CNRS Nantes University US2B US2B
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***  VIRAL PROTEIN,RNA BINDING PROTEIN 07-AUG-12 4GH9  ***

elNémo ID: 2411221736062541729

Job options:

ID        	=	 2411221736062541729
JOBID     	=	 VIRAL PROTEIN,RNA BINDING PROTEIN 07-AUG-12 4GH9
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    VIRAL PROTEIN,RNA BINDING PROTEIN       07-AUG-12   4GH9              
TITLE     CRYSTAL STRUCTURE OF MARBURG VIRUS VP35 RNA BINDING DOMAIN            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POLYMERASE COFACTOR VP35;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 204-329;                                      
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MARBURG VIRUS;                                  
SOURCE   3 ORGANISM_COMMON: MARV;                                               
SOURCE   4 ORGANISM_TAXID: 33727;                                               
SOURCE   5 STRAIN: MUSOKE;                                                      
SOURCE   6 GENE: VP35;                                                          
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: R2;                                        
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET46B                                    
KEYWDS    VIRAL POLYMERASE, INTERFERON INHIBITION, DOUBLE STRANDED VIRAL RNA,   
KEYWDS   2 VIRAL PROTEIN, RNA BINDING PROTEIN                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.BALE,J.JEAN-PHILIPPE,Z.A.BORNHOLDT,C.K.KIMBERLIN,P.HALFMANN,        
AUTHOR   2 M.A.ZANDONATTI,J.KUNERT,G.J.A.KROON,Y.KAWAOKA,I.J.MACRAE,I.A.WILSON, 
AUTHOR   3 E.O.SAPHIRE                                                          
REVDAT   3   13-SEP-23 4GH9    1       REMARK SEQADV                            
REVDAT   2   24-OCT-12 4GH9    1       JRNL                                     
REVDAT   1   15-AUG-12 4GH9    0                                                
JRNL        AUTH   S.BALE,J.P.JULIEN,Z.A.BORNHOLDT,C.R.KIMBERLIN,P.HALFMANN,    
JRNL        AUTH 2 M.A.ZANDONATTI,J.KUNERT,G.J.KROON,Y.KAWAOKA,I.J.MACRAE,      
JRNL        AUTH 3 I.A.WILSON,E.O.SAPHIRE                                       
JRNL        TITL   MARBURG VIRUS VP35 CAN BOTH FULLY COAT THE BACKBONE AND CAP  
JRNL        TITL 2 THE ENDS OF DSRNA FOR INTERFERON ANTAGONISM.                 
JRNL        REF    PLOS PATHOG.                  V.   8 02916 2012              
JRNL        REFN                   ISSN 1553-7366                               
JRNL        PMID   23028316                                                     
JRNL        DOI    10.1371/JOURNAL.PPAT.1002916                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8_1069)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.68                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 15720                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.164                           
REMARK   3   R VALUE            (WORKING SET) : 0.161                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 783                             
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 26.6850 -  2.9971    1.00     2603   132  0.1634 0.1784        
REMARK   3     2  2.9971 -  2.3794    1.00     2501   127  0.1605 0.2423        
REMARK   3     3  2.3794 -  2.0788    1.00     2484   130  0.1420 0.2251        
REMARK   3     4  2.0788 -  1.8887    1.00     2460   136  0.1584 0.2434        
REMARK   3     5  1.8887 -  1.7534    1.00     2441   142  0.1756 0.2969        
REMARK   3     6  1.7534 -  1.6500    1.00     2448   116  0.1857 0.2745        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.170            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.610           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 21.89                          
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      :  0.006            983                                  
REMARK   3   ANGLE     :  1.004           1330                                  
REMARK   3   CHIRALITY :  0.067            152                                  
REMARK   3   PLANARITY :  0.005            175                                  
REMARK   3   DIHEDRAL  : 12.990            356                                  
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 4GH9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-AUG-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000074180.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-AUG-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : DOUBLE FLAT CRYSTAL, SI(111)       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK                             
REMARK 200  DATA SCALING SOFTWARE          : D*TREK                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15759                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.440                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : 0.05900                            
REMARK 200   FOR THE DATA SET  : 11.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.75                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.44600                            
REMARK 200   FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3KS8                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2-2.4 M AMMONIUM SULPHATE, 100 MM        
REMARK 280  SODIUM ACETATE, PH 4.6, VAPOR DIFFUSION, HANGING DROP,              
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       32.96250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       32.96250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       21.26200            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       45.44000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       21.26200            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       45.44000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       32.96250            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       21.26200            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       45.44000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       32.96250            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       21.26200            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       45.44000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 516  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 542  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 546  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 602  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   184                                                      
REMARK 465     ALA A   185                                                      
REMARK 465     HIS A   186                                                      
REMARK 465     HIS A   187                                                      
REMARK 465     HIS A   188                                                      
REMARK 465     HIS A   189                                                      
REMARK 465     HIS A   190                                                      
REMARK 465     HIS A   191                                                      
REMARK 465     VAL A   192                                                      
REMARK 465     ASP A   193                                                      
REMARK 465     ASP A   194                                                      
REMARK 465     ASP A   195                                                      
REMARK 465     ASP A   196                                                      
REMARK 465     LYS A   197                                                      
REMARK 465     GLU A   198                                                      
REMARK 465     ASN A   199                                                      
REMARK 465     LEU A   200                                                      
REMARK 465     TYR A   201                                                      
REMARK 465     PHE A   202                                                      
REMARK 465     GLN A   203                                                      
REMARK 465     SER A   204                                                      
REMARK 465     LYS A   205                                                      
REMARK 465     PRO A   206                                                      
REMARK 465     ASN A   207                                                      
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 406                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3KS8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3FKE   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3L2A   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3L26   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3L25   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4GHA   RELATED DB: PDB                                   
DBREF  4GH9 A  204   329  UNP    P35259   VP35_MABVM     204    329             
SEQADV 4GH9 MET A  184  UNP  P35259              EXPRESSION TAG                 
SEQADV 4GH9 ALA A  185  UNP  P35259              EXPRESSION TAG                 
SEQADV 4GH9 HIS A  186  UNP  P35259              EXPRESSION TAG                 
SEQADV 4GH9 HIS A  187  UNP  P35259              EXPRESSION TAG                 
SEQADV 4GH9 HIS A  188  UNP  P35259              EXPRESSION TAG                 
SEQADV 4GH9 HIS A  189  UNP  P35259              EXPRESSION TAG                 
SEQADV 4GH9 HIS A  190  UNP  P35259              EXPRESSION TAG                 
SEQADV 4GH9 HIS A  191  UNP  P35259              EXPRESSION TAG                 
SEQADV 4GH9 VAL A  192  UNP  P35259              EXPRESSION TAG                 
SEQADV 4GH9 ASP A  193  UNP  P35259              EXPRESSION TAG                 
SEQADV 4GH9 ASP A  194  UNP  P35259              EXPRESSION TAG                 
SEQADV 4GH9 ASP A  195  UNP  P35259              EXPRESSION TAG                 
SEQADV 4GH9 ASP A  196  UNP  P35259              EXPRESSION TAG                 
SEQADV 4GH9 LYS A  197  UNP  P35259              EXPRESSION TAG                 
SEQADV 4GH9 GLU A  198  UNP  P35259              EXPRESSION TAG                 
SEQADV 4GH9 ASN A  199  UNP  P35259              EXPRESSION TAG                 
SEQADV 4GH9 LEU A  200  UNP  P35259              EXPRESSION TAG                 
SEQADV 4GH9 TYR A  201  UNP  P35259              EXPRESSION TAG                 
SEQADV 4GH9 PHE A  202  UNP  P35259              EXPRESSION TAG                 
SEQADV 4GH9 GLN A  203  UNP  P35259              EXPRESSION TAG                 
SEQADV 4GH9 CYS A  296  UNP  P35259    SER   296 VARIANT                        
SEQRES   1 A  146  MET ALA HIS HIS HIS HIS HIS HIS VAL ASP ASP ASP ASP          
SEQRES   2 A  146  LYS GLU ASN LEU TYR PHE GLN SER LYS PRO ASN LEU SER          
SEQRES   3 A  146  ALA LYS ASP LEU ALA LEU LEU LEU PHE THR HIS LEU PRO          
SEQRES   4 A  146  GLY ASN ASN THR PRO PHE HIS ILE LEU ALA GLN VAL LEU          
SEQRES   5 A  146  SER LYS ILE ALA TYR LYS SER GLY LYS SER GLY ALA PHE          
SEQRES   6 A  146  LEU ASP ALA PHE HIS GLN ILE LEU SER GLU GLY GLU ASN          
SEQRES   7 A  146  ALA GLN ALA ALA LEU THR ARG LEU SER ARG THR PHE ASP          
SEQRES   8 A  146  ALA PHE LEU GLY VAL VAL PRO PRO VAL ILE ARG VAL LYS          
SEQRES   9 A  146  ASN PHE GLN THR VAL PRO ARG PRO CYS GLN LYS SER LEU          
SEQRES  10 A  146  ARG ALA VAL PRO PRO ASN PRO THR ILE ASP LYS GLY TRP          
SEQRES  11 A  146  VAL CYS VAL TYR SER SER GLU GLN GLY GLU THR ARG ALA          
SEQRES  12 A  146  LEU LYS ILE                                                  
HET    ACT  A 401       4                                                       
HET    ACT  A 402       4                                                       
HET    ACT  A 403       4                                                       
HET    ACT  A 404       4                                                       
HET    ACT  A 405       4                                                       
HET    ACT  A 406       4                                                       
HETNAM     ACT ACETATE ION                                                      
FORMUL   2  ACT    6(C2 H3 O2 1-)                                               
FORMUL   8  HOH   *117(H2 O)                                                    
HELIX    1   1 SER A  209  THR A  219  1                                  11    
HELIX    2   2 THR A  226  SER A  242  1                                  17    
HELIX    3   3 LYS A  244  GLU A  258  1                                  15    
HELIX    4   4 ASN A  261  PHE A  273  1                                  13    
HELIX    5   5 ASP A  274  LEU A  277  5                                   4    
HELIX    6   6 ASN A  288  VAL A  292  5                                   5    
HELIX    7   7 PRO A  293  LYS A  298  5                                   6    
HELIX    8   8 THR A  308  LYS A  311  5                                   4    
SHEET    1   A 4 VAL A 283  ARG A 285  0                                        
SHEET    2   A 4 TRP A 313  SER A 318  1  O  VAL A 316   N  ILE A 284           
SHEET    3   A 4 THR A 324  LYS A 328 -1  O  ARG A 325   N  TYR A 317           
SHEET    4   A 4 LEU A 300  ARG A 301 -1  N  ARG A 301   O  ALA A 326           
SITE     1 AC1  7 ARG A 268  ARG A 271  THR A 272  LYS A 328                    
SITE     2 AC1  7 ILE A 329  ACT A 405  HOH A 569                               
SITE     1 AC2  5 LEU A 216  THR A 219  HIS A 220  HIS A 253                    
SITE     2 AC2  5 HOH A 558                                                     
SITE     1 AC3  4 TYR A 240  VAL A 303  PRO A 304  HOH A 539                    
SITE     1 AC4  4 LYS A 211  GLY A 223  HOH A 559  HOH A 570                    
SITE     1 AC5  6 ARG A 271  ASP A 310  LYS A 311  GLY A 312                    
SITE     2 AC5  6 ACT A 401  HOH A 580                                          
SITE     1 AC6  2 PRO A 293  ARG A 294                                          
CRYST1   42.524   90.880   65.925  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.023516  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011004  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015169        0.00000                         
ATOM      1  N   LEU A 208      26.541   9.362  -8.758  1.00 34.52           N  
ANISOU    1  N   LEU A 208     2349   4961   5805  -1062   1341   -106       N  
ATOM      2  CA  LEU A 208      25.678   8.783  -7.727  1.00 34.06           C  
ANISOU    2  CA  LEU A 208     2336   4962   5642   -754   1500   -807       C  
ATOM      3  C   LEU A 208      24.343   9.518  -7.650  1.00 35.11           C  
ANISOU    3  C   LEU A 208     2839   4919   5582   -834    661  -1208       C  
ATOM      4  O   LEU A 208      24.298  10.700  -7.307  1.00 36.58           O  
ANISOU    4  O   LEU A 208     2858   5173   5867  -1046     45  -1150       O  
ATOM      5  CB  LEU A 208      26.382   8.822  -6.368  1.00 36.69           C  
ANISOU    5  CB  LEU A 208     3153   5066   5723   -584   1587  -1226       C  
ATOM      6  CG  LEU A 208      25.718   8.099  -5.194  1.00 39.45           C  
ANISOU    6  CG  LEU A 208     3806   5168   6016   -524    925  -1180       C  
ATOM      7  CD1 LEU A 208      25.735   6.589  -5.401  1.00 40.44           C  
ANISOU    7  CD1 LEU A 208     4197   5122   6046   -336    805  -1266       C  
ATOM      8  CD2 LEU A 208      26.382   8.478  -3.871  1.00 40.29           C  
ANISOU    8  CD2 LEU A 208     3852   5327   6130   -537    739   -966       C  
ATOM      9  N   SER A 209      23.258   8.811  -7.963  1.00 30.77           N  
ANISOU    9  N   SER A 209     2122   4675   4895   -986    932  -1577       N  
ATOM     10  CA  SER A 209      21.930   9.411  -7.979  1.00 29.89           C  
ANISOU   10  CA  SER A 209     2320   4494   4543  -1017    719  -1873       C  
ATOM     11  C   SER A 209      21.400   9.605  -6.564  1.00 28.64           C  
ANISOU   11  C   SER A 209     1996   4350   4537   -742    523  -1994       C  
ATOM     12  O   SER A 209      21.872   8.964  -5.623  1.00 28.50           O  
ANISOU   12  O   SER A 209     2123   4536   4168   -531    183  -2377       O  
ATOM     13  CB  SER A 209      20.954   8.533  -8.760  1.00 31.62           C  
ANISOU   13  CB  SER A 209     3225   4374   4414  -1363   1269  -1797       C  
ATOM     14  OG  SER A 209      20.707   7.319  -8.073  1.00 31.73           O  
ANISOU   14  OG  SER A 209     3141   4301   4614  -1706   1276  -2047       O  
ATOM     15  N   ALA A 210      20.412  10.484  -6.420  1.00 26.00           N  
ANISOU   15  N   ALA A 210     1668   3697   4513   -502    508  -1932       N  
ATOM     16  CA  ALA A 210      19.742  10.664  -5.138  1.00 26.13           C  
ANISOU   16  CA  ALA A 210     1892   3380   4657   -132    514  -1776       C  
ATOM     17  C   ALA A 210      19.126   9.343  -4.672  1.00 25.41           C  
ANISOU   17  C   ALA A 210     1890   3361   4403   -304    220  -1823       C  
ATOM     18  O   ALA A 210      19.224   8.981  -3.500  1.00 23.60           O  
ANISOU   18  O   ALA A 210     1654   3435   3880   -499   -181  -1580       O  
ATOM     19  CB  ALA A 210      18.677  11.752  -5.235  1.00 26.99           C  
ANISOU   19  CB  ALA A 210     2195   3298   4764    334     48  -1192       C  
ATOM     20  N   LYS A 211      18.506   8.626  -5.605  1.00 24.18           N  
ANISOU   20  N   LYS A 211     1721   3167   4299   -268   -177  -1880       N  
ATOM     21  CA  LYS A 211      17.950   7.307  -5.318  1.00 25.54           C  
ANISOU   21  CA  LYS A 211     2160   3152   4390   -535   -535  -1582       C  
ATOM     22  C   LYS A 211      18.976   6.344  -4.713  1.00 26.19           C  
ANISOU   22  C   LYS A 211     1876   3348   4726   -231   -329  -1967       C  
ATOM     23  O   LYS A 211      18.735   5.739  -3.663  1.00 26.17           O  
ANISOU   23  O   LYS A 211     1973   3341   4630    103   -214  -1931       O  
ATOM     24  CB  LYS A 211      17.351   6.689  -6.584  1.00 25.47           C  
ANISOU   24  CB  LYS A 211     2824   2898   3954   -631   -769  -1482       C  
ATOM     25  CG  LYS A 211      16.917   5.235  -6.414  1.00 27.07           C  
ANISOU   25  CG  LYS A 211     3114   2875   4295   -808  -1036  -1256       C  
ATOM     26  CD  LYS A 211      16.549   4.587  -7.749  1.00 29.14           C  
ANISOU   26  CD  LYS A 211     3630   2857   4586   -820  -1003  -1367       C  
ATOM     27  CE  LYS A 211      16.118   3.139  -7.558  1.00 29.71           C  
ANISOU   27  CE  LYS A 211     3774   2964   4550   -809   -965  -1553       C  
ATOM     28  NZ  LYS A 211      16.010   2.382  -8.842  1.00 32.10           N  
ANISOU   28  NZ  LYS A 211     4117   3232   4849   -919   -580  -1614       N  
ATOM     29  N   ASP A 212      20.119   6.199  -5.370  1.00 26.80           N  
ANISOU   29  N   ASP A 212     2031   3359   4792    182   -319  -2167       N  
ATOM     30  CA  ASP A 212      21.115   5.248  -4.894  1.00 26.98           C  
ANISOU   30  CA  ASP A 212     1867   3590   4793    400    -23  -2129       C  
ATOM     31  C   ASP A 212      21.796   5.714  -3.616  1.00 26.16           C  
ANISOU   31  C   ASP A 212     1599   3499   4840     35    322  -1792       C  
ATOM     32  O   ASP A 212      22.138   4.907  -2.756  1.00 27.66           O  
ANISOU   32  O   ASP A 212     1591   3725   5196     72     48  -1722       O  
ATOM     33  CB  ASP A 212      22.126   4.931  -5.988  1.00 30.56           C  
ANISOU   33  CB  ASP A 212     3030   3958   4624    542    203  -1958       C  
ATOM     34  CG  ASP A 212      21.498   4.177  -7.140  1.00 33.43           C  
ANISOU   34  CG  ASP A 212     3952   4016   4732    716    478  -1853       C  
ATOM     35  OD1 ASP A 212      20.526   3.423  -6.904  1.00 34.73           O  
ANISOU   35  OD1 ASP A 212     4251   3970   4974   1159    254  -1596       O  
ATOM     36  OD2 ASP A 212      21.961   4.351  -8.280  1.00 34.47           O  
ANISOU   36  OD2 ASP A 212     4311   4327   4459    471    920  -1656       O  
ATOM     37  N   LEU A 213      21.961   7.022  -3.483  1.00 26.12           N  
ANISOU   37  N   LEU A 213     1717   3439   4769   -299    689  -1885       N  
ATOM     38  CA  LEU A 213      22.484   7.581  -2.251  1.00 24.21           C  
ANISOU   38  CA  LEU A 213     1530   3179   4489   -345    396  -1831       C  
ATOM     39  C   LEU A 213      21.540   7.230  -1.098  1.00 23.58           C  
ANISOU   39  C   LEU A 213     1493   2927   4539   -167    303  -1922       C  
ATOM     40  O   LEU A 213      21.972   6.748  -0.049  1.00 22.51           O  
ANISOU   40  O   LEU A 213     1487   2735   4329   -250    360  -1952       O  
ATOM     41  CB  LEU A 213      22.666   9.092  -2.392  1.00 25.64           C  
ANISOU   41  CB  LEU A 213     1822   3301   4618   -551     -7  -1631       C  
ATOM     42  CG  LEU A 213      23.103   9.874  -1.159  1.00 26.95           C  
ANISOU   42  CG  LEU A 213     2253   3379   4609   -792   -783  -1193       C  
ATOM     43  CD1 LEU A 213      24.393   9.303  -0.568  1.00 26.06           C  
ANISOU   43  CD1 LEU A 213     1957   3553   4391   -698   -972   -786       C  
ATOM     44  CD2 LEU A 213      23.283  11.332  -1.531  1.00 28.58           C  
ANISOU   44  CD2 LEU A 213     2644   3404   4810  -1168   -480  -1274       C  
ATOM     45  N   ALA A 214      20.240   7.440  -1.309  1.00 22.00           N  
ANISOU   45  N   ALA A 214     1356   2633   4369   -223    199  -1509       N  
ATOM     46  CA  ALA A 214      19.259   7.122  -0.283  1.00 20.68           C  
ANISOU   46  CA  ALA A 214     1226   2389   4243     -1    -78  -1267       C  
ATOM     47  C   ALA A 214      19.308   5.640   0.079  1.00 22.30           C  
ANISOU   47  C   ALA A 214     1420   2277   4774     44   -160  -1640       C  
ATOM     48  O   ALA A 214      19.304   5.288   1.255  1.00 21.56           O  
ANISOU   48  O   ALA A 214     1482   2159   4551    293   -559  -1586       O  
ATOM     49  CB  ALA A 214      17.845   7.535  -0.728  1.00 21.53           C  
ANISOU   49  CB  ALA A 214     1277   2592   4312    -98    287  -1259       C  
ATOM     50  N   LEU A 215      19.365   4.777  -0.935  1.00 22.82           N  
ANISOU   50  N   LEU A 215     1500   2291   4877    150   -342  -1700       N  
ATOM     51  CA  LEU A 215      19.477   3.337  -0.702  1.00 22.20           C  
ANISOU   51  CA  LEU A 215     1454   2425   4557    146   -319  -1767       C  
ATOM     52  C   LEU A 215      20.726   2.978   0.101  1.00 22.12           C  
ANISOU   52  C   LEU A 215     1420   2500   4485    -84    153  -1842       C  
ATOM     53  O   LEU A 215      20.666   2.150   1.004  1.00 25.50           O  
ANISOU   53  O   LEU A 215     1626   2701   5361   -151    348  -1879       O  
ATOM     54  CB  LEU A 215      19.437   2.569  -2.021  1.00 22.71           C  
ANISOU   54  CB  LEU A 215     1534   2539   4554     33   -499  -1536       C  
ATOM     55  CG  LEU A 215      18.036   2.540  -2.636  1.00 24.79           C  
ANISOU   55  CG  LEU A 215     1831   2909   4679    -42   -707  -1632       C  
ATOM     56  CD1 LEU A 215      18.071   1.983  -4.049  1.00 25.05           C  
ANISOU   56  CD1 LEU A 215     2147   3001   4368    385  -1055  -1850       C  
ATOM     57  CD2 LEU A 215      17.107   1.715  -1.752  1.00 27.74           C  
ANISOU   57  CD2 LEU A 215     1889   3357   5293    562   -823  -1751       C  
ATOM     58  N   LEU A 216      21.851   3.614  -0.213  1.00 20.59           N  
ANISOU   58  N   LEU A 216     1299   2512   4013   -162    172  -1656       N  
ATOM     59  CA  LEU A 216      23.073   3.369   0.549  1.00 20.38           C  
ANISOU   59  CA  LEU A 216     1231   2553   3960   -173     68  -1367       C  
