CNRS Nantes University UFIP UFIP
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***  2cm5  ***

elNémo ID: 21083121482279288

Job options:

ID        	=	 21083121482279288
JOBID     	=	 2cm5
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 2cm5

HEADER    PROTEIN TRANSPORT                       04-MAY-06   2CM5              
TITLE     CRYSTAL STRUCTURE OF THE C2B DOMAIN OF RABPHILIN                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RABPHILIN-3A;                                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: C2B DOMAIN AND LINKER, RESIDUES 519-684;                   
COMPND   5 SYNONYM: C2B DOMAIN, EXOPHILIN-1;                                    
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: RAT;                                                
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: B843;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PGEX-2T;                                   
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX-2T-RABPHILIN3A-519-684               
KEYWDS    PROTEIN TRANSPORT, ZINC-FINGER, RABPHILIN3A, CA2+ BINDING,            
KEYWDS   2 METAL-BINDING, SYNAPTIC EXOCYTOSIS, C2A-C2B LINKER                   
KEYWDS   3 FRAGMENT, C2B, ZINC, SYNAPSE, C2 DOMAIN, TRANSPORT                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.SCHLICKER,P.MONTAVILLE,G.M.SHELDRICK,S.BECKER                       
REVDAT   5   24-FEB-09 2CM5    1       VERSN                                    
REVDAT   4   20-FEB-07 2CM5    1       REVDAT JRNL                              
REVDAT   3   08-JAN-07 2CM5    1       HEADER JRNL                              
REVDAT   2   02-JAN-07 2CM5    1       JRNL                                     
REVDAT   1   04-DEC-06 2CM5    0                                                
JRNL        AUTH   P.MONTAVILLE,C.SCHLICKER,A.LEONOV,M.ZWECKSTETTER,            
JRNL        AUTH 2 G.M.SHELDRICK,S.BECKER                                       
JRNL        TITL   THE C2A-C2B LINKER DEFINES THE HIGH AFFINITY CA2+            
JRNL        TITL 2 BINDING MODE OF RABPHILIN-3A.                                
JRNL        REF    J.BIOL.CHEM.                  V. 282  5015 2007              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   17166855                                                     
JRNL        DOI    10.1074/JBC.M606746200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.28 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.28                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.11                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.75                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.2                           
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.1453                 
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.144                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.1937                 
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5                      
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 3060                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 61145                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL                   
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 26423                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 1103                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 22                                            
REMARK   3   SOLVENT ATOMS      : 68                                            
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : NULL                    
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : NULL                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL                    
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : NULL                    
REMARK   3   NUMBER OF RESTRAINTS                     : 13375                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.011                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.030                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL                    
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.0342                  
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.061                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.067                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.024                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.004                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.061                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.088                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : NULL                                
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2CM5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  04-MAY-06.                 
REMARK 100 THE PDBE ID CODE IS EBI-28531.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-NOV-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 89.7                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95,0.9796                        
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33387                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.280                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.110                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.750                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.2                               
REMARK 200  DATA REDUNDANCY                : 1.720                              
REMARK 200  R MERGE                    (I) : 0.03000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.3800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.28                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 72.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.16                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.840                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHELXC, SHELXD, SHELXE                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2                        
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 8.5,20 % PEG MME           
REMARK 280  2000 OR 20 % PEG 8000                                               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       26.94900            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       30.02150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.94900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       30.02150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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: PQS                                                   
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      HOH A2036  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   519                                                      
REMARK 465     SER A   520                                                      
REMARK 465     ALA A   521                                                      
REMARK 465     ARG A   522                                                      
REMARK 465     GLY A   523                                                      
REMARK 465     GLN A   531                                                      
REMARK 465     VAL A   532                                                      
REMARK 465     GLU A   533                                                      
REMARK 465     ARG A   534                                                      
REMARK 465     ILE A   535                                                      
REMARK 465     GLY A   536                                                      
REMARK 465     ASP A   537                                                      
REMARK 465     MSE A   588                                                      
REMARK 465     GLY A   589                                                      
REMARK 465     LYS A   590                                                      
REMARK 465     GLU A   678                                                      
REMARK 465     ASN A   679                                                      
REMARK 465     HIS A   680                                                      
REMARK 465     VAL A   681                                                      
REMARK 465     SER A   682                                                      
REMARK 465     SER A   683                                                      
REMARK 465     ASP A   684                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     MSE A 524    CB   CG  SE    CE                                   
REMARK 470     ILE A 538    CG1  CG2  CD1                                       
REMARK 470     GLN A 553    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 581    CD   CE   NZ                                        
REMARK 470     ASP A 587    CB   CG   OD1  OD2                                  
REMARK 470     LYS A 591    CB   CG   CD   CE   NZ                              
REMARK 470     LYS A 595    CD   CE   NZ                                        
REMARK 470     LYS A 600    CD   CE   NZ                                        
REMARK 470     LYS A 601    CG   CD   CE   NZ                                   
REMARK 470     LYS A 622    CE   NZ                                             
REMARK 470     GLN A 645    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 653    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 654    CZ   NH1  NH2                                       
REMARK 470     LYS A 656    CG   CD   CE   NZ                                   
REMARK 470     LYS A 663    NZ                                                  
REMARK 470     LYS A 668    CE   NZ                                             
REMARK 470     ASN A 677    CB   CG   OD1  ND2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 541   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    TYR A 550   CB  -  CG  -  CD2 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    TYR A 575   CB  -  CG  -  CD1 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG A 671   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ARG A 671   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     MSE A  549                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1678  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 571A  OD1                                                    
REMARK 620 2 GLU A 529   O    87.6                                              
REMARK 620 3 ASP A 633   OD1  70.9 102.9                                        
REMARK 620 4 ASP A 633   OD2 117.8  84.2  51.7                                  
REMARK 620 5 ASP A 639   OD2 162.4  91.8 126.2  79.6                            
REMARK 620 6 MSE A 570   O    80.1  84.1 149.7 158.1  82.3                      
REMARK 620 7 ASP A 631   OD2  83.4 170.7  76.6 102.3  95.9  91.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1679  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2014   O                                                      
REMARK 620 2 ASP A 577   OD2  78.5                                              
REMARK 620 3 ASP A 571A  OD1  87.1 128.2                                        
REMARK 620 4 ASP A 571A  OD2  90.0  79.0  51.2                                  
REMARK 620 5 TYR A 632   O    97.2  83.2 148.3 159.1                            
REMARK 620 6 ASP A 633   OD1  86.6 155.4  69.6 120.8  79.3                      
REMARK 620 7 ASP A 631   OD1 174.4  95.9  96.1  88.4  82.5  98.8                
REMARK 620 8 ASP A 631   OD2 142.3 137.1  62.0  86.8  99.0  63.5  43.0          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A1678                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A1679                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ZBD   RELATED DB: PDB                                   
REMARK 900  STRUCTURAL BASIS OF RAB EFFECTOR SPECIFICITY                        
REMARK 900  : CRYSTALSTRUCTURE OF THE SMALL G PROTEIN                           
REMARK 900  RAB3A COMPLEXED WITH THEEFFECTOR DOMAIN OF                          
REMARK 900  RABPHILIN-3A                                                        
REMARK 900 RELATED ID: 2CHD   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE C2A DOMAIN OF                              
REMARK 900  RABPHILIN-3A                                                        
REMARK 900 RELATED ID: 2CM6   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE C2B DOMAIN OF                              
REMARK 900  RABPHILIN3A                                                         
REMARK 900 RELATED ID: 3RPB   RELATED DB: PDB                                   
REMARK 900  THE C2B-DOMAIN OF RABPHILIN: STRUCTURAL                             
REMARK 900  VARIATIONS IN A JANUS-FACED DOMAIN                                  
DBREF  2CM5 A  519   684  UNP    P47709   RP3A_RAT       519    684             
SEQRES   1 A  166  GLY SER ALA ARG GLY MSE ALA LEU TYR GLU GLU GLU GLN          
SEQRES   2 A  166  VAL GLU ARG ILE GLY ASP ILE GLU GLU ARG GLY LYS ILE          
SEQRES   3 A  166  LEU VAL SER LEU MSE TYR SER THR GLN GLN GLY GLY LEU          
SEQRES   4 A  166  ILE VAL GLY ILE ILE ARG CYS VAL HIS LEU ALA ALA MSE          
SEQRES   5 A  166  ASP ALA ASN GLY TYR SER ASP PRO PHE VAL LYS LEU TRP          
SEQRES   6 A  166  LEU LYS PRO ASP MSE GLY LYS LYS ALA LYS HIS LYS THR          
SEQRES   7 A  166  GLN ILE LYS LYS LYS THR LEU ASN PRO GLU PHE ASN GLU          
SEQRES   8 A  166  GLU PHE PHE TYR ASP ILE LYS HIS SER ASP LEU ALA LYS          
SEQRES   9 A  166  LYS SER LEU ASP ILE SER VAL TRP ASP TYR ASP ILE GLY          
SEQRES  10 A  166  LYS SER ASN ASP TYR ILE GLY GLY CYS GLN LEU GLY ILE          
SEQRES  11 A  166  SER ALA LYS GLY GLU ARG LEU LYS HIS TRP TYR GLU CYS          
SEQRES  12 A  166  LEU LYS ASN LYS ASP LYS LYS ILE GLU ARG TRP HIS GLN          
SEQRES  13 A  166  LEU GLN ASN GLU ASN HIS VAL SER SER ASP                      
MODRES 2CM5 MSE A  524  MET  SELENOMETHIONINE                                   
MODRES 2CM5 MSE A  549  MET  SELENOMETHIONINE                                   
MODRES 2CM5 MSE A  570  MET  SELENOMETHIONINE                                   
HET    MSE  A 524       4                                                       
HET    MSE  A 549       8                                                       
HET    MSE  A 570       8                                                       
HET     CA  A1678       1                                                       
HET     CA  A1679       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      CA CALCIUM ION                                                      
FORMUL   1  MSE    3(C5 H11 N O2 SE)                                            
FORMUL   2   CA    2(CA 2+)                                                     
FORMUL   4  HOH   *68(H2 O1)                                                    
HELIX    1   1 LYS A  616  LYS A  622  5                                   7    
HELIX    2   2 LYS A  651  ASN A  664  1                                  14    
SHEET    1  AA 4 GLU A 606  ASP A 614  0                                        
SHEET    2  AA 4 GLY A 556  VAL A 565 -1  O  LEU A 557   N  TYR A 613           
SHEET    3  AA 4 LYS A 543  SER A 551 -1  O  LYS A 543   N  VAL A 565           
SHEET    4  AA 4 ILE A 669  GLN A 674 -1  O  ILE A 669   N  LEU A 548           
SHEET    1  AB 4 LYS A 593  LYS A 595  0                                        
SHEET    2  AB 4 PRO A 578  LYS A 585 -1  O  LEU A 582   N  HIS A 594           
SHEET    3  AB 4 SER A 624  ASP A 631 -1  O  SER A 624   N  LYS A 585           
SHEET    4  AB 4 ASP A 639  GLY A 647 -1  O  ASP A 639   N  ASP A 631           
LINK         C   MSE A 524                 N   ALA A 525     1555   1555  1.33  
LINK         C   LEU A 548                 N   MSE A 549     1555   1555  1.33  
LINK         C   MSE A 549                 N   TYR A 550     1555   1555  1.33  
LINK         C   ALA A 569                 N   MSE A 570     1555   1555  1.33  
LINK         C   MSE A 570                 N  AASP A 571     1555   1555  1.34  
LINK        CA    CA A1678                 OD1AASP A 571     1555   1555  2.36  
LINK        CA    CA A1678                 O   GLU A 529     1555   1555  2.28  
LINK        CA    CA A1678                 OD1 ASP A 633     1555   1555  2.58  
LINK        CA    CA A1678                 OD2 ASP A 633     1555   1555  2.48  
LINK        CA    CA A1678                 OD2 ASP A 639     1555   1555  2.33  
LINK        CA    CA A1678                 O   MSE A 570     1555   1555  2.38  
LINK        CA    CA A1678                 OD2 ASP A 631     1555   1555  2.27  
LINK        CA    CA A1679                 OD2 ASP A 577     1555   1555  2.32  
LINK        CA    CA A1679                 OD1AASP A 571     1555   1555  2.69  
LINK        CA    CA A1679                 OD2AASP A 571     1555   1555  2.37  
LINK        CA    CA A1679                 O   TYR A 632     1555   1555  2.42  
LINK        CA    CA A1679                 OD1 ASP A 633     1555   1555  2.31  
LINK        CA    CA A1679                 OD1 ASP A 631     1555   1555  2.39  
LINK        CA    CA A1679                 OD2 ASP A 631     1555   1555  3.22  
LINK        CA    CA A1679                 O   HOH A2014     1555   1555  2.40  
CISPEP   1 LYS A  585    PRO A  586          0        -2.48                     
SITE     1 AC1  6 GLU A 529  MSE A 570  ASP A 571  ASP A 631                    
SITE     2 AC1  6 ASP A 633  ASP A 639                                          
SITE     1 AC2  6 ASP A 571  ASP A 577  ASP A 631  TYR A 632                    
SITE     2 AC2  6 ASP A 633  HOH A2014                                          
CRYST1   53.898   60.043   41.928  90.00  90.00  90.00 P 21 21 2     4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018554  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016655  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.023850        0.00000                         
HETATM    1  N   MSE A 524      25.797  11.890 -11.491  1.00 39.91           N  
ANISOU    1  N   MSE A 524     5875   7671   1617  -2747   1408    -52       N  
HETATM    2  CA  MSE A 524      25.461  12.000 -12.923  1.00 25.48           C  
ANISOU    2  CA  MSE A 524     2128   5006   2548    888    809   1903       C  
HETATM    3  C   MSE A 524      26.496  12.862 -13.656  1.00 17.80           C  
ANISOU    3  C   MSE A 524     2302   2829   1632    331    -46    590       C  
HETATM    4  O   MSE A 524      27.659  12.883 -13.204  1.00 24.32           O  
ANISOU    4  O   MSE A 524     2814   4145   2280   -343   -821   1294       O  
ATOM      5  N   ALA A 525      26.139  13.542 -14.743  1.00 16.33           N  
ANISOU    5  N   ALA A 525     2103   2571   1532    145   -140    419       N  
ATOM      6  CA  ALA A 525      27.087  14.212 -15.632  1.00 16.60           C  
ANISOU    6  CA  ALA A 525     2037   2691   1580    355    -51    527       C  
ATOM      7  C   ALA A 525      26.912  15.724 -15.720  1.00 21.59           C  
ANISOU    7  C   ALA A 525     2952   2534   2718   -242    509    215       C  
ATOM      8  O   ALA A 525      27.629  16.413 -16.477  1.00 24.14           O  
ANISOU    8  O   ALA A 525     3331   3226   2616    -96     53   1262       O  
ATOM      9  CB  ALA A 525      26.935  13.570 -17.006  1.00 21.87           C  
ANISOU    9  CB  ALA A 525     3779   2937   1593   1377    300    210       C  
ATOM     10  N   LEU A 526      25.969  16.271 -14.950  1.00 18.82           N  
ANISOU   10  N   LEU A 526     2936   2699   1517    535   -500    214       N  
ATOM     11  CA  LEU A 526      25.690  17.707 -14.919  1.00 19.17           C  
ANISOU   11  CA  LEU A 526     3215   2515   1554    191   -740    264       C  
ATOM     12  C   LEU A 526      25.837  18.314 -13.515  1.00 23.03           C  
ANISOU   12  C   LEU A 526     5067   2287   1395    300  -1074    548       C  
ATOM     13  O   LEU A 526      25.085  19.196 -13.108  1.00 33.70           O  
ANISOU   13  O   LEU A 526     8603   2283   1920   1785  -1945   -258       O  
ATOM     14  CB  LEU A 526      24.319  17.988 -15.537  1.00 19.20           C  
ANISOU   14  CB  LEU A 526     2964   2793   1538    658   -311     67       C  
ATOM     15  CG  LEU A 526      24.260  17.691 -17.051  1.00 17.55           C  
ANISOU   15  CG  LEU A 526     2525   2716   1427     51   -426    306       C  
ATOM     16  CD1 LEU A 526      22.836  17.738 -17.585  1.00 22.45           C  
ANISOU   16  CD1 LEU A 526     2720   2925   2887   1263   -954  -1227       C  
ATOM     17  CD2 LEU A 526      25.126  18.642 -17.851  1.00 22.08           C  
ANISOU   17  CD2 LEU A 526     4431   1897   2060   -175    223    218       C  
ATOM     18  N   TYR A 527      26.864  17.883 -12.809  1.00 24.22           N  
ANISOU   18  N   TYR A 527     4694   2438   2069   -939  -1642    944       N  
ATOM     19  CA  TYR A 527      27.514  18.379 -11.601  1.00 27.03           C  
ANISOU   19  CA  TYR A 527     5341   2699   2231   -499  -1637    156       C  
ATOM     20  C   TYR A 527      26.561  18.186 -10.439  1.00 29.59           C  
ANISOU   20  C   TYR A 527     6591   2366   2285   -162  -1116    563       C  
ATOM     21  O   TYR A 527      26.527  18.807  -9.379  1.00 31.70           O  
ANISOU   21  O   TYR A 527     7223   2670   2150   -103  -1246    603       O  
ATOM     22  CB  TYR A 527      28.045  19.790 -11.876  1.00 29.09           C  
ANISOU   22  CB  TYR A 527     4486   3031   3536   -892   -657   -601       C  
ATOM     23  CG  TYR A 527      28.921  19.837 -13.120  1.00 37.11           C  
ANISOU   23  CG  TYR A 527     4189   5251   4660   -425      2    616       C  
ATOM     24  CD1 TYR A 527      30.149  19.167 -13.166  1.00 46.51           C  
ANISOU   24  CD1 TYR A 527     5611   6454   5606   1170    762   1439       C  
ATOM     25  CD2 TYR A 527      28.529  20.548 -14.245  1.00 34.88           C  
ANISOU   25  CD2 TYR A 527     3315   5637   4299   -856    -57    501       C  
ATOM     26  CE1 TYR A 527      30.927  19.231 -14.316  1.00 50.47           C  
ANISOU   26  CE1 TYR A 527     5353   7232   6590    972   1354   1732       C  
ATOM     27  CE2 TYR A 527      29.290  20.620 -15.393  1.00 41.40           C  
ANISOU   27  CE2 TYR A 527     4385   6313   5032   -316    813   1002       C  
ATOM     28  CZ  TYR A 527      30.504  19.951 -15.420  1.00 47.71           C  
ANISOU   28  CZ  TYR A 527     4743   7110   6276    198   1727   1904       C  
ATOM     29  OH  TYR A 527      31.273  20.009 -16.561  1.00 53.96           O  
ANISOU   29  OH  TYR A 527     6284   7427   6790    641   2672   1448       O  
ATOM     30  N   GLU A 528      25.716  17.152 -10.580  1.00 29.48           N  
ANISOU   30  N   GLU A 528     6205   3153   1842   -466  -1063    741       N  
ATOM     31  CA  GLU A 528      24.709  16.823  -9.576  1.00 25.28           C  
ANISOU   31  CA  GLU A 528     5271   2617   1719    700  -1024    274       C  
ATOM     32  C   GLU A 528      25.259  16.394  -8.227  1.00 22.47           C  
ANISOU   32  C   GLU A 528     4812   2052   1672    130  -1046    256       C  
ATOM     33  O   GLU A 528      24.654  16.546  -7.146  1.00 26.73           O  
ANISOU   33  O   GLU A 528     5742   2835   1579   1385  -1153   -218       O  
ATOM     34  CB  GLU A 528      23.844  15.686 -10.136  1.00 24.93           C  
ANISOU   34  CB  GLU A 528     3960   3993   1519    513   -658   -272       C  
ATOM     35  CG  GLU A 528      22.831  16.080 -11.169  1.00 25.33           C  
ANISOU   35  CG  GLU A 528     3749   4750   1123    629    -73    458       C  
ATOM     36  CD  GLU A 528      23.417  15.757 -12.541  1.00 21.73           C  
ANISOU   36  CD  GLU A 528     2917   3865   1475   1160   -443   -423       C  
ATOM     37  OE1 GLU A 528      24.657  15.594 -12.601  1.00 22.64           O  
ANISOU   37  OE1 GLU A 528     2854   3286   2461    960   -329    363       O  
ATOM     38  OE2 GLU A 528      22.595  15.686 -13.479  1.00 22.33           O  
ANISOU   38  OE2 GLU A 528     2939   4126   1419   -363   -333     73       O  
ATOM     39  N   GLU A 529      26.468  15.833  -8.268  1.00 22.57           N  
ANISOU   39  N   GLU A 529     5039   2064   1472    290   -914    383       N  
ATOM     40  CA  GLU A 529      27.102  15.455  -7.010  1.00 20.81           C  
ANISOU   40  CA  GLU A 529     4313   2551   1044    415   -451    225       C  
ATOM     41  C   GLU A 529      28.046  16.496  -6.479  1.00 23.52           C  
ANISOU   41  C   GLU A 529     5430   2470   1036    -38   -847    598       C  
ATOM     42  O   GLU A 529      28.851  16.185  -5.588  1.00 22.17           O  
ANISOU   42  O   GLU A 529     5276   2450    697     -1   -703    289       O  
ATOM     43  CB  GLU A 529      27.841  14.140  -7.266  1.00 19.26           C  
ANISOU   43  CB  GLU A 529     3471   2544   1304    222   -357    370       C  
ATOM     44  CG  GLU A 529      26.938  13.021  -7.731  1.00 19.15           C  
ANISOU   44  CG  GLU A 529     3264   2490   1523    528   -783    273       C  
ATOM     45  CD  GLU A 529      27.615  11.668  -7.695  1.00 18.27           C  
ANISOU   45  CD  GLU A 529     3257   2556   1128    601   -531    189       C  
ATOM     46  OE1 GLU A 529      28.478  11.425  -8.562  1.00 24.14           O  
ANISOU   46  OE1 GLU A 529     4950   2701   1522    484    423   -350       O  
ATOM     47  OE2 GLU A 529      27.284  10.881  -6.755  1.00 19.54           O  
ANISOU   47  OE2 GLU A 529     3702   2291   1430    454   -343    164       O  
ATOM     48  N   GLU A 530      28.026  17.733  -6.990  1.00 32.12           N  
ANISOU   48  N   GLU A 530     7784   2144   2274    309  -1911    414       N  
ATOM     49  CA  GLU A 530      28.937  18.708  -6.375  1.00 37.82           C  
ANISOU   49  CA  GLU A 530     9267   2218   2884   -401  -1597   -124       C  
ATOM     50  C   GLU A 530      28.180  19.562  -5.369  1.00 46.37           C  
ANISOU   50  C   GLU A 530    11539   1911   4170   -464   -172   -318       C  
ATOM     51  O   GLU A 530      27.051  20.024  -5.438  1.00 64.50           O  
ANISOU   51  O   GLU A 530    13665   1932   8909   2305   1260   1126       O  
ATOM     52  CB  GLU A 530      29.659  19.556  -7.411  1.00 40.38           C  
ANISOU   52  CB  GLU A 530     8766   3593   2985   -966  -1973    286       C  
ATOM     53  CG  GLU A 530      30.578  18.836  -8.379  1.00 42.62           C  
ANISOU   53  CG  GLU A 530     9164   4778   2252    -54  -2085    789       C  
