISOU 2952  C   ASP A 632     9397  10383   9276    606    163    -68       C  
ATOM   2953  O   ASP A 632     -43.545  26.271   6.967  1.00 74.99           O  
ANISOU 2953  O   ASP A 632     9167  10286   9040    572    146    -87       O  
ATOM   2954  CB  ASP A 632     -41.259  28.053   8.195  1.00 83.30           C  
ANISOU 2954  CB  ASP A 632    10433  10935  10283    638    211    -13       C  
ATOM   2955  CG  ASP A 632     -41.184  29.370   7.454  1.00 88.46           C  
ANISOU 2955  CG  ASP A 632    11099  11602  10908    770    282     68       C  
ATOM   2956  OD1 ASP A 632     -41.807  29.486   6.376  1.00100.12           O  
ANISOU 2956  OD1 ASP A 632    12503  13235  12305    840    295     97       O  
ATOM   2957  OD2 ASP A 632     -40.514  30.300   7.961  1.00 77.90           O  
ANISOU 2957  OD2 ASP A 632     9845  10126   9627    803    330    101       O  
ATOM   2958  N   GLU A 633     -42.410  26.925   5.126  1.00 68.54           N  
ANISOU 2958  N   GLU A 633     8345   9473   8223    670    182    -44       N  
ATOM   2959  CA  GLU A 633     -43.506  26.642   4.203  1.00 62.68           C  
ANISOU 2959  CA  GLU A 633     7487   8965   7362    692    179    -48       C  
ATOM   2960  C   GLU A 633     -43.572  25.146   3.884  1.00 64.59           C  
ANISOU 2960  C   GLU A 633     7683   9266   7591    553    127   -150       C  
ATOM   2961  O   GLU A 633     -44.646  24.599   3.659  1.00 75.67           O  
ANISOU 2961  O   GLU A 633     8999  10848   8903    515    114   -185       O  
ATOM   2962  CB  GLU A 633     -43.382  27.466   2.918  1.00 61.13           C  
ANISOU 2962  CB  GLU A 633     7252   8860   7114    814    221     19       C  
ATOM   2963  N   ASP A 634     -42.423  24.485   3.883  1.00 63.61           N  
ANISOU 2963  N   ASP A 634     7620   8992   7556    476    104   -201       N  
ATOM   2964  CA  ASP A 634     -42.368  23.044   3.637  1.00 66.68           C  
ANISOU 2964  CA  ASP A 634     7988   9403   7946    344     68   -299       C  
ATOM   2965  C   ASP A 634     -42.677  22.234   4.888  1.00 62.84           C  
ANISOU 2965  C   ASP A 634     7539   8842   7494    241     44   -350       C  
ATOM   2966  O   ASP A 634     -42.737  21.002   4.833  1.00 60.05           O  
ANISOU 2966  O   ASP A 634     7179   8495   7141    125     26   -432       O  
ATOM   2967  CB  ASP A 634     -40.973  22.634   3.151  1.00 75.43           C  
ANISOU 2967  CB  ASP A 634     9151  10374   9133    312     59   -327       C  
ATOM   2968  CG  ASP A 634     -40.775  22.851   1.671  1.00 82.04           C  
ANISOU 2968  CG  ASP A 634     9928  11322   9920    363     72   -317       C  
ATOM   2969  OD1 ASP A 634     -41.584  23.575   1.047  1.00 89.14           O  
ANISOU 2969  OD1 ASP A 634    10753  12388  10730    451     95   -266       O  
ATOM   2970  OD2 ASP A 634     -39.794  22.292   1.134  1.00 81.31           O  
ANISOU 2970  OD2 ASP A 634     9864  11154   9876    321     60   -355       O  
ATOM   2971  N   GLY A 635     -42.832  22.925   6.017  1.00 60.97           N  
ANISOU 2971  N   GLY A 635     7348   8526   7290    281     51   -302       N  
ATOM   2972  CA  GLY A 635     -42.972  22.272   7.308  1.00 53.41           C  
ANISOU 2972  CA  GLY A 635     6438   7477   6380    194     29   -339       C  
ATOM   2973  C   GLY A 635     -41.693  21.641   7.848  1.00 53.80           C  
ANISOU 2973  C   GLY A 635     6576   7328   6538    130     13   -370       C  
ATOM   2974  O   GLY A 635     -41.742  20.831   8.780  1.00 46.02           O  
ANISOU 2974  O   GLY A 635     5625   6273   5588     47     -4   -410       O  
ATOM   2975  N   ARG A 636     -40.544  21.990   7.269  1.00 50.74           N  
ANISOU 2975  N   ARG A 636     6224   6858   6199    172     20   -349       N  
ATOM   2976  CA  ARG A 636     -39.273  21.481   7.783  1.00 54.63           C  
ANISOU 2976  CA  ARG A 636     6794   7176   6787    125      7   -369       C  
ATOM   2977  C   ARG A 636     -38.827  22.256   9.035  1.00 47.51           C  
ANISOU 2977  C   ARG A 636     5955   6151   5945    156     13   -323       C  
ATOM   2978  O   ARG A 636     -38.066  23.222   8.962  1.00 45.98           O  
ANISOU 2978  O   ARG A 636     5796   5893   5783    220     33   -278       O  
ATOM   2979  CB  ARG A 636     -38.197  21.481   6.699  1.00 50.61           C  
ANISOU 2979  CB  ARG A 636     6294   6635   6302    149     12   -371       C  
ATOM   2980  CG  ARG A 636     -38.313  20.321   5.722  1.00 56.86           C  
ANISOU 2980  CG  ARG A 636     7046   7497   7061     81      4   -439       C  
ATOM   2981  CD  ARG A 636     -37.294  20.436   4.566  1.00 59.31           C  
ANISOU 2981  CD  ARG A 636     7357   7789   7388    115      9   -436       C  
ATOM   2982  NE  ARG A 636     -37.657  21.493   3.629  1.00 54.90           N  
ANISOU 2982  NE  ARG A 636     6743   7348   6770    208     27   -387       N  
ATOM   2983  CZ  ARG A 636     -36.916  22.562   3.364  1.00 52.11           C  
ANISOU 2983  CZ  ARG A 636     6415   6941   6442    295     45   -326       C  
ATOM   2984  NH1 ARG A 636     -35.736  22.720   3.942  1.00 47.24           N  
ANISOU 2984  NH1 ARG A 636     5874   6167   5907    291     42   -315       N  
ATOM   2985  NH2 ARG A 636     -37.362  23.469   2.500  1.00 47.43           N  
ANISOU 2985  NH2 ARG A 636     5772   6462   5789    384     70   -277       N  
ATOM   2986  N   ILE A 637     -39.310  21.816  10.184  1.00 37.27           N  
ANISOU 2986  N   ILE A 637     4675   4826   4661    102     -1   -340       N  
ATOM   2987  CA  ILE A 637     -39.134  22.577  11.412  1.00 45.34           C  
ANISOU 2987  CA  ILE A 637     5743   5762   5723    125      6   -301       C  
ATOM   2988  C   ILE A 637     -37.664  22.700  11.818  1.00 39.03           C  
ANISOU 2988  C   ILE A 637     5009   4817   5003    121      6   -292       C  
ATOM   2989  O   ILE A 637     -37.170  23.804  12.034  1.00 53.28           O  
ANISOU 2989  O   ILE A 637     6843   6571   6828    175     32   -250       O  
ATOM   2990  CB  ILE A 637     -40.010  22.023  12.572  1.00 54.36           C  
ANISOU 2990  CB  ILE A 637     6883   6915   6858     65    -11   -322       C  
ATOM   2991  CG1 ILE A 637     -39.886  22.915  13.802  1.00 58.41           C  
ANISOU 2991  CG1 ILE A 637     7436   7351   7405     94      0   -281       C  
ATOM   2992  CG2 ILE A 637     -39.638  20.581  12.901  1.00 51.95           C  
ANISOU 2992  CG2 ILE A 637     6601   6548   6587    -31    -34   -377       C  
ATOM   2993  CD1 ILE A 637     -40.616  24.228  13.669  1.00 69.27           C  
ANISOU 2993  CD1 ILE A 637     8791   8793   8733    183     34   -228       C  
ATOM   2994  N   TYR A 638     -36.956  21.582  11.906  1.00 32.40           N  
ANISOU 2994  N   TYR A 638     4192   3916   4203     58    -15   -331       N  
ATOM   2995  CA  TYR A 638     -35.531  21.637  12.233  1.00 42.56           C  
ANISOU 2995  CA  TYR A 638     5529   5089   5553     58    -15   -322       C  
ATOM   2996  C   TYR A 638     -34.726  22.508  11.251  1.00 46.93           C  
ANISOU 2996  C   TYR A 638     6086   5636   6110    119      4   -296       C  
ATOM   2997  O   TYR A 638     -33.870  23.282  11.677  1.00 52.22           O  
ANISOU 2997  O   TYR A 638     6792   6236   6813    141     20   -271       O  
ATOM   2998  CB  TYR A 638     -34.937  20.224  12.366  1.00 40.49           C  
ANISOU 2998  CB  TYR A 638     5289   4771   5324     -5    -34   -361       C  
ATOM   2999  CG  TYR A 638     -35.453  19.509  13.591  1.00 52.82           C  
ANISOU 2999  CG  TYR A 638     6866   6308   6897    -60    -45   -375       C  
ATOM   3000  CD1 TYR A 638     -36.653  18.792  13.552  1.00 53.06           C  
ANISOU 3000  CD1 TYR A 638     6870   6405   6887   -108    -48   -409       C  
ATOM   3001  CD2 TYR A 638     -34.771  19.588  14.811  1.00 51.14           C  
ANISOU 3001  CD2 TYR A 638     6689   6015   6728    -68    -49   -354       C  
ATOM   3002  CE1 TYR A 638     -37.146  18.154  14.690  1.00 51.49           C  
ANISOU 3002  CE1 TYR A 638     6688   6180   6698   -160    -54   -420       C  
ATOM   3003  CE2 TYR A 638     -35.261  18.948  15.948  1.00 55.36           C  
ANISOU 3003  CE2 TYR A 638     7235   6529   7270   -114    -58   -361       C  
ATOM   3004  CZ  TYR A 638     -36.448  18.237  15.876  1.00 50.24           C  
ANISOU 3004  CZ  TYR A 638     6567   5935   6587   -159    -60   -393       C  
ATOM   3005  OH  TYR A 638     -36.931  17.606  16.993  1.00 55.59           O  
ANISOU 3005  OH  TYR A 638     7260   6591   7273   -206    -65   -400       O  
ATOM   3006  N   ASP A 639     -35.000  22.398   9.951  1.00 45.92           N  
ANISOU 3006  N   ASP A 639     5920   5585   5944    143      8   -306       N  
ATOM   3007  CA  ASP A 639     -34.295  23.238   8.987  1.00 46.79           C  
ANISOU 3007  CA  ASP A 639     6031   5693   6053    204     30   -278       C  
ATOM   3008  C   ASP A 639     -34.567  24.716   9.313  1.00 42.92           C  
ANISOU 3008  C   ASP A 639     5557   5200   5552    271     69   -224       C  
ATOM   3009  O   ASP A 639     -33.644  25.523   9.422  1.00 44.45           O  
ANISOU 3009  O   ASP A 639     5791   5320   5777    296     94   -200       O  
ATOM   3010  CB  ASP A 639     -34.642  22.872   7.522  1.00 43.52           C  
ANISOU 3010  CB  ASP A 639     5564   5381   5591    220     28   -296       C  
ATOM   3011  CG  ASP A 639     -33.977  21.555   7.047  1.00 46.75           C  
ANISOU 3011  CG  ASP A 639     5978   5763   6024    159      4   -350       C  
ATOM   3012  OD1 ASP A 639     -33.088  21.013   7.735  1.00 54.33           O  
ANISOU 3012  OD1 ASP A 639     6984   6621   7038    122     -7   -362       O  
ATOM   3013  OD2 ASP A 639     -34.355  21.047   5.973  1.00 54.64           O  
ANISOU 3013  OD2 ASP A 639     6931   6847   6981    149      2   -379       O  
ATOM   3014  N   SER A 640     -35.833  25.048   9.517  1.00 38.19           N  
ANISOU 3014  N   SER A 640     4927   4679   4905    297     80   -206       N  
ATOM   3015  CA  SER A 640     -36.231  26.415   9.826  1.00 45.23           C  
ANISOU 3015  CA  SER A 640     5837   5569   5781    369    128   -151       C  
ATOM   3016  C   SER A 640     -35.456  26.993  10.999  1.00 46.36           C  
ANISOU 3016  C   SER A 640     6046   5588   5980    347    146   -143       C  
ATOM   3017  O   SER A 640     -34.973  28.122  10.945  1.00 41.09           O  
ANISOU 3017  O   SER A 640     5420   4869   5325    393    197   -110       O  
ATOM   3018  CB  SER A 640     -37.726  26.477  10.164  1.00 46.05           C  
ANISOU 3018  CB  SER A 640     5898   5773   5826    388    129   -139       C  
ATOM   3019  OG  SER A 640     -38.522  26.427   9.004  1.00 50.15           O  
ANISOU 3019  OG  SER A 640     6349   6432   6272    435    134   -128       O  
ATOM   3020  N   ILE A 641     -35.376  26.224  12.078  1.00 47.01           N  
ANISOU 3020  N   ILE A 641     6139   5629   6093    274    110   -175       N  
ATOM   3021  CA  ILE A 641     -34.706  26.685  13.287  1.00 42.75           C  
ANISOU 3021  CA  ILE A 641     5650   4994   5599    244    124   -173       C  
ATOM   3022  C   ILE A 641     -33.234  26.971  13.019  1.00 38.59           C  
ANISOU 3022  C   ILE A 641     5159   4395   5111    235    138   -177       C  
ATOM   3023  O   ILE A 641     -32.711  28.003  13.430  1.00 38.84           O  
ANISOU 3023  O   ILE A 641     5232   4369   5158    244    183   -161       O  
ATOM   3024  CB  ILE A 641     -34.831  25.666  14.432  1.00 40.19           C  
ANISOU 3024  CB  ILE A 641     5322   4651   5296    170     80   -204       C  
ATOM   3025  CG1 ILE A 641     -36.265  25.623  14.962  1.00 39.02           C  
ANISOU 3025  CG1 ILE A 641     5147   4566   5111    172     75   -199       C  
ATOM   3026  CG2 ILE A 641     -33.916  26.044  15.562  1.00 38.72           C  
ANISOU 3026  CG2 ILE A 641     5178   4381   5152    134     91   -205       C  
ATOM   3027  CD1 ILE A 641     -36.472  24.559  16.006  1.00 42.37           C  
ANISOU 3027  CD1 ILE A 641     5569   4977   5554    100     35   -228       C  
ATOM   3028  N   LEU A 642     -32.581  26.041  12.330  1.00 41.06           N  
ANISOU 3028  N   LEU A 642     5455   4712   5435    214    103   -202       N  
ATOM   3029  CA  LEU A 642     -31.181  26.151  11.940  1.00 41.18           C  
ANISOU 3029  CA  LEU A 642     5493   4676   5479    207    108   -208       C  
ATOM   3030  C   LEU A 642     -30.933  27.392  11.064  1.00 47.45           C  
ANISOU 3030  C   LEU A 642     6304   5465   6258    268    162   -177       C  
ATOM   3031  O   LEU A 642     -30.024  28.189  11.339  1.00 46.88           O  
ANISOU 3031  O   LEU A 642     6273   5334   6207    260    198   -172       O  
ATOM   3032  CB  LEU A 642     -30.783  24.876  11.197  1.00 52.99           C  
ANISOU 3032  CB  LEU A 642     6964   6191   6980    186     66   -237       C  
ATOM   3033  CG  LEU A 642     -29.311  24.547  10.979  1.00 73.19           C  
ANISOU 3033  CG  LEU A 642     9538   8703   9568    168     55   -249       C  
ATOM   3034  CD1 LEU A 642     -29.191  23.073  10.647  1.00 81.67           C  
ANISOU 3034  CD1 LEU A 642    10595   9787  10650    139     17   -279       C  
ATOM   3035  CD2 LEU A 642     -28.709  25.402   9.874  1.00 75.68           C  
ANISOU 3035  CD2 LEU A 642     9859   9020   9875    212     85   -233       C  
ATOM   3036  N   LEU A 643     -31.761  27.564  10.033  1.00 42.54           N  
ANISOU 3036  N   LEU A 643     5652   4914   5597    326    173   -157       N  
ATOM   3037  CA  LEU A 643     -31.684  28.729   9.145  1.00 44.77           C  
ANISOU 3037  CA  LEU A 643     5950   5201   5859    400    231   -117       C  
ATOM   3038  C   LEU A 643     -31.990  30.086   9.802  1.00 50.26           C  
ANISOU 3038  C   LEU A 643     6695   5850   6552    435    303    -80       C  
ATOM   3039  O   LEU A 643     -31.287  31.076   9.555  1.00 52.14           O  
ANISOU 3039  O   LEU A 643     6981   6029   6801    457    363    -62       O  
ATOM   3040  CB  LEU A 643     -32.575  28.524   7.915  1.00 42.33           C  
ANISOU 3040  CB  LEU A 643     5584   5001   5497    460    225    -99       C  
ATOM   3041  CG  LEU A 643     -32.130  27.362   7.022  1.00 40.33           C  
ANISOU 3041  CG  LEU A 643     5290   4787   5245    427    173   -138       C  
ATOM   3042  CD1 LEU A 643     -33.225  26.958   6.025  1.00 50.09           C  
ANISOU 3042  CD1 LEU A 643     6457   6156   6419    463    161   -136       C  
ATOM   3043  CD2 LEU A 643     -30.823  27.712   6.326  1.00 36.30           C  
ANISOU 3043  CD2 LEU A 643     4807   4225   4761    437    189   -136       C  
ATOM   3044  N   TYR A 644     -33.036  30.150  10.619  1.00 37.78           N  
ANISOU 3044  N   TYR A 644     5109   4292   4956    439    305    -71       N  
ATOM   3045  CA  TYR A 644     -33.316  31.391  11.329  1.00 39.99           C  
ANISOU 3045  CA  TYR A 644     5441   4518   5235    468    378    -40       C  
ATOM   3046  C   TYR A 644     -32.253  31.728  12.384  1.00 41.71           C  
ANISOU 3046  C   TYR A 644     5715   4634   5500    393    397    -70       C  
ATOM   3047  O   TYR A 644     -32.114  32.888  12.770  1.00 53.13           O  
ANISOU 3047  O   TYR A 644     7220   6017   6951    406    476    -53       O  
ATOM   3048  CB  TYR A 644     -34.727  31.388  11.926  1.00 45.78           C  
ANISOU 3048  CB  TYR A 644     6150   5310   5934    495    376    -21       C  
ATOM   3049  CG  TYR A 644     -35.804  31.700  10.905  1.00 49.53           C  
ANISOU 3049  CG  TYR A 644     6584   5890   6346    597    400     28       C  
ATOM   3050  CD1 TYR A 644     -36.781  30.761  10.580  1.00 50.62           C  
ANISOU 3050  CD1 TYR A 644     6645   6150   6440    597    342     18       C  
ATOM   3051  CD2 TYR A 644     -35.832  32.929  10.248  1.00 45.12           C  
ANISOU 3051  CD2 TYR A 644     6062   5316   5767    692    487     86       C  
ATOM   3052  CE1 TYR A 644     -37.769  31.045   9.648  1.00 42.12           C  
ANISOU 3052  CE1 TYR A 644     5517   5195   5293    689    364     62       C  
ATOM   3053  CE2 TYR A 644     -36.818  33.222   9.311  1.00 42.56           C  
ANISOU 3053  CE2 TYR A 644     5691   5105   5375    797    512    140       C  
ATOM   3054  CZ  TYR A 644     -37.779  32.273   9.021  1.00 43.79           C  
ANISOU 3054  CZ  TYR A 644     5759   5398   5481    794    447    127       C  
ATOM   3055  OH  TYR A 644     -38.755  32.552   8.100  1.00 51.00           O  
ANISOU 3055  OH  TYR A 644     6614   6449   6315    897    471    179       O  
ATOM   3056  N   GLN A 645     -31.496  30.734  12.844  1.00 35.44           N  
ANISOU 3056  N   GLN A 645     4902   3829   4735    314    333   -114       N  
ATOM   3057  CA  GLN A 645     -30.339  31.033  13.694  1.00 41.93           C  
ANISOU 3057  CA  GLN A 645     5762   4580   5588    244    350   -143       C  
ATOM   3058  C   GLN A 645     -29.273  31.755  12.877  1.00 38.99           C  
ANISOU 3058  C   GLN A 645     5424   4168   5222    254    399   -141       C  
ATOM   3059  O   GLN A 645     -28.802  32.820  13.261  1.00 45.57           O  
ANISOU 3059  O   GLN A 645     6312   4941   6060    236    471   -143       O  
ATOM   3060  CB  GLN A 645     -29.702  29.769  14.275  1.00 42.55           C  
ANISOU 3060  CB  GLN A 645     5809   4671   5690    173    274   -180       C  
ATOM   3061  CG  GLN A 645     -30.572  28.903  15.149  1.00 42.42           C  
ANISOU 3061  CG  GLN A 645     5762   4685   5672    149    225   -188       C  
ATOM   3062  CD  GLN A 645     -29.763  27.779  15.759  1.00 46.17           C  
ANISOU 3062  CD  GLN A 645     6217   5157   6169     87    169   -217       C  
ATOM   3063  OE1 GLN A 645     -28.883  28.025  16.577  1.00 51.51           O  
ANISOU 3063  OE1 GLN A 645     6907   5805   6858     40    180   -231       O  
ATOM   3064  NE2 GLN A 645     -30.051  26.541  15.365  1.00 46.99           N  
ANISOU 3064  NE2 GLN A 645     6287   5294   6272     88    115   -225       N  
ATOM   3065  N   LEU A 646     -28.882  31.155  11.754  1.00 37.33           N  
ANISOU 3065  N   LEU A 646     5183   3993   5008    277    362   -140       N  
ATOM   3066  CA  LEU A 646     -27.885  31.763  10.869  1.00 39.35           C  
ANISOU 3066  CA  LEU A 646     5465   4219   5266    289    403   -137       C  
ATOM   3067  C   LEU A 646     -28.320  33.138  10.394  1.00 43.50           C  
ANISOU 3067  C   LEU A 646     6042   4713   5775    357    499    -95       C  
ATOM   3068  O   LEU A 646     -27.484  34.008  10.207  1.00 47.98           O  
ANISOU 3068  O   LEU A 646     6659   5222   6348    344    564    -97       O  
ATOM   3069  CB  LEU A 646     -27.598  30.868   9.675  1.00 31.70           C  
ANISOU 3069  CB  LEU A 646     4450   3302   4292    313    347   -140       C  
ATOM   3070  CG  LEU A 646     -27.107  29.473  10.031  1.00 35.62           C  
ANISOU 3070  CG  LEU A 646     4907   3820   4807    256    265   -177       C  
ATOM   3071  CD1 LEU A 646     -27.419  28.509   8.911  1.00 27.68           C  
ANISOU 3071  CD1 LEU A 646     3854   2874   3789    289    217   -179       C  
ATOM   3072  CD2 LEU A 646     -25.613  29.491  10.360  1.00 40.50           C  
ANISOU 3072  CD2 LEU A 646     5541   4403   5443    199    265   -204       C  
ATOM   3073  N   ALA A 647     -29.627  33.334  10.215  1.00 39.87           N  
ANISOU 3073  N   ALA A 647     5568   4293   5287    430    514    -55       N  
ATOM   3074  CA  ALA A 647     -30.170  34.655   9.879  1.00 41.10           C  
ANISOU 3074  CA  ALA A 647     5776   4419   5421    511    616     -2       C  
ATOM   3075  C   ALA A 647     -30.119  35.627  11.053  1.00 45.92           C  
ANISOU 3075  C   ALA A 647     6459   4941   6046    474    694    -10       C  
ATOM   3076  O   ALA A 647     -30.380  36.822  10.889  1.00 44.23           O  
ANISOU 3076  O   ALA A 647     6309   4674   5821    531    799     29       O  
ATOM   3077  CB  ALA A 647     -31.598  34.537   9.372  1.00 36.56           C  
ANISOU 3077  CB  ALA A 647     5155   3934   4802    606    608     47       C  
ATOM   3078  N   GLU A 648     -29.773  35.114  12.232  1.00 45.02           N  
ANISOU 3078  N   GLU A 648     6337   4812   5957    379    649    -60       N  
ATOM   3079  CA  GLU A 648     -29.836  35.896  13.473  1.00 50.82           C  
ANISOU 3079  CA  GLU A 648     7128   5479   6701    332    713    -76       C  
ATOM   3080  C   GLU A 648     -31.251  36.415  13.784  1.00 51.11           C  
ANISOU 3080  C   GLU A 648     7178   5524   6715    408    757    -30       C  
ATOM   3081  O   GLU A 648     -31.432  37.504  14.336  1.00 57.71           O  
ANISOU 3081  O   GLU A 648     8086   6290   7552    414    855    -20       O  
ATOM   3082  CB  GLU A 648     -28.834  37.047  13.445  1.00 48.55           C  
ANISOU 3082  CB  GLU A 648     6920   5101   6423    296    817    -91       C  
ATOM   3083  CG  GLU A 648     -27.399  36.585  13.536  1.00 53.39           C  
ANISOU 3083  CG  GLU A 648     7517   5715   7054    198    775   -147       C  
ATOM   3084  CD  GLU A 648     -26.434  37.738  13.718  1.00 61.84           C  
ANISOU 3084  CD  GLU A 648     8666   6704   8127    136    883   -177       C  
ATOM   3085  OE1 GLU A 648     -26.764  38.869  13.300  1.00 69.59           O  
ANISOU 3085  OE1 GLU A 648     9721   7619   9101    191    994   -144       O  
ATOM   3086  OE2 GLU A 648     -25.345  37.516  14.286  1.00 64.08           O  
ANISOU 3086  OE2 GLU A 648     8937   6995   8415     33    863   -233       O  
ATOM   3087  N   GLU A 649     -32.253  35.629  13.423  1.00 43.03           N  
ANISOU 3087  N   GLU A 649     6088   4593   5668    463    689     -4       N  
ATOM   3088  CA  GLU A 649     -33.626  35.974  13.744  1.00 37.21           C  
ANISOU 3088  CA  GLU A 649     5348   3889   4900    534    716     38       C  
ATOM   3089  C   GLU A 649     -33.988  35.335  15.078  1.00 39.22           C  
ANISOU 3089  C   GLU A 649     5577   4155   5168    459    658      0       C  
ATOM   3090  O   GLU A 649     -34.733  34.359  15.126  1.00 39.22           O  
ANISOU 3090  O   GLU A 649     5511   4240   5153    462    577     -2       O  
ATOM   3091  CB  GLU A 649     -34.558  35.492  12.635  1.00 45.76           C  
ANISOU 3091  CB  GLU A 649     6364   5087   5938    628    678     82       C  
ATOM   3092  CG  GLU A 649     -34.634  36.433  11.449  1.00 56.03           C  
ANISOU 3092  CG  GLU A 649     7693   6387   7209    739    763    144       C  
ATOM   3093  CD  GLU A 649     -35.414  37.704  11.747  1.00 69.90           C  
ANISOU 3093  CD  GLU A 649     9514   8104   8942    828    879    203       C  
ATOM   3094  OE1 GLU A 649     -35.102  38.391  12.741  1.00 72.90           O  
ANISOU 3094  OE1 GLU A 649     9968   8379   9352    779    942    182       O  
ATOM   3095  OE2 GLU A 649     -36.338  38.024  10.973  1.00 81.89           O  
ANISOU 3095  OE2 GLU A 649    11007   9702  10407    950    912    271       O  
ATOM   3096  N   TYR A 650     -33.459  35.898  16.161  1.00 40.17           N  
ANISOU 3096  N   TYR A 650     5752   4195   5315    388    703    -32       N  
ATOM   3097  CA  TYR A 650     -33.466  35.226  17.459  1.00 41.93           C  
ANISOU 3097  CA  TYR A 650     5948   4427   5556    299    642    -76       C  
ATOM   3098  C   TYR A 650     -34.868  34.929  17.981  1.00 38.81           C  
ANISOU 3098  C   TYR A 650     5519   4091   5137    337    614    -53       C  
ATOM   3099  O   TYR A 650     -35.165  33.817  18.391  1.00 36.35           O  
ANISOU 3099  O   TYR A 650     5147   3836   4826    297    523    -74       O  
ATOM   3100  CB  TYR A 650     -32.645  36.026  18.466  1.00 48.18           C  
ANISOU 3100  CB  TYR A 650     6802   5134   6370    216    710   -116       C  
ATOM   3101  CG  TYR A 650     -31.216  36.298  18.005  1.00 49.95           C  
ANISOU 3101  CG  TYR A 650     7055   5314   6611    164    738   -146       C  
ATOM   3102  CD1 TYR A 650     -30.784  37.591  17.737  1.00 48.72           C  
ANISOU 3102  CD1 TYR A 650     6982   5076   6455    172    858   -142       C  
ATOM   3103  CD2 TYR A 650     -30.306  35.257  17.848  1.00 49.61           C  
ANISOU 3103  CD2 TYR A 650     6957   5311   6580    109    650   -178       C  
ATOM   3104  CE1 TYR A 650     -29.491  37.841  17.338  1.00 55.32           C  
ANISOU 3104  CE1 TYR A 650     7842   5878   7300    116    885   -175       C  
ATOM   3105  CE2 TYR A 650     -29.007  35.497  17.448  1.00 54.66           C  
ANISOU 3105  CE2 TYR A 650     7617   5924   7228     62    674   -205       C  
ATOM   3106  CZ  TYR A 650     -28.605  36.794  17.189  1.00 57.22           C  
ANISOU 3106  CZ  TYR A 650     8019   6173   7549     62    789   -206       C  
ATOM   3107  OH  TYR A 650     -27.314  37.056  16.783  1.00 54.83           O  
ANISOU 3107  OH  TYR A 650     7735   5848   7248      8    816   -237       O  
ATOM   3108  N   ASP A 651     -35.733  35.926  17.917  1.00 40.00           N  
ANISOU 3108  N   ASP A 651     5709   4229   5262    419    696     -7       N  
ATOM   3109  CA  ASP A 651     -37.123  35.781  18.309  1.00 35.87           C  
ANISOU 3109  CA  ASP A 651     5151   3772   4704    470    679     22       C  
ATOM   3110  C   ASP A 651     -37.930  34.714  17.565  1.00 38.79           C  
ANISOU 3110  C   ASP A 651     5432   4267   5038    510    591     38       C  
ATOM   3111  O   ASP A 651     -38.715  33.998  18.174  1.00 48.68           O  
ANISOU 3111  O   ASP A 651     6636   5583   6276    486    531     26       O  
ATOM   3112  CB  ASP A 651     -37.841  37.112  18.166  1.00 34.23           C  
ANISOU 3112  CB  ASP A 651     5005   3533   4469    573    797     80       C  
ATOM   3113  CG  ASP A 651     -39.085  37.162  18.984  1.00 50.38           C  
ANISOU 3113  CG  ASP A 651     7032   5624   6486    604    795     99       C  
ATOM   3114  OD1 ASP A 651     -38.995  36.890  20.211  1.00 50.91           O  
ANISOU 3114  OD1 ASP A 651     7100   5665   6579    514    765     54       O  
ATOM   3115  OD2 ASP A 651     -40.146  37.459  18.401  1.00 64.39           O  
ANISOU 3115  OD2 ASP A 651     8785   7471   8208    719    823    160       O  
ATOM   3116  N   ILE A 652     -37.775  34.632  16.250  1.00 44.24           N  
ANISOU 3116  N   ILE A 652     6102   4998   5708    568    591     62       N  
ATOM   3117  CA  ILE A 652     -38.463  33.597  15.482  1.00 42.33           C  
ANISOU 3117  CA  ILE A 652     5774   4882   5428    591    513     66       C  
ATOM   3118  C   ILE A 652     -37.990  32.217  15.926  1.00 46.40           C  
ANISOU 3118  C   ILE A 652     6248   5406   5975    481    412      4       C  
ATOM   3119  O   ILE A 652     -38.789  31.290  16.055  1.00 55.54           O  
ANISOU 3119  O   ILE A 652     7346   6648   7107    461    349    -10       O  
ATOM   3120  CB  ILE A 652     -38.236  33.759  13.975  1.00 41.92           C  
ANISOU 3120  CB  ILE A 652     5705   4872   5350    664    532     98       C  
ATOM   3121  CG1 ILE A 652     -38.932  35.020  13.471  1.00 44.89           C  
ANISOU 3121  CG1 ILE A 652     6112   5265   5681    795    633    175       C  
ATOM   3122  CG2 ILE A 652     -38.751  32.542  13.230  1.00 47.51           C  
ANISOU 3122  CG2 ILE A 652     6321   5708   6021    656    446     82       C  
ATOM   3123  CD1 ILE A 652     -38.429  35.471  12.098  1.00 42.01           C  
ANISOU 3123  CD1 ILE A 652     5755   4906   5301    868    677    211       C  
ATOM   3124  N   VAL A 653     -36.688  32.093  16.173  1.00 36.91           N  
ANISOU 3124  N   VAL A 653     5080   4118   4824    411    405    -32       N  
ATOM   3125  CA  VAL A 653     -36.116  30.842  16.655  1.00 37.88           C  
ANISOU 3125  CA  VAL A 653     5174   4239   4979    318    323    -82       C  
ATOM   3126  C   VAL A 653     -36.766  30.376  17.955  1.00 43.26           C  
ANISOU 3126  C   VAL A 653     5840   4933   5663    267    288   -100       C  
ATOM   3127  O   VAL A 653     -37.108  29.201  18.106  1.00 40.61           O  
ANISOU 3127  O   VAL A 653     5460   4645   5324    226    220   -123       O  
ATOM   3128  CB  VAL A 653     -34.607  30.958  16.896  1.00 34.64           C  
ANISOU 3128  CB  VAL A 653     4802   3745   4614    257    331   -111       C  
ATOM   3129  CG1 VAL A 653     -34.084  29.657  17.478  1.00 25.86           C  
ANISOU 3129  CG1 VAL A 653     3659   2639   3528    177    253   -151       C  
ATOM   3130  CG2 VAL A 653     -33.888  31.294  15.595  1.00 32.90           C  
ANISOU 3130  CG2 VAL A 653     4593   3514   4392    298    358    -98       C  
ATOM   3131  N   ILE A 654     -36.926  31.296  18.901  1.00 44.26           N  
ANISOU 3131  N   ILE A 654     6009   5012   5797    265    340    -92       N  
ATOM   3132  CA  ILE A 654     -37.543  30.949  20.172  1.00 40.20           C  
ANISOU 3132  CA  ILE A 654     5481   4509   5285    219    311   -107       C  
ATOM   3133  C   ILE A 654     -38.993  30.522  19.942  1.00 42.65           C  
ANISOU 3133  C   ILE A 654     5741   4919   5546    263    282    -87       C  
ATOM   3134  O   ILE A 654     -39.432  29.494  20.460  1.00 41.93           O  
ANISOU 3134  O   ILE A 654     5610   4870   5453    212    219   -110       O  
ATOM   3135  CB  ILE A 654     -37.403  32.087  21.209  1.00 40.81           C  
ANISOU 3135  CB  ILE A 654     5615   4515   5376    204    382   -106       C  
ATOM   3136  CG1 ILE A 654     -35.919  32.449  21.392  1.00 41.31           C  
ANISOU 3136  CG1 ILE A 654     5719   4500   5477    145    410   -136       C  
ATOM   3137  CG2 ILE A 654     -38.010  31.696  22.550  1.00 30.55           C  
ANISOU 3137  CG2 ILE A 654     4297   3233   4079    154    347   -123       C  
ATOM   3138  CD1 ILE A 654     -35.023  31.262  21.690  1.00 32.74           C  
ANISOU 3138  CD1 ILE A 654     4598   3425   4417     68    332   -173       C  
ATOM   3139  N   THR A 655     -39.723  31.276  19.127  1.00 39.23           N  
ANISOU 3139  N   THR A 655     5305   4531   5069    358    332    -42       N  
ATOM   3140  CA  THR A 655     -41.096  30.900  18.797  1.00 37.98           C  
ANISOU 3140  CA  THR A 655     5086   4495   4849    404    306    -22       C  
ATOM   3141  C   THR A 655     -41.200  29.492  18.218  1.00 38.71           C  
ANISOU 3141  C   THR A 655     5116   4663   4929    356    227    -57       C  
ATOM   3142  O   THR A 655     -42.040  28.709  18.637  1.00 48.16           O  
ANISOU 3142  O   THR A 655     6269   5929   6100    319    181    -76       O  
ATOM   3143  CB  THR A 655     -41.710  31.842  17.779  1.00 41.86           C  
ANISOU 3143  CB  THR A 655     5575   5044   5287    526    371     38       C  
ATOM   3144  OG1 THR A 655     -41.638  33.184  18.268  1.00 47.85           O  
ANISOU 3144  OG1 THR A 655     6404   5719   6056    577    463     72       O  
ATOM   3145  CG2 THR A 655     -43.152  31.463  17.556  1.00 34.77           C  
ANISOU 3145  CG2 THR A 655     4603   4295   4313    569    345     56       C  
ATOM   3146  N   LEU A 656     -40.353  29.179  17.246  1.00 42.40           N  
ANISOU 3146  N   LEU A 656     5582   5114   5412    352    217    -68       N  
ATOM   3147  CA  LEU A 656     -40.343  27.854  16.633  1.00 39.31           C  
ANISOU 3147  CA  LEU A 656     5142   4781   5012    303    154   -106       C  
ATOM   3148  C   LEU A 656     -39.934  26.738  17.613  1.00 41.66           C  
ANISOU 3148  C   LEU A 656     5446   5027   5354    200    100   -153       C  
ATOM   3149  O   LEU A 656     -40.473  25.633  17.557  1.00 46.88           O  
ANISOU 3149  O   LEU A 656     6069   5747   5997    153     57   -184       O  
ATOM   3150  CB  LEU A 656     -39.428  27.844  15.396  1.00 44.83           C  
ANISOU 3150  CB  LEU A 656     5846   5465   5722    325    162   -106       C  
ATOM   3151  CG  LEU A 656     -39.802  28.771  14.224  1.00 43.16           C  
ANISOU 3151  CG  LEU A 656     5619   5317   5461    431    213    -57       C  
ATOM   3152  CD1 LEU A 656     -38.777  28.683  13.086  1.00 31.96           C  
ANISOU 3152  CD1 LEU A 656     4208   3876   4062    441    215    -62       C  
ATOM   3153  CD2 LEU A 656     -41.193  28.465  13.709  1.00 36.40           C  
ANISOU 3153  CD2 LEU A 656     4688   4618   4524    468    199    -46       C  
ATOM   3154  N   VAL A 657     -38.980  27.017  18.502  1.00 39.74           N  
ANISOU 3154  N   VAL A 657     5252   4682   5166    165    109   -159       N  
ATOM   3155  CA  VAL A 657     -38.581  26.037  19.504  1.00 45.30           C  
ANISOU 3155  CA  VAL A 657     5960   5345   5907     83     65   -191       C  
ATOM   3156  C   VAL A 657     -39.697  25.820  20.534  1.00 40.69           C  
ANISOU 3156  C   VAL A 657     5357   4800   5302     58     48   -194       C  
ATOM   3157  O   VAL A 657     -39.923  24.697  20.998  1.00 37.32           O  
ANISOU 3157  O   VAL A 657     4914   4385   4881     -2      6   -221       O  
ATOM   3158  CB  VAL A 657     -37.270  26.441  20.221  1.00 50.36           C  
ANISOU 3158  CB  VAL A 657     6644   5891   6598     53     80   -195       C  
ATOM   3159  CG1 VAL A 657     -36.990  25.500  21.379  1.00 42.52           C  
ANISOU 3159  CG1 VAL A 657     5648   4874   5633    -18     40   -217       C  
ATOM   3160  CG2 VAL A 657     -36.108  26.436  19.243  1.00 47.86           C  
ANISOU 3160  CG2 VAL A 657     6341   5542   6301     65     88   -199       C  
ATOM   3161  N   ASN A 658     -40.404  26.895  20.870  1.00 37.50           N  
ANISOU 3161  N   ASN A 658     4959   4415   4873    106     87   -165       N  
ATOM   3162  CA  ASN A 658     -41.487  26.818  21.837  1.00 36.62           C  
ANISOU 3162  CA  ASN A 658     4829   4346   4738     90     75   -165       C  
ATOM   3163  C   ASN A 658     -42.604  25.937  21.314  1.00 43.72           C  
ANISOU 3163  C   ASN A 658     5671   5356   5584     82     40   -178       C  
ATOM   3164  O   ASN A 658     -43.184  25.153  22.066  1.00 48.37           O  
ANISOU 3164  O   ASN A 658     6241   5970   6166     24      5   -201       O  
ATOM   3165  CB  ASN A 658     -42.014  28.214  22.206  1.00 35.59           C  
ANISOU 3165  CB  ASN A 658     4721   4212   4588    155    135   -127       C  
ATOM   3166  CG  ASN A 658     -41.054  28.987  23.133  1.00 39.32           C  
ANISOU 3166  CG  ASN A 658     5251   4576   5111    130    172   -130       C  
ATOM   3167  OD1 ASN A 658     -40.058  28.438  23.628  1.00 34.21           O  
ANISOU 3167  OD1 ASN A 658     4616   3875   4508     62    145   -158       O  
ATOM   3168  ND2 ASN A 658     -41.350  30.266  23.353  1.00 36.29           N  
ANISOU 3168  ND2 ASN A 658     4904   4169   4716    184    242   -101       N  
ATOM   3169  N   SER A 659     -42.898  26.050  20.020  1.00 40.33           N  
ANISOU 3169  N   SER A 659     5212   4999   5111    134     52   -167       N  
ATOM   3170  CA  SER A 659     -43.886  25.176  19.406  1.00 31.52           C  
ANISOU 3170  CA  SER A 659     4036   4005   3936    114     22   -190       C  
ATOM   3171  C   SER A 659     -43.394  23.741  19.354  1.00 33.81           C  
ANISOU 3171  C   SER A 659     4325   4264   4255     22    -20   -243       C  
ATOM   3172  O   SER A 659     -44.108  22.802  19.720  1.00 33.40           O  
ANISOU 3172  O   SER A 659     4249   4260   4182    -43    -47   -276       O  
ATOM   3173  CB  SER A 659     -44.230  25.652  17.997  1.00 33.69           C  
ANISOU 3173  CB  SER A 659     4271   4377   4152    193     48   -165       C  
ATOM   3174  OG  SER A 659     -44.972  26.850  18.052  1.00 51.04           O  
ANISOU 3174  OG  SER A 659     6462   6627   6306    287     92   -111       O  
ATOM   3175  N   LEU A 660     -42.170  23.568  18.879  1.00 26.36           N  
ANISOU 3175  N   LEU A 660     3415   3240   3362     17    -19   -249       N  
ATOM   3176  CA  LEU A 660     -41.630  22.229  18.731  1.00 29.37           C  
ANISOU 3176  CA  LEU A 660     3805   3585   3771    -57    -47   -293       C  
ATOM   3177  C   LEU A 660     -41.539  21.523  20.096  1.00 42.26           C  
ANISOU 3177  C   LEU A 660     5462   5153   5441   -125    -68   -308       C  
ATOM   3178  O   LEU A 660     -41.863  20.337  20.211  1.00 41.37           O  
ANISOU 3178  O   LEU A 660     5345   5050   5324   -191    -85   -344       O  
ATOM   3179  CB  LEU A 660     -40.257  22.291  18.070  1.00 31.40           C  
ANISOU 3179  CB  LEU A 660     4092   3764   4073    -39    -39   -289       C  
ATOM   3180  CG  LEU A 660     -39.541  20.960  18.096  1.00 30.64           C  
ANISOU 3180  CG  LEU A 660     4018   3610   4015   -105    -59   -325       C  
ATOM   3181  CD1 LEU A 660     -40.335  19.995  17.244  1.00 31.32           C  
ANISOU 3181  CD1 LEU A 660     4068   3777   4054   -145    -66   -367       C  
ATOM   3182  CD2 LEU A 660     -38.129  21.113  17.602  1.00 28.17           C  
ANISOU 3182  CD2 LEU A 660     3735   3222   3745    -81    -52   -316       C  
ATOM   3183  N   LEU A 661     -41.101  22.250  21.125  1.00 33.76           N  
ANISOU 3183  N   LEU A 661     4415   4013   4400   -111    -60   -281       N  
ATOM   3184  CA  LEU A 661     -40.916  21.643  22.443  1.00 34.02           C  
ANISOU 3184  CA  LEU A 661     4468   3992   4467   -167    -79   -289       C  
ATOM   3185  C   LEU A 661     -42.271  21.387  23.100  1.00 39.15           C  
ANISOU 3185  C   LEU A 661     5089   4709   5076   -197    -92   -298       C  
ATOM   3186  O   LEU A 661     -42.519  20.312  23.655  1.00 39.96           O  
ANISOU 3186  O   LEU A 661     5195   4803   5186   -261   -110   -322       O  
ATOM   3187  CB  LEU A 661     -40.009  22.508  23.333  1.00 26.50           C  
ANISOU 3187  CB  LEU A 661     3546   2967   3556   -152    -65   -264       C  
ATOM   3188  CG  LEU A 661     -39.799  21.969  24.748  1.00 29.04           C  
ANISOU 3188  CG  LEU A 661     3879   3249   3906   -204    -83   -266       C  
ATOM   3189  CD1 LEU A 661     -39.370  20.535  24.679  1.00 23.18           C  
ANISOU 3189  CD1 LEU A 661     3146   2478   3184   -247   -103   -284       C  
ATOM   3190  CD2 LEU A 661     -38.791  22.788  25.544  1.00 23.50           C  
ANISOU 3190  CD2 LEU A 661     3199   2494   3237   -199    -67   -249       C  
ATOM   3191  N   SER A 662     -43.160  22.371  23.012  1.00 38.15           N  
ANISOU 3191  N   SER A 662     4938   4652   4906   -148    -77   -277       N  
ATOM   3192  CA  SER A 662     -44.519  22.211  23.516  1.00 29.42           C  
ANISOU 3192  CA  SER A 662     3796   3632   3750   -168    -88   -285       C  
ATOM   3193  C   SER A 662     -45.185  20.965  22.932  1.00 42.13           C  
ANISOU 3193  C   SER A 662     5375   5313   5321   -230   -107   -329       C  
ATOM   3194  O   SER A 662     -45.797  20.186  23.657  1.00 49.35           O  
ANISOU 3194  O   SER A 662     6283   6243   6225   -295   -123   -353       O  
ATOM   3195  CB  SER A 662     -45.345  23.444  23.189  1.00 28.05           C  
ANISOU 3195  CB  SER A 662     3596   3540   3524    -87    -61   -250       C  
ATOM   3196  OG  SER A 662     -46.628  23.316  23.738  1.00 44.21           O  
ANISOU 3196  OG  SER A 662     5603   5676   5517   -103    -73   -255       O  
ATOM   3197  N   ASP A 663     -45.045  20.780  21.618  1.00 47.38           N  
ANISOU 3197  N   ASP A 663     6022   6019   5962   -214    -99   -343       N  
ATOM   3198  CA  ASP A 663     -45.628  19.632  20.909  1.00 53.05           C  
ANISOU 3198  CA  ASP A 663     6710   6811   6637   -281   -106   -395       C  
ATOM   3199  C   ASP A 663     -45.023  18.289  21.335  1.00 45.84           C  
ANISOU 3199  C   ASP A 663     5843   5799   5774   -367   -112   -432       C  
ATOM   3200  O   ASP A 663     -45.732  17.298  21.470  1.00 56.43           O  
ANISOU 3200  O   ASP A 663     7175   7178   7087   -445   -112   -476       O  
ATOM   3201  CB  ASP A 663     -45.491  19.795  19.387  1.00 53.32           C  
ANISOU 3201  CB  ASP A 663     6714   6910   6636   -243    -92   -402       C  
ATOM   3202  CG  ASP A 663     -46.427  20.852  18.818  1.00 62.88           C  
ANISOU 3202  CG  ASP A 663     7865   8259   7769   -163    -79   -369       C  
ATOM   3203  OD1 ASP A 663     -47.394  21.235  19.507  1.00 71.75           O  
ANISOU 3203  OD1 ASP A 663     8960   9449   8851   -153    -82   -354       O  
ATOM   3204  OD2 ASP A 663     -46.197  21.307  17.672  1.00 67.92           O  
ANISOU 3204  OD2 ASP A 663     8480   8943   8383   -105    -64   -354       O  
ATOM   3205  N   THR A 664     -43.714  18.257  21.536  1.00 36.38           N  
ANISOU 3205  N   THR A 664     4695   4480   4647   -350   -110   -413       N  
ATOM   3206  CA  THR A 664     -43.043  17.052  21.994  1.00 41.00           C  
ANISOU 3206  CA  THR A 664     5328   4968   5281   -409   -107   -433       C  
ATOM   3207  C   THR A 664     -43.502  16.635  23.398  1.00 49.52           C  
ANISOU 3207  C   THR A 664     6422   6023   6372   -455   -116   -430       C  
ATOM   3208  O   THR A 664     -43.774  15.458  23.658  1.00 48.73           O  
ANISOU 3208  O   THR A 664     6344   5901   6272   -526   -106   -462       O  
ATOM   3209  CB  THR A 664     -41.531  17.259  21.981  1.00 48.77           C  
ANISOU 3209  CB  THR A 664     6352   5848   6328   -367   -104   -403       C  
ATOM   3210  OG1 THR A 664     -41.144  17.680  20.672  1.00 60.15           O  
ANISOU 3210  OG1 THR A 664     7780   7317   7758   -324    -96   -406       O  
ATOM   3211  CG2 THR A 664     -40.799  15.974  22.339  1.00 47.18           C  
ANISOU 3211  CG2 THR A 664     6200   5555   6171   -411    -94   -415       C  
ATOM   3212  N   LEU A 665     -43.595  17.603  24.303  1.00 41.77           N  
ANISOU 3212  N   LEU A 665     5430   5042   5397   -418   -129   -392       N  
ATOM   3213  CA  LEU A 665     -44.067  17.310  25.654  1.00 43.87           C  
ANISOU 3213  CA  LEU A 665     5703   5296   5670   -457   -139   -387       C  
ATOM   3214  C   LEU A 665     -45.478  16.728  25.640  1.00 47.63           C  
ANISOU 3214  C   LEU A 665     6148   5863   6086   -518   -142   -425       C  
ATOM   3215  O   LEU A 665     -45.716  15.665  26.221  1.00 52.82           O  
ANISOU 3215  O   LEU A 665     6829   6490   6751   -587   -137   -447       O  
ATOM   3216  CB  LEU A 665     -43.986  18.548  26.561  1.00 33.06           C  
ANISOU 3216  CB  LEU A 665     4325   3923   4312   -409   -147   -347       C  
ATOM   3217  CG  LEU A 665     -42.577  19.113  26.683  1.00 27.50           C  
ANISOU 3217  CG  LEU A 665     3649   3138   3660   -366   -140   -317       C  
ATOM   3218  CD1 LEU A 665     -42.583  20.450  27.361  1.00 26.43           C  
ANISOU 3218  CD1 LEU A 665     3506   3008   3527   -326   -134   -289       C  
ATOM   3219  CD2 LEU A 665     -41.721  18.142  27.421  1.00 32.41           C  
ANISOU 3219  CD2 LEU A 665     4303   3683   4327   -401   -143   -312       C  
ATOM   3220  N   SER A 666     -46.412  17.402  24.970  1.00 41.32           N  
ANISOU 3220  N   SER A 666     5297   5180   5222   -492   -144   -432       N  
ATOM   3221  CA  SER A 666     -47.819  16.976  25.037  1.00 36.34           C  
ANISOU 3221  CA  SER A 666     4624   4663   4521   -549   -148   -467       C  
ATOM   3222  C   SER A 666     -48.093  15.663  24.329  1.00 37.00           C  
ANISOU 3222  C   SER A 666     4713   4768   4579   -638   -130   -530       C  
ATOM   3223  O   SER A 666     -49.068  14.994  24.632  1.00 48.22           O  
ANISOU 3223  O   SER A 666     6117   6250   5954   -715   -127   -569       O  
ATOM   3224  CB  SER A 666     -48.766  18.054  24.516  1.00 35.00           C  
ANISOU 3224  CB  SER A 666     4389   4632   4277   -488   -151   -451       C  
ATOM   3225  OG  SER A 666     -48.679  18.175  23.111  1.00 54.81           O  
ANISOU 3225  OG  SER A 666     6871   7204   6751   -459   -138   -463       O  
ATOM   3226  N   ALA A 667     -47.219  15.286  23.400  1.00 54.42           N  
ANISOU 3226  N   ALA A 667     6945   6919   6812   -633   -114   -543       N  
ATOM   3227  CA  ALA A 667     -47.466  14.127  22.536  1.00 67.94           C  
ANISOU 3227  CA  ALA A 667     8663   8657   8495   -716    -87   -609       C  
ATOM   3228  C   ALA A 667     -46.682  12.877  22.936  1.00 68.85           C  
ANISOU 3228  C   ALA A 667     8858   8627   8674   -774    -58   -626       C  
ATOM   3229  O   ALA A 667     -46.976  11.776  22.473  1.00 73.48           O  
ANISOU 3229  O   ALA A 667     9465   9215   9239   -861    -23   -686       O  
ATOM   3230  CB  ALA A 667     -47.204  14.483  21.053  1.00 68.50           C  
ANISOU 3230  CB  ALA A 667     8700   8789   8537   -677    -80   -620       C  
ATOM   3231  N   SER A 668     -45.677  13.054  23.783  1.00 75.00           N  
ANISOU 3231  N   SER A 668     9683   9288   9527   -725    -67   -573       N  
ATOM   3232  CA  SER A 668     -44.925  11.930  24.331  1.00 75.16           C  
ANISOU 3232  CA  SER A 668     9777   9176   9604   -759    -37   -571       C  
ATOM   3233  C   SER A 668     -45.637  11.382  25.565  1.00 77.97           C  
ANISOU 3233  C   SER A 668    10149   9521   9955   -818    -32   -574       C  
ATOM   3234  O   SER A 668     -46.352  12.115  26.250  1.00 78.16           O  
ANISOU 3234  O   SER A 668    10130   9615   9954   -806    -64   -556       O  
ATOM   3235  CB  SER A 668     -43.522  12.388  24.709  1.00 68.89           C  
ANISOU 3235  CB  SER A 668     9012   8286   8878   -676    -48   -509       C  
ATOM   3236  OG  SER A 668     -43.597  13.554  25.513  1.00 67.34           O  
ANISOU 3236  OG  SER A 668     8780   8121   8684   -623    -85   -465       O  
ATOM   3237  N   ASP A 669     -45.450  10.098  25.850  1.00 79.15           N  
ANISOU 3237  N   ASP A 669    10363   9580  10128   -878     13   -593       N  
ATOM   3238  CA  ASP A 669     -46.071   9.510  27.031  1.00 86.97           C  
ANISOU 3238  CA  ASP A 669    11378  10550  11118   -933     25   -592       C  
ATOM   3239  C   ASP A 669     -45.200   9.754  28.251  1.00 83.54           C  
ANISOU 3239  C   ASP A 669    10966  10033  10743   -867      8   -517       C  
ATOM   3240  O   ASP A 669     -43.975   9.824  28.148  1.00 82.78           O  
ANISOU 3240  O   ASP A 669    10896   9864  10695   -801     12   -477       O  
ATOM   3241  CB  ASP A 669     -46.340   8.017  26.832  1.00 93.94           C  
ANISOU 3241  CB  ASP A 669    12327  11371  11996  -1032     95   -647       C  
ATOM   3242  CG  ASP A 669     -47.507   7.761  25.893  1.00 96.28           C  
ANISOU 3242  CG  ASP A 669    12587  11783  12214  -1127    112   -733       C  
ATOM   3243  OD1 ASP A 669     -48.475   8.553  25.918  1.00 91.77           O  
ANISOU 3243  OD1 ASP A 669    11937  11348  11583  -1132     68   -745       O  
ATOM   3244  OD2 ASP A 669     -47.456   6.772  25.132  1.00 96.91           O  
ANISOU 3244  OD2 ASP A 669    12714  11823  12287  -1196    172   -791       O  
ATOM   3245  N   LEU A 670     -45.841   9.905  29.402  1.00 77.55           N  
ANISOU 3245  N   LEU A 670    10190   9300   9974   -885    -11   -500       N  
ATOM   3246  CA  LEU A 670     -45.126  10.201  30.634  1.00 77.25           C  
ANISOU 3246  CA  LEU A 670    10160   9210   9981   -829    -30   -433       C  
ATOM   3247  C   LEU A 670     -44.228   9.036  31.038  1.00 77.18           C  
ANISOU 3247  C   LEU A 670    10226   9078  10019   -825     21   -403       C  
ATOM   3248  O   LEU A 670     -43.235   9.223  31.744  1.00 86.03           O  
ANISOU 3248  O   LEU A 670    11353  10155  11178   -759     13   -342       O  
ATOM   3249  CB  LEU A 670     -46.120  10.517  31.751  1.00 77.87           C  
ANISOU 3249  CB  LEU A 670    10205   9349  10034   -860    -57   -428       C  
ATOM   3250  CG  LEU A 670     -47.220  11.500  31.349  1.00 73.34           C  
ANISOU 3250  CG  LEU A 670     9561   8904   9400   -868    -94   -459       C  
ATOM   3251  CD1 LEU A 670     -48.233  11.657  32.475  1.00 73.82           C  
ANISOU 3251  CD1 LEU A 670     9593   9021   9433   -904   -116   -456       C  
ATOM   3252  CD2 LEU A 670     -46.611  12.840  30.966  1.00 70.11           C  
ANISOU 3252  CD2 LEU A 670     9114   8521   9002   -780   -127   -427       C  
ATOM   3253  N   ASP A 671     -44.581   7.838  30.580  1.00 68.37           N  
ANISOU 3253  N   ASP A 671     9167   7915   8895   -894     80   -447       N  
ATOM   3254  CA  ASP A 671     -43.856   6.623  30.940  1.00 67.84           C  
ANISOU 3254  CA  ASP A 671     9185   7723   8868   -889    146   -418       C  
ATOM   3255  C   ASP A 671     -42.523   6.538  30.219  1.00 78.47           C  
ANISOU 3255  C   ASP A 671    10559   9004  10251   -816    164   -390       C  
ATOM   3256  O   ASP A 671     -41.607   5.848  30.665  1.00 85.99           O  
ANISOU 3256  O   ASP A 671    11567   9866  11242   -768    206   -337       O  
ATOM   3257  CB  ASP A 671     -44.693   5.384  30.619  1.00 69.33           C  
ANISOU 3257  CB  ASP A 671     9435   7873   9034   -996    218   -483       C  
ATOM   3258  N   GLN A 672     -42.417   7.240  29.097  1.00 79.36           N  
ANISOU 3258  N   GLN A 672    10633   9171  10351   -801    135   -422       N  
ATOM   3259  CA  GLN A 672     -41.215   7.184  28.277  1.00 77.91           C  
ANISOU 3259  CA  GLN A 672    10471   8935  10196   -739    150   -404       C  
ATOM   3260  C   GLN A 672     -40.314   8.412  28.447  1.00 66.01           C  
ANISOU 3260  C   GLN A 672     8908   7466   8706   -648     90   -351       C  
ATOM   3261  O   GLN A 672     -40.781   9.556  28.391  1.00 66.62           O  
ANISOU 3261  O   GLN A 672     8921   7631   8761   -643     37   -361       O  
ATOM   3262  CB  GLN A 672     -41.599   7.000  26.808  1.00 88.62           C  
ANISOU 3262  CB  GLN A 672    11828  10317  11525   -789    169   -478       C  
ATOM   3263  CG  GLN A 672     -42.258   5.660  26.505  1.00 95.19           C  
ANISOU 3263  CG  GLN A 672    12729  11097  12343   -887    247   -539       C  
ATOM   3264  CD  GLN A 672     -41.280   4.498  26.567  1.00 99.20           C  
ANISOU 3264  CD  GLN A 672    13333  11462  12896   -860    325   -509       C  
ATOM   3265  OE1 GLN A 672     -40.411   4.442  27.437  1.00 99.14           O  
ANISOU 3265  OE1 GLN A 672    13345  11397  12926   -780    326   -430       O  
ATOM   3266  NE2 GLN A 672     -41.420   3.562  25.637  1.00102.94           N  
ANISOU 3266  NE2 GLN A 672    13866  11885  13362   -924    397   -571       N  
ATOM   3267  N   PRO A 673     -39.014   8.167  28.658  1.00 45.65           N  
ANISOU 3267  N   PRO A 673     6357   4826   6164   -576    107   -296       N  
ATOM   3268  CA  PRO A 673     -37.984   9.194  28.831  1.00 44.78           C  
ANISOU 3268  CA  PRO A 673     6201   4748   6067   -498     63   -249       C  
ATOM   3269  C   PRO A 673     -38.019  10.208  27.702  1.00 46.69           C  
ANISOU 3269  C   PRO A 673     6399   5048   6294   -490     28   -284       C  
ATOM   3270  O   PRO A 673     -38.144   9.824  26.534  1.00 58.04           O  
ANISOU 3270  O   PRO A 673     7856   6472   7724   -512     50   -328       O  
ATOM   3271  CB  PRO A 673     -36.672   8.397  28.746  1.00 50.17           C  
ANISOU 3271  CB  PRO A 673     6931   5354   6778   -436    107   -203       C  
ATOM   3272  CG  PRO A 673     -37.025   7.024  29.122  1.00 55.06           C  
ANISOU 3272  CG  PRO A 673     7622   5893   7405   -468    173   -200       C  
ATOM   3273  CD  PRO A 673     -38.460   6.806  28.712  1.00 52.32           C  
ANISOU 3273  CD  PRO A 673     7283   5564   7033   -568    181   -275       C  
ATOM   3274  N   LEU A 674     -37.879  11.485  28.035  1.00 45.19           N  
ANISOU 3274  N   LEU A 674     6154   4919   6098   -459    -20   -266       N  
ATOM   3275  CA  LEU A 674     -37.850  12.537  27.021  1.00 51.16           C  
ANISOU 3275  CA  LEU A 674     6873   5724   6840   -440    -45   -289       C  
ATOM   3276  C   LEU A 674     -36.606  12.471  26.139  1.00 46.88           C  
ANISOU 3276  C   LEU A 674     6347   5146   6319   -391    -33   -278       C  
ATOM   3277  O   LEU A 674     -36.637  12.884  24.987  1.00 49.75           O  
ANISOU 3277  O   LEU A 674     6698   5533   6672   -385    -38   -307       O  
ATOM   3278  CB  LEU A 674     -37.869  13.903  27.693  1.00 52.55           C  
ANISOU 3278  CB  LEU A 674     7001   5957   7010   -416    -82   -268       C  
ATOM   3279  CG  LEU A 674     -39.197  14.458  28.164  1.00 47.21           C  
ANISOU 3279  CG  LEU A 674     6293   5340   6303   -451   -102   -287       C  
ATOM   3280  CD1 LEU A 674     -38.956  15.900  28.582  1.00 36.15           C  
ANISOU 3280  CD1 LEU A 674     4856   3978   4900   -416   -125   -267       C  
ATOM   3281  CD2 LEU A 674     -40.231  14.342  27.042  1.00 38.69           C  
ANISOU 3281  CD2 LEU A 674     5205   4305   5189   -482    -98   -336       C  
ATOM   3282  N   VAL A 675     -35.521  11.955  26.710  1.00 41.96           N  
ANISOU 3282  N   VAL A 675     5747   4477   5720   -352    -16   -233       N  
ATOM   3283  CA  VAL A 675     -34.186  12.053  26.145  1.00 43.74           C  
ANISOU 3283  CA  VAL A 675     5975   4683   5961   -296    -11   -211       C  
ATOM   3284  C   VAL A 675     -33.405  10.756  26.352  1.00 56.99           C  
ANISOU 3284  C   VAL A 675     7705   6292   7657   -266     35   -176       C  
ATOM   3285  O   VAL A 675     -33.154  10.348  27.486  1.00 64.64           O  
ANISOU 3285  O   VAL A 675     8679   7251   8630   -249     46   -131       O  
ATOM   3286  CB  VAL A 675     -33.373  13.166  26.846  1.00 47.40           C  
ANISOU 3286  CB  VAL A 675     6393   5195   6422   -259    -41   -175       C  
ATOM   3287  CG1 VAL A 675     -31.987  13.263  26.228  1.00 47.77           C  
ANISOU 3287  CG1 VAL A 675     6439   5235   6477   -206    -34   -155       C  
ATOM   3288  CG2 VAL A 675     -34.102  14.510  26.792  1.00 38.43           C  
ANISOU 3288  CG2 VAL A 675     5216   4115   5269   -279    -72   -201       C  
ATOM   3289  N   GLY A 676     -33.008  10.112  25.262  1.00 59.33           N  
ANISOU 3289  N   GLY A 676     8039   6542   7963   -255     66   -195       N  
ATOM   3290  CA  GLY A 676     -32.213   8.903  25.354  1.00 67.01           C  
ANISOU 3290  CA  GLY A 676     9067   7441   8953   -216    120   -158       C  
ATOM   3291  C   GLY A 676     -30.720   9.177  25.422  1.00 72.24           C  
ANISOU 3291  C   GLY A 676     9708   8121   9617   -134    114   -105       C  
ATOM   3292  O   GLY A 676     -30.284  10.326  25.448  1.00 67.10           O  
ANISOU 3292  O   GLY A 676     9000   7538   8956   -119     68   -101       O  
ATOM   3293  N   PRO A 677     -29.918   8.111  25.474  1.00 85.10           N  
ANISOU 3293  N   PRO A 677    11385   9692  11257    -80    166    -62       N  
ATOM   3294  CA  PRO A 677     -28.458   8.247  25.386  1.00 92.26           C  
ANISOU 3294  CA  PRO A 677    12271  10625  12158      2    166    -12       C  
ATOM   3295  C   PRO A 677     -27.960   8.691  23.994  1.00 88.61           C  
ANISOU 3295  C   PRO A 677    11800  10170  11699      9    151    -50       C  
ATOM   3296  O   PRO A 677     -26.904   9.322  23.891  1.00 81.28           O  
ANISOU 3296  O   PRO A 677    10828   9297  10758     56    126    -25       O  
ATOM   3297  CB  PRO A 677     -27.958   6.836  25.721  1.00 94.20           C  
ANISOU 3297  CB  PRO A 677    12583  10796  12412     60    240     43       C  
ATOM   3298  CG  PRO A 677     -29.083   6.216  26.517  1.00 91.44           C  
ANISOU 3298  CG  PRO A 677    12273  10400  12069      9    268     38       C  
ATOM   3299  CD  PRO A 677     -30.332   6.766  25.909  1.00 86.75           C  
ANISOU 3299  CD  PRO A 677    11668   9816  11477    -88    234    -47       C  
ATOM   3300  N   ASP A 678     -28.717   8.376  22.947  1.00 87.74           N  
ANISOU 3300  N   ASP A 678    11724  10013  11598    -42    167   -112       N  
ATOM   3301  CA  ASP A 678     -28.299   8.686  21.583  1.00 92.49           C  
ANISOU 3301  CA  ASP A 678    12319  10620  12201    -35    158   -147       C  
ATOM   3302  C   ASP A 678     -28.701  10.096  21.144  1.00 95.90           C  
ANISOU 3302  C   ASP A 678    12689  11128  12620    -67     97   -184       C  
ATOM   3303  O   ASP A 678     -28.122  10.654  20.211  1.00 99.97           O  
ANISOU 3303  O   ASP A 678    13183  11669  13134    -47     80   -198       O  
ATOM   3304  CB  ASP A 678     -28.878   7.659  20.605  1.00 94.26           C  
ANISOU 3304  CB  ASP A 678    12609  10771  12437    -76    210   -200       C  
ATOM   3305  N   ASP A 679     -29.691  10.666  21.824  1.00 89.90           N  
ANISOU 3305  N   ASP A 679    11903  10403  11852   -113     70   -197       N  
ATOM   3306  CA  ASP A 679     -30.260  11.951  21.432  1.00 74.38           C  
ANISOU 3306  CA  ASP A 679     9888   8501   9871   -139     26   -229       C  
ATOM   3307  C   ASP A 679     -29.270  13.116  21.474  1.00 70.07           C  
ANISOU 3307  C   ASP A 679     9298   8005   9320    -99     -4   -205       C  
ATOM   3308  O   ASP A 679     -28.389  13.164  22.327  1.00 77.20           O  
ANISOU 3308  O   ASP A 679    10188   8923  10221    -67     -5   -161       O  
ATOM   3309  CB  ASP A 679     -31.478  12.248  22.295  1.00 67.85           C  
ANISOU 3309  CB  ASP A 679     9046   7699   9033   -188     10   -240       C  
ATOM   3310  CG  ASP A 679     -32.612  11.288  22.031  1.00 76.74           C  
ANISOU 3310  CG  ASP A 679    10208   8795  10155   -245     39   -281       C  
ATOM   3311  OD1 ASP A 679     -32.609  10.667  20.949  1.00 78.07           O  
ANISOU 3311  OD1 ASP A 679    10403   8935  10324   -257     66   -316       O  
ATOM   3312  OD2 ASP A 679     -33.509  11.152  22.893  1.00 78.78           O  
ANISOU 3312  OD2 ASP A 679    10466   9060  10405   -284     37   -283       O  
ATOM   3313  N   ASN A 680     -29.417  14.053  20.541  1.00 55.89           N  
ANISOU 3313  N   ASN A 680     7478   6241   7515   -104    -23   -234       N  
ATOM   3314  CA  ASN A 680     -28.558  15.234  20.511  1.00 50.70           C  
ANISOU 3314  CA  ASN A 680     6787   5626   6852    -78    -41   -219       C  
ATOM   3315  C   ASN A 680     -29.336  16.532  20.285  1.00 43.95           C  
ANISOU 3315  C   ASN A 680     5906   4810   5984    -98    -58   -241       C  
ATOM   3316  O   ASN A 680     -30.508  16.513  19.907  1.00 45.85           O  
ANISOU 3316  O   ASN A 680     6148   5059   6216   -122    -59   -267       O  
ATOM   3317  CB  ASN A 680     -27.447  15.086  19.452  1.00 57.62           C  
ANISOU 3317  CB  ASN A 680     7669   6493   7732    -39    -34   -218       C  
ATOM   3318  CG  ASN A 680     -27.995  14.975  18.026  1.00 59.15           C  
ANISOU 3318  CG  ASN A 680     7873   6678   7925    -49    -29   -259       C  
ATOM   3319  OD1 ASN A 680     -28.879  15.740  17.612  1.00 59.48           O  
ANISOU 3319  OD1 ASN A 680     7895   6750   7954    -69    -41   -283       O  
ATOM   3320  ND2 ASN A 680     -27.466  14.018  17.269  1.00 55.93           N  
ANISOU 3320  ND2 ASN A 680     7491   6233   7526    -31     -9   -265       N  
ATOM   3321  N   SER A 681     -28.659  17.653  20.506  1.00 43.28           N  
ANISOU 3321  N   SER A 681     5799   4753   5892    -86    -63   -229       N  
ATOM   3322  CA  SER A 681     -29.241  18.979  20.328  1.00 52.98           C  
ANISOU 3322  CA  SER A 681     7014   6008   7110    -94    -63   -243       C  
ATOM   3323  C   SER A 681     -29.776  19.222  18.923  1.00 56.72           C  
ANISOU 3323  C   SER A 681     7488   6488   7575    -80    -59   -265       C  
ATOM   3324  O   SER A 681     -30.606  20.104  18.724  1.00 60.71           O  
ANISOU 3324  O   SER A 681     7984   7018   8066    -78    -54   -271       O  
ATOM   3325  CB  SER A 681     -28.197  20.048  20.641  1.00 56.17           C  
ANISOU 3325  CB  SER A 681     7404   6431   7508    -89    -55   -233       C  
ATOM   3326  OG  SER A 681     -27.286  19.574  21.613  1.00 68.38           O  
ANISOU 3326  OG  SER A 681     8939   7989   9053    -93    -58   -211       O  
ATOM   3327  N   GLU A 682     -29.281  18.474  17.941  1.00 62.67           N  
ANISOU 3327  N   GLU A 682     8251   7226   8335    -64    -58   -274       N  
ATOM   3328  CA  GLU A 682     -29.767  18.640  16.570  1.00 71.54           C  
ANISOU 3328  CA  GLU A 682     9367   8369   9445    -52    -54   -297       C  
ATOM   3329  C   GLU A 682     -31.110  17.960  16.335  1.00 72.19           C  
ANISOU 3329  C   GLU A 682     9446   8471   9511    -81    -55   -323       C  
ATOM   3330  O   GLU A 682     -31.906  18.412  15.505  1.00 76.28           O  
ANISOU 3330  O   GLU A 682     9943   9037  10003    -75    -54   -339       O  
ATOM   3331  CB  GLU A 682     -28.750  18.145  15.532  1.00 65.37           C  
ANISOU 3331  CB  GLU A 682     8595   7572   8673    -28    -51   -303       C  
ATOM   3332  CG  GLU A 682     -27.591  19.090  15.259  1.00 77.68           C  
ANISOU 3332  CG  GLU A 682    10147   9136  10234      0    -47   -287       C  
ATOM   3333  CD  GLU A 682     -26.261  18.542  15.752  1.00 88.68           C  
ANISOU 3333  CD  GLU A 682    11546  10509  11638     11    -48   -268       C  
ATOM   3334  OE1 GLU A 682     -25.207  19.046  15.298  1.00 91.81           O  
ANISOU 3334  OE1 GLU A 682    11935  10916  12031     31    -45   -262       O  
ATOM   3335  OE2 GLU A 682     -26.269  17.605  16.584  1.00 86.48           O  
ANISOU 3335  OE2 GLU A 682    11279  10211  11368      2    -49   -256       O  
ATOM   3336  N   THR A 683     -31.370  16.880  17.061  1.00 61.00           N  
ANISOU 3336  N   THR A 683     8048   7024   8104   -113    -54   -328       N  
ATOM   3337  CA  THR A 683     -32.555  16.087  16.777  1.00 61.38           C  
ANISOU 3337  CA  THR A 683     8098   7090   8134   -155    -47   -363       C  
ATOM   3338  C   THR A 683     -33.585  16.052  17.924  1.00 64.81           C  
ANISOU 3338  C   THR A 683     8528   7539   8559   -190    -53   -361       C  
ATOM   3339  O   THR A 683     -34.782  15.902  17.668  1.00 63.29           O  
ANISOU 3339  O   THR A 683     8318   7393   8334   -223    -52   -390       O  
ATOM   3340  CB  THR A 683     -32.157  14.656  16.377  1.00 71.16           C  
ANISOU 3340  CB  THR A 683     9373   8277   9387   -174    -24   -384       C  
ATOM   3341  OG1 THR A 683     -31.394  14.057  17.433  1.00 75.51           O  
ANISOU 3341  OG1 THR A 683     9956   8768   9967   -164    -16   -351       O  
ATOM   3342  CG2 THR A 683     -31.288  14.699  15.112  1.00 76.39           C  