ATOM     60  C   LEU A 216      22.888   3.729   2.020  1.00 20.74           C  
ANISOU   60  C   LEU A 216     1252   2421   4206    -14    224  -1295       C  
ATOM     61  O   LEU A 216      23.317   2.990   2.906  1.00 22.29           O  
ANISOU   61  O   LEU A 216     1327   2548   4593     80    305  -1064       O  
ATOM     62  CB  LEU A 216      24.251   4.140  -0.050  1.00 20.02           C  
ANISOU   62  CB  LEU A 216     1138   2707   3762     51    147  -1119       C  
ATOM     63  CG  LEU A 216      24.749   3.578  -1.380  1.00 22.81           C  
ANISOU   63  CG  LEU A 216     1305   3083   4276     94    354  -1073       C  
ATOM     64  CD1 LEU A 216      25.639   4.592  -2.092  1.00 24.39           C  
ANISOU   64  CD1 LEU A 216     1431   3264   4573   -283    622   -994       C  
ATOM     65  CD2 LEU A 216      25.497   2.266  -1.165  1.00 23.57           C  
ANISOU   65  CD2 LEU A 216     1359   3144   4453      0   -123  -1465       C  
ATOM     66  N   LEU A 217      22.233   4.862   2.276  1.00 20.37           N  
ANISOU   66  N   LEU A 217     1414   2378   3947     32    623  -1151       N  
ATOM     67  CA  LEU A 217      21.966   5.295   3.640  1.00 18.98           C  
ANISOU   67  CA  LEU A 217     1203   2029   3979   -160    467  -1041       C  
ATOM     68  C   LEU A 217      21.037   4.289   4.331  1.00 19.20           C  
ANISOU   68  C   LEU A 217     1154   2133   4008   -178    332   -932       C  
ATOM     69  O   LEU A 217      21.210   3.980   5.512  1.00 20.17           O  
ANISOU   69  O   LEU A 217     1180   2192   4292     21   -111  -1011       O  
ATOM     70  CB  LEU A 217      21.333   6.691   3.649  1.00 19.97           C  
ANISOU   70  CB  LEU A 217     1554   2059   3973   -579    200   -984       C  
ATOM     71  CG  LEU A 217      22.171   7.830   3.048  1.00 20.42           C  
ANISOU   71  CG  LEU A 217     1405   2048   4304   -297    -56  -1106       C  
ATOM     72  CD1 LEU A 217      21.458   9.175   3.160  1.00 18.60           C  
ANISOU   72  CD1 LEU A 217     1189   1775   4102     67   -158  -1318       C  
ATOM     73  CD2 LEU A 217      23.533   7.896   3.710  1.00 23.42           C  
ANISOU   73  CD2 LEU A 217     1753   2284   4860   -134   -693  -1189       C  
ATOM     74  N   PHE A 218      20.064   3.777   3.578  1.00 19.04           N  
ANISOU   74  N   PHE A 218     1147   2089   3999   -161    206  -1042       N  
ATOM     75  CA  PHE A 218      19.107   2.817   4.116  1.00 20.90           C  
ANISOU   75  CA  PHE A 218     1281   2223   4439    -43     59  -1396       C  
ATOM     76  C   PHE A 218      19.800   1.583   4.692  1.00 22.11           C  
ANISOU   76  C   PHE A 218     1475   2213   4712    -84    424  -1490       C  
ATOM     77  O   PHE A 218      19.298   0.977   5.635  1.00 23.91           O  
ANISOU   77  O   PHE A 218     1726   2150   5207   -214    837  -1384       O  
ATOM     78  CB  PHE A 218      18.113   2.347   3.045  1.00 21.50           C  
ANISOU   78  CB  PHE A 218     1347   2343   4480    185   -442  -1284       C  
ATOM     79  CG  PHE A 218      16.987   3.314   2.756  1.00 21.78           C  
ANISOU   79  CG  PHE A 218     1406   2259   4613    192   -402  -1540       C  
ATOM     80  CD1 PHE A 218      16.999   4.615   3.244  1.00 21.83           C  
ANISOU   80  CD1 PHE A 218     1322   2460   4511    139    223  -1112       C  
ATOM     81  CD2 PHE A 218      15.907   2.899   1.990  1.00 24.10           C  
ANISOU   81  CD2 PHE A 218     1573   2437   5147    169   -548  -1541       C  
ATOM     82  CE1 PHE A 218      15.966   5.488   2.965  1.00 23.55           C  
ANISOU   82  CE1 PHE A 218     1500   2576   4872   -328    552  -1312       C  
ATOM     83  CE2 PHE A 218      14.866   3.761   1.712  1.00 25.89           C  
ANISOU   83  CE2 PHE A 218     1809   2578   5448    -11   -375  -1781       C  
ATOM     84  CZ  PHE A 218      14.897   5.062   2.194  1.00 26.56           C  
ANISOU   84  CZ  PHE A 218     2230   2620   5242   -157    200  -1662       C  
ATOM     85  N   THR A 219      20.957   1.212   4.135  1.00 21.76           N  
ANISOU   85  N   THR A 219     1380   2251   4636    -35     76  -1681       N  
ATOM     86  CA  THR A 219      21.622  -0.013   4.571  1.00 21.67           C  
ANISOU   86  CA  THR A 219     1461   2319   4454    -18    563  -1272       C  
ATOM     87  C   THR A 219      22.113   0.090   6.011  1.00 23.42           C  
ANISOU   87  C   THR A 219     1799   2343   4756    175    573  -1259       C  
ATOM     88  O   THR A 219      22.456  -0.928   6.623  1.00 26.14           O  
ANISOU   88  O   THR A 219     2420   2588   4924    -64    844  -1366       O  
ATOM     89  CB  THR A 219      22.838  -0.390   3.675  1.00 20.48           C  
ANISOU   89  CB  THR A 219     1340   2288   4153      6    389  -1323       C  
ATOM     90  OG1 THR A 219      23.903   0.539   3.900  1.00 20.45           O  
ANISOU   90  OG1 THR A 219     1344   2382   4044     67    414  -1255       O  
ATOM     91  CG2 THR A 219      22.472  -0.366   2.215  1.00 21.50           C  
ANISOU   91  CG2 THR A 219     1500   2462   4206   -362    335  -1654       C  
ATOM     92  N   HIS A 220      22.158   1.316   6.537  1.00 21.35           N  
ANISOU   92  N   HIS A 220     1436   2183   4492    158    513   -942       N  
ATOM     93  CA  HIS A 220      22.665   1.567   7.881  1.00 20.00           C  
ANISOU   93  CA  HIS A 220     1285   1962   4352    -84    624   -665       C  
ATOM     94  C   HIS A 220      21.572   1.896   8.885  1.00 19.34           C  
ANISOU   94  C   HIS A 220     1163   2027   4158    256    270   -307       C  
ATOM     95  O   HIS A 220      21.860   2.091  10.064  1.00 23.00           O  
ANISOU   95  O   HIS A 220     1625   2190   4924    397   -304   -172       O  
ATOM     96  CB  HIS A 220      23.664   2.731   7.872  1.00 20.83           C  
ANISOU   96  CB  HIS A 220     1327   2253   4334    -94    637   -860       C  
ATOM     97  CG  HIS A 220      24.803   2.547   6.925  1.00 22.37           C  
ANISOU   97  CG  HIS A 220     1464   2328   4708     44    463  -1236       C  
ATOM     98  ND1 HIS A 220      25.899   1.769   7.225  1.00 24.65           N  
ANISOU   98  ND1 HIS A 220     1676   2738   4951    293    456  -1267       N  
ATOM     99  CD2 HIS A 220      25.027   3.054   5.690  1.00 23.60           C  
ANISOU   99  CD2 HIS A 220     1648   2318   5003     19    466  -1482       C  
ATOM    100  CE1 HIS A 220      26.747   1.799   6.213  1.00 25.63           C  
ANISOU  100  CE1 HIS A 220     1808   2700   5231     87    654  -1483       C  
ATOM    101  NE2 HIS A 220      26.242   2.572   5.268  1.00 24.46           N  
ANISOU  101  NE2 HIS A 220     1694   2437   5164    -49    754  -1303       N  
ATOM    102  N   LEU A 221      20.322   1.965   8.427  1.00 18.62           N  
ANISOU  102  N   LEU A 221     1108   1928   4039    188    257   -368       N  
ATOM    103  CA  LEU A 221      19.226   2.416   9.286  1.00 16.99           C  
ANISOU  103  CA  LEU A 221     1036   1549   3868     25    320   -383       C  
ATOM    104  C   LEU A 221      18.406   1.263   9.838  1.00 21.11           C  
ANISOU  104  C   LEU A 221     2168   1762   4089    207     -6   -281       C  
ATOM    105  O   LEU A 221      18.046   0.344   9.101  1.00 20.17           O  
ANISOU  105  O   LEU A 221     2221   1323   4120    -54      4   -499       O  
ATOM    106  CB  LEU A 221      18.290   3.354   8.517  1.00 16.07           C  
ANISOU  106  CB  LEU A 221     1080   1445   3581    -94    171   -145       C  
ATOM    107  CG  LEU A 221      18.819   4.765   8.247  1.00 16.03           C  
ANISOU  107  CG  LEU A 221     1072   1538   3481    265    395   -124       C  
ATOM    108  CD1 LEU A 221      17.886   5.510   7.302  1.00 16.91           C  
ANISOU  108  CD1 LEU A 221     1148   1686   3592    289    210    228       C  
ATOM    109  CD2 LEU A 221      18.975   5.511   9.557  1.00 17.81           C  
ANISOU  109  CD2 LEU A 221     1244   1749   3773    108    154    -90       C  
ATOM    110  N   PRO A 222      18.082   1.326  11.137  1.00 20.79           N  
ANISOU  110  N   PRO A 222     1670   2026   4203     54    -97   -320       N  
ATOM    111  CA  PRO A 222      17.213   0.311  11.735  1.00 21.75           C  
ANISOU  111  CA  PRO A 222     1859   2163   4242   -347    500   -515       C  
ATOM    112  C   PRO A 222      15.780   0.481  11.255  1.00 21.16           C  
ANISOU  112  C   PRO A 222     1785   2122   4131   -249    719   -564       C  
ATOM    113  O   PRO A 222      15.366   1.591  10.892  1.00 21.96           O  
ANISOU  113  O   PRO A 222     1861   2088   4394   -319    366   -617       O  
ATOM    114  CB  PRO A 222      17.330   0.584  13.240  1.00 24.79           C  
ANISOU  114  CB  PRO A 222     2519   2324   4577   -340    441   -360       C  
ATOM    115  CG  PRO A 222      17.765   1.997  13.349  1.00 24.35           C  
ANISOU  115  CG  PRO A 222     2472   2186   4595    309    567   -520       C  
ATOM    116  CD  PRO A 222      18.557   2.315  12.122  1.00 19.39           C  
ANISOU  116  CD  PRO A 222     1197   2008   4163     11    468   -693       C  
ATOM    117  N   GLY A 223      15.038  -0.620  11.232  1.00 19.85           N  
ANISOU  117  N   GLY A 223     1232   2242   4069   -269    535   -521       N  
ATOM    118  CA  GLY A 223      13.641  -0.583  10.848  1.00 21.08           C  
ANISOU  118  CA  GLY A 223     1267   2300   4443   -314    455   -216       C  
ATOM    119  C   GLY A 223      13.406  -0.206   9.399  1.00 21.66           C  
ANISOU  119  C   GLY A 223     1356   2275   4600   -353    502     10       C  
ATOM    120  O   GLY A 223      14.308  -0.286   8.558  1.00 22.54           O  
ANISOU  120  O   GLY A 223     1450   2208   4906    -87    460    257       O  
ATOM    121  N   ASN A 224      12.174   0.211   9.117  1.00 24.07           N  
ANISOU  121  N   ASN A 224     1631   2374   5140    -64    636     95       N  
ATOM    122  CA  ASN A 224      11.730   0.527   7.768  1.00 25.06           C  
ANISOU  122  CA  ASN A 224     1712   2523   5287   -162    579    -53       C  
ATOM    123  C   ASN A 224      10.749   1.686   7.821  1.00 22.58           C  
ANISOU  123  C   ASN A 224     1238   2439   4905     58    129   -155       C  
ATOM    124  O   ASN A 224       9.978   1.804   8.779  1.00 24.05           O  
ANISOU  124  O   ASN A 224     1580   2416   5143    236    745      9       O  
ATOM    125  CB  ASN A 224      11.038  -0.682   7.128  1.00 28.93           C  
ANISOU  125  CB  ASN A 224     2632   2800   5561   -159    951   -214       C  
ATOM    126  CG  ASN A 224      11.892  -1.931   7.156  1.00 35.66           C  
ANISOU  126  CG  ASN A 224     4065   3466   6019   -581    937   -159       C  
ATOM    127  OD1 ASN A 224      12.824  -2.078   6.364  1.00 37.21           O  
ANISOU  127  OD1 ASN A 224     4100   3715   6322   -408    790   -366       O  
ATOM    128  ND2 ASN A 224      11.569  -2.851   8.062  1.00 39.12           N  
ANISOU  128  ND2 ASN A 224     4885   3719   6259   -901    816   -276       N  
ATOM    129  N   ASN A 225      10.778   2.537   6.801  1.00 21.90           N  
ANISOU  129  N   ASN A 225     1212   2499   4611    245    -54   -342       N  
ATOM    130  CA  ASN A 225       9.824   3.650   6.697  1.00 21.79           C  
ANISOU  130  CA  ASN A 225     1253   2567   4460    342   -259   -584       C  
ATOM    131  C   ASN A 225       9.768   4.520   7.952  1.00 18.90           C  
ANISOU  131  C   ASN A 225     1167   2247   3766    470   -111   -532       C  
ATOM    132  O   ASN A 225       8.698   5.005   8.343  1.00 20.49           O  
ANISOU  132  O   ASN A 225     1089   2633   4063    255     74   -395       O  
ATOM    133  CB  ASN A 225       8.426   3.128   6.345  1.00 24.80           C  
ANISOU  133  CB  ASN A 225     1433   2890   5101   -242     62  -1097       C  
ATOM    134  CG  ASN A 225       8.400   2.380   5.029  1.00 31.80           C  
ANISOU  134  CG  ASN A 225     2937   3435   5710   -666    -75   -990       C  
ATOM    135  OD1 ASN A 225       8.865   2.883   4.004  1.00 35.55           O  
ANISOU  135  OD1 ASN A 225     3852   3658   5997   -468   -148   -993       O  
ATOM    136  ND2 ASN A 225       7.867   1.161   5.051  1.00 33.69           N  
ANISOU  136  ND2 ASN A 225     3520   3589   5690   -676   -158  -1253       N  
ATOM    137  N   THR A 226      10.921   4.710   8.587  1.00 18.32           N  
ANISOU  137  N   THR A 226     1120   2047   3792    363   -232   -529       N  
ATOM    138  CA  THR A 226      11.020   5.548   9.783  1.00 19.79           C  
ANISOU  138  CA  THR A 226     1735   2031   3755    191    201   -650       C  
ATOM    139  C   THR A 226      11.279   7.001   9.375  1.00 18.73           C  
ANISOU  139  C   THR A 226     1369   2182   3565    612    350   -476       C  
ATOM    140  O   THR A 226      11.589   7.271   8.215  1.00 18.63           O  
ANISOU  140  O   THR A 226      945   2523   3609    201    -28   -282       O  
ATOM    141  CB  THR A 226      12.173   5.079  10.697  1.00 17.88           C  
ANISOU  141  CB  THR A 226     1345   1871   3579      2     66   -242       C  
ATOM    142  OG1 THR A 226      13.431   5.496  10.144  1.00 17.95           O  
ANISOU  142  OG1 THR A 226     1185   1829   3806   -114    218   -353       O  
ATOM    143  CG2 THR A 226      12.155   3.560  10.877  1.00 20.25           C  
ANISOU  143  CG2 THR A 226     2272   1803   3618    -42    155   -364       C  
ATOM    144  N   PRO A 227      11.150   7.947  10.321  1.00 18.71           N  
ANISOU  144  N   PRO A 227     1448   2119   3542    235    880   -494       N  
ATOM    145  CA  PRO A 227      11.457   9.337   9.958  1.00 18.00           C  
ANISOU  145  CA  PRO A 227     1516   2033   3292    245    939   -492       C  
ATOM    146  C   PRO A 227      12.888   9.518   9.445  1.00 16.27           C  
ANISOU  146  C   PRO A 227     1029   2153   2998    255    466   -507       C  
ATOM    147  O   PRO A 227      13.146  10.447   8.685  1.00 17.24           O  
ANISOU  147  O   PRO A 227     1042   2386   3124    433    123   -322       O  
ATOM    148  CB  PRO A 227      11.242  10.089  11.272  1.00 17.97           C  
ANISOU  148  CB  PRO A 227     1447   1895   3487    -22   1056   -264       C  
ATOM    149  CG  PRO A 227      10.126   9.299  11.937  1.00 18.35           C  
ANISOU  149  CG  PRO A 227     1485   1857   3630     -8    967   -647       C  
ATOM    150  CD  PRO A 227      10.483   7.860  11.635  1.00 19.15           C  
ANISOU  150  CD  PRO A 227     1737   2007   3534    272    974   -654       C  
ATOM    151  N   PHE A 228      13.794   8.633   9.844  1.00 15.62           N  
ANISOU  151  N   PHE A 228      907   2104   2924    306    216   -459       N  
ATOM    152  CA  PHE A 228      15.173   8.717   9.361  1.00 16.18           C  
ANISOU  152  CA  PHE A 228     1003   2244   2901    527   -373   -187       C  
ATOM    153  C   PHE A 228      15.298   8.245   7.925  1.00 17.59           C  
ANISOU  153  C   PHE A 228     1084   2104   3495    378   -415   -449       C  
ATOM    154  O   PHE A 228      16.188   8.691   7.200  1.00 16.43           O  
ANISOU  154  O   PHE A 228      945   1930   3366    -37    271   -434       O  
ATOM    155  CB  PHE A 228      16.127   7.966  10.291  1.00 16.76           C  
ANISOU  155  CB  PHE A 228      908   2303   3159    341   -247   -208       C  
ATOM    156  CG  PHE A 228      16.205   8.580  11.650  1.00 17.76           C  
ANISOU  156  CG  PHE A 228     1014   2653   3080    156   -397   -438       C  
ATOM    157  CD1 PHE A 228      17.141   9.561  11.930  1.00 19.89           C  
ANISOU  157  CD1 PHE A 228     1704   2608   3246    232   -244   -400       C  
ATOM    158  CD2 PHE A 228      15.305   8.212  12.637  1.00 18.38           C  
ANISOU  158  CD2 PHE A 228      930   2896   3156    -36    280   -516       C  
ATOM    159  CE1 PHE A 228      17.190  10.149  13.181  1.00 20.69           C  
ANISOU  159  CE1 PHE A 228     2079   2629   3153    308   -417   -386       C  
ATOM    160  CE2 PHE A 228      15.347   8.793  13.883  1.00 21.99           C  
ANISOU  160  CE2 PHE A 228     1909   3074   3373    300     23   -751       C  
ATOM    161  CZ  PHE A 228      16.293   9.765  14.158  1.00 21.19           C  
ANISOU  161  CZ  PHE A 228     1915   2705   3433    481   -373   -851       C  
ATOM    162  N   HIS A 229      14.397   7.359   7.504  1.00 18.36           N  
ANISOU  162  N   HIS A 229     1235   1963   3778    302   -678   -628       N  
ATOM    163  CA  HIS A 229      14.365   6.952   6.107  1.00 18.71           C  
ANISOU  163  CA  HIS A 229     1264   1993   3851    104   -729   -698       C  
ATOM    164  C   HIS A 229      13.873   8.116   5.261  1.00 18.03           C  
ANISOU  164  C   HIS A 229     1172   1920   3759    371   -318   -736       C  
ATOM    165  O   HIS A 229      14.435   8.409   4.210  1.00 18.01           O  
ANISOU  165  O   HIS A 229     1181   2062   3599    178     -4   -651       O  
ATOM    166  CB  HIS A 229      13.481   5.725   5.898  1.00 18.55           C  
ANISOU  166  CB  HIS A 229     1098   1787   4163    -37     36   -756       C  
ATOM    167  CG  HIS A 229      14.047   4.467   6.475  1.00 19.30           C  
ANISOU  167  CG  HIS A 229     1196   1766   4371    -95    316   -855       C  
ATOM    168  ND1 HIS A 229      13.919   4.135   7.806  1.00 20.28           N  
ANISOU  168  ND1 HIS A 229     1354   1713   4638   -228    450   -928       N  
ATOM    169  CD2 HIS A 229      14.761   3.468   5.903  1.00 20.28           C  
ANISOU  169  CD2 HIS A 229     1522   1679   4506   -204    451  -1062       C  
ATOM    170  CE1 HIS A 229      14.520   2.977   8.027  1.00 20.24           C  
ANISOU  170  CE1 HIS A 229     1480   1704   4506     23    584   -928       C  
ATOM    171  NE2 HIS A 229      15.046   2.556   6.890  1.00 20.69           N  
ANISOU  171  NE2 HIS A 229     1623   1607   4630   -113    827   -917       N  
ATOM    172  N   ILE A 230      12.825   8.793   5.725  1.00 16.70           N  
ANISOU  172  N   ILE A 230     1087   1770   3487    367   -228   -588       N  
ATOM    173  CA  ILE A 230      12.368   9.989   5.029  1.00 16.74           C  
ANISOU  173  CA  ILE A 230     1002   1840   3520    172    171   -614       C  
ATOM    174  C   ILE A 230      13.481  11.035   4.981  1.00 16.97           C  
ANISOU  174  C   ILE A 230      970   1897   3580     98   -101   -696       C  
ATOM    175  O   ILE A 230      13.740  11.621   3.931  1.00 18.31           O  
ANISOU  175  O   ILE A 230     1266   1901   3789    446   -450   -696       O  
ATOM    176  CB  ILE A 230      11.114  10.604   5.677  1.00 18.97           C  
ANISOU  176  CB  ILE A 230     1174   1981   4052    103    429   -605       C  
ATOM    177  CG1 ILE A 230      10.056   9.528   5.927  1.00 21.11           C  
ANISOU  177  CG1 ILE A 230     1396   2389   4235   -502    161   -745       C  
ATOM    178  CG2 ILE A 230      10.566  11.724   4.795  1.00 19.55           C  
ANISOU  178  CG2 ILE A 230     1446   1890   4090    450    142   -441       C  
ATOM    179  CD1 ILE A 230       9.500   8.910   4.662  1.00 21.62           C  
ANISOU  179  CD1 ILE A 230     1606   2460   4147   -499    480   -705       C  
ATOM    180  N   LEU A 231      14.148  11.251   6.110  1.00 16.71           N  
ANISOU  180  N   LEU A 231      931   2049   3371     13    -62   -759       N  
ATOM    181  CA  LEU A 231      15.226  12.234   6.165  1.00 14.89           C  
ANISOU  181  CA  LEU A 231      845   2032   2781   -102    -73   -800       C  
ATOM    182  C   LEU A 231      16.318  11.866   5.156  1.00 16.19           C  
ANISOU  182  C   LEU A 231      985   1972   3195    150    194   -832       C  
ATOM    183  O   LEU A 231      16.814  12.725   4.427  1.00 16.57           O  
ANISOU  183  O   LEU A 231     1107   1886   3301    -51     42  -1016       O  
ATOM    184  CB  LEU A 231      15.813  12.316   7.571  1.00 16.09           C  
ANISOU  184  CB  LEU A 231     1235   2108   2769   -418   -431   -731       C  
ATOM    185  CG  LEU A 231      16.953  13.327   7.710  1.00 18.74           C  
ANISOU  185  CG  LEU A 231     1375   2464   3280    -77   -232   -916       C  
ATOM    186  CD1 LEU A 231      16.441  14.730   7.378  1.00 17.35           C  
ANISOU  186  CD1 LEU A 231     1024   2207   3360    139    -18  -1067       C  
ATOM    187  CD2 LEU A 231      17.531  13.265   9.106  1.00 19.79           C  
ANISOU  187  CD2 LEU A 231     1532   2805   3182   -414     -2   -618       C  
ATOM    188  N   ALA A 232      16.670  10.585   5.105  1.00 17.24           N  
ANISOU  188  N   ALA A 232     1077   1965   3508    184    137   -920       N  
ATOM    189  CA  ALA A 232      17.686  10.121   4.159  1.00 17.75           C  
ANISOU  189  CA  ALA A 232     1104   2052   3587    237    369   -564       C  
ATOM    190  C   ALA A 232      17.312  10.474   2.718  1.00 17.50           C  
ANISOU  190  C   ALA A 232      980   2270   3401     -4    290   -701       C  
ATOM    191  O   ALA A 232      18.153  10.923   1.934  1.00 18.89           O  
ANISOU  191  O   ALA A 232     1370   2343   3464    154   -113   -929       O  
ATOM    192  CB  ALA A 232      17.916   8.622   4.305  1.00 18.68           C  
ANISOU  192  CB  ALA A 232     1533   1881   3683    491    475   -167       C  
ATOM    193  N   GLN A 233      16.039  10.288   2.375  1.00 17.20           N  
ANISOU  193  N   GLN A 233     1032   2218   3286    176    268   -802       N  
ATOM    194  CA  GLN A 233      15.564  10.623   1.046  1.00 19.36           C  
ANISOU  194  CA  GLN A 233     1147   2472   3736   -224   -215   -899       C  
ATOM    195  C   GLN A 233      15.608  12.124   0.784  1.00 19.28           C  
ANISOU  195  C   GLN A 233     1228   2323   3775    197   -222  -1002       C  
ATOM    196  O   GLN A 233      16.039  12.563  -0.285  1.00 19.11           O  
ANISOU  196  O   GLN A 233     1173   2312   3777    -42   -195  -1130       O  
ATOM    197  CB  GLN A 233      14.137  10.102   0.850  1.00 20.57           C  
ANISOU  197  CB  GLN A 233     1554   2720   3542   -741   -521   -634       C  
ATOM    198  CG  GLN A 233      14.044   8.595   0.813  1.00 22.27           C  
ANISOU  198  CG  GLN A 233     1947   2831   3684   -860   -478   -974       C  
ATOM    199  CD  GLN A 233      12.615   8.115   0.647  1.00 27.41           C  
ANISOU  199  CD  GLN A 233     2551   3404   4460   -870   -547  -1291       C  
ATOM    200  OE1 GLN A 233      11.757   8.387   1.483  1.00 31.29           O  
ANISOU  200  OE1 GLN A 233     3318   3792   4778  -1160   -973  -1154       O  
ATOM    201  NE2 GLN A 233      12.351   7.410  -0.441  1.00 29.93           N  
ANISOU  201  NE2 GLN A 233     2879   3766   4729   -792   -644  -1356       N  
ATOM    202  N   VAL A 234      15.153  12.903   1.760  1.00 18.90           N  
ANISOU  202  N   VAL A 234     1363   2100   3718    313   -245   -929       N  
ATOM    203  CA  VAL A 234      15.117  14.359   1.633  1.00 17.76           C  
ANISOU  203  CA  VAL A 234     1085   2166   3497    378    -64   -713       C  
ATOM    204  C   VAL A 234      16.534  14.930   1.480  1.00 17.82           C  
ANISOU  204  C   VAL A 234     1143   2191   3435    258   -328   -669       C  
ATOM    205  O   VAL A 234      16.796  15.741   0.587  1.00 17.92           O  
ANISOU  205  O   VAL A 234     1090   2254   3465     35   -152   -629       O  
ATOM    206  CB  VAL A 234      14.378  15.003   2.823  1.00 16.85           C  
ANISOU  206  CB  VAL A 234      913   2234   3257     61   -297   -512       C  
ATOM    207  CG1 VAL A 234      14.549  16.502   2.814  1.00 18.57           C  
ANISOU  207  CG1 VAL A 234     1094   2226   3735    133    223   -513       C  