ATOM     54  CD  GLU A 530      31.623  19.710  -9.037  1.00 48.75           C  
ANISOU   54  CD  GLU A 530     9466   5295   3763   -895  -1158   -480       C  
ATOM     55  OE1 GLU A 530      31.947  20.780  -8.485  1.00 57.21           O  
ANISOU   55  OE1 GLU A 530    10431   3350   7958    466  -1129   -588       O  
ATOM     56  OE2 GLU A 530      32.131  19.330 -10.122  1.00 67.54           O  
ANISOU   56  OE2 GLU A 530    12208   7747   5709  -1362   1580  -1093       O  
ATOM     57  N   ILE A 538      31.494  27.181   3.046  1.00 45.57           N  
ANISOU   57  N   ILE A 538     6846   7495   2974   3796  -1289   -213       N  
ATOM     58  CA  ILE A 538      30.426  26.784   3.983  1.00 42.23           C  
ANISOU   58  CA  ILE A 538     7141   5160   3744   1919  -1226  -1662       C  
ATOM     59  C   ILE A 538      30.878  26.671   5.426  1.00 33.56           C  
ANISOU   59  C   ILE A 538     6445   2828   3477   1610   -526  -1044       C  
ATOM     60  O   ILE A 538      31.463  25.624   5.784  1.00 45.60           O  
ANISOU   60  O   ILE A 538     7774   4632   4919   4053   -932  -1766       O  
ATOM     61  CB  ILE A 538      29.843  25.414   3.547  1.00 62.10           C  
ANISOU   61  CB  ILE A 538     7780   7886   7928   1310   -402  -6318       C  
ATOM     62  N   GLU A 539      30.677  27.630   6.313  1.00 26.99           N  
ANISOU   62  N   GLU A 539     5683   1740   2831    521    396   -186       N  
ATOM     63  CA  GLU A 539      31.397  27.614   7.576  1.00 29.83           C  
ANISOU   63  CA  GLU A 539     6360   2112   2861   -667    160     26       C  
ATOM     64  C   GLU A 539      30.980  26.442   8.472  1.00 31.60           C  
ANISOU   64  C   GLU A 539     5828   2486   3693     44    365    841       C  
ATOM     65  O   GLU A 539      31.895  25.760   8.976  1.00 28.97           O  
ANISOU   65  O   GLU A 539     5792   1835   3379   -101   -319   -341       O  
ATOM     66  CB  GLU A 539      31.215  28.918   8.380  1.00 29.94           C  
ANISOU   66  CB  GLU A 539     6042   2577   2757   -764    700   -229       C  
ATOM     67  CG  GLU A 539      31.967  28.875   9.719  1.00 34.91           C  
ANISOU   67  CG  GLU A 539     6917   4009   2339   -430    806   -526       C  
ATOM     68  CD  GLU A 539      31.677  30.047  10.637  1.00 31.00           C  
ANISOU   68  CD  GLU A 539     5705   3737   2336   1210   -345    -60       C  
ATOM     69  OE1 GLU A 539      30.635  30.715  10.427  1.00 37.71           O  
ANISOU   69  OE1 GLU A 539     5308   4455   4566    928   -485   1217       O  
ATOM     70  OE2 GLU A 539      32.507  30.257  11.545  1.00 26.43           O  
ANISOU   70  OE2 GLU A 539     4054   2884   3105    182    313   -463       O  
ATOM     71  N   GLU A 540      29.660  26.274   8.621  1.00 27.14           N  
ANISOU   71  N   GLU A 540     5806   1657   2850    752   1087    189       N  
ATOM     72  CA  GLU A 540      29.108  25.157   9.389  1.00 22.04           C  
ANISOU   72  CA  GLU A 540     5145   1730   1499   1079    835    -16       C  
ATOM     73  C   GLU A 540      29.214  23.805   8.685  1.00 19.01           C  
ANISOU   73  C   GLU A 540     4139   1633   1449    807    360     29       C  
ATOM     74  O   GLU A 540      28.595  23.488   7.677  1.00 29.41           O  
ANISOU   74  O   GLU A 540     6611   2582   1982   2361  -1125   -530       O  
ATOM     75  CB  GLU A 540      27.630  25.381   9.711  1.00 23.61           C  
ANISOU   75  CB  GLU A 540     5010   1713   2247   1214    617    -12       C  
ATOM     76  CG  GLU A 540      27.057  24.442  10.754  1.00 23.80           C  
ANISOU   76  CG  GLU A 540     4626   2282   2136    369    348   -194       C  
ATOM     77  CD  GLU A 540      27.878  24.211  12.004  1.00 27.97           C  
ANISOU   77  CD  GLU A 540     6323   2143   2164   -178   -291    -11       C  
ATOM     78  OE1 GLU A 540      28.088  25.193  12.745  1.00 29.12           O  
ANISOU   78  OE1 GLU A 540     6880   2161   2023   -225      8    -48       O  
ATOM     79  OE2 GLU A 540      28.302  23.061  12.272  1.00 22.41           O  
ANISOU   79  OE2 GLU A 540     4831   2193   1490   -261    171   -112       O  
ATOM     80  N   ARG A 541      30.053  22.962   9.244  1.00 15.22           N  
ANISOU   80  N   ARG A 541     3193   1235   1357    106    431    187       N  
ATOM     81  CA  ARG A 541      30.327  21.654   8.650  1.00 13.96           C  
ANISOU   81  CA  ARG A 541     2784   1202   1318     20    285     82       C  
ATOM     82  C   ARG A 541      29.529  20.561   9.331  1.00 12.31           C  
ANISOU   82  C   ARG A 541     2159   1379   1140    -93    -19     30       C  
ATOM     83  O   ARG A 541      29.404  19.462   8.774  1.00 14.13           O  
ANISOU   83  O   ARG A 541     2494   1412   1464   -155    226    -71       O  
ATOM     84  CB  ARG A 541      31.812  21.252   8.742  1.00 18.28           C  
ANISOU   84  CB  ARG A 541     2493   1760   2692   -268    879   -432       C  
ATOM     85  CG  ARG A 541      32.815  22.272   8.221  1.00 22.95           C  
ANISOU   85  CG  ARG A 541     3327   1912   3480   -678   1156   -327       C  
ATOM     86  CD  ARG A 541      32.358  22.830   6.898  1.00 29.64           C  
ANISOU   86  CD  ARG A 541     5115   2866   3280   -449   1659    205       C  
ATOM     87  NE  ARG A 541      32.637  21.871   5.827  1.00 33.27           N  
ANISOU   87  NE  ARG A 541     6799   2996   2847    687   2365    851       N  
ATOM     88  CZ  ARG A 541      32.308  22.123   4.556  1.00 37.36           C  
ANISOU   88  CZ  ARG A 541     9554   1808   2832    489   2207   1009       C  
ATOM     89  NH1 ARG A 541      31.903  23.345   4.233  1.00 51.56           N  
ANISOU   89  NH1 ARG A 541    14220   1585   3785   1116    598    455       N  
ATOM     90  NH2 ARG A 541      32.413  21.112   3.702  1.00 43.04           N  
ANISOU   90  NH2 ARG A 541    11209   1323   3821    599   -323    593       N  
ATOM     91  N   GLY A 542      28.982  20.812  10.513  1.00 13.10           N  
ANISOU   91  N   GLY A 542     2710   1313    953     -4    -65    253       N  
ATOM     92  CA  GLY A 542      28.250  19.784  11.251  1.00 13.62           C  
ANISOU   92  CA  GLY A 542     2142   1871   1163    -88   -249    580       C  
ATOM     93  C   GLY A 542      28.911  19.418  12.577  1.00  9.84           C  
ANISOU   93  C   GLY A 542     1814    866   1058     87   -128    194       C  
ATOM     94  O   GLY A 542      30.012  19.876  12.879  1.00 11.73           O  
ANISOU   94  O   GLY A 542     1989   1476    991   -253    -97    142       O  
ATOM     95  N   LYS A 543      28.216  18.597  13.333  1.00 10.33           N  
ANISOU   95  N   LYS A 543     1765   1007   1152     75   -107    290       N  
ATOM     96  CA  LYS A 543      28.688  18.075  14.620  1.00 11.34           C  
ANISOU   96  CA  LYS A 543     2430   1002    878    208     84    135       C  
ATOM     97  C   LYS A 543      28.620  16.565  14.650  1.00  9.47           C  
ANISOU   97  C   LYS A 543     1722   1047    829    -15    -87    219       C  
ATOM     98  O   LYS A 543      27.772  15.981  13.960  1.00 12.62           O  
ANISOU   98  O   LYS A 543     1782   1315   1699     88   -586    134       O  
ATOM     99  CB  LYS A 543      27.803  18.657  15.717  1.00 18.73           C  
ANISOU   99  CB  LYS A 543     4004   1622   1492    991    930    307       C  
ATOM    100  CG  LYS A 543      27.923  20.186  15.851  1.00 27.06           C  
ANISOU  100  CG  LYS A 543     5865   1751   2664    860   1653   -462       C  
ATOM    101  CD  LYS A 543      28.041  20.521  17.341  1.00 38.49           C  
ANISOU  101  CD  LYS A 543     8206   3139   3278   1137   -254  -1204       C  
ATOM    102  CE  LYS A 543      29.462  20.623  17.873  1.00 47.08           C  
ANISOU  102  CE  LYS A 543     8605   4181   5100   2018  -1377   -295       C  
ATOM    103  NZ  LYS A 543      29.643  21.471  19.085  1.00 53.93           N  
ANISOU  103  NZ  LYS A 543     9179   4554   6760   4268  -4472  -1299       N  
ATOM    104  N   ILE A 544      29.513  15.936  15.404  1.00  9.16           N  
ANISOU  104  N   ILE A 544     1654    948    879    -59   -212     86       N  
ATOM    105  CA  ILE A 544      29.583  14.476  15.477  1.00  8.57           C  
ANISOU  105  CA  ILE A 544     1587    930    739    -61     56     87       C  
ATOM    106  C   ILE A 544      29.564  14.072  16.956  1.00  7.61           C  
ANISOU  106  C   ILE A 544     1098   1057    737   -118    -74    114       C  
ATOM    107  O   ILE A 544      30.214  14.718  17.799  1.00  9.85           O  
ANISOU  107  O   ILE A 544     1661   1066   1016   -175   -310    -46       O  
ATOM    108  CB  ILE A 544      30.839  13.938  14.767  1.00  9.03           C  
ANISOU  108  CB  ILE A 544     1539   1210    682    -20      4    127       C  
ATOM    109  CG1 ILE A 544      30.889  12.401  14.661  1.00 11.24           C  
ANISOU  109  CG1 ILE A 544     1968   1254   1046    321    122    -19       C  
ATOM    110  CG2 ILE A 544      32.139  14.470  15.339  1.00 12.00           C  
ANISOU  110  CG2 ILE A 544     1608   1957    995   -310   -235    521       C  
ATOM    111  CD1 ILE A 544      31.872  11.883  13.617  1.00 13.35           C  
ANISOU  111  CD1 ILE A 544     2159   1751   1164    469    340    -13       C  
ATOM    112  N   LEU A 545      28.822  12.999  17.226  1.00  7.27           N  
ANISOU  112  N   LEU A 545     1093   1014    655    -72    122     23       N  
ATOM    113  CA  LEU A 545      28.738  12.434  18.564  1.00  7.12           C  
ANISOU  113  CA  LEU A 545     1077    979    649    100    102     72       C  
ATOM    114  C   LEU A 545      29.594  11.167  18.618  1.00  7.73           C  
ANISOU  114  C   LEU A 545     1156   1021    759    139     90    -74       C  
ATOM    115  O   LEU A 545      29.318  10.195  17.869  1.00  8.74           O  
ANISOU  115  O   LEU A 545     1353    973    997     68    -43   -103       O  
ATOM    116  CB  LEU A 545      27.273  12.078  18.883  1.00  8.16           C  
ANISOU  116  CB  LEU A 545     1009   1504    587     44    101     40       C  
ATOM    117  CG  LEU A 545      26.994  11.465  20.262  1.00  9.05           C  
ANISOU  117  CG  LEU A 545     1324   1279    834   -339     79     75       C  
ATOM    118  CD1 LEU A 545      27.458  12.370  21.407  1.00 11.37           C  
ANISOU  118  CD1 LEU A 545     1770   1867    684   -236   -214    -81       C  
ATOM    119  CD2 LEU A 545      25.500  11.203  20.424  1.00 10.37           C  
ANISOU  119  CD2 LEU A 545     1288   1660    993   -367    224    164       C  
ATOM    120  N   VAL A 546      30.620  11.179  19.470  1.00  7.93           N  
ANISOU  120  N   VAL A 546     1382    757    875    184   -128     27       N  
ATOM    121  CA  VAL A 546      31.632  10.123  19.570  1.00  8.58           C  
ANISOU  121  CA  VAL A 546     1315    941   1006    189    -49     60       C  
ATOM    122  C   VAL A 546      31.728   9.610  20.995  1.00  8.05           C  
ANISOU  122  C   VAL A 546     1329    871    858    383   -113   -140       C  
ATOM    123  O   VAL A 546      31.753  10.422  21.951  1.00  9.23           O  
ANISOU  123  O   VAL A 546     1545    940   1022    270     54   -262       O  
ATOM    124  CB  VAL A 546      33.013  10.637  19.127  1.00  9.32           C  
ANISOU  124  CB  VAL A 546     1295   1080   1165    181   -122     69       C  
ATOM    125  CG1 VAL A 546      34.055   9.528  19.199  1.00 10.84           C  
ANISOU  125  CG1 VAL A 546     1442   1475   1201    484     75     82       C  
ATOM    126  CG2 VAL A 546      32.968  11.262  17.740  1.00 11.01           C  
ANISOU  126  CG2 VAL A 546     1220   1797   1166    286     94    308       C  
ATOM    127  N   SER A 547      31.769   8.297  21.154  1.00  8.00           N  
ANISOU  127  N   SER A 547     1409    930    702    227   -125   -104       N  
ATOM    128  CA  SER A 547      32.053   7.670  22.438  1.00  8.45           C  
ANISOU  128  CA  SER A 547     1452   1166    594    241     -8    -14       C  
ATOM    129  C   SER A 547      33.442   7.030  22.417  1.00  8.34           C  
ANISOU  129  C   SER A 547     1419   1017    732    202    -49     32       C  
ATOM    130  O   SER A 547      33.900   6.469  21.427  1.00  8.90           O  
ANISOU  130  O   SER A 547     1354   1257    770    188    -75   -121       O  
ATOM    131  CB  SER A 547      31.032   6.588  22.791  1.00 10.75           C  
ANISOU  131  CB  SER A 547     1474   1486   1125    102    114    154       C  
ATOM    132  OG  SER A 547      31.045   5.467  21.961  1.00 12.66           O  
ANISOU  132  OG  SER A 547     2105   1481   1223   -190     51     47       O  
ATOM    133  N   LEU A 548      34.095   7.107  23.544  1.00  8.21           N  
ANISOU  133  N   LEU A 548     1412    874    834    156    -79   -163       N  
ATOM    134  CA  LEU A 548      35.364   6.477  23.841  1.00  9.05           C  
ANISOU  134  CA  LEU A 548     1470   1075    895    246   -117     17       C  
ATOM    135  C   LEU A 548      35.271   5.678  25.131  1.00  9.07           C  
ANISOU  135  C   LEU A 548     1337   1197    911    276     27     -2       C  
ATOM    136  O   LEU A 548      34.792   6.233  26.118  1.00 10.59           O  
ANISOU  136  O   LEU A 548     1763   1252   1009    440    320     59       O  
ATOM    137  CB  LEU A 548      36.493   7.508  23.957  1.00  8.67           C  
ANISOU  137  CB  LEU A 548     1320   1080    893    334   -106    -26       C  
ATOM    138  CG  LEU A 548      36.822   8.402  22.784  1.00 10.28           C  
ANISOU  138  CG  LEU A 548     1735   1164   1005    119      9     22       C  
ATOM    139  CD1 LEU A 548      37.868   9.426  23.143  1.00 11.38           C  
ANISOU  139  CD1 LEU A 548     1776   1132   1418    107     85    -80       C  
ATOM    140  CD2 LEU A 548      37.320   7.567  21.591  1.00 12.41           C  
ANISOU  140  CD2 LEU A 548     1864   1616   1236   -175    402   -242       C  
HETATM  141  N   MSE A 549      35.703   4.423  25.110  1.00 10.89           N  
ANISOU  141  N   MSE A 549     2213   1197    727    457    150     90       N  
HETATM  142  CA  MSE A 549      35.724   3.594  26.335  1.00 10.55           C  
ANISOU  142  CA  MSE A 549     1917   1336    756    458    227    145       C  
HETATM  143  C   MSE A 549      36.979   2.725  26.298  1.00 10.95           C  
ANISOU  143  C   MSE A 549     2021   1161    978    429    132    127       C  
HETATM  144  O   MSE A 549      37.172   2.010  25.329  1.00 12.80           O  
ANISOU  144  O   MSE A 549     2200   1617   1046    868     22    -42       O  
HETATM  145  CB  MSE A 549      34.483   2.715  26.487  1.00 13.09           C  
ANISOU  145  CB  MSE A 549     2052   1473   1450    331    281    297       C  
HETATM  146  CG  MSE A 549      34.469   1.984  27.813  1.00 16.17           C  
ANISOU  146  CG  MSE A 549     3009   1780   1355   -408    246    262       C  
HETATM  147 SE   MSE A 549      32.970   0.981  28.138  0.66 27.93          SE  
ANISOU  147 SE   MSE A 549     3503   2952   4156   -150   1437   1573      SE  
HETATM  148  CE  MSE A 549      33.436  -0.495  27.267  1.00 67.54           C  
ANISOU  148  CE  MSE A 549    10268   6377   9018   7720   7055   5798       C  
ATOM    149  N   TYR A 550      37.817   2.794  27.325  1.00 12.00           N  
ANISOU  149  N   TYR A 550     2264   1420    876    754     90    157       N  
ATOM    150  CA  TYR A 550      38.896   1.840  27.448  1.00 12.37           C  
ANISOU  150  CA  TYR A 550     1998   1587   1115    683    273    290       C  
ATOM    151  C   TYR A 550      38.332   0.642  28.228  1.00 12.98           C  
ANISOU  151  C   TYR A 550     2011   1635   1284    988    609    479       C  
ATOM    152  O   TYR A 550      38.006   0.785  29.415  1.00 15.23           O  
ANISOU  152  O   TYR A 550     2571   2086   1131    582    397    418       O  
ATOM    153  CB  TYR A 550      40.168   2.370  28.143  1.00 15.52           C  
ANISOU  153  CB  TYR A 550     2094   2438   1366    514    153    172       C  
ATOM    154  CG  TYR A 550      41.208   1.256  27.957  1.00 17.04           C  
ANISOU  154  CG  TYR A 550     2070   2965   1440    843    114    535       C  
ATOM    155  CD1 TYR A 550      41.923   1.210  26.772  1.00 14.69           C  
ANISOU  155  CD1 TYR A 550     2032   2040   1507    317    205    190       C  
ATOM    156  CD2 TYR A 550      41.492   0.267  28.892  1.00 20.08           C  
ANISOU  156  CD2 TYR A 550     2995   3140   1495   1200    346    666       C  
ATOM    157  CE1 TYR A 550      42.872   0.215  26.569  1.00 17.30           C  
ANISOU  157  CE1 TYR A 550     1863   2787   1923    739    161    487       C  
ATOM    158  CE2 TYR A 550      42.401  -0.739  28.710  1.00 20.27           C  
ANISOU  158  CE2 TYR A 550     2530   3183   1989   1078    241    750       C  
ATOM    159  CZ  TYR A 550      43.102  -0.753  27.528  1.00 17.37           C  
ANISOU  159  CZ  TYR A 550     1414   3117   2070    736     -5    667       C  
ATOM    160  OH  TYR A 550      44.003  -1.762  27.358  1.00 18.24           O  
ANISOU  160  OH  TYR A 550     1704   2325   2901    440     89    323       O  
ATOM    161  N   SER A 551      38.262  -0.520  27.609  1.00 13.23           N  
ANISOU  161  N   SER A 551     2035   1653   1338    657    290    495       N  
ATOM    162  CA  SER A 551      37.787  -1.721  28.283  1.00 14.82           C  
ANISOU  162  CA  SER A 551     2298   1942   1392    379    300    620       C  
ATOM    163  C   SER A 551      38.924  -2.579  28.824  1.00 15.72           C  
ANISOU  163  C   SER A 551     2442   1834   1698    440    418    918       C  
ATOM    164  O   SER A 551      39.745  -3.126  28.058  1.00 20.12           O  
ANISOU  164  O   SER A 551     3439   2174   2031   1199    824   1093       O  
ATOM    165  CB  SER A 551      36.996  -2.587  27.301  1.00 17.64           C  
ANISOU  165  CB  SER A 551     2772   1772   2158    368     47    284       C  
ATOM    166  OG  SER A 551      36.685  -3.859  27.870  1.00 21.08           O  
ANISOU  166  OG  SER A 551     3766   1767   2475    299     88    412       O  
ATOM    167  N   THR A 552      38.966  -2.720  30.142  1.00 17.78           N  
ANISOU  167  N   THR A 552     3150   1857   1749    859    497   1144       N  
ATOM    168  CA  THR A 552      39.994  -3.563  30.742  1.00 19.29           C  
ANISOU  168  CA  THR A 552     3406   2065   1861   1090    644   1391       C  
ATOM    169  C   THR A 552      39.678  -5.028  30.564  1.00 21.18           C  
ANISOU  169  C   THR A 552     3846   2013   2188   1148    671   1326       C  
ATOM    170  O   THR A 552      40.584  -5.871  30.634  1.00 30.20           O  
ANISOU  170  O   THR A 552     4869   2413   4191   1828   -403    575       O  
ATOM    171  CB  THR A 552      40.114  -3.293  32.253  1.00 22.85           C  
ANISOU  171  CB  THR A 552     4325   2441   1916   1476    224   1252       C  
ATOM    172  OG1 THR A 552      38.852  -3.590  32.861  1.00 29.28           O  
ANISOU  172  OG1 THR A 552     5636   3524   1965    568   1273    821       O  
ATOM    173  CG2 THR A 552      40.432  -1.837  32.486  1.00 23.93           C  
ANISOU  173  CG2 THR A 552     4154   2541   2396   1515    -96    943       C  
ATOM    174  N   GLN A 553      38.416  -5.379  30.336  1.00 23.00           N  
ANISOU  174  N   GLN A 553     3997   2295   2447    622   1030   1322       N  
ATOM    175  CA  GLN A 553      38.139  -6.807  30.133  1.00 26.30           C  
ANISOU  175  CA  GLN A 553     4846   2450   2697    306   1313   1173       C  
ATOM    176  C   GLN A 553      38.685  -7.238  28.776  1.00 26.28           C  
ANISOU  176  C   GLN A 553     5031   2040   2912    786   1577   1371       C  
ATOM    177  O   GLN A 553      39.320  -8.280  28.674  1.00 29.12           O  
ANISOU  177  O   GLN A 553     5280   2564   3222   1335    707   1090       O  
ATOM    178  CB  GLN A 553      36.652  -7.114  30.221  1.00 35.20           C  
ANISOU  178  CB  GLN A 553     5115   2433   5826    -71   2677    379       C  
ATOM    179  N   GLN A 554      38.422  -6.409  27.766  1.00 24.25           N  
ANISOU  179  N   GLN A 554     4250   2232   2731    842   1537   1261       N  
ATOM    180  CA  GLN A 554      38.856  -6.614  26.388  1.00 22.13           C  
ANISOU  180  CA  GLN A 554     4334   1698   2376     66    679    495       C  
ATOM    181  C   GLN A 554      40.264  -6.117  26.137  1.00 20.10           C  
ANISOU  181  C   GLN A 554     4228   2170   1238    338    899    796       C  
ATOM    182  O   GLN A 554      40.806  -6.537  25.097  1.00 26.29           O  
ANISOU  182  O   GLN A 554     5537   2596   1855   1605   1438    814       O  
ATOM    183  CB  GLN A 554      37.884  -5.955  25.398  1.00 24.69           C  
ANISOU  183  CB  GLN A 554     3986   2728   2667    921   1215    739       C  
ATOM    184  CG  GLN A 554      36.486  -6.597  25.419  1.00 32.25           C  
ANISOU  184  CG  GLN A 554     4000   4829   3424    410    884    935       C  
ATOM    185  CD  GLN A 554      36.439  -7.970  24.794  1.00 35.74           C  
ANISOU  185  CD  GLN A 554     4561   4250   4768   -541    488   1373       C  
ATOM    186  OE1 GLN A 554      37.410  -8.446  24.191  1.00 49.79           O  
ANISOU  186  OE1 GLN A 554     5390   4401   9128  -2048   1949  -2205       O  
ATOM    187  NE2 GLN A 554      35.312  -8.661  24.896  1.00 45.36           N  
ANISOU  187  NE2 GLN A 554     4241   5415   7579   -648     51   1982       N  
ATOM    188  N   GLY A 555      40.907  -5.295  26.944  1.00 21.01           N  
ANISOU  188  N   GLY A 555     3460   2256   2269    672    322    719       N  
ATOM    189  CA  GLY A 555      42.228  -4.864  26.542  1.00 18.56           C  
ANISOU  189  CA  GLY A 555     3450   2251   1350   1013    370    747       C  
ATOM    190  C   GLY A 555      42.249  -3.959  25.362  1.00 17.18           C  
ANISOU  190  C   GLY A 555     3214   2297   1019   1289    280    512       C  
ATOM    191  O   GLY A 555      43.147  -4.086  24.492  1.00 20.04           O  
ANISOU  191  O   GLY A 555     3297   2837   1480   1333    648    786       O  
ATOM    192  N   GLY A 556      41.324  -3.036  25.187  1.00 17.20           N  
ANISOU  192  N   GLY A 556     2278   2641   1618    916    166    973       N  
ATOM    193  CA  GLY A 556      41.535  -2.044  24.139  1.00 13.98           C  
ANISOU  193  CA  GLY A 556     2099   1948   1266    954    250    365       C  
ATOM    194  C   GLY A 556      40.476  -0.974  24.169  1.00 11.64           C  
ANISOU  194  C   GLY A 556     1454   1831   1139    529     81    320       C  
ATOM    195  O   GLY A 556      39.617  -0.952  25.052  1.00 13.71           O  
ANISOU  195  O   GLY A 556     1844   2020   1343    709    388    405       O  
ATOM    196  N   LEU A 557      40.593  -0.098  23.187  1.00 10.94           N  
ANISOU  196  N   LEU A 557     1610   1574    972    500     15    161       N  
ATOM    197  CA  LEU A 557      39.733   1.080  23.046  1.00 10.36           C  
ANISOU  197  CA  LEU A 557     1494   1487    956    434    138    178       C  
ATOM    198  C   LEU A 557      38.543   0.760  22.161  1.00  9.55           C  
ANISOU  198  C   LEU A 557     1550    880   1200    454     60    195       C  
ATOM    199  O   LEU A 557      38.722   0.250  21.040  1.00 10.28           O  
ANISOU  199  O   LEU A 557     1529   1221   1157    484     12     77       O  
ATOM    200  CB  LEU A 557      40.511   2.228  22.405  1.00 10.50           C  
ANISOU  200  CB  LEU A 557     1536   1291   1163    297    252   -248       C  
ATOM    201  CG  LEU A 557      39.738   3.538  22.203  1.00 10.92           C  
ANISOU  201  CG  LEU A 557     1529   1288   1331    223     56      8       C  
ATOM    202  CD1 LEU A 557      39.367   4.181  23.548  1.00 15.51           C  
ANISOU  202  CD1 LEU A 557     2166   1449   2277    225    840   -588       C  
ATOM    203  CD2 LEU A 557      40.571   4.475  21.362  1.00 13.92           C  
ANISOU  203  CD2 LEU A 557     2122   1561   1607   -257     -2     96       C  
ATOM    204  N   ILE A 558      37.348   1.044  22.681  1.00  9.87           N  
ANISOU  204  N   ILE A 558     1570   1333    849    430    -47     25       N  
ATOM    205  CA  ILE A 558      36.121   1.013  21.864  1.00 10.13           C  
ANISOU  205  CA  ILE A 558     1525   1216   1108    338    -94     53       C  
ATOM    206  C   ILE A 558      35.719   2.429  21.485  1.00  9.59           C  
ANISOU  206  C   ILE A 558     1745   1028    869    183   -361   -138       C  
ATOM    207  O   ILE A 558      35.524   3.278  22.347  1.00  9.86           O  
ANISOU  207  O   ILE A 558     1617   1169    961    150   -214   -220       O  
ATOM    208  CB  ILE A 558      34.982   0.343  22.641  1.00 11.02           C  
ANISOU  208  CB  ILE A 558     1777   1053   1356    162     79   -110       C  
ATOM    209  CG1 ILE A 558      35.357  -1.077  23.074  1.00 16.41           C  
ANISOU  209  CG1 ILE A 558     2721   1109   2405    251    266    225       C  
ATOM    210  CG2 ILE A 558      33.720   0.372  21.804  1.00 15.57           C  
ANISOU  210  CG2 ILE A 558     1674   1867   2373    -81   -138   -125       C  
ATOM    211  CD1 ILE A 558      34.762  -1.608  24.312  1.00 24.85           C  
ANISOU  211  CD1 ILE A 558     5306   1905   2231   -271    108    739       C  
ATOM    212  N   VAL A 559      35.648   2.689  20.186  1.00  9.00           N  
ANISOU  212  N   VAL A 559     1287   1223    910    434   -344   -118       N  
ATOM    213  CA  VAL A 559      35.256   3.976  19.626  1.00  9.55           C  
ANISOU  213  CA  VAL A 559     1512   1159    956    492   -232    -77       C  
ATOM    214  C   VAL A 559      33.864   3.854  19.023  1.00  9.52           C  
ANISOU  214  C   VAL A 559     1684    988    946    467   -408    -48       C  
ATOM    215  O   VAL A 559      33.682   3.023  18.136  1.00 11.16           O  
ANISOU  215  O   VAL A 559     1709   1366   1164    339   -231   -314       O  
ATOM    216  CB  VAL A 559      36.232   4.466  18.529  1.00 11.07           C  
ANISOU  216  CB  VAL A 559     1861   1327   1016    173   -217    -42       C  
ATOM    217  CG1 VAL A 559      35.715   5.778  18.009  1.00 12.44           C  
ANISOU  217  CG1 VAL A 559     2128   1391   1206    436    256     37       C  
ATOM    218  CG2 VAL A 559      37.671   4.538  19.053  1.00 11.99           C  
ANISOU  218  CG2 VAL A 559     1774   1288   1495    -27   -127   -214       C  
ATOM    219  N   GLY A 560      32.909   4.618  19.503  1.00  8.72           N  
ANISOU  219  N   GLY A 560     1403    910   1001    201   -246    -78       N  