ANISOU 3342  CG2 THR A 683    10034   8937  10054   -142    -19   -392       C  
ATOM   3343  N   ASN A 684     -33.135  16.204  19.172  1.00 45.39           N  
ANISOU 3343  N   ASN A 684     6077   5049   6118   -185    -59   -328       N  
ATOM   3344  CA  ASN A 684     -34.053  16.177  20.303  1.00 39.90           C  
ANISOU 3344  CA  ASN A 684     5378   4367   5416   -217    -66   -324       C  
ATOM   3345  C   ASN A 684     -34.489  17.592  20.699  1.00 33.67           C  
ANISOU 3345  C   ASN A 684     4559   3623   4611   -200    -78   -310       C  
ATOM   3346  O   ASN A 684     -33.653  18.452  20.976  1.00 40.41           O  
ANISOU 3346  O   ASN A 684     5410   4468   5476   -173    -78   -287       O  
ATOM   3347  CB  ASN A 684     -33.409  15.413  21.467  1.00 51.38           C  
ANISOU 3347  CB  ASN A 684     6857   5769   6895   -221    -60   -296       C  
ATOM   3348  CG  ASN A 684     -34.316  15.301  22.693  1.00 50.59           C  
ANISOU 3348  CG  ASN A 684     6753   5680   6788   -256    -67   -291       C  
ATOM   3349  OD1 ASN A 684     -34.531  16.276  23.417  1.00 53.18           O  
ANISOU 3349  OD1 ASN A 684     7057   6040   7110   -252    -82   -276       O  
ATOM   3350  ND2 ASN A 684     -34.807  14.092  22.957  1.00 40.28           N  
ANISOU 3350  ND2 ASN A 684     5477   4343   5486   -293    -49   -303       N  
ATOM   3351  N   PRO A 685     -35.810  17.844  20.695  1.00 37.72           N  
ANISOU 3351  N   PRO A 685     5052   4189   5093   -219    -82   -326       N  
ATOM   3352  CA  PRO A 685     -36.410  19.151  21.014  1.00 38.53           C  
ANISOU 3352  CA  PRO A 685     5130   4334   5175   -196    -84   -311       C  
ATOM   3353  C   PRO A 685     -36.040  19.653  22.417  1.00 39.53           C  
ANISOU 3353  C   PRO A 685     5264   4433   5321   -201    -87   -286       C  
ATOM   3354  O   PRO A 685     -35.808  20.849  22.577  1.00 45.78           O  
ANISOU 3354  O   PRO A 685     6053   5229   6112   -175    -75   -271       O  
ATOM   3355  CB  PRO A 685     -37.930  18.886  20.937  1.00 28.14           C  
ANISOU 3355  CB  PRO A 685     3790   3085   3817   -224    -89   -333       C  
ATOM   3356  CG  PRO A 685     -38.078  17.671  20.148  1.00 25.52           C  
ANISOU 3356  CG  PRO A 685     3463   2756   3477   -260    -85   -369       C  
ATOM   3357  CD  PRO A 685     -36.833  16.841  20.354  1.00 36.70           C  
ANISOU 3357  CD  PRO A 685     4919   4085   4939   -266    -79   -362       C  
ATOM   3358  N   VAL A 686     -36.004  18.770  23.415  1.00 34.90           N  
ANISOU 3358  N   VAL A 686     4688   3822   4750   -236    -96   -282       N  
ATOM   3359  CA  VAL A 686     -35.523  19.159  24.744  1.00 37.18           C  
ANISOU 3359  CA  VAL A 686     4976   4096   5053   -243    -99   -259       C  
ATOM   3360  C   VAL A 686     -34.052  19.587  24.718  1.00 37.44           C  
ANISOU 3360  C   VAL A 686     5014   4107   5105   -219    -91   -243       C  
ATOM   3361  O   VAL A 686     -33.705  20.676  25.197  1.00 43.22           O  
ANISOU 3361  O   VAL A 686     5738   4849   5835   -216    -81   -236       O  
ATOM   3362  CB  VAL A 686     -35.680  18.045  25.800  1.00 37.19           C  
ANISOU 3362  CB  VAL A 686     4987   4080   5065   -277   -107   -251       C  
ATOM   3363  CG1 VAL A 686     -35.176  18.548  27.166  1.00 34.67           C  
ANISOU 3363  CG1 VAL A 686     4654   3766   4753   -282   -111   -226       C  
ATOM   3364  CG2 VAL A 686     -37.117  17.601  25.895  1.00 37.48           C  
ANISOU 3364  CG2 VAL A 686     5018   4143   5079   -312   -113   -272       C  
ATOM   3365  N   LEU A 687     -33.185  18.745  24.162  1.00 32.42           N  
ANISOU 3365  N   LEU A 687     4392   3444   4484   -207    -89   -240       N  
ATOM   3366  CA  LEU A 687     -31.774  19.132  24.036  1.00 36.36           C  
ANISOU 3366  CA  LEU A 687     4888   3936   4991   -183    -82   -226       C  
ATOM   3367  C   LEU A 687     -31.591  20.390  23.189  1.00 37.19           C  
ANISOU 3367  C   LEU A 687     4990   4052   5088   -164    -69   -237       C  
ATOM   3368  O   LEU A 687     -30.770  21.247  23.513  1.00 48.31           O  
ANISOU 3368  O   LEU A 687     6393   5468   6496   -164    -56   -232       O  
ATOM   3369  CB  LEU A 687     -30.921  17.984  23.498  1.00 36.42           C  
ANISOU 3369  CB  LEU A 687     4911   3914   5011   -164    -79   -218       C  
ATOM   3370  CG  LEU A 687     -30.861  16.800  24.455  1.00 44.28           C  
ANISOU 3370  CG  LEU A 687     5918   4892   6015   -172    -78   -195       C  
ATOM   3371  CD1 LEU A 687     -29.930  15.721  23.929  1.00 36.26           C  
ANISOU 3371  CD1 LEU A 687     4925   3841   5010   -140    -62   -180       C  
ATOM   3372  CD2 LEU A 687     -30.466  17.265  25.889  1.00 25.15           C  
ANISOU 3372  CD2 LEU A 687     3468   2503   3584   -181    -84   -169       C  
ATOM   3373  N   LEU A 688     -32.362  20.504  22.113  1.00 40.68           N  
ANISOU 3373  N   LEU A 688     5435   4501   5521   -149    -66   -252       N  
ATOM   3374  CA  LEU A 688     -32.253  21.653  21.228  1.00 38.23           C  
ANISOU 3374  CA  LEU A 688     5125   4200   5201   -119    -47   -255       C  
ATOM   3375  C   LEU A 688     -32.606  22.937  21.969  1.00 40.22           C  
ANISOU 3375  C   LEU A 688     5379   4460   5444   -122    -25   -248       C  
ATOM   3376  O   LEU A 688     -31.896  23.952  21.869  1.00 42.35           O  
ANISOU 3376  O   LEU A 688     5659   4718   5715   -114      4   -246       O  
ATOM   3377  CB  LEU A 688     -33.174  21.491  20.023  1.00 40.65           C  
ANISOU 3377  CB  LEU A 688     5424   4533   5488    -99    -47   -267       C  
ATOM   3378  CG  LEU A 688     -33.178  22.718  19.111  1.00 50.78           C  
ANISOU 3378  CG  LEU A 688     6706   5831   6756    -55    -21   -260       C  
ATOM   3379  CD1 LEU A 688     -32.406  22.431  17.827  1.00 47.94           C  
ANISOU 3379  CD1 LEU A 688     6348   5466   6400    -32    -21   -267       C  
ATOM   3380  CD2 LEU A 688     -34.598  23.146  18.798  1.00 56.53           C  
ANISOU 3380  CD2 LEU A 688     7418   6612   7449    -34    -13   -257       C  
ATOM   3381  N   ALA A 689     -33.704  22.887  22.719  1.00 37.03           N  
ANISOU 3381  N   ALA A 689     4966   4074   5029   -138    -32   -247       N  
ATOM   3382  CA  ALA A 689     -34.194  24.056  23.438  1.00 30.64           C  
ANISOU 3382  CA  ALA A 689     4161   3270   4210   -139     -6   -242       C  
ATOM   3383  C   ALA A 689     -33.218  24.477  24.516  1.00 28.87           C  
ANISOU 3383  C   ALA A 689     3941   3029   3998   -173      6   -243       C  
ATOM   3384  O   ALA A 689     -33.016  25.674  24.732  1.00 32.91           O  
ANISOU 3384  O   ALA A 689     4469   3529   4506   -175     47   -246       O  
ATOM   3385  CB  ALA A 689     -35.565  23.771  24.032  1.00 30.46           C  
ANISOU 3385  CB  ALA A 689     4124   3278   4170   -151    -22   -242       C  
ATOM   3386  N   ARG A 690     -32.605  23.498  25.180  1.00 31.75           N  
ANISOU 3386  N   ARG A 690     4293   3398   4375   -201    -22   -240       N  
ATOM   3387  CA  ARG A 690     -31.596  23.797  26.202  1.00 37.13           C  
ANISOU 3387  CA  ARG A 690     4963   4088   5056   -234    -13   -241       C  
ATOM   3388  C   ARG A 690     -30.403  24.506  25.605  1.00 38.68           C  
ANISOU 3388  C   ARG A 690     5168   4279   5251   -231     15   -250       C  
ATOM   3389  O   ARG A 690     -29.894  25.473  26.173  1.00 49.39           O  
ANISOU 3389  O   ARG A 690     6526   5644   6598   -262     48   -264       O  
ATOM   3390  CB  ARG A 690     -31.128  22.539  26.922  1.00 40.49           C  
ANISOU 3390  CB  ARG A 690     5369   4530   5487   -247    -44   -225       C  
ATOM   3391  CG  ARG A 690     -31.836  22.300  28.247  1.00 42.69           C  
ANISOU 3391  CG  ARG A 690     5632   4828   5761   -277    -57   -219       C  
ATOM   3392  CD  ARG A 690     -31.584  20.887  28.768  1.00 43.82           C  
ANISOU 3392  CD  ARG A 690     5763   4976   5909   -274    -82   -195       C  
ATOM   3393  NE  ARG A 690     -32.701  20.412  29.572  1.00 46.95           N  
ANISOU 3393  NE  ARG A 690     6158   5375   6305   -294    -96   -190       N  
ATOM   3394  CZ  ARG A 690     -32.849  19.161  29.985  1.00 52.14           C  
ANISOU 3394  CZ  ARG A 690     6818   6023   6968   -293   -109   -169       C  
ATOM   3395  NH1 ARG A 690     -31.936  18.254  29.678  1.00 55.05           N  
ANISOU 3395  NH1 ARG A 690     7195   6377   7344   -266   -106   -148       N  
ATOM   3396  NH2 ARG A 690     -33.917  18.823  30.701  1.00 55.28           N  
ANISOU 3396  NH2 ARG A 690     7216   6425   7364   -317   -119   -169       N  
ATOM   3397  N   ARG A 691     -29.963  24.024  24.450  1.00 44.84           N  
ANISOU 3397  N   ARG A 691     5953   5046   6037   -198      5   -246       N  
ATOM   3398  CA  ARG A 691     -28.890  24.678  23.720  1.00 40.74           C  
ANISOU 3398  CA  ARG A 691     5443   4522   5515   -192     31   -255       C  
ATOM   3399  C   ARG A 691     -29.228  26.124  23.349  1.00 45.64           C  
ANISOU 3399  C   ARG A 691     6092   5119   6129   -187     82   -266       C  
ATOM   3400  O   ARG A 691     -28.397  27.019  23.548  1.00 45.55           O  
ANISOU 3400  O   ARG A 691     6091   5106   6110   -217    122   -282       O  
ATOM   3401  CB  ARG A 691     -28.506  23.884  22.474  1.00 44.54           C  
ANISOU 3401  CB  ARG A 691     5926   4993   6005   -153     11   -249       C  
ATOM   3402  CG  ARG A 691     -27.390  24.560  21.688  1.00 53.73           C  
ANISOU 3402  CG  ARG A 691     7097   6155   7164   -147     36   -257       C  
ATOM   3403  CD  ARG A 691     -26.890  23.721  20.535  1.00 55.05           C  
ANISOU 3403  CD  ARG A 691     7261   6316   7338   -111     15   -252       C  
ATOM   3404  NE  ARG A 691     -25.510  24.071  20.228  1.00 65.73           N  
ANISOU 3404  NE  ARG A 691     8609   7684   8682   -116     29   -258       N  
ATOM   3405  CZ  ARG A 691     -24.796  23.498  19.273  1.00 82.80           C  
ANISOU 3405  CZ  ARG A 691    10768   9847  10847    -87     16   -254       C  
ATOM   3406  NH1 ARG A 691     -25.340  22.550  18.519  1.00 97.92           N  
ANISOU 3406  NH1 ARG A 691    12687  11742  12775    -55     -6   -249       N  
ATOM   3407  NH2 ARG A 691     -23.546  23.882  19.064  1.00 83.59           N  
ANISOU 3407  NH2 ARG A 691    10858   9971  10933    -96     29   -260       N  
ATOM   3408  N   MET A 692     -30.430  26.361  22.812  1.00 37.69           N  
ANISOU 3408  N   MET A 692     5100   4100   5122   -151     88   -257       N  
ATOM   3409  CA  MET A 692     -30.828  27.732  22.466  1.00 38.11           C  
ANISOU 3409  CA  MET A 692     5186   4127   5166   -130    148   -256       C  
ATOM   3410  C   MET A 692     -30.883  28.645  23.692  1.00 38.50           C  
ANISOU 3410  C   MET A 692     5252   4166   5211   -174    189   -269       C  
ATOM   3411  O   MET A 692     -30.413  29.781  23.652  1.00 39.34           O  
ANISOU 3411  O   MET A 692     5392   4243   5313   -188    253   -282       O  
ATOM   3412  CB  MET A 692     -32.171  27.781  21.729  1.00 39.49           C  
ANISOU 3412  CB  MET A 692     5364   4313   5329    -72    148   -236       C  
ATOM   3413  CG  MET A 692     -32.227  27.044  20.407  1.00 50.20           C  
ANISOU 3413  CG  MET A 692     6703   5687   6682    -33    118   -230       C  
ATOM   3414  SD  MET A 692     -30.967  27.472  19.174  1.00 61.06           S  
ANISOU 3414  SD  MET A 692     8096   7040   8064    -11    144   -231       S  
ATOM   3415  CE  MET A 692     -31.998  27.362  17.742  1.00 76.65           C  
ANISOU 3415  CE  MET A 692    10056   9052  10015     60    141   -212       C  
ATOM   3416  N   ALA A 693     -31.475  28.155  24.775  1.00 35.52           N  
ANISOU 3416  N   ALA A 693     4852   3811   4832   -200    159   -269       N  
ATOM   3417  CA  ALA A 693     -31.552  28.940  26.008  1.00 35.20           C  
ANISOU 3417  CA  ALA A 693     4822   3768   4786   -248    196   -286       C  
ATOM   3418  C   ALA A 693     -30.161  29.366  26.456  1.00 38.92           C  
ANISOU 3418  C   ALA A 693     5290   4246   5250   -309    224   -314       C  
ATOM   3419  O   ALA A 693     -29.938  30.530  26.766  1.00 48.87           O  
ANISOU 3419  O   ALA A 693     6583   5482   6503   -343    292   -337       O  
ATOM   3420  CB  ALA A 693     -32.251  28.149  27.120  1.00 26.32           C  
ANISOU 3420  CB  ALA A 693     3663   2676   3660   -271    149   -281       C  
ATOM   3421  N   SER A 694     -29.234  28.413  26.491  1.00 37.54           N  
ANISOU 3421  N   SER A 694     5078   4111   5076   -324    178   -313       N  
ATOM   3422  CA  SER A 694     -27.889  28.658  27.018  1.00 45.25           C  
ANISOU 3422  CA  SER A 694     6034   5126   6033   -383    196   -339       C  
ATOM   3423  C   SER A 694     -26.994  29.508  26.116  1.00 48.79           C  
ANISOU 3423  C   SER A 694     6512   5552   6475   -391    247   -359       C  
ATOM   3424  O   SER A 694     -26.038  30.114  26.594  1.00 50.78           O  
ANISOU 3424  O   SER A 694     6758   5833   6704   -456    286   -392       O  
ATOM   3425  CB  SER A 694     -27.176  27.343  27.329  1.00 47.64           C  
ANISOU 3425  CB  SER A 694     6284   5488   6330   -381    135   -321       C  
ATOM   3426  OG  SER A 694     -26.566  26.813  26.176  1.00 46.54           O  
ANISOU 3426  OG  SER A 694     6146   5340   6198   -339    116   -308       O  
ATOM   3427  N   ILE A 695     -27.297  29.540  24.818  1.00 45.52           N  
ANISOU 3427  N   ILE A 695     6126   5093   6076   -329    249   -340       N  
ATOM   3428  CA  ILE A 695     -26.592  30.403  23.878  1.00 34.40           C  
ANISOU 3428  CA  ILE A 695     4754   3653   4664   -328    303   -354       C  
ATOM   3429  C   ILE A 695     -27.194  31.812  23.856  1.00 42.57           C  
ANISOU 3429  C   ILE A 695     5851   4626   5699   -330    391   -364       C  
ATOM   3430  O   ILE A 695     -26.465  32.794  23.774  1.00 46.44           O  
ANISOU 3430  O   ILE A 695     6375   5092   6177   -374    462   -393       O  
ATOM   3431  CB  ILE A 695     -26.600  29.805  22.430  1.00 50.72           C  
ANISOU 3431  CB  ILE A 695     6821   5707   6745   -256    270   -327       C  
ATOM   3432  CG1 ILE A 695     -25.674  28.590  22.320  1.00 43.69           C  
ANISOU 3432  CG1 ILE A 695     5882   4866   5851   -257    207   -322       C  
ATOM   3433  CG2 ILE A 695     -26.153  30.836  21.408  1.00 47.34           C  
ANISOU 3433  CG2 ILE A 695     6437   5236   6313   -243    334   -334       C  
ATOM   3434  CD1 ILE A 695     -25.869  27.830  21.020  1.00 40.72           C  
ANISOU 3434  CD1 ILE A 695     5505   4477   5490   -191    170   -299       C  
ATOM   3435  N   TYR A 696     -28.521  31.912  23.950  1.00 46.72           N  
ANISOU 3435  N   TYR A 696     6393   5126   6233   -283    392   -339       N  
ATOM   3436  CA  TYR A 696     -29.202  33.203  23.792  1.00 44.12           C  
ANISOU 3436  CA  TYR A 696     6127   4733   5901   -259    481   -335       C  
ATOM   3437  C   TYR A 696     -29.649  33.914  25.082  1.00 44.60           C  
ANISOU 3437  C   TYR A 696     6210   4779   5956   -310    531   -358       C  
ATOM   3438  O   TYR A 696     -29.602  35.142  25.160  1.00 53.02           O  
ANISOU 3438  O   TYR A 696     7340   5788   7018   -329    630   -375       O  
ATOM   3439  CB  TYR A 696     -30.412  33.081  22.855  1.00 41.27           C  
ANISOU 3439  CB  TYR A 696     5775   4361   5544   -157    470   -287       C  
ATOM   3440  CG  TYR A 696     -30.103  32.615  21.449  1.00 48.47           C  
ANISOU 3440  CG  TYR A 696     6674   5283   6458   -102    440   -266       C  
ATOM   3441  CD1 TYR A 696     -28.830  32.726  20.916  1.00 49.07           C  
ANISOU 3441  CD1 TYR A 696     6757   5351   6537   -131    453   -285       C  
ATOM   3442  CD2 TYR A 696     -31.104  32.089  20.640  1.00 55.98           C  
ANISOU 3442  CD2 TYR A 696     7605   6261   7404    -24    402   -230       C  
ATOM   3443  CE1 TYR A 696     -28.558  32.304  19.612  1.00 50.54           C  
ANISOU 3443  CE1 TYR A 696     6931   5546   6725    -80    426   -267       C  
ATOM   3444  CE2 TYR A 696     -30.840  31.670  19.343  1.00 57.20           C  
ANISOU 3444  CE2 TYR A 696     7745   6432   7558     21    378   -215       C  
ATOM   3445  CZ  TYR A 696     -29.570  31.782  18.838  1.00 52.02           C  
ANISOU 3445  CZ  TYR A 696     7098   5758   6909     -4    389   -232       C  
ATOM   3446  OH  TYR A 696     -29.314  31.362  17.560  1.00 57.33           O  
ANISOU 3446  OH  TYR A 696     7754   6447   7580     41    365   -218       O  
ATOM   3447  N   PHE A 697     -30.120  33.173  26.077  1.00 39.26           N  
ANISOU 3447  N   PHE A 697     5487   4149   5279   -332    471   -358       N  
ATOM   3448  CA  PHE A 697     -30.686  33.842  27.250  1.00 49.23           C  
ANISOU 3448  CA  PHE A 697     6770   5399   6536   -373    517   -376       C  
ATOM   3449  C   PHE A 697     -29.635  34.483  28.147  1.00 50.01           C  
ANISOU 3449  C   PHE A 697     6874   5507   6618   -481    571   -433       C  
ATOM   3450  O   PHE A 697     -29.906  35.479  28.812  1.00 52.81           O  
ANISOU 3450  O   PHE A 697     7274   5825   6967   -520    651   -460       O  
ATOM   3451  CB  PHE A 697     -31.606  32.920  28.054  1.00 41.33           C  
ANISOU 3451  CB  PHE A 697     5720   4446   5537   -363    441   -358       C  
ATOM   3452  CG  PHE A 697     -32.763  32.389  27.264  1.00 47.16           C  
ANISOU 3452  CG  PHE A 697     6452   5187   6281   -272    399   -312       C  
ATOM   3453  CD1 PHE A 697     -33.144  32.991  26.068  1.00 49.21           C  
ANISOU 3453  CD1 PHE A 697     6752   5407   6538   -196    444   -285       C  
ATOM   3454  CD2 PHE A 697     -33.480  31.292  27.714  1.00 38.67           C  
ANISOU 3454  CD2 PHE A 697     5328   4160   5206   -264    320   -297       C  
ATOM   3455  CE1 PHE A 697     -34.214  32.490  25.327  1.00 45.22           C  
ANISOU 3455  CE1 PHE A 697     6228   4928   6025   -116    406   -246       C  
ATOM   3456  CE2 PHE A 697     -34.547  30.787  26.978  1.00 41.99           C  
ANISOU 3456  CE2 PHE A 697     5737   4596   5622   -193    285   -263       C  
ATOM   3457  CZ  PHE A 697     -34.916  31.386  25.788  1.00 39.00           C  
ANISOU 3457  CZ  PHE A 697     5388   4195   5234   -121    326   -239       C  
ATOM   3458  N   ASP A 698     -28.434  33.924  28.151  1.00 56.73           N  
ANISOU 3458  N   ASP A 698     7680   6415   7458   -529    533   -454       N  
ATOM   3459  CA  ASP A 698     -27.373  34.451  28.993  1.00 70.77           C  
ANISOU 3459  CA  ASP A 698     9447   8232   9208   -639    579   -512       C  
ATOM   3460  C   ASP A 698     -26.463  35.405  28.220  1.00 72.59           C  
ANISOU 3460  C   ASP A 698     9730   8421   9429   -672    664   -544       C  
ATOM   3461  O   ASP A 698     -25.438  35.856  28.727  1.00 78.86           O  
ANISOU 3461  O   ASP A 698    10514   9257  10193   -772    708   -600       O  
ATOM   3462  CB  ASP A 698     -26.587  33.306  29.639  1.00 80.00           C  
ANISOU 3462  CB  ASP A 698    10526   9512  10358   -676    494   -514       C  
ATOM   3463  CG  ASP A 698     -27.404  32.558  30.693  1.00 94.12           C  
ANISOU 3463  CG  ASP A 698    12270  11341  12149   -668    434   -493       C  
ATOM   3464  OD1 ASP A 698     -27.202  31.331  30.844  1.00 98.54           O  
ANISOU 3464  OD1 ASP A 698    12769  11963  12708   -643    351   -464       O  
ATOM   3465  OD2 ASP A 698     -28.258  33.194  31.365  1.00 95.57           O  
ANISOU 3465  OD2 ASP A 698    12483  11493  12337   -685    474   -505       O  
ATOM   3466  N   ASN A 699     -26.859  35.716  26.991  1.00 66.90           N  
ANISOU 3466  N   ASN A 699     9063   7626   8731   -590    690   -510       N  
ATOM   3467  CA  ASN A 699     -26.136  36.662  26.155  1.00 57.23           C  
ANISOU 3467  CA  ASN A 699     7899   6345   7500   -608    778   -531       C  
ATOM   3468  C   ASN A 699     -26.971  37.920  26.019  1.00 57.83           C  
ANISOU 3468  C   ASN A 699     8072   6314   7587   -579    893   -526       C  
ATOM   3469  O   ASN A 699     -27.901  37.960  25.225  1.00 62.44           O  
ANISOU 3469  O   ASN A 699     8685   6849   8189   -470    893   -470       O  
ATOM   3470  CB  ASN A 699     -25.880  36.042  24.781  1.00 55.91           C  
ANISOU 3470  CB  ASN A 699     7718   6178   7346   -527    724   -490       C  
ATOM   3471  CG  ASN A 699     -25.068  36.950  23.859  1.00 58.47           C  
ANISOU 3471  CG  ASN A 699     8101   6451   7664   -544    809   -509       C  
ATOM   3472  OD1 ASN A 699     -25.353  38.145  23.716  1.00 59.48           O  
ANISOU 3472  OD1 ASN A 699     8314   6492   7794   -546    922   -518       O  
ATOM   3473  ND2 ASN A 699     -24.058  36.374  23.215  1.00 42.38           N  
ANISOU 3473  ND2 ASN A 699     6022   4463   5617   -551    761   -513       N  
ATOM   3474  N   ALA A 700     -26.647  38.943  26.802  1.00 66.29           N  
ANISOU 3474  N   ALA A 700     9191   7353   8642   -675    996   -584       N  
ATOM   3475  CA  ALA A 700     -27.438  40.176  26.840  1.00 67.23           C  
ANISOU 3475  CA  ALA A 700     9413   7363   8770   -651   1122   -581       C  
ATOM   3476  C   ALA A 700     -27.718  40.783  25.461  1.00 69.28           C  
ANISOU 3476  C   ALA A 700     9749   7531   9045   -548   1188   -531       C  
ATOM   3477  O   ALA A 700     -28.823  41.261  25.197  1.00 70.99           O  
ANISOU 3477  O   ALA A 700    10019   7682   9272   -452   1238   -481       O  
ATOM   3478  CB  ALA A 700     -26.775  41.204  27.744  1.00 62.47           C  
ANISOU 3478  CB  ALA A 700     8858   6734   8143   -790   1239   -664       C  
ATOM   3479  N   GLY A 701     -26.719  40.770  24.586  1.00 63.00           N  
ANISOU 3479  N   GLY A 701     8954   6739   8244   -564   1192   -541       N  
ATOM   3480  CA  GLY A 701     -26.881  41.338  23.259  1.00 67.48           C  
ANISOU 3480  CA  GLY A 701     9590   7228   8823   -470   1256   -494       C  
ATOM   3481  C   GLY A 701     -27.965  40.650  22.444  1.00 69.07           C  
ANISOU 3481  C   GLY A 701     9757   7447   9038   -321   1175   -409       C  
ATOM   3482  O   GLY A 701     -28.659  41.273  21.636  1.00 68.38           O  
ANISOU 3482  O   GLY A 701     9730   7296   8954   -216   1243   -354       O  
ATOM   3483  N   ILE A 702     -28.115  39.351  22.658  1.00 65.05           N  
ANISOU 3483  N   ILE A 702     9149   7033   8532   -311   1035   -398       N  
ATOM   3484  CA  ILE A 702     -29.074  38.569  21.898  1.00 57.99           C  
ANISOU 3484  CA  ILE A 702     8213   6175   7646   -191    952   -331       C  
ATOM   3485  C   ILE A 702     -30.431  38.530  22.590  1.00 57.64           C  
ANISOU 3485  C   ILE A 702     8164   6137   7600   -143    942   -302       C  
ATOM   3486  O   ILE A 702     -31.462  38.714  21.944  1.00 54.12           O  
ANISOU 3486  O   ILE A 702     7733   5681   7148    -32    958   -243       O  
ATOM   3487  CB  ILE A 702     -28.535  37.154  21.632  1.00 53.63           C  
ANISOU 3487  CB  ILE A 702     7567   5712   7097   -203    817   -333       C  
ATOM   3488  CG1 ILE A 702     -27.352  37.242  20.649  1.00 46.99           C  
ANISOU 3488  CG1 ILE A 702     6735   4865   6255   -218    830   -346       C  
ATOM   3489  CG2 ILE A 702     -29.646  36.245  21.111  1.00 34.73           C  
ANISOU 3489  CG2 ILE A 702     5125   3364   4706   -104    732   -279       C  
ATOM   3490  CD1 ILE A 702     -26.587  35.952  20.476  1.00 44.96           C  
ANISOU 3490  CD1 ILE A 702     6396   4689   5998   -241    716   -356       C  
ATOM   3491  N   SER A 703     -30.419  38.333  23.905  1.00 55.16           N  
ANISOU 3491  N   SER A 703     7825   5848   7285   -227    921   -343       N  
ATOM   3492  CA  SER A 703     -31.646  38.264  24.689  1.00 51.30           C  
ANISOU 3492  CA  SER A 703     7327   5371   6794   -194    907   -322       C  
ATOM   3493  C   SER A 703     -32.570  39.477  24.511  1.00 53.96           C  
ANISOU 3493  C   SER A 703     7750   5629   7124   -117   1027   -287       C  
ATOM   3494  O   SER A 703     -33.789  39.324  24.465  1.00 63.95           O  
ANISOU 3494  O   SER A 703     9001   6917   8380    -29   1006   -237       O  
ATOM   3495  CB  SER A 703     -31.341  38.045  26.173  1.00 50.10           C  
ANISOU 3495  CB  SER A 703     7143   5253   6640   -307    884   -377       C  
ATOM   3496  OG  SER A 703     -32.541  38.152  26.929  1.00 57.50           O  
ANISOU 3496  OG  SER A 703     8083   6191   7574   -276    887   -359       O  
ATOM   3497  N   ARG A 704     -32.005  40.675  24.414  1.00 44.33           N  
ANISOU 3497  N   ARG A 704     6620   4318   5905   -149   1159   -310       N  
ATOM   3498  CA  ARG A 704     -32.826  41.867  24.208  1.00 51.25           C  
ANISOU 3498  CA  ARG A 704     7592   5106   6774    -65   1292   -270       C  
ATOM   3499  C   ARG A 704     -33.612  41.827  22.890  1.00 56.43           C  
ANISOU 3499  C   ARG A 704     8247   5774   7419     92   1287   -183       C  
ATOM   3500  O   ARG A 704     -34.624  42.516  22.745  1.00 54.14           O  
ANISOU 3500  O   ARG A 704     8007   5451   7115    196   1365   -127       O  
ATOM   3501  CB  ARG A 704     -31.975  43.136  24.271  1.00 59.85           C  
ANISOU 3501  CB  ARG A 704     8789   6085   7867   -136   1447   -315       C  
ATOM   3502  N   GLN A 705     -33.135  41.039  21.927  1.00 56.15           N  
ANISOU 3502  N   GLN A 705     8155   5795   7386    112   1201   -170       N  
ATOM   3503  CA  GLN A 705     -33.809  40.924  20.633  1.00 59.10           C  
ANISOU 3503  CA  GLN A 705     8513   6201   7742    252   1189    -93       C  
ATOM   3504  C   GLN A 705     -34.965  39.938  20.708  1.00 61.38           C  
ANISOU 3504  C   GLN A 705     8712   6596   8012    313   1077    -58       C  
ATOM   3505  O   GLN A 705     -35.711  39.764  19.744  1.00 54.12           O  
ANISOU 3505  O   GLN A 705     7764   5733   7067    426   1060      4       O  
ATOM   3506  CB  GLN A 705     -32.835  40.488  19.540  1.00 53.20           C  
ANISOU 3506  CB  GLN A 705     7740   5472   7002    244   1146    -98       C  
ATOM   3507  CG  GLN A 705     -31.868  41.569  19.106  1.00 61.19           C  
ANISOU 3507  CG  GLN A 705     8844   6383   8021    216   1271   -115       C  
ATOM   3508  CD  GLN A 705     -30.891  41.076  18.060  1.00 70.60           C  
ANISOU 3508  CD  GLN A 705    10002   7603   9218    205   1219   -122       C  
ATOM   3509  OE1 GLN A 705     -31.267  40.798  16.920  1.00 74.61           O  
ANISOU 3509  OE1 GLN A 705    10482   8154   9714    307   1189    -66       O  
ATOM   3510  NE2 GLN A 705     -29.626  40.969  18.441  1.00 72.84           N  
ANISOU 3510  NE2 GLN A 705    10286   7876   9515     80   1209   -192       N  
ATOM   3511  N   ILE A 706     -35.106  39.293  21.861  1.00 56.79           N  
ANISOU 3511  N   ILE A 706     8086   6052   7441    233   1006    -99       N  
ATOM   3512  CA  ILE A 706     -36.158  38.310  22.050  1.00 54.06           C  
ANISOU 3512  CA  ILE A 706     7659   5805   7077    270    902    -76       C  
ATOM   3513  C   ILE A 706     -37.279  38.913  22.891  1.00 56.74           C  
ANISOU 3513  C   ILE A 706     8025   6134   7399    308    955    -54       C  
ATOM   3514  O   ILE A 706     -37.028  39.700  23.804  1.00 60.67           O  
ANISOU 3514  O   ILE A 706     8585   6557   7910    251   1035    -86       O  
ATOM   3515  CB  ILE A 706     -35.595  37.033  22.699  1.00 48.96           C  
ANISOU 3515  CB  ILE A 706     6939   5213   6452    165    779   -128       C  
ATOM   3516  CG1 ILE A 706     -34.489  36.450  21.815  1.00 40.37           C  
ANISOU 3516  CG1 ILE A 706     5827   4135   5377    139    733   -144       C  
ATOM   3517  CG2 ILE A 706     -36.701  36.019  22.950  1.00 43.93           C  
ANISOU 3517  CG2 ILE A 706     6227   4668   5797    192    683   -109       C  
ATOM   3518  CD1 ILE A 706     -33.748  35.285  22.442  1.00 35.88           C  
ANISOU 3518  CD1 ILE A 706     5197   3608   4827     43    632   -190       C  
ATOM   3519  N   HIS A 707     -38.518  38.576  22.559  1.00 56.80           N  
ANISOU 3519  N   HIS A 707     7986   6224   7372    403    918     -2       N  
ATOM   3520  CA  HIS A 707     -39.662  39.113  23.285  1.00 50.36           C  
ANISOU 3520  CA  HIS A 707     7189   5414   6532    454    965     26       C  
ATOM   3521  C   HIS A 707     -39.723  38.437  24.646  1.00 52.34           C  
ANISOU 3521  C   HIS A 707     7399   5688   6800    347    890    -27       C  
ATOM   3522  O   HIS A 707     -39.694  37.210  24.740  1.00 53.81           O  
ANISOU 3522  O   HIS A 707     7506   5949   6991    299    772    -49       O  
ATOM   3523  CB  HIS A 707     -40.946  38.903  22.477  1.00 55.06           C  
ANISOU 3523  CB  HIS A 707     7732   6116   7073    586    943     98       C  
ATOM   3524  CG  HIS A 707     -42.191  39.393  23.159  1.00 79.55           C  
ANISOU 3524  CG  HIS A 707    10842   9244  10140    651    985    133       C  
ATOM   3525  ND1 HIS A 707     -42.256  40.599  23.816  1.00 91.01           N  
ANISOU 3525  ND1 HIS A 707    12387  10593  11599    668   1111    140       N  
ATOM   3526  CD2 HIS A 707     -43.425  38.840  23.253  1.00 85.59           C  
ANISOU 3526  CD2 HIS A 707    11533  10130  10857    703    923    163       C  
ATOM   3527  CE1 HIS A 707     -43.478  40.767  24.306  1.00 87.84           C  
ANISOU 3527  CE1 HIS A 707    11969  10247  11158    735   1122    177       C  
ATOM   3528  NE2 HIS A 707     -44.203  39.717  23.977  1.00 86.31           N  
ANISOU 3528  NE2 HIS A 707    11671  10193  10928    757   1007    191       N  
ATOM   3529  N   VAL A 708     -39.784  39.243  25.702  1.00 52.73           N  
ANISOU 3529  N   VAL A 708     7506   5670   6859    309    967    -49       N  
ATOM   3530  CA  VAL A 708     -39.758  38.729  27.071  1.00 50.68           C  
ANISOU 3530  CA  VAL A 708     7211   5429   6614    204    909   -101       C  
ATOM   3531  C   VAL A 708     -40.776  37.602  27.330  1.00 54.29           C  
ANISOU 3531  C   VAL A 708     7578   6000   7050    221    791    -85       C  
ATOM   3532  O   VAL A 708     -40.517  36.697  28.129  1.00 51.91           O  
ANISOU 3532  O   VAL A 708     7225   5735   6766    130    704   -126       O  
ATOM   3533  CB  VAL A 708     -39.935  39.870  28.105  1.00 58.42           C  
ANISOU 3533  CB  VAL A 708     8269   6329   7599    178   1022   -121       C  
ATOM   3534  CG1 VAL A 708     -41.230  40.639  27.848  1.00 53.39           C  
ANISOU 3534  CG1 VAL A 708     7669   5691   6925    314   1100    -52       C  
ATOM   3535  CG2 VAL A 708     -39.890  39.314  29.528  1.00 56.24           C  
ANISOU 3535  CG2 VAL A 708     7949   6086   7336     67    957   -175       C  
ATOM   3536  N   LYS A 709     -41.921  37.653  26.647  1.00 52.24           N  
ANISOU 3536  N   LYS A 709     7297   5803   6748    338    794    -24       N  
ATOM   3537  CA  LYS A 709     -42.924  36.588  26.740  1.00 53.52           C  
ANISOU 3537  CA  LYS A 709     7371   6084   6879    351    689    -12       C  
ATOM   3538  C   LYS A 709     -42.482  35.255  26.116  1.00 59.03           C  
ANISOU 3538  C   LYS A 709     8000   6842   7586    307    579    -32       C  
ATOM   3539  O   LYS A 709     -42.772  34.181  26.661  1.00 58.13           O  
ANISOU 3539  O   LYS A 709     7826   6788   7472    248    487    -57       O  
ATOM   3540  CB  LYS A 709     -44.246  37.029  26.114  1.00 58.60           C  
ANISOU 3540  CB  LYS A 709     8003   6801   7463    488    727     57       C  
ATOM   3541  CG  LYS A 709     -45.386  36.070  26.393  1.00 69.88           C  
ANISOU 3541  CG  LYS A 709     9343   8358   8849    490    633     63       C  
ATOM   3542  CD  LYS A 709     -45.531  35.829  27.891  1.00 82.90           C  
ANISOU 3542  CD  LYS A 709    10987   9990  10520    400    602     21       C  
ATOM   3543  CE  LYS A 709     -46.720  34.937  28.215  1.00 94.93           C  
ANISOU 3543  CE  LYS A 709    12430  11640  12000    400    518     26       C  
ATOM   3544  NZ  LYS A 709     -46.903  34.777  29.693  1.00104.78           N  
ANISOU 3544  NZ  LYS A 709    13673  12870  13267    319    493     -9       N  
ATOM   3545  N   ASN A 710     -41.803  35.322  24.969  1.00 53.47           N  
ANISOU 3545  N   ASN A 710     7309   6121   6888    338    594    -21       N  
ATOM   3546  CA  ASN A 710     -41.238  34.132  24.342  1.00 46.66           C  
ANISOU 3546  CA  ASN A 710     6392   5299   6038    294    503    -44       C  
ATOM   3547  C   ASN A 710     -40.207  33.497  25.237  1.00 34.80           C  
ANISOU 3547  C   ASN A 710     4886   3755   4583    175    453   -100       C  
ATOM   3548  O   ASN A 710     -40.174  32.284  25.418  1.00 40.13           O  
ANISOU 3548  O   ASN A 710     5507   4476   5264    124    365   -121       O  
ATOM   3549  CB  ASN A 710     -40.576  34.484  23.013  1.00 60.91           C  
ANISOU 3549  CB  ASN A 710     8220   7080   7844    346    540    -24       C  
ATOM   3550  CG  ASN A 710     -41.554  34.556  21.881  1.00 69.34           C  
ANISOU 3550  CG  ASN A 710     9254   8237   8856    459    548     31       C  
ATOM   3551  OD1 ASN A 710     -42.439  35.407  21.864  1.00 83.41           O  
ANISOU 3551  OD1 ASN A 710    11055  10037  10600    549    616     78       O  
ATOM   3552  ND2 ASN A 710     -41.405  33.660  20.921  1.00 71.88           N  
ANISOU 3552  ND2 ASN A 710     9523   8623   9167    458    484     25       N  
ATOM   3553  N   LYS A 711     -39.353  34.338  25.798  1.00 42.83           N  
ANISOU 3553  N   LYS A 711     5961   4686   5628    131    520   -123       N  
ATOM   3554  CA  LYS A 711     -38.326  33.880  26.720  1.00 47.00           C  
ANISOU 3554  CA  LYS A 711     6480   5189   6189     20    484   -174       C  
ATOM   3555  C   LYS A 711     -38.952  33.230  27.963  1.00 46.95           C  
ANISOU 3555  C   LYS A 711     6431   5227   6179    -29    426   -189       C  
ATOM   3556  O   LYS A 711     -38.469  32.203  28.453  1.00 50.30           O  
ANISOU 3556  O   LYS A 711     6814   5679   6620    -95    353   -213       O  
ATOM   3557  CB  LYS A 711     -37.413  35.051  27.082  1.00 47.72           C  
ANISOU 3557  CB  LYS A 711     6640   5194   6296    -22    581   -201       C  
ATOM   3558  CG  LYS A 711     -36.220  34.679  27.907  1.00 50.74           C  
ANISOU 3558  CG  LYS A 711     7006   5572   6701   -134    553   -253       C  
ATOM   3559  CD  LYS A 711     -35.304  35.867  28.117  1.00 58.31           C  
ANISOU 3559  CD  LYS A 711     8031   6457   7666   -185    657   -288       C  
ATOM   3560  CE  LYS A 711     -34.588  35.744  29.462  1.00 73.95           C  
ANISOU 3560  CE  LYS A 711     9990   8457   9651   -302    646   -343       C  
ATOM   3561  NZ  LYS A 711     -33.319  36.528  29.498  1.00 81.65           N  
ANISOU 3561  NZ  LYS A 711    11006   9390  10627   -379    723   -391       N  
ATOM   3562  N   GLU A 712     -40.048  33.815  28.447  1.00 49.27           N  
ANISOU 3562  N   GLU A 712     6738   5530   6451     10    462   -169       N  
ATOM   3563  CA  GLU A 712     -40.806  33.258  29.570  1.00 52.71           C  
ANISOU 3563  CA  GLU A 712     7134   6015   6880    -27    410   -179       C  
ATOM   3564  C   GLU A 712     -41.340  31.858  29.261  1.00 44.86           C  
ANISOU 3564  C   GLU A 712     6071   5100   5872    -27    309   -171       C  
ATOM   3565  O   GLU A 712     -41.122  30.909  30.021  1.00 46.28           O  
ANISOU 3565  O   GLU A 712     6216   5302   6068    -97    244   -194       O  
ATOM   3566  CB  GLU A 712     -41.976  34.178  29.936  1.00 68.51           C  
ANISOU 3566  CB  GLU A 712     9161   8019   8852     34    472   -152       C  
ATOM   3567  CG  GLU A 712     -41.642  35.292  30.922  1.00 82.61           C  
ANISOU 3567  CG  GLU A 712    11006   9729  10651     -6    560   -177       C  
ATOM   3568  CD  GLU A 712     -42.785  36.296  31.095  1.00 90.47           C  
ANISOU 3568  CD  GLU A 712    12041  10716  11617     75    639   -142       C  
ATOM   3569  OE1 GLU A 712     -43.936  35.980  30.710  1.00 92.99           O  
ANISOU 3569  OE1 GLU A 712    12323  11112  11899    153    606   -100       O  
ATOM   3570  OE2 GLU A 712     -42.526  37.407  31.613  1.00 87.92           O  
ANISOU 3570  OE2 GLU A 712    11788  10315  11304     61    740   -157       O  
ATOM   3571  N   ILE A 713     -42.037  31.737  28.136  1.00 37.51           N  
ANISOU 3571  N   ILE A 713     5123   4217   4910     50    304   -139       N  
ATOM   3572  CA  ILE A 713     -42.624  30.467  27.725  1.00 36.25           C  
ANISOU 3572  CA  ILE A 713     4903   4138   4731     44    222   -139       C  
ATOM   3573  C   ILE A 713     -41.558  29.393  27.604  1.00 41.52           C  
ANISOU 3573  C   ILE A 713     5556   4785   5434    -22    166   -168       C  
ATOM   3574  O   ILE A 713     -41.763  28.249  28.027  1.00 40.30           O  
ANISOU 3574  O   ILE A 713     5365   4663   5282    -72    103   -184       O  
ATOM   3575  CB  ILE A 713     -43.346  30.615  26.376  1.00 42.44           C  
ANISOU 3575  CB  ILE A 713     5670   4987   5469    135    236   -105       C  
ATOM   3576  CG1 ILE A 713     -44.427  31.690  26.475  1.00 51.20           C  
ANISOU 3576  CG1 ILE A 713     6792   6127   6534    219    299    -65       C  
ATOM   3577  CG2 ILE A 713     -43.922  29.285  25.919  1.00 43.57           C  
ANISOU 3577  CG2 ILE A 713     5750   5219   5587    112    160   -118       C  
ATOM   3578  CD1 ILE A 713     -45.187  31.659  27.784  1.00 55.19           C  
ANISOU 3578  CD1 ILE A 713     7285   6652   7032    186    285    -74       C  
ATOM   3579  N   CYS A 714     -40.419  29.769  27.017  1.00 35.37           N  
ANISOU 3579  N   CYS A 714     4808   3949   4680    -20    196   -173       N  
ATOM   3580  CA  CYS A 714     -39.335  28.828  26.805  1.00 29.58           C  
ANISOU 3580  CA  CYS A 714     4063   3199   3977    -69    151   -194       C  
ATOM   3581  C   CYS A 714     -38.805  28.324  28.135  1.00 30.67           C  
ANISOU 3581  C   CYS A 714     4190   3323   4139   -148    121   -217       C  
ATOM   3582  O   CYS A 714     -38.702  27.119  28.347  1.00 41.05           O  
ANISOU 3582  O   CYS A 714     5476   4659   5462   -182     64   -225       O  
ATOM   3583  CB  CYS A 714     -38.220  29.464  25.955  1.00 46.24           C  
ANISOU 3583  CB  CYS A 714     6207   5258   6103    -50    195   -194       C  
ATOM   3584  SG  CYS A 714     -36.997  28.302  25.284  1.00 46.59           S  
ANISOU 3584  SG  CYS A 714     6233   5297   6173    -83    142   -211       S  
ATOM   3585  N   MET A 715     -38.466  29.237  29.037  1.00 32.70           N  
ANISOU 3585  N   MET A 715     4472   3548   4404   -175    166   -228       N  
ATOM   3586  CA  MET A 715     -38.029  28.818  30.376  1.00 33.62           C  
ANISOU 3586  CA  MET A 715     4569   3671   4534   -248    140   -248       C  
ATOM   3587  C   MET A 715     -39.056  27.896  31.025  1.00 31.92           C  
ANISOU 3587  C   MET A 715     4317   3503   4308   -261     84   -241       C  
ATOM   3588  O   MET A 715     -38.724  26.881  31.635  1.00 38.88           O  
ANISOU 3588  O   MET A 715     5171   4401   5201   -304     36   -246       O  
ATOM   3589  CB  MET A 715     -37.788  30.030  31.263  1.00 33.29           C  
ANISOU 3589  CB  MET A 715     4557   3600   4493   -280    204   -267       C  
ATOM   3590  CG  MET A 715     -36.789  31.005  30.683  1.00 50.57           C  
ANISOU 3590  CG  MET A 715     6789   5737   6688   -280    273   -280       C  
ATOM   3591  SD  MET A 715     -35.108  30.518  31.072  1.00 87.42           S  
ANISOU 3591  SD  MET A 715    11432  10417  11368   -358    251   -310       S  
ATOM   3592  CE  MET A 715     -34.981  31.133  32.756  1.00 63.90           C  
ANISOU 3592  CE  MET A 715     8445   7454   8379   -441    284   -346       C  
ATOM   3593  N   LEU A 716     -40.322  28.248  30.894  1.00 31.71           N  
ANISOU 3593  N   LEU A 716     4291   3503   4256   -219     94   -227       N  
ATOM   3594  CA  LEU A 716     -41.372  27.413  31.457  1.00 31.35           C  
ANISOU 3594  CA  LEU A 716     4209   3510   4193   -235     45   -224       C  
ATOM   3595  C   LEU A 716     -41.276  25.992  30.872  1.00 42.16           C  
ANISOU 3595  C   LEU A 716     5553   4898   5566   -250    -11   -226       C  
ATOM   3596  O   LEU A 716     -41.184  25.012  31.612  1.00 43.24           O  
ANISOU 3596  O   LEU A 716     5673   5043   5715   -298    -51   -233       O  
ATOM   3597  CB  LEU A 716     -42.740  28.045  31.190  1.00 28.89           C  
ANISOU 3597  CB  LEU A 716     3896   3240   3842   -178     68   -205       C  
ATOM   3598  CG  LEU A 716     -43.872  27.686  32.122  1.00 47.04           C  
ANISOU 3598  CG  LEU A 716     6164   5592   6117   -199     37   -205       C  
ATOM   3599  CD1 LEU A 716     -43.489  28.039  33.555  1.00 46.50           C  
ANISOU 3599  CD1 LEU A 716     6103   5495   6071   -252     47   -220       C  
ATOM   3600  CD2 LEU A 716     -45.136  28.419  31.685  1.00 47.80           C  
ANISOU 3600  CD2 LEU A 716     6256   5741   6165   -126     68   -181       C  
ATOM   3601  N   LEU A 717     -41.279  25.891  29.542  1.00 42.36           N  
ANISOU 3601  N   LEU A 717     5582   4931   5582   -208     -7   -221       N  
ATOM   3602  CA  LEU A 717     -41.173  24.600  28.860  1.00 40.38           C  
ANISOU 3602  CA  LEU A 717     5315   4693   5333   -225    -48   -230       C  
ATOM   3603  C   LEU A 717     -39.924  23.806  29.274  1.00 37.88           C  
ANISOU 3603  C   LEU A 717     5006   4330   5055   -267    -67   -237       C  
ATOM   3604  O   LEU A 717     -39.999  22.583  29.443  1.00 35.20           O  
ANISOU 3604  O   LEU A 717     4658   3995   4722   -299    -99   -242       O  
ATOM   3605  CB  LEU A 717     -41.251  24.767  27.335  1.00 29.06           C  
ANISOU 3605  CB  LEU A 717     3882   3277   3881   -173    -34   -226       C  
ATOM   3606  CG  LEU A 717     -42.563  25.315  26.776  1.00 36.13           C  
ANISOU 3606  CG  LEU A 717     4757   4246   4724   -121    -18   -213       C  
ATOM   3607  CD1 LEU A 717     -42.384  25.658  25.313  1.00 26.63           C  
ANISOU 3607  CD1 LEU A 717     3555   3060   3505    -63      5   -202       C  
ATOM   3608  CD2 LEU A 717     -43.765  24.344  26.973  1.00 30.39           C  
ANISOU 3608  CD2 LEU A 717     3991   3597   3961   -155    -56   -227       C  
ATOM   3609  N   LEU A 718     -38.786  24.486  29.434  1.00 32.56           N  
ANISOU 3609  N   LEU A 718     4349   3618   4402   -267    -42   -235       N  
ATOM   3610  CA  LEU A 718     -37.595  23.835  30.025  1.00 42.00           C  
ANISOU 3610  CA  LEU A 718     5542   4793   5624   -302    -58   -236       C  
ATOM   3611  C   LEU A 718     -37.826  23.323  31.460  1.00 35.90           C  
ANISOU 3611  C   LEU A 718     4749   4039   4852   -346    -80   -232       C  
ATOM   3612  O   LEU A 718     -37.479  22.168  31.774  1.00 32.95           O  
ANISOU 3612  O   LEU A 718     4367   3664   4489   -363   -106   -223       O  
ATOM   3613  CB  LEU A 718     -36.352  24.741  29.967  1.00 33.07           C  
ANISOU 3613  CB  LEU A 718     4424   3638   4503   -303    -23   -241       C  
ATOM   3614  CG  LEU A 718     -35.898  24.968  28.519  1.00 39.79           C  
ANISOU 3614  CG  LEU A 718     5294   4467   5357   -262     -6   -241       C  
ATOM   3615  CD1 LEU A 718     -34.828  26.023  28.419  1.00 33.36           C  
ANISOU 3615  CD1 LEU A 718     4499   3629   4548   -266     38   -251       C  
ATOM   3616  CD2 LEU A 718     -35.439  23.665  27.884  1.00 40.05           C  
ANISOU 3616  CD2 LEU A 718     5320   4497   5402   -257    -41   -237       C  
ATOM   3617  N   ASN A 719     -38.405  24.169  32.320  1.00 27.52           N  
ANISOU 3617  N   ASN A 719     3683   2994   3780   -359    -65   -236       N  
ATOM   3618  CA  ASN A 719     -38.772  23.745  33.677  1.00 35.41           C  
ANISOU 3618  CA  ASN A 719     4660   4019   4776   -399    -86   -233       C  
ATOM   3619  C   ASN A 719     -39.643  22.491  33.645  1.00 37.75           C  
ANISOU 3619  C   ASN A 719     4947   4330   5067   -407   -123   -226       C  
ATOM   3620  O   ASN A 719     -39.428  21.540  34.406  1.00 38.60           O  
ANISOU 3620  O   ASN A 719     5044   4441   5183   -434   -145   -215       O  
ATOM   3621  CB  ASN A 719     -39.508  24.864  34.426  1.00 42.74           C  
ANISOU 3621  CB  ASN A 719     5588   4963   5689   -407    -61   -242       C  
ATOM   3622  CG  ASN A 719     -38.603  26.016  34.802  1.00 46.26           C  
ANISOU 3622  CG  ASN A 719     6045   5392   6139   -424    -15   -257       C  
ATOM   3623  OD1 ASN A 719     -37.406  25.833  34.999  1.00 53.13           O  
ANISOU 3623  OD1 ASN A 719     6906   6264   7018   -449    -14   -261       O  
ATOM   3624  ND2 ASN A 719     -39.172  27.218  34.888  1.00 47.35           N  
ANISOU 3624  ND2 ASN A 719     6206   5519   6266   -411     31   -266       N  
ATOM   3625  N   ILE A 720     -40.614  22.495  32.736  1.00 33.63           N  
ANISOU 3625  N   ILE A 720     4430   3821   4526   -383   -124   -233       N  
ATOM   3626  CA  ILE A 720     -41.542  21.385  32.580  1.00 40.46           C  
ANISOU 3626  CA  ILE A 720     5287   4708   5377   -402   -150   -238       C  
ATOM   3627  C   ILE A 720     -40.831  20.119  32.094  1.00 38.91           C  
ANISOU 3627  C   ILE A 720     5107   4477   5202   -413   -159   -237       C  
ATOM   3628  O   ILE A 720     -41.196  18.992  32.456  1.00 38.87           O  
ANISOU 3628  O   ILE A 720     5105   4468   5196   -446   -172   -238       O  
ATOM   3629  CB  ILE A 720     -42.699  21.770  31.620  1.00 33.84           C  
ANISOU 3629  CB  ILE A 720     4440   3916   4501   -374   -145   -249       C  
ATOM   3630  CG1 ILE A 720     -43.593  22.828  32.266  1.00 29.92           C  
ANISOU 3630  CG1 ILE A 720     3930   3459   3979   -359   -133   -243       C  
ATOM   3631  CG2 ILE A 720     -43.510  20.544  31.211  1.00 28.43           C  
ANISOU 3631  CG2 ILE A 720     3747   3262   3795   -406   -165   -266       C  
ATOM   3632  CD1 ILE A 720     -44.692  23.382  31.307  1.00 31.71           C  
ANISOU 3632  CD1 ILE A 720     4142   3748   4157   -311   -119   -242       C  
ATOM   3633  N   SER A 721     -39.799  20.298  31.285  1.00 39.27           N  
ANISOU 3633  N   SER A 721     5165   4491   5263   -385   -146   -235       N  
ATOM   3634  CA  SER A 721     -39.072  19.139  30.798  1.00 41.26           C  
ANISOU 3634  CA  SER A 721     5436   4707   5535   -387   -148   -231       C  
ATOM   3635  C   SER A 721     -38.232  18.549  31.933  1.00 35.01           C  
ANISOU 3635  C   SER A 721     4643   3898   4762   -401   -152   -206       C  
ATOM   3636  O   SER A 721     -38.131  17.327  32.060  1.00 35.54           O  
ANISOU 3636  O   SER A 721     4727   3938   4838   -412   -151   -195       O  
ATOM   3637  CB  SER A 721     -38.269  19.459  29.516  1.00 43.80           C  
ANISOU 3637  CB  SER A 721     5770   5009   5864   -351   -135   -236       C  
ATOM   3638  OG  SER A 721     -37.050  20.115  29.794  1.00 53.79           O  
ANISOU 3638  OG  SER A 721     7033   6259   7145   -335   -124   -223       O  
ATOM   3639  N   SER A 722     -37.674  19.422  32.780  1.00 35.38           N  
ANISOU 3639  N   SER A 722     4670   3963   4810   -401   -149   -195       N  
ATOM   3640  CA  SER A 722     -37.026  19.006  34.042  1.00 37.28           C  
ANISOU 3640  CA  SER A 722     4893   4217   5054   -416   -154   -169       C  
ATOM   3641  C   SER A 722     -38.007  18.255  34.954  1.00 40.29           C  
ANISOU 3641  C   SER A 722     5271   4609   5430   -445   -168   -161       C  
ATOM   3642  O   SER A 722     -37.692  17.187  35.487  1.00 45.38           O  
ANISOU 3642  O   SER A 722     5921   5241   6082   -446   -167   -134       O  
ATOM   3643  CB  SER A 722     -36.462  20.206  34.810  1.00 33.33           C  
ANISOU 3643  CB  SER A 722     4366   3754   4546   -427   -145   -173       C  
ATOM   3644  OG  SER A 722     -35.655  21.040  33.996  1.00 42.05           O  
ANISOU 3644  OG  SER A 722     5478   4849   5653   -409   -125   -187       O  
ATOM   3645  N   ILE A 723     -39.195  18.826  35.140  1.00 35.00           N  
ANISOU 3645  N   ILE A 723     4592   3962   4744   -465   -176   -181       N  
ATOM   3646  CA  ILE A 723     -40.239  18.177  35.930  1.00 34.89           C  
ANISOU 3646  CA  ILE A 723     4573   3963   4719   -498   -190   -179       C  
ATOM   3647  C   ILE A 723     -40.540  16.775  35.419  1.00 40.42           C  
ANISOU 3647  C   ILE A 723     5305   4628   5425   -510   -185   -180       C  
ATOM   3648  O   ILE A 723     -40.711  15.838  36.209  1.00 41.59           O  
ANISOU 3648  O   ILE A 723     5461   4765   5576   -531   -183   -161       O  
ATOM   3649  CB  ILE A 723     -41.529  19.008  35.938  1.00 43.29           C  
ANISOU 3649  CB  ILE A 723     5623   5066   5758   -510   -197   -203       C  
ATOM   3650  CG1 ILE A 723     -41.385  20.182  36.911  1.00 45.36           C  
ANISOU 3650  CG1 ILE A 723     5861   5356   6016   -513   -193   -201       C  
ATOM   3651  CG2 ILE A 723     -42.719  18.149  36.334  1.00 40.58           C  
ANISOU 3651  CG2 ILE A 723     5280   4742   5399   -547   -211   -210       C  
ATOM   3652  CD1 ILE A 723     -42.627  21.013  37.015  1.00 45.82           C  
ANISOU 3652  CD1 ILE A 723     5909   5450   6048   -513   -193   -217       C  
ATOM   3653  N   ARG A 724     -40.587  16.640  34.092  1.00 37.20           N  
ANISOU 3653  N   ARG A 724     4917   4201   5017   -497   -176   -201       N  
ATOM   3654  CA  ARG A 724     -40.814  15.365  33.423  1.00 30.81           C  
ANISOU 3654  CA  ARG A 724     4143   3353   4210   -516   -160   -213       C  
ATOM   3655  C   ARG A 724     -39.762  14.297  33.721  1.00 33.49           C  
ANISOU 3655  C   ARG A 724     4514   3635   4576   -500   -138   -179       C  
ATOM   3656  O   ARG A 724     -40.095  13.124  33.918  1.00 36.47           O  
ANISOU 3656  O   ARG A 724     4925   3975   4957   -526   -116   -176       O  
ATOM   3657  CB  ARG A 724     -40.873  15.596  31.917  1.00 43.82           C  
ANISOU 3657  CB  ARG A 724     5798   5002   5850   -501   -153   -244       C  
ATOM   3658  CG  ARG A 724     -42.243  15.905  31.387  1.00 34.42           C  
ANISOU 3658  CG  ARG A 724     4588   3871   4620   -527   -161   -280       C  
ATOM   3659  CD  ARG A 724     -43.065  14.640  31.304  1.00 41.04           C  
ANISOU 3659  CD  ARG A 724     5448   4705   5442   -586   -148   -308       C  
ATOM   3660  NE  ARG A 724     -43.845  14.614  30.067  1.00 45.34           N  
ANISOU 3660  NE  ARG A 724     5980   5299   5948   -605   -142   -352       N  
ATOM   3661  CZ  ARG A 724     -43.639  13.755  29.077  1.00 52.48           C  
ANISOU 3661  CZ  ARG A 724     6912   6174   6853   -626   -117   -380       C  
ATOM   3662  NH1 ARG A 724     -42.693  12.831  29.159  1.00 51.91           N  
ANISOU 3662  NH1 ARG A 724     6890   6013   6821   -625    -91   -365       N  
ATOM   3663  NH2 ARG A 724     -44.392  13.812  28.001  1.00 67.36           N  
ANISOU 3663  NH2 ARG A 724     8774   8127   8693   -647   -114   -422       N  
ATOM   3664  N   GLU A 725     -38.492  14.688  33.732  1.00 35.51           N  
ANISOU 3664  N   GLU A 725     4760   3886   4847   -456   -136   -152       N  
ATOM   3665  CA  GLU A 725     -37.422  13.726  34.013  1.00 44.78           C  
ANISOU 3665  CA  GLU A 725     5956   5020   6038   -424   -113   -110       C  
ATOM   3666  C   GLU A 725     -37.429  13.300  35.489  1.00 49.41           C  
ANISOU 3666  C   GLU A 725     6530   5623   6621   -429   -112    -69       C  
ATOM   3667  O   GLU A 725     -37.217  12.128  35.806  1.00 56.75           O  
ANISOU 3667  O   GLU A 725     7493   6510   7559   -417    -81    -36       O  
ATOM   3668  CB  GLU A 725     -36.039  14.241  33.544  1.00 44.15           C  
ANISOU 3668  CB  GLU A 725     5862   4947   5965   -376   -111    -94       C  
ATOM   3669  CG  GLU A 725     -36.077  14.784  32.100  1.00 55.24           C  
ANISOU 3669  CG  GLU A 725     7276   6340   7372   -370   -113   -133       C  
ATOM   3670  CD  GLU A 725     -34.720  15.183  31.538  1.00 54.42           C  
ANISOU 3670  CD  GLU A 725     7165   6238   7274   -326   -109   -120       C  
ATOM   3671  OE1 GLU A 725     -33.975  14.289  31.083  1.00 53.40           O  
ANISOU 3671  OE1 GLU A 725     7063   6070   7156   -295    -87   -101       O  
ATOM   3672  OE2 GLU A 725     -34.418  16.395  31.512  1.00 53.80           O  
ANISOU 3672  OE2 GLU A 725     7057   6197   7188   -323   -120   -131       O  
ATOM   3673  N   LEU A 726     -37.691  14.242  36.387  1.00 46.27           N  
ANISOU 3673  N   LEU A 726     6086   5286   6210   -446   -139    -70       N  
ATOM   3674  CA  LEU A 726     -37.952  13.896  37.786  1.00 50.54           C  
ANISOU 3674  CA  LEU A 726     6608   5854   6742   -460   -142    -39       C  
ATOM   3675  C   LEU A 726     -39.070  12.868  37.891  1.00 44.28           C  
ANISOU 3675  C   LEU A 726     5854   5021   5950   -498   -128    -47       C  
ATOM   3676  O   LEU A 726     -38.926  11.843  38.553  1.00 45.66           O  
ANISOU 3676  O   LEU A 726     6052   5168   6129   -489   -103     -7       O  
ATOM   3677  CB  LEU A 726     -38.361  15.136  38.569  1.00 43.02           C  
ANISOU 3677  CB  LEU A 726     5603   4968   5772   -486   -171    -56       C  
ATOM   3678  CG  LEU A 726     -37.239  16.156  38.681  1.00 39.91           C  
ANISOU 3678  CG  LEU A 726     5172   4620   5373   -466   -174    -52       C  
ATOM   3679  CD1 LEU A 726     -37.776  17.501  39.153  1.00 34.83           C  
ANISOU 3679  CD1 LEU A 726     4496   4023   4716   -498   -189    -85       C  
ATOM   3680  CD2 LEU A 726     -36.166  15.607  39.607  1.00 32.86           C  
ANISOU 3680  CD2 LEU A 726     4251   3763   4470   -438   -165      0       C  
ATOM   3681  N   TYR A 727     -40.179  13.149  37.216  1.00 38.74           N  
ANISOU 3681  N   TYR A 727     5160   4320   5238   -538   -139    -98       N  
ATOM   3682  CA  TYR A 727     -41.362  12.311  37.319  1.00 39.22           C  
ANISOU 3682  CA  TYR A 727     5250   4363   5290   -591   -127   -119       C  
ATOM   3683  C   TYR A 727     -41.101  10.893  36.853  1.00 47.00           C  
ANISOU 3683  C   TYR A 727     6300   5267   6290   -592    -77   -111       C  
ATOM   3684  O   TYR A 727     -41.601   9.927  37.437  1.00 57.47           O  
ANISOU 3684  O   TYR A 727     7660   6561   7616   -624    -49   -100       O  
ATOM   3685  CB  TYR A 727     -42.514  12.891  36.502  1.00 40.11           C  
ANISOU 3685  CB  TYR A 727     5349   4512   5377   -629   -146   -177       C  
ATOM   3686  CG  TYR A 727     -43.741  12.013  36.564  1.00 47.64           C  
ANISOU 3686  CG  TYR A 727     6326   5464   6310   -695   -131   -208       C  
ATOM   3687  CD1 TYR A 727     -44.510  11.953  37.725  1.00 43.39           C  
ANISOU 3687  CD1 TYR A 727     5770   4958   5757   -729   -144   -199       C  
ATOM   3688  CD2 TYR A 727     -44.123  11.229  35.477  1.00 44.17           C  
ANISOU 3688  CD2 TYR A 727     5926   4994   5862   -730   -100   -249       C  
ATOM   3689  CE1 TYR A 727     -45.622  11.153  37.803  1.00 49.98           C  
ANISOU 3689  CE1 TYR A 727     6625   5795   6569   -797   -128   -230       C  
ATOM   3690  CE2 TYR A 727     -45.242  10.415  35.545  1.00 45.52           C  
ANISOU 3690  CE2 TYR A 727     6117   5170   6006   -805    -80   -285       C  
ATOM   3691  CZ  TYR A 727     -45.992  10.385  36.714  1.00 48.08           C  
ANISOU 3691  CZ  TYR A 727     6425   5528   6317   -839    -94   -275       C  
ATOM   3692  OH  TYR A 727     -47.110   9.580  36.809  1.00 48.23           O  
ANISOU 3692  OH  TYR A 727     6464   5556   6306   -921    -72   -315       O  
ATOM   3693  N   PHE A 728     -40.345  10.774  35.772  1.00 45.26           N  
ANISOU 3693  N   PHE A 728     6103   5010   6084   -560    -60   -117       N  
ATOM   3694  CA  PHE A 728     -40.021   9.471  35.218  1.00 47.83           C  
ANISOU 3694  CA  PHE A 728     6498   5251   6426   -558     -3   -112       C  
ATOM   3695  C   PHE A 728     -39.152   8.661  36.192  1.00 45.28           C  
ANISOU 3695  C   PHE A 728     6200   4888   6118   -508     32    -38       C  
ATOM   3696  O   PHE A 728     -39.278   7.445  36.302  1.00 43.03           O  
ANISOU 3696  O   PHE A 728     5979   4529   5842   -517     90    -24       O  
ATOM   3697  CB  PHE A 728     -39.306   9.635  33.872  1.00 47.88           C  
ANISOU 3697  CB  PHE A 728     6517   5234   6442   -527      4   -131       C  
ATOM   3698  CG  PHE A 728     -38.721   8.365  33.358  1.00 48.53           C  
ANISOU 3698  CG  PHE A 728     6671   5225   6544   -510     68   -118       C  
ATOM   3699  CD1 PHE A 728     -39.505   7.464  32.653  1.00 56.20           C  
ANISOU 3699  CD1 PHE A 728     7698   6144   7510   -573    113   -169       C  
ATOM   3700  CD2 PHE A 728     -37.401   8.048  33.609  1.00 46.61           C  
ANISOU 3700  CD2 PHE A 728     6440   4953   6318   -432     90    -55       C  
ATOM   3701  CE1 PHE A 728     -38.977   6.280  32.189  1.00 50.14           C  
ANISOU 3701  CE1 PHE A 728     7008   5281   6761   -560    185   -160       C  
ATOM   3702  CE2 PHE A 728     -36.871   6.867  33.155  1.00 52.40           C  
ANISOU 3702  CE2 PHE A 728     7245   5595   7067   -406    158    -37       C  
ATOM   3703  CZ  PHE A 728     -37.658   5.979  32.439  1.00 49.44           C  
ANISOU 3703  CZ  PHE A 728     6937   5153   6695   -470    209    -90       C  
ATOM   3704  N   ASN A 729     -38.262   9.342  36.896  1.00 42.61           N  
ANISOU 3704  N   ASN A 729     5809   4604   5779   -454      4      9       N  
ATOM   3705  CA  ASN A 729     -37.398   8.655  37.839  1.00 50.41           C  
ANISOU 3705  CA  ASN A 729     6803   5581   6768   -395     35     85       C  
ATOM   3706  C   ASN A 729     -38.047   8.513  39.203  1.00 53.71           C  
ANISOU 3706  C   ASN A 729     7201   6032   7174   -420     28    111       C  
ATOM   3707  O   ASN A 729     -37.411   8.077  40.159  1.00 51.19           O  
ANISOU 3707  O   ASN A 729     6872   5730   6849   -369     48    181       O  
ATOM   3708  CB  ASN A 729     -36.042   9.350  37.939  1.00 52.42           C  
ANISOU 3708  CB  ASN A 729     7004   5897   7016   -328     15    123       C  
ATOM   3709  CG  ASN A 729     -35.207   9.155  36.693  1.00 55.67           C  
ANISOU 3709  CG  ASN A 729     7446   6264   7441   -288     36    117       C  
ATOM   3710  OD1 ASN A 729     -34.866   8.026  36.333  1.00 58.78           O  
ANISOU 3710  OD1 ASN A 729     7905   6582   7848   -255     93    144       O  
ATOM   3711  ND2 ASN A 729     -34.879  10.254  36.021  1.00 50.72           N  
ANISOU 3711  ND2 ASN A 729     6780   5681   6811   -291     -3     81       N  
ATOM   3712  N   LYS A 730     -39.320   8.883  39.278  1.00 55.83           N  
ANISOU 3712  N   LYS A 730     7460   6319   7434   -493      0     58       N  
ATOM   3713  CA  LYS A 730     -40.132   8.626  40.461  1.00 53.97           C  
ANISOU 3713  CA  LYS A 730     7215   6105   7186   -529     -3     73       C  
ATOM   3714  C   LYS A 730     -39.718   9.469  41.655  1.00 51.55           C  
ANISOU 3714  C   LYS A 730     6830   5891   6864   -504    -44    110       C  
ATOM   3715  O   LYS A 730     -39.863   9.041  42.802  1.00 45.62           O  
ANISOU 3715  O   LYS A 730     6069   5159   6104   -501    -35    153       O  
ATOM   3716  CB  LYS A 730     -40.091   7.142  40.832  1.00 56.95           C  
ANISOU 3716  CB  LYS A 730     7665   6400   7573   -517     68    118       C  
ATOM   3717  CG  LYS A 730     -40.640   6.223  39.759  1.00 60.77           C  
ANISOU 3717  CG  LYS A 730     8233   6788   8069   -563    123     70       C  
ATOM   3718  CD  LYS A 730     -40.126   4.798  39.922  1.00 67.10           C  
ANISOU 3718  CD  LYS A 730     9120   7487   8886   -523    213    126       C  
ATOM   3719  CE  LYS A 730     -41.036   3.806  39.204  1.00 75.72           C  
ANISOU 3719  CE  LYS A 730    10303   8485   9983   -604    278     66       C  
ATOM   3720  NZ  LYS A 730     -41.670   4.382  37.968  1.00 76.31           N  
ANISOU 3720  NZ  LYS A 730    10361   8587  10047   -672    243    -27       N  
ATOM   3721  N   GLN A 731     -39.209  10.667  41.384  1.00 45.57           N  
ANISOU 3721  N   GLN A 731     6019   5193   6101   -490    -85     90       N  
ATOM   3722  CA  GLN A 731     -38.895  11.618  42.448  1.00 41.38           C  
ANISOU 3722  CA  GLN A 731     5414   4758   5552   -486   -120    107       C  
ATOM   3723  C   GLN A 731     -40.112  12.501  42.796  1.00 46.06           C  
ANISOU 3723  C   GLN A 731     5976   5391   6132   -548   -159     56       C  
ATOM   3724  O   GLN A 731     -40.130  13.713  42.532  1.00 45.65           O  
ANISOU 3724  O   GLN A 731     5890   5380   6074   -559   -187     19       O  
ATOM   3725  CB  GLN A 731     -37.669  12.451  42.073  1.00 33.33           C  
ANISOU 3725  CB  GLN A 731     4355   3781   4527   -446   -131    110       C  
ATOM   3726  CG  GLN A 731     -36.377  11.656  42.135  1.00 47.86           C  
ANISOU 3726  CG  GLN A 731     6201   5619   6365   -375    -96    175       C  
ATOM   3727  CD  GLN A 731     -35.147  12.505  41.821  1.00 78.64           C  
ANISOU 3727  CD  GLN A 731    10052   9578  10249   -344   -108    174       C  
ATOM   3728  OE1 GLN A 731     -35.214  13.459  41.042  1.00 81.05           O  
ANISOU 3728  OE1 GLN A 731    10353   9882  10562   -370   -128    120       O  
ATOM   3729  NE2 GLN A 731     -34.015  12.154  42.428  1.00 92.05           N  
ANISOU 3729  NE2 GLN A 731    11714  11337  11923   -288    -91    236       N  
ATOM   3730  N   TRP A 732     -41.112  11.874  43.413  1.00 38.75           N  
ANISOU 3730  N   TRP A 732     5066   4455   5202   -586   -155     59       N  
ATOM   3731  CA  TRP A 732     -42.439  12.468  43.602  1.00 42.73           C  
ANISOU 3731  CA  TRP A 732     5553   4991   5691   -645   -186     10       C  
ATOM   3732  C   TRP A 732     -42.442  13.831  44.271  1.00 44.51           C  
ANISOU 3732  C   TRP A 732     5713   5298   5902   -652   -223     -4       C  