ATOM    208  CG2 VAL A 234      12.875  14.640   2.775  1.00 16.16           C  
ANISOU  208  CG2 VAL A 234      812   2314   3015   -140    -80   -368       C  
ATOM    209  N   LEU A 235      17.446  14.482   2.337  1.00 15.87           N  
ANISOU  209  N   LEU A 235      937   2182   2913    443   -172   -448       N  
ATOM    210  CA  LEU A 235      18.837  14.940   2.279  1.00 15.45           C  
ANISOU  210  CA  LEU A 235      874   2119   2878    156   -252   -728       C  
ATOM    211  C   LEU A 235      19.534  14.501   0.993  1.00 17.07           C  
ANISOU  211  C   LEU A 235     1379   2049   3059    347    -20   -634       C  
ATOM    212  O   LEU A 235      20.350  15.246   0.426  1.00 16.68           O  
ANISOU  212  O   LEU A 235     1330   1869   3139    284    186   -792       O  
ATOM    213  CB  LEU A 235      19.630  14.421   3.481  1.00 14.87           C  
ANISOU  213  CB  LEU A 235      835   2059   2755      4   -116   -820       C  
ATOM    214  CG  LEU A 235      19.239  14.882   4.889  1.00 16.26           C  
ANISOU  214  CG  LEU A 235     1450   2013   2714   -322   -302  -1022       C  
ATOM    215  CD1 LEU A 235      20.249  14.373   5.921  1.00 17.17           C  
ANISOU  215  CD1 LEU A 235     1474   2157   2894     77   -913   -809       C  
ATOM    216  CD2 LEU A 235      19.089  16.399   4.959  1.00 15.87           C  
ANISOU  216  CD2 LEU A 235     1257   2011   2763   -631    498   -881       C  
ATOM    217  N   SER A 236      19.230  13.287   0.543  1.00 15.74           N  
ANISOU  217  N   SER A 236     1476   1759   2746    120    298   -492       N  
ATOM    218  CA  SER A 236      19.870  12.752  -0.651  1.00 17.56           C  
ANISOU  218  CA  SER A 236     1641   1866   3165    -64    271   -878       C  
ATOM    219  C   SER A 236      19.518  13.597  -1.862  1.00 18.49           C  
ANISOU  219  C   SER A 236     1422   2088   3516   -101    160   -822       C  
ATOM    220  O   SER A 236      20.372  13.883  -2.698  1.00 17.99           O  
ANISOU  220  O   SER A 236     1038   2495   3304    134    198   -936       O  
ATOM    221  CB  SER A 236      19.467  11.297  -0.890  1.00 20.43           C  
ANISOU  221  CB  SER A 236     2511   1849   3405    322    773   -476       C  
ATOM    222  OG  SER A 236      20.047  10.448   0.080  1.00 22.19           O  
ANISOU  222  OG  SER A 236     2586   2055   3789    188    369   -483       O  
ATOM    223  N   LYS A 237      18.258  14.010  -1.951  1.00 19.20           N  
ANISOU  223  N   LYS A 237     1482   1979   3834     -1   -102   -914       N  
ATOM    224  CA  LYS A 237      17.829  14.819  -3.077  1.00 18.97           C  
ANISOU  224  CA  LYS A 237     1050   2327   3829     90    -62   -798       C  
ATOM    225  C   LYS A 237      18.516  16.186  -3.063  1.00 19.61           C  
ANISOU  225  C   LYS A 237     1622   2254   3574     -3   -199   -702       C  
ATOM    226  O   LYS A 237      18.987  16.667  -4.099  1.00 19.33           O  
ANISOU  226  O   LYS A 237     1560   2417   3367    -71     86   -664       O  
ATOM    227  CB  LYS A 237      16.311  14.991  -3.073  1.00 21.15           C  
ANISOU  227  CB  LYS A 237     1213   2898   3924    442   -378   -674       C  
ATOM    228  CG  LYS A 237      15.818  15.951  -4.140  1.00 27.60           C  
ANISOU  228  CG  LYS A 237     1694   3854   4938    553   -389   -671       C  
ATOM    229  CD  LYS A 237      14.308  15.939  -4.253  1.00 32.24           C  
ANISOU  229  CD  LYS A 237     2050   4503   5695    731   -902   -512       C  
ATOM    230  CE  LYS A 237      13.820  17.074  -5.139  1.00 36.82           C  
ANISOU  230  CE  LYS A 237     2877   4950   6163    739  -1016   -310       C  
ATOM    231  NZ  LYS A 237      12.334  17.060  -5.274  1.00 39.71           N  
ANISOU  231  NZ  LYS A 237     3429   5249   6411    691   -889   -402       N  
ATOM    232  N   ILE A 238      18.576  16.803  -1.886  1.00 17.32           N  
ANISOU  232  N   ILE A 238     1576   1798   3205    -25     33   -982       N  
ATOM    233  CA  ILE A 238      19.204  18.113  -1.746  1.00 17.58           C  
ANISOU  233  CA  ILE A 238     1506   2083   3091    141   -568  -1091       C  
ATOM    234  C   ILE A 238      20.700  18.027  -2.037  1.00 17.75           C  
ANISOU  234  C   ILE A 238     1491   2167   3086   -194   -652   -656       C  
ATOM    235  O   ILE A 238      21.241  18.855  -2.767  1.00 17.90           O  
ANISOU  235  O   ILE A 238     1753   2225   2822    -80   -311   -426       O  
ATOM    236  CB  ILE A 238      18.948  18.716  -0.355  1.00 18.22           C  
ANISOU  236  CB  ILE A 238     1333   2216   3373     22    -47  -1319       C  
ATOM    237  CG1 ILE A 238      17.452  18.986  -0.186  1.00 20.00           C  
ANISOU  237  CG1 ILE A 238     1629   2444   3527    345    272  -1388       C  
ATOM    238  CG2 ILE A 238      19.757  20.006  -0.157  1.00 17.56           C  
ANISOU  238  CG2 ILE A 238     1195   2126   3350    -59   -410  -1116       C  
ATOM    239  CD1 ILE A 238      17.037  19.182   1.244  1.00 21.51           C  
ANISOU  239  CD1 ILE A 238     1931   2458   3784   -276    621  -1468       C  
ATOM    240  N   ALA A 239      21.358  17.007  -1.493  1.00 18.10           N  
ANISOU  240  N   ALA A 239     1403   2238   3236   -103   -409   -802       N  
ATOM    241  CA  ALA A 239      22.785  16.825  -1.746  1.00 17.47           C  
ANISOU  241  CA  ALA A 239     1162   2378   3099    221   -204   -547       C  
ATOM    242  C   ALA A 239      23.035  16.644  -3.234  1.00 19.24           C  
ANISOU  242  C   ALA A 239     1710   2577   3025    -42   -436   -397       C  
ATOM    243  O   ALA A 239      23.928  17.278  -3.798  1.00 19.06           O  
ANISOU  243  O   ALA A 239     1560   2897   2785    -82     74   -356       O  
ATOM    244  CB  ALA A 239      23.334  15.641  -0.961  1.00 19.63           C  
ANISOU  244  CB  ALA A 239     1623   2626   3209     -7   -232   -399       C  
ATOM    245  N   TYR A 240      22.235  15.791  -3.873  1.00 18.76           N  
ANISOU  245  N   TYR A 240     1868   2533   2726    -84   -472   -538       N  
ATOM    246  CA  TYR A 240      22.384  15.551  -5.302  1.00 18.67           C  
ANISOU  246  CA  TYR A 240     1877   2573   2644   -791    -87   -801       C  
ATOM    247  C   TYR A 240      22.265  16.843  -6.112  1.00 18.54           C  
ANISOU  247  C   TYR A 240     1743   2679   2620   -596   -199   -344       C  
ATOM    248  O   TYR A 240      23.107  17.122  -6.963  1.00 19.73           O  
ANISOU  248  O   TYR A 240     2009   2697   2788   -905     74   -422       O  
ATOM    249  CB  TYR A 240      21.359  14.530  -5.816  1.00 20.51           C  
ANISOU  249  CB  TYR A 240     2324   2902   2567   -936    -72  -1171       C  
ATOM    250  CG  TYR A 240      21.518  14.277  -7.293  1.00 26.86           C  
ANISOU  250  CG  TYR A 240     3789   3458   2958  -1286    369  -1370       C  
ATOM    251  CD1 TYR A 240      22.465  13.369  -7.761  1.00 30.72           C  
ANISOU  251  CD1 TYR A 240     4647   3831   3193  -1165    548  -1479       C  
ATOM    252  CD2 TYR A 240      20.742  14.958  -8.224  1.00 29.06           C  
ANISOU  252  CD2 TYR A 240     4401   3646   2994  -1409    618  -1303       C  
ATOM    253  CE1 TYR A 240      22.629  13.146  -9.113  1.00 34.42           C  
ANISOU  253  CE1 TYR A 240     5465   4018   3594  -1292    218  -1573       C  
ATOM    254  CE2 TYR A 240      20.896  14.736  -9.580  1.00 33.12           C  
ANISOU  254  CE2 TYR A 240     5358   3881   3345  -1454    257  -1387       C  
ATOM    255  CZ  TYR A 240      21.840  13.831 -10.018  1.00 36.00           C  
ANISOU  255  CZ  TYR A 240     5927   4182   3569  -1341    167  -1481       C  
ATOM    256  OH  TYR A 240      21.996  13.612 -11.364  1.00 39.86           O  
ANISOU  256  OH  TYR A 240     6665   4587   3892  -1192    -82  -1697       O  
ATOM    257  N   LYS A 241      21.223  17.629  -5.837  1.00 18.60           N  
ANISOU  257  N   LYS A 241     1669   2576   2823   -371   -409   -274       N  
ATOM    258  CA  LYS A 241      20.962  18.848  -6.599  1.00 20.23           C  
ANISOU  258  CA  LYS A 241     1560   2810   3318   -450   -638   -344       C  
ATOM    259  C   LYS A 241      22.030  19.912  -6.377  1.00 20.19           C  
ANISOU  259  C   LYS A 241     1709   2767   3196   -285   -465   -466       C  
ATOM    260  O   LYS A 241      22.194  20.818  -7.195  1.00 21.14           O  
ANISOU  260  O   LYS A 241     2250   2734   3048   -608   -427   -350       O  
ATOM    261  CB  LYS A 241      19.594  19.420  -6.239  1.00 21.85           C  
ANISOU  261  CB  LYS A 241     1312   3202   3788   -305   -842     19       C  
ATOM    262  CG  LYS A 241      18.425  18.630  -6.808  1.00 27.61           C  
ANISOU  262  CG  LYS A 241     1847   3858   4785    -62   -734     58       C  
ATOM    263  CD  LYS A 241      17.114  19.108  -6.217  1.00 35.32           C  
ANISOU  263  CD  LYS A 241     3700   4266   5456    -30   -225    224       C  
ATOM    264  CE  LYS A 241      16.934  20.607  -6.405  1.00 40.65           C  
ANISOU  264  CE  LYS A 241     5175   4551   5720   -784    155    342       C  
ATOM    265  NZ  LYS A 241      16.678  20.998  -7.820  1.00 42.06           N  
ANISOU  265  NZ  LYS A 241     5496   4766   5717  -1355    710    497       N  
ATOM    266  N   SER A 242      22.751  19.796  -5.267  1.00 19.64           N  
ANISOU  266  N   SER A 242     1423   2878   3161    -95   -599   -519       N  
ATOM    267  CA  SER A 242      23.785  20.764  -4.910  1.00 19.36           C  
ANISOU  267  CA  SER A 242     1330   2965   3061   -755   -269   -624       C  
ATOM    268  C   SER A 242      25.146  20.367  -5.467  1.00 21.09           C  
ANISOU  268  C   SER A 242     1812   3016   3183   -556   -359   -257       C  
ATOM    269  O   SER A 242      26.141  21.059  -5.236  1.00 23.18           O  
ANISOU  269  O   SER A 242     2051   3111   3645   -729   -529    -76       O  
ATOM    270  CB  SER A 242      23.892  20.888  -3.392  1.00 22.18           C  
ANISOU  270  CB  SER A 242     1964   3384   3079   -786    485  -1078       C  
ATOM    271  OG  SER A 242      22.636  21.213  -2.820  1.00 26.06           O  
ANISOU  271  OG  SER A 242     2817   3637   3447   -567    103   -811       O  
ATOM    272  N   GLY A 243      25.191  19.253  -6.191  1.00 21.96           N  
ANISOU  272  N   GLY A 243     2185   2824   3335   -332   -397   -193       N  
ATOM    273  CA  GLY A 243      26.437  18.766  -6.761  1.00 21.59           C  
ANISOU  273  CA  GLY A 243     1677   2983   3543    -31   -199   -252       C  
ATOM    274  C   GLY A 243      27.336  18.151  -5.706  1.00 22.33           C  
ANISOU  274  C   GLY A 243     1432   3260   3794    139   -345   -221       C  
ATOM    275  O   GLY A 243      28.563  18.052  -5.883  1.00 25.02           O  
ANISOU  275  O   GLY A 243     2017   3467   4024    351   -186    110       O  
ATOM    276  N   LYS A 244      26.727  17.723  -4.603  1.00 23.73           N  
ANISOU  276  N   LYS A 244     2101   3264   3651    539   -437   -467       N  
ATOM    277  CA  LYS A 244      27.491  17.237  -3.458  1.00 24.14           C  
ANISOU  277  CA  LYS A 244     2236   3423   3512    462   -520   -883       C  
ATOM    278  C   LYS A 244      27.101  15.858  -2.936  1.00 26.04           C  
ANISOU  278  C   LYS A 244     2800   3562   3532    867   -196   -788       C  
ATOM    279  O   LYS A 244      27.330  15.562  -1.764  1.00 24.96           O  
ANISOU  279  O   LYS A 244     2421   3708   3354   1034     17   -713       O  
ATOM    280  CB  LYS A 244      27.378  18.228  -2.312  1.00 25.25           C  
ANISOU  280  CB  LYS A 244     2671   3402   3522     26   -943   -964       C  
ATOM    281  CG  LYS A 244      28.093  19.507  -2.567  1.00 24.98           C  
ANISOU  281  CG  LYS A 244     2550   3201   3740    -70   -570   -988       C  
ATOM    282  CD  LYS A 244      28.474  20.132  -1.258  1.00 25.91           C  
ANISOU  282  CD  LYS A 244     2812   3165   3869    -36     58  -1138       C  
ATOM    283  CE  LYS A 244      29.254  21.383  -1.496  1.00 25.56           C  
ANISOU  283  CE  LYS A 244     2739   3014   3959   -408    381   -628       C  
ATOM    284  NZ  LYS A 244      29.884  21.898  -0.257  1.00 25.32           N  
ANISOU  284  NZ  LYS A 244     3229   2924   3467   -590     71   -765       N  
ATOM    285  N   SER A 245      26.519  15.019  -3.785  1.00 26.15           N  
ANISOU  285  N   SER A 245     2703   3557   3674    947   -178   -758       N  
ATOM    286  CA  SER A 245      26.154  13.674  -3.353  1.00 26.15           C  
ANISOU  286  CA  SER A 245     2693   3571   3672    911    214   -771       C  
ATOM    287  C   SER A 245      27.384  12.910  -2.853  1.00 23.90           C  
ANISOU  287  C   SER A 245     1877   3647   3555    665    732   -493       C  
ATOM    288  O   SER A 245      27.342  12.275  -1.805  1.00 23.96           O  
ANISOU  288  O   SER A 245     2147   3412   3543    775    353   -547       O  
ATOM    289  CB  SER A 245      25.462  12.908  -4.480  1.00 31.19           C  
ANISOU  289  CB  SER A 245     3928   3778   4145    985     46   -686       C  
ATOM    290  OG  SER A 245      26.288  12.844  -5.622  1.00 33.73           O  
ANISOU  290  OG  SER A 245     4553   3908   4356   1078    -83   -821       O  
ATOM    291  N   GLY A 246      28.483  12.995  -3.598  1.00 25.22           N  
ANISOU  291  N   GLY A 246     1999   3811   3774    900    478   -376       N  
ATOM    292  CA  GLY A 246      29.719  12.344  -3.203  1.00 25.59           C  
ANISOU  292  CA  GLY A 246     2175   3701   3847    906    902   -288       C  
ATOM    293  C   GLY A 246      30.264  12.849  -1.881  1.00 23.57           C  
ANISOU  293  C   GLY A 246     1652   3438   3865    668   1010   -140       C  
ATOM    294  O   GLY A 246      30.599  12.058  -1.003  1.00 26.05           O  
ANISOU  294  O   GLY A 246     2306   3509   4085    595   1020    -40       O  
ATOM    295  N   ALA A 247      30.350  14.168  -1.732  1.00 23.87           N  
ANISOU  295  N   ALA A 247     1968   3174   3928    390    671   -116       N  
ATOM    296  CA  ALA A 247      30.868  14.759  -0.501  1.00 22.82           C  
ANISOU  296  CA  ALA A 247     1958   2848   3864    228    799   -133       C  
ATOM    297  C   ALA A 247      29.981  14.429   0.699  1.00 21.89           C  
ANISOU  297  C   ALA A 247     1582   2540   4195    142    793    -11       C  
ATOM    298  O   ALA A 247      30.475  14.228   1.802  1.00 20.85           O  
ANISOU  298  O   ALA A 247     1233   2566   4122    187    663    188       O  
ATOM    299  CB  ALA A 247      31.026  16.261  -0.648  1.00 22.90           C  
ANISOU  299  CB  ALA A 247     2063   2913   3723    204    115   -249       C  
ATOM    300  N   PHE A 248      28.668  14.400   0.482  1.00 20.49           N  
ANISOU  300  N   PHE A 248     1387   2463   3936    324    788   -332       N  
ATOM    301  CA  PHE A 248      27.740  14.020   1.535  1.00 18.90           C  
ANISOU  301  CA  PHE A 248     1236   2132   3814    287    518   -494       C  
ATOM    302  C   PHE A 248      27.966  12.574   1.976  1.00 20.39           C  
ANISOU  302  C   PHE A 248     1509   2207   4032    331    668   -719       C  
ATOM    303  O   PHE A 248      28.047  12.290   3.171  1.00 20.58           O  
ANISOU  303  O   PHE A 248     1441   2296   4083    -30    832   -851       O  
ATOM    304  CB  PHE A 248      26.298  14.229   1.059  1.00 20.83           C  
ANISOU  304  CB  PHE A 248     1357   2274   4283    280    443   -742       C  
ATOM    305  CG  PHE A 248      25.259  13.705   2.004  1.00 21.73           C  
ANISOU  305  CG  PHE A 248     1477   2294   4484   -470    628   -939       C  
ATOM    306  CD1 PHE A 248      25.113  14.242   3.269  1.00 22.05           C  
ANISOU  306  CD1 PHE A 248     1649   2300   4427   -427   1026  -1056       C  
ATOM    307  CD2 PHE A 248      24.406  12.693   1.610  1.00 26.30           C  
ANISOU  307  CD2 PHE A 248     2549   2564   4881  -1034   1291   -728       C  
ATOM    308  CE1 PHE A 248      24.148  13.767   4.130  1.00 23.99           C  
ANISOU  308  CE1 PHE A 248     2125   2369   4620   -881    989   -836       C  
ATOM    309  CE2 PHE A 248      23.434  12.211   2.468  1.00 28.88           C  
ANISOU  309  CE2 PHE A 248     3425   2523   5024  -1120   1525   -543       C  
ATOM    310  CZ  PHE A 248      23.307  12.748   3.728  1.00 26.08           C  
ANISOU  310  CZ  PHE A 248     2955   2328   4627   -939   1579   -846       C  
ATOM    311  N   LEU A 249      28.080  11.666   1.010  1.00 20.11           N  
ANISOU  311  N   LEU A 249     1425   2250   3967    386    517   -720       N  
ATOM    312  CA  LEU A 249      28.337  10.268   1.334  1.00 20.38           C  
ANISOU  312  CA  LEU A 249     1653   2086   4005    202    633  -1084       C  
ATOM    313  C   LEU A 249      29.663  10.102   2.086  1.00 17.56           C  
ANISOU  313  C   LEU A 249     1018   2134   3518    -46    378   -670       C  
ATOM    314  O   LEU A 249      29.743   9.354   3.063  1.00 18.43           O  
ANISOU  314  O   LEU A 249     1088   2271   3646    -91    368   -901       O  
ATOM    315  CB  LEU A 249      28.318   9.389   0.076  1.00 21.14           C  
ANISOU  315  CB  LEU A 249     1761   2251   4019     83    690  -1316       C  
ATOM    316  CG  LEU A 249      28.476   7.897   0.374  1.00 22.28           C  
ANISOU  316  CG  LEU A 249     1464   2711   4289     59    416  -1482       C  
ATOM    317  CD1 LEU A 249      27.330   7.384   1.254  1.00 22.12           C  
ANISOU  317  CD1 LEU A 249     1364   2762   4280    -83    503  -1260       C  
ATOM    318  CD2 LEU A 249      28.577   7.098  -0.912  1.00 24.60           C  
ANISOU  318  CD2 LEU A 249     1960   2919   4467    230   -248  -1471       C  
ATOM    319  N   ASP A 250      30.699  10.811   1.637  1.00 17.03           N  
ANISOU  319  N   ASP A 250      826   2432   3211    -77     56   -250       N  
ATOM    320  CA  ASP A 250      32.001  10.739   2.304  1.00 18.58           C  
ANISOU  320  CA  ASP A 250      926   2687   3447    109    302   -194       C  
ATOM    321  C   ASP A 250      31.932  11.277   3.742  1.00 17.87           C  
ANISOU  321  C   ASP A 250      946   2310   3532    148    245   -267       C  
ATOM    322  O   ASP A 250      32.542  10.716   4.651  1.00 15.89           O  
ANISOU  322  O   ASP A 250      957   1817   3265    199    -60   -149       O  
ATOM    323  CB  ASP A 250      33.062  11.486   1.494  1.00 22.36           C  
ANISOU  323  CB  ASP A 250     1327   3062   4108     92    837   -117       C  
ATOM    324  CG  ASP A 250      33.329  10.842   0.136  1.00 25.24           C  
ANISOU  324  CG  ASP A 250     1384   3312   4896    -50    676     88       C  
ATOM    325  OD1 ASP A 250      33.076   9.628  -0.018  1.00 26.51           O  
ANISOU  325  OD1 ASP A 250     1905   3272   4896    172    563   -295       O  
ATOM    326  OD2 ASP A 250      33.817  11.548  -0.777  1.00 26.79           O  
ANISOU  326  OD2 ASP A 250     1398   3639   5142     20    522    393       O  
ATOM    327  N   ALA A 251      31.149  12.340   3.945  1.00 17.69           N  
ANISOU  327  N   ALA A 251     1158   1993   3571    -35    733   -235       N  
ATOM    328  CA  ALA A 251      30.993  12.946   5.263  1.00 17.28           C  
ANISOU  328  CA  ALA A 251     1028   1877   3659     69    440   -283       C  
ATOM    329  C   ALA A 251      30.229  12.002   6.179  1.00 16.72           C  
ANISOU  329  C   ALA A 251     1066   1583   3705   -179    457   -446       C  
ATOM    330  O   ALA A 251      30.562  11.834   7.349  1.00 16.74           O  
ANISOU  330  O   ALA A 251     1064   1702   3596   -265    304   -684       O  
ATOM    331  CB  ALA A 251      30.261  14.281   5.154  1.00 17.84           C  
ANISOU  331  CB  ALA A 251     1051   2042   3684    122     40   -360       C  
ATOM    332  N   PHE A 252      29.193  11.385   5.620  1.00 14.77           N  
ANISOU  332  N   PHE A 252      952   1507   3153   -323     80   -293       N  
ATOM    333  CA  PHE A 252      28.420  10.383   6.332  1.00 15.73           C  
ANISOU  333  CA  PHE A 252      927   1688   3363   -191    -67   -448       C  
ATOM    334  C   PHE A 252      29.318   9.221   6.763  1.00 15.66           C  
ANISOU  334  C   PHE A 252      910   1625   3416    146     -7   -434       C  
ATOM    335  O   PHE A 252      29.301   8.810   7.919  1.00 17.74           O  
ANISOU  335  O   PHE A 252     1021   1842   3876    100   -279   -315       O  
ATOM    336  CB  PHE A 252      27.277   9.904   5.431  1.00 15.33           C  
ANISOU  336  CB  PHE A 252      990   1751   3084   -175   -466   -404       C  
ATOM    337  CG  PHE A 252      26.473   8.758   5.996  1.00 16.98           C  
ANISOU  337  CG  PHE A 252      939   1920   3593   -143    -66   -322       C  
ATOM    338  CD1 PHE A 252      25.483   8.977   6.949  1.00 16.60           C  
ANISOU  338  CD1 PHE A 252      898   2096   3313   -223    246   -104       C  
ATOM    339  CD2 PHE A 252      26.675   7.463   5.532  1.00 19.44           C  
ANISOU  339  CD2 PHE A 252     1590   1908   3886   -681     40   -558       C  
ATOM    340  CE1 PHE A 252      24.742   7.912   7.454  1.00 16.02           C  
ANISOU  340  CE1 PHE A 252      959   1958   3169     97    485   -323       C  
ATOM    341  CE2 PHE A 252      25.925   6.395   6.028  1.00 19.65           C  
ANISOU  341  CE2 PHE A 252     1146   2250   4070   -198    423   -510       C  
ATOM    342  CZ  PHE A 252      24.955   6.621   6.985  1.00 19.71           C  
ANISOU  342  CZ  PHE A 252     1280   2414   3796   -106    536   -437       C  
ATOM    343  N   HIS A 253      30.109   8.706   5.832  1.00 15.83           N  
ANISOU  343  N   HIS A 253      903   1877   3235    215    122   -421       N  
ATOM    344  CA  HIS A 253      31.007   7.597   6.148  1.00 16.14           C  
ANISOU  344  CA  HIS A 253      983   1838   3312    209    188   -618       C  
ATOM    345  C   HIS A 253      32.009   7.975   7.232  1.00 18.40           C  
ANISOU  345  C   HIS A 253     1135   1969   3886     80    349   -778       C  
ATOM    346  O   HIS A 253      32.362   7.158   8.089  1.00 19.79           O  
ANISOU  346  O   HIS A 253     1113   2199   4206   -176    141   -507       O  
ATOM    347  CB  HIS A 253      31.744   7.125   4.891  1.00 16.35           C  
ANISOU  347  CB  HIS A 253     1115   1691   3406     73    398   -851       C  
ATOM    348  CG  HIS A 253      30.903   6.302   3.971  1.00 18.29           C  
ANISOU  348  CG  HIS A 253     1202   1720   4025   -143    406  -1163       C  
ATOM    349  ND1 HIS A 253      31.272   6.023   2.673  1.00 22.08           N  
ANISOU  349  ND1 HIS A 253     1544   2082   4763    -58    132   -998       N  
ATOM    350  CD2 HIS A 253      29.716   5.675   4.167  1.00 19.95           C  
ANISOU  350  CD2 HIS A 253     1245   2041   4295   -149    138  -1235       C  
ATOM    351  CE1 HIS A 253      30.347   5.268   2.106  1.00 22.48           C  
ANISOU  351  CE1 HIS A 253     1725   2109   4709   -500    396  -1213       C  
ATOM    352  NE2 HIS A 253      29.390   5.045   2.991  1.00 22.02           N  
ANISOU  352  NE2 HIS A 253     1799   2082   4487   -567    450  -1213       N  
ATOM    353  N   GLN A 254      32.472   9.217   7.188  1.00 15.23           N  
ANISOU  353  N   GLN A 254      905   1614   3266    -93      8   -744       N  
ATOM    354  CA  GLN A 254      33.423   9.691   8.193  1.00 16.06           C  
ANISOU  354  CA  GLN A 254      899   2037   3164   -304     24   -376       C  
ATOM    355  C   GLN A 254      32.807   9.621   9.585  1.00 16.19           C  
ANISOU  355  C   GLN A 254      889   2014   3248    -97     44   -639       C  
ATOM    356  O   GLN A 254      33.424   9.134  10.529  1.00 18.84           O  