ATOM    220  CA  GLY A 560      31.557   4.682  18.990  1.00 11.01           C  
ANISOU  220  CA  GLY A 560     1584   1299   1302    241   -499     14       C  
ATOM    221  C   GLY A 560      31.360   5.895  18.120  1.00  9.67           C  
ANISOU  221  C   GLY A 560     1528   1058   1088    323   -372   -237       C  
ATOM    222  O   GLY A 560      31.639   6.990  18.575  1.00 10.44           O  
ANISOU  222  O   GLY A 560     1690   1219   1060    239   -395   -292       O  
ATOM    223  N   ILE A 561      30.919   5.688  16.874  1.00  8.76           N  
ANISOU  223  N   ILE A 561     1318   1015    993    136   -226   -198       N  
ATOM    224  CA  ILE A 561      30.445   6.761  16.058  1.00  9.13           C  
ANISOU  224  CA  ILE A 561     1495    951   1022     85   -176   -123       C  
ATOM    225  C   ILE A 561      28.911   6.682  16.072  1.00 10.43           C  
ANISOU  225  C   ILE A 561     1447   1065   1451    253   -291    -71       C  
ATOM    226  O   ILE A 561      28.321   5.789  15.463  1.00 10.57           O  
ANISOU  226  O   ILE A 561     1557   1099   1360     -9   -192     -8       O  
ATOM    227  CB  ILE A 561      31.027   6.681  14.649  1.00 10.94           C  
ANISOU  227  CB  ILE A 561     1832   1272   1051      2    -84   -169       C  
ATOM    228  CG1 ILE A 561      32.546   6.691  14.631  1.00 11.90           C  
ANISOU  228  CG1 ILE A 561     1781   1690   1051    149     80    -43       C  
ATOM    229  CG2 ILE A 561      30.451   7.804  13.812  1.00 14.32           C  
ANISOU  229  CG2 ILE A 561     1857   2330   1253    380    165    436       C  
ATOM    230  CD1 ILE A 561      33.217   7.881  15.278  1.00 15.32           C  
ANISOU  230  CD1 ILE A 561     1675   2421   1724   -108    -33   -571       C  
ATOM    231  N   ILE A 562      28.278   7.589  16.802  1.00  9.68           N  
ANISOU  231  N   ILE A 562     1599   1174    904     15    118    110       N  
ATOM    232  CA  ILE A 562      26.849   7.479  17.061  1.00  9.58           C  
ANISOU  232  CA  ILE A 562     1590   1036   1015    -12    119     90       C  
ATOM    233  C   ILE A 562      26.078   8.108  15.925  1.00  9.87           C  
ANISOU  233  C   ILE A 562     1578    958   1215    -47     -8     -8       C  
ATOM    234  O   ILE A 562      25.275   7.444  15.266  1.00 10.10           O  
ANISOU  234  O   ILE A 562     1496   1063   1280   -145      4     21       O  
ATOM    235  CB  ILE A 562      26.503   8.054  18.445  1.00 12.35           C  
ANISOU  235  CB  ILE A 562     2372   1256   1065    -54    584    194       C  
ATOM    236  CG1 ILE A 562      27.207   7.355  19.581  1.00 17.58           C  
ANISOU  236  CG1 ILE A 562     3766   1859   1054     15   -216    -53       C  
ATOM    237  CG2 ILE A 562      24.986   7.934  18.673  1.00 13.55           C  
ANISOU  237  CG2 ILE A 562     2560   1281   1307   -449    955     41       C  
ATOM    238  CD1 ILE A 562      28.660   7.528  19.776  1.00 29.93           C  
ANISOU  238  CD1 ILE A 562     4540   3438   3395  -1191  -2302    717       C  
ATOM    239  N   ARG A 563      26.308   9.407  15.715  1.00  9.63           N  
ANISOU  239  N   ARG A 563     1611    967   1080     -7   -106     11       N  
ATOM    240  CA  ARG A 563      25.572  10.126  14.698  1.00 10.65           C  
ANISOU  240  CA  ARG A 563     1674   1109   1262    119   -160     89       C  
ATOM    241  C   ARG A 563      26.294  11.416  14.357  1.00  8.73           C  
ANISOU  241  C   ARG A 563     1662    908    749    271    -86   -153       C  
ATOM    242  O   ARG A 563      27.154  11.878  15.131  1.00 10.42           O  
ANISOU  242  O   ARG A 563     1883   1218    859    -17   -241     -8       O  
ATOM    243  CB  ARG A 563      24.163  10.444  15.183  1.00 11.46           C  
ANISOU  243  CB  ARG A 563     1588   1240   1526     61   -268    -75       C  
ATOM    244  CG  ARG A 563      24.040  11.399  16.335  1.00 11.63           C  
ANISOU  244  CG  ARG A 563     1481   1153   1786   -312    227   -122       C  
ATOM    245  CD  ARG A 563      22.594  11.766  16.674  1.00 13.82           C  
ANISOU  245  CD  ARG A 563     1596   1443   2212   -262    432   -137       C  
ATOM    246  NE  ARG A 563      21.839  10.583  17.067  1.00 15.13           N  
ANISOU  246  NE  ARG A 563     1610   1914   2225   -558    470   -151       N  
ATOM    247  CZ  ARG A 563      21.267  10.301  18.198  1.00 15.24           C  
ANISOU  247  CZ  ARG A 563     2424   1273   2094   -138    503    134       C  
ATOM    248  NH1 ARG A 563      21.207  11.159  19.216  1.00 24.42           N  
ANISOU  248  NH1 ARG A 563     4337   2360   2583   -929   1048   -665       N  
ATOM    249  NH2 ARG A 563      20.728   9.101  18.346  1.00 22.21           N  
ANISOU  249  NH2 ARG A 563     3797   1475   3166   -624   1350      1       N  
ATOM    250  N   CYS A 564      25.887  12.037  13.254  1.00 10.44           N  
ANISOU  250  N   CYS A 564     1596   1237   1133    -95   -405    109       N  
ATOM    251  CA  CYS A 564      26.217  13.411  12.994  1.00 10.58           C  
ANISOU  251  CA  CYS A 564     1730   1162   1125    209     11    200       C  
ATOM    252  C   CYS A 564      24.922  14.233  12.824  1.00  9.63           C  
ANISOU  252  C   CYS A 564     1544   1215    901     14    -52    -50       C  
ATOM    253  O   CYS A 564      23.892  13.678  12.469  1.00 11.31           O  
ANISOU  253  O   CYS A 564     1783   1358   1156   -103   -363    123       O  
ATOM    254  CB  CYS A 564      27.042  13.517  11.725  1.00 10.98           C  
ANISOU  254  CB  CYS A 564     1725   1322   1126     75     74   -125       C  
ATOM    255  SG  CYS A 564      28.622  12.675  11.659  0.92 12.04           S  
ANISOU  255  SG  CYS A 564     1942   1625   1007    352     53    -10       S  
ATOM    256  N   VAL A 565      25.023  15.535  13.066  1.00 10.75           N  
ANISOU  256  N   VAL A 565     1822   1107   1157    199   -236   -102       N  
ATOM    257  CA  VAL A 565      23.903  16.444  12.934  1.00 10.70           C  
ANISOU  257  CA  VAL A 565     1616   1419   1030    173   -218     99       C  
ATOM    258  C   VAL A 565      24.348  17.715  12.169  1.00  9.92           C  
ANISOU  258  C   VAL A 565     1585   1404    778    339    -19    103       C  
ATOM    259  O   VAL A 565      25.378  18.292  12.423  1.00 11.53           O  
ANISOU  259  O   VAL A 565     1816   1164   1403    249   -198     24       O  
ATOM    260  CB  VAL A 565      23.263  16.822  14.269  1.00 12.61           C  
ANISOU  260  CB  VAL A 565     1569   2073   1150    424    162    498       C  
ATOM    261  CG1 VAL A 565      22.074  17.760  14.099  1.00 14.34           C  
ANISOU  261  CG1 VAL A 565     2175   1939   1333    717   -305   -192       C  
ATOM    262  CG2 VAL A 565      22.772  15.557  14.975  1.00 15.06           C  
ANISOU  262  CG2 VAL A 565     2516   1831   1374    358    398    273       C  
ATOM    263  N   HIS A 566      23.608  18.168  11.177  1.00 11.93           N  
ANISOU  263  N   HIS A 566     1926   1740    867    366   -167    107       N  
ATOM    264  CA  HIS A 566      23.673  19.383  10.439  1.00 13.48           C  
ANISOU  264  CA  HIS A 566     2613   1842    667    703    -47    165       C  
ATOM    265  C   HIS A 566      24.955  19.405   9.617  1.00 12.67           C  
ANISOU  265  C   HIS A 566     2624   1593    598    175    -59   -132       C  
ATOM    266  O   HIS A 566      25.626  20.416   9.517  1.00 14.00           O  
ANISOU  266  O   HIS A 566     2663   1479   1178    240   -407    -91       O  
ATOM    267  CB  HIS A 566      23.569  20.554  11.414  1.00 15.62           C  
ANISOU  267  CB  HIS A 566     2961   1817   1154    640    260    -38       C  
ATOM    268  CG  HIS A 566      22.731  21.693  10.949  1.00 24.35           C  
ANISOU  268  CG  HIS A 566     4078   2206   2967   1408    -23      6       C  
ATOM    269  ND1 HIS A 566      23.237  22.956  10.785  1.00 32.25           N  
ANISOU  269  ND1 HIS A 566     5732   2194   4328   1081  -1161    587       N  
ATOM    270  CD2 HIS A 566      21.416  21.763  10.620  1.00 32.66           C  
ANISOU  270  CD2 HIS A 566     4509   3166   4733   1729  -1111    235       C  
ATOM    271  CE1 HIS A 566      22.285  23.771  10.365  1.00 37.15           C  
ANISOU  271  CE1 HIS A 566     6683   2564   4869   1982  -1078    415       C  
ATOM    272  NE2 HIS A 566      21.173  23.062  10.262  1.00 38.05           N  
ANISOU  272  NE2 HIS A 566     5717   3332   5408   2517  -1042    154       N  
ATOM    273  N   LEU A 567      25.222  18.229   9.007  1.00 11.72           N  
ANISOU  273  N   LEU A 567     2105   1650    698    199   -217   -225       N  
ATOM    274  CA  LEU A 567      26.370  18.150   8.119  1.00 12.25           C  
ANISOU  274  CA  LEU A 567     2130   1225   1300    134     66    -42       C  
ATOM    275  C   LEU A 567      26.187  19.126   6.971  1.00 12.41           C  
ANISOU  275  C   LEU A 567     2465   1184   1067    296     80   -156       C  
ATOM    276  O   LEU A 567      25.047  19.376   6.550  1.00 15.02           O  
ANISOU  276  O   LEU A 567     2569   2063   1077     -4   -317     34       O  
ATOM    277  CB  LEU A 567      26.572  16.728   7.562  1.00 11.86           C  
ANISOU  277  CB  LEU A 567     1878   1175   1456    124     24     -5       C  
ATOM    278  CG  LEU A 567      26.999  15.652   8.598  1.00 12.32           C  
ANISOU  278  CG  LEU A 567     1998   1301   1383    176    -45     43       C  
ATOM    279  CD1 LEU A 567      27.107  14.316   7.870  1.00 14.24           C  
ANISOU  279  CD1 LEU A 567     2582   1087   1743    -85    207    157       C  
ATOM    280  CD2 LEU A 567      28.277  16.021   9.297  1.00 13.12           C  
ANISOU  280  CD2 LEU A 567     2060   1747   1178     75      5    118       C  
ATOM    281  N   ALA A 568      27.308  19.619   6.469  1.00 12.81           N  
ANISOU  281  N   ALA A 568     2516   1435    917    176   -160     77       N  
ATOM    282  CA  ALA A 568      27.293  20.354   5.190  1.00 15.59           C  
ANISOU  282  CA  ALA A 568     3462   1614    848     69     56     69       C  
ATOM    283  C   ALA A 568      26.724  19.500   4.066  1.00 15.19           C  
ANISOU  283  C   ALA A 568     3569   1501    701     27     34    282       C  
ATOM    284  O   ALA A 568      27.050  18.309   3.965  1.00 16.30           O  
ANISOU  284  O   ALA A 568     3576   1559   1058     30   -248    101       O  
ATOM    285  CB  ALA A 568      28.703  20.816   4.833  1.00 16.59           C  
ANISOU  285  CB  ALA A 568     3516   1669   1118    -40     17    371       C  
ATOM    286  N   ALA A 569      25.910  20.081   3.215  1.00 17.28           N  
ANISOU  286  N   ALA A 569     3812   1848    903    187   -211    207       N  
ATOM    287  CA  ALA A 569      25.361  19.438   2.047  1.00 17.30           C  
ANISOU  287  CA  ALA A 569     3845   1653   1075    377   -348    115       C  
ATOM    288  C   ALA A 569      26.324  19.511   0.865  1.00 18.39           C  
ANISOU  288  C   ALA A 569     4587   1445    954     -3   -152    173       C  
ATOM    289  O   ALA A 569      26.573  20.628   0.458  1.00 23.48           O  
ANISOU  289  O   ALA A 569     5722   1577   1622     74    274    359       O  
ATOM    290  CB  ALA A 569      24.073  20.135   1.638  1.00 21.76           C  
ANISOU  290  CB  ALA A 569     4714   2108   1445   1195   -922   -330       C  
HETATM  291  N   MSE A 570      26.778  18.362   0.368  1.00 18.62           N  
ANISOU  291  N   MSE A 570     4609   1667    797    107   -199    -75       N  
HETATM  292  CA  MSE A 570      27.884  18.329  -0.588  1.00 19.06           C  
ANISOU  292  CA  MSE A 570     4509   1905    829    164   -224    283       C  
HETATM  293  C   MSE A 570      27.389  17.754  -1.937  1.00 18.52           C  
ANISOU  293  C   MSE A 570     4345   1810    881    329   -163     94       C  
HETATM  294  O   MSE A 570      28.208  17.421  -2.798  1.00 18.80           O  
ANISOU  294  O   MSE A 570     4403   1633   1108    239     27    164       O  
HETATM  295  CB  MSE A 570      29.123  17.625  -0.018  1.00 21.27           C  
ANISOU  295  CB  MSE A 570     4591   2564    928    322   -206    705       C  
HETATM  296  CG  MSE A 570      29.809  18.273   1.173  1.00 20.93           C  
ANISOU  296  CG  MSE A 570     4552   2448    951    -95   -203   1011       C  
HETATM  297 SE   MSE A 570      30.291  20.017   1.049  0.66 31.51          SE  
ANISOU  297 SE   MSE A 570     5213   3351   3407    -37   -709  -1163      SE  
HETATM  298  CE  MSE A 570      31.827  19.795   0.192  1.00 23.69           C  
ANISOU  298  CE  MSE A 570     4694   2457   1850   -933   -844   1082       C  
ATOM    299  N  AASP A 571      26.061  17.649  -2.113  0.50 19.36           N  
ANISOU  299  N  AASP A 571     4302   2223    829    706   -371    223       N  
ATOM    300  CA AASP A 571      25.413  17.295  -3.385  0.50 21.11           C  
ANISOU  300  CA AASP A 571     4668   2357    994    976   -738    287       C  
ATOM    301  C  AASP A 571      24.368  18.352  -3.753  0.50 22.12           C  
ANISOU  301  C  AASP A 571     4701   2591   1112   1227   -523    229       C  
ATOM    302  O  AASP A 571      23.895  19.136  -2.909  0.50 22.14           O  
ANISOU  302  O  AASP A 571     4571   2558   1281    950   -319    165       O  
ATOM    303  CB AASP A 571      24.736  15.923  -3.340  0.50 21.15           C  
ANISOU  303  CB AASP A 571     4273   2488   1276    913  -1078    186       C  
ATOM    304  CG AASP A 571      25.686  14.790  -3.002  0.50 18.16           C  
ANISOU  304  CG AASP A 571     3341   2325   1234    378   -869    439       C  
ATOM    305  OD1AASP A 571      26.827  14.797  -3.517  0.50 18.20           O  
ANISOU  305  OD1AASP A 571     3484   2180   1250     -2   -662   -134       O  
ATOM    306  OD2AASP A 571      25.291  13.870  -2.235  0.50 17.99           O  
ANISOU  306  OD2AASP A 571     3680   2011   1146    372   -444     49       O  
ATOM    307  N  AALA A 572      23.996  18.426  -5.018  0.50 24.33           N  
ANISOU  307  N  AALA A 572     5293   2609   1342   1654  -1046      0       N  
ATOM    308  CA AALA A 572      23.138  19.523  -5.462  0.50 26.74           C  
ANISOU  308  CA AALA A 572     5758   2571   1829   1781  -1172     29       C  
ATOM    309  C  AALA A 572      21.719  19.387  -4.943  0.50 26.95           C  
ANISOU  309  C  AALA A 572     5236   2921   2082   1664  -1853    -11       C  
ATOM    310  O  AALA A 572      20.937  20.344  -4.958  0.50 32.48           O  
ANISOU  310  O  AALA A 572     5799   3691   2850   2325  -1387    288       O  
ATOM    311  CB AALA A 572      23.175  19.602  -6.998  0.50 27.82           C  
ANISOU  311  CB AALA A 572     6298   2457   1817   1268  -1759    203       C  
ATOM    312  N   ASN A 573      21.375  18.171  -4.478  1.00 29.42           N  
ANISOU  312  N   ASN A 573     5742   2940   2495   1082  -1487   -382       N  
ATOM    313  CA  ASN A 573      20.022  17.970  -3.977  1.00 29.67           C  
ANISOU  313  CA  ASN A 573     5440   3774   2059   1050  -2048    -18       C  
ATOM    314  C   ASN A 573      19.841  18.558  -2.578  1.00 30.34           C  
ANISOU  314  C   ASN A 573     5503   3600   2425   1648  -1716   -307       C  
ATOM    315  O   ASN A 573      18.758  18.460  -1.987  1.00 31.93           O  
ANISOU  315  O   ASN A 573     4931   3794   3407   2152  -1834   -958       O  
ATOM    316  CB  ASN A 573      19.653  16.485  -3.961  1.00 28.47           C  
ANISOU  316  CB  ASN A 573     4780   3750   2287   1211  -1440   -356       C  
ATOM    317  CG  ASN A 573      20.647  15.637  -3.192  1.00 26.26           C  
ANISOU  317  CG  ASN A 573     4073   3559   2346   1011   -943   -118       C  
ATOM    318  OD1 ASN A 573      21.483  16.171  -2.474  1.00 27.68           O  
ANISOU  318  OD1 ASN A 573     3746   3813   2957   1421  -1089   -586       O  
ATOM    319  ND2 ASN A 573      20.565  14.315  -3.349  1.00 28.92           N  
ANISOU  319  ND2 ASN A 573     3766   3558   3666    985   -751   -193       N  
ATOM    320  N   GLY A 574      20.874  19.175  -2.025  1.00 26.77           N  
ANISOU  320  N   GLY A 574     5121   3255   1796   1995  -1357   -479       N  
ATOM    321  CA  GLY A 574      20.816  19.709  -0.669  1.00 26.26           C  
ANISOU  321  CA  GLY A 574     5282   2919   1775   2253  -1119   -312       C  
ATOM    322  C   GLY A 574      21.128  18.674   0.398  1.00 23.94           C  
ANISOU  322  C   GLY A 574     4573   2800   1722   1992   -970   -342       C  
ATOM    323  O   GLY A 574      20.861  18.965   1.559  1.00 29.69           O  
ANISOU  323  O   GLY A 574     5384   4230   1667   3045   -822   -232       O  
ATOM    324  N   TYR A 575      21.687  17.538   0.006  1.00 24.36           N  
ANISOU  324  N   TYR A 575     4364   2963   1927   2167   -921   -183       N  
ATOM    325  CA  TYR A 575      22.032  16.487   0.950  1.00 22.55           C  
ANISOU  325  CA  TYR A 575     3548   2799   2221   1672  -1007    -52       C  
ATOM    326  C   TYR A 575      23.484  16.033   0.789  1.00 17.64           C  
ANISOU  326  C   TYR A 575     3464   2223   1017   1322   -811   -317       C  
ATOM    327  O   TYR A 575      24.193  16.639  -0.021  1.00 20.24           O  
ANISOU  327  O   TYR A 575     4210   2456   1023   1110   -589   -268       O  
ATOM    328  CB  TYR A 575      21.086  15.305   0.708  1.00 25.87           C  
ANISOU  328  CB  TYR A 575     3312   3380   3138   1399  -1089   -106       C  
ATOM    329  CG  TYR A 575      19.656  15.661   1.047  1.00 31.01           C  
ANISOU  329  CG  TYR A 575     3314   5602   2868   1577  -1001    204       C  
ATOM    330  CD1 TYR A 575      19.262  15.497   2.357  1.00 35.73           C  
ANISOU  330  CD1 TYR A 575     4385   6746   2444   2802  -1007   -647       C  
ATOM    331  CD2 TYR A 575      18.751  16.135   0.101  1.00 33.43           C  
ANISOU  331  CD2 TYR A 575     2781   7065   2857   1203  -1204    133       C  
ATOM    332  CE1 TYR A 575      17.982  15.802   2.720  1.00 40.02           C  
ANISOU  332  CE1 TYR A 575     4397   8082   2727   2613   -699   -745       C  
ATOM    333  CE2 TYR A 575      17.455  16.447   0.485  1.00 38.22           C  
ANISOU  333  CE2 TYR A 575     3590   7940   2993   2540  -1025   -669       C  
ATOM    334  CZ  TYR A 575      17.077  16.278   1.804  1.00 41.24           C  
ANISOU  334  CZ  TYR A 575     4416   7873   3382   3444   -344   -207       C  
ATOM    335  OH  TYR A 575      15.807  16.556   2.274  1.00 53.44           O  
ANISOU  335  OH  TYR A 575     4387  11911   4005   3596   -150   -412       O  
ATOM    336  N   SER A 576      23.855  15.002   1.523  1.00 18.87           N  
ANISOU  336  N   SER A 576     3201   2852   1118   1575   -602     74       N  
ATOM    337  CA  SER A 576      25.126  14.307   1.442  1.00 13.89           C  
ANISOU  337  CA  SER A 576     2538   1838    903    643   -480     72       C  
ATOM    338  C   SER A 576      24.856  12.813   1.634  1.00 13.51           C  
ANISOU  338  C   SER A 576     2287   1901    948    389   -527     23       C  
ATOM    339  O   SER A 576      23.737  12.466   2.019  1.00 15.12           O  
ANISOU  339  O   SER A 576     2182   2308   1255    200   -568   -426       O  
ATOM    340  CB  SER A 576      26.158  14.825   2.468  1.00 14.56           C  
ANISOU  340  CB  SER A 576     2927   1803    803    119   -452    233       C  
ATOM    341  OG  SER A 576      26.580  16.162   2.194  1.00 15.33           O  
ANISOU  341  OG  SER A 576     2794   1717   1315    326   -192    333       O  
ATOM    342  N   ASP A 577      25.890  12.007   1.379  1.00 13.15           N  
ANISOU  342  N   ASP A 577     2564   1547    886    247     38    191       N  
ATOM    343  CA  ASP A 577      25.843  10.561   1.579  1.00 10.71           C  
ANISOU  343  CA  ASP A 577     1780   1504    784   -142    -67     50       C  
ATOM    344  C   ASP A 577      26.969  10.186   2.544  1.00 10.61           C  
ANISOU  344  C   ASP A 577     1944   1399    691     88    -34    -27       C  
ATOM    345  O   ASP A 577      28.043   9.725   2.113  1.00 11.28           O  
ANISOU  345  O   ASP A 577     2063   1500    725    307      7     10       O  
ATOM    346  CB  ASP A 577      25.992   9.855   0.248  1.00 13.29           C  
ANISOU  346  CB  ASP A 577     2243   1943    864     20   -217   -203       C  
ATOM    347  CG  ASP A 577      24.910  10.306  -0.740  1.00 14.57           C  
ANISOU  347  CG  ASP A 577     2236   2435    866    192   -175   -161       C  
ATOM    348  OD1 ASP A 577      23.690  10.006  -0.545  1.00 17.51           O  
ANISOU  348  OD1 ASP A 577     2349   2953   1353   -417   -411   -101       O  
ATOM    349  OD2 ASP A 577      25.329  10.930  -1.751  1.00 15.20           O  
ANISOU  349  OD2 ASP A 577     2707   2006   1061   -117   -319     -2       O  
ATOM    350  N   PRO A 578      26.783  10.474   3.823  1.00 10.11           N  
ANISOU  350  N   PRO A 578     1728   1403    712    197    -41    -33       N  
ATOM    351  CA  PRO A 578      27.952  10.508   4.710  1.00 10.14           C  
ANISOU  351  CA  PRO A 578     1768   1257    828    112   -113   -127       C  
ATOM    352  C   PRO A 578      28.467   9.148   5.163  1.00  8.44           C  
ANISOU  352  C   PRO A 578     1344   1123    741   -129   -131   -147       C  
ATOM    353  O   PRO A 578      27.777   8.157   5.353  1.00 10.39           O  
ANISOU  353  O   PRO A 578     1537   1381   1028   -367     10    -73       O  
ATOM    354  CB  PRO A 578      27.438  11.256   5.957  1.00 13.20           C  
ANISOU  354  CB  PRO A 578     2162   1746   1107    469   -189   -552       C  
ATOM    355  CG  PRO A 578      25.990  11.415   5.800  1.00 18.61           C  
ANISOU  355  CG  PRO A 578     2195   3770   1105    803   -150   -877       C  
ATOM    356  CD  PRO A 578      25.530  10.875   4.479  1.00 12.22           C  
ANISOU  356  CD  PRO A 578     1900   1811    933    566    -90   -156       C  
ATOM    357  N   PHE A 579      29.789   9.091   5.356  1.00  9.56           N  
ANISOU  357  N   PHE A 579     1343   1406    882   -184    -98    191       N  
ATOM    358  CA  PHE A 579      30.496   8.032   6.045  1.00  8.86           C  
ANISOU  358  CA  PHE A 579     1399   1248    719     -8     41     55       C  
ATOM    359  C   PHE A 579      31.686   8.645   6.811  1.00  8.95           C  
ANISOU  359  C   PHE A 579     1520   1285    594    -78     24    114       C  
ATOM    360  O   PHE A 579      32.151   9.760   6.511  1.00 10.60           O  
ANISOU  360  O   PHE A 579     1852   1267    906   -253     52    103       O  
ATOM    361  CB  PHE A 579      30.937   6.911   5.118  1.00 10.87           C  
ANISOU  361  CB  PHE A 579     2018   1425    686      1     16    -76       C  
ATOM    362  CG  PHE A 579      32.042   7.235   4.129  1.00 10.73           C  
ANISOU  362  CG  PHE A 579     1996   1147    933    155    171   -254       C  
ATOM    363  CD1 PHE A 579      31.747   7.845   2.915  1.00 11.17           C  
ANISOU  363  CD1 PHE A 579     1935   1532    779    -46    224   -224       C  
ATOM    364  CD2 PHE A 579      33.377   6.940   4.393  1.00 14.10           C  
ANISOU  364  CD2 PHE A 579     2027   1859   1471    260    193    172       C  
ATOM    365  CE1 PHE A 579      32.711   8.134   1.988  1.00 13.16           C  
ANISOU  365  CE1 PHE A 579     2034   2103    862   -506    260   -380       C  
ATOM    366  CE2 PHE A 579      34.365   7.202   3.462  1.00 15.49           C  
ANISOU  366  CE2 PHE A 579     2030   1989   1867    204    417    -84       C  
ATOM    367  CZ  PHE A 579      34.024   7.788   2.250  1.00 14.41           C  
ANISOU  367  CZ  PHE A 579     1952   2365   1158   -541    385   -503       C  
ATOM    368  N   VAL A 580      32.141   7.903   7.817  1.00  9.85           N  
ANISOU  368  N   VAL A 580     1446   1503    794   -118    -32    290       N  
ATOM    369  CA  VAL A 580      33.194   8.372   8.726  1.00  9.95           C  
ANISOU  369  CA  VAL A 580     1565   1346    871      3   -152    254       C  
ATOM    370  C   VAL A 580      34.396   7.419   8.675  1.00  9.66           C  
ANISOU  370  C   VAL A 580     1514   1152   1004    -98   -257   -158       C  
ATOM    371  O   VAL A 580      34.206   6.191   8.730  1.00 11.93           O  
ANISOU  371  O   VAL A 580     1811   1165   1556   -151    -78    -55       O  
ATOM    372  CB  VAL A 580      32.670   8.512  10.161  1.00 10.41           C  
ANISOU  372  CB  VAL A 580     1636   1418    902    -63    -51    206       C  
ATOM    373  CG1 VAL A 580      33.697   9.090  11.114  1.00 12.84           C  
ANISOU  373  CG1 VAL A 580     1776   2071   1033   -123   -217    145       C  
ATOM    374  CG2 VAL A 580      31.453   9.432  10.183  1.00 12.50           C  
ANISOU  374  CG2 VAL A 580     1817   1999    931    234   -148     20       C  
ATOM    375  N   LYS A 581      35.586   7.986   8.571  1.00  9.80           N  
ANISOU  375  N   LYS A 581     1578   1246    899   -109   -226     58       N  
ATOM    376  CA  LYS A 581      36.857   7.230   8.610  1.00 10.61           C  
ANISOU  376  CA  LYS A 581     1424   1173   1433   -304   -138    223       C  
ATOM    377  C   LYS A 581      37.609   7.552   9.894  1.00 11.03           C  
ANISOU  377  C   LYS A 581     1400   1264   1529   -214   -229    234       C  
ATOM    378  O   LYS A 581      37.656   8.709  10.307  1.00 12.77           O  
ANISOU  378  O   LYS A 581     2253   1383   1216     72   -326     88       O  
ATOM    379  CB  LYS A 581      37.760   7.587   7.424  1.00 13.26           C  
ANISOU  379  CB  LYS A 581     1692   1786   1560   -420    154    -78       C  
ATOM    380  CG  LYS A 581      37.152   7.178   6.096  1.00 18.71           C  
ANISOU  380  CG  LYS A 581     3123   2499   1489   -609    -11   -257       C  
ATOM    381  N   LEU A 582      38.164   6.514  10.489  1.00 10.56           N  
ANISOU  381  N   LEU A 582     1540   1367   1106    107     74    105       N  
ATOM    382  CA  LEU A 582      38.957   6.607  11.693  1.00 11.14           C  
ANISOU  382  CA  LEU A 582     1614   1628    988    216     91    -71       C  
ATOM    383  C   LEU A 582      40.403   6.157  11.439  1.00 11.58           C  
ANISOU  383  C   LEU A 582     1569   1521   1311    148    -18   -293       C  
ATOM    384  O   LEU A 582      40.566   5.116  10.767  1.00 12.50           O  
ANISOU  384  O   LEU A 582     1698   1468   1582    117   -102   -433       O  
ATOM    385  CB  LEU A 582      38.374   5.669  12.748  1.00 14.38           C  
ANISOU  385  CB  LEU A 582     2139   2421    905   -224    107     47       C  