ATOM   3733  O   TRP A 732     -43.140  14.752  43.832  1.00 44.46           O  
ANISOU 3733  O   TRP A 732     5695   5311   5886   -674   -243    -50       O  
ATOM   3734  CB  TRP A 732     -43.307  11.525  44.418  1.00 42.58           C  
ANISOU 3734  CB  TRP A 732     5554   4960   5665   -682   -174     26       C  
ATOM   3735  CG  TRP A 732     -43.152  10.086  44.033  1.00 55.57           C  
ANISOU 3735  CG  TRP A 732     7272   6517   7325   -675   -119     50       C  
ATOM   3736  CD1 TRP A 732     -42.707   9.063  44.829  1.00 56.26           C  
ANISOU 3736  CD1 TRP A 732     7384   6573   7418   -645    -79    114       C  
ATOM   3737  CD2 TRP A 732     -43.449   9.502  42.759  1.00 59.01           C  
ANISOU 3737  CD2 TRP A 732     7769   6883   7770   -697    -88      9       C  
ATOM   3738  NE1 TRP A 732     -42.719   7.880  44.128  1.00 57.21           N  
ANISOU 3738  NE1 TRP A 732     7587   6595   7553   -647    -18    116       N  
ATOM   3739  CE2 TRP A 732     -43.169   8.123  42.855  1.00 60.61           C  
ANISOU 3739  CE2 TRP A 732     8041   7003   7987   -685    -24     47       C  
ATOM   3740  CE3 TRP A 732     -43.929  10.010  41.547  1.00 55.98           C  
ANISOU 3740  CE3 TRP A 732     7388   6502   7380   -724   -103    -54       C  
ATOM   3741  CZ2 TRP A 732     -43.350   7.249  41.783  1.00 55.66           C  
ANISOU 3741  CZ2 TRP A 732     7487   6290   7369   -710     27     15       C  
ATOM   3742  CZ3 TRP A 732     -44.109   9.137  40.486  1.00 53.53           C  
ANISOU 3742  CZ3 TRP A 732     7140   6123   7074   -748    -60    -84       C  
ATOM   3743  CH2 TRP A 732     -43.816   7.776  40.610  1.00 49.81           C  
ANISOU 3743  CH2 TRP A 732     6741   5565   6620   -746      5    -54       C  
ATOM   3744  N   GLN A 733     -41.659  13.962  45.338  1.00 36.06           N  
ANISOU 3744  N   GLN A 733     4598   4278   4823   -632   -226     38       N  
ATOM   3745  CA  GLN A 733     -41.696  15.179  46.132  1.00 29.04           C  
ANISOU 3745  CA  GLN A 733     3649   3467   3917   -652   -252     19       C  
ATOM   3746  C   GLN A 733     -40.980  16.325  45.426  1.00 35.27           C  
ANISOU 3746  C   GLN A 733     4425   4267   4708   -639   -251    -12       C  
ATOM   3747  O   GLN A 733     -41.482  17.446  45.383  1.00 40.67           O  
ANISOU 3747  O   GLN A 733     5095   4973   5386   -662   -262    -53       O  
ATOM   3748  CB  GLN A 733     -41.112  14.929  47.530  1.00 31.73           C  
ANISOU 3748  CB  GLN A 733     3939   3876   4240   -643   -251     69       C  
ATOM   3749  CG  GLN A 733     -40.888  16.211  48.352  1.00 52.55           C  
ANISOU 3749  CG  GLN A 733     6510   6602   6855   -670   -269     45       C  
ATOM   3750  CD  GLN A 733     -42.174  16.751  48.980  1.00 67.87           C  
ANISOU 3750  CD  GLN A 733     8436   8565   8786   -719   -291     11       C  
ATOM   3751  OE1 GLN A 733     -42.873  16.033  49.694  1.00 72.84           O  
ANISOU 3751  OE1 GLN A 733     9065   9201   9411   -734   -299     34       O  
ATOM   3752  NE2 GLN A 733     -42.485  18.022  48.718  1.00 69.75           N  
ANISOU 3752  NE2 GLN A 733     8666   8814   9021   -741   -296    -40       N  
ATOM   3753  N   GLU A 734     -39.800  16.051  44.874  1.00 37.97           N  
ANISOU 3753  N   GLU A 734     4775   4593   5058   -598   -233     11       N  
ATOM   3754  CA  GLU A 734     -39.062  17.088  44.165  1.00 30.07           C  
ANISOU 3754  CA  GLU A 734     3766   3601   4059   -589   -228    -19       C  
ATOM   3755  C   GLU A 734     -39.870  17.519  42.928  1.00 35.72           C  
ANISOU 3755  C   GLU A 734     4525   4260   4788   -594   -230    -64       C  
ATOM   3756  O   GLU A 734     -39.929  18.714  42.589  1.00 30.85           O  
ANISOU 3756  O   GLU A 734     3902   3653   4168   -603   -227   -100       O  
ATOM   3757  CB  GLU A 734     -37.672  16.589  43.770  1.00 41.44           C  
ANISOU 3757  CB  GLU A 734     5206   5039   5500   -542   -210     16       C  
ATOM   3758  CG  GLU A 734     -36.727  17.690  43.273  1.00 50.33           C  
ANISOU 3758  CG  GLU A 734     6311   6193   6618   -541   -202    -13       C  
ATOM   3759  CD  GLU A 734     -36.512  18.772  44.309  1.00 55.86           C  
ANISOU 3759  CD  GLU A 734     6954   6980   7292   -583   -203    -35       C  
ATOM   3760  OE1 GLU A 734     -36.401  18.438  45.511  1.00 72.65           O  
ANISOU 3760  OE1 GLU A 734     9033   9174   9395   -592   -210     -5       O  
ATOM   3761  OE2 GLU A 734     -36.460  19.958  43.929  1.00 49.79           O  
ANISOU 3761  OE2 GLU A 734     6186   6209   6521   -608   -192    -82       O  
ATOM   3762  N   THR A 735     -40.501  16.547  42.264  1.00 27.84           N  
ANISOU 3762  N   THR A 735     3571   3207   3802   -591   -227    -62       N  
ATOM   3763  CA  THR A 735     -41.414  16.876  41.169  1.00 40.26           C  
ANISOU 3763  CA  THR A 735     5172   4751   5375   -599   -231   -104       C  
ATOM   3764  C   THR A 735     -42.447  17.889  41.696  1.00 45.10           C  
ANISOU 3764  C   THR A 735     5759   5410   5969   -627   -246   -131       C  
ATOM   3765  O   THR A 735     -42.603  18.967  41.119  1.00 39.38           O  
ANISOU 3765  O   THR A 735     5034   4692   5239   -616   -241   -158       O  
ATOM   3766  CB  THR A 735     -42.124  15.625  40.564  1.00 34.37           C  
ANISOU 3766  CB  THR A 735     4469   3957   4632   -613   -222   -107       C  
ATOM   3767  OG1 THR A 735     -41.160  14.617  40.222  1.00 35.24           O  
ANISOU 3767  OG1 THR A 735     4612   4017   4762   -584   -197    -76       O  
ATOM   3768  CG2 THR A 735     -42.924  16.002  39.336  1.00 31.66           C  
ANISOU 3768  CG2 THR A 735     4142   3609   4279   -619   -224   -151       C  
ATOM   3769  N   LEU A 736     -43.106  17.572  42.816  1.00 37.09           N  
ANISOU 3769  N   LEU A 736     4724   4426   4942   -657   -260   -121       N  
ATOM   3770  CA  LEU A 736     -44.134  18.468  43.365  1.00 36.62           C  
ANISOU 3770  CA  LEU A 736     4640   4412   4862   -681   -274   -145       C  
ATOM   3771  C   LEU A 736     -43.654  19.893  43.634  1.00 38.13           C  
ANISOU 3771  C   LEU A 736     4809   4629   5050   -674   -262   -161       C  
ATOM   3772  O   LEU A 736     -44.307  20.845  43.217  1.00 47.07           O  
ANISOU 3772  O   LEU A 736     5947   5767   6171   -666   -254   -187       O  
ATOM   3773  CB  LEU A 736     -44.816  17.875  44.604  1.00 37.44           C  
ANISOU 3773  CB  LEU A 736     4722   4549   4954   -716   -291   -129       C  
ATOM   3774  CG  LEU A 736     -45.727  16.696  44.263  1.00 43.15           C  
ANISOU 3774  CG  LEU A 736     5476   5248   5671   -739   -293   -131       C  
ATOM   3775  CD1 LEU A 736     -46.338  16.125  45.512  1.00 41.82           C  
ANISOU 3775  CD1 LEU A 736     5290   5110   5492   -775   -306   -113       C  
ATOM   3776  CD2 LEU A 736     -46.801  17.101  43.232  1.00 43.47           C  
ANISOU 3776  CD2 LEU A 736     5527   5301   5690   -744   -297   -172       C  
ATOM   3777  N   SER A 737     -42.526  20.055  44.324  1.00 31.67           N  
ANISOU 3777  N   SER A 737     3966   3832   4237   -677   -254   -146       N  
ATOM   3778  CA  SER A 737     -42.070  21.412  44.630  1.00 38.80           C  
ANISOU 3778  CA  SER A 737     4851   4760   5133   -688   -233   -172       C  
ATOM   3779  C   SER A 737     -41.648  22.175  43.375  1.00 41.16           C  
ANISOU 3779  C   SER A 737     5182   5016   5441   -659   -206   -193       C  
ATOM   3780  O   SER A 737     -41.840  23.392  43.301  1.00 49.76           O  
ANISOU 3780  O   SER A 737     6279   6103   6523   -662   -178   -221       O  
ATOM   3781  CB  SER A 737     -40.994  21.453  45.742  1.00 45.43           C  
ANISOU 3781  CB  SER A 737     5642   5657   5961   -711   -228   -158       C  
ATOM   3782  OG  SER A 737     -39.789  20.817  45.366  1.00 52.31           O  
ANISOU 3782  OG  SER A 737     6511   6525   6839   -686   -223   -132       O  
ATOM   3783  N   GLN A 738     -41.086  21.465  42.394  1.00 40.47           N  
ANISOU 3783  N   GLN A 738     5117   4890   5368   -630   -208   -179       N  
ATOM   3784  CA  GLN A 738     -40.810  22.051  41.066  1.00 41.96           C  
ANISOU 3784  CA  GLN A 738     5339   5037   5566   -598   -186   -196       C  
ATOM   3785  C   GLN A 738     -42.112  22.396  40.348  1.00 35.58           C  
ANISOU 3785  C   GLN A 738     4553   4217   4748   -580   -186   -211       C  
ATOM   3786  O   GLN A 738     -42.246  23.462  39.745  1.00 34.65           O  
ANISOU 3786  O   GLN A 738     4454   4087   4626   -557   -157   -228       O  
ATOM   3787  CB  GLN A 738     -40.036  21.073  40.193  1.00 38.39           C  
ANISOU 3787  CB  GLN A 738     4904   4552   5130   -571   -191   -177       C  
ATOM   3788  CG  GLN A 738     -38.686  20.701  40.720  1.00 45.06           C  
ANISOU 3788  CG  GLN A 738     5726   5420   5977   -572   -188   -154       C  
ATOM   3789  CD  GLN A 738     -37.639  21.665  40.262  1.00 62.84           C  
ANISOU 3789  CD  GLN A 738     7976   7674   8226   -568   -161   -173       C  
ATOM   3790  OE1 GLN A 738     -36.922  21.406  39.279  1.00 72.58           O  
ANISOU 3790  OE1 GLN A 738     9228   8877   9470   -539   -154   -168       O  
ATOM   3791  NE2 GLN A 738     -37.557  22.811  40.940  1.00 56.51           N  
ANISOU 3791  NE2 GLN A 738     7156   6906   7411   -603   -139   -200       N  
ATOM   3792  N   MET A 739     -43.070  21.479  40.408  1.00 32.51           N  
ANISOU 3792  N   MET A 739     4163   3838   4351   -589   -213   -204       N  
ATOM   3793  CA  MET A 739     -44.394  21.743  39.855  1.00 33.41           C  
ANISOU 3793  CA  MET A 739     4283   3970   4442   -576   -216   -218       C  
ATOM   3794  C   MET A 739     -45.011  22.998  40.463  1.00 38.90           C  
ANISOU 3794  C   MET A 739     4967   4694   5119   -572   -198   -229       C  
ATOM   3795  O   MET A 739     -45.578  23.821  39.758  1.00 46.58           O  
ANISOU 3795  O   MET A 739     5953   5672   6075   -535   -176   -236       O  
ATOM   3796  CB  MET A 739     -45.312  20.551  40.052  1.00 30.96           C  
ANISOU 3796  CB  MET A 739     3966   3679   4118   -605   -244   -215       C  
ATOM   3797  CG  MET A 739     -46.611  20.668  39.289  1.00 44.74           C  
ANISOU 3797  CG  MET A 739     5710   5463   5827   -596   -247   -233       C  
ATOM   3798  SD  MET A 739     -46.424  20.366  37.531  1.00 48.69           S  
ANISOU 3798  SD  MET A 739     6232   5943   6324   -565   -235   -244       S  
ATOM   3799  CE  MET A 739     -46.296  18.575  37.505  1.00 44.67           C  
ANISOU 3799  CE  MET A 739     5743   5403   5829   -615   -247   -247       C  
ATOM   3800  N   GLU A 740     -44.852  23.165  41.770  1.00 42.96           N  
ANISOU 3800  N   GLU A 740     5458   5229   5634   -607   -202   -228       N  
ATOM   3801  CA  GLU A 740     -45.435  24.300  42.475  1.00 41.12           C  
ANISOU 3801  CA  GLU A 740     5218   5019   5385   -611   -181   -241       C  
ATOM   3802  C   GLU A 740     -44.810  25.650  42.087  1.00 40.77           C  
ANISOU 3802  C   GLU A 740     5202   4942   5348   -588   -125   -257       C  
ATOM   3803  O   GLU A 740     -45.510  26.661  42.020  1.00 45.52           O  
ANISOU 3803  O   GLU A 740     5819   5543   5932   -562    -91   -265       O  
ATOM   3804  CB  GLU A 740     -45.357  24.051  43.982  1.00 40.63           C  
ANISOU 3804  CB  GLU A 740     5121   4994   5322   -661   -199   -239       C  
ATOM   3805  CG  GLU A 740     -45.917  25.148  44.856  1.00 54.12           C  
ANISOU 3805  CG  GLU A 740     6821   6728   7015   -674   -175   -257       C  
ATOM   3806  CD  GLU A 740     -46.113  24.666  46.285  1.00 75.25           C  
ANISOU 3806  CD  GLU A 740     9454   9453   9683   -724   -205   -252       C  
ATOM   3807  OE1 GLU A 740     -45.506  23.620  46.645  1.00 79.92           O  
ANISOU 3807  OE1 GLU A 740    10025  10055  10285   -744   -233   -231       O  
ATOM   3808  OE2 GLU A 740     -46.872  25.324  47.042  1.00 78.06           O  
ANISOU 3808  OE2 GLU A 740     9799   9838  10022   -736   -196   -265       O  
ATOM   3809  N   LEU A 741     -43.502  25.668  41.838  1.00 34.64           N  
ANISOU 3809  N   LEU A 741     4433   4138   4592   -597   -111   -261       N  
ATOM   3810  CA  LEU A 741     -42.819  26.883  41.378  1.00 38.16           C  
ANISOU 3810  CA  LEU A 741     4910   4545   5043   -585    -52   -280       C  
ATOM   3811  C   LEU A 741     -43.231  27.331  39.971  1.00 45.68           C  
ANISOU 3811  C   LEU A 741     5902   5463   5993   -520    -26   -273       C  
ATOM   3812  O   LEU A 741     -42.876  28.436  39.542  1.00 32.11           O  
ANISOU 3812  O   LEU A 741     4219   3705   4276   -500     34   -285       O  
ATOM   3813  CB  LEU A 741     -41.307  26.675  41.383  1.00 54.38           C  
ANISOU 3813  CB  LEU A 741     6956   6594   7112   -613    -47   -286       C  
ATOM   3814  CG  LEU A 741     -40.603  26.519  42.733  1.00 54.37           C  
ANISOU 3814  CG  LEU A 741     6911   6644   7105   -674    -54   -294       C  
ATOM   3815  CD1 LEU A 741     -39.134  26.204  42.499  1.00 42.73           C  
ANISOU 3815  CD1 LEU A 741     5421   5179   5634   -687    -52   -293       C  
ATOM   3816  CD2 LEU A 741     -40.762  27.784  43.553  1.00 38.46           C  
ANISOU 3816  CD2 LEU A 741     4900   4637   5076   -713     -3   -330       C  
ATOM   3817  N   LEU A 742     -43.959  26.473  39.252  1.00 48.41           N  
ANISOU 3817  N   LEU A 742     6239   5825   6329   -490    -65   -255       N  
ATOM   3818  CA  LEU A 742     -44.441  26.805  37.910  1.00 47.90           C  
ANISOU 3818  CA  LEU A 742     6198   5750   6250   -427    -46   -246       C  
ATOM   3819  C   LEU A 742     -45.424  27.964  37.920  1.00 51.51           C  
ANISOU 3819  C   LEU A 742     6672   6220   6681   -381     -1   -241       C  
ATOM   3820  O   LEU A 742     -45.523  28.718  36.944  1.00 49.78           O  
ANISOU 3820  O   LEU A 742     6482   5982   6451   -320     44   -230       O  
ATOM   3821  CB  LEU A 742     -45.107  25.592  37.261  1.00 40.21           C  
ANISOU 3821  CB  LEU A 742     5204   4812   5263   -420    -95   -237       C  
ATOM   3822  CG  LEU A 742     -44.298  24.881  36.178  1.00 43.68           C  
ANISOU 3822  CG  LEU A 742     5654   5222   5720   -412   -107   -236       C  
ATOM   3823  CD1 LEU A 742     -42.803  24.882  36.497  1.00 44.99           C  
ANISOU 3823  CD1 LEU A 742     5829   5343   5921   -438    -97   -239       C  
ATOM   3824  CD2 LEU A 742     -44.831  23.475  35.967  1.00 36.12           C  
ANISOU 3824  CD2 LEU A 742     4678   4292   4754   -437   -152   -237       C  
ATOM   3825  N   ASP A 743     -46.146  28.087  39.034  1.00 47.96           N  
ANISOU 3825  N   ASP A 743     6203   5802   6216   -405     -9   -245       N  
ATOM   3826  CA  ASP A 743     -47.224  29.054  39.189  1.00 44.62           C  
ANISOU 3826  CA  ASP A 743     5792   5401   5762   -359     31   -236       C  
ATOM   3827  C   ASP A 743     -48.307  28.898  38.118  1.00 48.41           C  
ANISOU 3827  C   ASP A 743     6259   5935   6200   -289     22   -211       C  
ATOM   3828  O   ASP A 743     -48.789  29.876  37.545  1.00 50.75           O  
ANISOU 3828  O   ASP A 743     6579   6233   6471   -213     77   -192       O  
ATOM   3829  CB  ASP A 743     -46.691  30.481  39.205  1.00 48.87           C  
ANISOU 3829  CB  ASP A 743     6381   5875   6311   -337    118   -244       C  
ATOM   3830  CG  ASP A 743     -47.656  31.442  39.887  1.00 71.60           C  
ANISOU 3830  CG  ASP A 743     9275   8766   9165   -308    166   -239       C  
ATOM   3831  OD1 ASP A 743     -48.326  31.020  40.861  1.00 66.69           O  
ANISOU 3831  OD1 ASP A 743     8616   8194   8529   -343    125   -244       O  
ATOM   3832  OD2 ASP A 743     -47.760  32.609  39.448  1.00 82.07           O  
ANISOU 3832  OD2 ASP A 743    10652  10049  10482   -248    249   -229       O  
ATOM   3833  N   LEU A 744     -48.697  27.655  37.869  1.00 41.07           N  
ANISOU 3833  N   LEU A 744     5291   5056   5257   -315    -42   -213       N  
ATOM   3834  CA  LEU A 744     -49.653  27.351  36.823  1.00 34.89           C  
ANISOU 3834  CA  LEU A 744     4485   4344   4427   -266    -55   -199       C  
ATOM   3835  C   LEU A 744     -50.862  26.656  37.425  1.00 46.53           C  
ANISOU 3835  C   LEU A 744     5914   5906   5860   -298   -100   -204       C  
ATOM   3836  O   LEU A 744     -51.998  26.998  37.112  1.00 58.71           O  
ANISOU 3836  O   LEU A 744     7432   7530   7345   -248    -92   -189       O  
ATOM   3837  CB  LEU A 744     -49.024  26.422  35.788  1.00 32.76           C  
ANISOU 3837  CB  LEU A 744     4214   4061   4172   -281    -82   -207       C  
ATOM   3838  CG  LEU A 744     -48.183  27.047  34.682  1.00 49.12           C  
ANISOU 3838  CG  LEU A 744     6320   6082   6261   -229    -40   -197       C  
ATOM   3839  CD1 LEU A 744     -47.765  25.965  33.683  1.00 47.37           C  
ANISOU 3839  CD1 LEU A 744     6089   5864   6047   -248    -74   -208       C  
ATOM   3840  CD2 LEU A 744     -48.940  28.180  33.996  1.00 42.07           C  
ANISOU 3840  CD2 LEU A 744     5435   5227   5324   -134     14   -168       C  
ATOM   3841  N   LEU A 745     -50.603  25.666  38.279  1.00 34.38           N  
ANISOU 3841  N   LEU A 745     4362   4354   4347   -378   -145   -222       N  
ATOM   3842  CA  LEU A 745     -51.651  24.897  38.921  1.00 34.63           C  
ANISOU 3842  CA  LEU A 745     4355   4459   4345   -422   -187   -230       C  
ATOM   3843  C   LEU A 745     -52.011  25.472  40.282  1.00 39.54           C  
ANISOU 3843  C   LEU A 745     4969   5087   4966   -436   -183   -228       C  
ATOM   3844  O   LEU A 745     -51.204  26.158  40.917  1.00 43.29           O  
ANISOU 3844  O   LEU A 745     5470   5500   5480   -440   -155   -228       O  
ATOM   3845  CB  LEU A 745     -51.241  23.432  39.063  1.00 26.45           C  
ANISOU 3845  CB  LEU A 745     3315   3402   3333   -497   -230   -247       C  
ATOM   3846  CG  LEU A 745     -50.925  22.644  37.796  1.00 29.09           C  
ANISOU 3846  CG  LEU A 745     3657   3727   3667   -499   -235   -257       C  
ATOM   3847  CD1 LEU A 745     -50.825  21.162  38.104  1.00 32.00           C  
ANISOU 3847  CD1 LEU A 745     4026   4080   4050   -576   -265   -273       C  
ATOM   3848  CD2 LEU A 745     -51.966  22.883  36.739  1.00 28.65           C  
ANISOU 3848  CD2 LEU A 745     3574   3764   3546   -457   -227   -259       C  
ATOM   3849  N   PRO A 746     -53.230  25.190  40.731  1.00 39.91           N  
ANISOU 3849  N   PRO A 746     4979   5218   4966   -449   -208   -230       N  
ATOM   3850  CA  PRO A 746     -53.690  25.643  42.048  1.00 42.79           C  
ANISOU 3850  CA  PRO A 746     5332   5601   5326   -466   -209   -229       C  
ATOM   3851  C   PRO A 746     -53.098  24.802  43.174  1.00 47.36           C  
ANISOU 3851  C   PRO A 746     5905   6144   5946   -550   -245   -241       C  
ATOM   3852  O   PRO A 746     -53.733  23.852  43.632  1.00 47.07           O  
ANISOU 3852  O   PRO A 746     5840   6153   5890   -601   -285   -248       O  
ATOM   3853  CB  PRO A 746     -55.203  25.434  41.975  1.00 50.84           C  
ANISOU 3853  CB  PRO A 746     6307   6737   6273   -455   -230   -227       C  
ATOM   3854  CG  PRO A 746     -55.377  24.320  41.006  1.00 48.14           C  
ANISOU 3854  CG  PRO A 746     5949   6433   5909   -484   -260   -241       C  
ATOM   3855  CD  PRO A 746     -54.289  24.490  39.984  1.00 48.15           C  
ANISOU 3855  CD  PRO A 746     5986   6359   5949   -451   -234   -236       C  
ATOM   3856  N   PHE A 747     -51.893  25.152  43.611  1.00 52.82           N  
ANISOU 3856  N   PHE A 747     6621   6761   6689   -563   -225   -242       N  
ATOM   3857  CA  PHE A 747     -51.480  24.918  44.989  1.00 49.58           C  
ANISOU 3857  CA  PHE A 747     6195   6340   6302   -622   -242   -247       C  
ATOM   3858  C   PHE A 747     -51.987  26.020  45.912  1.00 43.63           C  
ANISOU 3858  C   PHE A 747     5436   5609   5533   -613   -215   -253       C  
ATOM   3859  O   PHE A 747     -51.510  26.170  47.037  1.00 49.11           O  
ANISOU 3859  O   PHE A 747     6118   6294   6246   -657   -214   -261       O  
ATOM   3860  CB  PHE A 747     -49.956  24.815  45.081  1.00 46.64           C  
ANISOU 3860  CB  PHE A 747     5840   5903   5978   -644   -230   -248       C  
ATOM   3861  CG  PHE A 747     -49.373  23.699  44.262  1.00 43.59           C  
ANISOU 3861  CG  PHE A 747     5464   5488   5610   -650   -252   -240       C  
ATOM   3862  CD1 PHE A 747     -49.542  23.669  42.888  1.00 43.55           C  
ANISOU 3862  CD1 PHE A 747     5479   5475   5595   -609   -242   -241       C  
ATOM   3863  CD2 PHE A 747     -48.657  22.679  44.867  1.00 41.41           C  
ANISOU 3863  CD2 PHE A 747     5178   5198   5358   -694   -276   -230       C  
ATOM   3864  CE1 PHE A 747     -49.007  22.643  42.132  1.00 34.44           C  
ANISOU 3864  CE1 PHE A 747     4336   4291   4457   -619   -257   -238       C  
ATOM   3865  CE2 PHE A 747     -48.119  21.651  44.116  1.00 37.45           C  
ANISOU 3865  CE2 PHE A 747     4694   4662   4874   -694   -286   -221       C  
ATOM   3866  CZ  PHE A 747     -48.295  21.633  42.747  1.00 45.68           C  
ANISOU 3866  CZ  PHE A 747     5758   5689   5908   -661   -276   -228       C  
ATOM   3867  N   ALA A 753     -57.519  28.460  42.899  1.00 56.00           N  
ANISOU 3867  N   ALA A 753     6946   7520   6812   -270   -129   -173       N  
ATOM   3868  CA  ALA A 753     -58.021  27.579  41.852  1.00 55.51           C  
ANISOU 3868  CA  ALA A 753     6844   7544   6703   -272   -166   -175       C  
ATOM   3869  C   ALA A 753     -58.864  28.349  40.841  1.00 74.16           C  
ANISOU 3869  C   ALA A 753     9189   9998   8989   -158   -125   -140       C  
ATOM   3870  O   ALA A 753     -58.449  28.552  39.699  1.00 91.53           O  
ANISOU 3870  O   ALA A 753    11406  12184  11189   -106    -98   -126       O  
ATOM   3871  CB  ALA A 753     -58.841  26.438  42.459  1.00 42.14           C  
ANISOU 3871  CB  ALA A 753     5098   5938   4975   -356   -231   -199       C  
ATOM   3872  N   ARG A 754     -60.048  28.776  41.267  1.00 68.74           N  
ANISOU 3872  N   ARG A 754     8467   9416   8236   -114   -118   -122       N  
ATOM   3873  CA  ARG A 754     -60.991  29.438  40.374  1.00 67.20           C  
ANISOU 3873  CA  ARG A 754     8242   9340   7952      4    -80    -80       C  
ATOM   3874  C   ARG A 754     -60.319  30.571  39.605  1.00 60.15           C  
ANISOU 3874  C   ARG A 754     7409   8360   7084    110      2    -42       C  
ATOM   3875  O   ARG A 754     -60.567  30.758  38.414  1.00 54.33           O  
ANISOU 3875  O   ARG A 754     6653   7692   6295    190     25    -13       O  
ATOM   3876  CB  ARG A 754     -62.188  29.975  41.161  1.00 70.73           C  
ANISOU 3876  CB  ARG A 754     8655   9885   8334     50    -70    -59       C  
ATOM   3877  CG  ARG A 754     -63.300  28.960  41.369  1.00 75.25           C  
ANISOU 3877  CG  ARG A 754     9144  10618   8830    -15   -140    -83       C  
ATOM   3878  CD  ARG A 754     -64.502  29.590  42.053  1.00 90.31           C  
ANISOU 3878  CD  ARG A 754    11014  12635  10663     46   -125    -56       C  
ATOM   3879  NE  ARG A 754     -65.672  28.717  42.016  1.00 98.88           N  
ANISOU 3879  NE  ARG A 754    12011  13906  11654     -2   -183    -75       N  
ATOM   3880  CZ  ARG A 754     -65.842  27.662  42.807  1.00105.75           C  
ANISOU 3880  CZ  ARG A 754    12856  14789  12537   -133   -248   -124       C  
ATOM   3881  NH1 ARG A 754     -64.915  27.344  43.701  1.00104.19           N  
ANISOU 3881  NH1 ARG A 754    12709  14436  12441   -218   -266   -150       N  
ATOM   3882  NH2 ARG A 754     -66.938  26.923  42.704  1.00110.46           N  
ANISOU 3882  NH2 ARG A 754    13373  15559  13038   -180   -291   -145       N  
ATOM   3883  N   LYS A 755     -59.468  31.324  40.294  1.00 56.86           N  
ANISOU 3883  N   LYS A 755     7064   7799   6743    107     49    -45       N  
ATOM   3884  CA  LYS A 755     -58.729  32.409  39.669  1.00 62.44           C  
ANISOU 3884  CA  LYS A 755     7841   8403   7481    191    136    -16       C  
ATOM   3885  C   LYS A 755     -57.948  31.915  38.461  1.00 72.27           C  
ANISOU 3885  C   LYS A 755     9091   9622   8747    183    122    -21       C  
ATOM   3886  O   LYS A 755     -57.991  32.523  37.389  1.00 80.98           O  
ANISOU 3886  O   LYS A 755    10208  10742   9820    285    175     19       O  
ATOM   3887  CB  LYS A 755     -57.770  33.048  40.668  1.00 68.22           C  
ANISOU 3887  CB  LYS A 755     8645   8982   8295    143    180    -40       C  
ATOM   3888  N   LYS A 756     -57.239  30.804  38.640  1.00 69.81           N  
ANISOU 3888  N   LYS A 756     8768   9272   8486     67     53    -67       N  
ATOM   3889  CA  LYS A 756     -56.380  30.258  37.593  1.00 60.09           C  
ANISOU 3889  CA  LYS A 756     7545   8002   7284     48     38    -78       C  
ATOM   3890  C   LYS A 756     -57.134  29.545  36.474  1.00 61.71           C  
ANISOU 3890  C   LYS A 756     7687   8346   7416     69      2    -72       C  
ATOM   3891  O   LYS A 756     -56.663  29.513  35.337  1.00 76.91           O  
ANISOU 3891  O   LYS A 756     9618  10261   9341    102     16    -64       O  
ATOM   3892  CB  LYS A 756     -55.309  29.340  38.192  1.00 51.49           C  
ANISOU 3892  CB  LYS A 756     6471   6822   6272    -74    -13   -123       C  
ATOM   3893  CG  LYS A 756     -54.057  30.091  38.605  1.00 48.14           C  
ANISOU 3893  CG  LYS A 756     6114   6255   5922    -84     37   -130       C  
ATOM   3894  CD  LYS A 756     -53.119  29.242  39.417  1.00 53.15           C  
ANISOU 3894  CD  LYS A 756     6750   6827   6618   -195    -11   -167       C  
ATOM   3895  CE  LYS A 756     -51.820  30.007  39.701  1.00 65.19           C  
ANISOU 3895  CE  LYS A 756     8333   8233   8204   -209     41   -178       C  
ATOM   3896  NZ  LYS A 756     -52.063  31.453  40.002  1.00 67.37           N  
ANISOU 3896  NZ  LYS A 756     8653   8474   8471   -148    127   -164       N  
ATOM   3897  N   ALA A 757     -58.288  28.964  36.783  1.00 48.00           N  
ANISOU 3897  N   ALA A 757     5885   6742   5612     43    -42    -81       N  
ATOM   3898  CA  ALA A 757     -59.104  28.372  35.729  1.00 53.61           C  
ANISOU 3898  CA  ALA A 757     6526   7608   6236     59    -67    -80       C  
ATOM   3899  C   ALA A 757     -59.651  29.480  34.853  1.00 56.48           C  
ANISOU 3899  C   ALA A 757     6879   8052   6530    209     -2    -20       C  
ATOM   3900  O   ALA A 757     -59.886  29.286  33.661  1.00 60.35           O  
ANISOU 3900  O   ALA A 757     7328   8640   6963    249     -1     -9       O  
ATOM   3901  CB  ALA A 757     -60.240  27.540  36.298  1.00 50.80           C  
ANISOU 3901  CB  ALA A 757     6101   7387   5815    -10   -123   -108       C  
ATOM   3902  N   GLN A 758     -59.848  30.649  35.450  1.00 67.65           N  
ANISOU 3902  N   GLN A 758     8331   9426   7947    294     58     21       N  
ATOM   3903  CA  GLN A 758     -60.346  31.798  34.712  1.00 75.98           C  
ANISOU 3903  CA  GLN A 758     9390  10542   8939    452    137     90       C  
ATOM   3904  C   GLN A 758     -59.240  32.364  33.832  1.00 75.29           C  
ANISOU 3904  C   GLN A 758     9369  10333   8907    504    194    110       C  
ATOM   3905  O   GLN A 758     -59.491  32.802  32.712  1.00 79.34           O  
ANISOU 3905  O   GLN A 758     9864  10920   9362    612    236    157       O  
ATOM   3906  CB  GLN A 758     -60.918  32.851  35.668  1.00 78.80           C  
ANISOU 3906  CB  GLN A 758     9777  10883   9282    527    195    126       C  
ATOM   3907  CG  GLN A 758     -62.416  32.668  35.926  1.00 85.47           C  
ANISOU 3907  CG  GLN A 758    10534  11926  10016    560    168    144       C  
ATOM   3908  CD  GLN A 758     -62.817  32.912  37.375  1.00 88.67           C  
ANISOU 3908  CD  GLN A 758    10954  12299  10438    527    164    132       C  
ATOM   3909  OE1 GLN A 758     -62.391  33.885  38.005  1.00 87.67           O  
ANISOU 3909  OE1 GLN A 758    10906  12038  10366    567    234    149       O  
ATOM   3910  NE2 GLN A 758     -63.646  32.021  37.909  1.00 91.78           N  
ANISOU 3910  NE2 GLN A 758    11273  12818  10783    446     88     99       N  
ATOM   3911  N   ASP A 759     -58.014  32.329  34.341  1.00 72.13           N  
ANISOU 3911  N   ASP A 759     9039   9756   8612    424    194     74       N  
ATOM   3912  CA  ASP A 759     -56.849  32.744  33.571  1.00 74.54           C  
ANISOU 3912  CA  ASP A 759     9406   9940   8975    449    240     81       C  
ATOM   3913  C   ASP A 759     -56.508  31.749  32.465  1.00 69.73           C  
ANISOU 3913  C   ASP A 759     8754   9381   8358    408    185     59       C  
ATOM   3914  O   ASP A 759     -55.747  32.078  31.555  1.00 69.83           O  
ANISOU 3914  O   ASP A 759     8801   9334   8395    449    221     74       O  
ATOM   3915  CB  ASP A 759     -55.625  32.922  34.479  1.00 84.06           C  
ANISOU 3915  CB  ASP A 759    10688  10965  10286    363    252     42       C  
ATOM   3916  CG  ASP A 759     -55.625  34.254  35.208  1.00 93.97           C  
ANISOU 3916  CG  ASP A 759    12013  12132  11559    423    347     67       C  
ATOM   3917  OD1 ASP A 759     -54.550  34.661  35.709  1.00 89.81           O  
ANISOU 3917  OD1 ASP A 759    11555  11462  11108    370    383     39       O  
ATOM   3918  OD2 ASP A 759     -56.701  34.892  35.278  1.00101.41           O  
ANISOU 3918  OD2 ASP A 759    12943  13156  12435    521    390    112       O  
ATOM   3919  N   PHE A 760     -57.055  30.537  32.546  1.00 60.20           N  
ANISOU 3919  N   PHE A 760     7476   8279   7117    321    103     20       N  
ATOM   3920  CA  PHE A 760     -56.696  29.477  31.604  1.00 56.76           C  
ANISOU 3920  CA  PHE A 760     7008   7879   6680    260     53    -14       C  
ATOM   3921  C   PHE A 760     -56.845  29.925  30.162  1.00 62.40           C  
ANISOU 3921  C   PHE A 760     7698   8674   7335    367     93     27       C  
ATOM   3922  O   PHE A 760     -56.117  29.463  29.283  1.00 63.09           O  
ANISOU 3922  O   PHE A 760     7791   8732   7449    341     80      9       O  
ATOM   3923  CB  PHE A 760     -57.534  28.225  31.844  1.00 47.91           C  
ANISOU 3923  CB  PHE A 760     5814   6883   5508    163    -20    -59       C  
ATOM   3924  CG  PHE A 760     -57.146  27.056  30.980  1.00 39.28           C  
ANISOU 3924  CG  PHE A 760     4696   5811   4418     83    -63   -105       C  
ATOM   3925  CD1 PHE A 760     -56.182  26.155  31.403  1.00 42.16           C  
ANISOU 3925  CD1 PHE A 760     5101   6050   4868    -27    -99   -151       C  
ATOM   3926  CD2 PHE A 760     -57.759  26.845  29.760  1.00 43.55           C  
ANISOU 3926  CD2 PHE A 760     5172   6505   4872    120    -62   -100       C  
ATOM   3927  CE1 PHE A 760     -55.831  25.069  30.625  1.00 48.90           C  
ANISOU 3927  CE1 PHE A 760     5940   6912   5726    -99   -129   -192       C  
ATOM   3928  CE2 PHE A 760     -57.409  25.760  28.968  1.00 47.14           C  
ANISOU 3928  CE2 PHE A 760     5607   6976   5328     38    -95   -149       C  
ATOM   3929  CZ  PHE A 760     -56.437  24.874  29.403  1.00 46.20           C  
ANISOU 3929  CZ  PHE A 760     5539   6713   5300    -71   -126   -195       C  
ATOM   3930  N   SER A 761     -57.789  30.832  29.929  1.00 67.35           N  
ANISOU 3930  N   SER A 761     8300   9409   7882    493    144     86       N  
ATOM   3931  CA  SER A 761     -58.050  31.347  28.590  1.00 76.25           C  
ANISOU 3931  CA  SER A 761     9397  10635   8938    614    190    139       C  
ATOM   3932  C   SER A 761     -56.943  32.290  28.119  1.00 70.95           C  
ANISOU 3932  C   SER A 761     8815   9805   8336    685    264    174       C  
ATOM   3933  O   SER A 761     -56.776  32.503  26.920  1.00 71.16           O  
ANISOU 3933  O   SER A 761     8829   9878   8332    758    292    205       O  
ATOM   3934  CB  SER A 761     -59.395  32.078  28.556  1.00 86.00           C  
ANISOU 3934  CB  SER A 761    10578  12038  10060    743    232    203       C  
ATOM   3935  OG  SER A 761     -60.348  31.418  29.371  1.00 94.12           O  
ANISOU 3935  OG  SER A 761    11544  13177  11040    671    173    170       O  
ATOM   3936  N   ASN A 762     -56.193  32.851  29.064  1.00 63.98           N  
ANISOU 3936  N   ASN A 762     8021   8745   7543    659    298    165       N  
ATOM   3937  CA  ASN A 762     -55.142  33.807  28.748  1.00 63.16           C  
ANISOU 3937  CA  ASN A 762     8009   8484   7503    712    378    191       C  
ATOM   3938  C   ASN A 762     -53.754  33.174  28.651  1.00 63.26           C  
ANISOU 3938  C   ASN A 762     8060   8367   7610    599    339    134       C  
ATOM   3939  O   ASN A 762     -52.783  33.855  28.328  1.00 68.14           O  
ANISOU 3939  O   ASN A 762     8749   8860   8281    626    398    145       O  
ATOM   3940  CB  ASN A 762     -55.119  34.936  29.778  1.00 67.63           C  
ANISOU 3940  CB  ASN A 762     8655   8939   8104    751    458    213       C  
ATOM   3941  CG  ASN A 762     -56.461  35.621  29.923  1.00 79.75           C  
ANISOU 3941  CG  ASN A 762    10161  10593   9547    875    507    275       C  
ATOM   3942  OD1 ASN A 762     -57.058  36.051  28.934  1.00 84.94           O  
ANISOU 3942  OD1 ASN A 762    10787  11360  10125   1005    551    339       O  
ATOM   3943  ND2 ASN A 762     -56.944  35.730  31.166  1.00 73.11           N  
ANISOU 3943  ND2 ASN A 762     9326   9741   8712    839    501    259       N  
ATOM   3944  N   LEU A 763     -53.656  31.881  28.949  1.00 52.75           N  
ANISOU 3944  N   LEU A 763     6683   7063   6295    476    245     75       N  
ATOM   3945  CA  LEU A 763     -52.390  31.171  28.793  1.00 51.65           C  
ANISOU 3945  CA  LEU A 763     6571   6818   6234    380    207     28       C  
ATOM   3946  C   LEU A 763     -51.997  31.166  27.322  1.00 57.91           C  
ANISOU 3946  C   LEU A 763     7354   7637   7010    433    222     45       C  
ATOM   3947  O   LEU A 763     -52.863  31.162  26.437  1.00 60.72           O  
ANISOU 3947  O   LEU A 763     7651   8137   7283    505    226     75       O  
ATOM   3948  CB  LEU A 763     -52.497  29.723  29.262  1.00 46.41           C  
ANISOU 3948  CB  LEU A 763     5860   6192   5580    254    115    -30       C  
ATOM   3949  CG  LEU A 763     -52.530  29.390  30.744  1.00 50.62           C  
ANISOU 3949  CG  LEU A 763     6404   6677   6151    167     82    -61       C  
ATOM   3950  CD1 LEU A 763     -52.917  27.933  30.920  1.00 47.97           C  
ANISOU 3950  CD1 LEU A 763     6015   6411   5801     66      3   -106       C  
ATOM   3951  CD2 LEU A 763     -51.186  29.674  31.352  1.00 50.54           C  
ANISOU 3951  CD2 LEU A 763     6463   6508   6232    121    101    -78       C  
ATOM   3952  N   ASP A 764     -50.692  31.168  27.072  1.00 51.38           N  
ANISOU 3952  N   ASP A 764     6581   6684   6257    397    231     26       N  
ATOM   3953  CA  ASP A 764     -50.157  31.004  25.730  1.00 51.30           C  
ANISOU 3953  CA  ASP A 764     6564   6687   6242    427    234     33       C  
ATOM   3954  C   ASP A 764     -50.662  29.679  25.188  1.00 55.60           C  
ANISOU 3954  C   ASP A 764     7029   7354   6744    367    158     -3       C  
ATOM   3955  O   ASP A 764     -50.865  28.741  25.955  1.00 62.19           O  
ANISOU 3955  O   ASP A 764     7842   8198   7590    270     99    -47       O  
ATOM   3956  CB  ASP A 764     -48.632  30.970  25.801  1.00 66.33           C  
ANISOU 3956  CB  ASP A 764     8530   8436   8236    366    238      4       C  
ATOM   3957  CG  ASP A 764     -47.978  31.233  24.465  1.00 78.04           C  
ANISOU 3957  CG  ASP A 764    10025   9905   9719    421    268     23       C  
ATOM   3958  OD1 ASP A 764     -48.005  32.400  24.019  1.00 89.78           O  
ANISOU 3958  OD1 ASP A 764    11551  11370  11191    523    349     74       O  
ATOM   3959  OD2 ASP A 764     -47.425  30.276  23.875  1.00 76.11           O  
ANISOU 3959  OD2 ASP A 764     9759   9667   9494    363    216    -11       O  
ATOM   3960  N   ASP A 765     -50.851  29.589  23.875  1.00 60.57           N  
ANISOU 3960  N   ASP A 765     7616   8076   7320    421    163     14       N  
ATOM   3961  CA  ASP A 765     -51.355  28.357  23.263  1.00 66.04           C  
ANISOU 3961  CA  ASP A 765     8234   8896   7963    357    102    -28       C  
ATOM   3962  C   ASP A 765     -50.401  27.185  23.461  1.00 56.75           C  
ANISOU 3962  C   ASP A 765     7080   7622   6859    231     49    -92       C  
ATOM   3963  O   ASP A 765     -50.823  26.030  23.477  1.00 60.97           O  
ANISOU 3963  O   ASP A 765     7572   8223   7371    144      0   -139       O  
ATOM   3964  CB  ASP A 765     -51.610  28.557  21.772  1.00 80.25           C  
ANISOU 3964  CB  ASP A 765     9984  10814   9692    438    125      1       C  
ATOM   3965  CG  ASP A 765     -52.542  29.717  21.492  1.00 92.18           C  
ANISOU 3965  CG  ASP A 765    11470  12432  11122    583    186     76       C  
ATOM   3966  OD1 ASP A 765     -53.759  29.588  21.768  1.00 93.70           O  
ANISOU 3966  OD1 ASP A 765    11597  12773  11232    596    172     83       O  
ATOM   3967  OD2 ASP A 765     -52.053  30.756  20.990  1.00 96.38           O  
ANISOU 3967  OD2 ASP A 765    12049  12901  11669    685    253    131       O  
ATOM   3968  N   ASN A 766     -49.115  27.488  23.605  1.00 44.83           N  
ANISOU 3968  N   ASN A 766     5640   5959   5435    223     66    -91       N  
ATOM   3969  CA  ASN A 766     -48.108  26.458  23.816  1.00 49.73           C  
ANISOU 3969  CA  ASN A 766     6286   6485   6124    121     24   -140       C  
ATOM   3970  C   ASN A 766     -48.183  25.853  25.218  1.00 58.85           C  
ANISOU 3970  C   ASN A 766     7453   7593   7314     34    -12   -169       C  
ATOM   3971  O   ASN A 766     -47.960  24.659  25.401  1.00 63.71           O  
ANISOU 3971  O   ASN A 766     8064   8193   7951    -53    -53   -210       O  
ATOM   3972  CB  ASN A 766     -46.711  27.007  23.539  1.00 51.40           C  
ANISOU 3972  CB  ASN A 766     6559   6567   6404    142     54   -129       C  
ATOM   3973  CG  ASN A 766     -46.396  27.074  22.054  1.00 58.85           C  
ANISOU 3973  CG  ASN A 766     7489   7547   7326    192     69   -119       C  
ATOM   3974  OD1 ASN A 766     -45.781  28.032  21.575  1.00 60.20           O  
ANISOU 3974  OD1 ASN A 766     7696   7663   7514    260    118    -85       O  
ATOM   3975  ND2 ASN A 766     -46.827  26.056  21.314  1.00 64.85           N  
ANISOU 3975  ND2 ASN A 766     8195   8400   8045    155     32   -150       N  
ATOM   3976  N   ILE A 767     -48.512  26.669  26.211  1.00 51.36           N  
ANISOU 3976  N   ILE A 767     6523   6621   6369     60     11   -145       N  
ATOM   3977  CA  ILE A 767     -48.633  26.146  27.564  1.00 46.07           C  
ANISOU 3977  CA  ILE A 767     5859   5919   5727    -18    -22   -169       C  
ATOM   3978  C   ILE A 767     -49.887  25.291  27.769  1.00 49.80           C  
ANISOU 3978  C   ILE A 767     6273   6510   6139    -62    -61   -191       C  
ATOM   3979  O   ILE A 767     -49.797  24.223  28.380  1.00 46.11           O  
ANISOU 3979  O   ILE A 767     5805   6020   5696   -153   -101   -226       O  
ATOM   3980  CB  ILE A 767     -48.567  27.255  28.640  1.00 40.05           C  
ANISOU 3980  CB  ILE A 767     5133   5094   4988     12     16   -144       C  
ATOM   3981  CG1 ILE A 767     -47.241  28.006  28.556  1.00 43.45           C  
ANISOU 3981  CG1 ILE A 767     5624   5404   5479     29     59   -136       C  
ATOM   3982  CG2 ILE A 767     -48.691  26.639  30.008  1.00 52.12           C  
ANISOU 3982  CG2 ILE A 767     6659   6602   6541    -71    -22   -169       C  
ATOM   3983  CD1 ILE A 767     -46.032  27.106  28.376  1.00 36.99           C  
ANISOU 3983  CD1 ILE A 767     4820   4518   4716    -38     25   -166       C  
ATOM   3984  N   VAL A 768     -51.039  25.741  27.254  1.00 45.53           N  
ANISOU 3984  N   VAL A 768     5683   6102   5515      1    -46   -169       N  
ATOM   3985  CA  VAL A 768     -52.316  25.061  27.536  1.00 49.70           C  
ANISOU 3985  CA  VAL A 768     6150   6761   5973    -43    -79   -191       C  
ATOM   3986  C   VAL A 768     -52.350  23.578  27.141  1.00 45.83           C  
ANISOU 3986  C   VAL A 768     5636   6305   5475   -148   -120   -249       C  
ATOM   3987  O   VAL A 768     -53.025  22.780  27.794  1.00 54.24           O  
ANISOU 3987  O   VAL A 768     6678   7415   6517   -226   -149   -282       O  
ATOM   3988  CB  VAL A 768     -53.584  25.784  26.940  1.00 57.20           C  
ANISOU 3988  CB  VAL A 768     7037   7880   6817     52    -54   -154       C  
ATOM   3989  CG1 VAL A 768     -53.799  27.146  27.568  1.00 60.81           C  
ANISOU 3989  CG1 VAL A 768     7523   8307   7275    149     -6    -98       C  
ATOM   3990  CG2 VAL A 768     -53.488  25.902  25.459  1.00 53.74           C  
ANISOU 3990  CG2 VAL A 768     6570   7513   6337    109    -34   -142       C  
ATOM   3991  N   LYS A 769     -51.619  23.194  26.100  1.00 43.50           N  
ANISOU 3991  N   LYS A 769     5350   5981   5198   -154   -116   -264       N  
ATOM   3992  CA  LYS A 769     -51.608  21.784  25.705  1.00 44.33           C  
ANISOU 3992  CA  LYS A 769     5443   6104   5297   -256   -142   -323       C  
ATOM   3993  C   LYS A 769     -50.760  20.930  26.649  1.00 34.45           C  
ANISOU 3993  C   LYS A 769     4250   4708   4131   -339   -161   -346       C  
ATOM   3994  O   LYS A 769     -50.792  19.705  26.607  1.00 35.37           O  
ANISOU 3994  O   LYS A 769     4372   4817   4250   -429   -173   -392       O  
ATOM   3995  CB  LYS A 769     -51.201  21.605  24.231  1.00 52.85           C  
ANISOU 3995  CB  LYS A 769     6507   7215   6358   -236   -130   -335       C  
ATOM   3996  CG  LYS A 769     -50.109  22.542  23.728  1.00 58.56           C  
ANISOU 3996  CG  LYS A 769     7271   7845   7133   -149   -103   -292       C  
ATOM   3997  CD  LYS A 769     -49.576  22.051  22.376  1.00 65.32           C  
ANISOU 3997  CD  LYS A 769     8119   8715   7984   -156    -99   -315       C  
ATOM   3998  CE  LYS A 769     -48.594  23.026  21.735  1.00 62.53           C  
ANISOU 3998  CE  LYS A 769     7799   8291   7670    -65    -70   -272       C  
ATOM   3999  NZ  LYS A 769     -49.229  24.135  20.956  1.00 59.17           N  
ANISOU 3999  NZ  LYS A 769     7331   7976   7173     47    -36   -223       N  
ATOM   4000  N   ASN A 770     -50.023  21.591  27.533  1.00 39.54           N  
ANISOU 4000  N   ASN A 770     4939   5244   4840   -308   -155   -313       N  
ATOM   4001  CA  ASN A 770     -49.211  20.892  28.521  1.00 33.84           C  
ANISOU 4001  CA  ASN A 770     4264   4403   4191   -371   -171   -324       C  
ATOM   4002  C   ASN A 770     -49.876  20.733  29.902  1.00 35.79           C  
ANISOU 4002  C   ASN A 770     4504   4660   4434   -414   -189   -325       C  
ATOM   4003  O   ASN A 770     -49.525  19.840  30.676  1.00 38.96           O  
ANISOU 4003  O   ASN A 770     4931   4998   4875   -481   -203   -339       O  
ATOM   4004  CB  ASN A 770     -47.835  21.547  28.598  1.00 38.17           C  
ANISOU 4004  CB  ASN A 770     4859   4835   4809   -328   -154   -296       C  
ATOM   4005  CG  ASN A 770     -47.124  21.513  27.252  1.00 38.22           C  
ANISOU 4005  CG  ASN A 770     4873   4825   4822   -297   -140   -300       C  
ATOM   4006  OD1 ASN A 770     -46.805  20.448  26.744  1.00 42.03           O  
ANISOU 4006  OD1 ASN A 770     5364   5291   5315   -346   -149   -330       O  
ATOM   4007  ND2 ASN A 770     -46.910  22.675  26.658  1.00 42.92           N  
ANISOU 4007  ND2 ASN A 770     5470   5426   5410   -216   -112   -269       N  
ATOM   4008  N   ILE A 771     -50.864  21.574  30.191  1.00 36.12           N  
ANISOU 4008  N   ILE A 771     4510   4788   4424   -371   -185   -306       N  
ATOM   4009  CA  ILE A 771     -51.580  21.497  31.454  1.00 39.87           C  
ANISOU 4009  CA  ILE A 771     4974   5287   4889   -408   -202   -306       C  
ATOM   4010  C   ILE A 771     -52.185  20.113  31.755  1.00 41.75           C  
ANISOU 4010  C   ILE A 771     5197   5560   5105   -510   -227   -349       C  
ATOM   4011  O   ILE A 771     -52.056  19.615  32.863  1.00 50.69           O  
ANISOU 4011  O   ILE A 771     6350   6638   6272   -562   -241   -352       O  
ATOM   4012  CB  ILE A 771     -52.676  22.553  31.516  1.00 43.76           C  
ANISOU 4012  CB  ILE A 771     5426   5887   5315   -339   -189   -280       C  
ATOM   4013  CG1 ILE A 771     -52.055  23.947  31.428  1.00 40.41           C  
ANISOU 4013  CG1 ILE A 771     5032   5401   4919   -243   -149   -237       C  
ATOM   4014  CG2 ILE A 771     -53.482  22.374  32.758  1.00 28.08           C  
ANISOU 4014  CG2 ILE A 771     3421   3935   3311   -382   -210   -286       C  
ATOM   4015  CD1 ILE A 771     -51.519  24.436  32.704  1.00 48.01           C  
ANISOU 4015  CD1 ILE A 771     6033   6270   5939   -253   -143   -225       C  
ATOM   4016  N   PRO A 772     -52.848  19.483  30.777  1.00 46.48           N  
ANISOU 4016  N   PRO A 772     5763   6254   5643   -542   -226   -384       N  
ATOM   4017  CA  PRO A 772     -53.421  18.182  31.152  1.00 41.51           C  
ANISOU 4017  CA  PRO A 772     5131   5648   4994   -652   -237   -431       C  
ATOM   4018  C   PRO A 772     -52.396  17.192  31.720  1.00 37.28           C  
ANISOU 4018  C   PRO A 772     4660   4964   4539   -710   -235   -439       C  
ATOM   4019  O   PRO A 772     -52.701  16.553  32.727  1.00 36.47           O  
ANISOU 4019  O   PRO A 772     4570   4841   4447   -772   -243   -448       O  
ATOM   4020  CB  PRO A 772     -54.048  17.679  29.844  1.00 38.89           C  
ANISOU 4020  CB  PRO A 772     4758   5432   4588   -683   -227   -475       C  
ATOM   4021  CG  PRO A 772     -54.385  18.937  29.094  1.00 39.56           C  
ANISOU 4021  CG  PRO A 772     4794   5616   4620   -576   -220   -439       C  
ATOM   4022  CD  PRO A 772     -53.275  19.921  29.432  1.00 44.36           C  
ANISOU 4022  CD  PRO A 772     5451   6095   5309   -489   -211   -385       C  
ATOM   4023  N   ASN A 773     -51.225  17.064  31.100  1.00 48.42           N  
ANISOU 4023  N   ASN A 773     6110   6282   6004   -686   -221   -432       N  
ATOM   4024  CA  ASN A 773     -50.137  16.236  31.648  1.00 44.69           C  
ANISOU 4024  CA  ASN A 773     5698   5674   5607   -718   -214   -425       C  
ATOM   4025  C   ASN A 773     -49.599  16.741  32.982  1.00 35.39           C  
ANISOU 4025  C   ASN A 773     4536   4433   4480   -691   -227   -382       C  
ATOM   4026  O   ASN A 773     -49.280  15.951  33.855  1.00 34.28           O  
ANISOU 4026  O   ASN A 773     4425   4228   4373   -733   -226   -376       O  
ATOM   4027  CB  ASN A 773     -48.972  16.136  30.649  1.00 48.88           C  
ANISOU 4027  CB  ASN A 773     6260   6133   6178   -685   -197   -422       C  
ATOM   4028  CG  ASN A 773     -49.178  15.057  29.617  1.00 53.90           C  
ANISOU 4028  CG  ASN A 773     6907   6784   6789   -745   -175   -472       C  
ATOM   4029  OD1 ASN A 773     -50.152  14.299  29.684  1.00 43.35           O  
ANISOU 4029  OD1 ASN A 773     5559   5506   5406   -823   -168   -514       O  
ATOM   4030  ND2 ASN A 773     -48.258  14.978  28.645  1.00 46.94           N  
ANISOU 4030  ND2 ASN A 773     6047   5852   5934   -716   -160   -473       N  
ATOM   4031  N   LEU A 774     -49.488  18.058  33.124  1.00 35.21           N  
ANISOU 4031  N   LEU A 774     4493   4428   4457   -620   -232   -352       N  
ATOM   4032  CA  LEU A 774     -49.098  18.652  34.398  1.00 42.22           C  
ANISOU 4032  CA  LEU A 774     5387   5273   5380   -604   -241   -321       C  
ATOM   4033  C   LEU A 774     -50.013  18.175  35.526  1.00 47.06           C  
ANISOU 4033  C   LEU A 774     5984   5925   5972   -660   -258   -327       C  
ATOM   4034  O   LEU A 774     -49.539  17.785  36.591  1.00 49.96           O  
ANISOU 4034  O   LEU A 774     6369   6238   6377   -685   -264   -312       O  
ATOM   4035  CB  LEU A 774     -49.060  20.189  34.323  1.00 31.34           C  
ANISOU 4035  CB  LEU A 774     3996   3917   3996   -528   -230   -297       C  
ATOM   4036  CG  LEU A 774     -47.851  20.698  33.518  1.00 43.21           C  
ANISOU 4036  CG  LEU A 774     5526   5356   5536   -479   -209   -284       C  
ATOM   4037  CD1 LEU A 774     -47.663  22.223  33.584  1.00 35.31           C  
ANISOU 4037  CD1 LEU A 774     4528   4351   4536   -411   -183   -261       C  
ATOM   4038  CD2 LEU A 774     -46.552  19.985  33.955  1.00 36.15           C  
ANISOU 4038  CD2 LEU A 774     4664   4369   4701   -507   -211   -277       C  
ATOM   4039  N   LEU A 775     -51.320  18.196  35.286  1.00 40.30           N  
ANISOU 4039  N   LEU A 775     5090   5172   5050   -677   -265   -349       N  
ATOM   4040  CA  LEU A 775     -52.279  17.752  36.288  1.00 40.88           C  
ANISOU 4040  CA  LEU A 775     5144   5293   5094   -734   -282   -360       C  
ATOM   4041  C   LEU A 775     -52.110  16.264  36.570  1.00 39.90           C  
ANISOU 4041  C   LEU A 775     5055   5114   4993   -817   -276   -381       C  
ATOM   4042  O   LEU A 775     -52.212  15.838  37.706  1.00 42.81           O  
ANISOU 4042  O   LEU A 775     5432   5458   5377   -854   -284   -371       O  
ATOM   4043  CB  LEU A 775     -53.720  18.064  35.855  1.00 44.04           C  
ANISOU 4043  CB  LEU A 775     5489   5835   5407   -735   -289   -381       C  
ATOM   4044  CG  LEU A 775     -54.185  19.528  35.879  1.00 41.33           C  
ANISOU 4044  CG  LEU A 775     5112   5560   5032   -648   -287   -352       C  
ATOM   4045  CD1 LEU A 775     -55.394  19.768  34.963  1.00 29.06           C  
ANISOU 4045  CD1 LEU A 775     3501   4158   3383   -627   -284   -367       C  
ATOM   4046  CD2 LEU A 775     -54.487  19.971  37.305  1.00 36.36           C  
ANISOU 4046  CD2 LEU A 775     4476   4926   4413   -651   -301   -332       C  
ATOM   4047  N   ILE A 776     -51.839  15.471  35.542  1.00 41.44           N  
ANISOU 4047  N   ILE A 776     5274   5284   5187   -844   -255   -408       N  
ATOM   4048  CA  ILE A 776     -51.704  14.025  35.731  1.00 43.25           C  
ANISOU 4048  CA  ILE A 776     5549   5449   5435   -922   -232   -429       C  
ATOM   4049  C   ILE A 776     -50.434  13.674  36.499  1.00 44.39           C  
ANISOU 4049  C   ILE A 776     5742   5471   5655   -900   -223   -386       C  
ATOM   4050  O   ILE A 776     -50.391  12.691  37.236  1.00 42.93           O  
ANISOU 4050  O   ILE A 776     5591   5233   5488   -947   -206   -381       O  
ATOM   4051  CB  ILE A 776     -51.701  13.283  34.398  1.00 39.16           C  
ANISOU 4051  CB  ILE A 776     5050   4933   4897   -959   -202   -475       C  
ATOM   4052  CG1 ILE A 776     -53.113  13.265  33.811  1.00 47.07           C  
ANISOU 4052  CG1 ILE A 776     5999   6078   5809  -1011   -205   -527       C  
ATOM   4053  CG2 ILE A 776     -51.200  11.856  34.574  1.00 31.24           C  
ANISOU 4053  CG2 ILE A 776     4116   3821   3932  -1021   -162   -486       C  
ATOM   4054  CD1 ILE A 776     -53.154  12.734  32.395  1.00 55.67           C  
ANISOU 4054  CD1 ILE A 776     7090   7197   6865  -1045   -177   -577       C  
ATOM   4055  N   ILE A 777     -49.401  14.487  36.325  1.00 41.75           N  
ANISOU 4055  N   ILE A 777     5408   5098   5358   -826   -230   -353       N  
ATOM   4056  CA  ILE A 777     -48.171  14.303  37.070  1.00 44.92           C  
ANISOU 4056  CA  ILE A 777     5837   5411   5818   -797   -224   -310       C  
ATOM   4057  C   ILE A 777     -48.374  14.745  38.514  1.00 47.99           C  
ANISOU 4057  C   ILE A 777     6200   5823   6210   -798   -246   -282       C  
ATOM   4058  O   ILE A 777     -47.979  14.051  39.453  1.00 47.50           O  
ANISOU 4058  O   ILE A 777     6157   5718   6173   -814   -239   -255       O  
ATOM   4059  CB  ILE A 777     -47.030  15.118  36.457  1.00 38.79           C  
ANISOU 4059  CB  ILE A 777     5062   4604   5071   -728   -223   -290       C  
ATOM   4060  CG1 ILE A 777     -46.680  14.558  35.065  1.00 40.70           C  
ANISOU 4060  CG1 ILE A 777     5333   4816   5317   -727   -200   -314       C  
ATOM   4061  CG2 ILE A 777     -45.841  15.130  37.398  1.00 31.17           C  
ANISOU 4061  CG2 ILE A 777     4108   3585   4152   -700   -222   -245       C  
ATOM   4062  CD1 ILE A 777     -45.835  15.492  34.213  1.00 42.02           C  
ANISOU 4062  CD1 ILE A 777     5494   4974   5499   -662   -201   -304       C  
ATOM   4063  N   THR A 778     -48.989  15.910  38.677  1.00 39.47           N  
ANISOU 4063  N   THR A 778     5079   4814   5103   -775   -268   -286       N  
ATOM   4064  CA  THR A 778     -49.259  16.452  39.987  1.00 39.07           C  
ANISOU 4064  CA  THR A 778     5000   4792   5051   -777   -287   -267       C  
ATOM   4065  C   THR A 778     -50.089  15.501  40.836  1.00 43.87           C  
ANISOU 4065  C   THR A 778     5608   5418   5641   -841   -293   -273       C  
ATOM   4066  O   THR A 778     -49.723  15.190  41.969  1.00 46.59           O  
ANISOU 4066  O   THR A 778     5955   5738   6010   -852   -297   -244       O  
ATOM   4067  CB  THR A 778     -49.985  17.780  39.871  1.00 42.74           C  
ANISOU 4067  CB  THR A 778     5428   5329   5481   -742   -298   -275       C  
ATOM   4068  OG1 THR A 778     -49.112  18.721  39.232  1.00 42.86           O  
ANISOU 4068  OG1 THR A 778     5451   5316   5518   -682   -284   -265       O  
ATOM   4069  CG2 THR A 778     -50.382  18.300  41.265  1.00 29.62           C  
ANISOU 4069  CG2 THR A 778     3739   3700   3814   -752   -315   -261       C  
ATOM   4070  N   LEU A 779     -51.201  15.038  40.282  1.00 42.90           N  
ANISOU 4070  N   LEU A 779     5481   5347   5473   -887   -291   -311       N  
ATOM   4071  CA  LEU A 779     -52.113  14.181  41.023  1.00 51.54           C  
ANISOU 4071  CA  LEU A 779     6575   6467   6542   -959   -292   -324       C  
ATOM   4072  C   LEU A 779     -51.496  12.817  41.292  1.00 49.96           C  
ANISOU 4072  C   LEU A 779     6432   6172   6378   -995   -260   -311       C  
ATOM   4073  O   LEU A 779     -51.812  12.166  42.288  1.00 52.72           O  
ANISOU 4073  O   LEU A 779     6792   6512   6729  -1037   -255   -299       O  
ATOM   4074  CB  LEU A 779     -53.445  14.016  40.278  1.00 53.16           C  
ANISOU 4074  CB  LEU A 779     6756   6767   6677  -1007   -293   -376       C  
ATOM   4075  CG  LEU A 779     -54.441  15.180  40.305  1.00 54.53           C  
ANISOU 4075  CG  LEU A 779     6867   7059   6795   -977   -322   -382       C  
ATOM   4076  CD1 LEU A 779     -55.805  14.677  39.885  1.00 67.65           C  
ANISOU 4076  CD1 LEU A 779     8499   8828   8377  -1045   -321   -431       C  
ATOM   4077  CD2 LEU A 779     -54.532  15.789  41.677  1.00 49.85           C  
ANISOU 4077  CD2 LEU A 779     6252   6474   6215   -960   -345   -351       C  
ATOM   4078  N   SER A 780     -50.614  12.388  40.403  1.00 47.98           N  
ANISOU 4078  N   SER A 780     6221   5851   6157   -975   -231   -311       N  
ATOM   4079  CA  SER A 780     -50.010  11.074  40.535  1.00 47.70           C  
ANISOU 4079  CA  SER A 780     6250   5720   6155   -999   -187   -295       C  
ATOM   4080  C   SER A 780     -48.808  11.069  41.475  1.00 47.36           C  
ANISOU 4080  C   SER A 780     6215   5618   6160   -942   -185   -229       C  
ATOM   4081  O   SER A 780     -48.476  10.036  42.055  1.00 58.87           O  
ANISOU 4081  O   SER A 780     7717   7013   7639   -953   -150   -199       O  
ATOM   4082  CB  SER A 780     -49.608  10.528  39.176  1.00 49.90           C  
ANISOU 4082  CB  SER A 780     6570   5949   6440  -1003   -151   -324       C  
ATOM   4083  OG  SER A 780     -48.680   9.479  39.354  1.00 55.52           O  
ANISOU 4083  OG  SER A 780     7347   6553   7196   -993   -103   -291       O  
ATOM   4084  N   CYS A 781     -48.152  12.215  41.623  1.00 40.29           N  
ANISOU 4084  N   CYS A 781     5279   4750   5278   -881   -216   -207       N  
ATOM   4085  CA  CYS A 781     -47.108  12.352  42.634  1.00 38.82           C  
ANISOU 4085  CA  CYS A 781     5082   4546   5123   -836   -220   -150       C  
ATOM   4086  C   CYS A 781     -47.728  12.377  44.021  1.00 46.18           C  
ANISOU 4086  C   CYS A 781     5984   5523   6040   -864   -239   -133       C  
ATOM   4087  O   CYS A 781     -47.116  11.933  44.988  1.00 51.97           O  
ANISOU 4087  O   CYS A 781     6717   6240   6790   -847   -229    -84       O  
ATOM   4088  CB  CYS A 781     -46.348  13.651  42.439  1.00 39.40           C  
ANISOU 4088  CB  CYS A 781     5118   4648   5205   -782   -243   -144       C  
ATOM   4089  SG  CYS A 781     -45.089  13.567  41.195  1.00 46.65           S  
ANISOU 4089  SG  CYS A 781     6067   5505   6151   -732   -219   -139       S  
ATOM   4090  N   ILE A 782     -48.935  12.933  44.108  1.00 42.80           N  
ANISOU 4090  N   ILE A 782     5523   5161   5576   -901   -266   -170       N  
ATOM   4091  CA  ILE A 782     -49.637  13.066  45.370  1.00 44.68           C  
ANISOU 4091  CA  ILE A 782     5728   5452   5797   -930   -288   -161       C  
ATOM   4092  C   ILE A 782     -50.077  11.686  45.815  1.00 51.12           C  
ANISOU 4092  C   ILE A 782     6583   6230   6609   -982   -259   -152       C  
ATOM   4093  O   ILE A 782     -49.875  11.305  46.958  1.00 49.40           O  
ANISOU 4093  O   ILE A 782     6361   6009   6401   -982   -257   -111       O  
ATOM   4094  CB  ILE A 782     -50.838  14.031  45.260  1.00 40.33           C  
ANISOU 4094  CB  ILE A 782     5134   4987   5203   -948   -320   -201       C  
ATOM   4095  CG1 ILE A 782     -50.345  15.469  45.165  1.00 38.60           C  
ANISOU 4095  CG1 ILE A 782     4881   4795   4991   -892   -337   -198       C  
ATOM   4096  CG2 ILE A 782     -51.773  13.893  46.460  1.00 28.72           C  
ANISOU 4096  CG2 ILE A 782     3636   3569   3708   -992   -339   -199       C  
ATOM   4097  CD1 ILE A 782     -51.430  16.457  44.870  1.00 38.20           C  
ANISOU 4097  CD1 ILE A 782     4797   4819   4898   -889   -355   -230       C  
ATOM   4098  N   SER A 783     -50.646  10.918  44.899  1.00 54.15           N  
ANISOU 4098  N   SER A 783     7009   6586   6977  -1028   -231   -192       N  
ATOM   4099  CA  SER A 783     -51.058   9.565  45.236  1.00 54.45           C  
ANISOU 4099  CA  SER A 783     7100   6575   7013  -1087   -187   -191       C  
ATOM   4100  C   SER A 783     -49.880   8.744  45.745  1.00 51.85           C  
ANISOU 4100  C   SER A 783     6816   6156   6727  -1042   -145   -125       C  
ATOM   4101  O   SER A 783     -50.028   7.911  46.629  1.00 56.00           O  
ANISOU 4101  O   SER A 783     7369   6652   7256  -1063   -116    -93       O  
ATOM   4102  CB  SER A 783     -51.682   8.868  44.027  1.00 53.31           C  
ANISOU 4102  CB  SER A 783     6999   6411   6844  -1150   -151   -252       C  
ATOM   4103  OG  SER A 783     -51.788   7.475  44.267  1.00 53.78           O  
ANISOU 4103  OG  SER A 783     7131   6392   6912  -1203    -88   -249       O  
ATOM   4104  N   ASN A 784     -48.706   8.976  45.179  1.00 49.24           N  
ANISOU 4104  N   ASN A 784     6494   5787   6427   -975   -138   -101       N  
ATOM   4105  CA  ASN A 784     -47.537   8.196  45.550  1.00 55.88           C  
ANISOU 4105  CA  ASN A 784     7375   6556   7302   -919    -94    -33       C  
ATOM   4106  C   ASN A 784     -46.957   8.581  46.924  1.00 53.64           C  
ANISOU 4106  C   ASN A 784     7037   6320   7021   -871   -118     31       C  
ATOM   4107  O   ASN A 784     -46.557   7.706  47.700  1.00 50.76           O  
ANISOU 4107  O   ASN A 784     6700   5921   6666   -847    -79     91       O  
ATOM   4108  CB  ASN A 784     -46.480   8.261  44.436  1.00 55.91           C  
ANISOU 4108  CB  ASN A 784     7402   6511   7329   -865    -76    -31       C  
ATOM   4109  CG  ASN A 784     -46.808   7.333  43.272  1.00 62.43           C  
ANISOU 4109  CG  ASN A 784     8303   7260   8157   -909    -22    -76       C  
ATOM   4110  OD1 ASN A 784     -47.089   6.149  43.470  1.00 64.22           O  
ANISOU 4110  OD1 ASN A 784     8597   7418   8387   -945     38    -69       O  
ATOM   4111  ND2 ASN A 784     -46.772   7.866  42.056  1.00 59.07           N  
ANISOU 4111  ND2 ASN A 784     7869   6847   7727   -909    -38   -123       N  
ATOM   4112  N   MET A 785     -46.914   9.885  47.207  1.00 47.87           N  
ANISOU 4112  N   MET A 785     6234   5674   6281   -857   -176     19       N  
ATOM   4113  CA  MET A 785     -46.414  10.402  48.477  1.00 55.55           C  
ANISOU 4113  CA  MET A 785     7144   6712   7249   -826   -202     65       C  
ATOM   4114  C   MET A 785     -47.327   9.955  49.618  1.00 60.44           C  
ANISOU 4114  C   MET A 785     7755   7359   7851   -870   -205     77       C  
ATOM   4115  O   MET A 785     -46.869   9.506  50.669  1.00 55.83           O  
ANISOU 4115  O   MET A 785     7157   6790   7267   -843   -192    138       O  
ATOM   4116  CB  MET A 785     -46.347  11.928  48.436  1.00 55.46           C  
ANISOU 4116  CB  MET A 785     7069   6775   7229   -819   -251     31       C  
ATOM   4117  CG  MET A 785     -45.248  12.476  47.538  1.00 58.57           C  
ANISOU 4117  CG  MET A 785     7463   7152   7639   -770   -246     29       C  
ATOM   4118  SD  MET A 785     -43.624  11.933  48.087  1.00 59.28           S  
ANISOU 4118  SD  MET A 785     7544   7241   7740   -701   -218    106       S  
ATOM   4119  CE  MET A 785     -43.644  12.452  49.805  1.00 51.08           C  
ANISOU 4119  CE  MET A 785     6424   6308   6676   -712   -246    135       C  
ATOM   4120  N   ILE A 786     -48.629  10.072  49.392  1.00 53.57           N  
ANISOU 4120  N   ILE A 786     6889   6507   6960   -937   -223     21       N  
ATOM   4121  CA  ILE A 786     -49.603   9.673  50.381  1.00 49.13           C  
ANISOU 4121  CA  ILE A 786     6317   5974   6376   -988   -228     24       C  
ATOM   4122  C   ILE A 786     -49.415   8.210  50.762  1.00 56.15           C  
ANISOU 4122  C   ILE A 786     7271   6785   7277   -990   -165     73       C  