ANISOU  356  O   GLN A 254     1140   2238   3779    171    -82   -391       O  
ATOM    357  CB  GLN A 254      33.875  11.121   7.902  1.00 15.73           C  
ANISOU  357  CB  GLN A 254      855   2104   3016   -323    107   -263       C  
ATOM    358  CG  GLN A 254      34.854  11.660   8.934  1.00 17.46           C  
ANISOU  358  CG  GLN A 254      896   2370   3369     59     84   -470       C  
ATOM    359  CD  GLN A 254      36.149  10.876   8.940  1.00 22.39           C  
ANISOU  359  CD  GLN A 254     1578   2765   4165   -242   -195   -474       C  
ATOM    360  OE1 GLN A 254      36.546  10.317   7.917  1.00 21.98           O  
ANISOU  360  OE1 GLN A 254     1176   2846   4327    -83   -401   -384       O  
ATOM    361  NE2 GLN A 254      36.806  10.817  10.093  1.00 25.01           N  
ANISOU  361  NE2 GLN A 254     2287   2965   4249   -177     92   -361       N  
ATOM    362  N   ILE A 255      31.568  10.088   9.703  1.00 14.85           N  
ANISOU  362  N   ILE A 255      774   1789   3080     28    -33   -126       N  
ATOM    363  CA  ILE A 255      30.909  10.099  10.997  1.00 15.68           C  
ANISOU  363  CA  ILE A 255      869   1778   3308    -38    239   -290       C  
ATOM    364  C   ILE A 255      30.681   8.675  11.516  1.00 17.71           C  
ANISOU  364  C   ILE A 255     1043   2042   3644   -205    273   -374       C  
ATOM    365  O   ILE A 255      30.910   8.400  12.698  1.00 19.13           O  
ANISOU  365  O   ILE A 255     1052   2368   3849   -208    276   -462       O  
ATOM    366  CB  ILE A 255      29.594  10.893  10.942  1.00 15.02           C  
ANISOU  366  CB  ILE A 255      856   1829   3021    301    110   -158       C  
ATOM    367  CG1 ILE A 255      29.893  12.349  10.572  1.00 17.14           C  
ANISOU  367  CG1 ILE A 255     1699   1925   2890   1012     79   -299       C  
ATOM    368  CG2 ILE A 255      28.889  10.845  12.282  1.00 16.54           C  
ANISOU  368  CG2 ILE A 255     1311   1866   3106    121    216    390       C  
ATOM    369  CD1 ILE A 255      28.668  13.183  10.257  1.00 18.38           C  
ANISOU  369  CD1 ILE A 255     1982   2072   2931    795    -49   -348       C  
ATOM    370  N   LEU A 256      30.251   7.773  10.633  1.00 16.60           N  
ANISOU  370  N   LEU A 256      950   1756   3599    -73    176   -515       N  
ATOM    371  CA  LEU A 256      30.100   6.365  10.996  1.00 18.91           C  
ANISOU  371  CA  LEU A 256     1059   2348   3778   -194   -402   -213       C  
ATOM    372  C   LEU A 256      31.404   5.782  11.533  1.00 19.51           C  
ANISOU  372  C   LEU A 256     1150   2341   3919    398   -350      3       C  
ATOM    373  O   LEU A 256      31.392   4.988  12.473  1.00 17.84           O  
ANISOU  373  O   LEU A 256     1129   1866   3782     81   -104    238       O  
ATOM    374  CB  LEU A 256      29.649   5.528   9.797  1.00 19.87           C  
ANISOU  374  CB  LEU A 256     1119   2756   3676      6   -623   -292       C  
ATOM    375  CG  LEU A 256      28.223   5.739   9.290  1.00 24.96           C  
ANISOU  375  CG  LEU A 256     1956   3168   4362   -372   -540   -541       C  
ATOM    376  CD1 LEU A 256      27.796   4.584   8.406  1.00 25.54           C  
ANISOU  376  CD1 LEU A 256     2352   2911   4441   -577   -897   -691       C  
ATOM    377  CD2 LEU A 256      27.278   5.883  10.452  1.00 26.22           C  
ANISOU  377  CD2 LEU A 256     2133   3446   4381   -643    379   -294       C  
ATOM    378  N   SER A 257      32.522   6.188  10.938  1.00 21.01           N  
ANISOU  378  N   SER A 257     1121   2681   4180     -1   -340    434       N  
ATOM    379  CA  SER A 257      33.823   5.622  11.306  1.00 23.78           C  
ANISOU  379  CA  SER A 257     1300   3028   4708    248   -332    514       C  
ATOM    380  C   SER A 257      34.256   6.085  12.690  1.00 24.46           C  
ANISOU  380  C   SER A 257     1317   3336   4641    410   -252    492       C  
ATOM    381  O   SER A 257      35.155   5.498  13.305  1.00 28.67           O  
ANISOU  381  O   SER A 257     1596   3798   5499    560   -186    669       O  
ATOM    382  CB  SER A 257      34.890   5.976  10.271  1.00 24.26           C  
ANISOU  382  CB  SER A 257     1286   2961   4971     25    128    571       C  
ATOM    383  OG  SER A 257      35.360   7.303  10.445  1.00 26.58           O  
ANISOU  383  OG  SER A 257     1733   3094   5273   -221   -365    358       O  
ATOM    384  N   GLU A 258      33.608   7.137  13.179  1.00 26.00           N  
ANISOU  384  N   GLU A 258     1359   3383   5136    214   -129    573       N  
ATOM    385  CA  GLU A 258      33.892   7.666  14.503  1.00 28.20           C  
ANISOU  385  CA  GLU A 258     1895   3642   5179    167   -286    771       C  
ATOM    386  C   GLU A 258      32.976   7.056  15.570  1.00 29.22           C  
ANISOU  386  C   GLU A 258     2118   3633   5351    115   -738   1072       C  
ATOM    387  O   GLU A 258      32.999   7.459  16.727  1.00 33.95           O  
ANISOU  387  O   GLU A 258     3282   4016   5600    -56   -571    889       O  
ATOM    388  CB  GLU A 258      33.821   9.195  14.478  1.00 28.32           C  
ANISOU  388  CB  GLU A 258     2100   3805   4855    304   -375    511       C  
ATOM    389  CG  GLU A 258      34.829   9.788  13.494  1.00 28.28           C  
ANISOU  389  CG  GLU A 258     1995   3763   4985    185   -158    495       C  
ATOM    390  CD  GLU A 258      34.734  11.298  13.339  1.00 33.05           C  
ANISOU  390  CD  GLU A 258     3205   4118   5234    270    247    126       C  
ATOM    391  OE1 GLU A 258      33.919  11.935  14.041  1.00 38.41           O  
ANISOU  391  OE1 GLU A 258     4584   4412   5597    576    556     84       O  
ATOM    392  OE2 GLU A 258      35.484  11.847  12.503  1.00 31.18           O  
ANISOU  392  OE2 GLU A 258     2812   4024   5011    -17    -81   -129       O  
ATOM    393  N   GLY A 259      32.176   6.073  15.177  1.00 28.40           N  
ANISOU  393  N   GLY A 259     1878   3453   5460    302   -481   1493       N  
ATOM    394  CA  GLY A 259      31.396   5.318  16.143  1.00 32.33           C  
ANISOU  394  CA  GLY A 259     2971   3648   5667    -77    -81   1181       C  
ATOM    395  C   GLY A 259      29.944   5.740  16.245  1.00 32.86           C  
ANISOU  395  C   GLY A 259     3267   3657   5561   -278   -137   1172       C  
ATOM    396  O   GLY A 259      29.145   5.137  16.974  1.00 35.00           O  
ANISOU  396  O   GLY A 259     3549   3999   5751   -165   -251   1358       O  
ATOM    397  N   GLU A 260      29.589   6.787  15.522  1.00 26.80           N  
ANISOU  397  N   GLU A 260     2010   3185   4988     27     65    850       N  
ATOM    398  CA  GLU A 260      28.208   7.211  15.502  1.00 25.84           C  
ANISOU  398  CA  GLU A 260     1521   3637   4659   -507   -460    -48       C  
ATOM    399  C   GLU A 260      27.473   6.316  14.530  1.00 26.22           C  
ANISOU  399  C   GLU A 260     1572   4036   4354   -744   -403   -765       C  
ATOM    400  O   GLU A 260      28.001   5.967  13.476  1.00 30.91           O  
ANISOU  400  O   GLU A 260     2079   4833   4833  -1117   -343  -1155       O  
ATOM    401  CB  GLU A 260      28.100   8.652  15.039  1.00 27.35           C  
ANISOU  401  CB  GLU A 260     1400   3990   5004    629    -36    106       C  
ATOM    402  CG  GLU A 260      28.781   9.642  15.935  1.00 29.28           C  
ANISOU  402  CG  GLU A 260     1572   4473   5081    978    -44     68       C  
ATOM    403  CD  GLU A 260      28.250  11.055  15.746  1.00 33.11           C  
ANISOU  403  CD  GLU A 260     2075   4837   5669    546    108    302       C  
ATOM    404  OE1 GLU A 260      27.085  11.211  15.309  1.00 31.67           O  
ANISOU  404  OE1 GLU A 260     1516   5105   5410     97    690    149       O  
ATOM    405  OE2 GLU A 260      29.002  12.008  16.036  1.00 35.33           O  
ANISOU  405  OE2 GLU A 260     2220   5100   6105    281     11    141       O  
ATOM    406  N   ASN A 261      26.261   5.925  14.885  1.00 20.04           N  
ANISOU  406  N   ASN A 261     1129   2988   3496   -565    241   -461       N  
ATOM    407  CA  ASN A 261      25.432   5.192  13.943  1.00 18.66           C  
ANISOU  407  CA  ASN A 261      948   2839   3305    380   -108   -315       C  
ATOM    408  C   ASN A 261      24.622   6.151  13.071  1.00 18.79           C  
ANISOU  408  C   ASN A 261     1086   2580   3475    140    153   -517       C  
ATOM    409  O   ASN A 261      24.675   7.365  13.260  1.00 18.93           O  
ANISOU  409  O   ASN A 261     1576   2331   3285   -286    355   -300       O  
ATOM    410  CB  ASN A 261      24.544   4.186  14.667  1.00 20.54           C  
ANISOU  410  CB  ASN A 261     1137   2982   3686    538     94   -272       C  
ATOM    411  CG  ASN A 261      25.326   3.012  15.218  1.00 26.67           C  
ANISOU  411  CG  ASN A 261     2724   3363   4047    990    772   -336       C  
ATOM    412  OD1 ASN A 261      26.440   2.718  14.767  1.00 29.13           O  
ANISOU  412  OD1 ASN A 261     3189   3311   4567   1439    613   -477       O  
ATOM    413  ND2 ASN A 261      24.743   2.321  16.189  1.00 29.83           N  
ANISOU  413  ND2 ASN A 261     3617   3539   4178    975    400   -255       N  
ATOM    414  N   ALA A 262      23.879   5.600  12.119  1.00 18.15           N  
ANISOU  414  N   ALA A 262     1002   2469   3425    177     16   -822       N  
ATOM    415  CA  ALA A 262      23.345   6.390  11.020  1.00 15.70           C  
ANISOU  415  CA  ALA A 262      902   2020   3043    -54    225   -812       C  
ATOM    416  C   ALA A 262      22.267   7.408  11.421  1.00 15.19           C  
ANISOU  416  C   ALA A 262      864   1939   2967    -46    321   -566       C  
ATOM    417  O   ALA A 262      22.186   8.475  10.819  1.00 18.44           O  
ANISOU  417  O   ALA A 262     1402   1742   3861   -244    461   -879       O  
ATOM    418  CB  ALA A 262      22.842   5.486   9.902  1.00 16.77           C  
ANISOU  418  CB  ALA A 262     1456   1886   3030   -497   -142   -952       C  
ATOM    419  N   GLN A 263      21.443   7.085  12.416  1.00 15.09           N  
ANISOU  419  N   GLN A 263      907   2021   2806    -94    497   -477       N  
ATOM    420  CA  GLN A 263      20.391   8.028  12.809  1.00 15.10           C  
ANISOU  420  CA  GLN A 263      943   2014   2780   -354    483   -312       C  
ATOM    421  C   GLN A 263      20.997   9.346  13.275  1.00 16.04           C  
ANISOU  421  C   GLN A 263      877   1979   3236   -197     57   -427       C  
ATOM    422  O   GLN A 263      20.622  10.423  12.804  1.00 16.67           O  
ANISOU  422  O   GLN A 263     1244   1772   3318   -145    134   -562       O  
ATOM    423  CB  GLN A 263      19.481   7.458  13.908  1.00 14.97           C  
ANISOU  423  CB  GLN A 263      977   2169   2541   -453    525     80       C  
ATOM    424  CG  GLN A 263      18.514   6.387  13.423  1.00 15.81           C  
ANISOU  424  CG  GLN A 263     1081   2193   2733   -612    445     79       C  
ATOM    425  CD  GLN A 263      17.522   5.974  14.501  1.00 16.37           C  
ANISOU  425  CD  GLN A 263      935   2220   3066   -491     29    -79       C  
ATOM    426  OE1 GLN A 263      17.673   6.330  15.667  1.00 19.46           O  
ANISOU  426  OE1 GLN A 263     1447   2048   3899   -398    262    -52       O  
ATOM    427  NE2 GLN A 263      16.496   5.215  14.107  1.00 18.09           N  
ANISOU  427  NE2 GLN A 263     1056   2480   3337   -597    -50    -78       N  
ATOM    428  N   ALA A 264      21.945   9.244  14.198  1.00 15.32           N  
ANISOU  428  N   ALA A 264      784   2064   2974   -120    -18   -339       N  
ATOM    429  CA  ALA A 264      22.609  10.413  14.752  1.00 15.24           C  
ANISOU  429  CA  ALA A 264      784   2132   2875   -180   -170   -262       C  
ATOM    430  C   ALA A 264      23.489  11.092  13.706  1.00 14.95           C  
ANISOU  430  C   ALA A 264      852   2246   2582     78    322   -216       C  
ATOM    431  O   ALA A 264      23.581  12.315  13.673  1.00 17.71           O  
ANISOU  431  O   ALA A 264     1685   2397   2645   -171    -60    -65       O  
ATOM    432  CB  ALA A 264      23.436  10.025  15.965  1.00 19.71           C  
ANISOU  432  CB  ALA A 264     1791   2339   3357   -437    435    148       C  
ATOM    433  N   ALA A 265      24.146  10.297  12.864  1.00 16.04           N  
ANISOU  433  N   ALA A 265     1114   2358   2622    182    478   -385       N  
ATOM    434  CA  ALA A 265      24.975  10.853  11.795  1.00 15.98           C  
ANISOU  434  CA  ALA A 265     1000   2310   2760     -7    347   -221       C  
ATOM    435  C   ALA A 265      24.145  11.745  10.868  1.00 16.27           C  
ANISOU  435  C   ALA A 265     1066   2279   2836     30    114   -506       C  
ATOM    436  O   ALA A 265      24.588  12.808  10.445  1.00 17.89           O  
ANISOU  436  O   ALA A 265     1494   2575   2728   -136    147   -476       O  
ATOM    437  CB  ALA A 265      25.643   9.737  10.994  1.00 17.59           C  
ANISOU  437  CB  ALA A 265     1504   2316   2865   -252    682   -353       C  
ATOM    438  N   LEU A 266      22.930  11.306  10.562  1.00 16.89           N  
ANISOU  438  N   LEU A 266      951   2234   3234    119    272   -590       N  
ATOM    439  CA  LEU A 266      22.068  12.050   9.652  1.00 15.43           C  
ANISOU  439  CA  LEU A 266      963   1907   2992   -119   -351   -643       C  
ATOM    440  C   LEU A 266      21.529  13.341  10.256  1.00 15.93           C  
ANISOU  440  C   LEU A 266     1209   1976   2867    121    297   -565       C  
ATOM    441  O   LEU A 266      21.458  14.362   9.573  1.00 16.69           O  
ANISOU  441  O   LEU A 266     1519   1925   2896   -188    298   -611       O  
ATOM    442  CB  LEU A 266      20.903  11.180   9.176  1.00 14.82           C  
ANISOU  442  CB  LEU A 266     1021   1780   2831   -462   -104   -485       C  
ATOM    443  CG  LEU A 266      21.299  10.105   8.166  1.00 16.10           C  
ANISOU  443  CG  LEU A 266     1460   1696   2963   -684    176   -662       C  
ATOM    444  CD1 LEU A 266      20.100   9.241   7.820  1.00 17.72           C  
ANISOU  444  CD1 LEU A 266     1774   1777   3183   -395   -720   -737       C  
ATOM    445  CD2 LEU A 266      21.901  10.725   6.911  1.00 18.24           C  
ANISOU  445  CD2 LEU A 266     2354   1688   2889   -227    901   -613       C  
ATOM    446  N   THR A 267      21.123  13.303  11.521  1.00 17.18           N  
ANISOU  446  N   THR A 267     1655   2021   2853     43     44   -304       N  
ATOM    447  CA  THR A 267      20.676  14.532  12.161  1.00 18.50           C  
ANISOU  447  CA  THR A 267     1880   2033   3116   -466    817   -503       C  
ATOM    448  C   THR A 267      21.861  15.482  12.310  1.00 20.25           C  
ANISOU  448  C   THR A 267     2284   2078   3331   -725    817   -510       C  
ATOM    449  O   THR A 267      21.721  16.687  12.118  1.00 19.74           O  
ANISOU  449  O   THR A 267     2155   1757   3587   -880    542   -587       O  
ATOM    450  CB  THR A 267      19.961  14.296  13.512  1.00 20.87           C  
ANISOU  450  CB  THR A 267     2394   2155   3381   -485    730   -460       C  
ATOM    451  OG1 THR A 267      20.833  13.606  14.415  1.00 21.23           O  
ANISOU  451  OG1 THR A 267     2322   2321   3422   -145    738   -466       O  
ATOM    452  CG2 THR A 267      18.688  13.481  13.307  1.00 22.40           C  
ANISOU  452  CG2 THR A 267     2579   2278   3653   -593    522   -657       C  
ATOM    453  N   ARG A 268      23.033  14.934  12.616  1.00 18.99           N  
ANISOU  453  N   ARG A 268     1889   2110   3215   -969    701   -237       N  
ATOM    454  CA  ARG A 268      24.241  15.751  12.686  1.00 19.93           C  
ANISOU  454  CA  ARG A 268     2125   2242   3206   -605    583   -468       C  
ATOM    455  C   ARG A 268      24.511  16.421  11.342  1.00 20.49           C  
ANISOU  455  C   ARG A 268     2606   2282   2896   -707    563   -629       C  
ATOM    456  O   ARG A 268      24.715  17.631  11.283  1.00 22.60           O  
ANISOU  456  O   ARG A 268     2992   2613   2984   -970    -29   -786       O  
ATOM    457  CB  ARG A 268      25.442  14.916  13.122  1.00 20.18           C  
ANISOU  457  CB  ARG A 268     1757   2462   3448   -838    -36   -291       C  
ATOM    458  CG  ARG A 268      26.768  15.665  13.123  1.00 18.43           C  
ANISOU  458  CG  ARG A 268     1226   2372   3403   -333   -149   -363       C  
ATOM    459  CD  ARG A 268      27.824  14.845  13.818  1.00 20.86           C  
ANISOU  459  CD  ARG A 268     1738   2485   3702   -483     14   -188       C  
ATOM    460  NE  ARG A 268      29.150  15.437  13.691  1.00 23.34           N  
ANISOU  460  NE  ARG A 268     2328   2560   3981   -571    357   -187       N  
ATOM    461  CZ  ARG A 268      30.250  14.905  14.208  1.00 26.05           C  
ANISOU  461  CZ  ARG A 268     2911   2583   4403   -442    822   -239       C  
ATOM    462  NH1 ARG A 268      30.182  13.765  14.882  1.00 27.59           N  
ANISOU  462  NH1 ARG A 268     3766   2448   4271   -273   1007   -214       N  
ATOM    463  NH2 ARG A 268      31.418  15.513  14.054  1.00 26.31           N  
ANISOU  463  NH2 ARG A 268     2333   2717   4946   -539    812   -202       N  
ATOM    464  N   LEU A 269      24.488  15.647  10.259  1.00 18.92           N  
ANISOU  464  N   LEU A 269     2391   2089   2708   -499    498   -641       N  
ATOM    465  CA  LEU A 269      24.734  16.214   8.933  1.00 15.76           C  
ANISOU  465  CA  LEU A 269     1657   1907   2425      3    498   -695       C  
ATOM    466  C   LEU A 269      23.678  17.236   8.537  1.00 15.93           C  
ANISOU  466  C   LEU A 269     1371   2161   2522   -185    370   -703       C  
ATOM    467  O   LEU A 269      23.993  18.248   7.901  1.00 16.91           O  
ANISOU  467  O   LEU A 269     1761   2291   2373    -71     46   -164       O  
ATOM    468  CB  LEU A 269      24.804  15.121   7.874  1.00 15.67           C  
ANISOU  468  CB  LEU A 269     1406   1807   2740    589    303   -664       C  
ATOM    469  CG  LEU A 269      26.087  14.307   7.946  1.00 18.55           C  
ANISOU  469  CG  LEU A 269     1566   2164   3317    469     65   -101       C  
ATOM    470  CD1 LEU A 269      25.922  13.007   7.189  1.00 21.97           C  
ANISOU  470  CD1 LEU A 269     2762   2095   3491    540    -44   -572       C  
ATOM    471  CD2 LEU A 269      27.238  15.130   7.374  1.00 20.53           C  
ANISOU  471  CD2 LEU A 269     1390   2806   3603    522     49    125       C  
ATOM    472  N   SER A 270      22.427  16.979   8.914  1.00 17.36           N  
ANISOU  472  N   SER A 270     1492   2211   2894   -311    988   -835       N  
ATOM    473  CA  SER A 270      21.351  17.900   8.568  1.00 18.10           C  
ANISOU  473  CA  SER A 270     1343   2294   3240   -160    910   -645       C  
ATOM    474  C   SER A 270      21.589  19.299   9.144  1.00 21.85           C  
ANISOU  474  C   SER A 270     2279   2376   3645   -215   1241   -676       C  
ATOM    475  O   SER A 270      21.111  20.292   8.597  1.00 25.42           O  
ANISOU  475  O   SER A 270     3600   2138   3921    159   1151   -459       O  
ATOM    476  CB  SER A 270      19.985  17.348   9.011  1.00 21.37           C  
ANISOU  476  CB  SER A 270     1950   2793   3375    298   1299   -445       C  
ATOM    477  OG  SER A 270      19.807  17.477  10.409  1.00 26.56           O  
ANISOU  477  OG  SER A 270     2839   3069   4182    137   1253   -868       O  
ATOM    478  N   ARG A 271      22.350  19.388  10.227  1.00 24.46           N  
ANISOU  478  N   ARG A 271     3354   2378   3560   -475   1611  -1006       N  
ATOM    479  CA  ARG A 271      22.582  20.687  10.849  1.00 27.98           C  
ANISOU  479  CA  ARG A 271     4445   2495   3691   -657    954  -1186       C  
ATOM    480  C   ARG A 271      23.990  21.259  10.630  1.00 27.76           C  
ANISOU  480  C   ARG A 271     4454   2741   3352   -721    780   -870       C  
ATOM    481  O   ARG A 271      24.289  22.358  11.097  1.00 29.84           O  
ANISOU  481  O   ARG A 271     5405   2604   3328   -677    837   -886       O  
ATOM    482  CB  ARG A 271      22.230  20.646  12.339  1.00 32.79           C  
ANISOU  482  CB  ARG A 271     5938   2738   3783   -405    843  -1334       C  
ATOM    483  CG  ARG A 271      23.041  19.663  13.145  1.00 38.42           C  
ANISOU  483  CG  ARG A 271     7106   3312   4179   -438    566  -1134       C  
ATOM    484  CD  ARG A 271      22.626  19.648  14.617  1.00 41.84           C  
ANISOU  484  CD  ARG A 271     7650   3655   4592   -680    598   -960       C  
ATOM    485  NE  ARG A 271      23.373  18.646  15.381  1.00 43.79           N  
ANISOU  485  NE  ARG A 271     8022   3886   4731  -1153    242   -780       N  
ATOM    486  CZ  ARG A 271      22.954  17.404  15.605  1.00 45.40           C  
ANISOU  486  CZ  ARG A 271     8451   4090   4708  -1086     22   -873       C  
ATOM    487  NH1 ARG A 271      21.782  17.003  15.135  1.00 46.54           N  
ANISOU  487  NH1 ARG A 271     8717   4043   4925  -1195    -83  -1057       N  
ATOM    488  NH2 ARG A 271      23.705  16.562  16.304  1.00 45.43           N  
ANISOU  488  NH2 ARG A 271     8435   4212   4614  -1103    180   -834       N  
ATOM    489  N   THR A 272      24.845  20.533   9.910  1.00 25.75           N  
ANISOU  489  N   THR A 272     3592   3065   3125   -816    777   -599       N  
ATOM    490  CA  THR A 272      26.217  21.002   9.672  1.00 26.41           C  
ANISOU  490  CA  THR A 272     3572   3231   3231  -1108    303   -333       C  
ATOM    491  C   THR A 272      26.643  21.053   8.197  1.00 23.37           C  
ANISOU  491  C   THR A 272     2940   3011   2930  -1022    479   -542       C  
ATOM    492  O   THR A 272      27.453  21.895   7.806  1.00 26.88           O  
ANISOU  492  O   THR A 272     3512   3517   3185  -1772    236   -628       O  
ATOM    493  CB  THR A 272      27.263  20.164  10.452  1.00 28.63           C  
ANISOU  493  CB  THR A 272     3741   3613   3525  -1405   -181   -163       C  
ATOM    494  OG1 THR A 272      27.163  18.785  10.070  1.00 30.69           O  
ANISOU  494  OG1 THR A 272     4093   3796   3774  -1206   -460    -77       O  
ATOM    495  CG2 THR A 272      27.055  20.294  11.953  1.00 27.91           C  
ANISOU  495  CG2 THR A 272     3453   3759   3392  -1669   -198     -2       C  
ATOM    496  N   PHE A 273      26.115  20.151   7.380  1.00 17.50           N  
ANISOU  496  N   PHE A 273     1715   2544   2390   -331    223   -548       N  
ATOM    497  CA  PHE A 273      26.559  20.040   5.992  1.00 17.25           C  
ANISOU  497  CA  PHE A 273     2004   2190   2359    -89   -191   -646       C  
ATOM    498  C   PHE A 273      25.987  21.230   5.216  1.00 17.40           C  
ANISOU  498  C   PHE A 273     1904   2207   2502   -258     28   -364       C  
ATOM    499  O   PHE A 273      24.782  21.514   5.312  1.00 16.64           O  
ANISOU  499  O   PHE A 273     1661   2232   2430   -478    253   -369       O  
ATOM    500  CB  PHE A 273      26.078  18.706   5.416  1.00 14.86           C  
ANISOU  500  CB  PHE A 273     1247   1924   2474     23     33   -805       C  
ATOM    501  CG  PHE A 273      26.697  18.336   4.101  1.00 15.17           C  
ANISOU  501  CG  PHE A 273     1024   2175   2564    165    222   -674       C  
ATOM    502  CD1 PHE A 273      27.964  17.751   4.048  1.00 18.75           C  
ANISOU  502  CD1 PHE A 273     1815   2561   2749    555    500   -532       C  
ATOM    503  CD2 PHE A 273      26.000  18.527   2.915  1.00 17.86           C  
ANISOU  503  CD2 PHE A 273     1676   2453   2656    227    269   -609       C  
ATOM    504  CE1 PHE A 273      28.533  17.386   2.823  1.00 17.84           C  
ANISOU  504  CE1 PHE A 273     1581   2546   2651    673    -43   -535       C  