ATOM    386  CG  LEU A 582      37.009   5.976  13.291  1.00 19.59           C  
ANISOU  386  CG  LEU A 582     3005   2252   2187    -24   1359     23       C  
ATOM    387  CD1 LEU A 582      36.734   5.052  14.471  1.00 20.08           C  
ANISOU  387  CD1 LEU A 582     2491   3647   1491   -170    623    308       C  
ATOM    388  CD2 LEU A 582      36.877   7.430  13.721  1.00 27.31           C  
ANISOU  388  CD2 LEU A 582     3712   2624   4042   -197   1295   -976       C  
ATOM    389  N   TRP A 583      41.360   6.897  11.985  1.00 11.41           N  
ANISOU  389  N   TRP A 583     1602   1569   1163    248    -52   -487       N  
ATOM    390  CA  TRP A 583      42.770   6.533  11.889  1.00 11.03           C  
ANISOU  390  CA  TRP A 583     1550   1350   1290    184     81    -15       C  
ATOM    391  C   TRP A 583      43.413   6.818  13.242  1.00 12.13           C  
ANISOU  391  C   TRP A 583     1660   1364   1584    -70   -230     96       C  
ATOM    392  O   TRP A 583      43.511   7.969  13.675  1.00 12.28           O  
ANISOU  392  O   TRP A 583     1840   1381   1446    171   -187     43       O  
ATOM    393  CB  TRP A 583      43.449   7.293  10.734  1.00 17.39           C  
ANISOU  393  CB  TRP A 583     2691   2343   1572   -113    713     89       C  
ATOM    394  CG  TRP A 583      44.951   7.150  10.708  1.00 21.40           C  
ANISOU  394  CG  TRP A 583     2631   3246   2256   -207   1329   -202       C  
ATOM    395  CD1 TRP A 583      45.681   6.038  11.009  1.00 20.06           C  
ANISOU  395  CD1 TRP A 583     2155   3363   2102   -196    958   -673       C  
ATOM    396  CD2 TRP A 583      45.902   8.169  10.373  1.00 27.74           C  
ANISOU  396  CD2 TRP A 583     3231   3833   3474   -649   1696     94       C  
ATOM    397  NE1 TRP A 583      47.031   6.291  10.880  1.00 26.13           N  
ANISOU  397  NE1 TRP A 583     2231   4473   3224   -489    954   -208       N  
ATOM    398  CE2 TRP A 583      47.188   7.593  10.487  1.00 28.39           C  
ANISOU  398  CE2 TRP A 583     2877   4776   3136   -867   1599     86       C  
ATOM    399  CE3 TRP A 583      45.812   9.520   9.971  1.00 35.41           C  
ANISOU  399  CE3 TRP A 583     4350   4530   4574  -1022   1560   1551       C  
ATOM    400  CZ2 TRP A 583      48.335   8.332  10.222  1.00 32.62           C  
ANISOU  400  CZ2 TRP A 583     3385   5381   3628  -1451   2003   -548       C  
ATOM    401  CZ3 TRP A 583      46.945  10.261   9.708  1.00 37.95           C  
ANISOU  401  CZ3 TRP A 583     4976   4906   4538  -1769   1674    830       C  
ATOM    402  CH2 TRP A 583      48.199   9.647   9.837  1.00 39.60           C  
ANISOU  402  CH2 TRP A 583     4514   5872   4658  -1880   2392    705       C  
ATOM    403  N   LEU A 584      43.891   5.734  13.880  1.00 11.22           N  
ANISOU  403  N   LEU A 584     1862   1330   1073      6     97     46       N  
ATOM    404  CA  LEU A 584      44.628   5.909  15.121  1.00 12.66           C  
ANISOU  404  CA  LEU A 584     1722   1893   1195     -1     63    156       C  
ATOM    405  C   LEU A 584      46.115   6.123  14.815  1.00 13.85           C  
ANISOU  405  C   LEU A 584     1608   1973   1680    221     89    539       C  
ATOM    406  O   LEU A 584      46.778   5.158  14.459  1.00 19.07           O  
ANISOU  406  O   LEU A 584     2327   2272   2645    761    714    787       O  
ATOM    407  CB  LEU A 584      44.405   4.674  16.009  1.00 12.42           C  
ANISOU  407  CB  LEU A 584     1663   1849   1205      9    -47    156       C  
ATOM    408  CG  LEU A 584      44.957   4.829  17.407  1.00 11.02           C  
ANISOU  408  CG  LEU A 584     1519   1501   1169    -23     20     69       C  
ATOM    409  CD1 LEU A 584      44.120   5.856  18.173  1.00 15.37           C  
ANISOU  409  CD1 LEU A 584     1778   2038   2025     23     97   -558       C  
ATOM    410  CD2 LEU A 584      44.999   3.483  18.117  1.00 20.25           C  
ANISOU  410  CD2 LEU A 584     3828   1755   2112     80  -1005    504       C  
ATOM    411  N   LYS A 585      46.531   7.380  14.899  1.00 15.31           N  
ANISOU  411  N   LYS A 585     1880   2394   1544   -249    446   -148       N  
ATOM    412  CA  LYS A 585      47.858   7.855  14.591  1.00 19.63           C  
ANISOU  412  CA  LYS A 585     2265   3380   1814   -945    343   -243       C  
ATOM    413  C   LYS A 585      48.784   7.625  15.779  1.00 16.12           C  
ANISOU  413  C   LYS A 585     1637   2479   2008   -678    712     42       C  
ATOM    414  O   LYS A 585      48.319   7.738  16.911  1.00 13.54           O  
ANISOU  414  O   LYS A 585     1597   1744   1804     10    465    191       O  
ATOM    415  CB  LYS A 585      47.818   9.355  14.376  1.00 22.94           C  
ANISOU  415  CB  LYS A 585     2343   3708   2667  -1241   -353    904       C  
ATOM    416  CG  LYS A 585      46.925   9.872  13.278  1.00 27.89           C  
ANISOU  416  CG  LYS A 585     3206   4869   2521  -1943   -729   1531       C  
ATOM    417  CD  LYS A 585      47.205  11.311  12.920  1.00 28.97           C  
ANISOU  417  CD  LYS A 585     2993   4720   3293  -1155    -37   1837       C  
ATOM    418  CE  LYS A 585      46.806  12.267  14.027  1.00 29.20           C  
ANISOU  418  CE  LYS A 585     3482   4802   2810  -1162   -814   1729       C  
ATOM    419  NZ  LYS A 585      47.152  13.655  13.593  1.00 35.30           N  
ANISOU  419  NZ  LYS A 585     5901   4728   2783   -739    150   1928       N  
ATOM    420  N   PRO A 586      50.062   7.415  15.547  1.00 18.24           N  
ANISOU  420  N   PRO A 586     2069   2131   2730    243   1087    351       N  
ATOM    421  CA  PRO A 586      50.653   7.335  14.218  1.00 22.13           C  
ANISOU  421  CA  PRO A 586     2360   3004   3043   -265   1515   -212       C  
ATOM    422  C   PRO A 586      50.701   5.985  13.505  1.00 22.63           C  
ANISOU  422  C   PRO A 586     2889   3039   2669    379    488   -190       C  
ATOM    423  O   PRO A 586      51.628   5.832  12.692  1.00 38.94           O  
ANISOU  423  O   PRO A 586     3492   5520   5783  -1298   1943  -3480       O  
ATOM    424  CB  PRO A 586      52.106   7.756  14.522  1.00 22.05           C  
ANISOU  424  CB  PRO A 586     2245   3239   2895     44   1342   -333       C  
ATOM    425  CG  PRO A 586      52.351   7.221  15.898  1.00 23.32           C  
ANISOU  425  CG  PRO A 586     1981   2990   3890    649   1450    882       C  
ATOM    426  CD  PRO A 586      51.043   7.315  16.634  1.00 20.43           C  
ANISOU  426  CD  PRO A 586     1654   2871   3238    481   1027   1044       C  
ATOM    427  N   ASP A 587      49.835   4.993  13.670  1.00 26.16           N  
ANISOU  427  N   ASP A 587     4392   2225   3322    397   1200    128       N  
ATOM    428  CA  ASP A 587      50.128   3.605  13.256  1.00 27.37           C  
ANISOU  428  CA  ASP A 587     3360   3356   3682    515   -637  -1946       C  
ATOM    429  C   ASP A 587      49.781   3.478  11.764  1.00 31.03           C  
ANISOU  429  C   ASP A 587     3338   4519   3933   -723  -1359  -1020       C  
ATOM    430  O   ASP A 587      48.860   4.198  11.392  1.00 35.06           O  
ANISOU  430  O   ASP A 587     3037   5985   4300   -418   -228    800       O  
ATOM    431  N   LYS A 591      45.079  -2.175  10.284  1.00 33.51           N  
ANISOU  431  N   LYS A 591     5029   2613   5090   -775    712  -1144       N  
ATOM    432  CA  LYS A 591      44.773  -2.289  11.723  1.00 25.67           C  
ANISOU  432  CA  LYS A 591     2572   2102   5080    755     79    238       C  
ATOM    433  C   LYS A 591      44.548  -0.959  12.431  1.00 24.14           C  
ANISOU  433  C   LYS A 591     2765   2440   3968    184    268     67       C  
ATOM    434  O   LYS A 591      43.754  -0.828  13.390  1.00 23.38           O  
ANISOU  434  O   LYS A 591     3436   2331   3115    170    168    794       O  
ATOM    435  N   ALA A 592      45.227   0.110  12.013  1.00 17.60           N  
ANISOU  435  N   ALA A 592     1720   2251   2716    666   -104     33       N  
ATOM    436  CA  ALA A 592      45.010   1.464  12.518  1.00 17.41           C  
ANISOU  436  CA  ALA A 592     2293   2343   1978    499   -565   -118       C  
ATOM    437  C   ALA A 592      43.733   2.119  12.016  1.00 12.62           C  
ANISOU  437  C   ALA A 592     2048   1518   1228    294     -4     83       C  
ATOM    438  O   ALA A 592      43.328   3.163  12.544  1.00 14.82           O  
ANISOU  438  O   ALA A 592     2366   1745   1521    213    344   -151       O  
ATOM    439  CB  ALA A 592      46.168   2.371  12.130  1.00 21.33           C  
ANISOU  439  CB  ALA A 592     2111   2898   3095     28     75  -1856       C  
ATOM    440  N   LYS A 593      43.090   1.572  10.992  1.00 15.12           N  
ANISOU  440  N   LYS A 593     1696   1840   2211    371   -366   -411       N  
ATOM    441  CA  LYS A 593      41.997   2.290  10.323  1.00 14.01           C  
ANISOU  441  CA  LYS A 593     1343   2229   1750    309     62   -156       C  
ATOM    442  C   LYS A 593      40.692   1.534  10.354  1.00 13.14           C  
ANISOU  442  C   LYS A 593     1607   1706   1680    238   -116   -573       C  
ATOM    443  O   LYS A 593      40.637   0.311  10.277  1.00 19.46           O  
ANISOU  443  O   LYS A 593     2100   1736   3557    403    -18   -764       O  
ATOM    444  CB  LYS A 593      42.479   2.522   8.883  1.00 19.10           C  
ANISOU  444  CB  LYS A 593     2473   2934   1851     95    270     56       C  
ATOM    445  CG  LYS A 593      43.676   3.455   8.925  1.00 25.85           C  
ANISOU  445  CG  LYS A 593     1743   5508   2570   -438    722    107       C  
ATOM    446  CD  LYS A 593      44.069   3.851   7.507  1.00 32.39           C  
ANISOU  446  CD  LYS A 593     2276   6942   3088   -447    945   1096       C  
ATOM    447  CE  LYS A 593      45.227   4.834   7.614  1.00 40.36           C  
ANISOU  447  CE  LYS A 593     4380   7570   3384  -1980    471   1700       C  
ATOM    448  NZ  LYS A 593      44.834   6.180   7.087  1.00 51.47           N  
ANISOU  448  NZ  LYS A 593     5828   6049   7679  -1501  -2913   -608       N  
ATOM    449  N   HIS A 594      39.587   2.288  10.473  1.00 11.93           N  
ANISOU  449  N   HIS A 594     1364   1255   1914    -66    401    284       N  
ATOM    450  CA  HIS A 594      38.256   1.755  10.351  1.00 12.02           C  
ANISOU  450  CA  HIS A 594     1541   1411   1617   -267    200    191       C  
ATOM    451  C   HIS A 594      37.365   2.723   9.565  1.00 12.31           C  
ANISOU  451  C   HIS A 594     1768   1396   1515     80      5   -196       C  
ATOM    452  O   HIS A 594      37.720   3.915   9.462  1.00 13.10           O  
ANISOU  452  O   HIS A 594     1971   1496   1510    -59    298    137       O  
ATOM    453  CB  HIS A 594      37.593   1.578  11.720  1.00 13.32           C  
ANISOU  453  CB  HIS A 594     1445   1997   1619   -377    304    110       C  
ATOM    454  CG  HIS A 594      38.232   0.621  12.674  1.00 15.66           C  
ANISOU  454  CG  HIS A 594     1926   2449   1574   -466    185    376       C  
ATOM    455  ND1 HIS A 594      38.081  -0.738  12.528  1.00 18.12           N  
ANISOU  455  ND1 HIS A 594     2153   2363   2369   -260   -180    587       N  
ATOM    456  CD2 HIS A 594      38.994   0.828  13.779  1.00 19.75           C  
ANISOU  456  CD2 HIS A 594     1863   3190   2449    323   -453   -128       C  
ATOM    457  CE1 HIS A 594      38.733  -1.347  13.498  1.00 23.27           C  
ANISOU  457  CE1 HIS A 594     2313   2969   3560     55   -833    843       C  
ATOM    458  NE2 HIS A 594      39.296  -0.432  14.270  1.00 22.50           N  
ANISOU  458  NE2 HIS A 594     2499   3624   2424    574   -432    256       N  
ATOM    459  N   LYS A 595      36.212   2.250   9.112  1.00 12.86           N  
ANISOU  459  N   LYS A 595     1943   1333   1612    154    -91   -207       N  
ATOM    460  CA  LYS A 595      35.245   3.136   8.479  1.00 13.62           C  
ANISOU  460  CA  LYS A 595     1837   1772   1567     96   -122     -7       C  
ATOM    461  C   LYS A 595      33.843   2.655   8.765  1.00 12.52           C  
ANISOU  461  C   LYS A 595     1903   1281   1573     33   -169     -4       C  
ATOM    462  O   LYS A 595      33.594   1.451   8.827  1.00 13.97           O  
ANISOU  462  O   LYS A 595     2164   1283   1862    193    140   -163       O  
ATOM    463  CB  LYS A 595      35.506   3.166   6.963  1.00 19.58           C  
ANISOU  463  CB  LYS A 595     2350   3522   1567   -250   -120    359       C  
ATOM    464  CG  LYS A 595      35.344   1.790   6.366  1.00 26.09           C  
ANISOU  464  CG  LYS A 595     3296   4909   1707   -507   -236  -1151       C  
ATOM    465  N   THR A 596      32.923   3.623   8.879  1.00 12.52           N  
ANISOU  465  N   THR A 596     1788   1120   1849   -130     86    382       N  
ATOM    466  CA  THR A 596      31.519   3.282   8.936  1.00 11.01           C  
ANISOU  466  CA  THR A 596     1815   1008   1362   -136    116    206       C  
ATOM    467  C   THR A 596      30.927   2.948   7.566  1.00 13.01           C  
ANISOU  467  C   THR A 596     2314   1279   1349   -534    170     19       C  
ATOM    468  O   THR A 596      31.548   3.179   6.526  1.00 13.47           O  
ANISOU  468  O   THR A 596     2021   1647   1451    -37    336   -143       O  
ATOM    469  CB  THR A 596      30.661   4.446   9.486  1.00 11.34           C  
ANISOU  469  CB  THR A 596     1972   1097   1241     68    -50    178       C  
ATOM    470  OG1 THR A 596      30.620   5.536   8.545  1.00 11.01           O  
ANISOU  470  OG1 THR A 596     1829   1051   1302     -1    258    196       O  
ATOM    471  CG2 THR A 596      31.175   4.963  10.807  1.00 13.35           C  
ANISOU  471  CG2 THR A 596     2404   1342   1325     55   -212     63       C  
ATOM    472  N   GLN A 597      29.690   2.434   7.615  1.00 11.94           N  
ANISOU  472  N   GLN A 597     2089   1187   1261   -243     49     20       N  
ATOM    473  CA  GLN A 597      28.843   2.385   6.439  1.00 13.45           C  
ANISOU  473  CA  GLN A 597     2390   1455   1267   -285    -66    102       C  
ATOM    474  C   GLN A 597      28.535   3.764   5.875  1.00 12.95           C  
ANISOU  474  C   GLN A 597     2163   1369   1390    -44   -244   -176       C  
ATOM    475  O   GLN A 597      28.713   4.792   6.520  1.00 11.32           O  
ANISOU  475  O   GLN A 597     1739   1458   1103   -207     33    -44       O  
ATOM    476  CB  GLN A 597      27.533   1.690   6.775  1.00 14.66           C  
ANISOU  476  CB  GLN A 597     2065   1808   1696   -164   -193    166       C  
ATOM    477  CG  GLN A 597      26.561   2.632   7.465  1.00 16.94           C  
ANISOU  477  CG  GLN A 597     2009   2076   2350   -114   -353   -329       C  
ATOM    478  CD  GLN A 597      25.439   1.855   8.116  1.00 23.91           C  
ANISOU  478  CD  GLN A 597     2108   3302   3676     26    457    227       C  
ATOM    479  OE1 GLN A 597      24.493   1.468   7.418  1.00 23.60           O  
ANISOU  479  OE1 GLN A 597     1833   2435   4699    -13     71   1085       O  
ATOM    480  NE2 GLN A 597      25.585   1.637   9.397  1.00 27.95           N  
ANISOU  480  NE2 GLN A 597     2352   4281   3988     94    504   1216       N  
ATOM    481  N   ILE A 598      28.049   3.766   4.641  1.00 11.93           N  
ANISOU  481  N   ILE A 598     1946   1408   1179   -351      2      9       N  
ATOM    482  CA  ILE A 598      27.557   4.953   3.981  1.00 11.94           C  
ANISOU  482  CA  ILE A 598     1987   1360   1191   -575     32     92       C  
ATOM    483  C   ILE A 598      26.049   5.071   4.201  1.00 13.12           C  
ANISOU  483  C   ILE A 598     1920   1886   1180   -301   -229   -268       C  
ATOM    484  O   ILE A 598      25.285   4.126   3.934  1.00 16.40           O  
ANISOU  484  O   ILE A 598     1810   2151   2268   -392   -409   -571       O  
ATOM    485  CB  ILE A 598      27.822   4.921   2.471  1.00 12.70           C  
ANISOU  485  CB  ILE A 598     2198   1463   1165   -490    -17    -15       C  
ATOM    486  CG1 ILE A 598      29.302   4.864   2.135  1.00 15.37           C  
ANISOU  486  CG1 ILE A 598     2112   2581   1145   -464    -10   -411       C  
ATOM    487  CG2 ILE A 598      27.084   6.109   1.849  1.00 17.41           C  
ANISOU  487  CG2 ILE A 598     2975   2321   1320    108   -303    222       C  
ATOM    488  CD1 ILE A 598      29.626   4.239   0.798  1.00 17.20           C  
ANISOU  488  CD1 ILE A 598     2977   2158   1401   -563    546   -301       C  
ATOM    489  N   LYS A 599      25.639   6.208   4.724  1.00 13.96           N  
ANISOU  489  N   LYS A 599     2176   1719   1409   -186   -175    -53       N  
ATOM    490  CA  LYS A 599      24.209   6.492   4.858  1.00 13.33           C  
ANISOU  490  CA  LYS A 599     2047   1602   1415   -250   -374    -90       C  
ATOM    491  C   LYS A 599      23.778   7.366   3.682  1.00 16.11           C  
ANISOU  491  C   LYS A 599     2352   2063   1706   -601   -805    234       C  
ATOM    492  O   LYS A 599      24.479   8.302   3.298  1.00 20.94           O  
ANISOU  492  O   LYS A 599     2985   2270   2699   -934  -1216    857       O  
ATOM    493  CB  LYS A 599      23.913   7.183   6.177  1.00 14.29           C  
ANISOU  493  CB  LYS A 599     1943   1925   1561   -110   -268   -166       C  
ATOM    494  CG  LYS A 599      24.159   6.344   7.429  1.00 15.13           C  
ANISOU  494  CG  LYS A 599     2756   1608   1386    475     -3   -316       C  
ATOM    495  CD  LYS A 599      23.259   5.129   7.504  1.00 19.70           C  
ANISOU  495  CD  LYS A 599     4210   1157   2120    277   -629   -167       C  
ATOM    496  CE  LYS A 599      23.346   4.482   8.879  1.00 29.29           C  
ANISOU  496  CE  LYS A 599     5135   2764   3228    633    300   1446       C  
ATOM    497  NZ  LYS A 599      22.406   3.377   9.197  1.00 37.98           N  
ANISOU  497  NZ  LYS A 599     3978   3284   7166   1563   2993   2097       N  
ATOM    498  N   LYS A 600      22.638   7.095   3.060  1.00 16.12           N  
ANISOU  498  N   LYS A 600     2042   2606   1478   -288   -513   -250       N  
ATOM    499  CA  LYS A 600      22.280   7.798   1.848  1.00 15.39           C  
ANISOU  499  CA  LYS A 600     1576   2697   1574    -85   -506   -247       C  
ATOM    500  C   LYS A 600      21.391   9.003   2.146  1.00 15.69           C  
ANISOU  500  C   LYS A 600     1788   2539   1635   -256   -302   -339       C  
ATOM    501  O   LYS A 600      20.472   8.941   2.955  1.00 18.43           O  
ANISOU  501  O   LYS A 600     2190   3018   1795     88     27   -180       O  
ATOM    502  CB  LYS A 600      21.613   6.765   0.945  1.00 19.17           C  
ANISOU  502  CB  LYS A 600     2347   3100   1836    368   -882   -831       C  
ATOM    503  CG  LYS A 600      22.508   5.699   0.354  1.00 25.42           C  
ANISOU  503  CG  LYS A 600     3023   2808   3829    625   -830  -1090       C  
ATOM    504  N   LYS A 601      21.609  10.128   1.474  1.00 16.88           N  
ANISOU  504  N   LYS A 601     2078   2720   1615    -75   -461    -71       N  
ATOM    505  CA  LYS A 601      20.737  11.280   1.398  1.00 17.37           C  
ANISOU  505  CA  LYS A 601     2485   2792   1324    150   -874   -439       C  
ATOM    506  C   LYS A 601      20.266  11.756   2.763  1.00 17.44           C  
ANISOU  506  C   LYS A 601     1822   3373   1432     44   -641   -324       C  
ATOM    507  O   LYS A 601      19.065  11.750   3.032  1.00 20.21           O  
ANISOU  507  O   LYS A 601     1646   3864   2168    329   -843   -342       O  
ATOM    508  CB  LYS A 601      19.500  10.974   0.520  1.00 31.05           C  
ANISOU  508  CB  LYS A 601     2247   6677   2874   1432  -1297  -2831       C  
ATOM    509  N   THR A 602      21.272  12.170   3.555  1.00 14.37           N  
ANISOU  509  N   THR A 602     1710   2465   1286     -2   -368   -485       N  
ATOM    510  CA  THR A 602      20.966  12.695   4.884  1.00 14.70           C  
ANISOU  510  CA  THR A 602     2040   2170   1374   -146   -122   -407       C  
ATOM    511  C   THR A 602      22.080  13.595   5.375  1.00 13.32           C  
ANISOU  511  C   THR A 602     1844   1792   1426    318   -472   -363       C  
ATOM    512  O   THR A 602      23.251  13.317   5.114  1.00 15.86           O  
ANISOU  512  O   THR A 602     1849   2198   1979    250   -193   -535       O  
ATOM    513  CB  THR A 602      20.748  11.546   5.895  1.00 15.54           C  
ANISOU  513  CB  THR A 602     2224   2259   1420    -40    -79   -334       C  
ATOM    514  OG1 THR A 602      20.413  12.101   7.167  1.00 16.64           O  
ANISOU  514  OG1 THR A 602     2222   2748   1352   -284   -112   -494       O  
ATOM    515  CG2 THR A 602      22.006  10.736   6.066  1.00 18.00           C  
ANISOU  515  CG2 THR A 602     2519   2924   1395    319   -205    -97       C  
ATOM    516  N   LEU A 603      21.690  14.652   6.072  1.00 12.94           N  
ANISOU  516  N   LEU A 603     2105   1772   1037    331   -351   -202       N  
ATOM    517  CA  LEU A 603      22.630  15.527   6.769  1.00 12.79           C  
ANISOU  517  CA  LEU A 603     2215   1646    997    136   -259    -70       C  
ATOM    518  C   LEU A 603      22.711  15.172   8.236  1.00 11.33           C  
ANISOU  518  C   LEU A 603     1692   1635    977    275   -168   -146       C  
ATOM    519  O   LEU A 603      23.513  15.783   8.952  1.00 12.63           O  
ANISOU  519  O   LEU A 603     1949   1734   1117    235   -298   -234       O  
ATOM    520  CB  LEU A 603      22.164  16.990   6.620  1.00 17.38           C  
ANISOU  520  CB  LEU A 603     3610   1576   1420     99    -55    154       C  
ATOM    521  CG  LEU A 603      22.044  17.445   5.166  1.00 18.92           C  
ANISOU  521  CG  LEU A 603     3265   2334   1590    805   -601    319       C  
ATOM    522  CD1 LEU A 603      21.610  18.901   5.125  1.00 20.00           C  
ANISOU  522  CD1 LEU A 603     3466   1922   2210    104   -678    496       C  
ATOM    523  CD2 LEU A 603      23.354  17.203   4.407  1.00 17.36           C  
ANISOU  523  CD2 LEU A 603     3311   1966   1317   -325   -298    166       C  
ATOM    524  N   ASN A 604      21.897  14.225   8.683  1.00 13.42           N  
ANISOU  524  N   ASN A 604     1761   2199   1139     27     62    -45       N  
ATOM    525  CA  ASN A 604      21.824  13.784  10.074  1.00 12.68           C  
ANISOU  525  CA  ASN A 604     1917   1871   1029    244    159   -212       C  
ATOM    526  C   ASN A 604      22.007  12.283  10.186  1.00 12.18           C  
ANISOU  526  C   ASN A 604     1781   1833   1016     59    -34   -285       C  
ATOM    527  O   ASN A 604      21.102  11.610  10.691  1.00 13.59           O  
ANISOU  527  O   ASN A 604     1714   1856   1593    148      1   -152       O  
ATOM    528  CB  ASN A 604      20.478  14.140  10.716  1.00 14.56           C  
ANISOU  528  CB  ASN A 604     1903   2444   1186    431    174    -74       C  
ATOM    529  CG  ASN A 604      19.952  15.523  10.497  1.00 20.42           C  
ANISOU  529  CG  ASN A 604     2313   2664   2784    956   -987   -862       C  
ATOM    530  OD1 ASN A 604      18.889  15.938  10.066  1.00 28.69           O  
ANISOU  530  OD1 ASN A 604     2260   3621   5019   1213  -1643  -1265       O  
ATOM    531  ND2 ASN A 604      20.819  16.447  10.844  1.00 13.54           N  
ANISOU  531  ND2 ASN A 604     1636   2321   1189    963   -115   -152       N  
ATOM    532  N   PRO A 605      23.103  11.725   9.704  1.00 11.24           N  
ANISOU  532  N   PRO A 605     1912   1506    853     -3    -30   -301       N  
ATOM    533  CA  PRO A 605      23.223  10.255   9.636  1.00 12.14           C  
ANISOU  533  CA  PRO A 605     1862   1555   1197     12   -452   -364       C  
ATOM    534  C   PRO A 605      23.235   9.605  11.011  1.00 11.52           C  
ANISOU  534  C   PRO A 605     1263   1573   1539    217   -547    -57       C  
ATOM    535  O   PRO A 605      23.915  10.084  11.915  1.00 12.62           O  
ANISOU  535  O   PRO A 605     2063   1607   1125     -7   -497     73       O  
ATOM    536  CB  PRO A 605      24.592  10.018   8.973  1.00 12.43           C  
ANISOU  536  CB  PRO A 605     1901   1400   1422    123   -357   -312       C  
ATOM    537  CG  PRO A 605      25.323  11.266   9.294  1.00 12.02           C  
ANISOU  537  CG  PRO A 605     1864   1246   1459    196   -210   -230       C  
ATOM    538  CD  PRO A 605      24.307  12.390   9.194  1.00 11.86           C  
ANISOU  538  CD  PRO A 605     1980   1421   1106    363    251     32       C  
ATOM    539  N   GLU A 606      22.504   8.502  11.153  1.00 13.50           N  
ANISOU  539  N   GLU A 606     1779   1409   1940    173   -493    -86       N  
ATOM    540  CA  GLU A 606      22.443   7.706  12.364  1.00 14.37           C  
ANISOU  540  CA  GLU A 606     1737   1503   2222    183   -463    123       C  
ATOM    541  C   GLU A 606      23.284   6.457  12.117  1.00 14.83           C  
ANISOU  541  C   GLU A 606     2049   1509   2077    325   -978   -258       C  
ATOM    542  O   GLU A 606      22.850   5.542  11.405  1.00 24.96           O  
ANISOU  542  O   GLU A 606     2460   1948   5075    418  -2164  -1247       O  
ATOM    543  CB  GLU A 606      20.984   7.384  12.646  1.00 17.79           C  
ANISOU  543  CB  GLU A 606     1976   2292   2493    -13   -113     73       C  
ATOM    544  CG  GLU A 606      20.649   6.711  13.938  1.00 18.39           C  
ANISOU  544  CG  GLU A 606     2216   2382   2388   -387   -209    -60       C  
ATOM    545  CD  GLU A 606      20.771   7.639  15.125  1.00 20.29           C  
ANISOU  545  CD  GLU A 606     3169   2095   2446   -381   -251    -19       C  
ATOM    546  OE1 GLU A 606      21.053   8.848  14.934  1.00 19.96           O  
ANISOU  546  OE1 GLU A 606     2374   2030   3180    -85     67      1       O  
ATOM    547  OE2 GLU A 606      20.590   7.110  16.218  1.00 22.37           O  
ANISOU  547  OE2 GLU A 606     3696   2436   2368     38   -123     72       O  
ATOM    548  N   PHE A 607      24.482   6.371  12.609  1.00 10.42           N  
ANISOU  548  N   PHE A 607     1693   1244   1024     98   -297   -231       N  
ATOM    549  CA  PHE A 607      25.396   5.248  12.417  1.00 10.84           C  
ANISOU  549  CA  PHE A 607     1574   1377   1167     97    -74   -109       C  
ATOM    550  C   PHE A 607      25.277   4.203  13.521  1.00 10.84           C  
ANISOU  550  C   PHE A 607     1609   1129   1379     48   -106    -96       C  
ATOM    551  O   PHE A 607      25.142   3.019  13.213  1.00 12.83           O  
ANISOU  551  O   PHE A 607     1803   1213   1860    123   -142   -255       O  