ATOM   4123  O   ILE A 786     -49.495   7.849  51.936  1.00 68.16           O  
ANISOU 4123  O   ILE A 786     8777   8328   8792   -989   -160    118       O  
ATOM   4124  CB  ILE A 786     -51.019   9.910  49.878  1.00 42.61           C  
ANISOU 4124  CB  ILE A 786     5489   5183   5518  -1060   -249    -47       C  
ATOM   4125  CG1 ILE A 786     -51.278  11.410  49.759  1.00 38.89           C  
ANISOU 4125  CG1 ILE A 786     4952   4794   5030  -1045   -304    -80       C  
ATOM   4126  CG2 ILE A 786     -52.023   9.296  50.847  1.00 43.83           C  
ANISOU 4126  CG2 ILE A 786     5644   5360   5648  -1121   -246    -45       C  
ATOM   4127  CD1 ILE A 786     -52.626  11.756  49.160  1.00 40.46           C  
ANISOU 4127  CD1 ILE A 786     5138   5046   5187  -1096   -324   -144       C  
ATOM   4128  N   HIS A 787     -49.153   7.378  49.763  1.00 54.42           N  
ANISOU 4128  N   HIS A 787     7128   6474   7075   -991   -111     64       N  
ATOM   4129  CA  HIS A 787     -48.934   5.951  49.978  1.00 57.16           C  
ANISOU 4129  CA  HIS A 787     7556   6726   7437   -988    -32    109       C  
ATOM   4130  C   HIS A 787     -47.665   5.714  50.788  1.00 55.17           C  
ANISOU 4130  C   HIS A 787     7291   6470   7202   -892    -11    206       C  
ATOM   4131  O   HIS A 787     -47.611   4.833  51.647  1.00 58.21           O  
ANISOU 4131  O   HIS A 787     7707   6825   7587   -877     36    266       O  
ATOM   4132  CB  HIS A 787     -48.835   5.219  48.636  1.00 62.70           C  
ANISOU 4132  CB  HIS A 787     8342   7330   8152  -1007     27     72       C  
ATOM   4133  CG  HIS A 787     -48.563   3.750  48.767  1.00 65.55           C  
ANISOU 4133  CG  HIS A 787     8802   7573   8530  -1001    125    117       C  
ATOM   4134  ND1 HIS A 787     -47.294   3.225  48.713  1.00 60.26           N  
ANISOU 4134  ND1 HIS A 787     8171   6837   7889   -907    177    191       N  
ATOM   4135  CD2 HIS A 787     -49.405   2.706  48.956  1.00 64.10           C  
ANISOU 4135  CD2 HIS A 787     8691   7328   8337  -1077    189     99       C  
ATOM   4136  CE1 HIS A 787     -47.363   1.907  48.866  1.00 59.80           C  
ANISOU 4136  CE1 HIS A 787     8210   6671   7840   -917    274    222       C  
ATOM   4137  NE2 HIS A 787     -48.623   1.571  49.010  1.00 62.34           N  
ANISOU 4137  NE2 HIS A 787     8557   6988   8140  -1023    285    164       N  
ATOM   4138  N   ILE A 788     -46.641   6.507  50.508  1.00 52.31           N  
ANISOU 4138  N   ILE A 788     6882   6146   6849   -827    -42    221       N  
ATOM   4139  CA  ILE A 788     -45.384   6.389  51.225  1.00 49.98           C  
ANISOU 4139  CA  ILE A 788     6557   5877   6557   -735    -27    309       C  
ATOM   4140  C   ILE A 788     -45.563   6.805  52.686  1.00 46.23           C  
ANISOU 4140  C   ILE A 788     6003   5505   6058   -735    -65    344       C  
ATOM   4141  O   ILE A 788     -44.966   6.211  53.584  1.00 47.29           O  
ANISOU 4141  O   ILE A 788     6129   5656   6185   -678    -33    427       O  
ATOM   4142  CB  ILE A 788     -44.283   7.220  50.533  1.00 43.70           C  
ANISOU 4142  CB  ILE A 788     5722   5112   5768   -680    -53    304       C  
ATOM   4143  CG1 ILE A 788     -43.751   6.462  49.324  1.00 52.63           C  
ANISOU 4143  CG1 ILE A 788     6937   6137   6925   -650      4    305       C  
ATOM   4144  CG2 ILE A 788     -43.146   7.529  51.477  1.00 37.55           C  
ANISOU 4144  CG2 ILE A 788     4871   4422   4974   -605    -64    376       C  
ATOM   4145  CD1 ILE A 788     -42.866   7.307  48.407  1.00 58.33           C  
ANISOU 4145  CD1 ILE A 788     7628   6879   7653   -613    -24    282       C  
ATOM   4146  N   LEU A 789     -46.409   7.811  52.908  1.00 45.81           N  
ANISOU 4146  N   LEU A 789     5893   5523   5989   -796   -130    282       N  
ATOM   4147  CA  LEU A 789     -46.631   8.380  54.233  1.00 47.63           C  
ANISOU 4147  CA  LEU A 789     6043   5859   6196   -806   -172    301       C  
ATOM   4148  C   LEU A 789     -47.537   7.487  55.073  1.00 58.91           C  
ANISOU 4148  C   LEU A 789     7499   7270   7614   -845   -148    324       C  
ATOM   4149  O   LEU A 789     -47.529   7.560  56.300  1.00 59.02           O  
ANISOU 4149  O   LEU A 789     7457   7358   7609   -836   -163    367       O  
ATOM   4150  CB  LEU A 789     -47.229   9.787  54.134  1.00 39.08           C  
ANISOU 4150  CB  LEU A 789     4899   4850   5101   -853   -239    227       C  
ATOM   4151  CG  LEU A 789     -46.349  10.885  53.538  1.00 46.73           C  
ANISOU 4151  CG  LEU A 789     5830   5851   6075   -820   -262    203       C  
ATOM   4152  CD1 LEU A 789     -47.093  12.204  53.461  1.00 42.52           C  
ANISOU 4152  CD1 LEU A 789     5253   5372   5529   -865   -312    133       C  
ATOM   4153  CD2 LEU A 789     -45.074  11.050  54.330  1.00 53.23           C  
ANISOU 4153  CD2 LEU A 789     6594   6744   6887   -762   -258    263       C  
ATOM   4154  N   ASN A 790     -48.322   6.650  54.402  1.00 59.02           N  
ANISOU 4154  N   ASN A 790     7598   7190   7636   -895   -108    292       N  
ATOM   4155  CA  ASN A 790     -49.184   5.700  55.091  1.00 52.97           C  
ANISOU 4155  CA  ASN A 790     6873   6392   6860   -942    -71    309       C  
ATOM   4156  C   ASN A 790     -48.485   4.408  55.511  1.00 52.22           C  
ANISOU 4156  C   ASN A 790     6842   6220   6777   -880     14    402       C  
ATOM   4157  O   ASN A 790     -48.986   3.685  56.365  1.00 62.86           O  
ANISOU 4157  O   ASN A 790     8213   7555   8115   -899     48    438       O  
ATOM   4158  CB  ASN A 790     -50.419   5.383  54.250  1.00 49.67           C  
ANISOU 4158  CB  ASN A 790     6514   5923   6436  -1039    -60    225       C  
ATOM   4159  CG  ASN A 790     -51.495   6.427  54.398  1.00 50.90           C  
ANISOU 4159  CG  ASN A 790     6601   6177   6563  -1104   -136    156       C  
ATOM   4160  OD1 ASN A 790     -51.541   7.140  55.400  1.00 59.15           O  
ANISOU 4160  OD1 ASN A 790     7569   7313   7594  -1092   -186    174       O  
ATOM   4161  ND2 ASN A 790     -52.373   6.524  53.408  1.00 44.64           N  
ANISOU 4161  ND2 ASN A 790     5832   5375   5755  -1171   -142     76       N  
ATOM   4162  N   GLU A 791     -47.341   4.106  54.912  1.00 49.47           N  
ANISOU 4162  N   GLU A 791     6525   5821   6449   -801     55    444       N  
ATOM   4163  CA  GLU A 791     -46.588   2.932  55.327  1.00 62.84           C  
ANISOU 4163  CA  GLU A 791     8278   7448   8149   -721    144    544       C  
ATOM   4164  C   GLU A 791     -46.353   2.989  56.838  1.00 67.67           C  
ANISOU 4164  C   GLU A 791     8814   8161   8735   -675    128    625       C  
ATOM   4165  O   GLU A 791     -46.218   4.072  57.414  1.00 64.85           O  
ANISOU 4165  O   GLU A 791     8349   7934   8358   -675     49    613       O  
ATOM   4166  CB  GLU A 791     -45.251   2.846  54.587  1.00 60.90           C  
ANISOU 4166  CB  GLU A 791     8048   7170   7919   -627    174    585       C  
ATOM   4167  CG  GLU A 791     -45.341   2.428  53.126  1.00 75.38           C  
ANISOU 4167  CG  GLU A 791     9977   8882   9781   -657    217    526       C  
ATOM   4168  CD  GLU A 791     -44.025   2.659  52.372  1.00 93.66           C  
ANISOU 4168  CD  GLU A 791    12284  11194  12108   -568    223    553       C  
ATOM   4169  OE1 GLU A 791     -43.263   3.580  52.758  1.00 96.38           O  
ANISOU 4169  OE1 GLU A 791    12528  11654  12436   -518    163    576       O  
ATOM   4170  OE2 GLU A 791     -43.751   1.923  51.393  1.00 93.93           O  
ANISOU 4170  OE2 GLU A 791    12411  11114  12166   -554    291    547       O  
ATOM   4171  N   SER A 792     -46.321   1.824  57.480  1.00 73.67           N  
ANISOU 4171  N   SER A 792     9636   8863   9494   -636    211    707       N  
ATOM   4172  CA  SER A 792     -46.046   1.752  58.914  1.00 77.08           C  
ANISOU 4172  CA  SER A 792     9998   9394   9896   -580    207    797       C  
ATOM   4173  C   SER A 792     -44.650   2.263  59.251  1.00 76.46           C  
ANISOU 4173  C   SER A 792     9826   9430   9796   -470    184    867       C  
ATOM   4174  O   SER A 792     -44.470   3.001  60.221  1.00 79.21           O  
ANISOU 4174  O   SER A 792    10060   9925  10111   -461    124    884       O  
ATOM   4175  CB  SER A 792     -46.204   0.322  59.422  1.00 83.90           C  
ANISOU 4175  CB  SER A 792    10960  10157  10763   -546    317    881       C  
ATOM   4176  OG  SER A 792     -47.563   0.044  59.710  1.00 95.27           O  
ANISOU 4176  OG  SER A 792    12438  11557  12202   -657    318    826       O  
ATOM   4177  N   LYS A 793     -43.671   1.864  58.440  1.00 67.44           N  
ANISOU 4177  N   LYS A 793     8732   8225   8667   -391    236    902       N  
ATOM   4178  CA  LYS A 793     -42.283   2.249  58.647  1.00 62.80           C  
ANISOU 4178  CA  LYS A 793     8060   7749   8052   -284    224    970       C  
ATOM   4179  C   LYS A 793     -42.154   3.761  58.680  1.00 61.12           C  
ANISOU 4179  C   LYS A 793     7728   7673   7823   -334    116    894       C  
ATOM   4180  O   LYS A 793     -41.116   4.287  59.065  1.00 64.23           O  
ANISOU 4180  O   LYS A 793     8026   8196   8181   -272     93    934       O  
ATOM   4181  CB  LYS A 793     -41.393   1.704  57.518  1.00 56.27           C  
ANISOU 4181  CB  LYS A 793     7311   6823   7247   -211    288    994       C  
ATOM   4182  CG  LYS A 793     -41.517   2.498  56.229  1.00 60.08           C  
ANISOU 4182  CG  LYS A 793     7804   7266   7758   -280    235    881       C  
ATOM   4183  CD  LYS A 793     -40.547   2.040  55.150  1.00 73.81           C  
ANISOU 4183  CD  LYS A 793     9605   8924   9515   -204    291    906       C  
ATOM   4184  CE  LYS A 793     -41.083   0.850  54.371  1.00 75.49           C  
ANISOU 4184  CE  LYS A 793     9970   8945   9765   -226    386    896       C  
ATOM   4185  NZ  LYS A 793     -40.231   0.593  53.176  1.00 70.27           N  
ANISOU 4185  NZ  LYS A 793     9367   8208   9126   -170    427    896       N  
ATOM   4186  N   TYR A 794     -43.192   4.469  58.249  1.00 55.68           N  
ANISOU 4186  N   TYR A 794     7043   6959   7153   -446     58    784       N  
ATOM   4187  CA  TYR A 794     -43.072   5.915  58.179  1.00 53.70           C  
ANISOU 4187  CA  TYR A 794     6696   6816   6890   -489    -29    711       C  
ATOM   4188  C   TYR A 794     -43.364   6.578  59.521  1.00 50.59           C  
ANISOU 4188  C   TYR A 794     6196   6567   6460   -519    -81    715       C  
ATOM   4189  O   TYR A 794     -44.512   6.673  59.940  1.00 47.68           O  
ANISOU 4189  O   TYR A 794     5832   6191   6095   -593   -107    675       O  
ATOM   4190  CB  TYR A 794     -43.935   6.519  57.070  1.00 49.21           C  
ANISOU 4190  CB  TYR A 794     6170   6174   6353   -579    -66    597       C  
ATOM   4191  CG  TYR A 794     -43.378   7.847  56.620  1.00 57.02           C  
ANISOU 4191  CG  TYR A 794     7090   7239   7337   -587   -124    541       C  
ATOM   4192  CD1 TYR A 794     -42.564   7.933  55.497  1.00 56.22           C  
ANISOU 4192  CD1 TYR A 794     7019   7090   7252   -549   -108    530       C  
ATOM   4193  CD2 TYR A 794     -43.618   9.007  57.348  1.00 55.48           C  
ANISOU 4193  CD2 TYR A 794     6802   7161   7118   -633   -186    500       C  
ATOM   4194  CE1 TYR A 794     -42.029   9.143  55.095  1.00 55.90           C  
ANISOU 4194  CE1 TYR A 794     6919   7114   7205   -558   -153    479       C  
ATOM   4195  CE2 TYR A 794     -43.086  10.225  56.957  1.00 56.71           C  
ANISOU 4195  CE2 TYR A 794     6903   7376   7267   -644   -224    447       C  
ATOM   4196  CZ  TYR A 794     -42.291  10.286  55.827  1.00 64.84           C  
ANISOU 4196  CZ  TYR A 794     7967   8355   8315   -607   -207    437       C  
ATOM   4197  OH  TYR A 794     -41.755  11.489  55.427  1.00 73.83           O  
ANISOU 4197  OH  TYR A 794     9058   9546   9447   -622   -237    385       O  
ATOM   4198  N   GLN A 795     -42.314   7.030  60.194  1.00 55.52           N  
ANISOU 4198  N   GLN A 795     6721   7331   7045   -463    -95    762       N  
ATOM   4199  CA  GLN A 795     -42.475   7.681  61.490  1.00 59.13           C  
ANISOU 4199  CA  GLN A 795     7068   7939   7461   -493   -141    764       C  
ATOM   4200  C   GLN A 795     -42.153   9.169  61.419  1.00 44.99           C  
ANISOU 4200  C   GLN A 795     5189   6251   5653   -544   -203    683       C  
ATOM   4201  O   GLN A 795     -40.994   9.563  61.321  1.00 46.66           O  
ANISOU 4201  O   GLN A 795     5343   6547   5838   -501   -201    699       O  
ATOM   4202  CB  GLN A 795     -41.584   7.034  62.551  1.00 67.37           C  
ANISOU 4202  CB  GLN A 795     8048   9094   8455   -397   -103    884       C  
ATOM   4203  CG  GLN A 795     -41.758   5.539  62.737  1.00 76.72           C  
ANISOU 4203  CG  GLN A 795     9320  10178   9650   -329    -23    981       C  
ATOM   4204  CD  GLN A 795     -41.086   5.054  64.016  1.00 83.06           C  
ANISOU 4204  CD  GLN A 795    10044  11121  10395   -239      7   1101       C  
ATOM   4205  OE1 GLN A 795     -41.568   5.316  65.125  1.00 84.36           O  
ANISOU 4205  OE1 GLN A 795    10135  11387  10530   -275    -25   1105       O  
ATOM   4206  NE2 GLN A 795     -39.962   4.356  63.869  1.00 78.28           N  
ANISOU 4206  NE2 GLN A 795     9446  10531   9768   -117     70   1200       N  
ATOM   4207  N   SER A 796     -43.186   9.990  61.478  1.00 45.71           N  
ANISOU 4207  N   SER A 796     5272   6338   5757   -635   -252    596       N  
ATOM   4208  CA  SER A 796     -43.009  11.423  61.560  1.00 44.80           C  
ANISOU 4208  CA  SER A 796     5082   6315   5626   -689   -299    519       C  
ATOM   4209  C   SER A 796     -44.139  11.997  62.402  1.00 46.56           C  
ANISOU 4209  C   SER A 796     5269   6582   5840   -767   -339    471       C  
ATOM   4210  O   SER A 796     -45.256  11.504  62.366  1.00 42.04           O  
ANISOU 4210  O   SER A 796     4754   5931   5289   -797   -342    463       O  
ATOM   4211  CB  SER A 796     -43.038  12.038  60.170  1.00 47.40           C  
ANISOU 4211  CB  SER A 796     5469   6549   5991   -712   -306    444       C  
ATOM   4212  OG  SER A 796     -42.894  13.444  60.246  1.00 58.09           O  
ANISOU 4212  OG  SER A 796     6762   7977   7331   -764   -339    370       O  
ATOM   4213  N   SER A 797     -43.847  13.042  63.158  1.00 47.77           N  
ANISOU 4213  N   SER A 797     5326   6866   5958   -804   -367    436       N  
ATOM   4214  CA  SER A 797     -44.868  13.678  63.972  1.00 44.58           C  
ANISOU 4214  CA  SER A 797     4884   6509   5544   -876   -403    387       C  
ATOM   4215  C   SER A 797     -45.769  14.576  63.123  1.00 46.53           C  
ANISOU 4215  C   SER A 797     5184   6672   5824   -934   -426    292       C  
ATOM   4216  O   SER A 797     -46.830  14.978  63.568  1.00 52.21           O  
ANISOU 4216  O   SER A 797     5896   7399   6541   -987   -452    252       O  
ATOM   4217  CB  SER A 797     -44.243  14.462  65.132  1.00 37.21           C  
ANISOU 4217  CB  SER A 797     3831   5750   4558   -900   -416    380       C  
ATOM   4218  OG  SER A 797     -43.290  15.421  64.682  1.00 41.69           O  
ANISOU 4218  OG  SER A 797     4365   6363   5113   -913   -409    332       O  
ATOM   4219  N   THR A 798     -45.350  14.893  61.903  1.00 58.26           N  
ANISOU 4219  N   THR A 798     6719   8082   7335   -919   -414    260       N  
ATOM   4220  CA  THR A 798     -46.198  15.691  61.008  1.00 55.19           C  
ANISOU 4220  CA  THR A 798     6381   7615   6973   -959   -429    180       C  
ATOM   4221  C   THR A 798     -46.766  14.881  59.843  1.00 49.18           C  
ANISOU 4221  C   THR A 798     5716   6722   6246   -940   -418    184       C  
ATOM   4222  O   THR A 798     -47.318  15.443  58.906  1.00 50.52           O  
ANISOU 4222  O   THR A 798     5929   6832   6434   -958   -425    127       O  
ATOM   4223  CB  THR A 798     -45.484  16.955  60.476  1.00 49.62           C  
ANISOU 4223  CB  THR A 798     5658   6928   6266   -971   -422    121       C  
ATOM   4224  OG1 THR A 798     -44.244  16.588  59.853  1.00 48.91           O  
ANISOU 4224  OG1 THR A 798     5577   6827   6180   -920   -397    155       O  
ATOM   4225  CG2 THR A 798     -45.228  17.944  61.619  1.00 46.91           C  
ANISOU 4225  CG2 THR A 798     5227   6711   5886  -1018   -428     90       C  
ATOM   4226  N   LYS A 799     -46.627  13.563  59.927  1.00 46.39           N  
ANISOU 4226  N   LYS A 799     5397   6331   5899   -903   -394    252       N  
ATOM   4227  CA  LYS A 799     -47.268  12.630  59.012  1.00 43.76           C  
ANISOU 4227  CA  LYS A 799     5156   5878   5593   -901   -375    254       C  
ATOM   4228  C   LYS A 799     -48.627  13.150  58.555  1.00 56.59           C  
ANISOU 4228  C   LYS A 799     6808   7474   7222   -961   -402    181       C  
ATOM   4229  O   LYS A 799     -48.854  13.391  57.368  1.00 60.43           O  
ANISOU 4229  O   LYS A 799     7340   7895   7724   -964   -400    137       O  
ATOM   4230  CB  LYS A 799     -47.465  11.278  59.715  1.00 51.75           C  
ANISOU 4230  CB  LYS A 799     6191   6871   6600   -885   -346    326       C  
ATOM   4231  CG  LYS A 799     -47.591  10.088  58.776  1.00 58.12           C  
ANISOU 4231  CG  LYS A 799     7099   7549   7433   -867   -298    347       C  
ATOM   4232  CD  LYS A 799     -48.028   8.811  59.487  1.00 61.22           C  
ANISOU 4232  CD  LYS A 799     7531   7909   7822   -865   -259    408       C  
ATOM   4233  CE  LYS A 799     -47.421   8.676  60.869  1.00 76.01           C  
ANISOU 4233  CE  LYS A 799     9329   9884   9666   -822   -257    485       C  
ATOM   4234  NZ  LYS A 799     -45.933   8.733  60.870  1.00 89.89           N  
ANISOU 4234  NZ  LYS A 799    11048  11691  11415   -739   -237    541       N  
ATOM   4235  N   GLY A 800     -49.530  13.326  59.512  1.00 48.23           N  
ANISOU 4235  N   GLY A 800     5712   6472   6142  -1004   -428    170       N  
ATOM   4236  CA  GLY A 800     -50.896  13.695  59.211  1.00 33.32           C  
ANISOU 4236  CA  GLY A 800     3841   4573   4247  -1055   -453    111       C  
ATOM   4237  C   GLY A 800     -51.089  15.051  58.564  1.00 44.16           C  
ANISOU 4237  C   GLY A 800     5202   5959   5618  -1062   -472     46       C  
ATOM   4238  O   GLY A 800     -51.969  15.199  57.717  1.00 51.67           O  
ANISOU 4238  O   GLY A 800     6189   6877   6567  -1079   -478      4       O  
ATOM   4239  N   GLN A 801     -50.310  16.051  58.959  1.00 44.34           N  
ANISOU 4239  N   GLN A 801     5175   6036   5638  -1050   -475     36       N  
ATOM   4240  CA  GLN A 801     -50.467  17.362  58.336  1.00 58.93           C  
ANISOU 4240  CA  GLN A 801     7022   7882   7486  -1052   -478    -23       C  
ATOM   4241  C   GLN A 801     -49.907  17.363  56.904  1.00 57.34           C  
ANISOU 4241  C   GLN A 801     6875   7603   7309  -1017   -456    -33       C  
ATOM   4242  O   GLN A 801     -50.300  18.187  56.072  1.00 54.99           O  
ANISOU 4242  O   GLN A 801     6600   7282   7012  -1011   -454    -77       O  
ATOM   4243  CB  GLN A 801     -49.855  18.497  59.178  1.00 71.34           C  
ANISOU 4243  CB  GLN A 801     8533   9529   9045  -1065   -476    -43       C  
ATOM   4244  CG  GLN A 801     -49.917  19.862  58.462  1.00 87.37           C  
ANISOU 4244  CG  GLN A 801    10579  11537  11078  -1062   -460   -102       C  
ATOM   4245  CD  GLN A 801     -49.255  21.007  59.226  1.00 99.14           C  
ANISOU 4245  CD  GLN A 801    12021  13091  12556  -1087   -442   -132       C  
ATOM   4246  OE1 GLN A 801     -48.236  20.827  59.902  1.00103.52           O  
ANISOU 4246  OE1 GLN A 801    12529  13704  13102  -1095   -436   -110       O  
ATOM   4247  NE2 GLN A 801     -49.832  22.201  59.106  1.00 97.30           N  
ANISOU 4247  NE2 GLN A 801    11800  12853  12318  -1099   -426   -184       N  
ATOM   4248  N   GLN A 802     -48.994  16.439  56.620  1.00 49.16           N  
ANISOU 4248  N   GLN A 802     5860   6529   6288   -986   -437     11       N  
ATOM   4249  CA  GLN A 802     -48.463  16.316  55.267  1.00 51.73           C  
ANISOU 4249  CA  GLN A 802     6238   6780   6637   -953   -417      4       C  
ATOM   4250  C   GLN A 802     -49.526  15.703  54.363  1.00 54.44           C  
ANISOU 4250  C   GLN A 802     6639   7064   6983   -968   -417    -16       C  
ATOM   4251  O   GLN A 802     -49.807  16.242  53.288  1.00 57.09           O  
ANISOU 4251  O   GLN A 802     7000   7370   7321   -961   -416    -55       O  
ATOM   4252  CB  GLN A 802     -47.156  15.506  55.222  1.00 48.96           C  
ANISOU 4252  CB  GLN A 802     5893   6410   6300   -911   -392     59       C  
ATOM   4253  CG  GLN A 802     -45.919  16.270  55.723  1.00 39.53           C  
ANISOU 4253  CG  GLN A 802     4639   5284   5094   -895   -386     66       C  
ATOM   4254  CD  GLN A 802     -44.643  15.418  55.711  1.00 55.58           C  
ANISOU 4254  CD  GLN A 802     6671   7319   7130   -842   -361    130       C  
ATOM   4255  OE1 GLN A 802     -44.171  14.977  54.643  1.00 61.60           O  
ANISOU 4255  OE1 GLN A 802     7484   8009   7913   -807   -341    138       O  
ATOM   4256  NE2 GLN A 802     -44.066  15.200  56.897  1.00 45.34           N  
ANISOU 4256  NE2 GLN A 802     5309   6114   5805   -833   -360    176       N  
ATOM   4257  N   ILE A 803     -50.124  14.593  54.808  1.00 41.00           N  
ANISOU 4257  N   ILE A 803     4953   5350   5274   -992   -415      9       N  
ATOM   4258  CA  ILE A 803     -51.180  13.940  54.044  1.00 39.29           C  
ANISOU 4258  CA  ILE A 803     4787   5091   5051  -1025   -410    -18       C  
ATOM   4259  C   ILE A 803     -52.252  14.969  53.718  1.00 50.10           C  
ANISOU 4259  C   ILE A 803     6135   6508   6394  -1046   -438    -74       C  
ATOM   4260  O   ILE A 803     -52.621  15.160  52.563  1.00 51.71           O  
ANISOU 4260  O   ILE A 803     6365   6690   6591  -1042   -433   -109       O  
ATOM   4261  CB  ILE A 803     -51.874  12.817  54.829  1.00 36.88           C  
ANISOU 4261  CB  ILE A 803     4494   4784   4733  -1065   -403      7       C  
ATOM   4262  CG1 ILE A 803     -50.898  11.730  55.263  1.00 45.04           C  
ANISOU 4262  CG1 ILE A 803     5554   5773   5788  -1033   -365     75       C  
ATOM   4263  CG2 ILE A 803     -52.991  12.212  54.012  1.00 39.96           C  
ANISOU 4263  CG2 ILE A 803     4931   5144   5106  -1115   -393    -35       C  
ATOM   4264  CD1 ILE A 803     -50.263  10.999  54.158  1.00 53.08           C  
ANISOU 4264  CD1 ILE A 803     6638   6698   6830  -1006   -322     85       C  
ATOM   4265  N   ASP A 804     -52.752  15.634  54.750  1.00 46.41           N  
ANISOU 4265  N   ASP A 804     5616   6110   5906  -1063   -463    -80       N  
ATOM   4266  CA  ASP A 804     -53.845  16.581  54.570  1.00 51.47           C  
ANISOU 4266  CA  ASP A 804     6237   6803   6517  -1075   -483   -125       C  
ATOM   4267  C   ASP A 804     -53.483  17.618  53.524  1.00 47.75           C  
ANISOU 4267  C   ASP A 804     5778   6313   6053  -1031   -471   -151       C  
ATOM   4268  O   ASP A 804     -54.269  17.904  52.615  1.00 55.84           O  
ANISOU 4268  O   ASP A 804     6815   7346   7054  -1024   -472   -181       O  
ATOM   4269  CB  ASP A 804     -54.197  17.269  55.890  1.00 42.15           C  
ANISOU 4269  CB  ASP A 804     5001   5696   5319  -1091   -505   -125       C  
ATOM   4270  CG  ASP A 804     -54.839  16.319  56.883  1.00 59.87           C  
ANISOU 4270  CG  ASP A 804     7231   7969   7547  -1136   -520   -104       C  
ATOM   4271  OD1 ASP A 804     -55.496  15.334  56.453  1.00 64.55           O  
ANISOU 4271  OD1 ASP A 804     7858   8539   8128  -1167   -515   -107       O  
ATOM   4272  OD2 ASP A 804     -54.692  16.563  58.100  1.00 68.55           O  
ANISOU 4272  OD2 ASP A 804     8285   9119   8643  -1147   -533    -86       O  
ATOM   4273  N   SER A 805     -52.287  18.173  53.671  1.00 41.07           N  
ANISOU 4273  N   SER A 805     4923   5449   5233  -1002   -457   -139       N  
ATOM   4274  CA  SER A 805     -51.777  19.216  52.794  1.00 40.17           C  
ANISOU 4274  CA  SER A 805     4823   5311   5130   -963   -437   -161       C  
ATOM   4275  C   SER A 805     -51.677  18.753  51.337  1.00 42.08           C  
ANISOU 4275  C   SER A 805     5112   5496   5381   -940   -424   -167       C  
ATOM   4276  O   SER A 805     -51.860  19.543  50.417  1.00 44.90           O  
ANISOU 4276  O   SER A 805     5482   5846   5731   -909   -412   -190       O  
ATOM   4277  CB  SER A 805     -50.406  19.661  53.296  1.00 39.83           C  
ANISOU 4277  CB  SER A 805     4760   5264   5108   -952   -421   -148       C  
ATOM   4278  OG  SER A 805     -49.872  20.678  52.469  1.00 55.70           O  
ANISOU 4278  OG  SER A 805     6790   7246   7129   -921   -395   -172       O  
ATOM   4279  N   LEU A 806     -51.382  17.471  51.146  1.00 36.39           N  
ANISOU 4279  N   LEU A 806     4417   4736   4674   -953   -421   -144       N  
ATOM   4280  CA  LEU A 806     -51.299  16.882  49.823  1.00 38.63           C  
ANISOU 4280  CA  LEU A 806     4746   4966   4965   -941   -405   -153       C  
ATOM   4281  C   LEU A 806     -52.712  16.699  49.276  1.00 46.77           C  
ANISOU 4281  C   LEU A 806     5783   6033   5957   -970   -415   -187       C  
ATOM   4282  O   LEU A 806     -52.970  16.912  48.082  1.00 50.79           O  
ANISOU 4282  O   LEU A 806     6307   6537   6452   -953   -406   -211       O  
ATOM   4283  CB  LEU A 806     -50.562  15.533  49.858  1.00 30.35           C  
ANISOU 4283  CB  LEU A 806     3732   3858   3942   -946   -385   -117       C  
ATOM   4284  CG  LEU A 806     -49.066  15.507  50.194  1.00 37.29           C  
ANISOU 4284  CG  LEU A 806     4606   4713   4851   -908   -371    -77       C  
ATOM   4285  CD1 LEU A 806     -48.636  14.107  50.594  1.00 36.46           C  
ANISOU 4285  CD1 LEU A 806     4527   4566   4759   -909   -348    -30       C  
ATOM   4286  CD2 LEU A 806     -48.209  16.004  49.026  1.00 37.03           C  
ANISOU 4286  CD2 LEU A 806     4593   4640   4837   -867   -355    -89       C  
ATOM   4287  N   LYS A 807     -53.630  16.310  50.155  1.00 46.92           N  
ANISOU 4287  N   LYS A 807     5781   6098   5950  -1015   -432   -188       N  
ATOM   4288  CA  LYS A 807     -55.023  16.110  49.761  1.00 44.87           C  
ANISOU 4288  CA  LYS A 807     5514   5894   5640  -1052   -442   -222       C  
ATOM   4289  C   LYS A 807     -55.681  17.432  49.404  1.00 44.92           C  
ANISOU 4289  C   LYS A 807     5488   5967   5613  -1014   -453   -244       C  
ATOM   4290  O   LYS A 807     -56.588  17.478  48.576  1.00 53.43           O  
ANISOU 4290  O   LYS A 807     6560   7096   6645  -1017   -454   -272       O  
ATOM   4291  CB  LYS A 807     -55.804  15.386  50.860  1.00 44.28           C  
ANISOU 4291  CB  LYS A 807     5425   5855   5545  -1111   -456   -217       C  
ATOM   4292  CG  LYS A 807     -55.467  13.911  50.960  1.00 46.64           C  
ANISOU 4292  CG  LYS A 807     5770   6086   5865  -1152   -430   -199       C  
ATOM   4293  CD  LYS A 807     -56.211  13.253  52.088  1.00 49.72           C  
ANISOU 4293  CD  LYS A 807     6149   6508   6235  -1209   -438   -190       C  
ATOM   4294  CE  LYS A 807     -55.913  11.759  52.147  1.00 59.36           C  
ANISOU 4294  CE  LYS A 807     7429   7649   7475  -1247   -396   -170       C  
ATOM   4295  NZ  LYS A 807     -56.704  11.099  53.240  1.00 67.54           N  
ANISOU 4295  NZ  LYS A 807     8458   8714   8489  -1306   -398   -161       N  
ATOM   4296  N   ASN A 808     -55.210  18.510  50.017  1.00 40.90           N  
ANISOU 4296  N   ASN A 808     4959   5461   5121   -976   -454   -232       N  
ATOM   4297  CA  ASN A 808     -55.688  19.835  49.654  1.00 46.76           C  
ANISOU 4297  CA  ASN A 808     5685   6245   5837   -927   -447   -246       C  
ATOM   4298  C   ASN A 808     -55.316  20.202  48.211  1.00 52.87           C  
ANISOU 4298  C   ASN A 808     6486   6988   6614   -878   -423   -254       C  
ATOM   4299  O   ASN A 808     -56.174  20.609  47.429  1.00 60.79           O  
ANISOU 4299  O   ASN A 808     7479   8047   7572   -850   -419   -267       O  
ATOM   4300  CB  ASN A 808     -55.162  20.883  50.631  1.00 53.56           C  
ANISOU 4300  CB  ASN A 808     6530   7102   6719   -908   -439   -238       C  
ATOM   4301  CG  ASN A 808     -55.896  22.203  50.514  1.00 66.09           C  
ANISOU 4301  CG  ASN A 808     8105   8734   8273   -862   -422   -250       C  
ATOM   4302  OD1 ASN A 808     -55.306  23.231  50.155  1.00 71.79           O  
ANISOU 4302  OD1 ASN A 808     8846   9418   9012   -816   -387   -252       O  
ATOM   4303  ND2 ASN A 808     -57.196  22.183  50.805  1.00 63.17           N  
ANISOU 4303  ND2 ASN A 808     7706   8443   7852   -872   -442   -258       N  
ATOM   4304  N   VAL A 809     -54.043  20.043  47.860  1.00 49.10           N  
ANISOU 4304  N   VAL A 809     6038   6433   6185   -864   -407   -242       N  
ATOM   4305  CA  VAL A 809     -53.567  20.317  46.509  1.00 37.36           C  
ANISOU 4305  CA  VAL A 809     4578   4911   4706   -820   -385   -248       C  
ATOM   4306  C   VAL A 809     -54.361  19.509  45.468  1.00 45.08           C  
ANISOU 4306  C   VAL A 809     5560   5921   5647   -838   -390   -267       C  
ATOM   4307  O   VAL A 809     -54.906  20.073  44.520  1.00 38.91           O  
ANISOU 4307  O   VAL A 809     4771   5184   4829   -799   -380   -278       O  
ATOM   4308  CB  VAL A 809     -52.062  20.013  46.423  1.00 40.98           C  
ANISOU 4308  CB  VAL A 809     5064   5288   5220   -815   -371   -231       C  
ATOM   4309  CG1 VAL A 809     -51.520  20.237  44.999  1.00 39.50           C  
ANISOU 4309  CG1 VAL A 809     4905   5061   5042   -772   -349   -237       C  
ATOM   4310  CG2 VAL A 809     -51.299  20.866  47.440  1.00 28.05           C  
ANISOU 4310  CG2 VAL A 809     3412   3641   3606   -808   -362   -221       C  
ATOM   4311  N   ALA A 810     -54.442  18.195  45.680  1.00 47.37           N  
ANISOU 4311  N   ALA A 810     5862   6194   5941   -899   -399   -271       N  
ATOM   4312  CA  ALA A 810     -55.251  17.289  44.856  1.00 42.84           C  
ANISOU 4312  CA  ALA A 810     5294   5657   5327   -942   -398   -300       C  
ATOM   4313  C   ALA A 810     -56.670  17.791  44.682  1.00 53.67           C  
ANISOU 4313  C   ALA A 810     6620   7147   6624   -942   -411   -322       C  
ATOM   4314  O   ALA A 810     -57.242  17.726  43.591  1.00 61.45           O  
ANISOU 4314  O   ALA A 810     7594   8190   7562   -940   -404   -347       O  
ATOM   4315  CB  ALA A 810     -55.299  15.891  45.476  1.00 35.20           C  
ANISOU 4315  CB  ALA A 810     4350   4654   4371  -1017   -396   -301       C  
ATOM   4316  N   ARG A 811     -57.247  18.263  45.777  1.00 48.08           N  
ANISOU 4316  N   ARG A 811     5882   6487   5901   -945   -429   -313       N  
ATOM   4317  CA  ARG A 811     -58.652  18.632  45.793  1.00 47.96           C  
ANISOU 4317  CA  ARG A 811     5819   6595   5809   -947   -443   -330       C  
ATOM   4318  C   ARG A 811     -58.852  19.868  44.937  1.00 44.46           C  
ANISOU 4318  C   ARG A 811     5359   6199   5335   -858   -427   -322       C  
ATOM   4319  O   ARG A 811     -59.788  19.943  44.147  1.00 53.56           O  
ANISOU 4319  O   ARG A 811     6479   7455   6417   -846   -426   -338       O  
ATOM   4320  CB  ARG A 811     -59.117  18.886  47.232  1.00 43.39           C  
ANISOU 4320  CB  ARG A 811     5215   6047   5226   -966   -465   -318       C  
ATOM   4321  CG  ARG A 811     -60.508  19.458  47.353  1.00 59.72           C  
ANISOU 4321  CG  ARG A 811     7231   8246   7215   -952   -478   -329       C  
ATOM   4322  CD  ARG A 811     -60.829  19.852  48.806  1.00 65.67           C  
ANISOU 4322  CD  ARG A 811     7961   9018   7973   -962   -496   -315       C  
ATOM   4323  N   GLN A 812     -57.961  20.835  45.099  1.00 35.82           N  
ANISOU 4323  N   GLN A 812     4286   5033   4289   -796   -409   -297       N  
ATOM   4324  CA  GLN A 812     -58.011  22.068  44.329  1.00 49.69           C  
ANISOU 4324  CA  GLN A 812     6042   6811   6027   -704   -379   -283       C  
ATOM   4325  C   GLN A 812     -57.661  21.873  42.846  1.00 56.84           C  
ANISOU 4325  C   GLN A 812     6963   7708   6927   -676   -362   -289       C  
ATOM   4326  O   GLN A 812     -58.140  22.619  41.983  1.00 55.42           O  
ANISOU 4326  O   GLN A 812     6767   7592   6700   -605   -342   -280       O  
ATOM   4327  CB  GLN A 812     -57.083  23.106  44.953  1.00 60.34           C  
ANISOU 4327  CB  GLN A 812     7420   8076   7432   -662   -353   -263       C  
ATOM   4328  CG  GLN A 812     -57.466  23.476  46.370  1.00 77.96           C  
ANISOU 4328  CG  GLN A 812     9633  10327   9663   -682   -363   -260       C  
ATOM   4329  CD  GLN A 812     -56.479  24.423  47.003  1.00 83.75           C  
ANISOU 4329  CD  GLN A 812    10393  10980  10449   -661   -332   -252       C  
ATOM   4330  OE1 GLN A 812     -56.720  24.954  48.087  1.00 84.78           O  
ANISOU 4330  OE1 GLN A 812    10511  11124  10579   -670   -328   -252       O  
ATOM   4331  NE2 GLN A 812     -55.355  24.643  46.327  1.00 84.77           N  
ANISOU 4331  NE2 GLN A 812    10558  11030  10621   -639   -305   -249       N  
ATOM   4332  N   CYS A 813     -56.812  20.890  42.552  1.00 50.31           N  
ANISOU 4332  N   CYS A 813     6166   6804   6145   -726   -367   -301       N  
ATOM   4333  CA  CYS A 813     -56.484  20.592  41.166  1.00 48.75           C  
ANISOU 4333  CA  CYS A 813     5982   6599   5942   -710   -353   -312       C  
ATOM   4334  C   CYS A 813     -57.722  20.009  40.515  1.00 46.11           C  
ANISOU 4334  C   CYS A 813     5606   6390   5525   -745   -363   -341       C  
ATOM   4335  O   CYS A 813     -58.001  20.276  39.356  1.00 37.94           O  
ANISOU 4335  O   CYS A 813     4552   5419   4446   -704   -349   -346       O  
ATOM   4336  CB  CYS A 813     -55.312  19.619  41.055  1.00 37.24           C  
ANISOU 4336  CB  CYS A 813     4569   5030   4550   -755   -351   -317       C  
ATOM   4337  SG  CYS A 813     -53.717  20.400  41.398  1.00 53.28           S  
ANISOU 4337  SG  CYS A 813     6639   6941   6663   -705   -333   -286       S  
ATOM   4338  N   MET A 814     -58.471  19.231  41.286  1.00 36.87           N  
ANISOU 4338  N   MET A 814     4417   5265   4328   -823   -385   -362       N  
ATOM   4339  CA  MET A 814     -59.676  18.600  40.786  1.00 38.11           C  
ANISOU 4339  CA  MET A 814     4530   5553   4398   -877   -392   -399       C  
ATOM   4340  C   MET A 814     -60.754  19.600  40.409  1.00 44.76           C  
ANISOU 4340  C   MET A 814     5310   6544   5152   -805   -392   -388       C  
ATOM   4341  O   MET A 814     -61.381  19.457  39.352  1.00 52.59           O  
ANISOU 4341  O   MET A 814     6262   7650   6069   -804   -385   -409       O  
ATOM   4342  CB  MET A 814     -60.222  17.577  41.773  1.00 45.77           C  
ANISOU 4342  CB  MET A 814     5499   6532   5359   -980   -410   -424       C  
ATOM   4343  CG  MET A 814     -59.593  16.214  41.617  1.00 52.67           C  
ANISOU 4343  CG  MET A 814     6425   7309   6277  -1065   -395   -450       C  
ATOM   4344  SD  MET A 814     -59.092  15.918  39.908  1.00 73.17           S  
ANISOU 4344  SD  MET A 814     9040   9894   8867  -1055   -366   -475       S  
ATOM   4345  CE  MET A 814     -59.338  14.149  39.808  1.00 82.18           C  
ANISOU 4345  CE  MET A 814    10218  11007   9998  -1197   -341   -533       C  
ATOM   4346  N   ILE A 815     -60.970  20.624  41.229  1.00 39.34           N  
ANISOU 4346  N   ILE A 815     4613   5867   4469   -742   -394   -353       N  
ATOM   4347  CA  ILE A 815     -61.988  21.597  40.853  1.00 43.29           C  
ANISOU 4347  CA  ILE A 815     5059   6507   4881   -658   -384   -333       C  
ATOM   4348  C   ILE A 815     -61.505  22.391  39.642  1.00 45.66           C  
ANISOU 4348  C   ILE A 815     5369   6798   5181   -558   -349   -307       C  
ATOM   4349  O   ILE A 815     -62.268  22.637  38.697  1.00 48.27           O  
ANISOU 4349  O   ILE A 815     5650   7267   5425   -510   -338   -304       O  
ATOM   4350  CB  ILE A 815     -62.399  22.535  41.988  1.00 46.26           C  
ANISOU 4350  CB  ILE A 815     5426   6894   5256   -608   -383   -303       C  
ATOM   4351  CG1 ILE A 815     -61.438  23.720  42.053  1.00 57.38           C  
ANISOU 4351  CG1 ILE A 815     6885   8185   6732   -516   -345   -263       C  
ATOM   4352  CG2 ILE A 815     -62.507  21.763  43.338  1.00 54.79           C  
ANISOU 4352  CG2 ILE A 815     6511   7940   6366   -708   -418   -323       C  
ATOM   4353  CD1 ILE A 815     -62.047  24.955  42.667  1.00 65.12           C  
ANISOU 4353  CD1 ILE A 815     7853   9207   7682   -431   -320   -229       C  
ATOM   4354  N   TYR A 816     -60.232  22.769  39.669  1.00 48.85           N  
ANISOU 4354  N   TYR A 816     5836   7049   5677   -528   -329   -289       N  
ATOM   4355  CA  TYR A 816     -59.581  23.411  38.538  1.00 49.34           C  
ANISOU 4355  CA  TYR A 816     5920   7076   5753   -446   -294   -267       C  
ATOM   4356  C   TYR A 816     -59.752  22.552  37.278  1.00 53.35           C  
ANISOU 4356  C   TYR A 816     6400   7655   6215   -482   -301   -298       C  
ATOM   4357  O   TYR A 816     -60.231  23.024  36.245  1.00 53.36           O  
ANISOU 4357  O   TYR A 816     6364   7761   6148   -412   -282   -283       O  
ATOM   4358  CB  TYR A 816     -58.100  23.626  38.857  1.00 43.83           C  
ANISOU 4358  CB  TYR A 816     5291   6201   5162   -446   -280   -257       C  
ATOM   4359  CG  TYR A 816     -57.256  24.140  37.703  1.00 45.15           C  
ANISOU 4359  CG  TYR A 816     5488   6312   5353   -379   -245   -241       C  
ATOM   4360  CD1 TYR A 816     -57.133  25.498  37.454  1.00 53.11           C  
ANISOU 4360  CD1 TYR A 816     6516   7305   6360   -272   -196   -201       C  
ATOM   4361  CD2 TYR A 816     -56.571  23.265  36.875  1.00 36.19           C  
ANISOU 4361  CD2 TYR A 816     4369   5137   4245   -422   -255   -264       C  
ATOM   4362  CE1 TYR A 816     -56.354  25.973  36.402  1.00 43.42           C  
ANISOU 4362  CE1 TYR A 816     5318   6024   5155   -212   -161   -185       C  
ATOM   4363  CE2 TYR A 816     -55.796  23.727  35.816  1.00 41.22           C  
ANISOU 4363  CE2 TYR A 816     5031   5727   4904   -362   -225   -249       C  
ATOM   4364  CZ  TYR A 816     -55.689  25.080  35.588  1.00 39.41           C  
ANISOU 4364  CZ  TYR A 816     4817   5485   4671   -258   -180   -209       C  
ATOM   4365  OH  TYR A 816     -54.899  25.547  34.556  1.00 38.85           O  
ANISOU 4365  OH  TYR A 816     4775   5364   4623   -201   -147   -193       O  
ATOM   4366  N   ALA A 817     -59.390  21.279  37.389  1.00 42.05           N  
ANISOU 4366  N   ALA A 817     4989   6171   4818   -591   -324   -340       N  
ATOM   4367  CA  ALA A 817     -59.520  20.342  36.292  1.00 42.62           C  
ANISOU 4367  CA  ALA A 817     5044   6298   4852   -647   -324   -381       C  
ATOM   4368  C   ALA A 817     -60.941  20.344  35.718  1.00 56.50           C  
ANISOU 4368  C   ALA A 817     6719   8266   6483   -647   -328   -399       C  
ATOM   4369  O   ALA A 817     -61.128  20.356  34.503  1.00 62.41           O  
ANISOU 4369  O   ALA A 817     7433   9105   7176   -622   -314   -408       O  
ATOM   4370  CB  ALA A 817     -59.129  18.951  36.741  1.00 33.71           C  
ANISOU 4370  CB  ALA A 817     3953   5085   3770   -770   -337   -423       C  
ATOM   4371  N   GLY A 818     -61.935  20.335  36.600  1.00 62.15           N  
ANISOU 4371  N   GLY A 818     7395   9070   7148   -674   -346   -403       N  
ATOM   4372  CA  GLY A 818     -63.328  20.224  36.197  1.00 49.51           C  
ANISOU 4372  CA  GLY A 818     5708   7686   5418   -689   -353   -425       C  
ATOM   4373  C   GLY A 818     -63.842  21.431  35.446  1.00 47.18           C  
ANISOU 4373  C   GLY A 818     5360   7521   5046   -549   -331   -375       C  
ATOM   4374  O   GLY A 818     -64.618  21.294  34.503  1.00 63.37           O  
ANISOU 4374  O   GLY A 818     7338   9752   6990   -545   -325   -392       O  
ATOM   4375  N   MET A 819     -63.407  22.613  35.864  1.00 42.58           N  
ANISOU 4375  N   MET A 819     4813   6852   4514   -435   -310   -314       N  
ATOM   4376  CA  MET A 819     -63.726  23.853  35.168  1.00 45.16           C  
ANISOU 4376  CA  MET A 819     5110   7265   4783   -284   -272   -254       C  
ATOM   4377  C   MET A 819     -63.084  23.945  33.762  1.00 55.60           C  
ANISOU 4377  C   MET A 819     6439   8578   6108   -237   -247   -247       C  
ATOM   4378  O   MET A 819     -63.558  24.699  32.910  1.00 54.24           O  
ANISOU 4378  O   MET A 819     6221   8530   5857   -125   -216   -205       O  
ATOM   4379  CB  MET A 819     -63.279  25.054  36.001  1.00 48.98           C  
ANISOU 4379  CB  MET A 819     5652   7623   5334   -188   -242   -198       C  
ATOM   4380  CG  MET A 819     -63.820  25.072  37.430  1.00 59.59           C  
ANISOU 4380  CG  MET A 819     6993   8965   6683   -227   -265   -203       C  
ATOM   4381  SD  MET A 819     -63.199  26.460  38.401  1.00 70.08           S  
ANISOU 4381  SD  MET A 819     8396  10137   8094   -132   -220   -150       S  
ATOM   4382  CE  MET A 819     -64.119  27.818  37.680  1.00 73.09           C  
ANISOU 4382  CE  MET A 819     8739  10660   8371     48   -158    -79       C  
ATOM   4383  N   ILE A 820     -61.998  23.207  33.536  1.00 43.90           N  
ANISOU 4383  N   ILE A 820     5014   6951   4714   -314   -256   -282       N  
ATOM   4384  CA  ILE A 820     -61.337  23.212  32.238  1.00 51.15           C  
ANISOU 4384  CA  ILE A 820     5941   7854   5641   -280   -235   -280       C  
ATOM   4385  C   ILE A 820     -61.422  21.850  31.547  1.00 50.86           C  
ANISOU 4385  C   ILE A 820     5878   7874   5574   -405   -256   -352       C  
ATOM   4386  O   ILE A 820     -60.631  21.553  30.660  1.00 42.60           O  
ANISOU 4386  O   ILE A 820     4856   6766   4562   -414   -246   -366       O  
ATOM   4387  CB  ILE A 820     -59.832  23.576  32.348  1.00 52.04           C  
ANISOU 4387  CB  ILE A 820     6147   7745   5882   -253   -218   -260       C  
ATOM   4388  CG1 ILE A 820     -59.077  22.501  33.138  1.00 42.09           C  
ANISOU 4388  CG1 ILE A 820     4940   6340   4711   -379   -248   -305       C  
ATOM   4389  CG2 ILE A 820     -59.638  24.963  32.944  1.00 46.29           C  
ANISOU 4389  CG2 ILE A 820     5456   6947   5186   -139   -182   -197       C  
ATOM   4390  CD1 ILE A 820     -57.575  22.531  32.906  1.00 37.01           C  
ANISOU 4390  CD1 ILE A 820     4371   5518   4174   -372   -235   -298       C  
ATOM   4391  N   GLN A 821     -62.384  21.026  31.945  1.00 49.62           N  
ANISOU 4391  N   GLN A 821     5672   7831   5349   -506   -281   -401       N  
ATOM   4392  CA  GLN A 821     -62.423  19.646  31.482  1.00 46.25           C  
ANISOU 4392  CA  GLN A 821     5238   7429   4905   -649   -289   -480       C  
ATOM   4393  C   GLN A 821     -62.640  19.450  29.974  1.00 53.42           C  
ANISOU 4393  C   GLN A 821     6089   8478   5731   -646   -272   -506       C  
ATOM   4394  O   GLN A 821     -62.202  18.442  29.417  1.00 64.50           O  
ANISOU 4394  O   GLN A 821     7515   9836   7155   -746   -266   -565       O  
ATOM   4395  CB  GLN A 821     -63.471  18.861  32.259  1.00 43.87           C  
ANISOU 4395  CB  GLN A 821     4899   7227   4542   -763   -310   -529       C  
ATOM   4396  CG  GLN A 821     -64.895  19.135  31.828  1.00 44.82           C  
ANISOU 4396  CG  GLN A 821     4906   7617   4507   -743   -312   -536       C  
ATOM   4397  CD  GLN A 821     -65.872  18.227  32.530  1.00 49.81           C  
ANISOU 4397  CD  GLN A 821     5503   8346   5076   -879   -330   -598       C  
ATOM   4398  OE1 GLN A 821     -66.343  18.534  33.620  1.00 51.63           O  
ANISOU 4398  OE1 GLN A 821     5730   8579   5307   -867   -349   -574       O  
ATOM   4399  NE2 GLN A 821     -66.168  17.090  31.915  1.00 53.97           N  
ANISOU 4399  NE2 GLN A 821     6008   8949   5550  -1016   -320   -681       N  
ATOM   4400  N   TYR A 822     -63.314  20.381  29.308  1.00 41.96           N  
ANISOU 4400  N   TYR A 822     4561   7200   4183   -531   -259   -462       N  
ATOM   4401  CA  TYR A 822     -63.548  20.197  27.874  1.00 55.13           C  
ANISOU 4401  CA  TYR A 822     6161   9023   5761   -527   -243   -485       C  
ATOM   4402  C   TYR A 822     -62.471  20.897  27.047  1.00 62.07           C  
ANISOU 4402  C   TYR A 822     7085   9793   6707   -417   -219   -435       C  
ATOM   4403  O   TYR A 822     -62.597  21.052  25.829  1.00 57.67           O  
ANISOU 4403  O   TYR A 822     6470   9362   6078   -373   -202   -432       O  
ATOM   4404  CB  TYR A 822     -64.957  20.645  27.457  1.00 50.30           C  
ANISOU 4404  CB  TYR A 822     5424   8704   4983   -472   -239   -471       C  
ATOM   4405  CG  TYR A 822     -66.063  19.913  28.193  1.00 48.24           C  
ANISOU 4405  CG  TYR A 822     5111   8574   4644   -593   -262   -528       C  
ATOM   4406  CD1 TYR A 822     -66.999  20.607  28.953  1.00 56.55           C  
ANISOU 4406  CD1 TYR A 822     6115   9739   5631   -522   -271   -483       C  
ATOM   4407  CD2 TYR A 822     -66.158  18.530  28.141  1.00 51.25           C  
ANISOU 4407  CD2 TYR A 822     5498   8958   5017   -778   -269   -629       C  
ATOM   4408  CE1 TYR A 822     -68.021  19.941  29.631  1.00 62.53           C  
ANISOU 4408  CE1 TYR A 822     6821  10623   6312   -635   -293   -537       C  
ATOM   4409  CE2 TYR A 822     -67.170  17.849  28.818  1.00 54.26           C  
ANISOU 4409  CE2 TYR A 822     5837   9456   5325   -897   -283   -686       C  
ATOM   4410  CZ  TYR A 822     -68.097  18.561  29.559  1.00 57.13           C  
ANISOU 4410  CZ  TYR A 822     6144   9942   5621   -826   -300   -639       C  
ATOM   4411  OH  TYR A 822     -69.091  17.886  30.220  1.00 56.55           O  
ANISOU 4411  OH  TYR A 822     6026   9988   5472   -946   -315   -697       O  
ATOM   4412  N   ARG A 823     -61.406  21.309  27.721  1.00 56.18           N  
ANISOU 4412  N   ARG A 823     6436   8817   6092   -377   -217   -398       N  
ATOM   4413  CA  ARG A 823     -60.279  21.909  27.034  1.00 58.34           C  
ANISOU 4413  CA  ARG A 823     6762   8967   6438   -290   -193   -357       C  
ATOM   4414  C   ARG A 823     -59.044  21.014  27.177  1.00 51.99           C  
ANISOU 4414  C   ARG A 823     6044   7957   5753   -387   -203   -401       C  
ATOM   4415  O   ARG A 823     -57.916  21.477  27.223  1.00 53.68           O  
ANISOU 4415  O   ARG A 823     6328   8005   6064   -335   -192   -367       O  
ATOM   4416  CB  ARG A 823     -60.067  23.362  27.486  1.00 57.75           C  
ANISOU 4416  CB  ARG A 823     6720   8825   6397   -140   -166   -270       C  
ATOM   4417  CG  ARG A 823     -61.061  24.326  26.801  1.00 53.67           C  
ANISOU 4417  CG  ARG A 823     6120   8514   5756     -5   -136   -212       C  
ATOM   4418  CD  ARG A 823     -60.968  25.751  27.308  1.00 56.77           C  
ANISOU 4418  CD  ARG A 823     6556   8837   6177    142    -94   -127       C  
ATOM   4419  NE  ARG A 823     -61.711  25.924  28.558  1.00 65.89           N  
ANISOU 4419  NE  ARG A 823     7704  10013   7317    132   -107   -120       N  
ATOM   4420  CZ  ARG A 823     -61.707  27.033  29.296  1.00 62.69           C  
ANISOU 4420  CZ  ARG A 823     7344   9534   6942    232    -71    -60       C  
ATOM   4421  NH1 ARG A 823     -60.988  28.085  28.926  1.00 74.51           N  
ANISOU 4421  NH1 ARG A 823     8901  10924   8486    347    -14     -2       N  
ATOM   4422  NH2 ARG A 823     -62.417  27.087  30.413  1.00 60.92           N  
ANISOU 4422  NH2 ARG A 823     7109   9340   6700    211    -86    -61       N  
ATOM   4423  N   MET A 824     -59.309  19.713  27.243  1.00 50.82           N  
ANISOU 4423  N   MET A 824     5889   7831   5590   -530   -219   -476       N  
ATOM   4424  CA  MET A 824     -58.304  18.660  27.198  1.00 44.52           C  
ANISOU 4424  CA  MET A 824     5163   6870   4880   -628   -218   -523       C  
ATOM   4425  C   MET A 824     -59.111  17.456  26.742  1.00 47.05           C  
ANISOU 4425  C   MET A 824     5438   7321   5119   -763   -216   -608       C  
ATOM   4426  O   MET A 824     -60.323  17.447  26.898  1.00 46.09           O  
ANISOU 4426  O   MET A 824     5242   7376   4894   -791   -223   -627       O  
ATOM   4427  CB  MET A 824     -57.712  18.408  28.585  1.00 52.06           C  
ANISOU 4427  CB  MET A 824     6197   7645   5939   -665   -232   -513       C  
ATOM   4428  CG  MET A 824     -58.603  17.579  29.522  1.00 47.94           C  
ANISOU 4428  CG  MET A 824     5661   7172   5383   -776   -247   -557       C  
ATOM   4429  SD  MET A 824     -57.984  17.350  31.211  1.00 58.31           S  
ANISOU 4429  SD  MET A 824     7053   8295   6806   -807   -263   -535       S  
ATOM   4430  CE  MET A 824     -58.293  18.951  31.956  1.00 47.00           C  
ANISOU 4430  CE  MET A 824     5597   6894   5368   -676   -274   -460       C  
ATOM   4431  N   PRO A 825     -58.459  16.443  26.161  1.00 49.63           N  
ANISOU 4431  N   PRO A 825     5807   7567   5483   -852   -199   -663       N  
ATOM   4432  CA  PRO A 825     -59.228  15.301  25.652  1.00 48.20           C  
ANISOU 4432  CA  PRO A 825     5587   7509   5218   -992   -183   -755       C  
ATOM   4433  C   PRO A 825     -59.986  14.586  26.769  1.00 59.22           C  
ANISOU 4433  C   PRO A 825     6990   8914   6595  -1102   -188   -793       C  
ATOM   4434  O   PRO A 825     -59.494  14.519  27.892  1.00 51.99           O  
ANISOU 4434  O   PRO A 825     6144   7837   5771  -1100   -199   -763       O  
ATOM   4435  CB  PRO A 825     -58.145  14.379  25.054  1.00 53.08           C  
ANISOU 4435  CB  PRO A 825     6280   7975   5912  -1057   -155   -797       C  
ATOM   4436  CG  PRO A 825     -56.835  14.936  25.531  1.00 59.64           C  
ANISOU 4436  CG  PRO A 825     7192   8596   6872   -960   -166   -725       C  
ATOM   4437  CD  PRO A 825     -57.062  16.400  25.709  1.00 59.74           C  
ANISOU 4437  CD  PRO A 825     7160   8672   6865   -818   -187   -647       C  
ATOM   4438  N   ARG A 826     -61.176  14.069  26.478  1.00 61.78           N  
ANISOU 4438  N   ARG A 826     7240   9436   6798  -1199   -180   -860       N  
ATOM   4439  CA  ARG A 826     -61.918  13.370  27.515  1.00 62.91           C  
ANISOU 4439  CA  ARG A 826     7391   9591   6920  -1311   -181   -900       C  
ATOM   4440  C   ARG A 826     -61.044  12.237  28.038  1.00 63.40           C  
ANISOU 4440  C   ARG A 826     7572   9422   7094  -1408   -154   -933       C  
ATOM   4441  O   ARG A 826     -61.033  11.950  29.235  1.00 56.23           O  
ANISOU 4441  O   ARG A 826     6714   8411   6239  -1439   -161   -919       O  
ATOM   4442  CB  ARG A 826     -63.256  12.826  27.001  1.00 46.02           C  
ANISOU 4442  CB  ARG A 826     5156   7701   4627  -1427   -166   -984       C  
ATOM   4443  CG  ARG A 826     -64.295  12.615  28.100  1.00 52.51           C  
ANISOU 4443  CG  ARG A 826     5951   8603   5397  -1495   -181  -1001       C  
ATOM   4444  CD  ARG A 826     -64.437  13.886  28.954  1.00 69.97           C  
ANISOU 4444  CD  ARG A 826     8140  10818   7628  -1343   -225   -901       C  
ATOM   4445  NE  ARG A 826     -65.404  13.815  30.056  1.00 71.12           N  
ANISOU 4445  NE  ARG A 826     8256  11038   7726  -1390   -244   -908       N  
ATOM   4446  CZ  ARG A 826     -65.764  12.705  30.697  1.00 82.26           C  
ANISOU 4446  CZ  ARG A 826     9703  12417   9136  -1545   -229   -976       C  
ATOM   4447  NH1 ARG A 826     -65.247  11.529  30.362  1.00 90.49           N  
ANISOU 4447  NH1 ARG A 826    10818  13342  10222  -1671   -186  -1045       N  
ATOM   4448  NH2 ARG A 826     -66.646  12.775  31.688  1.00 79.53           N  
ANISOU 4448  NH2 ARG A 826     9324  12149   8745  -1573   -250   -973       N  
ATOM   4449  N   GLU A 827     -60.313  11.609  27.123  1.00 64.16           N  
ANISOU 4449  N   GLU A 827     7711   9443   7222  -1449   -119   -971       N  
ATOM   4450  CA  GLU A 827     -59.446  10.483  27.441  1.00 65.02           C  
ANISOU 4450  CA  GLU A 827     7936   9338   7430  -1531    -79  -1000       C  
ATOM   4451  C   GLU A 827     -58.516  10.778  28.607  1.00 67.17           C  
ANISOU 4451  C   GLU A 827     8287   9408   7827  -1451   -100   -920       C  
ATOM   4452  O   GLU A 827     -58.328   9.939  29.482  1.00 78.51           O  
ANISOU 4452  O   GLU A 827     9796  10717   9317  -1521    -78   -931       O  
ATOM   4453  CB  GLU A 827     -58.612  10.105  26.216  1.00 82.84           C  
ANISOU 4453  CB  GLU A 827    10223  11538   9713  -1537    -45  -1030       C  
ATOM   4454  CG  GLU A 827     -57.580   9.026  26.495  1.00100.04           C  
ANISOU 4454  CG  GLU A 827    12528  13484  12000  -1594      2  -1045       C  
ATOM   4455  CD  GLU A 827     -56.203   9.369  25.936  1.00113.20           C  
ANISOU 4455  CD  GLU A 827    14242  15013  13757  -1490     -1   -994       C  
ATOM   4456  OE1 GLU A 827     -56.125   9.913  24.811  1.00115.53           O  
ANISOU 4456  OE1 GLU A 827    14481  15405  14012  -1440    -10   -997       O  
ATOM   4457  OE2 GLU A 827     -55.197   9.099  26.633  1.00114.81           O  
ANISOU 4457  OE2 GLU A 827    14535  15021  14068  -1456      7   -949       O  
ATOM   4458  N   THR A 828     -57.930  11.968  28.625  1.00 59.15           N  
ANISOU 4458  N   THR A 828     7255   8365   6853  -1305   -138   -840       N  
ATOM   4459  CA  THR A 828     -56.982  12.299  29.673  1.00 58.74           C  
ANISOU 4459  CA  THR A 828     7270   8137   6913  -1233   -156   -770       C  
ATOM   4460  C   THR A 828     -57.699  12.811  30.919  1.00 63.94           C  
ANISOU 4460  C   THR A 828     7899   8840   7554  -1216   -189   -737       C  
ATOM   4461  O   THR A 828     -57.263  12.551  32.044  1.00 67.12           O  
ANISOU 4461  O   THR A 828     8358   9117   8029  -1223   -193   -708       O  
ATOM   4462  CB  THR A 828     -55.919  13.330  29.219  1.00 60.00           C  
ANISOU 4462  CB  THR A 828     7437   8228   7132  -1098   -172   -705       C  
ATOM   4463  OG1 THR A 828     -56.412  14.656  29.435  1.00 75.11           O  
ANISOU 4463  OG1 THR A 828     9289  10242   9009   -997   -205   -654       O  
ATOM   4464  CG2 THR A 828     -55.558  13.133  27.763  1.00 45.23           C  
ANISOU 4464  CG2 THR A 828     5558   6387   5241  -1099   -149   -738       C  
ATOM   4465  N   TYR A 829     -58.796  13.536  30.734  1.00 58.37           N  
ANISOU 4465  N   TYR A 829     7104   8323   6752  -1188   -211   -737       N  
ATOM   4466  CA  TYR A 829     -59.560  13.990  31.895  1.00 58.01           C  
ANISOU 4466  CA  TYR A 829     7028   8330   6683  -1176   -240   -710       C  
ATOM   4467  C   TYR A 829     -60.105  12.793  32.650  1.00 58.49           C  
ANISOU 4467  C   TYR A 829     7117   8376   6732  -1315   -224   -764       C  
ATOM   4468  O   TYR A 829     -60.345  12.861  33.842  1.00 56.02           O  
ANISOU 4468  O   TYR A 829     6814   8031   6441  -1320   -243   -739       O  
ATOM   4469  CB  TYR A 829     -60.708  14.913  31.495  1.00 49.20           C  
ANISOU 4469  CB  TYR A 829     5808   7435   5452  -1118   -258   -701       C  
ATOM   4470  CG  TYR A 829     -61.566  15.340  32.656  1.00 46.92           C  
ANISOU 4470  CG  TYR A 829     5485   7212   5130  -1108   -285   -677       C  
ATOM   4471  CD1 TYR A 829     -61.165  16.364  33.498  1.00 54.15           C  
ANISOU 4471  CD1 TYR A 829     6420   8048   6107  -1001   -305   -604       C  
ATOM   4472  CD2 TYR A 829     -62.783  14.718  32.915  1.00 49.08           C  
ANISOU 4472  CD2 TYR A 829     5708   7632   5309  -1213   -287   -732       C  
ATOM   4473  CE1 TYR A 829     -61.955  16.764  34.577  1.00 55.11           C  
ANISOU 4473  CE1 TYR A 829     6512   8230   6199   -992   -328   -584       C  
ATOM   4474  CE2 TYR A 829     -63.581  15.113  33.974  1.00 47.32           C  
ANISOU 4474  CE2 TYR A 829     5451   7474   5053  -1202   -313   -710       C  
ATOM   4475  CZ  TYR A 829     -63.162  16.133  34.805  1.00 53.74           C  
ANISOU 4475  CZ  TYR A 829     6285   8202   5932  -1089   -334   -635       C  
ATOM   4476  OH  TYR A 829     -63.954  16.516  35.864  1.00 56.67           O  
ANISOU 4476  OH  TYR A 829     6624   8638   6271  -1079   -357   -615       O  
ATOM   4477  N   SER A 830     -60.293  11.686  31.950  1.00 65.82           N  
ANISOU 4477  N   SER A 830     8060   9322   7625  -1432   -184   -840       N  
ATOM   4478  CA  SER A 830     -60.859  10.506  32.576  1.00 72.01           C  
ANISOU 4478  CA  SER A 830     8877  10091   8391  -1576   -155   -899       C  
ATOM   4479  C   SER A 830     -59.810   9.724  33.361  1.00 78.53           C  
ANISOU 4479  C   SER A 830     9818  10684   9337  -1596   -128   -875       C  
ATOM   4480  O   SER A 830     -60.103   9.197  34.433  1.00 82.87           O  
ANISOU 4480  O   SER A 830    10400  11186   9902  -1654   -121   -875       O  
ATOM   4481  CB  SER A 830     -61.516   9.605  31.533  1.00 70.05           C  
ANISOU 4481  CB  SER A 830     8607   9958   8052  -1708   -109   -998       C  
ATOM   4482  OG  SER A 830     -62.023   8.437  32.148  1.00 72.04           O  
ANISOU 4482  OG  SER A 830     8904  10178   8290  -1855    -67  -1059       O  
ATOM   4483  N   THR A 831     -58.593   9.636  32.830  1.00 77.21           N  
ANISOU 4483  N   THR A 831     9709  10379   9249  -1544   -109   -852       N  
ATOM   4484  CA  THR A 831     -57.541   8.910  33.528  1.00 72.40           C  
ANISOU 4484  CA  THR A 831     9202   9561   8745  -1546    -80   -820       C  
ATOM   4485  C   THR A 831     -57.128   9.722  34.731  1.00 71.22           C  
ANISOU 4485  C   THR A 831     9051   9356   8655  -1449   -127   -737       C  
ATOM   4486  O   THR A 831     -56.554   9.199  35.679  1.00 74.38           O  
ANISOU 4486  O   THR A 831     9513   9624   9122  -1453   -112   -703       O  
ATOM   4487  CB  THR A 831     -56.300   8.671  32.653  1.00 76.33           C  
ANISOU 4487  CB  THR A 831     9757   9937   9308  -1504    -50   -811       C  
ATOM   4488  OG1 THR A 831     -55.448   9.823  32.697  1.00 81.25           O  
ANISOU 4488  OG1 THR A 831    10362  10527   9984  -1365    -96   -736       O  
ATOM   4489  CG2 THR A 831     -56.701   8.367  31.224  1.00 79.57           C  
ANISOU 4489  CG2 THR A 831    10138  10447   9648  -1565    -21   -886       C  
ATOM   4490  N   LEU A 832     -57.445  11.009  34.679  1.00 69.22           N  
ANISOU 4490  N   LEU A 832     8722   9209   8370  -1360   -178   -704       N  
ATOM   4491  CA  LEU A 832     -57.114  11.941  35.744  1.00 66.92           C  
ANISOU 4491  CA  LEU A 832     8421   8882   8125  -1270   -219   -633       C  
ATOM   4492  C   LEU A 832     -58.164  11.892  36.847  1.00 76.70           C  
ANISOU 4492  C   LEU A 832     9628  10194   9321  -1319   -238   -638       C  
ATOM   4493  O   LEU A 832     -57.863  12.049  38.022  1.00 84.34           O  
ANISOU 4493  O   LEU A 832    10615  11093  10339  -1295   -255   -594       O  
ATOM   4494  CB  LEU A 832     -57.001  13.349  35.160  1.00 67.90           C  
ANISOU 4494  CB  LEU A 832     8491   9076   8233  -1154   -249   -598       C  
ATOM   4495  CG  LEU A 832     -56.771  14.562  36.053  1.00 60.42           C  
ANISOU 4495  CG  LEU A 832     7525   8114   7318  -1057   -282   -534       C  
ATOM   4496  CD1 LEU A 832     -56.263  15.703  35.218  1.00 64.07           C  
ANISOU 4496  CD1 LEU A 832     7969   8589   7786   -949   -286   -502       C  
ATOM   4497  CD2 LEU A 832     -58.065  14.947  36.692  1.00 60.15           C  
ANISOU 4497  CD2 LEU A 832     7431   8214   7211  -1072   -306   -540       C  
ATOM   4498  N   ILE A 833     -59.410  11.682  36.462  1.00 83.75           N  
ANISOU 4498  N   ILE A 833    10467  11241  10115  -1391   -236   -694       N  
ATOM   4499  CA  ILE A 833     -60.483  11.594  37.433  1.00 77.85           C  
ANISOU 4499  CA  ILE A 833     9684  10579   9316  -1445   -254   -706       C  
ATOM   4500  C   ILE A 833     -60.360  10.268  38.185  1.00 75.31           C  
ANISOU 4500  C   ILE A 833     9438  10144   9034  -1553   -216   -728       C  
ATOM   4501  O   ILE A 833     -60.584  10.207  39.393  1.00 73.27           O  
ANISOU 4501  O   ILE A 833     9186   9862   8793  -1565   -232   -703       O  
ATOM   4502  CB  ILE A 833     -61.869  11.730  36.740  1.00 79.77           C  
ANISOU 4502  CB  ILE A 833     9838  11042   9427  -1494   -260   -762       C  
ATOM   4503  CG1 ILE A 833     -62.910  12.299  37.705  1.00 82.85           C  
ANISOU 4503  CG1 ILE A 833    10166  11553   9762  -1485   -298   -745       C  
ATOM   4504  CG2 ILE A 833     -62.320  10.408  36.129  1.00 78.49           C  
ANISOU 4504  CG2 ILE A 833     9698  10910   9215  -1644   -209   -851       C  
ATOM   4505  CD1 ILE A 833     -62.733  13.772  37.981  1.00 82.22           C  
ANISOU 4505  CD1 ILE A 833    10047  11494   9698  -1337   -337   -673       C  
ATOM   4506  N   ASN A 834     -59.970   9.217  37.468  1.00 75.32           N  
ANISOU 4506  N   ASN A 834     9499  10070   9049  -1625   -161   -773       N  
ATOM   4507  CA  ASN A 834     -59.874   7.879  38.041  1.00 79.08           C  
ANISOU 4507  CA  ASN A 834    10060  10430   9558  -1729   -105   -797       C  
ATOM   4508  C   ASN A 834     -58.498   7.615  38.632  1.00 88.64           C  
ANISOU 4508  C   ASN A 834    11353  11444  10883  -1661    -88   -728       C  
ATOM   4509  O   ASN A 834     -57.760   6.745  38.168  1.00 97.55           O  
ANISOU 4509  O   ASN A 834    12559  12449  12055  -1686    -30   -739       O  
ATOM   4510  CB  ASN A 834     -60.223   6.825  36.992  1.00 79.40           C  
ANISOU 4510  CB  ASN A 834    10131  10489   9549  -1852    -38   -887       C  
ATOM   4511  CG  ASN A 834     -61.709   6.799  36.668  1.00 86.84           C  
ANISOU 4511  CG  ASN A 834    10992  11639  10363  -1953    -43   -964       C  
ATOM   4512  OD1 ASN A 834     -62.121   6.335  35.601  1.00 94.03           O  
ANISOU 4512  OD1 ASN A 834    11888  12631  11207  -2039     -5  -1043       O  
ATOM   4513  ND2 ASN A 834     -62.524   7.307  37.593  1.00 74.76           N  