ATOM    505  CE2 PHE A 273      26.555  18.164   1.691  1.00 20.01           C  
ANISOU  505  CE2 PHE A 273     2239   2604   2760    304    307   -715       C  
ATOM    506  CZ  PHE A 273      27.821  17.596   1.641  1.00 18.51           C  
ANISOU  506  CZ  PHE A 273     1780   2506   2745    423    293   -563       C  
ATOM    507  N   ASP A 274      26.837  21.935   4.467  1.00 16.56           N  
ANISOU  507  N   ASP A 274     1731   2170   2391    -71    -56   -398       N  
ATOM    508  CA  ASP A 274      26.438  23.239   3.923  1.00 16.44           C  
ANISOU  508  CA  ASP A 274     1174   2418   2655   -391   -565   -202       C  
ATOM    509  C   ASP A 274      25.228  23.231   2.990  1.00 15.95           C  
ANISOU  509  C   ASP A 274     1004   2426   2631   -550   -353   -317       C  
ATOM    510  O   ASP A 274      24.470  24.205   2.936  1.00 18.16           O  
ANISOU  510  O   ASP A 274     1390   2574   2935   -475     74   -392       O  
ATOM    511  CB  ASP A 274      27.615  24.015   3.309  1.00 18.08           C  
ANISOU  511  CB  ASP A 274     1275   2787   2807   -337    302    132       C  
ATOM    512  CG  ASP A 274      28.240  23.332   2.091  1.00 19.70           C  
ANISOU  512  CG  ASP A 274     1121   3220   3144   -679    173    304       C  
ATOM    513  OD1 ASP A 274      29.251  23.882   1.593  1.00 22.30           O  
ANISOU  513  OD1 ASP A 274     1268   3661   3544   -603    120    710       O  
ATOM    514  OD2 ASP A 274      27.756  22.278   1.622  1.00 21.49           O  
ANISOU  514  OD2 ASP A 274     1830   3285   3048   -697     99   -437       O  
ATOM    515  N   ALA A 275      25.036  22.126   2.281  1.00 15.30           N  
ANISOU  515  N   ALA A 275      981   2427   2406   -552    -89   -531       N  
ATOM    516  CA  ALA A 275      23.922  22.011   1.348  1.00 15.91           C  
ANISOU  516  CA  ALA A 275      931   2475   2641   -400   -198   -531       C  
ATOM    517  C   ALA A 275      22.558  22.064   2.052  1.00 17.56           C  
ANISOU  517  C   ALA A 275     1028   2589   3053   -297   -142   -506       C  
ATOM    518  O   ALA A 275      21.546  22.338   1.410  1.00 18.66           O  
ANISOU  518  O   ALA A 275     1025   2911   3155   -421   -188   -529       O  
ATOM    519  CB  ALA A 275      24.050  20.725   0.533  1.00 17.42           C  
ANISOU  519  CB  ALA A 275     1719   2495   2405   -264     -1   -658       C  
ATOM    520  N   PHE A 276      22.529  21.808   3.359  1.00 16.37           N  
ANISOU  520  N   PHE A 276      926   2256   3037   -139   -288   -622       N  
ATOM    521  CA  PHE A 276      21.254  21.647   4.073  1.00 17.92           C  
ANISOU  521  CA  PHE A 276     1028   2325   3457    104    291   -361       C  
ATOM    522  C   PHE A 276      20.869  22.859   4.918  1.00 19.90           C  
ANISOU  522  C   PHE A 276     1043   2663   3854   -170    112   -574       C  
ATOM    523  O   PHE A 276      19.759  22.932   5.461  1.00 23.16           O  
ANISOU  523  O   PHE A 276     1375   2877   4548   -162    692   -666       O  
ATOM    524  CB  PHE A 276      21.310  20.415   4.983  1.00 18.09           C  
ANISOU  524  CB  PHE A 276     1145   2317   3412     20    397   -309       C  
ATOM    525  CG  PHE A 276      21.718  19.159   4.277  1.00 17.13           C  
ANISOU  525  CG  PHE A 276     1092   2259   3159   -374    173   -176       C  
ATOM    526  CD1 PHE A 276      21.248  18.869   3.002  1.00 19.74           C  
ANISOU  526  CD1 PHE A 276     1681   2353   3466   -488    176   -239       C  
ATOM    527  CD2 PHE A 276      22.576  18.261   4.893  1.00 16.59           C  
ANISOU  527  CD2 PHE A 276      900   2314   3090   -411    -33   -208       C  
ATOM    528  CE1 PHE A 276      21.637  17.703   2.354  1.00 17.86           C  
ANISOU  528  CE1 PHE A 276     1123   2450   3213   -583   -248   -120       C  
ATOM    529  CE2 PHE A 276      22.967  17.106   4.256  1.00 17.85           C  
ANISOU  529  CE2 PHE A 276     1335   2505   2944   -297    -77   -400       C  
ATOM    530  CZ  PHE A 276      22.496  16.819   2.987  1.00 17.90           C  
ANISOU  530  CZ  PHE A 276     1152   2755   2894   -602   -531   -295       C  
ATOM    531  N   LEU A 277      21.786  23.806   5.052  1.00 21.22           N  
ANISOU  531  N   LEU A 277     1120   2797   4143     24    -94   -733       N  
ATOM    532  CA  LEU A 277      21.581  24.900   5.989  1.00 24.42           C  
ANISOU  532  CA  LEU A 277     1433   3032   4814    302   -262   -898       C  
ATOM    533  C   LEU A 277      20.493  25.856   5.533  1.00 27.44           C  
ANISOU  533  C   LEU A 277     1936   2920   5570     64   -271   -866       C  
ATOM    534  O   LEU A 277      20.563  26.405   4.442  1.00 27.85           O  
ANISOU  534  O   LEU A 277     1970   3010   5601    108   -661   -334       O  
ATOM    535  CB  LEU A 277      22.898  25.636   6.229  1.00 24.77           C  
ANISOU  535  CB  LEU A 277     1522   3403   4485    504   -681  -1063       C  
ATOM    536  CG  LEU A 277      23.997  24.686   6.706  1.00 29.44           C  
ANISOU  536  CG  LEU A 277     2600   3878   4707    -98   -465  -1123       C  
ATOM    537  CD1 LEU A 277      25.257  25.466   7.032  1.00 29.71           C  
ANISOU  537  CD1 LEU A 277     2588   3945   4757   -461   -525  -1385       C  
ATOM    538  CD2 LEU A 277      23.530  23.866   7.908  1.00 32.06           C  
ANISOU  538  CD2 LEU A 277     3292   4130   4759   -198   -433  -1038       C  
ATOM    539  N   GLY A 278      19.475  26.030   6.372  1.00 27.42           N  
ANISOU  539  N   GLY A 278     1709   2662   6048    227    229  -1103       N  
ATOM    540  CA  GLY A 278      18.397  26.963   6.100  1.00 29.58           C  
ANISOU  540  CA  GLY A 278     1923   2601   6714    270   -539  -1062       C  
ATOM    541  C   GLY A 278      17.382  26.501   5.073  1.00 30.96           C  
ANISOU  541  C   GLY A 278     2315   2526   6921    -12     54  -1376       C  
ATOM    542  O   GLY A 278      16.442  27.231   4.760  1.00 34.16           O  
ANISOU  542  O   GLY A 278     3145   2427   7408    160    181  -1528       O  
ATOM    543  N   VAL A 279      17.570  25.299   4.540  1.00 28.59           N  
ANISOU  543  N   VAL A 279     2016   2604   6243   -522    558  -1348       N  
ATOM    544  CA  VAL A 279      16.661  24.760   3.534  1.00 27.00           C  
ANISOU  544  CA  VAL A 279     1853   2837   5569   -189   1041  -1193       C  
ATOM    545  C   VAL A 279      15.316  24.393   4.159  1.00 23.41           C  
ANISOU  545  C   VAL A 279     1387   2780   4729     64    433  -1022       C  
ATOM    546  O   VAL A 279      15.261  23.733   5.195  1.00 23.37           O  
ANISOU  546  O   VAL A 279     1374   2699   4805     61    263  -1153       O  
ATOM    547  CB  VAL A 279      17.278  23.534   2.831  1.00 26.42           C  
ANISOU  547  CB  VAL A 279     1838   2882   5318   -300   1166   -827       C  
ATOM    548  CG1 VAL A 279      16.302  22.919   1.838  1.00 29.10           C  
ANISOU  548  CG1 VAL A 279     2096   2956   6005   -214   1351   -942       C  
ATOM    549  CG2 VAL A 279      18.571  23.942   2.122  1.00 25.99           C  
ANISOU  549  CG2 VAL A 279     1665   3083   5128   -143   1028   -527       C  
ATOM    550  N   VAL A 280      14.238  24.847   3.532  1.00 21.39           N  
ANISOU  550  N   VAL A 280     1274   2869   3984     33    673   -635       N  
ATOM    551  CA  VAL A 280      12.892  24.545   4.022  1.00 19.63           C  
ANISOU  551  CA  VAL A 280     1073   2744   3640     43    425   -582       C  
ATOM    552  C   VAL A 280      12.495  23.125   3.612  1.00 19.42           C  
ANISOU  552  C   VAL A 280     1086   2730   3562    -80    491   -613       C  
ATOM    553  O   VAL A 280      12.928  22.627   2.567  1.00 20.02           O  
ANISOU  553  O   VAL A 280     1304   2790   3512     98    622   -953       O  
ATOM    554  CB  VAL A 280      11.866  25.587   3.518  1.00 26.93           C  
ANISOU  554  CB  VAL A 280     2515   3084   4632    501    522   -892       C  
ATOM    555  CG1 VAL A 280      12.371  26.995   3.803  1.00 27.62           C  
ANISOU  555  CG1 VAL A 280     2670   3158   4668    619    703   -618       C  
ATOM    556  CG2 VAL A 280      11.594  25.406   2.029  1.00 32.74           C  
ANISOU  556  CG2 VAL A 280     3600   3441   5400    517     76   -582       C  
ATOM    557  N   PRO A 281      11.692  22.446   4.447  1.00 19.35           N  
ANISOU  557  N   PRO A 281     1114   2658   3580   -274    482   -664       N  
ATOM    558  CA  PRO A 281      11.334  21.055   4.134  1.00 19.92           C  
ANISOU  558  CA  PRO A 281     1381   2655   3533   -228    608   -625       C  
ATOM    559  C   PRO A 281      10.423  20.981   2.918  1.00 18.21           C  
ANISOU  559  C   PRO A 281     1143   2505   3271    -80    720   -464       C  
ATOM    560  O   PRO A 281       9.642  21.909   2.686  1.00 19.03           O  
ANISOU  560  O   PRO A 281     1246   2449   3537   -261    310   -281       O  
ATOM    561  CB  PRO A 281      10.558  20.590   5.378  1.00 20.76           C  
ANISOU  561  CB  PRO A 281     2041   2713   3133   -474    492   -505       C  
ATOM    562  CG  PRO A 281      10.686  21.692   6.390  1.00 21.83           C  
ANISOU  562  CG  PRO A 281     2499   2572   3223   -279    762   -645       C  
ATOM    563  CD  PRO A 281      11.014  22.943   5.651  1.00 20.95           C  
ANISOU  563  CD  PRO A 281     1830   2679   3453   -329   1033   -696       C  
ATOM    564  N   PRO A 282      10.505  19.887   2.153  1.00 17.62           N  
ANISOU  564  N   PRO A 282     1065   2562   3067     62    216   -483       N  
ATOM    565  CA  PRO A 282       9.598  19.697   1.013  1.00 15.91           C  
ANISOU  565  CA  PRO A 282      837   2522   2686    399    -14   -335       C  
ATOM    566  C   PRO A 282       8.189  19.399   1.496  1.00 16.06           C  
ANISOU  566  C   PRO A 282      963   2603   2537    400   -369   -164       C  
ATOM    567  O   PRO A 282       8.015  18.832   2.575  1.00 17.28           O  
ANISOU  567  O   PRO A 282     1436   2791   2338    525    -31    -23       O  
ATOM    568  CB  PRO A 282      10.178  18.463   0.314  1.00 16.44           C  
ANISOU  568  CB  PRO A 282      946   2527   2774    485     74   -461       C  
ATOM    569  CG  PRO A 282      10.834  17.685   1.428  1.00 17.24           C  
ANISOU  569  CG  PRO A 282     1117   2535   2898    398   -322   -477       C  
ATOM    570  CD  PRO A 282      11.409  18.738   2.350  1.00 18.03           C  
ANISOU  570  CD  PRO A 282     1225   2586   3040    535   -426   -381       C  
ATOM    571  N   VAL A 283       7.198  19.778   0.699  1.00 15.27           N  
ANISOU  571  N   VAL A 283      692   2465   2643    233     43     -9       N  
ATOM    572  CA  VAL A 283       5.817  19.377   0.950  1.00 15.44           C  
ANISOU  572  CA  VAL A 283      727   2403   2736     51    130   -241       C  
ATOM    573  C   VAL A 283       5.532  18.089   0.181  1.00 19.08           C  
ANISOU  573  C   VAL A 283     1717   2693   2841    256    -14   -691       C  
ATOM    574  O   VAL A 283       5.784  18.010  -1.024  1.00 20.27           O  
ANISOU  574  O   VAL A 283     1879   3012   2809   -158   -222   -438       O  
ATOM    575  CB  VAL A 283       4.828  20.473   0.519  1.00 15.52           C  
ANISOU  575  CB  VAL A 283      790   2421   2685   -113    388   -164       C  
ATOM    576  CG1 VAL A 283       3.385  19.947   0.597  1.00 18.69           C  
ANISOU  576  CG1 VAL A 283      908   2929   3266    237     -3   -260       C  
ATOM    577  CG2 VAL A 283       4.997  21.695   1.391  1.00 14.73           C  
ANISOU  577  CG2 VAL A 283     1007   2183   2408    -43    538   -361       C  
ATOM    578  N   ILE A 284       5.042  17.076   0.894  1.00 18.25           N  
ANISOU  578  N   ILE A 284     1846   2297   2789    172     24   -849       N  
ATOM    579  CA  ILE A 284       4.683  15.793   0.304  1.00 17.68           C  
ANISOU  579  CA  ILE A 284     1295   2400   3023    318   -121   -571       C  
ATOM    580  C   ILE A 284       3.174  15.618   0.373  1.00 18.10           C  
ANISOU  580  C   ILE A 284     1616   2315   2946   -118   -261   -621       C  
ATOM    581  O   ILE A 284       2.585  15.647   1.456  1.00 18.39           O  
ANISOU  581  O   ILE A 284     2112   2180   2697   -134   -116   -605       O  
ATOM    582  CB  ILE A 284       5.346  14.638   1.058  1.00 19.96           C  
ANISOU  582  CB  ILE A 284     1392   2883   3309    231   -393   -748       C  
ATOM    583  CG1 ILE A 284       6.867  14.782   1.002  1.00 21.35           C  
ANISOU  583  CG1 ILE A 284     1383   3178   3550    579   -760   -553       C  
ATOM    584  CG2 ILE A 284       4.898  13.293   0.481  1.00 23.11           C  
ANISOU  584  CG2 ILE A 284     2514   2974   3295    528   -110  -1005       C  
ATOM    585  CD1 ILE A 284       7.582  13.813   1.910  1.00 23.49           C  
ANISOU  585  CD1 ILE A 284     1728   3289   3909   1048   -489   -798       C  
ATOM    586  N   ARG A 285       2.544  15.450  -0.783  1.00 18.41           N  
ANISOU  586  N   ARG A 285     1408   2354   3233    168   -252   -795       N  
ATOM    587  CA  ARG A 285       1.090  15.330  -0.822  1.00 19.69           C  
ANISOU  587  CA  ARG A 285     1442   2573   3465   -110   -415   -533       C  
ATOM    588  C   ARG A 285       0.621  13.923  -0.459  1.00 19.74           C  
ANISOU  588  C   ARG A 285     1208   2791   3501   -149    -88   -484       C  
ATOM    589  O   ARG A 285       1.200  12.928  -0.895  1.00 22.82           O  
ANISOU  589  O   ARG A 285     1421   3346   3904   -384    293   -481       O  
ATOM    590  CB  ARG A 285       0.561  15.757  -2.189  1.00 24.72           C  
ANISOU  590  CB  ARG A 285     2611   2685   4096    387   -275   -346       C  
ATOM    591  CG  ARG A 285       0.506  17.272  -2.343  1.00 28.64           C  
ANISOU  591  CG  ARG A 285     3085   3324   4473    113   -107   -362       C  
ATOM    592  CD  ARG A 285      -0.679  17.880  -1.573  1.00 31.32           C  
ANISOU  592  CD  ARG A 285     3386   3689   4826    426   -687   -636       C  
ATOM    593  NE  ARG A 285      -1.935  17.725  -2.307  1.00 36.55           N  
ANISOU  593  NE  ARG A 285     4404   4076   5406    492   -867   -445       N  
ATOM    594  CZ  ARG A 285      -2.777  16.702  -2.160  1.00 40.13           C  
ANISOU  594  CZ  ARG A 285     5218   4373   5655    680  -1480   -268       C  
ATOM    595  NH1 ARG A 285      -2.516  15.738  -1.288  1.00 39.29           N  
ANISOU  595  NH1 ARG A 285     5497   4158   5273    850  -2098     56       N  
ATOM    596  NH2 ARG A 285      -3.889  16.644  -2.884  1.00 42.27           N  
ANISOU  596  NH2 ARG A 285     5556   4591   5913    603  -1597   -336       N  
ATOM    597  N   VAL A 286      -0.416  13.853   0.370  1.00 19.42           N  
ANISOU  597  N   VAL A 286     1079   2810   3490    147    165   -394       N  
ATOM    598  CA  VAL A 286      -1.026  12.582   0.747  1.00 19.47           C  
ANISOU  598  CA  VAL A 286      943   2949   3504   -259    165   -137       C  
ATOM    599  C   VAL A 286      -2.547  12.717   0.654  1.00 21.16           C  
ANISOU  599  C   VAL A 286     1368   3050   3621   -135    -90   -420       C  
ATOM    600  O   VAL A 286      -3.078  13.828   0.732  1.00 20.34           O  
ANISOU  600  O   VAL A 286     1431   2824   3472   -287     73   -538       O  
ATOM    601  CB  VAL A 286      -0.631  12.157   2.182  1.00 19.39           C  
ANISOU  601  CB  VAL A 286     1313   2946   3108    402    527    -85       C  
ATOM    602  CG1 VAL A 286       0.873  11.821   2.264  1.00 19.78           C  
ANISOU  602  CG1 VAL A 286     1188   3226   3103    186   -258    142       C  
ATOM    603  CG2 VAL A 286      -0.998  13.236   3.187  1.00 20.52           C  
ANISOU  603  CG2 VAL A 286     2133   2669   2995    385    644   -171       C  
ATOM    604  N   LYS A 287      -3.242  11.596   0.468  1.00 20.77           N  
ANISOU  604  N   LYS A 287     1121   3337   3434   -333   -120   -792       N  
ATOM    605  CA  LYS A 287      -4.705  11.612   0.509  1.00 23.71           C  
ANISOU  605  CA  LYS A 287     1640   3534   3835   -337   -143  -1056       C  
ATOM    606  C   LYS A 287      -5.158  12.068   1.891  1.00 22.38           C  
ANISOU  606  C   LYS A 287     1574   3127   3802     40   -315   -948       C  
ATOM    607  O   LYS A 287      -6.019  12.936   2.029  1.00 22.97           O  
ANISOU  607  O   LYS A 287     1605   3121   4001    716   -470   -917       O  
ATOM    608  CB  LYS A 287      -5.286  10.227   0.220  1.00 27.71           C  
ANISOU  608  CB  LYS A 287     2537   3827   4165   -452   -515  -1381       C  
ATOM    609  CG  LYS A 287      -5.246   9.809  -1.238  1.00 32.45           C  
ANISOU  609  CG  LYS A 287     3469   4034   4825   -578   -473  -1483       C  
ATOM    610  CD  LYS A 287      -5.994   8.502  -1.444  1.00 34.53           C  
ANISOU  610  CD  LYS A 287     3409   4368   5342   -680   -911  -1298       C  
ATOM    611  CE  LYS A 287      -5.900   8.026  -2.882  1.00 38.82           C  
ANISOU  611  CE  LYS A 287     4406   4626   5717   -832   -900  -1340       C  
ATOM    612  NZ  LYS A 287      -6.707   6.790  -3.107  1.00 41.76           N  
ANISOU  612  NZ  LYS A 287     4943   4898   6027   -852   -606  -1258       N  
ATOM    613  N   ASN A 288      -4.558  11.463   2.910  1.00 21.58           N  
ANISOU  613  N   ASN A 288     1624   2747   3829   -143   -281   -631       N  
ATOM    614  CA  ASN A 288      -4.810  11.813   4.299  1.00 17.43           C  
ANISOU  614  CA  ASN A 288      911   2568   3144    -19   -412   -310       C  
ATOM    615  C   ASN A 288      -3.619  11.362   5.121  1.00 18.17           C  
ANISOU  615  C   ASN A 288      897   2781   3225   -236   -210   -288       C  
ATOM    616  O   ASN A 288      -2.679  10.781   4.573  1.00 17.46           O  
ANISOU  616  O   ASN A 288     1003   2321   3312    341    102   -580       O  
ATOM    617  CB  ASN A 288      -6.127  11.196   4.816  1.00 17.44           C  
ANISOU  617  CB  ASN A 288      958   2246   3422   -170   -301   -368       C  
ATOM    618  CG  ASN A 288      -6.190   9.689   4.634  1.00 21.01           C  
ANISOU  618  CG  ASN A 288     1197   2318   4470      6   -348   -540       C  
ATOM    619  OD1 ASN A 288      -5.166   9.002   4.614  1.00 21.97           O  
ANISOU  619  OD1 ASN A 288     1254   2219   4875    -14     23   -625       O  
ATOM    620  ND2 ASN A 288      -7.407   9.162   4.504  1.00 20.21           N  
ANISOU  620  ND2 ASN A 288     1247   2111   4321    320   -393   -523       N  
ATOM    621  N   PHE A 289      -3.629  11.630   6.419  1.00 19.01           N  
ANISOU  621  N   PHE A 289      847   3157   3218   -287   -113    -22       N  
ATOM    622  CA  PHE A 289      -2.424  11.338   7.204  1.00 19.04           C  
ANISOU  622  CA  PHE A 289      849   3150   3233   -185   -222    -16       C  
ATOM    623  C   PHE A 289      -2.276   9.856   7.502  1.00 22.90           C  
ANISOU  623  C   PHE A 289     1061   3468   4169   -122   -172     56       C  
ATOM    624  O   PHE A 289      -1.206   9.401   7.885  1.00 22.90           O  
ANISOU  624  O   PHE A 289     1091   3575   4036    221   -265   -285       O  
ATOM    625  CB  PHE A 289      -2.353  12.203   8.459  1.00 21.57           C  
ANISOU  625  CB  PHE A 289     1189   3272   3736   -138   -147     -5       C  
ATOM    626  CG  PHE A 289      -2.373  13.673   8.158  1.00 23.66           C  
ANISOU  626  CG  PHE A 289     1858   3330   3801   -334   -347   -190       C  
ATOM    627  CD1 PHE A 289      -1.381  14.239   7.371  1.00 22.94           C  
ANISOU  627  CD1 PHE A 289     1623   3436   3657    160   -128   -287       C  
ATOM    628  CD2 PHE A 289      -3.401  14.481   8.625  1.00 22.94           C  
ANISOU  628  CD2 PHE A 289     1452   3443   3822   -324   -231   -274       C  
ATOM    629  CE1 PHE A 289      -1.401  15.590   7.069  1.00 23.81           C  
ANISOU  629  CE1 PHE A 289     1988   3511   3547   -213    299   -112       C  
ATOM    630  CE2 PHE A 289      -3.431  15.828   8.331  1.00 23.42           C  
ANISOU  630  CE2 PHE A 289     1628   3532   3738   -521   -395   -176       C  
ATOM    631  CZ  PHE A 289      -2.426  16.389   7.552  1.00 23.43           C  
ANISOU  631  CZ  PHE A 289     1639   3651   3615    -17   -245    -47       C  
ATOM    632  N   GLN A 290      -3.345   9.098   7.282  1.00 25.27           N  
ANISOU  632  N   GLN A 290     1272   3517   4812   -292    171    315       N  
ATOM    633  CA  GLN A 290      -3.277   7.640   7.342  1.00 28.04           C  
ANISOU  633  CA  GLN A 290     1652   3455   5545   -656   -233    616       C  
ATOM    634  C   GLN A 290      -2.255   7.096   6.331  1.00 27.15           C  
ANISOU  634  C   GLN A 290     1690   3163   5465   -256   -953    514       C  
ATOM    635  O   GLN A 290      -1.691   6.017   6.516  1.00 30.55           O  
ANISOU  635  O   GLN A 290     2740   3039   5827   -516  -1513    615       O  
ATOM    636  CB  GLN A 290      -4.667   7.037   7.091  1.00 32.76           C  
ANISOU  636  CB  GLN A 290     2148   3879   6419   -649   -651    650       C  
ATOM    637  CG  GLN A 290      -4.650   5.597   6.613  1.00 36.28           C  
ANISOU  637  CG  GLN A 290     2328   4490   6968   -886   -443    456       C  
ATOM    638  CD  GLN A 290      -5.437   4.674   7.515  1.00 44.00           C  
ANISOU  638  CD  GLN A 290     4298   5092   7328    -96   -240    316       C  
ATOM    639  OE1 GLN A 290      -4.870   3.996   8.379  1.00 49.51           O  
ANISOU  639  OE1 GLN A 290     5629   5442   7742    233    -14    203       O  
ATOM    640  NE2 GLN A 290      -6.753   4.634   7.317  1.00 41.45           N  
ANISOU  640  NE2 GLN A 290     3409   5157   7182   -121   -185    100       N  
ATOM    641  N   THR A 291      -2.009   7.868   5.276  1.00 25.09           N  
ANISOU  641  N   THR A 291     1490   2808   5235   -155   -624    531       N  
ATOM    642  CA  THR A 291      -1.067   7.500   4.221  1.00 24.75           C  
ANISOU  642  CA  THR A 291     1844   2814   4745    135   -401   -207       C  
ATOM    643  C   THR A 291       0.386   7.536   4.712  1.00 23.67           C  
ANISOU  643  C   THR A 291     2009   2747   4238    186   -416   -428       C  
ATOM    644  O   THR A 291       1.238   6.803   4.213  1.00 25.35           O  
ANISOU  644  O   THR A 291     2495   3294   3842    282   -177   -676       O  
ATOM    645  CB  THR A 291      -1.221   8.439   3.004  1.00 27.08           C  
ANISOU  645  CB  THR A 291     2308   3265   4717    510   -486   -570       C  
ATOM    646  OG1 THR A 291      -2.592   8.460   2.583  1.00 32.06           O  
ANISOU  646  OG1 THR A 291     3830   3458   4894    230   -488   -597       O  
ATOM    647  CG2 THR A 291      -0.353   7.985   1.846  1.00 30.77           C  
ANISOU  647  CG2 THR A 291     3382   3453   4858    210   -278   -661       C  
ATOM    648  N   VAL A 292       0.661   8.399   5.685  1.00 19.93           N  
ANISOU  648  N   VAL A 292     1199   2536   3838   -490   -332   -297       N  
ATOM    649  CA  VAL A 292       1.998   8.516   6.262  1.00 18.58           C  
ANISOU  649  CA  VAL A 292      941   2404   3714    -35    123   -163       C  
ATOM    650  C   VAL A 292       2.368   7.175   6.910  1.00 20.50           C  
ANISOU  650  C   VAL A 292     1069   2783   3939    365    120   -110       C  
ATOM    651  O   VAL A 292       1.550   6.588   7.614  1.00 21.81           O  
ANISOU  651  O   VAL A 292     1232   2827   4227    -25   -139    206       O  
ATOM    652  CB  VAL A 292       2.036   9.669   7.305  1.00 18.39           C  
ANISOU  652  CB  VAL A 292     1026   2246   3714    214   -310    251       C  
ATOM    653  CG1 VAL A 292       3.382   9.748   8.004  1.00 18.18           C  