ATOM    552  CB  PHE A 607      26.854   5.710  12.361  1.00 12.31           C  
ANISOU  552  CB  PHE A 607     1595   1656   1426    -13   -208    239       C  
ATOM    553  CG  PHE A 607      27.156   6.661  11.232  1.00 11.04           C  
ANISOU  553  CG  PHE A 607     1498   1423   1274    333    126      1       C  
ATOM    554  CD1 PHE A 607      27.232   6.217   9.912  1.00 13.25           C  
ANISOU  554  CD1 PHE A 607     1865   1879   1289    302      7   -137       C  
ATOM    555  CD2 PHE A 607      27.395   8.024  11.453  1.00 11.13           C  
ANISOU  555  CD2 PHE A 607     1425   1405   1399    376    -13    112       C  
ATOM    556  CE1 PHE A 607      27.568   7.068   8.882  1.00 13.85           C  
ANISOU  556  CE1 PHE A 607     2004   2093   1165     32   -291    -91       C  
ATOM    557  CE2 PHE A 607      27.716   8.858  10.409  1.00 10.69           C  
ANISOU  557  CE2 PHE A 607     1124   1581   1358    117     27     76       C  
ATOM    558  CZ  PHE A 607      27.782   8.402   9.111  1.00 13.27           C  
ANISOU  558  CZ  PHE A 607     1656   2007   1378    118     37    -97       C  
ATOM    559  N   ASN A 608      25.371   4.610  14.771  1.00 10.78           N  
ANISOU  559  N   ASN A 608     1595   1232   1269    155   -105     58       N  
ATOM    560  CA  ASN A 608      25.387   3.704  15.921  1.00 10.53           C  
ANISOU  560  CA  ASN A 608     1608    941   1453    -26   -168     38       C  
ATOM    561  C   ASN A 608      26.340   2.534  15.702  1.00 10.33           C  
ANISOU  561  C   ASN A 608     1730    830   1364    -67    191     27       C  
ATOM    562  O   ASN A 608      25.924   1.382  15.908  1.00 12.61           O  
ANISOU  562  O   ASN A 608     1716    927   2147     13    244    199       O  
ATOM    563  CB  ASN A 608      23.979   3.192  16.238  1.00 12.93           C  
ANISOU  563  CB  ASN A 608     1760   1387   1764     22    313    -90       C  
ATOM    564  CG  ASN A 608      23.098   4.339  16.701  1.00 16.23           C  
ANISOU  564  CG  ASN A 608     1950   1733   2486    268    240   -389       C  
ATOM    565  OD1 ASN A 608      23.346   5.006  17.707  1.00 21.23           O  
ANISOU  565  OD1 ASN A 608     2677   2108   3280   -254    734  -1187       O  
ATOM    566  ND2 ASN A 608      22.073   4.551  15.920  1.00 20.51           N  
ANISOU  566  ND2 ASN A 608     2208   2066   3517    412    -85    749       N  
ATOM    567  N   GLU A 609      27.576   2.801  15.367  1.00 10.54           N  
ANISOU  567  N   GLU A 609     1498   1100   1408    -62   -208     98       N  
ATOM    568  CA  GLU A 609      28.565   1.760  15.042  1.00 10.26           C  
ANISOU  568  CA  GLU A 609     1445   1213   1241     -9   -170    294       C  
ATOM    569  C   GLU A 609      29.727   1.893  16.044  1.00 10.19           C  
ANISOU  569  C   GLU A 609     1738    859   1276    151   -311   -154       C  
ATOM    570  O   GLU A 609      30.152   3.002  16.402  1.00 14.29           O  
ANISOU  570  O   GLU A 609     2529    820   2079     73   -787   -241       O  
ATOM    571  CB  GLU A 609      29.049   1.904  13.609  1.00 15.72           C  
ANISOU  571  CB  GLU A 609     2523   2355   1095    290   -104     28       C  
ATOM    572  CG  GLU A 609      28.206   1.408  12.451  1.00 18.68           C  
ANISOU  572  CG  GLU A 609     2900   2874   1323   -422   -231     60       C  
ATOM    573  CD  GLU A 609      28.869   1.350  11.090  1.00 19.73           C  
ANISOU  573  CD  GLU A 609     3225   3071   1201   -127   -218    -14       C  
ATOM    574  OE1 GLU A 609      29.871   0.608  10.865  1.00 20.30           O  
ANISOU  574  OE1 GLU A 609     2299   3439   1977   -622   -248   -240       O  
ATOM    575  OE2 GLU A 609      28.374   2.020  10.163  1.00 20.26           O  
ANISOU  575  OE2 GLU A 609     2571   3178   1950  -1094    -61   1064       O  
ATOM    576  N   GLU A 610      30.268   0.761  16.464  1.00  8.99           N  
ANISOU  576  N   GLU A 610     1177    783   1456    140   -109   -158       N  
ATOM    577  CA  GLU A 610      31.417   0.682  17.369  1.00 10.96           C  
ANISOU  577  CA  GLU A 610     1249   1208   1708    179   -179     23       C  
ATOM    578  C   GLU A 610      32.574  -0.075  16.734  1.00 10.14           C  
ANISOU  578  C   GLU A 610     1194   1198   1461    109   -378   -261       C  
ATOM    579  O   GLU A 610      32.348  -1.041  16.019  1.00 12.31           O  
ANISOU  579  O   GLU A 610     1474   1283   1922   -245    -40   -416       O  
ATOM    580  CB  GLU A 610      31.083   0.008  18.726  1.00 14.49           C  
ANISOU  580  CB  GLU A 610     1777   2032   1698    715    -37    336       C  
ATOM    581  CG  GLU A 610      30.230   0.915  19.598  1.00 17.27           C  
ANISOU  581  CG  GLU A 610     2463   2184   1915    309    267   -255       C  
ATOM    582  CD  GLU A 610      29.999   0.481  21.018  1.00 22.49           C  
ANISOU  582  CD  GLU A 610     3817   2683   2045   -218    739   -203       C  
ATOM    583  OE1 GLU A 610      30.312  -0.695  21.292  1.00 25.09           O  
ANISOU  583  OE1 GLU A 610     3399   3201   2933   -279   -593    718       O  
ATOM    584  OE2 GLU A 610      29.510   1.337  21.818  1.00 33.98           O  
ANISOU  584  OE2 GLU A 610     6226   3492   3193  -1440   2560  -1252       O  
ATOM    585  N   PHE A 611      33.783   0.363  17.030  1.00  8.89           N  
ANISOU  585  N   PHE A 611     1235   1190    954    -35    -93    -87       N  
ATOM    586  CA  PHE A 611      35.039  -0.127  16.505  1.00  9.96           C  
ANISOU  586  CA  PHE A 611     1259   1262   1264     -2     12    -32       C  
ATOM    587  C   PHE A 611      36.027  -0.396  17.638  1.00  9.30           C  
ANISOU  587  C   PHE A 611     1218    903   1411   -124   -146    -93       C  
ATOM    588  O   PHE A 611      35.984   0.319  18.666  1.00 13.77           O  
ANISOU  588  O   PHE A 611     2054   1538   1640    608   -457   -502       O  
ATOM    589  CB  PHE A 611      35.704   0.896  15.538  1.00 10.70           C  
ANISOU  589  CB  PHE A 611     1172   1644   1248   -215   -115     73       C  
ATOM    590  CG  PHE A 611      34.750   1.261  14.404  1.00 10.62           C  
ANISOU  590  CG  PHE A 611     1216   1673   1145   -116   -106    -11       C  
ATOM    591  CD1 PHE A 611      34.590   0.430  13.301  1.00 13.23           C  
ANISOU  591  CD1 PHE A 611     2032   2063    932    107    -80    -12       C  
ATOM    592  CD2 PHE A 611      33.991   2.406  14.458  1.00 13.25           C  
ANISOU  592  CD2 PHE A 611     1829   1755   1450    131   -357     81       C  
ATOM    593  CE1 PHE A 611      33.666   0.739  12.307  1.00 12.76           C  
ANISOU  593  CE1 PHE A 611     2292   1759    797   -131   -134     52       C  
ATOM    594  CE2 PHE A 611      33.070   2.743  13.477  1.00 13.53           C  
ANISOU  594  CE2 PHE A 611     1995   1749   1397    171   -423     17       C  
ATOM    595  CZ  PHE A 611      32.903   1.908  12.396  1.00 12.77           C  
ANISOU  595  CZ  PHE A 611     1854   1720   1276   -237   -152    112       C  
ATOM    596  N   PHE A 612      36.947  -1.335  17.450  1.00 10.15           N  
ANISOU  596  N   PHE A 612     1779    930   1149    141   -110     -6       N  
ATOM    597  CA  PHE A 612      37.855  -1.741  18.513  1.00 10.55           C  
ANISOU  597  CA  PHE A 612     1558   1091   1360     55   -104    184       C  
ATOM    598  C   PHE A 612      39.300  -1.645  18.069  1.00 11.52           C  
ANISOU  598  C   PHE A 612     1612   1399   1366   -125     -6   -137       C  
ATOM    599  O   PHE A 612      39.616  -2.060  16.943  1.00 13.31           O  
ANISOU  599  O   PHE A 612     1584   2087   1388    -26   -162   -432       O  
ATOM    600  CB  PHE A 612      37.558  -3.180  18.934  1.00 11.36           C  
ANISOU  600  CB  PHE A 612     1699   1069   1549     96    -11    255       C  
ATOM    601  CG  PHE A 612      38.401  -3.716  20.069  1.00  9.92           C  
ANISOU  601  CG  PHE A 612     1306    949   1515    -66    140    276       C  
ATOM    602  CD1 PHE A 612      38.149  -3.330  21.374  1.00 12.88           C  
ANISOU  602  CD1 PHE A 612     1679   1775   1439    267    252    391       C  
ATOM    603  CD2 PHE A 612      39.460  -4.558  19.812  1.00 11.23           C  
ANISOU  603  CD2 PHE A 612     1612    849   1806     56   -170   -136       C  
ATOM    604  CE1 PHE A 612      38.938  -3.805  22.404  1.00 15.29           C  
ANISOU  604  CE1 PHE A 612     2286   2050   1473    343     55    432       C  
ATOM    605  CE2 PHE A 612      40.244  -5.056  20.844  1.00 12.98           C  
ANISOU  605  CE2 PHE A 612     1704   1052   2177    134   -313     46       C  
ATOM    606  CZ  PHE A 612      40.003  -4.631  22.124  1.00 13.18           C  
ANISOU  606  CZ  PHE A 612     2014   1169   1824    -34   -283    502       C  
ATOM    607  N   TYR A 613      40.134  -1.112  18.946  1.00  9.32           N  
ANISOU  607  N   TYR A 613     1446   1154    941     58    168     14       N  
ATOM    608  CA  TYR A 613      41.585  -1.161  18.773  1.00 11.40           C  
ANISOU  608  CA  TYR A 613     1407   1431   1494   -177    229    439       C  
ATOM    609  C   TYR A 613      42.232  -1.931  19.917  1.00 10.49           C  
ANISOU  609  C   TYR A 613     1384   1294   1307    123    222     87       C  
ATOM    610  O   TYR A 613      42.041  -1.549  21.077  1.00 11.85           O  
ANISOU  610  O   TYR A 613     1507   1640   1354    296    139    -24       O  
ATOM    611  CB  TYR A 613      42.178   0.260  18.778  1.00 10.80           C  
ANISOU  611  CB  TYR A 613     1527   1340   1238    -74    261    150       C  
ATOM    612  CG  TYR A 613      41.833   1.118  17.580  1.00 10.62           C  
ANISOU  612  CG  TYR A 613     1683   1066   1288    -47    263     40       C  
ATOM    613  CD1 TYR A 613      42.460   0.878  16.367  1.00 11.53           C  
ANISOU  613  CD1 TYR A 613     2111   1236   1033    106    139   -108       C  
ATOM    614  CD2 TYR A 613      40.925   2.166  17.627  1.00 13.14           C  
ANISOU  614  CD2 TYR A 613     2285   1305   1404    359    177    -50       C  
ATOM    615  CE1 TYR A 613      42.194   1.633  15.232  1.00 13.20           C  
ANISOU  615  CE1 TYR A 613     2158   1501   1358    197     79    207       C  
ATOM    616  CE2 TYR A 613      40.657   2.934  16.514  1.00 13.85           C  
ANISOU  616  CE2 TYR A 613     1965   1506   1789    292    251    332       C  
ATOM    617  CZ  TYR A 613      41.288   2.669  15.316  1.00 13.06           C  
ANISOU  617  CZ  TYR A 613     2353   1128   1483     61     51     65       C  
ATOM    618  OH  TYR A 613      40.999   3.454  14.212  1.00 15.08           O  
ANISOU  618  OH  TYR A 613     2437   1494   1798    224     50    343       O  
ATOM    619  N   ASP A 614      43.055  -2.943  19.622  1.00 12.40           N  
ANISOU  619  N   ASP A 614     1652   1453   1609    229     40   -200       N  
ATOM    620  CA  ASP A 614      43.863  -3.608  20.640  1.00 14.51           C  
ANISOU  620  CA  ASP A 614     1931   1433   2151    442   -168    -62       C  
ATOM    621  C   ASP A 614      44.999  -2.690  21.074  1.00 14.96           C  
ANISOU  621  C   ASP A 614     2007   2041   1634     -4   -202    367       C  
ATOM    622  O   ASP A 614      45.843  -2.343  20.236  1.00 17.57           O  
ANISOU  622  O   ASP A 614     2072   2750   1854     98    109    222       O  
ATOM    623  CB  ASP A 614      44.525  -4.866  20.102  1.00 19.73           C  
ANISOU  623  CB  ASP A 614     2757   1579   3160    772    432    -28       C  
ATOM    624  CG  ASP A 614      43.670  -6.083  19.983  1.00 20.40           C  
ANISOU  624  CG  ASP A 614     3050   1598   3103    637    987   -576       C  
ATOM    625  OD1 ASP A 614      43.178  -6.593  20.995  1.00 23.14           O  
ANISOU  625  OD1 ASP A 614     3178   2660   2953    -40   -161    390       O  
ATOM    626  OD2 ASP A 614      43.557  -6.495  18.823  1.00 25.28           O  
ANISOU  626  OD2 ASP A 614     4110   2402   3094    262    590   -565       O  
ATOM    627  N   ILE A 615      45.065  -2.310  22.323  1.00 14.38           N  
ANISOU  627  N   ILE A 615     1772   1789   1902    200    103    -68       N  
ATOM    628  CA  ILE A 615      46.102  -1.368  22.733  1.00 14.18           C  
ANISOU  628  CA  ILE A 615     1609   1588   2190    482   -136    -58       C  
ATOM    629  C   ILE A 615      46.127  -1.383  24.257  1.00 13.03           C  
ANISOU  629  C   ILE A 615     1483   1331   2138    224    -20     70       C  
ATOM    630  O   ILE A 615      45.072  -1.507  24.872  1.00 16.99           O  
ANISOU  630  O   ILE A 615     1441   2563   2452    211     47     74       O  
ATOM    631  CB  ILE A 615      45.867   0.049  22.186  1.00 14.32           C  
ANISOU  631  CB  ILE A 615     1534   1730   2178    310   -504    113       C  
ATOM    632  CG1 ILE A 615      47.080   0.953  22.410  1.00 16.51           C  
ANISOU  632  CG1 ILE A 615     1837   2168   2266   -132   -790    599       C  
ATOM    633  CG2 ILE A 615      44.551   0.658  22.705  1.00 14.70           C  
ANISOU  633  CG2 ILE A 615     1712   1313   2560    379   -620   -289       C  
ATOM    634  CD1 ILE A 615      47.045   2.344  21.786  1.00 19.89           C  
ANISOU  634  CD1 ILE A 615     2381   2466   2709   -115    170   1045       C  
ATOM    635  N   LYS A 616      47.308  -1.275  24.816  1.00 13.99           N  
ANISOU  635  N   LYS A 616     1461   1732   2125    402      1    -18       N  
ATOM    636  CA  LYS A 616      47.456  -1.051  26.252  1.00 16.24           C  
ANISOU  636  CA  LYS A 616     1987   2010   2172    485   -215   -132       C  
ATOM    637  C   LYS A 616      46.968   0.333  26.615  1.00 15.97           C  
ANISOU  637  C   LYS A 616     2345   1988   1736    633    -96    148       C  
ATOM    638  O   LYS A 616      47.199   1.266  25.870  1.00 16.40           O  
ANISOU  638  O   LYS A 616     2513   2197   1521    681   -141    202       O  
ATOM    639  CB  LYS A 616      48.942  -1.166  26.668  1.00 20.16           C  
ANISOU  639  CB  LYS A 616     2323   2682   2655    815   -715    611       C  
ATOM    640  CG  LYS A 616      49.469  -2.579  26.668  1.00 25.46           C  
ANISOU  640  CG  LYS A 616     3306   3248   3121   1735   -647    203       C  
ATOM    641  CD  LYS A 616      50.893  -2.708  27.183  1.00 30.31           C  
ANISOU  641  CD  LYS A 616     3585   4493   3438   2309  -1049     62       C  
ATOM    642  CE  LYS A 616      51.226  -2.095  28.525  1.00 33.33           C  
ANISOU  642  CE  LYS A 616     2661   7406   2597    756     94    134       C  
ATOM    643  NZ  LYS A 616      52.676  -2.292  28.929  1.00 40.00           N  
ANISOU  643  NZ  LYS A 616     3404   8646   3146   1949   -796   -146       N  
ATOM    644  N   HIS A 617      46.363   0.502  27.785  1.00 15.67           N  
ANISOU  644  N   HIS A 617     2266   1807   1881    360     56    110       N  
ATOM    645  CA  HIS A 617      45.845   1.801  28.169  1.00 17.58           C  
ANISOU  645  CA  HIS A 617     3213   1755   1710    584    235    348       C  
ATOM    646  C   HIS A 617      46.869   2.921  28.172  1.00 18.08           C  
ANISOU  646  C   HIS A 617     3559   1710   1601    414   -119    340       C  
ATOM    647  O   HIS A 617      46.699   4.025  27.651  1.00 18.18           O  
ANISOU  647  O   HIS A 617     3413   1440   2055    611   -309     42       O  
ATOM    648  CB  HIS A 617      45.273   1.622  29.587  1.00 23.18           C  
ANISOU  648  CB  HIS A 617     4474   2192   2141    653   1111    275       C  
ATOM    649  CG  HIS A 617      44.813   2.885  30.205  1.00 31.38           C  
ANISOU  649  CG  HIS A 617     5540   2734   3651    782   2090   -386       C  
ATOM    650  ND1 HIS A 617      43.547   3.364  29.951  1.00 37.01           N  
ANISOU  650  ND1 HIS A 617     4998   3212   5850    809   2774  -1255       N  
ATOM    651  CD2 HIS A 617      45.405   3.738  31.080  1.00 34.06           C  
ANISOU  651  CD2 HIS A 617     6144   2504   4293    553   2335   -753       C  
ATOM    652  CE1 HIS A 617      43.374   4.477  30.635  1.00 38.01           C  
ANISOU  652  CE1 HIS A 617     5555   2852   6035    476   3146  -1042       C  
ATOM    653  NE2 HIS A 617      44.478   4.727  31.321  1.00 36.01           N  
ANISOU  653  NE2 HIS A 617     6448   2216   5019    595   2574   -409       N  
ATOM    654  N   SER A 618      48.016   2.672  28.781  1.00 20.47           N  
ANISOU  654  N   SER A 618     4183   1740   1852    118   -886    520       N  
ATOM    655  CA  SER A 618      49.066   3.701  28.817  1.00 23.03           C  
ANISOU  655  CA  SER A 618     4374   2318   2058   -240   -860    228       C  
ATOM    656  C   SER A 618      49.539   4.028  27.419  1.00 20.55           C  
ANISOU  656  C   SER A 618     3652   2164   1993   -172  -1242    514       C  
ATOM    657  O   SER A 618      50.066   5.114  27.107  1.00 22.47           O  
ANISOU  657  O   SER A 618     4155   2030   2354   -183   -964    345       O  
ATOM    658  CB  SER A 618      50.208   3.216  29.713  1.00 31.01           C  
ANISOU  658  CB  SER A 618     5581   3700   2502  -1416  -2108   1416       C  
ATOM    659  OG  SER A 618      50.723   1.933  29.376  1.00 36.16           O  
ANISOU  659  OG  SER A 618     3949   4796   4996    127  -1899   1991       O  
ATOM    660  N   ASP A 619      49.386   3.091  26.472  1.00 17.42           N  
ANISOU  660  N   ASP A 619     2762   1847   2010    116   -571    520       N  
ATOM    661  CA  ASP A 619      49.871   3.428  25.118  1.00 19.34           C  
ANISOU  661  CA  ASP A 619     2823   2326   2201    203   -368    711       C  
ATOM    662  C   ASP A 619      48.883   4.338  24.388  1.00 15.45           C  
ANISOU  662  C   ASP A 619     2205   2295   1372   -150   -470    252       C  
ATOM    663  O   ASP A 619      49.244   4.986  23.392  1.00 14.97           O  
ANISOU  663  O   ASP A 619     2244   1843   1600    383    -23    200       O  
ATOM    664  CB  ASP A 619      50.132   2.171  24.310  1.00 19.14           C  
ANISOU  664  CB  ASP A 619     2724   2411   2137    115    286    813       C  
ATOM    665  CG  ASP A 619      51.398   1.428  24.689  1.00 21.27           C  
ANISOU  665  CG  ASP A 619     2868   2203   3009     63   -272    390       C  
ATOM    666  OD1 ASP A 619      52.309   2.045  25.275  1.00 28.13           O  
ANISOU  666  OD1 ASP A 619     3722   2864   4103    116  -1305     -6       O  
ATOM    667  OD2 ASP A 619      51.429   0.236  24.327  1.00 25.54           O  
ANISOU  667  OD2 ASP A 619     2769   2408   4529    149    172   -206       O  
ATOM    668  N   LEU A 620      47.659   4.470  24.868  1.00 16.83           N  
ANISOU  668  N   LEU A 620     1986   2448   1960   -629   -410    640       N  
ATOM    669  CA  LEU A 620      46.811   5.529  24.341  1.00 17.12           C  
ANISOU  669  CA  LEU A 620     1923   2940   1643   -263     75    831       C  
ATOM    670  C   LEU A 620      47.413   6.927  24.519  1.00 15.55           C  
ANISOU  670  C   LEU A 620     1770   2578   1560    245   -110    470       C  
ATOM    671  O   LEU A 620      47.039   7.873  23.779  1.00 16.95           O  
ANISOU  671  O   LEU A 620     2209   2578   1653    573   -230    389       O  
ATOM    672  CB  LEU A 620      45.382   5.511  24.931  1.00 25.54           C  
ANISOU  672  CB  LEU A 620     1520   5234   2949   -540   -221    796       C  
ATOM    673  CG  LEU A 620      44.347   4.615  24.247  1.00 28.46           C  
ANISOU  673  CG  LEU A 620     2754   4778   3282  -1703    272   1002       C  
ATOM    674  CD1 LEU A 620      42.997   4.614  24.962  1.00 32.76           C  
ANISOU  674  CD1 LEU A 620     2179   5419   4849  -1387    145   2006       C  
ATOM    675  CD2 LEU A 620      44.128   4.985  22.779  1.00 29.06           C  
ANISOU  675  CD2 LEU A 620     2893   4960   3187   -574   -551    182       C  
ATOM    676  N   ALA A 621      48.341   7.105  25.435  1.00 17.92           N  
ANISOU  676  N   ALA A 621     3067   2131   1611   1026   -777   -347       N  
ATOM    677  CA  ALA A 621      48.995   8.394  25.683  1.00 20.70           C  
ANISOU  677  CA  ALA A 621     3364   2111   2391   1313  -1481   -763       C  
ATOM    678  C   ALA A 621      50.024   8.720  24.616  1.00 23.50           C  
ANISOU  678  C   ALA A 621     3484   2267   3178     53  -1429   -674       C  
ATOM    679  O   ALA A 621      50.706   9.756  24.626  1.00 28.55           O  
ANISOU  679  O   ALA A 621     5100   2063   3686   -311  -2459     51       O  
ATOM    680  CB  ALA A 621      49.581   8.405  27.109  1.00 27.74           C  
ANISOU  680  CB  ALA A 621     5271   2568   2701   1437  -2215   -949       C  
ATOM    681  N   LYS A 622      50.165   7.831  23.648  1.00 18.24           N  
ANISOU  681  N   LYS A 622     2089   2314   2527    283  -1254   -287       N  
ATOM    682  CA  LYS A 622      51.042   8.005  22.530  1.00 19.43           C  
ANISOU  682  CA  LYS A 622     1921   2000   3463   -228   -916     61       C  
ATOM    683  C   LYS A 622      50.302   8.281  21.244  1.00 14.98           C  
ANISOU  683  C   LYS A 622     1492   1436   2764   -189   -244    -70       C  
ATOM    684  O   LYS A 622      50.968   8.481  20.248  1.00 19.76           O  
ANISOU  684  O   LYS A 622     1630   2179   3700   -312    186    764       O  
ATOM    685  CB  LYS A 622      51.879   6.749  22.232  1.00 27.39           C  
ANISOU  685  CB  LYS A 622     2757   3229   4421   1203    370   1237       C  
ATOM    686  CG  LYS A 622      53.098   6.561  23.038  1.00 31.54           C  
ANISOU  686  CG  LYS A 622     3856   4696   3432   1927     73   1719       C  
ATOM    687  CD  LYS A 622      53.016   6.030  24.457  1.00 38.69           C  
ANISOU  687  CD  LYS A 622     4680   7241   2779  -3522   -452   1141       C  
ATOM    688  N   LYS A 623      48.970   8.221  21.301  1.00 13.42           N  
ANISOU  688  N   LYS A 623     1550   1619   1928     34   -182    182       N  
ATOM    689  CA  LYS A 623      48.205   8.166  20.070  1.00 11.89           C  
ANISOU  689  CA  LYS A 623     1363   1549   1606     68    140    -66       C  
ATOM    690  C   LYS A 623      47.228   9.349  19.965  1.00 11.21           C  
ANISOU  690  C   LYS A 623     1206   1445   1607    -65   -108   -194       C  
ATOM    691  O   LYS A 623      46.930  10.069  20.908  1.00 11.82           O  
ANISOU  691  O   LYS A 623     1669   1111   1709    -51   -281   -268       O  
ATOM    692  CB  LYS A 623      47.346   6.924  20.001  1.00 12.49           C  
ANISOU  692  CB  LYS A 623     1794   1432   1518    -71    -36    244       C  
ATOM    693  CG  LYS A 623      48.061   5.645  20.334  1.00 14.19           C  
ANISOU  693  CG  LYS A 623     1814   1629   1948    183    -45    186       C  
ATOM    694  CD  LYS A 623      49.111   5.324  19.309  1.00 18.96           C  
ANISOU  694  CD  LYS A 623     2202   2863   2141   1004    289   1039       C  
ATOM    695  CE  LYS A 623      49.735   3.949  19.608  1.00 21.36           C  
ANISOU  695  CE  LYS A 623     2584   2280   3251    900    507    389       C  
ATOM    696  NZ  LYS A 623      51.002   3.796  18.840  1.00 26.39           N  
ANISOU  696  NZ  LYS A 623     2970   3593   3462   1584    828    907       N  
ATOM    697  N   SER A 624      46.711   9.511  18.763  1.00 11.73           N  
ANISOU  697  N   SER A 624     1293   1614   1549   -177   -109    -73       N  
ATOM    698  CA  SER A 624      45.660  10.473  18.506  1.00 11.98           C  
ANISOU  698  CA  SER A 624     1406   1754   1392    -27    -15    -76       C  
ATOM    699  C   SER A 624      44.753   9.866  17.426  1.00 12.94           C  
ANISOU  699  C   SER A 624     1503   2385   1030    178    -69   -134       C  
ATOM    700  O   SER A 624      45.209   9.241  16.477  1.00 18.41           O  
ANISOU  700  O   SER A 624     1609   3851   1537    345    -71   -899       O  
ATOM    701  CB  SER A 624      46.226  11.824  18.072  1.00 18.89           C  
ANISOU  701  CB  SER A 624     2305   1910   2961   -180   -286    658       C  
ATOM    702  OG  SER A 624      45.256  12.844  18.156  1.00 26.79           O  
ANISOU  702  OG  SER A 624     3088   1878   5212     78    398    835       O  
ATOM    703  N   LEU A 625      43.449  10.061  17.555  1.00 13.24           N  
ANISOU  703  N   LEU A 625     1592   1939   1500    601   -387   -343       N  
ATOM    704  CA  LEU A 625      42.443   9.531  16.649  1.00 12.18           C  
ANISOU  704  CA  LEU A 625     1298   1894   1437    689    -46   -649       C  
ATOM    705  C   LEU A 625      41.998  10.612  15.694  1.00 13.35           C  
ANISOU  705  C   LEU A 625     1752   1872   1449    652   -626   -827       C  
ATOM    706  O   LEU A 625      41.403  11.599  16.071  1.00 16.33           O  
ANISOU  706  O   LEU A 625     2997   2011   1198   1118   -480   -601       O  
ATOM    707  CB  LEU A 625      41.283   9.019  17.486  1.00 15.79           C  
ANISOU  707  CB  LEU A 625     1699   2762   1539    252    256   -926       C  
ATOM    708  CG  LEU A 625      40.205   8.279  16.734  1.00 16.02           C  
ANISOU  708  CG  LEU A 625     1873   2290   1922    135    203   -747       C  
ATOM    709  CD1 LEU A 625      40.785   6.982  16.218  1.00 17.45           C  
ANISOU  709  CD1 LEU A 625     2091   2293   2248    243    349   -789       C  
ATOM    710  CD2 LEU A 625      39.005   8.022  17.656  1.00 27.13           C  
ANISOU  710  CD2 LEU A 625     2326   2694   5286   -251   1856  -1305       C  
ATOM    711  N   ASP A 626      42.324  10.408  14.435  1.00 13.01           N  
ANISOU  711  N   ASP A 626     1670   1721   1553    622   -354   -618       N  
ATOM    712  CA  ASP A 626      41.876  11.273  13.357  1.00 13.25           C  
ANISOU  712  CA  ASP A 626     1544   1910   1581    340   -196   -412       C  
ATOM    713  C   ASP A 626      40.526  10.793  12.842  1.00 11.51           C  
ANISOU  713  C   ASP A 626     1556   1424   1392    277   -165    -80       C  
ATOM    714  O   ASP A 626      40.442   9.651  12.391  1.00 14.97           O  
ANISOU  714  O   ASP A 626     2012   1598   2078    358   -427   -468       O  
ATOM    715  CB  ASP A 626      42.871  11.261  12.204  1.00 18.49           C  
ANISOU  715  CB  ASP A 626     1789   3191   2043   -225    256   -396       C  
ATOM    716  CG  ASP A 626      42.725  12.233  11.079  1.00 23.85           C  
ANISOU  716  CG  ASP A 626     2873   3548   2640   -940    489    258       C  
ATOM    717  OD1 ASP A 626      41.860  12.109  10.185  1.00 28.55           O  
ANISOU  717  OD1 ASP A 626     4386   3670   2791    359   -469     73       O  