ANISOU 4513  ND2 ASN A 834     9404  10207   8793  -1946    -90   -944       N  
ATOM   4514  N   ILE A 835     -58.167   8.372  39.668  1.00 85.25           N  
ANISOU 4514  N   ILE A 835    10903  10993  10495  -1576   -136   -658       N  
ATOM   4515  CA  ILE A 835     -56.831   8.355  40.238  1.00 80.55           C  
ANISOU 4515  CA  ILE A 835    10361  10247   9996  -1495   -131   -586       C  
ATOM   4516  C   ILE A 835     -56.883   8.660  41.737  1.00 79.08           C  
ANISOU 4516  C   ILE A 835    10159  10053   9833  -1467   -164   -532       C  
ATOM   4517  O   ILE A 835     -57.481   9.648  42.180  1.00 68.08           O  
ANISOU 4517  O   ILE A 835     8696   8764   8407  -1435   -218   -522       O  
ATOM   4518  CB  ILE A 835     -55.969   9.405  39.559  1.00 74.04           C  
ANISOU 4518  CB  ILE A 835     9510   9419   9202  -1384   -163   -553       C  
ATOM   4519  CG1 ILE A 835     -54.520   9.285  40.014  1.00 74.55           C  
ANISOU 4519  CG1 ILE A 835     9628   9341   9357  -1311   -151   -487       C  
ATOM   4520  CG2 ILE A 835     -56.497  10.782  39.882  1.00 75.63           C  
ANISOU 4520  CG2 ILE A 835     9629   9737   9370  -1321   -225   -532       C  
ATOM   4521  CD1 ILE A 835     -53.592  10.175  39.230  1.00 74.90           C  
ANISOU 4521  CD1 ILE A 835     9657   9371   9431  -1217   -171   -463       C  
TER    4522      ILE A 835                                                      
ATOM   4523  N   LEU B 200     -50.665   9.502  -1.659  1.00 68.01           N  
ANISOU 4523  N   LEU B 200     8642   8609   8588    527    306    343       N  
ATOM   4524  CA  LEU B 200     -51.749   9.259  -2.618  1.00 68.40           C  
ANISOU 4524  CA  LEU B 200     8795   8460   8734    477    308    296       C  
ATOM   4525  C   LEU B 200     -51.276   9.321  -4.063  1.00 58.72           C  
ANISOU 4525  C   LEU B 200     7609   7177   7524    450    300    265       C  
ATOM   4526  O   LEU B 200     -50.754  10.332  -4.529  1.00 53.73           O  
ANISOU 4526  O   LEU B 200     6946   6605   6866    387    246    218       O  
ATOM   4527  CB  LEU B 200     -52.924  10.235  -2.436  1.00 63.53           C  
ANISOU 4527  CB  LEU B 200     8192   7789   8159    375    246    218       C  
ATOM   4528  CG  LEU B 200     -53.825  10.358  -3.682  1.00 63.35           C  
ANISOU 4528  CG  LEU B 200     8248   7617   8207    307    228    157       C  
ATOM   4529  CD1 LEU B 200     -54.704   9.132  -3.865  1.00 61.37           C  
ANISOU 4529  CD1 LEU B 200     8065   7240   8011    334    289    174       C  
ATOM   4530  CD2 LEU B 200     -54.682  11.629  -3.715  1.00 58.11           C  
ANISOU 4530  CD2 LEU B 200     7584   6934   7563    215    163     86       C  
ATOM   4531  N   ASN B 201     -51.488   8.224  -4.768  1.00 50.12           N  
ANISOU 4531  N   ASN B 201     6595   5969   6481    491    365    288       N  
ATOM   4532  CA  ASN B 201     -51.193   8.173  -6.175  1.00 50.24           C  
ANISOU 4532  CA  ASN B 201     6654   5918   6517    462    363    254       C  
ATOM   4533  C   ASN B 201     -52.455   7.846  -6.971  1.00 44.03           C  
ANISOU 4533  C   ASN B 201     5949   4974   5806    397    373    194       C  
ATOM   4534  O   ASN B 201     -52.931   6.711  -6.982  1.00 45.83           O  
ANISOU 4534  O   ASN B 201     6239   5104   6071    428    454    213       O  
ATOM   4535  CB  ASN B 201     -50.074   7.172  -6.449  1.00 48.94           C  
ANISOU 4535  CB  ASN B 201     6497   5779   6319    569    440    329       C  
ATOM   4536  CG  ASN B 201     -49.767   7.042  -7.918  1.00 53.10           C  
ANISOU 4536  CG  ASN B 201     7072   6235   6868    540    443    293       C  
ATOM   4537  OD1 ASN B 201     -50.260   7.820  -8.742  1.00 53.98           O  
ANISOU 4537  OD1 ASN B 201     7196   6305   7009    443    379    215       O  
ATOM   4538  ND2 ASN B 201     -48.957   6.052  -8.263  1.00 59.31           N  
ANISOU 4538  ND2 ASN B 201     7885   7010   7638    633    525    355       N  
ATOM   4539  N   VAL B 202     -52.991   8.871  -7.615  1.00 42.60           N  
ANISOU 4539  N   VAL B 202     5764   4780   5642    305    299    122       N  
ATOM   4540  CA  VAL B 202     -54.160   8.757  -8.477  1.00 44.41           C  
ANISOU 4540  CA  VAL B 202     6047   4905   5923    236    296     59       C  
ATOM   4541  C   VAL B 202     -54.027   7.699  -9.585  1.00 49.34           C  
ANISOU 4541  C   VAL B 202     6732   5445   6569    242    361     49       C  
ATOM   4542  O   VAL B 202     -55.030   7.191 -10.078  1.00 46.40           O  
ANISOU 4542  O   VAL B 202     6405   4991   6233    190    390      1       O  
ATOM   4543  CB  VAL B 202     -54.486  10.138  -9.081  1.00 43.26           C  
ANISOU 4543  CB  VAL B 202     5877   4786   5772    161    212      3       C  
ATOM   4544  CG1 VAL B 202     -55.095  10.004 -10.448  1.00 50.41           C  
ANISOU 4544  CG1 VAL B 202     6820   5630   6704    111    210    -48       C  
ATOM   4545  CG2 VAL B 202     -55.381  10.949  -8.120  1.00 35.96           C  
ANISOU 4545  CG2 VAL B 202     4928   3883   4853    130    171    -11       C  
ATOM   4546  N   ASN B 203     -52.794   7.359  -9.963  1.00 49.71           N  
ANISOU 4546  N   ASN B 203     6777   5521   6590    301    391     89       N  
ATOM   4547  CA  ASN B 203     -52.558   6.366 -11.014  1.00 48.75           C  
ANISOU 4547  CA  ASN B 203     6717   5318   6487    311    463     79       C  
ATOM   4548  C   ASN B 203     -52.232   4.960 -10.497  1.00 48.41           C  
ANISOU 4548  C   ASN B 203     6728   5214   6453    402    587    145       C  
ATOM   4549  O   ASN B 203     -51.953   4.048 -11.276  1.00 49.78           O  
ANISOU 4549  O   ASN B 203     6964   5309   6642    420    670    142       O  
ATOM   4550  CB  ASN B 203     -51.440   6.840 -11.959  1.00 51.31           C  
ANISOU 4550  CB  ASN B 203     7016   5701   6778    320    427     79       C  
ATOM   4551  CG  ASN B 203     -51.858   8.026 -12.818  1.00 44.38           C  
ANISOU 4551  CG  ASN B 203     6114   4847   5903    230    335     11       C  
ATOM   4552  OD1 ASN B 203     -52.932   8.025 -13.412  1.00 44.68           O  
ANISOU 4552  OD1 ASN B 203     6176   4830   5970    162    327    -48       O  
ATOM   4553  ND2 ASN B 203     -51.005   9.043 -12.883  1.00 41.28           N  
ANISOU 4553  ND2 ASN B 203     5668   4545   5472    231    274     21       N  
ATOM   4554  N   GLU B 204     -52.263   4.798  -9.182  1.00 49.66           N  
ANISOU 4554  N   GLU B 204     6863   5407   6599    464    609    207       N  
ATOM   4555  CA  GLU B 204     -51.889   3.544  -8.542  1.00 52.68           C  
ANISOU 4555  CA  GLU B 204     7290   5745   6981    575    736    292       C  
ATOM   4556  C   GLU B 204     -52.759   2.360  -8.978  1.00 62.48           C  
ANISOU 4556  C   GLU B 204     8641   6813   8284    540    853    255       C  
ATOM   4557  O   GLU B 204     -52.257   1.241  -9.118  1.00 69.57           O  
ANISOU 4557  O   GLU B 204     9608   7634   9190    620    983    307       O  
ATOM   4558  CB  GLU B 204     -51.926   3.714  -7.024  1.00 54.59           C  
ANISOU 4558  CB  GLU B 204     7475   6071   7194    637    727    360       C  
ATOM   4559  CG  GLU B 204     -51.769   2.440  -6.218  1.00 68.76           C  
ANISOU 4559  CG  GLU B 204     9318   7817   8991    759    867    458       C  
ATOM   4560  CD  GLU B 204     -52.261   2.614  -4.790  1.00 85.38           C  
ANISOU 4560  CD  GLU B 204    11375   9982  11083    788    852    499       C  
ATOM   4561  OE1 GLU B 204     -51.900   3.634  -4.156  1.00 89.35           O  
ANISOU 4561  OE1 GLU B 204    11776  10641  11532    784    752    506       O  
ATOM   4562  OE2 GLU B 204     -53.021   1.743  -4.307  1.00 92.15           O  
ANISOU 4562  OE2 GLU B 204    12299  10731  11984    806    947    519       O  
ATOM   4563  N   ASN B 205     -54.052   2.601  -9.193  1.00 53.51           N  
ANISOU 4563  N   ASN B 205     7522   5623   7187    421    817    165       N  
ATOM   4564  CA  ASN B 205     -54.952   1.550  -9.666  1.00 54.61           C  
ANISOU 4564  CA  ASN B 205     7757   5617   7377    356    926    106       C  
ATOM   4565  C   ASN B 205     -56.181   2.100 -10.391  1.00 54.78           C  
ANISOU 4565  C   ASN B 205     7766   5635   7415    205    852    -13       C  
ATOM   4566  O   ASN B 205     -56.467   3.292 -10.320  1.00 57.39           O  
ANISOU 4566  O   ASN B 205     8019   6061   7724    168    723    -34       O  
ATOM   4567  CB  ASN B 205     -55.367   0.621  -8.518  1.00 59.97           C  
ANISOU 4567  CB  ASN B 205     8487   6221   8080    413   1040    163       C  
ATOM   4568  CG  ASN B 205     -56.238   1.313  -7.490  1.00 64.70           C  
ANISOU 4568  CG  ASN B 205     9025   6880   8676    380    956    159       C  
ATOM   4569  OD1 ASN B 205     -57.309   1.828  -7.813  1.00 64.52           O  
ANISOU 4569  OD1 ASN B 205     8987   6860   8668    263    888     69       O  
ATOM   4570  ND2 ASN B 205     -55.785   1.322  -6.240  1.00 66.68           N  
ANISOU 4570  ND2 ASN B 205     9238   7193   8903    490    965    259       N  
ATOM   4571  N   ASN B 206     -56.903   1.225 -11.086  1.00 53.80           N  
ANISOU 4571  N   ASN B 206     7715   5406   7320    120    944    -91       N  
ATOM   4572  CA  ASN B 206     -58.042   1.642 -11.910  1.00 52.81           C  
ANISOU 4572  CA  ASN B 206     7566   5305   7192    -23    885   -206       C  
ATOM   4573  C   ASN B 206     -59.208   2.267 -11.143  1.00 58.87           C  
ANISOU 4573  C   ASN B 206     8283   6126   7958    -73    811   -227       C  
ATOM   4574  O   ASN B 206     -59.920   3.116 -11.675  1.00 56.88           O  
ANISOU 4574  O   ASN B 206     7974   5955   7685   -150    715   -287       O  
ATOM   4575  CB  ASN B 206     -58.535   0.483 -12.778  1.00 52.80           C  
ANISOU 4575  CB  ASN B 206     7651   5197   7213   -117   1016   -296       C  
ATOM   4576  CG  ASN B 206     -57.793   0.399 -14.102  1.00 60.69           C  
ANISOU 4576  CG  ASN B 206     8663   6197   8198   -131   1024   -331       C  
ATOM   4577  OD1 ASN B 206     -57.970  -0.545 -14.879  1.00 70.46           O  
ANISOU 4577  OD1 ASN B 206     9973   7349   9449   -203   1139   -404       O  
ATOM   4578  ND2 ASN B 206     -56.950   1.394 -14.362  1.00 52.58           N  
ANISOU 4578  ND2 ASN B 206     7568   5267   7143    -70    909   -285       N  
ATOM   4579  N   ILE B 207     -59.389   1.841  -9.895  1.00 64.32           N  
ANISOU 4579  N   ILE B 207     8995   6776   8668    -20    863   -169       N  
ATOM   4580  CA  ILE B 207     -60.449   2.329  -9.018  1.00 63.28           C  
ANISOU 4580  CA  ILE B 207     8821   6687   8536    -55    805   -178       C  
ATOM   4581  C   ILE B 207     -60.218   3.783  -8.602  1.00 58.65           C  
ANISOU 4581  C   ILE B 207     8141   6225   7920    -16    657   -141       C  
ATOM   4582  O   ILE B 207     -61.121   4.622  -8.671  1.00 53.10           O  
ANISOU 4582  O   ILE B 207     7388   5586   7203    -78    571   -186       O  
ATOM   4583  CB  ILE B 207     -60.512   1.449  -7.760  1.00 67.98           C  
ANISOU 4583  CB  ILE B 207     9465   7206   9158     11    909   -110       C  
ATOM   4584  CG1 ILE B 207     -60.988   0.039  -8.137  1.00 71.52           C  
ANISOU 4584  CG1 ILE B 207    10020   7514   9641    -52   1075   -163       C  
ATOM   4585  CG2 ILE B 207     -61.380   2.097  -6.694  1.00 60.74           C  
ANISOU 4585  CG2 ILE B 207     8492   6352   8236      0    833    -99       C  
ATOM   4586  CD1 ILE B 207     -61.004  -0.943  -6.984  1.00 75.51           C  
ANISOU 4586  CD1 ILE B 207    10592   7921  10177     22   1208    -88       C  
ATOM   4587  N   LEU B 208     -58.992   4.067  -8.178  1.00 57.98           N  
ANISOU 4587  N   LEU B 208     8034   6177   7819     87    639    -60       N  
ATOM   4588  CA  LEU B 208     -58.557   5.414  -7.818  1.00 48.78           C  
ANISOU 4588  CA  LEU B 208     6790   5124   6623    116    520    -33       C  
ATOM   4589  C   LEU B 208     -58.537   6.340  -9.049  1.00 48.97           C  
ANISOU 4589  C   LEU B 208     6784   5194   6629     56    438    -90       C  
ATOM   4590  O   LEU B 208     -59.007   7.485  -8.994  1.00 44.40           O  
ANISOU 4590  O   LEU B 208     6156   4679   6036     26    350   -110       O  
ATOM   4591  CB  LEU B 208     -57.157   5.323  -7.200  1.00 50.66           C  
ANISOU 4591  CB  LEU B 208     7009   5405   6835    228    540     58       C  
ATOM   4592  CG  LEU B 208     -56.762   6.158  -5.981  1.00 57.64           C  
ANISOU 4592  CG  LEU B 208     7819   6396   7685    280    477    111       C  
ATOM   4593  CD1 LEU B 208     -57.955   6.419  -5.066  1.00 48.51           C  
ANISOU 4593  CD1 LEU B 208     6649   5238   6544    244    451     94       C  
ATOM   4594  CD2 LEU B 208     -55.640   5.446  -5.226  1.00 52.98           C  
ANISOU 4594  CD2 LEU B 208     7222   5842   7066    401    548    209       C  
ATOM   4595  N   ARG B 209     -57.998   5.839 -10.164  1.00 44.39           N  
ANISOU 4595  N   ARG B 209     6237   4579   6050     47    478   -112       N  
ATOM   4596  CA  ARG B 209     -57.922   6.628 -11.393  1.00 45.83           C  
ANISOU 4596  CA  ARG B 209     6392   4809   6213     -1    410   -160       C  
ATOM   4597  C   ARG B 209     -59.294   7.128 -11.861  1.00 48.14           C  
ANISOU 4597  C   ARG B 209     6659   5132   6499    -89    364   -229       C  
ATOM   4598  O   ARG B 209     -59.449   8.306 -12.182  1.00 48.46           O  
ANISOU 4598  O   ARG B 209     6652   5243   6518    -99    281   -235       O  
ATOM   4599  CB  ARG B 209     -57.235   5.848 -12.518  1.00 44.25           C  
ANISOU 4599  CB  ARG B 209     6235   4562   6015     -3    472   -179       C  
ATOM   4600  CG  ARG B 209     -57.314   6.544 -13.877  1.00 45.26           C  
ANISOU 4600  CG  ARG B 209     6333   4741   6121    -60    410   -234       C  
ATOM   4601  CD  ARG B 209     -56.250   7.635 -14.026  1.00 48.33           C  
ANISOU 4601  CD  ARG B 209     6678   5199   6486    -10    335   -191       C  
ATOM   4602  NE  ARG B 209     -56.535   8.536 -15.139  1.00 47.94           N  
ANISOU 4602  NE  ARG B 209     6594   5205   6415    -57    269   -233       N  
ATOM   4603  CZ  ARG B 209     -55.818   9.615 -15.434  1.00 43.96           C  
ANISOU 4603  CZ  ARG B 209     6055   4756   5890    -34    208   -209       C  
ATOM   4604  NH1 ARG B 209     -54.764   9.923 -14.694  1.00 39.22           N  
ANISOU 4604  NH1 ARG B 209     5445   4176   5283     21    199   -155       N  
ATOM   4605  NH2 ARG B 209     -56.161  10.389 -16.468  1.00 35.72           N  
ANISOU 4605  NH2 ARG B 209     4986   3758   4828    -68    162   -238       N  
ATOM   4606  N   GLU B 210     -60.283   6.237 -11.891  1.00 52.52           N  
ANISOU 4606  N   GLU B 210     7246   5641   7068   -151    426   -278       N  
ATOM   4607  CA  GLU B 210     -61.628   6.588 -12.363  1.00 57.07           C  
ANISOU 4607  CA  GLU B 210     7787   6274   7623   -238    390   -346       C  
ATOM   4608  C   GLU B 210     -62.307   7.617 -11.454  1.00 53.81           C  
ANISOU 4608  C   GLU B 210     7324   5921   7200   -219    314   -317       C  
ATOM   4609  O   GLU B 210     -63.008   8.517 -11.914  1.00 55.30           O  
ANISOU 4609  O   GLU B 210     7464   6191   7358   -244    250   -338       O  
ATOM   4610  CB  GLU B 210     -62.499   5.334 -12.482  1.00 60.76           C  
ANISOU 4610  CB  GLU B 210     8299   6686   8101   -322    487   -414       C  
ATOM   4611  CG  GLU B 210     -63.778   5.529 -13.295  1.00 68.84           C  
ANISOU 4611  CG  GLU B 210     9275   7799   9082   -428    461   -501       C  
ATOM   4612  N   LYS B 211     -62.088   7.491 -10.157  1.00 46.03           N  
ANISOU 4612  N   LYS B 211     6351   4901   6237   -166    327   -263       N  
ATOM   4613  CA  LYS B 211     -62.670   8.431  -9.224  1.00 53.89           C  
ANISOU 4613  CA  LYS B 211     7304   5946   7224   -148    264   -238       C  
ATOM   4614  C   LYS B 211     -62.062   9.793  -9.492  1.00 49.90           C  
ANISOU 4614  C   LYS B 211     6762   5499   6699   -112    187   -213       C  
ATOM   4615  O   LYS B 211     -62.752  10.822  -9.434  1.00 48.72           O  
ANISOU 4615  O   LYS B 211     6578   5403   6532   -119    132   -217       O  
ATOM   4616  CB  LYS B 211     -62.363   7.977  -7.800  1.00 64.57           C  
ANISOU 4616  CB  LYS B 211     8674   7260   8600    -92    299   -183       C  
ATOM   4617  CG  LYS B 211     -63.045   8.761  -6.707  1.00 63.51           C  
ANISOU 4617  CG  LYS B 211     8501   7169   8460    -81    247   -163       C  
ATOM   4618  CD  LYS B 211     -63.024   7.932  -5.440  1.00 71.82           C  
ANISOU 4618  CD  LYS B 211     9575   8181   9534    -42    304   -121       C  
ATOM   4619  CE  LYS B 211     -63.470   8.732  -4.243  1.00 81.82           C  
ANISOU 4619  CE  LYS B 211    10800   9497  10792    -21    252    -95       C  
ATOM   4620  NZ  LYS B 211     -63.461   7.889  -3.018  1.00 90.63           N  
ANISOU 4620  NZ  LYS B 211    11929  10582  11923     23    310    -48       N  
ATOM   4621  N   PHE B 212     -60.762   9.779  -9.794  1.00 41.59           N  
ANISOU 4621  N   PHE B 212     5721   4434   5647    -73    194   -187       N  
ATOM   4622  CA  PHE B 212     -60.013  11.003 -10.079  1.00 53.27           C  
ANISOU 4622  CA  PHE B 212     7172   5959   7107    -50    137   -168       C  
ATOM   4623  C   PHE B 212     -60.567  11.746 -11.296  1.00 48.11           C  
ANISOU 4623  C   PHE B 212     6501   5345   6433    -84    100   -202       C  
ATOM   4624  O   PHE B 212     -60.668  12.973 -11.297  1.00 45.35           O  
ANISOU 4624  O   PHE B 212     6130   5031   6069    -73     57   -190       O  
ATOM   4625  CB  PHE B 212     -58.514  10.709 -10.248  1.00 60.45           C  
ANISOU 4625  CB  PHE B 212     8092   6862   8012     -8    158   -137       C  
ATOM   4626  CG  PHE B 212     -57.790  11.729 -11.075  1.00 49.46           C  
ANISOU 4626  CG  PHE B 212     6682   5509   6600     -9    115   -140       C  
ATOM   4627  CD1 PHE B 212     -57.476  12.971 -10.550  1.00 40.88           C  
ANISOU 4627  CD1 PHE B 212     5571   4464   5499     -2     75   -126       C  
ATOM   4628  CD2 PHE B 212     -57.444  11.452 -12.388  1.00 53.85           C  
ANISOU 4628  CD2 PHE B 212     7252   6059   7152    -23    123   -162       C  
ATOM   4629  CE1 PHE B 212     -56.814  13.926 -11.314  1.00 37.51           C  
ANISOU 4629  CE1 PHE B 212     5136   4061   5054     -9     50   -130       C  
ATOM   4630  CE2 PHE B 212     -56.786  12.396 -13.159  1.00 48.77           C  
ANISOU 4630  CE2 PHE B 212     6592   5449   6489    -22     88   -161       C  
ATOM   4631  CZ  PHE B 212     -56.471  13.641 -12.614  1.00 41.20           C  
ANISOU 4631  CZ  PHE B 212     5614   4522   5518    -15     54   -143       C  
ATOM   4632  N   GLU B 213     -60.940  10.994 -12.321  1.00 50.01           N  
ANISOU 4632  N   GLU B 213     6751   5582   6668   -125    127   -245       N  
ATOM   4633  CA  GLU B 213     -61.510  11.588 -13.527  1.00 52.81           C  
ANISOU 4633  CA  GLU B 213     7075   6000   6989   -153     96   -274       C  
ATOM   4634  C   GLU B 213     -62.891  12.178 -13.251  1.00 51.06           C  
ANISOU 4634  C   GLU B 213     6818   5837   6745   -166     69   -280       C  
ATOM   4635  O   GLU B 213     -63.193  13.298 -13.676  1.00 51.73           O  
ANISOU 4635  O   GLU B 213     6874   5980   6803   -142     32   -261       O  
ATOM   4636  CB  GLU B 213     -61.544  10.572 -14.678  1.00 53.18           C  
ANISOU 4636  CB  GLU B 213     7133   6046   7026   -204    137   -328       C  
ATOM   4637  CG  GLU B 213     -60.185   9.912 -14.929  1.00 66.53           C  
ANISOU 4637  CG  GLU B 213     8865   7674   8740   -180    175   -316       C  
ATOM   4638  CD  GLU B 213     -60.084   9.237 -16.285  1.00 75.29           C  
ANISOU 4638  CD  GLU B 213     9982   8792   9833   -228    208   -370       C  
ATOM   4639  OE1 GLU B 213     -60.975   9.480 -17.125  1.00 85.74           O  
ANISOU 4639  OE1 GLU B 213    11265  10193  11119   -277    188   -415       O  
ATOM   4640  OE2 GLU B 213     -59.115   8.472 -16.513  1.00 66.76           O  
ANISOU 4640  OE2 GLU B 213     8944   7651   8771   -212    257   -366       O  
ATOM   4641  N   ASN B 214     -63.723  11.434 -12.526  1.00 57.04           N  
ANISOU 4641  N   ASN B 214     7580   6581   7512   -198     94   -301       N  
ATOM   4642  CA  ASN B 214     -65.074  11.897 -12.186  1.00 56.23           C  
ANISOU 4642  CA  ASN B 214     7438   6544   7381   -210     71   -306       C  
ATOM   4643  C   ASN B 214     -65.070  13.224 -11.451  1.00 44.95           C  
ANISOU 4643  C   ASN B 214     6000   5125   5955   -149     29   -252       C  
ATOM   4644  O   ASN B 214     -65.855  14.119 -11.749  1.00 55.72           O  
ANISOU 4644  O   ASN B 214     7330   6559   7283   -129      4   -239       O  
ATOM   4645  CB  ASN B 214     -65.792  10.857 -11.334  1.00 56.74           C  
ANISOU 4645  CB  ASN B 214     7517   6578   7463   -254    111   -333       C  
ATOM   4646  CG  ASN B 214     -66.125   9.610 -12.113  1.00 61.55           C  
ANISOU 4646  CG  ASN B 214     8138   7186   8062   -337    170   -405       C  
ATOM   4647  OD1 ASN B 214     -66.268   9.651 -13.342  1.00 60.80           O  
ANISOU 4647  OD1 ASN B 214     8015   7159   7928   -374    165   -444       O  
ATOM   4648  ND2 ASN B 214     -66.250   8.489 -11.409  1.00 54.03           N  
ANISOU 4648  ND2 ASN B 214     7229   6156   7142   -371    235   -424       N  
ATOM   4649  N   TYR B 215     -64.171  13.338 -10.485  1.00 45.08           N  
ANISOU 4649  N   TYR B 215     6045   5076   6006   -117     32   -221       N  
ATOM   4650  CA  TYR B 215     -64.014  14.569  -9.732  1.00 41.55           C  
ANISOU 4650  CA  TYR B 215     5597   4629   5562    -74      7   -183       C  
ATOM   4651  C   TYR B 215     -63.376  15.679 -10.566  1.00 40.48           C  
ANISOU 4651  C   TYR B 215     5464   4505   5412    -49     -6   -166       C  
ATOM   4652  O   TYR B 215     -63.735  16.844 -10.409  1.00 42.02           O  
ANISOU 4652  O   TYR B 215     5658   4714   5595    -20    -14   -143       O  
ATOM   4653  CB  TYR B 215     -63.189  14.310  -8.476  1.00 47.79           C  
ANISOU 4653  CB  TYR B 215     6404   5374   6380    -59     18   -163       C  
ATOM   4654  CG  TYR B 215     -63.899  13.478  -7.434  1.00 50.39           C  
ANISOU 4654  CG  TYR B 215     6732   5690   6724    -68     35   -165       C  
ATOM   4655  CD1 TYR B 215     -65.070  12.798  -7.743  1.00 49.93           C  
ANISOU 4655  CD1 TYR B 215     6666   5648   6658   -106     47   -195       C  
ATOM   4656  CD2 TYR B 215     -63.386  13.360  -6.143  1.00 48.68           C  
ANISOU 4656  CD2 TYR B 215     6517   5457   6522    -44     43   -138       C  
ATOM   4657  CE1 TYR B 215     -65.716  12.029  -6.803  1.00 52.12           C  
ANISOU 4657  CE1 TYR B 215     6947   5908   6950   -121     71   -198       C  
ATOM   4658  CE2 TYR B 215     -64.019  12.591  -5.194  1.00 48.60           C  
ANISOU 4658  CE2 TYR B 215     6507   5434   6525    -46     64   -133       C  
ATOM   4659  CZ  TYR B 215     -65.186  11.927  -5.526  1.00 50.46           C  
ANISOU 4659  CZ  TYR B 215     6745   5667   6761    -85     80   -162       C  
ATOM   4660  OH  TYR B 215     -65.812  11.156  -4.573  1.00 48.60           O  
ANISOU 4660  OH  TYR B 215     6514   5413   6540    -92    108   -158       O  
ATOM   4661  N   ALA B 216     -62.428  15.328 -11.440  1.00 37.65           N  
ANISOU 4661  N   ALA B 216     5115   4135   5055    -57      0   -175       N  
ATOM   4662  CA  ALA B 216     -61.856  16.313 -12.374  1.00 40.04           C  
ANISOU 4662  CA  ALA B 216     5421   4451   5342    -36     -7   -160       C  
ATOM   4663  C   ALA B 216     -62.919  16.930 -13.289  1.00 37.43           C  
ANISOU 4663  C   ALA B 216     5063   4184   4973    -19    -14   -152       C  
ATOM   4664  O   ALA B 216     -62.950  18.152 -13.481  1.00 33.24           O  
ANISOU 4664  O   ALA B 216     4540   3658   4430     21     -8   -118       O  
ATOM   4665  CB  ALA B 216     -60.722  15.706 -13.208  1.00 32.36           C  
ANISOU 4665  CB  ALA B 216     4458   3464   4373    -48      0   -173       C  
ATOM   4666  N   ARG B 217     -63.776  16.081 -13.855  1.00 43.97           N  
ANISOU 4666  N   ARG B 217     5860   5071   5777    -48    -16   -182       N  
ATOM   4667  CA  ARG B 217     -64.887  16.544 -14.694  1.00 53.31           C  
ANISOU 4667  CA  ARG B 217     6995   6356   6904    -30    -23   -174       C  
ATOM   4668  C   ARG B 217     -65.689  17.639 -13.997  1.00 41.70           C  
ANISOU 4668  C   ARG B 217     5521   4902   5422     24    -23   -127       C  
ATOM   4669  O   ARG B 217     -65.970  18.686 -14.584  1.00 44.05           O  
ANISOU 4669  O   ARG B 217     5808   5243   5686     84    -13    -82       O  
ATOM   4670  CB  ARG B 217     -65.815  15.386 -15.076  1.00 55.75           C  
ANISOU 4670  CB  ARG B 217     7261   6740   7181    -93    -19   -229       C  
ATOM   4671  CG  ARG B 217     -65.115  14.252 -15.819  1.00 75.76           C  
ANISOU 4671  CG  ARG B 217     9807   9251   9725   -152     -1   -282       C  
ATOM   4672  CD  ARG B 217     -66.016  13.021 -15.928  1.00 95.13           C  
ANISOU 4672  CD  ARG B 217    12237  11752  12156   -235     25   -352       C  
ATOM   4673  NE  ARG B 217     -65.406  11.937 -16.700  1.00114.09           N  
ANISOU 4673  NE  ARG B 217    14659  14123  14566   -296     61   -410       N  
ATOM   4674  CZ  ARG B 217     -65.948  10.728 -16.839  1.00129.38           C  
ANISOU 4674  CZ  ARG B 217    16596  16069  16493   -386    107   -485       C  
ATOM   4675  NH1 ARG B 217     -65.337   9.794 -17.557  1.00130.93           N  
ANISOU 4675  NH1 ARG B 217    16824  16226  16700   -439    154   -538       N  
ATOM   4676  NH2 ARG B 217     -67.108  10.449 -16.252  1.00137.61           N  
ANISOU 4676  NH2 ARG B 217    17614  17158  17515   -429    117   -512       N  
ATOM   4677  N   ILE B 218     -66.053  17.390 -12.742  1.00 43.29           N  
ANISOU 4677  N   ILE B 218     5734   5066   5649     11    -24   -133       N  
ATOM   4678  CA  ILE B 218     -66.804  18.356 -11.945  1.00 41.25           C  
ANISOU 4678  CA  ILE B 218     5478   4812   5382     59    -20    -94       C  
ATOM   4679  C   ILE B 218     -66.052  19.678 -11.794  1.00 46.40           C  
ANISOU 4679  C   ILE B 218     6179   5396   6054    107      5    -54       C  
ATOM   4680  O   ILE B 218     -66.633  20.764 -11.923  1.00 46.82           O  
ANISOU 4680  O   ILE B 218     6237   5469   6082    170     30     -8       O  
ATOM   4681  CB  ILE B 218     -67.089  17.803 -10.544  1.00 42.34           C  
ANISOU 4681  CB  ILE B 218     5626   4910   5553     31    -25   -112       C  
ATOM   4682  CG1 ILE B 218     -67.940  16.537 -10.632  1.00 43.57           C  
ANISOU 4682  CG1 ILE B 218     5743   5123   5689    -25    -32   -155       C  
ATOM   4683  CG2 ILE B 218     -67.731  18.880  -9.669  1.00 37.90           C  
ANISOU 4683  CG2 ILE B 218     5074   4341   4986     81    -16    -73       C  
ATOM   4684  CD1 ILE B 218     -68.139  15.850  -9.278  1.00 47.36           C  
ANISOU 4684  CD1 ILE B 218     6237   5553   6204    -53    -29   -169       C  
ATOM   4685  N   VAL B 219     -64.758  19.584 -11.507  1.00 36.85           N  
ANISOU 4685  N   VAL B 219     5006   4111   4885     78      8    -72       N  
ATOM   4686  CA  VAL B 219     -63.954  20.781 -11.362  1.00 36.62           C  
ANISOU 4686  CA  VAL B 219     5024   4020   4870     98     40    -51       C  
ATOM   4687  C   VAL B 219     -63.870  21.523 -12.700  1.00 43.65           C  
ANISOU 4687  C   VAL B 219     5919   4933   5734    141     63    -18       C  
ATOM   4688  O   VAL B 219     -63.990  22.756 -12.746  1.00 37.74           O  
ANISOU 4688  O   VAL B 219     5207   4154   4980    189    111     21       O  
ATOM   4689  CB  VAL B 219     -62.573  20.455 -10.757  1.00 41.04           C  
ANISOU 4689  CB  VAL B 219     5604   4527   5462     49     37    -82       C  
ATOM   4690  CG1 VAL B 219     -61.592  21.624 -10.954  1.00 41.63           C  
ANISOU 4690  CG1 VAL B 219     5721   4553   5541     47     76    -76       C  
ATOM   4691  CG2 VAL B 219     -62.737  20.126  -9.284  1.00 39.58           C  
ANISOU 4691  CG2 VAL B 219     5416   4327   5295     28     30    -97       C  
ATOM   4692  N   PHE B 220     -63.691  20.773 -13.788  1.00 51.48           N  
ANISOU 4692  N   PHE B 220     6877   5976   6707    128     39    -31       N  
ATOM   4693  CA  PHE B 220     -63.751  21.367 -15.124  1.00 59.68           C  
ANISOU 4693  CA  PHE B 220     7904   7062   7709    175     57      5       C  
ATOM   4694  C   PHE B 220     -65.028  22.211 -15.255  1.00 52.49           C  
ANISOU 4694  C   PHE B 220     6977   6213   6754    255     85     62       C  
ATOM   4695  O   PHE B 220     -64.969  23.414 -15.534  1.00 54.69           O  
ANISOU 4695  O   PHE B 220     7293   6462   7026    320    139    117       O  
ATOM   4696  CB  PHE B 220     -63.688  20.299 -16.232  1.00 62.68           C  
ANISOU 4696  CB  PHE B 220     8235   7518   8063    144     25    -27       C  
ATOM   4697  CG  PHE B 220     -62.357  19.594 -16.339  1.00 84.20           C  
ANISOU 4697  CG  PHE B 220    10982  10185  10824     90     12    -66       C  
ATOM   4698  CD1 PHE B 220     -61.273  20.014 -15.591  1.00100.29           C  
ANISOU 4698  CD1 PHE B 220    13068  12134  12901     75     25    -68       C  
ATOM   4699  CD2 PHE B 220     -62.180  18.523 -17.205  1.00 81.72           C  
ANISOU 4699  CD2 PHE B 220    10638   9916  10496     52     -7   -104       C  
ATOM   4700  CE1 PHE B 220     -60.043  19.375 -15.688  1.00 92.32           C  
ANISOU 4700  CE1 PHE B 220    12069  11095  11913     37     15    -95       C  
ATOM   4701  CE2 PHE B 220     -60.945  17.884 -17.306  1.00 78.86           C  
ANISOU 4701  CE2 PHE B 220    10300   9501  10164     17    -10   -131       C  
ATOM   4702  CZ  PHE B 220     -59.882  18.313 -16.548  1.00 80.24           C  
ANISOU 4702  CZ  PHE B 220    10514   9600  10372     16     -2   -121       C  
ATOM   4703  N   GLN B 221     -66.179  21.584 -15.040  1.00 46.32           N  
ANISOU 4703  N   GLN B 221     6141   5519   5941    251     58     53       N  
ATOM   4704  CA  GLN B 221     -67.460  22.296 -15.128  1.00 52.03           C  
ANISOU 4704  CA  GLN B 221     6833   6329   6608    334     82    112       C  
ATOM   4705  C   GLN B 221     -67.556  23.481 -14.168  1.00 50.27           C  
ANISOU 4705  C   GLN B 221     6677   6011   6414    389    135    156       C  
ATOM   4706  O   GLN B 221     -68.152  24.496 -14.507  1.00 55.46           O  
ANISOU 4706  O   GLN B 221     7341   6697   7033    486    188    230       O  
ATOM   4707  CB  GLN B 221     -68.635  21.340 -14.916  1.00 52.20           C  
ANISOU 4707  CB  GLN B 221     6780   6467   6588    302     42     81       C  
ATOM   4708  CG  GLN B 221     -68.586  20.134 -15.834  1.00 70.20           C  
ANISOU 4708  CG  GLN B 221     9001   8835   8838    229      7     21       C  
ATOM   4709  CD  GLN B 221     -69.708  19.146 -15.582  1.00 91.33           C  
ANISOU 4709  CD  GLN B 221    11610  11618  11472    172    -18    -27       C  
ATOM   4710  OE1 GLN B 221     -69.797  18.111 -16.250  1.00100.37           O  
ANISOU 4710  OE1 GLN B 221    12710  12835  12590     96    -33    -89       O  
ATOM   4711  NE2 GLN B 221     -70.575  19.458 -14.618  1.00 92.93           N  
ANISOU 4711  NE2 GLN B 221    11809  11831  11669    201    -15     -3       N  
ATOM   4712  N   PHE B 222     -66.962  23.356 -12.982  1.00 46.42           N  
ANISOU 4712  N   PHE B 222     6236   5415   5985    329    130    114       N  
ATOM   4713  CA  PHE B 222     -66.977  24.434 -11.986  1.00 47.76           C  
ANISOU 4713  CA  PHE B 222     6473   5491   6183    359    186    137       C  
ATOM   4714  C   PHE B 222     -66.170  25.652 -12.422  1.00 55.13           C  
ANISOU 4714  C   PHE B 222     7480   6335   7132    391    263    168       C  
ATOM   4715  O   PHE B 222     -66.585  26.790 -12.206  1.00 60.94           O  
ANISOU 4715  O   PHE B 222     8267   7024   7863    459    341    218       O  
ATOM   4716  CB  PHE B 222     -66.466  23.929 -10.629  1.00 43.71           C  
ANISOU 4716  CB  PHE B 222     5979   4910   5720    277    160     76       C  
ATOM   4717  CG  PHE B 222     -66.336  25.004  -9.585  1.00 46.50           C  
ANISOU 4717  CG  PHE B 222     6398   5170   6099    284    221     80       C  
ATOM   4718  CD1 PHE B 222     -67.343  25.935  -9.396  1.00 56.31           C  
ANISOU 4718  CD1 PHE B 222     7665   6412   7321    365    276    134       C  
ATOM   4719  CD2 PHE B 222     -65.225  25.061  -8.763  1.00 55.44           C  
ANISOU 4719  CD2 PHE B 222     7565   6229   7271    208    228     26       C  
ATOM   4720  CE1 PHE B 222     -67.233  26.921  -8.419  1.00 55.20           C  
ANISOU 4720  CE1 PHE B 222     7594   6174   7205    363    346    129       C  
ATOM   4721  CE2 PHE B 222     -65.109  26.044  -7.782  1.00 57.85           C  
ANISOU 4721  CE2 PHE B 222     7929   6458   7593    196    291     14       C  
ATOM   4722  CZ  PHE B 222     -66.117  26.972  -7.611  1.00 49.98           C  
ANISOU 4722  CZ  PHE B 222     6967   5439   6584    270    353     62       C  
ATOM   4723  N   ASN B 223     -65.005  25.416 -13.017  1.00 55.86           N  
ANISOU 4723  N   ASN B 223     7583   6398   7244    342    251    138       N  
ATOM   4724  CA  ASN B 223     -64.207  26.511 -13.562  1.00 50.84           C  
ANISOU 4724  CA  ASN B 223     7015   5684   6620    363    328    163       C  
ATOM   4725  C   ASN B 223     -64.923  27.187 -14.718  1.00 50.65           C  
ANISOU 4725  C   ASN B 223     6983   5716   6547    477    377    250       C  
ATOM   4726  O   ASN B 223     -64.931  28.414 -14.807  1.00 56.99           O  
ANISOU 4726  O   ASN B 223     7857   6444   7352    540    477    303       O  
ATOM   4727  CB  ASN B 223     -62.814  26.029 -13.971  1.00 44.29           C  
ANISOU 4727  CB  ASN B 223     6185   4829   5813    285    298    113       C  
ATOM   4728  CG  ASN B 223     -61.836  26.047 -12.812  1.00 48.58           C  
ANISOU 4728  CG  ASN B 223     6764   5297   6396    193    302     48       C  
ATOM   4729  OD1 ASN B 223     -61.914  26.917 -11.942  1.00 53.13           O  
ANISOU 4729  OD1 ASN B 223     7395   5804   6987    184    364     41       O  
ATOM   4730  ND2 ASN B 223     -60.913  25.087 -12.788  1.00 41.59           N  
ANISOU 4730  ND2 ASN B 223     5846   4436   5521    125    242     -1       N  
ATOM   4731  N   ASN B 224     -65.529  26.380 -15.591  1.00 48.53           N  
ANISOU 4731  N   ASN B 224     6627   5584   6228    504    316    265       N  
ATOM   4732  CA  ASN B 224     -66.373  26.892 -16.674  1.00 57.29           C  
ANISOU 4732  CA  ASN B 224     7699   6799   7270    622    353    353       C  
ATOM   4733  C   ASN B 224     -67.436  27.876 -16.179  1.00 63.87           C  
ANISOU 4733  C   ASN B 224     8561   7630   8078    729    428    431       C  
ATOM   4734  O   ASN B 224     -67.610  28.957 -16.741  1.00 64.20           O  
ANISOU 4734  O   ASN B 224     8643   7655   8094    840    523    519       O  
ATOM   4735  CB  ASN B 224     -67.066  25.745 -17.418  1.00 56.40           C  
ANISOU 4735  CB  ASN B 224     7470   6865   7094    610    270    336       C  
ATOM   4736  CG  ASN B 224     -66.141  25.026 -18.398  1.00 66.02           C  
ANISOU 4736  CG  ASN B 224     8661   8108   8315    548    226    292       C  
ATOM   4737  OD1 ASN B 224     -64.982  25.411 -18.593  1.00 56.87           O  
ANISOU 4737  OD1 ASN B 224     7564   6844   7201    524    252    283       O  
ATOM   4738  ND2 ASN B 224     -66.659  23.969 -19.023  1.00 67.84           N  
ANISOU 4738  ND2 ASN B 224     8798   8484   8495    515    164    257       N  
ATOM   4739  N   SER B 225     -68.151  27.484 -15.129  1.00 66.93           N  
ANISOU 4739  N   SER B 225     8928   8033   8470    704    394    403       N  
ATOM   4740  CA  SER B 225     -69.191  28.320 -14.547  1.00 65.39           C  
ANISOU 4740  CA  SER B 225     8757   7838   8250    803    460    471       C  
ATOM   4741  C   SER B 225     -68.618  29.612 -13.965  1.00 66.08           C  
ANISOU 4741  C   SER B 225     8975   7740   8393    825    578    491       C  
ATOM   4742  O   SER B 225     -69.240  30.665 -14.062  1.00 69.48           O  
ANISOU 4742  O   SER B 225     9451   8151   8796    948    682    582       O  
ATOM   4743  CB  SER B 225     -69.950  27.544 -13.473  1.00 66.88           C  
ANISOU 4743  CB  SER B 225     8899   8073   8439    752    392    424       C  
ATOM   4744  OG  SER B 225     -70.607  28.430 -12.586  1.00 71.20           O  
ANISOU 4744  OG  SER B 225     9500   8563   8991    820    463    468       O  
ATOM   4745  N   ARG B 226     -67.436  29.531 -13.361  1.00 60.94           N  
ANISOU 4745  N   ARG B 226     8383   6961   7812    706    572    407       N  
ATOM   4746  CA  ARG B 226     -66.755  30.721 -12.855  1.00 60.94           C  
ANISOU 4746  CA  ARG B 226     8505   6790   7860    693    691    402       C  
ATOM   4747  C   ARG B 226     -66.501  31.741 -13.955  1.00 64.51           C  
ANISOU 4747  C   ARG B 226     9018   7197   8297    785    802    482       C  
ATOM   4748  O   ARG B 226     -66.609  32.943 -13.721  1.00 68.20           O  
ANISOU 4748  O   ARG B 226     9587   7547   8778    845    941    528       O  
ATOM   4749  CB  ARG B 226     -65.416  30.355 -12.220  1.00 61.36           C  
ANISOU 4749  CB  ARG B 226     8585   6760   7970    539    656    292       C  
ATOM   4750  CG  ARG B 226     -65.516  29.433 -11.027  1.00 63.15           C  
ANISOU 4750  CG  ARG B 226     8764   7016   8214    453    565    218       C  
ATOM   4751  CD  ARG B 226     -64.149  28.864 -10.673  1.00 60.35           C  
ANISOU 4751  CD  ARG B 226     8405   6632   7895    322    516    127       C  
ATOM   4752  NE  ARG B 226     -63.217  29.903 -10.269  1.00 55.60           N  
ANISOU 4752  NE  ARG B 226     7894   5911   7322    262    615     89       N  
ATOM   4753  CZ  ARG B 226     -61.944  29.688  -9.968  1.00 58.58           C  
ANISOU 4753  CZ  ARG B 226     8272   6269   7716    149    598     12       C  
ATOM   4754  NH1 ARG B 226     -61.440  28.465 -10.040  1.00 54.19           N  
ANISOU 4754  NH1 ARG B 226     7638   5795   7156    102    489    -21       N  
ATOM   4755  NH2 ARG B 226     -61.177  30.702  -9.596  1.00 62.08           N  
ANISOU 4755  NH2 ARG B 226     8797   6617   8176     83    700    -32       N  
ATOM   4756  N   GLN B 227     -66.154  31.256 -15.147  1.00 68.04           N  
ANISOU 4756  N   GLN B 227     9406   7730   8717    795    751    498       N  
ATOM   4757  CA  GLN B 227     -65.821  32.128 -16.282  1.00 77.72           C  
ANISOU 4757  CA  GLN B 227    10680   8923   9927    881    850    576       C  
ATOM   4758  C   GLN B 227     -67.041  32.667 -17.012  1.00 83.65           C  
ANISOU 4758  C   GLN B 227    11401   9779  10603   1065    913    712       C  
ATOM   4759  O   GLN B 227     -67.107  33.856 -17.322  1.00 88.44           O  
ANISOU 4759  O   GLN B 227    12097  10299  11206   1172   1059    800       O  
ATOM   4760  CB  GLN B 227     -64.911  31.414 -17.286  1.00 74.51           C  
ANISOU 4760  CB  GLN B 227    10219   8573   9516    820    772    541       C  
ATOM   4761  CG  GLN B 227     -63.434  31.668 -17.068  1.00 75.02           C  
ANISOU 4761  CG  GLN B 227    10361   8498   9644    699    802    463       C  
ATOM   4762  CD  GLN B 227     -62.559  31.014 -18.125  1.00 73.10           C  
ANISOU 4762  CD  GLN B 227    10067   8315   9393    655    732    439       C  
ATOM   4763  OE1 GLN B 227     -62.533  31.430 -19.286  1.00 72.95           O  
ANISOU 4763  OE1 GLN B 227    10046   8328   9342    739    778    511       O  
ATOM   4764  NE2 GLN B 227     -61.824  29.992 -17.719  1.00 71.01           N  
ANISOU 4764  NE2 GLN B 227     9759   8067   9153    532    629    343       N  
ATOM   4765  N   ALA B 228     -67.992  31.789 -17.312  1.00 84.76           N  
ANISOU 4765  N   ALA B 228    11415  10115  10677   1103    811    730       N  
ATOM   4766  CA  ALA B 228     -69.248  32.218 -17.903  1.00 86.24           C  
ANISOU 4766  CA  ALA B 228    11548  10447  10773   1278    860    857       C  
ATOM   4767  C   ALA B 228     -69.962  33.111 -16.900  1.00 92.36           C  
ANISOU 4767  C   ALA B 228    12402  11129  11559   1356    963    907       C  
ATOM   4768  O   ALA B 228     -70.929  33.794 -17.237  1.00 99.97           O  
ANISOU 4768  O   ALA B 228    13358  12171  12456   1527   1048   1033       O  
ATOM   4769  CB  ALA B 228     -70.107  31.020 -18.266  1.00 86.23           C  
ANISOU 4769  CB  ALA B 228    11387  10684  10693   1266    726    838       C  
ATOM   4770  N   ASN B 229     -69.473  33.093 -15.663  1.00 93.37           N  
ANISOU 4770  N   ASN B 229    12605  11103  11768   1234    959    811       N  
ATOM   4771  CA  ASN B 229     -69.973  33.978 -14.619  1.00100.87           C  
ANISOU 4771  CA  ASN B 229    13648  11935  12742   1283   1066    838       C  
ATOM   4772  C   ASN B 229     -71.335  33.534 -14.088  1.00101.42           C  
ANISOU 4772  C   ASN B 229    13630  12151  12753   1345   1007    869       C  
ATOM   4773  O   ASN B 229     -71.851  34.086 -13.116  1.00105.89           O  
ANISOU 4773  O   ASN B 229    14257  12641  13336   1378   1073    882       O  
ATOM   4774  CB  ASN B 229     -70.034  35.412 -15.148  1.00109.00           C  
ANISOU 4774  CB  ASN B 229    14791  12860  13763   1434   1259    958       C  
ATOM   4775  CG  ASN B 229     -70.367  36.414 -14.076  1.00117.06           C  
ANISOU 4775  CG  ASN B 229    15939  13719  14821   1470   1399    974       C  
ATOM   4776  OD1 ASN B 229     -69.477  37.049 -13.510  1.00119.53           O  
ANISOU 4776  OD1 ASN B 229    16379  13827  15209   1374   1493    905       O  
ATOM   4777  ND2 ASN B 229     -71.655  36.561 -13.781  1.00121.53           N  
ANISOU 4777  ND2 ASN B 229    16467  14381  15328   1602   1419   1059       N  
ATOM   4778  N   GLY B 230     -71.903  32.518 -14.726  1.00 98.38           N  
ANISOU 4778  N   GLY B 230    13100  11982  12298   1350    884    872       N  
ATOM   4779  CA  GLY B 230     -73.222  32.037 -14.372  1.00 97.98           C  
ANISOU 4779  CA  GLY B 230    12949  12102  12176   1402    825    900       C  
ATOM   4780  C   GLY B 230     -73.246  31.228 -13.092  1.00100.69           C  
ANISOU 4780  C   GLY B 230    13280  12406  12572   1262    732    786       C  
ATOM   4781  O   GLY B 230     -72.420  31.416 -12.199  1.00 96.43           O  
ANISOU 4781  O   GLY B 230    12834  11684  12120   1162    751    711       O  
ATOM   4782  N   ASN B 231     -74.208  30.317 -13.009  1.00105.76           N  
ANISOU 4782  N   ASN B 231    13800  13233  13151   1252    634    773       N  
ATOM   4783  CA  ASN B 231     -74.412  29.517 -11.810  1.00102.67           C  
ANISOU 4783  CA  ASN B 231    13389  12824  12797   1137    551    681       C  
ATOM   4784  C   ASN B 231     -73.809  28.121 -11.921  1.00 95.85           C  
ANISOU 4784  C   ASN B 231    12462  11996  11961    978    427    568       C  
ATOM   4785  O   ASN B 231     -73.529  27.635 -13.020  1.00100.49           O  
ANISOU 4785  O   ASN B 231    12992  12675  12516    962    390    562       O  
ATOM   4786  CB  ASN B 231     -75.908  29.430 -11.484  1.00105.81           C  
ANISOU 4786  CB  ASN B 231    13704  13387  13111   1222    538    737       C  
ATOM   4787  CG  ASN B 231     -76.715  28.810 -12.611  1.00105.78           C  
ANISOU 4787  CG  ASN B 231    13555  13646  12991   1266    482    773       C  
ATOM   4788  OD1 ASN B 231     -76.600  27.616 -12.893  1.00106.84           O  
ANISOU 4788  OD1 ASN B 231    13607  13871  13115   1145    381    686       O  
ATOM   4789  ND2 ASN B 231     -77.544  29.620 -13.257  1.00104.82           N  
ANISOU 4789  ND2 ASN B 231    13399  13654  12774   1441    559    902       N  
ATOM   4790  N   PHE B 232     -73.602  27.495 -10.768  1.00 82.88           N  
ANISOU 4790  N   PHE B 232    10834  10279  10377    867    373    483       N  
ATOM   4791  CA  PHE B 232     -73.163  26.108 -10.693  1.00 72.62           C  
ANISOU 4791  CA  PHE B 232     9481   9008   9103    728    271    384       C  
ATOM   4792  C   PHE B 232     -73.312  25.636  -9.259  1.00 66.96           C  
ANISOU 4792  C   PHE B 232     8777   8231   8432    654    235    325       C  
ATOM   4793  O   PHE B 232     -73.195  26.427  -8.320  1.00 72.78           O  
ANISOU 4793  O   PHE B 232     9589   8855   9210    674    288    335       O  
ATOM   4794  CB  PHE B 232     -71.715  25.939 -11.169  1.00 71.28           C  
ANISOU 4794  CB  PHE B 232     9358   8734   8991    654    265    336       C  
ATOM   4795  CG  PHE B 232     -71.311  24.505 -11.371  1.00 63.84           C  
ANISOU 4795  CG  PHE B 232     8358   7837   8061    539    176    253       C  
ATOM   4796  CD1 PHE B 232     -71.799  23.781 -12.449  1.00 59.27           C  
ANISOU 4796  CD1 PHE B 232     7690   7413   7416    535    136    250       C  
ATOM   4797  CD2 PHE B 232     -70.454  23.876 -10.477  1.00 59.42           C  
ANISOU 4797  CD2 PHE B 232     7834   7171   7572    436    143    179       C  
ATOM   4798  CE1 PHE B 232     -71.443  22.452 -12.634  1.00 56.12           C  
ANISOU 4798  CE1 PHE B 232     7253   7040   7032    424     74    168       C  
ATOM   4799  CE2 PHE B 232     -70.088  22.549 -10.656  1.00 56.22           C  
ANISOU 4799  CE2 PHE B 232     7388   6795   7179    345     81    113       C  
ATOM   4800  CZ  PHE B 232     -70.585  21.836 -11.736  1.00 58.58           C  
ANISOU 4800  CZ  PHE B 232     7612   7224   7420    335     52    105       C  
ATOM   4801  N   ASP B 233     -73.587  24.347  -9.097  1.00 58.29           N  
ANISOU 4801  N   ASP B 233     7610   7212   7328    567    155    264       N  
ATOM   4802  CA  ASP B 233     -73.874  23.784  -7.788  1.00 50.55           C  
ANISOU 4802  CA  ASP B 233     6627   6198   6380    506    121    217       C  
ATOM   4803  C   ASP B 233     -72.923  22.635  -7.492  1.00 43.56           C  
ANISOU 4803  C   ASP B 233     5748   5251   5554    385     70    134       C  
ATOM   4804  O   ASP B 233     -73.265  21.479  -7.720  1.00 50.09           O  
ANISOU 4804  O   ASP B 233     6515   6156   6361    323     23     93       O  
ATOM   4805  CB  ASP B 233     -75.330  23.292  -7.750  1.00 64.24           C  
ANISOU 4805  CB  ASP B 233     8272   8098   8040    526     90    232       C  
ATOM   4806  CG  ASP B 233     -75.937  23.325  -6.348  1.00 73.99           C  
ANISOU 4806  CG  ASP B 233     9518   9301   9294    522     86    226       C  
ATOM   4807  OD1 ASP B 233     -75.174  23.258  -5.351  1.00 75.59           O  
ANISOU 4807  OD1 ASP B 233     9780   9370   9572    467     84    185       O  
ATOM   4808  OD2 ASP B 233     -77.186  23.409  -6.249  1.00 72.66           O  
ANISOU 4808  OD2 ASP B 233     9291   9259   9058    576     84    263       O  
ATOM   4809  N   ILE B 234     -71.728  22.944  -6.986  1.00 52.81           N  
ANISOU 4809  N   ILE B 234     6987   6287   6789    351     88    110       N  
ATOM   4810  CA  ILE B 234     -70.740  21.899  -6.695  1.00 58.54           C  
ANISOU 4810  CA  ILE B 234     7717   6964   7563    256     49     46       C  
ATOM   4811  C   ILE B 234     -71.311  20.760  -5.839  1.00 52.51           C  
ANISOU 4811  C   ILE B 234     6913   6234   6806    203      7     10       C  
ATOM   4812  O   ILE B 234     -71.152  19.582  -6.167  1.00 54.29           O  
ANISOU 4812  O   ILE B 234     7111   6484   7035    144    -21    -28       O  
ATOM   4813  CB  ILE B 234     -69.490  22.446  -5.974  1.00 71.55           C  
ANISOU 4813  CB  ILE B 234     9430   8493   9265    228     75     25       C  
ATOM   4814  CG1 ILE B 234     -69.131  23.838  -6.480  1.00 81.59           C  
ANISOU 4814  CG1 ILE B 234    10759   9709  10533    281    142     61       C  
ATOM   4815  CG2 ILE B 234     -68.309  21.494  -6.164  1.00 71.57           C  
ANISOU 4815  CG2 ILE B 234     9427   8469   9296    158     45    -20       C  
ATOM   4816  CD1 ILE B 234     -67.804  24.336  -5.945  1.00 84.85           C  
ANISOU 4816  CD1 ILE B 234    11229  10022  10988    228    174     23       C  
ATOM   4817  N   ALA B 235     -71.972  21.114  -4.742  1.00 45.15           N  
ANISOU 4817  N   ALA B 235     5984   5295   5875    224     13     23       N  
ATOM   4818  CA  ALA B 235     -72.499  20.111  -3.818  1.00 47.45           C  
ANISOU 4818  CA  ALA B 235     6244   5609   6175    177    -18     -6       C  
ATOM   4819  C   ALA B 235     -73.430  19.134  -4.521  1.00 54.31           C  
ANISOU 4819  C   ALA B 235     7050   6588   6999    148    -43    -22       C  
ATOM   4820  O   ALA B 235     -73.352  17.920  -4.311  1.00 53.18           O  
ANISOU 4820  O   ALA B 235     6893   6440   6874     78    -57    -65       O  
ATOM   4821  CB  ALA B 235     -73.207  20.771  -2.654  1.00 42.92           C  
ANISOU 4821  CB  ALA B 235     5679   5029   5601    214     -6     16       C  
ATOM   4822  N   ASN B 236     -74.313  19.661  -5.360  1.00 51.71           N  
ANISOU 4822  N   ASN B 236     6681   6363   6605    201    -36     12       N  
ATOM   4823  CA  ASN B 236     -75.269  18.806  -6.038  1.00 51.68           C  
ANISOU 4823  CA  ASN B 236     6601   6496   6538    162    -55    -12       C  
ATOM   4824  C   ASN B 236     -74.552  17.778  -6.894  1.00 51.74           C  
ANISOU 4824  C   ASN B 236     6606   6493   6560     82    -62    -68       C  
ATOM   4825  O   ASN B 236     -74.930  16.598  -6.933  1.00 53.12           O  
ANISOU 4825  O   ASN B 236     6750   6707   6725     -2    -67   -124       O  
ATOM   4826  CB  ASN B 236     -76.222  19.633  -6.892  1.00 71.73           C  
ANISOU 4826  CB  ASN B 236     9087   9179   8989    246    -44     43       C  
ATOM   4827  CG  ASN B 236     -77.392  18.823  -7.394  1.00 82.21           C  
ANISOU 4827  CG  ASN B 236    10317  10687  10233    199    -63     13       C  
ATOM   4828  OD1 ASN B 236     -78.235  18.383  -6.609  1.00 89.28           O  
ANISOU 4828  OD1 ASN B 236    11182  11628  11112    167    -75     -5       O  
ATOM   4829  ND2 ASN B 236     -77.450  18.612  -8.706  1.00 80.49           N  
ANISOU 4829  ND2 ASN B 236    10046  10584   9954    186    -64      1       N  
ATOM   4830  N   GLU B 237     -73.506  18.241  -7.572  1.00 48.26           N  
ANISOU 4830  N   GLU B 237     6202   5991   6142    106    -52    -54       N  
ATOM   4831  CA  GLU B 237     -72.707  17.400  -8.444  1.00 51.83           C  
ANISOU 4831  CA  GLU B 237     6659   6426   6609     44    -54   -100       C  
ATOM   4832  C   GLU B 237     -72.095  16.236  -7.688  1.00 52.74           C  
ANISOU 4832  C   GLU B 237     6808   6444   6786    -31    -51   -148       C  
ATOM   4833  O   GLU B 237     -72.182  15.088  -8.137  1.00 50.60           O  
ANISOU 4833  O   GLU B 237     6522   6194   6508   -106    -41   -202       O  
ATOM   4834  CB  GLU B 237     -71.616  18.233  -9.117  1.00 61.21           C  
ANISOU 4834  CB  GLU B 237     7887   7553   7816     91    -42    -69       C  
ATOM   4835  CG  GLU B 237     -72.168  19.371  -9.961  1.00 67.48           C  
ANISOU 4835  CG  GLU B 237     8655   8436   8549    179    -26     -9       C  
ATOM   4836  CD  GLU B 237     -73.000  18.866 -11.127  1.00 81.96           C  
ANISOU 4836  CD  GLU B 237    10404  10440  10299    163    -37    -24       C  
ATOM   4837  OE1 GLU B 237     -72.497  18.005 -11.876  1.00 89.32           O  
ANISOU 4837  OE1 GLU B 237    11324  11380  11232     93    -46    -77       O  
ATOM   4838  OE2 GLU B 237     -74.150  19.325 -11.297  1.00 86.52           O  
ANISOU 4838  OE2 GLU B 237    10921  11151  10800    219    -34     16       O  
ATOM   4839  N   PHE B 238     -71.482  16.528  -6.539  1.00 45.11           N  
ANISOU 4839  N   PHE B 238     5889   5378   5874    -10    -49   -130       N  
ATOM   4840  CA  PHE B 238     -70.873  15.486  -5.715  1.00 40.06           C  
ANISOU 4840  CA  PHE B 238     5277   4657   5286    -57    -40   -156       C  
ATOM   4841  C   PHE B 238     -71.925  14.597  -5.057  1.00 42.15           C  
ANISOU 4841  C   PHE B 238     5517   4955   5542   -102    -34   -181       C  
ATOM   4842  O   PHE B 238     -71.713  13.394  -4.843  1.00 45.78           O  
ANISOU 4842  O   PHE B 238     5994   5371   6029   -156     -6   -213       O  
ATOM   4843  CB  PHE B 238     -69.942  16.102  -4.660  1.00 42.20           C  
ANISOU 4843  CB  PHE B 238     5587   4847   5600    -22    -39   -129       C  
ATOM   4844  CG  PHE B 238     -68.605  16.540  -5.207  1.00 43.13           C  
ANISOU 4844  CG  PHE B 238     5735   4918   5736    -10    -34   -123       C  
ATOM   4845  CD1 PHE B 238     -68.418  17.831  -5.681  1.00 40.38           C  
ANISOU 4845  CD1 PHE B 238     5400   4571   5373     32    -30    -99       C  
ATOM   4846  CD2 PHE B 238     -67.538  15.655  -5.241  1.00 39.07           C  
ANISOU 4846  CD2 PHE B 238     5238   4357   5249    -35    -22   -138       C  
ATOM   4847  CE1 PHE B 238     -67.200  18.234  -6.177  1.00 45.46           C  
ANISOU 4847  CE1 PHE B 238     6071   5172   6030     33    -21    -99       C  
ATOM   4848  CE2 PHE B 238     -66.309  16.047  -5.740  1.00 43.76           C  
ANISOU 4848  CE2 PHE B 238     5853   4922   5852    -26    -19   -133       C  
ATOM   4849  CZ  PHE B 238     -66.136  17.342  -6.211  1.00 48.50           C  
ANISOU 4849  CZ  PHE B 238     6463   5526   6438      2    -21   -118       C  
ATOM   4850  N   ILE B 239     -73.059  15.198  -4.721  1.00 35.57           N  
ANISOU 4850  N   ILE B 239     4648   4197   4670    -75    -49   -162       N  
ATOM   4851  CA  ILE B 239     -74.184  14.432  -4.216  1.00 41.80           C  
ANISOU 4851  CA  ILE B 239     5404   5040   5438   -122    -45   -188       C  
ATOM   4852  C   ILE B 239     -74.589  13.414  -5.283  1.00 55.05           C  
ANISOU 4852  C   ILE B 239     7053   6785   7080   -206    -24   -249       C  
ATOM   4853  O   ILE B 239     -74.761  12.224  -5.002  1.00 63.62           O  
ANISOU 4853  O   ILE B 239     8149   7839   8182   -283     10   -295       O  
ATOM   4854  CB  ILE B 239     -75.367  15.361  -3.836  1.00 47.75           C  
ANISOU 4854  CB  ILE B 239     6115   5887   6141    -69    -66   -152       C  
ATOM   4855  CG1 ILE B 239     -75.073  16.058  -2.502  1.00 47.40           C  
ANISOU 4855  CG1 ILE B 239     6106   5763   6140    -15    -71   -113       C  
ATOM   4856  CG2 ILE B 239     -76.675  14.583  -3.761  1.00 40.49           C  
ANISOU 4856  CG2 ILE B 239     5139   5074   5173   -130    -63   -188       C  
ATOM   4857  CD1 ILE B 239     -75.885  17.309  -2.254  1.00 52.93           C  
ANISOU 4857  CD1 ILE B 239     6788   6521   6801     63    -78    -65       C  
ATOM   4858  N   SER B 240     -74.710  13.880  -6.519  1.00 45.82           N  
ANISOU 4858  N   SER B 240     5847   5706   5857   -194    -35   -250       N  
ATOM   4859  CA  SER B 240     -74.998  12.989  -7.635  1.00 56.91           C  
ANISOU 4859  CA  SER B 240     7216   7188   7217   -282    -14   -317       C  
ATOM   4860  C   SER B 240     -74.000  11.819  -7.776  1.00 63.04           C  
ANISOU 4860  C   SER B 240     8056   7841   8056   -350     30   -365       C  
ATOM   4861  O   SER B 240     -74.412  10.659  -7.888  1.00 69.12           O  
ANISOU 4861  O   SER B 240     8826   8617   8819   -449     76   -433       O  
ATOM   4862  CB  SER B 240     -75.078  13.795  -8.934  1.00 57.94           C  
ANISOU 4862  CB  SER B 240     7298   7436   7282   -239    -33   -297       C  
ATOM   4863  OG  SER B 240     -75.352  12.953 -10.032  1.00 63.45           O  
ANISOU 4863  OG  SER B 240     7952   8229   7927   -331    -13   -370       O  
ATOM   4864  N   ILE B 241     -72.701  12.122  -7.766  1.00 60.34           N  
ANISOU 4864  N   ILE B 241     7768   7389   7769   -298     27   -330       N  
ATOM   4865  CA  ILE B 241     -71.661  11.102  -7.952  1.00 54.37           C  
ANISOU 4865  CA  ILE B 241     7071   6523   7066   -339     72   -360       C  
ATOM   4866  C   ILE B 241     -71.541  10.138  -6.775  1.00 56.97           C  
ANISOU 4866  C   ILE B 241     7447   6749   7449   -360    118   -363       C  
ATOM   4867  O   ILE B 241     -71.237   8.955  -6.960  1.00 56.56           O  
ANISOU 4867  O   ILE B 241     7438   6630   7422   -418    184   -403       O  
ATOM   4868  CB  ILE B 241     -70.279  11.738  -8.214  1.00 56.82           C  
ANISOU 4868  CB  ILE B 241     7415   6763   7409   -271     54   -316       C  
ATOM   4869  CG1 ILE B 241     -70.250  12.389  -9.590  1.00 69.46           C  
ANISOU 4869  CG1 ILE B 241     8981   8449   8962   -261     31   -321       C  
ATOM   4870  CG2 ILE B 241     -69.174  10.696  -8.142  1.00 53.45           C  
ANISOU 4870  CG2 ILE B 241     7048   6224   7035   -290    104   -329       C  
ATOM   4871  CD1 ILE B 241     -68.869  12.806 -10.004  1.00 76.23           C  
ANISOU 4871  CD1 ILE B 241     9875   9238   9851   -216     24   -292       C  
ATOM   4872  N   LEU B 242     -71.787  10.649  -5.568  1.00 53.55           N  
ANISOU 4872  N   LEU B 242     7012   6304   7032   -309     92   -316       N  
ATOM   4873  CA  LEU B 242     -71.655   9.849  -4.350  1.00 60.13           C  
ANISOU 4873  CA  LEU B 242     7883   7051   7912   -311    133   -303       C  
ATOM   4874  C   LEU B 242     -72.922   9.051  -4.024  1.00 64.43           C  
ANISOU 4874  C   LEU B 242     8412   7630   8437   -388    169   -348       C  
ATOM   4875  O   LEU B 242     -72.865   8.059  -3.302  1.00 62.40           O  
ANISOU 4875  O   LEU B 242     8197   7292   8218   -411    231   -351       O  
ATOM   4876  CB  LEU B 242     -71.251  10.732  -3.152  1.00 52.08           C  
ANISOU 4876  CB  LEU B 242     6863   6010   6915   -227     93   -237       C  
ATOM   4877  CG  LEU B 242     -69.870  11.405  -3.205  1.00 48.91           C  
ANISOU 4877  CG  LEU B 242     6480   5568   6534   -165     73   -199       C  
ATOM   4878  CD1 LEU B 242     -69.791  12.578  -2.260  1.00 52.26           C  
ANISOU 4878  CD1 LEU B 242     6889   6009   6958   -108     30   -159       C  
ATOM   4879  CD2 LEU B 242     -68.758  10.415  -2.902  1.00 48.01           C  
ANISOU 4879  CD2 LEU B 242     6409   5371   6459   -153    125   -183       C  
ATOM   4880  N   SER B 243     -74.063   9.476  -4.556  1.00 66.47           N  
ANISOU 4880  N   SER B 243     8607   8016   8631   -424    137   -379       N  
ATOM   4881  CA  SER B 243     -75.321   8.818  -4.213  1.00 76.80           C  
ANISOU 4881  CA  SER B 243     9888   9382   9908   -504    166   -426       C  
ATOM   4882  C   SER B 243     -75.354   7.387  -4.736  1.00 82.38           C  
ANISOU 4882  C   SER B 243    10635  10041  10625   -620    259   -506       C  
ATOM   4883  O   SER B 243     -76.092   6.544  -4.223  1.00 81.22           O  
ANISOU 4883  O   SER B 243    10498   9883  10478   -696    316   -547       O  
ATOM   4884  CB  SER B 243     -76.512   9.609  -4.749  1.00 78.39           C  
ANISOU 4884  CB  SER B 243    10000   9763  10021   -512    114   -438       C  
ATOM   4885  OG  SER B 243     -76.403   9.791  -6.149  1.00 86.24           O  
ANISOU 4885  OG  SER B 243    10961  10841  10966   -535    105   -470       O  
ATOM   4886  N   SER B 244     -74.538   7.121  -5.752  1.00 86.77           N  
ANISOU 4886  N   SER B 244    11218  10562  11188   -637    283   -532       N  
ATOM   4887  CA  SER B 244     -74.461   5.795  -6.354  1.00 94.00           C  
ANISOU 4887  CA  SER B 244    12182  11418  12114   -748    386   -614       C  
ATOM   4888  C   SER B 244     -73.137   5.077  -6.049  1.00 95.21           C  
ANISOU 4888  C   SER B 244    12435  11390  12349   -702    456   -578       C  
ATOM   4889  O   SER B 244     -72.594   4.361  -6.893  1.00 99.32           O  
ANISOU 4889  O   SER B 244    13001  11855  12881   -751    524   -624       O  
ATOM   4890  CB  SER B 244     -74.690   5.888  -7.866  1.00100.83           C  
ANISOU 4890  CB  SER B 244    12997  12404  12911   -820    376   -686       C  
ATOM   4891  OG  SER B 244     -76.019   6.306  -8.146  1.00103.78           O  
ANISOU 4891  OG  SER B 244    13272  12967  13194   -874    335   -724       O  
ATOM   4892  N   ALA B 245     -72.624   5.277  -4.838  1.00 86.45           N  
ANISOU 4892  N   ALA B 245    11353  10204  11290   -603    443   -493       N  
ATOM   4893  CA  ALA B 245     -71.452   4.549  -4.365  1.00 80.76           C  
ANISOU 4893  CA  ALA B 245    10715   9337  10635   -544    517   -443       C  
ATOM   4894  C   ALA B 245     -71.774   3.895  -3.033  1.00 80.93           C  
ANISOU 4894  C   ALA B 245    10771   9287  10691   -527    578   -407       C  
ATOM   4895  O   ALA B 245     -72.575   4.413  -2.258  1.00 80.41           O  
ANISOU 4895  O   ALA B 245    10658   9286  10608   -519    524   -392       O  
ATOM   4896  CB  ALA B 245     -70.265   5.478  -4.219  1.00 78.45           C  
ANISOU 4896  CB  ALA B 245    10410   9043  10355   -425    444   -364       C  
ATOM   4897  N   ASN B 246     -71.144   2.756  -2.765  1.00 81.58           N  
ANISOU 4897  N   ASN B 246    10940   9236  10821   -513    699   -388       N  
ATOM   4898  CA  ASN B 246     -71.439   1.987  -1.559  1.00 73.05           C  
ANISOU 4898  CA  ASN B 246     9903   8077   9775   -494    782   -350       C  
ATOM   4899  C   ASN B 246     -70.299   1.971  -0.540  1.00 65.03           C  
ANISOU 4899  C   ASN B 246     8910   7004   8795   -345    795   -231       C  
ATOM   4900  O   ASN B 246     -69.119   1.877  -0.900  1.00 62.05           O  
ANISOU 4900  O   ASN B 246     8560   6587   8430   -276    815   -190       O  
ATOM   4901  CB  ASN B 246     -71.842   0.560  -1.930  1.00 79.86           C  
ANISOU 4901  CB  ASN B 246    10853   8830  10659   -602    944   -421       C  
ATOM   4902  CG  ASN B 246     -73.119   0.510  -2.757  1.00 88.50           C  
ANISOU 4902  CG  ASN B 246    11910  10014  11703   -768    938   -548       C  
ATOM   4903  OD1 ASN B 246     -73.082   0.279  -3.969  1.00 87.51           O  
ANISOU 4903  OD1 ASN B 246    11791   9905  11554   -854    965   -631       O  