ANISOU  653  CG1 VAL A 292     1184   2379   3342    443   -567    286       C  
ATOM    654  CG2 VAL A 292       1.720  11.001   6.649  1.00 17.75           C  
ANISOU  654  CG2 VAL A 292     1527   1683   3534     56   -231    360       C  
ATOM    655  N   PRO A 293       3.591   6.667   6.655  1.00 22.68           N  
ANISOU  655  N   PRO A 293     1302   2997   4320    523    450     98       N  
ATOM    656  CA  PRO A 293       3.925   5.334   7.174  1.00 23.16           C  
ANISOU  656  CA  PRO A 293     1388   3098   4313    734    324     64       C  
ATOM    657  C   PRO A 293       3.739   5.222   8.684  1.00 24.02           C  
ANISOU  657  C   PRO A 293     1314   3127   4687    490    156    280       C  
ATOM    658  O   PRO A 293       3.978   6.192   9.407  1.00 23.66           O  
ANISOU  658  O   PRO A 293     1211   3172   4607   -198    240    300       O  
ATOM    659  CB  PRO A 293       5.407   5.172   6.811  1.00 22.55           C  
ANISOU  659  CB  PRO A 293     1370   3096   4101    759    379    124       C  
ATOM    660  CG  PRO A 293       5.608   6.074   5.648  1.00 24.07           C  
ANISOU  660  CG  PRO A 293     1364   3373   4407    463    653    -18       C  
ATOM    661  CD  PRO A 293       4.690   7.248   5.865  1.00 22.75           C  
ANISOU  661  CD  PRO A 293     1212   3315   4118    602    231    -10       C  
ATOM    662  N   ARG A 294       3.292   4.055   9.138  1.00 24.72           N  
ANISOU  662  N   ARG A 294     1337   3172   4882    330   -360    250       N  
ATOM    663  CA  ARG A 294       3.097   3.799  10.563  1.00 27.95           C  
ANISOU  663  CA  ARG A 294     1561   3439   5620   -142    -31    289       C  
ATOM    664  C   ARG A 294       4.270   4.246  11.464  1.00 25.14           C  
ANISOU  664  C   ARG A 294     1373   3204   4973    -63    150    294       C  
ATOM    665  O   ARG A 294       4.047   4.919  12.466  1.00 24.58           O  
ANISOU  665  O   ARG A 294     1271   3079   4988     92    118    354       O  
ATOM    666  CB  ARG A 294       2.743   2.322  10.807  1.00 34.25           C  
ANISOU  666  CB  ARG A 294     2305   4030   6679   -535   -336      3       C  
ATOM    667  CG  ARG A 294       2.332   2.001  12.235  1.00 41.17           C  
ANISOU  667  CG  ARG A 294     3181   4763   7699   -297   -930    -87       C  
ATOM    668  CD  ARG A 294       1.010   2.671  12.586  1.00 48.79           C  
ANISOU  668  CD  ARG A 294     4358   5611   8569    -14  -1373    -43       C  
ATOM    669  NE  ARG A 294      -0.008   2.444  11.560  1.00 54.98           N  
ANISOU  669  NE  ARG A 294     5398   6219   9274    356  -1414     45       N  
ATOM    670  CZ  ARG A 294      -0.785   3.399  11.054  1.00 56.48           C  
ANISOU  670  CZ  ARG A 294     5329   6517   9615    810   -994     43       C  
ATOM    671  NH1 ARG A 294      -0.658   4.643  11.483  1.00 55.13           N  
ANISOU  671  NH1 ARG A 294     4812   6481   9654   1096   -812     57       N  
ATOM    672  NH2 ARG A 294      -1.687   3.112  10.120  1.00 58.73           N  
ANISOU  672  NH2 ARG A 294     5820   6773   9722    852   -747    -26       N  
ATOM    673  N   PRO A 295       5.524   3.894  11.107  1.00 22.50           N  
ANISOU  673  N   PRO A 295     1131   3103   4314    304    129     46       N  
ATOM    674  CA  PRO A 295       6.619   4.316  11.994  1.00 21.18           C  
ANISOU  674  CA  PRO A 295     1095   2962   3991    326    317     -7       C  
ATOM    675  C   PRO A 295       6.873   5.826  12.031  1.00 20.69           C  
ANISOU  675  C   PRO A 295     1038   2935   3889    243    269    -99       C  
ATOM    676  O   PRO A 295       7.724   6.264  12.804  1.00 22.87           O  
ANISOU  676  O   PRO A 295     1567   3009   4114    187    510    198       O  
ATOM    677  CB  PRO A 295       7.844   3.599  11.403  1.00 22.76           C  
ANISOU  677  CB  PRO A 295     1397   2951   4301    590    551   -117       C  
ATOM    678  CG  PRO A 295       7.288   2.446  10.655  1.00 23.75           C  
ANISOU  678  CG  PRO A 295     1472   3019   4533    482    414     31       C  
ATOM    679  CD  PRO A 295       5.992   2.937  10.086  1.00 22.29           C  
ANISOU  679  CD  PRO A 295     1429   2907   4133    703    502   -177       C  
ATOM    680  N   CYS A 296       6.160   6.600  11.215  1.00 19.85           N  
ANISOU  680  N   CYS A 296     1313   2846   3382    944    175    -79       N  
ATOM    681  CA  CYS A 296       6.310   8.057  11.201  1.00 20.21           C  
ANISOU  681  CA  CYS A 296     1355   2727   3598    517    282    -93       C  
ATOM    682  C   CYS A 296       5.174   8.766  11.932  1.00 19.21           C  
ANISOU  682  C   CYS A 296     1115   2756   3426    329    575   -226       C  
ATOM    683  O   CYS A 296       5.276   9.957  12.223  1.00 18.00           O  
ANISOU  683  O   CYS A 296      931   2479   3430    303   -169   -128       O  
ATOM    684  CB  CYS A 296       6.355   8.594   9.765  1.00 20.73           C  
ANISOU  684  CB  CYS A 296     1310   2812   3756    478    621   -360       C  
ATOM    685  SG  CYS A 296       7.862   8.227   8.846  1.00 21.17           S  
ANISOU  685  SG  CYS A 296     1204   2681   4158    325    424   -279       S  
ATOM    686  N   GLN A 297       4.087   8.050  12.207  1.00 19.36           N  
ANISOU  686  N   GLN A 297     1011   2924   3422    -14    546    144       N  
ATOM    687  CA  GLN A 297       2.892   8.694  12.762  1.00 19.82           C  
ANISOU  687  CA  GLN A 297     1000   3108   3422   -320    373    222       C  
ATOM    688  C   GLN A 297       3.141   9.474  14.048  1.00 20.04           C  
ANISOU  688  C   GLN A 297     1021   3081   3512   -297    387    245       C  
ATOM    689  O   GLN A 297       2.659  10.595  14.207  1.00 19.75           O  
ANISOU  689  O   GLN A 297     1125   3009   3369     99    130   -171       O  
ATOM    690  CB  GLN A 297       1.788   7.660  13.001  1.00 20.22           C  
ANISOU  690  CB  GLN A 297      912   3301   3471   -252    133     92       C  
ATOM    691  CG  GLN A 297       1.283   7.046  11.735  1.00 23.80           C  
ANISOU  691  CG  GLN A 297     1078   3716   4250    111     66    147       C  
ATOM    692  CD  GLN A 297       0.237   7.904  11.058  1.00 27.82           C  
ANISOU  692  CD  GLN A 297     1654   4248   4668    -88    470    -71       C  
ATOM    693  OE1 GLN A 297      -0.472   8.682  11.712  1.00 28.47           O  
ANISOU  693  OE1 GLN A 297     1632   4381   4806   -495    356   -188       O  
ATOM    694  NE2 GLN A 297       0.128   7.767   9.743  1.00 29.67           N  
ANISOU  694  NE2 GLN A 297     1996   4442   4835   -555    854   -215       N  
ATOM    695  N   LYS A 298       3.899   8.883  14.964  1.00 19.76           N  
ANISOU  695  N   LYS A 298     1154   3130   3224     78    166    569       N  
ATOM    696  CA  LYS A 298       4.114   9.500  16.266  1.00 20.52           C  
ANISOU  696  CA  LYS A 298     1393   3322   3081   -401    237    451       C  
ATOM    697  C   LYS A 298       5.037  10.707  16.208  1.00 21.26           C  
ANISOU  697  C   LYS A 298     1840   3303   2934    220    309    263       C  
ATOM    698  O   LYS A 298       5.168  11.443  17.190  1.00 20.66           O  
ANISOU  698  O   LYS A 298     1828   3221   2803    224    493   -147       O  
ATOM    699  CB  LYS A 298       4.632   8.474  17.269  1.00 22.42           C  
ANISOU  699  CB  LYS A 298     1455   3635   3428   -692    345    843       C  
ATOM    700  CG  LYS A 298       3.573   7.473  17.705  1.00 24.99           C  
ANISOU  700  CG  LYS A 298     1775   3899   3823   -639    368   1408       C  
ATOM    701  CD  LYS A 298       4.072   6.635  18.856  1.00 29.27           C  
ANISOU  701  CD  LYS A 298     2693   3986   4442   -497    894   1812       C  
ATOM    702  CE  LYS A 298       2.914   5.960  19.572  1.00 32.84           C  
ANISOU  702  CE  LYS A 298     3531   4131   4816   -489   1100   1712       C  
ATOM    703  NZ  LYS A 298       3.369   5.312  20.826  1.00 35.81           N  
ANISOU  703  NZ  LYS A 298     4103   4258   5244   -288   1256   1648       N  
ATOM    704  N   SER A 299       5.667  10.909  15.055  1.00 18.29           N  
ANISOU  704  N   SER A 299      956   3005   2989    450     70    392       N  
ATOM    705  CA  SER A 299       6.557  12.039  14.871  1.00 19.61           C  
ANISOU  705  CA  SER A 299     1188   3083   3178    669     49    368       C  
ATOM    706  C   SER A 299       5.889  13.195  14.131  1.00 18.03           C  
ANISOU  706  C   SER A 299      934   2968   2950    567   -126     21       C  
ATOM    707  O   SER A 299       6.539  14.192  13.832  1.00 20.71           O  
ANISOU  707  O   SER A 299     1584   3103   3181    582    288     14       O  
ATOM    708  CB  SER A 299       7.826  11.598  14.137  1.00 19.59           C  
ANISOU  708  CB  SER A 299     1257   2979   3206    822    157    422       C  
ATOM    709  OG  SER A 299       8.525  10.620  14.894  1.00 21.30           O  
ANISOU  709  OG  SER A 299     1398   3333   3362    407     46    626       O  
ATOM    710  N   LEU A 300       4.592  13.074  13.846  1.00 16.73           N  
ANISOU  710  N   LEU A 300      819   2855   2683    184   -211    -35       N  
ATOM    711  CA  LEU A 300       3.872  14.159  13.186  1.00 16.06           C  
ANISOU  711  CA  LEU A 300      930   2725   2446    516   -295   -270       C  
ATOM    712  C   LEU A 300       3.532  15.289  14.159  1.00 18.71           C  
ANISOU  712  C   LEU A 300     1702   2775   2630    454    323   -182       C  
ATOM    713  O   LEU A 300       3.134  15.040  15.300  1.00 21.40           O  
ANISOU  713  O   LEU A 300     2245   3137   2750    225    914    -88       O  
ATOM    714  CB  LEU A 300       2.591  13.634  12.526  1.00 17.02           C  
ANISOU  714  CB  LEU A 300     1202   2869   2397    200   -382   -329       C  
ATOM    715  CG  LEU A 300       2.796  12.705  11.329  1.00 19.28           C  
ANISOU  715  CG  LEU A 300     1799   2928   2596   -206   -322   -424       C  
ATOM    716  CD1 LEU A 300       1.456  12.181  10.833  1.00 21.21           C  
ANISOU  716  CD1 LEU A 300     1821   3188   3050    351   -511   -225       C  
ATOM    717  CD2 LEU A 300       3.532  13.432  10.207  1.00 21.17           C  
ANISOU  717  CD2 LEU A 300     2251   3083   2710    -88     33   -518       C  
ATOM    718  N   ARG A 301       3.680  16.528  13.699  1.00 17.97           N  
ANISOU  718  N   ARG A 301     1435   2464   2930    920    473   -215       N  
ATOM    719  CA  ARG A 301       3.400  17.702  14.527  1.00 17.93           C  
ANISOU  719  CA  ARG A 301     1242   2597   2973    663    606   -168       C  
ATOM    720  C   ARG A 301       2.643  18.738  13.715  1.00 18.08           C  
ANISOU  720  C   ARG A 301     1255   2535   3078    537    659   -297       C  
ATOM    721  O   ARG A 301       2.640  18.697  12.489  1.00 20.17           O  
ANISOU  721  O   ARG A 301     1905   2507   3253    450    251   -281       O  
ATOM    722  CB  ARG A 301       4.703  18.349  15.008  1.00 19.99           C  
ANISOU  722  CB  ARG A 301     1185   2790   3622    608    142    -47       C  
ATOM    723  CG  ARG A 301       5.603  17.462  15.837  1.00 22.10           C  
ANISOU  723  CG  ARG A 301     1722   2981   3693    386    -42    662       C  
ATOM    724  CD  ARG A 301       5.009  17.174  17.207  1.00 24.50           C  
ANISOU  724  CD  ARG A 301     1964   3254   4091    209      1    597       C  
ATOM    725  NE  ARG A 301       5.957  16.462  18.070  1.00 26.36           N  
ANISOU  725  NE  ARG A 301     2428   3314   4273    271   -470    653       N  
ATOM    726  CZ  ARG A 301       6.055  15.137  18.152  1.00 28.84           C  
ANISOU  726  CZ  ARG A 301     2940   3619   4399    367   -146    393       C  
ATOM    727  NH1 ARG A 301       5.259  14.361  17.425  1.00 29.22           N  
ANISOU  727  NH1 ARG A 301     3409   3647   4047    -77    -88     75       N  
ATOM    728  NH2 ARG A 301       6.949  14.585  18.967  1.00 30.66           N  
ANISOU  728  NH2 ARG A 301     3192   3696   4763    586   -259    527       N  
ATOM    729  N   ALA A 302       2.006  19.678  14.403  1.00 17.48           N  
ANISOU  729  N   ALA A 302     1112   2565   2963    325    380   -163       N  
ATOM    730  CA  ALA A 302       1.519  20.879  13.748  1.00 15.74           C  
ANISOU  730  CA  ALA A 302      983   2482   2514    490    534   -142       C  
ATOM    731  C   ALA A 302       2.714  21.570  13.086  1.00 19.33           C  
ANISOU  731  C   ALA A 302     1970   2566   2810    312    772   -223       C  
ATOM    732  O   ALA A 302       3.824  21.545  13.624  1.00 20.61           O  
ANISOU  732  O   ALA A 302     2375   2529   2928    495    614   -182       O  
ATOM    733  CB  ALA A 302       0.865  21.801  14.769  1.00 16.79           C  
ANISOU  733  CB  ALA A 302     1333   2527   2519    850    472   -205       C  
ATOM    734  N   VAL A 303       2.504  22.160  11.913  1.00 19.51           N  
ANISOU  734  N   VAL A 303     2123   2503   2786     77   1143   -420       N  
ATOM    735  CA  VAL A 303       3.583  22.877  11.244  1.00 20.38           C  
ANISOU  735  CA  VAL A 303     2185   2663   2897   -167   1059   -549       C  
ATOM    736  C   VAL A 303       3.904  24.163  12.006  1.00 21.56           C  
ANISOU  736  C   VAL A 303     2198   2618   3374    315   1162   -794       C  
ATOM    737  O   VAL A 303       3.002  24.937  12.327  1.00 23.27           O  
ANISOU  737  O   VAL A 303     2057   2895   3890    143   1355   -737       O  
ATOM    738  CB  VAL A 303       3.229  23.203   9.776  1.00 22.15           C  
ANISOU  738  CB  VAL A 303     2161   3061   3194   -294    806   -160       C  
ATOM    739  CG1 VAL A 303       4.397  23.899   9.081  1.00 22.27           C  
ANISOU  739  CG1 VAL A 303     1470   3423   3568   -171   1023    102       C  
ATOM    740  CG2 VAL A 303       2.845  21.935   9.028  1.00 21.83           C  
ANISOU  740  CG2 VAL A 303     2194   3114   2987    163    544   -325       C  
ATOM    741  N   PRO A 304       5.191  24.377  12.324  1.00 22.14           N  
ANISOU  741  N   PRO A 304     2324   2526   3563     92   1130  -1158       N  
ATOM    742  CA  PRO A 304       5.662  25.579  13.019  1.00 27.54           C  
ANISOU  742  CA  PRO A 304     2916   2787   4760    239   1080  -1049       C  
ATOM    743  C   PRO A 304       5.763  26.768  12.056  1.00 31.68           C  
ANISOU  743  C   PRO A 304     3048   2890   6097     54   1833  -1220       C  
ATOM    744  O   PRO A 304       5.609  26.571  10.849  1.00 30.72           O  
ANISOU  744  O   PRO A 304     2502   2742   6427    210   1486   -823       O  
ATOM    745  CB  PRO A 304       7.045  25.153  13.524  1.00 27.11           C  
ANISOU  745  CB  PRO A 304     3048   2823   4430    421    304  -1122       C  
ATOM    746  CG  PRO A 304       7.509  24.186  12.520  1.00 23.20           C  
ANISOU  746  CG  PRO A 304     2329   2645   3839    282     80  -1251       C  
ATOM    747  CD  PRO A 304       6.284  23.410  12.115  1.00 21.46           C  
ANISOU  747  CD  PRO A 304     1829   2726   3599    -27    125  -1237       C  
ATOM    748  N   PRO A 305       5.983  27.989  12.582  1.00 36.84           N  
ANISOU  748  N   PRO A 305     3644   3368   6984   -623   2341  -1321       N  
ATOM    749  CA  PRO A 305       6.093  29.195  11.750  1.00 40.59           C  
ANISOU  749  CA  PRO A 305     4418   3625   7379   -524   2471  -1224       C  
ATOM    750  C   PRO A 305       7.127  29.084  10.627  1.00 42.86           C  
ANISOU  750  C   PRO A 305     4519   3967   7799   -719   1953   -985       C  
ATOM    751  O   PRO A 305       6.795  29.282   9.455  1.00 48.01           O  
ANISOU  751  O   PRO A 305     5710   4225   8305   -650   1466   -640       O  
ATOM    752  CB  PRO A 305       6.535  30.262  12.754  1.00 41.94           C  
ANISOU  752  CB  PRO A 305     4980   3608   7347   -524   2602  -1365       C  
ATOM    753  CG  PRO A 305       5.918  29.830  14.035  1.00 41.32           C  
ANISOU  753  CG  PRO A 305     4827   3524   7349   -548   2453  -1417       C  
ATOM    754  CD  PRO A 305       5.953  28.321  14.020  1.00 39.20           C  
ANISOU  754  CD  PRO A 305     4230   3421   7243   -968   2098  -1375       C  
ATOM    755  N   ASN A 306       8.366  28.767  10.978  1.00 35.96           N  
ANISOU  755  N   ASN A 306     2808   3729   7126   -964   1645  -1159       N  
ATOM    756  CA  ASN A 306       9.423  28.712   9.972  1.00 34.69           C  
ANISOU  756  CA  ASN A 306     2588   3671   6922   -742   1613  -1159       C  
ATOM    757  C   ASN A 306      10.222  27.420  10.012  1.00 31.09           C  
ANISOU  757  C   ASN A 306     2203   3469   6142   -496   1371  -1224       C  
ATOM    758  O   ASN A 306      11.370  27.418  10.450  1.00 31.95           O  
ANISOU  758  O   ASN A 306     2339   3546   6255   -310   1493  -1364       O  
ATOM    759  CB  ASN A 306      10.366  29.905  10.126  1.00 39.52           C  
ANISOU  759  CB  ASN A 306     3310   4058   7647   -712   1369  -1171       C  
ATOM    760  CG  ASN A 306       9.671  31.226   9.884  1.00 43.55           C  
ANISOU  760  CG  ASN A 306     3967   4541   8038   -324   1199  -1169       C  
ATOM    761  OD1 ASN A 306       9.375  31.581   8.742  1.00 46.12           O  
ANISOU  761  OD1 ASN A 306     4406   4715   8401    173   1288   -959       O  
ATOM    762  ND2 ASN A 306       9.407  31.965  10.957  1.00 45.64           N  
ANISOU  762  ND2 ASN A 306     4427   4805   8109   -705    665  -1275       N  
ATOM    763  N   PRO A 307       9.624  26.314   9.548  1.00 26.33           N  
ANISOU  763  N   PRO A 307     1654   3258   5093   -342    579  -1247       N  
ATOM    764  CA  PRO A 307      10.361  25.050   9.616  1.00 23.94           C  
ANISOU  764  CA  PRO A 307     1639   3063   4393     11    853  -1196       C  
ATOM    765  C   PRO A 307      11.553  25.022   8.665  1.00 22.30           C  
ANISOU  765  C   PRO A 307     1434   2803   4236    134    590  -1077       C  
ATOM    766  O   PRO A 307      11.478  25.505   7.535  1.00 23.38           O  
ANISOU  766  O   PRO A 307     1699   2679   4505    318    408   -701       O  
ATOM    767  CB  PRO A 307       9.320  24.014   9.187  1.00 23.37           C  
ANISOU  767  CB  PRO A 307     1613   3048   4220   -300    495  -1328       C  
ATOM    768  CG  PRO A 307       8.381  24.777   8.318  1.00 25.14           C  
ANISOU  768  CG  PRO A 307     2035   2949   4569   -232    275  -1243       C  
ATOM    769  CD  PRO A 307       8.302  26.154   8.915  1.00 24.78           C  
ANISOU  769  CD  PRO A 307     1692   2934   4788   -682    563  -1216       C  
ATOM    770  N   THR A 308      12.658  24.479   9.154  1.00 21.21           N  
ANISOU  770  N   THR A 308     1260   2666   4134    100    318  -1088       N  
ATOM    771  CA  THR A 308      13.815  24.198   8.314  1.00 20.44           C  
ANISOU  771  CA  THR A 308     1215   2525   4028    132    261  -1034       C  
ATOM    772  C   THR A 308      14.328  22.811   8.647  1.00 21.11           C  
ANISOU  772  C   THR A 308     1271   2740   4011    -41    352  -1292       C  
ATOM    773  O   THR A 308      14.158  22.323   9.765  1.00 21.90           O  
ANISOU  773  O   THR A 308     1438   2780   4105    204    185  -1441       O  
ATOM    774  CB  THR A 308      14.947  25.210   8.537  1.00 24.61           C  
ANISOU  774  CB  THR A 308     1685   2792   4872     58    330  -1375       C  
ATOM    775  OG1 THR A 308      15.323  25.208   9.918  1.00 25.30           O  
ANISOU  775  OG1 THR A 308     1807   3062   4742    -29    124  -1467       O  
ATOM    776  CG2 THR A 308      14.513  26.610   8.129  1.00 25.39           C  
ANISOU  776  CG2 THR A 308     1996   2517   5135   -105    340  -1283       C  
ATOM    777  N   ILE A 309      14.961  22.181   7.666  1.00 21.34           N  
ANISOU  777  N   ILE A 309     1372   2855   3879    320    248  -1244       N  
ATOM    778  CA  ILE A 309      15.501  20.844   7.838  1.00 21.45           C  
ANISOU  778  CA  ILE A 309     1309   3182   3658    267    118  -1394       C  
ATOM    779  C   ILE A 309      16.548  20.810   8.946  1.00 24.46           C  
ANISOU  779  C   ILE A 309     1613   3646   4036   -277    506  -1422       C  
ATOM    780  O   ILE A 309      16.587  19.866   9.738  1.00 26.51           O  
ANISOU  780  O   ILE A 309     2068   3878   4126   -689   -150  -1411       O  
ATOM    781  CB  ILE A 309      16.065  20.314   6.506  1.00 23.21           C  
ANISOU  781  CB  ILE A 309     1752   3461   3607    834   -138  -1482       C  
ATOM    782  CG1 ILE A 309      14.892  20.059   5.554  1.00 23.83           C  
ANISOU  782  CG1 ILE A 309     1935   3758   3360    621   -371  -1335       C  
ATOM    783  CG2 ILE A 309      16.874  19.049   6.723  1.00 26.73           C  
ANISOU  783  CG2 ILE A 309     2660   3890   3607    765    487  -1423       C  
ATOM    784  CD1 ILE A 309      15.273  19.863   4.130  1.00 25.06           C  
ANISOU  784  CD1 ILE A 309     1879   3899   3743    363    189  -1193       C  
ATOM    785  N   ASP A 310      17.366  21.858   9.025  1.00 24.65           N  
ANISOU  785  N   ASP A 310     1782   3595   3989   -909    713  -1444       N  
ATOM    786  CA  ASP A 310      18.440  21.898  10.013  1.00 25.99           C  
ANISOU  786  CA  ASP A 310     1771   3828   4278   -686    916  -1365       C  
ATOM    787  C   ASP A 310      17.945  22.104  11.442  1.00 28.13           C  
ANISOU  787  C   ASP A 310     1923   4172   4593   -572    362  -1621       C  
ATOM    788  O   ASP A 310      18.736  22.085  12.379  1.00 31.26           O  
ANISOU  788  O   ASP A 310     2391   4507   4981   -667    214  -1783       O  
ATOM    789  CB  ASP A 310      19.536  22.918   9.640  1.00 30.01           C  
ANISOU  789  CB  ASP A 310     2413   3894   5094   -761   1317  -1407       C  
ATOM    790  CG  ASP A 310      19.010  24.342   9.483  1.00 32.99           C  
ANISOU  790  CG  ASP A 310     2907   4019   5608   -697   1554  -1006       C  
ATOM    791  OD1 ASP A 310      17.869  24.624   9.881  1.00 32.13           O  
ANISOU  791  OD1 ASP A 310     2653   3988   5568   -529    807   -927       O  
ATOM    792  OD2 ASP A 310      19.764  25.199   8.971  1.00 37.09           O  
ANISOU  792  OD2 ASP A 310     3844   4098   6150   -409   1621  -1188       O  
ATOM    793  N   LYS A 311      16.635  22.279  11.608  1.00 27.72           N  
ANISOU  793  N   LYS A 311     2149   4057   4326     25    537  -1634       N  
ATOM    794  CA  LYS A 311      16.044  22.349  12.939  1.00 28.82           C  
ANISOU  794  CA  LYS A 311     2460   4148   4343    174    316  -1584       C  
ATOM    795  C   LYS A 311      15.188  21.128  13.276  1.00 25.31           C  
ANISOU  795  C   LYS A 311     1574   4028   4015     46    -43  -1514       C  
ATOM    796  O   LYS A 311      14.448  21.138  14.263  1.00 25.70           O  
ANISOU  796  O   LYS A 311     1619   4087   4060     -2     38  -1481       O  
ATOM    797  CB  LYS A 311      15.236  23.636  13.105  1.00 30.02           C  
ANISOU  797  CB  LYS A 311     2448   4387   4571    -87   1091  -1732       C  
ATOM    798  CG  LYS A 311      16.081  24.901  13.002  1.00 37.37           C  
ANISOU  798  CG  LYS A 311     4178   4862   5157   -456    481  -1594       C  
ATOM    799  CD  LYS A 311      17.145  24.956  14.088  1.00 43.25           C  
ANISOU  799  CD  LYS A 311     5646   5138   5652   -329    604  -1492       C  
ATOM    800  CE  LYS A 311      18.044  26.177  13.918  1.00 47.17           C  
ANISOU  800  CE  LYS A 311     6752   5209   5961   -262    700  -1443       C  
ATOM    801  NZ  LYS A 311      17.260  27.443  13.870  1.00 49.93           N  