ATOM    718  OD2 ASP A 626      43.576  13.148  11.014  1.00 46.48           O  
ANISOU  718  OD2 ASP A 626     7323   4281   6057  -3420   -101    550       O  
ATOM    719  N   ILE A 627      39.518  11.646  12.885  1.00 12.88           N  
ANISOU  719  N   ILE A 627     1731   1691   1471    480   -434   -325       N  
ATOM    720  CA  ILE A 627      38.147  11.371  12.475  1.00 12.51           C  
ANISOU  720  CA  ILE A 627     1720   1871   1163    482   -395   -445       C  
ATOM    721  C   ILE A 627      37.815  12.279  11.301  1.00 12.30           C  
ANISOU  721  C   ILE A 627     1668   1474   1530    258   -532   -390       C  
ATOM    722  O   ILE A 627      37.935  13.506  11.414  1.00 17.48           O  
ANISOU  722  O   ILE A 627     3340   1543   1759     82   -924   -594       O  
ATOM    723  CB AILE A 627      37.137  11.566  13.619  0.50 16.40           C  
ANISOU  723  CB AILE A 627     1794   3298   1140    357   -382   -789       C  
ATOM    724  CG1AILE A 627      37.559  10.702  14.819  0.50 16.02           C  
ANISOU  724  CG1AILE A 627     1775   3076   1236   -215      8   -465       C  
ATOM    725  CG2AILE A 627      35.710  11.289  13.221  0.50 20.94           C  
ANISOU  725  CG2AILE A 627     1781   4506   1669    226   -315  -1134       C  
ATOM    726  CD1AILE A 627      36.654  10.953  16.028  0.50 24.73           C  
ANISOU  726  CD1AILE A 627     1856   6236   1305   -488    222   -666       C  
ATOM    727  N   SER A 628      37.439  11.693  10.181  1.00 11.48           N  
ANISOU  727  N   SER A 628     1721   1354   1288    -36   -437   -163       N  
ATOM    728  CA  SER A 628      37.067  12.499   9.024  1.00 13.14           C  
ANISOU  728  CA  SER A 628     2003   1469   1522   -301   -446    164       C  
ATOM    729  C   SER A 628      35.729  12.018   8.449  1.00 11.26           C  
ANISOU  729  C   SER A 628     2047   1074   1157   -112   -487     53       C  
ATOM    730  O   SER A 628      35.459  10.816   8.434  1.00 12.34           O  
ANISOU  730  O   SER A 628     1957    987   1744     52   -531     18       O  
ATOM    731  CB  SER A 628      38.186  12.487   7.991  1.00 15.96           C  
ANISOU  731  CB  SER A 628     2414   1863   1786   -673    -50    -11       C  
ATOM    732  OG  SER A 628      38.509  11.186   7.537  1.00 16.07           O  
ANISOU  732  OG  SER A 628     2911   1908   1287   -220    -53    193       O  
ATOM    733  N   VAL A 629      34.946  13.004   8.029  1.00 11.04           N  
ANISOU  733  N   VAL A 629     1968    930   1296   -156   -323     69       N  
ATOM    734  CA  VAL A 629      33.593  12.761   7.549  1.00  9.54           C  
ANISOU  734  CA  VAL A 629     1826   1073    724    -56   -149   -101       C  
ATOM    735  C   VAL A 629      33.555  13.133   6.072  1.00  9.36           C  
ANISOU  735  C   VAL A 629     2095    706    756     80     26   -114       C  
ATOM    736  O   VAL A 629      34.017  14.238   5.712  1.00 10.61           O  
ANISOU  736  O   VAL A 629     2174    880    979   -138   -282     36       O  
ATOM    737  CB  VAL A 629      32.512  13.509   8.361  1.00 10.98           C  
ANISOU  737  CB  VAL A 629     2190   1265    715     79     61    -13       C  
ATOM    738  CG1 VAL A 629      31.121  13.153   7.856  1.00 11.83           C  
ANISOU  738  CG1 VAL A 629     1982   1491   1020    373    190   -338       C  
ATOM    739  CG2 VAL A 629      32.694  13.194   9.856  1.00 13.30           C  
ANISOU  739  CG2 VAL A 629     2815   1524    715    -88     -7     20       C  
ATOM    740  N   TRP A 630      33.027  12.221   5.282  1.00  9.32           N  
ANISOU  740  N   TRP A 630     1928    971    641   -287     27     21       N  
ATOM    741  CA  TRP A 630      33.028  12.263   3.841  1.00 10.01           C  
ANISOU  741  CA  TRP A 630     2143    968    691   -398     12     49       C  
ATOM    742  C   TRP A 630      31.646  12.094   3.233  1.00 11.22           C  
ANISOU  742  C   TRP A 630     2219   1416    626   -377    -66     14       C  
ATOM    743  O   TRP A 630      30.808  11.417   3.831  1.00 11.92           O  
ANISOU  743  O   TRP A 630     2114   1483    930   -500   -429    400       O  
ATOM    744  CB  TRP A 630      33.954  11.163   3.285  1.00 12.13           C  
ANISOU  744  CB  TRP A 630     2256   1372    981   -361    208   -355       C  
ATOM    745  CG  TRP A 630      35.382  11.357   3.733  1.00 13.36           C  
ANISOU  745  CG  TRP A 630     2223   1771   1082   -211    198   -106       C  
ATOM    746  CD1 TRP A 630      35.957  10.925   4.873  1.00 14.30           C  
ANISOU  746  CD1 TRP A 630     2384   1823   1227    236    112   -224       C  
ATOM    747  CD2 TRP A 630      36.440  12.029   3.023  1.00 14.02           C  
ANISOU  747  CD2 TRP A 630     2099   1639   1590   -184    309   -220       C  
ATOM    748  NE1 TRP A 630      37.280  11.282   4.947  1.00 17.32           N  
ANISOU  748  NE1 TRP A 630     2439   2320   1823    172   -156   -373       N  
ATOM    749  CE2 TRP A 630      37.611  11.961   3.825  1.00 16.19           C  
ANISOU  749  CE2 TRP A 630     2029   1717   2407    205    145   -262       C  
ATOM    750  CE3 TRP A 630      36.519  12.691   1.793  1.00 16.65           C  
ANISOU  750  CE3 TRP A 630     2197   2421   1706   -214    759     53       C  
ATOM    751  CZ2 TRP A 630      38.811  12.527   3.420  1.00 20.82           C  
ANISOU  751  CZ2 TRP A 630     2089   2617   3204   -195     84   -257       C  
ATOM    752  CZ3 TRP A 630      37.724  13.256   1.394  1.00 19.80           C  
ANISOU  752  CZ3 TRP A 630     2349   3102   2071   -420   1022   -133       C  
ATOM    753  CH2 TRP A 630      38.847  13.166   2.211  1.00 20.09           C  
ANISOU  753  CH2 TRP A 630     2201   2402   3029   -257    759   -502       C  
ATOM    754  N   ASP A 631      31.437  12.725   2.067  1.00 10.98           N  
ANISOU  754  N   ASP A 631     2032   1450    692   -237     88     79       N  
ATOM    755  CA  ASP A 631      30.224  12.527   1.312  1.00 11.29           C  
ANISOU  755  CA  ASP A 631     2349   1243    698    -82   -171   -108       C  
ATOM    756  C   ASP A 631      30.556  11.623   0.129  1.00 11.64           C  
ANISOU  756  C   ASP A 631     2065   1314   1043   -254    177   -255       C  
ATOM    757  O   ASP A 631      31.287  11.979  -0.774  1.00 13.01           O  
ANISOU  757  O   ASP A 631     2455   1477   1010   -380    243   -136       O  
ATOM    758  CB  ASP A 631      29.673  13.865   0.840  1.00 11.92           C  
ANISOU  758  CB  ASP A 631     2582   1255    692    -41   -143   -100       C  
ATOM    759  CG  ASP A 631      28.807  13.758  -0.409  1.00 13.04           C  
ANISOU  759  CG  ASP A 631     2642   1542    770    -70   -243    151       C  
ATOM    760  OD1 ASP A 631      27.893  12.896  -0.428  1.00 13.34           O  
ANISOU  760  OD1 ASP A 631     2420   1889    761    -88   -148    -67       O  
ATOM    761  OD2 ASP A 631      29.033  14.513  -1.384  1.00 14.86           O  
ANISOU  761  OD2 ASP A 631     3360   1585    702    160     36    142       O  
ATOM    762  N   TYR A 632      30.042  10.394   0.128  1.00 10.79           N  
ANISOU  762  N   TYR A 632     2194   1156    748   -112      8    -61       N  
ATOM    763  CA  TYR A 632      30.237   9.439  -0.947  1.00 11.54           C  
ANISOU  763  CA  TYR A 632     2558   1175    654   -155   -101    -44       C  
ATOM    764  C   TYR A 632      29.555   9.927  -2.230  1.00 11.99           C  
ANISOU  764  C   TYR A 632     2316   1617    622     22     31    -49       C  
ATOM    765  O   TYR A 632      28.383  10.316  -2.207  1.00 12.59           O  
ANISOU  765  O   TYR A 632     2239   1600    944   -101    -30   -186       O  
ATOM    766  CB  TYR A 632      29.688   8.056  -0.581  1.00 11.40           C  
ANISOU  766  CB  TYR A 632     2204   1202    925   -119    176   -136       C  
ATOM    767  CG  TYR A 632      29.818   7.049  -1.723  1.00 15.06           C  
ANISOU  767  CG  TYR A 632     3414   1237   1071   -260    295   -247       C  
ATOM    768  CD1 TYR A 632      31.021   6.429  -1.959  1.00 19.14           C  
ANISOU  768  CD1 TYR A 632     4345   1313   1614    465    997   -106       C  
ATOM    769  CD2 TYR A 632      28.739   6.753  -2.537  1.00 21.34           C  
ANISOU  769  CD2 TYR A 632     4496   2383   1231  -1042   -207   -463       C  
ATOM    770  CE1 TYR A 632      31.192   5.513  -2.990  1.00 24.14           C  
ANISOU  770  CE1 TYR A 632     5694   1842   1637    155   1687   -312       C  
ATOM    771  CE2 TYR A 632      28.902   5.845  -3.550  1.00 28.27           C  
ANISOU  771  CE2 TYR A 632     6125   2592   2024  -1223   -233  -1043       C  
ATOM    772  CZ  TYR A 632      30.101   5.238  -3.771  1.00 29.81           C  
ANISOU  772  CZ  TYR A 632     7187   2560   1580   -502    906   -496       C  
ATOM    773  OH  TYR A 632      30.147   4.337  -4.823  1.00 45.51           O  
ANISOU  773  OH  TYR A 632    10941   4611   1740   1808   -675  -1433       O  
ATOM    774  N   ASP A 633      30.338   9.902  -3.316  1.00 12.86           N  
ANISOU  774  N   ASP A 633     2370   1994    521    -27    -42   -293       N  
ATOM    775  CA  ASP A 633      29.788  10.184  -4.635  1.00 14.02           C  
ANISOU  775  CA  ASP A 633     3177   1614    536   -297   -224    -79       C  
ATOM    776  C   ASP A 633      30.090   9.012  -5.581  1.00 13.46           C  
ANISOU  776  C   ASP A 633     2593   1956    566   -517    106   -249       C  
ATOM    777  O   ASP A 633      31.129   8.355  -5.508  1.00 14.66           O  
ANISOU  777  O   ASP A 633     2743   2016    810   -380     36   -277       O  
ATOM    778  CB  ASP A 633      30.385  11.491  -5.154  1.00 14.74           C  
ANISOU  778  CB  ASP A 633     2684   1809   1106   -276    169    -52       C  
ATOM    779  CG  ASP A 633      29.937  12.772  -4.496  1.00 12.99           C  
ANISOU  779  CG  ASP A 633     2871   1583    483   -292     11    192       C  
ATOM    780  OD1 ASP A 633      28.860  12.801  -3.858  1.00 14.85           O  
ANISOU  780  OD1 ASP A 633     2782   2168    692   -311     31   -258       O  
ATOM    781  OD2 ASP A 633      30.699  13.770  -4.606  1.00 16.79           O  
ANISOU  781  OD2 ASP A 633     3376   1793   1209   -576    121    192       O  
ATOM    782  N   ILE A 634      29.102   8.770  -6.462  1.00 15.25           N  
ANISOU  782  N   ILE A 634     3102   1925    769   -301   -292   -365       N  
ATOM    783  CA  ILE A 634      29.164   7.633  -7.376  1.00 15.20           C  
ANISOU  783  CA  ILE A 634     3033   2067    674   -331   -136   -383       C  
ATOM    784  C   ILE A 634      29.973   7.942  -8.607  1.00 15.65           C  
ANISOU  784  C   ILE A 634     2548   2312   1086   -570      4   -443       C  
ATOM    785  O   ILE A 634      30.566   7.004  -9.169  1.00 18.22           O  
ANISOU  785  O   ILE A 634     2535   2810   1579    -25    130   -326       O  
ATOM    786  CB  ILE A 634      27.741   7.157  -7.750  1.00 22.95           C  
ANISOU  786  CB  ILE A 634     3476   3198   2044  -1766    741  -1268       C  
ATOM    787  CG1 ILE A 634      27.023   6.759  -6.465  1.00 26.08           C  
ANISOU  787  CG1 ILE A 634     4028   3392   2491  -1258    556    292       C  
ATOM    788  CG2 ILE A 634      27.809   6.061  -8.801  1.00 37.85           C  
ANISOU  788  CG2 ILE A 634     2668   6450   5265  -1107    534  -4436       C  
ATOM    789  CD1 ILE A 634      25.526   6.585  -6.589  1.00 29.78           C  
ANISOU  789  CD1 ILE A 634     3775   3793   3747   -802   1568    124       C  
ATOM    790  N   GLY A 635      30.041   9.205  -9.011  1.00 18.03           N  
ANISOU  790  N   GLY A 635     3448   2437    964   -698    225   -333       N  
ATOM    791  CA  GLY A 635      30.591   9.600 -10.312  1.00 15.89           C  
ANISOU  791  CA  GLY A 635     2630   2522    885   -221    172   -356       C  
ATOM    792  C   GLY A 635      31.677  10.644 -10.214  1.00 14.79           C  
ANISOU  792  C   GLY A 635     2684   2137    800    -45    125   -104       C  
ATOM    793  O   GLY A 635      31.959  11.301 -11.199  1.00 18.36           O  
ANISOU  793  O   GLY A 635     3905   2132    939   -260    305     -8       O  
ATOM    794  N   LYS A 636      32.300  10.789  -9.052  1.00 16.97           N  
ANISOU  794  N   LYS A 636     2940   2650    859   -652    137   -156       N  
ATOM    795  CA  LYS A 636      33.366  11.698  -8.746  1.00 18.10           C  
ANISOU  795  CA  LYS A 636     3097   2597   1183   -892      2    281       C  
ATOM    796  C   LYS A 636      34.025  11.311  -7.425  1.00 16.69           C  
ANISOU  796  C   LYS A 636     3627   2225    487  -1192    223   -359       C  
ATOM    797  O   LYS A 636      33.569  10.439  -6.709  1.00 18.20           O  
ANISOU  797  O   LYS A 636     3303   2762    849   -961    369    161       O  
ATOM    798  CB  LYS A 636      32.945  13.158  -8.610  1.00 20.90           C  
ANISOU  798  CB  LYS A 636     3692   2724   1527   -764    -94   -178       C  
ATOM    799  CG  LYS A 636      31.840  13.523  -7.682  1.00 21.03           C  
ANISOU  799  CG  LYS A 636     4104   2496   1391   -757    170     36       C  
ATOM    800  CD  LYS A 636      31.573  15.026  -7.695  1.00 21.54           C  
ANISOU  800  CD  LYS A 636     4203   2543   1439   -535    -15    181       C  
ATOM    801  CE  LYS A 636      32.566  15.830  -6.922  1.00 22.05           C  
ANISOU  801  CE  LYS A 636     4661   2462   1253  -1091    427    172       C  
ATOM    802  NZ  LYS A 636      32.802  15.457  -5.541  1.00 24.74           N  
ANISOU  802  NZ  LYS A 636     5579   2358   1463   -609   -338    -17       N  
ATOM    803  N   SER A 637      35.128  12.032  -7.158  1.00 17.46           N  
ANISOU  803  N   SER A 637     2924   2607   1105   -854    179   -248       N  
ATOM    804  CA  SER A 637      35.786  11.842  -5.890  1.00 15.85           C  
ANISOU  804  CA  SER A 637     2759   2222   1040   -614    288   -260       C  
ATOM    805  C   SER A 637      34.858  12.165  -4.736  1.00 15.13           C  
ANISOU  805  C   SER A 637     2650   2045   1055   -312    214    -71       C  
ATOM    806  O   SER A 637      34.029  13.049  -4.882  1.00 17.26           O  
ANISOU  806  O   SER A 637     2833   2699   1027     35     30     64       O  
ATOM    807  CB  SER A 637      37.010  12.738  -5.813  1.00 18.22           C  
ANISOU  807  CB  SER A 637     2946   2913   1062   -991    310   -454       C  
ATOM    808  OG  SER A 637      38.048  12.356  -6.681  1.00 19.50           O  
ANISOU  808  OG  SER A 637     3302   2473   1634  -1070    864   -293       O  
ATOM    809  N   ASN A 638      35.030  11.479  -3.607  1.00 15.53           N  
ANISOU  809  N   ASN A 638     3033   1850   1018   -104    313   -147       N  
ATOM    810  CA  ASN A 638      34.170  11.778  -2.463  1.00 15.11           C  
ANISOU  810  CA  ASN A 638     2876   1863   1002   -533    334   -150       C  
ATOM    811  C   ASN A 638      34.492  13.175  -1.970  1.00 15.47           C  
ANISOU  811  C   ASN A 638     2727   2090   1061   -844    621   -385       C  
ATOM    812  O   ASN A 638      35.655  13.600  -2.042  1.00 18.07           O  
ANISOU  812  O   ASN A 638     2564   3088   1213   -993     11   -242       O  
ATOM    813  CB  ASN A 638      34.384  10.737  -1.363  1.00 13.60           C  
ANISOU  813  CB  ASN A 638     2024   2125   1018   -266      6   -106       C  
ATOM    814  CG  ASN A 638      34.051   9.325  -1.837  1.00 13.23           C  
ANISOU  814  CG  ASN A 638     1967   1984   1076   -373    258    102       C  
ATOM    815  OD1 ASN A 638      33.179   9.125  -2.687  1.00 13.83           O  
ANISOU  815  OD1 ASN A 638     2119   2036   1099   -220    187   -308       O  
ATOM    816  ND2 ASN A 638      34.764   8.318  -1.307  1.00 17.10           N  
ANISOU  816  ND2 ASN A 638     2658   2135   1703   -271   -105    317       N  
ATOM    817  N   ASP A 639      33.464  13.894  -1.490  1.00 15.98           N  
ANISOU  817  N   ASP A 639     2983   2277    814   -646    507   -618       N  
ATOM    818  CA  ASP A 639      33.660  15.236  -0.960  1.00 17.71           C  
ANISOU  818  CA  ASP A 639     3969   1944    815   -485    -73   -293       C  
ATOM    819  C   ASP A 639      33.976  15.216   0.535  1.00 14.27           C  
ANISOU  819  C   ASP A 639     2937   1635    850   -831    119   -161       C  
ATOM    820  O   ASP A 639      33.329  14.492   1.269  1.00 15.29           O  
ANISOU  820  O   ASP A 639     2697   2009   1105   -866    220     52       O  
ATOM    821  CB  ASP A 639      32.413  16.111  -1.221  1.00 19.93           C  
ANISOU  821  CB  ASP A 639     4423   1986   1164   -294   -329     47       C  
ATOM    822  CG  ASP A 639      32.266  16.528  -2.661  1.00 18.80           C  
ANISOU  822  CG  ASP A 639     3708   2574    860   -117    133   -233       C  
ATOM    823  OD1 ASP A 639      33.302  16.926  -3.246  1.00 28.38           O  
ANISOU  823  OD1 ASP A 639     4414   4752   1616  -1962   -186    222       O  
ATOM    824  OD2 ASP A 639      31.133  16.485  -3.213  1.00 19.32           O  
ANISOU  824  OD2 ASP A 639     4037   2096   1209   -724   -266   -193       O  
ATOM    825  N   TYR A 640      34.929  16.029   0.947  1.00 15.17           N  
ANISOU  825  N   TYR A 640     2873   1939    951   -967    152    -76       N  
ATOM    826  CA  TYR A 640      35.262  16.155   2.368  1.00 13.90           C  
ANISOU  826  CA  TYR A 640     2936   1481    865  -1130    481   -404       C  
ATOM    827  C   TYR A 640      34.245  17.046   3.054  1.00 12.91           C  
ANISOU  827  C   TYR A 640     2670   1220   1014   -791    172     99       C  
ATOM    828  O   TYR A 640      34.029  18.184   2.627  1.00 17.79           O  
ANISOU  828  O   TYR A 640     3921   1550   1290   -547    274    544       O  
ATOM    829  CB  TYR A 640      36.651  16.722   2.468  1.00 16.03           C  
ANISOU  829  CB  TYR A 640     2606   2428   1057   -880    126     61       C  
ATOM    830  CG  TYR A 640      37.168  16.974   3.858  1.00 15.14           C  
ANISOU  830  CG  TYR A 640     2675   2015   1063   -676     78     12       C  
ATOM    831  CD1 TYR A 640      37.517  15.939   4.702  1.00 18.03           C  
ANISOU  831  CD1 TYR A 640     3504   2237   1110   -636    263    263       C  
ATOM    832  CD2 TYR A 640      37.344  18.269   4.343  1.00 18.75           C  
ANISOU  832  CD2 TYR A 640     3419   2088   1617   -556   -260   -162       C  
ATOM    833  CE1 TYR A 640      38.001  16.115   5.981  1.00 17.27           C  
ANISOU  833  CE1 TYR A 640     3021   2517   1024   -368    347    331       C  
ATOM    834  CE2 TYR A 640      37.844  18.479   5.621  1.00 20.03           C  
ANISOU  834  CE2 TYR A 640     3447   2280   1883   -465   -521   -419       C  
ATOM    835  CZ  TYR A 640      38.171  17.405   6.426  1.00 20.16           C  
ANISOU  835  CZ  TYR A 640     3186   2846   1628   -407   -256    -98       C  
ATOM    836  OH  TYR A 640      38.652  17.684   7.685  1.00 21.69           O  
ANISOU  836  OH  TYR A 640     3177   3546   1518  -1124    -71     22       O  
ATOM    837  N   ILE A 641      33.623  16.543   4.125  1.00 11.68           N  
ANISOU  837  N   ILE A 641     2482   1030    927     21    230    218       N  
ATOM    838  CA  ILE A 641      32.693  17.347   4.912  1.00 11.84           C  
ANISOU  838  CA  ILE A 641     2485    894   1121    -41     -6   -126       C  
ATOM    839  C   ILE A 641      33.463  18.061   6.003  1.00 12.22           C  
ANISOU  839  C   ILE A 641     2570   1015   1057   -172    -27     42       C  
ATOM    840  O   ILE A 641      33.429  19.273   6.156  1.00 14.91           O  
ANISOU  840  O   ILE A 641     3170   1074   1422     -7   -266   -342       O  
ATOM    841  CB  ILE A 641      31.493  16.523   5.421  1.00 11.89           C  
ANISOU  841  CB  ILE A 641     2289   1354    874    -27     23    -88       C  
ATOM    842  CG1 ILE A 641      30.666  15.986   4.254  1.00 13.88           C  
ANISOU  842  CG1 ILE A 641     2120   2017   1137   -173   -290    238       C  
ATOM    843  CG2 ILE A 641      30.584  17.323   6.334  1.00 15.77           C  
ANISOU  843  CG2 ILE A 641     2227   1971   1795    540     53   -215       C  
ATOM    844  CD1 ILE A 641      29.574  14.999   4.562  1.00 14.76           C  
ANISOU  844  CD1 ILE A 641     1886   2562   1160   -307     76    -51       C  
ATOM    845  N   GLY A 642      34.189  17.323   6.807  1.00 12.61           N  
ANISOU  845  N   GLY A 642     2641   1243    907      5      4    -89       N  
ATOM    846  CA  GLY A 642      34.957  17.970   7.865  1.00 12.29           C  
ANISOU  846  CA  GLY A 642     2309   1141   1218    -31    -43    -88       C  
ATOM    847  C   GLY A 642      35.555  16.900   8.768  1.00 11.25           C  
ANISOU  847  C   GLY A 642     2167   1038   1069   -163     21   -129       C  
ATOM    848  O   GLY A 642      35.351  15.699   8.570  1.00 14.65           O  
ANISOU  848  O   GLY A 642     3192   1040   1334    -65   -326   -166       O  
ATOM    849  N   GLY A 643      36.298  17.289   9.789  1.00 12.86           N  
ANISOU  849  N   GLY A 643     2246   1337   1305    -39   -174   -225       N  
ATOM    850  CA  GLY A 643      37.043  16.366  10.602  1.00 12.43           C  
ANISOU  850  CA  GLY A 643     2151   1330   1243    146      1   -249       C  
ATOM    851  C   GLY A 643      37.273  16.882  12.018  1.00 14.07           C  
ANISOU  851  C   GLY A 643     2158   1598   1590     36   -564   -552       C  
ATOM    852  O   GLY A 643      37.065  18.040  12.375  1.00 17.72           O  
ANISOU  852  O   GLY A 643     2495   1916   2323    446   -388  -1041       O  
ATOM    853  N   CYS A 644      37.740  15.979  12.861  1.00 17.05           N  
ANISOU  853  N   CYS A 644     2246   2498   1732    879   -925   -677       N  
ATOM    854  CA  CYS A 644      38.313  16.473  14.107  1.00 23.34           C  
ANISOU  854  CA  CYS A 644     3525   3349   1994   1860  -1388  -1378       C  
ATOM    855  C   CYS A 644      39.294  15.404  14.591  1.00 25.24           C  
ANISOU  855  C   CYS A 644     4339   3177   2076   1788  -1889   -968       C  
ATOM    856  O   CYS A 644      39.218  14.210  14.275  1.00 34.79           O  
ANISOU  856  O   CYS A 644     4538   3673   5009   2552  -3324  -2358       O  
ATOM    857  CB  CYS A 644      37.256  16.819  15.128  1.00 24.15           C  
ANISOU  857  CB  CYS A 644     3605   3858   1714   1141  -1029   -892       C  
ATOM    858  SG  CYS A 644      36.394  15.351  15.752  1.00 35.87           S  
ANISOU  858  SG  CYS A 644     2923   3396   7309   1333   -312   -593       S  
ATOM    859  N   GLN A 645      40.252  15.906  15.322  1.00 17.91           N  
ANISOU  859  N   GLN A 645     3006   2541   1259   1435   -519   -488       N  
ATOM    860  CA  GLN A 645      41.246  15.043  15.917  1.00 14.68           C  
ANISOU  860  CA  GLN A 645     2127   2135   1315    824   -163   -174       C  
ATOM    861  C   GLN A 645      40.930  14.933  17.417  1.00 12.69           C  
ANISOU  861  C   GLN A 645     1466   1985   1371    805    -50   -178       C  
ATOM    862  O   GLN A 645      40.706  15.947  18.086  1.00 17.35           O  
ANISOU  862  O   GLN A 645     3108   1952   1533    438    -64   -445       O  
ATOM    863  CB  GLN A 645      42.609  15.627  15.676  1.00 21.58           C  
ANISOU  863  CB  GLN A 645     2571   3317   2311    466    427   1146       C  
ATOM    864  N   LEU A 646      40.890  13.730  17.946  1.00 12.95           N  
ANISOU  864  N   LEU A 646     1719   1917   1286    493   -286   -314       N  
ATOM    865  CA  LEU A 646      40.660  13.471  19.360  1.00 13.09           C  
ANISOU  865  CA  LEU A 646     1808   1851   1315     35    -36   -408       C  
ATOM    866  C   LEU A 646      41.888  12.723  19.870  1.00 12.68           C  
ANISOU  866  C   LEU A 646     2256   1438   1125     87   -226   -196       C  
ATOM    867  O   LEU A 646      42.056  11.551  19.482  1.00 15.25           O  
ANISOU  867  O   LEU A 646     2984   1415   1394     94   -107   -202       O  
ATOM    868  CB  LEU A 646      39.483  12.558  19.639  1.00 17.37           C  
ANISOU  868  CB  LEU A 646     2172   1947   2479   -220    385   -700       C  
ATOM    869  CG  LEU A 646      38.113  12.993  19.231  1.00 17.46           C  
ANISOU  869  CG  LEU A 646     2211   1653   2770   -767   -255   -293       C  
ATOM    870  CD1 LEU A 646      37.030  12.056  19.810  1.00 15.97           C  
ANISOU  870  CD1 LEU A 646     2274   2144   1649   -644     80   -349       C  
ATOM    871  CD2 LEU A 646      37.900  14.430  19.681  1.00 19.55           C  
ANISOU  871  CD2 LEU A 646     2995   1631   2804    -13   -627     14       C  
ATOM    872  N   GLY A 647      42.676  13.371  20.706  1.00 12.24           N  
ANISOU  872  N   GLY A 647     1729   1540   1381   -312     52    -41       N  
ATOM    873  CA  GLY A 647      43.885  12.714  21.103  1.00 13.15           C  
ANISOU  873  CA  GLY A 647     1855   1580   1562   -386   -116    345       C  
ATOM    874  C   GLY A 647      44.940  13.699  21.613  1.00 10.28           C  
ANISOU  874  C   GLY A 647     1664   1362    879   -128    177    120       C  
ATOM    875  O   GLY A 647      44.627  14.859  21.822  1.00 12.86           O  
ANISOU  875  O   GLY A 647     1718   1552   1617     17    350   -280       O  
ATOM    876  N   ILE A 648      46.167  13.192  21.793  1.00 12.07           N  
ANISOU  876  N   ILE A 648     1740   1518   1330     40    -44   -248       N  
ATOM    877  CA  ILE A 648      47.156  13.998  22.505  1.00 12.74           C  
ANISOU  877  CA  ILE A 648     1409   1698   1734    -81    403   -619       C  
ATOM    878  C   ILE A 648      47.630  15.241  21.786  1.00 16.74           C  
ANISOU  878  C   ILE A 648     1203   1939   3218      4    781     11       C  
ATOM    879  O   ILE A 648      48.224  16.108  22.438  1.00 21.69           O  
ANISOU  879  O   ILE A 648     1104   2093   5043   -353     84     55       O  
ATOM    880  CB  ILE A 648      48.378  13.134  22.872  1.00 12.54           C  
ANISOU  880  CB  ILE A 648     1096   1636   2034   -348    440   -465       C  
ATOM    881  CG1 ILE A 648      49.173  12.589  21.695  1.00 13.04           C  
ANISOU  881  CG1 ILE A 648     1403   1375   2175    -17    443   -388       C  
ATOM    882  CG2 ILE A 648      47.888  12.011  23.757  1.00 15.29           C  
ANISOU  882  CG2 ILE A 648     1408   2518   1884   -634   -133    171       C  
ATOM    883  CD1 ILE A 648      50.416  11.827  22.092  1.00 14.83           C  
ANISOU  883  CD1 ILE A 648     1915   1277   2443    339    450    -39       C  