ATOM   4904  ND2 ASN B 246     -74.258   0.732  -2.101  1.00 89.54           N  
ANISOU 4904  ND2 ASN B 246    11991  10222  11809   -812    903   -566       N  
ATOM   4905  N   GLY B 247     -70.670   2.067   0.733  1.00 57.33           N  
ANISOU 4905  N   GLY B 247     7914   6042   7826   -297    783   -176       N  
ATOM   4906  CA  GLY B 247     -69.713   2.053   1.827  1.00 58.78           C  
ANISOU 4906  CA  GLY B 247     8100   6207   8027   -158    795    -63       C  
ATOM   4907  C   GLY B 247     -69.996   3.091   2.902  1.00 53.88           C  
ANISOU 4907  C   GLY B 247     7397   5690   7384   -106    683    -20       C  
ATOM   4908  O   GLY B 247     -70.477   4.180   2.610  1.00 61.62           O  
ANISOU 4908  O   GLY B 247     8315   6763   8334   -141    569    -60       O  
ATOM   4909  N   THR B 248     -69.674   2.764   4.148  1.00 51.24           N  
ANISOU 4909  N   THR B 248     7063   5345   7060    -14    722     66       N  
ATOM   4910  CA  THR B 248     -69.958   3.665   5.265  1.00 53.96           C  
ANISOU 4910  CA  THR B 248     7332   5788   7382     30    629    102       C  
ATOM   4911  C   THR B 248     -69.338   5.053   5.081  1.00 50.76           C  
ANISOU 4911  C   THR B 248     6858   5484   6944     60    502    102       C  
ATOM   4912  O   THR B 248     -69.966   6.066   5.394  1.00 53.87           O  
ANISOU 4912  O   THR B 248     7198   5955   7317     38    410     78       O  
ATOM   4913  CB  THR B 248     -69.537   3.053   6.630  1.00 63.45           C  
ANISOU 4913  CB  THR B 248     8537   6980   8592    137    698    204       C  
ATOM   4914  OG1 THR B 248     -68.115   2.875   6.673  1.00 73.72           O  
ANISOU 4914  OG1 THR B 248     9839   8288   9883    244    731    279       O  
ATOM   4915  CG2 THR B 248     -70.225   1.706   6.850  1.00 49.84           C  
ANISOU 4915  CG2 THR B 248     6893   5139   6905    105    839    206       C  
ATOM   4916  N   ARG B 249     -68.112   5.104   4.570  1.00 44.14           N  
ANISOU 4916  N   ARG B 249     6027   4644   6101    109    508    127       N  
ATOM   4917  CA  ARG B 249     -67.454   6.390   4.329  1.00 46.69           C  
ANISOU 4917  CA  ARG B 249     6293   5054   6392    125    405    119       C  
ATOM   4918  C   ARG B 249     -68.171   7.196   3.250  1.00 48.12           C  
ANISOU 4918  C   ARG B 249     6467   5251   6567     39    335     38       C  
ATOM   4919  O   ARG B 249     -68.258   8.422   3.332  1.00 48.44           O  
ANISOU 4919  O   ARG B 249     6462   5360   6584     37    249     24       O  
ATOM   4920  CB  ARG B 249     -65.976   6.201   3.952  1.00 53.79           C  
ANISOU 4920  CB  ARG B 249     7200   5955   7281    190    433    162       C  
ATOM   4921  CG  ARG B 249     -65.084   5.736   5.098  1.00 60.32           C  
ANISOU 4921  CG  ARG B 249     8004   6826   8091    301    482    258       C  
ATOM   4922  CD  ARG B 249     -65.105   6.712   6.275  1.00 57.95           C  
ANISOU 4922  CD  ARG B 249     7621   6645   7753    325    405    275       C  
ATOM   4923  NE  ARG B 249     -64.107   6.361   7.284  1.00 61.59           N  
ANISOU 4923  NE  ARG B 249     8038   7188   8176    433    445    366       N  
ATOM   4924  CZ  ARG B 249     -64.067   6.871   8.516  1.00 64.50           C  
ANISOU 4924  CZ  ARG B 249     8332   7670   8505    467    408    395       C  
ATOM   4925  NH1 ARG B 249     -64.972   7.758   8.911  1.00 56.74           N  
ANISOU 4925  NH1 ARG B 249     7322   6712   7524    403    335    340       N  
ATOM   4926  NH2 ARG B 249     -63.119   6.490   9.362  1.00 68.13           N  
ANISOU 4926  NH2 ARG B 249     8739   8229   8917    570    450    481       N  
ATOM   4927  N   ASN B 250     -68.691   6.507   2.240  1.00 49.26           N  
ANISOU 4927  N   ASN B 250     6656   5335   6725    -31    381    -14       N  
ATOM   4928  CA  ASN B 250     -69.411   7.183   1.166  1.00 49.76           C  
ANISOU 4928  CA  ASN B 250     6701   5438   6769   -106    322    -85       C  
ATOM   4929  C   ASN B 250     -70.749   7.742   1.631  1.00 44.75           C  
ANISOU 4929  C   ASN B 250     6026   4865   6114   -142    272   -109       C  
ATOM   4930  O   ASN B 250     -71.130   8.861   1.265  1.00 43.89           O  
ANISOU 4930  O   ASN B 250     5875   4824   5975   -149    196   -128       O  
ATOM   4931  CB  ASN B 250     -69.580   6.257  -0.041  1.00 58.76           C  
ANISOU 4931  CB  ASN B 250     7888   6521   7916   -179    390   -143       C  
ATOM   4932  CG  ASN B 250     -68.263   5.996  -0.760  1.00 60.52           C  
ANISOU 4932  CG  ASN B 250     8145   6699   8151   -142    421   -125       C  
ATOM   4933  OD1 ASN B 250     -67.572   6.930  -1.167  1.00 65.96           O  
ANISOU 4933  OD1 ASN B 250     8804   7436   8823   -110    352   -115       O  
ATOM   4934  ND2 ASN B 250     -67.908   4.721  -0.912  1.00 52.83           N  
ANISOU 4934  ND2 ASN B 250     7238   5629   7205   -145    534   -120       N  
ATOM   4935  N   ALA B 251     -71.452   6.959   2.444  1.00 41.18           N  
ANISOU 4935  N   ALA B 251     5587   4386   5675   -159    323   -102       N  
ATOM   4936  CA  ALA B 251     -72.672   7.423   3.090  1.00 46.13           C  
ANISOU 4936  CA  ALA B 251     6171   5075   6282   -182    279   -114       C  
ATOM   4937  C   ALA B 251     -72.345   8.671   3.900  1.00 43.14           C  
ANISOU 4937  C   ALA B 251     5746   4755   5889   -110    199    -71       C  
ATOM   4938  O   ALA B 251     -73.079   9.659   3.864  1.00 42.93           O  
ANISOU 4938  O   ALA B 251     5681   4795   5834   -118    135    -88       O  
ATOM   4939  CB  ALA B 251     -73.257   6.328   3.999  1.00 46.98           C  
ANISOU 4939  CB  ALA B 251     6305   5134   6411   -199    357   -102       C  
ATOM   4940  N   GLN B 252     -71.225   8.623   4.614  1.00 37.83           N  
ANISOU 4940  N   GLN B 252     5078   4065   5231    -39    212    -16       N  
ATOM   4941  CA  GLN B 252     -70.801   9.747   5.433  1.00 33.41           C  
ANISOU 4941  CA  GLN B 252     4474   3566   4653     13    150     12       C  
ATOM   4942  C   GLN B 252     -70.476  10.970   4.573  1.00 37.83           C  
ANISOU 4942  C   GLN B 252     5023   4157   5194      5     92    -17       C  
ATOM   4943  O   GLN B 252     -70.938  12.075   4.860  1.00 45.12           O  
ANISOU 4943  O   GLN B 252     5920   5125   6098      9     42    -26       O  
ATOM   4944  CB  GLN B 252     -69.619   9.340   6.309  1.00 32.01           C  
ANISOU 4944  CB  GLN B 252     4291   3393   4480     84    185     73       C  
ATOM   4945  CG  GLN B 252     -69.121  10.433   7.232  1.00 41.26           C  
ANISOU 4945  CG  GLN B 252     5409   4646   5622    121    131     89       C  
ATOM   4946  CD  GLN B 252     -68.249   9.882   8.349  1.00 52.80           C  
ANISOU 4946  CD  GLN B 252     6842   6150   7071    191    169    155       C  
ATOM   4947  OE1 GLN B 252     -68.515  10.100   9.539  1.00 51.41           O  
ANISOU 4947  OE1 GLN B 252     6623   6032   6877    216    156    177       O  
ATOM   4948  NE2 GLN B 252     -67.207   9.150   7.970  1.00 51.00           N  
ANISOU 4948  NE2 GLN B 252     6632   5903   6843    232    220    191       N  
ATOM   4949  N   LEU B 253     -69.710  10.773   3.502  1.00 33.28           N  
ANISOU 4949  N   LEU B 253     4472   3550   4623     -3    106    -29       N  
ATOM   4950  CA  LEU B 253     -69.402  11.865   2.566  1.00 40.78           C  
ANISOU 4950  CA  LEU B 253     5416   4521   5556    -11     61    -53       C  
ATOM   4951  C   LEU B 253     -70.638  12.427   1.859  1.00 43.01           C  
ANISOU 4951  C   LEU B 253     5688   4836   5817    -46     31    -87       C  
ATOM   4952  O   LEU B 253     -70.801  13.652   1.753  1.00 44.73           O  
ANISOU 4952  O   LEU B 253     5893   5086   6016    -29     -7    -88       O  
ATOM   4953  CB  LEU B 253     -68.370  11.424   1.530  1.00 40.33           C  
ANISOU 4953  CB  LEU B 253     5388   4430   5508    -13     86    -58       C  
ATOM   4954  CG  LEU B 253     -66.973  11.204   2.102  1.00 41.58           C  
ANISOU 4954  CG  LEU B 253     5543   4589   5668     37    108    -16       C  
ATOM   4955  CD1 LEU B 253     -66.193  10.248   1.213  1.00 43.19           C  
ANISOU 4955  CD1 LEU B 253     5783   4742   5885     41    158    -12       C  
ATOM   4956  CD2 LEU B 253     -66.264  12.531   2.247  1.00 34.48           C  
ANISOU 4956  CD2 LEU B 253     4616   3738   4744     49     62    -20       C  
ATOM   4957  N   LEU B 254     -71.499  11.540   1.363  1.00 35.28           N  
ANISOU 4957  N   LEU B 254     4715   3855   4836    -95     57   -115       N  
ATOM   4958  CA  LEU B 254     -72.775  11.980   0.793  1.00 38.35           C  
ANISOU 4958  CA  LEU B 254     5073   4312   5187   -126     31   -144       C  
ATOM   4959  C   LEU B 254     -73.545  12.915   1.737  1.00 34.90           C  
ANISOU 4959  C   LEU B 254     4606   3922   4732    -91     -7   -121       C  
ATOM   4960  O   LEU B 254     -74.016  13.980   1.333  1.00 38.15           O  
ANISOU 4960  O   LEU B 254     4998   4385   5111    -66    -38   -116       O  
ATOM   4961  CB  LEU B 254     -73.650  10.783   0.427  1.00 41.37           C  
ANISOU 4961  CB  LEU B 254     5455   4701   5561   -202     74   -187       C  
ATOM   4962  CG  LEU B 254     -75.002  11.163  -0.183  1.00 46.87           C  
ANISOU 4962  CG  LEU B 254     6102   5507   6199   -240     47   -219       C  
ATOM   4963  CD1 LEU B 254     -74.821  11.612  -1.626  1.00 41.85           C  
ANISOU 4963  CD1 LEU B 254     5452   4922   5529   -247     30   -240       C  
ATOM   4964  CD2 LEU B 254     -76.015  10.020  -0.080  1.00 41.40           C  
ANISOU 4964  CD2 LEU B 254     5400   4836   5492   -327     93   -267       C  
ATOM   4965  N   GLU B 255     -73.672  12.534   3.001  1.00 36.54           N  
ANISOU 4965  N   GLU B 255     4812   4113   4959    -80      4   -101       N  
ATOM   4966  CA  GLU B 255     -74.448  13.373   3.909  1.00 40.18           C  
ANISOU 4966  CA  GLU B 255     5246   4620   5402    -49    -28    -84       C  
ATOM   4967  C   GLU B 255     -73.788  14.734   4.168  1.00 38.06           C  
ANISOU 4967  C   GLU B 255     4982   4349   5131      1    -53    -66       C  
ATOM   4968  O   GLU B 255     -74.479  15.747   4.323  1.00 42.38           O  
ANISOU 4968  O   GLU B 255     5517   4932   5654     28    -72    -59       O  
ATOM   4969  CB  GLU B 255     -74.777  12.649   5.205  1.00 38.91           C  
ANISOU 4969  CB  GLU B 255     5077   4449   5258    -50    -10    -68       C  
ATOM   4970  CG  GLU B 255     -75.597  13.503   6.149  1.00 52.34           C  
ANISOU 4970  CG  GLU B 255     6747   6199   6938    -20    -43    -52       C  
ATOM   4971  CD  GLU B 255     -76.038  12.749   7.383  1.00 59.60           C  
ANISOU 4971  CD  GLU B 255     7655   7120   7872    -23    -26    -36       C  
ATOM   4972  OE1 GLU B 255     -76.871  13.300   8.140  1.00 64.44           O  
ANISOU 4972  OE1 GLU B 255     8240   7778   8465     -6    -51    -27       O  
ATOM   4973  OE2 GLU B 255     -75.552  11.612   7.598  1.00 57.64           O  
ANISOU 4973  OE2 GLU B 255     7426   6822   7651    -37     19    -27       O  
ATOM   4974  N   SER B 256     -72.456  14.757   4.183  1.00 38.34           N  
ANISOU 4974  N   SER B 256     5036   4343   5187     11    -43    -61       N  
ATOM   4975  CA  SER B 256     -71.692  16.005   4.347  1.00 38.37           C  
ANISOU 4975  CA  SER B 256     5049   4343   5185     36    -52    -59       C  
ATOM   4976  C   SER B 256     -71.874  16.986   3.189  1.00 36.10           C  
ANISOU 4976  C   SER B 256     4780   4056   4881     45    -57    -66       C  
ATOM   4977  O   SER B 256     -71.982  18.192   3.393  1.00 38.94           O  
ANISOU 4977  O   SER B 256     5152   4414   5229     70    -53    -63       O  
ATOM   4978  CB  SER B 256     -70.204  15.701   4.519  1.00 41.32           C  
ANISOU 4978  CB  SER B 256     5428   4697   5572     36    -38    -55       C  
ATOM   4979  OG  SER B 256     -70.009  14.815   5.598  1.00 45.26           O  
ANISOU 4979  OG  SER B 256     5907   5210   6081     46    -24    -33       O  
ATOM   4980  N   TRP B 257     -71.887  16.477   1.965  1.00 44.17           N  
ANISOU 4980  N   TRP B 257     5806   5079   5899     28    -56    -75       N  
ATOM   4981  CA  TRP B 257     -72.180  17.343   0.834  1.00 43.15           C  
ANISOU 4981  CA  TRP B 257     5683   4969   5743     48    -58    -72       C  
ATOM   4982  C   TRP B 257     -73.590  17.941   0.939  1.00 39.55           C  
ANISOU 4982  C   TRP B 257     5204   4573   5250     80    -64    -54       C  
ATOM   4983  O   TRP B 257     -73.774  19.133   0.669  1.00 37.44           O  
ANISOU 4983  O   TRP B 257     4953   4309   4964    129    -51    -32       O  
ATOM   4984  CB  TRP B 257     -71.942  16.611  -0.489  1.00 36.82           C  
ANISOU 4984  CB  TRP B 257     4880   4175   4936     19    -55    -89       C  
ATOM   4985  CG  TRP B 257     -70.484  16.606  -0.874  1.00 29.41           C  
ANISOU 4985  CG  TRP B 257     3970   3183   4023     13    -45    -94       C  
ATOM   4986  CD1 TRP B 257     -69.632  15.540  -0.874  1.00 24.97           C  
ANISOU 4986  CD1 TRP B 257     3417   2587   3485    -13    -33   -105       C  
ATOM   4987  CD2 TRP B 257     -69.714  17.736  -1.284  1.00 34.31           C  
ANISOU 4987  CD2 TRP B 257     4615   3779   4641     37    -39    -87       C  
ATOM   4988  NE1 TRP B 257     -68.385  15.931  -1.275  1.00 29.90           N  
ANISOU 4988  NE1 TRP B 257     4061   3184   4118     -5    -28   -103       N  
ATOM   4989  CE2 TRP B 257     -68.403  17.277  -1.533  1.00 33.19           C  
ANISOU 4989  CE2 TRP B 257     4488   3604   4520     17    -32    -97       C  
ATOM   4990  CE3 TRP B 257     -70.005  19.092  -1.476  1.00 39.15           C  
ANISOU 4990  CE3 TRP B 257     5246   4393   5237     75    -26    -70       C  
ATOM   4991  CZ2 TRP B 257     -67.383  18.125  -1.976  1.00 29.09           C  
ANISOU 4991  CZ2 TRP B 257     3991   3060   4000     22    -22    -99       C  
ATOM   4992  CZ3 TRP B 257     -68.992  19.935  -1.899  1.00 48.33           C  
ANISOU 4992  CZ3 TRP B 257     6443   5513   6407     80     -4    -71       C  
ATOM   4993  CH2 TRP B 257     -67.694  19.448  -2.147  1.00 39.78           C  
ANISOU 4993  CH2 TRP B 257     5367   4406   5342     47     -6    -90       C  
ATOM   4994  N   LYS B 258     -74.564  17.124   1.358  1.00 36.47           N  
ANISOU 4994  N   LYS B 258     4780   4229   4848     57    -75    -61       N  
ATOM   4995  CA  LYS B 258     -75.913  17.609   1.695  1.00 36.55           C  
ANISOU 4995  CA  LYS B 258     4759   4312   4817     89    -83    -42       C  
ATOM   4996  C   LYS B 258     -75.912  18.703   2.751  1.00 36.89           C  
ANISOU 4996  C   LYS B 258     4824   4323   4869    139    -75    -18       C  
ATOM   4997  O   LYS B 258     -76.632  19.682   2.618  1.00 41.21           O  
ANISOU 4997  O   LYS B 258     5371   4904   5382    196    -63     12       O  
ATOM   4998  CB  LYS B 258     -76.814  16.467   2.163  1.00 36.93           C  
ANISOU 4998  CB  LYS B 258     4770   4407   4855     40    -91    -61       C  
ATOM   4999  CG  LYS B 258     -77.472  15.725   1.022  1.00 43.96           C  
ANISOU 4999  CG  LYS B 258     5623   5378   5703    -10    -90    -90       C  
ATOM   5000  CD  LYS B 258     -78.052  14.392   1.458  1.00 42.60           C  
ANISOU 5000  CD  LYS B 258     5432   5219   5534    -87    -76   -127       C  
ATOM   5001  CE  LYS B 258     -78.427  13.561   0.237  1.00 49.20           C  
ANISOU 5001  CE  LYS B 258     6240   6121   6331   -163    -59   -177       C  
ATOM   5002  NZ  LYS B 258     -78.829  12.175   0.599  1.00 59.99           N  
ANISOU 5002  NZ  LYS B 258     7610   7473   7711   -256    -22   -225       N  
ATOM   5003  N   ILE B 259     -75.121  18.534   3.810  1.00 36.82           N  
ANISOU 5003  N   ILE B 259     4833   4258   4901    119    -73    -30       N  
ATOM   5004  CA  ILE B 259     -74.979  19.593   4.808  1.00 35.62           C  
ANISOU 5004  CA  ILE B 259     4703   4077   4754    149    -57    -24       C  
ATOM   5005  C   ILE B 259     -74.436  20.855   4.156  1.00 38.00           C  
ANISOU 5005  C   ILE B 259     5051   4335   5053    179    -22    -19       C  
ATOM   5006  O   ILE B 259     -74.880  21.954   4.456  1.00 37.70           O  
ANISOU 5006  O   ILE B 259     5039   4284   5001    223     10     -3       O  
ATOM   5007  CB  ILE B 259     -74.039  19.183   5.974  1.00 40.53           C  
ANISOU 5007  CB  ILE B 259     5322   4671   5406    117    -59    -43       C  
ATOM   5008  CG1 ILE B 259     -74.739  18.221   6.927  1.00 37.07           C  
ANISOU 5008  CG1 ILE B 259     4846   4270   4971    106    -78    -35       C  
ATOM   5009  CG2 ILE B 259     -73.606  20.390   6.751  1.00 39.64           C  
ANISOU 5009  CG2 ILE B 259     5234   4533   5294    126    -32    -55       C  
ATOM   5010  CD1 ILE B 259     -73.792  17.284   7.588  1.00 35.45           C  
ANISOU 5010  CD1 ILE B 259     4628   4053   4788     82    -76    -38       C  
ATOM   5011  N   LEU B 260     -73.459  20.698   3.267  1.00 38.49           N  
ANISOU 5011  N   LEU B 260     5130   4367   5128    157    -18    -31       N  
ATOM   5012  CA  LEU B 260     -72.936  21.845   2.524  1.00 47.54           C  
ANISOU 5012  CA  LEU B 260     6324   5468   6270    183     23    -25       C  
ATOM   5013  C   LEU B 260     -73.978  22.395   1.552  1.00 50.31           C  
ANISOU 5013  C   LEU B 260     6673   5859   6582    250     39     19       C  
ATOM   5014  O   LEU B 260     -74.196  23.604   1.483  1.00 46.63           O  
ANISOU 5014  O   LEU B 260     6250   5361   6105    305     92     46       O  
ATOM   5015  CB  LEU B 260     -71.666  21.481   1.755  1.00 44.89           C  
ANISOU 5015  CB  LEU B 260     6000   5102   5953    144     20    -45       C  
ATOM   5016  CG  LEU B 260     -70.381  21.187   2.519  1.00 43.96           C  
ANISOU 5016  CG  LEU B 260     5883   4960   5860     92     18    -80       C  
ATOM   5017  CD1 LEU B 260     -69.197  21.337   1.548  1.00 51.01           C  
ANISOU 5017  CD1 LEU B 260     6799   5823   6759     72     31    -93       C  
ATOM   5018  CD2 LEU B 260     -70.232  22.135   3.691  1.00 36.65           C  
ANISOU 5018  CD2 LEU B 260     4976   4016   4934     83     50   -101       C  
ATOM   5019  N   GLU B 261     -74.620  21.507   0.803  1.00 50.00           N  
ANISOU 5019  N   GLU B 261     6584   5897   6516    245      3     27       N  
ATOM   5020  CA  GLU B 261     -75.607  21.930  -0.185  1.00 60.56           C  
ANISOU 5020  CA  GLU B 261     7898   7315   7798    310     14     71       C  
ATOM   5021  C   GLU B 261     -76.748  22.703   0.469  1.00 60.65           C  
ANISOU 5021  C   GLU B 261     7904   7363   7775    381     37    113       C  
ATOM   5022  O   GLU B 261     -77.271  23.670  -0.092  1.00 57.81           O  
ANISOU 5022  O   GLU B 261     7557   7031   7375    469     80    167       O  
ATOM   5023  CB  GLU B 261     -76.150  20.723  -0.943  1.00 59.99           C  
ANISOU 5023  CB  GLU B 261     7760   7343   7693    268    -28     54       C  
ATOM   5024  CG  GLU B 261     -77.108  21.081  -2.051  1.00 71.21           C  
ANISOU 5024  CG  GLU B 261     9134   8887   9037    327    -20     94       C  
ATOM   5025  CD  GLU B 261     -78.537  20.821  -1.665  1.00 82.49           C  
ANISOU 5025  CD  GLU B 261    10497  10438  10407    342    -37    108       C  
ATOM   5026  OE1 GLU B 261     -78.849  19.650  -1.355  1.00 88.69           O  
ANISOU 5026  OE1 GLU B 261    11243  11260  11194    260    -70     60       O  
ATOM   5027  OE2 GLU B 261     -79.341  21.783  -1.670  1.00 84.36           O  
ANISOU 5027  OE2 GLU B 261    10724  10734  10594    439    -10    169       O  
ATOM   5028  N   SER B 262     -77.109  22.269   1.669  1.00 55.09           N  
ANISOU 5028  N   SER B 262     7185   6661   7087    350     14     93       N  
ATOM   5029  CA  SER B 262     -78.210  22.844   2.424  1.00 50.73           C  
ANISOU 5029  CA  SER B 262     6623   6148   6504    409     29    126       C  
ATOM   5030  C   SER B 262     -77.852  24.209   2.986  1.00 51.93           C  
ANISOU 5030  C   SER B 262     6851   6201   6678    459     97    142       C  
ATOM   5031  O   SER B 262     -78.649  24.839   3.669  1.00 63.22           O  
ANISOU 5031  O   SER B 262     8290   7642   8089    515    125    170       O  
ATOM   5032  CB  SER B 262     -78.567  21.902   3.564  1.00 55.45           C  
ANISOU 5032  CB  SER B 262     7183   6767   7118    352    -15     95       C  
ATOM   5033  OG  SER B 262     -79.057  22.617   4.675  1.00 75.72           O  
ANISOU 5033  OG  SER B 262     9768   9317   9685    392      7    110       O  
ATOM   5034  N   MET B 263     -76.656  24.673   2.660  1.00 61.68           N  
ANISOU 5034  N   MET B 263     8144   7342   7950    435    131    120       N  
ATOM   5035  CA  MET B 263     -76.056  25.818   3.320  1.00 66.43           C  
ANISOU 5035  CA  MET B 263     8825   7835   8581    439    204    105       C  
ATOM   5036  C   MET B 263     -75.891  27.024   2.395  1.00 74.63           C  
ANISOU 5036  C   MET B 263     9933   8814   9609    509    293    147       C  
ATOM   5037  O   MET B 263     -75.851  28.160   2.855  1.00 81.83           O  
ANISOU 5037  O   MET B 263    10919   9641  10531    540    382    151       O  
ATOM   5038  CB  MET B 263     -74.694  25.386   3.859  1.00 71.71           C  
ANISOU 5038  CB  MET B 263     9502   8448   9295    336    184     35       C  
ATOM   5039  CG  MET B 263     -74.068  26.308   4.863  1.00 73.99           C  
ANISOU 5039  CG  MET B 263     9848   8658   9607    301    246     -9       C  
ATOM   5040  SD  MET B 263     -72.746  25.447   5.717  1.00 74.35           S  
ANISOU 5040  SD  MET B 263     9855   8717   9679    187    196    -82       S  
ATOM   5041  CE  MET B 263     -73.610  24.021   6.363  1.00100.06           C  
ANISOU 5041  CE  MET B 263    13026  12066  12928    191    108    -63       C  
ATOM   5042  N   LYS B 264     -75.791  26.775   1.094  1.00 80.34           N  
ANISOU 5042  N   LYS B 264    10635   9578  10311    534    278    176       N  
ATOM   5043  CA  LYS B 264     -75.565  27.847   0.124  1.00 92.72           C  
ANISOU 5043  CA  LYS B 264    12267  11094  11869    607    365    224       C  
ATOM   5044  C   LYS B 264     -76.612  28.971   0.168  1.00104.08           C  
ANISOU 5044  C   LYS B 264    13745  12531  13268    737    456    304       C  
ATOM   5045  O   LYS B 264     -77.782  28.744   0.498  1.00104.55           O  
ANISOU 5045  O   LYS B 264    13751  12690  13285    792    428    342       O  
ATOM   5046  CB  LYS B 264     -75.466  27.275  -1.298  1.00 90.38           C  
ANISOU 5046  CB  LYS B 264    11920  10876  11543    620    324    249       C  
ATOM   5047  N   SER B 265     -76.179  30.185  -0.119  1.00111.20           N  
ANISOU 5047  N   SER B 265    14747  13318  14186    785    574    330       N  
ATOM   5048  CA  SER B 265     -77.028  31.345  -0.366  1.00118.12           C  
ANISOU 5048  CA  SER B 265    15681  14176  15025    933    690    425       C  
ATOM   5049  C   SER B 265     -77.768  31.766   0.900  1.00118.49           C  
ANISOU 5049  C   SER B 265    15753  14196  15071    958    728    424       C  
ATOM   5050  O   SER B 265     -78.772  32.536   0.770  1.00120.12           O  
ANISOU 5050  O   SER B 265    15983  14425  15230   1103    811    519       O  
ATOM   5051  CB  SER B 265     -78.028  31.050  -1.486  1.00119.50           C  
ANISOU 5051  CB  SER B 265    15769  14520  15118   1051    658    522       C  
ATOM   5052  OG  SER B 265     -78.874  32.163  -1.719  1.00118.12           O  
ANISOU 5052  OG  SER B 265    15640  14344  14894   1217    778    632       O  
ATOM   5053  N   LYS B 266     -77.334  31.383   2.050  1.00115.36           N  
ANISOU 5053  N   LYS B 266    15356  13759  14719    842    684    334       N  
ATOM   5054  CA  LYS B 266     -78.027  31.725   3.286  1.00115.49           C  
ANISOU 5054  CA  LYS B 266    15389  13758  14734    859    713    326       C  
ATOM   5055  C   LYS B 266     -77.324  32.840   4.053  1.00118.38           C  
ANISOU 5055  C   LYS B 266    15879  13953  15147    811    841    269       C  
ATOM   5056  O   LYS B 266     -76.286  33.351   3.625  1.00119.40           O  
ANISOU 5056  O   LYS B 266    16080  13977  15308    760    910    233       O  
ATOM   5057  CB  LYS B 266     -78.161  30.493   4.185  1.00112.93           C  
ANISOU 5057  CB  LYS B 266    14968  13524  14416    764    579    266       C  
ATOM   5058  CG  LYS B 266     -79.223  29.501   3.752  1.00109.00           C  
ANISOU 5058  CG  LYS B 266    14355  13196  13863    811    477    316       C  
ATOM   5059  CD  LYS B 266     -79.423  28.413   4.797  1.00105.65           C  
ANISOU 5059  CD  LYS B 266    13858  12835  13452    723    375    260       C  
ATOM   5060  CE  LYS B 266     -80.577  27.498   4.407  1.00108.87           C  
ANISOU 5060  CE  LYS B 266    14158  13408  13798    758    294    302       C  
ATOM   5061  NZ  LYS B 266     -80.981  26.567   5.499  1.00108.18           N  
ANISOU 5061  NZ  LYS B 266    14010  13375  13719    691    217    261       N  
ATOM   5062  N   ASP B 267     -77.914  33.219   5.182  1.00117.92           N  
ANISOU 5062  N   ASP B 267    15844  13872  15087    823    879    257       N  
ATOM   5063  CA  ASP B 267     -77.260  34.098   6.137  1.00113.02           C  
ANISOU 5063  CA  ASP B 267    15324  13110  14508    742    988    174       C  
ATOM   5064  C   ASP B 267     -76.252  33.250   6.894  1.00104.30           C  
ANISOU 5064  C   ASP B 267    14158  12037  13432    572    886     57       C  
ATOM   5065  O   ASP B 267     -76.628  32.277   7.548  1.00109.66           O  
ANISOU 5065  O   ASP B 267    14740  12824  14102    544    767     44       O  
ATOM   5066  CB  ASP B 267     -78.282  34.686   7.112  1.00114.83           C  
ANISOU 5066  CB  ASP B 267    15587  13322  14720    812   1054    198       C  
ATOM   5067  N   ILE B 268     -74.975  33.613   6.795  1.00 92.61           N  
ANISOU 5067  N   ILE B 268    12732  10473  11983    464    938    -22       N  
ATOM   5068  CA  ILE B 268     -73.901  32.829   7.401  1.00 82.70           C  
ANISOU 5068  CA  ILE B 268    11409   9270  10742    314    848   -122       C  
ATOM   5069  C   ILE B 268     -74.029  32.769   8.913  1.00 75.96           C  
ANISOU 5069  C   ILE B 268    10530   8448   9886    245    836   -191       C  
ATOM   5070  O   ILE B 268     -73.394  33.536   9.630  1.00 77.28           O  
ANISOU 5070  O   ILE B 268    10755   8547  10060    151    929   -280       O  
ATOM   5071  CB  ILE B 268     -72.516  33.382   7.022  1.00 87.98           C  
ANISOU 5071  CB  ILE B 268    12142   9855  11432    210    924   -197       C  
ATOM   5072  CG1 ILE B 268     -72.434  34.884   7.335  1.00 88.76           C  
ANISOU 5072  CG1 ILE B 268    12381   9801  11543    195   1114   -235       C  
ATOM   5073  CG2 ILE B 268     -72.228  33.109   5.545  1.00 83.49           C  
ANISOU 5073  CG2 ILE B 268    11569   9289  10866    261    897   -135       C  
ATOM   5074  CD1 ILE B 268     -71.117  35.549   6.931  1.00 80.24           C  
ANISOU 5074  CD1 ILE B 268    11377   8630  10480     83   1213   -314       C  
ATOM   5075  N   ASN B 269     -74.862  31.850   9.389  1.00 70.77           N  
ANISOU 5075  N   ASN B 269     9780   7899   9213    286    724   -154       N  
ATOM   5076  CA  ASN B 269     -75.080  31.670  10.813  1.00 67.07           C  
ANISOU 5076  CA  ASN B 269     9271   7477   8736    234    699   -206       C  
ATOM   5077  C   ASN B 269     -74.965  30.201  11.196  1.00 64.40           C  
ANISOU 5077  C   ASN B 269     8806   7271   8391    196    547   -209       C  
ATOM   5078  O   ASN B 269     -75.954  29.465  11.187  1.00 70.14           O  
ANISOU 5078  O   ASN B 269     9473   8070   9106    266    470   -146       O  
ATOM   5079  CB  ASN B 269     -76.442  32.222  11.224  1.00 70.23           C  
ANISOU 5079  CB  ASN B 269     9704   7860   9121    342    748   -148       C  
ATOM   5080  CG  ASN B 269     -76.591  32.326  12.725  1.00 69.89           C  
ANISOU 5080  CG  ASN B 269     9642   7840   9071    282    754   -213       C  
ATOM   5081  OD1 ASN B 269     -75.925  31.612  13.477  1.00 78.02           O  
ANISOU 5081  OD1 ASN B 269    10596   8949  10100    182    677   -279       O  
ATOM   5082  ND2 ASN B 269     -77.466  33.214  13.171  1.00 69.58           N  
ANISOU 5082  ND2 ASN B 269     9671   7742   9024    351    849   -191       N  
ATOM   5083  N   ILE B 270     -73.745  29.792  11.532  1.00 57.90           N  
ANISOU 5083  N   ILE B 270     7943   6483   7571     86    516   -282       N  
ATOM   5084  CA  ILE B 270     -73.431  28.401  11.828  1.00 52.41           C  
ANISOU 5084  CA  ILE B 270     7140   5903   6872     55    394   -279       C  
ATOM   5085  C   ILE B 270     -74.523  27.714  12.659  1.00 52.22           C  
ANISOU 5085  C   ILE B 270     7052   5952   6836    103    327   -241       C  
ATOM   5086  O   ILE B 270     -75.016  26.644  12.308  1.00 59.26           O  
ANISOU 5086  O   ILE B 270     7886   6901   7730    143    244   -186       O  
ATOM   5087  CB  ILE B 270     -72.052  28.290  12.524  1.00 43.64           C  
ANISOU 5087  CB  ILE B 270     5991   4842   5747    -63    394   -367       C  
ATOM   5088  CG1 ILE B 270     -70.969  28.857  11.607  1.00 47.06           C  
ANISOU 5088  CG1 ILE B 270     6479   5214   6187   -115    452   -403       C  
ATOM   5089  CG2 ILE B 270     -71.738  26.841  12.898  1.00 36.42           C  
ANISOU 5089  CG2 ILE B 270     4968   4047   4823    -73    284   -347       C  
ATOM   5090  CD1 ILE B 270     -69.551  28.753  12.143  1.00 48.32           C  
ANISOU 5090  CD1 ILE B 270     6591   5448   6319   -234    454   -489       C  
ATOM   5091  N   VAL B 271     -74.924  28.345  13.748  1.00 50.91           N  
ANISOU 5091  N   VAL B 271     6901   5782   6659     92    372   -273       N  
ATOM   5092  CA  VAL B 271     -75.890  27.730  14.636  1.00 52.66           C  
ANISOU 5092  CA  VAL B 271     7061   6078   6870    129    312   -243       C  
ATOM   5093  C   VAL B 271     -77.280  27.534  14.012  1.00 47.50           C  
ANISOU 5093  C   VAL B 271     6410   5428   6212    238    287   -154       C  
ATOM   5094  O   VAL B 271     -77.917  26.507  14.234  1.00 39.67           O  
ANISOU 5094  O   VAL B 271     5346   4515   5213    261    205   -117       O  
ATOM   5095  CB  VAL B 271     -75.982  28.519  15.938  1.00 54.73           C  
ANISOU 5095  CB  VAL B 271     7339   6339   7117     89    371   -304       C  
ATOM   5096  CG1 VAL B 271     -76.977  27.862  16.894  1.00 49.04           C  
ANISOU 5096  CG1 VAL B 271     6549   5700   6382    129    306   -270       C  
ATOM   5097  CG2 VAL B 271     -74.595  28.623  16.557  1.00 53.65           C  
ANISOU 5097  CG2 VAL B 271     7178   6241   6966    -32    391   -398       C  
ATOM   5098  N   GLU B 272     -77.747  28.508  13.237  1.00 48.90           N  
ANISOU 5098  N   GLU B 272     6665   5528   6386    307    364   -119       N  
ATOM   5099  CA  GLU B 272     -79.089  28.427  12.652  1.00 55.89           C  
ANISOU 5099  CA  GLU B 272     7541   6448   7249    420    349    -31       C  
ATOM   5100  C   GLU B 272     -79.129  27.411  11.515  1.00 54.00           C  
ANISOU 5100  C   GLU B 272     7247   6267   7005    433    271     11       C  
ATOM   5101  O   GLU B 272     -80.104  26.674  11.338  1.00 54.45           O  
ANISOU 5101  O   GLU B 272     7241   6411   7035    475    209     59       O  
ATOM   5102  CB  GLU B 272     -79.541  29.793  12.149  1.00 48.95           C  
ANISOU 5102  CB  GLU B 272     6761   5480   6359    507    470      7       C  
ATOM   5103  CG  GLU B 272     -79.535  30.848  13.225  1.00 58.09           C  
ANISOU 5103  CG  GLU B 272     7988   6562   7522    490    570    -41       C  
ATOM   5104  N   VAL B 273     -78.049  27.382  10.754  1.00 40.85           N  
ANISOU 5104  N   VAL B 273     5604   4556   5359    387    279    -14       N  
ATOM   5105  CA  VAL B 273     -77.893  26.454   9.651  1.00 42.23           C  
ANISOU 5105  CA  VAL B 273     5737   4776   5533    386    216     12       C  
ATOM   5106  C   VAL B 273     -77.853  25.005  10.130  1.00 46.23           C  
ANISOU 5106  C   VAL B 273     6159   5361   6047    332    121     -2       C  
ATOM   5107  O   VAL B 273     -78.368  24.101   9.467  1.00 51.38           O  
ANISOU 5107  O   VAL B 273     6763   6073   6685    344     68     28       O  
ATOM   5108  CB  VAL B 273     -76.592  26.779   8.895  1.00 45.08           C  
ANISOU 5108  CB  VAL B 273     6145   5066   5918    340    251    -21       C  
ATOM   5109  CG1 VAL B 273     -76.064  25.555   8.179  1.00 49.60           C  
ANISOU 5109  CG1 VAL B 273     6661   5684   6499    300    174    -22       C  
ATOM   5110  CG2 VAL B 273     -76.830  27.940   7.943  1.00 46.50           C  
ANISOU 5110  CG2 VAL B 273     6402   5179   6087    416    342     22       C  
ATOM   5111  N   GLY B 274     -77.232  24.785  11.284  1.00 44.29           N  
ANISOU 5111  N   GLY B 274     5894   5116   5816    270    110    -50       N  
ATOM   5112  CA  GLY B 274     -77.098  23.447  11.816  1.00 36.11           C  
ANISOU 5112  CA  GLY B 274     4788   4144   4787    230     40    -54       C  
ATOM   5113  C   GLY B 274     -78.443  22.955  12.324  1.00 38.80           C  
ANISOU 5113  C   GLY B 274     5084   4548   5109    268      4    -19       C  
ATOM   5114  O   GLY B 274     -78.836  21.826  12.052  1.00 33.42           O  
ANISOU 5114  O   GLY B 274     4357   3913   4426    259    -43      1       O  
ATOM   5115  N   LYS B 275     -79.129  23.806  13.086  1.00 39.57           N  
ANISOU 5115  N   LYS B 275     5199   4645   5192    303     36    -16       N  
ATOM   5116  CA  LYS B 275     -80.493  23.550  13.509  1.00 39.39           C  
ANISOU 5116  CA  LYS B 275     5137   4686   5141    348     10     22       C  
ATOM   5117  C   LYS B 275     -81.409  23.296  12.313  1.00 48.10           C  
ANISOU 5117  C   LYS B 275     6224   5837   6213    397     -6     71       C  
ATOM   5118  O   LYS B 275     -82.097  22.276  12.256  1.00 39.96           O  
ANISOU 5118  O   LYS B 275     5135   4881   5167    384    -55     86       O  
ATOM   5119  CB  LYS B 275     -81.026  24.723  14.329  1.00 46.23           C  
ANISOU 5119  CB  LYS B 275     6040   5531   5992    392     64     21       C  
ATOM   5120  CG  LYS B 275     -80.516  24.738  15.762  1.00 57.86           C  
ANISOU 5120  CG  LYS B 275     7497   7008   7478    338     65    -29       C  
ATOM   5121  CD  LYS B 275     -81.267  25.753  16.607  1.00 51.92           C  
ANISOU 5121  CD  LYS B 275     6776   6245   6708    380    116    -30       C  
ATOM   5122  CE  LYS B 275     -80.808  27.177  16.357  1.00 47.20           C  
ANISOU 5122  CE  LYS B 275     6274   5545   6115    389    220    -59       C  
ATOM   5123  NZ  LYS B 275     -81.795  28.128  16.925  1.00 47.77           N  
ANISOU 5123  NZ  LYS B 275     6387   5598   6166    456    284    -40       N  
ATOM   5124  N   GLN B 276     -81.425  24.223  11.358  1.00 55.50           N  
ANISOU 5124  N   GLN B 276     7211   6741   7137    451     44     95       N  
ATOM   5125  CA  GLN B 276     -82.272  24.057  10.179  1.00 49.55           C  
ANISOU 5125  CA  GLN B 276     6428   6061   6337    505     33    145       C  
ATOM   5126  C   GLN B 276     -81.990  22.716   9.506  1.00 43.84           C  
ANISOU 5126  C   GLN B 276     5654   5381   5621    435    -27    125       C  
ATOM   5127  O   GLN B 276     -82.910  22.012   9.118  1.00 47.95           O  
ANISOU 5127  O   GLN B 276     6115   6002   6101    434    -61    142       O  
ATOM   5128  CB  GLN B 276     -82.122  25.232   9.200  1.00 41.55           C  
ANISOU 5128  CB  GLN B 276     5478   5001   5309    579    105    181       C  
ATOM   5129  CG  GLN B 276     -82.940  26.469   9.585  1.00 43.35           C  
ANISOU 5129  CG  GLN B 276     5749   5216   5506    683    179    228       C  
ATOM   5130  CD  GLN B 276     -82.508  27.728   8.840  1.00 64.73           C  
ANISOU 5130  CD  GLN B 276     8547   7830   8216    750    281    257       C  
ATOM   5131  OE1 GLN B 276     -81.506  27.729   8.118  1.00 74.95           O  
ANISOU 5131  OE1 GLN B 276     9873   9064   9540    709    291    233       O  
ATOM   5132  NE2 GLN B 276     -83.262  28.811   9.018  1.00 69.94           N  
ANISOU 5132  NE2 GLN B 276     9254   8473   8845    859    366    313       N  
ATOM   5133  N   TYR B 277     -80.725  22.332   9.414  1.00 41.39           N  
ANISOU 5133  N   TYR B 277     5367   5000   5358    372    -32     85       N  
ATOM   5134  CA  TYR B 277     -80.400  21.072   8.766  1.00 36.95           C  
ANISOU 5134  CA  TYR B 277     4771   4462   4806    311    -72     68       C  
ATOM   5135  C   TYR B 277     -80.931  19.866   9.533  1.00 40.05           C  
ANISOU 5135  C   TYR B 277     5112   4904   5202    265   -110     57       C  
ATOM   5136  O   TYR B 277     -81.530  18.969   8.950  1.00 47.04           O  
ANISOU 5136  O   TYR B 277     5958   5851   6065    234   -129     55       O  
ATOM   5137  CB  TYR B 277     -78.883  20.922   8.521  1.00 34.57           C  
ANISOU 5137  CB  TYR B 277     4505   4079   4551    264    -63     35       C  
ATOM   5138  CG  TYR B 277     -78.566  19.559   7.950  1.00 29.19           C  
ANISOU 5138  CG  TYR B 277     3796   3412   3883    207    -92     19       C  
ATOM   5139  CD1 TYR B 277     -78.706  19.301   6.591  1.00 31.21           C  
ANISOU 5139  CD1 TYR B 277     4044   3695   4118    203    -95     22       C  
ATOM   5140  CD2 TYR B 277     -78.186  18.522   8.772  1.00 30.77           C  
ANISOU 5140  CD2 TYR B 277     3977   3602   4111    163   -106      4       C  
ATOM   5141  CE1 TYR B 277     -78.457  18.047   6.075  1.00 29.25           C  
ANISOU 5141  CE1 TYR B 277     3779   3453   3882    143   -107      0       C  
ATOM   5142  CE2 TYR B 277     -77.942  17.277   8.274  1.00 34.54           C  
ANISOU 5142  CE2 TYR B 277     4443   4077   4603    116   -112     -7       C  
ATOM   5143  CZ  TYR B 277     -78.078  17.037   6.927  1.00 36.78           C  
ANISOU 5143  CZ  TYR B 277     4727   4377   4870    101   -110    -15       C  
ATOM   5144  OH  TYR B 277     -77.809  15.774   6.451  1.00 44.70           O  
ANISOU 5144  OH  TYR B 277     5728   5365   5889     46   -102    -35       O  
ATOM   5145  N   LEU B 278     -80.691  19.835  10.839  1.00 43.96           N  
ANISOU 5145  N   LEU B 278     5606   5375   5722    254   -112     47       N  
ATOM   5146  CA  LEU B 278     -81.049  18.675  11.662  1.00 43.94           C  
ANISOU 5146  CA  LEU B 278     5562   5406   5728    215   -137     43       C  
ATOM   5147  C   LEU B 278     -82.564  18.528  11.794  1.00 40.82           C  
ANISOU 5147  C   LEU B 278     5122   5099   5287    232   -153     63       C  
ATOM   5148  O   LEU B 278     -83.089  17.412  11.839  1.00 32.94           O  
ANISOU 5148  O   LEU B 278     4090   4143   4284    185   -166     55       O  
ATOM   5149  CB  LEU B 278     -80.399  18.776  13.052  1.00 36.57           C  
ANISOU 5149  CB  LEU B 278     4629   4444   4822    210   -133     34       C  
ATOM   5150  CG  LEU B 278     -78.869  18.657  13.134  1.00 35.02           C  
ANISOU 5150  CG  LEU B 278     4453   4196   4658    183   -121     13       C  
ATOM   5151  CD1 LEU B 278     -78.351  19.102  14.503  1.00 37.44           C  
ANISOU 5151  CD1 LEU B 278     4746   4512   4965    183   -113     -1       C  
ATOM   5152  CD2 LEU B 278     -78.400  17.238  12.827  1.00 30.96           C  
ANISOU 5152  CD2 LEU B 278     3925   3673   4166    147   -125     18       C  
ATOM   5153  N   GLU B 279     -83.249  19.666  11.866  1.00 33.23           N  
ANISOU 5153  N   GLU B 279     4167   4169   4291    299   -141     87       N  
ATOM   5154  CA  GLU B 279     -84.699  19.709  11.900  1.00 35.41           C  
ANISOU 5154  CA  GLU B 279     4396   4551   4508    332   -154    115       C  
ATOM   5155  C   GLU B 279     -85.260  19.163  10.590  1.00 46.12           C  
ANISOU 5155  C   GLU B 279     5713   5993   5816    310   -164    115       C  
ATOM   5156  O   GLU B 279     -86.050  18.212  10.579  1.00 43.41           O  
ANISOU 5156  O   GLU B 279     5316   5734   5444    258   -183    102       O  
ATOM   5157  CB  GLU B 279     -85.164  21.150  12.123  1.00 37.92           C  
ANISOU 5157  CB  GLU B 279     4740   4872   4796    427   -121    151       C  
ATOM   5158  CG  GLU B 279     -84.907  21.642  13.551  1.00 38.47           C  
ANISOU 5158  CG  GLU B 279     4835   4886   4897    436   -109    140       C  
ATOM   5159  CD  GLU B 279     -85.047  23.148  13.714  1.00 44.28           C  
ANISOU 5159  CD  GLU B 279     5626   5580   5618    519    -50    162       C  
ATOM   5160  OE1 GLU B 279     -85.537  23.834  12.791  1.00 42.52           O  
ANISOU 5160  OE1 GLU B 279     5417   5382   5354    592    -17    205       O  
ATOM   5161  OE2 GLU B 279     -84.662  23.650  14.788  1.00 49.31           O  
ANISOU 5161  OE2 GLU B 279     6292   6162   6282    512    -27    138       O  
ATOM   5162  N   GLN B 280     -84.817  19.758   9.486  1.00 48.61           N  
ANISOU 5162  N   GLN B 280     6055   6293   6123    343   -144    126       N  
ATOM   5163  CA  GLN B 280     -85.172  19.299   8.145  1.00 49.78           C  
ANISOU 5163  CA  GLN B 280     6163   6530   6221    320   -151    122       C  
ATOM   5164  C   GLN B 280     -84.967  17.793   8.027  1.00 50.12           C  
ANISOU 5164  C   GLN B 280     6184   6570   6288    205   -168     68       C  
ATOM   5165  O   GLN B 280     -85.829  17.077   7.516  1.00 49.89           O  
ANISOU 5165  O   GLN B 280     6096   6655   6204    154   -176     48       O  
ATOM   5166  CB  GLN B 280     -84.329  20.034   7.091  1.00 43.17           C  
ANISOU 5166  CB  GLN B 280     5372   5639   5393    360   -125    135       C  
ATOM   5167  CG  GLN B 280     -84.123  19.244   5.810  1.00 66.87           C  
ANISOU 5167  CG  GLN B 280     8346   8687   8376    300   -135    106       C  
ATOM   5168  CD  GLN B 280     -82.658  19.178   5.370  1.00 82.88           C  
ANISOU 5168  CD  GLN B 280    10434  10586  10470    270   -124     82       C  
ATOM   5169  OE1 GLN B 280     -82.099  20.146   4.838  1.00 84.99           O  
ANISOU 5169  OE1 GLN B 280    10743  10806  10742    328    -98    107       O  
ATOM   5170  NE2 GLN B 280     -82.037  18.021   5.584  1.00 85.32           N  
ANISOU 5170  NE2 GLN B 280    10750  10839  10827    181   -134     36       N  
ATOM   5171  N   GLN B 281     -83.828  17.311   8.516  1.00 44.93           N  
ANISOU 5171  N   GLN B 281     5574   5789   5707    164   -162     44       N  
ATOM   5172  CA  GLN B 281     -83.500  15.896   8.392  1.00 55.79           C  
ANISOU 5172  CA  GLN B 281     6948   7136   7114     70   -156      2       C  
ATOM   5173  C   GLN B 281     -84.405  14.975   9.212  1.00 52.75           C  
ANISOU 5173  C   GLN B 281     6528   6798   6719     18   -156    -11       C  
ATOM   5174  O   GLN B 281     -84.725  13.871   8.778  1.00 48.89           O  
ANISOU 5174  O   GLN B 281     6021   6334   6219    -67   -137    -50       O  
ATOM   5175  CB  GLN B 281     -82.027  15.636   8.725  1.00 63.70           C  
ANISOU 5175  CB  GLN B 281     8006   8008   8190     60   -141     -5       C  
ATOM   5176  CG  GLN B 281     -81.654  14.162   8.728  1.00 78.60           C  
ANISOU 5176  CG  GLN B 281     9903   9848  10112    -18   -116    -33       C  
ATOM   5177  CD  GLN B 281     -80.165  13.936   8.865  1.00 97.44           C  
ANISOU 5177  CD  GLN B 281    12335  12130  12556    -11    -97    -29       C  
ATOM   5178  OE1 GLN B 281     -79.399  14.203   7.938  1.00111.54           O  
ANISOU 5178  OE1 GLN B 281    14146  13886  14350     -7    -95    -38       O  
ATOM   5179  NE2 GLN B 281     -79.743  13.434  10.022  1.00 97.94           N  
ANISOU 5179  NE2 GLN B 281    12406  12152  12655     -3    -83    -11       N  
ATOM   5180  N   PHE B 282     -84.811  15.417  10.397  1.00 54.64           N  
ANISOU 5180  N   PHE B 282     6757   7044   6959     63   -169     16       N  
ATOM   5181  CA  PHE B 282     -85.703  14.618  11.224  1.00 53.89           C  
ANISOU 5181  CA  PHE B 282     6627   6997   6853     19   -169      9       C  
ATOM   5182  C   PHE B 282     -87.098  14.550  10.610  1.00 51.06           C  
ANISOU 5182  C   PHE B 282     6201   6791   6407     -6   -178     -2       C  
ATOM   5183  O   PHE B 282     -87.766  13.514  10.653  1.00 52.84           O  
ANISOU 5183  O   PHE B 282     6397   7067   6614    -92   -163    -38       O  
ATOM   5184  CB  PHE B 282     -85.779  15.194  12.633  1.00 57.55           C  
ANISOU 5184  CB  PHE B 282     7092   7441   7335     79   -183     42       C  
ATOM   5185  CG  PHE B 282     -86.876  14.603  13.466  1.00 53.86           C  
ANISOU 5185  CG  PHE B 282     6580   7042   6842     50   -187     43       C  
ATOM   5186  CD1 PHE B 282     -86.780  13.305  13.942  1.00 53.17           C  
ANISOU 5186  CD1 PHE B 282     6499   6912   6790    -21   -159     25       C  
ATOM   5187  CD2 PHE B 282     -87.998  15.346  13.780  1.00 50.67           C  
ANISOU 5187  CD2 PHE B 282     6133   6742   6379     99   -211     66       C  
ATOM   5188  CE1 PHE B 282     -87.785  12.758  14.713  1.00 52.13           C  
ANISOU 5188  CE1 PHE B 282     6330   6839   6637    -52   -156     25       C  
ATOM   5189  CE2 PHE B 282     -89.004  14.807  14.545  1.00 48.55           C  
ANISOU 5189  CE2 PHE B 282     5820   6544   6084     70   -216     66       C  
ATOM   5190  CZ  PHE B 282     -88.895  13.512  15.013  1.00 54.60           C  
ANISOU 5190  CZ  PHE B 282     6592   7264   6888    -11   -190     43       C  
ATOM   5191  N   LEU B 283     -87.539  15.668  10.050  1.00 44.02           N  
ANISOU 5191  N   LEU B 283     5286   5982   5458     71   -195     29       N  
ATOM   5192  CA  LEU B 283     -88.800  15.719   9.328  1.00 49.72           C  
ANISOU 5192  CA  LEU B 283     5930   6885   6078     64   -204     28       C  
ATOM   5193  C   LEU B 283     -88.809  14.698   8.184  1.00 53.79           C  
ANISOU 5193  C   LEU B 283     6419   7451   6566    -47   -187    -33       C  
ATOM   5194  O   LEU B 283     -89.673  13.826   8.121  1.00 48.88           O  
ANISOU 5194  O   LEU B 283     5744   6932   5895   -140   -178    -78       O  
ATOM   5195  CB  LEU B 283     -88.988  17.117   8.761  1.00 51.96           C  
ANISOU 5195  CB  LEU B 283     6206   7228   6309    187   -208     87       C  
ATOM   5196  CG  LEU B 283     -90.374  17.565   8.324  1.00 57.03           C  
ANISOU 5196  CG  LEU B 283     6759   8081   6830    239   -216    121       C  
ATOM   5197  CD1 LEU B 283     -91.443  17.332   9.415  1.00 58.23           C  
ANISOU 5197  CD1 LEU B 283     6863   8313   6949    231   -231    127       C  
ATOM   5198  CD2 LEU B 283     -90.254  19.025   7.995  1.00 56.42           C  
ANISOU 5198  CD2 LEU B 283     6709   7997   6730    386   -197    196       C  
ATOM   5199  N   GLN B 284     -87.840  14.815   7.283  1.00 45.26           N  
ANISOU 5199  N   GLN B 284     5379   6301   5516    -44   -177    -42       N  
ATOM   5200  CA  GLN B 284     -87.654  13.827   6.223  1.00 56.51           C  
ANISOU 5200  CA  GLN B 284     6794   7747   6928   -153   -153   -107       C  
ATOM   5201  C   GLN B 284     -87.629  12.396   6.768  1.00 54.69           C  
ANISOU 5201  C   GLN B 284     6588   7447   6745   -275   -115   -165       C  
ATOM   5202  O   GLN B 284     -88.172  11.475   6.165  1.00 62.80           O  
ANISOU 5202  O   GLN B 284     7581   8553   7729   -391    -85   -232       O  
ATOM   5203  CB  GLN B 284     -86.384  14.133   5.415  1.00 63.43           C  
ANISOU 5203  CB  GLN B 284     7728   8518   7854   -125   -146   -102       C  
ATOM   5204  CG  GLN B 284     -86.455  15.470   4.650  1.00 75.85           C  
ANISOU 5204  CG  GLN B 284     9281  10165   9373    -13   -164    -47       C  
ATOM   5205  CD  GLN B 284     -85.134  15.859   3.989  1.00 77.98           C  
ANISOU 5205  CD  GLN B 284     9616  10314   9699     18   -155    -39       C  
ATOM   5206  OE1 GLN B 284     -84.217  15.045   3.877  1.00 69.56           O  
ANISOU 5206  OE1 GLN B 284     8595   9137   8697    -51   -139    -80       O  
ATOM   5207  NE2 GLN B 284     -85.038  17.111   3.550  1.00 79.87           N  
ANISOU 5207  NE2 GLN B 284     9862  10573   9913    127   -156     18       N  
ATOM   5208  N   TYR B 285     -87.019  12.215   7.929  1.00 52.61           N  
ANISOU 5208  N   TYR B 285     6381   7042   6565   -250   -108   -141       N  
ATOM   5209  CA  TYR B 285     -86.948  10.897   8.550  1.00 56.50           C  
ANISOU 5209  CA  TYR B 285     6906   7453   7107   -342    -57   -177       C  
ATOM   5210  C   TYR B 285     -88.302  10.370   9.052  1.00 65.12           C  
ANISOU 5210  C   TYR B 285     7942   8657   8144   -411    -47   -204       C  
ATOM   5211  O   TYR B 285     -88.584   9.175   8.951  1.00 66.16           O  
ANISOU 5211  O   TYR B 285     8083   8775   8279   -530     14   -263       O  
ATOM   5212  CB  TYR B 285     -85.953  10.912   9.705  1.00 52.08           C  
ANISOU 5212  CB  TYR B 285     6408   6741   6637   -278    -52   -130       C  
ATOM   5213  CG  TYR B 285     -86.090   9.711  10.592  1.00 58.08           C  
ANISOU 5213  CG  TYR B 285     7193   7437   7438   -339      4   -141       C  
ATOM   5214  CD1 TYR B 285     -85.700   8.456  10.150  1.00 70.11           C  
ANISOU 5214  CD1 TYR B 285     8766   8876   8996   -429     82   -184       C  
ATOM   5215  CD2 TYR B 285     -86.626   9.824  11.859  1.00 56.00           C  
ANISOU 5215  CD2 TYR B 285     6909   7191   7177   -304    -11   -106       C  
ATOM   5216  CE1 TYR B 285     -85.832   7.347  10.956  1.00 77.31           C  
ANISOU 5216  CE1 TYR B 285     9712   9715   9947   -477    153   -187       C  
ATOM   5217  CE2 TYR B 285     -86.760   8.728  12.671  1.00 68.28           C  
ANISOU 5217  CE2 TYR B 285     8489   8685   8768   -353     47   -109       C  
ATOM   5218  CZ  TYR B 285     -86.363   7.490  12.220  1.00 81.28           C  
ANISOU 5218  CZ  TYR B 285    10190  10241  10451   -436    134   -146       C  
ATOM   5219  OH  TYR B 285     -86.503   6.393  13.040  1.00 89.91           O  
ANISOU 5219  OH  TYR B 285    11319  11261  11582   -476    213   -140       O  
ATOM   5220  N   THR B 286     -89.119  11.249   9.629  1.00 59.91           N  
ANISOU 5220  N   THR B 286     7228   8101   7434   -337    -96   -160       N  
ATOM   5221  CA  THR B 286     -90.458  10.854  10.038  1.00 58.27           C  
ANISOU 5221  CA  THR B 286     6954   8027   7159   -397    -94   -183       C  
ATOM   5222  C   THR B 286     -91.278  10.612   8.786  1.00 56.21           C  
ANISOU 5222  C   THR B 286     6618   7946   6793   -485    -86   -244       C  
ATOM   5223  O   THR B 286     -92.193   9.795   8.773  1.00 57.45           O  
ANISOU 5223  O   THR B 286     6728   8204   6896   -603    -54   -304       O  
ATOM   5224  CB  THR B 286     -91.177  11.937  10.862  1.00 54.19           C  
ANISOU 5224  CB  THR B 286     6391   7596   6601   -286   -148   -118       C  
ATOM   5225  OG1 THR B 286     -91.230  13.159  10.114  1.00 57.80           O  
ANISOU 5225  OG1 THR B 286     6819   8137   7003   -185   -184    -77       O  
ATOM   5226  CG2 THR B 286     -90.483  12.169  12.195  1.00 53.31           C  
ANISOU 5226  CG2 THR B 286     6340   7337   6580   -213   -155    -69       C  
ATOM   5227  N   ASP B 287     -90.939  11.346   7.734  1.00 63.63           N  
ANISOU 5227  N   ASP B 287     7542   8935   7699   -430   -110   -229       N  
ATOM   5228  CA  ASP B 287     -91.649  11.273   6.466  1.00 61.59           C  
ANISOU 5228  CA  ASP B 287     7198   8877   7327   -493   -108   -276       C  
ATOM   5229  C   ASP B 287     -91.470   9.889   5.851  1.00 63.51           C  
ANISOU 5229  C   ASP B 287     7463   9086   7582   -669    -41   -382       C  
ATOM   5230  O   ASP B 287     -92.440   9.266   5.423  1.00 72.46           O  
ANISOU 5230  O   ASP B 287     8521  10385   8624   -794    -15   -456       O  
ATOM   5231  CB  ASP B 287     -91.123  12.353   5.529  1.00 74.17           C  
ANISOU 5231  CB  ASP B 287     8787  10498   8897   -380   -140   -226       C  
ATOM   5232  CG  ASP B 287     -91.976  12.515   4.301  1.00 97.41           C  
ANISOU 5232  CG  ASP B 287    11619  13692  11700   -407   -147   -250       C  
ATOM   5233  OD1 ASP B 287     -93.212  12.647   4.459  1.00101.34           O  
ANISOU 5233  OD1 ASP B 287    12019  14396  12091   -410   -162   -245       O  
ATOM   5234  OD2 ASP B 287     -91.413  12.511   3.180  1.00102.26           O  
ANISOU 5234  OD2 ASP B 287    12235  14314  12303   -423   -137   -272       O  
ATOM   5235  N   ASN B 288     -90.225   9.415   5.816  1.00 63.71           N  
ANISOU 5235  N   ASN B 288     7590   8899   7717   -681     -5   -391       N  
ATOM   5236  CA  ASN B 288     -89.906   8.060   5.367  1.00 65.42           C  
ANISOU 5236  CA  ASN B 288     7856   9032   7967   -835     81   -483       C  
ATOM   5237  C   ASN B 288     -90.620   7.004   6.177  1.00 64.90           C  
ANISOU 5237  C   ASN B 288     7799   8951   7908   -951    144   -533       C  
ATOM   5238  O   ASN B 288     -91.215   6.081   5.634  1.00 76.07           O  
ANISOU 5238  O   ASN B 288     9190  10441   9271  -1113    210   -634       O  
ATOM   5239  CB  ASN B 288     -88.408   7.793   5.488  1.00 69.35           C  
ANISOU 5239  CB  ASN B 288     8469   9291   8589   -792    112   -457       C  
ATOM   5240  CG  ASN B 288     -87.593   8.608   4.519  1.00 68.80           C  
ANISOU 5240  CG  ASN B 288     8402   9220   8518   -712     70   -429       C  
ATOM   5241  OD1 ASN B 288     -88.056   8.931   3.424  1.00 62.87           O  
ANISOU 5241  OD1 ASN B 288     7581   8630   7678   -738     50   -460       O  
ATOM   5242  ND2 ASN B 288     -86.363   8.949   4.914  1.00 70.76           N  
ANISOU 5242  ND2 ASN B 288     8728   9298   8860   -615     59   -369       N  
ATOM   5243  N   LEU B 289     -90.534   7.139   7.490  1.00 71.12           N  
ANISOU 5243  N   LEU B 289     8622   9640   8759   -874    131   -467       N  
ATOM   5244  CA  LEU B 289     -91.120   6.173   8.407  1.00 76.99           C  
ANISOU 5244  CA  LEU B 289     9385  10344   9522   -964    195   -497       C  
ATOM   5245  C   LEU B 289     -92.619   5.969   8.153  1.00 84.38           C  
ANISOU 5245  C   LEU B 289    10216  11510  10335  -1080    197   -567       C  
ATOM   5246  O   LEU B 289     -93.147   4.875   8.344  1.00 93.39           O  
ANISOU 5246  O   LEU B 289    11372  12642  11470  -1229    283   -643       O  
ATOM   5247  CB  LEU B 289     -90.882   6.627   9.844  1.00 74.14           C  
ANISOU 5247  CB  LEU B 289     9052   9889   9227   -836    157   -402       C  
ATOM   5248  CG  LEU B 289     -90.644   5.529  10.874  1.00 78.15           C  
ANISOU 5248  CG  LEU B 289     9639  10236   9819   -878    244   -399       C  
ATOM   5249  CD1 LEU B 289     -89.522   4.594  10.423  1.00 77.85           C  
ANISOU 5249  CD1 LEU B 289     9704  10012   9862   -922    340   -423       C  
ATOM   5250  CD2 LEU B 289     -90.321   6.163  12.208  1.00 78.90           C  
ANISOU 5250  CD2 LEU B 289     9743  10269   9964   -735    192   -300       C  
ATOM   5251  N   TYR B 290     -93.298   7.027   7.725  1.00 79.27           N  
ANISOU 5251  N   TYR B 290     9463  11073   9583  -1011    111   -539       N  
ATOM   5252  CA  TYR B 290     -94.727   6.961   7.476  1.00 80.00           C  
ANISOU 5252  CA  TYR B 290     9434  11425   9537  -1101    103   -592       C  
ATOM   5253  C   TYR B 290     -94.987   6.149   6.215  1.00 89.64           C  
ANISOU 5253  C   TYR B 290    10618  12757  10683  -1282    167   -717       C  
ATOM   5254  O   TYR B 290     -95.906   5.335   6.171  1.00 97.74           O  
ANISOU 5254  O   TYR B 290    11595  13904  11638  -1449    225   -812       O  
ATOM   5255  CB  TYR B 290     -95.301   8.370   7.335  1.00 75.38           C  
ANISOU 5255  CB  TYR B 290     8748  11037   8857   -949      4   -509       C  
ATOM   5256  CG  TYR B 290     -96.809   8.446   7.405  1.00 73.17           C  
ANISOU 5256  CG  TYR B 290     8335  11034   8430   -998    -16   -532       C  
ATOM   5257  CD1 TYR B 290     -97.471   8.452   8.624  1.00 74.61           C  
ANISOU 5257  CD1 TYR B 290     8507  11224   8619   -975    -28   -498       C  
ATOM   5258  CD2 TYR B 290     -97.570   8.531   6.248  1.00 75.73           C  
ANISOU 5258  CD2 TYR B 290     8536  11636   8603  -1064    -22   -585       C  
ATOM   5259  CE1 TYR B 290     -98.862   8.530   8.687  1.00 78.51           C  
ANISOU 5259  CE1 TYR B 290     8872  11988   8972  -1018    -47   -517       C  
ATOM   5260  CE2 TYR B 290     -98.954   8.610   6.299  1.00 77.24           C  
ANISOU 5260  CE2 TYR B 290     8591  12114   8645  -1106    -40   -604       C  
ATOM   5261  CZ  TYR B 290     -99.595   8.610   7.520  1.00 78.39           C  
ANISOU 5261  CZ  TYR B 290     8729  12254   8799  -1083    -52   -570       C  
ATOM   5262  OH  TYR B 290    -100.971   8.686   7.563  1.00 81.89           O  
ANISOU 5262  OH  TYR B 290     9032  12996   9087  -1125    -70   -587       O  
ATOM   5263  N   LYS B 291     -94.156   6.363   5.200  1.00 92.28           N  
ANISOU 5263  N   LYS B 291    10977  13053  11033  -1257    163   -722       N  
ATOM   5264  CA  LYS B 291     -94.279   5.657   3.925  1.00 95.05           C  
ANISOU 5264  CA  LYS B 291    11294  13508  11314  -1423    223   -843       C  
ATOM   5265  C   LYS B 291     -93.750   4.222   3.999  1.00 98.63           C  
ANISOU 5265  C   LYS B 291    11866  13747  11862  -1586    352   -938       C  
ATOM   5266  O   LYS B 291     -93.608   3.553   2.975  1.00104.97           O  
ANISOU 5266  O   LYS B 291    12675  14576  12635  -1726    421  -1043       O  
ATOM   5267  CB  LYS B 291     -93.544   6.425   2.819  1.00 91.45           C  
ANISOU 5267  CB  LYS B 291    10824  13081  10843  -1328    173   -807       C  
ATOM   5268  N   LYS B 292     -93.452   3.760   5.209  1.00 97.57           N  
ANISOU 5268  N   LYS B 292    11829  13403  11838  -1560    395   -897       N  
ATOM   5269  CA  LYS B 292     -92.948   2.407   5.414  1.00 96.14           C  
ANISOU 5269  CA  LYS B 292    11776  13000  11754  -1687    536   -964       C  
ATOM   5270  C   LYS B 292     -93.977   1.597   6.187  1.00103.17           C  
ANISOU 5270  C   LYS B 292    12658  13924  12618  -1821    612  -1023       C  
ATOM   5271  O   LYS B 292     -93.938   0.369   6.196  1.00108.10           O  
ANISOU 5271  O   LYS B 292    13369  14421  13285  -1977    756  -1111       O  
ATOM   5272  CB  LYS B 292     -91.615   2.433   6.173  1.00 92.49           C  
ANISOU 5272  CB  LYS B 292    11443  12255  11444  -1537    544   -858       C  
ATOM   5273  N   ASN B 293     -94.903   2.299   6.831  1.00106.61           N  
ANISOU 5273  N   ASN B 293    12993  14530  12982  -1759    523   -974       N  
ATOM   5274  CA  ASN B 293     -95.965   1.654   7.583  1.00112.81           C  
ANISOU 5274  CA  ASN B 293    13754  15378  13730  -1880    580  -1024       C  
ATOM   5275  C   ASN B 293     -97.337   1.956   7.003  1.00115.00           C  
ANISOU 5275  C   ASN B 293    13864  16003  13827  -1982    535  -1099       C  
ATOM   5276  O   ASN B 293     -97.934   1.128   6.308  1.00121.95           O  
ANISOU 5276  O   ASN B 293    14710  16999  14627  -2199    625  -1241       O  
ATOM   5277  CB  ASN B 293     -95.943   2.111   9.045  1.00117.78           C  
ANISOU 5277  CB  ASN B 293    14409  15914  14430  -1722    525   -900       C  
ATOM   5278  CG  ASN B 293     -94.542   2.219   9.609  1.00117.22           C  
ANISOU 5278  CG  ASN B 293    14461  15568  14508  -1566    526   -796       C  
ATOM   5279  OD1 ASN B 293     -93.669   1.406   9.307  1.00115.64           O  
ANISOU 5279  OD1 ASN B 293    14371  15175  14392  -1614    627   -826       O  
ATOM   5280  ND2 ASN B 293     -94.321   3.232  10.443  1.00116.31           N  
ANISOU 5280  ND2 ASN B 293    14327  15443  14422  -1378    419   -675       N  
ATOM   5281  N   MET B 294     -97.819   3.159   7.301  1.00107.12           N  
ANISOU 5281  N   MET B 294    12762  15176  12762  -1823    403  -1001       N  
ATOM   5282  CA  MET B 294     -99.201   3.531   7.044  1.00102.00           C  
ANISOU 5282  CA  MET B 294    11946  14870  11938  -1878    353  -1037       C  
ATOM   5283  C   MET B 294     -99.428   3.890   5.589  1.00105.60           C  
ANISOU 5283  C   MET B 294    12289  15576  12258  -1921    323  -1094       C  
ATOM   5284  O   MET B 294    -100.244   3.267   4.911  1.00105.85           O  
ANISOU 5284  O   MET B 294    12230  15824  12163  -2120    379  -1225       O  
ATOM   5285  CB  MET B 294     -99.608   4.713   7.919  1.00 95.66           C  
ANISOU 5285  CB  MET B 294    11083  14149  11114  -1671    235   -899       C  
ATOM   5286  CG  MET B 294     -99.308   4.513   9.385  1.00 90.05           C  
ANISOU 5286  CG  MET B 294    10475  13206  10535  -1601    248   -829       C  
ATOM   5287  SD  MET B 294    -100.341   3.215  10.092  1.00172.97           S  
ANISOU 5287  SD  MET B 294    20974  23738  21010  -1822    358   -935       S  
ATOM   5288  CE  MET B 294    -101.957   3.982  10.029  1.00133.82           C  
ANISOU 5288  CE  MET B 294    15810  19190  15845  -1816    266   -933       C  
ATOM   5289  N   ASN B 295     -98.701   4.895   5.112  1.00106.10           N  
ANISOU 5289  N   ASN B 295    12354  15618  12343  -1739    241   -997       N  
ATOM   5290  CA  ASN B 295     -98.924   5.433   3.781  1.00104.73           C  
ANISOU 5290  CA  ASN B 295    12061  15698  12033  -1733    200  -1019       C  
ATOM   5291  C   ASN B 295    -100.399   5.678   3.496  1.00112.49           C  
ANISOU 5291  C   ASN B 295    12854  17078  12810  -1791    168  -1054       C  
ATOM   5292  O   ASN B 295    -100.854   5.470   2.363  1.00121.82           O  
ANISOU 5292  O   ASN B 295    13922  18515  13851  -1912    187  -1147       O  
ATOM   5293  CB  ASN B 295     -98.340   4.500   2.715  1.00 99.47           C  
ANISOU 5293  CB  ASN B 295    11443  14968  11383  -1910    291  -1149       C  