ANISOU  801  NZ  LYS A 311     7473   5327   6172   -421    859  -1398       N  
ATOM    802  N   GLY A 312      15.298  20.079  12.463  1.00 23.36           N  
ANISOU  802  N   GLY A 312     1329   3657   3890     69    242  -1354       N  
ATOM    803  CA  GLY A 312      14.628  18.820  12.744  1.00 22.15           C  
ANISOU  803  CA  GLY A 312     1408   3298   3708    325   -119  -1175       C  
ATOM    804  C   GLY A 312      13.311  18.615  12.014  1.00 19.88           C  
ANISOU  804  C   GLY A 312     1157   3013   3385    354   -256   -651       C  
ATOM    805  O   GLY A 312      12.585  17.657  12.281  1.00 21.60           O  
ANISOU  805  O   GLY A 312     1386   3245   3578    123    152    -59       O  
ATOM    806  N   TRP A 313      12.997  19.500  11.078  1.00 17.25           N  
ANISOU  806  N   TRP A 313     1065   2532   2959    217   -535   -805       N  
ATOM    807  CA  TRP A 313      11.732  19.394  10.358  1.00 17.42           C  
ANISOU  807  CA  TRP A 313      965   2718   2934    168   -358   -714       C  
ATOM    808  C   TRP A 313      11.978  18.764   9.003  1.00 20.23           C  
ANISOU  808  C   TRP A 313     1863   2566   3255    -30   -251   -680       C  
ATOM    809  O   TRP A 313      12.451  19.424   8.073  1.00 22.63           O  
ANISOU  809  O   TRP A 313     2341   2647   3609   -309    162   -749       O  
ATOM    810  CB  TRP A 313      11.093  20.771  10.229  1.00 19.30           C  
ANISOU  810  CB  TRP A 313     1064   3267   3004     94   -453   -652       C  
ATOM    811  CG  TRP A 313      10.829  21.379  11.559  1.00 20.52           C  
ANISOU  811  CG  TRP A 313     1113   3706   2976    204    238   -759       C  
ATOM    812  CD1 TRP A 313      11.575  22.334  12.191  1.00 22.72           C  
ANISOU  812  CD1 TRP A 313     1760   3772   3100    307    495   -920       C  
ATOM    813  CD2 TRP A 313       9.763  21.043  12.456  1.00 20.86           C  
ANISOU  813  CD2 TRP A 313     1040   3915   2970    198     12   -445       C  
ATOM    814  NE1 TRP A 313      11.023  22.628  13.417  1.00 23.52           N  
ANISOU  814  NE1 TRP A 313     1897   3945   3095    310    441   -735       N  
ATOM    815  CE2 TRP A 313       9.911  21.849  13.603  1.00 21.55           C  
ANISOU  815  CE2 TRP A 313     1211   3823   3154    476    398   -460       C  
ATOM    816  CE3 TRP A 313       8.692  20.146  12.395  1.00 22.91           C  
ANISOU  816  CE3 TRP A 313     1218   4352   3136    395    112   -566       C  
ATOM    817  CZ2 TRP A 313       9.028  21.784  14.681  1.00 25.96           C  
ANISOU  817  CZ2 TRP A 313     2050   4354   3461    643    350   -806       C  
ATOM    818  CZ3 TRP A 313       7.814  20.086  13.464  1.00 26.95           C  
ANISOU  818  CZ3 TRP A 313     2008   4718   3513    279    -56   -663       C  
ATOM    819  CH2 TRP A 313       7.986  20.899  14.590  1.00 26.31           C  
ANISOU  819  CH2 TRP A 313     2052   4483   3461    235    107  -1018       C  
ATOM    820  N   VAL A 314      11.654  17.479   8.899  1.00 17.53           N  
ANISOU  820  N   VAL A 314     1262   2312   3085    133   -590   -575       N  
ATOM    821  CA  VAL A 314      12.062  16.670   7.753  1.00 15.32           C  
ANISOU  821  CA  VAL A 314     1113   2189   2519   -102   -223   -933       C  
ATOM    822  C   VAL A 314      11.260  16.968   6.488  1.00 16.45           C  
ANISOU  822  C   VAL A 314     1158   2307   2787    100    242   -650       C  
ATOM    823  O   VAL A 314      11.819  17.101   5.398  1.00 17.51           O  
ANISOU  823  O   VAL A 314     1469   2146   3039    411    486   -523       O  
ATOM    824  CB  VAL A 314      11.934  15.171   8.067  1.00 16.72           C  
ANISOU  824  CB  VAL A 314     1599   2309   2445    -30     -6   -382       C  
ATOM    825  CG1 VAL A 314      12.283  14.345   6.852  1.00 17.48           C  
ANISOU  825  CG1 VAL A 314     1815   2375   2451   -340      0   -375       C  
ATOM    826  CG2 VAL A 314      12.809  14.795   9.258  1.00 17.70           C  
ANISOU  826  CG2 VAL A 314     1631   2621   2471   -341     80   -579       C  
ATOM    827  N   CYS A 315       9.940  17.060   6.641  1.00 15.45           N  
ANISOU  827  N   CYS A 315      832   2350   2687    193   -135   -662       N  
ATOM    828  CA  CYS A 315       9.043  17.333   5.525  1.00 15.57           C  
ANISOU  828  CA  CYS A 315      853   2404   2659    215    249   -519       C  
ATOM    829  C   CYS A 315       7.727  17.836   6.085  1.00 15.42           C  
ANISOU  829  C   CYS A 315      847   2510   2500    429    245   -255       C  
ATOM    830  O   CYS A 315       7.492  17.768   7.291  1.00 16.11           O  
ANISOU  830  O   CYS A 315      822   2857   2441     78    392    -83       O  
ATOM    831  CB  CYS A 315       8.789  16.075   4.692  1.00 17.78           C  
ANISOU  831  CB  CYS A 315     1290   2421   3044    260    311   -340       C  
ATOM    832  SG  CYS A 315       7.998  14.716   5.592  1.00 18.22           S  
ANISOU  832  SG  CYS A 315     1344   2565   3015    -84    115   -478       S  
ATOM    833  N   VAL A 316       6.881  18.343   5.199  1.00 14.35           N  
ANISOU  833  N   VAL A 316      653   2376   2425    276     55    -18       N  
ATOM    834  CA  VAL A 316       5.524  18.742   5.558  1.00 15.09           C  
ANISOU  834  CA  VAL A 316      741   2327   2665   -156     39   -363       C  
ATOM    835  C   VAL A 316       4.565  17.888   4.742  1.00 17.35           C  
ANISOU  835  C   VAL A 316      904   2703   2984   -264    320   -238       C  
ATOM    836  O   VAL A 316       4.629  17.885   3.516  1.00 18.69           O  
ANISOU  836  O   VAL A 316     1053   2965   3082    -91    583   -460       O  
ATOM    837  CB  VAL A 316       5.284  20.236   5.237  1.00 16.03           C  
ANISOU  837  CB  VAL A 316      824   2332   2936   -253    113   -360       C  
ATOM    838  CG1 VAL A 316       3.801  20.602   5.380  1.00 15.80           C  
ANISOU  838  CG1 VAL A 316      749   2467   2786   -249    150    -59       C  
ATOM    839  CG2 VAL A 316       6.150  21.120   6.138  1.00 16.63           C  
ANISOU  839  CG2 VAL A 316      976   2417   2926   -507   -115   -402       C  
ATOM    840  N   TYR A 317       3.696  17.139   5.416  1.00 14.65           N  
ANISOU  840  N   TYR A 317      728   2341   2499   -294    150   -198       N  
ATOM    841  CA  TYR A 317       2.701  16.351   4.708  1.00 15.00           C  
ANISOU  841  CA  TYR A 317      721   2269   2710    219     52   -144       C  
ATOM    842  C   TYR A 317       1.466  17.214   4.543  1.00 17.27           C  
ANISOU  842  C   TYR A 317      919   2662   2982    199   -210   -200       C  
ATOM    843  O   TYR A 317       1.031  17.875   5.489  1.00 18.31           O  
ANISOU  843  O   TYR A 317     1292   2727   2937    205   -192   -214       O  
ATOM    844  CB  TYR A 317       2.346  15.086   5.484  1.00 16.87           C  
ANISOU  844  CB  TYR A 317     1324   2068   3017    -35     61   -210       C  
ATOM    845  CG  TYR A 317       3.431  14.032   5.500  1.00 17.50           C  
ANISOU  845  CG  TYR A 317     1375   2116   3157    -13    282   -284       C  
ATOM    846  CD1 TYR A 317       3.653  13.226   4.393  1.00 18.06           C  
ANISOU  846  CD1 TYR A 317     1323   2201   3336    256    526   -376       C  
ATOM    847  CD2 TYR A 317       4.205  13.819   6.637  1.00 17.96           C  
ANISOU  847  CD2 TYR A 317     1401   2062   3360   -155    192   -389       C  
ATOM    848  CE1 TYR A 317       4.635  12.250   4.407  1.00 18.53           C  
ANISOU  848  CE1 TYR A 317     1354   2417   3269    417    479   -666       C  
ATOM    849  CE2 TYR A 317       5.183  12.847   6.662  1.00 18.28           C  
ANISOU  849  CE2 TYR A 317     1474   2237   3233     41     20   -571       C  
ATOM    850  CZ  TYR A 317       5.393  12.063   5.547  1.00 18.02           C  
ANISOU  850  CZ  TYR A 317     1173   2361   3313    467    287   -639       C  
ATOM    851  OH  TYR A 317       6.368  11.090   5.566  1.00 20.72           O  
ANISOU  851  OH  TYR A 317     1813   2498   3564    530    233   -793       O  
ATOM    852  N   SER A 318       0.911  17.210   3.339  1.00 17.55           N  
ANISOU  852  N   SER A 318      782   2865   3020    195    114    -42       N  
ATOM    853  CA  SER A 318      -0.250  18.031   3.029  1.00 19.33           C  
ANISOU  853  CA  SER A 318     1069   2822   3453    372   -428    -49       C  
ATOM    854  C   SER A 318      -1.374  17.146   2.515  1.00 17.11           C  
ANISOU  854  C   SER A 318      799   2703   2999    296     18    -62       C  
ATOM    855  O   SER A 318      -1.213  16.464   1.504  1.00 18.11           O  
ANISOU  855  O   SER A 318     1340   2522   3021    247    210   -115       O  
ATOM    856  CB  SER A 318       0.111  19.080   1.972  1.00 21.20           C  
ANISOU  856  CB  SER A 318     1050   3051   3955    192   -286    167       C  
ATOM    857  OG  SER A 318      -1.060  19.704   1.456  1.00 23.99           O  
ANISOU  857  OG  SER A 318     1197   3253   4664    224     67    176       O  
ATOM    858  N   SER A 319      -2.516  17.155   3.196  1.00 18.20           N  
ANISOU  858  N   SER A 319      834   2952   3128    149     20   -236       N  
ATOM    859  CA  SER A 319      -3.611  16.314   2.764  1.00 21.44           C  
ANISOU  859  CA  SER A 319     1058   3533   3555    477   -143   -250       C  
ATOM    860  C   SER A 319      -4.335  16.977   1.605  1.00 29.53           C  
ANISOU  860  C   SER A 319     2176   4569   4477   1138  -1125   -896       C  
ATOM    861  O   SER A 319      -4.055  18.129   1.256  1.00 32.44           O  
ANISOU  861  O   SER A 319     3068   4772   4485   1222  -1849  -1019       O  
ATOM    862  CB  SER A 319      -4.580  16.031   3.917  1.00 24.58           C  
ANISOU  862  CB  SER A 319     1343   3945   4050     66    541   -840       C  
ATOM    863  OG  SER A 319      -5.276  17.204   4.295  1.00 27.08           O  
ANISOU  863  OG  SER A 319     1777   4101   4410   -159    829  -1583       O  
ATOM    864  N   GLU A 320      -5.261  16.226   1.022  1.00 32.73           N  
ANISOU  864  N   GLU A 320     2703   4886   4846   1371  -1487  -1127       N  
ATOM    865  CA  GLU A 320      -6.077  16.657  -0.105  1.00 38.60           C  
ANISOU  865  CA  GLU A 320     3606   5421   5638   2080  -1658  -1532       C  
ATOM    866  C   GLU A 320      -6.651  18.069   0.091  1.00 41.68           C  
ANISOU  866  C   GLU A 320     4583   5244   6011   1879  -1833  -1977       C  
ATOM    867  O   GLU A 320      -6.733  18.866  -0.854  1.00 39.20           O  
ANISOU  867  O   GLU A 320     4381   4807   5707   1954  -2508  -1927       O  
ATOM    868  CB  GLU A 320      -7.212  15.642  -0.283  1.00 42.27           C  
ANISOU  868  CB  GLU A 320     4120   5984   5956   2347  -1472  -1803       C  
ATOM    869  CG  GLU A 320      -7.835  15.616  -1.655  1.00 48.03           C  
ANISOU  869  CG  GLU A 320     5531   6389   6330   2155  -1029  -1842       C  
ATOM    870  CD  GLU A 320      -7.034  14.789  -2.630  1.00 52.42           C  
ANISOU  870  CD  GLU A 320     6716   6491   6710   2182  -1084  -1633       C  
ATOM    871  OE1 GLU A 320      -6.412  13.797  -2.195  1.00 55.17           O  
ANISOU  871  OE1 GLU A 320     7551   6542   6869   2216  -1542  -1239       O  
ATOM    872  OE2 GLU A 320      -7.025  15.135  -3.830  1.00 53.41           O  
ANISOU  872  OE2 GLU A 320     6950   6572   6772   1955   -668  -1722       O  
ATOM    873  N   GLN A 321      -7.019  18.373   1.333  1.00 43.28           N  
ANISOU  873  N   GLN A 321     4770   5345   6328   1348   -921  -1951       N  
ATOM    874  CA  GLN A 321      -7.703  19.620   1.676  1.00 42.37           C  
ANISOU  874  CA  GLN A 321     4353   5170   6575    649   -517  -1931       C  
ATOM    875  C   GLN A 321      -6.737  20.738   2.050  1.00 40.68           C  
ANISOU  875  C   GLN A 321     4125   5067   6265    879  -1236  -1712       C  
ATOM    876  O   GLN A 321      -7.146  21.884   2.267  1.00 39.91           O  
ANISOU  876  O   GLN A 321     4154   4932   6078   1421  -1450  -1662       O  
ATOM    877  CB  GLN A 321      -8.646  19.385   2.854  1.00 42.57           C  
ANISOU  877  CB  GLN A 321     3842   5295   7038    163    639  -1644       C  
ATOM    878  CG  GLN A 321      -9.408  18.078   2.785  1.00 47.49           C  
ANISOU  878  CG  GLN A 321     4850   5506   7689    348    966  -1498       C  
ATOM    879  CD  GLN A 321      -9.813  17.585   4.157  1.00 52.25           C  
ANISOU  879  CD  GLN A 321     5603   5662   8587    322    582  -1241       C  
ATOM    880  OE1 GLN A 321      -9.014  16.972   4.868  1.00 54.11           O  
ANISOU  880  OE1 GLN A 321     5935   5700   8925    569    506  -1138       O  
ATOM    881  NE2 GLN A 321     -11.053  17.868   4.550  1.00 53.93           N  
ANISOU  881  NE2 GLN A 321     5842   5749   8899    287    322  -1303       N  
ATOM    882  N   GLY A 322      -5.459  20.403   2.147  1.00 36.45           N  
ANISOU  882  N   GLY A 322     3459   4765   5624    576  -2317  -1392       N  
ATOM    883  CA  GLY A 322      -4.475  21.377   2.570  1.00 36.98           C  
ANISOU  883  CA  GLY A 322     3922   4850   5278    459  -2420  -1512       C  
ATOM    884  C   GLY A 322      -4.330  21.424   4.077  1.00 36.31           C  
ANISOU  884  C   GLY A 322     3980   4926   4888    497  -2325  -1566       C  
ATOM    885  O   GLY A 322      -3.759  22.373   4.610  1.00 40.47           O  
ANISOU  885  O   GLY A 322     5349   4906   5121    499  -2106  -1884       O  
ATOM    886  N   GLU A 323      -4.848  20.415   4.775  1.00 31.13           N  
ANISOU  886  N   GLU A 323     2792   4861   4174   1039  -1618  -1507       N  
ATOM    887  CA  GLU A 323      -4.444  20.230   6.166  1.00 27.21           C  
ANISOU  887  CA  GLU A 323     1950   4549   3840   1141   -605  -1440       C  
ATOM    888  C   GLU A 323      -3.017  19.727   6.143  1.00 23.99           C  
ANISOU  888  C   GLU A 323     1764   3845   3506   1112   -165  -1010       C  
ATOM    889  O   GLU A 323      -2.653  18.917   5.283  1.00 26.76           O  
ANISOU  889  O   GLU A 323     2417   4175   3576   1065    -23   -781       O  
ATOM    890  CB  GLU A 323      -5.343  19.251   6.910  1.00 33.57           C  
ANISOU  890  CB  GLU A 323     3045   5138   4572   1573    412  -1627       C  
ATOM    891  CG  GLU A 323      -6.626  19.891   7.430  1.00 42.30           C  
ANISOU  891  CG  GLU A 323     4388   6003   5682   1951    795  -1333       C  
ATOM    892  CD  GLU A 323      -6.378  21.222   8.152  1.00 52.82           C  
ANISOU  892  CD  GLU A 323     6804   6760   6506   1953   1091   -743       C  
ATOM    893  OE1 GLU A 323      -6.049  21.204   9.361  1.00 56.10           O  
ANISOU  893  OE1 GLU A 323     7678   7148   6490   1765   1907   -633       O  
ATOM    894  OE2 GLU A 323      -6.514  22.292   7.510  1.00 55.81           O  
ANISOU  894  OE2 GLU A 323     7407   6811   6989   2289   1058   -549       O  
ATOM    895  N   THR A 324      -2.213  20.212   7.081  1.00 19.42           N  
ANISOU  895  N   THR A 324     1271   3114   2996    745   -161   -784       N  
ATOM    896  CA  THR A 324      -0.775  19.940   7.072  1.00 19.18           C  
ANISOU  896  CA  THR A 324     1290   2857   3143    881   -186   -325       C  
ATOM    897  C   THR A 324      -0.250  19.419   8.409  1.00 19.19           C  
ANISOU  897  C   THR A 324     1416   2856   3021    587    164   -190       C  
ATOM    898  O   THR A 324      -0.762  19.760   9.478  1.00 17.51           O  
ANISOU  898  O   THR A 324     1150   2695   2808    455    394   -277       O  
ATOM    899  CB  THR A 324       0.019  21.221   6.727  1.00 21.61           C  
ANISOU  899  CB  THR A 324     2182   2744   3284    881    178   -138       C  
ATOM    900  OG1 THR A 324      -0.271  22.232   7.700  1.00 20.21           O  
ANISOU  900  OG1 THR A 324     1799   2395   3485    764    238   -119       O  
ATOM    901  CG2 THR A 324      -0.356  21.734   5.351  1.00 23.31           C  
ANISOU  901  CG2 THR A 324     2938   2770   3147   1059    437   -161       C  
ATOM    902  N   ARG A 325       0.790  18.593   8.332  1.00 17.33           N  
ANISOU  902  N   ARG A 325     1007   2765   2812     79    -23   -141       N  
ATOM    903  CA  ARG A 325       1.530  18.158   9.506  1.00 17.16           C  
ANISOU  903  CA  ARG A 325      875   3135   2512   -180    196     22       C  
ATOM    904  C   ARG A 325       2.990  18.147   9.129  1.00 17.99           C  
ANISOU  904  C   ARG A 325     1090   3212   2533    119    446    -62       C  
ATOM    905  O   ARG A 325       3.330  17.771   8.017  1.00 21.79           O  
ANISOU  905  O   ARG A 325     1502   4001   2779    440    807   -269       O  
ATOM    906  CB  ARG A 325       1.134  16.738   9.904  1.00 19.76           C  
ANISOU  906  CB  ARG A 325     1639   3300   2570   -270   1094    115       C  
ATOM    907  CG  ARG A 325      -0.322  16.569  10.315  1.00 22.98           C  
ANISOU  907  CG  ARG A 325     1921   3733   3077     94   1380    -28       C  
ATOM    908  CD  ARG A 325      -0.612  17.217  11.651  1.00 25.23           C  
ANISOU  908  CD  ARG A 325     2062   4260   3265     26   1396    135       C  
ATOM    909  NE  ARG A 325      -1.977  16.930  12.090  1.00 26.79           N  
ANISOU  909  NE  ARG A 325     2034   4551   3593   -178   1463    123       N  
ATOM    910  CZ  ARG A 325      -3.033  17.681  11.790  1.00 29.13           C  
ANISOU  910  CZ  ARG A 325     1933   5023   4113   -482   1272    210       C  
ATOM    911  NH1 ARG A 325      -2.890  18.775  11.053  1.00 30.52           N  
ANISOU  911  NH1 ARG A 325     2148   5311   4139   -513    562    295       N  
ATOM    912  NH2 ARG A 325      -4.237  17.339  12.233  1.00 30.12           N  
ANISOU  912  NH2 ARG A 325     1851   5197   4396   -391   1232     84       N  
ATOM    913  N   ALA A 326       3.859  18.541  10.047  1.00 16.13           N  
ANISOU  913  N   ALA A 326      709   2661   2758    119    143    -15       N  
ATOM    914  CA  ALA A 326       5.291  18.388   9.802  1.00 16.09           C  
ANISOU  914  CA  ALA A 326      757   2362   2992     91     31     99       C  
ATOM    915  C   ALA A 326       5.836  17.144  10.498  1.00 16.89           C  
ANISOU  915  C   ALA A 326      941   2373   3103    481    159    131       C  
ATOM    916  O   ALA A 326       5.357  16.749  11.568  1.00 18.76           O  
ANISOU  916  O   ALA A 326     1462   2164   3502    217    284    591       O  
ATOM    917  CB  ALA A 326       6.050  19.637  10.234  1.00 17.48           C  
ANISOU  917  CB  ALA A 326     1296   2351   2993   -157    113   -249       C  
ATOM    918  N   LEU A 327       6.834  16.522   9.872  1.00 14.87           N  
ANISOU  918  N   LEU A 327      874   2193   2583    595     -6    -10       N  
ATOM    919  CA  LEU A 327       7.513  15.370  10.448  1.00 15.57           C  
ANISOU  919  CA  LEU A 327      935   1969   3013    341    179   -212       C  
ATOM    920  C   LEU A 327       8.730  15.849  11.244  1.00 17.51           C  
ANISOU  920  C   LEU A 327     1281   2216   3155     43    105   -397       C  
ATOM    921  O   LEU A 327       9.645  16.460  10.683  1.00 16.17           O  
ANISOU  921  O   LEU A 327      815   2232   3098   -101     10   -365       O  
ATOM    922  CB  LEU A 327       7.967  14.432   9.332  1.00 17.93           C  
ANISOU  922  CB  LEU A 327     1787   1939   3087    170    325   -505       C  
ATOM    923  CG  LEU A 327       8.588  13.099   9.748  1.00 19.40           C  
ANISOU  923  CG  LEU A 327     2222   2043   3105    508    532   -391       C  
ATOM    924  CD1 LEU A 327       7.574  12.271  10.512  1.00 21.75           C  
ANISOU  924  CD1 LEU A 327     2851   2138   3274    491    289   -319       C  
ATOM    925  CD2 LEU A 327       9.127  12.336   8.526  1.00 20.56           C  
ANISOU  925  CD2 LEU A 327     2461   2110   3243    763    541   -510       C  
ATOM    926  N   LYS A 328       8.743  15.572  12.542  1.00 18.44           N  
ANISOU  926  N   LYS A 328     1256   2575   3175     94    -60   -418       N  
ATOM    927  CA  LYS A 328       9.778  16.100  13.429  1.00 19.72           C  
ANISOU  927  CA  LYS A 328      998   2976   3519    172     -3   -620       C  
ATOM    928  C   LYS A 328      10.756  15.017  13.863  1.00 23.08           C  
ANISOU  928  C   LYS A 328     1727   3032   4010   -109   -523   -226       C  
ATOM    929  O   LYS A 328      10.350  13.918  14.242  1.00 24.76           O  
ANISOU  929  O   LYS A 328     2043   3027   4337   -465   -588    -23       O  
ATOM    930  CB  LYS A 328       9.144  16.741  14.668  1.00 22.01           C  
ANISOU  930  CB  LYS A 328     1162   3472   3730    -33     13  -1038       C  
ATOM    931  CG  LYS A 328      10.149  17.345  15.655  1.00 27.33           C  
ANISOU  931  CG  LYS A 328     2006   4023   4354   -410   -455  -1530       C  
ATOM    932  CD  LYS A 328      10.708  18.647  15.109  1.00 34.66           C  
ANISOU  932  CD  LYS A 328     3774   4620   4777   -762   -822  -1767       C  
ATOM    933  CE  LYS A 328      11.698  19.292  16.066  1.00 40.25           C  
ANISOU  933  CE  LYS A 328     5119   5160   5014   -765  -1335  -1916       C  
ATOM    934  NZ  LYS A 328      11.173  19.401  17.463  1.00 44.10           N  
ANISOU  934  NZ  LYS A 328     5926   5524   5306  -1068  -2313  -1857       N  
ATOM    935  N   ILE A 329      12.045  15.346  13.816  1.00 22.44           N  
ANISOU  935  N   ILE A 329     1534   3134   3858   -181   -582   -389       N  
ATOM    936  CA  ILE A 329      13.104  14.416  14.162  1.00 25.08           C  
ANISOU  936  CA  ILE A 329     2000   3502   4026    -28   -457   -834       C  
ATOM    937  C   ILE A 329      14.103  15.100  15.104  1.00 28.97           C  
ANISOU  937  C   ILE A 329     2802   3700   4506    585   -656   -720       C  
ATOM    938  O   ILE A 329      14.023  16.308  15.346  1.00 27.81           O  
ANISOU  938  O   ILE A 329     2161   3812   4595    280   -805   -609       O  
ATOM    939  CB  ILE A 329      13.816  13.948  12.875  1.00 27.78           C  
ANISOU  939  CB  ILE A 329     2597   3734   4224    254    175  -1041       C  
ATOM    940  CG1 ILE A 329      14.359  12.529  13.015  1.00 31.46           C  
ANISOU  940  CG1 ILE A 329     3633   3991   4330   -226     -3   -807       C  
ATOM    941  CG2 ILE A 329      14.894  14.942  12.457  1.00 28.35           C  
ANISOU  941  CG2 ILE A 329     2507   3947   4316     39    554   -844       C  
ATOM    942  CD1 ILE A 329      14.686  11.905  11.676  1.00 28.57           C  
ANISOU  942  CD1 ILE A 329     2874   3816   4165   -302    300   -929       C  
ATOM    943  OXT ILE A 329      15.013  14.480  15.662  1.00 31.27           O  
ANISOU  943  OXT ILE A 329     3236   3918   4726    627  -1197   -950       O  
TER     944      ILE A 329                                                      
HETATM  945  C   ACT A 401      26.673  18.387  15.630  1.00 37.65           C  
ANISOU  945  C   ACT A 401     4020   4507   5780    468   -485    730       C  
HETATM  946  O   ACT A 401      25.754  19.198  15.392  1.00 39.17           O  
ANISOU  946  O   ACT A 401     4370   4642   5870    259  -1111    903       O  
HETATM  947  OXT ACT A 401      26.391  17.440  16.399  1.00 33.86           O  
ANISOU  947  OXT ACT A 401     3338   4162   5365    652   -731    848       O  
HETATM  948  CH3 ACT A 401      28.035  18.541  15.024  1.00 37.83           C  
ANISOU  948  CH3 ACT A 401     3821   4597   5956    144   -499    755       C  
HETATM  949  C   ACT A 402      27.597   2.486   2.018  1.00 30.59           C  
ANISOU  949  C   ACT A 402     2215   4056   5352  -1159    363  -1445       C  
HETATM  950  O   ACT A 402      27.433   3.289   2.959  1.00 29.52           O  