ATOM    884  N   SER A 649      47.423  15.348  20.478  1.00 20.03           N  
ANISOU  884  N   SER A 649     2701   1757   3155   1139   1239    453       N  
ATOM    885  CA  SER A 649      47.911  16.572  19.792  1.00 26.55           C  
ANISOU  885  CA  SER A 649     2891   2388   4808   1370   1855   1424       C  
ATOM    886  C   SER A 649      46.711  17.481  19.519  1.00 23.02           C  
ANISOU  886  C   SER A 649     2785   2674   3290   1261   1751   1536       C  
ATOM    887  O   SER A 649      46.776  18.471  18.791  1.00 34.03           O  
ANISOU  887  O   SER A 649     4078   3433   5417   2152   2972   2817       O  
ATOM    888  CB  SER A 649      48.741  16.217  18.570  1.00 33.52           C  
ANISOU  888  CB  SER A 649     2411   5296   5031   1949   2230   2117       C  
ATOM    889  OG ASER A 649      50.093  15.755  18.678  0.50 34.37           O  
ANISOU  889  OG ASER A 649     3600   6837   2622   3743     31   -255       O  
ATOM    890  N   ALA A 650      45.547  17.230  20.134  1.00 17.38           N  
ANISOU  890  N   ALA A 650     2390   2026   2188    613   1066    103       N  
ATOM    891  CA  ALA A 650      44.428  18.167  20.055  1.00 13.38           C  
ANISOU  891  CA  ALA A 650     1983   1729   1373    237    580    231       C  
ATOM    892  C   ALA A 650      44.531  19.304  21.056  1.00 13.01           C  
ANISOU  892  C   ALA A 650     1623   1413   1906    328    102    251       C  
ATOM    893  O   ALA A 650      45.445  19.401  21.872  1.00 14.80           O  
ANISOU  893  O   ALA A 650     1719   1620   2284     93    -74    247       O  
ATOM    894  CB  ALA A 650      43.103  17.401  20.268  1.00 16.62           C  
ANISOU  894  CB  ALA A 650     2173   2260   1882   -254    215   -162       C  
ATOM    895  N   LYS A 651      43.545  20.200  21.010  1.00 15.41           N  
ANISOU  895  N   LYS A 651     1968   1891   1996    728    147     96       N  
ATOM    896  CA  LYS A 651      43.350  21.302  21.932  1.00 16.38           C  
ANISOU  896  CA  LYS A 651     2316   1316   2593    114    756    110       C  
ATOM    897  C   LYS A 651      41.922  21.301  22.463  1.00 15.14           C  
ANISOU  897  C   LYS A 651     2251    858   2643     72    630   -215       C  
ATOM    898  O   LYS A 651      41.045  20.669  21.914  1.00 15.35           O  
ANISOU  898  O   LYS A 651     2205   1495   2133    256    323   -150       O  
ATOM    899  CB  LYS A 651      43.658  22.639  21.240  1.00 23.32           C  
ANISOU  899  CB  LYS A 651     3547   1737   3577    323   1827    668       C  
ATOM    900  CG  LYS A 651      45.129  22.747  20.850  1.00 26.85           C  
ANISOU  900  CG  LYS A 651     4217   1620   4367    426   3249    419       C  
ATOM    901  CD  LYS A 651      45.563  24.169  20.578  1.00 30.83           C  
ANISOU  901  CD  LYS A 651     5098   2214   4403  -1002   1806    293       C  
ATOM    902  CE  LYS A 651      46.905  24.253  19.864  1.00 36.08           C  
ANISOU  902  CE  LYS A 651     5752   2647   5310  -1171   2534   1208       C  
ATOM    903  NZ  LYS A 651      46.774  25.364  18.856  1.00 50.24           N  
ANISOU  903  NZ  LYS A 651     6890   4579   7620   1115   4108   3214       N  
ATOM    904  N   GLY A 652      41.668  21.993  23.556  1.00 15.95           N  
ANISOU  904  N   GLY A 652     2192   1598   2271   -251    610   -218       N  
ATOM    905  CA  GLY A 652      40.323  22.313  24.025  1.00 14.44           C  
ANISOU  905  CA  GLY A 652     2124   1293   2071   -131    475   -151       C  
ATOM    906  C   GLY A 652      39.539  21.037  24.333  1.00 11.76           C  
ANISOU  906  C   GLY A 652     1884   1133   1453    122    305   -125       C  
ATOM    907  O   GLY A 652      40.078  20.080  24.923  1.00 13.88           O  
ANISOU  907  O   GLY A 652     2267   1219   1787     65   -280   -104       O  
ATOM    908  N   GLU A 653      38.259  21.028  23.995  1.00 13.08           N  
ANISOU  908  N   GLU A 653     1757   1265   1949    144    360    -44       N  
ATOM    909  CA  GLU A 653      37.377  19.944  24.394  1.00 13.08           C  
ANISOU  909  CA  GLU A 653     1974   1454   1544      7    449     58       C  
ATOM    910  C   GLU A 653      37.781  18.609  23.761  1.00 11.45           C  
ANISOU  910  C   GLU A 653     1287   1262   1800    108    139    228       C  
ATOM    911  O   GLU A 653      37.511  17.548  24.349  1.00 13.66           O  
ANISOU  911  O   GLU A 653     1808   1427   1957   -208   -251    401       O  
ATOM    912  CB  GLU A 653      35.935  20.318  24.038  1.00 20.60           C  
ANISOU  912  CB  GLU A 653     1644   1518   4665    282   1052    -62       C  
ATOM    913  N   ARG A 654      38.405  18.632  22.575  1.00 12.89           N  
ANISOU  913  N   ARG A 654     2097   1360   1441    239     35      2       N  
ATOM    914  CA  ARG A 654      38.854  17.420  21.895  1.00 11.34           C  
ANISOU  914  CA  ARG A 654     1444   1160   1705     10   -173     -9       C  
ATOM    915  C   ARG A 654      39.971  16.748  22.718  1.00 11.36           C  
ANISOU  915  C   ARG A 654     1722    961   1634   -204   -338    178       C  
ATOM    916  O   ARG A 654      40.015  15.539  22.840  1.00 15.30           O  
ANISOU  916  O   ARG A 654     2170    913   2731   -302   -783    264       O  
ATOM    917  CB  ARG A 654      39.277  17.643  20.425  1.00 12.97           C  
ANISOU  917  CB  ARG A 654     2067   1408   1453    359   -339   -178       C  
ATOM    918  CG  ARG A 654      38.126  18.016  19.510  1.00 17.09           C  
ANISOU  918  CG  ARG A 654     2775   1772   1947    606   -885   -203       C  
ATOM    919  CD  ARG A 654      38.519  18.556  18.144  1.00 22.79           C  
ANISOU  919  CD  ARG A 654     4257   2804   1598    956   -927   -135       C  
ATOM    920  NE  ARG A 654      39.517  19.632  18.089  1.00 43.28           N  
ANISOU  920  NE  ARG A 654    10699   4121   1625  -2668    312     91       N  
ATOM    921  N   LEU A 655      40.896  17.561  23.226  1.00 10.00           N  
ANISOU  921  N   LEU A 655     1657    817   1324    -93   -191     14       N  
ATOM    922  CA  LEU A 655      41.945  17.053  24.121  1.00  9.51           C  
ANISOU  922  CA  LEU A 655     1436    875   1302      1    -10    -44       C  
ATOM    923  C   LEU A 655      41.361  16.481  25.394  1.00 10.29           C  
ANISOU  923  C   LEU A 655     1387   1239   1286    -84      7     47       C  
ATOM    924  O   LEU A 655      41.695  15.394  25.887  1.00 10.22           O  
ANISOU  924  O   LEU A 655     1581   1250   1054    -63    -25     -7       O  
ATOM    925  CB  LEU A 655      42.947  18.186  24.388  1.00  9.45           C  
ANISOU  925  CB  LEU A 655     1628    983    978   -133    -92     23       C  
ATOM    926  CG  LEU A 655      44.157  17.789  25.248  1.00 10.84           C  
ANISOU  926  CG  LEU A 655     1435   1175   1508    -68    -91    208       C  
ATOM    927  CD1 LEU A 655      45.035  16.774  24.516  1.00 14.20           C  
ANISOU  927  CD1 LEU A 655     1436   2260   1697    161    307    122       C  
ATOM    928  CD2 LEU A 655      44.915  19.054  25.633  1.00 13.96           C  
ANISOU  928  CD2 LEU A 655     1502   1901   1902   -693   -249    334       C  
ATOM    929  N   LYS A 656      40.444  17.274  26.008  1.00 10.72           N  
ANISOU  929  N   LYS A 656     1726   1115   1231    -41     27    -34       N  
ATOM    930  CA  LYS A 656      39.857  16.851  27.270  1.00 11.76           C  
ANISOU  930  CA  LYS A 656     1844   1445   1181   -293    106   -220       C  
ATOM    931  C   LYS A 656      39.135  15.531  27.126  1.00 11.06           C  
ANISOU  931  C   LYS A 656     1849   1312   1040   -210     16    -55       C  
ATOM    932  O   LYS A 656      39.142  14.692  28.040  1.00 10.87           O  
ANISOU  932  O   LYS A 656     1723   1452    953    110    284      9       O  
ATOM    933  CB  LYS A 656      38.893  17.939  27.742  1.00 14.25           C  
ANISOU  933  CB  LYS A 656     2619   1451   1345   -129    421   -289       C  
ATOM    934  N   HIS A 657      38.416  15.295  26.055  1.00  8.76           N  
ANISOU  934  N   HIS A 657     1558    735   1036     33    110     66       N  
ATOM    935  CA  HIS A 657      37.732  14.040  25.845  1.00  8.35           C  
ANISOU  935  CA  HIS A 657     1153    913   1106    -30    276      4       C  
ATOM    936  C   HIS A 657      38.675  12.863  25.913  1.00  9.07           C  
ANISOU  936  C   HIS A 657     1345    822   1278     51    249    -68       C  
ATOM    937  O   HIS A 657      38.425  11.838  26.530  1.00  9.80           O  
ANISOU  937  O   HIS A 657     1584   1042   1099    -80    -73    111       O  
ATOM    938  CB  HIS A 657      37.042  14.051  24.462  0.82  8.67           C  
ANISOU  938  CB  HIS A 657     1335    828   1131    -68    237     -3       C  
ATOM    939  CG  HIS A 657      36.049  12.931  24.222  0.82  7.34           C  
ANISOU  939  CG  HIS A 657     1115    857    819    -13    294      2       C  
ATOM    940  ND1 HIS A 657      35.261  12.868  23.110  0.82  8.01           N  
ANISOU  940  ND1 HIS A 657     1297    915    830    -46    245     91       N  
ATOM    941  CD2 HIS A 657      35.710  11.851  24.936  0.82  7.61           C  
ANISOU  941  CD2 HIS A 657      926   1170    797   -158    210    146       C  
ATOM    942  CE1 HIS A 657      34.490  11.799  23.176  0.82  7.81           C  
ANISOU  942  CE1 HIS A 657     1125    918    924     12     59     97       C  
ATOM    943  NE2 HIS A 657      34.739  11.134  24.295  0.82  7.08           N  
ANISOU  943  NE2 HIS A 657      911    732   1046    119    103     97       N  
ATOM    944  N   TRP A 658      39.808  12.986  25.221  1.00 10.01           N  
ANISOU  944  N   TRP A 658     1346   1065   1394    160    314   -132       N  
ATOM    945  CA  TRP A 658      40.851  11.951  25.302  1.00  9.49           C  
ANISOU  945  CA  TRP A 658     1169   1113   1323     67     12   -200       C  
ATOM    946  C   TRP A 658      41.347  11.742  26.711  1.00 10.19           C  
ANISOU  946  C   TRP A 658     1500   1033   1338     16    104   -110       C  
ATOM    947  O   TRP A 658      41.494  10.591  27.164  1.00 11.15           O  
ANISOU  947  O   TRP A 658     1598   1041   1597    117   -168    -83       O  
ATOM    948  CB  TRP A 658      41.996  12.337  24.361  1.00 10.20           C  
ANISOU  948  CB  TRP A 658     1113   1396   1366    -28     65   -261       C  
ATOM    949  CG  TRP A 658      42.932  11.233  23.952  1.00 10.19           C  
ANISOU  949  CG  TRP A 658     1235   1361   1278     61     81   -132       C  
ATOM    950  CD1 TRP A 658      44.223  11.034  24.338  1.00 12.43           C  
ANISOU  950  CD1 TRP A 658     1490   1846   1387    408   -185   -346       C  
ATOM    951  CD2 TRP A 658      42.609  10.177  23.045  1.00  9.64           C  
ANISOU  951  CD2 TRP A 658     1238   1027   1397    -51    166     15       C  
ATOM    952  NE1 TRP A 658      44.754   9.893  23.725  1.00 12.51           N  
ANISOU  952  NE1 TRP A 658     1403   1975   1375    365     25   -345       N  
ATOM    953  CE2 TRP A 658      43.749   9.368  22.919  1.00 10.26           C  
ANISOU  953  CE2 TRP A 658     1575   1104   1220    191     15    133       C  
ATOM    954  CE3 TRP A 658      41.454   9.835  22.310  1.00 10.25           C  
ANISOU  954  CE3 TRP A 658     1214   1132   1550   -379    309    -66       C  
ATOM    955  CZ2 TRP A 658      43.804   8.245  22.114  1.00 10.73           C  
ANISOU  955  CZ2 TRP A 658     1363   1002   1712    -99    446      3       C  
ATOM    956  CZ3 TRP A 658      41.524   8.723  21.512  1.00 12.52           C  
ANISOU  956  CZ3 TRP A 658     1363   1059   2336   -377    114   -285       C  
ATOM    957  CH2 TRP A 658      42.668   7.939  21.409  1.00 12.53           C  
ANISOU  957  CH2 TRP A 658     1496   1333   1930   -251    412   -274       C  
ATOM    958  N   TYR A 659      41.608  12.853  27.399  1.00  9.41           N  
ANISOU  958  N   TYR A 659     1382   1067   1127     93     24    -18       N  
ATOM    959  CA  TYR A 659      42.099  12.715  28.741  1.00 10.50           C  
ANISOU  959  CA  TYR A 659     1471   1258   1262     13   -162     81       C  
ATOM    960  C   TYR A 659      41.080  12.039  29.655  1.00 11.44           C  
ANISOU  960  C   TYR A 659     1635   1575   1135   -121   -223    221       C  
ATOM    961  O   TYR A 659      41.437  11.260  30.546  1.00 13.17           O  
ANISOU  961  O   TYR A 659     2042   1682   1281    -10   -280    321       O  
ATOM    962  CB  TYR A 659      42.463  14.106  29.307  1.00 12.47           C  
ANISOU  962  CB  TYR A 659     1671   1470   1598   -214   -496    -54       C  
ATOM    963  CG  TYR A 659      43.708  14.747  28.746  1.00 12.92           C  
ANISOU  963  CG  TYR A 659     1782   1705   1422   -347   -384   -107       C  
ATOM    964  CD1 TYR A 659      44.612  14.074  27.948  1.00 15.43           C  
ANISOU  964  CD1 TYR A 659     2285   1873   1704   -199     50     49       C  
ATOM    965  CD2 TYR A 659      43.970  16.076  29.097  1.00 13.56           C  
ANISOU  965  CD2 TYR A 659     1924   1776   1451   -522   -318    -82       C  
ATOM    966  CE1 TYR A 659      45.754  14.750  27.482  1.00 15.99           C  
ANISOU  966  CE1 TYR A 659     1822   1992   2263    182    -61    633       C  
ATOM    967  CE2 TYR A 659      45.085  16.768  28.661  1.00 15.04           C  
ANISOU  967  CE2 TYR A 659     1950   1998   1765   -603   -468    182       C  
ATOM    968  CZ  TYR A 659      45.967  16.067  27.848  1.00 15.44           C  
ANISOU  968  CZ  TYR A 659     1833   2087   1947   -163   -226    859       C  
ATOM    969  OH  TYR A 659      47.096  16.736  27.403  1.00 19.80           O  
ANISOU  969  OH  TYR A 659     1540   2917   3065   -429   -409    833       O  
ATOM    970  N   GLU A 660      39.784  12.286  29.444  1.00 11.14           N  
ANISOU  970  N   GLU A 660     1559   1277   1398   -208   -149    140       N  
ATOM    971  CA  GLU A 660      38.814  11.662  30.320  1.00 12.13           C  
ANISOU  971  CA  GLU A 660     1876   1646   1085   -711   -172    -42       C  
ATOM    972  C   GLU A 660      38.778  10.160  30.102  1.00 13.05           C  
ANISOU  972  C   GLU A 660     2154   1697   1107   -840    -81    -73       C  
ATOM    973  O   GLU A 660      38.570   9.400  31.022  1.00 15.18           O  
ANISOU  973  O   GLU A 660     3020   1484   1264     34    -74     89       O  
ATOM    974  CB  GLU A 660      37.424  12.273  30.060  1.00 14.23           C  
ANISOU  974  CB  GLU A 660     1846   2280   1282   -494    265    259       C  
ATOM    975  CG  GLU A 660      37.336  13.710  30.558  1.00 19.39           C  
ANISOU  975  CG  GLU A 660     2630   2335   2401    -42    252     85       C  
ATOM    976  CD  GLU A 660      37.010  13.786  32.026  1.00 23.82           C  
ANISOU  976  CD  GLU A 660     2641   3913   2495    688    292   -924       C  
ATOM    977  OE1 GLU A 660      37.511  12.916  32.736  1.00 37.28           O  
ANISOU  977  OE1 GLU A 660     6062   6314   1790   2333    588    -91       O  
ATOM    978  OE2 GLU A 660      36.263  14.684  32.421  1.00 40.30           O  
ANISOU  978  OE2 GLU A 660     3591   7133   4587   2583   -614  -2945       O  
ATOM    979  N   CYS A 661      38.915   9.684  28.868  1.00 14.18           N  
ANISOU  979  N   CYS A 661     2540   1593   1253   -501     20    -98       N  
ATOM    980  CA  CYS A 661      39.061   8.262  28.612  1.00 15.99           C  
ANISOU  980  CA  CYS A 661     3315   1485   1275   -526    268    114       C  
ATOM    981  C   CYS A 661      40.328   7.722  29.267  1.00 19.95           C  
ANISOU  981  C   CYS A 661     4575   1555   1448    -35   -612    246       C  
ATOM    982  O   CYS A 661      40.280   6.700  29.943  1.00 27.92           O  
ANISOU  982  O   CYS A 661     7581   1542   1485   -476  -1531    276       O  
ATOM    983  CB  CYS A 661      39.042   8.029  27.096  1.00 14.37           C  
ANISOU  983  CB  CYS A 661     2527   1641   1291   -238     72    -38       C  
ATOM    984  SG  CYS A 661      39.297   6.316  26.623  1.00 16.03           S  
ANISOU  984  SG  CYS A 661     2647   1813   1630   -149   -221   -247       S  
ATOM    985  N   LEU A 662      41.481   8.361  29.123  1.00 19.46           N  
ANISOU  985  N   LEU A 662     3647   2058   1689    657   -674   -166       N  
ATOM    986  CA  LEU A 662      42.729   7.941  29.745  1.00 22.48           C  
ANISOU  986  CA  LEU A 662     4440   2080   2021   1219  -1096   -133       C  
ATOM    987  C   LEU A 662      42.571   7.874  31.263  1.00 21.00           C  
ANISOU  987  C   LEU A 662     4193   1726   2062    487  -1106    201       C  
ATOM    988  O   LEU A 662      43.066   6.949  31.897  1.00 30.26           O  
ANISOU  988  O   LEU A 662     6828   2334   2337   1588  -1843     18       O  
ATOM    989  CB  LEU A 662      43.878   8.888  29.414  1.00 23.76           C  
ANISOU  989  CB  LEU A 662     3168   3969   1890   1419   -252   -267       C  
ATOM    990  CG  LEU A 662      44.391   9.085  28.004  1.00 31.57           C  
ANISOU  990  CG  LEU A 662     4682   5377   1934   1669    159   -387       C  
ATOM    991  CD1 LEU A 662      45.607  10.019  27.952  1.00 33.43           C  
ANISOU  991  CD1 LEU A 662     4144   5830   2729   1954   1044    577       C  
ATOM    992  CD2 LEU A 662      44.732   7.743  27.373  1.00 41.87           C  
ANISOU  992  CD2 LEU A 662     6942   6119   2846   2195    908  -1110       C  
ATOM    993  N   LYS A 663      41.879   8.840  31.877  1.00 18.62           N  
ANISOU  993  N   LYS A 663     3384   1992   1698    217   -732    406       N  
ATOM    994  CA  LYS A 663      41.722   8.854  33.331  1.00 21.36           C  
ANISOU  994  CA  LYS A 663     3392   3070   1654   -488   -880    213       C  
ATOM    995  C   LYS A 663      40.657   7.914  33.881  1.00 23.97           C  
ANISOU  995  C   LYS A 663     4578   3005   1523  -1162   -412   -356       C  
ATOM    996  O   LYS A 663      40.640   7.670  35.118  1.00 28.76           O  
ANISOU  996  O   LYS A 663     5448   3620   1859  -1896  -1168    537       O  
ATOM    997  CB  LYS A 663      41.389  10.281  33.799  1.00 21.56           C  
ANISOU  997  CB  LYS A 663     3562   3022   1609  -1033   -400    -75       C  
ATOM    998  CG  LYS A 663      42.441  11.321  33.444  1.00 32.84           C  
ANISOU  998  CG  LYS A 663     4296   3949   4233  -1941   -155   -125       C  
ATOM    999  CD  LYS A 663      42.299  12.660  34.130  1.00 35.70           C  
ANISOU  999  CD  LYS A 663     5386   3451   4727  -2150    -45    185       C  
ATOM   1000  CE  LYS A 663      42.246  13.881  33.244  1.00 37.24           C  
ANISOU 1000  CE  LYS A 663     6828   4001   3320  -1897    983     86       C  
ATOM   1001  N   ASN A 664      39.754   7.372  33.075  1.00 20.70           N  
ANISOU 1001  N   ASN A 664     3985   2390   1489   -709   -461     71       N  
ATOM   1002  CA  ASN A 664      38.604   6.590  33.541  1.00 21.21           C  
ANISOU 1002  CA  ASN A 664     4271   2256   1531   -809    -66   -256       C  
ATOM   1003  C   ASN A 664      38.414   5.280  32.792  1.00 19.45           C  
ANISOU 1003  C   ASN A 664     4176   2122   1093   -604   -115     18       C  
ATOM   1004  O   ASN A 664      37.611   5.143  31.872  1.00 23.48           O  
ANISOU 1004  O   ASN A 664     5413   2050   1458   -284   -892   -132       O  
ATOM   1005  CB  ASN A 664      37.326   7.428  33.375  1.00 23.40           C  
ANISOU 1005  CB  ASN A 664     4260   2756   1875   -469    653   -577       C  
ATOM   1006  CG  ASN A 664      37.372   8.671  34.243  1.00 20.78           C  
ANISOU 1006  CG  ASN A 664     4426   2009   1460   -893    348    167       C  
ATOM   1007  OD1 ASN A 664      37.661   9.781  33.762  1.00 22.46           O  
ANISOU 1007  OD1 ASN A 664     3592   2293   2647   -464    396    928       O  
ATOM   1008  ND2 ASN A 664      37.099   8.452  35.521  1.00 26.17           N  
ANISOU 1008  ND2 ASN A 664     6245   2305   1394  -1750    557   -161       N  
ATOM   1009  N   LYS A 665      39.154   4.253  33.195  1.00 18.21           N  
ANISOU 1009  N   LYS A 665     3077   2422   1421   -489    370    -16       N  
ATOM   1010  CA  LYS A 665      38.932   2.939  32.586  1.00 18.23           C  
ANISOU 1010  CA  LYS A 665     3041   2197   1689   -419   -492    317       C  
ATOM   1011  C   LYS A 665      37.505   2.443  32.814  1.00 15.37           C  
ANISOU 1011  C   LYS A 665     2879   1747   1212     53    -62    -15       C  
ATOM   1012  O   LYS A 665      36.905   2.655  33.862  1.00 17.73           O  
ANISOU 1012  O   LYS A 665     3585   2011   1142    693     49    143       O  
ATOM   1013  CB  LYS A 665      39.941   1.963  33.154  1.00 21.51           C  
ANISOU 1013  CB  LYS A 665     2817   2689   2669    -94     -1    817       C  
ATOM   1014  CG  LYS A 665      41.376   2.395  32.803  1.00 23.94           C  
ANISOU 1014  CG  LYS A 665     2917   3617   2563   -326    188    465       C  
ATOM   1015  CD  LYS A 665      42.330   1.368  33.387  1.00 31.53           C  
ANISOU 1015  CD  LYS A 665     2755   4566   4660     -9    -88    886       C  
ATOM   1016  CE  LYS A 665      43.768   1.660  33.074  1.00 34.55           C  
ANISOU 1016  CE  LYS A 665     2669   5175   5284   -411   -111   -769       C  
ATOM   1017  NZ  LYS A 665      44.603   0.439  33.265  1.00 49.66           N  
ANISOU 1017  NZ  LYS A 665     3487   8626   6755   1697    317   2526       N  
ATOM   1018  N   ASP A 666      36.963   1.759  31.818  1.00 12.89           N  
ANISOU 1018  N   ASP A 666     2349   1407   1142    274    -59    133       N  
ATOM   1019  CA  ASP A 666      35.659   1.103  31.877  1.00 14.43           C  
ANISOU 1019  CA  ASP A 666     2480   1561   1441    148     41    187       C  
ATOM   1020  C   ASP A 666      34.505   2.079  32.037  1.00 14.03           C  
ANISOU 1020  C   ASP A 666     2407   1428   1496     -1    684    329       C  
ATOM   1021  O   ASP A 666      33.423   1.670  32.481  1.00 18.76           O  
ANISOU 1021  O   ASP A 666     2382   2031   2716   -252    564    652       O  
ATOM   1022  CB  ASP A 666      35.618   0.021  32.972  1.00 16.82           C  
ANISOU 1022  CB  ASP A 666     2931   1666   1793    274    468    379       C  
ATOM   1023  CG  ASP A 666      36.588  -1.091  32.620  1.00 19.61           C  
ANISOU 1023  CG  ASP A 666     3704   2194   1552   1047     26    368       C  
ATOM   1024  OD1 ASP A 666      36.591  -1.623  31.493  1.00 18.56           O  
ANISOU 1024  OD1 ASP A 666     3199   2225   1629    484    635    279       O  
ATOM   1025  OD2 ASP A 666      37.430  -1.443  33.477  1.00 28.83           O  
ANISOU 1025  OD2 ASP A 666     3795   5187   1973   2016    -54    401       O  
ATOM   1026  N   LYS A 667      34.667   3.346  31.704  1.00 13.61           N  
ANISOU 1026  N   LYS A 667     2205   1458   1510    -10    187    374       N  
ATOM   1027  CA  LYS A 667      33.576   4.302  31.578  1.00 12.73           C  
ANISOU 1027  CA  LYS A 667     2360   1471   1008     40    164    171       C  
ATOM   1028  C   LYS A 667      33.408   4.703  30.112  1.00 12.55           C  
ANISOU 1028  C   LYS A 667     2134   1684    950     33    200    103       C  
ATOM   1029  O   LYS A 667      34.407   4.955  29.428  1.00 13.05           O  
ANISOU 1029  O   LYS A 667     2143   1746   1071    -25    230    157       O  
ATOM   1030  CB  LYS A 667      33.906   5.550  32.390  1.00 15.79           C  
ANISOU 1030  CB  LYS A 667     3041   1749   1210    176    -82   -107       C  
ATOM   1031  CG  LYS A 667      33.792   5.322  33.884  1.00 14.75           C  
ANISOU 1031  CG  LYS A 667     2796   1586   1223      4    -76     11       C  
ATOM   1032  CD  LYS A 667      33.632   6.659  34.592  1.00 13.55           C  
ANISOU 1032  CD  LYS A 667     1964   1771   1413   -154    345   -206       C  
ATOM   1033  CE  LYS A 667      33.730   6.550  36.072  1.00 16.92           C  
ANISOU 1033  CE  LYS A 667     2829   2097   1503    290   -252   -426       C  
ATOM   1034  NZ  LYS A 667      33.895   7.884  36.714  1.00 18.54           N  
ANISOU 1034  NZ  LYS A 667     3310   2173   1563   -400    387   -470       N  
ATOM   1035  N   LYS A 668      32.179   4.790  29.630  1.00 12.09           N  
ANISOU 1035  N   LYS A 668     2121   1579    895     32    224   -121       N  
ATOM   1036  CA  LYS A 668      31.915   5.288  28.287  1.00 11.72           C  
ANISOU 1036  CA  LYS A 668     2128   1333    992   -109     48   -120       C  
ATOM   1037  C   LYS A 668      31.833   6.813  28.296  1.00 12.69           C  
ANISOU 1037  C   LYS A 668     2679   1352    789     74    647   -190       C  
ATOM   1038  O   LYS A 668      30.930   7.346  28.934  1.00 14.31           O  
ANISOU 1038  O   LYS A 668     2645   1668   1123    195    686    -77       O  
ATOM   1039  CB  LYS A 668      30.633   4.713  27.726  1.00 15.18           C  
ANISOU 1039  CB  LYS A 668     2118   1887   1762   -157   -289    177       C  
ATOM   1040  CG  LYS A 668      30.271   4.973  26.276  1.00 16.42           C  
ANISOU 1040  CG  LYS A 668     2562   1905   1771    346   -652   -233       C  
ATOM   1041  CD  LYS A 668      28.946   4.232  25.947  1.00 27.14           C  
ANISOU 1041  CD  LYS A 668     4045   3468   2798  -1162  -1553    215       C  
ATOM   1042  N   ILE A 669      32.766   7.470  27.592  1.00 10.14           N  
ANISOU 1042  N   ILE A 669     1920   1272    662    281    -13    193       N  
ATOM   1043  CA  ILE A 669      32.798   8.925  27.587  1.00 10.51           C  
ANISOU 1043  CA  ILE A 669     1602   1335   1057    282     59    173       C  
ATOM   1044  C   ILE A 669      32.281   9.395  26.236  1.00  8.02           C  
ANISOU 1044  C   ILE A 669     1284    787    976     84      8     39       C  
ATOM   1045  O   ILE A 669      32.994   9.135  25.241  1.00  9.53           O  
ANISOU 1045  O   ILE A 669     1352   1235   1033     45    172    -28       O  
ATOM   1046  CB  ILE A 669      34.241   9.416  27.817  1.00 10.42           C  
ANISOU 1046  CB  ILE A 669     1701   1578    682    252   -136   -301       C  
ATOM   1047  CG1 ILE A 669      34.965   8.678  28.924  1.00 14.74           C  
ANISOU 1047  CG1 ILE A 669     2352   2068   1180    -71   -555    234       C  
ATOM   1048  CG2 ILE A 669      34.218  10.906  28.077  1.00 12.74           C  
ANISOU 1048  CG2 ILE A 669     2077   1641   1122    199   -314   -466       C  
ATOM   1049  CD1 ILE A 669      34.365   8.887  30.294  1.00 19.47           C  
ANISOU 1049  CD1 ILE A 669     4612   1839    945    228   -236    467       C  