ATOM   5294  CG  ASN B 295     -98.488   5.052   1.303  1.00100.38           C  
ANISOU 5294  CG  ASN B 295    11432  15348  11358  -1900    248  -1169       C  
ATOM   5295  OD1 ASN B 295     -97.827   6.022   0.933  1.00101.59           O  
ANISOU 5295  OD1 ASN B 295    11593  15468  11537  -1712    176  -1062       O  
ATOM   5296  ND2 ASN B 295     -99.361   4.429   0.503  1.00 99.02           N  
ANISOU 5296  ND2 ASN B 295    11140  15452  11031  -2107    299  -1310       N  
ATOM   5297  N   GLU B 296    -101.146   6.102   4.517  1.00109.60           N  
ANISOU 5297  N   GLU B 296    12445  16779  12418  -1708    122   -982       N  
ATOM   5298  CA  GLU B 296    -102.519   6.535   4.322  1.00104.91           C  
ANISOU 5298  CA  GLU B 296    11663  16577  11623  -1713     78   -981       C  
ATOM   5299  C   GLU B 296    -102.520   7.291   3.012  1.00111.31           C  
ANISOU 5299  C   GLU B 296    12359  17627  12305  -1632     32   -954       C  
ATOM   5300  O   GLU B 296    -103.243   6.946   2.086  1.00118.03           O  
ANISOU 5300  O   GLU B 296    13070  18789  12987  -1776     55  -1054       O  
ATOM   5301  CB  GLU B 296    -102.959   7.455   5.466  1.00 93.72           C  
ANISOU 5301  CB  GLU B 296    10230  15165  10215  -1513      2   -840       C  
ATOM   5302  N   GLY B 297    -101.652   8.292   2.935  1.00109.04           N  
ANISOU 5302  N   GLY B 297    12138  17190  12101  -1409    -25   -822       N  
ATOM   5303  CA  GLY B 297    -101.439   9.057   1.727  1.00108.74           C  
ANISOU 5303  CA  GLY B 297    12025  17318  11974  -1304    -61   -776       C  
ATOM   5304  C   GLY B 297    -100.495  10.168   2.124  1.00107.71           C  
ANISOU 5304  C   GLY B 297    12005  16945  11974  -1051   -113   -619       C  
ATOM   5305  O   GLY B 297     -99.587   9.965   2.922  1.00108.17           O  
ANISOU 5305  O   GLY B 297    12222  16665  12214  -1031   -100   -602       O  
ATOM   5306  N   LEU B 298    -100.729  11.355   1.584  1.00104.41           N  
ANISOU 5306  N   LEU B 298    11503  16712  11457   -858   -162   -504       N  
ATOM   5307  CA  LEU B 298    -100.049  12.553   2.047  1.00 95.81           C  
ANISOU 5307  CA  LEU B 298    10508  15427  10468   -612   -200   -351       C  
ATOM   5308  C   LEU B 298    -100.722  13.001   3.333  1.00 87.73           C  
ANISOU 5308  C   LEU B 298     9485  14397   9452   -514   -226   -274       C  
ATOM   5309  O   LEU B 298    -101.796  13.601   3.309  1.00 92.43           O  
ANISOU 5309  O   LEU B 298     9949  15274   9894   -422   -249   -210       O  
ATOM   5310  CB  LEU B 298    -100.149  13.660   1.000  1.00 91.20           C  
ANISOU 5310  CB  LEU B 298     9837  15049   9767   -436   -223   -249       C  
ATOM   5311  CG  LEU B 298     -99.939  13.231  -0.450  1.00 79.08           C  
ANISOU 5311  CG  LEU B 298     8230  13671   8147   -542   -202   -330       C  
ATOM   5312  CD1 LEU B 298    -100.725  14.126  -1.388  1.00 72.56           C  
ANISOU 5312  CD1 LEU B 298     7235  13218   7117   -399   -220   -240       C  
ATOM   5313  CD2 LEU B 298     -98.466  13.226  -0.805  1.00 76.09           C  
ANISOU 5313  CD2 LEU B 298     8002  12978   7932   -527   -190   -333       C  
ATOM   5314  N   ALA B 299    -100.084  12.706   4.461  1.00 77.52           N  
ANISOU 5314  N   ALA B 299     8332  12792   8329   -528   -220   -276       N  
ATOM   5315  CA  ALA B 299    -100.641  13.039   5.766  1.00 73.25           C  
ANISOU 5315  CA  ALA B 299     7802  12220   7810   -450   -242   -214       C  
ATOM   5316  C   ALA B 299    -100.106  14.375   6.270  1.00 67.51           C  
ANISOU 5316  C   ALA B 299     7155  11339   7158   -210   -269    -73       C  
ATOM   5317  O   ALA B 299     -99.104  14.883   5.766  1.00 68.97           O  
ANISOU 5317  O   ALA B 299     7418  11372   7415   -129   -265    -36       O  
ATOM   5318  CB  ALA B 299    -100.343  11.934   6.768  1.00 71.77           C  
ANISOU 5318  CB  ALA B 299     7710  11808   7751   -601   -212   -296       C  
ATOM   5319  N   THR B 300    -100.780  14.939   7.267  1.00 54.24           N  
ANISOU 5319  N   THR B 300     5457   9695   5457   -105   -290      0       N  
ATOM   5320  CA  THR B 300    -100.315  16.161   7.911  1.00 59.96           C  
ANISOU 5320  CA  THR B 300     6269  10254   6257    102   -300    120       C  
ATOM   5321  C   THR B 300     -98.999  15.931   8.646  1.00 70.22           C  
ANISOU 5321  C   THR B 300     7731  11195   7755     76   -292     97       C  
ATOM   5322  O   THR B 300     -98.814  14.906   9.303  1.00 77.30           O  
ANISOU 5322  O   THR B 300     8667  11975   8728    -64   -285     21       O  
ATOM   5323  CB  THR B 300    -101.358  16.707   8.905  1.00 69.08           C  
ANISOU 5323  CB  THR B 300     7373  11524   7350    204   -316    191       C  
ATOM   5324  OG1 THR B 300    -102.288  17.548   8.211  1.00 73.12           O  
ANISOU 5324  OG1 THR B 300     7764  12329   7690    342   -316    276       O  
ATOM   5325  CG2 THR B 300    -100.677  17.510  10.003  1.00 76.70           C  
ANISOU 5325  CG2 THR B 300     8470  12221   8451    336   -315    262       C  
ATOM   5326  N   ASN B 301     -98.087  16.890   8.531  1.00 69.49           N  
ANISOU 5326  N   ASN B 301     7729  10938   7737    212   -285    166       N  
ATOM   5327  CA  ASN B 301     -96.914  16.941   9.396  1.00 66.92           C  
ANISOU 5327  CA  ASN B 301     7542  10305   7578    221   -280    164       C  
ATOM   5328  C   ASN B 301     -97.206  16.403  10.793  1.00 64.22           C  
ANISOU 5328  C   ASN B 301     7218   9890   7291    166   -291    142       C  
ATOM   5329  O   ASN B 301     -96.578  15.445  11.243  1.00 66.35           O  
ANISOU 5329  O   ASN B 301     7546  10005   7658     49   -282     78       O  
ATOM   5330  CB  ASN B 301     -96.375  18.370   9.485  1.00 71.92           C  
ANISOU 5330  CB  ASN B 301     8248  10830   8249    406   -266    260       C  
ATOM   5331  CG  ASN B 301     -95.414  18.701   8.361  1.00 80.81           C  
ANISOU 5331  CG  ASN B 301     9420  11882   9402    432   -247    264       C  
ATOM   5332  OD1 ASN B 301     -94.747  17.819   7.819  1.00 68.37           O  
ANISOU 5332  OD1 ASN B 301     7862  10242   7872    307   -248    190       O  
ATOM   5333  ND2 ASN B 301     -95.337  19.978   8.004  1.00 92.46           N  
ANISOU 5333  ND2 ASN B 301    10920  13359  10851    597   -219    355       N  
ATOM   5334  N   VAL B 302     -98.162  17.026  11.474  1.00 56.64           N  
ANISOU 5334  N   VAL B 302     6210   9046   6266    260   -304    202       N  
ATOM   5335  CA  VAL B 302     -98.523  16.625  12.829  1.00 57.38           C  
ANISOU 5335  CA  VAL B 302     6312   9088   6401    224   -316    190       C  
ATOM   5336  C   VAL B 302     -98.836  15.134  12.898  1.00 56.12           C  
ANISOU 5336  C   VAL B 302     6117   8967   6240     29   -310     93       C  
ATOM   5337  O   VAL B 302     -98.539  14.473  13.893  1.00 57.75           O  
ANISOU 5337  O   VAL B 302     6376   9031   6537    -36   -304     65       O  
ATOM   5338  CB  VAL B 302     -99.737  17.419  13.347  1.00 60.59           C  
ANISOU 5338  CB  VAL B 302     6645   9672   6704    343   -330    264       C  
ATOM   5339  CG1 VAL B 302    -100.257  16.808  14.640  1.00 60.72           C  
ANISOU 5339  CG1 VAL B 302     6650   9674   6746    278   -345    240       C  
ATOM   5340  CG2 VAL B 302     -99.366  18.880  13.552  1.00 60.02           C  
ANISOU 5340  CG2 VAL B 302     6641   9507   6658    535   -312    359       C  
ATOM   5341  N   ASN B 303     -99.438  14.611  11.834  1.00 61.42           N  
ANISOU 5341  N   ASN B 303     6697   9836   6804    -64   -302     42       N  
ATOM   5342  CA  ASN B 303     -99.884  13.223  11.812  1.00 68.39           C  
ANISOU 5342  CA  ASN B 303     7542  10779   7666   -265   -278    -62       C  
ATOM   5343  C   ASN B 303     -98.737  12.254  11.544  1.00 69.77           C  
ANISOU 5343  C   ASN B 303     7814  10733   7960   -387   -236   -136       C  
ATOM   5344  O   ASN B 303     -98.697  11.156  12.099  1.00 79.99           O  
ANISOU 5344  O   ASN B 303     9145  11935   9311   -518   -198   -199       O  
ATOM   5345  CB  ASN B 303    -100.989  13.032  10.771  1.00 66.12           C  
ANISOU 5345  CB  ASN B 303     7110  10811   7203   -335   -277   -102       C  
ATOM   5346  CG  ASN B 303    -102.309  13.637  11.205  1.00 73.73           C  
ANISOU 5346  CG  ASN B 303     7960  12021   8035   -249   -307    -42       C  
ATOM   5347  OD1 ASN B 303    -102.548  13.848  12.394  1.00 61.26           O  
ANISOU 5347  OD1 ASN B 303     6408  10369   6499   -192   -322      0       O  
ATOM   5348  ND2 ASN B 303    -103.175  13.921  10.239  1.00 78.40           N  
ANISOU 5348  ND2 ASN B 303     8415  12918   8455   -235   -315    -35       N  
ATOM   5349  N   LYS B 304     -97.807  12.667  10.689  1.00 58.90           N  
ANISOU 5349  N   LYS B 304     6485   9274   6620   -336   -235   -122       N  
ATOM   5350  CA  LYS B 304     -96.542  11.960  10.532  1.00 60.52           C  
ANISOU 5350  CA  LYS B 304     6798   9246   6952   -409   -199   -168       C  
ATOM   5351  C   LYS B 304     -95.793  11.868  11.858  1.00 58.12           C  
ANISOU 5351  C   LYS B 304     6594   8708   6781   -366   -195   -134       C  
ATOM   5352  O   LYS B 304     -95.273  10.812  12.216  1.00 64.17           O  
ANISOU 5352  O   LYS B 304     7423   9329   7630   -465   -149   -181       O  
ATOM   5353  CB  LYS B 304     -95.670  12.649   9.482  1.00 65.22           C  
ANISOU 5353  CB  LYS B 304     7424   9798   7559   -331   -208   -142       C  
ATOM   5354  CG  LYS B 304     -96.336  12.800   8.124  1.00 77.09           C  
ANISOU 5354  CG  LYS B 304     8821  11547   8923   -357   -211   -166       C  
ATOM   5355  CD  LYS B 304     -95.474  13.615   7.173  1.00 80.58           C  
ANISOU 5355  CD  LYS B 304     9296  11940   9380   -255   -220   -122       C  
ATOM   5356  CE  LYS B 304     -96.082  13.664   5.781  1.00 80.49           C  
ANISOU 5356  CE  LYS B 304     9172  12184   9225   -285   -219   -147       C  
ATOM   5357  NZ  LYS B 304     -95.259  14.479   4.844  1.00 75.87           N  
ANISOU 5357  NZ  LYS B 304     8619  11553   8653   -178   -223    -96       N  
ATOM   5358  N   ILE B 305     -95.742  12.982  12.581  1.00 54.20           N  
ANISOU 5358  N   ILE B 305     6110   8184   6301   -214   -235    -51       N  
ATOM   5359  CA  ILE B 305     -95.015  13.043  13.843  1.00 52.40           C  
ANISOU 5359  CA  ILE B 305     5961   7764   6184   -165   -236    -17       C  
ATOM   5360  C   ILE B 305     -95.677  12.170  14.904  1.00 62.80           C  
ANISOU 5360  C   ILE B 305     7261   9092   7510   -242   -220    -38       C  
ATOM   5361  O   ILE B 305     -94.998  11.555  15.726  1.00 72.81           O  
ANISOU 5361  O   ILE B 305     8593  10199   8872   -266   -195    -40       O  
ATOM   5362  CB  ILE B 305     -94.918  14.488  14.368  1.00 51.82           C  
ANISOU 5362  CB  ILE B 305     5902   7675   6113      2   -270     64       C  
ATOM   5363  CG1 ILE B 305     -94.095  15.350  13.409  1.00 49.63           C  
ANISOU 5363  CG1 ILE B 305     5664   7347   5847     78   -269     88       C  
ATOM   5364  CG2 ILE B 305     -94.311  14.507  15.763  1.00 49.08           C  
ANISOU 5364  CG2 ILE B 305     5615   7172   5861     35   -272     87       C  
ATOM   5365  CD1 ILE B 305     -92.801  14.705  12.965  1.00 52.60           C  
ANISOU 5365  CD1 ILE B 305     6112   7561   6313     11   -246     47       C  
ATOM   5366  N   LYS B 306     -97.004  12.121  14.879  1.00 64.83           N  
ANISOU 5366  N   LYS B 306     7425   9550   7659   -274   -233    -50       N  
ATOM   5367  CA  LYS B 306     -97.758  11.297  15.816  1.00 63.16           C  
ANISOU 5367  CA  LYS B 306     7187   9368   7441   -357   -215    -74       C  
ATOM   5368  C   LYS B 306     -97.549   9.813  15.538  1.00 63.08           C  
ANISOU 5368  C   LYS B 306     7213   9285   7471   -532   -142   -160       C  
ATOM   5369  O   LYS B 306     -97.428   9.009  16.463  1.00 60.58           O  
ANISOU 5369  O   LYS B 306     6942   8855   7222   -582   -101   -167       O  
ATOM   5370  CB  LYS B 306     -99.248  11.639  15.752  1.00 65.67           C  
ANISOU 5370  CB  LYS B 306     7386   9945   7619   -354   -244    -68       C  
ATOM   5371  CG  LYS B 306     -99.607  12.974  16.386  1.00 68.65           C  
ANISOU 5371  CG  LYS B 306     7740  10378   7966   -177   -296     24       C  
ATOM   5372  CD  LYS B 306    -101.113  13.167  16.451  1.00 69.28           C  
ANISOU 5372  CD  LYS B 306     7699  10720   7905   -173   -318     36       C  
ATOM   5373  CE  LYS B 306    -101.470  14.590  16.847  1.00 73.79           C  
ANISOU 5373  CE  LYS B 306     8250  11352   8432     20   -355    135       C  
ATOM   5374  NZ  LYS B 306    -102.939  14.766  17.020  1.00 79.31           N  
ANISOU 5374  NZ  LYS B 306     8830  12313   8991     39   -375    157       N  
ATOM   5375  N   SER B 307     -97.507   9.455  14.259  1.00 63.30           N  
ANISOU 5375  N   SER B 307     7223   9375   7453   -621   -116   -223       N  
ATOM   5376  CA  SER B 307     -97.223   8.083  13.855  1.00 67.53           C  
ANISOU 5376  CA  SER B 307     7807   9823   8028   -791    -29   -313       C  
ATOM   5377  C   SER B 307     -95.821   7.661  14.283  1.00 69.70           C  
ANISOU 5377  C   SER B 307     8208   9828   8449   -759     13   -288       C  
ATOM   5378  O   SER B 307     -95.602   6.518  14.685  1.00 75.28           O  
ANISOU 5378  O   SER B 307     8977  10408   9218   -854     96   -323       O  
ATOM   5379  CB  SER B 307     -97.380   7.927  12.342  1.00 70.76           C  
ANISOU 5379  CB  SER B 307     8168  10363   8354   -883    -13   -387       C  
ATOM   5380  OG  SER B 307     -97.622   6.575  11.991  1.00 76.82           O  
ANISOU 5380  OG  SER B 307     8953  11120   9117  -1083     82   -496       O  
ATOM   5381  N   PHE B 308     -94.876   8.591  14.195  1.00 66.73           N  
ANISOU 5381  N   PHE B 308     7867   9368   8120   -623    -37   -225       N  
ATOM   5382  CA  PHE B 308     -93.524   8.356  14.682  1.00 60.88           C  
ANISOU 5382  CA  PHE B 308     7227   8403   7501   -571     -9   -189       C  
ATOM   5383  C   PHE B 308     -93.535   8.172  16.188  1.00 66.36           C  
ANISOU 5383  C   PHE B 308     7943   9022   8249   -524     -4   -138       C  
ATOM   5384  O   PHE B 308     -93.000   7.198  16.708  1.00 70.42           O  
ANISOU 5384  O   PHE B 308     8522   9397   8838   -563     67   -138       O  
ATOM   5385  CB  PHE B 308     -92.638   9.543  14.347  1.00 51.18           C  
ANISOU 5385  CB  PHE B 308     6017   7136   6294   -440    -68   -137       C  
ATOM   5386  CG  PHE B 308     -91.369   9.589  15.138  1.00 51.63           C  
ANISOU 5386  CG  PHE B 308     6150   7011   6455   -362    -60    -87       C  
ATOM   5387  CD1 PHE B 308     -90.258   8.879  14.729  1.00 61.44           C  
ANISOU 5387  CD1 PHE B 308     7465   8112   7767   -395     -6   -103       C  
ATOM   5388  CD2 PHE B 308     -91.282  10.357  16.283  1.00 52.12           C  
ANISOU 5388  CD2 PHE B 308     6207   7060   6537   -256   -103    -25       C  
ATOM   5389  CE1 PHE B 308     -89.084   8.931  15.448  1.00 63.80           C  
ANISOU 5389  CE1 PHE B 308     7819   8277   8146   -318      2    -52       C  
ATOM   5390  CE2 PHE B 308     -90.119  10.410  17.009  1.00 53.77           C  
ANISOU 5390  CE2 PHE B 308     6469   7136   6824   -192    -96     14       C  
ATOM   5391  CZ  PHE B 308     -89.016   9.699  16.591  1.00 59.32           C  
ANISOU 5391  CZ  PHE B 308     7234   7716   7588   -220    -45      4       C  
ATOM   5392  N   ILE B 309     -94.145   9.131  16.875  1.00 61.27           N  
ANISOU 5392  N   ILE B 309     7243   8474   7563   -432    -72    -90       N  
ATOM   5393  CA  ILE B 309     -94.241   9.121  18.322  1.00 58.89           C  
ANISOU 5393  CA  ILE B 309     6946   8129   7299   -378    -79    -40       C  
ATOM   5394  C   ILE B 309     -94.909   7.856  18.834  1.00 66.79           C  
ANISOU 5394  C   ILE B 309     7947   9126   8302   -493    -10    -74       C  
ATOM   5395  O   ILE B 309     -94.451   7.258  19.801  1.00 76.77           O  
ANISOU 5395  O   ILE B 309     9259  10273   9638   -478     33    -41       O  
ATOM   5396  CB  ILE B 309     -95.008  10.349  18.818  1.00 57.17           C  
ANISOU 5396  CB  ILE B 309     6663   8041   7019   -277   -156      4       C  
ATOM   5397  CG1 ILE B 309     -94.057  11.539  18.961  1.00 45.16           C  
ANISOU 5397  CG1 ILE B 309     5176   6448   5537   -144   -199     55       C  
ATOM   5398  CG2 ILE B 309     -95.751  10.045  20.136  1.00 57.96           C  
ANISOU 5398  CG2 ILE B 309     6733   8173   7114   -277   -156     27       C  
ATOM   5399  CD1 ILE B 309     -94.778  12.821  19.328  1.00 51.23           C  
ANISOU 5399  CD1 ILE B 309     5895   7325   6243    -39   -254     97       C  
ATOM   5400  N   ASP B 310     -95.987   7.448  18.178  1.00 68.78           N  
ANISOU 5400  N   ASP B 310     8144   9517   8471   -609      8   -140       N  
ATOM   5401  CA  ASP B 310     -96.719   6.248  18.567  1.00 80.50           C  
ANISOU 5401  CA  ASP B 310     9630  11008   9948   -743     87   -188       C  
ATOM   5402  C   ASP B 310     -95.842   5.006  18.427  1.00 82.75           C  
ANISOU 5402  C   ASP B 310    10020  11097  10325   -823    202   -216       C  
ATOM   5403  O   ASP B 310     -95.965   4.056  19.199  1.00 86.53           O  
ANISOU 5403  O   ASP B 310    10542  11489  10848   -874    285   -214       O  
ATOM   5404  CB  ASP B 310     -97.978   6.092  17.706  1.00 86.91           C  
ANISOU 5404  CB  ASP B 310    10353  12031  10637   -870     88   -270       C  
ATOM   5405  CG  ASP B 310     -98.975   5.119  18.298  1.00 96.57           C  
ANISOU 5405  CG  ASP B 310    11556  13305  11832  -1002    155   -317       C  
ATOM   5406  OD1 ASP B 310     -99.684   4.442  17.523  1.00 98.93           O  
ANISOU 5406  OD1 ASP B 310    11819  13712  12057  -1168    211   -415       O  
ATOM   5407  OD2 ASP B 310     -99.057   5.033  19.543  1.00102.24           O  
ANISOU 5407  OD2 ASP B 310    12291  13961  12595   -946    155   -260       O  
ATOM   5408  N   THR B 311     -94.954   5.024  17.438  1.00 79.42           N  
ANISOU 5408  N   THR B 311     9642  10603   9931   -824    216   -237       N  
ATOM   5409  CA  THR B 311     -94.091   3.884  17.153  1.00 80.44           C  
ANISOU 5409  CA  THR B 311     9874  10549  10140   -891    333   -263       C  
ATOM   5410  C   THR B 311     -92.872   3.818  18.079  1.00 82.58           C  
ANISOU 5410  C   THR B 311    10219  10643  10515   -762    351   -169       C  
ATOM   5411  O   THR B 311     -92.586   2.775  18.663  1.00 88.94           O  
ANISOU 5411  O   THR B 311    11095  11316  11382   -787    459   -152       O  
ATOM   5412  CB  THR B 311     -93.627   3.896  15.680  1.00 84.98           C  
ANISOU 5412  CB  THR B 311    10464  11128  10698   -948    343   -325       C  
ATOM   5413  OG1 THR B 311     -94.686   3.417  14.838  1.00 84.23           O  
ANISOU 5413  OG1 THR B 311    10317  11174  10512  -1116    380   -432       O  
ATOM   5414  CG2 THR B 311     -92.399   3.017  15.494  1.00 87.78           C  
ANISOU 5414  CG2 THR B 311    10934  11268  11151   -955    446   -320       C  
ATOM   5415  N   LYS B 312     -92.163   4.933  18.218  1.00 76.62           N  
ANISOU 5415  N   LYS B 312     9445   9894   9772   -623    255   -108       N  
ATOM   5416  CA  LYS B 312     -90.931   4.963  19.000  1.00 78.18           C  
ANISOU 5416  CA  LYS B 312     9695   9962  10050   -504    265    -27       C  
ATOM   5417  C   LYS B 312     -91.151   5.195  20.498  1.00 82.31           C  
ANISOU 5417  C   LYS B 312    10188  10504  10583   -418    237     44       C  
ATOM   5418  O   LYS B 312     -90.199   5.455  21.231  1.00 86.03           O  
ANISOU 5418  O   LYS B 312    10674  10916  11098   -309    224    113       O  
ATOM   5419  CB  LYS B 312     -89.968   6.021  18.447  1.00 81.60           C  
ANISOU 5419  CB  LYS B 312    10125  10391  10489   -412    188     -6       C  
ATOM   5420  CG  LYS B 312     -88.829   5.486  17.570  1.00 82.46           C  
ANISOU 5420  CG  LYS B 312    10306  10379  10647   -428    249    -19       C  
ATOM   5421  CD  LYS B 312     -89.324   4.890  16.258  1.00 84.76           C  
ANISOU 5421  CD  LYS B 312    10609  10689  10906   -565    299   -111       C  
ATOM   5422  CE  LYS B 312     -88.381   5.216  15.097  1.00 79.94           C  
ANISOU 5422  CE  LYS B 312    10027  10041  10307   -551    284   -129       C  
ATOM   5423  NZ  LYS B 312     -86.943   4.923  15.377  1.00 74.27           N  
ANISOU 5423  NZ  LYS B 312     9377   9176   9665   -469    326    -71       N  
ATOM   5424  N   LEU B 313     -92.395   5.097  20.955  1.00 81.38           N  
ANISOU 5424  N   LEU B 313    10021  10483  10417   -471    228     25       N  
ATOM   5425  CA  LEU B 313     -92.694   5.293  22.373  1.00 81.63           C  
ANISOU 5425  CA  LEU B 313    10019  10542  10453   -396    202     88       C  
ATOM   5426  C   LEU B 313     -93.655   4.244  22.933  1.00 88.80           C  
ANISOU 5426  C   LEU B 313    10930  11453  11355   -489    283     72       C  
ATOM   5427  O   LEU B 313     -94.072   4.330  24.088  1.00 84.71           O  
ANISOU 5427  O   LEU B 313    10379  10972  10833   -440    265    120       O  
ATOM   5428  CB  LEU B 313     -93.245   6.698  22.632  1.00 81.33           C  
ANISOU 5428  CB  LEU B 313     9901  10644  10356   -322     79    101       C  
ATOM   5429  CG  LEU B 313     -92.233   7.843  22.605  1.00 86.56           C  
ANISOU 5429  CG  LEU B 313    10566  11288  11036   -206      9    136       C  
ATOM   5430  CD1 LEU B 313     -92.912   9.164  22.950  1.00 89.51           C  
ANISOU 5430  CD1 LEU B 313    10874  11784  11351   -137    -85    148       C  
ATOM   5431  CD2 LEU B 313     -91.082   7.564  23.561  1.00 84.17           C  
ANISOU 5431  CD2 LEU B 313    10297  10885  10799   -126     39    200       C  
ATOM   5432  N   LYS B 314     -93.999   3.260  22.109  1.00 95.13           N  
ANISOU 5432  N   LYS B 314    11774  12219  12153   -630    378     -1       N  
ATOM   5433  CA  LYS B 314     -94.759   2.104  22.570  1.00 97.53           C  
ANISOU 5433  CA  LYS B 314    12105  12491  12462   -737    490    -25       C  
ATOM   5434  C   LYS B 314     -94.060   0.801  22.197  1.00103.65           C  
ANISOU 5434  C   LYS B 314    12995  13079  13308   -803    651    -40       C  
ATOM   5435  O   LYS B 314     -93.877   0.500  21.018  1.00103.64           O  
ANISOU 5435  O   LYS B 314    13029  13048  13300   -896    694   -114       O  
ATOM   5436  CB  LYS B 314     -96.174   2.127  21.991  1.00 95.21           C  
ANISOU 5436  CB  LYS B 314    11741  12362  12073   -880    470   -120       C  
ATOM   5437  CG  LYS B 314     -97.003   3.326  22.423  1.00 91.76           C  
ANISOU 5437  CG  LYS B 314    11193  12114  11559   -809    330    -96       C  
ATOM   5438  CD  LYS B 314     -98.463   3.156  22.036  1.00 97.86           C  
ANISOU 5438  CD  LYS B 314    11889  13066  12228   -949    330   -179       C  
ATOM   5439  CE  LYS B 314     -99.346   4.161  22.758  1.00102.98           C  
ANISOU 5439  CE  LYS B 314    12436  13887  12806   -864    215   -136       C  
ATOM   5440  NZ  LYS B 314    -100.698   4.256  22.141  1.00103.59           N  
ANISOU 5440  NZ  LYS B 314    12415  14187  12757   -977    192   -211       N  
ATOM   5441  N   LYS B 315     -93.673   0.032  23.209  1.00107.36           N  
ANISOU 5441  N   LYS B 315    13524  13425  13841   -748    748     36       N  
ATOM   5442  CA  LYS B 315     -93.537  -1.413  23.065  1.00117.33           C  
ANISOU 5442  CA  LYS B 315    14900  14523  15158   -841    941     16       C  
ATOM   5443  C   LYS B 315     -94.898  -2.082  22.907  1.00128.64           C  
ANISOU 5443  C   LYS B 315    16326  16009  16543  -1030   1016    -84       C  
ATOM   5444  O   LYS B 315     -95.475  -2.575  23.876  1.00138.11           O  
ANISOU 5444  O   LYS B 315    17530  17195  17750  -1041   1075    -52       O  
ATOM   5445  CB  LYS B 315     -92.797  -2.004  24.267  1.00116.40           C  
ANISOU 5445  CB  LYS B 315    14840  14275  15111   -707   1031    142       C  
ATOM   5446  N   ALA B 316     -95.406  -2.096  21.678  1.00126.81           N  
ANISOU 5446  N   ALA B 316    16076  15851  16255  -1184   1014   -207       N  
ATOM   5447  CA  ALA B 316     -95.871  -3.329  21.055  1.00126.72           C  
ANISOU 5447  CA  ALA B 316    16144  15760  16245  -1387   1190   -316       C  
ATOM   5448  C   ALA B 316     -97.171  -3.811  21.690  1.00134.85           C  
ANISOU 5448  C   ALA B 316    17142  16866  17229  -1510   1244   -361       C  
ATOM   5449  O   ALA B 316     -98.122  -4.162  20.991  1.00137.51           O  
ANISOU 5449  O   ALA B 316    17450  17304  17493  -1709   1287   -492       O  
ATOM   5450  CB  ALA B 316     -94.801  -4.406  21.148  1.00119.09           C  
ANISOU 5450  CB  ALA B 316    15329  14536  15385  -1352   1372   -266       C  
ATOM   5451  N   ASP B 317     -97.205  -3.826  23.018  1.00139.02           N  
ANISOU 5451  N   ASP B 317    17669  17359  17793  -1395   1241   -254       N  
ATOM   5452  CA  ASP B 317     -98.400  -4.230  23.749  1.00142.75           C  
ANISOU 5452  CA  ASP B 317    18110  17903  18227  -1493   1284   -281       C  
ATOM   5453  C   ASP B 317     -99.175  -3.017  24.254  1.00145.01           C  
ANISOU 5453  C   ASP B 317    18246  18423  18430  -1420   1085   -255       C  
ATOM   5454  O   ASP B 317     -99.736  -3.038  25.349  1.00147.58           O  
ANISOU 5454  O   ASP B 317    18538  18784  18750  -1382   1076   -202       O  
ATOM   5455  CB  ASP B 317     -98.029  -5.142  24.921  1.00142.59           C  
ANISOU 5455  CB  ASP B 317    18190  17693  18297  -1419   1433   -179       C  
ATOM   5456  CG  ASP B 317     -96.572  -5.557  24.897  1.00140.78           C  
ANISOU 5456  CG  ASP B 317    18074  17251  18166  -1286   1524    -88       C  
ATOM   5457  OD1 ASP B 317     -96.001  -5.667  23.791  1.00141.34           O  
ANISOU 5457  OD1 ASP B 317    18192  17264  18248  -1336   1554   -147       O  
ATOM   5458  OD2 ASP B 317     -95.996  -5.774  25.984  1.00140.76           O  
ANISOU 5458  OD2 ASP B 317    18106  17154  18222  -1128   1566     46       O  
ATOM   5459  N   LYS B 318     -99.201  -1.961  23.448  1.00144.30           N  
ANISOU 5459  N   LYS B 318    18067  18485  18275  -1393    935   -287       N  
ATOM   5460  CA  LYS B 318    -100.075  -0.823  23.704  1.00143.42           C  
ANISOU 5460  CA  LYS B 318    17817  18607  18069  -1344    767   -278       C  
ATOM   5461  C   LYS B 318     -99.515   0.065  24.810  1.00141.02           C  
ANISOU 5461  C   LYS B 318    17486  18289  17806  -1124    656   -145       C  
ATOM   5462  O   LYS B 318    -100.125   1.067  25.184  1.00141.61           O  
ANISOU 5462  O   LYS B 318    17459  18530  17816  -1053    523   -120       O  
ATOM   5463  CB  LYS B 318    -101.481  -1.300  24.074  1.00144.09           C  
ANISOU 5463  CB  LYS B 318    17848  18821  18080  -1492    809   -343       C  
ATOM   5464  N   SER B 319     -98.351  -0.310  25.330  1.00135.33           N  
ANISOU 5464  N   SER B 319    16854  17378  17186  -1015    718    -60       N  
ATOM   5465  CA  SER B 319     -97.886   0.200  26.615  1.00126.13           C  
ANISOU 5465  CA  SER B 319    15668  16196  16059   -835    655     61       C  
ATOM   5466  C   SER B 319     -96.800   1.254  26.429  1.00110.46           C  
ANISOU 5466  C   SER B 319    13667  14208  14094   -684    544    114       C  
ATOM   5467  O   SER B 319     -95.928   1.117  25.571  1.00106.39           O  
ANISOU 5467  O   SER B 319    13209  13602  13613   -686    576     97       O  
ATOM   5468  CB  SER B 319     -97.365  -0.944  27.488  1.00130.34           C  
ANISOU 5468  CB  SER B 319    16296  16551  16676   -804    807    134       C  
ATOM   5469  OG  SER B 319     -97.577  -0.673  28.863  1.00133.44           O  
ANISOU 5469  OG  SER B 319    16640  16991  17070   -694    763    223       O  
ATOM   5470  N   TRP B 320     -96.858   2.306  27.240  1.00 99.31           N  
ANISOU 5470  N   TRP B 320    12181  12895  12659   -558    420    173       N  
ATOM   5471  CA  TRP B 320     -95.929   3.422  27.114  1.00 93.14           C  
ANISOU 5471  CA  TRP B 320    11378  12125  11885   -429    316    211       C  
ATOM   5472  C   TRP B 320     -94.530   3.030  27.576  1.00 94.72           C  
ANISOU 5472  C   TRP B 320    11642  12182  12164   -327    375    289       C  
ATOM   5473  O   TRP B 320     -94.358   2.464  28.656  1.00100.74           O  
ANISOU 5473  O   TRP B 320    12418  12899  12960   -271    434    360       O  
ATOM   5474  CB  TRP B 320     -96.429   4.627  27.914  1.00 92.27           C  
ANISOU 5474  CB  TRP B 320    11178  12154  11726   -335    189    244       C  
ATOM   5475  CG  TRP B 320     -97.519   5.392  27.228  1.00 99.58           C  
ANISOU 5475  CG  TRP B 320    12035  13238  12564   -387    108    182       C  
ATOM   5476  CD1 TRP B 320     -98.751   5.693  27.733  1.00103.69           C  
ANISOU 5476  CD1 TRP B 320    12482  13900  13017   -403     62    176       C  
ATOM   5477  CD2 TRP B 320     -97.477   5.953  25.911  1.00103.69           C  
ANISOU 5477  CD2 TRP B 320    12547  13805  13046   -417     67    128       C  
ATOM   5478  NE1 TRP B 320     -99.478   6.407  26.811  1.00104.15           N  
ANISOU 5478  NE1 TRP B 320    12483  14099  12992   -435     -2    126       N  
ATOM   5479  CE2 TRP B 320     -98.719   6.580  25.684  1.00102.29           C  
ANISOU 5479  CE2 TRP B 320    12285  13808  12771   -442      1     97       C  
ATOM   5480  CE3 TRP B 320     -96.511   5.986  24.901  1.00105.51           C  
ANISOU 5480  CE3 TRP B 320    12829  13950  13310   -419     82    107       C  
ATOM   5481  CZ2 TRP B 320     -99.019   7.232  24.490  1.00104.29           C  
ANISOU 5481  CZ2 TRP B 320    12502  14165  12958   -461    -46     53       C  
ATOM   5482  CZ3 TRP B 320     -96.811   6.634  23.716  1.00105.17           C  
ANISOU 5482  CZ3 TRP B 320    12754  14001  13206   -447     32     57       C  
ATOM   5483  CH2 TRP B 320     -98.054   7.248  23.521  1.00106.30           C  
ANISOU 5483  CH2 TRP B 320    12809  14329  13249   -464    -29     33       C  
ATOM   5484  N   LYS B 321     -93.533   3.334  26.752  1.00 93.53           N  
ANISOU 5484  N   LYS B 321    11524  11976  12036   -297    361    280       N  
ATOM   5485  CA  LYS B 321     -92.176   2.854  26.981  1.00 93.84           C  
ANISOU 5485  CA  LYS B 321    11623  11891  12140   -212    430    348       C  
ATOM   5486  C   LYS B 321     -91.449   3.608  28.092  1.00 95.23           C  
ANISOU 5486  C   LYS B 321    11748  12116  12318    -61    359    431       C  
ATOM   5487  O   LYS B 321     -90.490   3.095  28.666  1.00101.88           O  
ANISOU 5487  O   LYS B 321    12617  12893  13199     24    424    508       O  
ATOM   5488  CB  LYS B 321     -91.374   2.918  25.678  1.00 95.69           C  
ANISOU 5488  CB  LYS B 321    11906  12060  12392   -239    438    305       C  
ATOM   5489  CG  LYS B 321     -89.992   2.295  25.757  1.00101.49           C  
ANISOU 5489  CG  LYS B 321    12707  12667  13187   -159    525    372       C  
ATOM   5490  CD  LYS B 321     -89.301   2.332  24.407  1.00100.26           C  
ANISOU 5490  CD  LYS B 321    12600  12451  13046   -198    534    321       C  
ATOM   5491  CE  LYS B 321     -90.169   1.696  23.333  1.00 99.24           C  
ANISOU 5491  CE  LYS B 321    12509  12295  12903   -362    596    221       C  
ATOM   5492  NZ  LYS B 321     -89.432   1.583  22.042  1.00100.91           N  
ANISOU 5492  NZ  LYS B 321    12772  12437  13131   -400    622    175       N  
ATOM   5493  N   ILE B 322     -91.896   4.823  28.394  1.00 93.16           N  
ANISOU 5493  N   ILE B 322    11410  11978  12009    -28    234    415       N  
ATOM   5494  CA  ILE B 322     -91.295   5.587  29.486  1.00101.51           C  
ANISOU 5494  CA  ILE B 322    12414  13096  13059     94    172    475       C  
ATOM   5495  C   ILE B 322     -92.331   6.243  30.402  1.00107.94           C  
ANISOU 5495  C   ILE B 322    13154  14029  13827    110     98    476       C  
ATOM   5496  O   ILE B 322     -93.002   7.200  30.019  1.00114.45           O  
ANISOU 5496  O   ILE B 322    13945  14933  14609     90     15    426       O  
ATOM   5497  CB  ILE B 322     -90.280   6.639  28.978  1.00104.63           C  
ANISOU 5497  CB  ILE B 322    12802  13503  13451    147    101    459       C  
ATOM   5498  CG1 ILE B 322     -90.960   7.675  28.085  1.00106.28           C  
ANISOU 5498  CG1 ILE B 322    12993  13770  13620    101     17    386       C  
ATOM   5499  CG2 ILE B 322     -89.134   5.963  28.234  1.00109.26           C  
ANISOU 5499  CG2 ILE B 322    13454  13979  14081    150    175    472       C  
ATOM   5500  CD1 ILE B 322     -90.004   8.722  27.556  1.00109.19           C  
ANISOU 5500  CD1 ILE B 322    13366  14136  13987    146    -37    368       C  
ATOM   5501  N   SER B 323     -92.439   5.722  31.620  1.00107.56           N  
ANISOU 5501  N   SER B 323    13084  13997  13787    157    136    541       N  
ATOM   5502  CA  SER B 323     -93.440   6.173  32.581  1.00107.52           C  
ANISOU 5502  CA  SER B 323    13011  14100  13741    172     79    548       C  
ATOM   5503  C   SER B 323     -93.395   7.673  32.851  1.00100.50           C  
ANISOU 5503  C   SER B 323    12064  13311  12811    231    -36    527       C  
ATOM   5504  O   SER B 323     -92.420   8.350  32.518  1.00100.38           O  
ANISOU 5504  O   SER B 323    12057  13282  12803    271    -66    516       O  
ATOM   5505  CB  SER B 323     -93.290   5.410  33.896  1.00112.06           C  
ANISOU 5505  CB  SER B 323    13569  14675  14332    235    141    634       C  
ATOM   5506  OG  SER B 323     -93.473   4.019  33.695  1.00116.07           O  
ANISOU 5506  OG  SER B 323    14144  15079  14879    178    269    655       O  
ATOM   5507  N   ASN B 324     -94.463   8.177  33.462  1.00 93.69           N  
ANISOU 5507  N   ASN B 324    11148  12545  11906    232    -89    518       N  
ATOM   5508  CA  ASN B 324     -94.578   9.589  33.819  1.00 90.59           C  
ANISOU 5508  CA  ASN B 324    10708  12240  11473    288   -180    499       C  
ATOM   5509  C   ASN B 324     -94.910  10.491  32.644  1.00 86.65           C  
ANISOU 5509  C   ASN B 324    10226  11751  10946    260   -228    439       C  
ATOM   5510  O   ASN B 324     -94.562  11.669  32.658  1.00 90.60           O  
ANISOU 5510  O   ASN B 324    10719  12275  11431    311   -276    421       O  
ATOM   5511  CB  ASN B 324     -93.301  10.099  34.489  1.00 97.97           C  
ANISOU 5511  CB  ASN B 324    11626  13177  12420    368   -192    524       C  
ATOM   5512  CG  ASN B 324     -92.995   9.383  35.788  1.00106.55           C  
ANISOU 5512  CG  ASN B 324    12674  14295  13514    420   -153    594       C  
ATOM   5513  OD1 ASN B 324     -91.906   9.531  36.345  1.00110.62           O  
ANISOU 5513  OD1 ASN B 324    13166  14834  14031    481   -146    623       O  
ATOM   5514  ND2 ASN B 324     -93.952   8.596  36.278  1.00105.05           N  
ANISOU 5514  ND2 ASN B 324    12473  14119  13322    396   -121    624       N  
ATOM   5515  N   LEU B 325     -95.573   9.946  31.630  1.00 78.13           N  
ANISOU 5515  N   LEU B 325     9169  10659   9857    178   -204    406       N  
ATOM   5516  CA  LEU B 325     -96.003  10.756  30.494  1.00 76.48           C  
ANISOU 5516  CA  LEU B 325     8963  10488   9609    159   -246    359       C  
ATOM   5517  C   LEU B 325     -97.345  11.420  30.765  1.00 72.82           C  
ANISOU 5517  C   LEU B 325     8442  10153   9075    173   -296    355       C  
ATOM   5518  O   LEU B 325     -98.314  10.740  31.090  1.00 79.73           O  
ANISOU 5518  O   LEU B 325     9284  11087   9923    122   -281    357       O  
ATOM   5519  CB  LEU B 325     -96.122   9.905  29.228  1.00 71.32           C  
ANISOU 5519  CB  LEU B 325     8346   9792   8961     60   -198    320       C  
ATOM   5520  CG  LEU B 325     -94.854   9.377  28.577  1.00 68.44           C  
ANISOU 5520  CG  LEU B 325     8046   9302   8657     45   -148    316       C  
ATOM   5521  CD1 LEU B 325     -95.228   8.507  27.397  1.00 68.16           C  
ANISOU 5521  CD1 LEU B 325     8041   9242   8616    -68    -95    267       C  
ATOM   5522  CD2 LEU B 325     -93.949  10.526  28.160  1.00 69.26           C  
ANISOU 5522  CD2 LEU B 325     8164   9385   8766    113   -195    310       C  
ATOM   5523  N   THR B 326     -97.402  12.744  30.634  1.00 68.62           N  
ANISOU 5523  N   THR B 326     7900   9662   8509    244   -345    350       N  
ATOM   5524  CA  THR B 326     -98.688  13.437  30.614  1.00 68.63           C  
ANISOU 5524  CA  THR B 326     7852   9790   8432    270   -384    351       C  
ATOM   5525  C   THR B 326     -99.427  12.968  29.360  1.00 67.10           C  
ANISOU 5525  C   THR B 326     7645   9660   8191    191   -373    320       C  
ATOM   5526  O   THR B 326     -98.882  13.003  28.259  1.00 55.04           O  
ANISOU 5526  O   THR B 326     6153   8085   6675    169   -360    296       O  
ATOM   5527  CB  THR B 326     -98.538  14.981  30.580  1.00 53.43           C  
ANISOU 5527  CB  THR B 326     5940   7878   6485    370   -414    355       C  
ATOM   5528  OG1 THR B 326     -97.800  15.429  31.721  1.00 61.47           O  
ANISOU 5528  OG1 THR B 326     6967   8848   7541    423   -417    366       O  
ATOM   5529  CG2 THR B 326     -99.903  15.659  30.578  1.00 52.58           C  
ANISOU 5529  CG2 THR B 326     5781   7907   6290    416   -441    372       C  
ATOM   5530  N   VAL B 327    -100.662  12.513  29.524  1.00 64.11           N  
ANISOU 5530  N   VAL B 327     7208   9400   7751    143   -376    317       N  
ATOM   5531  CA  VAL B 327    -101.381  11.960  28.392  1.00 62.14           C  
ANISOU 5531  CA  VAL B 327     6931   9236   7443     46   -359    275       C  
ATOM   5532  C   VAL B 327    -102.798  12.509  28.282  1.00 62.64           C  
ANISOU 5532  C   VAL B 327     6910   9500   7392     68   -397    283       C  
ATOM   5533  O   VAL B 327    -103.443  12.804  29.280  1.00 61.77           O  
ANISOU 5533  O   VAL B 327     6760   9455   7254    118   -422    315       O  
ATOM   5534  CB  VAL B 327    -101.382  10.418  28.437  1.00 66.65           C  
ANISOU 5534  CB  VAL B 327     7520   9752   8051    -88   -293    243       C  
ATOM   5535  CG1 VAL B 327    -102.186   9.840  27.270  1.00 67.24           C  
ANISOU 5535  CG1 VAL B 327     7560   9934   8053   -213   -268    181       C  
ATOM   5536  CG2 VAL B 327     -99.949   9.897  28.420  1.00 55.44           C  
ANISOU 5536  CG2 VAL B 327     6185   8144   6736    -91   -247    247       C  
ATOM   5537  N   ILE B 328    -103.248  12.678  27.046  1.00 70.91           N  
ANISOU 5537  N   ILE B 328     7925  10653   8364     39   -400    257       N  
ATOM   5538  CA  ILE B 328    -104.585  13.152  26.753  1.00 75.11           C  
ANISOU 5538  CA  ILE B 328     8363  11408   8768     63   -430    268       C  
ATOM   5539  C   ILE B 328    -105.024  12.486  25.460  1.00 85.53           C  
ANISOU 5539  C   ILE B 328     9639  12843  10015    -60   -406    209       C  
ATOM   5540  O   ILE B 328    -104.257  12.440  24.497  1.00 98.38           O  
ANISOU 5540  O   ILE B 328    11311  14396  11675    -83   -388    183       O  
ATOM   5541  CB  ILE B 328    -104.617  14.677  26.559  1.00 72.50           C  
ANISOU 5541  CB  ILE B 328     8031  11120   8395    229   -463    326       C  
ATOM   5542  CG1 ILE B 328    -104.663  15.400  27.910  1.00 71.13           C  
ANISOU 5542  CG1 ILE B 328     7871  10905   8250    339   -483    376       C  
ATOM   5543  CG2 ILE B 328    -105.817  15.074  25.698  1.00 75.65           C  
ANISOU 5543  CG2 ILE B 328     8333  11763   8647    252   -477    339       C  
ATOM   5544  CD1 ILE B 328    -103.305  15.721  28.507  1.00 70.53           C  
ANISOU 5544  CD1 ILE B 328     7888  10617   8293    384   -473    381       C  
ATOM   5545  N   ASN B 329    -106.244  11.958  25.440  1.00 80.34           N  
ANISOU 5545  N   ASN B 329     8891  12376   9257   -148   -403    180       N  
ATOM   5546  CA  ASN B 329    -106.778  11.298  24.252  1.00 87.61           C  
ANISOU 5546  CA  ASN B 329     9752  13446  10089   -287   -376    109       C  
ATOM   5547  C   ASN B 329    -105.872  10.202  23.693  1.00 92.15           C  
ANISOU 5547  C   ASN B 329    10407  13852  10754   -428   -311     36       C  
ATOM   5548  O   ASN B 329    -106.015   9.801  22.535  1.00 93.52           O  
ANISOU 5548  O   ASN B 329    10551  14113  10869   -533   -284    -28       O  
ATOM   5549  CB  ASN B 329    -107.069  12.324  23.157  1.00 99.93           C  
ANISOU 5549  CB  ASN B 329    11254  15172  11544   -190   -409    138       C  
ATOM   5550  CG  ASN B 329    -108.312  13.150  23.440  1.00107.48           C  
ANISOU 5550  CG  ASN B 329    12102  16371  12365    -83   -452    198       C  
ATOM   5551  OD1 ASN B 329    -108.668  14.032  22.659  1.00112.49           O  
ANISOU 5551  OD1 ASN B 329    12681  17161  12901     22   -471    242       O  
ATOM   5552  ND2 ASN B 329    -108.980  12.867  24.556  1.00105.87           N  
ANISOU 5552  ND2 ASN B 329    11868  16205  12154   -100   -461    208       N  
ATOM   5553  N   GLY B 330    -104.939   9.721  24.513  1.00 93.85           N  
ANISOU 5553  N   GLY B 330    10720  13834  11105   -427   -280     49       N  
ATOM   5554  CA  GLY B 330    -104.007   8.693  24.083  1.00 87.95           C  
ANISOU 5554  CA  GLY B 330    10060  12907  10450   -537   -206     -4       C  
ATOM   5555  C   GLY B 330    -102.845   9.264  23.298  1.00 83.21           C  
ANISOU 5555  C   GLY B 330     9522  12191   9905   -463   -220     10       C  
ATOM   5556  O   GLY B 330    -102.285   8.590  22.435  1.00 83.59           O  
ANISOU 5556  O   GLY B 330     9614  12162   9983   -557   -168    -45       O  
ATOM   5557  N   VAL B 331    -102.492  10.513  23.592  1.00 82.11           N  
ANISOU 5557  N   VAL B 331     9387  12036   9775   -297   -282     80       N  
ATOM   5558  CA  VAL B 331    -101.334  11.157  22.973  1.00 82.74           C  
ANISOU 5558  CA  VAL B 331     9531  11994   9912   -219   -293     98       C  
ATOM   5559  C   VAL B 331    -100.544  11.975  24.002  1.00 74.71           C  
ANISOU 5559  C   VAL B 331     8566  10848   8973    -81   -321    163       C  
ATOM   5560  O   VAL B 331    -101.125  12.726  24.799  1.00 68.87           O  
ANISOU 5560  O   VAL B 331     7789  10180   8198      9   -359    207       O  
ATOM   5561  CB  VAL B 331    -101.728  12.041  21.755  1.00107.01           C  
ANISOU 5561  CB  VAL B 331    12552  15220  12887   -169   -324    101       C  
ATOM   5562  CG1 VAL B 331    -102.497  13.270  22.202  1.00105.92           C  
ANISOU 5562  CG1 VAL B 331    12358  15213  12675    -26   -375    169       C  
ATOM   5563  CG2 VAL B 331    -100.489  12.449  20.976  1.00108.85           C  
ANISOU 5563  CG2 VAL B 331    12858  15314  13185   -124   -318    104       C  
ATOM   5564  N   PRO B 332     -99.214  11.797  24.009  1.00 62.88           N  
ANISOU 5564  N   PRO B 332     7149   9167   7575    -71   -298    163       N  
ATOM   5565  CA  PRO B 332     -98.315  12.447  24.966  1.00 55.21           C  
ANISOU 5565  CA  PRO B 332     6223   8080   6674     34   -316    209       C  
ATOM   5566  C   PRO B 332     -97.995  13.870  24.537  1.00 57.19           C  
ANISOU 5566  C   PRO B 332     6487   8337   6906    146   -349    233       C  
ATOM   5567  O   PRO B 332     -97.050  14.083  23.782  1.00 72.48           O  
ANISOU 5567  O   PRO B 332     8472  10185   8880    153   -338    221       O  
ATOM   5568  CB  PRO B 332     -97.063  11.580  24.885  1.00 58.28           C  
ANISOU 5568  CB  PRO B 332     6682   8305   7157    -14   -267    195       C  
ATOM   5569  CG  PRO B 332     -97.095  11.057  23.483  1.00 54.30           C  
ANISOU 5569  CG  PRO B 332     6187   7814   6630   -105   -238    144       C  
ATOM   5570  CD  PRO B 332     -98.530  10.731  23.260  1.00 58.86           C  
ANISOU 5570  CD  PRO B 332     6691   8558   7116   -179   -240    115       C  
ATOM   5571  N   ILE B 333     -98.760  14.829  25.038  1.00 56.96           N  
ANISOU 5571  N   ILE B 333     6420   8402   6821    234   -381    267       N  
ATOM   5572  CA  ILE B 333     -98.714  16.194  24.532  1.00 63.73           C  
ANISOU 5572  CA  ILE B 333     7291   9279   7644    344   -391    294       C  
ATOM   5573  C   ILE B 333     -97.371  16.890  24.725  1.00 69.70           C  
ANISOU 5573  C   ILE B 333     8127   9877   8480    398   -379    296       C  
ATOM   5574  O   ILE B 333     -97.030  17.787  23.952  1.00 79.10           O  
ANISOU 5574  O   ILE B 333     9352  11043   9660    457   -367    305       O  
ATOM   5575  CB  ILE B 333     -99.841  17.067  25.127  1.00 66.70           C  
ANISOU 5575  CB  ILE B 333     7618   9781   7944    438   -411    338       C  
ATOM   5576  CG1 ILE B 333     -99.545  17.406  26.592  1.00 67.74           C  
ANISOU 5576  CG1 ILE B 333     7773   9840   8127    485   -417    353       C  
ATOM   5577  CG2 ILE B 333    -101.180  16.359  24.978  1.00 62.70           C  
ANISOU 5577  CG2 ILE B 333     7020   9455   7346    377   -425    333       C  
ATOM   5578  CD1 ILE B 333    -100.265  18.640  27.102  1.00 67.45           C  
ANISOU 5578  CD1 ILE B 333     7724   9871   8035    606   -419    396       C  
ATOM   5579  N   TRP B 334     -96.609  16.492  25.739  1.00 66.56           N  
ANISOU 5579  N   TRP B 334     7754   9384   8153    378   -374    289       N  
ATOM   5580  CA  TRP B 334     -95.262  17.044  25.902  1.00 72.25           C  
ANISOU 5580  CA  TRP B 334     8537   9977   8939    408   -360    280       C  
ATOM   5581  C   TRP B 334     -94.299  16.409  24.902  1.00 69.88           C  
ANISOU 5581  C   TRP B 334     8275   9593   8682    347   -341    254       C  
ATOM   5582  O   TRP B 334     -93.422  17.083  24.357  1.00 71.50           O  
ANISOU 5582  O   TRP B 334     8529   9726   8912    375   -329    244       O  
ATOM   5583  CB  TRP B 334     -94.749  16.888  27.339  1.00 68.62           C  
ANISOU 5583  CB  TRP B 334     8073   9476   8522    415   -361    284       C  
ATOM   5584  CG  TRP B 334     -95.466  17.771  28.297  1.00 68.53           C  
ANISOU 5584  CG  TRP B 334     8038   9526   8473    484   -374    301       C  
ATOM   5585  CD1 TRP B 334     -96.279  17.382  29.313  1.00 67.94           C  
ANISOU 5585  CD1 TRP B 334     7911   9526   8376    484   -392    320       C  
ATOM   5586  CD2 TRP B 334     -95.467  19.205  28.308  1.00 70.93           C  
ANISOU 5586  CD2 TRP B 334     8377   9817   8757    564   -359    302       C  
ATOM   5587  NE1 TRP B 334     -96.782  18.483  29.967  1.00 65.60           N  
ANISOU 5587  NE1 TRP B 334     7610   9269   8045    561   -396    332       N  
ATOM   5588  CE2 TRP B 334     -96.298  19.615  29.369  1.00 65.12           C  
ANISOU 5588  CE2 TRP B 334     7607   9150   7987    611   -369    320       C  
ATOM   5589  CE3 TRP B 334     -94.846  20.181  27.522  1.00 67.20           C  
ANISOU 5589  CE3 TRP B 334     7966   9273   8292    601   -328    290       C  
ATOM   5590  CZ2 TRP B 334     -96.523  20.957  29.669  1.00 57.91           C  
ANISOU 5590  CZ2 TRP B 334     6726   8231   7048    694   -342    325       C  
ATOM   5591  CZ3 TRP B 334     -95.064  21.515  27.828  1.00 63.88           C  
ANISOU 5591  CZ3 TRP B 334     7582   8841   7849    682   -295    295       C  
ATOM   5592  CH2 TRP B 334     -95.896  21.890  28.892  1.00 61.24           C  
ANISOU 5592  CH2 TRP B 334     7217   8570   7481    728   -299    312       C  
ATOM   5593  N   ALA B 335     -94.475  15.117  24.650  1.00 57.31           N  
ANISOU 5593  N   ALA B 335     6667   8009   7101    261   -329    241       N  
ATOM   5594  CA  ALA B 335     -93.677  14.443  23.641  1.00 59.06           C  
ANISOU 5594  CA  ALA B 335     6926   8156   7359    201   -303    215       C  
ATOM   5595  C   ALA B 335     -93.967  15.038  22.264  1.00 62.44           C  
ANISOU 5595  C   ALA B 335     7355   8633   7738    210   -310    202       C  
ATOM   5596  O   ALA B 335     -93.056  15.347  21.495  1.00 55.28           O  
ANISOU 5596  O   ALA B 335     6492   7652   6860    219   -299    192       O  
ATOM   5597  CB  ALA B 335     -93.964  12.956  23.653  1.00 60.15           C  
ANISOU 5597  CB  ALA B 335     7054   8290   7511    102   -270    199       C  
ATOM   5598  N   LEU B 336     -95.252  15.196  21.962  1.00 61.24           N  
ANISOU 5598  N   LEU B 336     7145   8620   7504    213   -326    208       N  
ATOM   5599  CA  LEU B 336     -95.677  15.768  20.695  1.00 55.59           C  
ANISOU 5599  CA  LEU B 336     6411   7991   6722    236   -330    209       C  
ATOM   5600  C   LEU B 336     -95.109  17.166  20.533  1.00 59.02           C  
ANISOU 5600  C   LEU B 336     6892   8369   7165    349   -327    240       C  
ATOM   5601  O   LEU B 336     -94.615  17.526  19.471  1.00 65.01           O  
ANISOU 5601  O   LEU B 336     7678   9101   7922    364   -315    236       O  
ATOM   5602  CB  LEU B 336     -97.197  15.820  20.630  1.00 51.83           C  
ANISOU 5602  CB  LEU B 336     5849   7705   6139    241   -347    222       C  
ATOM   5603  CG  LEU B 336     -97.782  16.485  19.397  1.00 45.55           C  
ANISOU 5603  CG  LEU B 336     5012   7044   5249    289   -350    239       C  
ATOM   5604  CD1 LEU B 336     -97.223  15.816  18.168  1.00 44.93           C  
ANISOU 5604  CD1 LEU B 336     4947   6944   5182    200   -333    192       C  
ATOM   5605  CD2 LEU B 336     -99.295  16.372  19.434  1.00 37.33           C  
ANISOU 5605  CD2 LEU B 336     3870   6222   4092    284   -366    252       C  
ATOM   5606  N   ILE B 337     -95.185  17.959  21.592  1.00 54.53           N  
ANISOU 5606  N   ILE B 337     6335   7778   6605    425   -331    267       N  
ATOM   5607  CA  ILE B 337     -94.663  19.312  21.541  1.00 55.76           C  
ANISOU 5607  CA  ILE B 337     6548   7865   6772    522   -308    287       C  
ATOM   5608  C   ILE B 337     -93.152  19.290  21.261  1.00 57.46           C  
ANISOU 5608  C   ILE B 337     6831   7933   7068    489   -290    256       C  
ATOM   5609  O   ILE B 337     -92.651  20.014  20.382  1.00 43.25           O  
ANISOU 5609  O   ILE B 337     5076   6087   5269    527   -265    259       O  
ATOM   5610  CB  ILE B 337     -94.996  20.082  22.834  1.00 59.74           C  
ANISOU 5610  CB  ILE B 337     7056   8367   7274    591   -303    308       C  
ATOM   5611  CG1 ILE B 337     -96.501  20.386  22.868  1.00 67.43           C  
ANISOU 5611  CG1 ILE B 337     7968   9497   8154    653   -313    352       C  
ATOM   5612  CG2 ILE B 337     -94.152  21.358  22.938  1.00 56.54           C  
ANISOU 5612  CG2 ILE B 337     6731   7848   6903    658   -259    306       C  
ATOM   5613  CD1 ILE B 337     -96.964  21.209  24.050  1.00 69.17           C  
ANISOU 5613  CD1 ILE B 337     8194   9724   8363    732   -303    377       C  
ATOM   5614  N   PHE B 338     -92.447  18.430  21.990  1.00 52.63           N  
ANISOU 5614  N   PHE B 338     6223   7257   6516    423   -298    231       N  
ATOM   5615  CA  PHE B 338     -91.012  18.313  21.854  1.00 48.96           C  
ANISOU 5615  CA  PHE B 338     5809   6677   6118    393   -282    205       C  
ATOM   5616  C   PHE B 338     -90.591  17.941  20.434  1.00 53.87           C  
ANISOU 5616  C   PHE B 338     6451   7273   6744    356   -273    191       C  
ATOM   5617  O   PHE B 338     -89.663  18.535  19.887  1.00 55.84           O  
ANISOU 5617  O   PHE B 338     6749   7447   7019    373   -255    180       O  
ATOM   5618  CB  PHE B 338     -90.432  17.305  22.851  1.00 53.95           C  
ANISOU 5618  CB  PHE B 338     6427   7274   6798    343   -286    197       C  
ATOM   5619  CG  PHE B 338     -88.965  17.017  22.623  1.00 53.47           C  
ANISOU 5619  CG  PHE B 338     6406   7120   6793    314   -268    178       C  
ATOM   5620  CD1 PHE B 338     -87.992  17.881  23.102  1.00 53.99           C  
ANISOU 5620  CD1 PHE B 338     6498   7138   6878    342   -256    163       C  
ATOM   5621  CD2 PHE B 338     -88.564  15.901  21.901  1.00 49.88           C  
ANISOU 5621  CD2 PHE B 338     5959   6629   6363    256   -255    171       C  
ATOM   5622  CE1 PHE B 338     -86.635  17.624  22.887  1.00 57.05           C  
ANISOU 5622  CE1 PHE B 338     6910   7462   7304    316   -241    146       C  
ATOM   5623  CE2 PHE B 338     -87.217  15.634  21.682  1.00 50.57           C  
ANISOU 5623  CE2 PHE B 338     6079   6639   6495    241   -236    162       C  
ATOM   5624  CZ  PHE B 338     -86.249  16.498  22.172  1.00 54.32           C  
ANISOU 5624  CZ  PHE B 338     6571   7085   6984    273   -233    152       C  
ATOM   5625  N   TYR B 339     -91.264  16.964  19.836  1.00 49.02           N  
ANISOU 5625  N   TYR B 339     5798   6724   6102    297   -281    184       N  
ATOM   5626  CA  TYR B 339     -90.863  16.500  18.508  1.00 50.46           C  
ANISOU 5626  CA  TYR B 339     5996   6890   6288    248   -269    161       C  
ATOM   5627  C   TYR B 339     -91.313  17.396  17.363  1.00 51.15           C  
ANISOU 5627  C   TYR B 339     6076   7045   6314    301   -269    176       C  
ATOM   5628  O   TYR B 339     -90.757  17.330  16.270  1.00 60.91           O  
ANISOU 5628  O   TYR B 339     7334   8253   7556    281   -258    161       O  
ATOM   5629  CB  TYR B 339     -91.321  15.069  18.257  1.00 52.67           C  
ANISOU 5629  CB  TYR B 339     6243   7206   6561    145   -261    133       C  
ATOM   5630  CG  TYR B 339     -90.497  14.057  18.991  1.00 51.92           C  
ANISOU 5630  CG  TYR B 339     6179   7009   6540     97   -236    125       C  
ATOM   5631  CD1 TYR B 339     -91.032  13.355  20.054  1.00 52.17           C  
ANISOU 5631  CD1 TYR B 339     6185   7061   6576     72   -230    135       C  
ATOM   5632  CD2 TYR B 339     -89.174  13.814  18.635  1.00 49.25           C  
ANISOU 5632  CD2 TYR B 339     5892   6559   6260     88   -215    116       C  
ATOM   5633  CE1 TYR B 339     -90.289  12.431  20.745  1.00 50.46           C  
ANISOU 5633  CE1 TYR B 339     5994   6756   6420     48   -196    143       C  
ATOM   5634  CE2 TYR B 339     -88.417  12.886  19.329  1.00 56.58           C  
ANISOU 5634  CE2 TYR B 339     6844   7409   7246     64   -183    124       C  
ATOM   5635  CZ  TYR B 339     -88.987  12.199  20.390  1.00 56.00           C  
ANISOU 5635  CZ  TYR B 339     6745   7357   7175     49   -171    141       C  
ATOM   5636  OH  TYR B 339     -88.261  11.265  21.096  1.00 59.47           O  
ANISOU 5636  OH  TYR B 339     7206   7724   7666     43   -128    164       O  
ATOM   5637  N   LEU B 340     -92.325  18.217  17.606  1.00 45.36           N  
ANISOU 5637  N   LEU B 340     5310   6408   5517    377   -275    212       N  
ATOM   5638  CA  LEU B 340     -92.716  19.220  16.632  1.00 43.66           C  
ANISOU 5638  CA  LEU B 340     5093   6258   5239    461   -261    247       C  
ATOM   5639  C   LEU B 340     -91.631  20.285  16.600  1.00 43.27           C  
ANISOU 5639  C   LEU B 340     5127   6070   5242    524   -227    256       C  
ATOM   5640  O   LEU B 340     -91.244  20.769  15.533  1.00 40.99           O  
ANISOU 5640  O   LEU B 340     4867   5763   4945    555   -205    266       O  
ATOM   5641  CB  LEU B 340     -94.076  19.832  16.991  1.00 47.14           C  
ANISOU 5641  CB  LEU B 340     5478   6839   5592    544   -264    296       C  
ATOM   5642  CG  LEU B 340     -95.287  18.899  16.892  1.00 47.29           C  
ANISOU 5642  CG  LEU B 340     5401   7032   5535    480   -293    286       C  
ATOM   5643  CD1 LEU B 340     -96.566  19.625  17.256  1.00 52.41           C  
ANISOU 5643  CD1 LEU B 340     5993   7829   6090    579   -296    343       C  
ATOM   5644  CD2 LEU B 340     -95.404  18.326  15.498  1.00 51.65           C  
ANISOU 5644  CD2 LEU B 340     5911   7676   6036    418   -294    260       C  
ATOM   5645  N   LEU B 341     -91.135  20.637  17.779  1.00 41.89           N  
ANISOU 5645  N   LEU B 341     4991   5806   5120    535   -219    247       N  
ATOM   5646  CA  LEU B 341     -89.982  21.517  17.904  1.00 41.88           C  
ANISOU 5646  CA  LEU B 341     5068   5672   5172    560   -181    233       C  
ATOM   5647  C   LEU B 341     -88.758  20.900  17.190  1.00 40.89           C  
ANISOU 5647  C   LEU B 341     4969   5466   5099    488   -185    197       C  
ATOM   5648  O   LEU B 341     -88.094  21.545  16.376  1.00 36.70           O  
ANISOU 5648  O   LEU B 341     4489   4876   4581    511   -154    196       O  
ATOM   5649  CB  LEU B 341     -89.683  21.731  19.385  1.00 47.36           C  
ANISOU 5649  CB  LEU B 341     5775   6317   5902    554   -179    214       C  
ATOM   5650  CG  LEU B 341     -89.320  23.158  19.787  1.00 59.43           C  
ANISOU 5650  CG  LEU B 341     7373   7769   7441    616   -119    211       C  
ATOM   5651  CD1 LEU B 341     -90.564  24.045  19.772  1.00 47.00           C  
ANISOU 5651  CD1 LEU B 341     5797   6258   5803    721    -88    264       C  
ATOM   5652  CD2 LEU B 341     -88.647  23.171  21.151  1.00 65.88           C  
ANISOU 5652  CD2 LEU B 341     8195   8540   8297    572   -119    168       C  
ATOM   5653  N   ARG B 342     -88.495  19.637  17.503  1.00 36.13           N  
ANISOU 5653  N   ARG B 342     4336   4863   4527    406   -215    172       N  
ATOM   5654  CA  ARG B 342     -87.418  18.861  16.915  1.00 39.44           C  
ANISOU 5654  CA  ARG B 342     4777   5215   4993    340   -214    143       C  
ATOM   5655  C   ARG B 342     -87.462  18.834  15.384  1.00 53.45           C  
ANISOU 5655  C   ARG B 342     6556   7012   6742    335   -208    143       C  
ATOM   5656  O   ARG B 342     -86.458  18.516  14.730  1.00 48.50           O  
ANISOU 5656  O   ARG B 342     5959   6316   6152    298   -200    121       O  
ATOM   5657  CB  ARG B 342     -87.466  17.438  17.476  1.00 41.27           C  
ANISOU 5657  CB  ARG B 342     4975   5457   5248    269   -229    131       C  
ATOM   5658  CG  ARG B 342     -86.462  16.439  16.881  1.00 44.28           C  
ANISOU 5658  CG  ARG B 342     5380   5771   5676    205   -216    108       C  
ATOM   5659  CD  ARG B 342     -85.031  16.642  17.384  1.00 39.84           C  
ANISOU 5659  CD  ARG B 342     4852   5122   5164    214   -203    102       C  
ATOM   5660  NE  ARG B 342     -84.182  17.096  16.296  1.00 57.27           N  
ANISOU 5660  NE  ARG B 342     7100   7277   7382    215   -191     88       N  
ATOM   5661  CZ  ARG B 342     -83.436  16.293  15.549  1.00 51.37           C  
ANISOU 5661  CZ  ARG B 342     6370   6486   6662    173   -179     75       C  
ATOM   5662  NH1 ARG B 342     -83.398  14.993  15.782  1.00 55.60           N  
ANISOU 5662  NH1 ARG B 342     6895   7011   7219    129   -166     77       N  
ATOM   5663  NH2 ARG B 342     -82.713  16.797  14.577  1.00 61.36           N  
ANISOU 5663  NH2 ARG B 342     7670   7711   7935    178   -171     63       N  
ATOM   5664  N   ALA B 343     -88.617  19.155  14.799  1.00 49.50           N  
ANISOU 5664  N   ALA B 343     6017   6622   6170    375   -212    169       N  
ATOM   5665  CA  ALA B 343     -88.699  19.186  13.336  1.00 36.43           C  
ANISOU 5665  CA  ALA B 343     4352   5015   4476    377   -206    173       C  
ATOM   5666  C   ALA B 343     -88.781  20.595  12.782  1.00 36.74           C  
ANISOU 5666  C   ALA B 343     4421   5056   4480    486   -173    218       C  
ATOM   5667  O   ALA B 343     -88.939  20.775  11.581  1.00 60.36           O  
ANISOU 5667  O   ALA B 343     7399   8108   7428    510   -163    235       O  
ATOM   5668  CB  ALA B 343     -89.873  18.348  12.838  1.00 33.41           C  
ANISOU 5668  CB  ALA B 343     3889   4786   4021    329   -226    165       C  
ATOM   5669  N   GLY B 344     -88.669  21.590  13.654  1.00 38.77           N  
ANISOU 5669  N   GLY B 344     4724   5249   4757    552   -145    238       N  
ATOM   5670  CA  GLY B 344     -88.742  22.982  13.244  1.00 40.95           C  
ANISOU 5670  CA  GLY B 344     5049   5502   5007    662    -88    284       C  
ATOM   5671  C   GLY B 344     -90.154  23.543  13.118  1.00 49.98           C  
ANISOU 5671  C   GLY B 344     6148   6783   6060    767    -73    351       C  
ATOM   5672  O   GLY B 344     -90.339  24.665  12.629  1.00 50.70           O  
ANISOU 5672  O   GLY B 344     6278   6869   6117    878    -12    407       O  
ATOM   5673  N   LEU B 345     -91.149  22.767  13.551  1.00 50.80           N  
ANISOU 5673  N   LEU B 345     6169   7014   6118    735   -121    350       N  
ATOM   5674  CA  LEU B 345     -92.555  23.169  13.432  1.00 51.58           C  
ANISOU 5674  CA  LEU B 345     6204   7281   6114    829   -114    414       C  
ATOM   5675  C   LEU B 345     -93.067  23.852  14.696  1.00 48.26           C  
ANISOU 5675  C   LEU B 345     5805   6839   5694    897    -93    440       C  
ATOM   5676  O   LEU B 345     -93.876  23.289  15.427  1.00 51.47           O  
ANISOU 5676  O   LEU B 345     6147   7337   6071    868   -133    435       O  
ATOM   5677  CB  LEU B 345     -93.440  21.967  13.085  1.00 51.57           C  
ANISOU 5677  CB  LEU B 345     6092   7458   6045    747   -171    392       C  
ATOM   5678  CG  LEU B 345     -92.989  21.091  11.912  1.00 55.24           C  
ANISOU 5678  CG  LEU B 345     6530   7951   6507    652   -191    347       C  
ATOM   5679  CD1 LEU B 345     -93.825  19.818  11.858  1.00 57.55           C  
ANISOU 5679  CD1 LEU B 345     6727   8394   6747    538   -233    302       C  
ATOM   5680  CD2 LEU B 345     -93.030  21.839  10.565  1.00 45.53           C  
ANISOU 5680  CD2 LEU B 345     5293   6794   5213    742   -158    399       C  
ATOM   5681  N   ILE B 346     -92.597  25.074  14.932  1.00 50.10           N  
ANISOU 5681  N   ILE B 346     6130   6947   5959    982    -21    465       N  
ATOM   5682  CA  ILE B 346     -92.962  25.842  16.116  1.00 54.45           C  
ANISOU 5682  CA  ILE B 346     6718   7453   6516   1045     17    481       C  
ATOM   5683  C   ILE B 346     -94.432  26.277  16.125  1.00 57.41           C  
ANISOU 5683  C   ILE B 346     7035   7990   6786   1169     34    564       C  
ATOM   5684  O   ILE B 346     -95.086  26.267  17.173  1.00 59.65           O  