ANISOU  950  O   ACT A 402     2173   3657   5385   -987    828  -1657       O  
HETATM  951  OXT ACT A 402      28.409   2.843   1.130  1.00 30.45           O  
ANISOU  951  OXT ACT A 402     2043   4221   5308   -989    340  -1541       O  
HETATM  952  CH3 ACT A 402      26.862   1.172   1.967  1.00 29.97           C  
ANISOU  952  CH3 ACT A 402     2156   4068   5164  -1123    194  -1430       C  
HETATM  953  C   ACT A 403       1.750  27.671  10.718  1.00 54.96           C  
ANISOU  953  C   ACT A 403     8352   6221   6308    923  -1012    483       C  
HETATM  954  O   ACT A 403       2.670  27.635   9.871  1.00 53.94           O  
ANISOU  954  O   ACT A 403     8323   6195   5977   1004   -929    464       O  
HETATM  955  OXT ACT A 403       0.788  26.897  10.515  1.00 56.45           O  
ANISOU  955  OXT ACT A 403     8593   6307   6548    874  -1011    397       O  
HETATM  956  CH3 ACT A 403       1.796  28.585  11.908  1.00 53.89           C  
ANISOU  956  CH3 ACT A 403     8158   6134   6185    946   -936    474       C  
HETATM  957  C   ACT A 404      16.661  -3.474  11.901  1.00 53.98           C  
ANISOU  957  C   ACT A 404     8477   4201   7832   1985   -336    152       C  
HETATM  958  O   ACT A 404      17.794  -3.707  11.424  1.00 54.07           O  
ANISOU  958  O   ACT A 404     8416   4116   8010   2488   -623    106       O  
HETATM  959  OXT ACT A 404      15.690  -3.642  11.132  1.00 54.11           O  
ANISOU  959  OXT ACT A 404     8611   4228   7718   1940   -353    192       O  
HETATM  960  CH3 ACT A 404      16.477  -3.018  13.317  1.00 54.15           C  
ANISOU  960  CH3 ACT A 404     8522   4201   7854   1748   -140    108       C  
HETATM  961  C   ACT A 405      18.623  20.295  14.929  1.00 53.56           C  
ANISOU  961  C   ACT A 405     6756   7585   6009   2264    383   1994       C  
HETATM  962  O   ACT A 405      19.555  19.558  14.541  1.00 50.08           O  
ANISOU  962  O   ACT A 405     5889   7470   5670   2886   -160   2205       O  
HETATM  963  OXT ACT A 405      17.468  19.849  14.749  1.00 55.43           O  
ANISOU  963  OXT ACT A 405     6976   7676   6408   2062    735   1948       O  
HETATM  964  CH3 ACT A 405      18.869  21.633  15.565  1.00 53.21           C  
ANISOU  964  CH3 ACT A 405     6858   7521   5837   2175    477   1634       C  
HETATM  965  C   ACT A 406       3.491   1.554   6.707  1.00 50.71           C  
ANISOU  965  C   ACT A 406     6623   4776   7868   1236  -1202  -1902       C  
HETATM  966  O   ACT A 406       4.208   0.652   7.191  1.00 52.96           O  
ANISOU  966  O   ACT A 406     7111   4972   8039   1323   -993  -1825       O  
HETATM  967  OXT ACT A 406       2.592   1.993   7.453  1.00 49.94           O  
ANISOU  967  OXT ACT A 406     6539   4617   7821    939  -1300  -1935       O  
HETATM  968  CH3 ACT A 406       3.700   2.078   5.316  1.00 49.88           C  
ANISOU  968  CH3 ACT A 406     6434   4774   7743   1246  -1290  -2004       C  
HETATM  969  O   HOH A 501      16.743   0.363   6.457  1.00 24.21           O  
ANISOU  969  O   HOH A 501     1542   2115   5541     71    207  -1161       O  
HETATM  970  O   HOH A 502       7.444   8.173  14.731  1.00 22.25           O  
ANISOU  970  O   HOH A 502     2379   2146   3930    229    455     22       O  
HETATM  971  O   HOH A 503      15.753   4.430  11.343  1.00 20.69           O  
ANISOU  971  O   HOH A 503     1288   2097   4478   -204   -180   -844       O  
HETATM  972  O   HOH A 504      19.988   6.693  17.241  1.00 18.76           O  
ANISOU  972  O   HOH A 504     1176   2212   3738     67   -175    435       O  
HETATM  973  O   HOH A 505       1.745  19.075  17.375  1.00 27.93           O  
ANISOU  973  O   HOH A 505     2849   4412   3352   1502    -21   -535       O  
HETATM  974  O   HOH A 506      29.611  21.381   4.482  1.00 22.94           O  
ANISOU  974  O   HOH A 506     1312   3324   4082     67    632    792       O  
HETATM  975  O   HOH A 507      -0.188  22.236  10.938  1.00 24.06           O  
ANISOU  975  O   HOH A 507     2768   2956   3419    863    365     63       O  
HETATM  976  O   HOH A 508      21.308  23.203  -1.135  1.00 24.00           O  
ANISOU  976  O   HOH A 508     3173   2357   3588    965   -337   -174       O  
HETATM  977  O   HOH A 509      21.143   4.297  14.011  1.00 24.40           O  
ANISOU  977  O   HOH A 509     1674   1813   5784    219   -683   -455       O  
HETATM  978  O   HOH A 510      19.428  13.903  16.730  1.00 29.88           O  
ANISOU  978  O   HOH A 510     2906   4862   3585   1651   1353   1305       O  
HETATM  979  O   HOH A 511      14.393  16.944  -0.704  1.00 27.16           O  
ANISOU  979  O   HOH A 511     1934   3177   5208    230  -1094  -1470       O  
HETATM  980  O   HOH A 512       6.455   9.550   3.155  1.00 31.09           O  
ANISOU  980  O   HOH A 512     3207   4842   3764   1949   -235  -1455       O  
HETATM  981  O   HOH A 513      32.237   4.424   7.373  1.00 33.56           O  
ANISOU  981  O   HOH A 513     4199   2620   5931   1004   1540    825       O  
HETATM  982  O   HOH A 514      -1.645   9.308  -0.830  1.00 29.83           O  
ANISOU  982  O   HOH A 514     1474   4060   5799    186    -46    260       O  
HETATM  983  O   HOH A 515      25.676  15.528  -6.661  1.00 24.10           O  
ANISOU  983  O   HOH A 515     1961   3181   4013   -107   -568    534       O  
HETATM  984  O   HOH A 516      19.152   0.000   0.000  0.50 31.34           O  
ANISOU  984  O   HOH A 516     4026   3159   4721      0      0    230       O  
HETATM  985  O   HOH A 517      17.527   9.667  -8.290  1.00 29.56           O  
ANISOU  985  O   HOH A 517     3468   2913   4850    114   -843   -943       O  
HETATM  986  O   HOH A 518      33.372   7.436   1.683  1.00 37.15           O  
ANISOU  986  O   HOH A 518     4505   3677   5933   -942   2552   -605       O  
HETATM  987  O   HOH A 519      14.544  -0.225   4.917  1.00 40.18           O  
ANISOU  987  O   HOH A 519     2557   4741   7970   -401   -731  -1959       O  
HETATM  988  O   HOH A 520      30.813  20.212   1.945  1.00 31.42           O  
ANISOU  988  O   HOH A 520     3088   4407   4442    308    325  -1833       O  
HETATM  989  O   HOH A 521      24.330   2.797  11.700  1.00 36.59           O  
ANISOU  989  O   HOH A 521     4744   2725   6434   -270  -2251  -1066       O  
HETATM  990  O   HOH A 522      11.221  11.346  15.077  1.00 29.46           O  
ANISOU  990  O   HOH A 522     2121   4130   4940   -118   -697  -1250       O  
HETATM  991  O   HOH A 523      17.637  23.545   6.724  1.00 33.49           O  
ANISOU  991  O   HOH A 523     4316   3666   4741   -463    965  -1322       O  
HETATM  992  O   HOH A 524      12.228   1.534   4.572  1.00 28.42           O  
ANISOU  992  O   HOH A 524     1838   4906   4055     -6    -82  -1549       O  
HETATM  993  O   HOH A 525      25.242  26.987   3.183  1.00 31.07           O  
ANISOU  993  O   HOH A 525     4920   3729   3154    218    958   -585       O  
HETATM  994  O   HOH A 526      10.406   0.290  11.628  1.00 36.74           O  
ANISOU  994  O   HOH A 526     2549   4301   7108    741   1548    969       O  
HETATM  995  O   HOH A 527      32.111  14.323   8.255  1.00 33.68           O  
ANISOU  995  O   HOH A 527     2560   3172   7065   -245  -1238  -1294       O  
HETATM  996  O   HOH A 528      19.114  11.595  -8.694  1.00 30.81           O  
ANISOU  996  O   HOH A 528     3457   3991   4259   -451   -921  -1283       O  
HETATM  997  O   HOH A 529      -7.980  14.264   3.453  1.00 30.65           O  
ANISOU  997  O   HOH A 529     2426   4212   5006    568   -342    777       O  
HETATM  998  O   HOH A 530      13.829  19.511  -1.191  1.00 34.14           O  
ANISOU  998  O   HOH A 530     2729   4764   5479   1066   -538   -267       O  
HETATM  999  O   HOH A 531      23.682   6.189  -8.890  1.00 38.78           O  
ANISOU  999  O   HOH A 531     5123   5029   4583    428   1587  -1834       O  
HETATM 1000  O   HOH A 532       4.724   6.080  14.857  1.00 29.00           O  
ANISOU 1000  O   HOH A 532     1633   3083   6301    -95   -389   -324       O  
HETATM 1001  O   HOH A 533      25.829  12.843  16.557  1.00 32.62           O  
ANISOU 1001  O   HOH A 533     2922   6115   3358  -1871   -261    411       O  
HETATM 1002  O   HOH A 534      38.044   7.447  10.758  1.00 35.50           O  
ANISOU 1002  O   HOH A 534     2854   4224   6410    430   -460    504       O  
HETATM 1003  O   HOH A 535      -0.695  10.128  14.255  1.00 31.41           O  
ANISOU 1003  O   HOH A 535     3178   4766   3989    391    274    706       O  
HETATM 1004  O   HOH A 536      30.611  15.814  -4.205  1.00 34.21           O  
ANISOU 1004  O   HOH A 536     3127   3630   6240    783     86    366       O  
HETATM 1005  O   HOH A 537      15.674  29.382   5.695  1.00 34.98           O  
ANISOU 1005  O   HOH A 537     3406   3892   5993    638   -558  -1502       O  
HETATM 1006  O   HOH A 538      26.044  -0.977   4.695  1.00 36.55           O  
ANISOU 1006  O   HOH A 538     2355   6948   4583    607   -304  -1175       O  
HETATM 1007  O   HOH A 539      -0.631  24.597   9.813  1.00 36.91           O  
ANISOU 1007  O   HOH A 539     4480   5132   4414   1640   1389   -438       O  
HETATM 1008  O   HOH A 540      29.259  14.598  -6.370  1.00 37.43           O  
ANISOU 1008  O   HOH A 540     2721   4309   7190    770    243  -1002       O  
HETATM 1009  O   HOH A 541      29.175   3.356  13.165  1.00 31.97           O  
ANISOU 1009  O   HOH A 541     2743   3495   5909   -762   -323    465       O  
HETATM 1010  O   HOH A 542       0.000   8.755  16.481  0.50 29.17           O  
ANISOU 1010  O   HOH A 542     2520   3796   4766      0     -8      0       O  
HETATM 1011  O   HOH A 543       4.670  22.350  16.063  1.00 39.84           O  
ANISOU 1011  O   HOH A 543     3620   8221   3297    376   -831  -1907       O  
HETATM 1012  O   HOH A 544       3.957  15.046  -3.206  1.00 37.99           O  
ANISOU 1012  O   HOH A 544     4131   6472   3832  -2140   1064  -1989       O  
HETATM 1013  O   HOH A 545      -3.026   9.573  11.176  1.00 32.22           O  
ANISOU 1013  O   HOH A 545     1610   5287   5343    156    628    638       O  
HETATM 1014  O   HOH A 546       0.000   6.016  16.481  0.50 35.53           O  
ANISOU 1014  O   HOH A 546     2499   4693   6309      0    575      0       O  
HETATM 1015  O   HOH A 547      19.498   1.997  -8.511  1.00 47.07           O  
ANISOU 1015  O   HOH A 547     9082   3411   5392  -2298    197   -676       O  
HETATM 1016  O   HOH A 548      31.012  25.081   2.857  1.00 50.01           O  
ANISOU 1016  O   HOH A 548     4182   9280   5539  -2997   -872   1223       O  
HETATM 1017  O   HOH A 549      17.293  17.124  11.068  1.00 40.27           O  
ANISOU 1017  O   HOH A 549     2020   6967   6314    346    800    649       O  
HETATM 1018  O   HOH A 550      31.006   8.546  18.094  1.00 32.74           O  
ANISOU 1018  O   HOH A 550     4415   2967   5058   -592  -1835   -102       O  
HETATM 1019  O   HOH A 551      15.594   5.752  -2.725  1.00 45.58           O  
ANISOU 1019  O   HOH A 551     5304   5297   6717  -1673  -2796   -469       O  
HETATM 1020  O   HOH A 552      20.238  21.658  -2.957  1.00 33.97           O  
ANISOU 1020  O   HOH A 552     5379   2812   4716   -435    523   -174       O  
HETATM 1021  O   HOH A 553      10.387   2.094  13.775  1.00 46.13           O  
ANISOU 1021  O   HOH A 553     4506   5939   7082   1879   2432   1261       O  
HETATM 1022  O   HOH A 554      -2.092  21.726  12.895  1.00 49.79           O  
ANISOU 1022  O   HOH A 554     3934   9934   5048  -2317   1228   -619       O  
HETATM 1023  O   HOH A 555      10.484  16.581  -2.758  1.00 41.23           O  
ANISOU 1023  O   HOH A 555     5513   4889   5264   -429   1149  -1415       O  
HETATM 1024  O   HOH A 556      29.966   6.153  19.250  1.00 42.88           O  
ANISOU 1024  O   HOH A 556     2745   4648   8898   -485   -890  -1554       O  
HETATM 1025  O   HOH A 557      13.164  26.157  11.910  1.00 54.11           O  
ANISOU 1025  O   HOH A 557     9414   4219   6925   2104     36  -2067       O  
HETATM 1026  O   HOH A 558      29.413   1.611  -0.798  1.00 47.84           O  
ANISOU 1026  O   HOH A 558     3366   7244   7567  -1081   1211  -4325       O  
HETATM 1027  O   HOH A 559      13.347  -4.319   9.771  1.00 50.77           O  
ANISOU 1027  O   HOH A 559     4940   7180   7171   1234  -2064  -1673       O  
HETATM 1028  O   HOH A 560      -0.163   4.574   8.326  1.00 44.12           O  
ANISOU 1028  O   HOH A 560     3733   7538   5493  -2079   -147   2524       O  
HETATM 1029  O   HOH A 561      33.277  13.991  15.897  1.00 42.14           O  
ANISOU 1029  O   HOH A 561     4187   8569   3256   1028    511    -44       O  
HETATM 1030  O   HOH A 562       3.943  11.644  19.723  1.00 49.63           O  
ANISOU 1030  O   HOH A 562     5653   7956   5247    717   3038   1111       O  
HETATM 1031  O   HOH A 563      28.820  24.005   6.892  1.00 52.28           O  
ANISOU 1031  O   HOH A 563     6593   5639   7633  -3634    125   -183       O  
HETATM 1032  O   HOH A 564       7.774  17.209  -2.579  1.00 42.87           O  
ANISOU 1032  O   HOH A 564     2785   8525   4977    986    330  -2077       O  
HETATM 1033  O   HOH A 565      30.269  19.344   6.517  1.00 43.41           O  
ANISOU 1033  O   HOH A 565     2607   7083   6803    662  -1652   -528       O  
HETATM 1034  O   HOH A 566      34.222  14.450   6.028  1.00 41.27           O  
ANISOU 1034  O   HOH A 566     3356   5064   7262  -1342  -1926   1565       O  
HETATM 1035  O   HOH A 567      20.134  11.247 -11.428  1.00 47.69           O  
ANISOU 1035  O   HOH A 567     5818   6329   5971  -2239   1069  -2023       O  
HETATM 1036  O   HOH A 568      30.883  23.999   5.340  1.00 48.45           O  
ANISOU 1036  O   HOH A 568     3761   8919   5730  -2222  -1247   -320       O  
HETATM 1037  O   HOH A 569      26.179  22.037  15.220  1.00 53.18           O  
ANISOU 1037  O   HOH A 569     4926   6094   9187   -998  -2046    505       O  
HETATM 1038  O   HOH A 570      19.367   5.922 -10.061  1.00 49.01           O  
ANISOU 1038  O   HOH A 570     8870   5584   4167  -1795    688  -1778       O  
HETATM 1039  O   HOH A 571      15.506  20.013  -3.113  1.00 46.55           O  
ANISOU 1039  O   HOH A 571     2891   9043   5752   -513  -1116   -611       O  
HETATM 1040  O   HOH A 572       1.330  10.132  -0.942  1.00 54.81           O  
ANISOU 1040  O   HOH A 572     9012   5454   6360   3691   2113    707       O  
HETATM 1041  O   HOH A 573      17.125   7.875 -10.216  1.00 49.30           O  
ANISOU 1041  O   HOH A 573     7338   5569   5825  -1010  -2313  -2304       O  
HETATM 1042  O   HOH A 574      15.295  10.173  -6.365  1.00 41.26           O  
ANISOU 1042  O   HOH A 574     3321   4855   7502    343   2067    -16       O  
HETATM 1043  O   HOH A 575      36.462  14.044   6.628  1.00 27.73           O  
ANISOU 1043  O   HOH A 575     2693   3869   3975  -1480   1309  -1864       O  
HETATM 1044  O   HOH A 576       0.388  16.813  17.511  1.00 47.05           O  
ANISOU 1044  O   HOH A 576     6658   6275   4944    583  -1242  -1800       O  
HETATM 1045  O   HOH A 577      33.031  26.669   2.908  1.00 40.28           O  
ANISOU 1045  O   HOH A 577     4987   4975   5340  -2861    511    527       O  
HETATM 1046  O   HOH A 578      32.446   4.937  19.294  1.00 36.90           O  
ANISOU 1046  O   HOH A 578     2998   3892   7130   -570    617   1587       O  
HETATM 1047  O   HOH A 579      -7.385   6.334   4.991  1.00 45.99           O  
ANISOU 1047  O   HOH A 579     3116   2941  11416    -72   1210   -543       O  
HETATM 1048  O   HOH A 580      17.406  17.062  13.734  1.00 36.29           O  
ANISOU 1048  O   HOH A 580     3820   5204   4764   -766  -1091   1292       O  
HETATM 1049  O   HOH A 581      29.464  17.448  11.328  1.00 51.97           O  
ANISOU 1049  O   HOH A 581     4159   4708  10880    418   1883   3178       O  
HETATM 1050  O   HOH A 582      25.493  -3.061   6.786  1.00 56.19           O  
ANISOU 1050  O   HOH A 582     6560   6655   8135  -3732   -108  -1382       O  
HETATM 1051  O   HOH A 583      22.212   1.772  13.085  1.00 50.33           O  
ANISOU 1051  O   HOH A 583     4258   4208  10659   1047  -2820  -2574       O  
HETATM 1052  O   HOH A 584      -3.371  14.323  12.583  1.00 48.78           O  
ANISOU 1052  O   HOH A 584     8288   5487   4761  -2298   -270    916       O  
HETATM 1053  O   HOH A 585      28.314  11.314  -6.784  1.00 56.75           O  
ANISOU 1053  O   HOH A 585     7305   7066   7191   2301   1014   -757       O  
HETATM 1054  O   HOH A 586      14.721   7.816  -2.820  1.00 46.89           O  
ANISOU 1054  O   HOH A 586     2412   7204   8201   1132    269   -639       O  
HETATM 1055  O   HOH A 587      -9.482  14.235  -4.408  1.00 42.65           O  
ANISOU 1055  O   HOH A 587     3346   6562   6296    670    826   1861       O  
HETATM 1056  O   HOH A 588      10.977  11.561  17.877  1.00 53.33           O  
ANISOU 1056  O   HOH A 588     6892   5368   8004  -2015    892    438       O  
HETATM 1057  O   HOH A 589       7.549   6.665   2.803  1.00 56.05           O  
ANISOU 1057  O   HOH A 589     7495   6844   6959  -3107   2260  -2555       O  
HETATM 1058  O   HOH A 590      16.190   9.746  -2.981  1.00 43.74           O  
ANISOU 1058  O   HOH A 590     3666   6284   6671   1940    934    594       O  
HETATM 1059  O   HOH A 591      25.274  28.592   5.103  1.00 52.30           O  
ANISOU 1059  O   HOH A 591    10666   3392   5815  -1473    845   -505       O  
HETATM 1060  O   HOH A 592       0.481   3.843   6.092  1.00 62.72           O  
ANISOU 1060  O   HOH A 592     4649  10378   8804  -1578  -3014   -321       O  
HETATM 1061  O   HOH A 593      26.098   0.799   9.946  1.00 50.03           O  
ANISOU 1061  O   HOH A 593     3243   9411   6354    780   -512  -3145       O  
HETATM 1062  O   HOH A 594      32.317  16.610   6.984  1.00 51.66           O  
ANISOU 1062  O   HOH A 594     7370   6424   5832  -3971   -722   -325       O  
HETATM 1063  O   HOH A 595       6.660   5.258  16.576  1.00 50.42           O  
ANISOU 1063  O   HOH A 595     5384   7297   6476  -2167  -2968    802       O  
HETATM 1064  O   HOH A 596       3.560   8.858   2.601  1.00 44.15           O  
ANISOU 1064  O   HOH A 596     4972   6215   5586   1615   1089   -707       O  
HETATM 1065  O   HOH A 597      12.250  15.216  -1.109  1.00 29.64           O  
ANISOU 1065  O   HOH A 597     2531   4740   3993    772   -320   -120       O  
HETATM 1066  O   HOH A 598      22.795  24.541  11.674  1.00 52.47           O  
ANISOU 1066  O   HOH A 598     6897   6279   6760   -110    658  -2184       O  
HETATM 1067  O   HOH A 599      17.414  13.795  -8.223  1.00 54.66           O  
ANISOU 1067  O   HOH A 599     6249   7239   7281  -1274  -2068    664       O  
HETATM 1068  O   HOH A 600      -9.706  15.094   2.276  1.00 42.05           O  
ANISOU 1068  O   HOH A 600     3094   6960   5922  -2067    963  -1003       O  
HETATM 1069  O   HOH A 601      11.285   4.023   0.528  1.00 55.25           O  
ANISOU 1069  O   HOH A 601     3121   6936  10935    747   1228   -314       O  
HETATM 1070  O   HOH A 602       0.000  25.385  16.481  0.50 49.58           O  
ANISOU 1070  O   HOH A 602     6747   5893   6198      0   1971      0       O  
HETATM 1071  O   HOH A 603      11.396   4.809   3.120  1.00 54.89           O  
ANISOU 1071  O   HOH A 603     3867  11494   5495   -790   -451  -3206       O  
HETATM 1072  O   HOH A 604      29.122  23.450   9.507  1.00 60.86           O  
ANISOU 1072  O   HOH A 604     9534   6367   7222  -4002   1158   1080       O  
HETATM 1073  O   HOH A 605      10.036  27.691   6.404  1.00 48.79           O  
ANISOU 1073  O   HOH A 605     3925   4763   9852      1   2832    637       O  
HETATM 1074  O   HOH A 606       3.145  12.128  -2.753  1.00 51.46           O  
ANISOU 1074  O   HOH A 606     6012   7253   6289   -236   2556  -2518       O  
HETATM 1075  O   HOH A 607      20.496  24.177  13.576  1.00 60.33           O  
ANISOU 1075  O   HOH A 607     6212   9575   7137  -2639    609  -4224       O  
HETATM 1076  O   HOH A 608       2.716  25.828  15.288  1.00 57.18           O  
ANISOU 1076  O   HOH A 608     4320   8481   8924    269    537  -4932       O  
HETATM 1077  O   HOH A 609      17.707  23.450  -8.987  1.00 34.50           O  
ANISOU 1077  O   HOH A 609     2929   6267   3911  -1854    405  -1847       O  
HETATM 1078  O   HOH A 610      11.324  25.076  15.355  1.00 53.27           O  
ANISOU 1078  O   HOH A 610     7925   5268   7047  -2400  -1693  -1320       O  
HETATM 1079  O   HOH A 611      -4.815   7.406   2.932  1.00 56.44           O  
ANISOU 1079  O   HOH A 611     9048   4874   7523   -580  -1407  -3107       O  
HETATM 1080  O   HOH A 612      30.914  16.403   9.113  1.00 50.71           O  
ANISOU 1080  O   HOH A 612     6364   5340   7561  -3025   2268  -1419       O  
HETATM 1081  O   HOH A 613      34.020  11.506  -3.444  1.00 50.79           O  
ANISOU 1081  O   HOH A 613     8017   4609   6670  -2986   1441  -1374       O  
HETATM 1082  O   HOH A 614      14.884   6.890 -10.558  1.00 55.51           O  
ANISOU 1082  O   HOH A 614     6481   7119   7493  -2099  -3138    818       O  
HETATM 1083  O   HOH A 615      12.369  21.950  -0.452  1.00 58.10           O  
ANISOU 1083  O   HOH A 615     7668   9676   4733   -166   2719  -1995       O  
HETATM 1084  O   HOH A 616      27.574  27.087   5.376  1.00 48.29           O  
ANISOU 1084  O   HOH A 616     3092   8788   6466    896  -1176  -1195       O  
HETATM 1085  O   HOH A 617       1.841   4.612  15.059  1.00 50.23           O  
ANISOU 1085  O   HOH A 617     5018   3195  10872    266   3528    621       O  
CONECT  945  946  947  948                                                      
CONECT  946  945                                                                
CONECT  947  945                                                                
CONECT  948  945                                                                
CONECT  949  950  951  952                                                      
CONECT  950  949                                                                
CONECT  951  949                                                                
CONECT  952  949                                                                
CONECT  953  954  955  956                                                      
CONECT  954  953                                                                
CONECT  955  953                                                                
CONECT  956  953                                                                
CONECT  957  958  959  960                                                      
CONECT  958  957                                                                
CONECT  959  957                                                                
CONECT  960  957                                                                
CONECT  961  962  963  964                                                      
CONECT  962  961                                                                
CONECT  963  961                                                                
CONECT  964  961                                                                
CONECT  965  966  967  968                                                      
CONECT  966  965                                                                
CONECT  967  965                                                                
CONECT  968  965                                                                
MASTER      286    0    6    8    4    0    9    6 1084    1   24   12          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: April 25th, 2023.