ATOM   1050  N   GLU A 670      31.103  10.035  26.224  1.00  8.77           N  
ANISOU 1050  N   GLU A 670     1540   1057    736    280    187     82       N  
ATOM   1051  CA  GLU A 670      30.401  10.432  25.001  1.00  9.59           C  
ANISOU 1051  CA  GLU A 670     1260   1337   1046    322     81    167       C  
ATOM   1052  C   GLU A 670      30.348  11.949  24.937  1.00  9.98           C  
ANISOU 1052  C   GLU A 670     1429   1425    936    670     24    203       C  
ATOM   1053  O   GLU A 670      29.918  12.578  25.889  1.00 11.01           O  
ANISOU 1053  O   GLU A 670     1681   1473   1029    348    119    -15       O  
ATOM   1054  CB  GLU A 670      28.973   9.878  24.936  1.00 14.78           C  
ANISOU 1054  CB  GLU A 670     1326   2492   1797     -7    108     45       C  
ATOM   1055  CG  GLU A 670      28.338   9.831  23.567  1.00 23.35           C  
ANISOU 1055  CG  GLU A 670     2353   3792   2728     91  -1052   -555       C  
ATOM   1056  CD  GLU A 670      27.117   8.935  23.583  1.00 32.07           C  
ANISOU 1056  CD  GLU A 670     2765   4727   4692   -539  -1759   -351       C  
ATOM   1057  OE1 GLU A 670      27.218   7.746  23.936  1.00 47.61           O  
ANISOU 1057  OE1 GLU A 670     2656   5338  10097  -1085  -1853   1599       O  
ATOM   1058  OE2 GLU A 670      26.040   9.443  23.256  1.00 34.81           O  
ANISOU 1058  OE2 GLU A 670     2580   5546   5099   -383  -1458   -181       O  
ATOM   1059  N   ARG A 671      30.800  12.498  23.837  1.00  9.34           N  
ANISOU 1059  N   ARG A 671     1625   1039    883    296     61   -133       N  
ATOM   1060  CA  ARG A 671      30.820  13.943  23.665  1.00  8.84           C  
ANISOU 1060  CA  ARG A 671     1519   1007    834    113   -202   -233       C  
ATOM   1061  C   ARG A 671      30.492  14.326  22.229  1.00  8.33           C  
ANISOU 1061  C   ARG A 671     1166   1097    902    144    -97    -80       C  
ATOM   1062  O   ARG A 671      30.836  13.611  21.305  1.00  9.54           O  
ANISOU 1062  O   ARG A 671     1535   1252    839    256     34    -56       O  
ATOM   1063  CB  ARG A 671      32.199  14.526  23.999  1.00 10.25           C  
ANISOU 1063  CB  ARG A 671     1427   1399   1070    167   -249   -191       C  
ATOM   1064  CG  ARG A 671      32.763  14.260  25.368  1.00 11.04           C  
ANISOU 1064  CG  ARG A 671     1488   1437   1268     92   -414   -182       C  
ATOM   1065  CD  ARG A 671      32.047  15.050  26.447  1.00 12.38           C  
ANISOU 1065  CD  ARG A 671     2118   1697    890    262   -269     76       C  
ATOM   1066  NE  ARG A 671      32.583  14.812  27.773  1.00 14.71           N  
ANISOU 1066  NE  ARG A 671     2695   1902    991    251   -475    317       N  
ATOM   1067  CZ  ARG A 671      32.257  13.862  28.607  1.00 12.96           C  
ANISOU 1067  CZ  ARG A 671     2129   2025    770     76   -120     78       C  
ATOM   1068  NH1 ARG A 671      31.375  12.905  28.361  1.00 17.79           N  
ANISOU 1068  NH1 ARG A 671     2652   2753   1354   -514     79   -297       N  
ATOM   1069  NH2 ARG A 671      32.902  13.846  29.792  1.00 15.63           N  
ANISOU 1069  NH2 ARG A 671     2799   2170    971     38   -442    385       N  
ATOM   1070  N   TRP A 672      29.911  15.500  22.077  1.00  9.89           N  
ANISOU 1070  N   TRP A 672     1595   1123   1038    206     13     34       N  
ATOM   1071  CA  TRP A 672      29.742  16.180  20.782  1.00  9.53           C  
ANISOU 1071  CA  TRP A 672     1722    927    970    182    136     -5       C  
ATOM   1072  C   TRP A 672      30.936  17.001  20.400  1.00  9.71           C  
ANISOU 1072  C   TRP A 672     1619   1366    705     25   -109    -46       C  
ATOM   1073  O   TRP A 672      31.446  17.714  21.265  1.00 12.26           O  
ANISOU 1073  O   TRP A 672     2025   1769    863   -224   -171   -189       O  
ATOM   1074  CB  TRP A 672      28.498  17.098  20.810  1.00  9.44           C  
ANISOU 1074  CB  TRP A 672     1676    909   1004    166     -9     -5       C  
ATOM   1075  CG  TRP A 672      27.210  16.366  20.875  1.00 10.48           C  
ANISOU 1075  CG  TRP A 672     1672   1149   1161     34   -124    113       C  
ATOM   1076  CD1 TRP A 672      26.456  16.025  21.972  1.00 10.58           C  
ANISOU 1076  CD1 TRP A 672     1391   1437   1191    288     39   -139       C  
ATOM   1077  CD2 TRP A 672      26.505  15.878  19.718  1.00 10.10           C  
ANISOU 1077  CD2 TRP A 672     1579   1078   1182    205   -145    123       C  
ATOM   1078  NE1 TRP A 672      25.339  15.350  21.558  1.00 11.41           N  
ANISOU 1078  NE1 TRP A 672     1335   1600   1400    243     53    -29       N  
ATOM   1079  CE2 TRP A 672      25.340  15.252  20.191  1.00 10.64           C  
ANISOU 1079  CE2 TRP A 672     1499   1132   1413    166   -133    -31       C  
ATOM   1080  CE3 TRP A 672      26.755  15.923  18.354  1.00 10.46           C  
ANISOU 1080  CE3 TRP A 672     1588   1190   1196    398   -198    -61       C  
ATOM   1081  CZ2 TRP A 672      24.401  14.652  19.337  1.00 12.41           C  
ANISOU 1081  CZ2 TRP A 672     1661   1278   1776    229   -406    -94       C  
ATOM   1082  CZ3 TRP A 672      25.843  15.339  17.503  1.00 12.57           C  
ANISOU 1082  CZ3 TRP A 672     1811   1539   1427    342   -673    180       C  
ATOM   1083  CH2 TRP A 672      24.685  14.715  18.015  1.00 13.73           C  
ANISOU 1083  CH2 TRP A 672     1888   1674   1654    115   -672    -72       C  
ATOM   1084  N   HIS A 673      31.346  16.951  19.142  1.00  8.93           N  
ANISOU 1084  N   HIS A 673     1416   1262    717     65    -88     16       N  
ATOM   1085  CA  HIS A 673      32.454  17.765  18.634  1.00 10.44           C  
ANISOU 1085  CA  HIS A 673     1703   1294    969   -159   -100     72       C  
ATOM   1086  C   HIS A 673      32.036  18.472  17.365  1.00  9.61           C  
ANISOU 1086  C   HIS A 673     1765    892    996   -270   -172    -41       C  
ATOM   1087  O   HIS A 673      31.262  17.965  16.549  1.00 11.06           O  
ANISOU 1087  O   HIS A 673     1920   1122   1159   -314   -395    -58       O  
ATOM   1088  CB  HIS A 673      33.646  16.854  18.349  1.00 13.34           C  
ANISOU 1088  CB  HIS A 673     1366   2309   1391     67     78    623       C  
ATOM   1089  CG  HIS A 673      34.190  16.273  19.608  1.00 11.70           C  
ANISOU 1089  CG  HIS A 673     1522   1801   1122    -65      6    243       C  
ATOM   1090  ND1 HIS A 673      34.813  17.048  20.549  1.00 13.65           N  
ANISOU 1090  ND1 HIS A 673     1702   1814   1669   -381   -148    205       N  
ATOM   1091  CD2 HIS A 673      34.178  15.000  20.093  1.00 10.62           C  
ANISOU 1091  CD2 HIS A 673     1384   1603   1050    214    -88     10       C  
ATOM   1092  CE1 HIS A 673      35.171  16.250  21.560  1.00 13.13           C  
ANISOU 1092  CE1 HIS A 673     1441   2005   1542   -239   -388     78       C  
ATOM   1093  NE2 HIS A 673      34.789  15.004  21.323  1.00 11.12           N  
ANISOU 1093  NE2 HIS A 673     1156   1932   1138   -230   -168    244       N  
ATOM   1094  N   GLN A 674      32.599  19.652  17.213  1.00 11.03           N  
ANISOU 1094  N   GLN A 674     1989   1205    996   -560   -204     43       N  
ATOM   1095  CA  GLN A 674      32.458  20.451  16.017  1.00 10.42           C  
ANISOU 1095  CA  GLN A 674     1675   1097   1186   -222    165    135       C  
ATOM   1096  C   GLN A 674      33.411  19.961  14.930  1.00  9.49           C  
ANISOU 1096  C   GLN A 674     1424   1036   1148    128    -75    247       C  
ATOM   1097  O   GLN A 674      34.604  19.836  15.160  1.00 15.02           O  
ANISOU 1097  O   GLN A 674     1513   2569   1625    423   -218     97       O  
ATOM   1098  CB  GLN A 674      32.750  21.917  16.368  1.00 14.66           C  
ANISOU 1098  CB  GLN A 674     2743    988   1840   -113    407    -55       C  
ATOM   1099  CG  GLN A 674      32.604  22.827  15.180  1.00 17.89           C  
ANISOU 1099  CG  GLN A 674     2883   1269   2647   -236    244    529       C  
ATOM   1100  CD  GLN A 674      31.202  23.053  14.698  1.00 27.48           C  
ANISOU 1100  CD  GLN A 674     3430   1718   5294    304   -772   1138       C  
ATOM   1101  OE1 GLN A 674      30.922  22.887  13.498  1.00 33.35           O  
ANISOU 1101  OE1 GLN A 674     3817   3084   5772  -1185  -1751   1319       O  
ATOM   1102  NE2 GLN A 674      30.369  23.455  15.644  1.00 42.10           N  
ANISOU 1102  NE2 GLN A 674     2756   4453   8786    725  -1208  -3466       N  
ATOM   1103  N   LEU A 675      32.857  19.681  13.737  1.00 11.07           N  
ANISOU 1103  N   LEU A 675     1687   1386   1131     19    -76    109       N  
ATOM   1104  CA  LEU A 675      33.704  19.360  12.618  1.00 10.84           C  
ANISOU 1104  CA  LEU A 675     1701   1159   1257    330    -53    121       C  
ATOM   1105  C   LEU A 675      34.375  20.611  12.056  1.00 12.13           C  
ANISOU 1105  C   LEU A 675     1927   1417   1266     93     69    181       C  
ATOM   1106  O   LEU A 675      33.744  21.661  11.985  1.00 14.29           O  
ANISOU 1106  O   LEU A 675     2186   1267   1977     33     35    345       O  
ATOM   1107  CB  LEU A 675      32.925  18.655  11.507  1.00 13.09           C  
ANISOU 1107  CB  LEU A 675     2288   1493   1194    -75     63     35       C  
ATOM   1108  CG  LEU A 675      32.280  17.320  11.931  1.00 12.42           C  
ANISOU 1108  CG  LEU A 675     2100   1518   1099    -49    104    -28       C  
ATOM   1109  CD1 LEU A 675      31.277  16.879  10.889  1.00 15.79           C  
ANISOU 1109  CD1 LEU A 675     2790   1528   1681    -19   -494   -245       C  
ATOM   1110  CD2 LEU A 675      33.353  16.290  12.145  1.00 12.90           C  
ANISOU 1110  CD2 LEU A 675     1874   1342   1687   -234    153    -31       C  
ATOM   1111  N   GLN A 676      35.637  20.454  11.704  1.00 14.60           N  
ANISOU 1111  N   GLN A 676     1923   1568   2056   -209    207   -523       N  
ATOM   1112  CA  GLN A 676      36.465  21.531  11.196  1.00 17.62           C  
ANISOU 1112  CA  GLN A 676     2340   2039   2314   -556    519   -491       C  
ATOM   1113  C   GLN A 676      36.798  21.248   9.739  1.00 16.02           C  
ANISOU 1113  C   GLN A 676     2576   1301   2209   -311    331   -336       C  
ATOM   1114  O   GLN A 676      36.780  20.082   9.324  1.00 17.06           O  
ANISOU 1114  O   GLN A 676     3046   1261   2177   -276   -162   -250       O  
ATOM   1115  CB  GLN A 676      37.770  21.686  11.975  1.00 26.86           C  
ANISOU 1115  CB  GLN A 676     2758   4450   2999  -1571    330  -2161       C  
ATOM   1116  CG  GLN A 676      37.596  21.752  13.478  1.00 35.88           C  
ANISOU 1116  CG  GLN A 676     5136   5529   2969  -1323   -202  -3349       C  
ATOM   1117  CD  GLN A 676      36.667  22.885  13.877  1.00 35.93           C  
ANISOU 1117  CD  GLN A 676     4565   6434   2652   -964   -478  -3386       C  
ATOM   1118  OE1 GLN A 676      36.420  23.805  13.093  1.00 46.90           O  
ANISOU 1118  OE1 GLN A 676     4586   9762   3472   1612  -1003  -2017       O  
ATOM   1119  NE2 GLN A 676      36.177  22.764  15.109  1.00 39.95           N  
ANISOU 1119  NE2 GLN A 676     4285   6241   4653  -2784   1687  -2958       N  
ATOM   1120  N   ASN A 677      37.089  22.279   8.985  1.00 24.04           N  
ANISOU 1120  N   ASN A 677     4396   1544   3196  -1294   2089   -565       N  
ATOM   1121  CA  ASN A 677      37.571  22.057   7.642  1.00 30.90           C  
ANISOU 1121  CA  ASN A 677     4752   2899   4088  -1697   3514   -782       C  
ATOM   1122  C   ASN A 677      39.092  21.927   7.622  1.00 42.10           C  
ANISOU 1122  C   ASN A 677     4643   7141   4213  -1776   2574  -2253       C  
ATOM   1123  O   ASN A 677      39.735  21.156   8.349  1.00 54.89           O  
ANISOU 1123  O   ASN A 677     5259  11946   3651   -832   1012  -2463       O  
TER    1124      ASN A 677                                                      
HETATM 1125 CA    CA A1678      29.126  15.339  -3.493  1.00 15.84          CA  
ANISOU 1125 CA    CA A1678     3520   1708    790    -18   -195     49      CA  
HETATM 1126 CA    CA A1679      27.020  12.288  -2.564  1.00 13.91          CA  
ANISOU 1126 CA    CA A1679     2751   1732    801    179   -305    -26      CA  
HETATM 1127  O   HOH A2001      20.251  16.384  -8.256  1.00 43.20           O  
ANISOU 1127  O   HOH A2001     5588   5757   5068   -763     40    467       O  
HETATM 1128  O   HOH A2002      41.588   7.874   7.683  1.00 35.83           O  
ANISOU 1128  O   HOH A2002     2273   7167   4173   -754   -167   -799       O  
HETATM 1129  O   HOH A2003      35.027  -3.491  12.671  1.00 34.04           O  
ANISOU 1129  O   HOH A2003     3436   4038   5460     60   -511    -93       O  
HETATM 1130  O   HOH A2004      17.923   9.521  12.260  1.00 37.53           O  
ANISOU 1130  O   HOH A2004     4477   4096   5688  -1512    541  -1282       O  
HETATM 1131  O   HOH A2005      38.265  -4.852  14.735  1.00 47.12           O  
ANISOU 1131  O   HOH A2005     7111   3269   7525   1293   2969    433       O  
HETATM 1132  O   HOH A2006      23.661  11.973  -9.442  1.00 23.10           O  
ANISOU 1132  O   HOH A2006     2178   3140   3457   -443   -173   1493       O  
HETATM 1133  O   HOH A2007      29.392  10.583 -13.403  1.00 17.25           O  
ANISOU 1133  O   HOH A2007     1854   3573   1128    -40    155    370       O  
HETATM 1134  O   HOH A2008      28.952  15.551 -13.259  1.00 26.73           O  
ANISOU 1134  O   HOH A2008     3116   4701   2340     60   -233    747       O  
HETATM 1135  O   HOH A2009      29.553  17.302 -17.580  1.00 18.83           O  
ANISOU 1135  O   HOH A2009     3132   2381   1642    735    150   -788       O  
HETATM 1136  O   HOH A2010      32.635  18.168 -18.048  1.00 28.03           O  
ANISOU 1136  O   HOH A2010     4701   2635   3314   -677  -1109     84       O  
HETATM 1137  O   HOH A2011      23.363  14.027 -15.574  1.00 22.66           O  
ANISOU 1137  O   HOH A2011     2267   4247   2096    217    -33    261       O  
HETATM 1138  O   HOH A2012      22.397  15.714  -6.191  1.00 31.42           O  
ANISOU 1138  O   HOH A2012     5000   4947   1990    349   -211   -261       O  
HETATM 1139  O   HOH A2013      29.181  12.975 -10.615  1.00 20.71           O  
ANISOU 1139  O   HOH A2013     3156   3118   1595    361   -157    -81       O  
HETATM 1140  O   HOH A2014      25.970  11.565  -4.595  1.00 18.72           O  
ANISOU 1140  O   HOH A2014     2678   3270   1163   -669   -596   -126       O  
HETATM 1141  O   HOH A2015      25.593  22.942   7.585  1.00 40.50           O  
ANISOU 1141  O   HOH A2015     4328   4555   6504    277   -849  -2050       O  
HETATM 1142  O   HOH A2016      28.723   4.007  21.358  1.00 19.25           O  
ANISOU 1142  O   HOH A2016     2561   2362   2393     -5    339    167       O  
HETATM 1143  O   HOH A2017      32.801   3.816  23.255  1.00 12.76           O  
ANISOU 1143  O   HOH A2017     1830   1640   1377    -40    -71    148       O  
HETATM 1144  O   HOH A2018      45.769  -4.818  25.363  1.00 32.93           O  
ANISOU 1144  O   HOH A2018     3501   3985   5026   1881    454    628       O  
HETATM 1145  O   HOH A2019      25.193  22.935   3.618  1.00 32.82           O  
ANISOU 1145  O   HOH A2019     5975   2662   3835   1217  -1065   -194       O  
HETATM 1146  O   HOH A2020      22.695  12.692  -1.631  1.00 28.08           O  
ANISOU 1146  O   HOH A2020     2486   3469   4712    492   -616     78       O  
HETATM 1147  O   HOH A2021      18.312  19.094   3.386  1.00 46.69           O  
ANISOU 1147  O   HOH A2021     6300   5592   5846   1479  -1282   1318       O  
HETATM 1148  O   HOH A2022      22.341   8.790  -2.925  1.00 36.26           O  
ANISOU 1148  O   HOH A2022     3047   6548   4181  -1480  -1385    430       O  
HETATM 1149  O   HOH A2023      40.269   5.051   7.859  1.00 28.15           O  
ANISOU 1149  O   HOH A2023     5112   4056   1527   1551    987    568       O  
HETATM 1150  O   HOH A2024      41.929  -2.290  14.799  1.00 29.19           O  
ANISOU 1150  O   HOH A2024     3515   4125   3453    920   -621   -777       O  
HETATM 1151  O   HOH A2025      36.408  -2.246  10.884  1.00 30.64           O  
ANISOU 1151  O   HOH A2025     3985   4528   3130   -230   -578   1004       O  
HETATM 1152  O   HOH A2026      36.270  -0.794   8.896  1.00 29.61           O  
ANISOU 1152  O   HOH A2026     4059   2092   5100    -41   -634    763       O  
HETATM 1153  O   HOH A2027      31.849  -0.490   8.814  1.00 34.17           O  
ANISOU 1153  O   HOH A2027     3398   2548   7039   -701  -1466   1909       O  
HETATM 1154  O   HOH A2028      32.075   2.396   3.936  1.00 30.23           O  
ANISOU 1154  O   HOH A2028     3958   5350   2180   1448   -144  -1223       O  
HETATM 1155  O   HOH A2029      28.114   1.142   3.283  1.00 29.34           O  
ANISOU 1155  O   HOH A2029     6051   2555   2540  -1306    101   -556       O  
HETATM 1156  O   HOH A2030      21.183   4.910   3.870  1.00 35.71           O  
ANISOU 1156  O   HOH A2030     4216   4332   5020  -1202  -1914    222       O  
HETATM 1157  O   HOH A2031      18.818  15.322   6.297  1.00 24.85           O  
ANISOU 1157  O   HOH A2031     2763   4425   2254   1502   -402   -893       O  
HETATM 1158  O   HOH A2032      20.417  10.830  13.257  1.00 19.99           O  
ANISOU 1158  O   HOH A2032     2443   2242   2911    579    394    296       O  
HETATM 1159  O   HOH A2033      18.866   5.355  16.937  1.00 27.14           O  
ANISOU 1159  O   HOH A2033     3139   2783   4391   -541    110   -800       O  
HETATM 1160  O   HOH A2034      20.638   7.782   8.744  1.00 21.42           O  
ANISOU 1160  O   HOH A2034     2997   2671   2471   -566   -631   -129       O  
HETATM 1161  O   HOH A2035      23.239   1.831  11.897  1.00 28.72           O  
ANISOU 1161  O   HOH A2035     2277   4055   4579   -927    973  -1815       O  
HETATM 1162  O   HOH A2036      26.949   0.000  18.452  0.50 22.90           O  
ANISOU 1162  O   HOH A2036     3205   3803   1695   1289      0      0       O  
HETATM 1163  O   HOH A2037      26.228   2.383  19.164  1.00 32.16           O  
ANISOU 1163  O   HOH A2037     5072   3492   3654   -261    -34  -1091       O  
HETATM 1164  O   HOH A2038      24.234   3.891  19.869  1.00 32.29           O  
ANISOU 1164  O   HOH A2038     4927   4570   2774    287    607    810       O  
HETATM 1165  O   HOH A2039      27.863   3.911  18.644  1.00 25.99           O  
ANISOU 1165  O   HOH A2039     2547   4309   3019    592   -704   -306       O  
HETATM 1166  O   HOH A2040      32.605  -2.618  13.779  1.00 20.94           O  
ANISOU 1166  O   HOH A2040     3662   2228   2065    -56    -72   -470       O  
HETATM 1167  O   HOH A2041      33.862  -2.972  17.999  1.00 25.77           O  
ANISOU 1167  O   HOH A2041     2821   2898   4070   -138  -1144     41       O  
HETATM 1168  O   HOH A2042      31.334   1.681  24.189  1.00 21.45           O  
ANISOU 1168  O   HOH A2042     2488   2578   3082    284    754    431       O  
HETATM 1169  O   HOH A2043      31.709  -2.756  20.425  1.00 32.95           O  
ANISOU 1169  O   HOH A2043     4651   3025   4844   -134     24    572       O  
HETATM 1170  O   HOH A2044      36.329  -3.214  15.311  1.00 18.97           O  
ANISOU 1170  O   HOH A2044     3292   2113   1803    524    -45   -822       O  
HETATM 1171  O   HOH A2045      42.214  -8.787  20.888  1.00 28.92           O  
ANISOU 1171  O   HOH A2045     4860   3545   2585    262    416   -399       O  
HETATM 1172  O   HOH A2046      44.185  -6.355  23.416  1.00 32.97           O  
ANISOU 1172  O   HOH A2046     4782   4138   3606   1369    830    -26       O  
HETATM 1173  O   HOH A2047      43.700  -3.108  16.733  1.00 23.75           O  
ANISOU 1173  O   HOH A2047     3454   3598   1972    542    580   -543       O  
HETATM 1174  O   HOH A2048      46.083  -1.836  29.639  1.00 24.00           O  
ANISOU 1174  O   HOH A2048     4033   2280   2807    644   -501    350       O  
HETATM 1175  O   HOH A2049      49.774  -1.361  23.258  1.00 20.53           O  
ANISOU 1175  O   HOH A2049     2331   3218   2251    542    203     80       O  
HETATM 1176  O   HOH A2050      48.386   1.723  17.214  1.00 31.98           O  
ANISOU 1176  O   HOH A2050     2207   4905   5040   1038    377  -2117       O  
HETATM 1177  O   HOH A2051      46.432  15.160  17.095  1.00 34.14           O  
ANISOU 1177  O   HOH A2051     5999   3010   3961    999   1832   1574       O  
HETATM 1178  O   HOH A2052      40.369   9.980   9.296  1.00 17.34           O  
ANISOU 1178  O   HOH A2052     2443   2413   1733    181   -386    -60       O  
HETATM 1179  O   HOH A2053      30.102   4.619 -10.416  1.00 20.73           O  
ANISOU 1179  O   HOH A2053     2924   2953   2001   -342    753   -393       O  
HETATM 1180  O   HOH A2054      37.345   9.084   0.216  1.00 33.30           O  
ANISOU 1180  O   HOH A2054     4043   4951   3659    -65   -671   -279       O  
HETATM 1181  O   HOH A2055      38.203  12.825  -2.431  1.00 30.86           O  
ANISOU 1181  O   HOH A2055     4100   4890   2736   -388    158      9       O  
HETATM 1182  O   HOH A2056      34.935   5.834  -2.760  1.00 38.53           O  
ANISOU 1182  O   HOH A2056     6164   3905   4570   1607   -835  -1802       O  
HETATM 1183  O   HOH A2057      48.217  21.215  20.113  1.00 43.08           O  
ANISOU 1183  O   HOH A2057     7626   4146   4595   1165  -2092   -349       O  
HETATM 1184  O   HOH A2058      43.587  23.519  25.168  1.00 27.38           O  
ANISOU 1184  O   HOH A2058     3404   2987   4010   -744   -208    934       O  
HETATM 1185  O   HOH A2059      35.035  16.972  25.347  1.00 26.98           O  
ANISOU 1185  O   HOH A2059     2099   3927   4225     22   -323   -314       O  
HETATM 1186  O   HOH A2060      34.554  15.837  30.854  1.00 23.78           O  
ANISOU 1186  O   HOH A2060     3662   2484   2890   -132    332    -30       O  
HETATM 1187  O   HOH A2061      37.233   4.845  29.232  1.00 15.81           O  
ANISOU 1187  O   HOH A2061     1890   2369   1750    157    181   -393       O  
HETATM 1188  O   HOH A2062      40.763   4.527  35.688  1.00 35.99           O  
ANISOU 1188  O   HOH A2062     5510   5003   3164    341  -1964     71       O  
HETATM 1189  O   HOH A2063      28.421   7.833  29.438  1.00 28.52           O  
ANISOU 1189  O   HOH A2063     2198   4812   3826    310     98   -863       O  
HETATM 1190  O   HOH A2064      24.438  11.397  23.961  1.00 31.62           O  
ANISOU 1190  O   HOH A2064     3493   3970   4550    460     78   -717       O  
HETATM 1191  O   HOH A2065      26.673   4.816  22.396  1.00 38.32           O  
ANISOU 1191  O   HOH A2065     4894   6362   3305   -734    358    596       O  
HETATM 1192  O   HOH A2066      34.847  19.756  19.522  1.00 19.44           O  
ANISOU 1192  O   HOH A2066     2424   1928   3034     68    114   -331       O  
HETATM 1193  O   HOH A2067      37.558  24.660  10.980  1.00 24.07           O  
ANISOU 1193  O   HOH A2067     3815   2172   3157     62    133   -414       O  
HETATM 1194  O   HOH A2068      34.373  25.852  13.558  1.00 36.32           O  
ANISOU 1194  O   HOH A2068     6397   3739   3663    165    349  -1249       O  
CONECT    1    2                                                                
CONECT    2    1    3                                                           
CONECT    3    2    4    5                                                      
CONECT    4    3                                                                
CONECT    5    3                                                                
CONECT   42 1125                                                                
CONECT  135  141                                                                
CONECT  141  135  142                                                           
CONECT  142  141  143  145                                                      
CONECT  143  142  144  149                                                      
CONECT  144  143                                                                
CONECT  145  142  146                                                           
CONECT  146  145  147                                                           
CONECT  147  146  148                                                           
CONECT  148  147                                                                
CONECT  149  143                                                                
CONECT  288  291                                                                
CONECT  291  288  292                                                           
CONECT  292  291  293  295                                                      
CONECT  293  292  294  299                                                      
CONECT  294  293 1125                                                           
CONECT  295  292  296                                                           
CONECT  296  295  297                                                           
CONECT  297  296  298                                                           
CONECT  298  297                                                                
CONECT  299  293                                                                
CONECT  305 1125 1126                                                           
CONECT  306 1126                                                                
CONECT  349 1126                                                                
CONECT  760 1126                                                                
CONECT  761 1125 1126                                                           
CONECT  765 1126                                                                
CONECT  780 1125 1126                                                           
CONECT  781 1125                                                                
CONECT  824 1125                                                                
CONECT 1125   42  294  305  761                                                 
CONECT 1125  780  781  824                                                      
CONECT 1126  305  306  349  760                                                 
CONECT 1126  761  765  780 1140                                                 
CONECT 1140 1126                                                                
MASTER      327    0    5    2    8    0    4    6 1193    1   40   13          
END                                                                             



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