ANISOU 5684  O   ILE B 346     7295   8312   7056   1181     20    567       O  
ATOM   5685  CB  ILE B 346     -92.060  27.081  16.282  1.00 63.73           C  
ANISOU 5685  CB  ILE B 346     8018   8446   7749   1093    113    475       C  
ATOM   5686  CG1 ILE B 346     -90.669  26.803  15.708  1.00 74.70           C  
ANISOU 5686  CG1 ILE B 346     9454   9718   9210   1000    108    417       C  
ATOM   5687  CG2 ILE B 346     -91.970  27.474  17.759  1.00 64.96           C  
ANISOU 5687  CG2 ILE B 346     8214   8522   7945   1077    134    439       C  
ATOM   5688  CD1 ILE B 346     -89.779  28.028  15.610  1.00 81.26           C  
ANISOU 5688  CD1 ILE B 346    10405  10383  10086   1037    212    407       C  
ATOM   5689  N   LYS B 347     -94.948  26.660  14.963  1.00 56.22           N  
ANISOU 5689  N   LYS B 347     6858   7949   6556   1266     65    634       N  
ATOM   5690  CA  LYS B 347     -96.345  27.052  14.858  1.00 64.35           C  
ANISOU 5690  CA  LYS B 347     7817   9168   7466   1396     82    724       C  
ATOM   5691  C   LYS B 347     -97.241  25.900  15.299  1.00 64.36           C  
ANISOU 5691  C   LYS B 347     7694   9344   7415   1308    -12    695       C  
ATOM   5692  O   LYS B 347     -98.156  26.072  16.118  1.00 50.90           O  
ANISOU 5692  O   LYS B 347     5954   7723   5665   1361    -14    727       O  
ATOM   5693  CB  LYS B 347     -96.697  27.446  13.426  1.00 71.22           C  
ANISOU 5693  CB  LYS B 347     8651  10165   8244   1503    121    804       C  
ATOM   5694  CG  LYS B 347     -98.008  28.209  13.323  1.00 78.85           C  
ANISOU 5694  CG  LYS B 347     9567  11311   9083   1686    174    922       C  
ATOM   5695  CD  LYS B 347     -98.819  27.800  12.095  1.00 86.33           C  
ANISOU 5695  CD  LYS B 347    10378  12533   9891   1725    142    976       C  
ATOM   5696  CE  LYS B 347     -98.061  27.999  10.796  1.00 86.04           C  
ANISOU 5696  CE  LYS B 347    10370  12459   9861   1741    175    990       C  
ATOM   5697  NZ  LYS B 347     -98.938  27.662   9.637  1.00 93.50           N  
ANISOU 5697  NZ  LYS B 347    11168  13707  10651   1787    150   1045       N  
ATOM   5698  N   GLU B 348     -96.960  24.722  14.751  1.00 63.19           N  
ANISOU 5698  N   GLU B 348     7487   9246   7276   1169    -80    631       N  
ATOM   5699  CA  GLU B 348     -97.729  23.529  15.070  1.00 60.90           C  
ANISOU 5699  CA  GLU B 348     7089   9108   6942   1061   -154    590       C  
ATOM   5700  C   GLU B 348     -97.567  23.120  16.538  1.00 61.49           C  
ANISOU 5700  C   GLU B 348     7190   9077   7095    989   -183    541       C  
ATOM   5701  O   GLU B 348     -98.525  22.683  17.179  1.00 64.04           O  
ANISOU 5701  O   GLU B 348     7440   9525   7367    971   -216    544       O  
ATOM   5702  CB  GLU B 348     -97.363  22.387  14.125  1.00 51.31           C  
ANISOU 5702  CB  GLU B 348     5828   7940   5728    922   -196    524       C  
ATOM   5703  CG  GLU B 348     -97.849  22.584  12.683  1.00 57.34           C  
ANISOU 5703  CG  GLU B 348     6520   8889   6378    979   -182    569       C  
ATOM   5704  CD  GLU B 348     -96.943  23.495  11.842  1.00 67.76           C  
ANISOU 5704  CD  GLU B 348     7925  10087   7733   1068   -126    608       C  
ATOM   5705  OE1 GLU B 348     -95.836  23.861  12.299  1.00 72.07           O  
ANISOU 5705  OE1 GLU B 348     8587  10400   8398   1058   -101    583       O  
ATOM   5706  OE2 GLU B 348     -97.344  23.848  10.713  1.00 62.95           O  
ANISOU 5706  OE2 GLU B 348     7262   9631   7027   1148   -103    664       O  
ATOM   5707  N   ALA B 349     -96.359  23.276  17.069  1.00 63.51           N  
ANISOU 5707  N   ALA B 349     7544   9119   7466    950   -167    498       N  
ATOM   5708  CA  ALA B 349     -96.095  22.979  18.477  1.00 59.38           C  
ANISOU 5708  CA  ALA B 349     7043   8504   7014    893   -188    457       C  
ATOM   5709  C   ALA B 349     -96.902  23.882  19.401  1.00 57.76           C  
ANISOU 5709  C   ALA B 349     6844   8332   6771   1004   -159    507       C  
ATOM   5710  O   ALA B 349     -97.378  23.455  20.449  1.00 59.82           O  
ANISOU 5710  O   ALA B 349     7067   8629   7033    970   -192    493       O  
ATOM   5711  CB  ALA B 349     -94.604  23.125  18.777  1.00 49.39           C  
ANISOU 5711  CB  ALA B 349     5873   7034   5861    843   -169    406       C  
ATOM   5712  N   LEU B 350     -97.035  25.142  19.010  1.00 61.80           N  
ANISOU 5712  N   LEU B 350     7409   8822   7251   1141    -86    568       N  
ATOM   5713  CA  LEU B 350     -97.723  26.126  19.830  1.00 65.27           C  
ANISOU 5713  CA  LEU B 350     7873   9267   7657   1260    -34    619       C  
ATOM   5714  C   LEU B 350     -99.213  25.819  19.845  1.00 60.58           C  
ANISOU 5714  C   LEU B 350     7166   8905   6948   1312    -70    676       C  
ATOM   5715  O   LEU B 350     -99.848  25.864  20.889  1.00 52.20           O  
ANISOU 5715  O   LEU B 350     6082   7882   5872   1332    -81    683       O  
ATOM   5716  CB  LEU B 350     -97.468  27.536  19.286  1.00 66.46           C  
ANISOU 5716  CB  LEU B 350     8123   9325   7802   1399     77    677       C  
ATOM   5717  CG  LEU B 350     -97.790  28.713  20.206  1.00 64.16           C  
ANISOU 5717  CG  LEU B 350     7909   8959   7512   1512    165    712       C  
ATOM   5718  CD1 LEU B 350     -97.011  28.607  21.496  1.00 63.14           C  
ANISOU 5718  CD1 LEU B 350     7829   8683   7478   1406    154    621       C  
ATOM   5719  CD2 LEU B 350     -97.485  30.027  19.519  1.00 62.62           C  
ANISOU 5719  CD2 LEU B 350     7824   8654   7315   1643    296    769       C  
ATOM   5720  N   GLN B 351     -99.756  25.500  18.675  1.00 64.80           N  
ANISOU 5720  N   GLN B 351     7622   9605   7393   1330    -87    711       N  
ATOM   5721  CA  GLN B 351    -101.166  25.177  18.532  1.00 59.23           C  
ANISOU 5721  CA  GLN B 351     6789   9158   6556   1369   -120    760       C  
ATOM   5722  C   GLN B 351    -101.558  24.086  19.511  1.00 61.70           C  
ANISOU 5722  C   GLN B 351     7037   9521   6885   1239   -195    698       C  
ATOM   5723  O   GLN B 351    -102.617  24.153  20.146  1.00 57.83           O  
ANISOU 5723  O   GLN B 351     6484   9167   6323   1288   -208    734       O  
ATOM   5724  CB  GLN B 351    -101.469  24.726  17.102  1.00 52.65           C  
ANISOU 5724  CB  GLN B 351     5870   8504   5632   1352   -139    774       C  
ATOM   5725  CG  GLN B 351    -101.452  25.858  16.100  1.00 57.71           C  
ANISOU 5725  CG  GLN B 351     6545   9166   6217   1521    -58    868       C  
ATOM   5726  CD  GLN B 351    -101.425  25.376  14.664  1.00 60.91           C  
ANISOU 5726  CD  GLN B 351     6876   9714   6554   1483    -78    865       C  
ATOM   5727  OE1 GLN B 351    -101.329  24.178  14.398  1.00 64.99           O  
ANISOU 5727  OE1 GLN B 351     7327  10290   7075   1315   -147    780       O  
ATOM   5728  NE2 GLN B 351    -101.501  26.313  13.727  1.00 57.61           N  
ANISOU 5728  NE2 GLN B 351     6471   9347   6071   1640     -8    958       N  
ATOM   5729  N   VAL B 352    -100.688  23.086  19.633  1.00 58.48           N  
ANISOU 5729  N   VAL B 352     6649   9001   6571   1079   -238    610       N  
ATOM   5730  CA  VAL B 352    -100.954  21.949  20.505  1.00 56.96           C  
ANISOU 5730  CA  VAL B 352     6404   8836   6401    950   -296    553       C  
ATOM   5731  C   VAL B 352    -101.066  22.388  21.952  1.00 61.19           C  
ANISOU 5731  C   VAL B 352     6975   9298   6978    995   -290    563       C  
ATOM   5732  O   VAL B 352    -101.957  21.947  22.673  1.00 68.28           O  
ANISOU 5732  O   VAL B 352     7804  10309   7831    974   -323    567       O  
ATOM   5733  CB  VAL B 352     -99.876  20.859  20.375  1.00 46.78           C  
ANISOU 5733  CB  VAL B 352     5147   7415   5211    794   -320    471       C  
ATOM   5734  CG1 VAL B 352     -99.967  19.902  21.545  1.00 42.84           C  
ANISOU 5734  CG1 VAL B 352     4628   6889   4759    693   -355    427       C  
ATOM   5735  CG2 VAL B 352    -100.009  20.127  19.027  1.00 42.04           C  
ANISOU 5735  CG2 VAL B 352     4490   6926   4556    715   -332    444       C  
ATOM   5736  N   LEU B 353    -100.163  23.267  22.366  1.00 61.54           N  
ANISOU 5736  N   LEU B 353     7125   9158   7101   1050   -245    562       N  
ATOM   5737  CA  LEU B 353    -100.184  23.797  23.722  1.00 58.89           C  
ANISOU 5737  CA  LEU B 353     6826   8747   6801   1090   -229    563       C  
ATOM   5738  C   LEU B 353    -101.394  24.705  23.971  1.00 66.17           C  
ANISOU 5738  C   LEU B 353     7723   9791   7628   1237   -195    641       C  
ATOM   5739  O   LEU B 353    -101.878  24.804  25.098  1.00 55.24           O  
ANISOU 5739  O   LEU B 353     6324   8424   6240   1255   -204    645       O  
ATOM   5740  CB  LEU B 353     -98.897  24.566  24.005  1.00 49.06           C  
ANISOU 5740  CB  LEU B 353     5698   7289   5652   1098   -176    529       C  
ATOM   5741  CG  LEU B 353     -98.596  24.839  25.478  1.00 57.55           C  
ANISOU 5741  CG  LEU B 353     6807   8276   6781   1084   -168    495       C  
ATOM   5742  CD1 LEU B 353     -98.698  23.558  26.309  1.00 53.20           C  
ANISOU 5742  CD1 LEU B 353     6183   7776   6253    973   -244    458       C  
ATOM   5743  CD2 LEU B 353     -97.219  25.477  25.613  1.00 59.20           C  
ANISOU 5743  CD2 LEU B 353     7119   8298   7075   1060   -114    444       C  
ATOM   5744  N   VAL B 354    -101.860  25.379  22.917  1.00 67.79           N  
ANISOU 5744  N   VAL B 354     7921  10082   7753   1351   -150    710       N  
ATOM   5745  CA  VAL B 354    -103.008  26.278  23.010  1.00 61.69           C  
ANISOU 5745  CA  VAL B 354     7123   9439   6876   1517   -103    804       C  
ATOM   5746  C   VAL B 354    -104.276  25.455  23.154  1.00 70.60           C  
ANISOU 5746  C   VAL B 354     8110  10814   7900   1487   -173    821       C  
ATOM   5747  O   VAL B 354    -105.162  25.787  23.948  1.00 79.26           O  
ANISOU 5747  O   VAL B 354     9174  11998   8943   1564   -168    863       O  
ATOM   5748  CB  VAL B 354    -103.148  27.170  21.760  1.00 57.75           C  
ANISOU 5748  CB  VAL B 354     6647   8986   6308   1661    -28    888       C  
ATOM   5749  CG1 VAL B 354    -104.486  27.899  21.761  1.00 59.84           C  
ANISOU 5749  CG1 VAL B 354     6857   9439   6440   1842     17   1000       C  
ATOM   5750  CG2 VAL B 354    -102.029  28.170  21.699  1.00 58.62           C  
ANISOU 5750  CG2 VAL B 354     6908   8851   6513   1708     64    879       C  
ATOM   5751  N   GLU B 355    -104.364  24.376  22.383  1.00 64.59           N  
ANISOU 5751  N   GLU B 355     7266  10168   7108   1368   -233    782       N  
ATOM   5752  CA  GLU B 355    -105.517  23.486  22.439  1.00 60.96           C  
ANISOU 5752  CA  GLU B 355     6668   9948   6545   1305   -293    778       C  
ATOM   5753  C   GLU B 355    -105.734  22.953  23.852  1.00 71.46           C  
ANISOU 5753  C   GLU B 355     7987  11240   7923   1231   -333    738       C  
ATOM   5754  O   GLU B 355    -106.799  22.424  24.169  1.00 82.81           O  
ANISOU 5754  O   GLU B 355     9321  12868   9275   1201   -371    745       O  
ATOM   5755  CB  GLU B 355    -105.345  22.324  21.459  1.00 57.08           C  
ANISOU 5755  CB  GLU B 355     6113   9537   6038   1149   -335    713       C  
ATOM   5756  CG  GLU B 355    -106.582  21.454  21.304  1.00 71.83           C  
ANISOU 5756  CG  GLU B 355     7833  11680   7780   1071   -380    700       C  
ATOM   5757  CD  GLU B 355    -107.812  22.254  20.923  1.00 70.00           C  
ANISOU 5757  CD  GLU B 355     7507  11707   7381   1233   -360    801       C  
ATOM   5758  OE1 GLU B 355    -107.682  23.201  20.118  1.00 62.40           O  
ANISOU 5758  OE1 GLU B 355     6571  10759   6377   1379   -308    874       O  
ATOM   5759  OE2 GLU B 355    -108.910  21.936  21.427  1.00 66.80           O  
ANISOU 5759  OE2 GLU B 355     7001  11498   6883   1221   -389    811       O  
ATOM   5760  N   ASN B 356    -104.716  23.095  24.695  1.00 66.75           N  
ANISOU 5760  N   ASN B 356     7493  10413   7457   1200   -322    696       N  
ATOM   5761  CA  ASN B 356    -104.765  22.562  26.051  1.00 70.03           C  
ANISOU 5761  CA  ASN B 356     7900  10782   7925   1129   -358    658       C  
ATOM   5762  C   ASN B 356    -104.726  23.663  27.105  1.00 78.22           C  
ANISOU 5762  C   ASN B 356     9005  11723   8991   1245   -316    689       C  
ATOM   5763  O   ASN B 356    -105.662  24.454  27.225  1.00 95.07           O  
ANISOU 5763  O   ASN B 356    11116  13966  11039   1378   -285    759       O  
ATOM   5764  CB  ASN B 356    -103.619  21.574  26.280  1.00 70.72           C  
ANISOU 5764  CB  ASN B 356     8027  10711   8131    976   -385    577       C  
ATOM   5765  CG  ASN B 356    -103.765  20.312  25.454  1.00 73.76           C  
ANISOU 5765  CG  ASN B 356     8348  11185   8493    841   -418    535       C  
ATOM   5766  OD1 ASN B 356    -104.852  19.991  24.975  1.00 80.37           O  
ANISOU 5766  OD1 ASN B 356     9090  12228   9221    830   -435    551       O  
ATOM   5767  ND2 ASN B 356    -102.665  19.587  25.283  1.00 79.72           N  
ANISOU 5767  ND2 ASN B 356     9152  11793   9343    734   -420    478       N  
ATOM   5768  N   GLU B 364     -99.319  24.329  34.128  1.00109.01           N  
ANISOU 5768  N   GLU B 364    13172  14865  13380    971   -270    361       N  
ATOM   5769  CA  GLU B 364     -98.126  24.768  33.414  1.00102.61           C  
ANISOU 5769  CA  GLU B 364    12439  13930  12617    943   -225    320       C  
ATOM   5770  C   GLU B 364     -98.427  25.970  32.525  1.00111.18           C  
ANISOU 5770  C   GLU B 364    13605  14964  13675   1038   -148    346       C  
ATOM   5771  O   GLU B 364     -97.793  26.162  31.487  1.00117.03           O  
ANISOU 5771  O   GLU B 364    14398  15630  14439   1031   -120    340       O  
ATOM   5772  CB  GLU B 364     -97.552  23.625  32.575  1.00 88.20           C  
ANISOU 5772  CB  GLU B 364    10588  12098  10825    865   -272    319       C  
ATOM   5773  CG  GLU B 364     -97.123  22.414  33.387  1.00 78.51           C  
ANISOU 5773  CG  GLU B 364     9297  10903   9631    782   -325    303       C  
ATOM   5774  CD  GLU B 364     -97.801  21.137  32.931  1.00 73.72           C  
ANISOU 5774  CD  GLU B 364     8629  10372   9010    744   -375    341       C  
ATOM   5775  OE1 GLU B 364     -98.660  21.208  32.027  1.00 78.22           O  
ANISOU 5775  OE1 GLU B 364     9191  10994   9533    776   -378    373       O  
ATOM   5776  OE2 GLU B 364     -97.476  20.061  33.477  1.00 65.49           O  
ANISOU 5776  OE2 GLU B 364     7545   9342   7997    683   -402    339       O  
ATOM   5777  N   GLN B 365     -99.398  26.778  32.939  1.00114.00           N  
ANISOU 5777  N   GLN B 365    13974  15360  13981   1137   -108    382       N  
ATOM   5778  CA  GLN B 365     -99.990  27.778  32.059  1.00114.05           C  
ANISOU 5778  CA  GLN B 365    14041  15352  13942   1259    -32    440       C  
ATOM   5779  C   GLN B 365     -99.438  29.169  32.357  1.00121.13           C  
ANISOU 5779  C   GLN B 365    15058  16102  14865   1302     90    402       C  
ATOM   5780  O   GLN B 365    -100.151  30.167  32.247  1.00125.92           O  
ANISOU 5780  O   GLN B 365    15720  16696  15427   1426    176    452       O  
ATOM   5781  CB  GLN B 365    -101.514  27.777  32.195  1.00105.93           C  
ANISOU 5781  CB  GLN B 365    12948  14476  12826   1360    -53    521       C  
ATOM   5782  N   SER B 366     -98.165  29.227  32.733  1.00120.11           N  
ANISOU 5782  N   SER B 366    14969  15866  14801   1197    108    311       N  
ATOM   5783  CA  SER B 366     -97.338  30.396  32.461  1.00116.37           C  
ANISOU 5783  CA  SER B 366    14622  15234  14361   1201    230    262       C  
ATOM   5784  C   SER B 366     -96.241  30.072  31.452  1.00110.07           C  
ANISOU 5784  C   SER B 366    13848  14365  13608   1129    220    234       C  
ATOM   5785  O   SER B 366     -95.446  30.938  31.086  1.00112.76           O  
ANISOU 5785  O   SER B 366    14291  14574  13980   1117    318    190       O  
ATOM   5786  CB  SER B 366     -96.721  30.929  33.756  1.00117.51           C  
ANISOU 5786  CB  SER B 366    14797  15321  14530   1128    281    164       C  
ATOM   5787  OG  SER B 366     -95.917  29.944  34.381  1.00116.63           O  
ANISOU 5787  OG  SER B 366    14602  15264  14449   1001    189    103       O  
ATOM   5788  N   PHE B 367     -96.204  28.821  31.007  1.00 98.98           N  
ANISOU 5788  N   PHE B 367    12355  13045  12208   1078    109    257       N  
ATOM   5789  CA  PHE B 367     -95.274  28.406  29.963  1.00 84.25           C  
ANISOU 5789  CA  PHE B 367    10505  11126  10380   1020     92    241       C  
ATOM   5790  C   PHE B 367     -95.758  28.849  28.586  1.00 83.86           C  
ANISOU 5790  C   PHE B 367    10499  11066  10299   1118    135    314       C  
ATOM   5791  O   PHE B 367     -94.985  29.374  27.785  1.00 84.27           O  
ANISOU 5791  O   PHE B 367    10628  11013  10380   1114    196    297       O  
ATOM   5792  CB  PHE B 367     -95.081  26.889  29.989  1.00 74.24           C  
ANISOU 5792  CB  PHE B 367     9136   9944   9127    933    -25    240       C  
ATOM   5793  CG  PHE B 367     -94.071  26.389  28.996  1.00 63.47           C  
ANISOU 5793  CG  PHE B 367     7788   8525   7804    868    -41    220       C  
ATOM   5794  CD1 PHE B 367     -92.716  26.573  29.213  1.00 73.68           C  
ANISOU 5794  CD1 PHE B 367     9118   9730   9145    789    -14    147       C  
ATOM   5795  CD2 PHE B 367     -94.477  25.736  27.844  1.00 61.79           C  
ANISOU 5795  CD2 PHE B 367     7544   8360   7572    883    -82    270       C  
ATOM   5796  CE1 PHE B 367     -91.785  26.114  28.300  1.00 74.97           C  
ANISOU 5796  CE1 PHE B 367     9294   9847   9343    735    -29    132       C  
ATOM   5797  CE2 PHE B 367     -93.551  25.275  26.928  1.00 74.23           C  
ANISOU 5797  CE2 PHE B 367     9136   9884   9186    824    -94    250       C  
ATOM   5798  CZ  PHE B 367     -92.203  25.464  27.157  1.00 75.68           C  
ANISOU 5798  CZ  PHE B 367     9362   9971   9422    756    -68    185       C  
ATOM   5799  N   LEU B 368     -97.042  28.633  28.318  1.00 82.30           N  
ANISOU 5799  N   LEU B 368    10242  10993  10034   1207    103    396       N  
ATOM   5800  CA  LEU B 368     -97.633  29.017  27.043  1.00 81.27           C  
ANISOU 5800  CA  LEU B 368    10128  10900   9852   1315    140    477       C  
ATOM   5801  C   LEU B 368     -97.448  30.508  26.789  1.00 84.65           C  
ANISOU 5801  C   LEU B 368    10685  11196  10283   1417    286    495       C  
ATOM   5802  O   LEU B 368     -97.393  30.948  25.637  1.00 86.46           O  
ANISOU 5802  O   LEU B 368    10958  11398  10494   1488    341    545       O  
ATOM   5803  CB  LEU B 368     -99.113  28.636  26.973  1.00 79.13           C  
ANISOU 5803  CB  LEU B 368     9760  10816   9489   1397     91    560       C  
ATOM   5804  CG  LEU B 368     -99.846  29.004  25.675  1.00 85.95           C  
ANISOU 5804  CG  LEU B 368    10614  11771  10273   1521    126    655       C  
ATOM   5805  CD1 LEU B 368     -99.191  28.388  24.439  1.00 76.68           C  
ANISOU 5805  CD1 LEU B 368     9424  10593   9116   1454     89    641       C  
ATOM   5806  CD2 LEU B 368    -101.322  28.610  25.758  1.00 94.07           C  
ANISOU 5806  CD2 LEU B 368    11528  13018  11196   1589     74    727       C  
ATOM   5807  N   THR B 369     -97.333  31.281  27.865  1.00 86.16           N  
ANISOU 5807  N   THR B 369    10940  11303  10495   1421    358    452       N  
ATOM   5808  CA  THR B 369     -97.121  32.721  27.736  1.00 92.01           C  
ANISOU 5808  CA  THR B 369    11822  11893  11245   1505    522    455       C  
ATOM   5809  C   THR B 369     -95.736  33.034  27.170  1.00 92.43           C  
ANISOU 5809  C   THR B 369    11963  11791  11367   1418    578    384       C  
ATOM   5810  O   THR B 369     -95.611  33.778  26.193  1.00 93.21           O  
ANISOU 5810  O   THR B 369    12147  11806  11461   1499    678    429       O  
ATOM   5811  CB  THR B 369     -97.306  33.452  29.075  1.00 94.79           C  
ANISOU 5811  CB  THR B 369    12225  12189  11604   1510    596    408       C  
ATOM   5812  OG1 THR B 369     -96.275  33.051  29.985  1.00103.59           O  
ANISOU 5812  OG1 THR B 369    13321  13261  12777   1343    552    285       O  
ATOM   5813  CG2 THR B 369     -98.669  33.129  29.678  1.00 90.88           C  
ANISOU 5813  CG2 THR B 369    11638  11852  11039   1595    537    479       C  
ATOM   5814  N   TYR B 370     -94.698  32.467  27.781  1.00 87.94           N  
ANISOU 5814  N   TYR B 370    11366  11192  10853   1259    518    278       N  
ATOM   5815  CA  TYR B 370     -93.341  32.650  27.279  1.00 91.73           C  
ANISOU 5815  CA  TYR B 370    11912  11552  11391   1162    558    205       C  
ATOM   5816  C   TYR B 370     -93.161  31.938  25.940  1.00 92.00           C  
ANISOU 5816  C   TYR B 370    11905  11626  11424   1168    489    257       C  
ATOM   5817  O   TYR B 370     -92.581  32.486  25.003  1.00 94.40           O  
ANISOU 5817  O   TYR B 370    12289  11831  11748   1184    563    261       O  
ATOM   5818  CB  TYR B 370     -92.305  32.149  28.289  1.00 98.24           C  
ANISOU 5818  CB  TYR B 370    12695  12376  12257   1000    505     89       C  
ATOM   5819  CG  TYR B 370     -90.871  32.356  27.839  1.00102.14           C  
ANISOU 5819  CG  TYR B 370    13245  12764  12799    893    547      8       C  
ATOM   5820  CD1 TYR B 370     -90.208  33.555  28.088  1.00105.81           C  
ANISOU 5820  CD1 TYR B 370    13828  13089  13284    854    693    -72       C  
ATOM   5821  CD2 TYR B 370     -90.182  31.357  27.163  1.00100.47           C  
ANISOU 5821  CD2 TYR B 370    12972  12593  12610    828    449      7       C  
ATOM   5822  CE1 TYR B 370     -88.897  33.752  27.676  1.00106.93           C  
ANISOU 5822  CE1 TYR B 370    14017  13148  13463    748    734   -152       C  
ATOM   5823  CE2 TYR B 370     -88.867  31.545  26.747  1.00103.74           C  
ANISOU 5823  CE2 TYR B 370    13432  12922  13061    734    486    -64       C  
ATOM   5824  CZ  TYR B 370     -88.233  32.744  27.006  1.00104.74           C  
ANISOU 5824  CZ  TYR B 370    13668  12924  13203    693    625   -144       C  
ATOM   5825  OH  TYR B 370     -86.933  32.938  26.599  1.00102.35           O  
ANISOU 5825  OH  TYR B 370    13407  12551  12931    590    664   -220       O  
ATOM   5826  N   PHE B 371     -93.670  30.714  25.854  1.00 84.37           N  
ANISOU 5826  N   PHE B 371    10818  10805  10435   1150    354    293       N  
ATOM   5827  CA  PHE B 371     -93.581  29.934  24.630  1.00 76.08           C  
ANISOU 5827  CA  PHE B 371     9720   9810   9378   1143    287    332       C  
ATOM   5828  C   PHE B 371     -94.148  30.683  23.420  1.00 76.85           C  
ANISOU 5828  C   PHE B 371     9867   9905   9429   1281    364    423       C  
ATOM   5829  O   PHE B 371     -93.596  30.604  22.327  1.00 77.59           O  
ANISOU 5829  O   PHE B 371     9979   9965   9535   1271    369    431       O  
ATOM   5830  CB  PHE B 371     -94.273  28.582  24.811  1.00 78.08           C  
ANISOU 5830  CB  PHE B 371     9842  10223   9602   1107    155    356       C  
ATOM   5831  CG  PHE B 371     -93.985  27.605  23.715  1.00 76.58           C  
ANISOU 5831  CG  PHE B 371     9603  10080   9416   1056     85    366       C  
ATOM   5832  CD1 PHE B 371     -92.723  27.521  23.164  1.00 84.42           C  
ANISOU 5832  CD1 PHE B 371    10640  10970  10465    982     96    316       C  
ATOM   5833  CD2 PHE B 371     -94.968  26.758  23.251  1.00 77.79           C  
ANISOU 5833  CD2 PHE B 371     9661  10384   9511   1072     14    417       C  
ATOM   5834  CE1 PHE B 371     -92.453  26.623  22.160  1.00 80.98           C  
ANISOU 5834  CE1 PHE B 371    10163  10573  10034    935     38    322       C  
ATOM   5835  CE2 PHE B 371     -94.706  25.860  22.244  1.00 79.82           C  
ANISOU 5835  CE2 PHE B 371     9876  10682   9770   1013    -39    414       C  
ATOM   5836  CZ  PHE B 371     -93.448  25.791  21.699  1.00 79.47           C  
ANISOU 5836  CZ  PHE B 371     9884  10525   9787    948    -27    369       C  
ATOM   5837  N   LYS B 372     -95.245  31.409  23.611  1.00 83.81           N  
ANISOU 5837  N   LYS B 372    10764  10830  10251   1417    427    497       N  
ATOM   5838  CA  LYS B 372     -95.771  32.254  22.546  1.00 87.19           C  
ANISOU 5838  CA  LYS B 372    11244  11258  10627   1574    524    597       C  
ATOM   5839  C   LYS B 372     -94.729  33.293  22.178  1.00 91.68           C  
ANISOU 5839  C   LYS B 372    11958  11623  11253   1572    659    562       C  
ATOM   5840  O   LYS B 372     -94.431  33.504  21.001  1.00 91.60           O  
ANISOU 5840  O   LYS B 372    11980  11586  11238   1616    697    604       O  
ATOM   5841  CB  LYS B 372     -97.044  32.964  22.991  1.00 91.46           C  
ANISOU 5841  CB  LYS B 372    11790  11867  11095   1731    591    683       C  
ATOM   5842  CG  LYS B 372     -98.328  32.229  22.665  1.00 92.20           C  
ANISOU 5842  CG  LYS B 372    11744  12199  11090   1801    495    770       C  
ATOM   5843  CD  LYS B 372     -99.497  33.205  22.611  1.00 90.67           C  
ANISOU 5843  CD  LYS B 372    11573  12071  10806   2008    599    889       C  
ATOM   5844  CE  LYS B 372    -100.796  32.490  22.291  1.00 95.28           C  
ANISOU 5844  CE  LYS B 372    12003  12925  11274   2072    505    972       C  
ATOM   5845  NZ  LYS B 372    -101.259  31.657  23.446  1.00100.26           N  
ANISOU 5845  NZ  LYS B 372    12543  13644  11905   1976    396    919       N  
ATOM   5846  N   ALA B 373     -94.172  33.946  23.192  1.00 96.58           N  
ANISOU 5846  N   ALA B 373    12665  12106  11925   1513    737    479       N  
ATOM   5847  CA  ALA B 373     -93.127  34.941  22.982  1.00102.48           C  
ANISOU 5847  CA  ALA B 373    13555  12653  12729   1481    878    422       C  
ATOM   5848  C   ALA B 373     -91.957  34.355  22.200  1.00105.48           C  
ANISOU 5848  C   ALA B 373    13921  13000  13156   1363    818    368       C  
ATOM   5849  O   ALA B 373     -91.252  35.071  21.489  1.00107.38           O  
ANISOU 5849  O   ALA B 373    14264  13109  13425   1370    924    359       O  
ATOM   5850  CB  ALA B 373     -92.651  35.500  24.314  1.00 97.46           C  
ANISOU 5850  CB  ALA B 373    12986  11911  12135   1388    948    311       C  
ATOM   5851  N   TYR B 374     -91.756  33.048  22.336  1.00105.46           N  
ANISOU 5851  N   TYR B 374    13796  13113  13162   1260    656    335       N  
ATOM   5852  CA  TYR B 374     -90.740  32.344  21.562  1.00104.96           C  
ANISOU 5852  CA  TYR B 374    13706  13037  13135   1160    589    296       C  
ATOM   5853  C   TYR B 374     -91.339  31.153  20.821  1.00109.47           C  
ANISOU 5853  C   TYR B 374    14157  13769  13668   1176    458    358       C  
ATOM   5854  O   TYR B 374     -91.690  31.254  19.645  1.00109.69           O  
ANISOU 5854  O   TYR B 374    14183  13836  13660   1262    474    433       O  
ATOM   5855  CB  TYR B 374     -89.601  31.879  22.470  1.00101.41           C  
ANISOU 5855  CB  TYR B 374    13238  12551  12742    993    542    175       C  
ATOM   5856  CG  TYR B 374     -88.751  30.780  21.873  1.00104.49           C  
ANISOU 5856  CG  TYR B 374    13564  12979  13160    895    437    148       C  
ATOM   5857  CD1 TYR B 374     -87.383  30.729  22.106  1.00108.16           C  
ANISOU 5857  CD1 TYR B 374    14050  13375  13672    770    444     53       C  
ATOM   5858  CD2 TYR B 374     -89.317  29.793  21.076  1.00100.56           C  
ANISOU 5858  CD2 TYR B 374    12980  12593  12634    926    340    213       C  
ATOM   5859  CE1 TYR B 374     -86.602  29.727  21.562  1.00104.48           C  
ANISOU 5859  CE1 TYR B 374    13527  12942  13227    694    357     37       C  
ATOM   5860  CE2 TYR B 374     -88.544  28.787  20.528  1.00 96.36           C  
ANISOU 5860  CE2 TYR B 374    12399  12083  12130    838    259    187       C  
ATOM   5861  CZ  TYR B 374     -87.188  28.758  20.774  1.00 97.59           C  
ANISOU 5861  CZ  TYR B 374    12583  12160  12336    731    268    104       C  
ATOM   5862  OH  TYR B 374     -86.415  27.758  20.231  1.00 95.14           O  
ANISOU 5862  OH  TYR B 374    12227  11871  12051    657    195     86       O  
ATOM   5863  N   ASP B 405     -92.873  15.401  33.337  1.00 91.89           N  
ANISOU 5863  N   ASP B 405    10885  12470  11559    455   -357    348       N  
ATOM   5864  CA  ASP B 405     -92.744  14.359  32.325  1.00 83.35           C  
ANISOU 5864  CA  ASP B 405     9835  11327  10507    406   -332    359       C  
ATOM   5865  C   ASP B 405     -91.510  14.583  31.457  1.00 71.51           C  
ANISOU 5865  C   ASP B 405     8383   9750   9038    397   -315    334       C  
ATOM   5866  O   ASP B 405     -91.365  15.630  30.826  1.00 81.04           O  
ANISOU 5866  O   ASP B 405     9621  10936  10233    408   -326    298       O  
ATOM   5867  CB  ASP B 405     -93.998  14.303  31.451  1.00 87.37           C  
ANISOU 5867  CB  ASP B 405    10349  11859  10986    376   -344    349       C  
ATOM   5868  CG  ASP B 405     -93.686  13.971  30.005  1.00 92.05           C  
ANISOU 5868  CG  ASP B 405    10990  12390  11597    329   -325    327       C  
ATOM   5869  OD1 ASP B 405     -92.593  13.428  29.740  1.00 91.80           O  
ANISOU 5869  OD1 ASP B 405    10988  12282  11609    312   -295    329       O  
ATOM   5870  OD2 ASP B 405     -94.534  14.253  29.132  1.00 91.91           O  
ANISOU 5870  OD2 ASP B 405    10971  12410  11540    313   -338    311       O  
ATOM   5871  N   PRO B 406     -90.624  13.594  31.430  1.00 51.24           N  
ANISOU 5871  N   PRO B 406     5824   7139   6506    383   -279    358       N  
ATOM   5872  CA  PRO B 406     -89.258  13.795  30.936  1.00 59.77           C  
ANISOU 5872  CA  PRO B 406     6933   8168   7609    385   -264    343       C  
ATOM   5873  C   PRO B 406     -89.226  14.708  29.715  1.00 65.76           C  
ANISOU 5873  C   PRO B 406     7741   8879   8364    369   -279    295       C  
ATOM   5874  O   PRO B 406     -88.236  15.404  29.491  1.00 61.81           O  
ANISOU 5874  O   PRO B 406     7261   8355   7869    376   -276    266       O  
ATOM   5875  CB  PRO B 406     -88.820  12.382  30.547  1.00 51.61           C  
ANISOU 5875  CB  PRO B 406     5922   7074   6613    364   -212    381       C  
ATOM   5876  CG  PRO B 406     -90.086  11.684  30.203  1.00 49.79           C  
ANISOU 5876  CG  PRO B 406     5701   6836   6381    318   -202    385       C  
ATOM   5877  CD  PRO B 406     -91.129  12.243  31.128  1.00 47.55           C  
ANISOU 5877  CD  PRO B 406     5367   6640   6058    340   -242    387       C  
ATOM   5878  N   TYR B 407     -90.304  14.701  28.937  1.00 64.15           N  
ANISOU 5878  N   TYR B 407     7552   8676   8145    347   -290    287       N  
ATOM   5879  CA  TYR B 407     -90.380  15.512  27.728  1.00 56.84           C  
ANISOU 5879  CA  TYR B 407     6667   7722   7209    345   -298    255       C  
ATOM   5880  C   TYR B 407     -90.767  16.951  28.052  1.00 58.08           C  
ANISOU 5880  C   TYR B 407     6825   7910   7331    396   -314    239       C  
ATOM   5881  O   TYR B 407     -90.397  17.880  27.333  1.00 52.56           O  
ANISOU 5881  O   TYR B 407     6170   7171   6630    412   -304    215       O  
ATOM   5882  CB  TYR B 407     -91.382  14.908  26.741  1.00 49.83           C  
ANISOU 5882  CB  TYR B 407     5780   6852   6302    302   -298    255       C  
ATOM   5883  CG  TYR B 407     -90.826  13.759  25.930  1.00 54.82           C  
ANISOU 5883  CG  TYR B 407     6441   7419   6971    242   -263    251       C  
ATOM   5884  CD1 TYR B 407     -91.140  12.444  26.247  1.00 64.37           C  
ANISOU 5884  CD1 TYR B 407     7640   8622   8196    195   -229    267       C  
ATOM   5885  CD2 TYR B 407     -89.987  13.989  24.848  1.00 52.63           C  
ANISOU 5885  CD2 TYR B 407     6206   7078   6711    232   -253    229       C  
ATOM   5886  CE1 TYR B 407     -90.635  11.391  25.509  1.00 60.41           C  
ANISOU 5886  CE1 TYR B 407     7177   8046   7730    139   -179    261       C  
ATOM   5887  CE2 TYR B 407     -89.476  12.943  24.104  1.00 50.92           C  
ANISOU 5887  CE2 TYR B 407     6021   6800   6528    179   -216    222       C  
ATOM   5888  CZ  TYR B 407     -89.803  11.646  24.439  1.00 55.43           C  
ANISOU 5888  CZ  TYR B 407     6587   7357   7115    132   -175    237       C  
ATOM   5889  OH  TYR B 407     -89.298  10.600  23.701  1.00 67.27           O  
ANISOU 5889  OH  TYR B 407     8129   8780   8650     79   -119    229       O  
ATOM   5890  N   ARG B 408     -91.513  17.128  29.137  1.00 47.74           N  
ANISOU 5890  N   ARG B 408     5475   6668   5996    422   -329    253       N  
ATOM   5891  CA  ARG B 408     -91.881  18.461  29.606  1.00 54.33           C  
ANISOU 5891  CA  ARG B 408     6317   7527   6800    474   -330    238       C  
ATOM   5892  C   ARG B 408     -90.644  19.175  30.121  1.00 56.13           C  
ANISOU 5892  C   ARG B 408     6566   7717   7047    474   -308    199       C  
ATOM   5893  O   ARG B 408     -90.505  20.402  30.016  1.00 49.90           O  
ANISOU 5893  O   ARG B 408     5819   6897   6246    498   -282    167       O  
ATOM   5894  CB  ARG B 408     -92.935  18.411  30.709  1.00 66.70           C  
ANISOU 5894  CB  ARG B 408     7831   9178   8333    500   -350    261       C  
ATOM   5895  CG  ARG B 408     -93.411  19.798  31.113  1.00 72.89           C  
ANISOU 5895  CG  ARG B 408     8633   9980   9084    559   -339    247       C  
ATOM   5896  CD  ARG B 408     -94.246  19.758  32.368  1.00 85.80           C  
ANISOU 5896  CD  ARG B 408    10213  11698  10690    584   -358    265       C  
ATOM   5897  NE  ARG B 408     -93.444  19.475  33.555  1.00 86.94           N  
ANISOU 5897  NE  ARG B 408    10322  11857  10853    563   -359    250       N  
ATOM   5898  CZ  ARG B 408     -93.959  19.239  34.757  1.00 80.56           C  
ANISOU 5898  CZ  ARG B 408     9457  11126  10026    577   -377    268       C  
ATOM   5899  NH1 ARG B 408     -95.278  19.248  34.925  1.00 73.74           N  
ANISOU 5899  NH1 ARG B 408     8569  10322   9126    607   -396    297       N  
ATOM   5900  NH2 ARG B 408     -93.157  18.992  35.785  1.00 77.05           N  
ANISOU 5900  NH2 ARG B 408     8973  10714   9589    563   -374    258       N  
ATOM   5901  N   LEU B 409     -89.741  18.385  30.682  1.00 60.32           N  
ANISOU 5901  N   LEU B 409     7064   8255   7599    446   -308    204       N  
ATOM   5902  CA  LEU B 409     -88.468  18.897  31.131  1.00 56.57           C  
ANISOU 5902  CA  LEU B 409     6590   7774   7129    433   -288    164       C  
ATOM   5903  C   LEU B 409     -87.634  19.340  29.931  1.00 57.92           C  
ANISOU 5903  C   LEU B 409     6824   7863   7321    412   -265    133       C  
ATOM   5904  O   LEU B 409     -87.037  20.421  29.948  1.00 60.96           O  
ANISOU 5904  O   LEU B 409     7241   8223   7699    403   -237     81       O  
ATOM   5905  CB  LEU B 409     -87.736  17.834  31.944  1.00 55.03           C  
ANISOU 5905  CB  LEU B 409     6335   7634   6942    425   -290    194       C  
ATOM   5906  CG  LEU B 409     -86.573  18.328  32.809  1.00 63.12           C  
ANISOU 5906  CG  LEU B 409     7321   8718   7943    414   -275    156       C  
ATOM   5907  CD1 LEU B 409     -86.845  19.726  33.356  1.00 63.78           C  
ANISOU 5907  CD1 LEU B 409     7417   8821   7997    409   -263     92       C  
ATOM   5908  CD2 LEU B 409     -86.307  17.339  33.933  1.00 57.75           C  
ANISOU 5908  CD2 LEU B 409     6559   8136   7249    435   -279    206       C  
ATOM   5909  N   ALA B 410     -87.600  18.526  28.879  1.00 51.25           N  
ANISOU 5909  N   ALA B 410     5999   6973   6501    397   -271    159       N  
ATOM   5910  CA  ALA B 410     -86.768  18.881  27.734  1.00 53.65           C  
ANISOU 5910  CA  ALA B 410     6358   7203   6824    378   -251    132       C  
ATOM   5911  C   ALA B 410     -87.233  20.203  27.157  1.00 55.76           C  
ANISOU 5911  C   ALA B 410     6679   7431   7075    403   -232    106       C  
ATOM   5912  O   ALA B 410     -86.405  21.050  26.796  1.00 55.75           O  
ANISOU 5912  O   ALA B 410     6724   7377   7080    392   -199     65       O  
ATOM   5913  CB  ALA B 410     -86.781  17.793  26.673  1.00 52.56           C  
ANISOU 5913  CB  ALA B 410     6232   7026   6711    357   -257    161       C  
ATOM   5914  N   VAL B 411     -88.556  20.388  27.096  1.00 47.06           N  
ANISOU 5914  N   VAL B 411     5574   6361   5948    442   -243    134       N  
ATOM   5915  CA  VAL B 411     -89.131  21.540  26.391  1.00 36.57           C  
ANISOU 5915  CA  VAL B 411     4298   5001   4596    490   -214    132       C  
ATOM   5916  C   VAL B 411     -88.936  22.840  27.161  1.00 47.21           C  
ANISOU 5916  C   VAL B 411     5680   6323   5932    512   -167     94       C  
ATOM   5917  O   VAL B 411     -88.626  23.880  26.578  1.00 60.05           O  
ANISOU 5917  O   VAL B 411     7377   7878   7560    530   -113     72       O  
ATOM   5918  CB  VAL B 411     -90.620  21.347  26.065  1.00 39.54           C  
ANISOU 5918  CB  VAL B 411     4647   5444   4931    533   -237    180       C  
ATOM   5919  CG1 VAL B 411     -91.192  22.619  25.476  1.00 52.70           C  
ANISOU 5919  CG1 VAL B 411     6364   7095   6564    608   -194    194       C  
ATOM   5920  CG2 VAL B 411     -90.816  20.200  25.096  1.00 39.58           C  
ANISOU 5920  CG2 VAL B 411     4628   5470   4940    494   -265    200       C  
ATOM   5921  N   TYR B 412     -89.128  22.779  28.473  1.00 54.62           N  
ANISOU 5921  N   TYR B 412     6575   7320   6860    507   -179     84       N  
ATOM   5922  CA  TYR B 412     -88.892  23.926  29.333  1.00 57.00           C  
ANISOU 5922  CA  TYR B 412     6904   7606   7148    509   -128     33       C  
ATOM   5923  C   TYR B 412     -87.429  24.279  29.188  1.00 57.02           C  
ANISOU 5923  C   TYR B 412     6936   7556   7171    445    -91    -31       C  
ATOM   5924  O   TYR B 412     -87.073  25.433  28.932  1.00 58.87           O  
ANISOU 5924  O   TYR B 412     7245   7716   7406    440    -20    -78       O  
ATOM   5925  CB  TYR B 412     -89.201  23.577  30.797  1.00 58.67           C  
ANISOU 5925  CB  TYR B 412     7043   7908   7340    502   -156     30       C  
ATOM   5926  CG  TYR B 412     -90.588  23.958  31.265  1.00 76.12           C  
ANISOU 5926  CG  TYR B 412     9246  10158   9518    567   -158     63       C  
ATOM   5927  CD1 TYR B 412     -91.673  23.120  31.045  1.00 83.72           C  
ANISOU 5927  CD1 TYR B 412    10164  11181  10466    600   -210    128       C  
ATOM   5928  CD2 TYR B 412     -90.810  25.155  31.937  1.00 81.56           C  
ANISOU 5928  CD2 TYR B 412     9974  10829  10186    590    -99     24       C  
ATOM   5929  CE1 TYR B 412     -92.939  23.467  31.473  1.00 86.10           C  
ANISOU 5929  CE1 TYR B 412    10450  11537  10729    661   -213    161       C  
ATOM   5930  CE2 TYR B 412     -92.071  25.510  32.366  1.00 83.89           C  
ANISOU 5930  CE2 TYR B 412    10263  11164  10448    659    -96     60       C  
ATOM   5931  CZ  TYR B 412     -93.133  24.663  32.132  1.00 85.86           C  
ANISOU 5931  CZ  TYR B 412    10458  11486  10678    698   -158    132       C  
ATOM   5932  OH  TYR B 412     -94.393  25.013  32.560  1.00 82.55           O  
ANISOU 5932  OH  TYR B 412    10024  11124  10217    769   -157    170       O  
ATOM   5933  N   LYS B 413     -86.587  23.263  29.349  1.00 48.85           N  
ANISOU 5933  N   LYS B 413     5846   6564   6151    399   -131    -30       N  
ATOM   5934  CA  LYS B 413     -85.145  23.423  29.228  1.00 51.99           C  
ANISOU 5934  CA  LYS B 413     6251   6945   6557    337   -105    -85       C  
ATOM   5935  C   LYS B 413     -84.751  24.118  27.929  1.00 57.30           C  
ANISOU 5935  C   LYS B 413     7011   7509   7250    333    -61   -104       C  
ATOM   5936  O   LYS B 413     -83.998  25.087  27.950  1.00 63.47           O  
ANISOU 5936  O   LYS B 413     7839   8247   8028    291      0   -172       O  
ATOM   5937  CB  LYS B 413     -84.458  22.066  29.314  1.00 54.80           C  
ANISOU 5937  CB  LYS B 413     6538   7360   6924    317   -153    -50       C  
ATOM   5938  CG  LYS B 413     -83.017  22.142  29.737  1.00 54.89           C  
ANISOU 5938  CG  LYS B 413     6516   7420   6919    261   -133   -102       C  
ATOM   5939  CD  LYS B 413     -82.502  20.766  30.110  1.00 58.17           C  
ANISOU 5939  CD  LYS B 413     6852   7917   7333    270   -171    -47       C  
ATOM   5940  CE  LYS B 413     -81.513  20.836  31.263  1.00 58.84           C  
ANISOU 5940  CE  LYS B 413     6854   8133   7369    237   -160    -84       C  
ATOM   5941  NZ  LYS B 413     -80.285  21.609  30.929  1.00 60.23           N  
ANISOU 5941  NZ  LYS B 413     7048   8311   7526    172   -121   -162       N  
ATOM   5942  N   LEU B 414     -85.258  23.623  26.800  1.00 54.60           N  
ANISOU 5942  N   LEU B 414     6690   7130   6926    370    -87    -48       N  
ATOM   5943  CA  LEU B 414     -84.929  24.217  25.505  1.00 57.98           C  
ANISOU 5943  CA  LEU B 414     7194   7465   7369    376    -48    -54       C  
ATOM   5944  C   LEU B 414     -85.444  25.646  25.394  1.00 62.31           C  
ANISOU 5944  C   LEU B 414     7822   7947   7904    419     29    -71       C  
ATOM   5945  O   LEU B 414     -84.656  26.578  25.237  1.00 64.25           O  
ANISOU 5945  O   LEU B 414     8132   8120   8158    386    101   -127       O  
ATOM   5946  CB  LEU B 414     -85.466  23.359  24.365  1.00 55.57           C  
ANISOU 5946  CB  LEU B 414     6881   7158   7073    406    -91      7       C  
ATOM   5947  CG  LEU B 414     -84.937  21.926  24.423  1.00 59.12           C  
ANISOU 5947  CG  LEU B 414     7271   7650   7543    364   -143     24       C  
ATOM   5948  CD1 LEU B 414     -85.566  21.076  23.345  1.00 62.73           C  
ANISOU 5948  CD1 LEU B 414     7724   8107   8005    377   -173     70       C  
ATOM   5949  CD2 LEU B 414     -83.400  21.880  24.349  1.00 58.35           C  
ANISOU 5949  CD2 LEU B 414     7178   7529   7463    311   -127    -18       C  
ATOM   5950  N   ILE B 415     -86.761  25.816  25.484  1.00 60.03           N  
ANISOU 5950  N   ILE B 415     7532   7684   7592    494     25    -20       N  
ATOM   5951  CA  ILE B 415     -87.372  27.139  25.371  1.00 63.40           C  
ANISOU 5951  CA  ILE B 415     8039   8048   8002    561    111    -16       C  
ATOM   5952  C   ILE B 415     -86.772  28.124  26.377  1.00 63.74           C  
ANISOU 5952  C   ILE B 415     8125   8046   8046    512    188    -99       C  
ATOM   5953  O   ILE B 415     -86.390  29.238  26.019  1.00 68.44           O  
ANISOU 5953  O   ILE B 415     8816   8538   8649    512    290   -136       O  
ATOM   5954  CB  ILE B 415     -88.917  27.083  25.552  1.00 59.95           C  
ANISOU 5954  CB  ILE B 415     7572   7679   7526    653     88     56       C  
ATOM   5955  CG1 ILE B 415     -89.610  26.651  24.259  1.00 57.57           C  
ANISOU 5955  CG1 ILE B 415     7258   7411   7205    713     57    130       C  
ATOM   5956  CG2 ILE B 415     -89.456  28.430  25.989  1.00 62.34           C  
ANISOU 5956  CG2 ILE B 415     7949   7929   7808    719    186     51       C  
ATOM   5957  CD1 ILE B 415     -89.455  25.185  23.941  1.00 62.90           C  
ANISOU 5957  CD1 ILE B 415     7854   8153   7892    654    -36    141       C  
ATOM   5958  N   GLY B 416     -86.682  27.704  27.633  1.00 61.12           N  
ANISOU 5958  N   GLY B 416     7722   7796   7703    465    149   -133       N  
ATOM   5959  CA  GLY B 416     -86.156  28.563  28.680  1.00 74.84           C  
ANISOU 5959  CA  GLY B 416     9484   9523   9430    404    220   -223       C  
ATOM   5960  C   GLY B 416     -84.640  28.612  28.847  1.00 80.95           C  
ANISOU 5960  C   GLY B 416    10248  10301  10210    289    240   -313       C  
ATOM   5961  O   GLY B 416     -84.123  29.555  29.445  1.00 87.61           O  
ANISOU 5961  O   GLY B 416    11131  11116  11039    224    326   -405       O  
ATOM   5962  N   ARG B 417     -83.927  27.611  28.330  1.00 71.48           N  
ANISOU 5962  N   ARG B 417     8994   9140   9024    261    170   -291       N  
ATOM   5963  CA  ARG B 417     -82.490  27.477  28.585  1.00 78.33           C  
ANISOU 5963  CA  ARG B 417     9825  10053   9884    160    175   -364       C  
ATOM   5964  C   ARG B 417     -82.183  27.446  30.087  1.00 78.50           C  
ANISOU 5964  C   ARG B 417     9764  10201   9863    101    170   -424       C  
ATOM   5965  O   ARG B 417     -81.259  28.110  30.553  1.00 78.16           O  
ANISOU 5965  O   ARG B 417     9721  10183   9792      7    231   -525       O  
ATOM   5966  CB  ARG B 417     -81.718  28.620  27.926  1.00 84.40           C  
ANISOU 5966  CB  ARG B 417    10695  10711  10662    105    279   -438       C  
ATOM   5967  CG  ARG B 417     -82.036  28.836  26.460  1.00 87.82           C  
ANISOU 5967  CG  ARG B 417    11215  11023  11131    172    300   -379       C  
ATOM   5968  CD  ARG B 417     -81.372  30.099  25.954  1.00 93.18           C  
ANISOU 5968  CD  ARG B 417    12006  11580  11819    123    424   -451       C  
ATOM   5969  NE  ARG B 417     -79.927  29.940  25.787  1.00102.03           N  
ANISOU 5969  NE  ARG B 417    13102  12731  12936     16    425   -521       N  
ATOM   5970  CZ  ARG B 417     -79.016  30.259  26.705  1.00104.95           C  
ANISOU 5970  CZ  ARG B 417    13434  13171  13271    -99    461   -628       C  
ATOM   5971  NH1 ARG B 417     -79.387  30.758  27.879  1.00100.89           N  
ANISOU 5971  NH1 ARG B 417    12907  12698  12726   -129    502   -684       N  
ATOM   5972  NH2 ARG B 417     -77.726  30.077  26.447  1.00109.37           N  
ANISOU 5972  NH2 ARG B 417    13963  13777  13818   -188    459   -682       N  
ATOM   5973  N   CYS B 418     -82.943  26.647  30.828  1.00 84.44           N  
ANISOU 5973  N   CYS B 418    10438  11042  10604    150    100   -366       N  
ATOM   5974  CA  CYS B 418     -83.032  26.781  32.285  1.00 91.83           C  
ANISOU 5974  CA  CYS B 418    11305  12091  11497    120    102   -411       C  
ATOM   5975  C   CYS B 418     -81.884  26.183  33.104  1.00 95.01           C  
ANISOU 5975  C   CYS B 418    11592  12651  11855     51     73   -448       C  
ATOM   5976  O   CYS B 418     -81.275  26.872  33.925  1.00 97.09           O  
ANISOU 5976  O   CYS B 418    11830  12988  12072    -32    124   -547       O  
ATOM   5977  CB  CYS B 418     -84.366  26.217  32.775  1.00 93.30           C  
ANISOU 5977  CB  CYS B 418    11454  12314  11684    205     45   -329       C  
ATOM   5978  SG  CYS B 418     -85.797  26.996  32.003  1.00 94.45           S  
ANISOU 5978  SG  CYS B 418    11709  12324  11853    298     84   -281       S  
ATOM   5979  N   ASP B 419     -81.601  24.902  32.908  1.00 93.74           N  
ANISOU 5979  N   ASP B 419    11362  12554  11703     86     -1   -369       N  
ATOM   5980  CA  ASP B 419     -80.559  24.258  33.696  1.00 92.57           C  
ANISOU 5980  CA  ASP B 419    11096  12574  11504     48    -24   -381       C  
ATOM   5981  C   ASP B 419     -79.252  24.118  32.904  1.00 85.59           C  
ANISOU 5981  C   ASP B 419    10213  11691  10617      2    -12   -403       C  
ATOM   5982  O   ASP B 419     -78.805  23.011  32.596  1.00 75.16           O  
ANISOU 5982  O   ASP B 419     8843  10412   9303     42    -55   -328       O  
ATOM   5983  CB  ASP B 419     -81.041  22.908  34.237  1.00 91.36           C  
ANISOU 5983  CB  ASP B 419    10855  12506  11350    126    -94   -273       C  
ATOM   5984  CG  ASP B 419     -80.272  22.472  35.461  1.00 89.82           C  
ANISOU 5984  CG  ASP B 419    10528  12516  11084    108   -105   -281       C  
ATOM   5985  OD1 ASP B 419     -79.878  23.350  36.253  1.00 90.58           O  
ANISOU 5985  OD1 ASP B 419    10589  12703  11123     35    -66   -379       O  
ATOM   5986  OD2 ASP B 419     -80.049  21.257  35.631  1.00 92.34           O  
ANISOU 5986  OD2 ASP B 419    10777  12910  11399    167   -142   -189       O  
ATOM   5987  N   LEU B 420     -78.641  25.257  32.594  1.00 91.03           N  
ANISOU 5987  N   LEU B 420    10962  12330  11295    -84     59   -507       N  
ATOM   5988  CA  LEU B 420     -77.469  25.297  31.719  1.00 94.46           C  
ANISOU 5988  CA  LEU B 420    11414  12747  11729   -134     79   -537       C  
ATOM   5989  C   LEU B 420     -76.331  24.389  32.184  1.00 94.32           C  
ANISOU 5989  C   LEU B 420    11267  12918  11654   -147     42   -517       C  
ATOM   5990  O   LEU B 420     -75.627  23.800  31.362  1.00 92.99           O  
ANISOU 5990  O   LEU B 420    11097  12736  11499   -132     24   -476       O  
ATOM   5991  CB  LEU B 420     -76.965  26.734  31.548  1.00 94.70           C  
ANISOU 5991  CB  LEU B 420    11523  12713  11745   -242    177   -668       C  
ATOM   5992  N   SER B 421     -76.150  24.275  33.495  1.00 94.58           N  
ANISOU 5992  N   SER B 421    11186  13136  11614   -167     35   -541       N  
ATOM   5993  CA  SER B 421     -75.097  23.422  34.037  1.00 93.62           C  
ANISOU 5993  CA  SER B 421    10925  13225  11420   -161      8   -509       C  
ATOM   5994  C   SER B 421     -75.321  21.965  33.643  1.00 94.58           C  
ANISOU 5994  C   SER B 421    11026  13326  11584    -37    -51   -358       C  
ATOM   5995  O   SER B 421     -74.382  21.164  33.624  1.00 92.15           O  
ANISOU 5995  O   SER B 421    10640  13136  11238     -7    -62   -306       O  
ATOM   5996  CB  SER B 421     -75.022  23.556  35.560  1.00 90.19           C  
ANISOU 5996  CB  SER B 421    10366  13008  10895   -191     11   -552       C  
ATOM   5997  OG  SER B 421     -74.524  24.828  35.933  1.00 88.16           O  
ANISOU 5997  OG  SER B 421    10113  12802  10582   -330     80   -709       O  
ATOM   5998  N   ARG B 422     -76.570  21.634  33.322  1.00 94.87           N  
ANISOU 5998  N   ARG B 422    11136  13215  11695     33    -77   -290       N  
ATOM   5999  CA  ARG B 422     -76.943  20.269  32.964  1.00 97.90           C  
ANISOU 5999  CA  ARG B 422    11516  13559  12125    134   -117   -160       C  
ATOM   6000  C   ARG B 422     -77.426  20.173  31.518  1.00 93.13           C  
ANISOU 6000  C   ARG B 422    11033  12749  11605    151   -122   -133       C  
ATOM   6001  O   ARG B 422     -78.600  19.909  31.264  1.00 86.71           O  
ANISOU 6001  O   ARG B 422    10270  11833  10841    194   -142    -88       O  
ATOM   6002  CB  ARG B 422     -78.018  19.747  33.921  1.00103.11           C  
ANISOU 6002  CB  ARG B 422    12133  14258  12785    196   -143    -99       C  
ATOM   6003  CG  ARG B 422     -78.156  18.235  33.937  1.00108.37           C  
ANISOU 6003  CG  ARG B 422    12765  14937  13473    291   -162     31       C  
ATOM   6004  CD  ARG B 422     -78.310  17.710  35.359  1.00114.00           C  
ANISOU 6004  CD  ARG B 422    13365  15819  14130    340   -169     82       C  
ATOM   6005  NE  ARG B 422     -79.649  17.923  35.896  1.00119.12           N  
ANISOU 6005  NE  ARG B 422    14034  16425  14802    351   -189     82       N  
ATOM   6006  CZ  ARG B 422     -80.024  17.574  37.123  1.00122.93           C  
ANISOU 6006  CZ  ARG B 422    14430  17033  15243    392   -198    122       C  
ATOM   6007  NH1 ARG B 422     -79.152  17.000  37.944  1.00120.94           N  
ANISOU 6007  NH1 ARG B 422    14062  16968  14922    431   -186    168       N  
ATOM   6008  NH2 ARG B 422     -81.269  17.802  37.531  1.00125.99           N  
ANISOU 6008  NH2 ARG B 422    14843  17375  15654    400   -218    120       N  
ATOM   6009  N   LYS B 423     -76.503  20.375  30.579  1.00 97.13           N  
ANISOU 6009  N   LYS B 423    11575  13212  12118    114   -104   -163       N  
ATOM   6010  CA  LYS B 423     -76.819  20.404  29.148  1.00 95.92           C  
ANISOU 6010  CA  LYS B 423    11530  12881  12034    122   -104   -149       C  
ATOM   6011  C   LYS B 423     -77.388  19.087  28.616  1.00100.30           C  
ANISOU 6011  C   LYS B 423    12100  13371  12639    197   -133    -43       C  
ATOM   6012  O   LYS B 423     -77.976  19.052  27.532  1.00 99.99           O  
ANISOU 6012  O   LYS B 423    12141  13197  12652    206   -139    -29       O  
ATOM   6013  CB  LYS B 423     -75.582  20.803  28.333  1.00 79.05           C  
ANISOU 6013  CB  LYS B 423     9415  10732   9887     68    -78   -199       C  
ATOM   6014  CG  LYS B 423     -75.361  22.308  28.216  1.00 69.85           C  
ANISOU 6014  CG  LYS B 423     8306   9526   8708    -21    -28   -314       C  
ATOM   6015  CD  LYS B 423     -73.876  22.639  28.069  1.00 74.18           C  
ANISOU 6015  CD  LYS B 423     8819  10160   9206    -96      2   -380       C  
ATOM   6016  CE  LYS B 423     -73.116  22.311  29.356  1.00 73.43           C  
ANISOU 6016  CE  LYS B 423     8583  10296   9021   -115     -3   -393       C  
ATOM   6017  NZ  LYS B 423     -71.653  22.600  29.283  1.00 57.18           N  
ANISOU 6017  NZ  LYS B 423     6468   8363   6894   -193     26   -459       N  
ATOM   6018  N   ASN B 424     -77.212  18.009  29.374  1.00 99.32           N  
ANISOU 6018  N   ASN B 424    11897  13347  12493    249   -142     29       N  
ATOM   6019  CA  ASN B 424     -77.689  16.706  28.938  1.00101.26           C  
ANISOU 6019  CA  ASN B 424    12165  13525  12786    310   -147    123       C  
ATOM   6020  C   ASN B 424     -78.897  16.212  29.724  1.00105.43           C  
ANISOU 6020  C   ASN B 424    12673  14063  13323    349   -161    171       C  
ATOM   6021  O   ASN B 424     -78.887  16.164  30.956  1.00105.62           O  
ANISOU 6021  O   ASN B 424    12618  14211  13302    371   -163    185       O  
ATOM   6022  CB  ASN B 424     -76.565  15.670  28.981  1.00107.91           C  
ANISOU 6022  CB  ASN B 424    12956  14439  13607    356   -122    189       C  
ATOM   6023  CG  ASN B 424     -76.774  14.541  27.983  1.00112.89           C  
ANISOU 6023  CG  ASN B 424    13651  14944  14299    391   -105    257       C  
ATOM   6024  OD1 ASN B 424     -77.905  14.231  27.600  1.00113.76           O  
ANISOU 6024  OD1 ASN B 424    13816  14950  14456    389   -112    271       O  
ATOM   6025  ND2 ASN B 424     -75.677  13.922  27.554  1.00114.08           N  
ANISOU 6025  ND2 ASN B 424    13793  15111  14442    419    -75    295       N  
ATOM   6026  N   ILE B 425     -79.940  15.857  28.982  1.00106.27           N  
ANISOU 6026  N   ILE B 425    12846  14049  13481    354   -169    193       N  
ATOM   6027  CA  ILE B 425     -81.168  15.292  29.529  1.00101.04           C  
ANISOU 6027  CA  ILE B 425    12175  13384  12832    381   -179    237       C  
ATOM   6028  C   ILE B 425     -81.562  14.131  28.615  1.00 96.18           C  
ANISOU 6028  C   ILE B 425    11612  12667  12266    389   -160    289       C  
ATOM   6029  O   ILE B 425     -82.383  14.296  27.711  1.00 96.32           O  
ANISOU 6029  O   ILE B 425    11686  12602  12310    360   -172    266       O  
ATOM   6030  CB  ILE B 425     -82.280  16.357  29.584  1.00 99.74           C  
ANISOU 6030  CB  ILE B 425    12037  13195  12664    359   -206    186       C  
ATOM   6031  CG1 ILE B 425     -81.931  17.426  30.629  1.00 96.51           C  
ANISOU 6031  CG1 ILE B 425    11580  12882  12206    344   -208    130       C  
ATOM   6032  CG2 ILE B 425     -83.621  15.724  29.906  1.00103.79           C  
ANISOU 6032  CG2 ILE B 425    12545  13700  13189    380   -219    231       C  
ATOM   6033  CD1 ILE B 425     -81.857  16.907  32.068  1.00 83.74           C  
ANISOU 6033  CD1 ILE B 425     9869  11400  10550    377   -211    168       C  
ATOM   6034  N   PRO B 426     -80.959  12.951  28.854  1.00 92.85           N  
ANISOU 6034  N   PRO B 426    11168  12260  11850    430   -119    359       N  
ATOM   6035  CA  PRO B 426     -80.822  11.841  27.900  1.00 91.43           C  
ANISOU 6035  CA  PRO B 426    11046  11978  11714    431    -75    398       C  
ATOM   6036  C   PRO B 426     -81.955  10.810  27.876  1.00 96.43           C  
ANISOU 6036  C   PRO B 426    11711  12548  12381    425    -44    437       C  
ATOM   6037  O   PRO B 426     -81.802   9.773  27.225  1.00 94.20           O  
ANISOU 6037  O   PRO B 426    11478  12180  12133    422     14    469       O  
ATOM   6038  CB  PRO B 426     -79.521  11.153  28.353  1.00 85.82           C  
ANISOU 6038  CB  PRO B 426    10294  11331  10983    493    -28    462       C  
ATOM   6039  CG  PRO B 426     -79.050  11.910  29.609  1.00 86.24           C  
ANISOU 6039  CG  PRO B 426    10252  11546  10972    518    -56    452       C  
ATOM   6040  CD  PRO B 426     -80.246  12.658  30.105  1.00 90.16           C  
ANISOU 6040  CD  PRO B 426    10742  12051  11465    484   -102    406       C  
ATOM   6041  N   ALA B 427     -83.058  11.068  28.572  1.00 99.65           N  
ANISOU 6041  N   ALA B 427    12092  12994  12775    418    -73    430       N  
ATOM   6042  CA  ALA B 427     -84.222  10.198  28.454  1.00 93.13           C  
ANISOU 6042  CA  ALA B 427    11296  12114  11975    391    -45    450       C  
ATOM   6043  C   ALA B 427     -84.843  10.363  27.066  1.00 87.55           C  
ANISOU 6043  C   ALA B 427    10650  11330  11287    321    -59    393       C  
ATOM   6044  O   ALA B 427     -85.325   9.404  26.459  1.00 89.10           O  
ANISOU 6044  O   ALA B 427    10889  11458  11509    278    -11    398       O  
ATOM   6045  CB  ALA B 427     -85.229  10.520  29.528  1.00 94.02           C  
ANISOU 6045  CB  ALA B 427    11358  12303  12061    402    -79    455       C  
ATOM   6046  N   VAL B 428     -84.810  11.591  26.565  1.00 76.62           N  
ANISOU 6046  N   VAL B 428     9267   9961   9883    308   -114    338       N  
ATOM   6047  CA  VAL B 428     -85.394  11.904  25.272  1.00 74.39           C  
ANISOU 6047  CA  VAL B 428     9028   9633   9605    257   -131    291       C  
ATOM   6048  C   VAL B 428     -84.344  12.032  24.158  1.00 85.68           C  
ANISOU 6048  C   VAL B 428    10501  11002  11054    245   -120    269       C  
ATOM   6049  O   VAL B 428     -84.687  12.339  23.014  1.00 90.59           O  
ANISOU 6049  O   VAL B 428    11154  11593  11674    209   -132    232       O  
ATOM   6050  CB  VAL B 428     -86.209  13.193  25.347  1.00 62.82           C  
ANISOU 6050  CB  VAL B 428     7544   8221   8103    264   -186    256       C  
ATOM   6051  CG1 VAL B 428     -87.198  13.110  26.495  1.00 63.03           C  
ANISOU 6051  CG1 VAL B 428     7525   8316   8108    280   -200    278       C  
ATOM   6052  CG2 VAL B 428     -85.291  14.380  25.537  1.00 46.71           C  
ANISOU 6052  CG2 VAL B 428     5502   6192   6052    293   -206    230       C  
ATOM   6053  N   THR B 429     -83.070  11.808  24.484  1.00 84.99           N  
ANISOU 6053  N   THR B 429    10406  10910  10976    279    -96    295       N  
ATOM   6054  CA  THR B 429     -82.032  11.780  23.451  1.00 78.36           C  
ANISOU 6054  CA  THR B 429     9606  10014  10154    269    -79    280       C  
ATOM   6055  C   THR B 429     -81.858  10.355  22.943  1.00 79.55           C  
ANISOU 6055  C   THR B 429     9797  10089  10339    256    -11    314       C  
ATOM   6056  O   THR B 429     -81.369   9.479  23.659  1.00 83.67           O  
ANISOU 6056  O   THR B 429    10307  10612  10870    300     42    374       O  
ATOM   6057  CB  THR B 429     -80.662  12.306  23.932  1.00 72.53           C  
ANISOU 6057  CB  THR B 429     8836   9324   9398    308    -83    285       C  
ATOM   6058  OG1 THR B 429     -80.788  13.634  24.459  1.00 69.49           O  
ANISOU 6058  OG1 THR B 429     8422   9000   8980    306   -128    243       O  
ATOM   6059  CG2 THR B 429     -79.702  12.337  22.766  1.00 73.46           C  
ANISOU 6059  CG2 THR B 429     8996   9384   9532    291    -70    266       C  
ATOM   6060  N   LEU B 430     -82.262  10.134  21.699  1.00 77.36           N  
ANISOU 6060  N   LEU B 430     9568   9749  10078    198     -2    276       N  
ATOM   6061  CA  LEU B 430     -82.309   8.793  21.133  1.00 77.99           C  
ANISOU 6061  CA  LEU B 430     9697   9746  10190    163     76    289       C  
ATOM   6062  C   LEU B 430     -81.308   8.606  19.989  1.00 75.88           C  
ANISOU 6062  C   LEU B 430     9475   9411   9943    152    102    275       C  
ATOM   6063  O   LEU B 430     -81.224   7.527  19.401  1.00 75.48           O  
ANISOU 6063  O   LEU B 430     9477   9281   9921    120    177    278       O  
ATOM   6064  CB  LEU B 430     -83.730   8.491  20.641  1.00 79.72           C  
ANISOU 6064  CB  LEU B 430     9926   9964  10401     83     78    246       C  
ATOM   6065  CG  LEU B 430     -84.882   8.800  21.605  1.00 76.19           C  
ANISOU 6065  CG  LEU B 430     9430   9595   9925     85     42    252       C  
ATOM   6066  CD1 LEU B 430     -86.226   8.673  20.906  1.00 77.46           C  
ANISOU 6066  CD1 LEU B 430     9589   9785  10059      2     35    200       C  
ATOM   6067  CD2 LEU B 430     -84.820   7.895  22.831  1.00 69.81           C  
ANISOU 6067  CD2 LEU B 430     8613   8776   9134    123    100    315       C  
ATOM   6068  N   SER B 431     -80.552   9.659  19.684  1.00 65.66           N  
ANISOU 6068  N   SER B 431     8167   8146   8634    175     48    255       N  
ATOM   6069  CA  SER B 431     -79.607   9.633  18.572  1.00 60.12           C  
ANISOU 6069  CA  SER B 431     7504   7391   7947    165     62    238       C  
ATOM   6070  C   SER B 431     -78.583  10.761  18.667  1.00 55.39           C  
ANISOU 6070  C   SER B 431     6879   6838   7328    202     15    229       C  
ATOM   6071  O   SER B 431     -78.768  11.732  19.412  1.00 51.52           O  
ANISOU 6071  O   SER B 431     6349   6415   6811    218    -31    218       O  
ATOM   6072  CB  SER B 431     -80.348   9.774  17.247  1.00 58.98           C  
ANISOU 6072  CB  SER B 431     7391   7217   7801     93     48    179       C  
ATOM   6073  OG  SER B 431     -80.630  11.142  17.000  1.00 64.22           O  
ANISOU 6073  OG  SER B 431     8032   7932   8436     98    -23    146       O  
ATOM   6074  N   ILE B 432     -77.516  10.643  17.881  1.00 51.24           N  
ANISO